data_9E0B
# 
_entry.id   9E0B 
# 
_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   9E0B         pdb_00009e0b 10.2210/pdb9e0b/pdb 
WWPDB D_1000289161 ?            ?                   
# 
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                        9E0B 
_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 'DI(HYDROXYETHYL)ETHER'                   106.120    6    ?                ? ? ? 
4  non-polymer syn 'FORMIC ACID'                             46.025     6    ?                ? ? ? 
5  non-polymer syn '(2,3-dihydro-1-benzofuran-5-yl)methanol' 150.174    2    ?                ? ? ? 
6  non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE         663.425    2    ?                ? ? ? 
7  non-polymer syn 'SULFATE ION'                             96.063     6    ?                ? ? ? 
8  non-polymer syn 'MAGNESIUM ION'                           24.305     2    ?                ? ? ? 
9  non-polymer syn 'PENTAETHYLENE GLYCOL'                    238.278    1    ?                ? ? ? 
10 non-polymer syn 'TRIETHYLENE GLYCOL'                      150.173    1    ?                ? ? ? 
11 water       nat water                                     18.015     2181 ?                ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2  'FLAVIN-ADENINE DINUCLEOTIDE'             FAD   
3  'DI(HYDROXYETHYL)ETHER'                   PEG   
4  'FORMIC ACID'                             FMT   
5  '(2,3-dihydro-1-benzofuran-5-yl)methanol' A1AQC 
6  NICOTINAMIDE-ADENINE-DINUCLEOTIDE         NAD   
7  'SULFATE ION'                             SO4   
8  'MAGNESIUM ION'                           MG    
9  'PENTAETHYLENE GLYCOL'                    1PE   
10 'TRIETHYLENE GLYCOL'                      PGE   
11 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 
1PE   non-polymer         . 'PENTAETHYLENE GLYCOL'                    PEG400 'C10 H22 O6'        238.278 
A1AQC non-polymer         . '(2,3-dihydro-1-benzofuran-5-yl)methanol' ?      'C9 H10 O2'         150.174 
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  ?    ?   ?   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  ?    ?   ?   A . n 
A 1 495  ASN 495  493  ?    ?   ?   A . n 
A 1 496  GLY 496  494  494  GLY GLY A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 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  ?    ?   ?   B . n 
B 1 495  ASN 495  493  ?    ?   ?   B . n 
B 1 496  GLY 496  494  ?    ?   ?   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 A1AQC ? ? A1AQC ? ? '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  PEG   1    1302 1302 PEG   PEG A . 
E  4  FMT   1    1303 1303 FMT   FMT A . 
F  5  A1AQC 1    1304 1304 A1AQC 222 A . 
G  4  FMT   1    1305 1305 FMT   FMT A . 
H  4  FMT   1    1306 1306 FMT   FMT A . 
I  6  NAD   1    1307 2002 NAD   NAD A . 
J  7  SO4   1    1308 1    SO4   SO4 A . 
K  7  SO4   1    1309 3    SO4   SO4 A . 
L  7  SO4   1    1310 4    SO4   SO4 A . 
M  7  SO4   1    1311 5    SO4   SO4 A . 
N  7  SO4   1    1312 6    SO4   SO4 A . 
O  8  MG    1    1313 1    MG    MG  A . 
P  2  FAD   1    1301 1301 FAD   FAD B . 
Q  9  1PE   1    1302 1302 1PE   1PE B . 
R  10 PGE   1    1303 1303 PGE   PGE B . 
S  4  FMT   1    1304 1304 FMT   FMT B . 
T  3  PEG   1    1305 1305 PEG   PEG B . 
U  3  PEG   1    1306 1306 PEG   PEG B . 
V  3  PEG   1    1307 1307 PEG   PEG B . 
W  4  FMT   1    1308 1308 FMT   FMT B . 
X  4  FMT   1    1309 1310 FMT   FMT B . 
Y  5  A1AQC 1    1310 1311 A1AQC 222 B . 
Z  3  PEG   1    1311 1312 PEG   PEG B . 
AA 6  NAD   1    1312 2002 NAD   NAD B . 
BA 7  SO4   1    1313 2    SO4   SO4 B . 
CA 8  MG    1    1314 2    MG    MG  B . 
DA 3  PEG   1    1315 1    PEG   PEG B . 
EA 11 HOH   1    1401 1822 HOH   HOH A . 
EA 11 HOH   2    1402 1835 HOH   HOH A . 
EA 11 HOH   3    1403 1492 HOH   HOH A . 
EA 11 HOH   4    1404 106  HOH   HOH A . 
EA 11 HOH   5    1405 1472 HOH   HOH A . 
EA 11 HOH   6    1406 1826 HOH   HOH A . 
EA 11 HOH   7    1407 859  HOH   HOH A . 
EA 11 HOH   8    1408 387  HOH   HOH A . 
EA 11 HOH   9    1409 1131 HOH   HOH A . 
EA 11 HOH   10   1410 260  HOH   HOH A . 
EA 11 HOH   11   1411 498  HOH   HOH A . 
EA 11 HOH   12   1412 2070 HOH   HOH A . 
EA 11 HOH   13   1413 749  HOH   HOH A . 
EA 11 HOH   14   1414 1305 HOH   HOH A . 
EA 11 HOH   15   1415 626  HOH   HOH A . 
EA 11 HOH   16   1416 1803 HOH   HOH A . 
EA 11 HOH   17   1417 1113 HOH   HOH A . 
EA 11 HOH   18   1418 1147 HOH   HOH A . 
EA 11 HOH   19   1419 2156 HOH   HOH A . 
EA 11 HOH   20   1420 2157 HOH   HOH A . 
EA 11 HOH   21   1421 1624 HOH   HOH A . 
EA 11 HOH   22   1422 1500 HOH   HOH A . 
EA 11 HOH   23   1423 831  HOH   HOH A . 
EA 11 HOH   24   1424 1589 HOH   HOH A . 
EA 11 HOH   25   1425 1631 HOH   HOH A . 
EA 11 HOH   26   1426 1948 HOH   HOH A . 
EA 11 HOH   27   1427 894  HOH   HOH A . 
EA 11 HOH   28   1428 1885 HOH   HOH A . 
EA 11 HOH   29   1429 1401 HOH   HOH A . 
EA 11 HOH   30   1430 1382 HOH   HOH A . 
EA 11 HOH   31   1431 1771 HOH   HOH A . 
EA 11 HOH   32   1432 1251 HOH   HOH A . 
EA 11 HOH   33   1433 172  HOH   HOH A . 
EA 11 HOH   34   1434 1098 HOH   HOH A . 
EA 11 HOH   35   1435 1923 HOH   HOH A . 
EA 11 HOH   36   1436 615  HOH   HOH A . 
EA 11 HOH   37   1437 561  HOH   HOH A . 
EA 11 HOH   38   1438 630  HOH   HOH A . 
EA 11 HOH   39   1439 311  HOH   HOH A . 
EA 11 HOH   40   1440 972  HOH   HOH A . 
EA 11 HOH   41   1441 1457 HOH   HOH A . 
EA 11 HOH   42   1442 2019 HOH   HOH A . 
EA 11 HOH   43   1443 2065 HOH   HOH A . 
EA 11 HOH   44   1444 1429 HOH   HOH A . 
EA 11 HOH   45   1445 458  HOH   HOH A . 
EA 11 HOH   46   1446 981  HOH   HOH A . 
EA 11 HOH   47   1447 1856 HOH   HOH A . 
EA 11 HOH   48   1448 1119 HOH   HOH A . 
EA 11 HOH   49   1449 1764 HOH   HOH A . 
EA 11 HOH   50   1450 367  HOH   HOH A . 
EA 11 HOH   51   1451 1182 HOH   HOH A . 
EA 11 HOH   52   1452 1938 HOH   HOH A . 
EA 11 HOH   53   1453 293  HOH   HOH A . 
EA 11 HOH   54   1454 2238 HOH   HOH A . 
EA 11 HOH   55   1455 953  HOH   HOH A . 
EA 11 HOH   56   1456 1278 HOH   HOH A . 
EA 11 HOH   57   1457 924  HOH   HOH A . 
EA 11 HOH   58   1458 346  HOH   HOH A . 
EA 11 HOH   59   1459 1947 HOH   HOH A . 
EA 11 HOH   60   1460 1603 HOH   HOH A . 
EA 11 HOH   61   1461 1209 HOH   HOH A . 
EA 11 HOH   62   1462 728  HOH   HOH A . 
EA 11 HOH   63   1463 543  HOH   HOH A . 
EA 11 HOH   64   1464 1813 HOH   HOH A . 
EA 11 HOH   65   1465 1186 HOH   HOH A . 
EA 11 HOH   66   1466 321  HOH   HOH A . 
EA 11 HOH   67   1467 233  HOH   HOH A . 
EA 11 HOH   68   1468 931  HOH   HOH A . 
EA 11 HOH   69   1469 711  HOH   HOH A . 
EA 11 HOH   70   1470 549  HOH   HOH A . 
EA 11 HOH   71   1471 1345 HOH   HOH A . 
EA 11 HOH   72   1472 1478 HOH   HOH A . 
EA 11 HOH   73   1473 1224 HOH   HOH A . 
EA 11 HOH   74   1474 46   HOH   HOH A . 
EA 11 HOH   75   1475 763  HOH   HOH A . 
EA 11 HOH   76   1476 625  HOH   HOH A . 
EA 11 HOH   77   1477 1285 HOH   HOH A . 
EA 11 HOH   78   1478 2050 HOH   HOH A . 
EA 11 HOH   79   1479 962  HOH   HOH A . 
EA 11 HOH   80   1480 880  HOH   HOH A . 
EA 11 HOH   81   1481 1887 HOH   HOH A . 
EA 11 HOH   82   1482 768  HOH   HOH A . 
EA 11 HOH   83   1483 1598 HOH   HOH A . 
EA 11 HOH   84   1484 2204 HOH   HOH A . 
EA 11 HOH   85   1485 481  HOH   HOH A . 
EA 11 HOH   86   1486 1087 HOH   HOH A . 
EA 11 HOH   87   1487 1482 HOH   HOH A . 
EA 11 HOH   88   1488 1134 HOH   HOH A . 
EA 11 HOH   89   1489 72   HOH   HOH A . 
EA 11 HOH   90   1490 1210 HOH   HOH A . 
EA 11 HOH   91   1491 2114 HOH   HOH A . 
EA 11 HOH   92   1492 2133 HOH   HOH A . 
EA 11 HOH   93   1493 109  HOH   HOH A . 
EA 11 HOH   94   1494 1080 HOH   HOH A . 
EA 11 HOH   95   1495 409  HOH   HOH A . 
EA 11 HOH   96   1496 245  HOH   HOH A . 
EA 11 HOH   97   1497 470  HOH   HOH A . 
EA 11 HOH   98   1498 1991 HOH   HOH A . 
EA 11 HOH   99   1499 1984 HOH   HOH A . 
EA 11 HOH   100  1500 1004 HOH   HOH A . 
EA 11 HOH   101  1501 478  HOH   HOH A . 
EA 11 HOH   102  1502 351  HOH   HOH A . 
EA 11 HOH   103  1503 1421 HOH   HOH A . 
EA 11 HOH   104  1504 594  HOH   HOH A . 
EA 11 HOH   105  1505 176  HOH   HOH A . 
EA 11 HOH   106  1506 500  HOH   HOH A . 
EA 11 HOH   107  1507 344  HOH   HOH A . 
EA 11 HOH   108  1508 364  HOH   HOH A . 
EA 11 HOH   109  1509 1018 HOH   HOH A . 
EA 11 HOH   110  1510 720  HOH   HOH A . 
EA 11 HOH   111  1511 1192 HOH   HOH A . 
EA 11 HOH   112  1512 196  HOH   HOH A . 
EA 11 HOH   113  1513 422  HOH   HOH A . 
EA 11 HOH   114  1514 1701 HOH   HOH A . 
EA 11 HOH   115  1515 379  HOH   HOH A . 
EA 11 HOH   116  1516 850  HOH   HOH A . 
EA 11 HOH   117  1517 1901 HOH   HOH A . 
EA 11 HOH   118  1518 864  HOH   HOH A . 
EA 11 HOH   119  1519 992  HOH   HOH A . 
EA 11 HOH   120  1520 456  HOH   HOH A . 
EA 11 HOH   121  1521 1740 HOH   HOH A . 
EA 11 HOH   122  1522 545  HOH   HOH A . 
EA 11 HOH   123  1523 1703 HOH   HOH A . 
EA 11 HOH   124  1524 827  HOH   HOH A . 
EA 11 HOH   125  1525 1358 HOH   HOH A . 
EA 11 HOH   126  1526 185  HOH   HOH A . 
EA 11 HOH   127  1527 861  HOH   HOH A . 
EA 11 HOH   128  1528 45   HOH   HOH A . 
EA 11 HOH   129  1529 609  HOH   HOH A . 
EA 11 HOH   130  1530 751  HOH   HOH A . 
EA 11 HOH   131  1531 2099 HOH   HOH A . 
EA 11 HOH   132  1532 793  HOH   HOH A . 
EA 11 HOH   133  1533 125  HOH   HOH A . 
EA 11 HOH   134  1534 362  HOH   HOH A . 
EA 11 HOH   135  1535 1459 HOH   HOH A . 
EA 11 HOH   136  1536 1077 HOH   HOH A . 
EA 11 HOH   137  1537 1755 HOH   HOH A . 
EA 11 HOH   138  1538 1362 HOH   HOH A . 
EA 11 HOH   139  1539 1397 HOH   HOH A . 
EA 11 HOH   140  1540 1141 HOH   HOH A . 
EA 11 HOH   141  1541 1693 HOH   HOH A . 
EA 11 HOH   142  1542 1878 HOH   HOH A . 
EA 11 HOH   143  1543 1277 HOH   HOH A . 
EA 11 HOH   144  1544 2193 HOH   HOH A . 
EA 11 HOH   145  1545 882  HOH   HOH A . 
EA 11 HOH   146  1546 1452 HOH   HOH A . 
EA 11 HOH   147  1547 744  HOH   HOH A . 
EA 11 HOH   148  1548 1219 HOH   HOH A . 
EA 11 HOH   149  1549 1672 HOH   HOH A . 
EA 11 HOH   150  1550 554  HOH   HOH A . 
EA 11 HOH   151  1551 920  HOH   HOH A . 
EA 11 HOH   152  1552 907  HOH   HOH A . 
EA 11 HOH   153  1553 1133 HOH   HOH A . 
EA 11 HOH   154  1554 231  HOH   HOH A . 
EA 11 HOH   155  1555 719  HOH   HOH A . 
EA 11 HOH   156  1556 1888 HOH   HOH A . 
EA 11 HOH   157  1557 184  HOH   HOH A . 
EA 11 HOH   158  1558 1616 HOH   HOH A . 
EA 11 HOH   159  1559 1533 HOH   HOH A . 
EA 11 HOH   160  1560 100  HOH   HOH A . 
EA 11 HOH   161  1561 735  HOH   HOH A . 
EA 11 HOH   162  1562 1568 HOH   HOH A . 
EA 11 HOH   163  1563 1368 HOH   HOH A . 
EA 11 HOH   164  1564 1907 HOH   HOH A . 
EA 11 HOH   165  1565 34   HOH   HOH A . 
EA 11 HOH   166  1566 404  HOH   HOH A . 
EA 11 HOH   167  1567 1685 HOH   HOH A . 
EA 11 HOH   168  1568 1156 HOH   HOH A . 
EA 11 HOH   169  1569 2    HOH   HOH A . 
EA 11 HOH   170  1570 1483 HOH   HOH A . 
EA 11 HOH   171  1571 139  HOH   HOH A . 
EA 11 HOH   172  1572 1924 HOH   HOH A . 
EA 11 HOH   173  1573 227  HOH   HOH A . 
EA 11 HOH   174  1574 874  HOH   HOH A . 
EA 11 HOH   175  1575 2118 HOH   HOH A . 
EA 11 HOH   176  1576 2231 HOH   HOH A . 
EA 11 HOH   177  1577 243  HOH   HOH A . 
EA 11 HOH   178  1578 898  HOH   HOH A . 
EA 11 HOH   179  1579 1446 HOH   HOH A . 
EA 11 HOH   180  1580 759  HOH   HOH A . 
EA 11 HOH   181  1581 66   HOH   HOH A . 
EA 11 HOH   182  1582 166  HOH   HOH A . 
EA 11 HOH   183  1583 1748 HOH   HOH A . 
EA 11 HOH   184  1584 171  HOH   HOH A . 
EA 11 HOH   185  1585 727  HOH   HOH A . 
EA 11 HOH   186  1586 1908 HOH   HOH A . 
EA 11 HOH   187  1587 5    HOH   HOH A . 
EA 11 HOH   188  1588 1395 HOH   HOH A . 
EA 11 HOH   189  1589 1311 HOH   HOH A . 
EA 11 HOH   190  1590 283  HOH   HOH A . 
EA 11 HOH   191  1591 1244 HOH   HOH A . 
EA 11 HOH   192  1592 507  HOH   HOH A . 
EA 11 HOH   193  1593 876  HOH   HOH A . 
EA 11 HOH   194  1594 1171 HOH   HOH A . 
EA 11 HOH   195  1595 198  HOH   HOH A . 
EA 11 HOH   196  1596 1202 HOH   HOH A . 
EA 11 HOH   197  1597 1990 HOH   HOH A . 
EA 11 HOH   198  1598 814  HOH   HOH A . 
EA 11 HOH   199  1599 504  HOH   HOH A . 
EA 11 HOH   200  1600 215  HOH   HOH A . 
EA 11 HOH   201  1601 1214 HOH   HOH A . 
EA 11 HOH   202  1602 581  HOH   HOH A . 
EA 11 HOH   203  1603 1347 HOH   HOH A . 
EA 11 HOH   204  1604 1659 HOH   HOH A . 
EA 11 HOH   205  1605 137  HOH   HOH A . 
EA 11 HOH   206  1606 635  HOH   HOH A . 
EA 11 HOH   207  1607 217  HOH   HOH A . 
EA 11 HOH   208  1608 95   HOH   HOH A . 
EA 11 HOH   209  1609 670  HOH   HOH A . 
EA 11 HOH   210  1610 544  HOH   HOH A . 
EA 11 HOH   211  1611 1439 HOH   HOH A . 
EA 11 HOH   212  1612 373  HOH   HOH A . 
EA 11 HOH   213  1613 1301 HOH   HOH A . 
EA 11 HOH   214  1614 1302 HOH   HOH A . 
EA 11 HOH   215  1615 1023 HOH   HOH A . 
EA 11 HOH   216  1616 645  HOH   HOH A . 
EA 11 HOH   217  1617 306  HOH   HOH A . 
EA 11 HOH   218  1618 51   HOH   HOH A . 
EA 11 HOH   219  1619 271  HOH   HOH A . 
EA 11 HOH   220  1620 120  HOH   HOH A . 
EA 11 HOH   221  1621 586  HOH   HOH A . 
EA 11 HOH   222  1622 1418 HOH   HOH A . 
EA 11 HOH   223  1623 1084 HOH   HOH A . 
EA 11 HOH   224  1624 105  HOH   HOH A . 
EA 11 HOH   225  1625 55   HOH   HOH A . 
EA 11 HOH   226  1626 1658 HOH   HOH A . 
EA 11 HOH   227  1627 867  HOH   HOH A . 
EA 11 HOH   228  1628 558  HOH   HOH A . 
EA 11 HOH   229  1629 1135 HOH   HOH A . 
EA 11 HOH   230  1630 1259 HOH   HOH A . 
EA 11 HOH   231  1631 388  HOH   HOH A . 
EA 11 HOH   232  1632 1476 HOH   HOH A . 
EA 11 HOH   233  1633 2150 HOH   HOH A . 
EA 11 HOH   234  1634 1109 HOH   HOH A . 
EA 11 HOH   235  1635 133  HOH   HOH A . 
EA 11 HOH   236  1636 1997 HOH   HOH A . 
EA 11 HOH   237  1637 277  HOH   HOH A . 
EA 11 HOH   238  1638 1605 HOH   HOH A . 
EA 11 HOH   239  1639 1115 HOH   HOH A . 
EA 11 HOH   240  1640 1433 HOH   HOH A . 
EA 11 HOH   241  1641 195  HOH   HOH A . 
EA 11 HOH   242  1642 662  HOH   HOH A . 
EA 11 HOH   243  1643 1222 HOH   HOH A . 
EA 11 HOH   244  1644 737  HOH   HOH A . 
EA 11 HOH   245  1645 219  HOH   HOH A . 
EA 11 HOH   246  1646 1447 HOH   HOH A . 
EA 11 HOH   247  1647 244  HOH   HOH A . 
EA 11 HOH   248  1648 134  HOH   HOH A . 
EA 11 HOH   249  1649 1033 HOH   HOH A . 
EA 11 HOH   250  1650 748  HOH   HOH A . 
EA 11 HOH   251  1651 2162 HOH   HOH A . 
EA 11 HOH   252  1652 418  HOH   HOH A . 
EA 11 HOH   253  1653 2166 HOH   HOH A . 
EA 11 HOH   254  1654 305  HOH   HOH A . 
EA 11 HOH   255  1655 142  HOH   HOH A . 
EA 11 HOH   256  1656 1812 HOH   HOH A . 
EA 11 HOH   257  1657 261  HOH   HOH A . 
EA 11 HOH   258  1658 211  HOH   HOH A . 
EA 11 HOH   259  1659 1900 HOH   HOH A . 
EA 11 HOH   260  1660 477  HOH   HOH A . 
EA 11 HOH   261  1661 170  HOH   HOH A . 
EA 11 HOH   262  1662 2217 HOH   HOH A . 
EA 11 HOH   263  1663 556  HOH   HOH A . 
EA 11 HOH   264  1664 1629 HOH   HOH A . 
EA 11 HOH   265  1665 1864 HOH   HOH A . 
EA 11 HOH   266  1666 1105 HOH   HOH A . 
EA 11 HOH   267  1667 482  HOH   HOH A . 
EA 11 HOH   268  1668 1543 HOH   HOH A . 
EA 11 HOH   269  1669 1281 HOH   HOH A . 
EA 11 HOH   270  1670 955  HOH   HOH A . 
EA 11 HOH   271  1671 901  HOH   HOH A . 
EA 11 HOH   272  1672 2140 HOH   HOH A . 
EA 11 HOH   273  1673 141  HOH   HOH A . 
EA 11 HOH   274  1674 1238 HOH   HOH A . 
EA 11 HOH   275  1675 577  HOH   HOH A . 
EA 11 HOH   276  1676 50   HOH   HOH A . 
EA 11 HOH   277  1677 1423 HOH   HOH A . 
EA 11 HOH   278  1678 937  HOH   HOH A . 
EA 11 HOH   279  1679 251  HOH   HOH A . 
EA 11 HOH   280  1680 2060 HOH   HOH A . 
EA 11 HOH   281  1681 104  HOH   HOH A . 
EA 11 HOH   282  1682 1415 HOH   HOH A . 
EA 11 HOH   283  1683 342  HOH   HOH A . 
EA 11 HOH   284  1684 330  HOH   HOH A . 
EA 11 HOH   285  1685 1988 HOH   HOH A . 
EA 11 HOH   286  1686 390  HOH   HOH A . 
EA 11 HOH   287  1687 164  HOH   HOH A . 
EA 11 HOH   288  1688 904  HOH   HOH A . 
EA 11 HOH   289  1689 979  HOH   HOH A . 
EA 11 HOH   290  1690 1124 HOH   HOH A . 
EA 11 HOH   291  1691 366  HOH   HOH A . 
EA 11 HOH   292  1692 338  HOH   HOH A . 
EA 11 HOH   293  1693 522  HOH   HOH A . 
EA 11 HOH   294  1694 17   HOH   HOH A . 
EA 11 HOH   295  1695 377  HOH   HOH A . 
EA 11 HOH   296  1696 1266 HOH   HOH A . 
EA 11 HOH   297  1697 212  HOH   HOH A . 
EA 11 HOH   298  1698 475  HOH   HOH A . 
EA 11 HOH   299  1699 2022 HOH   HOH A . 
EA 11 HOH   300  1700 732  HOH   HOH A . 
EA 11 HOH   301  1701 1139 HOH   HOH A . 
EA 11 HOH   302  1702 753  HOH   HOH A . 
EA 11 HOH   303  1703 1353 HOH   HOH A . 
EA 11 HOH   304  1704 64   HOH   HOH A . 
EA 11 HOH   305  1705 984  HOH   HOH A . 
EA 11 HOH   306  1706 1688 HOH   HOH A . 
EA 11 HOH   307  1707 1083 HOH   HOH A . 
EA 11 HOH   308  1708 1594 HOH   HOH A . 
EA 11 HOH   309  1709 1331 HOH   HOH A . 
EA 11 HOH   310  1710 1212 HOH   HOH A . 
EA 11 HOH   311  1711 780  HOH   HOH A . 
EA 11 HOH   312  1712 1045 HOH   HOH A . 
EA 11 HOH   313  1713 203  HOH   HOH A . 
EA 11 HOH   314  1714 127  HOH   HOH A . 
EA 11 HOH   315  1715 1385 HOH   HOH A . 
EA 11 HOH   316  1716 661  HOH   HOH A . 
EA 11 HOH   317  1717 628  HOH   HOH A . 
EA 11 HOH   318  1718 58   HOH   HOH A . 
EA 11 HOH   319  1719 786  HOH   HOH A . 
EA 11 HOH   320  1720 386  HOH   HOH A . 
EA 11 HOH   321  1721 303  HOH   HOH A . 
EA 11 HOH   322  1722 434  HOH   HOH A . 
EA 11 HOH   323  1723 578  HOH   HOH A . 
EA 11 HOH   324  1724 535  HOH   HOH A . 
EA 11 HOH   325  1725 1052 HOH   HOH A . 
EA 11 HOH   326  1726 250  HOH   HOH A . 
EA 11 HOH   327  1727 1929 HOH   HOH A . 
EA 11 HOH   328  1728 1074 HOH   HOH A . 
EA 11 HOH   329  1729 324  HOH   HOH A . 
EA 11 HOH   330  1730 1043 HOH   HOH A . 
EA 11 HOH   331  1731 1396 HOH   HOH A . 
EA 11 HOH   332  1732 395  HOH   HOH A . 
EA 11 HOH   333  1733 437  HOH   HOH A . 
EA 11 HOH   334  1734 36   HOH   HOH A . 
EA 11 HOH   335  1735 1790 HOH   HOH A . 
EA 11 HOH   336  1736 40   HOH   HOH A . 
EA 11 HOH   337  1737 1335 HOH   HOH A . 
EA 11 HOH   338  1738 1191 HOH   HOH A . 
EA 11 HOH   339  1739 2091 HOH   HOH A . 
EA 11 HOH   340  1740 343  HOH   HOH A . 
EA 11 HOH   341  1741 1643 HOH   HOH A . 
EA 11 HOH   342  1742 2127 HOH   HOH A . 
EA 11 HOH   343  1743 2058 HOH   HOH A . 
EA 11 HOH   344  1744 1062 HOH   HOH A . 
EA 11 HOH   345  1745 1260 HOH   HOH A . 
EA 11 HOH   346  1746 307  HOH   HOH A . 
EA 11 HOH   347  1747 699  HOH   HOH A . 
EA 11 HOH   348  1748 1857 HOH   HOH A . 
EA 11 HOH   349  1749 829  HOH   HOH A . 
EA 11 HOH   350  1750 1549 HOH   HOH A . 
EA 11 HOH   351  1751 1144 HOH   HOH A . 
EA 11 HOH   352  1752 345  HOH   HOH A . 
EA 11 HOH   353  1753 1456 HOH   HOH A . 
EA 11 HOH   354  1754 847  HOH   HOH A . 
EA 11 HOH   355  1755 1022 HOH   HOH A . 
EA 11 HOH   356  1756 314  HOH   HOH A . 
EA 11 HOH   357  1757 413  HOH   HOH A . 
EA 11 HOH   358  1758 757  HOH   HOH A . 
EA 11 HOH   359  1759 1175 HOH   HOH A . 
EA 11 HOH   360  1760 798  HOH   HOH A . 
EA 11 HOH   361  1761 316  HOH   HOH A . 
EA 11 HOH   362  1762 65   HOH   HOH A . 
EA 11 HOH   363  1763 2135 HOH   HOH A . 
EA 11 HOH   364  1764 969  HOH   HOH A . 
EA 11 HOH   365  1765 681  HOH   HOH A . 
EA 11 HOH   366  1766 890  HOH   HOH A . 
EA 11 HOH   367  1767 651  HOH   HOH A . 
EA 11 HOH   368  1768 840  HOH   HOH A . 
EA 11 HOH   369  1769 801  HOH   HOH A . 
EA 11 HOH   370  1770 486  HOH   HOH A . 
EA 11 HOH   371  1771 1987 HOH   HOH A . 
EA 11 HOH   372  1772 1247 HOH   HOH A . 
EA 11 HOH   373  1773 1067 HOH   HOH A . 
EA 11 HOH   374  1774 433  HOH   HOH A . 
EA 11 HOH   375  1775 1560 HOH   HOH A . 
EA 11 HOH   376  1776 740  HOH   HOH A . 
EA 11 HOH   377  1777 2158 HOH   HOH A . 
EA 11 HOH   378  1778 1048 HOH   HOH A . 
EA 11 HOH   379  1779 218  HOH   HOH A . 
EA 11 HOH   380  1780 1187 HOH   HOH A . 
EA 11 HOH   381  1781 680  HOH   HOH A . 
EA 11 HOH   382  1782 247  HOH   HOH A . 
EA 11 HOH   383  1783 1006 HOH   HOH A . 
EA 11 HOH   384  1784 427  HOH   HOH A . 
EA 11 HOH   385  1785 568  HOH   HOH A . 
EA 11 HOH   386  1786 41   HOH   HOH A . 
EA 11 HOH   387  1787 372  HOH   HOH A . 
EA 11 HOH   388  1788 91   HOH   HOH A . 
EA 11 HOH   389  1789 1269 HOH   HOH A . 
EA 11 HOH   390  1790 659  HOH   HOH A . 
EA 11 HOH   391  1791 694  HOH   HOH A . 
EA 11 HOH   392  1792 796  HOH   HOH A . 
EA 11 HOH   393  1793 485  HOH   HOH A . 
EA 11 HOH   394  1794 370  HOH   HOH A . 
EA 11 HOH   395  1795 1695 HOH   HOH A . 
EA 11 HOH   396  1796 676  HOH   HOH A . 
EA 11 HOH   397  1797 492  HOH   HOH A . 
EA 11 HOH   398  1798 1573 HOH   HOH A . 
EA 11 HOH   399  1799 181  HOH   HOH A . 
EA 11 HOH   400  1800 1410 HOH   HOH A . 
EA 11 HOH   401  1801 506  HOH   HOH A . 
EA 11 HOH   402  1802 950  HOH   HOH A . 
EA 11 HOH   403  1803 686  HOH   HOH A . 
EA 11 HOH   404  1804 48   HOH   HOH A . 
EA 11 HOH   405  1805 1255 HOH   HOH A . 
EA 11 HOH   406  1806 764  HOH   HOH A . 
EA 11 HOH   407  1807 1149 HOH   HOH A . 
EA 11 HOH   408  1808 1585 HOH   HOH A . 
EA 11 HOH   409  1809 328  HOH   HOH A . 
EA 11 HOH   410  1810 671  HOH   HOH A . 
EA 11 HOH   411  1811 563  HOH   HOH A . 
EA 11 HOH   412  1812 627  HOH   HOH A . 
EA 11 HOH   413  1813 1654 HOH   HOH A . 
EA 11 HOH   414  1814 469  HOH   HOH A . 
EA 11 HOH   415  1815 98   HOH   HOH A . 
EA 11 HOH   416  1816 510  HOH   HOH A . 
EA 11 HOH   417  1817 272  HOH   HOH A . 
EA 11 HOH   418  1818 1528 HOH   HOH A . 
EA 11 HOH   419  1819 168  HOH   HOH A . 
EA 11 HOH   420  1820 1384 HOH   HOH A . 
EA 11 HOH   421  1821 766  HOH   HOH A . 
EA 11 HOH   422  1822 758  HOH   HOH A . 
EA 11 HOH   423  1823 928  HOH   HOH A . 
EA 11 HOH   424  1824 1122 HOH   HOH A . 
EA 11 HOH   425  1825 1007 HOH   HOH A . 
EA 11 HOH   426  1826 1946 HOH   HOH A . 
EA 11 HOH   427  1827 587  HOH   HOH A . 
EA 11 HOH   428  1828 1287 HOH   HOH A . 
EA 11 HOH   429  1829 73   HOH   HOH A . 
EA 11 HOH   430  1830 309  HOH   HOH A . 
EA 11 HOH   431  1831 223  HOH   HOH A . 
EA 11 HOH   432  1832 891  HOH   HOH A . 
EA 11 HOH   433  1833 77   HOH   HOH A . 
EA 11 HOH   434  1834 189  HOH   HOH A . 
EA 11 HOH   435  1835 2024 HOH   HOH A . 
EA 11 HOH   436  1836 2049 HOH   HOH A . 
EA 11 HOH   437  1837 1961 HOH   HOH A . 
EA 11 HOH   438  1838 503  HOH   HOH A . 
EA 11 HOH   439  1839 194  HOH   HOH A . 
EA 11 HOH   440  1840 1230 HOH   HOH A . 
EA 11 HOH   441  1841 1155 HOH   HOH A . 
EA 11 HOH   442  1842 717  HOH   HOH A . 
EA 11 HOH   443  1843 546  HOH   HOH A . 
EA 11 HOH   444  1844 317  HOH   HOH A . 
EA 11 HOH   445  1845 1013 HOH   HOH A . 
EA 11 HOH   446  1846 20   HOH   HOH A . 
EA 11 HOH   447  1847 489  HOH   HOH A . 
EA 11 HOH   448  1848 359  HOH   HOH A . 
EA 11 HOH   449  1849 396  HOH   HOH A . 
EA 11 HOH   450  1850 691  HOH   HOH A . 
EA 11 HOH   451  1851 724  HOH   HOH A . 
EA 11 HOH   452  1852 266  HOH   HOH A . 
EA 11 HOH   453  1853 61   HOH   HOH A . 
EA 11 HOH   454  1854 360  HOH   HOH A . 
EA 11 HOH   455  1855 710  HOH   HOH A . 
EA 11 HOH   456  1856 908  HOH   HOH A . 
EA 11 HOH   457  1857 1103 HOH   HOH A . 
EA 11 HOH   458  1858 647  HOH   HOH A . 
EA 11 HOH   459  1859 1336 HOH   HOH A . 
EA 11 HOH   460  1860 772  HOH   HOH A . 
EA 11 HOH   461  1861 862  HOH   HOH A . 
EA 11 HOH   462  1862 1958 HOH   HOH A . 
EA 11 HOH   463  1863 86   HOH   HOH A . 
EA 11 HOH   464  1864 397  HOH   HOH A . 
EA 11 HOH   465  1865 518  HOH   HOH A . 
EA 11 HOH   466  1866 290  HOH   HOH A . 
EA 11 HOH   467  1867 822  HOH   HOH A . 
EA 11 HOH   468  1868 1868 HOH   HOH A . 
EA 11 HOH   469  1869 180  HOH   HOH A . 
EA 11 HOH   470  1870 281  HOH   HOH A . 
EA 11 HOH   471  1871 1159 HOH   HOH A . 
EA 11 HOH   472  1872 412  HOH   HOH A . 
EA 11 HOH   473  1873 889  HOH   HOH A . 
EA 11 HOH   474  1874 808  HOH   HOH A . 
EA 11 HOH   475  1875 1037 HOH   HOH A . 
EA 11 HOH   476  1876 1425 HOH   HOH A . 
EA 11 HOH   477  1877 214  HOH   HOH A . 
EA 11 HOH   478  1878 582  HOH   HOH A . 
EA 11 HOH   479  1879 399  HOH   HOH A . 
EA 11 HOH   480  1880 1432 HOH   HOH A . 
EA 11 HOH   481  1881 605  HOH   HOH A . 
EA 11 HOH   482  1882 148  HOH   HOH A . 
EA 11 HOH   483  1883 1579 HOH   HOH A . 
EA 11 HOH   484  1884 1690 HOH   HOH A . 
EA 11 HOH   485  1885 592  HOH   HOH A . 
EA 11 HOH   486  1886 590  HOH   HOH A . 
EA 11 HOH   487  1887 905  HOH   HOH A . 
EA 11 HOH   488  1888 836  HOH   HOH A . 
EA 11 HOH   489  1889 774  HOH   HOH A . 
EA 11 HOH   490  1890 646  HOH   HOH A . 
EA 11 HOH   491  1891 209  HOH   HOH A . 
EA 11 HOH   492  1892 978  HOH   HOH A . 
EA 11 HOH   493  1893 1604 HOH   HOH A . 
EA 11 HOH   494  1894 638  HOH   HOH A . 
EA 11 HOH   495  1895 1370 HOH   HOH A . 
EA 11 HOH   496  1896 2021 HOH   HOH A . 
EA 11 HOH   497  1897 1117 HOH   HOH A . 
EA 11 HOH   498  1898 599  HOH   HOH A . 
EA 11 HOH   499  1899 407  HOH   HOH A . 
EA 11 HOH   500  1900 75   HOH   HOH A . 
EA 11 HOH   501  1901 1172 HOH   HOH A . 
EA 11 HOH   502  1902 122  HOH   HOH A . 
EA 11 HOH   503  1903 226  HOH   HOH A . 
EA 11 HOH   504  1904 188  HOH   HOH A . 
EA 11 HOH   505  1905 249  HOH   HOH A . 
EA 11 HOH   506  1906 1559 HOH   HOH A . 
EA 11 HOH   507  1907 672  HOH   HOH A . 
EA 11 HOH   508  1908 1717 HOH   HOH A . 
EA 11 HOH   509  1909 289  HOH   HOH A . 
EA 11 HOH   510  1910 476  HOH   HOH A . 
EA 11 HOH   511  1911 2010 HOH   HOH A . 
EA 11 HOH   512  1912 2063 HOH   HOH A . 
EA 11 HOH   513  1913 1019 HOH   HOH A . 
EA 11 HOH   514  1914 872  HOH   HOH A . 
EA 11 HOH   515  1915 112  HOH   HOH A . 
EA 11 HOH   516  1916 1855 HOH   HOH A . 
EA 11 HOH   517  1917 1028 HOH   HOH A . 
EA 11 HOH   518  1918 2082 HOH   HOH A . 
EA 11 HOH   519  1919 634  HOH   HOH A . 
EA 11 HOH   520  1920 37   HOH   HOH A . 
EA 11 HOH   521  1921 961  HOH   HOH A . 
EA 11 HOH   522  1922 648  HOH   HOH A . 
EA 11 HOH   523  1923 517  HOH   HOH A . 
EA 11 HOH   524  1924 649  HOH   HOH A . 
EA 11 HOH   525  1925 1035 HOH   HOH A . 
EA 11 HOH   526  1926 1056 HOH   HOH A . 
EA 11 HOH   527  1927 1286 HOH   HOH A . 
EA 11 HOH   528  1928 163  HOH   HOH A . 
EA 11 HOH   529  1929 868  HOH   HOH A . 
EA 11 HOH   530  1930 997  HOH   HOH A . 
EA 11 HOH   531  1931 1106 HOH   HOH A . 
EA 11 HOH   532  1932 1505 HOH   HOH A . 
EA 11 HOH   533  1933 1779 HOH   HOH A . 
EA 11 HOH   534  1934 858  HOH   HOH A . 
EA 11 HOH   535  1935 479  HOH   HOH A . 
EA 11 HOH   536  1936 1477 HOH   HOH A . 
EA 11 HOH   537  1937 1744 HOH   HOH A . 
EA 11 HOH   538  1938 1280 HOH   HOH A . 
EA 11 HOH   539  1939 1756 HOH   HOH A . 
EA 11 HOH   540  1940 574  HOH   HOH A . 
EA 11 HOH   541  1941 329  HOH   HOH A . 
EA 11 HOH   542  1942 2139 HOH   HOH A . 
EA 11 HOH   543  1943 555  HOH   HOH A . 
EA 11 HOH   544  1944 1361 HOH   HOH A . 
EA 11 HOH   545  1945 1024 HOH   HOH A . 
EA 11 HOH   546  1946 1107 HOH   HOH A . 
EA 11 HOH   547  1947 1196 HOH   HOH A . 
EA 11 HOH   548  1948 701  HOH   HOH A . 
EA 11 HOH   549  1949 633  HOH   HOH A . 
EA 11 HOH   550  1950 174  HOH   HOH A . 
EA 11 HOH   551  1951 2032 HOH   HOH A . 
EA 11 HOH   552  1952 1891 HOH   HOH A . 
EA 11 HOH   553  1953 611  HOH   HOH A . 
EA 11 HOH   554  1954 392  HOH   HOH A . 
EA 11 HOH   555  1955 1593 HOH   HOH A . 
EA 11 HOH   556  1956 2159 HOH   HOH A . 
EA 11 HOH   557  1957 1638 HOH   HOH A . 
EA 11 HOH   558  1958 960  HOH   HOH A . 
EA 11 HOH   559  1959 320  HOH   HOH A . 
EA 11 HOH   560  1960 845  HOH   HOH A . 
EA 11 HOH   561  1961 692  HOH   HOH A . 
EA 11 HOH   562  1962 1374 HOH   HOH A . 
EA 11 HOH   563  1963 415  HOH   HOH A . 
EA 11 HOH   564  1964 1906 HOH   HOH A . 
EA 11 HOH   565  1965 791  HOH   HOH A . 
EA 11 HOH   566  1966 1547 HOH   HOH A . 
EA 11 HOH   567  1967 617  HOH   HOH A . 
EA 11 HOH   568  1968 835  HOH   HOH A . 
EA 11 HOH   569  1969 465  HOH   HOH A . 
EA 11 HOH   570  1970 2232 HOH   HOH A . 
EA 11 HOH   571  1971 783  HOH   HOH A . 
EA 11 HOH   572  1972 1223 HOH   HOH A . 
EA 11 HOH   573  1973 1136 HOH   HOH A . 
EA 11 HOH   574  1974 378  HOH   HOH A . 
EA 11 HOH   575  1975 1583 HOH   HOH A . 
EA 11 HOH   576  1976 705  HOH   HOH A . 
EA 11 HOH   577  1977 222  HOH   HOH A . 
EA 11 HOH   578  1978 505  HOH   HOH A . 
EA 11 HOH   579  1979 813  HOH   HOH A . 
EA 11 HOH   580  1980 254  HOH   HOH A . 
EA 11 HOH   581  1981 2234 HOH   HOH A . 
EA 11 HOH   582  1982 1846 HOH   HOH A . 
EA 11 HOH   583  1983 1666 HOH   HOH A . 
EA 11 HOH   584  1984 516  HOH   HOH A . 
EA 11 HOH   585  1985 43   HOH   HOH A . 
EA 11 HOH   586  1986 1681 HOH   HOH A . 
EA 11 HOH   587  1987 1014 HOH   HOH A . 
EA 11 HOH   588  1988 637  HOH   HOH A . 
EA 11 HOH   589  1989 515  HOH   HOH A . 
EA 11 HOH   590  1990 363  HOH   HOH A . 
EA 11 HOH   591  1991 1288 HOH   HOH A . 
EA 11 HOH   592  1992 1369 HOH   HOH A . 
EA 11 HOH   593  1993 239  HOH   HOH A . 
EA 11 HOH   594  1994 90   HOH   HOH A . 
EA 11 HOH   595  1995 1716 HOH   HOH A . 
EA 11 HOH   596  1996 246  HOH   HOH A . 
EA 11 HOH   597  1997 1093 HOH   HOH A . 
EA 11 HOH   598  1998 966  HOH   HOH A . 
EA 11 HOH   599  1999 865  HOH   HOH A . 
EA 11 HOH   600  2000 1176 HOH   HOH A . 
EA 11 HOH   601  2001 460  HOH   HOH A . 
EA 11 HOH   602  2002 708  HOH   HOH A . 
EA 11 HOH   603  2003 150  HOH   HOH A . 
EA 11 HOH   604  2004 490  HOH   HOH A . 
EA 11 HOH   605  2005 1564 HOH   HOH A . 
EA 11 HOH   606  2006 746  HOH   HOH A . 
EA 11 HOH   607  2007 1819 HOH   HOH A . 
EA 11 HOH   608  2008 4    HOH   HOH A . 
EA 11 HOH   609  2009 202  HOH   HOH A . 
EA 11 HOH   610  2010 685  HOH   HOH A . 
EA 11 HOH   611  2011 1462 HOH   HOH A . 
EA 11 HOH   612  2012 607  HOH   HOH A . 
EA 11 HOH   613  2013 2041 HOH   HOH A . 
EA 11 HOH   614  2014 921  HOH   HOH A . 
EA 11 HOH   615  2015 357  HOH   HOH A . 
EA 11 HOH   616  2016 1300 HOH   HOH A . 
EA 11 HOH   617  2017 866  HOH   HOH A . 
EA 11 HOH   618  2018 1670 HOH   HOH A . 
EA 11 HOH   619  2019 1264 HOH   HOH A . 
EA 11 HOH   620  2020 800  HOH   HOH A . 
EA 11 HOH   621  2021 502  HOH   HOH A . 
EA 11 HOH   622  2022 1618 HOH   HOH A . 
EA 11 HOH   623  2023 1780 HOH   HOH A . 
EA 11 HOH   624  2024 284  HOH   HOH A . 
EA 11 HOH   625  2025 591  HOH   HOH A . 
EA 11 HOH   626  2026 2155 HOH   HOH A . 
EA 11 HOH   627  2027 52   HOH   HOH A . 
EA 11 HOH   628  2028 1092 HOH   HOH A . 
EA 11 HOH   629  2029 2074 HOH   HOH A . 
EA 11 HOH   630  2030 534  HOH   HOH A . 
EA 11 HOH   631  2031 1501 HOH   HOH A . 
EA 11 HOH   632  2032 1467 HOH   HOH A . 
EA 11 HOH   633  2033 1419 HOH   HOH A . 
EA 11 HOH   634  2034 1235 HOH   HOH A . 
EA 11 HOH   635  2035 1121 HOH   HOH A . 
EA 11 HOH   636  2036 1986 HOH   HOH A . 
EA 11 HOH   637  2037 275  HOH   HOH A . 
EA 11 HOH   638  2038 915  HOH   HOH A . 
EA 11 HOH   639  2039 84   HOH   HOH A . 
EA 11 HOH   640  2040 918  HOH   HOH A . 
EA 11 HOH   641  2041 442  HOH   HOH A . 
EA 11 HOH   642  2042 1588 HOH   HOH A . 
EA 11 HOH   643  2043 1592 HOH   HOH A . 
EA 11 HOH   644  2044 975  HOH   HOH A . 
EA 11 HOH   645  2045 1795 HOH   HOH A . 
EA 11 HOH   646  2046 2017 HOH   HOH A . 
EA 11 HOH   647  2047 667  HOH   HOH A . 
EA 11 HOH   648  2048 585  HOH   HOH A . 
EA 11 HOH   649  2049 511  HOH   HOH A . 
EA 11 HOH   650  2050 438  HOH   HOH A . 
EA 11 HOH   651  2051 420  HOH   HOH A . 
EA 11 HOH   652  2052 1081 HOH   HOH A . 
EA 11 HOH   653  2053 547  HOH   HOH A . 
EA 11 HOH   654  2054 326  HOH   HOH A . 
EA 11 HOH   655  2055 1314 HOH   HOH A . 
EA 11 HOH   656  2056 1324 HOH   HOH A . 
EA 11 HOH   657  2057 1971 HOH   HOH A . 
EA 11 HOH   658  2058 1950 HOH   HOH A . 
EA 11 HOH   659  2059 1094 HOH   HOH A . 
EA 11 HOH   660  2060 1420 HOH   HOH A . 
EA 11 HOH   661  2061 1520 HOH   HOH A . 
EA 11 HOH   662  2062 1315 HOH   HOH A . 
EA 11 HOH   663  2063 618  HOH   HOH A . 
EA 11 HOH   664  2064 1913 HOH   HOH A . 
EA 11 HOH   665  2065 2128 HOH   HOH A . 
EA 11 HOH   666  2066 1792 HOH   HOH A . 
EA 11 HOH   667  2067 2051 HOH   HOH A . 
EA 11 HOH   668  2068 755  HOH   HOH A . 
EA 11 HOH   669  2069 2030 HOH   HOH A . 
EA 11 HOH   670  2070 795  HOH   HOH A . 
EA 11 HOH   671  2071 1068 HOH   HOH A . 
EA 11 HOH   672  2072 2105 HOH   HOH A . 
EA 11 HOH   673  2073 1597 HOH   HOH A . 
EA 11 HOH   674  2074 1910 HOH   HOH A . 
EA 11 HOH   675  2075 1686 HOH   HOH A . 
EA 11 HOH   676  2076 1239 HOH   HOH A . 
EA 11 HOH   677  2077 411  HOH   HOH A . 
EA 11 HOH   678  2078 1232 HOH   HOH A . 
EA 11 HOH   679  2079 703  HOH   HOH A . 
EA 11 HOH   680  2080 1101 HOH   HOH A . 
EA 11 HOH   681  2081 368  HOH   HOH A . 
EA 11 HOH   682  2082 1977 HOH   HOH A . 
EA 11 HOH   683  2083 819  HOH   HOH A . 
EA 11 HOH   684  2084 1661 HOH   HOH A . 
EA 11 HOH   685  2085 677  HOH   HOH A . 
EA 11 HOH   686  2086 1460 HOH   HOH A . 
EA 11 HOH   687  2087 1861 HOH   HOH A . 
EA 11 HOH   688  2088 2006 HOH   HOH A . 
EA 11 HOH   689  2089 2052 HOH   HOH A . 
EA 11 HOH   690  2090 1069 HOH   HOH A . 
EA 11 HOH   691  2091 785  HOH   HOH A . 
EA 11 HOH   692  2092 1116 HOH   HOH A . 
EA 11 HOH   693  2093 2123 HOH   HOH A . 
EA 11 HOH   694  2094 571  HOH   HOH A . 
EA 11 HOH   695  2095 1129 HOH   HOH A . 
EA 11 HOH   696  2096 1802 HOH   HOH A . 
EA 11 HOH   697  2097 1091 HOH   HOH A . 
EA 11 HOH   698  2098 2089 HOH   HOH A . 
EA 11 HOH   699  2099 702  HOH   HOH A . 
EA 11 HOH   700  2100 405  HOH   HOH A . 
EA 11 HOH   701  2101 848  HOH   HOH A . 
EA 11 HOH   702  2102 1096 HOH   HOH A . 
EA 11 HOH   703  2103 1960 HOH   HOH A . 
EA 11 HOH   704  2104 341  HOH   HOH A . 
EA 11 HOH   705  2105 333  HOH   HOH A . 
EA 11 HOH   706  2106 881  HOH   HOH A . 
EA 11 HOH   707  2107 190  HOH   HOH A . 
EA 11 HOH   708  2108 2132 HOH   HOH A . 
EA 11 HOH   709  2109 1726 HOH   HOH A . 
EA 11 HOH   710  2110 384  HOH   HOH A . 
EA 11 HOH   711  2111 837  HOH   HOH A . 
EA 11 HOH   712  2112 144  HOH   HOH A . 
EA 11 HOH   713  2113 2136 HOH   HOH A . 
EA 11 HOH   714  2114 1646 HOH   HOH A . 
EA 11 HOH   715  2115 1020 HOH   HOH A . 
EA 11 HOH   716  2116 1274 HOH   HOH A . 
EA 11 HOH   717  2117 1515 HOH   HOH A . 
EA 11 HOH   718  2118 286  HOH   HOH A . 
EA 11 HOH   719  2119 1207 HOH   HOH A . 
EA 11 HOH   720  2120 1416 HOH   HOH A . 
EA 11 HOH   721  2121 268  HOH   HOH A . 
EA 11 HOH   722  2122 884  HOH   HOH A . 
EA 11 HOH   723  2123 1511 HOH   HOH A . 
EA 11 HOH   724  2124 1536 HOH   HOH A . 
EA 11 HOH   725  2125 879  HOH   HOH A . 
EA 11 HOH   726  2126 789  HOH   HOH A . 
EA 11 HOH   727  2127 332  HOH   HOH A . 
EA 11 HOH   728  2128 1509 HOH   HOH A . 
EA 11 HOH   729  2129 990  HOH   HOH A . 
EA 11 HOH   730  2130 1496 HOH   HOH A . 
EA 11 HOH   731  2131 1570 HOH   HOH A . 
EA 11 HOH   732  2132 2109 HOH   HOH A . 
EA 11 HOH   733  2133 353  HOH   HOH A . 
EA 11 HOH   734  2134 1962 HOH   HOH A . 
EA 11 HOH   735  2135 745  HOH   HOH A . 
EA 11 HOH   736  2136 622  HOH   HOH A . 
EA 11 HOH   737  2137 1426 HOH   HOH A . 
EA 11 HOH   738  2138 232  HOH   HOH A . 
EA 11 HOH   739  2139 1521 HOH   HOH A . 
EA 11 HOH   740  2140 59   HOH   HOH A . 
EA 11 HOH   741  2141 730  HOH   HOH A . 
EA 11 HOH   742  2142 2124 HOH   HOH A . 
EA 11 HOH   743  2143 958  HOH   HOH A . 
EA 11 HOH   744  2144 533  HOH   HOH A . 
EA 11 HOH   745  2145 1390 HOH   HOH A . 
EA 11 HOH   746  2146 1998 HOH   HOH A . 
EA 11 HOH   747  2147 204  HOH   HOH A . 
EA 11 HOH   748  2148 1931 HOH   HOH A . 
EA 11 HOH   749  2149 1586 HOH   HOH A . 
EA 11 HOH   750  2150 1041 HOH   HOH A . 
EA 11 HOH   751  2151 88   HOH   HOH A . 
EA 11 HOH   752  2152 985  HOH   HOH A . 
EA 11 HOH   753  2153 1379 HOH   HOH A . 
EA 11 HOH   754  2154 459  HOH   HOH A . 
EA 11 HOH   755  2155 2009 HOH   HOH A . 
EA 11 HOH   756  2156 1815 HOH   HOH A . 
EA 11 HOH   757  2157 1667 HOH   HOH A . 
EA 11 HOH   758  2158 1190 HOH   HOH A . 
EA 11 HOH   759  2159 491  HOH   HOH A . 
EA 11 HOH   760  2160 2016 HOH   HOH A . 
EA 11 HOH   761  2161 1677 HOH   HOH A . 
EA 11 HOH   762  2162 816  HOH   HOH A . 
EA 11 HOH   763  2163 2185 HOH   HOH A . 
EA 11 HOH   764  2164 2207 HOH   HOH A . 
EA 11 HOH   765  2165 1827 HOH   HOH A . 
EA 11 HOH   766  2166 1689 HOH   HOH A . 
EA 11 HOH   767  2167 593  HOH   HOH A . 
EA 11 HOH   768  2168 1339 HOH   HOH A . 
EA 11 HOH   769  2169 1352 HOH   HOH A . 
EA 11 HOH   770  2170 532  HOH   HOH A . 
EA 11 HOH   771  2171 560  HOH   HOH A . 
EA 11 HOH   772  2172 2110 HOH   HOH A . 
EA 11 HOH   773  2173 1424 HOH   HOH A . 
EA 11 HOH   774  2174 722  HOH   HOH A . 
EA 11 HOH   775  2175 2134 HOH   HOH A . 
EA 11 HOH   776  2176 1898 HOH   HOH A . 
EA 11 HOH   777  2177 1363 HOH   HOH A . 
EA 11 HOH   778  2178 1267 HOH   HOH A . 
EA 11 HOH   779  2179 1591 HOH   HOH A . 
EA 11 HOH   780  2180 1818 HOH   HOH A . 
EA 11 HOH   781  2181 1872 HOH   HOH A . 
EA 11 HOH   782  2182 1949 HOH   HOH A . 
EA 11 HOH   783  2183 1721 HOH   HOH A . 
EA 11 HOH   784  2184 564  HOH   HOH A . 
EA 11 HOH   785  2185 1565 HOH   HOH A . 
EA 11 HOH   786  2186 743  HOH   HOH A . 
EA 11 HOH   787  2187 986  HOH   HOH A . 
EA 11 HOH   788  2188 1437 HOH   HOH A . 
EA 11 HOH   789  2189 1639 HOH   HOH A . 
EA 11 HOH   790  2190 1231 HOH   HOH A . 
EA 11 HOH   791  2191 1621 HOH   HOH A . 
EA 11 HOH   792  2192 589  HOH   HOH A . 
EA 11 HOH   793  2193 1882 HOH   HOH A . 
EA 11 HOH   794  2194 1076 HOH   HOH A . 
EA 11 HOH   795  2195 1030 HOH   HOH A . 
EA 11 HOH   796  2196 1884 HOH   HOH A . 
EA 11 HOH   797  2197 2144 HOH   HOH A . 
EA 11 HOH   798  2198 2012 HOH   HOH A . 
EA 11 HOH   799  2199 430  HOH   HOH A . 
EA 11 HOH   800  2200 1246 HOH   HOH A . 
EA 11 HOH   801  2201 696  HOH   HOH A . 
EA 11 HOH   802  2202 1343 HOH   HOH A . 
EA 11 HOH   803  2203 640  HOH   HOH A . 
EA 11 HOH   804  2204 2229 HOH   HOH A . 
EA 11 HOH   805  2205 1620 HOH   HOH A . 
EA 11 HOH   806  2206 1697 HOH   HOH A . 
EA 11 HOH   807  2207 784  HOH   HOH A . 
EA 11 HOH   808  2208 1227 HOH   HOH A . 
EA 11 HOH   809  2209 1932 HOH   HOH A . 
EA 11 HOH   810  2210 1894 HOH   HOH A . 
EA 11 HOH   811  2211 1608 HOH   HOH A . 
EA 11 HOH   812  2212 1743 HOH   HOH A . 
EA 11 HOH   813  2213 2045 HOH   HOH A . 
EA 11 HOH   814  2214 1034 HOH   HOH A . 
EA 11 HOH   815  2215 1883 HOH   HOH A . 
EA 11 HOH   816  2216 693  HOH   HOH A . 
EA 11 HOH   817  2217 1896 HOH   HOH A . 
EA 11 HOH   818  2218 1964 HOH   HOH A . 
EA 11 HOH   819  2219 1875 HOH   HOH A . 
EA 11 HOH   820  2220 2141 HOH   HOH A . 
EA 11 HOH   821  2221 1839 HOH   HOH A . 
EA 11 HOH   822  2222 1531 HOH   HOH A . 
EA 11 HOH   823  2223 926  HOH   HOH A . 
EA 11 HOH   824  2224 991  HOH   HOH A . 
EA 11 HOH   825  2225 1322 HOH   HOH A . 
EA 11 HOH   826  2226 754  HOH   HOH A . 
EA 11 HOH   827  2227 2020 HOH   HOH A . 
EA 11 HOH   828  2228 1257 HOH   HOH A . 
EA 11 HOH   829  2229 1692 HOH   HOH A . 
EA 11 HOH   830  2230 1696 HOH   HOH A . 
EA 11 HOH   831  2231 1909 HOH   HOH A . 
EA 11 HOH   832  2232 1443 HOH   HOH A . 
EA 11 HOH   833  2233 3    HOH   HOH A . 
EA 11 HOH   834  2234 1911 HOH   HOH A . 
EA 11 HOH   835  2235 2117 HOH   HOH A . 
EA 11 HOH   836  2236 2035 HOH   HOH A . 
EA 11 HOH   837  2237 1293 HOH   HOH A . 
EA 11 HOH   838  2238 936  HOH   HOH A . 
EA 11 HOH   839  2239 1729 HOH   HOH A . 
EA 11 HOH   840  2240 1978 HOH   HOH A . 
EA 11 HOH   841  2241 1050 HOH   HOH A . 
EA 11 HOH   842  2242 767  HOH   HOH A . 
EA 11 HOH   843  2243 1555 HOH   HOH A . 
EA 11 HOH   844  2244 1282 HOH   HOH A . 
EA 11 HOH   845  2245 1453 HOH   HOH A . 
EA 11 HOH   846  2246 2023 HOH   HOH A . 
EA 11 HOH   847  2247 1648 HOH   HOH A . 
EA 11 HOH   848  2248 1304 HOH   HOH A . 
EA 11 HOH   849  2249 1893 HOH   HOH A . 
EA 11 HOH   850  2250 1038 HOH   HOH A . 
EA 11 HOH   851  2251 860  HOH   HOH A . 
EA 11 HOH   852  2252 1954 HOH   HOH A . 
EA 11 HOH   853  2253 1199 HOH   HOH A . 
EA 11 HOH   854  2254 1787 HOH   HOH A . 
EA 11 HOH   855  2255 1797 HOH   HOH A . 
EA 11 HOH   856  2256 1008 HOH   HOH A . 
EA 11 HOH   857  2257 2029 HOH   HOH A . 
EA 11 HOH   858  2258 2072 HOH   HOH A . 
EA 11 HOH   859  2259 1158 HOH   HOH A . 
EA 11 HOH   860  2260 1634 HOH   HOH A . 
EA 11 HOH   861  2261 1538 HOH   HOH A . 
EA 11 HOH   862  2262 1655 HOH   HOH A . 
EA 11 HOH   863  2263 2187 HOH   HOH A . 
EA 11 HOH   864  2264 2004 HOH   HOH A . 
EA 11 HOH   865  2265 1029 HOH   HOH A . 
EA 11 HOH   866  2266 1881 HOH   HOH A . 
EA 11 HOH   867  2267 1303 HOH   HOH A . 
EA 11 HOH   868  2268 1705 HOH   HOH A . 
EA 11 HOH   869  2269 1769 HOH   HOH A . 
EA 11 HOH   870  2270 1360 HOH   HOH A . 
EA 11 HOH   871  2271 1820 HOH   HOH A . 
EA 11 HOH   872  2272 1271 HOH   HOH A . 
EA 11 HOH   873  2273 1088 HOH   HOH A . 
EA 11 HOH   874  2274 2237 HOH   HOH A . 
EA 11 HOH   875  2275 1181 HOH   HOH A . 
EA 11 HOH   876  2276 913  HOH   HOH A . 
EA 11 HOH   877  2277 1798 HOH   HOH A . 
EA 11 HOH   878  2278 1    HOH   HOH A . 
EA 11 HOH   879  2279 668  HOH   HOH A . 
EA 11 HOH   880  2280 1422 HOH   HOH A . 
EA 11 HOH   881  2281 1746 HOH   HOH A . 
EA 11 HOH   882  2282 1499 HOH   HOH A . 
EA 11 HOH   883  2283 1298 HOH   HOH A . 
EA 11 HOH   884  2284 1323 HOH   HOH A . 
EA 11 HOH   885  2285 2216 HOH   HOH A . 
EA 11 HOH   886  2286 1143 HOH   HOH A . 
EA 11 HOH   887  2287 1895 HOH   HOH A . 
EA 11 HOH   888  2288 1157 HOH   HOH A . 
EA 11 HOH   889  2289 1635 HOH   HOH A . 
EA 11 HOH   890  2290 1263 HOH   HOH A . 
EA 11 HOH   891  2291 1262 HOH   HOH A . 
EA 11 HOH   892  2292 1814 HOH   HOH A . 
EA 11 HOH   893  2293 1873 HOH   HOH A . 
EA 11 HOH   894  2294 1554 HOH   HOH A . 
EA 11 HOH   895  2295 1225 HOH   HOH A . 
EA 11 HOH   896  2296 1840 HOH   HOH A . 
EA 11 HOH   897  2297 2151 HOH   HOH A . 
EA 11 HOH   898  2298 2173 HOH   HOH A . 
EA 11 HOH   899  2299 1535 HOH   HOH A . 
EA 11 HOH   900  2300 1513 HOH   HOH A . 
EA 11 HOH   901  2301 1858 HOH   HOH A . 
EA 11 HOH   902  2302 2195 HOH   HOH A . 
EA 11 HOH   903  2303 1475 HOH   HOH A . 
EA 11 HOH   904  2304 1889 HOH   HOH A . 
EA 11 HOH   905  2305 182  HOH   HOH A . 
EA 11 HOH   906  2306 2226 HOH   HOH A . 
EA 11 HOH   907  2307 1388 HOH   HOH A . 
EA 11 HOH   908  2308 2188 HOH   HOH A . 
EA 11 HOH   909  2309 2073 HOH   HOH A . 
EA 11 HOH   910  2310 315  HOH   HOH A . 
EA 11 HOH   911  2311 1788 HOH   HOH A . 
EA 11 HOH   912  2312 2018 HOH   HOH A . 
EA 11 HOH   913  2313 2088 HOH   HOH A . 
EA 11 HOH   914  2314 1786 HOH   HOH A . 
EA 11 HOH   915  2315 614  HOH   HOH A . 
EA 11 HOH   916  2316 2178 HOH   HOH A . 
EA 11 HOH   917  2317 2149 HOH   HOH A . 
EA 11 HOH   918  2318 658  HOH   HOH A . 
EA 11 HOH   919  2319 2179 HOH   HOH A . 
EA 11 HOH   920  2320 2175 HOH   HOH A . 
EA 11 HOH   921  2321 1248 HOH   HOH A . 
EA 11 HOH   922  2322 1241 HOH   HOH A . 
EA 11 HOH   923  2323 1351 HOH   HOH A . 
EA 11 HOH   924  2324 663  HOH   HOH A . 
EA 11 HOH   925  2325 2038 HOH   HOH A . 
EA 11 HOH   926  2326 1292 HOH   HOH A . 
EA 11 HOH   927  2327 1877 HOH   HOH A . 
EA 11 HOH   928  2328 2066 HOH   HOH A . 
EA 11 HOH   929  2329 1852 HOH   HOH A . 
EA 11 HOH   930  2330 2039 HOH   HOH A . 
EA 11 HOH   931  2331 1985 HOH   HOH A . 
EA 11 HOH   932  2332 1166 HOH   HOH A . 
EA 11 HOH   933  2333 1551 HOH   HOH A . 
EA 11 HOH   934  2334 2044 HOH   HOH A . 
EA 11 HOH   935  2335 1208 HOH   HOH A . 
EA 11 HOH   936  2336 948  HOH   HOH A . 
EA 11 HOH   937  2337 877  HOH   HOH A . 
EA 11 HOH   938  2338 1354 HOH   HOH A . 
EA 11 HOH   939  2339 1562 HOH   HOH A . 
EA 11 HOH   940  2340 2163 HOH   HOH A . 
EA 11 HOH   941  2341 1905 HOH   HOH A . 
EA 11 HOH   942  2342 570  HOH   HOH A . 
EA 11 HOH   943  2343 1876 HOH   HOH A . 
EA 11 HOH   944  2344 2125 HOH   HOH A . 
EA 11 HOH   945  2345 870  HOH   HOH A . 
EA 11 HOH   946  2346 1290 HOH   HOH A . 
EA 11 HOH   947  2347 432  HOH   HOH A . 
EA 11 HOH   948  2348 1674 HOH   HOH A . 
EA 11 HOH   949  2349 2154 HOH   HOH A . 
EA 11 HOH   950  2350 1110 HOH   HOH A . 
EA 11 HOH   951  2351 1757 HOH   HOH A . 
EA 11 HOH   952  2352 2126 HOH   HOH A . 
EA 11 HOH   953  2353 1890 HOH   HOH A . 
EA 11 HOH   954  2354 1738 HOH   HOH A . 
EA 11 HOH   955  2355 1488 HOH   HOH A . 
EA 11 HOH   956  2356 1330 HOH   HOH A . 
EA 11 HOH   957  2357 1544 HOH   HOH A . 
EA 11 HOH   958  2358 1652 HOH   HOH A . 
EA 11 HOH   959  2359 1167 HOH   HOH A . 
EA 11 HOH   960  2360 2233 HOH   HOH A . 
EA 11 HOH   961  2361 1609 HOH   HOH A . 
EA 11 HOH   962  2362 797  HOH   HOH A . 
EA 11 HOH   963  2363 2147 HOH   HOH A . 
EA 11 HOH   964  2364 811  HOH   HOH A . 
EA 11 HOH   965  2365 1992 HOH   HOH A . 
EA 11 HOH   966  2366 1874 HOH   HOH A . 
EA 11 HOH   967  2367 1095 HOH   HOH A . 
EA 11 HOH   968  2368 2067 HOH   HOH A . 
EA 11 HOH   969  2369 1125 HOH   HOH A . 
EA 11 HOH   970  2370 435  HOH   HOH A . 
EA 11 HOH   971  2371 988  HOH   HOH A . 
EA 11 HOH   972  2372 1414 HOH   HOH A . 
EA 11 HOH   973  2373 2015 HOH   HOH A . 
EA 11 HOH   974  2374 1338 HOH   HOH A . 
EA 11 HOH   975  2375 1552 HOH   HOH A . 
EA 11 HOH   976  2376 1669 HOH   HOH A . 
EA 11 HOH   977  2377 1364 HOH   HOH A . 
EA 11 HOH   978  2378 1722 HOH   HOH A . 
EA 11 HOH   979  2379 2068 HOH   HOH A . 
EA 11 HOH   980  2380 770  HOH   HOH A . 
EA 11 HOH   981  2381 1880 HOH   HOH A . 
EA 11 HOH   982  2382 2078 HOH   HOH A . 
EA 11 HOH   983  2383 1503 HOH   HOH A . 
EA 11 HOH   984  2384 1791 HOH   HOH A . 
EA 11 HOH   985  2385 1959 HOH   HOH A . 
EA 11 HOH   986  2386 1341 HOH   HOH A . 
EA 11 HOH   987  2387 2037 HOH   HOH A . 
EA 11 HOH   988  2388 2146 HOH   HOH A . 
EA 11 HOH   989  2389 1892 HOH   HOH A . 
EA 11 HOH   990  2390 598  HOH   HOH A . 
EA 11 HOH   991  2391 2062 HOH   HOH A . 
EA 11 HOH   992  2392 2108 HOH   HOH A . 
EA 11 HOH   993  2393 1712 HOH   HOH A . 
EA 11 HOH   994  2394 1574 HOH   HOH A . 
EA 11 HOH   995  2395 2007 HOH   HOH A . 
EA 11 HOH   996  2396 2071 HOH   HOH A . 
EA 11 HOH   997  2397 1734 HOH   HOH A . 
EA 11 HOH   998  2398 1164 HOH   HOH A . 
EA 11 HOH   999  2399 1816 HOH   HOH A . 
EA 11 HOH   1000 2400 1153 HOH   HOH A . 
EA 11 HOH   1001 2401 2013 HOH   HOH A . 
EA 11 HOH   1002 2402 1306 HOH   HOH A . 
EA 11 HOH   1003 2403 1441 HOH   HOH A . 
EA 11 HOH   1004 2404 707  HOH   HOH A . 
EA 11 HOH   1005 2405 1777 HOH   HOH A . 
EA 11 HOH   1006 2406 1289 HOH   HOH A . 
EA 11 HOH   1007 2407 1904 HOH   HOH A . 
EA 11 HOH   1008 2408 1776 HOH   HOH A . 
EA 11 HOH   1009 2409 1215 HOH   HOH A . 
EA 11 HOH   1010 2410 1183 HOH   HOH A . 
EA 11 HOH   1011 2411 1963 HOH   HOH A . 
EA 11 HOH   1012 2412 1772 HOH   HOH A . 
EA 11 HOH   1013 2413 2192 HOH   HOH A . 
EA 11 HOH   1014 2414 1434 HOH   HOH A . 
EA 11 HOH   1015 2415 1680 HOH   HOH A . 
EA 11 HOH   1016 2416 2087 HOH   HOH A . 
EA 11 HOH   1017 2417 1879 HOH   HOH A . 
EA 11 HOH   1018 2418 957  HOH   HOH A . 
EA 11 HOH   1019 2419 382  HOH   HOH A . 
EA 11 HOH   1020 2420 2008 HOH   HOH A . 
EA 11 HOH   1021 2421 1730 HOH   HOH A . 
EA 11 HOH   1022 2422 1256 HOH   HOH A . 
EA 11 HOH   1023 2423 1897 HOH   HOH A . 
EA 11 HOH   1024 2424 1150 HOH   HOH A . 
EA 11 HOH   1025 2425 1507 HOH   HOH A . 
EA 11 HOH   1026 2426 1731 HOH   HOH A . 
EA 11 HOH   1027 2427 1071 HOH   HOH A . 
EA 11 HOH   1028 2428 1258 HOH   HOH A . 
EA 11 HOH   1029 2429 1061 HOH   HOH A . 
EA 11 HOH   1030 2430 2230 HOH   HOH A . 
EA 11 HOH   1031 2431 1132 HOH   HOH A . 
EA 11 HOH   1032 2432 1778 HOH   HOH A . 
EA 11 HOH   1033 2433 1371 HOH   HOH A . 
EA 11 HOH   1034 2434 2003 HOH   HOH A . 
EA 11 HOH   1035 2435 1378 HOH   HOH A . 
EA 11 HOH   1036 2436 1557 HOH   HOH A . 
EA 11 HOH   1037 2437 2056 HOH   HOH A . 
EA 11 HOH   1038 2438 2077 HOH   HOH A . 
EA 11 HOH   1039 2439 2182 HOH   HOH A . 
EA 11 HOH   1040 2440 1902 HOH   HOH A . 
EA 11 HOH   1041 2441 885  HOH   HOH A . 
EA 11 HOH   1042 2442 1662 HOH   HOH A . 
EA 11 HOH   1043 2443 999  HOH   HOH A . 
EA 11 HOH   1044 2444 788  HOH   HOH A . 
EA 11 HOH   1045 2445 1203 HOH   HOH A . 
EA 11 HOH   1046 2446 1886 HOH   HOH A . 
EA 11 HOH   1047 2447 1853 HOH   HOH A . 
EA 11 HOH   1048 2448 1739 HOH   HOH A . 
EA 11 HOH   1049 2449 2034 HOH   HOH A . 
EA 11 HOH   1050 2450 1556 HOH   HOH A . 
EA 11 HOH   1051 2451 1518 HOH   HOH A . 
EA 11 HOH   1052 2452 1376 HOH   HOH A . 
EA 11 HOH   1053 2453 2005 HOH   HOH A . 
EA 11 HOH   1054 2454 2115 HOH   HOH A . 
EA 11 HOH   1055 2455 2053 HOH   HOH A . 
EA 11 HOH   1056 2456 2064 HOH   HOH A . 
EA 11 HOH   1057 2457 1367 HOH   HOH A . 
EA 11 HOH   1058 2458 1047 HOH   HOH A . 
EA 11 HOH   1059 2459 1862 HOH   HOH A . 
EA 11 HOH   1060 2460 1989 HOH   HOH A . 
EA 11 HOH   1061 2461 2215 HOH   HOH A . 
EA 11 HOH   1062 2462 1903 HOH   HOH A . 
EA 11 HOH   1063 2463 1580 HOH   HOH A . 
EA 11 HOH   1064 2464 1198 HOH   HOH A . 
EA 11 HOH   1065 2465 2076 HOH   HOH A . 
EA 11 HOH   1066 2466 1161 HOH   HOH A . 
EA 11 HOH   1067 2467 1976 HOH   HOH A . 
FA 11 HOH   1    1401 1841 HOH   HOH B . 
FA 11 HOH   2    1402 1823 HOH   HOH B . 
FA 11 HOH   3    1403 1676 HOH   HOH B . 
FA 11 HOH   4    1404 1112 HOH   HOH B . 
FA 11 HOH   5    1405 1449 HOH   HOH B . 
FA 11 HOH   6    1406 1516 HOH   HOH B . 
FA 11 HOH   7    1407 1539 HOH   HOH B . 
FA 11 HOH   8    1408 2208 HOH   HOH B . 
FA 11 HOH   9    1409 2145 HOH   HOH B . 
FA 11 HOH   10   1410 1899 HOH   HOH B . 
FA 11 HOH   11   1411 1162 HOH   HOH B . 
FA 11 HOH   12   1412 608  HOH   HOH B . 
FA 11 HOH   13   1413 1584 HOH   HOH B . 
FA 11 HOH   14   1414 1436 HOH   HOH B . 
FA 11 HOH   15   1415 509  HOH   HOH B . 
FA 11 HOH   16   1416 1684 HOH   HOH B . 
FA 11 HOH   17   1417 959  HOH   HOH B . 
FA 11 HOH   18   1418 1728 HOH   HOH B . 
FA 11 HOH   19   1419 1127 HOH   HOH B . 
FA 11 HOH   20   1420 781  HOH   HOH B . 
FA 11 HOH   21   1421 1700 HOH   HOH B . 
FA 11 HOH   22   1422 805  HOH   HOH B . 
FA 11 HOH   23   1423 575  HOH   HOH B . 
FA 11 HOH   24   1424 888  HOH   HOH B . 
FA 11 HOH   25   1425 255  HOH   HOH B . 
FA 11 HOH   26   1426 762  HOH   HOH B . 
FA 11 HOH   27   1427 1070 HOH   HOH B . 
FA 11 HOH   28   1428 843  HOH   HOH B . 
FA 11 HOH   29   1429 1602 HOH   HOH B . 
FA 11 HOH   30   1430 846  HOH   HOH B . 
FA 11 HOH   31   1431 2206 HOH   HOH B . 
FA 11 HOH   32   1432 747  HOH   HOH B . 
FA 11 HOH   33   1433 439  HOH   HOH B . 
FA 11 HOH   34   1434 726  HOH   HOH B . 
FA 11 HOH   35   1435 1811 HOH   HOH B . 
FA 11 HOH   36   1436 1461 HOH   HOH B . 
FA 11 HOH   37   1437 1025 HOH   HOH B . 
FA 11 HOH   38   1438 2103 HOH   HOH B . 
FA 11 HOH   39   1439 1699 HOH   HOH B . 
FA 11 HOH   40   1440 1455 HOH   HOH B . 
FA 11 HOH   41   1441 1498 HOH   HOH B . 
FA 11 HOH   42   1442 140  HOH   HOH B . 
FA 11 HOH   43   1443 240  HOH   HOH B . 
FA 11 HOH   44   1444 1054 HOH   HOH B . 
FA 11 HOH   45   1445 2122 HOH   HOH B . 
FA 11 HOH   46   1446 1936 HOH   HOH B . 
FA 11 HOH   47   1447 1859 HOH   HOH B . 
FA 11 HOH   48   1448 776  HOH   HOH B . 
FA 11 HOH   49   1449 1838 HOH   HOH B . 
FA 11 HOH   50   1450 1490 HOH   HOH B . 
FA 11 HOH   51   1451 117  HOH   HOH B . 
FA 11 HOH   52   1452 1039 HOH   HOH B . 
FA 11 HOH   53   1453 1321 HOH   HOH B . 
FA 11 HOH   54   1454 947  HOH   HOH B . 
FA 11 HOH   55   1455 526  HOH   HOH B . 
FA 11 HOH   56   1456 1956 HOH   HOH B . 
FA 11 HOH   57   1457 1328 HOH   HOH B . 
FA 11 HOH   58   1458 1914 HOH   HOH B . 
FA 11 HOH   59   1459 779  HOH   HOH B . 
FA 11 HOH   60   1460 713  HOH   HOH B . 
FA 11 HOH   61   1461 2036 HOH   HOH B . 
FA 11 HOH   62   1462 424  HOH   HOH B . 
FA 11 HOH   63   1463 1342 HOH   HOH B . 
FA 11 HOH   64   1464 473  HOH   HOH B . 
FA 11 HOH   65   1465 242  HOH   HOH B . 
FA 11 HOH   66   1466 923  HOH   HOH B . 
FA 11 HOH   67   1467 909  HOH   HOH B . 
FA 11 HOH   68   1468 2168 HOH   HOH B . 
FA 11 HOH   69   1469 1313 HOH   HOH B . 
FA 11 HOH   70   1470 1393 HOH   HOH B . 
FA 11 HOH   71   1471 258  HOH   HOH B . 
FA 11 HOH   72   1472 1268 HOH   HOH B . 
FA 11 HOH   73   1473 2130 HOH   HOH B . 
FA 11 HOH   74   1474 1497 HOH   HOH B . 
FA 11 HOH   75   1475 1046 HOH   HOH B . 
FA 11 HOH   76   1476 1514 HOH   HOH B . 
FA 11 HOH   77   1477 2221 HOH   HOH B . 
FA 11 HOH   78   1478 833  HOH   HOH B . 
FA 11 HOH   79   1479 844  HOH   HOH B . 
FA 11 HOH   80   1480 1578 HOH   HOH B . 
FA 11 HOH   81   1481 2119 HOH   HOH B . 
FA 11 HOH   82   1482 576  HOH   HOH B . 
FA 11 HOH   83   1483 97   HOH   HOH B . 
FA 11 HOH   84   1484 1494 HOH   HOH B . 
FA 11 HOH   85   1485 274  HOH   HOH B . 
FA 11 HOH   86   1486 448  HOH   HOH B . 
FA 11 HOH   87   1487 210  HOH   HOH B . 
FA 11 HOH   88   1488 1599 HOH   HOH B . 
FA 11 HOH   89   1489 49   HOH   HOH B . 
FA 11 HOH   90   1490 308  HOH   HOH B . 
FA 11 HOH   91   1491 454  HOH   HOH B . 
FA 11 HOH   92   1492 2176 HOH   HOH B . 
FA 11 HOH   93   1493 595  HOH   HOH B . 
FA 11 HOH   94   1494 739  HOH   HOH B . 
FA 11 HOH   95   1495 1732 HOH   HOH B . 
FA 11 HOH   96   1496 941  HOH   HOH B . 
FA 11 HOH   97   1497 369  HOH   HOH B . 
FA 11 HOH   98   1498 1464 HOH   HOH B . 
FA 11 HOH   99   1499 130  HOH   HOH B . 
FA 11 HOH   100  1500 236  HOH   HOH B . 
FA 11 HOH   101  1501 464  HOH   HOH B . 
FA 11 HOH   102  1502 1100 HOH   HOH B . 
FA 11 HOH   103  1503 1270 HOH   HOH B . 
FA 11 HOH   104  1504 62   HOH   HOH B . 
FA 11 HOH   105  1505 44   HOH   HOH B . 
FA 11 HOH   106  1506 441  HOH   HOH B . 
FA 11 HOH   107  1507 623  HOH   HOH B . 
FA 11 HOH   108  1508 126  HOH   HOH B . 
FA 11 HOH   109  1509 1558 HOH   HOH B . 
FA 11 HOH   110  1510 934  HOH   HOH B . 
FA 11 HOH   111  1511 1012 HOH   HOH B . 
FA 11 HOH   112  1512 124  HOH   HOH B . 
FA 11 HOH   113  1513 1220 HOH   HOH B . 
FA 11 HOH   114  1514 296  HOH   HOH B . 
FA 11 HOH   115  1515 716  HOH   HOH B . 
FA 11 HOH   116  1516 1610 HOH   HOH B . 
FA 11 HOH   117  1517 1193 HOH   HOH B . 
FA 11 HOH   118  1518 1213 HOH   HOH B . 
FA 11 HOH   119  1519 318  HOH   HOH B . 
FA 11 HOH   120  1520 852  HOH   HOH B . 
FA 11 HOH   121  1521 1711 HOH   HOH B . 
FA 11 HOH   122  1522 56   HOH   HOH B . 
FA 11 HOH   123  1523 313  HOH   HOH B . 
FA 11 HOH   124  1524 1955 HOH   HOH B . 
FA 11 HOH   125  1525 15   HOH   HOH B . 
FA 11 HOH   126  1526 291  HOH   HOH B . 
FA 11 HOH   127  1527 1993 HOH   HOH B . 
FA 11 HOH   128  1528 159  HOH   HOH B . 
FA 11 HOH   129  1529 1550 HOH   HOH B . 
FA 11 HOH   130  1530 235  HOH   HOH B . 
FA 11 HOH   131  1531 715  HOH   HOH B . 
FA 11 HOH   132  1532 826  HOH   HOH B . 
FA 11 HOH   133  1533 1142 HOH   HOH B . 
FA 11 HOH   134  1534 429  HOH   HOH B . 
FA 11 HOH   135  1535 1540 HOH   HOH B . 
FA 11 HOH   136  1536 354  HOH   HOH B . 
FA 11 HOH   137  1537 2142 HOH   HOH B . 
FA 11 HOH   138  1538 312  HOH   HOH B . 
FA 11 HOH   139  1539 158  HOH   HOH B . 
FA 11 HOH   140  1540 1365 HOH   HOH B . 
FA 11 HOH   141  1541 771  HOH   HOH B . 
FA 11 HOH   142  1542 1673 HOH   HOH B . 
FA 11 HOH   143  1543 19   HOH   HOH B . 
FA 11 HOH   144  1544 1427 HOH   HOH B . 
FA 11 HOH   145  1545 474  HOH   HOH B . 
FA 11 HOH   146  1546 1308 HOH   HOH B . 
FA 11 HOH   147  1547 1994 HOH   HOH B . 
FA 11 HOH   148  1548 7    HOH   HOH B . 
FA 11 HOH   149  1549 60   HOH   HOH B . 
FA 11 HOH   150  1550 1075 HOH   HOH B . 
FA 11 HOH   151  1551 1279 HOH   HOH B . 
FA 11 HOH   152  1552 186  HOH   HOH B . 
FA 11 HOH   153  1553 700  HOH   HOH B . 
FA 11 HOH   154  1554 1724 HOH   HOH B . 
FA 11 HOH   155  1555 143  HOH   HOH B . 
FA 11 HOH   156  1556 697  HOH   HOH B . 
FA 11 HOH   157  1557 1299 HOH   HOH B . 
FA 11 HOH   158  1558 1194 HOH   HOH B . 
FA 11 HOH   159  1559 28   HOH   HOH B . 
FA 11 HOH   160  1560 2214 HOH   HOH B . 
FA 11 HOH   161  1561 1078 HOH   HOH B . 
FA 11 HOH   162  1562 1438 HOH   HOH B . 
FA 11 HOH   163  1563 298  HOH   HOH B . 
FA 11 HOH   164  1564 566  HOH   HOH B . 
FA 11 HOH   165  1565 600  HOH   HOH B . 
FA 11 HOH   166  1566 1026 HOH   HOH B . 
FA 11 HOH   167  1567 1633 HOH   HOH B . 
FA 11 HOH   168  1568 1090 HOH   HOH B . 
FA 11 HOH   169  1569 199  HOH   HOH B . 
FA 11 HOH   170  1570 30   HOH   HOH B . 
FA 11 HOH   171  1571 725  HOH   HOH B . 
FA 11 HOH   172  1572 452  HOH   HOH B . 
FA 11 HOH   173  1573 2086 HOH   HOH B . 
FA 11 HOH   174  1574 68   HOH   HOH B . 
FA 11 HOH   175  1575 147  HOH   HOH B . 
FA 11 HOH   176  1576 493  HOH   HOH B . 
FA 11 HOH   177  1577 129  HOH   HOH B . 
FA 11 HOH   178  1578 1408 HOH   HOH B . 
FA 11 HOH   179  1579 355  HOH   HOH B . 
FA 11 HOH   180  1580 2199 HOH   HOH B . 
FA 11 HOH   181  1581 451  HOH   HOH B . 
FA 11 HOH   182  1582 200  HOH   HOH B . 
FA 11 HOH   183  1583 799  HOH   HOH B . 
FA 11 HOH   184  1584 193  HOH   HOH B . 
FA 11 HOH   185  1585 35   HOH   HOH B . 
FA 11 HOH   186  1586 809  HOH   HOH B . 
FA 11 HOH   187  1587 241  HOH   HOH B . 
FA 11 HOH   188  1588 698  HOH   HOH B . 
FA 11 HOH   189  1589 1291 HOH   HOH B . 
FA 11 HOH   190  1590 1234 HOH   HOH B . 
FA 11 HOH   191  1591 1375 HOH   HOH B . 
FA 11 HOH   192  1592 416  HOH   HOH B . 
FA 11 HOH   193  1593 302  HOH   HOH B . 
FA 11 HOH   194  1594 1383 HOH   HOH B . 
FA 11 HOH   195  1595 2205 HOH   HOH B . 
FA 11 HOH   196  1596 769  HOH   HOH B . 
FA 11 HOH   197  1597 669  HOH   HOH B . 
FA 11 HOH   198  1598 2196 HOH   HOH B . 
FA 11 HOH   199  1599 917  HOH   HOH B . 
FA 11 HOH   200  1600 1120 HOH   HOH B . 
FA 11 HOH   201  1601 1442 HOH   HOH B . 
FA 11 HOH   202  1602 1309 HOH   HOH B . 
FA 11 HOH   203  1603 1805 HOH   HOH B . 
FA 11 HOH   204  1604 276  HOH   HOH B . 
FA 11 HOH   205  1605 1204 HOH   HOH B . 
FA 11 HOH   206  1606 89   HOH   HOH B . 
FA 11 HOH   207  1607 394  HOH   HOH B . 
FA 11 HOH   208  1608 933  HOH   HOH B . 
FA 11 HOH   209  1609 1943 HOH   HOH B . 
FA 11 HOH   210  1610 278  HOH   HOH B . 
FA 11 HOH   211  1611 213  HOH   HOH B . 
FA 11 HOH   212  1612 336  HOH   HOH B . 
FA 11 HOH   213  1613 588  HOH   HOH B . 
FA 11 HOH   214  1614 78   HOH   HOH B . 
FA 11 HOH   215  1615 74   HOH   HOH B . 
FA 11 HOH   216  1616 1249 HOH   HOH B . 
FA 11 HOH   217  1617 550  HOH   HOH B . 
FA 11 HOH   218  1618 1918 HOH   HOH B . 
FA 11 HOH   219  1619 169  HOH   HOH B . 
FA 11 HOH   220  1620 1003 HOH   HOH B . 
FA 11 HOH   221  1621 417  HOH   HOH B . 
FA 11 HOH   222  1622 1922 HOH   HOH B . 
FA 11 HOH   223  1623 616  HOH   HOH B . 
FA 11 HOH   224  1624 1917 HOH   HOH B . 
FA 11 HOH   225  1625 440  HOH   HOH B . 
FA 11 HOH   226  1626 322  HOH   HOH B . 
FA 11 HOH   227  1627 1804 HOH   HOH B . 
FA 11 HOH   228  1628 1009 HOH   HOH B . 
FA 11 HOH   229  1629 1000 HOH   HOH B . 
FA 11 HOH   230  1630 294  HOH   HOH B . 
FA 11 HOH   231  1631 237  HOH   HOH B . 
FA 11 HOH   232  1632 497  HOH   HOH B . 
FA 11 HOH   233  1633 1386 HOH   HOH B . 
FA 11 HOH   234  1634 461  HOH   HOH B . 
FA 11 HOH   235  1635 1926 HOH   HOH B . 
FA 11 HOH   236  1636 365  HOH   HOH B . 
FA 11 HOH   237  1637 403  HOH   HOH B . 
FA 11 HOH   238  1638 752  HOH   HOH B . 
FA 11 HOH   239  1639 1651 HOH   HOH B . 
FA 11 HOH   240  1640 495  HOH   HOH B . 
FA 11 HOH   241  1641 2075 HOH   HOH B . 
FA 11 HOH   242  1642 118  HOH   HOH B . 
FA 11 HOH   243  1643 1660 HOH   HOH B . 
FA 11 HOH   244  1644 1915 HOH   HOH B . 
FA 11 HOH   245  1645 1066 HOH   HOH B . 
FA 11 HOH   246  1646 1965 HOH   HOH B . 
FA 11 HOH   247  1647 499  HOH   HOH B . 
FA 11 HOH   248  1648 206  HOH   HOH B . 
FA 11 HOH   249  1649 679  HOH   HOH B . 
FA 11 HOH   250  1650 942  HOH   HOH B . 
FA 11 HOH   251  1651 494  HOH   HOH B . 
FA 11 HOH   252  1652 1178 HOH   HOH B . 
FA 11 HOH   253  1653 22   HOH   HOH B . 
FA 11 HOH   254  1654 12   HOH   HOH B . 
FA 11 HOH   255  1655 1233 HOH   HOH B . 
FA 11 HOH   256  1656 70   HOH   HOH B . 
FA 11 HOH   257  1657 1011 HOH   HOH B . 
FA 11 HOH   258  1658 712  HOH   HOH B . 
FA 11 HOH   259  1659 938  HOH   HOH B . 
FA 11 HOH   260  1660 839  HOH   HOH B . 
FA 11 HOH   261  1661 446  HOH   HOH B . 
FA 11 HOH   262  1662 2152 HOH   HOH B . 
FA 11 HOH   263  1663 666  HOH   HOH B . 
FA 11 HOH   264  1664 1996 HOH   HOH B . 
FA 11 HOH   265  1665 624  HOH   HOH B . 
FA 11 HOH   266  1666 339  HOH   HOH B . 
FA 11 HOH   267  1667 371  HOH   HOH B . 
FA 11 HOH   268  1668 619  HOH   HOH B . 
FA 11 HOH   269  1669 1111 HOH   HOH B . 
FA 11 HOH   270  1670 810  HOH   HOH B . 
FA 11 HOH   271  1671 964  HOH   HOH B . 
FA 11 HOH   272  1672 99   HOH   HOH B . 
FA 11 HOH   273  1673 115  HOH   HOH B . 
FA 11 HOH   274  1674 319  HOH   HOH B . 
FA 11 HOH   275  1675 288  HOH   HOH B . 
FA 11 HOH   276  1676 295  HOH   HOH B . 
FA 11 HOH   277  1677 965  HOH   HOH B . 
FA 11 HOH   278  1678 1059 HOH   HOH B . 
FA 11 HOH   279  1679 18   HOH   HOH B . 
FA 11 HOH   280  1680 398  HOH   HOH B . 
FA 11 HOH   281  1681 1174 HOH   HOH B . 
FA 11 HOH   282  1682 899  HOH   HOH B . 
FA 11 HOH   283  1683 401  HOH   HOH B . 
FA 11 HOH   284  1684 541  HOH   HOH B . 
FA 11 HOH   285  1685 761  HOH   HOH B . 
FA 11 HOH   286  1686 940  HOH   HOH B . 
FA 11 HOH   287  1687 2098 HOH   HOH B . 
FA 11 HOH   288  1688 2083 HOH   HOH B . 
FA 11 HOH   289  1689 23   HOH   HOH B . 
FA 11 HOH   290  1690 225  HOH   HOH B . 
FA 11 HOH   291  1691 224  HOH   HOH B . 
FA 11 HOH   292  1692 750  HOH   HOH B . 
FA 11 HOH   293  1693 1359 HOH   HOH B . 
FA 11 HOH   294  1694 512  HOH   HOH B . 
FA 11 HOH   295  1695 974  HOH   HOH B . 
FA 11 HOH   296  1696 280  HOH   HOH B . 
FA 11 HOH   297  1697 1042 HOH   HOH B . 
FA 11 HOH   298  1698 537  HOH   HOH B . 
FA 11 HOH   299  1699 1969 HOH   HOH B . 
FA 11 HOH   300  1700 381  HOH   HOH B . 
FA 11 HOH   301  1701 234  HOH   HOH B . 
FA 11 HOH   302  1702 282  HOH   HOH B . 
FA 11 HOH   303  1703 92   HOH   HOH B . 
FA 11 HOH   304  1704 24   HOH   HOH B . 
FA 11 HOH   305  1705 983  HOH   HOH B . 
FA 11 HOH   306  1706 967  HOH   HOH B . 
FA 11 HOH   307  1707 579  HOH   HOH B . 
FA 11 HOH   308  1708 1611 HOH   HOH B . 
FA 11 HOH   309  1709 1319 HOH   HOH B . 
FA 11 HOH   310  1710 197  HOH   HOH B . 
FA 11 HOH   311  1711 323  HOH   HOH B . 
FA 11 HOH   312  1712 689  HOH   HOH B . 
FA 11 HOH   313  1713 145  HOH   HOH B . 
FA 11 HOH   314  1714 1049 HOH   HOH B . 
FA 11 HOH   315  1715 391  HOH   HOH B . 
FA 11 HOH   316  1716 1051 HOH   HOH B . 
FA 11 HOH   317  1717 153  HOH   HOH B . 
FA 11 HOH   318  1718 54   HOH   HOH B . 
FA 11 HOH   319  1719 2120 HOH   HOH B . 
FA 11 HOH   320  1720 832  HOH   HOH B . 
FA 11 HOH   321  1721 1228 HOH   HOH B . 
FA 11 HOH   322  1722 654  HOH   HOH B . 
FA 11 HOH   323  1723 238  HOH   HOH B . 
FA 11 HOH   324  1724 887  HOH   HOH B . 
FA 11 HOH   325  1725 484  HOH   HOH B . 
FA 11 HOH   326  1726 620  HOH   HOH B . 
FA 11 HOH   327  1727 1350 HOH   HOH B . 
FA 11 HOH   328  1728 825  HOH   HOH B . 
FA 11 HOH   329  1729 103  HOH   HOH B . 
FA 11 HOH   330  1730 304  HOH   HOH B . 
FA 11 HOH   331  1731 946  HOH   HOH B . 
FA 11 HOH   332  1732 57   HOH   HOH B . 
FA 11 HOH   333  1733 1723 HOH   HOH B . 
FA 11 HOH   334  1734 871  HOH   HOH B . 
FA 11 HOH   335  1735 157  HOH   HOH B . 
FA 11 HOH   336  1736 643  HOH   HOH B . 
FA 11 HOH   337  1737 1177 HOH   HOH B . 
FA 11 HOH   338  1738 1809 HOH   HOH B . 
FA 11 HOH   339  1739 121  HOH   HOH B . 
FA 11 HOH   340  1740 462  HOH   HOH B . 
FA 11 HOH   341  1741 297  HOH   HOH B . 
FA 11 HOH   342  1742 684  HOH   HOH B . 
FA 11 HOH   343  1743 263  HOH   HOH B . 
FA 11 HOH   344  1744 138  HOH   HOH B . 
FA 11 HOH   345  1745 1179 HOH   HOH B . 
FA 11 HOH   346  1746 410  HOH   HOH B . 
FA 11 HOH   347  1747 160  HOH   HOH B . 
FA 11 HOH   348  1748 161  HOH   HOH B . 
FA 11 HOH   349  1749 1942 HOH   HOH B . 
FA 11 HOH   350  1750 393  HOH   HOH B . 
FA 11 HOH   351  1751 1625 HOH   HOH B . 
FA 11 HOH   352  1752 1682 HOH   HOH B . 
FA 11 HOH   353  1753 1675 HOH   HOH B . 
FA 11 HOH   354  1754 1935 HOH   HOH B . 
FA 11 HOH   355  1755 1708 HOH   HOH B . 
FA 11 HOH   356  1756 192  HOH   HOH B . 
FA 11 HOH   357  1757 603  HOH   HOH B . 
FA 11 HOH   358  1758 954  HOH   HOH B . 
FA 11 HOH   359  1759 177  HOH   HOH B . 
FA 11 HOH   360  1760 782  HOH   HOH B . 
FA 11 HOH   361  1761 47   HOH   HOH B . 
FA 11 HOH   362  1762 912  HOH   HOH B . 
FA 11 HOH   363  1763 32   HOH   HOH B . 
FA 11 HOH   364  1764 131  HOH   HOH B . 
FA 11 HOH   365  1765 1015 HOH   HOH B . 
FA 11 HOH   366  1766 356  HOH   HOH B . 
FA 11 HOH   367  1767 33   HOH   HOH B . 
FA 11 HOH   368  1768 1808 HOH   HOH B . 
FA 11 HOH   369  1769 1152 HOH   HOH B . 
FA 11 HOH   370  1770 976  HOH   HOH B . 
FA 11 HOH   371  1771 1236 HOH   HOH B . 
FA 11 HOH   372  1772 601  HOH   HOH B . 
FA 11 HOH   373  1773 31   HOH   HOH B . 
FA 11 HOH   374  1774 21   HOH   HOH B . 
FA 11 HOH   375  1775 1201 HOH   HOH B . 
FA 11 HOH   376  1776 539  HOH   HOH B . 
FA 11 HOH   377  1777 2218 HOH   HOH B . 
FA 11 HOH   378  1778 1466 HOH   HOH B . 
FA 11 HOH   379  1779 1297 HOH   HOH B . 
FA 11 HOH   380  1780 641  HOH   HOH B . 
FA 11 HOH   381  1781 53   HOH   HOH B . 
FA 11 HOH   382  1782 119  HOH   HOH B . 
FA 11 HOH   383  1783 221  HOH   HOH B . 
FA 11 HOH   384  1784 1645 HOH   HOH B . 
FA 11 HOH   385  1785 1751 HOH   HOH B . 
FA 11 HOH   386  1786 606  HOH   HOH B . 
FA 11 HOH   387  1787 264  HOH   HOH B . 
FA 11 HOH   388  1788 183  HOH   HOH B . 
FA 11 HOH   389  1789 939  HOH   HOH B . 
FA 11 HOH   390  1790 2033 HOH   HOH B . 
FA 11 HOH   391  1791 1916 HOH   HOH B . 
FA 11 HOH   392  1792 1325 HOH   HOH B . 
FA 11 HOH   393  1793 1750 HOH   HOH B . 
FA 11 HOH   394  1794 2153 HOH   HOH B . 
FA 11 HOH   395  1795 893  HOH   HOH B . 
FA 11 HOH   396  1796 2190 HOH   HOH B . 
FA 11 HOH   397  1797 1828 HOH   HOH B . 
FA 11 HOH   398  1798 652  HOH   HOH B . 
FA 11 HOH   399  1799 834  HOH   HOH B . 
FA 11 HOH   400  1800 741  HOH   HOH B . 
FA 11 HOH   401  1801 63   HOH   HOH B . 
FA 11 HOH   402  1802 123  HOH   HOH B . 
FA 11 HOH   403  1803 253  HOH   HOH B . 
FA 11 HOH   404  1804 299  HOH   HOH B . 
FA 11 HOH   405  1805 559  HOH   HOH B . 
FA 11 HOH   406  1806 2172 HOH   HOH B . 
FA 11 HOH   407  1807 1512 HOH   HOH B . 
FA 11 HOH   408  1808 903  HOH   HOH B . 
FA 11 HOH   409  1809 553  HOH   HOH B . 
FA 11 HOH   410  1810 162  HOH   HOH B . 
FA 11 HOH   411  1811 1761 HOH   HOH B . 
FA 11 HOH   412  1812 26   HOH   HOH B . 
FA 11 HOH   413  1813 1517 HOH   HOH B . 
FA 11 HOH   414  1814 1810 HOH   HOH B . 
FA 11 HOH   415  1815 1185 HOH   HOH B . 
FA 11 HOH   416  1816 531  HOH   HOH B . 
FA 11 HOH   417  1817 729  HOH   HOH B . 
FA 11 HOH   418  1818 38   HOH   HOH B . 
FA 11 HOH   419  1819 466  HOH   HOH B . 
FA 11 HOH   420  1820 1184 HOH   HOH B . 
FA 11 HOH   421  1821 11   HOH   HOH B . 
FA 11 HOH   422  1822 16   HOH   HOH B . 
FA 11 HOH   423  1823 841  HOH   HOH B . 
FA 11 HOH   424  1824 348  HOH   HOH B . 
FA 11 HOH   425  1825 963  HOH   HOH B . 
FA 11 HOH   426  1826 869  HOH   HOH B . 
FA 11 HOH   427  1827 444  HOH   HOH B . 
FA 11 HOH   428  1828 1387 HOH   HOH B . 
FA 11 HOH   429  1829 803  HOH   HOH B . 
FA 11 HOH   430  1830 1402 HOH   HOH B . 
FA 11 HOH   431  1831 1040 HOH   HOH B . 
FA 11 HOH   432  1832 431  HOH   HOH B . 
FA 11 HOH   433  1833 1541 HOH   HOH B . 
FA 11 HOH   434  1834 285  HOH   HOH B . 
FA 11 HOH   435  1835 1865 HOH   HOH B . 
FA 11 HOH   436  1836 765  HOH   HOH B . 
FA 11 HOH   437  1837 970  HOH   HOH B . 
FA 11 HOH   438  1838 83   HOH   HOH B . 
FA 11 HOH   439  1839 136  HOH   HOH B . 
FA 11 HOH   440  1840 93   HOH   HOH B . 
FA 11 HOH   441  1841 1200 HOH   HOH B . 
FA 11 HOH   442  1842 259  HOH   HOH B . 
FA 11 HOH   443  1843 613  HOH   HOH B . 
FA 11 HOH   444  1844 325  HOH   HOH B . 
FA 11 HOH   445  1845 102  HOH   HOH B . 
FA 11 HOH   446  1846 804  HOH   HOH B . 
FA 11 HOH   447  1847 220  HOH   HOH B . 
FA 11 HOH   448  1848 1766 HOH   HOH B . 
FA 11 HOH   449  1849 29   HOH   HOH B . 
FA 11 HOH   450  1850 414  HOH   HOH B . 
FA 11 HOH   451  1851 1626 HOH   HOH B . 
FA 11 HOH   452  1852 151  HOH   HOH B . 
FA 11 HOH   453  1853 389  HOH   HOH B . 
FA 11 HOH   454  1854 932  HOH   HOH B . 
FA 11 HOH   455  1855 273  HOH   HOH B . 
FA 11 HOH   456  1856 1548 HOH   HOH B . 
FA 11 HOH   457  1857 358  HOH   HOH B . 
FA 11 HOH   458  1858 1581 HOH   HOH B . 
FA 11 HOH   459  1859 1082 HOH   HOH B . 
FA 11 HOH   460  1860 352  HOH   HOH B . 
FA 11 HOH   461  1861 723  HOH   HOH B . 
FA 11 HOH   462  1862 128  HOH   HOH B . 
FA 11 HOH   463  1863 818  HOH   HOH B . 
FA 11 HOH   464  1864 731  HOH   HOH B . 
FA 11 HOH   465  1865 252  HOH   HOH B . 
FA 11 HOH   466  1866 265  HOH   HOH B . 
FA 11 HOH   467  1867 2171 HOH   HOH B . 
FA 11 HOH   468  1868 968  HOH   HOH B . 
FA 11 HOH   469  1869 629  HOH   HOH B . 
FA 11 HOH   470  1870 1389 HOH   HOH B . 
FA 11 HOH   471  1871 1553 HOH   HOH B . 
FA 11 HOH   472  1872 883  HOH   HOH B . 
FA 11 HOH   473  1873 1243 HOH   HOH B . 
FA 11 HOH   474  1874 155  HOH   HOH B . 
FA 11 HOH   475  1875 902  HOH   HOH B . 
FA 11 HOH   476  1876 76   HOH   HOH B . 
FA 11 HOH   477  1877 1001 HOH   HOH B . 
FA 11 HOH   478  1878 85   HOH   HOH B . 
FA 11 HOH   479  1879 1411 HOH   HOH B . 
FA 11 HOH   480  1880 402  HOH   HOH B . 
FA 11 HOH   481  1881 817  HOH   HOH B . 
FA 11 HOH   482  1882 27   HOH   HOH B . 
FA 11 HOH   483  1883 929  HOH   HOH B . 
FA 11 HOH   484  1884 6    HOH   HOH B . 
FA 11 HOH   485  1885 208  HOH   HOH B . 
FA 11 HOH   486  1886 300  HOH   HOH B . 
FA 11 HOH   487  1887 644  HOH   HOH B . 
FA 11 HOH   488  1888 1265 HOH   HOH B . 
FA 11 HOH   489  1889 178  HOH   HOH B . 
FA 11 HOH   490  1890 521  HOH   HOH B . 
FA 11 HOH   491  1891 1377 HOH   HOH B . 
FA 11 HOH   492  1892 1704 HOH   HOH B . 
FA 11 HOH   493  1893 1575 HOH   HOH B . 
FA 11 HOH   494  1894 436  HOH   HOH B . 
FA 11 HOH   495  1895 207  HOH   HOH B . 
FA 11 HOH   496  1896 1055 HOH   HOH B . 
FA 11 HOH   497  1897 807  HOH   HOH B . 
FA 11 HOH   498  1898 1473 HOH   HOH B . 
FA 11 HOH   499  1899 191  HOH   HOH B . 
FA 11 HOH   500  1900 1596 HOH   HOH B . 
FA 11 HOH   501  1901 1428 HOH   HOH B . 
FA 11 HOH   502  1902 480  HOH   HOH B . 
FA 11 HOH   503  1903 380  HOH   HOH B . 
FA 11 HOH   504  1904 146  HOH   HOH B . 
FA 11 HOH   505  1905 39   HOH   HOH B . 
FA 11 HOH   506  1906 569  HOH   HOH B . 
FA 11 HOH   507  1907 1506 HOH   HOH B . 
FA 11 HOH   508  1908 187  HOH   HOH B . 
FA 11 HOH   509  1909 2239 HOH   HOH B . 
FA 11 HOH   510  1910 1529 HOH   HOH B . 
FA 11 HOH   511  1911 790  HOH   HOH B . 
FA 11 HOH   512  1912 423  HOH   HOH B . 
FA 11 HOH   513  1913 111  HOH   HOH B . 
FA 11 HOH   514  1914 1636 HOH   HOH B . 
FA 11 HOH   515  1915 165  HOH   HOH B . 
FA 11 HOH   516  1916 656  HOH   HOH B . 
FA 11 HOH   517  1917 1005 HOH   HOH B . 
FA 11 HOH   518  1918 135  HOH   HOH B . 
FA 11 HOH   519  1919 69   HOH   HOH B . 
FA 11 HOH   520  1920 565  HOH   HOH B . 
FA 11 HOH   521  1921 79   HOH   HOH B . 
FA 11 HOH   522  1922 1320 HOH   HOH B . 
FA 11 HOH   523  1923 529  HOH   HOH B . 
FA 11 HOH   524  1924 1465 HOH   HOH B . 
FA 11 HOH   525  1925 513  HOH   HOH B . 
FA 11 HOH   526  1926 1118 HOH   HOH B . 
FA 11 HOH   527  1927 113  HOH   HOH B . 
FA 11 HOH   528  1928 821  HOH   HOH B . 
FA 11 HOH   529  1929 1637 HOH   HOH B . 
FA 11 HOH   530  1930 1334 HOH   HOH B . 
FA 11 HOH   531  1931 977  HOH   HOH B . 
FA 11 HOH   532  1932 1128 HOH   HOH B . 
FA 11 HOH   533  1933 665  HOH   HOH B . 
FA 11 HOH   534  1934 1044 HOH   HOH B . 
FA 11 HOH   535  1935 1016 HOH   HOH B . 
FA 11 HOH   536  1936 132  HOH   HOH B . 
FA 11 HOH   537  1937 508  HOH   HOH B . 
FA 11 HOH   538  1938 340  HOH   HOH B . 
FA 11 HOH   539  1939 514  HOH   HOH B . 
FA 11 HOH   540  1940 457  HOH   HOH B . 
FA 11 HOH   541  1941 580  HOH   HOH B . 
FA 11 HOH   542  1942 1650 HOH   HOH B . 
FA 11 HOH   543  1943 1469 HOH   HOH B . 
FA 11 HOH   544  1944 228  HOH   HOH B . 
FA 11 HOH   545  1945 301  HOH   HOH B . 
FA 11 HOH   546  1946 455  HOH   HOH B . 
FA 11 HOH   547  1947 483  HOH   HOH B . 
FA 11 HOH   548  1948 688  HOH   HOH B . 
FA 11 HOH   549  1949 1108 HOH   HOH B . 
FA 11 HOH   550  1950 973  HOH   HOH B . 
FA 11 HOH   551  1951 468  HOH   HOH B . 
FA 11 HOH   552  1952 584  HOH   HOH B . 
FA 11 HOH   553  1953 428  HOH   HOH B . 
FA 11 HOH   554  1954 792  HOH   HOH B . 
FA 11 HOH   555  1955 1296 HOH   HOH B . 
FA 11 HOH   556  1956 935  HOH   HOH B . 
FA 11 HOH   557  1957 488  HOH   HOH B . 
FA 11 HOH   558  1958 1919 HOH   HOH B . 
FA 11 HOH   559  1959 1130 HOH   HOH B . 
FA 11 HOH   560  1960 335  HOH   HOH B . 
FA 11 HOH   561  1961 175  HOH   HOH B . 
FA 11 HOH   562  1962 524  HOH   HOH B . 
FA 11 HOH   563  1963 179  HOH   HOH B . 
FA 11 HOH   564  1964 1355 HOH   HOH B . 
FA 11 HOH   565  1965 1180 HOH   HOH B . 
FA 11 HOH   566  1966 2104 HOH   HOH B . 
FA 11 HOH   567  1967 631  HOH   HOH B . 
FA 11 HOH   568  1968 1146 HOH   HOH B . 
FA 11 HOH   569  1969 519  HOH   HOH B . 
FA 11 HOH   570  1970 1168 HOH   HOH B . 
FA 11 HOH   571  1971 1140 HOH   HOH B . 
FA 11 HOH   572  1972 1647 HOH   HOH B . 
FA 11 HOH   573  1973 173  HOH   HOH B . 
FA 11 HOH   574  1974 1807 HOH   HOH B . 
FA 11 HOH   575  1975 1694 HOH   HOH B . 
FA 11 HOH   576  1976 1318 HOH   HOH B . 
FA 11 HOH   577  1977 1640 HOH   HOH B . 
FA 11 HOH   578  1978 13   HOH   HOH B . 
FA 11 HOH   579  1979 653  HOH   HOH B . 
FA 11 HOH   580  1980 2200 HOH   HOH B . 
FA 11 HOH   581  1981 1999 HOH   HOH B . 
FA 11 HOH   582  1982 110  HOH   HOH B . 
FA 11 HOH   583  1983 1017 HOH   HOH B . 
FA 11 HOH   584  1984 154  HOH   HOH B . 
FA 11 HOH   585  1985 2165 HOH   HOH B . 
FA 11 HOH   586  1986 1508 HOH   HOH B . 
FA 11 HOH   587  1987 419  HOH   HOH B . 
FA 11 HOH   588  1988 1221 HOH   HOH B . 
FA 11 HOH   589  1989 1451 HOH   HOH B . 
FA 11 HOH   590  1990 802  HOH   HOH B . 
FA 11 HOH   591  1991 152  HOH   HOH B . 
FA 11 HOH   592  1992 878  HOH   HOH B . 
FA 11 HOH   593  1993 156  HOH   HOH B . 
FA 11 HOH   594  1994 527  HOH   HOH B . 
FA 11 HOH   595  1995 704  HOH   HOH B . 
FA 11 HOH   596  1996 287  HOH   HOH B . 
FA 11 HOH   597  1997 256  HOH   HOH B . 
FA 11 HOH   598  1998 463  HOH   HOH B . 
FA 11 HOH   599  1999 567  HOH   HOH B . 
FA 11 HOH   600  2000 742  HOH   HOH B . 
FA 11 HOH   601  2001 201  HOH   HOH B . 
FA 11 HOH   602  2002 331  HOH   HOH B . 
FA 11 HOH   603  2003 642  HOH   HOH B . 
FA 11 HOH   604  2004 1614 HOH   HOH B . 
FA 11 HOH   605  2005 67   HOH   HOH B . 
FA 11 HOH   606  2006 925  HOH   HOH B . 
FA 11 HOH   607  2007 551  HOH   HOH B . 
FA 11 HOH   608  2008 863  HOH   HOH B . 
FA 11 HOH   609  2009 980  HOH   HOH B . 
FA 11 HOH   610  2010 1211 HOH   HOH B . 
FA 11 HOH   611  2011 1188 HOH   HOH B . 
FA 11 HOH   612  2012 1063 HOH   HOH B . 
FA 11 HOH   613  2013 1    HOH   HOH B . 
FA 11 HOH   614  2014 449  HOH   HOH B . 
FA 11 HOH   615  2015 528  HOH   HOH B . 
FA 11 HOH   616  2016 1275 HOH   HOH B . 
FA 11 HOH   617  2017 1099 HOH   HOH B . 
FA 11 HOH   618  2018 116  HOH   HOH B . 
FA 11 HOH   619  2019 2211 HOH   HOH B . 
FA 11 HOH   620  2020 350  HOH   HOH B . 
FA 11 HOH   621  2021 1749 HOH   HOH B . 
FA 11 HOH   622  2022 205  HOH   HOH B . 
FA 11 HOH   623  2023 857  HOH   HOH B . 
FA 11 HOH   624  2024 1216 HOH   HOH B . 
FA 11 HOH   625  2025 2055 HOH   HOH B . 
FA 11 HOH   626  2026 621  HOH   HOH B . 
FA 11 HOH   627  2027 2047 HOH   HOH B . 
FA 11 HOH   628  2028 14   HOH   HOH B . 
FA 11 HOH   629  2029 1430 HOH   HOH B . 
FA 11 HOH   630  2030 896  HOH   HOH B . 
FA 11 HOH   631  2031 1561 HOH   HOH B . 
FA 11 HOH   632  2032 706  HOH   HOH B . 
FA 11 HOH   633  2033 952  HOH   HOH B . 
FA 11 HOH   634  2034 1114 HOH   HOH B . 
FA 11 HOH   635  2035 1086 HOH   HOH B . 
FA 11 HOH   636  2036 597  HOH   HOH B . 
FA 11 HOH   637  2037 736  HOH   HOH B . 
FA 11 HOH   638  2038 71   HOH   HOH B . 
FA 11 HOH   639  2039 1053 HOH   HOH B . 
FA 11 HOH   640  2040 1522 HOH   HOH B . 
FA 11 HOH   641  2041 695  HOH   HOH B . 
FA 11 HOH   642  2042 1710 HOH   HOH B . 
FA 11 HOH   643  2043 310  HOH   HOH B . 
FA 11 HOH   644  2044 447  HOH   HOH B . 
FA 11 HOH   645  2045 327  HOH   HOH B . 
FA 11 HOH   646  2046 2209 HOH   HOH B . 
FA 11 HOH   647  2047 292  HOH   HOH B . 
FA 11 HOH   648  2048 467  HOH   HOH B . 
FA 11 HOH   649  2049 1272 HOH   HOH B . 
FA 11 HOH   650  2050 87   HOH   HOH B . 
FA 11 HOH   651  2051 1758 HOH   HOH B . 
FA 11 HOH   652  2052 262  HOH   HOH B . 
FA 11 HOH   653  2053 149  HOH   HOH B . 
FA 11 HOH   654  2054 426  HOH   HOH B . 
FA 11 HOH   655  2055 806  HOH   HOH B . 
FA 11 HOH   656  2056 1097 HOH   HOH B . 
FA 11 HOH   657  2057 1242 HOH   HOH B . 
FA 11 HOH   658  2058 1381 HOH   HOH B . 
FA 11 HOH   659  2059 1276 HOH   HOH B . 
FA 11 HOH   660  2060 487  HOH   HOH B . 
FA 11 HOH   661  2061 787  HOH   HOH B . 
FA 11 HOH   662  2062 443  HOH   HOH B . 
FA 11 HOH   663  2063 838  HOH   HOH B . 
FA 11 HOH   664  2064 1366 HOH   HOH B . 
FA 11 HOH   665  2065 2174 HOH   HOH B . 
FA 11 HOH   666  2066 1601 HOH   HOH B . 
FA 11 HOH   667  2067 520  HOH   HOH B . 
FA 11 HOH   668  2068 400  HOH   HOH B . 
FA 11 HOH   669  2069 270  HOH   HOH B . 
FA 11 HOH   670  2070 530  HOH   HOH B . 
FA 11 HOH   671  2071 375  HOH   HOH B . 
FA 11 HOH   672  2072 1763 HOH   HOH B . 
FA 11 HOH   673  2073 347  HOH   HOH B . 
FA 11 HOH   674  2074 1665 HOH   HOH B . 
FA 11 HOH   675  2075 525  HOH   HOH B . 
FA 11 HOH   676  2076 1444 HOH   HOH B . 
FA 11 HOH   677  2077 536  HOH   HOH B . 
FA 11 HOH   678  2078 42   HOH   HOH B . 
FA 11 HOH   679  2079 406  HOH   HOH B . 
FA 11 HOH   680  2080 2059 HOH   HOH B . 
FA 11 HOH   681  2081 1089 HOH   HOH B . 
FA 11 HOH   682  2082 1072 HOH   HOH B . 
FA 11 HOH   683  2083 376  HOH   HOH B . 
FA 11 HOH   684  2084 930  HOH   HOH B . 
FA 11 HOH   685  2085 101  HOH   HOH B . 
FA 11 HOH   686  2086 501  HOH   HOH B . 
FA 11 HOH   687  2087 1126 HOH   HOH B . 
FA 11 HOH   688  2088 1058 HOH   HOH B . 
FA 11 HOH   689  2089 1504 HOH   HOH B . 
FA 11 HOH   690  2090 1295 HOH   HOH B . 
FA 11 HOH   691  2091 1571 HOH   HOH B . 
FA 11 HOH   692  2092 216  HOH   HOH B . 
FA 11 HOH   693  2093 1502 HOH   HOH B . 
FA 11 HOH   694  2094 911  HOH   HOH B . 
FA 11 HOH   695  2095 337  HOH   HOH B . 
FA 11 HOH   696  2096 383  HOH   HOH B . 
FA 11 HOH   697  2097 906  HOH   HOH B . 
FA 11 HOH   698  2098 2143 HOH   HOH B . 
FA 11 HOH   699  2099 1595 HOH   HOH B . 
FA 11 HOH   700  2100 108  HOH   HOH B . 
FA 11 HOH   701  2101 1349 HOH   HOH B . 
FA 11 HOH   702  2102 385  HOH   HOH B . 
FA 11 HOH   703  2103 453  HOH   HOH B . 
FA 11 HOH   704  2104 2054 HOH   HOH B . 
FA 11 HOH   705  2105 1205 HOH   HOH B . 
FA 11 HOH   706  2106 655  HOH   HOH B . 
FA 11 HOH   707  2107 632  HOH   HOH B . 
FA 11 HOH   708  2108 1687 HOH   HOH B . 
FA 11 HOH   709  2109 471  HOH   HOH B . 
FA 11 HOH   710  2110 96   HOH   HOH B . 
FA 11 HOH   711  2111 1825 HOH   HOH B . 
FA 11 HOH   712  2112 1417 HOH   HOH B . 
FA 11 HOH   713  2113 1679 HOH   HOH B . 
FA 11 HOH   714  2114 1348 HOH   HOH B . 
FA 11 HOH   715  2115 1657 HOH   HOH B . 
FA 11 HOH   716  2116 269  HOH   HOH B . 
FA 11 HOH   717  2117 1169 HOH   HOH B . 
FA 11 HOH   718  2118 2219 HOH   HOH B . 
FA 11 HOH   719  2119 674  HOH   HOH B . 
FA 11 HOH   720  2120 230  HOH   HOH B . 
FA 11 HOH   721  2121 1869 HOH   HOH B . 
FA 11 HOH   722  2122 854  HOH   HOH B . 
FA 11 HOH   723  2123 1474 HOH   HOH B . 
FA 11 HOH   724  2124 1713 HOH   HOH B . 
FA 11 HOH   725  2125 709  HOH   HOH B . 
FA 11 HOH   726  2126 257  HOH   HOH B . 
FA 11 HOH   727  2127 421  HOH   HOH B . 
FA 11 HOH   728  2128 994  HOH   HOH B . 
FA 11 HOH   729  2129 1340 HOH   HOH B . 
FA 11 HOH   730  2130 1261 HOH   HOH B . 
FA 11 HOH   731  2131 81   HOH   HOH B . 
FA 11 HOH   732  2132 721  HOH   HOH B . 
FA 11 HOH   733  2133 1372 HOH   HOH B . 
FA 11 HOH   734  2134 8    HOH   HOH B . 
FA 11 HOH   735  2135 450  HOH   HOH B . 
FA 11 HOH   736  2136 349  HOH   HOH B . 
FA 11 HOH   737  2137 1060 HOH   HOH B . 
FA 11 HOH   738  2138 361  HOH   HOH B . 
FA 11 HOH   739  2139 374  HOH   HOH B . 
FA 11 HOH   740  2140 114  HOH   HOH B . 
FA 11 HOH   741  2141 1569 HOH   HOH B . 
FA 11 HOH   742  2142 548  HOH   HOH B . 
FA 11 HOH   743  2143 2202 HOH   HOH B . 
FA 11 HOH   744  2144 1373 HOH   HOH B . 
FA 11 HOH   745  2145 1741 HOH   HOH B . 
FA 11 HOH   746  2146 82   HOH   HOH B . 
FA 11 HOH   747  2147 610  HOH   HOH B . 
FA 11 HOH   748  2148 80   HOH   HOH B . 
FA 11 HOH   749  2149 733  HOH   HOH B . 
FA 11 HOH   750  2150 2093 HOH   HOH B . 
FA 11 HOH   751  2151 2061 HOH   HOH B . 
FA 11 HOH   752  2152 1951 HOH   HOH B . 
FA 11 HOH   753  2153 229  HOH   HOH B . 
FA 11 HOH   754  2154 982  HOH   HOH B . 
FA 11 HOH   755  2155 910  HOH   HOH B . 
FA 11 HOH   756  2156 678  HOH   HOH B . 
FA 11 HOH   757  2157 9    HOH   HOH B . 
FA 11 HOH   758  2158 1707 HOH   HOH B . 
FA 11 HOH   759  2159 1980 HOH   HOH B . 
FA 11 HOH   760  2160 690  HOH   HOH B . 
FA 11 HOH   761  2161 1691 HOH   HOH B . 
FA 11 HOH   762  2162 25   HOH   HOH B . 
FA 11 HOH   763  2163 1273 HOH   HOH B . 
FA 11 HOH   764  2164 657  HOH   HOH B . 
FA 11 HOH   765  2165 1170 HOH   HOH B . 
FA 11 HOH   766  2166 856  HOH   HOH B . 
FA 11 HOH   767  2167 1785 HOH   HOH B . 
FA 11 HOH   768  2168 1940 HOH   HOH B . 
FA 11 HOH   769  2169 1337 HOH   HOH B . 
FA 11 HOH   770  2170 596  HOH   HOH B . 
FA 11 HOH   771  2171 1824 HOH   HOH B . 
FA 11 HOH   772  2172 2028 HOH   HOH B . 
FA 11 HOH   773  2173 2183 HOH   HOH B . 
FA 11 HOH   774  2174 775  HOH   HOH B . 
FA 11 HOH   775  2175 107  HOH   HOH B . 
FA 11 HOH   776  2176 1934 HOH   HOH B . 
FA 11 HOH   777  2177 1927 HOH   HOH B . 
FA 11 HOH   778  2178 989  HOH   HOH B . 
FA 11 HOH   779  2179 1073 HOH   HOH B . 
FA 11 HOH   780  2180 267  HOH   HOH B . 
FA 11 HOH   781  2181 812  HOH   HOH B . 
FA 11 HOH   782  2182 756  HOH   HOH B . 
FA 11 HOH   783  2183 1495 HOH   HOH B . 
FA 11 HOH   784  2184 794  HOH   HOH B . 
FA 11 HOH   785  2185 824  HOH   HOH B . 
FA 11 HOH   786  2186 2213 HOH   HOH B . 
FA 11 HOH   787  2187 612  HOH   HOH B . 
FA 11 HOH   788  2188 1217 HOH   HOH B . 
FA 11 HOH   789  2189 2169 HOH   HOH B . 
FA 11 HOH   790  2190 334  HOH   HOH B . 
FA 11 HOH   791  2191 1527 HOH   HOH B . 
FA 11 HOH   792  2192 1867 HOH   HOH B . 
FA 11 HOH   793  2193 523  HOH   HOH B . 
FA 11 HOH   794  2194 851  HOH   HOH B . 
FA 11 HOH   795  2195 2040 HOH   HOH B . 
FA 11 HOH   796  2196 2137 HOH   HOH B . 
FA 11 HOH   797  2197 1844 HOH   HOH B . 
FA 11 HOH   798  2198 2027 HOH   HOH B . 
FA 11 HOH   799  2199 673  HOH   HOH B . 
FA 11 HOH   800  2200 1294 HOH   HOH B . 
FA 11 HOH   801  2201 1714 HOH   HOH B . 
FA 11 HOH   802  2202 1765 HOH   HOH B . 
FA 11 HOH   803  2203 1775 HOH   HOH B . 
FA 11 HOH   804  2204 2167 HOH   HOH B . 
FA 11 HOH   805  2205 1445 HOH   HOH B . 
FA 11 HOH   806  2206 2001 HOH   HOH B . 
FA 11 HOH   807  2207 1941 HOH   HOH B . 
FA 11 HOH   808  2208 1576 HOH   HOH B . 
FA 11 HOH   809  2209 855  HOH   HOH B . 
FA 11 HOH   810  2210 2080 HOH   HOH B . 
FA 11 HOH   811  2211 2184 HOH   HOH B . 
FA 11 HOH   812  2212 1036 HOH   HOH B . 
FA 11 HOH   813  2213 1836 HOH   HOH B . 
FA 11 HOH   814  2214 1671 HOH   HOH B . 
FA 11 HOH   815  2215 1668 HOH   HOH B . 
FA 11 HOH   816  2216 2210 HOH   HOH B . 
FA 11 HOH   817  2217 2046 HOH   HOH B . 
FA 11 HOH   818  2218 1532 HOH   HOH B . 
FA 11 HOH   819  2219 2131 HOH   HOH B . 
FA 11 HOH   820  2220 1966 HOH   HOH B . 
FA 11 HOH   821  2221 1653 HOH   HOH B . 
FA 11 HOH   822  2222 1944 HOH   HOH B . 
FA 11 HOH   823  2223 425  HOH   HOH B . 
FA 11 HOH   824  2224 682  HOH   HOH B . 
FA 11 HOH   825  2225 538  HOH   HOH B . 
FA 11 HOH   826  2226 540  HOH   HOH B . 
FA 11 HOH   827  2227 2106 HOH   HOH B . 
FA 11 HOH   828  2228 2026 HOH   HOH B . 
FA 11 HOH   829  2229 1973 HOH   HOH B . 
FA 11 HOH   830  2230 2201 HOH   HOH B . 
FA 11 HOH   831  2231 1079 HOH   HOH B . 
FA 11 HOH   832  2232 718  HOH   HOH B . 
FA 11 HOH   833  2233 886  HOH   HOH B . 
FA 11 HOH   834  2234 1245 HOH   HOH B . 
FA 11 HOH   835  2235 1829 HOH   HOH B . 
FA 11 HOH   836  2236 1725 HOH   HOH B . 
FA 11 HOH   837  2237 2011 HOH   HOH B . 
FA 11 HOH   838  2238 820  HOH   HOH B . 
FA 11 HOH   839  2239 734  HOH   HOH B . 
FA 11 HOH   840  2240 1727 HOH   HOH B . 
FA 11 HOH   841  2241 1833 HOH   HOH B . 
FA 11 HOH   842  2242 2084 HOH   HOH B . 
FA 11 HOH   843  2243 1435 HOH   HOH B . 
FA 11 HOH   844  2244 1664 HOH   HOH B . 
FA 11 HOH   845  2245 895  HOH   HOH B . 
FA 11 HOH   846  2246 2194 HOH   HOH B . 
FA 11 HOH   847  2247 1995 HOH   HOH B . 
FA 11 HOH   848  2248 1912 HOH   HOH B . 
FA 11 HOH   849  2249 675  HOH   HOH B . 
FA 11 HOH   850  2250 773  HOH   HOH B . 
FA 11 HOH   851  2251 2189 HOH   HOH B . 
FA 11 HOH   852  2252 1489 HOH   HOH B . 
FA 11 HOH   853  2253 2069 HOH   HOH B . 
FA 11 HOH   854  2254 2107 HOH   HOH B . 
FA 11 HOH   855  2255 1480 HOH   HOH B . 
FA 11 HOH   856  2256 1572 HOH   HOH B . 
FA 11 HOH   857  2257 2116 HOH   HOH B . 
FA 11 HOH   858  2258 1406 HOH   HOH B . 
FA 11 HOH   859  2259 1240 HOH   HOH B . 
FA 11 HOH   860  2260 1458 HOH   HOH B . 
FA 11 HOH   861  2261 1145 HOH   HOH B . 
FA 11 HOH   862  2262 1326 HOH   HOH B . 
FA 11 HOH   863  2263 2079 HOH   HOH B . 
FA 11 HOH   864  2264 167  HOH   HOH B . 
FA 11 HOH   865  2265 2057 HOH   HOH B . 
FA 11 HOH   866  2266 1678 HOH   HOH B . 
FA 11 HOH   867  2267 1970 HOH   HOH B . 
FA 11 HOH   868  2268 2100 HOH   HOH B . 
FA 11 HOH   869  2269 1928 HOH   HOH B . 
FA 11 HOH   870  2270 1530 HOH   HOH B . 
FA 11 HOH   871  2271 1523 HOH   HOH B . 
FA 11 HOH   872  2272 1525 HOH   HOH B . 
FA 11 HOH   873  2273 1801 HOH   HOH B . 
FA 11 HOH   874  2274 2    HOH   HOH B . 
FA 11 HOH   875  2275 2129 HOH   HOH B . 
FA 11 HOH   876  2276 1333 HOH   HOH B . 
FA 11 HOH   877  2277 2043 HOH   HOH B . 
FA 11 HOH   878  2278 1870 HOH   HOH B . 
FA 11 HOH   879  2279 849  HOH   HOH B . 
FA 11 HOH   880  2280 2160 HOH   HOH B . 
FA 11 HOH   881  2281 1832 HOH   HOH B . 
FA 11 HOH   882  2282 573  HOH   HOH B . 
FA 11 HOH   883  2283 1754 HOH   HOH B . 
FA 11 HOH   884  2284 2170 HOH   HOH B . 
FA 11 HOH   885  2285 496  HOH   HOH B . 
FA 11 HOH   886  2286 1253 HOH   HOH B . 
FA 11 HOH   887  2287 760  HOH   HOH B . 
FA 11 HOH   888  2288 1622 HOH   HOH B . 
FA 11 HOH   889  2289 1002 HOH   HOH B . 
FA 11 HOH   890  2290 1718 HOH   HOH B . 
FA 11 HOH   891  2291 900  HOH   HOH B . 
FA 11 HOH   892  2292 2097 HOH   HOH B . 
FA 11 HOH   893  2293 1329 HOH   HOH B . 
FA 11 HOH   894  2294 738  HOH   HOH B . 
FA 11 HOH   895  2295 1312 HOH   HOH B . 
FA 11 HOH   896  2296 1842 HOH   HOH B . 
FA 11 HOH   897  2297 2138 HOH   HOH B . 
FA 11 HOH   898  2298 445  HOH   HOH B . 
FA 11 HOH   899  2299 951  HOH   HOH B . 
FA 11 HOH   900  2300 1400 HOH   HOH B . 
FA 11 HOH   901  2301 1391 HOH   HOH B . 
FA 11 HOH   902  2302 998  HOH   HOH B . 
FA 11 HOH   903  2303 1481 HOH   HOH B . 
FA 11 HOH   904  2304 472  HOH   HOH B . 
FA 11 HOH   905  2305 1189 HOH   HOH B . 
FA 11 HOH   906  2306 1806 HOH   HOH B . 
FA 11 HOH   907  2307 1148 HOH   HOH B . 
FA 11 HOH   908  2308 1252 HOH   HOH B . 
FA 11 HOH   909  2309 1413 HOH   HOH B . 
FA 11 HOH   910  2310 1524 HOH   HOH B . 
FA 11 HOH   911  2311 2177 HOH   HOH B . 
FA 11 HOH   912  2312 2031 HOH   HOH B . 
FA 11 HOH   913  2313 604  HOH   HOH B . 
FA 11 HOH   914  2314 562  HOH   HOH B . 
FA 11 HOH   915  2315 1774 HOH   HOH B . 
FA 11 HOH   916  2316 94   HOH   HOH B . 
FA 11 HOH   917  2317 1173 HOH   HOH B . 
FA 11 HOH   918  2318 2181 HOH   HOH B . 
FA 11 HOH   919  2319 1403 HOH   HOH B . 
FA 11 HOH   920  2320 1206 HOH   HOH B . 
FA 11 HOH   921  2321 853  HOH   HOH B . 
FA 11 HOH   922  2322 1546 HOH   HOH B . 
FA 11 HOH   923  2323 1440 HOH   HOH B . 
FA 11 HOH   924  2324 778  HOH   HOH B . 
FA 11 HOH   925  2325 1617 HOH   HOH B . 
FA 11 HOH   926  2326 1250 HOH   HOH B . 
FA 11 HOH   927  2327 922  HOH   HOH B . 
FA 11 HOH   928  2328 1796 HOH   HOH B . 
FA 11 HOH   929  2329 2191 HOH   HOH B . 
FA 11 HOH   930  2330 1537 HOH   HOH B . 
FA 11 HOH   931  2331 1102 HOH   HOH B . 
FA 11 HOH   932  2332 842  HOH   HOH B . 
FA 11 HOH   933  2333 1582 HOH   HOH B . 
FA 11 HOH   934  2334 956  HOH   HOH B . 
FA 11 HOH   935  2335 1398 HOH   HOH B . 
FA 11 HOH   936  2336 1953 HOH   HOH B . 
FA 11 HOH   937  2337 2042 HOH   HOH B . 
FA 11 HOH   938  2338 2014 HOH   HOH B . 
FA 11 HOH   939  2339 552  HOH   HOH B . 
FA 11 HOH   940  2340 1486 HOH   HOH B . 
FA 11 HOH   941  2341 1783 HOH   HOH B . 
FA 11 HOH   942  2342 1753 HOH   HOH B . 
FA 11 HOH   943  2343 10   HOH   HOH B . 
FA 11 HOH   944  2344 1510 HOH   HOH B . 
FA 11 HOH   945  2345 2090 HOH   HOH B . 
FA 11 HOH   946  2346 2220 HOH   HOH B . 
FA 11 HOH   947  2347 1317 HOH   HOH B . 
FA 11 HOH   948  2348 2102 HOH   HOH B . 
FA 11 HOH   949  2349 4    HOH   HOH B . 
FA 11 HOH   950  2350 2113 HOH   HOH B . 
FA 11 HOH   951  2351 2180 HOH   HOH B . 
FA 11 HOH   952  2352 1834 HOH   HOH B . 
FA 11 HOH   953  2353 1632 HOH   HOH B . 
FA 11 HOH   954  2354 1031 HOH   HOH B . 
FA 11 HOH   955  2355 1409 HOH   HOH B . 
FA 11 HOH   956  2356 2025 HOH   HOH B . 
FA 11 HOH   957  2357 2212 HOH   HOH B . 
FA 11 HOH   958  2358 1983 HOH   HOH B . 
FA 11 HOH   959  2359 1781 HOH   HOH B . 
FA 11 HOH   960  2360 1768 HOH   HOH B . 
FA 11 HOH   961  2361 1229 HOH   HOH B . 
FA 11 HOH   962  2362 875  HOH   HOH B . 
FA 11 HOH   963  2363 2203 HOH   HOH B . 
FA 11 HOH   964  2364 1577 HOH   HOH B . 
FA 11 HOH   965  2365 914  HOH   HOH B . 
FA 11 HOH   966  2366 1863 HOH   HOH B . 
FA 11 HOH   967  2367 2198 HOH   HOH B . 
FA 11 HOH   968  2368 1843 HOH   HOH B . 
FA 11 HOH   969  2369 1545 HOH   HOH B . 
FA 11 HOH   970  2370 2002 HOH   HOH B . 
FA 11 HOH   971  2371 927  HOH   HOH B . 
FA 11 HOH   972  2372 1975 HOH   HOH B . 
FA 11 HOH   973  2373 1344 HOH   HOH B . 
FA 11 HOH   974  2374 1831 HOH   HOH B . 
FA 11 HOH   975  2375 1968 HOH   HOH B . 
FA 11 HOH   976  2376 1197 HOH   HOH B . 
FA 11 HOH   977  2377 1160 HOH   HOH B . 
FA 11 HOH   978  2378 873  HOH   HOH B . 
FA 11 HOH   979  2379 2112 HOH   HOH B . 
FA 11 HOH   980  2380 1830 HOH   HOH B . 
FA 11 HOH   981  2381 1821 HOH   HOH B . 
FA 11 HOH   982  2382 1773 HOH   HOH B . 
FA 11 HOH   983  2383 1316 HOH   HOH B . 
FA 11 HOH   984  2384 602  HOH   HOH B . 
FA 11 HOH   985  2385 1933 HOH   HOH B . 
FA 11 HOH   986  2386 1762 HOH   HOH B . 
FA 11 HOH   987  2387 1972 HOH   HOH B . 
FA 11 HOH   988  2388 1484 HOH   HOH B . 
FA 11 HOH   989  2389 1357 HOH   HOH B . 
FA 11 HOH   990  2390 949  HOH   HOH B . 
FA 11 HOH   991  2391 1747 HOH   HOH B . 
FA 11 HOH   992  2392 1399 HOH   HOH B . 
FA 11 HOH   993  2393 1534 HOH   HOH B . 
FA 11 HOH   994  2394 2228 HOH   HOH B . 
FA 11 HOH   995  2395 639  HOH   HOH B . 
FA 11 HOH   996  2396 1307 HOH   HOH B . 
FA 11 HOH   997  2397 1021 HOH   HOH B . 
FA 11 HOH   998  2398 1981 HOH   HOH B . 
FA 11 HOH   999  2399 1027 HOH   HOH B . 
FA 11 HOH   1000 2400 2186 HOH   HOH B . 
FA 11 HOH   1001 2401 650  HOH   HOH B . 
FA 11 HOH   1002 2402 1641 HOH   HOH B . 
FA 11 HOH   1003 2403 1607 HOH   HOH B . 
FA 11 HOH   1004 2404 2236 HOH   HOH B . 
FA 11 HOH   1005 2405 1921 HOH   HOH B . 
FA 11 HOH   1006 2406 1163 HOH   HOH B . 
FA 11 HOH   1007 2407 1952 HOH   HOH B . 
FA 11 HOH   1008 2408 1930 HOH   HOH B . 
FA 11 HOH   1009 2409 5    HOH   HOH B . 
FA 11 HOH   1010 2410 2101 HOH   HOH B . 
FA 11 HOH   1011 2411 1733 HOH   HOH B . 
FA 11 HOH   1012 2412 1346 HOH   HOH B . 
FA 11 HOH   1013 2413 1590 HOH   HOH B . 
FA 11 HOH   1014 2414 828  HOH   HOH B . 
FA 11 HOH   1015 2415 2121 HOH   HOH B . 
FA 11 HOH   1016 2416 1137 HOH   HOH B . 
FA 11 HOH   1017 2417 1920 HOH   HOH B . 
FA 11 HOH   1018 2418 248  HOH   HOH B . 
FA 11 HOH   1019 2419 557  HOH   HOH B . 
FA 11 HOH   1020 2420 1735 HOH   HOH B . 
FA 11 HOH   1021 2421 636  HOH   HOH B . 
FA 11 HOH   1022 2422 1698 HOH   HOH B . 
FA 11 HOH   1023 2423 1619 HOH   HOH B . 
FA 11 HOH   1024 2424 1405 HOH   HOH B . 
FA 11 HOH   1025 2425 2085 HOH   HOH B . 
FA 11 HOH   1026 2426 2111 HOH   HOH B . 
FA 11 HOH   1027 2427 1356 HOH   HOH B . 
FA 11 HOH   1028 2428 823  HOH   HOH B . 
FA 11 HOH   1029 2429 1218 HOH   HOH B . 
FA 11 HOH   1030 2430 1237 HOH   HOH B . 
FA 11 HOH   1031 2431 1254 HOH   HOH B . 
FA 11 HOH   1032 2432 1745 HOH   HOH B . 
FA 11 HOH   1033 2433 572  HOH   HOH B . 
FA 11 HOH   1034 2434 1957 HOH   HOH B . 
FA 11 HOH   1035 2435 1151 HOH   HOH B . 
FA 11 HOH   1036 2436 683  HOH   HOH B . 
FA 11 HOH   1037 2437 1925 HOH   HOH B . 
FA 11 HOH   1038 2438 1715 HOH   HOH B . 
FA 11 HOH   1039 2439 1057 HOH   HOH B . 
FA 11 HOH   1040 2440 583  HOH   HOH B . 
FA 11 HOH   1041 2441 1866 HOH   HOH B . 
FA 11 HOH   1042 2442 2096 HOH   HOH B . 
FA 11 HOH   1043 2443 1195 HOH   HOH B . 
FA 11 HOH   1044 2444 1392 HOH   HOH B . 
FA 11 HOH   1045 2445 1138 HOH   HOH B . 
FA 11 HOH   1046 2446 1104 HOH   HOH B . 
FA 11 HOH   1047 2447 971  HOH   HOH B . 
FA 11 HOH   1048 2448 1154 HOH   HOH B . 
FA 11 HOH   1049 2449 1123 HOH   HOH B . 
FA 11 HOH   1050 2450 1683 HOH   HOH B . 
FA 11 HOH   1051 2451 2095 HOH   HOH B . 
FA 11 HOH   1052 2452 2148 HOH   HOH B . 
FA 11 HOH   1053 2453 1310 HOH   HOH B . 
FA 11 HOH   1054 2454 1793 HOH   HOH B . 
FA 11 HOH   1055 2455 1871 HOH   HOH B . 
FA 11 HOH   1056 2456 1487 HOH   HOH B . 
FA 11 HOH   1057 2457 897  HOH   HOH B . 
FA 11 HOH   1058 2458 1563 HOH   HOH B . 
FA 11 HOH   1059 2459 1065 HOH   HOH B . 
FA 11 HOH   1060 2460 1407 HOH   HOH B . 
FA 11 HOH   1061 2461 2094 HOH   HOH B . 
FA 11 HOH   1062 2462 1760 HOH   HOH B . 
FA 11 HOH   1063 2463 1967 HOH   HOH B . 
FA 11 HOH   1064 2464 943  HOH   HOH B . 
FA 11 HOH   1065 2465 664  HOH   HOH B . 
FA 11 HOH   1066 2466 815  HOH   HOH B . 
FA 11 HOH   1067 2467 1526 HOH   HOH B . 
FA 11 HOH   1068 2468 1587 HOH   HOH B . 
FA 11 HOH   1069 2469 1937 HOH   HOH B . 
FA 11 HOH   1070 2470 1010 HOH   HOH B . 
FA 11 HOH   1071 2471 1770 HOH   HOH B . 
FA 11 HOH   1072 2472 945  HOH   HOH B . 
FA 11 HOH   1073 2473 1283 HOH   HOH B . 
FA 11 HOH   1074 2474 993  HOH   HOH B . 
FA 11 HOH   1075 2475 714  HOH   HOH B . 
FA 11 HOH   1076 2476 2197 HOH   HOH B . 
FA 11 HOH   1077 2477 1974 HOH   HOH B . 
FA 11 HOH   1078 2478 1784 HOH   HOH B . 
FA 11 HOH   1079 2479 1628 HOH   HOH B . 
FA 11 HOH   1080 2480 2161 HOH   HOH B . 
FA 11 HOH   1081 2481 1860 HOH   HOH B . 
FA 11 HOH   1082 2482 1332 HOH   HOH B . 
FA 11 HOH   1083 2483 1284 HOH   HOH B . 
FA 11 HOH   1084 2484 2164 HOH   HOH B . 
FA 11 HOH   1085 2485 1706 HOH   HOH B . 
FA 11 HOH   1086 2486 279  HOH   HOH B . 
FA 11 HOH   1087 2487 1394 HOH   HOH B . 
FA 11 HOH   1088 2488 892  HOH   HOH B . 
FA 11 HOH   1089 2489 1663 HOH   HOH B . 
FA 11 HOH   1090 2490 1404 HOH   HOH B . 
FA 11 HOH   1091 2491 987  HOH   HOH B . 
FA 11 HOH   1092 2492 1782 HOH   HOH B . 
FA 11 HOH   1093 2493 1982 HOH   HOH B . 
FA 11 HOH   1094 2494 1412 HOH   HOH B . 
FA 11 HOH   1095 2495 1945 HOH   HOH B . 
FA 11 HOH   1096 2496 1737 HOH   HOH B . 
FA 11 HOH   1097 2497 1979 HOH   HOH B . 
FA 11 HOH   1098 2498 687  HOH   HOH B . 
FA 11 HOH   1099 2499 1845 HOH   HOH B . 
FA 11 HOH   1100 2500 2235 HOH   HOH B . 
FA 11 HOH   1101 2501 1854 HOH   HOH B . 
FA 11 HOH   1102 2502 1709 HOH   HOH B . 
FA 11 HOH   1103 2503 1837 HOH   HOH B . 
FA 11 HOH   1104 2504 2000 HOH   HOH B . 
FA 11 HOH   1105 2505 1468 HOH   HOH B . 
FA 11 HOH   1106 2506 1649 HOH   HOH B . 
FA 11 HOH   1107 2507 1327 HOH   HOH B . 
FA 11 HOH   1108 2508 1032 HOH   HOH B . 
FA 11 HOH   1109 2509 1850 HOH   HOH B . 
FA 11 HOH   1110 2510 1851 HOH   HOH B . 
FA 11 HOH   1111 2511 1600 HOH   HOH B . 
FA 11 HOH   1112 2512 944  HOH   HOH B . 
FA 11 HOH   1113 2513 1702 HOH   HOH B . 
FA 11 HOH   1114 2514 2081 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 ARG 122  ? CG  ? A ARG 124  CG  
24  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
25  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
26  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
27  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
28  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
29  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
30  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
31  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
32  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
33  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
34  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
35  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
36  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
37  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
38  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
39  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
40  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
41  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
42  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
43  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
44  1 Y 1 A SER 137  ? OG  ? A SER 139  OG  
45  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
46  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
47  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
48  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
49  1 Y 1 A THR 156  ? OG1 ? A THR 158  OG1 
50  1 Y 1 A THR 156  ? CG2 ? A THR 158  CG2 
51  1 Y 1 A GLU 177  ? CG  ? A GLU 179  CG  
52  1 Y 1 A GLU 177  ? CD  ? A GLU 179  CD  
53  1 Y 1 A GLU 177  ? OE1 ? A GLU 179  OE1 
54  1 Y 1 A GLU 177  ? OE2 ? A GLU 179  OE2 
55  1 Y 1 A GLU 199  ? CG  ? A GLU 201  CG  
56  1 Y 1 A GLU 199  ? CD  ? A GLU 201  CD  
57  1 Y 1 A GLU 199  ? OE1 ? A GLU 201  OE1 
58  1 Y 1 A GLU 199  ? OE2 ? A GLU 201  OE2 
59  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
60  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
61  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
62  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
63  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
64  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
65  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
66  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
67  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
68  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
69  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
70  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
71  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
72  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
73  1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
74  1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
75  1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
76  1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
77  1 Y 1 A THR 481  ? OG1 ? A THR 483  OG1 
78  1 Y 1 A THR 481  ? CG2 ? A THR 483  CG2 
79  1 Y 1 A LEU 482  ? CG  ? A LEU 484  CG  
80  1 Y 1 A LEU 482  ? CD1 ? A LEU 484  CD1 
81  1 Y 1 A LEU 482  ? CD2 ? A LEU 484  CD2 
82  1 Y 1 A TYR 485  ? CG  ? A TYR 487  CG  
83  1 Y 1 A TYR 485  ? CD1 ? A TYR 487  CD1 
84  1 Y 1 A TYR 485  ? CD2 ? A TYR 487  CD2 
85  1 Y 1 A TYR 485  ? CE1 ? A TYR 487  CE1 
86  1 Y 1 A TYR 485  ? CE2 ? A TYR 487  CE2 
87  1 Y 1 A TYR 485  ? CZ  ? A TYR 487  CZ  
88  1 Y 1 A TYR 485  ? OH  ? A TYR 487  OH  
89  1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
90  1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
91  1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
92  1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
93  1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
94  1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
95  1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
96  1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
97  1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
98  1 Y 1 A VAL 500  ? CG1 ? A VAL 502  CG1 
99  1 Y 1 A VAL 500  ? CG2 ? A VAL 502  CG2 
100 1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
101 1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
102 1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
103 1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
104 1 Y 1 A ASP 532  ? CG  ? A ASP 534  CG  
105 1 Y 1 A ASP 532  ? OD1 ? A ASP 534  OD1 
106 1 Y 1 A ASP 532  ? OD2 ? A ASP 534  OD2 
107 1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
108 1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
109 1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
110 1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
111 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
112 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
113 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
114 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
115 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
116 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
117 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
118 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
119 1 Y 1 A SER 633  ? OG  ? A SER 635  OG  
120 1 Y 1 A GLU 785  ? CG  ? A GLU 787  CG  
121 1 Y 1 A GLU 785  ? CD  ? A GLU 787  CD  
122 1 Y 1 A GLU 785  ? OE1 ? A GLU 787  OE1 
123 1 Y 1 A GLU 785  ? OE2 ? A GLU 787  OE2 
124 1 Y 1 A LEU 824  ? CG  ? A LEU 826  CG  
125 1 Y 1 A LEU 824  ? CD1 ? A LEU 826  CD1 
126 1 Y 1 A LEU 824  ? CD2 ? A LEU 826  CD2 
127 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
128 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
129 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
130 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
131 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
132 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
133 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
134 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
135 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
136 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
137 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
138 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
139 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
140 1 Y 1 A ILE 912  ? CG1 ? A ILE 914  CG1 
141 1 Y 1 A ILE 912  ? CG2 ? A ILE 914  CG2 
142 1 Y 1 A ILE 912  ? CD1 ? A ILE 914  CD1 
143 1 Y 1 A GLU 932  ? CG  ? A GLU 934  CG  
144 1 Y 1 A GLU 932  ? CD  ? A GLU 934  CD  
145 1 Y 1 A GLU 932  ? OE1 ? A GLU 934  OE1 
146 1 Y 1 A GLU 932  ? OE2 ? A GLU 934  OE2 
147 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
148 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
149 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
150 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
151 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
152 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
153 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
154 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
155 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
156 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
157 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
158 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
159 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
160 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
161 1 Y 1 A ILE 949  ? CG1 ? A ILE 951  CG1 
162 1 Y 1 A ILE 949  ? CG2 ? A ILE 951  CG2 
163 1 Y 1 A ILE 949  ? CD1 ? A ILE 951  CD1 
164 1 Y 1 A ARG 952  ? CG  ? A ARG 954  CG  
165 1 Y 1 A ARG 952  ? CD  ? A ARG 954  CD  
166 1 Y 1 A ARG 952  ? NE  ? A ARG 954  NE  
167 1 Y 1 A ARG 952  ? CZ  ? A ARG 954  CZ  
168 1 Y 1 A ARG 952  ? NH1 ? A ARG 954  NH1 
169 1 Y 1 A ARG 952  ? NH2 ? A ARG 954  NH2 
170 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
171 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
172 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
173 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
174 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
175 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
176 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
177 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
178 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
179 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
180 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
181 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
182 1 Y 1 A SER 1228 ? OG  ? A SER 1230 OG  
183 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
184 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
185 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
186 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
187 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
188 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
189 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
190 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
191 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
192 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
193 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
194 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
195 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
196 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
197 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
198 1 Y 1 B ILE 60   ? CG1 ? B ILE 62   CG1 
199 1 Y 1 B ILE 60   ? CG2 ? B ILE 62   CG2 
200 1 Y 1 B ILE 60   ? CD1 ? B ILE 62   CD1 
201 1 Y 1 B SER 66   ? OG  ? B SER 68   OG  
202 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
203 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
204 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
205 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
206 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
207 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
208 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
209 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
210 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
211 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
212 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
213 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
214 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
215 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
216 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
217 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
218 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
219 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
220 1 Y 1 B ASP 127  ? CG  ? B ASP 129  CG  
221 1 Y 1 B ASP 127  ? OD1 ? B ASP 129  OD1 
222 1 Y 1 B ASP 127  ? OD2 ? B ASP 129  OD2 
223 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
224 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
225 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
226 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
227 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
228 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
229 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
230 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
231 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
232 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
233 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
234 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
235 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
236 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
237 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
238 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
239 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
240 1 Y 1 B LEU 155  ? CG  ? B LEU 157  CG  
241 1 Y 1 B LEU 155  ? CD1 ? B LEU 157  CD1 
242 1 Y 1 B LEU 155  ? CD2 ? B LEU 157  CD2 
243 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
244 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
245 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
246 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
247 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
248 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
249 1 Y 1 B GLU 193  ? CG  ? B GLU 195  CG  
250 1 Y 1 B GLU 193  ? CD  ? B GLU 195  CD  
251 1 Y 1 B GLU 193  ? OE1 ? B GLU 195  OE1 
252 1 Y 1 B GLU 193  ? OE2 ? B GLU 195  OE2 
253 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
254 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
255 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
256 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
257 1 Y 1 B LYS 209  ? CG  ? B LYS 211  CG  
258 1 Y 1 B LYS 209  ? CD  ? B LYS 211  CD  
259 1 Y 1 B LYS 209  ? CE  ? B LYS 211  CE  
260 1 Y 1 B LYS 209  ? NZ  ? B LYS 211  NZ  
261 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
262 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
263 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
264 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
265 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
266 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
267 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
268 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
269 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
270 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
271 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
272 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
273 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
274 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
275 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
276 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
277 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
278 1 Y 1 B HIS 479  ? CG  ? B HIS 481  CG  
279 1 Y 1 B HIS 479  ? ND1 ? B HIS 481  ND1 
280 1 Y 1 B HIS 479  ? CD2 ? B HIS 481  CD2 
281 1 Y 1 B HIS 479  ? CE1 ? B HIS 481  CE1 
282 1 Y 1 B HIS 479  ? NE2 ? B HIS 481  NE2 
283 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
284 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
285 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
286 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
287 1 Y 1 B THR 481  ? OG1 ? B THR 483  OG1 
288 1 Y 1 B THR 481  ? CG2 ? B THR 483  CG2 
289 1 Y 1 B LEU 482  ? CG  ? B LEU 484  CG  
290 1 Y 1 B LEU 482  ? CD1 ? B LEU 484  CD1 
291 1 Y 1 B LEU 482  ? CD2 ? B LEU 484  CD2 
292 1 Y 1 B TYR 485  ? CG  ? B TYR 487  CG  
293 1 Y 1 B TYR 485  ? CD1 ? B TYR 487  CD1 
294 1 Y 1 B TYR 485  ? CD2 ? B TYR 487  CD2 
295 1 Y 1 B TYR 485  ? CE1 ? B TYR 487  CE1 
296 1 Y 1 B TYR 485  ? CE2 ? B TYR 487  CE2 
297 1 Y 1 B TYR 485  ? CZ  ? B TYR 487  CZ  
298 1 Y 1 B TYR 485  ? OH  ? B TYR 487  OH  
299 1 Y 1 B VAL 487  ? CG1 ? B VAL 489  CG1 
300 1 Y 1 B VAL 487  ? CG2 ? B VAL 489  CG2 
301 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
302 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
303 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
304 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
305 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
306 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
307 1 Y 1 B LEU 490  ? CG  ? B LEU 492  CG  
308 1 Y 1 B LEU 490  ? CD1 ? B LEU 492  CD1 
309 1 Y 1 B LEU 490  ? CD2 ? B LEU 492  CD2 
310 1 Y 1 B LEU 491  ? CG  ? B LEU 493  CG  
311 1 Y 1 B LEU 491  ? CD1 ? B LEU 493  CD1 
312 1 Y 1 B LEU 491  ? CD2 ? B LEU 493  CD2 
313 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
314 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
315 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
316 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
317 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
318 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
319 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
320 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
321 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
322 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
323 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
324 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
325 1 Y 1 B VAL 508  ? CG1 ? B VAL 510  CG1 
326 1 Y 1 B VAL 508  ? CG2 ? B VAL 510  CG2 
327 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
328 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
329 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
330 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
331 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
332 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
333 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
334 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
335 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
336 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
337 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
338 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
339 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
340 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
341 1 Y 1 B ASP 796  ? CG  ? B ASP 798  CG  
342 1 Y 1 B ASP 796  ? OD1 ? B ASP 798  OD1 
343 1 Y 1 B ASP 796  ? OD2 ? B ASP 798  OD2 
344 1 Y 1 B GLU 854  ? CG  ? B GLU 856  CG  
345 1 Y 1 B GLU 854  ? CD  ? B GLU 856  CD  
346 1 Y 1 B GLU 854  ? OE1 ? B GLU 856  OE1 
347 1 Y 1 B GLU 854  ? OE2 ? B GLU 856  OE2 
348 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
349 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
350 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
351 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
352 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
353 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
354 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
355 1 Y 1 B ILE 912  ? CG1 ? B ILE 914  CG1 
356 1 Y 1 B ILE 912  ? CG2 ? B ILE 914  CG2 
357 1 Y 1 B ILE 912  ? CD1 ? B ILE 914  CD1 
358 1 Y 1 B LEU 914  ? CG  ? B LEU 916  CG  
359 1 Y 1 B LEU 914  ? CD1 ? B LEU 916  CD1 
360 1 Y 1 B LEU 914  ? CD2 ? B LEU 916  CD2 
361 1 Y 1 B SER 916  ? OG  ? B SER 918  OG  
362 1 Y 1 B GLU 917  ? CG  ? B GLU 919  CG  
363 1 Y 1 B GLU 917  ? CD  ? B GLU 919  CD  
364 1 Y 1 B GLU 917  ? OE1 ? B GLU 919  OE1 
365 1 Y 1 B GLU 917  ? OE2 ? B GLU 919  OE2 
366 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
367 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
368 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
369 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
370 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
371 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
372 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
373 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
374 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
375 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
376 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
377 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
378 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
379 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
380 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
381 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
382 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
383 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
384 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
385 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
386 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
387 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
388 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
389 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
390 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
391 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
392 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
393 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
394 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
395 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
396 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
397 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
398 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
399 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
400 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
401 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
402 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
403 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
404 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
405 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
406 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
407 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
408 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
409 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
410 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
411 1 Y 1 B SER 1228 ? OG  ? B SER 1230 OG  
412 1 Y 1 B MET 1230 ? CG  ? B MET 1232 CG  
413 1 Y 1 B MET 1230 ? SD  ? B MET 1232 SD  
414 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                   106.30 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9E0B 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.531 
_cell.length_a_esd                 ? 
_cell.length_b                     101.762 
_cell.length_b_esd                 ? 
_cell.length_c                     126.019 
_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                         9E0B 
_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                   9E0B 
_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             2.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.53 
_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 30 mM (2,3-dihydro-1-benzofuran-5-yl)methanol. Crystal was soaked in cryobuffer containing 125 mM (2,3-dihydro-1-benzofuran-5-yl)methanol 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   1.00010 
_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        1.00010 
_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                                       9E0B 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.47 
_reflns.d_resolution_low                               48.25 
_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                                     786650 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.106 
_reflns.pdbx_Rpim_I_all                                0.040 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.098 
_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                                    1.47 
_reflns_shell.d_res_low                                     1.50 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           143821 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             19700 
_reflns_shell.percent_possible_obs                          96.6 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7.3 
_reflns_shell.pdbx_chi_squared                              0.74 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               2.746 
_reflns_shell.pdbx_Rpim_I_all                               1.005 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.370 
_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                                  2.553 
_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                                 9E0B 
_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                            1.47 
_refine.ls_d_res_low                             45.01 
_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                     786650 
_refine.ls_number_reflns_R_free                  39493 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.41 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1782 
_refine.ls_R_factor_R_free                       0.2000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1770 
_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                          0.01 
_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                 22.44 
_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        17802 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         334 
_refine_hist.number_atoms_solvent             2181 
_refine_hist.number_atoms_total               20317 
_refine_hist.d_res_high                       1.47 
_refine_hist.d_res_low                        45.01 
# 
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  ? 18656 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.892  ? 25449 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.932 ? 6933  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.070  ? 2979  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3306  ? 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' 1.47 1.49  . . 1269 25037 96.00  . . . . 0.3379 . . . . . . . . . . . 0.3541 
'X-RAY DIFFRACTION' 1.49 1.50  . . 1306 24773 96.00  . . . . 0.3301 . . . . . . . . . . . 0.3312 
'X-RAY DIFFRACTION' 1.50 1.52  . . 1333 24790 96.00  . . . . 0.3381 . . . . . . . . . . . 0.3468 
'X-RAY DIFFRACTION' 1.52 1.54  . . 1420 24856 97.00  . . . . 0.2917 . . . . . . . . . . . 0.3084 
'X-RAY DIFFRACTION' 1.54 1.56  . . 1371 24800 97.00  . . . . 0.2832 . . . . . . . . . . . 0.2991 
'X-RAY DIFFRACTION' 1.56 1.58  . . 1265 25036 97.00  . . . . 0.2691 . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 1.58 1.61  . . 1336 24982 97.00  . . . . 0.2646 . . . . . . . . . . . 0.2979 
'X-RAY DIFFRACTION' 1.61 1.63  . . 1282 25000 97.00  . . . . 0.2534 . . . . . . . . . . . 0.2732 
'X-RAY DIFFRACTION' 1.63 1.66  . . 1336 25109 97.00  . . . . 0.2442 . . . . . . . . . . . 0.2682 
'X-RAY DIFFRACTION' 1.66 1.68  . . 1373 25102 97.00  . . . . 0.2390 . . . . . . . . . . . 0.2677 
'X-RAY DIFFRACTION' 1.68 1.71  . . 1303 24854 97.00  . . . . 0.2371 . . . . . . . . . . . 0.2602 
'X-RAY DIFFRACTION' 1.71 1.74  . . 1316 25171 97.00  . . . . 0.2220 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 1.74 1.78  . . 1383 25013 97.00  . . . . 0.2159 . . . . . . . . . . . 0.2410 
'X-RAY DIFFRACTION' 1.78 1.81  . . 1364 25006 97.00  . . . . 0.2168 . . . . . . . . . . . 0.2419 
'X-RAY DIFFRACTION' 1.81 1.85  . . 1342 24892 96.00  . . . . 0.2105 . . . . . . . . . . . 0.2386 
'X-RAY DIFFRACTION' 1.85 1.90  . . 1178 22573 87.00  . . . . 0.2187 . . . . . . . . . . . 0.2504 
'X-RAY DIFFRACTION' 1.90 1.94  . . 1217 23700 92.00  . . . . 0.2049 . . . . . . . . . . . 0.2267 
'X-RAY DIFFRACTION' 1.94 2.00  . . 1416 25439 99.00  . . . . 0.1806 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 2.00 2.05  . . 1367 25181 98.00  . . . . 0.1797 . . . . . . . . . . . 0.2081 
'X-RAY DIFFRACTION' 2.05 2.12  . . 1247 25539 98.00  . . . . 0.1719 . . . . . . . . . . . 0.1944 
'X-RAY DIFFRACTION' 2.12 2.20  . . 1239 25570 99.00  . . . . 0.1617 . . . . . . . . . . . 0.1914 
'X-RAY DIFFRACTION' 2.20 2.28  . . 1263 25221 97.00  . . . . 0.1723 . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 2.28 2.39  . . 1440 25385 99.00  . . . . 0.1654 . . . . . . . . . . . 0.1958 
'X-RAY DIFFRACTION' 2.39 2.51  . . 1276 25458 98.00  . . . . 0.1648 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 2.51 2.67  . . 1331 25198 98.00  . . . . 0.1677 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 2.67 2.88  . . 1309 25119 97.00  . . . . 0.1664 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 2.88 3.17  . . 1300 24696 96.00  . . . . 0.1672 . . . . . . . . . . . 0.1890 
'X-RAY DIFFRACTION' 3.17 3.62  . . 1135 22383 87.00  . . . . 0.1571 . . . . . . . . . . . 0.1750 
'X-RAY DIFFRACTION' 3.62 4.57  . . 1375 25586 99.00  . . . . 0.1316 . . . . . . . . . . . 0.1494 
'X-RAY DIFFRACTION' 4.57 45.01 . . 1401 25688 100.00 . . . . 0.1448 . . . . . . . . . . . 0.1611 
# 
_struct.entry_id                     9E0B 
_struct.title                        'Structure of proline utilization A complexed with (2,3-dihydro-1-benzofuran-5-yl)methanol' 
_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        9E0B 
_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 5  ? 
G  N N 4  ? 
H  N N 4  ? 
I  N N 6  ? 
J  N N 7  ? 
K  N N 7  ? 
L  N N 7  ? 
M  N N 7  ? 
N  N N 7  ? 
O  N N 8  ? 
P  N N 2  ? 
Q  N N 9  ? 
R  N N 10 ? 
S  N N 4  ? 
T  N N 3  ? 
U  N N 3  ? 
V  N N 3  ? 
W  N N 4  ? 
X  N N 4  ? 
Y  N N 5  ? 
Z  N N 3  ? 
AA N N 6  ? 
BA N N 7  ? 
CA N N 8  ? 
DA N N 3  ? 
EA N N 11 ? 
FA N N 11 ? 
# 
_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 9E0B A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9E0B 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 9E0B SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9E0B MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9E0B SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9E0B 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)' 12990 ? 
1 MORE         -132  ? 
1 'SSA (A^2)'  77720 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,EA                                        
3 1 B,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,FA                                
# 
_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   ? GLY A 79   ? SER A 57   GLY A 77   1 ? 21 
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 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P8   AA8 ASN A 162  ? GLN A 196  ? ASN A 160  GLN A 194  1 ? 35 
HELX_P HELX_P9   AA9 THR A 202  ? LYS A 216  ? THR A 200  LYS A 214  1 ? 15 
HELX_P HELX_P10  AB1 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P11  AB2 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P12  AB3 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P13  AB4 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P14  AB5 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P15  AB6 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P16  AB7 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P17  AB8 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P18  AB9 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P19  AC1 TYR A 375  ? ASP A 386  ? TYR A 373  ASP A 384  1 ? 12 
HELX_P HELX_P20  AC2 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P21  AC3 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P22  AC4 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P23  AC5 THR A 480  ? ALA A 486  ? THR A 478  ALA A 484  1 ? 7  
HELX_P HELX_P24  AC6 TYR A 487  ? LEU A 493  ? TYR A 485  LEU A 491  1 ? 7  
HELX_P HELX_P25  AC7 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P26  AC8 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P27  AC9 ASP A 518  ? ALA A 525  ? ASP A 516  ALA A 523  1 ? 8  
HELX_P HELX_P28  AD1 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P29  AD2 PHE A 543  ? ARG A 547  ? PHE A 541  ARG A 545  5 ? 5  
HELX_P HELX_P30  AD3 ASN A 557  ? ALA A 573  ? ASN A 555  ALA A 571  1 ? 17 
HELX_P HELX_P31  AD4 SER A 611  ? ALA A 631  ? SER A 609  ALA A 629  1 ? 21 
HELX_P HELX_P32  AD5 PRO A 633  ? GLY A 664  ? PRO A 631  GLY A 662  1 ? 32 
HELX_P HELX_P33  AD6 SER A 666  ? LEU A 692  ? SER A 664  LEU A 690  1 ? 27 
HELX_P HELX_P34  AD7 LEU A 712  ? ALA A 725  ? LEU A 710  ALA A 723  1 ? 14 
HELX_P HELX_P35  AD8 THR A 737  ? ALA A 751  ? THR A 735  ALA A 749  1 ? 15 
HELX_P HELX_P36  AD9 ASP A 764  ? ALA A 774  ? ASP A 762  ALA A 772  1 ? 11 
HELX_P HELX_P37  AE1 SER A 785  ? ASP A 798  ? SER A 783  ASP A 796  1 ? 14 
HELX_P HELX_P38  AE2 LEU A 826  ? ASP A 840  ? LEU A 824  ASP A 838  1 ? 15 
HELX_P HELX_P39  AE3 SER A 841  ? GLN A 844  ? SER A 839  GLN A 842  5 ? 4  
HELX_P HELX_P40  AE4 GLU A 856  ? HIS A 871  ? GLU A 854  HIS A 869  1 ? 16 
HELX_P HELX_P41  AE5 THR A 890  ? LEU A 907  ? THR A 888  LEU A 905  1 ? 18 
HELX_P HELX_P42  AE6 ALA A 917  ? GLY A 923  ? ALA A 915  GLY A 921  5 ? 7  
HELX_P HELX_P43  AE7 LYS A 935  ? LEU A 939  ? LYS A 933  LEU A 937  5 ? 5  
HELX_P HELX_P44  AE8 ARG A 954  ? ASP A 956  ? ARG A 952  ASP A 954  5 ? 3  
HELX_P HELX_P45  AE9 ASP A 957  ? THR A 968  ? ASP A 955  THR A 966  1 ? 12 
HELX_P HELX_P46  AF1 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P47  AF2 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P48  AF3 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P49  AF4 ASP A 1049 ? LYS A 1062 ? ASP A 1047 LYS A 1060 1 ? 14 
HELX_P HELX_P50  AF5 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P51  AF6 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P52  AF7 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P53  AF8 LEU A 1136 ? LYS A 1141 ? LEU A 1134 LYS A 1139 5 ? 6  
HELX_P HELX_P54  AF9 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P55  AG1 ASP A 1156 ? ASP A 1160 ? ASP A 1154 ASP A 1158 5 ? 5  
HELX_P HELX_P56  AG2 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P57  AG3 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P58  AG4 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P59  AG5 ASN A 1228 ? ALA A 1233 ? ASN A 1226 ALA A 1231 1 ? 6  
HELX_P HELX_P60  AG6 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P61  AG7 PRO B 44   ? THR B 57   ? PRO B 42   THR B 55   1 ? 14 
HELX_P HELX_P62  AG8 SER B 59   ? GLY B 79   ? SER B 57   GLY B 77   1 ? 21 
HELX_P HELX_P63  AG9 VAL B 86   ? TYR B 93   ? VAL B 84   TYR B 91   1 ? 8  
HELX_P HELX_P64  AH1 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P65  AH2 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P66  AH3 TRP B 132  ? LEU B 136  ? TRP B 130  LEU B 134  5 ? 5  
HELX_P HELX_P67  AH4 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P68  AH5 ASN B 162  ? GLN B 196  ? ASN B 160  GLN B 194  1 ? 35 
HELX_P HELX_P69  AH6 THR B 202  ? SER B 210  ? THR B 200  SER B 208  1 ? 9  
HELX_P HELX_P70  AH7 SER B 210  ? GLY B 217  ? SER B 208  GLY B 215  1 ? 8  
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  ? LEU B 327  ? ARG B 312  LEU B 325  1 ? 14 
HELX_P HELX_P78  AI6 ASP B 328  ? SER B 332  ? ASP B 326  SER B 330  5 ? 5  
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 LEU B 488  ? LEU B 493  ? LEU B 486  LEU B 491  1 ? 6  
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  ? MET B 574  ? ASN B 555  MET B 572  1 ? 18 
HELX_P HELX_P92  AK2 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P93  AK3 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P94  AK4 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P95  AK5 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P96  AK6 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P97  AK7 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P98  AK8 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P99  AK9 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P100 AL1 SER B 785  ? 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 ? ? I  NAD . O2A ? ? ? 1_555 O  MG  . MG ? ? A NAD 1307 A MG  1313 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc2  metalc ? ? O  MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? A MG  1313 A HOH 1569 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
metalc3  metalc ? ? O  MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? A MG  1313 A HOH 1587 1_555 ? ? ? ? ? ? ? 2.220 ? ? 
metalc4  metalc ? ? O  MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? A MG  1313 A HOH 2008 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc5  metalc ? ? O  MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? A MG  1313 A HOH 2233 1_555 ? ? ? ? ? ? ? 2.192 ? ? 
metalc6  metalc ? ? O  MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? A MG  1313 A HOH 2278 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc7  metalc ? ? AA NAD . O2A ? ? ? 1_555 CA MG  . MG ? ? B NAD 1312 B MG  1314 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc8  metalc ? ? CA MG  . MG  ? ? ? 1_555 FA HOH . O  ? ? B MG  1314 B HOH 1548 1_555 ? ? ? ? ? ? ? 1.941 ? ? 
metalc9  metalc ? ? CA MG  . MG  ? ? ? 1_555 FA HOH . O  ? ? B MG  1314 B HOH 1884 1_555 ? ? ? ? ? ? ? 1.916 ? ? 
metalc10 metalc ? ? CA MG  . MG  ? ? ? 1_555 FA HOH . O  ? ? B MG  1314 B HOH 2134 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc11 metalc ? ? CA MG  . MG  ? ? ? 1_555 FA HOH . O  ? ? B MG  1314 B HOH 2157 1_555 ? ? ? ? ? ? ? 2.187 ? ? 
metalc12 metalc ? ? CA MG  . MG  ? ? ? 1_555 FA HOH . O  ? ? B MG  1314 B HOH 2343 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
# 
_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 ? I  NAD . ? A NAD 1307 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 1569 ? 1_555 86.1  ? 
2  O2A ? I  NAD . ? A NAD 1307 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 1587 ? 1_555 91.9  ? 
3  O   ? EA HOH . ? A HOH 1569 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 1587 ? 1_555 96.4  ? 
4  O2A ? I  NAD . ? A NAD 1307 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2008 ? 1_555 87.0  ? 
5  O   ? EA HOH . ? A HOH 1569 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2008 ? 1_555 90.0  ? 
6  O   ? EA HOH . ? A HOH 1587 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2008 ? 1_555 173.4 ? 
7  O2A ? I  NAD . ? A NAD 1307 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2233 ? 1_555 97.9  ? 
8  O   ? EA HOH . ? A HOH 1569 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2233 ? 1_555 174.1 ? 
9  O   ? EA HOH . ? A HOH 1587 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2233 ? 1_555 79.2  ? 
10 O   ? EA HOH . ? A HOH 2008 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2233 ? 1_555 94.5  ? 
11 O2A ? I  NAD . ? A NAD 1307 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2278 ? 1_555 171.3 ? 
12 O   ? EA HOH . ? A HOH 1569 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2278 ? 1_555 85.3  ? 
13 O   ? EA HOH . ? A HOH 1587 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2278 ? 1_555 88.4  ? 
14 O   ? EA HOH . ? A HOH 2008 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2278 ? 1_555 93.6  ? 
15 O   ? EA HOH . ? A HOH 2233 ? 1_555 MG ? O  MG . ? A MG 1313 ? 1_555 O ? EA HOH . ? A HOH 2278 ? 1_555 90.6  ? 
16 O2A ? AA NAD . ? B NAD 1312 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 1548 ? 1_555 94.6  ? 
17 O2A ? AA NAD . ? B NAD 1312 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 1884 ? 1_555 96.6  ? 
18 O   ? FA HOH . ? B HOH 1548 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 1884 ? 1_555 114.1 ? 
19 O2A ? AA NAD . ? B NAD 1312 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2134 ? 1_555 82.7  ? 
20 O   ? FA HOH . ? B HOH 1548 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2134 ? 1_555 87.7  ? 
21 O   ? FA HOH . ? B HOH 1884 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2134 ? 1_555 158.2 ? 
22 O2A ? AA NAD . ? B NAD 1312 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2157 ? 1_555 88.6  ? 
23 O   ? FA HOH . ? B HOH 1548 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2157 ? 1_555 161.3 ? 
24 O   ? FA HOH . ? B HOH 1884 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2157 ? 1_555 83.8  ? 
25 O   ? FA HOH . ? B HOH 2134 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2157 ? 1_555 74.4  ? 
26 O2A ? AA NAD . ? B NAD 1312 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2343 ? 1_555 164.5 ? 
27 O   ? FA HOH . ? B HOH 1548 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2343 ? 1_555 93.1  ? 
28 O   ? FA HOH . ? B HOH 1884 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2343 ? 1_555 92.5  ? 
29 O   ? FA HOH . ? B HOH 2134 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2343 ? 1_555 84.2  ? 
30 O   ? FA HOH . ? B HOH 2157 ? 1_555 MG ? CA MG . ? B MG 1314 ? 1_555 O ? FA HOH . ? B HOH 2343 ? 1_555 79.9  ? 
# 
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 -3.22 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 0.46  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -2.56 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 4.07  
# 
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  GLY A 304  ? ILE A 307  ? GLY A 302  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  ? THR A 608  ? ASP A 597  THR A 606  
AA2 3  THR A 591  ? ASN A 596  ? THR A 589  ASN A 594  
AA3 1  GLN A 581  ? LEU A 582  ? GLN A 579  LEU A 580  
AA3 2  GLY A 585  ? PRO A 586  ? GLY A 583  PRO A 584  
AA4 1  LEU A 758  ? LEU A 760  ? LEU A 756  LEU A 758  
AA4 2  VAL A 729  ? LYS A 732  ? VAL A 727  LYS A 730  
AA4 3  ILE A 702  ? ILE A 705  ? ILE A 700  ILE A 703  
AA4 4  GLY A 779  ? THR A 783  ? GLY A 777  THR A 781  
AA4 5  LEU A 809  ? GLU A 812  ? LEU A 807  GLU A 810  
AA5 1  VAL A 911  ? GLN A 913  ? VAL A 909  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  GLY A 1165 ? GLU A 1169 ? GLY A 1163 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  LEU B 305  ? ILE B 307  ? LEU B 303  ILE B 305  
AA7 4  MET B 337  ? GLN B 342  ? MET B 335  GLN B 340  
AA7 5  ILE B 366  ? VAL B 371  ? ILE B 364  VAL B 369  
AA7 6  VAL B 418  ? ALA B 423  ? VAL B 416  ALA B 421  
AA7 7  GLU B 447  ? LEU B 451  ? GLU B 445  LEU B 449  
AA7 8  CYS B 472  ? PRO B 477  ? CYS B 470  PRO B 475  
AA7 9  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? GLU B 609  ? ASP B 597  GLU B 607  
AA8 3  GLU B 590  ? ASN B 596  ? GLU B 588  ASN B 594  
AA9 1  GLN B 581  ? LEU B 582  ? GLN B 579  LEU B 580  
AA9 2  GLY B 585  ? PRO B 586  ? GLY B 583  PRO B 584  
AB1 1  LEU B 758  ? LEU B 760  ? LEU B 756  LEU B 758  
AB1 2  VAL B 729  ? LYS B 732  ? VAL B 727  LYS B 730  
AB1 3  ILE B 702  ? ILE B 705  ? ILE B 700  ILE B 703  
AB1 4  GLY B 779  ? THR B 783  ? GLY B 777  THR B 781  
AB1 5  LEU B 809  ? GLU B 812  ? LEU B 807  GLU B 810  
AB2 1  VAL B 911  ? GLN B 913  ? VAL B 909  GLN B 911  
AB2 2  THR B 929  ? GLU B 932  ? THR B 927  GLU B 930  
AB2 3  VAL B 947  ? TYR B 953  ? VAL B 945  TYR B 951  
AB2 4  LEU B 849  ? GLN B 855  ? LEU B 847  GLN B 853  
AB2 5  ASN B 817  ? VAL B 821  ? ASN B 815  VAL B 819  
AB2 6  THR B 973  ? HIS B 977  ? THR B 971  HIS B 975  
AB2 7  ASN B 995  ? ILE B 998  ? ASN B 993  ILE B 996  
AB2 8  VAL B 1213 ? ASN B 1221 ? VAL B 1211 ASN B 1219 
AB2 9  GLU B 1092 ? ALA B 1100 ? GLU B 1090 ALA B 1098 
AB2 10 ASP B 1083 ? 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 MET A 337  ? N MET A 335  O MET A 367  ? O MET A 365  
AA1 5 6  N LEU A 370  ? N LEU A 368  O GLN A 421  ? O GLN A 419  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O GLY A 605  ? O GLY A 603  N VAL A 594  ? N VAL A 592  
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 1152 ? O SER A 1150 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O 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                   9E0B 
_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 B GLN 793  ? ? O B HOH 1401 ? ? 2.02 
2  1 OE1 A GLN 793  ? ? O A HOH 1401 ? ? 2.08 
3  1 O   B HOH 2121 ? ? O B HOH 2278 ? ? 2.10 
4  1 OD1 A ASP 375  ? B O A HOH 1402 ? ? 2.10 
5  1 OE1 B GLU 539  ? ? O B HOH 1402 ? ? 2.12 
6  1 O   B HOH 2218 ? ? O B HOH 2221 ? ? 2.13 
7  1 OD1 A ASP 796  ? ? O A HOH 1403 ? ? 2.14 
8  1 O   A LEU 1183 ? ? O A HOH 1404 ? ? 2.14 
9  1 OD1 A ASP 239  ? ? O A HOH 1405 ? ? 2.15 
10 1 ND2 A ASN 298  ? ? O A HOH 1406 ? ? 2.15 
11 1 OH  A TYR 995  ? ? O A HOH 1407 ? ? 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   ? ? -155.57 58.57   
2  1 LYS A 124  ? ? -125.98 -51.05  
3  1 GLU A 225  ? ? -172.63 143.70  
4  1 GLU A 308  ? ? -119.70 -134.89 
5  1 MET A 452  ? ? -147.00 -48.42  
6  1 LYS A 465  ? ? -117.76 -123.74 
7  1 ASP A 597  ? ? -171.67 98.90   
8  1 HIS A 694  ? ? -100.70 79.14   
9  1 PHE A 708  ? ? -119.18 74.51   
10 1 THR A 811  ? ? -124.83 -157.24 
11 1 GLN A 842  ? ? -93.54  52.25   
12 1 GLN A 938  ? ? -97.83  -81.84  
13 1 LEU A 970  ? ? -98.20  -88.43  
14 1 ALA A 1003 ? ? -140.49 39.92   
15 1 GLN A 1008 ? ? -119.99 77.00   
16 1 ALA B 22   ? ? -156.85 60.54   
17 1 ASN B 129  ? ? -66.17  66.04   
18 1 HIS B 133  ? ? -166.40 -21.89  
19 1 LEU B 223  ? ? 80.92   -1.35   
20 1 GLU B 308  ? ? -118.41 -136.01 
21 1 MET B 452  ? ? -136.22 -44.09  
22 1 VAL B 460  ? ? -124.22 -51.55  
23 1 LYS B 465  ? ? -119.51 -122.94 
24 1 TYR B 485  ? ? -161.85 27.75   
25 1 ASP B 597  ? ? -167.22 98.14   
26 1 THR B 689  ? ? -131.20 -43.25  
27 1 HIS B 694  ? ? -102.80 76.11   
28 1 PHE B 708  ? ? -119.00 74.68   
29 1 THR B 811  ? ? -125.08 -155.86 
30 1 GLN B 842  ? ? -93.10  54.20   
31 1 LEU B 970  ? ? -98.87  -88.23  
32 1 VAL B 1007 ? ? -121.42 -50.73  
33 1 GLN B 1008 ? ? -115.65 77.39   
34 1 ASP B 1154 ? ? -157.37 89.46   
# 
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 -25.5275 66.1849 92.7881 0.1525 ? 0.0185 ? 0.0131  ? 0.1295 ? 0.0043  ? 0.1301 ? 0.6284 ? 0.0057 ? 
0.1898 ? 0.0982 ? -0.0023 ? 0.1296 ? -0.0335 ? -0.1050 ? 0.0157  ? 0.0259 ? 0.0298 ? 0.0151  ? -0.0146 ? -0.0274 ? 0.0033  ? 
2 'X-RAY DIFFRACTION' ? refined 5.8577   31.5787 91.2015 0.1253 ? 0.0039 ? -0.0030 ? 0.1329 ? -0.0171 ? 0.1301 ? 0.1870 ? 0.0036 ? 
0.0522 ? 0.2042 ? -0.0704 ? 0.3614 ? 0.0113  ? -0.0278 ? -0.0034 ? 0.0396 ? 0.0028 ? -0.0056 ? 0.0212  ? -0.0733 ? -0.0178 ? 
# 
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 2466 ? 5.81 . 
2 1 O ? A HOH 2467 ? 5.82 . 
3 1 O ? B HOH 2514 ? 6.29 . 
# 
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 LEU 134 ? A LEU 136 
19 1 Y 1 A GLY 135 ? A GLY 137 
20 1 Y 1 A GLY 136 ? A GLY 138 
21 1 Y 1 A GLU 492 ? A GLU 494 
22 1 Y 1 A ASN 493 ? A ASN 495 
23 1 Y 1 B SER -1  ? B SER 1   
24 1 Y 1 B MET 0   ? B MET 2   
25 1 Y 1 B MET 1   ? B MET 3   
26 1 Y 1 B SER 2   ? B SER 4   
27 1 Y 1 B PRO 3   ? B PRO 5   
28 1 Y 1 B ASN 4   ? B ASN 6   
29 1 Y 1 B PRO 5   ? B PRO 7   
30 1 Y 1 B LEU 6   ? B LEU 8   
31 1 Y 1 B GLN 7   ? B GLN 9   
32 1 Y 1 B LYS 8   ? B LYS 10  
33 1 Y 1 B PRO 9   ? B PRO 11  
34 1 Y 1 B ALA 10  ? B ALA 12  
35 1 Y 1 B ILE 11  ? B ILE 13  
36 1 Y 1 B ASP 12  ? B ASP 14  
37 1 Y 1 B ALA 13  ? B ALA 15  
38 1 Y 1 B HIS 79  ? B HIS 81  
39 1 Y 1 B SER 80  ? B SER 82  
40 1 Y 1 B GLY 81  ? B GLY 83  
41 1 Y 1 B SER 82  ? B SER 84  
42 1 Y 1 B GLY 135 ? B GLY 137 
43 1 Y 1 B GLY 136 ? B GLY 138 
44 1 Y 1 B SER 137 ? B SER 139 
45 1 Y 1 B GLU 492 ? B GLU 494 
46 1 Y 1 B ASN 493 ? B ASN 495 
47 1 Y 1 B GLY 494 ? B GLY 496 
# 
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 
1PE   OH2    O  N N 1   
1PE   C12    C  N N 2   
1PE   C22    C  N N 3   
1PE   OH3    O  N N 4   
1PE   C13    C  N N 5   
1PE   C23    C  N N 6   
1PE   OH4    O  N N 7   
1PE   C14    C  N N 8   
1PE   C24    C  N N 9   
1PE   OH5    O  N N 10  
1PE   C15    C  N N 11  
1PE   C25    C  N N 12  
1PE   OH6    O  N N 13  
1PE   C16    C  N N 14  
1PE   C26    C  N N 15  
1PE   OH7    O  N N 16  
1PE   HO2    H  N N 17  
1PE   H121   H  N N 18  
1PE   H122   H  N N 19  
1PE   H221   H  N N 20  
1PE   H222   H  N N 21  
1PE   H131   H  N N 22  
1PE   H132   H  N N 23  
1PE   H231   H  N N 24  
1PE   H232   H  N N 25  
1PE   H141   H  N N 26  
1PE   H142   H  N N 27  
1PE   H241   H  N N 28  
1PE   H242   H  N N 29  
1PE   H151   H  N N 30  
1PE   H152   H  N N 31  
1PE   H251   H  N N 32  
1PE   H252   H  N N 33  
1PE   H161   H  N N 34  
1PE   H162   H  N N 35  
1PE   H261   H  N N 36  
1PE   H262   H  N N 37  
1PE   HO7    H  N N 38  
A1AQC C4     C  Y N 39  
A1AQC C5     C  N N 40  
A1AQC C6     C  N N 41  
A1AQC C7     C  Y N 42  
A1AQC C8     C  Y N 43  
A1AQC C      C  N N 44  
A1AQC O      O  N N 45  
A1AQC C1     C  Y N 46  
A1AQC C2     C  Y N 47  
A1AQC C3     C  Y N 48  
A1AQC O1     O  N N 49  
A1AQC H6     H  N N 50  
A1AQC H5     H  N N 51  
A1AQC H8     H  N N 52  
A1AQC H7     H  N N 53  
A1AQC H9     H  N N 54  
A1AQC H2     H  N N 55  
A1AQC H1     H  N N 56  
A1AQC H      H  N N 57  
A1AQC H3     H  N N 58  
A1AQC H4     H  N N 59  
ALA   N      N  N N 60  
ALA   CA     C  N S 61  
ALA   C      C  N N 62  
ALA   O      O  N N 63  
ALA   CB     C  N N 64  
ALA   OXT    O  N N 65  
ALA   H      H  N N 66  
ALA   H2     H  N N 67  
ALA   HA     H  N N 68  
ALA   HB1    H  N N 69  
ALA   HB2    H  N N 70  
ALA   HB3    H  N N 71  
ALA   HXT    H  N N 72  
ARG   N      N  N N 73  
ARG   CA     C  N S 74  
ARG   C      C  N N 75  
ARG   O      O  N N 76  
ARG   CB     C  N N 77  
ARG   CG     C  N N 78  
ARG   CD     C  N N 79  
ARG   NE     N  N N 80  
ARG   CZ     C  N N 81  
ARG   NH1    N  N N 82  
ARG   NH2    N  N N 83  
ARG   OXT    O  N N 84  
ARG   H      H  N N 85  
ARG   H2     H  N N 86  
ARG   HA     H  N N 87  
ARG   HB2    H  N N 88  
ARG   HB3    H  N N 89  
ARG   HG2    H  N N 90  
ARG   HG3    H  N N 91  
ARG   HD2    H  N N 92  
ARG   HD3    H  N N 93  
ARG   HE     H  N N 94  
ARG   HH11   H  N N 95  
ARG   HH12   H  N N 96  
ARG   HH21   H  N N 97  
ARG   HH22   H  N N 98  
ARG   HXT    H  N N 99  
ASN   N      N  N N 100 
ASN   CA     C  N S 101 
ASN   C      C  N N 102 
ASN   O      O  N N 103 
ASN   CB     C  N N 104 
ASN   CG     C  N N 105 
ASN   OD1    O  N N 106 
ASN   ND2    N  N N 107 
ASN   OXT    O  N N 108 
ASN   H      H  N N 109 
ASN   H2     H  N N 110 
ASN   HA     H  N N 111 
ASN   HB2    H  N N 112 
ASN   HB3    H  N N 113 
ASN   HD21   H  N N 114 
ASN   HD22   H  N N 115 
ASN   HXT    H  N N 116 
ASP   N      N  N N 117 
ASP   CA     C  N S 118 
ASP   C      C  N N 119 
ASP   O      O  N N 120 
ASP   CB     C  N N 121 
ASP   CG     C  N N 122 
ASP   OD1    O  N N 123 
ASP   OD2    O  N N 124 
ASP   OXT    O  N N 125 
ASP   H      H  N N 126 
ASP   H2     H  N N 127 
ASP   HA     H  N N 128 
ASP   HB2    H  N N 129 
ASP   HB3    H  N N 130 
ASP   HD2    H  N N 131 
ASP   HXT    H  N N 132 
CYS   N      N  N N 133 
CYS   CA     C  N R 134 
CYS   C      C  N N 135 
CYS   O      O  N N 136 
CYS   CB     C  N N 137 
CYS   SG     S  N N 138 
CYS   OXT    O  N N 139 
CYS   H      H  N N 140 
CYS   H2     H  N N 141 
CYS   HA     H  N N 142 
CYS   HB2    H  N N 143 
CYS   HB3    H  N N 144 
CYS   HG     H  N N 145 
CYS   HXT    H  N N 146 
FAD   PA     P  N R 147 
FAD   O1A    O  N N 148 
FAD   O2A    O  N N 149 
FAD   O5B    O  N N 150 
FAD   C5B    C  N N 151 
FAD   C4B    C  N R 152 
FAD   O4B    O  N N 153 
FAD   C3B    C  N S 154 
FAD   O3B    O  N N 155 
FAD   C2B    C  N R 156 
FAD   O2B    O  N N 157 
FAD   C1B    C  N R 158 
FAD   N9A    N  Y N 159 
FAD   C8A    C  Y N 160 
FAD   N7A    N  Y N 161 
FAD   C5A    C  Y N 162 
FAD   C6A    C  Y N 163 
FAD   N6A    N  N N 164 
FAD   N1A    N  Y N 165 
FAD   C2A    C  Y N 166 
FAD   N3A    N  Y N 167 
FAD   C4A    C  Y N 168 
FAD   N1     N  N N 169 
FAD   C2     C  N N 170 
FAD   O2     O  N N 171 
FAD   N3     N  N N 172 
FAD   C4     C  N N 173 
FAD   O4     O  N N 174 
FAD   C4X    C  N N 175 
FAD   N5     N  N N 176 
FAD   C5X    C  Y N 177 
FAD   C6     C  Y N 178 
FAD   C7     C  Y N 179 
FAD   C7M    C  N N 180 
FAD   C8     C  Y N 181 
FAD   C8M    C  N N 182 
FAD   C9     C  Y N 183 
FAD   C9A    C  Y N 184 
FAD   N10    N  N N 185 
FAD   C10    C  N N 186 
FAD   "C1'"  C  N N 187 
FAD   "C2'"  C  N S 188 
FAD   "O2'"  O  N N 189 
FAD   "C3'"  C  N S 190 
FAD   "O3'"  O  N N 191 
FAD   "C4'"  C  N R 192 
FAD   "O4'"  O  N N 193 
FAD   "C5'"  C  N N 194 
FAD   "O5'"  O  N N 195 
FAD   P      P  N R 196 
FAD   O1P    O  N N 197 
FAD   O2P    O  N N 198 
FAD   O3P    O  N N 199 
FAD   HOA2   H  N N 200 
FAD   H51A   H  N N 201 
FAD   H52A   H  N N 202 
FAD   H4B    H  N N 203 
FAD   H3B    H  N N 204 
FAD   HO3A   H  N N 205 
FAD   H2B    H  N N 206 
FAD   HO2A   H  N N 207 
FAD   H1B    H  N N 208 
FAD   H8A    H  N N 209 
FAD   H61A   H  N N 210 
FAD   H62A   H  N N 211 
FAD   H2A    H  N N 212 
FAD   HN3    H  N N 213 
FAD   H6     H  N N 214 
FAD   HM71   H  N N 215 
FAD   HM72   H  N N 216 
FAD   HM73   H  N N 217 
FAD   HM81   H  N N 218 
FAD   HM82   H  N N 219 
FAD   HM83   H  N N 220 
FAD   H9     H  N N 221 
FAD   "H1'1" H  N N 222 
FAD   "H1'2" H  N N 223 
FAD   "H2'"  H  N N 224 
FAD   "HO2'" H  N N 225 
FAD   "H3'"  H  N N 226 
FAD   "HO3'" H  N N 227 
FAD   "H4'"  H  N N 228 
FAD   "HO4'" H  N N 229 
FAD   "H5'1" H  N N 230 
FAD   "H5'2" H  N N 231 
FAD   HOP2   H  N N 232 
FMT   C      C  N N 233 
FMT   O1     O  N N 234 
FMT   O2     O  N N 235 
FMT   H      H  N N 236 
FMT   HO2    H  N N 237 
GLN   N      N  N N 238 
GLN   CA     C  N S 239 
GLN   C      C  N N 240 
GLN   O      O  N N 241 
GLN   CB     C  N N 242 
GLN   CG     C  N N 243 
GLN   CD     C  N N 244 
GLN   OE1    O  N N 245 
GLN   NE2    N  N N 246 
GLN   OXT    O  N N 247 
GLN   H      H  N N 248 
GLN   H2     H  N N 249 
GLN   HA     H  N N 250 
GLN   HB2    H  N N 251 
GLN   HB3    H  N N 252 
GLN   HG2    H  N N 253 
GLN   HG3    H  N N 254 
GLN   HE21   H  N N 255 
GLN   HE22   H  N N 256 
GLN   HXT    H  N N 257 
GLU   N      N  N N 258 
GLU   CA     C  N S 259 
GLU   C      C  N N 260 
GLU   O      O  N N 261 
GLU   CB     C  N N 262 
GLU   CG     C  N N 263 
GLU   CD     C  N N 264 
GLU   OE1    O  N N 265 
GLU   OE2    O  N N 266 
GLU   OXT    O  N N 267 
GLU   H      H  N N 268 
GLU   H2     H  N N 269 
GLU   HA     H  N N 270 
GLU   HB2    H  N N 271 
GLU   HB3    H  N N 272 
GLU   HG2    H  N N 273 
GLU   HG3    H  N N 274 
GLU   HE2    H  N N 275 
GLU   HXT    H  N N 276 
GLY   N      N  N N 277 
GLY   CA     C  N N 278 
GLY   C      C  N N 279 
GLY   O      O  N N 280 
GLY   OXT    O  N N 281 
GLY   H      H  N N 282 
GLY   H2     H  N N 283 
GLY   HA2    H  N N 284 
GLY   HA3    H  N N 285 
GLY   HXT    H  N N 286 
HIS   N      N  N N 287 
HIS   CA     C  N S 288 
HIS   C      C  N N 289 
HIS   O      O  N N 290 
HIS   CB     C  N N 291 
HIS   CG     C  Y N 292 
HIS   ND1    N  Y N 293 
HIS   CD2    C  Y N 294 
HIS   CE1    C  Y N 295 
HIS   NE2    N  Y N 296 
HIS   OXT    O  N N 297 
HIS   H      H  N N 298 
HIS   H2     H  N N 299 
HIS   HA     H  N N 300 
HIS   HB2    H  N N 301 
HIS   HB3    H  N N 302 
HIS   HD1    H  N N 303 
HIS   HD2    H  N N 304 
HIS   HE1    H  N N 305 
HIS   HE2    H  N N 306 
HIS   HXT    H  N N 307 
HOH   O      O  N N 308 
HOH   H1     H  N N 309 
HOH   H2     H  N N 310 
ILE   N      N  N N 311 
ILE   CA     C  N S 312 
ILE   C      C  N N 313 
ILE   O      O  N N 314 
ILE   CB     C  N S 315 
ILE   CG1    C  N N 316 
ILE   CG2    C  N N 317 
ILE   CD1    C  N N 318 
ILE   OXT    O  N N 319 
ILE   H      H  N N 320 
ILE   H2     H  N N 321 
ILE   HA     H  N N 322 
ILE   HB     H  N N 323 
ILE   HG12   H  N N 324 
ILE   HG13   H  N N 325 
ILE   HG21   H  N N 326 
ILE   HG22   H  N N 327 
ILE   HG23   H  N N 328 
ILE   HD11   H  N N 329 
ILE   HD12   H  N N 330 
ILE   HD13   H  N N 331 
ILE   HXT    H  N N 332 
LEU   N      N  N N 333 
LEU   CA     C  N S 334 
LEU   C      C  N N 335 
LEU   O      O  N N 336 
LEU   CB     C  N N 337 
LEU   CG     C  N N 338 
LEU   CD1    C  N N 339 
LEU   CD2    C  N N 340 
LEU   OXT    O  N N 341 
LEU   H      H  N N 342 
LEU   H2     H  N N 343 
LEU   HA     H  N N 344 
LEU   HB2    H  N N 345 
LEU   HB3    H  N N 346 
LEU   HG     H  N N 347 
LEU   HD11   H  N N 348 
LEU   HD12   H  N N 349 
LEU   HD13   H  N N 350 
LEU   HD21   H  N N 351 
LEU   HD22   H  N N 352 
LEU   HD23   H  N N 353 
LEU   HXT    H  N N 354 
LYS   N      N  N N 355 
LYS   CA     C  N S 356 
LYS   C      C  N N 357 
LYS   O      O  N N 358 
LYS   CB     C  N N 359 
LYS   CG     C  N N 360 
LYS   CD     C  N N 361 
LYS   CE     C  N N 362 
LYS   NZ     N  N N 363 
LYS   OXT    O  N N 364 
LYS   H      H  N N 365 
LYS   H2     H  N N 366 
LYS   HA     H  N N 367 
LYS   HB2    H  N N 368 
LYS   HB3    H  N N 369 
LYS   HG2    H  N N 370 
LYS   HG3    H  N N 371 
LYS   HD2    H  N N 372 
LYS   HD3    H  N N 373 
LYS   HE2    H  N N 374 
LYS   HE3    H  N N 375 
LYS   HZ1    H  N N 376 
LYS   HZ2    H  N N 377 
LYS   HZ3    H  N N 378 
LYS   HXT    H  N N 379 
MET   N      N  N N 380 
MET   CA     C  N S 381 
MET   C      C  N N 382 
MET   O      O  N N 383 
MET   CB     C  N N 384 
MET   CG     C  N N 385 
MET   SD     S  N N 386 
MET   CE     C  N N 387 
MET   OXT    O  N N 388 
MET   H      H  N N 389 
MET   H2     H  N N 390 
MET   HA     H  N N 391 
MET   HB2    H  N N 392 
MET   HB3    H  N N 393 
MET   HG2    H  N N 394 
MET   HG3    H  N N 395 
MET   HE1    H  N N 396 
MET   HE2    H  N N 397 
MET   HE3    H  N N 398 
MET   HXT    H  N N 399 
MG    MG     MG N N 400 
NAD   PA     P  N S 401 
NAD   O1A    O  N N 402 
NAD   O2A    O  N N 403 
NAD   O5B    O  N N 404 
NAD   C5B    C  N N 405 
NAD   C4B    C  N R 406 
NAD   O4B    O  N N 407 
NAD   C3B    C  N S 408 
NAD   O3B    O  N N 409 
NAD   C2B    C  N R 410 
NAD   O2B    O  N N 411 
NAD   C1B    C  N R 412 
NAD   N9A    N  Y N 413 
NAD   C8A    C  Y N 414 
NAD   N7A    N  Y N 415 
NAD   C5A    C  Y N 416 
NAD   C6A    C  Y N 417 
NAD   N6A    N  N N 418 
NAD   N1A    N  Y N 419 
NAD   C2A    C  Y N 420 
NAD   N3A    N  Y N 421 
NAD   C4A    C  Y N 422 
NAD   O3     O  N N 423 
NAD   PN     P  N N 424 
NAD   O1N    O  N N 425 
NAD   O2N    O  N N 426 
NAD   O5D    O  N N 427 
NAD   C5D    C  N N 428 
NAD   C4D    C  N R 429 
NAD   O4D    O  N N 430 
NAD   C3D    C  N S 431 
NAD   O3D    O  N N 432 
NAD   C2D    C  N R 433 
NAD   O2D    O  N N 434 
NAD   C1D    C  N R 435 
NAD   N1N    N  Y N 436 
NAD   C2N    C  Y N 437 
NAD   C3N    C  Y N 438 
NAD   C7N    C  N N 439 
NAD   O7N    O  N N 440 
NAD   N7N    N  N N 441 
NAD   C4N    C  Y N 442 
NAD   C5N    C  Y N 443 
NAD   C6N    C  Y N 444 
NAD   HOA2   H  N N 445 
NAD   H51A   H  N N 446 
NAD   H52A   H  N N 447 
NAD   H4B    H  N N 448 
NAD   H3B    H  N N 449 
NAD   HO3A   H  N N 450 
NAD   H2B    H  N N 451 
NAD   HO2A   H  N N 452 
NAD   H1B    H  N N 453 
NAD   H8A    H  N N 454 
NAD   H61A   H  N N 455 
NAD   H62A   H  N N 456 
NAD   H2A    H  N N 457 
NAD   H51N   H  N N 458 
NAD   H52N   H  N N 459 
NAD   H4D    H  N N 460 
NAD   H3D    H  N N 461 
NAD   HO3N   H  N N 462 
NAD   H2D    H  N N 463 
NAD   HO2N   H  N N 464 
NAD   H1D    H  N N 465 
NAD   H2N    H  N N 466 
NAD   H71N   H  N N 467 
NAD   H72N   H  N N 468 
NAD   H4N    H  N N 469 
NAD   H5N    H  N N 470 
NAD   H6N    H  N N 471 
PEG   C1     C  N N 472 
PEG   O1     O  N N 473 
PEG   C2     C  N N 474 
PEG   O2     O  N N 475 
PEG   C3     C  N N 476 
PEG   C4     C  N N 477 
PEG   O4     O  N N 478 
PEG   H11    H  N N 479 
PEG   H12    H  N N 480 
PEG   HO1    H  N N 481 
PEG   H21    H  N N 482 
PEG   H22    H  N N 483 
PEG   H31    H  N N 484 
PEG   H32    H  N N 485 
PEG   H41    H  N N 486 
PEG   H42    H  N N 487 
PEG   HO4    H  N N 488 
PGE   C1     C  N N 489 
PGE   O1     O  N N 490 
PGE   C2     C  N N 491 
PGE   O2     O  N N 492 
PGE   C3     C  N N 493 
PGE   C4     C  N N 494 
PGE   O4     O  N N 495 
PGE   C6     C  N N 496 
PGE   C5     C  N N 497 
PGE   O3     O  N N 498 
PGE   H1     H  N N 499 
PGE   H12    H  N N 500 
PGE   HO1    H  N N 501 
PGE   H2     H  N N 502 
PGE   H22    H  N N 503 
PGE   H3     H  N N 504 
PGE   H32    H  N N 505 
PGE   H4     H  N N 506 
PGE   H42    H  N N 507 
PGE   HO4    H  N N 508 
PGE   H6     H  N N 509 
PGE   H62    H  N N 510 
PGE   H5     H  N N 511 
PGE   H52    H  N N 512 
PHE   N      N  N N 513 
PHE   CA     C  N S 514 
PHE   C      C  N N 515 
PHE   O      O  N N 516 
PHE   CB     C  N N 517 
PHE   CG     C  Y N 518 
PHE   CD1    C  Y N 519 
PHE   CD2    C  Y N 520 
PHE   CE1    C  Y N 521 
PHE   CE2    C  Y N 522 
PHE   CZ     C  Y N 523 
PHE   OXT    O  N N 524 
PHE   H      H  N N 525 
PHE   H2     H  N N 526 
PHE   HA     H  N N 527 
PHE   HB2    H  N N 528 
PHE   HB3    H  N N 529 
PHE   HD1    H  N N 530 
PHE   HD2    H  N N 531 
PHE   HE1    H  N N 532 
PHE   HE2    H  N N 533 
PHE   HZ     H  N N 534 
PHE   HXT    H  N N 535 
PRO   N      N  N N 536 
PRO   CA     C  N S 537 
PRO   C      C  N N 538 
PRO   O      O  N N 539 
PRO   CB     C  N N 540 
PRO   CG     C  N N 541 
PRO   CD     C  N N 542 
PRO   OXT    O  N N 543 
PRO   H      H  N N 544 
PRO   HA     H  N N 545 
PRO   HB2    H  N N 546 
PRO   HB3    H  N N 547 
PRO   HG2    H  N N 548 
PRO   HG3    H  N N 549 
PRO   HD2    H  N N 550 
PRO   HD3    H  N N 551 
PRO   HXT    H  N N 552 
SER   N      N  N N 553 
SER   CA     C  N S 554 
SER   C      C  N N 555 
SER   O      O  N N 556 
SER   CB     C  N N 557 
SER   OG     O  N N 558 
SER   OXT    O  N N 559 
SER   H      H  N N 560 
SER   H2     H  N N 561 
SER   HA     H  N N 562 
SER   HB2    H  N N 563 
SER   HB3    H  N N 564 
SER   HG     H  N N 565 
SER   HXT    H  N N 566 
SO4   S      S  N N 567 
SO4   O1     O  N N 568 
SO4   O2     O  N N 569 
SO4   O3     O  N N 570 
SO4   O4     O  N N 571 
THR   N      N  N N 572 
THR   CA     C  N S 573 
THR   C      C  N N 574 
THR   O      O  N N 575 
THR   CB     C  N R 576 
THR   OG1    O  N N 577 
THR   CG2    C  N N 578 
THR   OXT    O  N N 579 
THR   H      H  N N 580 
THR   H2     H  N N 581 
THR   HA     H  N N 582 
THR   HB     H  N N 583 
THR   HG1    H  N N 584 
THR   HG21   H  N N 585 
THR   HG22   H  N N 586 
THR   HG23   H  N N 587 
THR   HXT    H  N N 588 
TRP   N      N  N N 589 
TRP   CA     C  N S 590 
TRP   C      C  N N 591 
TRP   O      O  N N 592 
TRP   CB     C  N N 593 
TRP   CG     C  Y N 594 
TRP   CD1    C  Y N 595 
TRP   CD2    C  Y N 596 
TRP   NE1    N  Y N 597 
TRP   CE2    C  Y N 598 
TRP   CE3    C  Y N 599 
TRP   CZ2    C  Y N 600 
TRP   CZ3    C  Y N 601 
TRP   CH2    C  Y N 602 
TRP   OXT    O  N N 603 
TRP   H      H  N N 604 
TRP   H2     H  N N 605 
TRP   HA     H  N N 606 
TRP   HB2    H  N N 607 
TRP   HB3    H  N N 608 
TRP   HD1    H  N N 609 
TRP   HE1    H  N N 610 
TRP   HE3    H  N N 611 
TRP   HZ2    H  N N 612 
TRP   HZ3    H  N N 613 
TRP   HH2    H  N N 614 
TRP   HXT    H  N N 615 
TYR   N      N  N N 616 
TYR   CA     C  N S 617 
TYR   C      C  N N 618 
TYR   O      O  N N 619 
TYR   CB     C  N N 620 
TYR   CG     C  Y N 621 
TYR   CD1    C  Y N 622 
TYR   CD2    C  Y N 623 
TYR   CE1    C  Y N 624 
TYR   CE2    C  Y N 625 
TYR   CZ     C  Y N 626 
TYR   OH     O  N N 627 
TYR   OXT    O  N N 628 
TYR   H      H  N N 629 
TYR   H2     H  N N 630 
TYR   HA     H  N N 631 
TYR   HB2    H  N N 632 
TYR   HB3    H  N N 633 
TYR   HD1    H  N N 634 
TYR   HD2    H  N N 635 
TYR   HE1    H  N N 636 
TYR   HE2    H  N N 637 
TYR   HH     H  N N 638 
TYR   HXT    H  N N 639 
VAL   N      N  N N 640 
VAL   CA     C  N S 641 
VAL   C      C  N N 642 
VAL   O      O  N N 643 
VAL   CB     C  N N 644 
VAL   CG1    C  N N 645 
VAL   CG2    C  N N 646 
VAL   OXT    O  N N 647 
VAL   H      H  N N 648 
VAL   H2     H  N N 649 
VAL   HA     H  N N 650 
VAL   HB     H  N N 651 
VAL   HG11   H  N N 652 
VAL   HG12   H  N N 653 
VAL   HG13   H  N N 654 
VAL   HG21   H  N N 655 
VAL   HG22   H  N N 656 
VAL   HG23   H  N N 657 
VAL   HXT    H  N N 658 
# 
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 
1PE   OH2   C12    sing N N 1   
1PE   OH2   HO2    sing N N 2   
1PE   C12   C22    sing N N 3   
1PE   C12   H121   sing N N 4   
1PE   C12   H122   sing N N 5   
1PE   C22   OH3    sing N N 6   
1PE   C22   H221   sing N N 7   
1PE   C22   H222   sing N N 8   
1PE   OH3   C23    sing N N 9   
1PE   C13   C23    sing N N 10  
1PE   C13   OH4    sing N N 11  
1PE   C13   H131   sing N N 12  
1PE   C13   H132   sing N N 13  
1PE   C23   H231   sing N N 14  
1PE   C23   H232   sing N N 15  
1PE   OH4   C24    sing N N 16  
1PE   C14   C24    sing N N 17  
1PE   C14   OH5    sing N N 18  
1PE   C14   H141   sing N N 19  
1PE   C14   H142   sing N N 20  
1PE   C24   H241   sing N N 21  
1PE   C24   H242   sing N N 22  
1PE   OH5   C25    sing N N 23  
1PE   C15   C25    sing N N 24  
1PE   C15   OH6    sing N N 25  
1PE   C15   H151   sing N N 26  
1PE   C15   H152   sing N N 27  
1PE   C25   H251   sing N N 28  
1PE   C25   H252   sing N N 29  
1PE   OH6   C26    sing N N 30  
1PE   C16   C26    sing N N 31  
1PE   C16   OH7    sing N N 32  
1PE   C16   H161   sing N N 33  
1PE   C16   H162   sing N N 34  
1PE   C26   H261   sing N N 35  
1PE   C26   H262   sing N N 36  
1PE   OH7   HO7    sing N N 37  
A1AQC C     O      sing N N 38  
A1AQC C1    C      sing N N 39  
A1AQC C1    C2     doub Y N 40  
A1AQC C2    C3     sing Y N 41  
A1AQC C3    C4     doub Y N 42  
A1AQC C4    O1     sing N N 43  
A1AQC O1    C5     sing N N 44  
A1AQC C5    C6     sing N N 45  
A1AQC C6    C7     sing N N 46  
A1AQC C4    C7     sing Y N 47  
A1AQC C7    C8     doub Y N 48  
A1AQC C8    C1     sing Y N 49  
A1AQC C5    H6     sing N N 50  
A1AQC C5    H5     sing N N 51  
A1AQC C6    H8     sing N N 52  
A1AQC C6    H7     sing N N 53  
A1AQC C8    H9     sing N N 54  
A1AQC C     H2     sing N N 55  
A1AQC C     H1     sing N N 56  
A1AQC O     H      sing N N 57  
A1AQC C2    H3     sing N N 58  
A1AQC C3    H4     sing N N 59  
ALA   N     CA     sing N N 60  
ALA   N     H      sing N N 61  
ALA   N     H2     sing N N 62  
ALA   CA    C      sing N N 63  
ALA   CA    CB     sing N N 64  
ALA   CA    HA     sing N N 65  
ALA   C     O      doub N N 66  
ALA   C     OXT    sing N N 67  
ALA   CB    HB1    sing N N 68  
ALA   CB    HB2    sing N N 69  
ALA   CB    HB3    sing N N 70  
ALA   OXT   HXT    sing N N 71  
ARG   N     CA     sing N N 72  
ARG   N     H      sing N N 73  
ARG   N     H2     sing N N 74  
ARG   CA    C      sing N N 75  
ARG   CA    CB     sing N N 76  
ARG   CA    HA     sing N N 77  
ARG   C     O      doub N N 78  
ARG   C     OXT    sing N N 79  
ARG   CB    CG     sing N N 80  
ARG   CB    HB2    sing N N 81  
ARG   CB    HB3    sing N N 82  
ARG   CG    CD     sing N N 83  
ARG   CG    HG2    sing N N 84  
ARG   CG    HG3    sing N N 85  
ARG   CD    NE     sing N N 86  
ARG   CD    HD2    sing N N 87  
ARG   CD    HD3    sing N N 88  
ARG   NE    CZ     sing N N 89  
ARG   NE    HE     sing N N 90  
ARG   CZ    NH1    sing N N 91  
ARG   CZ    NH2    doub N N 92  
ARG   NH1   HH11   sing N N 93  
ARG   NH1   HH12   sing N N 94  
ARG   NH2   HH21   sing N N 95  
ARG   NH2   HH22   sing N N 96  
ARG   OXT   HXT    sing N N 97  
ASN   N     CA     sing N N 98  
ASN   N     H      sing N N 99  
ASN   N     H2     sing N N 100 
ASN   CA    C      sing N N 101 
ASN   CA    CB     sing N N 102 
ASN   CA    HA     sing N N 103 
ASN   C     O      doub N N 104 
ASN   C     OXT    sing N N 105 
ASN   CB    CG     sing N N 106 
ASN   CB    HB2    sing N N 107 
ASN   CB    HB3    sing N N 108 
ASN   CG    OD1    doub N N 109 
ASN   CG    ND2    sing N N 110 
ASN   ND2   HD21   sing N N 111 
ASN   ND2   HD22   sing N N 112 
ASN   OXT   HXT    sing N N 113 
ASP   N     CA     sing N N 114 
ASP   N     H      sing N N 115 
ASP   N     H2     sing N N 116 
ASP   CA    C      sing N N 117 
ASP   CA    CB     sing N N 118 
ASP   CA    HA     sing N N 119 
ASP   C     O      doub N N 120 
ASP   C     OXT    sing N N 121 
ASP   CB    CG     sing N N 122 
ASP   CB    HB2    sing N N 123 
ASP   CB    HB3    sing N N 124 
ASP   CG    OD1    doub N N 125 
ASP   CG    OD2    sing N N 126 
ASP   OD2   HD2    sing N N 127 
ASP   OXT   HXT    sing N N 128 
CYS   N     CA     sing N N 129 
CYS   N     H      sing N N 130 
CYS   N     H2     sing N N 131 
CYS   CA    C      sing N N 132 
CYS   CA    CB     sing N N 133 
CYS   CA    HA     sing N N 134 
CYS   C     O      doub N N 135 
CYS   C     OXT    sing N N 136 
CYS   CB    SG     sing N N 137 
CYS   CB    HB2    sing N N 138 
CYS   CB    HB3    sing N N 139 
CYS   SG    HG     sing N N 140 
CYS   OXT   HXT    sing N N 141 
FAD   PA    O1A    doub N N 142 
FAD   PA    O2A    sing N N 143 
FAD   PA    O5B    sing N N 144 
FAD   PA    O3P    sing N N 145 
FAD   O2A   HOA2   sing N N 146 
FAD   O5B   C5B    sing N N 147 
FAD   C5B   C4B    sing N N 148 
FAD   C5B   H51A   sing N N 149 
FAD   C5B   H52A   sing N N 150 
FAD   C4B   O4B    sing N N 151 
FAD   C4B   C3B    sing N N 152 
FAD   C4B   H4B    sing N N 153 
FAD   O4B   C1B    sing N N 154 
FAD   C3B   O3B    sing N N 155 
FAD   C3B   C2B    sing N N 156 
FAD   C3B   H3B    sing N N 157 
FAD   O3B   HO3A   sing N N 158 
FAD   C2B   O2B    sing N N 159 
FAD   C2B   C1B    sing N N 160 
FAD   C2B   H2B    sing N N 161 
FAD   O2B   HO2A   sing N N 162 
FAD   C1B   N9A    sing N N 163 
FAD   C1B   H1B    sing N N 164 
FAD   N9A   C8A    sing Y N 165 
FAD   N9A   C4A    sing Y N 166 
FAD   C8A   N7A    doub Y N 167 
FAD   C8A   H8A    sing N N 168 
FAD   N7A   C5A    sing Y N 169 
FAD   C5A   C6A    sing Y N 170 
FAD   C5A   C4A    doub Y N 171 
FAD   C6A   N6A    sing N N 172 
FAD   C6A   N1A    doub Y N 173 
FAD   N6A   H61A   sing N N 174 
FAD   N6A   H62A   sing N N 175 
FAD   N1A   C2A    sing Y N 176 
FAD   C2A   N3A    doub Y N 177 
FAD   C2A   H2A    sing N N 178 
FAD   N3A   C4A    sing Y N 179 
FAD   N1    C2     sing N N 180 
FAD   N1    C10    doub N N 181 
FAD   C2    O2     doub N N 182 
FAD   C2    N3     sing N N 183 
FAD   N3    C4     sing N N 184 
FAD   N3    HN3    sing N N 185 
FAD   C4    O4     doub N N 186 
FAD   C4    C4X    sing N N 187 
FAD   C4X   N5     doub N N 188 
FAD   C4X   C10    sing N N 189 
FAD   N5    C5X    sing N N 190 
FAD   C5X   C6     doub Y N 191 
FAD   C5X   C9A    sing Y N 192 
FAD   C6    C7     sing Y N 193 
FAD   C6    H6     sing N N 194 
FAD   C7    C7M    sing N N 195 
FAD   C7    C8     doub Y N 196 
FAD   C7M   HM71   sing N N 197 
FAD   C7M   HM72   sing N N 198 
FAD   C7M   HM73   sing N N 199 
FAD   C8    C8M    sing N N 200 
FAD   C8    C9     sing Y N 201 
FAD   C8M   HM81   sing N N 202 
FAD   C8M   HM82   sing N N 203 
FAD   C8M   HM83   sing N N 204 
FAD   C9    C9A    doub Y N 205 
FAD   C9    H9     sing N N 206 
FAD   C9A   N10    sing N N 207 
FAD   N10   C10    sing N N 208 
FAD   N10   "C1'"  sing N N 209 
FAD   "C1'" "C2'"  sing N N 210 
FAD   "C1'" "H1'1" sing N N 211 
FAD   "C1'" "H1'2" sing N N 212 
FAD   "C2'" "O2'"  sing N N 213 
FAD   "C2'" "C3'"  sing N N 214 
FAD   "C2'" "H2'"  sing N N 215 
FAD   "O2'" "HO2'" sing N N 216 
FAD   "C3'" "O3'"  sing N N 217 
FAD   "C3'" "C4'"  sing N N 218 
FAD   "C3'" "H3'"  sing N N 219 
FAD   "O3'" "HO3'" sing N N 220 
FAD   "C4'" "O4'"  sing N N 221 
FAD   "C4'" "C5'"  sing N N 222 
FAD   "C4'" "H4'"  sing N N 223 
FAD   "O4'" "HO4'" sing N N 224 
FAD   "C5'" "O5'"  sing N N 225 
FAD   "C5'" "H5'1" sing N N 226 
FAD   "C5'" "H5'2" sing N N 227 
FAD   "O5'" P      sing N N 228 
FAD   P     O1P    doub N N 229 
FAD   P     O2P    sing N N 230 
FAD   P     O3P    sing N N 231 
FAD   O2P   HOP2   sing N N 232 
FMT   C     O1     doub N N 233 
FMT   C     O2     sing N N 234 
FMT   C     H      sing N N 235 
FMT   O2    HO2    sing N N 236 
GLN   N     CA     sing N N 237 
GLN   N     H      sing N N 238 
GLN   N     H2     sing N N 239 
GLN   CA    C      sing N N 240 
GLN   CA    CB     sing N N 241 
GLN   CA    HA     sing N N 242 
GLN   C     O      doub N N 243 
GLN   C     OXT    sing N N 244 
GLN   CB    CG     sing N N 245 
GLN   CB    HB2    sing N N 246 
GLN   CB    HB3    sing N N 247 
GLN   CG    CD     sing N N 248 
GLN   CG    HG2    sing N N 249 
GLN   CG    HG3    sing N N 250 
GLN   CD    OE1    doub N N 251 
GLN   CD    NE2    sing N N 252 
GLN   NE2   HE21   sing N N 253 
GLN   NE2   HE22   sing N N 254 
GLN   OXT   HXT    sing N N 255 
GLU   N     CA     sing N N 256 
GLU   N     H      sing N N 257 
GLU   N     H2     sing N N 258 
GLU   CA    C      sing N N 259 
GLU   CA    CB     sing N N 260 
GLU   CA    HA     sing N N 261 
GLU   C     O      doub N N 262 
GLU   C     OXT    sing N N 263 
GLU   CB    CG     sing N N 264 
GLU   CB    HB2    sing N N 265 
GLU   CB    HB3    sing N N 266 
GLU   CG    CD     sing N N 267 
GLU   CG    HG2    sing N N 268 
GLU   CG    HG3    sing N N 269 
GLU   CD    OE1    doub N N 270 
GLU   CD    OE2    sing N N 271 
GLU   OE2   HE2    sing N N 272 
GLU   OXT   HXT    sing N N 273 
GLY   N     CA     sing N N 274 
GLY   N     H      sing N N 275 
GLY   N     H2     sing N N 276 
GLY   CA    C      sing N N 277 
GLY   CA    HA2    sing N N 278 
GLY   CA    HA3    sing N N 279 
GLY   C     O      doub N N 280 
GLY   C     OXT    sing N N 281 
GLY   OXT   HXT    sing N N 282 
HIS   N     CA     sing N N 283 
HIS   N     H      sing N N 284 
HIS   N     H2     sing N N 285 
HIS   CA    C      sing N N 286 
HIS   CA    CB     sing N N 287 
HIS   CA    HA     sing N N 288 
HIS   C     O      doub N N 289 
HIS   C     OXT    sing N N 290 
HIS   CB    CG     sing N N 291 
HIS   CB    HB2    sing N N 292 
HIS   CB    HB3    sing N N 293 
HIS   CG    ND1    sing Y N 294 
HIS   CG    CD2    doub Y N 295 
HIS   ND1   CE1    doub Y N 296 
HIS   ND1   HD1    sing N N 297 
HIS   CD2   NE2    sing Y N 298 
HIS   CD2   HD2    sing N N 299 
HIS   CE1   NE2    sing Y N 300 
HIS   CE1   HE1    sing N N 301 
HIS   NE2   HE2    sing N N 302 
HIS   OXT   HXT    sing N N 303 
HOH   O     H1     sing N N 304 
HOH   O     H2     sing N N 305 
ILE   N     CA     sing N N 306 
ILE   N     H      sing N N 307 
ILE   N     H2     sing N N 308 
ILE   CA    C      sing N N 309 
ILE   CA    CB     sing N N 310 
ILE   CA    HA     sing N N 311 
ILE   C     O      doub N N 312 
ILE   C     OXT    sing N N 313 
ILE   CB    CG1    sing N N 314 
ILE   CB    CG2    sing N N 315 
ILE   CB    HB     sing N N 316 
ILE   CG1   CD1    sing N N 317 
ILE   CG1   HG12   sing N N 318 
ILE   CG1   HG13   sing N N 319 
ILE   CG2   HG21   sing N N 320 
ILE   CG2   HG22   sing N N 321 
ILE   CG2   HG23   sing N N 322 
ILE   CD1   HD11   sing N N 323 
ILE   CD1   HD12   sing N N 324 
ILE   CD1   HD13   sing N N 325 
ILE   OXT   HXT    sing N N 326 
LEU   N     CA     sing N N 327 
LEU   N     H      sing N N 328 
LEU   N     H2     sing N N 329 
LEU   CA    C      sing N N 330 
LEU   CA    CB     sing N N 331 
LEU   CA    HA     sing N N 332 
LEU   C     O      doub N N 333 
LEU   C     OXT    sing N N 334 
LEU   CB    CG     sing N N 335 
LEU   CB    HB2    sing N N 336 
LEU   CB    HB3    sing N N 337 
LEU   CG    CD1    sing N N 338 
LEU   CG    CD2    sing N N 339 
LEU   CG    HG     sing N N 340 
LEU   CD1   HD11   sing N N 341 
LEU   CD1   HD12   sing N N 342 
LEU   CD1   HD13   sing N N 343 
LEU   CD2   HD21   sing N N 344 
LEU   CD2   HD22   sing N N 345 
LEU   CD2   HD23   sing N N 346 
LEU   OXT   HXT    sing N N 347 
LYS   N     CA     sing N N 348 
LYS   N     H      sing N N 349 
LYS   N     H2     sing N N 350 
LYS   CA    C      sing N N 351 
LYS   CA    CB     sing N N 352 
LYS   CA    HA     sing N N 353 
LYS   C     O      doub N N 354 
LYS   C     OXT    sing N N 355 
LYS   CB    CG     sing N N 356 
LYS   CB    HB2    sing N N 357 
LYS   CB    HB3    sing N N 358 
LYS   CG    CD     sing N N 359 
LYS   CG    HG2    sing N N 360 
LYS   CG    HG3    sing N N 361 
LYS   CD    CE     sing N N 362 
LYS   CD    HD2    sing N N 363 
LYS   CD    HD3    sing N N 364 
LYS   CE    NZ     sing N N 365 
LYS   CE    HE2    sing N N 366 
LYS   CE    HE3    sing N N 367 
LYS   NZ    HZ1    sing N N 368 
LYS   NZ    HZ2    sing N N 369 
LYS   NZ    HZ3    sing N N 370 
LYS   OXT   HXT    sing N N 371 
MET   N     CA     sing N N 372 
MET   N     H      sing N N 373 
MET   N     H2     sing N N 374 
MET   CA    C      sing N N 375 
MET   CA    CB     sing N N 376 
MET   CA    HA     sing N N 377 
MET   C     O      doub N N 378 
MET   C     OXT    sing N N 379 
MET   CB    CG     sing N N 380 
MET   CB    HB2    sing N N 381 
MET   CB    HB3    sing N N 382 
MET   CG    SD     sing N N 383 
MET   CG    HG2    sing N N 384 
MET   CG    HG3    sing N N 385 
MET   SD    CE     sing N N 386 
MET   CE    HE1    sing N N 387 
MET   CE    HE2    sing N N 388 
MET   CE    HE3    sing N N 389 
MET   OXT   HXT    sing N N 390 
NAD   PA    O1A    doub N N 391 
NAD   PA    O2A    sing N N 392 
NAD   PA    O5B    sing N N 393 
NAD   PA    O3     sing N N 394 
NAD   O2A   HOA2   sing N N 395 
NAD   O5B   C5B    sing N N 396 
NAD   C5B   C4B    sing N N 397 
NAD   C5B   H51A   sing N N 398 
NAD   C5B   H52A   sing N N 399 
NAD   C4B   O4B    sing N N 400 
NAD   C4B   C3B    sing N N 401 
NAD   C4B   H4B    sing N N 402 
NAD   O4B   C1B    sing N N 403 
NAD   C3B   O3B    sing N N 404 
NAD   C3B   C2B    sing N N 405 
NAD   C3B   H3B    sing N N 406 
NAD   O3B   HO3A   sing N N 407 
NAD   C2B   O2B    sing N N 408 
NAD   C2B   C1B    sing N N 409 
NAD   C2B   H2B    sing N N 410 
NAD   O2B   HO2A   sing N N 411 
NAD   C1B   N9A    sing N N 412 
NAD   C1B   H1B    sing N N 413 
NAD   N9A   C8A    sing Y N 414 
NAD   N9A   C4A    sing Y N 415 
NAD   C8A   N7A    doub Y N 416 
NAD   C8A   H8A    sing N N 417 
NAD   N7A   C5A    sing Y N 418 
NAD   C5A   C6A    sing Y N 419 
NAD   C5A   C4A    doub Y N 420 
NAD   C6A   N6A    sing N N 421 
NAD   C6A   N1A    doub Y N 422 
NAD   N6A   H61A   sing N N 423 
NAD   N6A   H62A   sing N N 424 
NAD   N1A   C2A    sing Y N 425 
NAD   C2A   N3A    doub Y N 426 
NAD   C2A   H2A    sing N N 427 
NAD   N3A   C4A    sing Y N 428 
NAD   O3    PN     sing N N 429 
NAD   PN    O1N    doub N N 430 
NAD   PN    O2N    sing N N 431 
NAD   PN    O5D    sing N N 432 
NAD   O5D   C5D    sing N N 433 
NAD   C5D   C4D    sing N N 434 
NAD   C5D   H51N   sing N N 435 
NAD   C5D   H52N   sing N N 436 
NAD   C4D   O4D    sing N N 437 
NAD   C4D   C3D    sing N N 438 
NAD   C4D   H4D    sing N N 439 
NAD   O4D   C1D    sing N N 440 
NAD   C3D   O3D    sing N N 441 
NAD   C3D   C2D    sing N N 442 
NAD   C3D   H3D    sing N N 443 
NAD   O3D   HO3N   sing N N 444 
NAD   C2D   O2D    sing N N 445 
NAD   C2D   C1D    sing N N 446 
NAD   C2D   H2D    sing N N 447 
NAD   O2D   HO2N   sing N N 448 
NAD   C1D   N1N    sing N N 449 
NAD   C1D   H1D    sing N N 450 
NAD   N1N   C2N    sing Y N 451 
NAD   N1N   C6N    doub Y N 452 
NAD   C2N   C3N    doub Y N 453 
NAD   C2N   H2N    sing N N 454 
NAD   C3N   C7N    sing N N 455 
NAD   C3N   C4N    sing Y N 456 
NAD   C7N   O7N    doub N N 457 
NAD   C7N   N7N    sing N N 458 
NAD   N7N   H71N   sing N N 459 
NAD   N7N   H72N   sing N N 460 
NAD   C4N   C5N    doub Y N 461 
NAD   C4N   H4N    sing N N 462 
NAD   C5N   C6N    sing Y N 463 
NAD   C5N   H5N    sing N N 464 
NAD   C6N   H6N    sing N N 465 
PEG   C1    O1     sing N N 466 
PEG   C1    C2     sing N N 467 
PEG   C1    H11    sing N N 468 
PEG   C1    H12    sing N N 469 
PEG   O1    HO1    sing N N 470 
PEG   C2    O2     sing N N 471 
PEG   C2    H21    sing N N 472 
PEG   C2    H22    sing N N 473 
PEG   O2    C3     sing N N 474 
PEG   C3    C4     sing N N 475 
PEG   C3    H31    sing N N 476 
PEG   C3    H32    sing N N 477 
PEG   C4    O4     sing N N 478 
PEG   C4    H41    sing N N 479 
PEG   C4    H42    sing N N 480 
PEG   O4    HO4    sing N N 481 
PGE   C1    O1     sing N N 482 
PGE   C1    C2     sing N N 483 
PGE   C1    H1     sing N N 484 
PGE   C1    H12    sing N N 485 
PGE   O1    HO1    sing N N 486 
PGE   C2    O2     sing N N 487 
PGE   C2    H2     sing N N 488 
PGE   C2    H22    sing N N 489 
PGE   O2    C3     sing N N 490 
PGE   C3    C4     sing N N 491 
PGE   C3    H3     sing N N 492 
PGE   C3    H32    sing N N 493 
PGE   C4    O3     sing N N 494 
PGE   C4    H4     sing N N 495 
PGE   C4    H42    sing N N 496 
PGE   O4    C6     sing N N 497 
PGE   O4    HO4    sing N N 498 
PGE   C6    C5     sing N N 499 
PGE   C6    H6     sing N N 500 
PGE   C6    H62    sing N N 501 
PGE   C5    O3     sing N N 502 
PGE   C5    H5     sing N N 503 
PGE   C5    H52    sing N N 504 
PHE   N     CA     sing N N 505 
PHE   N     H      sing N N 506 
PHE   N     H2     sing N N 507 
PHE   CA    C      sing N N 508 
PHE   CA    CB     sing N N 509 
PHE   CA    HA     sing N N 510 
PHE   C     O      doub N N 511 
PHE   C     OXT    sing N N 512 
PHE   CB    CG     sing N N 513 
PHE   CB    HB2    sing N N 514 
PHE   CB    HB3    sing N N 515 
PHE   CG    CD1    doub Y N 516 
PHE   CG    CD2    sing Y N 517 
PHE   CD1   CE1    sing Y N 518 
PHE   CD1   HD1    sing N N 519 
PHE   CD2   CE2    doub Y N 520 
PHE   CD2   HD2    sing N N 521 
PHE   CE1   CZ     doub Y N 522 
PHE   CE1   HE1    sing N N 523 
PHE   CE2   CZ     sing Y N 524 
PHE   CE2   HE2    sing N N 525 
PHE   CZ    HZ     sing N N 526 
PHE   OXT   HXT    sing N N 527 
PRO   N     CA     sing N N 528 
PRO   N     CD     sing N N 529 
PRO   N     H      sing N N 530 
PRO   CA    C      sing N N 531 
PRO   CA    CB     sing N N 532 
PRO   CA    HA     sing N N 533 
PRO   C     O      doub N N 534 
PRO   C     OXT    sing N N 535 
PRO   CB    CG     sing N N 536 
PRO   CB    HB2    sing N N 537 
PRO   CB    HB3    sing N N 538 
PRO   CG    CD     sing N N 539 
PRO   CG    HG2    sing N N 540 
PRO   CG    HG3    sing N N 541 
PRO   CD    HD2    sing N N 542 
PRO   CD    HD3    sing N N 543 
PRO   OXT   HXT    sing N N 544 
SER   N     CA     sing N N 545 
SER   N     H      sing N N 546 
SER   N     H2     sing N N 547 
SER   CA    C      sing N N 548 
SER   CA    CB     sing N N 549 
SER   CA    HA     sing N N 550 
SER   C     O      doub N N 551 
SER   C     OXT    sing N N 552 
SER   CB    OG     sing N N 553 
SER   CB    HB2    sing N N 554 
SER   CB    HB3    sing N N 555 
SER   OG    HG     sing N N 556 
SER   OXT   HXT    sing N N 557 
SO4   S     O1     doub N N 558 
SO4   S     O2     doub N N 559 
SO4   S     O3     sing N N 560 
SO4   S     O4     sing N N 561 
THR   N     CA     sing N N 562 
THR   N     H      sing N N 563 
THR   N     H2     sing N N 564 
THR   CA    C      sing N N 565 
THR   CA    CB     sing N N 566 
THR   CA    HA     sing N N 567 
THR   C     O      doub N N 568 
THR   C     OXT    sing N N 569 
THR   CB    OG1    sing N N 570 
THR   CB    CG2    sing N N 571 
THR   CB    HB     sing N N 572 
THR   OG1   HG1    sing N N 573 
THR   CG2   HG21   sing N N 574 
THR   CG2   HG22   sing N N 575 
THR   CG2   HG23   sing N N 576 
THR   OXT   HXT    sing N N 577 
TRP   N     CA     sing N N 578 
TRP   N     H      sing N N 579 
TRP   N     H2     sing N N 580 
TRP   CA    C      sing N N 581 
TRP   CA    CB     sing N N 582 
TRP   CA    HA     sing N N 583 
TRP   C     O      doub N N 584 
TRP   C     OXT    sing N N 585 
TRP   CB    CG     sing N N 586 
TRP   CB    HB2    sing N N 587 
TRP   CB    HB3    sing N N 588 
TRP   CG    CD1    doub Y N 589 
TRP   CG    CD2    sing Y N 590 
TRP   CD1   NE1    sing Y N 591 
TRP   CD1   HD1    sing N N 592 
TRP   CD2   CE2    doub Y N 593 
TRP   CD2   CE3    sing Y N 594 
TRP   NE1   CE2    sing Y N 595 
TRP   NE1   HE1    sing N N 596 
TRP   CE2   CZ2    sing Y N 597 
TRP   CE3   CZ3    doub Y N 598 
TRP   CE3   HE3    sing N N 599 
TRP   CZ2   CH2    doub Y N 600 
TRP   CZ2   HZ2    sing N N 601 
TRP   CZ3   CH2    sing Y N 602 
TRP   CZ3   HZ3    sing N N 603 
TRP   CH2   HH2    sing N N 604 
TRP   OXT   HXT    sing N N 605 
TYR   N     CA     sing N N 606 
TYR   N     H      sing N N 607 
TYR   N     H2     sing N N 608 
TYR   CA    C      sing N N 609 
TYR   CA    CB     sing N N 610 
TYR   CA    HA     sing N N 611 
TYR   C     O      doub N N 612 
TYR   C     OXT    sing N N 613 
TYR   CB    CG     sing N N 614 
TYR   CB    HB2    sing N N 615 
TYR   CB    HB3    sing N N 616 
TYR   CG    CD1    doub Y N 617 
TYR   CG    CD2    sing Y N 618 
TYR   CD1   CE1    sing Y N 619 
TYR   CD1   HD1    sing N N 620 
TYR   CD2   CE2    doub Y N 621 
TYR   CD2   HD2    sing N N 622 
TYR   CE1   CZ     doub Y N 623 
TYR   CE1   HE1    sing N N 624 
TYR   CE2   CZ     sing Y N 625 
TYR   CE2   HE2    sing N N 626 
TYR   CZ    OH     sing N N 627 
TYR   OH    HH     sing N N 628 
TYR   OXT   HXT    sing N N 629 
VAL   N     CA     sing N N 630 
VAL   N     H      sing N N 631 
VAL   N     H2     sing N N 632 
VAL   CA    C      sing N N 633 
VAL   CA    CB     sing N N 634 
VAL   CA    HA     sing N N 635 
VAL   C     O      doub N N 636 
VAL   C     OXT    sing N N 637 
VAL   CB    CG1    sing N N 638 
VAL   CB    CG2    sing N N 639 
VAL   CB    HB     sing N N 640 
VAL   CG1   HG11   sing N N 641 
VAL   CG1   HG12   sing N N 642 
VAL   CG1   HG13   sing N N 643 
VAL   CG2   HG21   sing N N 644 
VAL   CG2   HG22   sing N N 645 
VAL   CG2   HG23   sing N N 646 
VAL   OXT   HXT    sing N N 647 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1R01GM132640 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6X9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9E0B 
_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]   0.009947 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002908 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009827 
_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]   0.008268 
_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   ? -49.174 93.753  103.484 1.00 46.44 ? 14   ALA   A N     1 
ATOM   2     C  CA    . ALA   A  1  16   ? -48.092 92.797  103.717 1.00 48.30 ? 14   ALA   A CA    1 
ATOM   3     C  C     . ALA   A  1  16   ? -48.643 91.385  103.904 1.00 47.30 ? 14   ALA   A C     1 
ATOM   4     O  O     . ALA   A  1  16   ? -49.355 91.117  104.869 1.00 50.14 ? 14   ALA   A O     1 
ATOM   5     C  CB    . ALA   A  1  16   ? -47.272 93.212  104.928 1.00 51.93 ? 14   ALA   A CB    1 
ATOM   6     N  N     . PRO   A  1  17   ? -48.310 90.479  102.986 1.00 45.06 ? 15   PRO   A N     1 
ATOM   7     C  CA    . PRO   A  1  17   ? -48.887 89.130  103.047 1.00 41.68 ? 15   PRO   A CA    1 
ATOM   8     C  C     . PRO   A  1  17   ? -48.368 88.363  104.252 1.00 40.74 ? 15   PRO   A C     1 
ATOM   9     O  O     . PRO   A  1  17   ? -47.198 88.477  104.628 1.00 39.32 ? 15   PRO   A O     1 
ATOM   10    C  CB    . PRO   A  1  17   ? -48.428 88.487  101.735 1.00 42.03 ? 15   PRO   A CB    1 
ATOM   11    C  CG    . PRO   A  1  17   ? -47.183 89.226  101.380 1.00 43.68 ? 15   PRO   A CG    1 
ATOM   12    C  CD    . PRO   A  1  17   ? -47.386 90.638  101.850 1.00 43.36 ? 15   PRO   A CD    1 
ATOM   13    N  N     . ALA   A  1  18   ? -49.257 87.589  104.867 1.00 36.35 ? 16   ALA   A N     1 
ATOM   14    C  CA    . ALA   A  1  18   ? -48.880 86.841  106.056 1.00 35.40 ? 16   ALA   A CA    1 
ATOM   15    C  C     . ALA   A  1  18   ? -47.831 85.795  105.687 1.00 31.19 ? 16   ALA   A C     1 
ATOM   16    O  O     . ALA   A  1  18   ? -47.896 85.208  104.601 1.00 29.82 ? 16   ALA   A O     1 
ATOM   17    C  CB    . ALA   A  1  18   ? -50.105 86.158  106.664 1.00 36.93 ? 16   ALA   A CB    1 
ATOM   18    N  N     . PRO   A  1  19   ? -46.852 85.547  106.552 1.00 30.95 ? 17   PRO   A N     1 
ATOM   19    C  CA    . PRO   A  1  19   ? -45.798 84.580  106.220 1.00 27.98 ? 17   PRO   A CA    1 
ATOM   20    C  C     . PRO   A  1  19   ? -46.372 83.190  106.012 1.00 24.87 ? 17   PRO   A C     1 
ATOM   21    O  O     . PRO   A  1  19   ? -47.164 82.697  106.818 1.00 29.68 ? 17   PRO   A O     1 
ATOM   22    C  CB    . PRO   A  1  19   ? -44.879 84.628  107.447 1.00 30.73 ? 17   PRO   A CB    1 
ATOM   23    C  CG    . PRO   A  1  19   ? -45.127 85.960  108.043 1.00 31.62 ? 17   PRO   A CG    1 
ATOM   24    C  CD    . PRO   A  1  19   ? -46.587 86.229  107.831 1.00 30.60 ? 17   PRO   A CD    1 
ATOM   25    N  N     . PHE   A  1  20   ? -45.971 82.566  104.906 1.00 24.92 ? 18   PHE   A N     1 
ATOM   26    C  CA    . PHE   A  1  20   ? -46.321 81.199  104.538 1.00 27.03 ? 18   PHE   A CA    1 
ATOM   27    C  C     . PHE   A  1  20   ? -47.803 81.008  104.255 1.00 26.98 ? 18   PHE   A C     1 
ATOM   28    O  O     . PHE   A  1  20   ? -48.254 79.864  104.141 1.00 27.11 ? 18   PHE   A O     1 
ATOM   29    C  CB    . PHE   A  1  20   ? -45.834 80.172  105.562 1.00 24.91 ? 18   PHE   A CB    1 
ATOM   30    C  CG    . PHE   A  1  20   ? -44.368 80.262  105.855 1.00 25.04 ? 18   PHE   A CG    1 
ATOM   31    C  CD1   . PHE   A  1  20   ? -43.435 79.784  104.948 1.00 23.42 ? 18   PHE   A CD1   1 
ATOM   32    C  CD2   . PHE   A  1  20   ? -43.921 80.817  107.044 1.00 25.44 ? 18   PHE   A CD2   1 
ATOM   33    C  CE1   . PHE   A  1  20   ? -42.068 79.862  105.224 1.00 23.41 ? 18   PHE   A CE1   1 
ATOM   34    C  CE2   . PHE   A  1  20   ? -42.566 80.896  107.321 1.00 26.98 ? 18   PHE   A CE2   1 
ATOM   35    C  CZ    . PHE   A  1  20   ? -41.646 80.422  106.415 1.00 25.88 ? 18   PHE   A CZ    1 
ATOM   36    N  N     . ALA   A  1  21   ? -48.568 82.092  104.134 1.00 27.69 ? 19   ALA   A N     1 
ATOM   37    C  CA    . ALA   A  1  21   ? -49.993 81.971  103.844 1.00 29.66 ? 19   ALA   A CA    1 
ATOM   38    C  C     . ALA   A  1  21   ? -50.249 81.341  102.485 1.00 30.38 ? 19   ALA   A C     1 
ATOM   39    O  O     . ALA   A  1  21   ? -51.327 80.780  102.269 1.00 31.45 ? 19   ALA   A O     1 
ATOM   40    C  CB    . ALA   A  1  21   ? -50.667 83.342  103.925 1.00 33.11 ? 19   ALA   A CB    1 
ATOM   41    N  N     . ASP   A  1  22   ? -49.286 81.418  101.573 1.00 28.01 ? 20   ASP   A N     1 
ATOM   42    C  CA    . ASP   A  1  22   ? -49.412 80.867  100.229 1.00 31.95 ? 20   ASP   A CA    1 
ATOM   43    C  C     . ASP   A  1  22   ? -48.238 79.953  99.923  1.00 24.36 ? 20   ASP   A C     1 
ATOM   44    O  O     . ASP   A  1  22   ? -47.731 79.925  98.800  1.00 24.65 ? 20   ASP   A O     1 
ATOM   45    C  CB    . ASP   A  1  22   ? -49.497 81.979  99.186  1.00 34.77 ? 20   ASP   A CB    1 
ATOM   46    C  CG    . ASP   A  1  22   ? -50.660 82.919  99.427  1.00 43.36 ? 20   ASP   A CG    1 
ATOM   47    O  OD1   . ASP   A  1  22   ? -51.757 82.434  99.773  1.00 48.57 ? 20   ASP   A OD1   1 
ATOM   48    O  OD2   . ASP   A  1  22   ? -50.475 84.144  99.270  1.00 52.94 ? 20   ASP   A OD2   1 
ATOM   49    N  N     . PHE   A  1  23   ? -47.790 79.187  100.918 1.00 21.29 ? 21   PHE   A N     1 
ATOM   50    C  CA    . PHE   A  1  23   ? -46.517 78.486  100.785 1.00 21.12 ? 21   PHE   A CA    1 
ATOM   51    C  C     . PHE   A  1  23   ? -46.548 77.472  99.647  1.00 21.46 ? 21   PHE   A C     1 
ATOM   52    O  O     . PHE   A  1  23   ? -45.709 77.510  98.741  1.00 21.86 ? 21   PHE   A O     1 
ATOM   53    C  CB    . PHE   A  1  23   ? -46.136 77.798  102.093 1.00 21.18 ? 21   PHE   A CB    1 
ATOM   54    C  CG    . PHE   A  1  23   ? -44.920 76.943  101.957 1.00 19.22 ? 21   PHE   A CG    1 
ATOM   55    C  CD1   . PHE   A  1  23   ? -43.690 77.512  101.656 1.00 22.33 ? 21   PHE   A CD1   1 
ATOM   56    C  CD2   . PHE   A  1  23   ? -44.997 75.568  102.088 1.00 22.14 ? 21   PHE   A CD2   1 
ATOM   57    C  CE1   . PHE   A  1  23   ? -42.556 76.723  101.494 1.00 20.92 ? 21   PHE   A CE1   1 
ATOM   58    C  CE2   . PHE   A  1  23   ? -43.867 74.774  101.934 1.00 24.78 ? 21   PHE   A CE2   1 
ATOM   59    C  CZ    . PHE   A  1  23   ? -42.646 75.353  101.641 1.00 20.07 ? 21   PHE   A CZ    1 
ATOM   60    N  N     . ALA   A  1  24   ? -47.490 76.527  99.698  1.00 22.27 ? 22   ALA   A N     1 
ATOM   61    C  CA    . ALA   A  1  24   ? -47.549 75.486  98.677  1.00 22.53 ? 22   ALA   A CA    1 
ATOM   62    C  C     . ALA   A  1  24   ? -48.957 74.917  98.564  1.00 21.14 ? 22   ALA   A C     1 
ATOM   63    O  O     . ALA   A  1  24   ? -49.151 73.702  98.714  1.00 20.66 ? 22   ALA   A O     1 
ATOM   64    C  CB    . ALA   A  1  24   ? -46.566 74.361  98.996  1.00 24.15 ? 22   ALA   A CB    1 
ATOM   65    N  N     . PRO   A  1  25   ? -49.953 75.742  98.269  1.00 23.42 ? 23   PRO   A N     1 
ATOM   66    C  CA    . PRO   A  1  25   ? -51.317 75.233  98.173  1.00 24.59 ? 23   PRO   A CA    1 
ATOM   67    C  C     . PRO   A  1  25   ? -51.413 74.229  97.042  1.00 22.96 ? 23   PRO   A C     1 
ATOM   68    O  O     . PRO   A  1  25   ? -50.835 74.436  95.967  1.00 23.33 ? 23   PRO   A O     1 
ATOM   69    C  CB    . PRO   A  1  25   ? -52.139 76.495  97.864  1.00 25.27 ? 23   PRO   A CB    1 
ATOM   70    C  CG    . PRO   A  1  25   ? -51.190 77.387  97.170  1.00 26.10 ? 23   PRO   A CG    1 
ATOM   71    C  CD    . PRO   A  1  25   ? -49.865 77.153  97.849  1.00 24.06 ? 23   PRO   A CD    1 
ATOM   72    N  N     . PRO   A  1  26   ? -52.087 73.108  97.257  1.00 22.73 ? 24   PRO   A N     1 
ATOM   73    C  CA    . PRO   A  1  26   ? -52.212 72.115  96.187  1.00 24.31 ? 24   PRO   A CA    1 
ATOM   74    C  C     . PRO   A  1  26   ? -53.057 72.655  95.045  1.00 22.32 ? 24   PRO   A C     1 
ATOM   75    O  O     . PRO   A  1  26   ? -53.873 73.564  95.212  1.00 22.43 ? 24   PRO   A O     1 
ATOM   76    C  CB    . PRO   A  1  26   ? -52.910 70.939  96.875  1.00 24.21 ? 24   PRO   A CB    1 
ATOM   77    C  CG    . PRO   A  1  26   ? -53.675 71.580  98.017  1.00 27.61 ? 24   PRO   A CG    1 
ATOM   78    C  CD    . PRO   A  1  26   ? -52.818 72.726  98.477  1.00 26.07 ? 24   PRO   A CD    1 
ATOM   79    N  N     . VAL   A  1  27   ? -52.837 72.070  93.861  1.00 20.32 ? 25   VAL   A N     1 
ATOM   80    C  CA    . VAL   A  1  27   ? -53.626 72.410  92.675  1.00 22.18 ? 25   VAL   A CA    1 
ATOM   81    C  C     . VAL   A  1  27   ? -55.114 72.300  92.961  1.00 25.38 ? 25   VAL   A C     1 
ATOM   82    O  O     . VAL   A  1  27   ? -55.906 73.157  92.549  1.00 27.24 ? 25   VAL   A O     1 
ATOM   83    C  CB    . VAL   A  1  27   ? -53.217 71.515  91.488  1.00 22.15 ? 25   VAL   A CB    1 
ATOM   84    C  CG1   . VAL   A  1  27   ? -54.162 71.713  90.326  1.00 24.16 ? 25   VAL   A CG1   1 
ATOM   85    C  CG2   . VAL   A  1  27   ? -51.779 71.814  91.068  1.00 23.62 ? 25   VAL   A CG2   1 
ATOM   86    N  N     . ARG   A  1  28   ? -55.517 71.247  93.662  1.00 25.73 ? 26   ARG   A N     1 
ATOM   87    C  CA    . ARG   A  1  28   ? -56.914 71.007  93.986  1.00 26.46 ? 26   ARG   A CA    1 
ATOM   88    C  C     . ARG   A  1  28   ? -56.968 70.294  95.325  1.00 28.25 ? 26   ARG   A C     1 
ATOM   89    O  O     . ARG   A  1  28   ? -55.982 69.672  95.741  1.00 25.02 ? 26   ARG   A O     1 
ATOM   90    C  CB    . ARG   A  1  28   ? -57.569 70.124  92.916  1.00 29.03 ? 26   ARG   A CB    1 
ATOM   91    C  CG    . ARG   A  1  28   ? -57.085 68.673  92.948  1.00 28.88 ? 26   ARG   A CG    1 
ATOM   92    C  CD    . ARG   A  1  28   ? -57.600 67.860  91.763  1.00 32.61 ? 26   ARG   A CD    1 
ATOM   93    N  NE    . ARG   A  1  28   ? -56.912 68.210  90.525  1.00 34.56 ? 26   ARG   A NE    1 
ATOM   94    C  CZ    . ARG   A  1  28   ? -57.429 68.977  89.576  1.00 35.72 ? 26   ARG   A CZ    1 
ATOM   95    N  NH1   . ARG   A  1  28   ? -58.659 69.459  89.668  1.00 35.63 ? 26   ARG   A NH1   1 
ATOM   96    N  NH2   . ARG   A  1  28   ? -56.691 69.279  88.515  1.00 31.96 ? 26   ARG   A NH2   1 
ATOM   97    N  N     . PRO   A  1  29   ? -58.099 70.363  96.030  1.00 26.83 ? 27   PRO   A N     1 
ATOM   98    C  CA    . PRO   A  1  29   ? -58.226 69.571  97.257  1.00 28.40 ? 27   PRO   A CA    1 
ATOM   99    C  C     . PRO   A  1  29   ? -58.042 68.093  96.941  1.00 25.60 ? 27   PRO   A C     1 
ATOM   100   O  O     . PRO   A  1  29   ? -58.516 67.589  95.923  1.00 25.54 ? 27   PRO   A O     1 
ATOM   101   C  CB    . PRO   A  1  29   ? -59.650 69.880  97.735  1.00 29.44 ? 27   PRO   A CB    1 
ATOM   102   C  CG    . PRO   A  1  29   ? -59.976 71.206  97.119  1.00 31.53 ? 27   PRO   A CG    1 
ATOM   103   C  CD    . PRO   A  1  29   ? -59.297 71.187  95.779  1.00 30.08 ? 27   PRO   A CD    1 
ATOM   104   N  N     . GLN   A  1  30   ? -57.324 67.403  97.816  1.00 25.79 ? 28   GLN   A N     1 
ATOM   105   C  CA    . GLN   A  1  30   ? -56.942 66.024  97.549  1.00 26.12 ? 28   GLN   A CA    1 
ATOM   106   C  C     . GLN   A  1  30   ? -58.102 65.094  97.880  1.00 26.41 ? 28   GLN   A C     1 
ATOM   107   O  O     . GLN   A  1  30   ? -58.533 65.021  99.035  1.00 27.83 ? 28   GLN   A O     1 
ATOM   108   C  CB    . GLN   A  1  30   ? -55.712 65.671  98.378  1.00 24.78 ? 28   GLN   A CB    1 
ATOM   109   C  CG    . GLN   A  1  30   ? -54.526 66.584  98.099  1.00 23.79 ? 28   GLN   A CG    1 
ATOM   110   C  CD    . GLN   A  1  30   ? -54.010 66.430  96.686  1.00 25.11 ? 28   GLN   A CD    1 
ATOM   111   O  OE1   . GLN   A  1  30   ? -53.295 65.476  96.381  1.00 24.11 ? 28   GLN   A OE1   1 
ATOM   112   N  NE2   . GLN   A  1  30   ? -54.374 67.362  95.812  1.00 22.39 ? 28   GLN   A NE2   1 
ATOM   113   N  N     . SER   A  1  31   ? -58.594 64.378  96.872  1.00 25.77 ? 29   SER   A N     1 
ATOM   114   C  CA    . SER   A  1  31   ? -59.663 63.409  97.082  1.00 22.86 ? 29   SER   A CA    1 
ATOM   115   C  C     . SER   A  1  31   ? -59.144 62.223  97.894  1.00 24.24 ? 29   SER   A C     1 
ATOM   116   O  O     . SER   A  1  31   ? -57.937 62.050  98.097  1.00 23.45 ? 29   SER   A O     1 
ATOM   117   C  CB    . SER   A  1  31   ? -60.189 62.908  95.742  1.00 22.54 ? 29   SER   A CB    1 
ATOM   118   O  OG    . SER   A  1  31   ? -59.210 62.120  95.085  1.00 21.16 ? 29   SER   A OG    1 
ATOM   119   N  N     . THR   A  1  32   ? -60.082 61.395  98.365  1.00 23.63 ? 30   THR   A N     1 
ATOM   120   C  CA    . THR   A  1  32   ? -59.711 60.158  99.045  1.00 22.44 ? 30   THR   A CA    1 
ATOM   121   C  C     . THR   A  1  32   ? -58.772 59.329  98.179  1.00 22.51 ? 30   THR   A C     1 
ATOM   122   O  O     . THR   A  1  32   ? -57.765 58.799  98.662  1.00 23.48 ? 30   THR   A O     1 
ATOM   123   C  CB    . THR   A  1  32   ? -60.974 59.355  99.372  1.00 24.24 ? 30   THR   A CB    1 
ATOM   124   O  OG1   . THR   A  1  32   ? -61.826 60.134  100.218 1.00 31.35 ? 30   THR   A OG1   1 
ATOM   125   C  CG2   . THR   A  1  32   ? -60.614 58.064  100.064 1.00 28.06 ? 30   THR   A CG2   1 
ATOM   126   N  N     . LEU   A  1  33   ? -59.076 59.228  96.887  1.00 21.69 ? 31   LEU   A N     1 
ATOM   127   C  CA    . LEU   A  1  33   ? -58.240 58.437  95.996  1.00 22.78 ? 31   LEU   A CA    1 
ATOM   128   C  C     . LEU   A  1  33   ? -56.865 59.064  95.823  1.00 21.72 ? 31   LEU   A C     1 
ATOM   129   O  O     . LEU   A  1  33   ? -55.859 58.351  95.763  1.00 20.74 ? 31   LEU   A O     1 
ATOM   130   C  CB    . LEU   A  1  33   ? -58.934 58.276  94.650  1.00 23.16 ? 31   LEU   A CB    1 
ATOM   131   C  CG    . LEU   A  1  33   ? -60.060 57.250  94.685  1.00 23.91 ? 31   LEU   A CG    1 
ATOM   132   C  CD1   . LEU   A  1  33   ? -60.907 57.355  93.443  1.00 22.79 ? 31   LEU   A CD1   1 
ATOM   133   C  CD2   . LEU   A  1  33   ? -59.484 55.841  94.834  1.00 27.80 ? 31   LEU   A CD2   1 
ATOM   134   N  N     . ARG   A  1  34   ? -56.802 60.394  95.720  1.00 19.24 ? 32   ARG   A N     1 
ATOM   135   C  CA    . ARG   A  1  34   ? -55.498 61.047  95.621  1.00 18.92 ? 32   ARG   A CA    1 
ATOM   136   C  C     . ARG   A  1  34   ? -54.716 60.894  96.910  1.00 17.99 ? 32   ARG   A C     1 
ATOM   137   O  O     . ARG   A  1  34   ? -53.495 60.703  96.883  1.00 19.47 ? 32   ARG   A O     1 
ATOM   138   C  CB    . ARG   A  1  34   ? -55.667 62.525  95.287  1.00 20.24 ? 32   ARG   A CB    1 
ATOM   139   C  CG    . ARG   A  1  34   ? -56.142 62.785  93.863  1.00 22.34 ? 32   ARG   A CG    1 
ATOM   140   C  CD    . ARG   A  1  34   ? -55.025 62.542  92.842  1.00 22.01 ? 32   ARG   A CD    1 
ATOM   141   N  NE    . ARG   A  1  34   ? -53.901 63.466  92.985  1.00 21.97 ? 32   ARG   A NE    1 
ATOM   142   C  CZ    . ARG   A  1  34   ? -53.803 64.633  92.359  1.00 26.58 ? 32   ARG   A CZ    1 
ATOM   143   N  NH1   . ARG   A  1  34   ? -54.748 65.061  91.531  1.00 23.65 ? 32   ARG   A NH1   1 
ATOM   144   N  NH2   . ARG   A  1  34   ? -52.726 65.390  92.561  1.00 23.11 ? 32   ARG   A NH2   1 
ATOM   145   N  N     . ARG   A  1  35   ? -55.394 60.972  98.057  1.00 19.88 ? 33   ARG   A N     1 
ATOM   146   C  CA    . ARG   A  1  35   ? -54.675 60.826  99.313  1.00 21.57 ? 33   ARG   A CA    1 
ATOM   147   C  C     . ARG   A  1  35   ? -54.123 59.419  99.474  1.00 21.65 ? 33   ARG   A C     1 
ATOM   148   O  O     . ARG   A  1  35   ? -53.060 59.240  100.078 1.00 21.16 ? 33   ARG   A O     1 
ATOM   149   C  CB    . ARG   A  1  35   ? -55.580 61.186  100.492 1.00 24.13 ? 33   ARG   A CB    1 
ATOM   150   C  CG    . ARG   A  1  35   ? -55.877 62.662  100.558 1.00 25.71 ? 33   ARG   A CG    1 
ATOM   151   C  CD    . ARG   A  1  35   ? -56.892 62.975  101.652 1.00 31.58 ? 33   ARG   A CD    1 
ATOM   152   N  NE    . ARG   A  1  35   ? -57.225 64.392  101.626 1.00 40.82 ? 33   ARG   A NE    1 
ATOM   153   C  CZ    . ARG   A  1  35   ? -56.497 65.336  102.206 1.00 47.12 ? 33   ARG   A CZ    1 
ATOM   154   N  NH1   . ARG   A  1  35   ? -55.414 65.039  102.907 1.00 48.09 ? 33   ARG   A NH1   1 
ATOM   155   N  NH2   . ARG   A  1  35   ? -56.860 66.610  102.072 1.00 48.91 ? 33   ARG   A NH2   1 
ATOM   156   N  N     . ALA   A  1  36   ? -54.820 58.415  98.933  1.00 20.42 ? 34   ALA   A N     1 
ATOM   157   C  CA    . ALA   A  1  36   ? -54.301 57.053  99.003  1.00 22.65 ? 34   ALA   A CA    1 
ATOM   158   C  C     . ALA   A  1  36   ? -53.033 56.911  98.177  1.00 21.68 ? 34   ALA   A C     1 
ATOM   159   O  O     . ALA   A  1  36   ? -52.124 56.163  98.552  1.00 22.47 ? 34   ALA   A O     1 
ATOM   160   C  CB    . ALA   A  1  36   ? -55.364 56.047  98.554  1.00 22.16 ? 34   ALA   A CB    1 
ATOM   161   N  N     . ILE   A  1  37   ? -52.939 57.652  97.073  1.00 18.25 ? 35   ILE   A N     1 
ATOM   162   C  CA    . ILE   A  1  37   ? -51.702 57.669  96.304  1.00 17.66 ? 35   ILE   A CA    1 
ATOM   163   C  C     . ILE   A  1  37   ? -50.573 58.247  97.136  1.00 18.55 ? 35   ILE   A C     1 
ATOM   164   O  O     . ILE   A  1  37   ? -49.503 57.642  97.272  1.00 18.89 ? 35   ILE   A O     1 
ATOM   165   C  CB    . ILE   A  1  37   ? -51.903 58.461  95.004  1.00 15.96 ? 35   ILE   A CB    1 
ATOM   166   C  CG1   . ILE   A  1  37   ? -52.901 57.739  94.108  1.00 18.78 ? 35   ILE   A CG1   1 
ATOM   167   C  CG2   . ILE   A  1  37   ? -50.571 58.645  94.312  1.00 18.01 ? 35   ILE   A CG2   1 
ATOM   168   C  CD1   . ILE   A  1  37   ? -53.395 58.586  92.962  1.00 19.44 ? 35   ILE   A CD1   1 
ATOM   169   N  N     . THR   A  1  38   ? -50.789 59.433  97.701  1.00 19.39 ? 36   THR   A N     1 
ATOM   170   C  CA    . THR   A  1  38   ? -49.715 60.095  98.426  1.00 19.09 ? 36   THR   A CA    1 
ATOM   171   C  C     . THR   A  1  38   ? -49.274 59.266  99.621  1.00 20.30 ? 36   THR   A C     1 
ATOM   172   O  O     . THR   A  1  38   ? -48.081 59.213  99.940  1.00 20.30 ? 36   THR   A O     1 
ATOM   173   C  CB    . THR   A  1  38   ? -50.177 61.481  98.856  1.00 21.47 ? 36   THR   A CB    1 
ATOM   174   O  OG1   . THR   A  1  38   ? -50.662 62.191  97.710  1.00 21.20 ? 36   THR   A OG1   1 
ATOM   175   C  CG2   . THR   A  1  38   ? -49.037 62.245  99.476  1.00 22.30 ? 36   THR   A CG2   1 
ATOM   176   N  N     . ALA   A  1  39   ? -50.218 58.579  100.262 1.00 20.22 ? 37   ALA   A N     1 
ATOM   177   C  CA    . ALA   A  1  39   ? -49.894 57.770  101.431 1.00 21.55 ? 37   ALA   A CA    1 
ATOM   178   C  C     . ALA   A  1  39   ? -48.934 56.633  101.101 1.00 22.63 ? 37   ALA   A C     1 
ATOM   179   O  O     . ALA   A  1  39   ? -48.213 56.157  101.986 1.00 24.17 ? 37   ALA   A O     1 
ATOM   180   C  CB    . ALA   A  1  39   ? -51.182 57.204  102.028 1.00 21.92 ? 37   ALA   A CB    1 
ATOM   181   N  N     . ALA   A  1  40   ? -48.918 56.175  99.852  1.00 20.16 ? 38   ALA   A N     1 
ATOM   182   C  CA    . ALA   A  1  40   ? -48.101 55.039  99.459  1.00 22.01 ? 38   ALA   A CA    1 
ATOM   183   C  C     . ALA   A  1  40   ? -46.744 55.449  98.919  1.00 21.54 ? 38   ALA   A C     1 
ATOM   184   O  O     . ALA   A  1  40   ? -45.938 54.571  98.593  1.00 20.94 ? 38   ALA   A O     1 
ATOM   185   C  CB    . ALA   A  1  40   ? -48.827 54.215  98.396  1.00 20.42 ? 38   ALA   A CB    1 
ATOM   186   N  N     . TYR   A  1  41   ? -46.488 56.756  98.821  1.00 19.83 ? 39   TYR   A N     1 
ATOM   187   C  CA    . TYR   A  1  41   ? -45.315 57.279  98.118  1.00 19.29 ? 39   TYR   A CA    1 
ATOM   188   C  C     . TYR   A  1  41   ? -44.036 56.545  98.501  1.00 19.94 ? 39   TYR   A C     1 
ATOM   189   O  O     . TYR   A  1  41   ? -43.292 56.074  97.631  1.00 19.04 ? 39   TYR   A O     1 
ATOM   190   C  CB    . TYR   A  1  41   ? -45.208 58.773  98.423  1.00 19.45 ? 39   TYR   A CB    1 
ATOM   191   C  CG    . TYR   A  1  41   ? -44.454 59.641  97.435  1.00 19.54 ? 39   TYR   A CG    1 
ATOM   192   C  CD1   . TYR   A  1  41   ? -43.395 59.151  96.690  1.00 18.97 ? 39   TYR   A CD1   1 
ATOM   193   C  CD2   . TYR   A  1  41   ? -44.793 60.979  97.285  1.00 20.45 ? 39   TYR   A CD2   1 
ATOM   194   C  CE1   . TYR   A  1  41   ? -42.702 59.972  95.816  1.00 18.69 ? 39   TYR   A CE1   1 
ATOM   195   C  CE2   . TYR   A  1  41   ? -44.115 61.797  96.416  1.00 20.86 ? 39   TYR   A CE2   1 
ATOM   196   C  CZ    . TYR   A  1  41   ? -43.063 61.290  95.694  1.00 19.86 ? 39   TYR   A CZ    1 
ATOM   197   O  OH    . TYR   A  1  41   ? -42.391 62.121  94.828  1.00 19.71 ? 39   TYR   A OH    1 
ATOM   198   N  N     . ARG   A  1  42   ? -43.761 56.436  99.804  1.00 21.36 ? 40   ARG   A N     1 
ATOM   199   C  CA    . ARG   A  1  42   ? -42.539 55.794  100.282 1.00 21.86 ? 40   ARG   A CA    1 
ATOM   200   C  C     . ARG   A  1  42   ? -42.850 54.680  101.275 1.00 20.49 ? 40   ARG   A C     1 
ATOM   201   O  O     . ARG   A  1  42   ? -42.064 54.411  102.193 1.00 24.03 ? 40   ARG   A O     1 
ATOM   202   C  CB    . ARG   A  1  42   ? -41.563 56.817  100.856 1.00 25.02 ? 40   ARG   A CB    1 
ATOM   203   C  CG    . ARG   A  1  42   ? -41.096 57.783  99.784  1.00 22.51 ? 40   ARG   A CG    1 
ATOM   204   C  CD    . ARG   A  1  42   ? -40.239 58.906  100.293 1.00 25.63 ? 40   ARG   A CD    1 
ATOM   205   N  NE    . ARG   A  1  42   ? -40.249 59.963  99.289  1.00 24.27 ? 40   ARG   A NE    1 
ATOM   206   C  CZ    . ARG   A  1  42   ? -39.471 59.984  98.218  1.00 22.01 ? 40   ARG   A CZ    1 
ATOM   207   N  NH1   . ARG   A  1  42   ? -38.496 59.096  98.048  1.00 21.57 ? 40   ARG   A NH1   1 
ATOM   208   N  NH2   . ARG   A  1  42   ? -39.674 60.917  97.291  1.00 20.45 ? 40   ARG   A NH2   1 
ATOM   209   N  N     . ARG   A  1  43   ? -43.977 54.015  101.073 1.00 21.15 ? 41   ARG   A N     1 
ATOM   210   C  CA    . ARG   A  1  43   ? -44.409 52.948  101.962 1.00 22.09 ? 41   ARG   A CA    1 
ATOM   211   C  C     . ARG   A  1  43   ? -43.354 51.844  102.002 1.00 25.16 ? 41   ARG   A C     1 
ATOM   212   O  O     . ARG   A  1  43   ? -42.803 51.476  100.963 1.00 22.12 ? 41   ARG   A O     1 
ATOM   213   C  CB    . ARG   A  1  43   ? -45.721 52.380  101.425 1.00 22.36 ? 41   ARG   A CB    1 
ATOM   214   C  CG    . ARG   A  1  43   ? -46.248 51.163  102.166 1.00 24.43 ? 41   ARG   A CG    1 
ATOM   215   C  CD    . ARG   A  1  43   ? -47.680 50.904  101.767 1.00 23.94 ? 41   ARG   A CD    1 
ATOM   216   N  NE    . ARG   A  1  43   ? -48.528 52.023  102.163 1.00 24.91 ? 41   ARG   A NE    1 
ATOM   217   C  CZ    . ARG   A  1  43   ? -49.655 52.364  101.558 1.00 21.62 ? 41   ARG   A CZ    1 
ATOM   218   N  NH1   . ARG   A  1  43   ? -50.098 51.706  100.502 1.00 24.15 ? 41   ARG   A NH1   1 
ATOM   219   N  NH2   . ARG   A  1  43   ? -50.356 53.393  102.026 1.00 25.98 ? 41   ARG   A NH2   1 
ATOM   220   N  N     . PRO   A  1  44   ? -43.040 51.306  103.178 1.00 25.44 ? 42   PRO   A N     1 
ATOM   221   C  CA    . PRO   A  1  44   ? -42.047 50.231  103.252 1.00 26.11 ? 42   PRO   A CA    1 
ATOM   222   C  C     . PRO   A  1  44   ? -42.386 49.090  102.303 1.00 21.35 ? 42   PRO   A C     1 
ATOM   223   O  O     . PRO   A  1  44   ? -43.549 48.742  102.098 1.00 24.59 ? 42   PRO   A O     1 
ATOM   224   C  CB    . PRO   A  1  44   ? -42.119 49.790  104.717 1.00 27.66 ? 42   PRO   A CB    1 
ATOM   225   C  CG    . PRO   A  1  44   ? -42.546 51.028  105.445 1.00 30.19 ? 42   PRO   A CG    1 
ATOM   226   C  CD    . PRO   A  1  44   ? -43.517 51.716  104.510 1.00 27.98 ? 42   PRO   A CD    1 
ATOM   227   N  N     . GLU   A  1  45   ? -41.340 48.528  101.689 1.00 24.71 ? 43   GLU   A N     1 
ATOM   228   C  CA    . GLU   A  1  45   ? -41.538 47.500  100.675 1.00 24.48 ? 43   GLU   A CA    1 
ATOM   229   C  C     . GLU   A  1  45   ? -42.234 46.264  101.236 1.00 25.40 ? 43   GLU   A C     1 
ATOM   230   O  O     . GLU   A  1  45   ? -43.037 45.631  100.538 1.00 25.89 ? 43   GLU   A O     1 
ATOM   231   C  CB    . GLU   A  1  45   ? -40.187 47.147  100.059 1.00 27.01 ? 43   GLU   A CB    1 
ATOM   232   C  CG    . GLU   A  1  45   ? -40.192 47.160  98.555  1.00 30.35 ? 43   GLU   A CG    1 
ATOM   233   C  CD    . GLU   A  1  45   ? -38.810 47.067  97.951  1.00 25.45 ? 43   GLU   A CD    1 
ATOM   234   O  OE1   . GLU   A  1  45   ? -37.851 47.632  98.526  1.00 24.36 ? 43   GLU   A OE1   1 
ATOM   235   O  OE2   . GLU   A  1  45   ? -38.694 46.421  96.893  1.00 23.29 ? 43   GLU   A OE2   1 
ATOM   236   N  N     . THR   A  1  46   ? -41.948 45.904  102.490 1.00 26.02 ? 44   THR   A N     1 
ATOM   237   C  CA    . THR   A  1  46   ? -42.631 44.773  103.116 1.00 30.46 ? 44   THR   A CA    1 
ATOM   238   C  C     . THR   A  1  46   ? -44.129 45.007  103.273 1.00 31.55 ? 44   THR   A C     1 
ATOM   239   O  O     . THR   A  1  46   ? -44.885 44.037  103.401 1.00 33.64 ? 44   THR   A O     1 
ATOM   240   C  CB    . THR   A  1  46   ? -42.023 44.472  104.486 1.00 28.37 ? 44   THR   A CB    1 
ATOM   241   O  OG1   . THR   A  1  46   ? -42.075 45.653  105.297 1.00 29.51 ? 44   THR   A OG1   1 
ATOM   242   C  CG2   . THR   A  1  46   ? -40.572 44.020  104.346 1.00 28.71 ? 44   THR   A CG2   1 
ATOM   243   N  N     . GLU   A  1  47   ? -44.574 46.261  103.278 1.00 27.13 ? 45   GLU   A N     1 
ATOM   244   C  CA    . GLU   A  1  47   ? -46.001 46.551  103.316 1.00 26.16 ? 45   GLU   A CA    1 
ATOM   245   C  C     . GLU   A  1  47   ? -46.633 46.568  101.931 1.00 26.05 ? 45   GLU   A C     1 
ATOM   246   O  O     . GLU   A  1  47   ? -47.825 46.262  101.794 1.00 28.03 ? 45   GLU   A O     1 
ATOM   247   C  CB    . GLU   A  1  47   ? -46.244 47.896  104.007 1.00 30.34 ? 45   GLU   A CB    1 
ATOM   248   C  CG    . GLU   A  1  47   ? -45.536 48.022  105.344 1.00 39.18 ? 45   GLU   A CG    1 
ATOM   249   C  CD    . GLU   A  1  47   ? -45.997 49.223  106.143 1.00 39.66 ? 45   GLU   A CD    1 
ATOM   250   O  OE1   . GLU   A  1  47   ? -46.861 49.979  105.645 1.00 45.35 ? 45   GLU   A OE1   1 
ATOM   251   O  OE2   . GLU   A  1  47   ? -45.498 49.404  107.274 1.00 51.10 ? 45   GLU   A OE2   1 
ATOM   252   N  N     . CYS   A  1  48   ? -45.860 46.905  100.895 1.00 23.11 ? 46   CYS   A N     1 
ATOM   253   C  CA    . CYS   A  1  48   ? -46.424 46.982  99.551  1.00 22.91 ? 46   CYS   A CA    1 
ATOM   254   C  C     . CYS   A  1  48   ? -46.683 45.611  98.951  1.00 21.44 ? 46   CYS   A C     1 
ATOM   255   O  O     . CYS   A  1  48   ? -47.656 45.428  98.213  1.00 23.14 ? 46   CYS   A O     1 
ATOM   256   C  CB    . CYS   A  1  48   ? -45.470 47.732  98.625  1.00 24.58 ? 46   CYS   A CB    1 
ATOM   257   S  SG    . CYS   A  1  48   ? -45.173 49.437  99.071  1.00 25.41 ? 46   CYS   A SG    1 
ATOM   258   N  N     . LEU   A  1  49   ? -45.801 44.650  99.211  1.00 24.33 ? 47   LEU   A N     1 
ATOM   259   C  CA    . LEU   A  1  49   ? -45.808 43.412  98.433  1.00 26.98 ? 47   LEU   A CA    1 
ATOM   260   C  C     . LEU   A  1  49   ? -46.984 42.481  98.706  1.00 26.19 ? 47   LEU   A C     1 
ATOM   261   O  O     . LEU   A  1  49   ? -47.556 41.947  97.744  1.00 25.93 ? 47   LEU   A O     1 
ATOM   262   C  CB    . LEU   A  1  49   ? -44.476 42.666  98.548  1.00 27.12 ? 47   LEU   A CB    1 
ATOM   263   C  CG    . LEU   A  1  49   ? -43.516 42.946  97.391  1.00 27.11 ? 47   LEU   A CG    1 
ATOM   264   C  CD1   . LEU   A  1  49   ? -44.089 42.453  96.069  1.00 25.02 ? 47   LEU   A CD1   1 
ATOM   265   C  CD2   . LEU   A  1  49   ? -43.213 44.432  97.316  1.00 23.60 ? 47   LEU   A CD2   1 
ATOM   266   N  N     . PRO   A  1  50   ? -47.367 42.238  99.959  1.00 27.81 ? 48   PRO   A N     1 
ATOM   267   C  CA    . PRO   A  1  50   ? -48.415 41.239  100.229 1.00 28.91 ? 48   PRO   A CA    1 
ATOM   268   C  C     . PRO   A  1  50   ? -49.685 41.472  99.422  1.00 28.31 ? 48   PRO   A C     1 
ATOM   269   O  O     . PRO   A  1  50   ? -50.190 40.521  98.805  1.00 30.98 ? 48   PRO   A O     1 
ATOM   270   C  CB    . PRO   A  1  50   ? -48.650 41.365  101.744 1.00 29.81 ? 48   PRO   A CB    1 
ATOM   271   C  CG    . PRO   A  1  50   ? -47.319 41.759  102.265 1.00 29.84 ? 48   PRO   A CG    1 
ATOM   272   C  CD    . PRO   A  1  50   ? -46.717 42.678  101.207 1.00 27.65 ? 48   PRO   A CD    1 
ATOM   273   N  N     . PRO   A  1  51   ? -50.244 42.695  99.377  1.00 27.51 ? 49   PRO   A N     1 
ATOM   274   C  CA    . PRO   A  1  51   ? -51.439 42.876  98.534  1.00 30.76 ? 49   PRO   A CA    1 
ATOM   275   C  C     . PRO   A  1  51   ? -51.167 42.698  97.053  1.00 25.17 ? 49   PRO   A C     1 
ATOM   276   O  O     . PRO   A  1  51   ? -52.073 42.289  96.316  1.00 28.26 ? 49   PRO   A O     1 
ATOM   277   C  CB    . PRO   A  1  51   ? -51.926 44.295  98.873  1.00 27.83 ? 49   PRO   A CB    1 
ATOM   278   C  CG    . PRO   A  1  51   ? -50.741 44.983  99.400  1.00 28.52 ? 49   PRO   A CG    1 
ATOM   279   C  CD    . PRO   A  1  51   ? -49.931 43.933  100.118 1.00 26.93 ? 49   PRO   A CD    1 
ATOM   280   N  N     . LEU   A  1  52   ? -49.953 43.000  96.590  1.00 27.54 ? 50   LEU   A N     1 
ATOM   281   C  CA    . LEU   A  1  52   ? -49.632 42.760  95.188  1.00 25.89 ? 50   LEU   A CA    1 
ATOM   282   C  C     . LEU   A  1  52   ? -49.554 41.265  94.902  1.00 24.37 ? 50   LEU   A C     1 
ATOM   283   O  O     . LEU   A  1  52   ? -50.085 40.789  93.895  1.00 23.96 ? 50   LEU   A O     1 
ATOM   284   C  CB    . LEU   A  1  52   ? -48.321 43.460  94.829  1.00 23.66 ? 50   LEU   A CB    1 
ATOM   285   C  CG    . LEU   A  1  52   ? -48.314 44.983  94.972  1.00 26.30 ? 50   LEU   A CG    1 
ATOM   286   C  CD1   . LEU   A  1  52   ? -46.897 45.534  94.780  1.00 22.58 ? 50   LEU   A CD1   1 
ATOM   287   C  CD2   . LEU   A  1  52   ? -49.263 45.612  93.967  1.00 25.73 ? 50   LEU   A CD2   1 
ATOM   288   N  N     . VAL   A  1  53   ? -48.915 40.509  95.793  1.00 26.38 ? 51   VAL   A N     1 
ATOM   289   C  CA    . VAL   A  1  53   ? -48.889 39.055  95.658  1.00 29.34 ? 51   VAL   A CA    1 
ATOM   290   C  C     . VAL   A  1  53   ? -50.307 38.499  95.584  1.00 28.26 ? 51   VAL   A C     1 
ATOM   291   O  O     . VAL   A  1  53   ? -50.628 37.667  94.723  1.00 27.86 ? 51   VAL   A O     1 
ATOM   292   C  CB    . VAL   A  1  53   ? -48.089 38.436  96.816  1.00 25.57 ? 51   VAL   A CB    1 
ATOM   293   C  CG1   . VAL   A  1  53   ? -48.237 36.921  96.810  1.00 28.79 ? 51   VAL   A CG1   1 
ATOM   294   C  CG2   . VAL   A  1  53   ? -46.626 38.851  96.727  1.00 25.40 ? 51   VAL   A CG2   1 
ATOM   295   N  N     . GLU   A  1  54   ? -51.186 38.970  96.474  1.00 27.60 ? 52   GLU   A N     1 
ATOM   296   C  CA    . GLU   A  1  54   ? -52.566 38.497  96.463  1.00 30.96 ? 52   GLU   A CA    1 
ATOM   297   C  C     . GLU   A  1  54   ? -53.245 38.816  95.137  1.00 26.63 ? 52   GLU   A C     1 
ATOM   298   O  O     . GLU   A  1  54   ? -53.865 37.943  94.519  1.00 30.69 ? 52   GLU   A O     1 
ATOM   299   C  CB    . GLU   A  1  54   ? -53.342 39.093  97.641  1.00 33.69 ? 52   GLU   A CB    1 
ATOM   300   N  N     . ALA   A  1  55   ? -53.095 40.060  94.658  1.00 26.41 ? 53   ALA   A N     1 
ATOM   301   C  CA    . ALA   A  1  55   ? -53.784 40.479  93.442  1.00 29.48 ? 53   ALA   A CA    1 
ATOM   302   C  C     . ALA   A  1  55   ? -53.239 39.771  92.212  1.00 25.78 ? 53   ALA   A C     1 
ATOM   303   O  O     . ALA   A  1  55   ? -53.971 39.585  91.231  1.00 29.19 ? 53   ALA   A O     1 
ATOM   304   C  CB    . ALA   A  1  55   ? -53.668 41.994  93.264  1.00 27.54 ? 53   ALA   A CB    1 
ATOM   305   N  N     . ALA   A  1  56   ? -51.968 39.377  92.241  1.00 25.02 ? 54   ALA   A N     1 
ATOM   306   C  CA    . ALA   A  1  56   ? -51.318 38.763  91.094  1.00 26.35 ? 54   ALA   A CA    1 
ATOM   307   C  C     . ALA   A  1  56   ? -51.432 37.243  91.088  1.00 31.91 ? 54   ALA   A C     1 
ATOM   308   O  O     . ALA   A  1  56   ? -50.973 36.603  90.135  1.00 27.32 ? 54   ALA   A O     1 
ATOM   309   C  CB    . ALA   A  1  56   ? -49.839 39.177  91.043  1.00 24.71 ? 54   ALA   A CB    1 
ATOM   310   N  N     . THR   A  1  57   ? -52.028 36.657  92.120  1.00 29.71 ? 55   THR   A N     1 
ATOM   311   C  CA    . THR   A  1  57   ? -52.152 35.208  92.198  1.00 27.37 ? 55   THR   A CA    1 
ATOM   312   C  C     . THR   A  1  57   ? -53.094 34.702  91.115  1.00 29.18 ? 55   THR   A C     1 
ATOM   313   O  O     . THR   A  1  57   ? -54.161 35.272  90.886  1.00 30.39 ? 55   THR   A O     1 
ATOM   314   C  CB    . THR   A  1  57   ? -52.686 34.830  93.578  1.00 32.82 ? 55   THR   A CB    1 
ATOM   315   O  OG1   . THR   A  1  57   ? -51.706 35.173  94.565  1.00 32.34 ? 55   THR   A OG1   1 
ATOM   316   C  CG2   . THR   A  1  57   ? -53.006 33.333  93.662  1.00 34.55 ? 55   THR   A CG2   1 
ATOM   317   N  N     . GLN   A  1  58   ? -52.692 33.628  90.438  1.00 28.45 ? 56   GLN   A N     1 
ATOM   318   C  CA    . GLN   A  1  58   ? -53.553 32.966  89.472  1.00 28.53 ? 56   GLN   A CA    1 
ATOM   319   C  C     . GLN   A  1  58   ? -53.589 31.474  89.775  1.00 29.84 ? 56   GLN   A C     1 
ATOM   320   O  O     . GLN   A  1  58   ? -52.772 30.955  90.537  1.00 30.97 ? 56   GLN   A O     1 
ATOM   321   C  CB    . GLN   A  1  58   ? -53.095 33.210  88.029  1.00 28.12 ? 56   GLN   A CB    1 
ATOM   322   C  CG    . GLN   A  1  58   ? -53.012 34.677  87.641  1.00 27.48 ? 56   GLN   A CG    1 
ATOM   323   C  CD    . GLN   A  1  58   ? -52.882 34.855  86.149  1.00 28.08 ? 56   GLN   A CD    1 
ATOM   324   O  OE1   . GLN   A  1  58   ? -53.873 34.788  85.423  1.00 29.68 ? 56   GLN   A OE1   1 
ATOM   325   N  NE2   . GLN   A  1  58   ? -51.653 35.064  85.675  1.00 30.52 ? 56   GLN   A NE2   1 
ATOM   326   N  N     . SER   A  1  59   ? -54.544 30.787  89.155  1.00 29.21 ? 57   SER   A N     1 
ATOM   327   C  CA    . SER   A  1  59   ? -54.729 29.365  89.403  1.00 29.74 ? 57   SER   A CA    1 
ATOM   328   C  C     . SER   A  1  59   ? -53.522 28.565  88.918  1.00 35.36 ? 57   SER   A C     1 
ATOM   329   O  O     . SER   A  1  59   ? -52.746 29.003  88.062  1.00 29.81 ? 57   SER   A O     1 
ATOM   330   C  CB    . SER   A  1  59   ? -55.974 28.858  88.680  1.00 34.13 ? 57   SER   A CB    1 
ATOM   331   O  OG    . SER   A  1  59   ? -55.781 28.873  87.274  1.00 34.12 ? 57   SER   A OG    1 
ATOM   332   N  N     . LYS   A  1  60   ? -53.382 27.360  89.474  1.00 31.48 ? 58   LYS   A N     1 
ATOM   333   C  CA    . LYS   A  1  60   ? -52.308 26.471  89.046  1.00 33.70 ? 58   LYS   A CA    1 
ATOM   334   C  C     . LYS   A  1  60   ? -52.402 26.172  87.553  1.00 32.27 ? 58   LYS   A C     1 
ATOM   335   O  O     . LYS   A  1  60   ? -51.384 26.158  86.852  1.00 35.69 ? 58   LYS   A O     1 
ATOM   336   C  CB    . LYS   A  1  60   ? -52.345 25.177  89.862  1.00 34.77 ? 58   LYS   A CB    1 
ATOM   337   C  CG    . LYS   A  1  60   ? -51.218 24.205  89.548  1.00 35.78 ? 58   LYS   A CG    1 
ATOM   338   C  CD    . LYS   A  1  60   ? -49.864 24.829  89.838  1.00 42.23 ? 58   LYS   A CD    1 
ATOM   339   C  CE    . LYS   A  1  60   ? -48.767 23.779  89.994  1.00 45.20 ? 58   LYS   A CE    1 
ATOM   340   N  NZ    . LYS   A  1  60   ? -48.307 23.225  88.691  1.00 47.41 ? 58   LYS   A NZ    1 
ATOM   341   N  N     . GLU   A  1  61   ? -53.616 25.933  87.050  1.00 32.92 ? 59   GLU   A N     1 
ATOM   342   C  CA    . GLU   A  1  61   ? -53.783 25.683  85.621  1.00 33.41 ? 59   GLU   A CA    1 
ATOM   343   C  C     . GLU   A  1  61   ? -53.277 26.858  84.794  1.00 35.65 ? 59   GLU   A C     1 
ATOM   344   O  O     . GLU   A  1  61   ? -52.584 26.668  83.788  1.00 34.75 ? 59   GLU   A O     1 
ATOM   345   C  CB    . GLU   A  1  61   ? -55.250 25.403  85.305  1.00 33.96 ? 59   GLU   A CB    1 
ATOM   346   N  N     . ILE   A  1  62   ? -53.610 28.082  85.204  1.00 33.31 ? 60   ILE   A N     1 
ATOM   347   C  CA    . ILE   A  1  62   ? -53.142 29.257  84.474  1.00 30.97 ? 60   ILE   A CA    1 
ATOM   348   C  C     . ILE   A  1  62   ? -51.630 29.394  84.572  1.00 30.88 ? 60   ILE   A C     1 
ATOM   349   O  O     . ILE   A  1  62   ? -50.956 29.706  83.582  1.00 30.08 ? 60   ILE   A O     1 
ATOM   350   C  CB    . ILE   A  1  62   ? -53.863 30.520  84.967  1.00 31.07 ? 60   ILE   A CB    1 
ATOM   351   C  CG1   . ILE   A  1  62   ? -55.270 30.558  84.388  1.00 35.43 ? 60   ILE   A CG1   1 
ATOM   352   C  CG2   . ILE   A  1  62   ? -53.079 31.769  84.579  1.00 30.72 ? 60   ILE   A CG2   1 
ATOM   353   C  CD1   . ILE   A  1  62   ? -56.101 31.593  84.998  1.00 35.34 ? 60   ILE   A CD1   1 
ATOM   354   N  N     . ARG   A  1  63   ? -51.072 29.181  85.764  1.00 29.54 ? 61   ARG   A N     1 
ATOM   355   C  CA    . ARG   A  1  63   ? -49.629 29.306  85.924  1.00 32.30 ? 61   ARG   A CA    1 
ATOM   356   C  C     . ARG   A  1  63   ? -48.880 28.295  85.067  1.00 31.60 ? 61   ARG   A C     1 
ATOM   357   O  O     . ARG   A  1  63   ? -47.840 28.618  84.481  1.00 30.85 ? 61   ARG   A O     1 
ATOM   358   C  CB    . ARG   A  1  63   ? -49.252 29.207  87.399  1.00 29.17 ? 61   ARG   A CB    1 
ATOM   359   C  CG    . ARG   A  1  63   ? -49.674 30.450  88.149  1.00 37.31 ? 61   ARG   A CG    1 
ATOM   360   C  CD    . ARG   A  1  63   ? -49.230 30.446  89.585  1.00 41.26 ? 61   ARG   A CD    1 
ATOM   361   N  NE    . ARG   A  1  63   ? -49.944 29.451  90.368  1.00 42.30 ? 61   ARG   A NE    1 
ATOM   362   C  CZ    . ARG   A  1  63   ? -49.385 28.353  90.851  1.00 44.77 ? 61   ARG   A CZ    1 
ATOM   363   N  NH1   . ARG   A  1  63   ? -48.109 28.081  90.641  1.00 42.79 ? 61   ARG   A NH1   1 
ATOM   364   N  NH2   . ARG   A  1  63   ? -50.123 27.515  91.572  1.00 43.73 ? 61   ARG   A NH2   1 
ATOM   365   N  N     . ASP   A  1  64   ? -49.400 27.072  84.967  1.00 32.98 ? 62   ASP   A N     1 
ATOM   366   C  CA    . ASP   A  1  64   ? -48.780 26.090  84.086  1.00 34.87 ? 62   ASP   A CA    1 
ATOM   367   C  C     . ASP   A  1  64   ? -48.934 26.487  82.622  1.00 32.22 ? 62   ASP   A C     1 
ATOM   368   O  O     . ASP   A  1  64   ? -47.984 26.373  81.838  1.00 32.97 ? 62   ASP   A O     1 
ATOM   369   C  CB    . ASP   A  1  64   ? -49.371 24.705  84.351  1.00 34.79 ? 62   ASP   A CB    1 
ATOM   370   C  CG    . ASP   A  1  64   ? -49.009 24.169  85.733  1.00 37.56 ? 62   ASP   A CG    1 
ATOM   371   O  OD1   . ASP   A  1  64   ? -48.173 24.791  86.421  1.00 38.03 ? 62   ASP   A OD1   1 
ATOM   372   O  OD2   . ASP   A  1  64   ? -49.558 23.116  86.130  1.00 43.00 ? 62   ASP   A OD2   1 
ATOM   373   N  N     . ALA   A  1  65   ? -50.118 26.975  82.237  1.00 28.35 ? 63   ALA   A N     1 
ATOM   374   C  CA    . ALA   A  1  65   ? -50.322 27.408  80.859  1.00 28.77 ? 63   ALA   A CA    1 
ATOM   375   C  C     . ALA   A  1  65   ? -49.434 28.597  80.520  1.00 32.20 ? 63   ALA   A C     1 
ATOM   376   O  O     . ALA   A  1  65   ? -48.874 28.671  79.419  1.00 30.41 ? 63   ALA   A O     1 
ATOM   377   C  CB    . ALA   A  1  65   ? -51.795 27.748  80.622  1.00 31.25 ? 63   ALA   A CB    1 
ATOM   378   N  N     . ALA   A  1  66   ? -49.296 29.540  81.454  1.00 29.30 ? 64   ALA   A N     1 
ATOM   379   C  CA    . ALA   A  1  66   ? -48.440 30.697  81.220  1.00 31.11 ? 64   ALA   A CA    1 
ATOM   380   C  C     . ALA   A  1  66   ? -46.979 30.284  81.096  1.00 30.82 ? 64   ALA   A C     1 
ATOM   381   O  O     . ALA   A  1  66   ? -46.252 30.795  80.235  1.00 29.59 ? 64   ALA   A O     1 
ATOM   382   C  CB    . ALA   A  1  66   ? -48.607 31.704  82.355  1.00 28.01 ? 64   ALA   A CB    1 
ATOM   383   N  N     . ALA   A  1  67   ? -46.532 29.364  81.955  1.00 27.99 ? 65   ALA   A N     1 
ATOM   384   C  CA    . ALA   A  1  67   ? -45.157 28.884  81.878  1.00 30.24 ? 65   ALA   A CA    1 
ATOM   385   C  C     . ALA   A  1  67   ? -44.885 28.223  80.534  1.00 30.76 ? 65   ALA   A C     1 
ATOM   386   O  O     . ALA   A  1  67   ? -43.803 28.392  79.955  1.00 33.20 ? 65   ALA   A O     1 
ATOM   387   C  CB    . ALA   A  1  67   ? -44.882 27.902  83.019  1.00 32.29 ? 65   ALA   A CB    1 
ATOM   388   N  N     . SER   A  1  68   ? -45.857 27.470  80.022  1.00 31.78 ? 66   SER   A N     1 
ATOM   389   C  CA    . SER   A  1  68   ? -45.696 26.823  78.726  1.00 34.58 ? 66   SER   A CA    1 
ATOM   390   C  C     . SER   A  1  68   ? -45.663 27.847  77.598  1.00 35.88 ? 66   SER   A C     1 
ATOM   391   O  O     . SER   A  1  68   ? -44.844 27.737  76.678  1.00 31.68 ? 66   SER   A O     1 
ATOM   392   C  CB    . SER   A  1  68   ? -46.821 25.814  78.509  1.00 35.70 ? 66   SER   A CB    1 
ATOM   393   O  OG    . SER   A  1  68   ? -46.774 25.276  77.202  1.00 43.21 ? 66   SER   A OG    1 
ATOM   394   N  N     . THR   A  1  69   ? -46.544 28.849  77.651  1.00 31.20 ? 67   THR   A N     1 
ATOM   395   C  CA    . THR   A  1  69   ? -46.513 29.911  76.651  1.00 29.66 ? 67   THR   A CA    1 
ATOM   396   C  C     . THR   A  1  69   ? -45.194 30.670  76.698  1.00 28.30 ? 67   THR   A C     1 
ATOM   397   O  O     . THR   A  1  69   ? -44.608 30.978  75.654  1.00 27.85 ? 67   THR   A O     1 
ATOM   398   C  CB    . THR   A  1  69   ? -47.686 30.866  76.868  1.00 29.78 ? 67   THR   A CB    1 
ATOM   399   O  OG1   . THR   A  1  69   ? -48.917 30.178  76.627  1.00 31.20 ? 67   THR   A OG1   1 
ATOM   400   C  CG2   . THR   A  1  69   ? -47.593 32.059  75.924  1.00 29.69 ? 67   THR   A CG2   1 
ATOM   401   N  N     . ALA   A  1  70   ? -44.717 30.987  77.902  1.00 27.36 ? 68   ALA   A N     1 
ATOM   402   C  CA    . ALA   A  1  70   ? -43.462 31.717  78.030  1.00 29.41 ? 68   ALA   A CA    1 
ATOM   403   C  C     . ALA   A  1  70   ? -42.295 30.892  77.510  1.00 31.84 ? 68   ALA   A C     1 
ATOM   404   O  O     . ALA   A  1  70   ? -41.399 31.427  76.847  1.00 31.44 ? 68   ALA   A O     1 
ATOM   405   C  CB    . ALA   A  1  70   ? -43.235 32.140  79.481  1.00 31.48 ? 68   ALA   A CB    1 
ATOM   406   N  N     . ARG   A  1  71   ? -42.296 29.585  77.786  1.00 31.55 ? 69   ARG   A N     1 
ATOM   407   C  CA    . ARG   A  1  71   ? -41.238 28.726  77.259  1.00 32.45 ? 69   ARG   A CA    1 
ATOM   408   C  C     . ARG   A  1  71   ? -41.277 28.691  75.737  1.00 33.22 ? 69   ARG   A C     1 
ATOM   409   O  O     . ARG   A  1  71   ? -40.238 28.811  75.078  1.00 34.46 ? 69   ARG   A O     1 
ATOM   410   C  CB    . ARG   A  1  71   ? -41.368 27.315  77.832  1.00 32.78 ? 69   ARG   A CB    1 
ATOM   411   C  CG    . ARG   A  1  71   ? -40.552 26.274  77.084  1.00 34.28 ? 69   ARG   A CG    1 
ATOM   412   C  CD    . ARG   A  1  71   ? -40.529 24.932  77.814  1.00 34.37 ? 69   ARG   A CD    1 
ATOM   413   N  NE    . ARG   A  1  71   ? -39.706 24.993  79.013  1.00 38.78 ? 69   ARG   A NE    1 
ATOM   414   C  CZ    . ARG   A  1  71   ? -38.381 24.974  79.004  1.00 39.23 ? 69   ARG   A CZ    1 
ATOM   415   N  NH1   . ARG   A  1  71   ? -37.700 24.900  77.871  1.00 39.97 ? 69   ARG   A NH1   1 
ATOM   416   N  NH2   . ARG   A  1  71   ? -37.723 25.043  80.157  1.00 40.62 ? 69   ARG   A NH2   1 
ATOM   417   N  N     . LYS   A  1  72   ? -42.474 28.544  75.167  1.00 28.50 ? 70   LYS   A N     1 
ATOM   418   C  CA    . LYS   A  1  72   ? -42.636 28.558  73.717  1.00 34.41 ? 70   LYS   A CA    1 
ATOM   419   C  C     . LYS   A  1  72   ? -42.138 29.867  73.109  1.00 35.38 ? 70   LYS   A C     1 
ATOM   420   O  O     . LYS   A  1  72   ? -41.449 29.859  72.082  1.00 33.96 ? 70   LYS   A O     1 
ATOM   421   C  CB    . LYS   A  1  72   ? -44.104 28.322  73.367  1.00 31.35 ? 70   LYS   A CB    1 
ATOM   422   C  CG    . LYS   A  1  72   ? -44.418 28.344  71.885  1.00 37.64 ? 70   LYS   A CG    1 
ATOM   423   C  CD    . LYS   A  1  72   ? -45.881 28.000  71.651  1.00 38.84 ? 70   LYS   A CD    1 
ATOM   424   C  CE    . LYS   A  1  72   ? -46.170 27.695  70.189  1.00 45.93 ? 70   LYS   A CE    1 
ATOM   425   N  NZ    . LYS   A  1  72   ? -45.856 28.847  69.301  1.00 58.81 ? 70   LYS   A NZ    1 
ATOM   426   N  N     . LEU   A  1  73   ? -42.473 31.004  73.729  1.00 30.05 ? 71   LEU   A N     1 
ATOM   427   C  CA    . LEU   A  1  73   ? -42.002 32.290  73.220  1.00 28.66 ? 71   LEU   A CA    1 
ATOM   428   C  C     . LEU   A  1  73   ? -40.487 32.407  73.322  1.00 31.56 ? 71   LEU   A C     1 
ATOM   429   O  O     . LEU   A  1  73   ? -39.833 32.906  72.399  1.00 30.65 ? 71   LEU   A O     1 
ATOM   430   C  CB    . LEU   A  1  73   ? -42.650 33.434  74.001  1.00 25.84 ? 71   LEU   A CB    1 
ATOM   431   C  CG    . LEU   A  1  73   ? -44.165 33.571  73.891  1.00 29.20 ? 71   LEU   A CG    1 
ATOM   432   C  CD1   . LEU   A  1  73   ? -44.652 34.607  74.891  1.00 27.79 ? 71   LEU   A CD1   1 
ATOM   433   C  CD2   . LEU   A  1  73   ? -44.555 33.962  72.485  1.00 29.39 ? 71   LEU   A CD2   1 
ATOM   434   N  N     . ILE   A  1  74   ? -39.916 31.965  74.443  1.00 27.40 ? 72   ILE   A N     1 
ATOM   435   C  CA    . ILE   A  1  74   ? -38.477 32.081  74.649  1.00 29.76 ? 72   ILE   A CA    1 
ATOM   436   C  C     . ILE   A  1  74   ? -37.726 31.129  73.730  1.00 32.90 ? 72   ILE   A C     1 
ATOM   437   O  O     . ILE   A  1  74   ? -36.662 31.467  73.199  1.00 31.64 ? 72   ILE   A O     1 
ATOM   438   C  CB    . ILE   A  1  74   ? -38.143 31.862  76.135  1.00 31.85 ? 72   ILE   A CB    1 
ATOM   439   C  CG1   . ILE   A  1  74   ? -38.637 33.055  76.959  1.00 29.70 ? 72   ILE   A CG1   1 
ATOM   440   C  CG2   . ILE   A  1  74   ? -36.646 31.638  76.338  1.00 29.91 ? 72   ILE   A CG2   1 
ATOM   441   C  CD1   . ILE   A  1  74   ? -38.729 32.770  78.438  1.00 32.87 ? 72   ILE   A CD1   1 
ATOM   442   N  N     . GLU   A  1  75   ? -38.267 29.929  73.521  1.00 33.83 ? 73   GLU   A N     1 
ATOM   443   C  CA    . GLU   A  1  75   ? -37.651 29.008  72.572  1.00 34.73 ? 73   GLU   A CA    1 
ATOM   444   C  C     . GLU   A  1  75   ? -37.656 29.594  71.166  1.00 36.49 ? 73   GLU   A C     1 
ATOM   445   O  O     . GLU   A  1  75   ? -36.673 29.465  70.428  1.00 34.56 ? 73   GLU   A O     1 
ATOM   446   C  CB    . GLU   A  1  75   ? -38.346 27.649  72.626  1.00 37.14 ? 73   GLU   A CB    1 
ATOM   447   C  CG    . GLU   A  1  75   ? -37.862 26.792  73.788  1.00 39.18 ? 73   GLU   A CG    1 
ATOM   448   C  CD    . GLU   A  1  75   ? -38.770 25.616  74.095  1.00 44.72 ? 73   GLU   A CD    1 
ATOM   449   O  OE1   . GLU   A  1  75   ? -39.829 25.489  73.442  1.00 44.15 ? 73   GLU   A OE1   1 
ATOM   450   O  OE2   . GLU   A  1  75   ? -38.423 24.822  75.000  1.00 47.19 ? 73   GLU   A OE2   1 
ATOM   451   N  N     . ALA   A  1  76   ? -38.741 30.274  70.792  1.00 35.57 ? 74   ALA   A N     1 
ATOM   452   C  CA    . ALA   A  1  76   ? -38.781 30.965  69.507  1.00 34.22 ? 74   ALA   A CA    1 
ATOM   453   C  C     . ALA   A  1  76   ? -37.740 32.078  69.443  1.00 36.45 ? 74   ALA   A C     1 
ATOM   454   O  O     . ALA   A  1  76   ? -37.026 32.216  68.443  1.00 40.55 ? 74   ALA   A O     1 
ATOM   455   C  CB    . ALA   A  1  76   ? -40.184 31.519  69.258  1.00 38.64 ? 74   ALA   A CB    1 
ATOM   456   N  N     . LEU   A  1  77   ? -37.649 32.893  70.501  1.00 34.54 ? 75   LEU   A N     1 
ATOM   457   C  CA    . LEU   A  1  77   ? -36.677 33.983  70.530  1.00 32.73 ? 75   LEU   A CA    1 
ATOM   458   C  C     . LEU   A  1  77   ? -35.257 33.452  70.393  1.00 38.55 ? 75   LEU   A C     1 
ATOM   459   O  O     . LEU   A  1  77   ? -34.478 33.924  69.557  1.00 39.29 ? 75   LEU   A O     1 
ATOM   460   C  CB    . LEU   A  1  77   ? -36.802 34.761  71.841  1.00 33.43 ? 75   LEU   A CB    1 
ATOM   461   C  CG    . LEU   A  1  77   ? -37.842 35.872  71.934  1.00 32.30 ? 75   LEU   A CG    1 
ATOM   462   C  CD1   . LEU   A  1  77   ? -37.781 36.493  73.314  1.00 33.10 ? 75   LEU   A CD1   1 
ATOM   463   C  CD2   . LEU   A  1  77   ? -37.577 36.910  70.867  1.00 34.93 ? 75   LEU   A CD2   1 
ATOM   464   N  N     . ARG   A  1  78   ? -34.902 32.471  71.219  1.00 33.93 ? 76   ARG   A N     1 
ATOM   465   C  CA    . ARG   A  1  78   ? -33.553 31.930  71.194  1.00 36.57 ? 76   ARG   A CA    1 
ATOM   466   C  C     . ARG   A  1  78   ? -33.264 31.138  69.928  1.00 38.06 ? 76   ARG   A C     1 
ATOM   467   O  O     . ARG   A  1  78   ? -32.092 30.951  69.588  1.00 42.23 ? 76   ARG   A O     1 
ATOM   468   C  CB    . ARG   A  1  78   ? -33.318 31.077  72.435  1.00 33.07 ? 76   ARG   A CB    1 
ATOM   469   C  CG    . ARG   A  1  78   ? -33.174 31.911  73.677  1.00 35.25 ? 76   ARG   A CG    1 
ATOM   470   C  CD    . ARG   A  1  78   ? -32.739 31.087  74.853  1.00 32.50 ? 76   ARG   A CD    1 
ATOM   471   N  NE    . ARG   A  1  78   ? -32.159 31.940  75.879  1.00 32.04 ? 76   ARG   A NE    1 
ATOM   472   C  CZ    . ARG   A  1  78   ? -31.720 31.506  77.050  1.00 31.58 ? 76   ARG   A CZ    1 
ATOM   473   N  NH1   . ARG   A  1  78   ? -31.798 30.229  77.386  1.00 35.02 ? 76   ARG   A NH1   1 
ATOM   474   N  NH2   . ARG   A  1  78   ? -31.196 32.375  77.908  1.00 33.66 ? 76   ARG   A NH2   1 
ATOM   475   N  N     . GLY   A  1  79   ? -34.294 30.675  69.228  1.00 40.01 ? 77   GLY   A N     1 
ATOM   476   C  CA    . GLY   A  1  79   ? -34.098 29.936  68.001  1.00 42.68 ? 77   GLY   A CA    1 
ATOM   477   C  C     . GLY   A  1  79   ? -33.911 30.774  66.759  1.00 46.72 ? 77   GLY   A C     1 
ATOM   478   O  O     . GLY   A  1  79   ? -33.735 30.223  65.671  1.00 47.99 ? 77   GLY   A O     1 
ATOM   479   N  N     . LYS   A  1  80   ? -33.947 32.100  66.882  1.00 47.40 ? 78   LYS   A N     1 
ATOM   480   C  CA    . LYS   A  1  80   ? -33.769 32.982  65.737  1.00 48.44 ? 78   LYS   A CA    1 
ATOM   481   C  C     . LYS   A  1  80   ? -32.812 34.130  66.029  1.00 47.58 ? 78   LYS   A C     1 
ATOM   482   O  O     . LYS   A  1  80   ? -32.734 35.071  65.230  1.00 54.52 ? 78   LYS   A O     1 
ATOM   483   C  CB    . LYS   A  1  80   ? -35.121 33.521  65.250  1.00 49.48 ? 78   LYS   A CB    1 
ATOM   484   C  CG    . LYS   A  1  80   ? -35.850 34.387  66.272  1.00 46.71 ? 78   LYS   A CG    1 
ATOM   485   C  CD    . LYS   A  1  80   ? -37.292 34.654  65.851  1.00 44.19 ? 78   LYS   A CD    1 
ATOM   486   C  CE    . LYS   A  1  80   ? -37.988 35.586  66.836  1.00 39.28 ? 78   LYS   A CE    1 
ATOM   487   N  NZ    . LYS   A  1  80   ? -39.391 35.934  66.431  1.00 32.20 ? 78   LYS   A NZ    1 
ATOM   488   N  N     . HIS   A  1  81   ? -32.086 34.076  67.142  1.00 46.85 ? 79   HIS   A N     1 
ATOM   489   C  CA    . HIS   A  1  81   ? -31.193 35.156  67.559  1.00 52.53 ? 79   HIS   A CA    1 
ATOM   490   C  C     . HIS   A  1  81   ? -30.178 35.540  66.480  1.00 58.71 ? 79   HIS   A C     1 
ATOM   491   O  O     . HIS   A  1  81   ? -29.530 34.680  65.885  1.00 63.46 ? 79   HIS   A O     1 
ATOM   492   C  CB    . HIS   A  1  81   ? -30.460 34.766  68.847  1.00 51.88 ? 79   HIS   A CB    1 
ATOM   493   N  N     . SER   A  1  84   ? -26.164 41.616  66.999  1.00 49.63 ? 82   SER   A N     1 
ATOM   494   C  CA    . SER   A  1  84   ? -25.548 40.668  66.080  1.00 49.61 ? 82   SER   A CA    1 
ATOM   495   C  C     . SER   A  1  84   ? -24.751 41.398  65.005  1.00 46.97 ? 82   SER   A C     1 
ATOM   496   O  O     . SER   A  1  84   ? -23.684 40.941  64.602  1.00 41.86 ? 82   SER   A O     1 
ATOM   497   C  CB    . SER   A  1  84   ? -26.606 39.767  65.435  1.00 53.94 ? 82   SER   A CB    1 
ATOM   498   N  N     . GLY   A  1  85   ? -25.280 42.529  64.538  1.00 46.49 ? 83   GLY   A N     1 
ATOM   499   C  CA    . GLY   A  1  85   ? -24.578 43.335  63.559  1.00 40.59 ? 83   GLY   A CA    1 
ATOM   500   C  C     . GLY   A  1  85   ? -23.222 43.789  64.066  1.00 33.60 ? 83   GLY   A C     1 
ATOM   501   O  O     . GLY   A  1  85   ? -22.194 43.546  63.426  1.00 33.42 ? 83   GLY   A O     1 
ATOM   502   N  N     . VAL   A  1  86   ? -23.217 44.458  65.221  1.00 36.07 ? 84   VAL   A N     1 
ATOM   503   C  CA    . VAL   A  1  86   ? -21.959 44.874  65.836  1.00 35.32 ? 84   VAL   A CA    1 
ATOM   504   C  C     . VAL   A  1  86   ? -21.101 43.659  66.160  1.00 34.58 ? 84   VAL   A C     1 
ATOM   505   O  O     . VAL   A  1  86   ? -19.890 43.649  65.906  1.00 30.99 ? 84   VAL   A O     1 
ATOM   506   C  CB    . VAL   A  1  86   ? -22.233 45.750  67.072  1.00 40.01 ? 84   VAL   A CB    1 
ATOM   507   C  CG1   . VAL   A  1  86   ? -20.980 45.891  67.926  1.00 37.97 ? 84   VAL   A CG1   1 
ATOM   508   C  CG2   . VAL   A  1  86   ? -22.743 47.117  66.640  1.00 39.52 ? 84   VAL   A CG2   1 
ATOM   509   N  N     . GLU   A  1  87   ? -21.719 42.607  66.705  1.00 35.19 ? 85   GLU   A N     1 
ATOM   510   C  CA    . GLU   A  1  87   ? -20.972 41.392  67.020  1.00 36.15 ? 85   GLU   A CA    1 
ATOM   511   C  C     . GLU   A  1  87   ? -20.292 40.823  65.782  1.00 36.04 ? 85   GLU   A C     1 
ATOM   512   O  O     . GLU   A  1  87   ? -19.117 40.436  65.832  1.00 37.28 ? 85   GLU   A O     1 
ATOM   513   C  CB    . GLU   A  1  87   ? -21.898 40.354  67.655  1.00 42.84 ? 85   GLU   A CB    1 
ATOM   514   N  N     . GLY   A  1  88   ? -21.008 40.774  64.656  1.00 33.26 ? 86   GLY   A N     1 
ATOM   515   C  CA    . GLY   A  1  88   ? -20.417 40.232  63.445  1.00 32.35 ? 86   GLY   A CA    1 
ATOM   516   C  C     . GLY   A  1  88   ? -19.274 41.072  62.917  1.00 30.84 ? 86   GLY   A C     1 
ATOM   517   O  O     . GLY   A  1  88   ? -18.321 40.540  62.342  1.00 32.88 ? 86   GLY   A O     1 
ATOM   518   N  N     . LEU   A  1  89   ? -19.346 42.389  63.112  1.00 31.40 ? 87   LEU   A N     1 
ATOM   519   C  CA    . LEU   A  1  89   ? -18.270 43.270  62.676  1.00 32.18 ? 87   LEU   A CA    1 
ATOM   520   C  C     . LEU   A  1  89   ? -17.034 43.063  63.542  1.00 26.90 ? 87   LEU   A C     1 
ATOM   521   O  O     . LEU   A  1  89   ? -15.918 42.927  63.028  1.00 28.94 ? 87   LEU   A O     1 
ATOM   522   C  CB    . LEU   A  1  89   ? -18.753 44.720  62.751  1.00 31.58 ? 87   LEU   A CB    1 
ATOM   523   C  CG    . LEU   A  1  89   ? -18.125 45.824  61.894  1.00 33.78 ? 87   LEU   A CG    1 
ATOM   524   C  CD1   . LEU   A  1  89   ? -18.843 47.139  62.160  1.00 34.01 ? 87   LEU   A CD1   1 
ATOM   525   C  CD2   . LEU   A  1  89   ? -16.641 45.976  62.163  1.00 36.51 ? 87   LEU   A CD2   1 
ATOM   526   N  N     . VAL   A  1  90   ? -17.224 43.037  64.863  1.00 28.96 ? 88   VAL   A N     1 
ATOM   527   C  CA    . VAL   A  1  90   ? -16.131 42.750  65.788  1.00 28.75 ? 88   VAL   A CA    1 
ATOM   528   C  C     . VAL   A  1  90   ? -15.460 41.428  65.440  1.00 28.77 ? 88   VAL   A C     1 
ATOM   529   O  O     . VAL   A  1  90   ? -14.229 41.312  65.471  1.00 27.98 ? 88   VAL   A O     1 
ATOM   530   C  CB    . VAL   A  1  90   ? -16.661 42.761  67.233  1.00 28.91 ? 88   VAL   A CB    1 
ATOM   531   C  CG1   . VAL   A  1  90   ? -15.649 42.153  68.180  1.00 33.15 ? 88   VAL   A CG1   1 
ATOM   532   C  CG2   . VAL   A  1  90   ? -17.017 44.176  67.647  1.00 28.50 ? 88   VAL   A CG2   1 
ATOM   533   N  N     . GLN   A  1  91   ? -16.259 40.409  65.110  1.00 31.04 ? 89   GLN   A N     1 
ATOM   534   C  CA    . GLN   A  1  91   ? -15.701 39.108  64.750  1.00 29.46 ? 89   GLN   A CA    1 
ATOM   535   C  C     . GLN   A  1  91   ? -14.919 39.181  63.445  1.00 32.29 ? 89   GLN   A C     1 
ATOM   536   O  O     . GLN   A  1  91   ? -13.783 38.700  63.362  1.00 33.84 ? 89   GLN   A O     1 
ATOM   537   C  CB    . GLN   A  1  91   ? -16.821 38.069  64.648  1.00 33.07 ? 89   GLN   A CB    1 
ATOM   538   N  N     . GLU   A  1  92   ? -15.506 39.793  62.414  1.00 30.52 ? 90   GLU   A N     1 
ATOM   539   C  CA    . GLU   A  1  92   ? -14.895 39.760  61.088  1.00 32.22 ? 90   GLU   A CA    1 
ATOM   540   C  C     . GLU   A  1  92   ? -13.530 40.438  61.078  1.00 28.98 ? 90   GLU   A C     1 
ATOM   541   O  O     . GLU   A  1  92   ? -12.593 39.964  60.423  1.00 30.13 ? 90   GLU   A O     1 
ATOM   542   C  CB    . GLU   A  1  92   ? -15.833 40.400  60.063  1.00 33.00 ? 90   GLU   A CB    1 
ATOM   543   C  CG    . GLU   A  1  92   ? -15.236 40.525  58.672  1.00 34.95 ? 90   GLU   A CG    1 
ATOM   544   C  CD    . GLU   A  1  92   ? -16.208 41.132  57.671  1.00 39.13 ? 90   GLU   A CD    1 
ATOM   545   O  OE1   . GLU   A  1  92   ? -17.398 41.295  58.016  1.00 40.67 ? 90   GLU   A OE1   1 
ATOM   546   O  OE2   . GLU   A  1  92   ? -15.778 41.451  56.541  1.00 40.68 ? 90   GLU   A OE2   1 
ATOM   547   N  N     . TYR   A  1  93   ? -13.389 41.535  61.815  1.00 26.50 ? 91   TYR   A N     1 
ATOM   548   C  CA    . TYR   A  1  93   ? -12.141 42.280  61.837  1.00 28.41 ? 91   TYR   A CA    1 
ATOM   549   C  C     . TYR   A  1  93   ? -11.339 42.060  63.108  1.00 29.40 ? 91   TYR   A C     1 
ATOM   550   O  O     . TYR   A  1  93   ? -10.360 42.774  63.335  1.00 27.72 ? 91   TYR   A O     1 
ATOM   551   C  CB    . TYR   A  1  93   ? -12.414 43.764  61.603  1.00 28.04 ? 91   TYR   A CB    1 
ATOM   552   C  CG    . TYR   A  1  93   ? -12.899 44.010  60.202  1.00 28.14 ? 91   TYR   A CG    1 
ATOM   553   C  CD1   . TYR   A  1  93   ? -11.998 44.112  59.146  1.00 28.94 ? 91   TYR   A CD1   1 
ATOM   554   C  CD2   . TYR   A  1  93   ? -14.253 44.099  59.922  1.00 28.90 ? 91   TYR   A CD2   1 
ATOM   555   C  CE1   . TYR   A  1  93   ? -12.438 44.318  57.852  1.00 30.07 ? 91   TYR   A CE1   1 
ATOM   556   C  CE2   . TYR   A  1  93   ? -14.701 44.310  58.633  1.00 32.27 ? 91   TYR   A CE2   1 
ATOM   557   C  CZ    . TYR   A  1  93   ? -13.787 44.421  57.607  1.00 29.57 ? 91   TYR   A CZ    1 
ATOM   558   O  OH    . TYR   A  1  93   ? -14.229 44.619  56.323  1.00 35.69 ? 91   TYR   A OH    1 
ATOM   559   N  N     . SER   A  1  94   ? -11.729 41.091  63.935  1.00 25.75 ? 92   SER   A N     1 
ATOM   560   C  CA    . SER   A  1  94   ? -10.982 40.741  65.145  1.00 25.34 ? 92   SER   A CA    1 
ATOM   561   C  C     . SER   A  1  94   ? -10.753 41.967  66.026  1.00 21.97 ? 92   SER   A C     1 
ATOM   562   O  O     . SER   A  1  94   ? -9.651  42.215  66.521  1.00 25.08 ? 92   SER   A O     1 
ATOM   563   C  CB    . SER   A  1  94   ? -9.664  40.046  64.809  1.00 28.95 ? 92   SER   A CB    1 
ATOM   564   O  OG    . SER   A  1  94   ? -9.880  38.964  63.919  1.00 30.03 ? 92   SER   A OG    1 
ATOM   565   N  N     . LEU   A  1  95   ? -11.816 42.747  66.207  1.00 20.81 ? 93   LEU   A N     1 
ATOM   566   C  CA    . LEU   A  1  95   ? -11.727 43.978  66.968  1.00 22.75 ? 93   LEU   A CA    1 
ATOM   567   C  C     . LEU   A  1  95   ? -11.747 43.684  68.458  1.00 22.00 ? 93   LEU   A C     1 
ATOM   568   O  O     . LEU   A  1  95   ? -12.511 42.842  68.933  1.00 23.78 ? 93   LEU   A O     1 
ATOM   569   C  CB    . LEU   A  1  95   ? -12.912 44.883  66.636  1.00 21.73 ? 93   LEU   A CB    1 
ATOM   570   C  CG    . LEU   A  1  95   ? -13.031 45.323  65.181  1.00 21.88 ? 93   LEU   A CG    1 
ATOM   571   C  CD1   . LEU   A  1  95   ? -14.134 46.371  65.081  1.00 24.91 ? 93   LEU   A CD1   1 
ATOM   572   C  CD2   . LEU   A  1  95   ? -11.697 45.853  64.638  1.00 22.86 ? 93   LEU   A CD2   1 
ATOM   573   N  N     . SER   A  1  96   ? -10.899 44.386  69.195  1.00 20.25 ? 94   SER   A N     1 
ATOM   574   C  CA    . SER   A  1  96   ? -11.087 44.457  70.632  1.00 21.03 ? 94   SER   A CA    1 
ATOM   575   C  C     . SER   A  1  96   ? -12.338 45.288  70.941  1.00 19.97 ? 94   SER   A C     1 
ATOM   576   O  O     . SER   A  1  96   ? -12.912 45.943  70.070  1.00 19.40 ? 94   SER   A O     1 
ATOM   577   C  CB    . SER   A  1  96   ? -9.865  45.113  71.265  1.00 21.68 ? 94   SER   A CB    1 
ATOM   578   O  OG    . SER   A  1  96   ? -9.828  46.489  70.909  1.00 19.67 ? 94   SER   A OG    1 
ATOM   579   N  N     . SER   A  1  97   ? -12.758 45.272  72.204  1.00 19.90 ? 95   SER   A N     1 
ATOM   580   C  CA    . SER   A  1  97   ? -13.909 46.086  72.584  1.00 20.66 ? 95   SER   A CA    1 
ATOM   581   C  C     . SER   A  1  97   ? -13.631 47.563  72.354  1.00 19.68 ? 95   SER   A C     1 
ATOM   582   O  O     . SER   A  1  97   ? -14.475 48.285  71.809  1.00 18.70 ? 95   SER   A O     1 
ATOM   583   C  CB    . SER   A  1  97   ? -14.279 45.827  74.041  1.00 24.05 ? 95   SER   A CB    1 
ATOM   584   O  OG    . SER   A  1  97   ? -14.778 44.515  74.180  1.00 33.41 ? 95   SER   A OG    1 
ATOM   585   N  N     . GLN   A  1  98   ? -12.446 48.030  72.745  1.00 18.20 ? 96   GLN   A N     1 
ATOM   586   C  CA    . GLN   A  1  98   ? -12.138 49.439  72.551  1.00 17.50 ? 96   GLN   A CA    1 
ATOM   587   C  C     . GLN   A  1  98   ? -12.093 49.783  71.072  1.00 15.98 ? 96   GLN   A C     1 
ATOM   588   O  O     . GLN   A  1  98   ? -12.524 50.868  70.675  1.00 16.32 ? 96   GLN   A O     1 
ATOM   589   C  CB    . GLN   A  1  98   ? -10.839 49.815  73.261  1.00 17.46 ? 96   GLN   A CB    1 
ATOM   590   C  CG    . GLN   A  1  98   ? -10.988 49.899  74.780  1.00 19.07 ? 96   GLN   A CG    1 
ATOM   591   C  CD    . GLN   A  1  98   ? -11.927 51.010  75.223  1.00 18.07 ? 96   GLN   A CD    1 
ATOM   592   O  OE1   . GLN   A  1  98   ? -13.153 50.845  75.245  1.00 20.16 ? 96   GLN   A OE1   1 
ATOM   593   N  NE2   . GLN   A  1  98   ? -11.358 52.157  75.573  1.00 21.29 ? 96   GLN   A NE2   1 
ATOM   594   N  N     . GLU   A  1  99   ? -11.586 48.869  70.238  1.00 15.59 ? 97   GLU   A N     1 
ATOM   595   C  CA    . GLU   A  1  99   ? -11.614 49.116  68.800  1.00 15.95 ? 97   GLU   A CA    1 
ATOM   596   C  C     . GLU   A  1  99   ? -13.044 49.199  68.292  1.00 16.67 ? 97   GLU   A C     1 
ATOM   597   O  O     . GLU   A  1  99   ? -13.369 50.071  67.478  1.00 16.77 ? 97   GLU   A O     1 
ATOM   598   C  CB    . GLU   A  1  99   ? -10.831 48.036  68.068  1.00 15.41 ? 97   GLU   A CB    1 
ATOM   599   C  CG    . GLU   A  1  99   ? -9.341  48.191  68.305  1.00 15.42 ? 97   GLU   A CG    1 
ATOM   600   C  CD    . GLU   A  1  99   ? -8.556  47.007  67.826  1.00 17.87 ? 97   GLU   A CD    1 
ATOM   601   O  OE1   . GLU   A  1  99   ? -9.170  46.004  67.401  1.00 18.99 ? 97   GLU   A OE1   1 
ATOM   602   O  OE2   . GLU   A  1  99   ? -7.313  47.081  67.888  1.00 19.13 ? 97   GLU   A OE2   1 
ATOM   603   N  N     . GLY   A  1  100  ? -13.910 48.298  68.758  1.00 16.69 ? 98   GLY   A N     1 
ATOM   604   C  CA    . GLY   A  1  100  ? -15.300 48.344  68.335  1.00 17.37 ? 98   GLY   A CA    1 
ATOM   605   C  C     . GLY   A  1  100  ? -15.956 49.656  68.709  1.00 17.49 ? 98   GLY   A C     1 
ATOM   606   O  O     . GLY   A  1  100  ? -16.643 50.274  67.896  1.00 17.55 ? 98   GLY   A O     1 
ATOM   607   N  N     . VAL   A  1  101  ? -15.733 50.108  69.945  1.00 15.79 ? 99   VAL   A N     1 
ATOM   608   C  CA    . VAL   A  1  101  ? -16.286 51.385  70.377  1.00 17.16 ? 99   VAL   A CA    1 
ATOM   609   C  C     . VAL   A  1  101  ? -15.721 52.522  69.543  1.00 16.16 ? 99   VAL   A C     1 
ATOM   610   O  O     . VAL   A  1  101  ? -16.464 53.395  69.073  1.00 16.82 ? 99   VAL   A O     1 
ATOM   611   C  CB    . VAL   A  1  101  ? -16.030 51.609  71.872  1.00 16.47 ? 99   VAL   A CB    1 
ATOM   612   C  CG1   . VAL   A  1  101  ? -16.476 53.014  72.249  1.00 17.14 ? 99   VAL   A CG1   1 
ATOM   613   C  CG2   . VAL   A  1  101  ? -16.776 50.550  72.682  1.00 17.98 ? 99   VAL   A CG2   1 
ATOM   614   N  N     . ALA   A  1  102  ? -14.393 52.534  69.356  1.00 14.97 ? 100  ALA   A N     1 
ATOM   615   C  CA    . ALA   A  1  102  ? -13.764 53.630  68.629  1.00 15.92 ? 100  ALA   A CA    1 
ATOM   616   C  C     . ALA   A  1  102  ? -14.254 53.665  67.194  1.00 14.02 ? 100  ALA   A C     1 
ATOM   617   O  O     . ALA   A  1  102  ? -14.487 54.743  66.639  1.00 17.15 ? 100  ALA   A O     1 
ATOM   618   C  CB    . ALA   A  1  102  ? -12.239 53.504  68.678  1.00 16.26 ? 100  ALA   A CB    1 
ATOM   619   N  N     . LEU   A  1  103  ? -14.415 52.488  66.584  1.00 15.51 ? 101  LEU   A N     1 
ATOM   620   C  CA    . LEU   A  1  103  ? -14.928 52.414  65.222  1.00 16.39 ? 101  LEU   A CA    1 
ATOM   621   C  C     . LEU   A  1  103  ? -16.318 53.022  65.129  1.00 17.17 ? 101  LEU   A C     1 
ATOM   622   O  O     . LEU   A  1  103  ? -16.612 53.781  64.201  1.00 19.03 ? 101  LEU   A O     1 
ATOM   623   C  CB    . LEU   A  1  103  ? -14.952 50.963  64.754  1.00 15.23 ? 101  LEU   A CB    1 
ATOM   624   C  CG    . LEU   A  1  103  ? -15.575 50.793  63.365  1.00 17.53 ? 101  LEU   A CG    1 
ATOM   625   C  CD1   . LEU   A  1  103  ? -14.750 51.548  62.335  1.00 20.31 ? 101  LEU   A CD1   1 
ATOM   626   C  CD2   . LEU   A  1  103  ? -15.682 49.329  63.017  1.00 20.46 ? 101  LEU   A CD2   1 
ATOM   627   N  N     . MET   A  1  104  ? -17.196 52.691  66.076  1.00 17.87 ? 102  MET   A N     1 
ATOM   628   C  CA    . MET   A  1  104  ? -18.544 53.242  66.012  1.00 15.96 ? 102  MET   A CA    1 
ATOM   629   C  C     . MET   A  1  104  ? -18.537 54.746  66.238  1.00 18.28 ? 102  MET   A C     1 
ATOM   630   O  O     . MET   A  1  104  ? -19.327 55.464  65.618  1.00 19.34 ? 102  MET   A O     1 
ATOM   631   C  CB    . MET   A  1  104  ? -19.456 52.536  67.017  1.00 16.59 ? 102  MET   A CB    1 
ATOM   632   C  CG    . MET   A  1  104  ? -19.601 51.055  66.734  1.00 18.48 ? 102  MET   A CG    1 
ATOM   633   S  SD    . MET   A  1  104  ? -20.045 50.709  64.999  1.00 29.03 ? 102  MET   A SD    1 
ATOM   634   C  CE    . MET   A  1  104  ? -21.724 51.307  64.962  1.00 27.72 ? 102  MET   A CE    1 
ATOM   635   N  N     . CYS   A  1  105  ? -17.637 55.242  67.093  1.00 15.72 ? 103  CYS   A N     1 
ATOM   636   C  CA    . CYS   A  1  105  ? -17.510 56.686  67.273  1.00 16.46 ? 103  CYS   A CA    1 
ATOM   637   C  C     . CYS   A  1  105  ? -17.054 57.353  65.988  1.00 21.03 ? 103  CYS   A C     1 
ATOM   638   O  O     . CYS   A  1  105  ? -17.569 58.413  65.616  1.00 21.47 ? 103  CYS   A O     1 
ATOM   639   C  CB    . CYS   A  1  105  ? -16.517 57.000  68.384  1.00 18.31 ? 103  CYS   A CB    1 
ATOM   640   S  SG    . CYS   A  1  105  ? -17.087 56.552  70.009  1.00 19.47 ? 103  CYS   A SG    1 
ATOM   641   N  N     . LEU   A  1  106  ? -16.068 56.762  65.308  1.00 17.70 ? 104  LEU   A N     1 
ATOM   642   C  CA    . LEU   A  1  106  ? -15.651 57.295  64.019  1.00 18.43 ? 104  LEU   A CA    1 
ATOM   643   C  C     . LEU   A  1  106  ? -16.799 57.267  63.025  1.00 21.96 ? 104  LEU   A C     1 
ATOM   644   O  O     . LEU   A  1  106  ? -17.011 58.231  62.280  1.00 22.01 ? 104  LEU   A O     1 
ATOM   645   C  CB    . LEU   A  1  106  ? -14.479 56.487  63.465  1.00 18.70 ? 104  LEU   A CB    1 
ATOM   646   C  CG    . LEU   A  1  106  ? -14.168 56.822  62.001  1.00 19.35 ? 104  LEU   A CG    1 
ATOM   647   C  CD1   . LEU   A  1  106  ? -13.673 58.255  61.891  1.00 21.54 ? 104  LEU   A CD1   1 
ATOM   648   C  CD2   . LEU   A  1  106  ? -13.170 55.841  61.427  1.00 25.04 ? 104  LEU   A CD2   1 
ATOM   649   N  N     . ALA   A  1  107  ? -17.536 56.159  62.981  1.00 19.00 ? 105  ALA   A N     1 
ATOM   650   C  CA    . ALA   A  1  107  ? -18.654 56.082  62.050  1.00 20.68 ? 105  ALA   A CA    1 
ATOM   651   C  C     . ALA   A  1  107  ? -19.680 57.168  62.352  1.00 24.83 ? 105  ALA   A C     1 
ATOM   652   O  O     . ALA   A  1  107  ? -20.170 57.836  61.433  1.00 23.00 ? 105  ALA   A O     1 
ATOM   653   C  CB    . ALA   A  1  107  ? -19.273 54.691  62.087  1.00 19.44 ? 105  ALA   A CB    1 
ATOM   654   N  N     . GLU   A  1  108  ? -19.990 57.378  63.638  1.00 22.43 ? 106  GLU   A N     1 
ATOM   655   C  CA    . GLU   A  1  108  ? -20.906 58.445  64.034  1.00 24.42 ? 106  GLU   A CA    1 
ATOM   656   C  C     . GLU   A  1  108  ? -20.432 59.790  63.499  1.00 28.18 ? 106  GLU   A C     1 
ATOM   657   O  O     . GLU   A  1  108  ? -21.220 60.565  62.942  1.00 29.21 ? 106  GLU   A O     1 
ATOM   658   C  CB    . GLU   A  1  108  ? -21.007 58.478  65.563  1.00 25.40 ? 106  GLU   A CB    1 
ATOM   659   C  CG    . GLU   A  1  108  ? -21.864 59.608  66.146  1.00 26.17 ? 106  GLU   A CG    1 
ATOM   660   C  CD    . GLU   A  1  108  ? -21.567 59.891  67.617  1.00 28.88 ? 106  GLU   A CD    1 
ATOM   661   O  OE1   . GLU   A  1  108  ? -21.114 58.970  68.336  1.00 27.49 ? 106  GLU   A OE1   1 
ATOM   662   O  OE2   . GLU   A  1  108  ? -21.778 61.045  68.055  1.00 31.88 ? 106  GLU   A OE2   1 
ATOM   663   N  N     . ALA   A  1  109  ? -19.132 60.065  63.625  1.00 23.78 ? 107  ALA   A N     1 
ATOM   664   C  CA    . ALA   A  1  109  ? -18.583 61.341  63.180  1.00 27.74 ? 107  ALA   A CA    1 
ATOM   665   C  C     . ALA   A  1  109  ? -18.642 61.471  61.664  1.00 29.92 ? 107  ALA   A C     1 
ATOM   666   O  O     . ALA   A  1  109  ? -18.948 62.549  61.140  1.00 32.32 ? 107  ALA   A O     1 
ATOM   667   C  CB    . ALA   A  1  109  ? -17.144 61.485  63.669  1.00 27.17 ? 107  ALA   A CB    1 
ATOM   668   N  N     . LEU   A  1  110  ? -18.332 60.388  60.943  1.00 24.55 ? 108  LEU   A N     1 
ATOM   669   C  CA    . LEU   A  1  110  ? -18.401 60.418  59.489  1.00 26.66 ? 108  LEU   A CA    1 
ATOM   670   C  C     . LEU   A  1  110  ? -19.826 60.642  59.007  1.00 29.23 ? 108  LEU   A C     1 
ATOM   671   O  O     . LEU   A  1  110  ? -20.036 61.258  57.955  1.00 29.75 ? 108  LEU   A O     1 
ATOM   672   C  CB    . LEU   A  1  110  ? -17.840 59.117  58.908  1.00 23.74 ? 108  LEU   A CB    1 
ATOM   673   C  CG    . LEU   A  1  110  ? -16.322 58.972  59.040  1.00 27.58 ? 108  LEU   A CG    1 
ATOM   674   C  CD1   . LEU   A  1  110  ? -15.878 57.556  58.722  1.00 25.06 ? 108  LEU   A CD1   1 
ATOM   675   C  CD2   . LEU   A  1  110  ? -15.632 59.970  58.111  1.00 28.74 ? 108  LEU   A CD2   1 
ATOM   676   N  N     . LEU   A  1  111  ? -20.814 60.146  59.752  1.00 27.87 ? 109  LEU   A N     1 
ATOM   677   C  CA    . LEU   A  1  111  ? -22.204 60.340  59.368  1.00 29.65 ? 109  LEU   A CA    1 
ATOM   678   C  C     . LEU   A  1  111  ? -22.690 61.757  59.624  1.00 36.47 ? 109  LEU   A C     1 
ATOM   679   O  O     . LEU   A  1  111  ? -23.755 62.127  59.117  1.00 37.86 ? 109  LEU   A O     1 
ATOM   680   C  CB    . LEU   A  1  111  ? -23.090 59.323  60.086  1.00 29.58 ? 109  LEU   A CB    1 
ATOM   681   C  CG    . LEU   A  1  111  ? -22.852 57.900  59.583  1.00 29.06 ? 109  LEU   A CG    1 
ATOM   682   C  CD1   . LEU   A  1  111  ? -23.600 56.895  60.427  1.00 30.73 ? 109  LEU   A CD1   1 
ATOM   683   C  CD2   . LEU   A  1  111  ? -23.226 57.776  58.116  1.00 30.71 ? 109  LEU   A CD2   1 
ATOM   684   N  N     . ARG   A  1  112  ? -21.943 62.551  60.391  1.00 33.69 ? 110  ARG   A N     1 
ATOM   685   C  CA    . ARG   A  1  112  ? -22.240 63.971  60.527  1.00 37.45 ? 110  ARG   A CA    1 
ATOM   686   C  C     . ARG   A  1  112  ? -21.851 64.762  59.288  1.00 38.70 ? 110  ARG   A C     1 
ATOM   687   O  O     . ARG   A  1  112  ? -22.262 65.919  59.158  1.00 42.94 ? 110  ARG   A O     1 
ATOM   688   C  CB    . ARG   A  1  112  ? -21.560 64.541  61.771  1.00 36.67 ? 110  ARG   A CB    1 
ATOM   689   C  CG    . ARG   A  1  112  ? -22.133 64.007  63.079  1.00 36.79 ? 110  ARG   A CG    1 
ATOM   690   C  CD    . ARG   A  1  112  ? -21.138 64.121  64.224  1.00 40.65 ? 110  ARG   A CD    1 
ATOM   691   N  NE    . ARG   A  1  112  ? -20.868 65.503  64.603  1.00 48.99 ? 110  ARG   A NE    1 
ATOM   692   C  CZ    . ARG   A  1  112  ? -21.501 66.156  65.570  1.00 57.04 ? 110  ARG   A CZ    1 
ATOM   693   N  NH1   . ARG   A  1  112  ? -22.464 65.585  66.276  1.00 55.95 ? 110  ARG   A NH1   1 
ATOM   694   N  NH2   . ARG   A  1  112  ? -21.156 67.413  65.838  1.00 59.43 ? 110  ARG   A NH2   1 
ATOM   695   N  N     . ILE   A  1  113  ? -21.067 64.173  58.391  1.00 39.94 ? 111  ILE   A N     1 
ATOM   696   C  CA    . ILE   A  1  113  ? -20.820 64.742  57.069  1.00 40.67 ? 111  ILE   A CA    1 
ATOM   697   C  C     . ILE   A  1  113  ? -22.054 64.477  56.216  1.00 42.81 ? 111  ILE   A C     1 
ATOM   698   O  O     . ILE   A  1  113  ? -22.363 63.313  55.922  1.00 43.19 ? 111  ILE   A O     1 
ATOM   699   C  CB    . ILE   A  1  113  ? -19.571 64.127  56.425  1.00 36.09 ? 111  ILE   A CB    1 
ATOM   700   C  CG1   . ILE   A  1  113  ? -18.325 64.471  57.241  1.00 34.93 ? 111  ILE   A CG1   1 
ATOM   701   C  CG2   . ILE   A  1  113  ? -19.445 64.592  54.981  1.00 42.12 ? 111  ILE   A CG2   1 
ATOM   702   C  CD1   . ILE   A  1  113  ? -17.078 63.791  56.733  1.00 35.99 ? 111  ILE   A CD1   1 
ATOM   703   N  N     . PRO   A  1  114  ? -22.782 65.515  55.793  1.00 46.74 ? 112  PRO   A N     1 
ATOM   704   C  CA    . PRO   A  1  114  ? -24.067 65.293  55.113  1.00 46.80 ? 112  PRO   A CA    1 
ATOM   705   C  C     . PRO   A  1  114  ? -23.963 64.607  53.757  1.00 46.11 ? 112  PRO   A C     1 
ATOM   706   O  O     . PRO   A  1  114  ? -24.689 63.644  53.494  1.00 52.38 ? 112  PRO   A O     1 
ATOM   707   C  CB    . PRO   A  1  114  ? -24.646 66.709  54.984  1.00 48.86 ? 112  PRO   A CB    1 
ATOM   708   C  CG    . PRO   A  1  114  ? -23.919 67.519  56.017  1.00 51.60 ? 112  PRO   A CG    1 
ATOM   709   C  CD    . PRO   A  1  114  ? -22.538 66.941  56.060  1.00 47.74 ? 112  PRO   A CD    1 
ATOM   710   N  N     . ASP   A  1  115  ? -23.078 65.086  52.885  1.00 50.17 ? 113  ASP   A N     1 
ATOM   711   C  CA    . ASP   A  1  115  ? -23.004 64.560  51.528  1.00 51.30 ? 113  ASP   A CA    1 
ATOM   712   C  C     . ASP   A  1  115  ? -22.275 63.223  51.503  1.00 48.50 ? 113  ASP   A C     1 
ATOM   713   O  O     . ASP   A  1  115  ? -21.157 63.105  52.012  1.00 47.80 ? 113  ASP   A O     1 
ATOM   714   C  CB    . ASP   A  1  115  ? -22.295 65.545  50.602  1.00 49.81 ? 113  ASP   A CB    1 
ATOM   715   C  CG    . ASP   A  1  115  ? -22.112 64.988  49.203  1.00 54.86 ? 113  ASP   A CG    1 
ATOM   716   O  OD1   . ASP   A  1  115  ? -23.134 64.726  48.530  1.00 55.38 ? 113  ASP   A OD1   1 
ATOM   717   O  OD2   . ASP   A  1  115  ? -20.949 64.797  48.781  1.00 51.33 ? 113  ASP   A OD2   1 
ATOM   718   N  N     . THR   A  1  116  ? -22.901 62.226  50.873  1.00 47.38 ? 114  THR   A N     1 
ATOM   719   C  CA    . THR   A  1  116  ? -22.329 60.884  50.840  1.00 46.74 ? 114  THR   A CA    1 
ATOM   720   C  C     . THR   A  1  116  ? -21.027 60.840  50.046  1.00 49.11 ? 114  THR   A C     1 
ATOM   721   O  O     . THR   A  1  116  ? -20.063 60.188  50.463  1.00 45.47 ? 114  THR   A O     1 
ATOM   722   C  CB    . THR   A  1  116  ? -23.350 59.902  50.269  1.00 45.96 ? 114  THR   A CB    1 
ATOM   723   O  OG1   . THR   A  1  116  ? -24.538 59.936  51.070  1.00 51.41 ? 114  THR   A OG1   1 
ATOM   724   C  CG2   . THR   A  1  116  ? -22.788 58.489  50.262  1.00 48.56 ? 114  THR   A CG2   1 
ATOM   725   N  N     . ALA   A  1  117  ? -20.978 61.519  48.897  1.00 44.64 ? 115  ALA   A N     1 
ATOM   726   C  CA    . ALA   A  1  117  ? -19.755 61.510  48.100  1.00 47.64 ? 115  ALA   A CA    1 
ATOM   727   C  C     . ALA   A  1  117  ? -18.596 62.141  48.861  1.00 44.96 ? 115  ALA   A C     1 
ATOM   728   O  O     . ALA   A  1  117  ? -17.462 61.651  48.799  1.00 42.68 ? 115  ALA   A O     1 
ATOM   729   C  CB    . ALA   A  1  117  ? -19.984 62.216  46.763  1.00 46.93 ? 115  ALA   A CB    1 
ATOM   730   N  N     . THR   A  1  118  ? -18.862 63.229  49.588  1.00 43.88 ? 116  THR   A N     1 
ATOM   731   C  CA    . THR   A  1  118  ? -17.810 63.859  50.378  1.00 43.18 ? 116  THR   A CA    1 
ATOM   732   C  C     . THR   A  1  118  ? -17.336 62.931  51.487  1.00 38.76 ? 116  THR   A C     1 
ATOM   733   O  O     . THR   A  1  118  ? -16.133 62.816  51.741  1.00 38.40 ? 116  THR   A O     1 
ATOM   734   C  CB    . THR   A  1  118  ? -18.317 65.172  50.971  1.00 44.10 ? 116  THR   A CB    1 
ATOM   735   O  OG1   . THR   A  1  118  ? -18.784 66.025  49.917  1.00 54.78 ? 116  THR   A OG1   1 
ATOM   736   C  CG2   . THR   A  1  118  ? -17.208 65.875  51.726  1.00 39.17 ? 116  THR   A CG2   1 
ATOM   737   N  N     . ARG   A  1  119  ? -18.272 62.260  52.156  1.00 38.07 ? 117  ARG   A N     1 
ATOM   738   C  CA    . ARG   A  1  119  ? -17.899 61.325  53.211  1.00 38.23 ? 117  ARG   A CA    1 
ATOM   739   C  C     . ARG   A  1  119  ? -17.064 60.180  52.650  1.00 39.02 ? 117  ARG   A C     1 
ATOM   740   O  O     . ARG   A  1  119  ? -16.035 59.807  53.223  1.00 37.13 ? 117  ARG   A O     1 
ATOM   741   C  CB    . ARG   A  1  119  ? -19.162 60.787  53.878  1.00 35.14 ? 117  ARG   A CB    1 
ATOM   742   C  CG    . ARG   A  1  119  ? -18.901 59.904  55.082  1.00 34.00 ? 117  ARG   A CG    1 
ATOM   743   C  CD    . ARG   A  1  119  ? -20.158 59.150  55.482  1.00 35.85 ? 117  ARG   A CD    1 
ATOM   744   N  NE    . ARG   A  1  119  ? -21.293 60.044  55.675  1.00 37.39 ? 117  ARG   A NE    1 
ATOM   745   C  CZ    . ARG   A  1  119  ? -22.476 59.888  55.098  1.00 36.55 ? 117  ARG   A CZ    1 
ATOM   746   N  NH1   . ARG   A  1  119  ? -22.728 58.859  54.305  1.00 37.59 ? 117  ARG   A NH1   1 
ATOM   747   N  NH2   . ARG   A  1  119  ? -23.435 60.779  55.334  1.00 45.69 ? 117  ARG   A NH2   1 
ATOM   748   N  N     . ASP   A  1  120  ? -17.496 59.614  51.519  1.00 39.90 ? 118  ASP   A N     1 
ATOM   749   C  CA    . ASP   A  1  120  ? -16.783 58.480  50.938  1.00 41.16 ? 118  ASP   A CA    1 
ATOM   750   C  C     . ASP   A  1  120  ? -15.392 58.884  50.470  1.00 40.37 ? 118  ASP   A C     1 
ATOM   751   O  O     . ASP   A  1  120  ? -14.442 58.099  50.579  1.00 36.92 ? 118  ASP   A O     1 
ATOM   752   C  CB    . ASP   A  1  120  ? -17.597 57.873  49.793  1.00 38.97 ? 118  ASP   A CB    1 
ATOM   753   C  CG    . ASP   A  1  120  ? -18.922 57.292  50.262  1.00 46.42 ? 118  ASP   A CG    1 
ATOM   754   O  OD1   . ASP   A  1  120  ? -19.208 57.351  51.477  1.00 45.80 ? 118  ASP   A OD1   1 
ATOM   755   O  OD2   . ASP   A  1  120  ? -19.682 56.772  49.416  1.00 46.90 ? 118  ASP   A OD2   1 
ATOM   756   N  N     . ALA   A  1  121  ? -15.252 60.109  49.957  1.00 38.98 ? 119  ALA   A N     1 
ATOM   757   C  CA    . ALA   A  1  121  ? -13.936 60.599  49.563  1.00 40.88 ? 119  ALA   A CA    1 
ATOM   758   C  C     . ALA   A  1  121  ? -13.036 60.799  50.774  1.00 39.97 ? 119  ALA   A C     1 
ATOM   759   O  O     . ALA   A  1  121  ? -11.860 60.419  50.751  1.00 41.66 ? 119  ALA   A O     1 
ATOM   760   C  CB    . ALA   A  1  121  ? -14.073 61.900  48.772  1.00 42.79 ? 119  ALA   A CB    1 
ATOM   761   N  N     . LEU   A  1  122  ? -13.571 61.393  51.844  1.00 41.23 ? 120  LEU   A N     1 
ATOM   762   C  CA    . LEU   A  1  122  ? -12.784 61.556  53.060  1.00 39.66 ? 120  LEU   A CA    1 
ATOM   763   C  C     . LEU   A  1  122  ? -12.326 60.207  53.597  1.00 38.52 ? 120  LEU   A C     1 
ATOM   764   O  O     . LEU   A  1  122  ? -11.168 60.051  53.998  1.00 38.80 ? 120  LEU   A O     1 
ATOM   765   C  CB    . LEU   A  1  122  ? -13.592 62.303  54.116  1.00 38.87 ? 120  LEU   A CB    1 
ATOM   766   C  CG    . LEU   A  1  122  ? -12.731 62.774  55.285  1.00 37.05 ? 120  LEU   A CG    1 
ATOM   767   C  CD1   . LEU   A  1  122  ? -11.716 63.790  54.791  1.00 44.96 ? 120  LEU   A CD1   1 
ATOM   768   C  CD2   . LEU   A  1  122  ? -13.581 63.351  56.398  1.00 35.31 ? 120  LEU   A CD2   1 
ATOM   769   N  N     . ILE   A  1  123  ? -13.220 59.216  53.599  1.00 38.36 ? 121  ILE   A N     1 
ATOM   770   C  CA    . ILE   A  1  123  ? -12.839 57.872  54.025  1.00 37.49 ? 121  ILE   A CA    1 
ATOM   771   C  C     . ILE   A  1  123  ? -11.715 57.338  53.150  1.00 39.20 ? 121  ILE   A C     1 
ATOM   772   O  O     . ILE   A  1  123  ? -10.658 56.930  53.644  1.00 38.24 ? 121  ILE   A O     1 
ATOM   773   C  CB    . ILE   A  1  123  ? -14.058 56.934  54.008  1.00 34.44 ? 121  ILE   A CB    1 
ATOM   774   C  CG1   . ILE   A  1  123  ? -15.063 57.319  55.101  1.00 33.87 ? 121  ILE   A CG1   1 
ATOM   775   C  CG2   . ILE   A  1  123  ? -13.604 55.479  54.125  1.00 33.26 ? 121  ILE   A CG2   1 
ATOM   776   C  CD1   . ILE   A  1  123  ? -16.403 56.634  54.964  1.00 32.60 ? 121  ILE   A CD1   1 
ATOM   777   N  N     . ARG   A  1  124  ? -11.924 57.353  51.831  1.00 36.97 ? 122  ARG   A N     1 
ATOM   778   C  CA    . ARG   A  1  124  ? -10.989 56.709  50.911  1.00 43.13 ? 122  ARG   A CA    1 
ATOM   779   C  C     . ARG   A  1  124  ? -9.631  57.400  50.908  1.00 46.72 ? 122  ARG   A C     1 
ATOM   780   O  O     . ARG   A  1  124  ? -8.586  56.738  50.948  1.00 47.06 ? 122  ARG   A O     1 
ATOM   781   C  CB    . ARG   A  1  124  ? -11.580 56.689  49.501  1.00 40.97 ? 122  ARG   A CB    1 
ATOM   782   N  N     . ASP   A  1  125  ? -9.622  58.732  50.866  1.00 45.28 ? 123  ASP   A N     1 
ATOM   783   C  CA    . ASP   A  1  125  ? -8.394  59.470  50.607  1.00 49.73 ? 123  ASP   A CA    1 
ATOM   784   C  C     . ASP   A  1  125  ? -7.692  59.969  51.862  1.00 49.77 ? 123  ASP   A C     1 
ATOM   785   O  O     . ASP   A  1  125  ? -6.483  60.217  51.810  1.00 51.53 ? 123  ASP   A O     1 
ATOM   786   C  CB    . ASP   A  1  125  ? -8.670  60.660  49.676  1.00 55.42 ? 123  ASP   A CB    1 
ATOM   787   C  CG    . ASP   A  1  125  ? -9.381  60.251  48.396  1.00 56.62 ? 123  ASP   A CG    1 
ATOM   788   O  OD1   . ASP   A  1  125  ? -9.101  59.147  47.877  1.00 58.81 ? 123  ASP   A OD1   1 
ATOM   789   O  OD2   . ASP   A  1  125  ? -10.225 61.034  47.909  1.00 56.68 ? 123  ASP   A OD2   1 
ATOM   790   N  N     . LYS   A  1  126  ? -8.401  60.109  52.982  1.00 44.98 ? 124  LYS   A N     1 
ATOM   791   C  CA    . LYS   A  1  126  ? -7.814  60.755  54.150  1.00 42.78 ? 124  LYS   A CA    1 
ATOM   792   C  C     . LYS   A  1  126  ? -7.896  59.901  55.413  1.00 45.48 ? 124  LYS   A C     1 
ATOM   793   O  O     . LYS   A  1  126  ? -6.887  59.711  56.098  1.00 48.80 ? 124  LYS   A O     1 
ATOM   794   C  CB    . LYS   A  1  126  ? -8.457  62.124  54.379  1.00 49.23 ? 124  LYS   A CB    1 
ATOM   795   N  N     . ILE   A  1  127  ? -9.084  59.394  55.744  1.00 40.87 ? 125  ILE   A N     1 
ATOM   796   C  CA    . ILE   A  1  127  ? -9.234  58.606  56.969  1.00 39.96 ? 125  ILE   A CA    1 
ATOM   797   C  C     . ILE   A  1  127  ? -8.463  57.297  56.855  1.00 43.50 ? 125  ILE   A C     1 
ATOM   798   O  O     . ILE   A  1  127  ? -7.633  56.964  57.708  1.00 46.81 ? 125  ILE   A O     1 
ATOM   799   C  CB    . ILE   A  1  127  ? -10.717 58.355  57.289  1.00 38.67 ? 125  ILE   A CB    1 
ATOM   800   C  CG1   . ILE   A  1  127  ? -11.513 59.661  57.273  1.00 43.28 ? 125  ILE   A CG1   1 
ATOM   801   C  CG2   . ILE   A  1  127  ? -10.854 57.684  58.653  1.00 38.16 ? 125  ILE   A CG2   1 
ATOM   802   C  CD1   . ILE   A  1  127  ? -11.005 60.689  58.243  1.00 39.32 ? 125  ILE   A CD1   1 
ATOM   803   N  N     . ALA   A  1  128  ? -8.730  56.535  55.792  1.00 42.21 ? 126  ALA   A N     1 
ATOM   804   C  CA    . ALA   A  1  128  ? -8.127  55.213  55.663  1.00 37.13 ? 126  ALA   A CA    1 
ATOM   805   C  C     . ALA   A  1  128  ? -6.619  55.305  55.498  1.00 48.24 ? 126  ALA   A C     1 
ATOM   806   O  O     . ALA   A  1  128  ? -5.880  54.468  56.029  1.00 43.09 ? 126  ALA   A O     1 
ATOM   807   C  CB    . ALA   A  1  128  ? -8.748  54.465  54.485  1.00 38.39 ? 126  ALA   A CB    1 
ATOM   808   N  N     . ASP   A  1  129  ? -6.144  56.320  54.776  1.00 63.08 ? 127  ASP   A N     1 
ATOM   809   C  CA    . ASP   A  1  129  ? -4.737  56.434  54.413  1.00 61.85 ? 127  ASP   A CA    1 
ATOM   810   C  C     . ASP   A  1  129  ? -3.848  56.897  55.560  1.00 62.15 ? 127  ASP   A C     1 
ATOM   811   O  O     . ASP   A  1  129  ? -2.630  56.991  55.373  1.00 67.84 ? 127  ASP   A O     1 
ATOM   812   C  CB    . ASP   A  1  129  ? -4.569  57.362  53.205  1.00 60.83 ? 127  ASP   A CB    1 
ATOM   813   N  N     . GLY   A  1  130  ? -4.407  57.191  56.730  1.00 57.98 ? 128  GLY   A N     1 
ATOM   814   C  CA    . GLY   A  1  130  ? -3.562  57.518  57.859  1.00 61.05 ? 128  GLY   A CA    1 
ATOM   815   C  C     . GLY   A  1  130  ? -4.222  58.292  58.980  1.00 59.13 ? 128  GLY   A C     1 
ATOM   816   O  O     . GLY   A  1  130  ? -5.078  57.764  59.697  1.00 55.00 ? 128  GLY   A O     1 
ATOM   817   N  N     . ASN   A  1  131  ? -3.822  59.552  59.135  1.00 62.82 ? 129  ASN   A N     1 
ATOM   818   C  CA    . ASN   A  1  131  ? -4.158  60.347  60.314  1.00 59.96 ? 129  ASN   A CA    1 
ATOM   819   C  C     . ASN   A  1  131  ? -5.629  60.744  60.274  1.00 51.76 ? 129  ASN   A C     1 
ATOM   820   O  O     . ASN   A  1  131  ? -6.004  61.728  59.633  1.00 55.97 ? 129  ASN   A O     1 
ATOM   821   C  CB    . ASN   A  1  131  ? -3.257  61.576  60.381  1.00 59.30 ? 129  ASN   A CB    1 
ATOM   822   N  N     . TRP   A  1  132  ? -6.471  59.976  60.971  1.00 50.06 ? 130  TRP   A N     1 
ATOM   823   C  CA    . TRP   A  1  132  ? -7.864  60.376  61.153  1.00 43.00 ? 130  TRP   A CA    1 
ATOM   824   C  C     . TRP   A  1  132  ? -7.977  61.611  62.035  1.00 41.56 ? 130  TRP   A C     1 
ATOM   825   O  O     . TRP   A  1  132  ? -8.961  62.356  61.937  1.00 44.80 ? 130  TRP   A O     1 
ATOM   826   C  CB    . TRP   A  1  132  ? -8.655  59.231  61.784  1.00 39.14 ? 130  TRP   A CB    1 
ATOM   827   C  CG    . TRP   A  1  132  ? -8.082  58.772  63.101  1.00 35.92 ? 130  TRP   A CG    1 
ATOM   828   C  CD1   . TRP   A  1  132  ? -7.176  57.770  63.291  1.00 31.62 ? 130  TRP   A CD1   1 
ATOM   829   C  CD2   . TRP   A  1  132  ? -8.374  59.300  64.405  1.00 28.95 ? 130  TRP   A CD2   1 
ATOM   830   N  NE1   . TRP   A  1  132  ? -6.889  57.636  64.630  1.00 31.30 ? 130  TRP   A NE1   1 
ATOM   831   C  CE2   . TRP   A  1  132  ? -7.607  58.565  65.336  1.00 24.23 ? 130  TRP   A CE2   1 
ATOM   832   C  CE3   . TRP   A  1  132  ? -9.203  60.322  64.875  1.00 30.35 ? 130  TRP   A CE3   1 
ATOM   833   C  CZ2   . TRP   A  1  132  ? -7.648  58.821  66.707  1.00 24.84 ? 130  TRP   A CZ2   1 
ATOM   834   C  CZ3   . TRP   A  1  132  ? -9.248  60.572  66.232  1.00 29.44 ? 130  TRP   A CZ3   1 
ATOM   835   C  CH2   . TRP   A  1  132  ? -8.475  59.824  67.135  1.00 27.75 ? 130  TRP   A CH2   1 
ATOM   836   N  N     . LYS   A  1  133  ? -6.990  61.831  62.908  1.00 43.89 ? 131  LYS   A N     1 
ATOM   837   C  CA    . LYS   A  1  133  ? -7.024  62.986  63.798  1.00 46.58 ? 131  LYS   A CA    1 
ATOM   838   C  C     . LYS   A  1  133  ? -7.011  64.288  63.011  1.00 54.35 ? 131  LYS   A C     1 
ATOM   839   O  O     . LYS   A  1  133  ? -7.683  65.256  63.389  1.00 59.02 ? 131  LYS   A O     1 
ATOM   840   C  CB    . LYS   A  1  133  ? -5.846  62.930  64.769  1.00 38.54 ? 131  LYS   A CB    1 
ATOM   841   N  N     . SER   A  1  134  ? -6.264  64.325  61.902  1.00 56.75 ? 132  SER   A N     1 
ATOM   842   C  CA    . SER   A  1  134  ? -6.182  65.527  61.078  1.00 60.67 ? 132  SER   A CA    1 
ATOM   843   C  C     . SER   A  1  134  ? -7.552  66.026  60.635  1.00 64.43 ? 132  SER   A C     1 
ATOM   844   O  O     . SER   A  1  134  ? -7.701  67.218  60.346  1.00 66.94 ? 132  SER   A O     1 
ATOM   845   C  CB    . SER   A  1  134  ? -5.294  65.266  59.860  1.00 61.76 ? 132  SER   A CB    1 
ATOM   846   N  N     . HIS   A  1  135  ? -8.549  65.149  60.585  1.00 64.33 ? 133  HIS   A N     1 
ATOM   847   C  CA    . HIS   A  1  135  ? -9.900  65.533  60.200  1.00 65.94 ? 133  HIS   A CA    1 
ATOM   848   C  C     . HIS   A  1  135  ? -10.889 65.021  61.244  1.00 63.46 ? 133  HIS   A C     1 
ATOM   849   O  O     . HIS   A  1  135  ? -12.013 65.514  61.350  1.00 66.40 ? 133  HIS   A O     1 
ATOM   850   C  CB    . HIS   A  1  135  ? -10.244 64.960  58.824  1.00 61.91 ? 133  HIS   A CB    1 
ATOM   851   C  CG    . HIS   A  1  135  ? -9.054  64.765  57.934  1.00 65.44 ? 133  HIS   A CG    1 
ATOM   852   N  ND1   . HIS   A  1  135  ? -8.154  63.737  58.111  1.00 66.41 ? 133  HIS   A ND1   1 
ATOM   853   C  CD2   . HIS   A  1  135  ? -8.618  65.466  56.860  1.00 66.88 ? 133  HIS   A CD2   1 
ATOM   854   C  CE1   . HIS   A  1  135  ? -7.212  63.813  57.187  1.00 65.53 ? 133  HIS   A CE1   1 
ATOM   855   N  NE2   . HIS   A  1  135  ? -7.472  64.853  56.414  1.00 63.61 ? 133  HIS   A NE2   1 
ATOM   856   N  N     . SER   A  1  139  ? -12.577 70.350  67.313  1.00 45.97 ? 137  SER   A N     1 
ATOM   857   C  CA    . SER   A  1  139  ? -13.366 71.147  68.254  1.00 50.55 ? 137  SER   A CA    1 
ATOM   858   C  C     . SER   A  1  139  ? -14.304 70.273  69.089  1.00 52.28 ? 137  SER   A C     1 
ATOM   859   O  O     . SER   A  1  139  ? -14.995 70.758  69.988  1.00 49.67 ? 137  SER   A O     1 
ATOM   860   C  CB    . SER   A  1  139  ? -14.169 72.216  67.510  1.00 49.27 ? 137  SER   A CB    1 
ATOM   861   N  N     . ARG   A  1  140  ? -14.322 68.980  68.778  1.00 37.42 ? 138  ARG   A N     1 
ATOM   862   C  CA    . ARG   A  1  140  ? -15.166 68.020  69.479  1.00 35.22 ? 138  ARG   A CA    1 
ATOM   863   C  C     . ARG   A  1  140  ? -14.501 66.660  69.359  1.00 33.24 ? 138  ARG   A C     1 
ATOM   864   O  O     . ARG   A  1  140  ? -14.242 66.196  68.243  1.00 31.47 ? 138  ARG   A O     1 
ATOM   865   C  CB    . ARG   A  1  140  ? -16.568 67.992  68.861  1.00 36.37 ? 138  ARG   A CB    1 
ATOM   866   C  CG    . ARG   A  1  140  ? -17.429 66.781  69.204  1.00 37.80 ? 138  ARG   A CG    1 
ATOM   867   C  CD    . ARG   A  1  140  ? -18.603 66.683  68.227  1.00 44.10 ? 138  ARG   A CD    1 
ATOM   868   N  NE    . ARG   A  1  140  ? -19.504 65.564  68.487  1.00 46.67 ? 138  ARG   A NE    1 
ATOM   869   C  CZ    . ARG   A  1  140  ? -19.339 64.337  68.007  1.00 50.09 ? 138  ARG   A CZ    1 
ATOM   870   N  NH1   . ARG   A  1  140  ? -18.265 64.005  67.305  1.00 45.21 ? 138  ARG   A NH1   1 
ATOM   871   N  NH2   . ARG   A  1  140  ? -20.276 63.420  68.235  1.00 43.49 ? 138  ARG   A NH2   1 
ATOM   872   N  N     . SER   A  1  141  ? -14.202 66.042  70.502  1.00 29.77 ? 139  SER   A N     1 
ATOM   873   C  CA    . SER   A  1  141  ? -13.650 64.698  70.504  1.00 26.37 ? 139  SER   A CA    1 
ATOM   874   C  C     . SER   A  1  141  ? -14.528 63.770  69.678  1.00 25.20 ? 139  SER   A C     1 
ATOM   875   O  O     . SER   A  1  141  ? -15.756 63.847  69.711  1.00 24.93 ? 139  SER   A O     1 
ATOM   876   C  CB    . SER   A  1  141  ? -13.579 64.176  71.940  1.00 26.86 ? 139  SER   A CB    1 
ATOM   877   O  OG    . SER   A  1  141  ? -13.155 62.820  71.968  1.00 24.18 ? 139  SER   A OG    1 
ATOM   878   N  N     . LEU   A  1  142  ? -13.886 62.888  68.917  1.00 23.88 ? 140  LEU   A N     1 
ATOM   879   C  CA    . LEU   A  1  142  ? -14.640 61.856  68.223  1.00 22.01 ? 140  LEU   A CA    1 
ATOM   880   C  C     . LEU   A  1  142  ? -15.410 60.972  69.194  1.00 19.73 ? 140  LEU   A C     1 
ATOM   881   O  O     . LEU   A  1  142  ? -16.385 60.321  68.802  1.00 20.48 ? 140  LEU   A O     1 
ATOM   882   C  CB    . LEU   A  1  142  ? -13.646 60.983  67.458  1.00 21.96 ? 140  LEU   A CB    1 
ATOM   883   C  CG    . LEU   A  1  142  ? -13.947 60.650  66.010  1.00 30.42 ? 140  LEU   A CG    1 
ATOM   884   C  CD1   . LEU   A  1  142  ? -13.802 61.885  65.139  1.00 30.84 ? 140  LEU   A CD1   1 
ATOM   885   C  CD2   . LEU   A  1  142  ? -12.975 59.583  65.584  1.00 29.25 ? 140  LEU   A CD2   1 
ATOM   886   N  N     . PHE   A  1  143  ? -15.011 60.968  70.462  1.00 18.55 ? 141  PHE   A N     1 
ATOM   887   C  CA    . PHE   A  1  143  ? -15.430 59.956  71.413  1.00 17.35 ? 141  PHE   A CA    1 
ATOM   888   C  C     . PHE   A  1  143  ? -16.442 60.480  72.422  1.00 19.76 ? 141  PHE   A C     1 
ATOM   889   O  O     . PHE   A  1  143  ? -16.667 59.831  73.439  1.00 19.85 ? 141  PHE   A O     1 
ATOM   890   C  CB    . PHE   A  1  143  ? -14.189 59.372  72.093  1.00 17.27 ? 141  PHE   A CB    1 
ATOM   891   C  CG    . PHE   A  1  143  ? -13.183 58.876  71.103  1.00 17.77 ? 141  PHE   A CG    1 
ATOM   892   C  CD1   . PHE   A  1  143  ? -13.541 57.881  70.210  1.00 17.48 ? 141  PHE   A CD1   1 
ATOM   893   C  CD2   . PHE   A  1  143  ? -11.915 59.432  71.016  1.00 17.50 ? 141  PHE   A CD2   1 
ATOM   894   C  CE1   . PHE   A  1  143  ? -12.664 57.423  69.266  1.00 18.32 ? 141  PHE   A CE1   1 
ATOM   895   C  CE2   . PHE   A  1  143  ? -11.021 58.971  70.067  1.00 19.88 ? 141  PHE   A CE2   1 
ATOM   896   C  CZ    . PHE   A  1  143  ? -11.390 57.970  69.190  1.00 17.38 ? 141  PHE   A CZ    1 
ATOM   897   N  N     . VAL   A  1  144  ? -17.079 61.620  72.130  1.00 19.25 ? 142  VAL   A N     1 
ATOM   898   C  CA    A VAL   A  1  144  ? -17.995 62.227  73.095  0.47 21.82 ? 142  VAL   A CA    1 
ATOM   899   C  CA    B VAL   A  1  144  ? -18.016 62.238  73.072  0.53 21.83 ? 142  VAL   A CA    1 
ATOM   900   C  C     . VAL   A  1  144  ? -19.101 61.259  73.499  1.00 22.38 ? 142  VAL   A C     1 
ATOM   901   O  O     . VAL   A  1  144  ? -19.523 61.238  74.662  1.00 22.02 ? 142  VAL   A O     1 
ATOM   902   C  CB    A VAL   A  1  144  ? -18.545 63.570  72.574  0.47 22.74 ? 142  VAL   A CB    1 
ATOM   903   C  CB    B VAL   A  1  144  ? -18.609 63.526  72.466  0.53 22.68 ? 142  VAL   A CB    1 
ATOM   904   C  CG1   A VAL   A  1  144  ? -17.419 64.573  72.411  0.47 24.25 ? 142  VAL   A CG1   1 
ATOM   905   C  CG1   B VAL   A  1  144  ? -19.760 64.048  73.321  0.53 20.86 ? 142  VAL   A CG1   1 
ATOM   906   C  CG2   A VAL   A  1  144  ? -19.293 63.379  71.272  0.47 23.61 ? 142  VAL   A CG2   1 
ATOM   907   C  CG2   B VAL   A  1  144  ? -17.530 64.583  72.335  0.53 24.27 ? 142  VAL   A CG2   1 
ATOM   908   N  N     . ASN   A  1  145  ? -19.583 60.440  72.565  1.00 19.77 ? 143  ASN   A N     1 
ATOM   909   C  CA    . ASN   A  1  145  ? -20.649 59.491  72.855  1.00 22.32 ? 143  ASN   A CA    1 
ATOM   910   C  C     . ASN   A  1  145  ? -20.143 58.066  73.032  1.00 21.79 ? 143  ASN   A C     1 
ATOM   911   O  O     . ASN   A  1  145  ? -20.924 57.118  72.911  1.00 20.02 ? 143  ASN   A O     1 
ATOM   912   C  CB    . ASN   A  1  145  ? -21.726 59.555  71.771  1.00 25.12 ? 143  ASN   A CB    1 
ATOM   913   C  CG    . ASN   A  1  145  ? -22.489 60.855  71.802  1.00 24.59 ? 143  ASN   A CG    1 
ATOM   914   O  OD1   . ASN   A  1  145  ? -22.963 61.276  72.853  1.00 30.22 ? 143  ASN   A OD1   1 
ATOM   915   N  ND2   . ASN   A  1  145  ? -22.589 61.513  70.658  1.00 27.98 ? 143  ASN   A ND2   1 
ATOM   916   N  N     . ALA   A  1  146  ? -18.855 57.896  73.337  1.00 17.44 ? 144  ALA   A N     1 
ATOM   917   C  CA    . ALA   A  1  146  ? -18.308 56.549  73.454  1.00 18.48 ? 144  ALA   A CA    1 
ATOM   918   C  C     . ALA   A  1  146  ? -18.942 55.747  74.587  1.00 18.31 ? 144  ALA   A C     1 
ATOM   919   O  O     . ALA   A  1  146  ? -18.972 54.515  74.519  1.00 22.27 ? 144  ALA   A O     1 
ATOM   920   C  CB    . ALA   A  1  146  ? -16.787 56.604  73.612  1.00 17.33 ? 144  ALA   A CB    1 
ATOM   921   N  N     . ALA   A  1  147  ? -19.427 56.399  75.650  1.00 21.27 ? 145  ALA   A N     1 
ATOM   922   C  CA    . ALA   A  1  147  ? -20.108 55.633  76.693  1.00 24.48 ? 145  ALA   A CA    1 
ATOM   923   C  C     . ALA   A  1  147  ? -21.313 54.901  76.125  1.00 23.65 ? 145  ALA   A C     1 
ATOM   924   O  O     . ALA   A  1  147  ? -21.558 53.734  76.452  1.00 23.86 ? 145  ALA   A O     1 
ATOM   925   C  CB    . ALA   A  1  147  ? -20.524 56.542  77.850  1.00 26.90 ? 145  ALA   A CB    1 
ATOM   926   N  N     . THR   A  1  148  ? -22.060 55.565  75.247  1.00 21.01 ? 146  THR   A N     1 
ATOM   927   C  CA    . THR   A  1  148  ? -23.206 54.934  74.611  1.00 20.83 ? 146  THR   A CA    1 
ATOM   928   C  C     . THR   A  1  148  ? -22.761 53.802  73.698  1.00 20.62 ? 146  THR   A C     1 
ATOM   929   O  O     . THR   A  1  148  ? -23.292 52.689  73.764  1.00 20.52 ? 146  THR   A O     1 
ATOM   930   C  CB    . THR   A  1  148  ? -23.977 55.994  73.829  1.00 25.04 ? 146  THR   A CB    1 
ATOM   931   O  OG1   . THR   A  1  148  ? -24.409 57.010  74.738  1.00 27.45 ? 146  THR   A OG1   1 
ATOM   932   C  CG2   . THR   A  1  148  ? -25.182 55.387  73.122  1.00 31.04 ? 146  THR   A CG2   1 
ATOM   933   N  N     . TRP   A  1  149  ? -21.776 54.066  72.835  1.00 18.70 ? 147  TRP   A N     1 
ATOM   934   C  CA    . TRP   A  1  149  ? -21.269 52.996  71.984  1.00 20.48 ? 147  TRP   A CA    1 
ATOM   935   C  C     . TRP   A  1  149  ? -20.662 51.867  72.800  1.00 19.09 ? 147  TRP   A C     1 
ATOM   936   O  O     . TRP   A  1  149  ? -20.745 50.706  72.393  1.00 19.55 ? 147  TRP   A O     1 
ATOM   937   C  CB    . TRP   A  1  149  ? -20.270 53.538  70.961  1.00 21.70 ? 147  TRP   A CB    1 
ATOM   938   C  CG    . TRP   A  1  149  ? -20.937 54.399  69.950  1.00 19.95 ? 147  TRP   A CG    1 
ATOM   939   C  CD1   . TRP   A  1  149  ? -20.743 55.730  69.756  1.00 24.57 ? 147  TRP   A CD1   1 
ATOM   940   C  CD2   . TRP   A  1  149  ? -21.944 53.997  69.015  1.00 22.41 ? 147  TRP   A CD2   1 
ATOM   941   N  NE1   . TRP   A  1  149  ? -21.553 56.185  68.743  1.00 23.25 ? 147  TRP   A NE1   1 
ATOM   942   C  CE2   . TRP   A  1  149  ? -22.296 55.136  68.269  1.00 23.03 ? 147  TRP   A CE2   1 
ATOM   943   C  CE3   . TRP   A  1  149  ? -22.560 52.776  68.718  1.00 23.04 ? 147  TRP   A CE3   1 
ATOM   944   C  CZ2   . TRP   A  1  149  ? -23.253 55.098  67.255  1.00 24.29 ? 147  TRP   A CZ2   1 
ATOM   945   C  CZ3   . TRP   A  1  149  ? -23.511 52.739  67.712  1.00 26.22 ? 147  TRP   A CZ3   1 
ATOM   946   C  CH2   . TRP   A  1  149  ? -23.845 53.891  66.992  1.00 27.51 ? 147  TRP   A CH2   1 
ATOM   947   N  N     . GLY   A  1  150  ? -20.042 52.177  73.944  1.00 18.25 ? 148  GLY   A N     1 
ATOM   948   C  CA    . GLY   A  1  150  ? -19.554 51.115  74.807  1.00 20.25 ? 148  GLY   A CA    1 
ATOM   949   C  C     . GLY   A  1  150  ? -20.676 50.214  75.277  1.00 21.71 ? 148  GLY   A C     1 
ATOM   950   O  O     . GLY   A  1  150  ? -20.521 48.991  75.351  1.00 23.09 ? 148  GLY   A O     1 
ATOM   951   N  N     . LEU   A  1  151  ? -21.832 50.806  75.582  1.00 21.91 ? 149  LEU   A N     1 
ATOM   952   C  CA    . LEU   A  1  151  ? -22.988 49.999  75.945  1.00 23.58 ? 149  LEU   A CA    1 
ATOM   953   C  C     . LEU   A  1  151  ? -23.418 49.114  74.782  1.00 23.16 ? 149  LEU   A C     1 
ATOM   954   O  O     . LEU   A  1  151  ? -23.691 47.925  74.966  1.00 27.25 ? 149  LEU   A O     1 
ATOM   955   C  CB    . LEU   A  1  151  ? -24.121 50.916  76.404  1.00 25.81 ? 149  LEU   A CB    1 
ATOM   956   C  CG    . LEU   A  1  151  ? -25.241 50.335  77.252  1.00 31.33 ? 149  LEU   A CG    1 
ATOM   957   C  CD1   . LEU   A  1  151  ? -24.684 49.598  78.461  1.00 30.94 ? 149  LEU   A CD1   1 
ATOM   958   C  CD2   . LEU   A  1  151  ? -26.113 51.485  77.703  1.00 34.91 ? 149  LEU   A CD2   1 
ATOM   959   N  N     . VAL   A  1  152  ? -23.448 49.669  73.569  1.00 21.02 ? 150  VAL   A N     1 
ATOM   960   C  CA    . VAL   A  1  152  ? -23.805 48.885  72.384  1.00 23.67 ? 150  VAL   A CA    1 
ATOM   961   C  C     . VAL   A  1  152  ? -22.828 47.732  72.174  1.00 26.33 ? 150  VAL   A C     1 
ATOM   962   O  O     . VAL   A  1  152  ? -23.229 46.590  71.919  1.00 26.29 ? 150  VAL   A O     1 
ATOM   963   C  CB    . VAL   A  1  152  ? -23.878 49.799  71.148  1.00 23.98 ? 150  VAL   A CB    1 
ATOM   964   C  CG1   . VAL   A  1  152  ? -24.003 48.972  69.876  1.00 27.81 ? 150  VAL   A CG1   1 
ATOM   965   C  CG2   . VAL   A  1  152  ? -25.026 50.783  71.287  1.00 26.01 ? 150  VAL   A CG2   1 
ATOM   966   N  N     . VAL   A  1  153  ? -21.531 48.018  72.262  1.00 22.78 ? 151  VAL   A N     1 
ATOM   967   C  CA    . VAL   A  1  153  ? -20.518 47.033  71.907  1.00 24.43 ? 151  VAL   A CA    1 
ATOM   968   C  C     . VAL   A  1  153  ? -20.333 46.004  73.015  1.00 25.02 ? 151  VAL   A C     1 
ATOM   969   O  O     . VAL   A  1  153  ? -20.263 44.797  72.750  1.00 27.74 ? 151  VAL   A O     1 
ATOM   970   C  CB    . VAL   A  1  153  ? -19.199 47.748  71.562  1.00 22.33 ? 151  VAL   A CB    1 
ATOM   971   C  CG1   . VAL   A  1  153  ? -18.089 46.738  71.351  1.00 24.34 ? 151  VAL   A CG1   1 
ATOM   972   C  CG2   . VAL   A  1  153  ? -19.380 48.600  70.326  1.00 22.33 ? 151  VAL   A CG2   1 
ATOM   973   N  N     . THR   A  1  154  ? -20.226 46.462  74.262  1.00 24.57 ? 152  THR   A N     1 
ATOM   974   C  CA    . THR   A  1  154  ? -19.813 45.614  75.371  1.00 25.99 ? 152  THR   A CA    1 
ATOM   975   C  C     . THR   A  1  154  ? -20.939 45.274  76.332  1.00 29.66 ? 152  THR   A C     1 
ATOM   976   O  O     . THR   A  1  154  ? -20.753 44.401  77.184  1.00 29.05 ? 152  THR   A O     1 
ATOM   977   C  CB    . THR   A  1  154  ? -18.686 46.281  76.179  1.00 26.63 ? 152  THR   A CB    1 
ATOM   978   O  OG1   . THR   A  1  154  ? -19.210 47.386  76.931  1.00 28.73 ? 152  THR   A OG1   1 
ATOM   979   C  CG2   . THR   A  1  154  ? -17.575 46.776  75.268  1.00 29.33 ? 152  THR   A CG2   1 
ATOM   980   N  N     . GLY   A  1  155  ? -22.083 45.943  76.242  1.00 27.67 ? 153  GLY   A N     1 
ATOM   981   C  CA    . GLY   A  1  155  ? -23.128 45.747  77.225  1.00 27.10 ? 153  GLY   A CA    1 
ATOM   982   C  C     . GLY   A  1  155  ? -22.873 46.387  78.573  1.00 30.44 ? 153  GLY   A C     1 
ATOM   983   O  O     . GLY   A  1  155  ? -23.726 46.272  79.462  1.00 31.19 ? 153  GLY   A O     1 
ATOM   984   N  N     . LYS   A  1  156  ? -21.738 47.053  78.760  1.00 27.26 ? 154  LYS   A N     1 
ATOM   985   C  CA    . LYS   A  1  156  ? -21.386 47.686  80.020  1.00 31.84 ? 154  LYS   A CA    1 
ATOM   986   C  C     . LYS   A  1  156  ? -21.369 49.198  79.852  1.00 32.57 ? 154  LYS   A C     1 
ATOM   987   O  O     . LYS   A  1  156  ? -20.984 49.716  78.798  1.00 26.74 ? 154  LYS   A O     1 
ATOM   988   C  CB    . LYS   A  1  156  ? -20.013 47.212  80.508  1.00 33.47 ? 154  LYS   A CB    1 
ATOM   989   N  N     . LEU   A  1  157  ? -21.790 49.901  80.894  1.00 30.88 ? 155  LEU   A N     1 
ATOM   990   C  CA    . LEU   A  1  157  ? -21.803 51.354  80.897  1.00 32.12 ? 155  LEU   A CA    1 
ATOM   991   C  C     . LEU   A  1  157  ? -20.597 51.864  81.672  1.00 37.47 ? 155  LEU   A C     1 
ATOM   992   O  O     . LEU   A  1  157  ? -20.343 51.426  82.799  1.00 38.58 ? 155  LEU   A O     1 
ATOM   993   C  CB    . LEU   A  1  157  ? -23.083 51.872  81.549  1.00 32.89 ? 155  LEU   A CB    1 
ATOM   994   C  CG    . LEU   A  1  157  ? -23.282 53.384  81.502  1.00 37.85 ? 155  LEU   A CG    1 
ATOM   995   C  CD1   . LEU   A  1  157  ? -23.403 53.858  80.060  1.00 35.62 ? 155  LEU   A CD1   1 
ATOM   996   C  CD2   . LEU   A  1  157  ? -24.522 53.755  82.302  1.00 42.92 ? 155  LEU   A CD2   1 
ATOM   997   N  N     . THR   A  1  158  ? -19.848 52.770  81.057  1.00 43.38 ? 156  THR   A N     1 
ATOM   998   C  CA    . THR   A  1  158  ? -18.830 53.551  81.740  1.00 43.41 ? 156  THR   A CA    1 
ATOM   999   C  C     . THR   A  1  158  ? -19.288 55.001  81.753  1.00 44.54 ? 156  THR   A C     1 
ATOM   1000  O  O     . THR   A  1  158  ? -19.816 55.501  80.756  1.00 51.76 ? 156  THR   A O     1 
ATOM   1001  C  CB    . THR   A  1  158  ? -17.481 53.433  81.026  1.00 41.97 ? 156  THR   A CB    1 
ATOM   1002  N  N     . SER   A  1  159  ? -19.112 55.671  82.891  1.00 32.77 ? 157  SER   A N     1 
ATOM   1003  C  CA    . SER   A  1  159  ? -19.624 57.030  83.019  1.00 29.64 ? 157  SER   A CA    1 
ATOM   1004  C  C     . SER   A  1  159  ? -18.786 58.021  82.217  1.00 32.20 ? 157  SER   A C     1 
ATOM   1005  O  O     . SER   A  1  159  ? -19.316 58.983  81.652  1.00 35.35 ? 157  SER   A O     1 
ATOM   1006  C  CB    . SER   A  1  159  ? -19.687 57.423  84.495  1.00 36.70 ? 157  SER   A CB    1 
ATOM   1007  O  OG    . SER   A  1  159  ? -18.789 56.639  85.265  1.00 40.89 ? 157  SER   A OG    1 
ATOM   1008  N  N     . THR   A  1  160  ? -17.484 57.809  82.160  1.00 28.45 ? 158  THR   A N     1 
ATOM   1009  C  CA    . THR   A  1  160  ? -16.599 58.648  81.376  1.00 25.43 ? 158  THR   A CA    1 
ATOM   1010  C  C     . THR   A  1  160  ? -15.864 57.783  80.364  1.00 21.88 ? 158  THR   A C     1 
ATOM   1011  O  O     . THR   A  1  160  ? -15.879 56.554  80.429  1.00 26.62 ? 158  THR   A O     1 
ATOM   1012  C  CB    . THR   A  1  160  ? -15.590 59.374  82.269  1.00 26.05 ? 158  THR   A CB    1 
ATOM   1013  O  OG1   . THR   A  1  160  ? -14.789 58.403  82.949  1.00 28.95 ? 158  THR   A OG1   1 
ATOM   1014  C  CG2   . THR   A  1  160  ? -16.305 60.252  83.279  1.00 31.67 ? 158  THR   A CG2   1 
ATOM   1015  N  N     . VAL   A  1  161  ? -15.202 58.463  79.437  1.00 18.10 ? 159  VAL   A N     1 
ATOM   1016  C  CA    . VAL   A  1  161  ? -14.647 57.868  78.231  1.00 18.63 ? 159  VAL   A CA    1 
ATOM   1017  C  C     . VAL   A  1  161  ? -13.133 57.919  78.338  1.00 17.67 ? 159  VAL   A C     1 
ATOM   1018  O  O     . VAL   A  1  161  ? -12.563 58.988  78.567  1.00 17.70 ? 159  VAL   A O     1 
ATOM   1019  C  CB    . VAL   A  1  161  ? -15.115 58.678  77.011  1.00 21.53 ? 159  VAL   A CB    1 
ATOM   1020  C  CG1   . VAL   A  1  161  ? -14.373 58.291  75.766  1.00 22.30 ? 159  VAL   A CG1   1 
ATOM   1021  C  CG2   . VAL   A  1  161  ? -16.638 58.551  76.847  1.00 24.43 ? 159  VAL   A CG2   1 
ATOM   1022  N  N     . ASN   A  1  162  ? -12.478 56.775  78.153  1.00 15.44 ? 160  ASN   A N     1 
ATOM   1023  C  CA    . ASN   A  1  162  ? -11.018 56.800  78.076  1.00 17.34 ? 160  ASN   A CA    1 
ATOM   1024  C  C     . ASN   A  1  162  ? -10.667 57.139  76.635  1.00 14.16 ? 160  ASN   A C     1 
ATOM   1025  O  O     . ASN   A  1  162  ? -10.479 56.267  75.779  1.00 16.09 ? 160  ASN   A O     1 
ATOM   1026  C  CB    . ASN   A  1  162  ? -10.410 55.481  78.527  1.00 18.37 ? 160  ASN   A CB    1 
ATOM   1027  C  CG    . ASN   A  1  162  ? -8.892  55.552  78.587  1.00 18.35 ? 160  ASN   A CG    1 
ATOM   1028  O  OD1   . ASN   A  1  162  ? -8.277  56.370  77.906  1.00 19.01 ? 160  ASN   A OD1   1 
ATOM   1029  N  ND2   . ASN   A  1  162  ? -8.294  54.715  79.411  1.00 21.43 ? 160  ASN   A ND2   1 
ATOM   1030  N  N     . ASP   A  1  163  ? -10.583 58.442  76.365  1.00 14.52 ? 161  ASP   A N     1 
ATOM   1031  C  CA    . ASP   A  1  163  ? -10.403 58.904  74.995  1.00 15.75 ? 161  ASP   A CA    1 
ATOM   1032  C  C     . ASP   A  1  163  ? -9.015  58.595  74.459  1.00 14.96 ? 161  ASP   A C     1 
ATOM   1033  O  O     . ASP   A  1  163  ? -8.845  58.448  73.251  1.00 16.07 ? 161  ASP   A O     1 
ATOM   1034  C  CB    . ASP   A  1  163  ? -10.747 60.393  74.844  1.00 17.65 ? 161  ASP   A CB    1 
ATOM   1035  C  CG    . ASP   A  1  163  ? -10.106 61.287  75.892  1.00 21.76 ? 161  ASP   A CG    1 
ATOM   1036  O  OD1   . ASP   A  1  163  ? -9.985  60.899  77.073  1.00 19.43 ? 161  ASP   A OD1   1 
ATOM   1037  O  OD2   . ASP   A  1  163  ? -9.769  62.428  75.515  1.00 23.69 ? 161  ASP   A OD2   1 
ATOM   1038  N  N     . ARG   A  1  164  ? -8.021  58.469  75.332  1.00 15.57 ? 162  ARG   A N     1 
ATOM   1039  C  CA    . ARG   A  1  164  ? -6.705  58.097  74.841  1.00 14.79 ? 162  ARG   A CA    1 
ATOM   1040  C  C     . ARG   A  1  164  ? -6.662  56.629  74.439  1.00 15.74 ? 162  ARG   A C     1 
ATOM   1041  O  O     . ARG   A  1  164  ? -6.005  56.278  73.453  1.00 15.53 ? 162  ARG   A O     1 
ATOM   1042  C  CB    . ARG   A  1  164  ? -5.645  58.433  75.885  1.00 17.17 ? 162  ARG   A CB    1 
ATOM   1043  C  CG    . ARG   A  1  164  ? -5.519  59.925  76.178  1.00 19.92 ? 162  ARG   A CG    1 
ATOM   1044  C  CD    . ARG   A  1  164  ? -5.617  60.780  74.924  1.00 27.01 ? 162  ARG   A CD    1 
ATOM   1045  N  NE    . ARG   A  1  164  ? -4.644  60.435  73.895  1.00 28.59 ? 162  ARG   A NE    1 
ATOM   1046  C  CZ    . ARG   A  1  164  ? -4.808  60.692  72.601  1.00 32.99 ? 162  ARG   A CZ    1 
ATOM   1047  N  NH1   . ARG   A  1  164  ? -5.904  61.281  72.145  1.00 33.85 ? 162  ARG   A NH1   1 
ATOM   1048  N  NH2   . ARG   A  1  164  ? -3.852  60.343  71.743  1.00 31.76 ? 162  ARG   A NH2   1 
ATOM   1049  N  N     . SER   A  1  165  ? -7.356  55.768  75.188  1.00 15.24 ? 163  SER   A N     1 
ATOM   1050  C  CA    . SER   A  1  165  ? -7.465  54.362  74.801  1.00 14.49 ? 163  SER   A CA    1 
ATOM   1051  C  C     . SER   A  1  165  ? -8.226  54.213  73.495  1.00 15.09 ? 163  SER   A C     1 
ATOM   1052  O  O     . SER   A  1  165  ? -7.830  53.437  72.615  1.00 14.81 ? 163  SER   A O     1 
ATOM   1053  C  CB    . SER   A  1  165  ? -8.148  53.567  75.914  1.00 16.23 ? 163  SER   A CB    1 
ATOM   1054  O  OG    . SER   A  1  165  ? -8.507  52.269  75.469  1.00 17.62 ? 163  SER   A OG    1 
ATOM   1055  N  N     . LEU   A  1  166  ? -9.320  54.961  73.345  1.00 14.78 ? 164  LEU   A N     1 
ATOM   1056  C  CA    . LEU   A  1  166  ? -10.075 54.916  72.103  1.00 16.27 ? 164  LEU   A CA    1 
ATOM   1057  C  C     . LEU   A  1  166  ? -9.269  55.467  70.937  1.00 14.52 ? 164  LEU   A C     1 
ATOM   1058  O  O     . LEU   A  1  166  ? -9.331  54.924  69.828  1.00 15.24 ? 164  LEU   A O     1 
ATOM   1059  C  CB    . LEU   A  1  166  ? -11.363 55.702  72.279  1.00 15.81 ? 164  LEU   A CB    1 
ATOM   1060  C  CG    . LEU   A  1  166  ? -12.302 54.970  73.223  1.00 15.52 ? 164  LEU   A CG    1 
ATOM   1061  C  CD1   . LEU   A  1  166  ? -13.470 55.867  73.492  1.00 16.65 ? 164  LEU   A CD1   1 
ATOM   1062  C  CD2   . LEU   A  1  166  ? -12.760 53.644  72.613  1.00 17.08 ? 164  LEU   A CD2   1 
ATOM   1063  N  N     . ALA   A  1  167  ? -8.529  56.554  71.154  1.00 15.30 ? 165  ALA   A N     1 
ATOM   1064  C  CA    . ALA   A  1  167  ? -7.722  57.089  70.062  1.00 15.25 ? 165  ALA   A CA    1 
ATOM   1065  C  C     . ALA   A  1  167  ? -6.678  56.069  69.621  1.00 16.26 ? 165  ALA   A C     1 
ATOM   1066  O  O     . ALA   A  1  167  ? -6.473  55.854  68.423  1.00 17.36 ? 165  ALA   A O     1 
ATOM   1067  C  CB    . ALA   A  1  167  ? -7.063  58.405  70.471  1.00 18.61 ? 165  ALA   A CB    1 
ATOM   1068  N  N     . ALA   A  1  168  ? -6.005  55.434  70.586  1.00 16.03 ? 166  ALA   A N     1 
ATOM   1069  C  CA    . ALA   A  1  168  ? -5.036  54.394  70.245  1.00 17.09 ? 166  ALA   A CA    1 
ATOM   1070  C  C     . ALA   A  1  168  ? -5.702  53.246  69.490  1.00 15.15 ? 166  ALA   A C     1 
ATOM   1071  O  O     . ALA   A  1  168  ? -5.174  52.760  68.480  1.00 15.98 ? 166  ALA   A O     1 
ATOM   1072  C  CB    . ALA   A  1  168  ? -4.370  53.883  71.526  1.00 16.58 ? 166  ALA   A CB    1 
ATOM   1073  N  N     . ALA   A  1  169  ? -6.888  52.825  69.948  1.00 14.48 ? 167  ALA   A N     1 
ATOM   1074  C  CA    . ALA   A  1  169  ? -7.577  51.707  69.320  1.00 14.21 ? 167  ALA   A CA    1 
ATOM   1075  C  C     . ALA   A  1  169  ? -8.008  52.057  67.901  1.00 14.46 ? 167  ALA   A C     1 
ATOM   1076  O  O     . ALA   A  1  169  ? -7.942  51.216  67.002  1.00 15.72 ? 167  ALA   A O     1 
ATOM   1077  C  CB    . ALA   A  1  169  ? -8.804  51.334  70.153  1.00 14.94 ? 167  ALA   A CB    1 
ATOM   1078  N  N     . LEU   A  1  170  ? -8.444  53.297  67.689  1.00 15.03 ? 168  LEU   A N     1 
ATOM   1079  C  CA    . LEU   A  1  170  ? -8.863  53.703  66.353  1.00 14.94 ? 168  LEU   A CA    1 
ATOM   1080  C  C     . LEU   A  1  170  ? -7.679  53.735  65.394  1.00 16.69 ? 168  LEU   A C     1 
ATOM   1081  O  O     . LEU   A  1  170  ? -7.758  53.228  64.270  1.00 17.58 ? 168  LEU   A O     1 
ATOM   1082  C  CB    . LEU   A  1  170  ? -9.542  55.065  66.431  1.00 16.88 ? 168  LEU   A CB    1 
ATOM   1083  C  CG    . LEU   A  1  170  ? -10.168 55.516  65.114  1.00 16.86 ? 168  LEU   A CG    1 
ATOM   1084  C  CD1   . LEU   A  1  170  ? -11.126 54.451  64.584  1.00 20.79 ? 168  LEU   A CD1   1 
ATOM   1085  C  CD2   . LEU   A  1  170  ? -10.872 56.839  65.338  1.00 19.02 ? 168  LEU   A CD2   1 
ATOM   1086  N  N     . THR   A  1  171  ? -6.560  54.316  65.834  1.00 16.24 ? 169  THR   A N     1 
ATOM   1087  C  CA    . THR   A  1  171  ? -5.362  54.302  65.006  1.00 17.16 ? 169  THR   A CA    1 
ATOM   1088  C  C     . THR   A  1  171  ? -4.965  52.869  64.682  1.00 15.98 ? 169  THR   A C     1 
ATOM   1089  O  O     . THR   A  1  171  ? -4.665  52.531  63.531  1.00 17.66 ? 169  THR   A O     1 
ATOM   1090  C  CB    . THR   A  1  171  ? -4.236  55.012  65.746  1.00 19.37 ? 169  THR   A CB    1 
ATOM   1091  O  OG1   . THR   A  1  171  ? -4.586  56.383  65.952  1.00 22.07 ? 169  THR   A OG1   1 
ATOM   1092  C  CG2   . THR   A  1  171  ? -2.930  54.935  64.961  1.00 20.45 ? 169  THR   A CG2   1 
ATOM   1093  N  N     . ARG   A  1  172  ? -4.994  52.003  65.696  1.00 15.69 ? 170  ARG   A N     1 
ATOM   1094  C  CA    . ARG   A  1  172  ? -4.586  50.618  65.498  1.00 16.96 ? 170  ARG   A CA    1 
ATOM   1095  C  C     . ARG   A  1  172  ? -5.492  49.911  64.502  1.00 17.50 ? 170  ARG   A C     1 
ATOM   1096  O  O     . ARG   A  1  172  ? -5.020  49.205  63.598  1.00 18.14 ? 170  ARG   A O     1 
ATOM   1097  C  CB    . ARG   A  1  172  ? -4.582  49.884  66.842  1.00 17.13 ? 170  ARG   A CB    1 
ATOM   1098  C  CG    . ARG   A  1  172  ? -3.924  48.509  66.767  1.00 16.89 ? 170  ARG   A CG    1 
ATOM   1099  C  CD    . ARG   A  1  172  ? -4.105  47.731  68.074  1.00 18.63 ? 170  ARG   A CD    1 
ATOM   1100  N  NE    . ARG   A  1  172  ? -3.830  48.533  69.254  1.00 17.16 ? 170  ARG   A NE    1 
ATOM   1101  C  CZ    . ARG   A  1  172  ? -4.754  48.996  70.085  1.00 15.85 ? 170  ARG   A CZ    1 
ATOM   1102  N  NH1   . ARG   A  1  172  ? -6.044  48.751  69.897  1.00 16.39 ? 170  ARG   A NH1   1 
ATOM   1103  N  NH2   . ARG   A  1  172  ? -4.379  49.731  71.122  1.00 17.07 ? 170  ARG   A NH2   1 
ATOM   1104  N  N     . LEU   A  1  173  ? -6.807  50.078  64.646  1.00 16.32 ? 171  LEU   A N     1 
ATOM   1105  C  CA    . LEU   A  1  173  ? -7.695  49.325  63.775  1.00 16.10 ? 171  LEU   A CA    1 
ATOM   1106  C  C     . LEU   A  1  173  ? -7.642  49.849  62.347  1.00 17.00 ? 171  LEU   A C     1 
ATOM   1107  O  O     . LEU   A  1  173  ? -7.698  49.065  61.399  1.00 18.79 ? 171  LEU   A O     1 
ATOM   1108  C  CB    . LEU   A  1  173  ? -9.124  49.311  64.331  1.00 18.59 ? 171  LEU   A CB    1 
ATOM   1109  C  CG    . LEU   A  1  173  ? -10.022 50.552  64.260  1.00 19.46 ? 171  LEU   A CG    1 
ATOM   1110  C  CD1   . LEU   A  1  173  ? -10.790 50.605  62.943  1.00 21.43 ? 171  LEU   A CD1   1 
ATOM   1111  C  CD2   . LEU   A  1  173  ? -10.999 50.588  65.428  1.00 19.01 ? 171  LEU   A CD2   1 
ATOM   1112  N  N     . ILE   A  1  174  ? -7.526  51.168  62.175  1.00 18.14 ? 172  ILE   A N     1 
ATOM   1113  C  CA    . ILE   A  1  174  ? -7.430  51.710  60.821  1.00 17.43 ? 172  ILE   A CA    1 
ATOM   1114  C  C     . ILE   A  1  174  ? -6.124  51.271  60.171  1.00 17.02 ? 172  ILE   A C     1 
ATOM   1115  O  O     . ILE   A  1  174  ? -6.097  50.883  58.999  1.00 19.88 ? 172  ILE   A O     1 
ATOM   1116  C  CB    . ILE   A  1  174  ? -7.574  53.244  60.848  1.00 19.35 ? 172  ILE   A CB    1 
ATOM   1117  C  CG1   . ILE   A  1  174  ? -8.993  53.649  61.226  1.00 21.72 ? 172  ILE   A CG1   1 
ATOM   1118  C  CG2   . ILE   A  1  174  ? -7.210  53.838  59.479  1.00 23.16 ? 172  ILE   A CG2   1 
ATOM   1119  C  CD1   . ILE   A  1  174  ? -9.132  55.130  61.516  1.00 22.13 ? 172  ILE   A CD1   1 
ATOM   1120  N  N     . SER   A  1  175  ? -5.019  51.305  60.926  1.00 18.39 ? 173  SER   A N     1 
ATOM   1121  C  CA    . SER   A  1  175  ? -3.741  50.918  60.341  1.00 18.52 ? 173  SER   A CA    1 
ATOM   1122  C  C     . SER   A  1  175  ? -3.700  49.430  60.048  1.00 19.23 ? 173  SER   A C     1 
ATOM   1123  O  O     . SER   A  1  175  ? -2.964  48.994  59.159  1.00 22.06 ? 173  SER   A O     1 
ATOM   1124  C  CB    . SER   A  1  175  ? -2.593  51.294  61.269  1.00 20.51 ? 173  SER   A CB    1 
ATOM   1125  O  OG    . SER   A  1  175  ? -2.456  52.700  61.362  1.00 24.98 ? 173  SER   A OG    1 
ATOM   1126  N  N     . ARG   A  1  176  ? -4.484  48.642  60.774  1.00 19.59 ? 174  ARG   A N     1 
ATOM   1127  C  CA    . ARG   A  1  176  ? -4.484  47.208  60.538  1.00 18.53 ? 174  ARG   A CA    1 
ATOM   1128  C  C     . ARG   A  1  176  ? -5.436  46.825  59.413  1.00 23.52 ? 174  ARG   A C     1 
ATOM   1129  O  O     . ARG   A  1  176  ? -5.099  45.986  58.574  1.00 25.99 ? 174  ARG   A O     1 
ATOM   1130  C  CB    . ARG   A  1  176  ? -4.877  46.500  61.837  1.00 23.16 ? 174  ARG   A CB    1 
ATOM   1131  C  CG    . ARG   A  1  176  ? -4.730  44.994  61.800  1.00 25.60 ? 174  ARG   A CG    1 
ATOM   1132  C  CD    . ARG   A  1  176  ? -4.948  44.420  63.192  1.00 22.87 ? 174  ARG   A CD    1 
ATOM   1133  N  NE    . ARG   A  1  176  ? -6.362  44.408  63.541  1.00 21.83 ? 174  ARG   A NE    1 
ATOM   1134  C  CZ    . ARG   A  1  176  ? -6.931  45.092  64.531  1.00 23.63 ? 174  ARG   A CZ    1 
ATOM   1135  N  NH1   . ARG   A  1  176  ? -6.223  45.835  65.379  1.00 20.17 ? 174  ARG   A NH1   1 
ATOM   1136  N  NH2   . ARG   A  1  176  ? -8.252  45.025  64.685  1.00 27.31 ? 174  ARG   A NH2   1 
ATOM   1137  N  N     . CYS   A  1  177  ? -6.625  47.431  59.370  1.00 22.00 ? 175  CYS   A N     1 
ATOM   1138  C  CA    . CYS   A  1  177  ? -7.682  46.965  58.484  1.00 23.70 ? 175  CYS   A CA    1 
ATOM   1139  C  C     . CYS   A  1  177  ? -8.119  47.962  57.421  1.00 25.55 ? 175  CYS   A C     1 
ATOM   1140  O  O     . CYS   A  1  177  ? -8.809  47.559  56.480  1.00 28.71 ? 175  CYS   A O     1 
ATOM   1141  C  CB    . CYS   A  1  177  ? -8.918  46.545  59.294  1.00 26.00 ? 175  CYS   A CB    1 
ATOM   1142  S  SG    . CYS   A  1  177  ? -8.544  45.370  60.624  1.00 30.20 ? 175  CYS   A SG    1 
ATOM   1143  N  N     . GLY   A  1  178  ? -7.786  49.238  57.561  1.00 25.21 ? 176  GLY   A N     1 
ATOM   1144  C  CA    . GLY   A  1  178  ? -7.994  50.178  56.478  1.00 26.10 ? 176  GLY   A CA    1 
ATOM   1145  C  C     . GLY   A  1  178  ? -9.444  50.516  56.161  1.00 25.14 ? 176  GLY   A C     1 
ATOM   1146  O  O     . GLY   A  1  178  ? -10.365 50.358  56.969  1.00 23.94 ? 176  GLY   A O     1 
ATOM   1147  N  N     . GLU   A  1  179  ? -9.622  51.004  54.936  1.00 26.04 ? 177  GLU   A N     1 
ATOM   1148  C  CA    . GLU   A  1  179  ? -10.939 51.421  54.462  1.00 23.63 ? 177  GLU   A CA    1 
ATOM   1149  C  C     . GLU   A  1  179  ? -12.031 50.375  54.642  1.00 21.39 ? 177  GLU   A C     1 
ATOM   1150  O  O     . GLU   A  1  179  ? -13.150 50.759  55.028  1.00 24.89 ? 177  GLU   A O     1 
ATOM   1151  C  CB    . GLU   A  1  179  ? -10.834 51.885  53.000  1.00 25.49 ? 177  GLU   A CB    1 
ATOM   1152  N  N     . PRO   A  1  180  ? -11.812 49.081  54.370  1.00 22.73 ? 178  PRO   A N     1 
ATOM   1153  C  CA    . PRO   A  1  180  ? -12.911 48.116  54.534  1.00 22.67 ? 178  PRO   A CA    1 
ATOM   1154  C  C     . PRO   A  1  180  ? -13.582 48.145  55.896  1.00 24.40 ? 178  PRO   A C     1 
ATOM   1155  O  O     . PRO   A  1  180  ? -14.817 48.109  55.959  1.00 24.21 ? 178  PRO   A O     1 
ATOM   1156  C  CB    . PRO   A  1  180  ? -12.236 46.771  54.246  1.00 28.25 ? 178  PRO   A CB    1 
ATOM   1157  C  CG    . PRO   A  1  180  ? -11.165 47.108  53.299  1.00 26.64 ? 178  PRO   A CG    1 
ATOM   1158  C  CD    . PRO   A  1  180  ? -10.646 48.453  53.726  1.00 24.03 ? 178  PRO   A CD    1 
ATOM   1159  N  N     . VAL   A  1  181  ? -12.813 48.227  56.987  1.00 21.62 ? 179  VAL   A N     1 
ATOM   1160  C  CA    . VAL   A  1  181  ? -13.430 48.237  58.307  1.00 20.04 ? 179  VAL   A CA    1 
ATOM   1161  C  C     . VAL   A  1  181  ? -14.163 49.549  58.549  1.00 21.18 ? 179  VAL   A C     1 
ATOM   1162  O  O     . VAL   A  1  181  ? -15.211 49.566  59.201  1.00 20.81 ? 179  VAL   A O     1 
ATOM   1163  C  CB    . VAL   A  1  181  ? -12.419 47.900  59.425  1.00 20.80 ? 179  VAL   A CB    1 
ATOM   1164  C  CG1   . VAL   A  1  181  ? -11.429 49.038  59.634  1.00 20.14 ? 179  VAL   A CG1   1 
ATOM   1165  C  CG2   . VAL   A  1  181  ? -13.164 47.603  60.728  1.00 25.50 ? 179  VAL   A CG2   1 
ATOM   1166  N  N     . ILE   A  1  182  ? -13.647 50.660  58.016  1.00 21.59 ? 180  ILE   A N     1 
ATOM   1167  C  CA    . ILE   A  1  182  ? -14.330 51.941  58.159  1.00 21.25 ? 180  ILE   A CA    1 
ATOM   1168  C  C     . ILE   A  1  182  ? -15.662 51.906  57.430  1.00 23.91 ? 180  ILE   A C     1 
ATOM   1169  O  O     . ILE   A  1  182  ? -16.688 52.351  57.952  1.00 22.37 ? 180  ILE   A O     1 
ATOM   1170  C  CB    . ILE   A  1  182  ? -13.446 53.092  57.653  1.00 21.60 ? 180  ILE   A CB    1 
ATOM   1171  C  CG1   . ILE   A  1  182  ? -12.150 53.160  58.454  1.00 21.54 ? 180  ILE   A CG1   1 
ATOM   1172  C  CG2   . ILE   A  1  182  ? -14.200 54.412  57.758  1.00 22.77 ? 180  ILE   A CG2   1 
ATOM   1173  C  CD1   . ILE   A  1  182  ? -11.067 53.986  57.790  1.00 24.49 ? 180  ILE   A CD1   1 
ATOM   1174  N  N     . ARG   A  1  183  ? -15.650 51.377  56.206  1.00 22.42 ? 181  ARG   A N     1 
ATOM   1175  C  CA    A ARG   A  1  183  ? -16.881 51.250  55.433  0.38 27.08 ? 181  ARG   A CA    1 
ATOM   1176  C  CA    B ARG   A  1  183  ? -16.876 51.237  55.424  0.62 27.09 ? 181  ARG   A CA    1 
ATOM   1177  C  C     . ARG   A  1  183  ? -17.911 50.415  56.179  1.00 26.54 ? 181  ARG   A C     1 
ATOM   1178  O  O     . ARG   A  1  183  ? -19.091 50.786  56.253  1.00 26.79 ? 181  ARG   A O     1 
ATOM   1179  C  CB    A ARG   A  1  183  ? -16.571 50.639  54.066  0.38 27.42 ? 181  ARG   A CB    1 
ATOM   1180  C  CB    B ARG   A  1  183  ? -16.529 50.567  54.093  0.62 27.36 ? 181  ARG   A CB    1 
ATOM   1181  C  CG    A ARG   A  1  183  ? -17.800 50.316  53.226  0.38 32.37 ? 181  ARG   A CG    1 
ATOM   1182  C  CG    B ARG   A  1  183  ? -17.691 50.349  53.137  0.62 32.44 ? 181  ARG   A CG    1 
ATOM   1183  C  CD    A ARG   A  1  183  ? -18.709 51.529  53.094  0.38 33.30 ? 181  ARG   A CD    1 
ATOM   1184  C  CD    B ARG   A  1  183  ? -18.092 51.648  52.459  0.62 34.98 ? 181  ARG   A CD    1 
ATOM   1185  N  NE    A ARG   A  1  183  ? -18.001 52.687  52.559  0.38 32.89 ? 181  ARG   A NE    1 
ATOM   1186  N  NE    B ARG   A  1  183  ? -19.085 52.384  53.234  0.62 31.33 ? 181  ARG   A NE    1 
ATOM   1187  C  CZ    A ARG   A  1  183  ? -18.407 53.940  52.702  0.38 34.89 ? 181  ARG   A CZ    1 
ATOM   1188  C  CZ    B ARG   A  1  183  ? -19.296 53.688  53.127  0.62 35.14 ? 181  ARG   A CZ    1 
ATOM   1189  N  NH1   A ARG   A  1  183  ? -19.499 54.239  53.388  0.38 34.36 ? 181  ARG   A NH1   1 
ATOM   1190  N  NH1   B ARG   A  1  183  ? -18.566 54.442  52.321  0.62 36.96 ? 181  ARG   A NH1   1 
ATOM   1191  N  NH2   A ARG   A  1  183  ? -17.697 54.919  52.147  0.38 36.34 ? 181  ARG   A NH2   1 
ATOM   1192  N  NH2   B ARG   A  1  183  ? -20.261 54.249  53.846  0.62 32.89 ? 181  ARG   A NH2   1 
ATOM   1193  N  N     . ARG   A  1  184  ? -17.486 49.284  56.741  1.00 23.11 ? 182  ARG   A N     1 
ATOM   1194  C  CA    . ARG   A  1  184  ? -18.417 48.443  57.483  1.00 25.01 ? 182  ARG   A CA    1 
ATOM   1195  C  C     . ARG   A  1  184  ? -18.932 49.156  58.724  1.00 24.99 ? 182  ARG   A C     1 
ATOM   1196  O  O     . ARG   A  1  184  ? -20.114 49.040  59.068  1.00 24.79 ? 182  ARG   A O     1 
ATOM   1197  C  CB    . ARG   A  1  184  ? -17.749 47.122  57.851  1.00 27.67 ? 182  ARG   A CB    1 
ATOM   1198  C  CG    . ARG   A  1  184  ? -17.616 46.169  56.675  1.00 33.74 ? 182  ARG   A CG    1 
ATOM   1199  C  CD    . ARG   A  1  184  ? -18.820 45.229  56.581  1.00 32.66 ? 182  ARG   A CD    1 
ATOM   1200  N  NE    . ARG   A  1  184  ? -18.671 44.088  57.476  1.00 35.06 ? 182  ARG   A NE    1 
ATOM   1201  C  CZ    . ARG   A  1  184  ? -19.478 43.810  58.491  1.00 32.84 ? 182  ARG   A CZ    1 
ATOM   1202  N  NH1   . ARG   A  1  184  ? -20.535 44.558  58.761  1.00 36.58 ? 182  ARG   A NH1   1 
ATOM   1203  N  NH2   . ARG   A  1  184  ? -19.226 42.744  59.245  1.00 32.68 ? 182  ARG   A NH2   1 
ATOM   1204  N  N     . GLY   A  1  185  ? -18.059 49.892  59.411  1.00 22.87 ? 183  GLY   A N     1 
ATOM   1205  C  CA    . GLY   A  1  185  ? -18.497 50.631  60.580  1.00 22.07 ? 183  GLY   A CA    1 
ATOM   1206  C  C     . GLY   A  1  185  ? -19.518 51.698  60.233  1.00 25.57 ? 183  GLY   A C     1 
ATOM   1207  O  O     . GLY   A  1  185  ? -20.529 51.849  60.916  1.00 21.43 ? 183  GLY   A O     1 
ATOM   1208  N  N     . VAL   A  1  186  ? -19.254 52.461  59.171  1.00 24.04 ? 184  VAL   A N     1 
ATOM   1209  C  CA    . VAL   A  1  186  ? -20.184 53.503  58.742  1.00 25.15 ? 184  VAL   A CA    1 
ATOM   1210  C  C     . VAL   A  1  186  ? -21.533 52.900  58.387  1.00 25.04 ? 184  VAL   A C     1 
ATOM   1211  O  O     . VAL   A  1  186  ? -22.587 53.400  58.800  1.00 24.27 ? 184  VAL   A O     1 
ATOM   1212  C  CB    . VAL   A  1  186  ? -19.593 54.296  57.563  1.00 25.93 ? 184  VAL   A CB    1 
ATOM   1213  C  CG1   . VAL   A  1  186  ? -20.692 55.114  56.874  1.00 25.90 ? 184  VAL   A CG1   1 
ATOM   1214  C  CG2   . VAL   A  1  186  ? -18.483 55.191  58.051  1.00 26.05 ? 184  VAL   A CG2   1 
ATOM   1215  N  N     . ASP   A  1  187  ? -21.523 51.813  57.618  1.00 23.59 ? 185  ASP   A N     1 
ATOM   1216  C  CA    . ASP   A  1  187  ? -22.785 51.201  57.214  1.00 26.32 ? 185  ASP   A CA    1 
ATOM   1217  C  C     . ASP   A  1  187  ? -23.543 50.653  58.416  1.00 28.70 ? 185  ASP   A C     1 
ATOM   1218  O  O     . ASP   A  1  187  ? -24.776 50.754  58.477  1.00 27.11 ? 185  ASP   A O     1 
ATOM   1219  C  CB    . ASP   A  1  187  ? -22.543 50.113  56.174  1.00 29.28 ? 185  ASP   A CB    1 
ATOM   1220  C  CG    . ASP   A  1  187  ? -22.055 50.674  54.848  1.00 34.00 ? 185  ASP   A CG    1 
ATOM   1221  O  OD1   . ASP   A  1  187  ? -22.205 51.894  54.621  1.00 37.95 ? 185  ASP   A OD1   1 
ATOM   1222  O  OD2   . ASP   A  1  187  ? -21.529 49.895  54.028  1.00 36.68 ? 185  ASP   A OD2   1 
ATOM   1223  N  N     . MET   A  1  188  ? -22.824 50.084  59.386  1.00 26.92 ? 186  MET   A N     1 
ATOM   1224  C  CA    . MET   A  1  188  ? -23.467 49.597  60.604  1.00 27.01 ? 186  MET   A CA    1 
ATOM   1225  C  C     . MET   A  1  188  ? -24.071 50.740  61.401  1.00 27.65 ? 186  MET   A C     1 
ATOM   1226  O  O     . MET   A  1  188  ? -25.228 50.669  61.834  1.00 27.03 ? 186  MET   A O     1 
ATOM   1227  C  CB    . MET   A  1  188  ? -22.450 48.855  61.465  1.00 29.43 ? 186  MET   A CB    1 
ATOM   1228  C  CG    . MET   A  1  188  ? -23.033 48.285  62.744  1.00 34.40 ? 186  MET   A CG    1 
ATOM   1229  S  SD    . MET   A  1  188  ? -24.148 46.929  62.352  1.00 45.63 ? 186  MET   A SD    1 
ATOM   1230  C  CE    . MET   A  1  188  ? -23.055 45.947  61.318  1.00 38.51 ? 186  MET   A CE    1 
ATOM   1231  N  N     . ALA   A  1  189  ? -23.289 51.796  61.632  1.00 25.39 ? 187  ALA   A N     1 
ATOM   1232  C  CA    . ALA   A  1  189  ? -23.796 52.918  62.412  1.00 26.82 ? 187  ALA   A CA    1 
ATOM   1233  C  C     . ALA   A  1  189  ? -24.978 53.575  61.716  1.00 27.29 ? 187  ALA   A C     1 
ATOM   1234  O  O     . ALA   A  1  189  ? -25.933 54.003  62.371  1.00 26.15 ? 187  ALA   A O     1 
ATOM   1235  C  CB    . ALA   A  1  189  ? -22.690 53.940  62.657  1.00 26.44 ? 187  ALA   A CB    1 
ATOM   1236  N  N     . MET   A  1  190  ? -24.926 53.667  60.388  1.00 25.49 ? 188  MET   A N     1 
ATOM   1237  C  CA    . MET   A  1  190  ? -26.034 54.260  59.643  1.00 26.95 ? 188  MET   A CA    1 
ATOM   1238  C  C     . MET   A  1  190  ? -27.308 53.448  59.817  1.00 26.85 ? 188  MET   A C     1 
ATOM   1239  O  O     . MET   A  1  190  ? -28.395 54.011  60.002  1.00 29.23 ? 188  MET   A O     1 
ATOM   1240  C  CB    . MET   A  1  190  ? -25.663 54.345  58.164  1.00 28.41 ? 188  MET   A CB    1 
ATOM   1241  C  CG    . MET   A  1  190  ? -26.610 55.185  57.331  1.00 38.24 ? 188  MET   A CG    1 
ATOM   1242  S  SD    . MET   A  1  190  ? -26.199 55.098  55.573  1.00 42.46 ? 188  MET   A SD    1 
ATOM   1243  C  CE    . MET   A  1  190  ? -24.429 55.377  55.624  1.00 35.88 ? 188  MET   A CE    1 
ATOM   1244  N  N     . ARG   A  1  191  ? -27.190 52.121  59.759  1.00 25.38 ? 189  ARG   A N     1 
ATOM   1245  C  CA    . ARG   A  1  191  ? -28.334 51.249  59.994  1.00 29.93 ? 189  ARG   A CA    1 
ATOM   1246  C  C     . ARG   A  1  191  ? -28.857 51.404  61.417  1.00 31.49 ? 189  ARG   A C     1 
ATOM   1247  O  O     . ARG   A  1  191  ? -30.068 51.521  61.640  1.00 29.76 ? 189  ARG   A O     1 
ATOM   1248  C  CB    . ARG   A  1  191  ? -27.931 49.796  59.731  1.00 30.44 ? 189  ARG   A CB    1 
ATOM   1249  C  CG    . ARG   A  1  191  ? -29.059 48.781  59.850  1.00 38.92 ? 189  ARG   A CG    1 
ATOM   1250  C  CD    . ARG   A  1  191  ? -28.517 47.365  60.040  1.00 45.43 ? 189  ARG   A CD    1 
ATOM   1251  N  NE    . ARG   A  1  191  ? -29.583 46.402  60.294  1.00 58.48 ? 189  ARG   A NE    1 
ATOM   1252  C  CZ    . ARG   A  1  191  ? -29.883 45.381  59.501  1.00 62.27 ? 189  ARG   A CZ    1 
ATOM   1253  N  NH1   . ARG   A  1  191  ? -29.186 45.126  58.405  1.00 58.97 ? 189  ARG   A NH1   1 
ATOM   1254  N  NH2   . ARG   A  1  191  ? -30.906 44.591  59.819  1.00 62.10 ? 189  ARG   A NH2   1 
ATOM   1255  N  N     . MET   A  1  192  ? -27.960 51.400  62.402  1.00 25.21 ? 190  MET   A N     1 
ATOM   1256  C  CA    . MET   A  1  192  ? -28.419 51.429  63.786  1.00 24.88 ? 190  MET   A CA    1 
ATOM   1257  C  C     . MET   A  1  192  ? -29.050 52.769  64.132  1.00 28.60 ? 190  MET   A C     1 
ATOM   1258  O  O     . MET   A  1  192  ? -30.116 52.820  64.754  1.00 27.69 ? 190  MET   A O     1 
ATOM   1259  C  CB    . MET   A  1  192  ? -27.265 51.125  64.739  1.00 29.23 ? 190  MET   A CB    1 
ATOM   1260  C  CG    . MET   A  1  192  ? -26.670 49.752  64.567  1.00 27.40 ? 190  MET   A CG    1 
ATOM   1261  S  SD    . MET   A  1  192  ? -25.362 49.511  65.781  1.00 39.63 ? 190  MET   A SD    1 
ATOM   1262  C  CE    . MET   A  1  192  ? -26.344 49.254  67.247  1.00 33.05 ? 190  MET   A CE    1 
ATOM   1263  N  N     . MET   A  1  193  ? -28.401 53.868  63.755  1.00 25.51 ? 191  MET   A N     1 
ATOM   1264  C  CA    A MET   A  1  193  ? -28.887 55.184  64.148  0.50 30.16 ? 191  MET   A CA    1 
ATOM   1265  C  CA    B MET   A  1  193  ? -28.896 55.177  64.154  0.50 30.17 ? 191  MET   A CA    1 
ATOM   1266  C  C     . MET   A  1  193  ? -30.079 55.649  63.322  1.00 29.11 ? 191  MET   A C     1 
ATOM   1267  O  O     . MET   A  1  193  ? -30.837 56.506  63.787  1.00 31.57 ? 191  MET   A O     1 
ATOM   1268  C  CB    A MET   A  1  193  ? -27.762 56.214  64.058  0.50 28.78 ? 191  MET   A CB    1 
ATOM   1269  C  CB    B MET   A  1  193  ? -27.777 56.215  64.109  0.50 28.78 ? 191  MET   A CB    1 
ATOM   1270  C  CG    A MET   A  1  193  ? -26.506 55.834  64.832  0.50 28.33 ? 191  MET   A CG    1 
ATOM   1271  C  CG    B MET   A  1  193  ? -26.763 56.067  65.228  0.50 28.08 ? 191  MET   A CG    1 
ATOM   1272  S  SD    A MET   A  1  193  ? -25.176 57.029  64.587  0.50 30.22 ? 191  MET   A SD    1 
ATOM   1273  S  SD    B MET   A  1  193  ? -25.765 57.554  65.406  0.50 33.46 ? 191  MET   A SD    1 
ATOM   1274  C  CE    A MET   A  1  193  ? -25.671 58.307  65.743  0.50 34.57 ? 191  MET   A CE    1 
ATOM   1275  C  CE    B MET   A  1  193  ? -24.929 57.597  63.817  0.50 30.45 ? 191  MET   A CE    1 
ATOM   1276  N  N     . GLY   A  1  194  ? -30.260 55.109  62.124  1.00 28.74 ? 192  GLY   A N     1 
ATOM   1277  C  CA    . GLY   A  1  194  ? -31.336 55.552  61.260  1.00 28.69 ? 192  GLY   A CA    1 
ATOM   1278  C  C     . GLY   A  1  194  ? -32.525 54.616  61.196  1.00 33.49 ? 192  GLY   A C     1 
ATOM   1279  O  O     . GLY   A  1  194  ? -33.617 55.029  60.784  1.00 30.17 ? 192  GLY   A O     1 
ATOM   1280  N  N     . GLU   A  1  195  ? -32.329 53.354  61.596  1.00 28.75 ? 193  GLU   A N     1 
ATOM   1281  C  CA    . GLU   A  1  195  ? -33.358 52.331  61.452  1.00 28.44 ? 193  GLU   A CA    1 
ATOM   1282  C  C     . GLU   A  1  195  ? -33.623 51.507  62.699  1.00 24.48 ? 193  GLU   A C     1 
ATOM   1283  O  O     . GLU   A  1  195  ? -34.689 50.886  62.773  1.00 24.00 ? 193  GLU   A O     1 
ATOM   1284  C  CB    . GLU   A  1  195  ? -33.013 51.357  60.316  1.00 31.22 ? 193  GLU   A CB    1 
ATOM   1285  C  CG    . GLU   A  1  195  ? -32.639 52.007  59.007  1.00 38.88 ? 193  GLU   A CG    1 
ATOM   1286  C  CD    . GLU   A  1  195  ? -32.111 50.997  58.013  1.00 45.90 ? 193  GLU   A CD    1 
ATOM   1287  O  OE1   . GLU   A  1  195  ? -32.396 49.792  58.188  1.00 48.97 ? 193  GLU   A OE1   1 
ATOM   1288  O  OE2   . GLU   A  1  195  ? -31.404 51.403  57.067  1.00 53.06 ? 193  GLU   A OE2   1 
ATOM   1289  N  N     . GLN   A  1  196  ? -32.702 51.449  63.660  1.00 29.48 ? 194  GLN   A N     1 
ATOM   1290  C  CA    . GLN   A  1  196  ? -32.878 50.626  64.851  1.00 27.40 ? 194  GLN   A CA    1 
ATOM   1291  C  C     . GLN   A  1  196  ? -33.162 51.445  66.099  1.00 29.30 ? 194  GLN   A C     1 
ATOM   1292  O  O     . GLN   A  1  196  ? -34.164 51.211  66.779  1.00 31.19 ? 194  GLN   A O     1 
ATOM   1293  C  CB    . GLN   A  1  196  ? -31.647 49.735  65.084  1.00 30.22 ? 194  GLN   A CB    1 
ATOM   1294  C  CG    . GLN   A  1  196  ? -31.792 48.833  66.306  1.00 39.17 ? 194  GLN   A CG    1 
ATOM   1295  C  CD    . GLN   A  1  196  ? -30.483 48.211  66.753  1.00 39.33 ? 194  GLN   A CD    1 
ATOM   1296  O  OE1   . GLN   A  1  196  ? -29.609 47.916  65.936  1.00 43.38 ? 194  GLN   A OE1   1 
ATOM   1297  N  NE2   . GLN   A  1  196  ? -30.342 48.009  68.062  1.00 45.40 ? 194  GLN   A NE2   1 
ATOM   1298  N  N     . PHE   A  1  197  ? -32.300 52.405  66.424  1.00 27.35 ? 195  PHE   A N     1 
ATOM   1299  C  CA    . PHE   A  1  197  ? -32.545 53.256  67.577  1.00 28.15 ? 195  PHE   A CA    1 
ATOM   1300  C  C     . PHE   A  1  197  ? -33.718 54.185  67.341  1.00 29.97 ? 195  PHE   A C     1 
ATOM   1301  O  O     . PHE   A  1  197  ? -34.310 54.678  68.306  1.00 28.14 ? 195  PHE   A O     1 
ATOM   1302  C  CB    . PHE   A  1  197  ? -31.304 54.080  67.885  1.00 30.22 ? 195  PHE   A CB    1 
ATOM   1303  C  CG    . PHE   A  1  197  ? -30.111 53.252  68.250  1.00 30.72 ? 195  PHE   A CG    1 
ATOM   1304  C  CD1   . PHE   A  1  197  ? -30.262 52.082  68.972  1.00 35.46 ? 195  PHE   A CD1   1 
ATOM   1305  C  CD2   . PHE   A  1  197  ? -28.840 53.644  67.871  1.00 32.39 ? 195  PHE   A CD2   1 
ATOM   1306  C  CE1   . PHE   A  1  197  ? -29.166 51.317  69.316  1.00 36.85 ? 195  PHE   A CE1   1 
ATOM   1307  C  CE2   . PHE   A  1  197  ? -27.737 52.878  68.215  1.00 33.93 ? 195  PHE   A CE2   1 
ATOM   1308  C  CZ    . PHE   A  1  197  ? -27.912 51.716  68.941  1.00 31.08 ? 195  PHE   A CZ    1 
ATOM   1309  N  N     . VAL   A  1  198  ? -34.043 54.450  66.084  1.00 25.65 ? 196  VAL   A N     1 
ATOM   1310  C  CA    . VAL   A  1  198  ? -35.216 55.225  65.718  1.00 25.98 ? 196  VAL   A CA    1 
ATOM   1311  C  C     . VAL   A  1  198  ? -35.918 54.498  64.587  1.00 23.51 ? 196  VAL   A C     1 
ATOM   1312  O  O     . VAL   A  1  198  ? -35.307 53.729  63.840  1.00 27.46 ? 196  VAL   A O     1 
ATOM   1313  C  CB    . VAL   A  1  198  ? -34.864 56.670  65.289  1.00 26.19 ? 196  VAL   A CB    1 
ATOM   1314  C  CG1   . VAL   A  1  198  ? -34.127 57.412  66.405  1.00 26.66 ? 196  VAL   A CG1   1 
ATOM   1315  C  CG2   . VAL   A  1  198  ? -34.038 56.662  64.009  1.00 26.75 ? 196  VAL   A CG2   1 
ATOM   1316  N  N     . THR   A  1  199  ? -37.227 54.720  64.480  1.00 22.94 ? 197  THR   A N     1 
ATOM   1317  C  CA    A THR   A  1  199  ? -37.953 54.213  63.327  0.68 22.82 ? 197  THR   A CA    1 
ATOM   1318  C  CA    B THR   A  1  199  ? -37.958 54.221  63.319  0.32 22.86 ? 197  THR   A CA    1 
ATOM   1319  C  C     . THR   A  1  199  ? -37.642 55.037  62.085  1.00 27.28 ? 197  THR   A C     1 
ATOM   1320  O  O     . THR   A  1  199  ? -37.621 54.500  60.977  1.00 27.94 ? 197  THR   A O     1 
ATOM   1321  C  CB    A THR   A  1  199  ? -39.448 54.202  63.649  0.68 22.67 ? 197  THR   A CB    1 
ATOM   1322  C  CB    B THR   A  1  199  ? -39.462 54.303  63.543  0.32 22.64 ? 197  THR   A CB    1 
ATOM   1323  O  OG1   A THR   A  1  199  ? -39.639 53.544  64.910  0.68 22.73 ? 197  THR   A OG1   1 
ATOM   1324  O  OG1   B THR   A  1  199  ? -39.782 55.561  64.149  0.32 20.37 ? 197  THR   A OG1   1 
ATOM   1325  C  CG2   A THR   A  1  199  ? -40.238 53.473  62.572  0.68 24.05 ? 197  THR   A CG2   1 
ATOM   1326  C  CG2   B THR   A  1  199  ? -39.927 53.171  64.404  0.32 22.62 ? 197  THR   A CG2   1 
ATOM   1327  N  N     . GLY   A  1  200  ? -37.398 56.324  62.257  1.00 23.49 ? 198  GLY   A N     1 
ATOM   1328  C  CA    . GLY   A  1  200  ? -37.014 57.175  61.154  1.00 25.36 ? 198  GLY   A CA    1 
ATOM   1329  C  C     . GLY   A  1  200  ? -36.453 58.465  61.697  1.00 25.12 ? 198  GLY   A C     1 
ATOM   1330  O  O     . GLY   A  1  200  ? -36.651 58.802  62.867  1.00 22.03 ? 198  GLY   A O     1 
ATOM   1331  N  N     . GLU   A  1  201  ? -35.729 59.177  60.835  1.00 25.62 ? 199  GLU   A N     1 
ATOM   1332  C  CA    . GLU   A  1  201  ? -35.189 60.466  61.247  1.00 24.36 ? 199  GLU   A CA    1 
ATOM   1333  C  C     . GLU   A  1  201  ? -36.282 61.521  61.327  1.00 25.08 ? 199  GLU   A C     1 
ATOM   1334  O  O     . GLU   A  1  201  ? -36.152 62.492  62.078  1.00 27.85 ? 199  GLU   A O     1 
ATOM   1335  C  CB    . GLU   A  1  201  ? -34.084 60.916  60.287  1.00 27.20 ? 199  GLU   A CB    1 
ATOM   1336  N  N     . THR   A  1  202  ? -37.368 61.338  60.578  1.00 23.24 ? 200  THR   A N     1 
ATOM   1337  C  CA    . THR   A  1  202  ? -38.470 62.283  60.560  1.00 22.73 ? 200  THR   A CA    1 
ATOM   1338  C  C     . THR   A  1  202  ? -39.769 61.504  60.654  1.00 22.71 ? 200  THR   A C     1 
ATOM   1339  O  O     . THR   A  1  202  ? -39.816 60.301  60.390  1.00 20.78 ? 200  THR   A O     1 
ATOM   1340  C  CB    . THR   A  1  202  ? -38.524 63.051  59.244  1.00 22.58 ? 200  THR   A CB    1 
ATOM   1341  O  OG1   . THR   A  1  202  ? -38.763 62.123  58.178  1.00 26.29 ? 200  THR   A OG1   1 
ATOM   1342  C  CG2   . THR   A  1  202  ? -37.210 63.809  58.994  1.00 24.27 ? 200  THR   A CG2   1 
ATOM   1343  N  N     . ILE   A  1  203  ? -40.839 62.209  61.024  1.00 21.54 ? 201  ILE   A N     1 
ATOM   1344  C  CA    . ILE   A  1  203  ? -42.119 61.524  61.169  1.00 21.23 ? 201  ILE   A CA    1 
ATOM   1345  C  C     . ILE   A  1  203  ? -42.567 60.922  59.843  1.00 23.00 ? 201  ILE   A C     1 
ATOM   1346  O  O     . ILE   A  1  203  ? -43.108 59.815  59.807  1.00 21.56 ? 201  ILE   A O     1 
ATOM   1347  C  CB    . ILE   A  1  203  ? -43.181 62.426  61.828  1.00 21.48 ? 201  ILE   A CB    1 
ATOM   1348  C  CG1   . ILE   A  1  203  ? -44.425 61.597  62.165  1.00 19.42 ? 201  ILE   A CG1   1 
ATOM   1349  C  CG2   . ILE   A  1  203  ? -43.533 63.613  60.936  1.00 22.20 ? 201  ILE   A CG2   1 
ATOM   1350  C  CD1   . ILE   A  1  203  ? -44.145 60.416  63.078  1.00 18.41 ? 201  ILE   A CD1   1 
ATOM   1351  N  N     . ARG   A  1  204  ? -42.296 61.608  58.729  1.00 21.55 ? 202  ARG   A N     1 
ATOM   1352  C  CA    . ARG   A  1  204  ? -42.676 61.080  57.421  1.00 22.25 ? 202  ARG   A CA    1 
ATOM   1353  C  C     . ARG   A  1  204  ? -41.946 59.785  57.106  1.00 22.48 ? 202  ARG   A C     1 
ATOM   1354  O  O     . ARG   A  1  204  ? -42.546 58.836  56.589  1.00 23.36 ? 202  ARG   A O     1 
ATOM   1355  C  CB    . ARG   A  1  204  ? -42.394 62.113  56.336  1.00 28.34 ? 202  ARG   A CB    1 
ATOM   1356  C  CG    . ARG   A  1  204  ? -43.565 63.016  56.062  1.00 36.45 ? 202  ARG   A CG    1 
ATOM   1357  C  CD    . ARG   A  1  204  ? -43.127 64.363  55.510  1.00 39.34 ? 202  ARG   A CD    1 
ATOM   1358  N  NE    . ARG   A  1  204  ? -44.251 65.289  55.529  1.00 40.23 ? 202  ARG   A NE    1 
ATOM   1359  C  CZ    . ARG   A  1  204  ? -44.717 65.874  56.625  1.00 39.56 ? 202  ARG   A CZ    1 
ATOM   1360  N  NH1   . ARG   A  1  204  ? -44.145 65.689  57.808  1.00 28.52 ? 202  ARG   A NH1   1 
ATOM   1361  N  NH2   . ARG   A  1  204  ? -45.787 66.660  56.533  1.00 34.50 ? 202  ARG   A NH2   1 
ATOM   1362  N  N     . GLU   A  1  205  ? -40.646 59.735  57.393  1.00 22.88 ? 203  GLU   A N     1 
ATOM   1363  C  CA    . GLU   A  1  205  ? -39.890 58.510  57.170  1.00 24.66 ? 203  GLU   A CA    1 
ATOM   1364  C  C     . GLU   A  1  205  ? -40.371 57.401  58.093  1.00 20.71 ? 203  GLU   A C     1 
ATOM   1365  O  O     . GLU   A  1  205  ? -40.513 56.250  57.670  1.00 23.90 ? 203  GLU   A O     1 
ATOM   1366  C  CB    . GLU   A  1  205  ? -38.404 58.773  57.385  1.00 25.11 ? 203  GLU   A CB    1 
ATOM   1367  C  CG    . GLU   A  1  205  ? -37.525 57.563  57.155  1.00 28.23 ? 203  GLU   A CG    1 
ATOM   1368  C  CD    . GLU   A  1  205  ? -36.048 57.911  57.223  1.00 34.97 ? 203  GLU   A CD    1 
ATOM   1369  O  OE1   . GLU   A  1  205  ? -35.541 58.166  58.342  1.00 32.83 ? 203  GLU   A OE1   1 
ATOM   1370  O  OE2   . GLU   A  1  205  ? -35.398 57.937  56.154  1.00 38.10 ? 203  GLU   A OE2   1 
ATOM   1371  N  N     . ALA   A  1  206  ? -40.639 57.735  59.357  1.00 20.95 ? 204  ALA   A N     1 
ATOM   1372  C  CA    . ALA   A  1  206  ? -41.125 56.733  60.296  1.00 20.82 ? 204  ALA   A CA    1 
ATOM   1373  C  C     . ALA   A  1  206  ? -42.470 56.174  59.857  1.00 21.11 ? 204  ALA   A C     1 
ATOM   1374  O  O     . ALA   A  1  206  ? -42.710 54.966  59.962  1.00 22.12 ? 204  ALA   A O     1 
ATOM   1375  C  CB    . ALA   A  1  206  ? -41.238 57.354  61.688  1.00 21.62 ? 204  ALA   A CB    1 
ATOM   1376  N  N     . LEU   A  1  207  ? -43.359 57.035  59.356  1.00 19.96 ? 205  LEU   A N     1 
ATOM   1377  C  CA    . LEU   A  1  207  ? -44.666 56.559  58.914  1.00 20.36 ? 205  LEU   A CA    1 
ATOM   1378  C  C     . LEU   A  1  207  ? -44.546 55.645  57.704  1.00 23.77 ? 205  LEU   A C     1 
ATOM   1379  O  O     . LEU   A  1  207  ? -45.265 54.644  57.605  1.00 25.36 ? 205  LEU   A O     1 
ATOM   1380  C  CB    . LEU   A  1  207  ? -45.577 57.742  58.607  1.00 22.88 ? 205  LEU   A CB    1 
ATOM   1381  C  CG    . LEU   A  1  207  ? -46.086 58.472  59.843  1.00 21.16 ? 205  LEU   A CG    1 
ATOM   1382  C  CD1   . LEU   A  1  207  ? -46.661 59.818  59.440  1.00 21.93 ? 205  LEU   A CD1   1 
ATOM   1383  C  CD2   . LEU   A  1  207  ? -47.122 57.624  60.577  1.00 21.77 ? 205  LEU   A CD2   1 
ATOM   1384  N  N     . LYS   A  1  208  ? -43.642 55.972  56.776  1.00 22.43 ? 206  LYS   A N     1 
ATOM   1385  C  CA    . LYS   A  1  208  ? -43.438 55.104  55.622  1.00 25.66 ? 206  LYS   A CA    1 
ATOM   1386  C  C     . LYS   A  1  208  ? -42.948 53.733  56.055  1.00 27.19 ? 206  LYS   A C     1 
ATOM   1387  O  O     . LYS   A  1  208  ? -43.405 52.710  55.533  1.00 28.95 ? 206  LYS   A O     1 
ATOM   1388  C  CB    . LYS   A  1  208  ? -42.449 55.743  54.645  1.00 29.63 ? 206  LYS   A CB    1 
ATOM   1389  C  CG    . LYS   A  1  208  ? -43.051 56.868  53.818  1.00 35.03 ? 206  LYS   A CG    1 
ATOM   1390  C  CD    . LYS   A  1  208  ? -42.060 57.413  52.779  1.00 35.97 ? 206  LYS   A CD    1 
ATOM   1391  C  CE    . LYS   A  1  208  ? -42.647 58.619  52.048  1.00 38.41 ? 206  LYS   A CE    1 
ATOM   1392  N  NZ    . LYS   A  1  208  ? -41.740 59.159  50.992  1.00 52.63 ? 206  LYS   A NZ    1 
ATOM   1393  N  N     . ARG   A  1  209  ? -42.040 53.691  57.027  1.00 24.69 ? 207  ARG   A N     1 
ATOM   1394  C  CA    . ARG   A  1  209  ? -41.472 52.436  57.499  1.00 25.43 ? 207  ARG   A CA    1 
ATOM   1395  C  C     . ARG   A  1  209  ? -42.415 51.648  58.395  1.00 25.98 ? 207  ARG   A C     1 
ATOM   1396  O  O     . ARG   A  1  209  ? -42.118 50.493  58.711  1.00 28.71 ? 207  ARG   A O     1 
ATOM   1397  C  CB    . ARG   A  1  209  ? -40.166 52.705  58.235  1.00 26.46 ? 207  ARG   A CB    1 
ATOM   1398  C  CG    . ARG   A  1  209  ? -39.102 53.278  57.325  1.00 27.95 ? 207  ARG   A CG    1 
ATOM   1399  C  CD    . ARG   A  1  209  ? -37.832 53.532  58.079  1.00 28.48 ? 207  ARG   A CD    1 
ATOM   1400  N  NE    . ARG   A  1  209  ? -36.807 54.100  57.216  1.00 32.50 ? 207  ARG   A NE    1 
ATOM   1401  C  CZ    . ARG   A  1  209  ? -35.672 54.620  57.658  1.00 35.36 ? 207  ARG   A CZ    1 
ATOM   1402  N  NH1   . ARG   A  1  209  ? -35.404 54.692  58.952  1.00 31.47 ? 207  ARG   A NH1   1 
ATOM   1403  N  NH2   . ARG   A  1  209  ? -34.786 55.085  56.779  1.00 39.84 ? 207  ARG   A NH2   1 
ATOM   1404  N  N     . SER   A  1  210  ? -43.536 52.234  58.811  1.00 24.54 ? 208  SER   A N     1 
ATOM   1405  C  CA    . SER   A  1  210  ? -44.448 51.534  59.707  1.00 22.61 ? 208  SER   A CA    1 
ATOM   1406  C  C     . SER   A  1  210  ? -45.442 50.650  58.970  1.00 25.01 ? 208  SER   A C     1 
ATOM   1407  O  O     . SER   A  1  210  ? -46.066 49.789  59.596  1.00 24.53 ? 208  SER   A O     1 
ATOM   1408  C  CB    . SER   A  1  210  ? -45.207 52.551  60.561  1.00 22.84 ? 208  SER   A CB    1 
ATOM   1409  O  OG    . SER   A  1  210  ? -44.304 53.259  61.383  1.00 24.69 ? 208  SER   A OG    1 
ATOM   1410  N  N     . LYS   A  1  211  ? -45.588 50.830  57.656  1.00 28.40 ? 209  LYS   A N     1 
ATOM   1411  C  CA    . LYS   A  1  211  ? -46.628 50.117  56.924  1.00 29.08 ? 209  LYS   A CA    1 
ATOM   1412  C  C     . LYS   A  1  211  ? -46.413 48.610  56.971  1.00 27.27 ? 209  LYS   A C     1 
ATOM   1413  O  O     . LYS   A  1  211  ? -47.379 47.842  57.062  1.00 29.20 ? 209  LYS   A O     1 
ATOM   1414  C  CB    . LYS   A  1  211  ? -46.666 50.610  55.481  1.00 34.42 ? 209  LYS   A CB    1 
ATOM   1415  C  CG    . LYS   A  1  211  ? -46.898 52.105  55.371  1.00 37.38 ? 209  LYS   A CG    1 
ATOM   1416  C  CD    . LYS   A  1  211  ? -46.759 52.587  53.942  1.00 45.37 ? 209  LYS   A CD    1 
ATOM   1417  C  CE    . LYS   A  1  211  ? -47.245 54.016  53.822  1.00 48.80 ? 209  LYS   A CE    1 
ATOM   1418  N  NZ    . LYS   A  1  211  ? -48.585 54.158  54.464  1.00 51.79 ? 209  LYS   A NZ    1 
ATOM   1419  N  N     . GLU   A  1  212  ? -45.153 48.173  56.929  1.00 27.54 ? 210  GLU   A N     1 
ATOM   1420  C  CA    . GLU   A  1  212  ? -44.854 46.745  56.878  1.00 31.53 ? 210  GLU   A CA    1 
ATOM   1421  C  C     . GLU   A  1  212  ? -45.409 46.017  58.096  1.00 29.32 ? 210  GLU   A C     1 
ATOM   1422  O  O     . GLU   A  1  212  ? -46.127 45.020  57.965  1.00 30.61 ? 210  GLU   A O     1 
ATOM   1423  C  CB    . GLU   A  1  212  ? -43.346 46.536  56.764  1.00 33.95 ? 210  GLU   A CB    1 
ATOM   1424  C  CG    . GLU   A  1  212  ? -42.916 45.086  56.846  1.00 43.65 ? 210  GLU   A CG    1 
ATOM   1425  C  CD    . GLU   A  1  212  ? -41.412 44.947  56.923  1.00 49.00 ? 210  GLU   A CD    1 
ATOM   1426  O  OE1   . GLU   A  1  212  ? -40.720 45.981  56.804  1.00 52.72 ? 210  GLU   A OE1   1 
ATOM   1427  O  OE2   . GLU   A  1  212  ? -40.922 43.813  57.107  1.00 56.16 ? 210  GLU   A OE2   1 
ATOM   1428  N  N     . LEU   A  1  213  ? -45.106 46.512  59.295  1.00 27.26 ? 211  LEU   A N     1 
ATOM   1429  C  CA    . LEU   A  1  213  ? -45.623 45.851  60.488  1.00 27.00 ? 211  LEU   A CA    1 
ATOM   1430  C  C     . LEU   A  1  213  ? -47.093 46.159  60.738  1.00 27.70 ? 211  LEU   A C     1 
ATOM   1431  O  O     . LEU   A  1  213  ? -47.801 45.328  61.313  1.00 26.13 ? 211  LEU   A O     1 
ATOM   1432  C  CB    . LEU   A  1  213  ? -44.759 46.177  61.704  1.00 23.29 ? 211  LEU   A CB    1 
ATOM   1433  C  CG    . LEU   A  1  213  ? -43.384 45.510  61.617  1.00 27.96 ? 211  LEU   A CG    1 
ATOM   1434  C  CD1   . LEU   A  1  213  ? -42.537 45.786  62.845  1.00 32.71 ? 211  LEU   A CD1   1 
ATOM   1435  C  CD2   . LEU   A  1  213  ? -43.550 44.008  61.401  1.00 34.12 ? 211  LEU   A CD2   1 
ATOM   1436  N  N     . GLU   A  1  214  ? -47.585 47.322  60.308  1.00 23.93 ? 212  GLU   A N     1 
ATOM   1437  C  CA    . GLU   A  1  214  ? -49.018 47.566  60.442  1.00 26.68 ? 212  GLU   A CA    1 
ATOM   1438  C  C     . GLU   A  1  214  ? -49.818 46.540  59.655  1.00 29.98 ? 212  GLU   A C     1 
ATOM   1439  O  O     . GLU   A  1  214  ? -50.886 46.104  60.100  1.00 28.11 ? 212  GLU   A O     1 
ATOM   1440  C  CB    . GLU   A  1  214  ? -49.374 48.985  60.012  1.00 23.52 ? 212  GLU   A CB    1 
ATOM   1441  C  CG    . GLU   A  1  214  ? -48.957 50.029  61.030  1.00 24.13 ? 212  GLU   A CG    1 
ATOM   1442  C  CD    . GLU   A  1  214  ? -49.344 51.425  60.617  1.00 27.80 ? 212  GLU   A CD    1 
ATOM   1443  O  OE1   . GLU   A  1  214  ? -49.616 51.643  59.417  1.00 31.99 ? 212  GLU   A OE1   1 
ATOM   1444  O  OE2   . GLU   A  1  214  ? -49.374 52.311  61.496  1.00 29.81 ? 212  GLU   A OE2   1 
ATOM   1445  N  N     . GLU   A  1  215  ? -49.296 46.117  58.499  1.00 26.80 ? 213  GLU   A N     1 
ATOM   1446  C  CA    . GLU   A  1  215  ? -49.983 45.126  57.681  1.00 32.82 ? 213  GLU   A CA    1 
ATOM   1447  C  C     . GLU   A  1  215  ? -50.058 43.772  58.370  1.00 35.38 ? 213  GLU   A C     1 
ATOM   1448  O  O     . GLU   A  1  215  ? -50.951 42.977  58.056  1.00 39.87 ? 213  GLU   A O     1 
ATOM   1449  C  CB    . GLU   A  1  215  ? -49.291 44.993  56.322  1.00 33.67 ? 213  GLU   A CB    1 
ATOM   1450  N  N     . LYS   A  1  216  ? -49.154 43.501  59.306  1.00 31.39 ? 214  LYS   A N     1 
ATOM   1451  C  CA    . LYS   A  1  216  ? -49.151 42.260  60.066  1.00 32.10 ? 214  LYS   A CA    1 
ATOM   1452  C  C     . LYS   A  1  216  ? -49.978 42.333  61.344  1.00 32.97 ? 214  LYS   A C     1 
ATOM   1453  O  O     . LYS   A  1  216  ? -50.184 41.302  61.992  1.00 36.23 ? 214  LYS   A O     1 
ATOM   1454  C  CB    . LYS   A  1  216  ? -47.713 41.844  60.383  1.00 30.82 ? 214  LYS   A CB    1 
ATOM   1455  C  CG    . LYS   A  1  216  ? -46.881 41.604  59.140  1.00 34.99 ? 214  LYS   A CG    1 
ATOM   1456  C  CD    . LYS   A  1  216  ? -45.434 41.274  59.476  1.00 47.30 ? 214  LYS   A CD    1 
ATOM   1457  C  CE    . LYS   A  1  216  ? -44.576 41.265  58.221  1.00 48.77 ? 214  LYS   A CE    1 
ATOM   1458  N  NZ    . LYS   A  1  216  ? -45.144 40.364  57.185  1.00 50.06 ? 214  LYS   A NZ    1 
ATOM   1459  N  N     . GLY   A  1  217  ? -50.472 43.510  61.718  1.00 26.83 ? 215  GLY   A N     1 
ATOM   1460  C  CA    . GLY   A  1  217  ? -51.309 43.649  62.892  1.00 27.29 ? 215  GLY   A CA    1 
ATOM   1461  C  C     . GLY   A  1  217  ? -50.704 44.479  63.998  1.00 27.23 ? 215  GLY   A C     1 
ATOM   1462  O  O     . GLY   A  1  217  ? -51.318 44.598  65.065  1.00 27.89 ? 215  GLY   A O     1 
ATOM   1463  N  N     . PHE   A  1  218  ? -49.515 45.033  63.795  1.00 24.68 ? 216  PHE   A N     1 
ATOM   1464  C  CA    . PHE   A  1  218  ? -48.959 45.943  64.777  1.00 20.94 ? 216  PHE   A CA    1 
ATOM   1465  C  C     . PHE   A  1  218  ? -49.571 47.323  64.603  1.00 24.06 ? 216  PHE   A C     1 
ATOM   1466  O  O     . PHE   A  1  218  ? -50.130 47.664  63.555  1.00 23.84 ? 216  PHE   A O     1 
ATOM   1467  C  CB    . PHE   A  1  218  ? -47.440 46.074  64.611  1.00 20.34 ? 216  PHE   A CB    1 
ATOM   1468  C  CG    . PHE   A  1  218  ? -46.668 44.859  65.046  1.00 23.71 ? 216  PHE   A CG    1 
ATOM   1469  C  CD1   . PHE   A  1  218  ? -46.533 43.766  64.200  1.00 27.27 ? 216  PHE   A CD1   1 
ATOM   1470  C  CD2   . PHE   A  1  218  ? -46.061 44.820  66.288  1.00 23.87 ? 216  PHE   A CD2   1 
ATOM   1471  C  CE1   . PHE   A  1  218  ? -45.819 42.652  64.597  1.00 28.62 ? 216  PHE   A CE1   1 
ATOM   1472  C  CE2   . PHE   A  1  218  ? -45.342 43.707  66.691  1.00 25.56 ? 216  PHE   A CE2   1 
ATOM   1473  C  CZ    . PHE   A  1  218  ? -45.218 42.623  65.842  1.00 25.70 ? 216  PHE   A CZ    1 
ATOM   1474  N  N     . SER   A  1  219  ? -49.446 48.128  65.648  1.00 21.59 ? 217  SER   A N     1 
ATOM   1475  C  CA    . SER   A  1  219  ? -49.729 49.549  65.576  1.00 19.58 ? 217  SER   A CA    1 
ATOM   1476  C  C     . SER   A  1  219  ? -48.511 50.292  66.102  1.00 19.62 ? 217  SER   A C     1 
ATOM   1477  O  O     . SER   A  1  219  ? -47.521 49.682  66.514  1.00 17.61 ? 217  SER   A O     1 
ATOM   1478  C  CB    . SER   A  1  219  ? -50.994 49.913  66.362  1.00 22.17 ? 217  SER   A CB    1 
ATOM   1479  O  OG    . SER   A  1  219  ? -50.840 49.597  67.729  1.00 23.58 ? 217  SER   A OG    1 
ATOM   1480  N  N     . TYR   A  1  220  ? -48.588 51.622  66.090  1.00 18.36 ? 218  TYR   A N     1 
ATOM   1481  C  CA    . TYR   A  1  220  ? -47.449 52.461  66.427  1.00 18.43 ? 218  TYR   A CA    1 
ATOM   1482  C  C     . TYR   A  1  220  ? -47.870 53.591  67.347  1.00 17.40 ? 218  TYR   A C     1 
ATOM   1483  O  O     . TYR   A  1  220  ? -48.992 54.093  67.279  1.00 18.52 ? 218  TYR   A O     1 
ATOM   1484  C  CB    . TYR   A  1  220  ? -46.812 53.074  65.175  1.00 18.36 ? 218  TYR   A CB    1 
ATOM   1485  C  CG    . TYR   A  1  220  ? -45.909 52.099  64.502  1.00 17.83 ? 218  TYR   A CG    1 
ATOM   1486  C  CD1   . TYR   A  1  220  ? -46.411 51.149  63.620  1.00 22.08 ? 218  TYR   A CD1   1 
ATOM   1487  C  CD2   . TYR   A  1  220  ? -44.548 52.111  64.758  1.00 18.43 ? 218  TYR   A CD2   1 
ATOM   1488  C  CE1   . TYR   A  1  220  ? -45.576 50.236  63.012  1.00 22.95 ? 218  TYR   A CE1   1 
ATOM   1489  C  CE2   . TYR   A  1  220  ? -43.710 51.205  64.155  1.00 20.48 ? 218  TYR   A CE2   1 
ATOM   1490  C  CZ    . TYR   A  1  220  ? -44.224 50.276  63.285  1.00 21.98 ? 218  TYR   A CZ    1 
ATOM   1491  O  OH    . TYR   A  1  220  ? -43.373 49.373  62.695  1.00 23.03 ? 218  TYR   A OH    1 
ATOM   1492  N  N     . SER   A  1  221  ? -46.947 53.978  68.217  1.00 16.27 ? 219  SER   A N     1 
ATOM   1493  C  CA    . SER   A  1  221  ? -47.036 55.231  68.954  1.00 16.69 ? 219  SER   A CA    1 
ATOM   1494  C  C     . SER   A  1  221  ? -45.710 55.946  68.753  1.00 17.30 ? 219  SER   A C     1 
ATOM   1495  O  O     . SER   A  1  221  ? -44.658 55.424  69.131  1.00 20.82 ? 219  SER   A O     1 
ATOM   1496  C  CB    . SER   A  1  221  ? -47.274 54.989  70.445  1.00 17.60 ? 219  SER   A CB    1 
ATOM   1497  O  OG    . SER   A  1  221  ? -47.376 56.241  71.125  1.00 19.76 ? 219  SER   A OG    1 
ATOM   1498  N  N     . TYR   A  1  222  ? -45.752 57.131  68.172  1.00 14.94 ? 220  TYR   A N     1 
ATOM   1499  C  CA    . TYR   A  1  222  ? -44.512 57.800  67.802  1.00 16.73 ? 220  TYR   A CA    1 
ATOM   1500  C  C     . TYR   A  1  222  ? -44.038 58.734  68.902  1.00 18.43 ? 220  TYR   A C     1 
ATOM   1501  O  O     . TYR   A  1  222  ? -44.826 59.483  69.484  1.00 18.53 ? 220  TYR   A O     1 
ATOM   1502  C  CB    . TYR   A  1  222  ? -44.695 58.560  66.496  1.00 17.16 ? 220  TYR   A CB    1 
ATOM   1503  C  CG    . TYR   A  1  222  ? -45.019 57.613  65.372  1.00 16.40 ? 220  TYR   A CG    1 
ATOM   1504  C  CD1   . TYR   A  1  222  ? -44.021 56.895  64.735  1.00 16.90 ? 220  TYR   A CD1   1 
ATOM   1505  C  CD2   . TYR   A  1  222  ? -46.326 57.413  64.976  1.00 16.57 ? 220  TYR   A CD2   1 
ATOM   1506  C  CE1   . TYR   A  1  222  ? -44.325 56.008  63.718  1.00 19.07 ? 220  TYR   A CE1   1 
ATOM   1507  C  CE2   . TYR   A  1  222  ? -46.640 56.542  63.965  1.00 18.72 ? 220  TYR   A CE2   1 
ATOM   1508  C  CZ    . TYR   A  1  222  ? -45.639 55.841  63.343  1.00 19.38 ? 220  TYR   A CZ    1 
ATOM   1509  O  OH    . TYR   A  1  222  ? -45.960 54.975  62.339  1.00 21.16 ? 220  TYR   A OH    1 
ATOM   1510  N  N     . ASP   A  1  223  ? -42.734 58.702  69.151  1.00 20.00 ? 221  ASP   A N     1 
ATOM   1511  C  CA    . ASP   A  1  223  ? -42.070 59.516  70.160  1.00 21.74 ? 221  ASP   A CA    1 
ATOM   1512  C  C     . ASP   A  1  223  ? -41.106 60.449  69.444  1.00 23.79 ? 221  ASP   A C     1 
ATOM   1513  O  O     . ASP   A  1  223  ? -40.083 59.998  68.909  1.00 22.71 ? 221  ASP   A O     1 
ATOM   1514  C  CB    . ASP   A  1  223  ? -41.309 58.598  71.104  1.00 22.32 ? 221  ASP   A CB    1 
ATOM   1515  C  CG    . ASP   A  1  223  ? -40.366 59.350  72.038  1.00 28.38 ? 221  ASP   A CG    1 
ATOM   1516  O  OD1   . ASP   A  1  223  ? -40.566 60.562  72.278  1.00 30.40 ? 221  ASP   A OD1   1 
ATOM   1517  O  OD2   . ASP   A  1  223  ? -39.417 58.709  72.526  1.00 35.67 ? 221  ASP   A OD2   1 
ATOM   1518  N  N     . MET   A  1  224  ? -41.419 61.742  69.447  1.00 23.78 ? 222  MET   A N     1 
ATOM   1519  C  CA    . MET   A  1  224  ? -40.581 62.754  68.818  1.00 23.03 ? 222  MET   A CA    1 
ATOM   1520  C  C     . MET   A  1  224  ? -39.345 63.098  69.642  1.00 26.97 ? 222  MET   A C     1 
ATOM   1521  O  O     . MET   A  1  224  ? -38.600 64.006  69.258  1.00 31.56 ? 222  MET   A O     1 
ATOM   1522  C  CB    . MET   A  1  224  ? -41.395 64.006  68.493  1.00 24.63 ? 222  MET   A CB    1 
ATOM   1523  C  CG    . MET   A  1  224  ? -42.572 63.739  67.562  1.00 24.61 ? 222  MET   A CG    1 
ATOM   1524  S  SD    . MET   A  1  224  ? -42.118 62.793  66.081  1.00 30.41 ? 222  MET   A SD    1 
ATOM   1525  C  CE    . MET   A  1  224  ? -41.106 63.989  65.227  1.00 33.90 ? 222  MET   A CE    1 
ATOM   1526  N  N     . LEU   A  1  225  ? -39.124 62.391  70.747  1.00 29.54 ? 223  LEU   A N     1 
ATOM   1527  C  CA    . LEU   A  1  225  ? -37.902 62.420  71.547  1.00 31.61 ? 223  LEU   A CA    1 
ATOM   1528  C  C     . LEU   A  1  225  ? -37.713 63.711  72.339  1.00 32.51 ? 223  LEU   A C     1 
ATOM   1529  O  O     . LEU   A  1  225  ? -36.656 63.898  72.947  1.00 34.32 ? 223  LEU   A O     1 
ATOM   1530  C  CB    . LEU   A  1  225  ? -36.646 62.045  70.743  1.00 31.50 ? 223  LEU   A CB    1 
ATOM   1531  C  CG    . LEU   A  1  225  ? -36.531 60.580  70.281  1.00 29.28 ? 223  LEU   A CG    1 
ATOM   1532  C  CD1   . LEU   A  1  225  ? -35.366 60.407  69.309  1.00 32.78 ? 223  LEU   A CD1   1 
ATOM   1533  C  CD2   . LEU   A  1  225  ? -36.375 59.611  71.463  1.00 30.16 ? 223  LEU   A CD2   1 
ATOM   1534  N  N     . GLY   A  1  226  ? -38.708 64.593  72.368  1.00 27.57 ? 224  GLY   A N     1 
ATOM   1535  C  CA    . GLY   A  1  226  ? -38.627 65.756  73.234  1.00 31.66 ? 224  GLY   A CA    1 
ATOM   1536  C  C     . GLY   A  1  226  ? -38.679 65.352  74.699  1.00 30.39 ? 224  GLY   A C     1 
ATOM   1537  O  O     . GLY   A  1  226  ? -39.399 64.430  75.087  1.00 25.56 ? 224  GLY   A O     1 
ATOM   1538  N  N     . GLU   A  1  227  ? -37.904 66.058  75.522  1.00 26.47 ? 225  GLU   A N     1 
ATOM   1539  C  CA    . GLU   A  1  227  ? -37.844 65.729  76.938  1.00 23.01 ? 225  GLU   A CA    1 
ATOM   1540  C  C     . GLU   A  1  227  ? -37.038 66.799  77.649  1.00 22.63 ? 225  GLU   A C     1 
ATOM   1541  O  O     . GLU   A  1  227  ? -36.071 67.321  77.089  1.00 21.61 ? 225  GLU   A O     1 
ATOM   1542  C  CB    . GLU   A  1  227  ? -37.162 64.373  77.113  1.00 28.88 ? 225  GLU   A CB    1 
ATOM   1543  C  CG    . GLU   A  1  227  ? -37.037 63.903  78.519  1.00 30.66 ? 225  GLU   A CG    1 
ATOM   1544  C  CD    . GLU   A  1  227  ? -36.541 62.474  78.580  1.00 35.75 ? 225  GLU   A CD    1 
ATOM   1545  O  OE1   . GLU   A  1  227  ? -36.440 61.835  77.504  1.00 30.86 ? 225  GLU   A OE1   1 
ATOM   1546  O  OE2   . GLU   A  1  227  ? -36.253 61.998  79.696  1.00 38.68 ? 225  GLU   A OE2   1 
ATOM   1547  N  N     . ALA   A  1  228  ? -37.450 67.125  78.873  1.00 22.10 ? 226  ALA   A N     1 
ATOM   1548  C  CA    . ALA   A  1  228  ? -36.667 67.976  79.760  1.00 21.13 ? 226  ALA   A CA    1 
ATOM   1549  C  C     . ALA   A  1  228  ? -36.284 69.295  79.080  1.00 18.51 ? 226  ALA   A C     1 
ATOM   1550  O  O     . ALA   A  1  228  ? -35.105 69.621  78.916  1.00 22.09 ? 226  ALA   A O     1 
ATOM   1551  C  CB    . ALA   A  1  228  ? -35.428 67.230  80.261  1.00 25.15 ? 226  ALA   A CB    1 
ATOM   1552  N  N     . ALA   A  1  229  ? -37.301 70.064  78.697  1.00 18.07 ? 227  ALA   A N     1 
ATOM   1553  C  CA    . ALA   A  1  229  ? -37.050 71.408  78.187  1.00 19.19 ? 227  ALA   A CA    1 
ATOM   1554  C  C     . ALA   A  1  229  ? -36.302 72.237  79.226  1.00 19.30 ? 227  ALA   A C     1 
ATOM   1555  O  O     . ALA   A  1  229  ? -36.637 72.230  80.415  1.00 18.47 ? 227  ALA   A O     1 
ATOM   1556  C  CB    . ALA   A  1  229  ? -38.365 72.099  77.833  1.00 18.92 ? 227  ALA   A CB    1 
ATOM   1557  N  N     . THR   A  1  230  ? -35.283 72.953  78.766  1.00 18.51 ? 228  THR   A N     1 
ATOM   1558  C  CA    . THR   A  1  230  ? -34.493 73.819  79.626  1.00 19.53 ? 228  THR   A CA    1 
ATOM   1559  C  C     . THR   A  1  230  ? -34.906 75.274  79.519  1.00 18.15 ? 228  THR   A C     1 
ATOM   1560  O  O     . THR   A  1  230  ? -34.746 76.034  80.478  1.00 18.38 ? 228  THR   A O     1 
ATOM   1561  C  CB    . THR   A  1  230  ? -33.011 73.681  79.250  1.00 20.69 ? 228  THR   A CB    1 
ATOM   1562  O  OG1   . THR   A  1  230  ? -32.636 72.297  79.328  1.00 29.11 ? 228  THR   A OG1   1 
ATOM   1563  C  CG2   . THR   A  1  230  ? -32.137 74.488  80.189  1.00 25.91 ? 228  THR   A CG2   1 
ATOM   1564  N  N     . THR   A  1  231  ? -35.456 75.675  78.383  1.00 18.45 ? 229  THR   A N     1 
ATOM   1565  C  CA    . THR   A  1  231  ? -35.827 77.057  78.130  1.00 16.51 ? 229  THR   A CA    1 
ATOM   1566  C  C     . THR   A  1  231  ? -37.227 77.081  77.539  1.00 16.76 ? 229  THR   A C     1 
ATOM   1567  O  O     . THR   A  1  231  ? -37.738 76.061  77.071  1.00 17.94 ? 229  THR   A O     1 
ATOM   1568  C  CB    . THR   A  1  231  ? -34.872 77.703  77.115  1.00 19.72 ? 229  THR   A CB    1 
ATOM   1569  O  OG1   . THR   A  1  231  ? -35.085 77.115  75.822  1.00 19.45 ? 229  THR   A OG1   1 
ATOM   1570  C  CG2   . THR   A  1  231  ? -33.408 77.496  77.525  1.00 19.93 ? 229  THR   A CG2   1 
ATOM   1571  N  N     . ALA   A  1  232  ? -37.830 78.266  77.565  1.00 16.54 ? 230  ALA   A N     1 
ATOM   1572  C  CA    . ALA   A  1  232  ? -39.090 78.464  76.854  1.00 17.99 ? 230  ALA   A CA    1 
ATOM   1573  C  C     . ALA   A  1  232  ? -38.947 78.100  75.381  1.00 20.12 ? 230  ALA   A C     1 
ATOM   1574  O  O     . ALA   A  1  232  ? -39.846 77.487  74.794  1.00 20.56 ? 230  ALA   A O     1 
ATOM   1575  C  CB    . ALA   A  1  232  ? -39.541 79.916  77.000  1.00 21.55 ? 230  ALA   A CB    1 
ATOM   1576  N  N     . ALA   A  1  233  ? -37.818 78.452  74.764  1.00 19.50 ? 231  ALA   A N     1 
ATOM   1577  C  CA    . ALA   A  1  233  ? -37.641 78.151  73.347  1.00 23.68 ? 231  ALA   A CA    1 
ATOM   1578  C  C     . ALA   A  1  233  ? -37.615 76.650  73.098  1.00 21.89 ? 231  ALA   A C     1 
ATOM   1579  O  O     . ALA   A  1  233  ? -38.172 76.178  72.100  1.00 22.16 ? 231  ALA   A O     1 
ATOM   1580  C  CB    . ALA   A  1  233  ? -36.373 78.807  72.806  1.00 23.29 ? 231  ALA   A CB    1 
ATOM   1581  N  N     . ASP   A  1  234  ? -36.979 75.884  73.992  1.00 19.43 ? 232  ASP   A N     1 
ATOM   1582  C  CA    . ASP   A  1  234  ? -36.978 74.428  73.866  1.00 21.71 ? 232  ASP   A CA    1 
ATOM   1583  C  C     . ASP   A  1  234  ? -38.393 73.897  73.934  1.00 20.47 ? 232  ASP   A C     1 
ATOM   1584  O  O     . ASP   A  1  234  ? -38.781 73.024  73.154  1.00 20.13 ? 232  ASP   A O     1 
ATOM   1585  C  CB    . ASP   A  1  234  ? -36.216 73.775  75.020  1.00 24.03 ? 232  ASP   A CB    1 
ATOM   1586  C  CG    . ASP   A  1  234  ? -34.731 73.963  74.952  1.00 31.01 ? 232  ASP   A CG    1 
ATOM   1587  O  OD1   . ASP   A  1  234  ? -34.183 74.229  73.863  1.00 29.65 ? 232  ASP   A OD1   1 
ATOM   1588  O  OD2   . ASP   A  1  234  ? -34.109 73.806  76.029  1.00 31.26 ? 232  ASP   A OD2   1 
ATOM   1589  N  N     . ALA   A  1  235  ? -39.160 74.372  74.915  1.00 19.34 ? 233  ALA   A N     1 
ATOM   1590  C  CA    . ALA   A  1  235  ? -40.523 73.893  75.083  1.00 17.67 ? 233  ALA   A CA    1 
ATOM   1591  C  C     . ALA   A  1  235  ? -41.363 74.213  73.858  1.00 20.23 ? 233  ALA   A C     1 
ATOM   1592  O  O     . ALA   A  1  235  ? -42.182 73.390  73.426  1.00 18.64 ? 233  ALA   A O     1 
ATOM   1593  C  CB    . ALA   A  1  235  ? -41.141 74.497  76.344  1.00 18.69 ? 233  ALA   A CB    1 
ATOM   1594  N  N     . GLU   A  1  236  ? -41.168 75.403  73.277  1.00 19.13 ? 234  GLU   A N     1 
ATOM   1595  C  CA    . GLU   A  1  236  ? -41.890 75.739  72.054  1.00 19.96 ? 234  GLU   A CA    1 
ATOM   1596  C  C     . GLU   A  1  236  ? -41.474 74.834  70.905  1.00 17.86 ? 234  GLU   A C     1 
ATOM   1597  O  O     . GLU   A  1  236  ? -42.315 74.417  70.103  1.00 19.75 ? 234  GLU   A O     1 
ATOM   1598  C  CB    . GLU   A  1  236  ? -41.667 77.207  71.683  1.00 22.95 ? 234  GLU   A CB    1 
ATOM   1599  C  CG    . GLU   A  1  236  ? -42.340 78.180  72.617  1.00 29.91 ? 234  GLU   A CG    1 
ATOM   1600  C  CD    . GLU   A  1  236  ? -41.662 79.539  72.663  1.00 41.50 ? 234  GLU   A CD    1 
ATOM   1601  O  OE1   . GLU   A  1  236  ? -40.876 79.851  71.739  1.00 43.69 ? 234  GLU   A OE1   1 
ATOM   1602  O  OE2   . GLU   A  1  236  ? -41.907 80.292  73.633  1.00 44.97 ? 234  GLU   A OE2   1 
ATOM   1603  N  N     . ARG   A  1  237  ? -40.181 74.533  70.800  1.00 17.85 ? 235  ARG   A N     1 
ATOM   1604  C  CA    . ARG   A  1  237  ? -39.723 73.648  69.735  1.00 20.95 ? 235  ARG   A CA    1 
ATOM   1605  C  C     . ARG   A  1  237  ? -40.319 72.257  69.895  1.00 21.14 ? 235  ARG   A C     1 
ATOM   1606  O  O     . ARG   A  1  237  ? -40.794 71.657  68.927  1.00 18.96 ? 235  ARG   A O     1 
ATOM   1607  C  CB    . ARG   A  1  237  ? -38.194 73.588  69.717  1.00 21.98 ? 235  ARG   A CB    1 
ATOM   1608  C  CG    . ARG   A  1  237  ? -37.627 72.668  68.652  1.00 28.56 ? 235  ARG   A CG    1 
ATOM   1609  C  CD    . ARG   A  1  237  ? -36.138 72.923  68.461  1.00 34.39 ? 235  ARG   A CD    1 
ATOM   1610  N  NE    . ARG   A  1  237  ? -35.430 72.852  69.733  1.00 41.51 ? 235  ARG   A NE    1 
ATOM   1611  C  CZ    . ARG   A  1  237  ? -34.920 71.741  70.242  1.00 41.35 ? 235  ARG   A CZ    1 
ATOM   1612  N  NH1   . ARG   A  1  237  ? -34.984 70.590  69.590  1.00 44.75 ? 235  ARG   A NH1   1 
ATOM   1613  N  NH2   . ARG   A  1  237  ? -34.334 71.784  71.435  1.00 38.18 ? 235  ARG   A NH2   1 
ATOM   1614  N  N     . TYR   A  1  238  ? -40.329 71.735  71.118  1.00 17.25 ? 236  TYR   A N     1 
ATOM   1615  C  CA    . TYR   A  1  238  ? -40.911 70.419  71.315  1.00 18.07 ? 236  TYR   A CA    1 
ATOM   1616  C  C     . TYR   A  1  238  ? -42.404 70.447  71.039  1.00 16.88 ? 236  TYR   A C     1 
ATOM   1617  O  O     . TYR   A  1  238  ? -42.951 69.491  70.479  1.00 19.39 ? 236  TYR   A O     1 
ATOM   1618  C  CB    . TYR   A  1  238  ? -40.624 69.931  72.731  1.00 16.63 ? 236  TYR   A CB    1 
ATOM   1619  C  CG    . TYR   A  1  238  ? -39.170 69.643  72.998  1.00 16.45 ? 236  TYR   A CG    1 
ATOM   1620  C  CD1   . TYR   A  1  238  ? -38.365 69.082  72.023  1.00 22.27 ? 236  TYR   A CD1   1 
ATOM   1621  C  CD2   . TYR   A  1  238  ? -38.611 69.928  74.230  1.00 17.95 ? 236  TYR   A CD2   1 
ATOM   1622  C  CE1   . TYR   A  1  238  ? -37.036 68.813  72.266  1.00 25.20 ? 236  TYR   A CE1   1 
ATOM   1623  C  CE2   . TYR   A  1  238  ? -37.292 69.660  74.485  1.00 21.54 ? 236  TYR   A CE2   1 
ATOM   1624  C  CZ    . TYR   A  1  238  ? -36.510 69.104  73.502  1.00 24.54 ? 236  TYR   A CZ    1 
ATOM   1625  O  OH    . TYR   A  1  238  ? -35.186 68.838  73.766  1.00 27.68 ? 236  TYR   A OH    1 
ATOM   1626  N  N     . TYR   A  1  239  ? -43.075 71.537  71.418  1.00 16.78 ? 237  TYR   A N     1 
ATOM   1627  C  CA    . TYR   A  1  239  ? -44.492 71.662  71.112  1.00 17.67 ? 237  TYR   A CA    1 
ATOM   1628  C  C     . TYR   A  1  239  ? -44.723 71.589  69.612  1.00 18.71 ? 237  TYR   A C     1 
ATOM   1629  O  O     . TYR   A  1  239  ? -45.581 70.835  69.145  1.00 17.24 ? 237  TYR   A O     1 
ATOM   1630  C  CB    . TYR   A  1  239  ? -45.064 72.970  71.655  1.00 17.34 ? 237  TYR   A CB    1 
ATOM   1631  C  CG    . TYR   A  1  239  ? -46.512 73.100  71.292  1.00 17.61 ? 237  TYR   A CG    1 
ATOM   1632  C  CD1   . TYR   A  1  239  ? -46.903 73.655  70.078  1.00 20.86 ? 237  TYR   A CD1   1 
ATOM   1633  C  CD2   . TYR   A  1  239  ? -47.497 72.635  72.145  1.00 18.81 ? 237  TYR   A CD2   1 
ATOM   1634  C  CE1   . TYR   A  1  239  ? -48.237 73.745  69.729  1.00 23.54 ? 237  TYR   A CE1   1 
ATOM   1635  C  CE2   . TYR   A  1  239  ? -48.821 72.725  71.813  1.00 19.81 ? 237  TYR   A CE2   1 
ATOM   1636  C  CZ    . TYR   A  1  239  ? -49.193 73.280  70.608  1.00 22.36 ? 237  TYR   A CZ    1 
ATOM   1637  O  OH    . TYR   A  1  239  ? -50.520 73.375  70.262  1.00 25.90 ? 237  TYR   A OH    1 
ATOM   1638  N  N     . ARG   A  1  240  ? -43.996 72.399  68.840  1.00 18.91 ? 238  ARG   A N     1 
ATOM   1639  C  CA    . ARG   A  1  240  ? -44.292 72.411  67.413  1.00 19.21 ? 238  ARG   A CA    1 
ATOM   1640  C  C     . ARG   A  1  240  ? -43.897 71.094  66.757  1.00 16.98 ? 238  ARG   A C     1 
ATOM   1641  O  O     . ARG   A  1  240  ? -44.504 70.699  65.759  1.00 18.56 ? 238  ARG   A O     1 
ATOM   1642  C  CB    . ARG   A  1  240  ? -43.679 73.631  66.719  1.00 20.88 ? 238  ARG   A CB    1 
ATOM   1643  C  CG    . ARG   A  1  240  ? -42.196 73.615  66.665  1.00 22.17 ? 238  ARG   A CG    1 
ATOM   1644  C  CD    . ARG   A  1  240  ? -41.685 74.825  65.877  1.00 22.35 ? 238  ARG   A CD    1 
ATOM   1645  N  NE    . ARG   A  1  240  ? -40.254 75.000  66.064  1.00 24.07 ? 238  ARG   A NE    1 
ATOM   1646  C  CZ    . ARG   A  1  240  ? -39.709 75.842  66.936  1.00 26.33 ? 238  ARG   A CZ    1 
ATOM   1647  N  NH1   . ARG   A  1  240  ? -40.452 76.652  67.681  1.00 24.28 ? 238  ARG   A NH1   1 
ATOM   1648  N  NH2   . ARG   A  1  240  ? -38.386 75.881  67.056  1.00 30.49 ? 238  ARG   A NH2   1 
ATOM   1649  N  N     . ASP   A  1  241  ? -42.906 70.386  67.313  1.00 18.05 ? 239  ASP   A N     1 
ATOM   1650  C  CA    . ASP   A  1  241  ? -42.585 69.049  66.820  1.00 18.69 ? 239  ASP   A CA    1 
ATOM   1651  C  C     . ASP   A  1  241  ? -43.735 68.082  67.074  1.00 19.01 ? 239  ASP   A C     1 
ATOM   1652  O  O     . ASP   A  1  241  ? -44.101 67.291  66.198  1.00 18.66 ? 239  ASP   A O     1 
ATOM   1653  C  CB    . ASP   A  1  241  ? -41.329 68.524  67.504  1.00 23.31 ? 239  ASP   A CB    1 
ATOM   1654  C  CG    . ASP   A  1  241  ? -40.062 69.215  67.029  1.00 29.92 ? 239  ASP   A CG    1 
ATOM   1655  O  OD1   . ASP   A  1  241  ? -40.130 70.083  66.125  1.00 32.39 ? 239  ASP   A OD1   1 
ATOM   1656  O  OD2   . ASP   A  1  241  ? -38.992 68.886  67.581  1.00 37.27 ? 239  ASP   A OD2   1 
ATOM   1657  N  N     . TYR   A  1  242  ? -44.315 68.124  68.275  1.00 17.37 ? 240  TYR   A N     1 
ATOM   1658  C  CA    . TYR   A  1  242  ? -45.474 67.283  68.552  1.00 16.32 ? 240  TYR   A CA    1 
ATOM   1659  C  C     . TYR   A  1  242  ? -46.644 67.646  67.654  1.00 14.63 ? 240  TYR   A C     1 
ATOM   1660  O  O     . TYR   A  1  242  ? -47.329 66.765  67.120  1.00 15.64 ? 240  TYR   A O     1 
ATOM   1661  C  CB    . TYR   A  1  242  ? -45.915 67.460  70.001  1.00 15.03 ? 240  TYR   A CB    1 
ATOM   1662  C  CG    . TYR   A  1  242  ? -45.036 66.836  71.042  1.00 14.69 ? 240  TYR   A CG    1 
ATOM   1663  C  CD1   . TYR   A  1  242  ? -44.417 65.617  70.826  1.00 16.40 ? 240  TYR   A CD1   1 
ATOM   1664  C  CD2   . TYR   A  1  242  ? -44.881 67.446  72.270  1.00 16.63 ? 240  TYR   A CD2   1 
ATOM   1665  C  CE1   . TYR   A  1  242  ? -43.621 65.045  71.816  1.00 18.04 ? 240  TYR   A CE1   1 
ATOM   1666  C  CE2   . TYR   A  1  242  ? -44.097 66.893  73.249  1.00 15.30 ? 240  TYR   A CE2   1 
ATOM   1667  C  CZ    . TYR   A  1  242  ? -43.490 65.685  73.028  1.00 15.58 ? 240  TYR   A CZ    1 
ATOM   1668  O  OH    . TYR   A  1  242  ? -42.696 65.141  74.018  1.00 17.23 ? 240  TYR   A OH    1 
ATOM   1669  N  N     . GLU   A  1  243  ? -46.906 68.942  67.502  1.00 13.84 ? 241  GLU   A N     1 
ATOM   1670  C  CA    . GLU   A  1  243  ? -48.039 69.373  66.703  1.00 15.62 ? 241  GLU   A CA    1 
ATOM   1671  C  C     . GLU   A  1  243  ? -47.871 68.929  65.257  1.00 16.86 ? 241  GLU   A C     1 
ATOM   1672  O  O     . GLU   A  1  243  ? -48.813 68.405  64.652  1.00 16.41 ? 241  GLU   A O     1 
ATOM   1673  C  CB    . GLU   A  1  243  ? -48.181 70.892  66.810  1.00 18.05 ? 241  GLU   A CB    1 
ATOM   1674  C  CG    . GLU   A  1  243  ? -49.262 71.483  65.937  1.00 21.64 ? 241  GLU   A CG    1 
ATOM   1675  C  CD    . GLU   A  1  243  ? -49.147 73.003  65.844  1.00 23.14 ? 241  GLU   A CD    1 
ATOM   1676  O  OE1   . GLU   A  1  243  ? -48.009 73.537  65.893  1.00 32.91 ? 241  GLU   A OE1   1 
ATOM   1677  O  OE2   . GLU   A  1  243  ? -50.189 73.649  65.702  1.00 24.54 ? 241  GLU   A OE2   1 
ATOM   1678  N  N     . SER   A  1  244  ? -46.669 69.094  64.704  1.00 17.67 ? 242  SER   A N     1 
ATOM   1679  C  CA    . SER   A  1  244  ? -46.444 68.675  63.323  1.00 18.01 ? 242  SER   A CA    1 
ATOM   1680  C  C     . SER   A  1  244  ? -46.541 67.160  63.188  1.00 17.50 ? 242  SER   A C     1 
ATOM   1681  O  O     . SER   A  1  244  ? -47.070 66.651  62.190  1.00 18.90 ? 242  SER   A O     1 
ATOM   1682  C  CB    . SER   A  1  244  ? -45.094 69.196  62.813  1.00 18.59 ? 242  SER   A CB    1 
ATOM   1683  O  OG    . SER   A  1  244  ? -44.020 68.689  63.575  1.00 24.25 ? 242  SER   A OG    1 
ATOM   1684  N  N     . ALA   A  1  245  ? -46.059 66.423  64.189  1.00 16.91 ? 243  ALA   A N     1 
ATOM   1685  C  CA    . ALA   A  1  245  ? -46.182 64.968  64.157  1.00 16.38 ? 243  ALA   A CA    1 
ATOM   1686  C  C     . ALA   A  1  245  ? -47.639 64.525  64.229  1.00 17.39 ? 243  ALA   A C     1 
ATOM   1687  O  O     . ALA   A  1  245  ? -48.038 63.592  63.532  1.00 17.33 ? 243  ALA   A O     1 
ATOM   1688  C  CB    . ALA   A  1  245  ? -45.353 64.347  65.279  1.00 18.14 ? 243  ALA   A CB    1 
ATOM   1689  N  N     . ILE   A  1  246  ? -48.446 65.159  65.085  1.00 15.71 ? 244  ILE   A N     1 
ATOM   1690  C  CA    . ILE   A  1  246  ? -49.861 64.794  65.145  1.00 16.13 ? 244  ILE   A CA    1 
ATOM   1691  C  C     . ILE   A  1  246  ? -50.512 64.941  63.781  1.00 18.19 ? 244  ILE   A C     1 
ATOM   1692  O  O     . ILE   A  1  246  ? -51.279 64.075  63.351  1.00 18.99 ? 244  ILE   A O     1 
ATOM   1693  C  CB    . ILE   A  1  246  ? -50.597 65.598  66.223  1.00 15.49 ? 244  ILE   A CB    1 
ATOM   1694  C  CG1   . ILE   A  1  246  ? -50.105 65.154  67.601  1.00 15.32 ? 244  ILE   A CG1   1 
ATOM   1695  C  CG2   . ILE   A  1  246  ? -52.105 65.395  66.090  1.00 16.60 ? 244  ILE   A CG2   1 
ATOM   1696  C  CD1   . ILE   A  1  246  ? -50.538 66.071  68.729  1.00 18.23 ? 244  ILE   A CD1   1 
ATOM   1697  N  N     . HIS   A  1  247  ? -50.204 66.029  63.069  1.00 16.78 ? 245  HIS   A N     1 
ATOM   1698  C  CA    . HIS   A  1  247  ? -50.773 66.192  61.737  1.00 17.18 ? 245  HIS   A CA    1 
ATOM   1699  C  C     . HIS   A  1  247  ? -50.354 65.046  60.832  1.00 16.85 ? 245  HIS   A C     1 
ATOM   1700  O  O     . HIS   A  1  247  ? -51.184 64.460  60.130  1.00 18.69 ? 245  HIS   A O     1 
ATOM   1701  C  CB    . HIS   A  1  247  ? -50.349 67.531  61.130  1.00 17.73 ? 245  HIS   A CB    1 
ATOM   1702  C  CG    . HIS   A  1  247  ? -51.062 68.707  61.712  1.00 19.54 ? 245  HIS   A CG    1 
ATOM   1703  N  ND1   . HIS   A  1  247  ? -52.415 68.906  61.559  1.00 19.32 ? 245  HIS   A ND1   1 
ATOM   1704  C  CD2   . HIS   A  1  247  ? -50.607 69.759  62.434  1.00 21.48 ? 245  HIS   A CD2   1 
ATOM   1705  C  CE1   . HIS   A  1  247  ? -52.768 70.022  62.170  1.00 22.71 ? 245  HIS   A CE1   1 
ATOM   1706  N  NE2   . HIS   A  1  247  ? -51.691 70.552  62.717  1.00 19.71 ? 245  HIS   A NE2   1 
ATOM   1707  N  N     . ALA   A  1  248  ? -49.066 64.710  60.838  1.00 16.08 ? 246  ALA   A N     1 
ATOM   1708  C  CA    . ALA   A  1  248  ? -48.587 63.666  59.945  1.00 17.93 ? 246  ALA   A CA    1 
ATOM   1709  C  C     . ALA   A  1  248  ? -49.178 62.316  60.325  1.00 20.01 ? 246  ALA   A C     1 
ATOM   1710  O  O     . ALA   A  1  248  ? -49.616 61.557  59.456  1.00 18.05 ? 246  ALA   A O     1 
ATOM   1711  C  CB    . ALA   A  1  248  ? -47.058 63.629  59.955  1.00 18.70 ? 246  ALA   A CB    1 
ATOM   1712  N  N     . ILE   A  1  249  ? -49.231 62.023  61.623  1.00 17.85 ? 247  ILE   A N     1 
ATOM   1713  C  CA    . ILE   A  1  249  ? -49.794 60.761  62.091  1.00 16.62 ? 247  ILE   A CA    1 
ATOM   1714  C  C     . ILE   A  1  249  ? -51.286 60.711  61.815  1.00 17.96 ? 247  ILE   A C     1 
ATOM   1715  O  O     . ILE   A  1  249  ? -51.821 59.678  61.400  1.00 18.67 ? 247  ILE   A O     1 
ATOM   1716  C  CB    . ILE   A  1  249  ? -49.506 60.598  63.591  1.00 15.02 ? 247  ILE   A CB    1 
ATOM   1717  C  CG1   . ILE   A  1  249  ? -47.998 60.489  63.826  1.00 16.57 ? 247  ILE   A CG1   1 
ATOM   1718  C  CG2   . ILE   A  1  249  ? -50.216 59.371  64.154  1.00 18.26 ? 247  ILE   A CG2   1 
ATOM   1719  C  CD1   . ILE   A  1  249  ? -47.591 60.782  65.282  1.00 17.25 ? 247  ILE   A CD1   1 
ATOM   1720  N  N     . GLY   A  1  250  ? -51.986 61.817  62.064  1.00 16.31 ? 248  GLY   A N     1 
ATOM   1721  C  CA    . GLY   A  1  250  ? -53.415 61.829  61.833  1.00 16.73 ? 248  GLY   A CA    1 
ATOM   1722  C  C     . GLY   A  1  250  ? -53.756 61.701  60.363  1.00 19.17 ? 248  GLY   A C     1 
ATOM   1723  O  O     . GLY   A  1  250  ? -54.723 61.026  60.000  1.00 19.16 ? 248  GLY   A O     1 
ATOM   1724  N  N     . LYS   A  1  251  ? -52.974 62.356  59.498  1.00 17.40 ? 249  LYS   A N     1 
ATOM   1725  C  CA    . LYS   A  1  251  ? -53.190 62.210  58.062  1.00 19.32 ? 249  LYS   A CA    1 
ATOM   1726  C  C     . LYS   A  1  251  ? -52.988 60.769  57.641  1.00 21.07 ? 249  LYS   A C     1 
ATOM   1727  O  O     . LYS   A  1  251  ? -53.707 60.261  56.774  1.00 21.11 ? 249  LYS   A O     1 
ATOM   1728  C  CB    . LYS   A  1  251  ? -52.210 63.083  57.280  1.00 19.56 ? 249  LYS   A CB    1 
ATOM   1729  C  CG    . LYS   A  1  251  ? -52.487 64.558  57.279  1.00 21.68 ? 249  LYS   A CG    1 
ATOM   1730  C  CD    . LYS   A  1  251  ? -51.295 65.244  56.631  1.00 23.21 ? 249  LYS   A CD    1 
ATOM   1731  C  CE    . LYS   A  1  251  ? -51.317 66.742  56.804  1.00 23.93 ? 249  LYS   A CE    1 
ATOM   1732  N  NZ    . LYS   A  1  251  ? -50.029 67.302  56.262  1.00 24.24 ? 249  LYS   A NZ    1 
ATOM   1733  N  N     . ALA   A  1  252  ? -52.000 60.099  58.238  1.00 18.30 ? 250  ALA   A N     1 
ATOM   1734  C  CA    . ALA   A  1  252  ? -51.698 58.722  57.874  1.00 19.61 ? 250  ALA   A CA    1 
ATOM   1735  C  C     . ALA   A  1  252  ? -52.692 57.768  58.499  1.00 21.55 ? 250  ALA   A C     1 
ATOM   1736  O  O     . ALA   A  1  252  ? -53.036 56.744  57.901  1.00 21.46 ? 250  ALA   A O     1 
ATOM   1737  C  CB    . ALA   A  1  252  ? -50.295 58.353  58.340  1.00 22.89 ? 250  ALA   A CB    1 
ATOM   1738  N  N     . SER   A  1  253  ? -53.139 58.075  59.716  1.00 20.46 ? 251  SER   A N     1 
ATOM   1739  C  CA    . SER   A  1  253  ? -54.132 57.226  60.351  1.00 19.34 ? 251  SER   A CA    1 
ATOM   1740  C  C     . SER   A  1  253  ? -55.351 57.090  59.464  1.00 21.94 ? 251  SER   A C     1 
ATOM   1741  O  O     . SER   A  1  253  ? -55.893 55.991  59.312  1.00 20.56 ? 251  SER   A O     1 
ATOM   1742  C  CB    . SER   A  1  253  ? -54.532 57.804  61.700  1.00 20.16 ? 251  SER   A CB    1 
ATOM   1743  O  OG    . SER   A  1  253  ? -55.529 56.995  62.281  1.00 22.72 ? 251  SER   A OG    1 
ATOM   1744  N  N     . ALA   A  1  254  ? -55.764 58.192  58.843  1.00 20.31 ? 252  ALA   A N     1 
ATOM   1745  C  CA    . ALA   A  1  254  ? -56.838 58.197  57.853  1.00 22.87 ? 252  ALA   A CA    1 
ATOM   1746  C  C     . ALA   A  1  254  ? -58.091 57.501  58.376  1.00 25.03 ? 252  ALA   A C     1 
ATOM   1747  O  O     . ALA   A  1  254  ? -58.704 56.664  57.705  1.00 23.87 ? 252  ALA   A O     1 
ATOM   1748  C  CB    . ALA   A  1  254  ? -56.377 57.612  56.518  1.00 27.57 ? 252  ALA   A CB    1 
ATOM   1749  N  N     . GLY   A  1  255  ? -58.472 57.850  59.598  1.00 23.14 ? 253  GLY   A N     1 
ATOM   1750  C  CA    . GLY   A  1  255  ? -59.701 57.334  60.152  1.00 23.63 ? 253  GLY   A CA    1 
ATOM   1751  C  C     . GLY   A  1  255  ? -59.632 55.947  60.748  1.00 21.85 ? 253  GLY   A C     1 
ATOM   1752  O  O     . GLY   A  1  255  ? -60.681 55.388  61.066  1.00 25.15 ? 253  GLY   A O     1 
ATOM   1753  N  N     . ARG   A  1  256  ? -58.439 55.370  60.923  1.00 21.97 ? 254  ARG   A N     1 
ATOM   1754  C  CA    . ARG   A  1  256  ? -58.358 54.039  61.518  1.00 21.45 ? 254  ARG   A CA    1 
ATOM   1755  C  C     . ARG   A  1  256  ? -58.719 54.037  62.993  1.00 21.97 ? 254  ARG   A C     1 
ATOM   1756  O  O     . ARG   A  1  256  ? -58.971 52.968  63.552  1.00 22.28 ? 254  ARG   A O     1 
ATOM   1757  C  CB    . ARG   A  1  256  ? -56.965 53.441  61.327  1.00 21.88 ? 254  ARG   A CB    1 
ATOM   1758  C  CG    . ARG   A  1  256  ? -56.772 52.764  59.986  1.00 27.31 ? 254  ARG   A CG    1 
ATOM   1759  C  CD    . ARG   A  1  256  ? -55.353 52.266  59.837  1.00 27.60 ? 254  ARG   A CD    1 
ATOM   1760  N  NE    . ARG   A  1  256  ? -54.432 53.359  59.568  1.00 24.84 ? 254  ARG   A NE    1 
ATOM   1761  C  CZ    . ARG   A  1  256  ? -53.113 53.228  59.532  1.00 26.43 ? 254  ARG   A CZ    1 
ATOM   1762  N  NH1   . ARG   A  1  256  ? -52.528 52.074  59.807  1.00 27.04 ? 254  ARG   A NH1   1 
ATOM   1763  N  NH2   . ARG   A  1  256  ? -52.366 54.276  59.200  1.00 23.59 ? 254  ARG   A NH2   1 
ATOM   1764  N  N     . GLY   A  1  257  ? -58.732 55.197  63.639  1.00 20.46 ? 255  GLY   A N     1 
ATOM   1765  C  CA    . GLY   A  1  257  ? -59.119 55.261  65.032  1.00 19.57 ? 255  GLY   A CA    1 
ATOM   1766  C  C     . GLY   A  1  257  ? -57.978 54.967  65.985  1.00 17.95 ? 255  GLY   A C     1 
ATOM   1767  O  O     . GLY   A  1  257  ? -56.838 54.691  65.611  1.00 19.95 ? 255  GLY   A O     1 
ATOM   1768  N  N     . ILE   A  1  258  ? -58.312 55.020  67.269  1.00 17.06 ? 256  ILE   A N     1 
ATOM   1769  C  CA    . ILE   A  1  258  ? -57.276 55.042  68.292  1.00 17.58 ? 256  ILE   A CA    1 
ATOM   1770  C  C     . ILE   A  1  258  ? -56.680 53.675  68.590  1.00 19.61 ? 256  ILE   A C     1 
ATOM   1771  O  O     . ILE   A  1  258  ? -55.586 53.603  69.165  1.00 18.00 ? 256  ILE   A O     1 
ATOM   1772  C  CB    . ILE   A  1  258  ? -57.787 55.705  69.576  1.00 16.51 ? 256  ILE   A CB    1 
ATOM   1773  C  CG1   . ILE   A  1  258  ? -58.927 54.888  70.196  1.00 18.57 ? 256  ILE   A CG1   1 
ATOM   1774  C  CG2   . ILE   A  1  258  ? -58.202 57.172  69.291  1.00 16.78 ? 256  ILE   A CG2   1 
ATOM   1775  C  CD1   . ILE   A  1  258  ? -59.453 55.490  71.462  1.00 21.21 ? 256  ILE   A CD1   1 
ATOM   1776  N  N     . TYR   A  1  259  ? -57.351 52.587  68.219  1.00 19.06 ? 257  TYR   A N     1 
ATOM   1777  C  CA    . TYR   A  1  259  ? -56.845 51.249  68.510  1.00 19.44 ? 257  TYR   A CA    1 
ATOM   1778  C  C     . TYR   A  1  259  ? -56.087 50.628  67.345  1.00 23.06 ? 257  TYR   A C     1 
ATOM   1779  O  O     . TYR   A  1  259  ? -54.967 50.150  67.536  1.00 24.86 ? 257  TYR   A O     1 
ATOM   1780  C  CB    . TYR   A  1  259  ? -57.976 50.326  68.976  1.00 21.95 ? 257  TYR   A CB    1 
ATOM   1781  C  CG    . TYR   A  1  259  ? -58.779 50.919  70.102  1.00 20.15 ? 257  TYR   A CG    1 
ATOM   1782  C  CD1   . TYR   A  1  259  ? -58.191 51.193  71.329  1.00 21.58 ? 257  TYR   A CD1   1 
ATOM   1783  C  CD2   . TYR   A  1  259  ? -60.127 51.223  69.937  1.00 21.41 ? 257  TYR   A CD2   1 
ATOM   1784  C  CE1   . TYR   A  1  259  ? -58.919 51.745  72.360  1.00 20.81 ? 257  TYR   A CE1   1 
ATOM   1785  C  CE2   . TYR   A  1  259  ? -60.860 51.778  70.967  1.00 24.77 ? 257  TYR   A CE2   1 
ATOM   1786  C  CZ    . TYR   A  1  259  ? -60.248 52.036  72.175  1.00 21.12 ? 257  TYR   A CZ    1 
ATOM   1787  O  OH    . TYR   A  1  259  ? -60.959 52.596  73.209  1.00 21.64 ? 257  TYR   A OH    1 
ATOM   1788  N  N     . GLU   A  1  260  ? -56.655 50.651  66.135  1.00 20.75 ? 258  GLU   A N     1 
ATOM   1789  C  CA    . GLU   A  1  260  ? -55.937 50.118  64.982  1.00 26.25 ? 258  GLU   A CA    1 
ATOM   1790  C  C     . GLU   A  1  260  ? -54.912 51.105  64.453  1.00 25.42 ? 258  GLU   A C     1 
ATOM   1791  O  O     . GLU   A  1  260  ? -53.868 50.697  63.928  1.00 29.83 ? 258  GLU   A O     1 
ATOM   1792  C  CB    . GLU   A  1  260  ? -56.907 49.771  63.850  1.00 27.28 ? 258  GLU   A CB    1 
ATOM   1793  C  CG    . GLU   A  1  260  ? -56.225 49.038  62.689  1.00 35.64 ? 258  GLU   A CG    1 
ATOM   1794  C  CD    . GLU   A  1  260  ? -57.034 49.043  61.400  1.00 41.00 ? 258  GLU   A CD    1 
ATOM   1795  O  OE1   . GLU   A  1  260  ? -58.282 49.038  61.468  1.00 43.98 ? 258  GLU   A OE1   1 
ATOM   1796  O  OE2   . GLU   A  1  260  ? -56.411 49.052  60.314  1.00 41.46 ? 258  GLU   A OE2   1 
ATOM   1797  N  N     . GLY   A  1  261  ? -55.181 52.397  64.598  1.00 20.11 ? 259  GLY   A N     1 
ATOM   1798  C  CA    . GLY   A  1  261  ? -54.367 53.417  63.996  1.00 19.78 ? 259  GLY   A CA    1 
ATOM   1799  C  C     . GLY   A  1  261  ? -53.273 53.898  64.921  1.00 20.48 ? 259  GLY   A C     1 
ATOM   1800  O  O     . GLY   A  1  261  ? -53.267 53.626  66.125  1.00 19.05 ? 259  GLY   A O     1 
ATOM   1801  N  N     . PRO   A  1  262  ? -52.314 54.620  64.355  1.00 16.59 ? 260  PRO   A N     1 
ATOM   1802  C  CA    . PRO   A  1  262  ? -51.157 55.072  65.131  1.00 17.33 ? 260  PRO   A CA    1 
ATOM   1803  C  C     . PRO   A  1  262  ? -51.517 56.228  66.045  1.00 17.77 ? 260  PRO   A C     1 
ATOM   1804  O  O     . PRO   A  1  262  ? -52.533 56.904  65.881  1.00 20.93 ? 260  PRO   A O     1 
ATOM   1805  C  CB    . PRO   A  1  262  ? -50.182 55.539  64.048  1.00 18.58 ? 260  PRO   A CB    1 
ATOM   1806  C  CG    . PRO   A  1  262  ? -51.099 55.988  62.923  1.00 21.27 ? 260  PRO   A CG    1 
ATOM   1807  C  CD    . PRO   A  1  262  ? -52.221 55.001  62.936  1.00 18.50 ? 260  PRO   A CD    1 
ATOM   1808  N  N     . GLY   A  1  263  ? -50.662 56.429  67.040  1.00 17.01 ? 261  GLY   A N     1 
ATOM   1809  C  CA    . GLY   A  1  263  ? -50.825 57.516  67.977  1.00 18.29 ? 261  GLY   A CA    1 
ATOM   1810  C  C     . GLY   A  1  263  ? -49.498 58.194  68.244  1.00 15.92 ? 261  GLY   A C     1 
ATOM   1811  O  O     . GLY   A  1  263  ? -48.493 57.898  67.585  1.00 16.70 ? 261  GLY   A O     1 
ATOM   1812  N  N     . ILE   A  1  264  ? -49.495 59.125  69.191  1.00 16.33 ? 262  ILE   A N     1 
ATOM   1813  C  CA    . ILE   A  1  264  ? -48.296 59.849  69.574  1.00 16.70 ? 262  ILE   A CA    1 
ATOM   1814  C  C     . ILE   A  1  264  ? -48.122 59.721  71.079  1.00 16.88 ? 262  ILE   A C     1 
ATOM   1815  O  O     . ILE   A  1  264  ? -49.091 59.534  71.825  1.00 15.70 ? 262  ILE   A O     1 
ATOM   1816  C  CB    . ILE   A  1  264  ? -48.377 61.329  69.133  1.00 16.39 ? 262  ILE   A CB    1 
ATOM   1817  C  CG1   . ILE   A  1  264  ? -47.004 61.977  69.205  1.00 17.72 ? 262  ILE   A CG1   1 
ATOM   1818  C  CG2   . ILE   A  1  264  ? -49.377 62.108  69.996  1.00 17.50 ? 262  ILE   A CG2   1 
ATOM   1819  C  CD1   . ILE   A  1  264  ? -46.982 63.383  68.610  1.00 20.26 ? 262  ILE   A CD1   1 
ATOM   1820  N  N     . SER   A  1  265  ? -46.871 59.770  71.521  1.00 15.19 ? 263  SER   A N     1 
ATOM   1821  C  CA    . SER   A  1  265  ? -46.546 59.834  72.937  1.00 16.65 ? 263  SER   A CA    1 
ATOM   1822  C  C     . SER   A  1  265  ? -45.799 61.133  73.189  1.00 18.71 ? 263  SER   A C     1 
ATOM   1823  O  O     . SER   A  1  265  ? -44.946 61.529  72.384  1.00 19.77 ? 263  SER   A O     1 
ATOM   1824  C  CB    . SER   A  1  265  ? -45.684 58.654  73.384  1.00 18.85 ? 263  SER   A CB    1 
ATOM   1825  O  OG    . SER   A  1  265  ? -46.426 57.445  73.368  1.00 21.15 ? 263  SER   A OG    1 
ATOM   1826  N  N     . ILE   A  1  266  ? -46.133 61.795  74.298  1.00 16.62 ? 264  ILE   A N     1 
ATOM   1827  C  CA    . ILE   A  1  266  ? -45.536 63.071  74.677  1.00 17.06 ? 264  ILE   A CA    1 
ATOM   1828  C  C     . ILE   A  1  266  ? -45.001 62.973  76.098  1.00 15.56 ? 264  ILE   A C     1 
ATOM   1829  O  O     . ILE   A  1  266  ? -45.433 62.140  76.897  1.00 15.67 ? 264  ILE   A O     1 
ATOM   1830  C  CB    . ILE   A  1  266  ? -46.508 64.263  74.557  1.00 17.78 ? 264  ILE   A CB    1 
ATOM   1831  C  CG1   . ILE   A  1  266  ? -47.623 64.191  75.609  1.00 18.10 ? 264  ILE   A CG1   1 
ATOM   1832  C  CG2   . ILE   A  1  266  ? -47.097 64.339  73.151  1.00 16.76 ? 264  ILE   A CG2   1 
ATOM   1833  C  CD1   . ILE   A  1  266  ? -48.393 65.493  75.723  1.00 20.28 ? 264  ILE   A CD1   1 
ATOM   1834  N  N     . LYS   A  1  267  ? -44.031 63.828  76.402  1.00 15.79 ? 265  LYS   A N     1 
ATOM   1835  C  CA    . LYS   A  1  267  ? -43.530 63.978  77.758  1.00 14.79 ? 265  LYS   A CA    1 
ATOM   1836  C  C     . LYS   A  1  267  ? -43.852 65.381  78.229  1.00 16.68 ? 265  LYS   A C     1 
ATOM   1837  O  O     . LYS   A  1  267  ? -43.543 66.356  77.540  1.00 16.08 ? 265  LYS   A O     1 
ATOM   1838  C  CB    . LYS   A  1  267  ? -42.018 63.757  77.806  1.00 17.83 ? 265  LYS   A CB    1 
ATOM   1839  C  CG    . LYS   A  1  267  ? -41.657 62.289  77.665  1.00 20.15 ? 265  LYS   A CG    1 
ATOM   1840  C  CD    . LYS   A  1  267  ? -40.160 62.088  77.575  1.00 25.56 ? 265  LYS   A CD    1 
ATOM   1841  C  CE    . LYS   A  1  267  ? -39.864 60.622  77.365  1.00 30.02 ? 265  LYS   A CE    1 
ATOM   1842  N  NZ    . LYS   A  1  267  ? -40.623 60.091  76.200  1.00 31.86 ? 265  LYS   A NZ    1 
ATOM   1843  N  N     . LEU   A  1  268  ? -44.500 65.484  79.383  1.00 13.96 ? 266  LEU   A N     1 
ATOM   1844  C  CA    . LEU   A  1  268  ? -44.832 66.805  79.894  1.00 15.67 ? 266  LEU   A CA    1 
ATOM   1845  C  C     . LEU   A  1  268  ? -43.590 67.644  80.135  1.00 15.59 ? 266  LEU   A C     1 
ATOM   1846  O  O     . LEU   A  1  268  ? -43.637 68.869  79.993  1.00 16.02 ? 266  LEU   A O     1 
ATOM   1847  C  CB    . LEU   A  1  268  ? -45.640 66.684  81.182  1.00 15.91 ? 266  LEU   A CB    1 
ATOM   1848  C  CG    . LEU   A  1  268  ? -46.971 65.952  80.996  1.00 17.53 ? 266  LEU   A CG    1 
ATOM   1849  C  CD1   . LEU   A  1  268  ? -47.714 65.843  82.311  1.00 20.03 ? 266  LEU   A CD1   1 
ATOM   1850  C  CD2   . LEU   A  1  268  ? -47.838 66.631  79.943  1.00 20.48 ? 266  LEU   A CD2   1 
ATOM   1851  N  N     . SER   A  1  269  ? -42.470 67.015  80.498  1.00 15.70 ? 267  SER   A N     1 
ATOM   1852  C  CA    . SER   A  1  269  ? -41.260 67.786  80.734  1.00 16.80 ? 267  SER   A CA    1 
ATOM   1853  C  C     . SER   A  1  269  ? -40.745 68.448  79.465  1.00 17.19 ? 267  SER   A C     1 
ATOM   1854  O  O     . SER   A  1  269  ? -39.951 69.386  79.557  1.00 17.28 ? 267  SER   A O     1 
ATOM   1855  C  CB    . SER   A  1  269  ? -40.153 66.919  81.332  1.00 17.81 ? 267  SER   A CB    1 
ATOM   1856  O  OG    . SER   A  1  269  ? -39.601 66.040  80.366  1.00 18.92 ? 267  SER   A OG    1 
ATOM   1857  N  N     . ALA   A  1  270  ? -41.147 67.952  78.290  1.00 14.61 ? 268  ALA   A N     1 
ATOM   1858  C  CA    . ALA   A  1  270  ? -40.765 68.604  77.041  1.00 17.75 ? 268  ALA   A CA    1 
ATOM   1859  C  C     . ALA   A  1  270  ? -41.514 69.906  76.815  1.00 16.18 ? 268  ALA   A C     1 
ATOM   1860  O  O     . ALA   A  1  270  ? -41.059 70.749  76.034  1.00 16.52 ? 268  ALA   A O     1 
ATOM   1861  C  CB    . ALA   A  1  270  ? -41.048 67.667  75.862  1.00 18.40 ? 268  ALA   A CB    1 
ATOM   1862  N  N     . LEU   A  1  271  ? -42.653 70.089  77.464  1.00 15.78 ? 269  LEU   A N     1 
ATOM   1863  C  CA    . LEU   A  1  271  ? -43.565 71.159  77.113  1.00 16.09 ? 269  LEU   A CA    1 
ATOM   1864  C  C     . LEU   A  1  271  ? -43.498 72.333  78.066  1.00 15.69 ? 269  LEU   A C     1 
ATOM   1865  O  O     . LEU   A  1  271  ? -44.188 73.331  77.849  1.00 18.08 ? 269  LEU   A O     1 
ATOM   1866  C  CB    . LEU   A  1  271  ? -44.986 70.628  77.020  1.00 17.16 ? 269  LEU   A CB    1 
ATOM   1867  C  CG    . LEU   A  1  271  ? -45.167 69.656  75.867  1.00 18.64 ? 269  LEU   A CG    1 
ATOM   1868  C  CD1   . LEU   A  1  271  ? -46.548 69.046  75.990  1.00 19.89 ? 269  LEU   A CD1   1 
ATOM   1869  C  CD2   . LEU   A  1  271  ? -45.035 70.439  74.582  1.00 18.69 ? 269  LEU   A CD2   1 
ATOM   1870  N  N     . HIS   A  1  272  ? -42.663 72.248  79.101  1.00 16.67 ? 270  HIS   A N     1 
ATOM   1871  C  CA    . HIS   A  1  272  ? -42.494 73.417  79.943  1.00 16.23 ? 270  HIS   A CA    1 
ATOM   1872  C  C     . HIS   A  1  272  ? -41.147 73.282  80.624  1.00 16.37 ? 270  HIS   A C     1 
ATOM   1873  O  O     . HIS   A  1  272  ? -40.813 72.189  81.097  1.00 17.09 ? 270  HIS   A O     1 
ATOM   1874  C  CB    . HIS   A  1  272  ? -43.595 73.513  80.997  1.00 17.65 ? 270  HIS   A CB    1 
ATOM   1875  C  CG    . HIS   A  1  272  ? -43.692 74.866  81.615  1.00 20.29 ? 270  HIS   A CG    1 
ATOM   1876  N  ND1   . HIS   A  1  272  ? -42.777 75.328  82.536  1.00 21.23 ? 270  HIS   A ND1   1 
ATOM   1877  C  CD2   . HIS   A  1  272  ? -44.576 75.872  81.422  1.00 23.45 ? 270  HIS   A CD2   1 
ATOM   1878  C  CE1   . HIS   A  1  272  ? -43.095 76.563  82.884  1.00 21.08 ? 270  HIS   A CE1   1 
ATOM   1879  N  NE2   . HIS   A  1  272  ? -44.188 76.913  82.228  1.00 23.75 ? 270  HIS   A NE2   1 
ATOM   1880  N  N     . PRO   A  1  273  ? -40.362 74.353  80.707  1.00 18.21 ? 271  PRO   A N     1 
ATOM   1881  C  CA    . PRO   A  1  273  ? -39.049 74.252  81.351  1.00 17.24 ? 271  PRO   A CA    1 
ATOM   1882  C  C     . PRO   A  1  273  ? -39.096 74.188  82.865  1.00 18.59 ? 271  PRO   A C     1 
ATOM   1883  O  O     . PRO   A  1  273  ? -38.058 73.931  83.476  1.00 18.57 ? 271  PRO   A O     1 
ATOM   1884  C  CB    . PRO   A  1  273  ? -38.343 75.531  80.894  1.00 18.32 ? 271  PRO   A CB    1 
ATOM   1885  C  CG    . PRO   A  1  273  ? -39.443 76.504  80.735  1.00 20.18 ? 271  PRO   A CG    1 
ATOM   1886  C  CD    . PRO   A  1  273  ? -40.610 75.702  80.172  1.00 19.38 ? 271  PRO   A CD    1 
ATOM   1887  N  N     . ARG   A  1  274  ? -40.244 74.397  83.494  1.00 15.85 ? 272  ARG   A N     1 
ATOM   1888  C  CA    . ARG   A  1  274  ? -40.350 74.320  84.947  1.00 17.96 ? 272  ARG   A CA    1 
ATOM   1889  C  C     . ARG   A  1  274  ? -41.461 73.367  85.338  1.00 19.31 ? 272  ARG   A C     1 
ATOM   1890  O  O     . ARG   A  1  274  ? -42.377 73.702  86.094  1.00 19.17 ? 272  ARG   A O     1 
ATOM   1891  C  CB    . ARG   A  1  274  ? -40.582 75.684  85.578  1.00 17.97 ? 272  ARG   A CB    1 
ATOM   1892  C  CG    . ARG   A  1  274  ? -39.448 76.665  85.327  1.00 17.83 ? 272  ARG   A CG    1 
ATOM   1893  C  CD    . ARG   A  1  274  ? -38.102 76.141  85.871  1.00 19.09 ? 272  ARG   A CD    1 
ATOM   1894  N  NE    . ARG   A  1  274  ? -38.162 75.723  87.270  1.00 20.08 ? 272  ARG   A NE    1 
ATOM   1895  C  CZ    . ARG   A  1  274  ? -38.100 76.555  88.307  1.00 18.13 ? 272  ARG   A CZ    1 
ATOM   1896  N  NH1   . ARG   A  1  274  ? -38.032 77.865  88.140  1.00 20.68 ? 272  ARG   A NH1   1 
ATOM   1897  N  NH2   . ARG   A  1  274  ? -38.119 76.060  89.541  1.00 21.78 ? 272  ARG   A NH2   1 
ATOM   1898  N  N     . TYR   A  1  275  ? -41.394 72.153  84.804  1.00 17.51 ? 273  TYR   A N     1 
ATOM   1899  C  CA    . TYR   A  1  275  ? -42.394 71.136  85.101  1.00 15.64 ? 273  TYR   A CA    1 
ATOM   1900  C  C     . TYR   A  1  275  ? -42.003 70.473  86.419  1.00 16.90 ? 273  TYR   A C     1 
ATOM   1901  O  O     . TYR   A  1  275  ? -41.200 69.539  86.466  1.00 18.34 ? 273  TYR   A O     1 
ATOM   1902  C  CB    . TYR   A  1  275  ? -42.473 70.145  83.944  1.00 16.56 ? 273  TYR   A CB    1 
ATOM   1903  C  CG    . TYR   A  1  275  ? -43.394 68.999  84.221  1.00 16.46 ? 273  TYR   A CG    1 
ATOM   1904  C  CD1   . TYR   A  1  275  ? -44.687 69.225  84.662  1.00 16.69 ? 273  TYR   A CD1   1 
ATOM   1905  C  CD2   . TYR   A  1  275  ? -42.974 67.685  84.036  1.00 16.03 ? 273  TYR   A CD2   1 
ATOM   1906  C  CE1   . TYR   A  1  275  ? -45.533 68.167  84.934  1.00 19.06 ? 273  TYR   A CE1   1 
ATOM   1907  C  CE2   . TYR   A  1  275  ? -43.813 66.626  84.302  1.00 17.19 ? 273  TYR   A CE2   1 
ATOM   1908  C  CZ    . TYR   A  1  275  ? -45.091 66.879  84.750  1.00 17.91 ? 273  TYR   A CZ    1 
ATOM   1909  O  OH    . TYR   A  1  275  ? -45.937 65.836  85.024  1.00 20.03 ? 273  TYR   A OH    1 
ATOM   1910  N  N     . SER   A  1  276  ? -42.571 70.981  87.508  1.00 16.57 ? 274  SER   A N     1 
ATOM   1911  C  CA    . SER   A  1  276  ? -42.278 70.449  88.828  1.00 13.97 ? 274  SER   A CA    1 
ATOM   1912  C  C     . SER   A  1  276  ? -43.378 70.883  89.776  1.00 16.18 ? 274  SER   A C     1 
ATOM   1913  O  O     . SER   A  1  276  ? -44.086 71.860  89.523  1.00 18.18 ? 274  SER   A O     1 
ATOM   1914  C  CB    . SER   A  1  276  ? -40.933 70.958  89.349  1.00 20.24 ? 274  SER   A CB    1 
ATOM   1915  O  OG    . SER   A  1  276  ? -41.033 72.333  89.679  1.00 24.21 ? 274  SER   A OG    1 
ATOM   1916  N  N     . ARG   A  1  277  ? -43.499 70.137  90.880  1.00 16.85 ? 275  ARG   A N     1 
ATOM   1917  C  CA    . ARG   A  1  277  ? -44.499 70.470  91.886  1.00 16.28 ? 275  ARG   A CA    1 
ATOM   1918  C  C     . ARG   A  1  277  ? -44.279 71.875  92.442  1.00 17.66 ? 275  ARG   A C     1 
ATOM   1919  O  O     . ARG   A  1  277  ? -45.239 72.586  92.734  1.00 17.93 ? 275  ARG   A O     1 
ATOM   1920  C  CB    . ARG   A  1  277  ? -44.504 69.428  93.011  1.00 17.73 ? 275  ARG   A CB    1 
ATOM   1921  C  CG    . ARG   A  1  277  ? -45.397 69.778  94.211  1.00 17.70 ? 275  ARG   A CG    1 
ATOM   1922  C  CD    . ARG   A  1  277  ? -46.863 69.975  93.816  1.00 18.03 ? 275  ARG   A CD    1 
ATOM   1923  N  NE    . ARG   A  1  277  ? -47.690 70.303  94.973  1.00 17.23 ? 275  ARG   A NE    1 
ATOM   1924  C  CZ    . ARG   A  1  277  ? -47.856 71.531  95.450  1.00 17.03 ? 275  ARG   A CZ    1 
ATOM   1925  N  NH1   . ARG   A  1  277  ? -47.218 72.568  94.929  1.00 18.40 ? 275  ARG   A NH1   1 
ATOM   1926  N  NH2   . ARG   A  1  277  ? -48.680 71.725  96.479  1.00 19.03 ? 275  ARG   A NH2   1 
ATOM   1927  N  N     . ALA   A  1  278  ? -43.023 72.293  92.594  1.00 18.35 ? 276  ALA   A N     1 
ATOM   1928  C  CA    . ALA   A  1  278  ? -42.770 73.627  93.135  1.00 18.82 ? 276  ALA   A CA    1 
ATOM   1929  C  C     . ALA   A  1  278  ? -43.337 74.707  92.235  1.00 18.64 ? 276  ALA   A C     1 
ATOM   1930  O  O     . ALA   A  1  278  ? -43.672 75.797  92.705  1.00 20.64 ? 276  ALA   A O     1 
ATOM   1931  C  CB    . ALA   A  1  278  ? -41.269 73.849  93.331  1.00 19.18 ? 276  ALA   A CB    1 
ATOM   1932  N  N     . GLN   A  1  279  ? -43.464 74.421  90.942  1.00 16.49 ? 277  GLN   A N     1 
ATOM   1933  C  CA    . GLN   A  1  279  ? -43.992 75.375  89.979  1.00 15.49 ? 277  GLN   A CA    1 
ATOM   1934  C  C     . GLN   A  1  279  ? -45.371 74.956  89.491  1.00 19.27 ? 277  GLN   A C     1 
ATOM   1935  O  O     . GLN   A  1  279  ? -45.739 75.231  88.349  1.00 17.06 ? 277  GLN   A O     1 
ATOM   1936  C  CB    . GLN   A  1  279  ? -43.026 75.521  88.801  1.00 19.80 ? 277  GLN   A CB    1 
ATOM   1937  C  CG    . GLN   A  1  279  ? -41.643 76.025  89.189  1.00 19.15 ? 277  GLN   A CG    1 
ATOM   1938  C  CD    . GLN   A  1  279  ? -41.710 77.402  89.810  1.00 22.09 ? 277  GLN   A CD    1 
ATOM   1939  O  OE1   . GLN   A  1  279  ? -42.545 78.227  89.434  1.00 29.19 ? 277  GLN   A OE1   1 
ATOM   1940  N  NE2   . GLN   A  1  279  ? -40.871 77.639  90.808  1.00 20.18 ? 277  GLN   A NE2   1 
ATOM   1941  N  N     . ALA   A  1  280  ? -46.144 74.294  90.358  1.00 17.18 ? 278  ALA   A N     1 
ATOM   1942  C  CA    . ALA   A  1  280  ? -47.442 73.752  89.954  1.00 19.70 ? 278  ALA   A CA    1 
ATOM   1943  C  C     . ALA   A  1  280  ? -48.337 74.807  89.328  1.00 18.89 ? 278  ALA   A C     1 
ATOM   1944  O  O     . ALA   A  1  280  ? -49.064 74.517  88.372  1.00 18.70 ? 278  ALA   A O     1 
ATOM   1945  C  CB    . ALA   A  1  280  ? -48.157 73.126  91.152  1.00 19.90 ? 278  ALA   A CB    1 
ATOM   1946  N  N     . ALA   A  1  281  ? -48.336 76.025  89.871  1.00 17.14 ? 279  ALA   A N     1 
ATOM   1947  C  CA    . ALA   A  1  281  ? -49.203 77.060  89.319  1.00 19.43 ? 279  ALA   A CA    1 
ATOM   1948  C  C     . ALA   A  1  281  ? -48.828 77.374  87.877  1.00 20.12 ? 279  ALA   A C     1 
ATOM   1949  O  O     . ALA   A  1  281  ? -49.706 77.524  87.016  1.00 20.30 ? 279  ALA   A O     1 
ATOM   1950  C  CB    . ALA   A  1  281  ? -49.146 78.325  90.179  1.00 23.55 ? 279  ALA   A CB    1 
ATOM   1951  N  N     . ARG   A  1  282  ? -47.529 77.475  87.590  1.00 17.53 ? 280  ARG   A N     1 
ATOM   1952  C  CA    . ARG   A  1  282  ? -47.135 77.706  86.205  1.00 17.84 ? 280  ARG   A CA    1 
ATOM   1953  C  C     . ARG   A  1  282  ? -47.454 76.506  85.333  1.00 17.90 ? 280  ARG   A C     1 
ATOM   1954  O  O     . ARG   A  1  282  ? -47.798 76.669  84.158  1.00 17.97 ? 280  ARG   A O     1 
ATOM   1955  C  CB    . ARG   A  1  282  ? -45.640 78.014  86.118  1.00 19.16 ? 280  ARG   A CB    1 
ATOM   1956  C  CG    . ARG   A  1  282  ? -45.250 79.333  86.761  1.00 21.74 ? 280  ARG   A CG    1 
ATOM   1957  C  CD    . ARG   A  1  282  ? -43.826 79.672  86.356  1.00 22.94 ? 280  ARG   A CD    1 
ATOM   1958  N  NE    . ARG   A  1  282  ? -43.752 79.807  84.909  1.00 21.86 ? 280  ARG   A NE    1 
ATOM   1959  C  CZ    . ARG   A  1  282  ? -42.626 79.798  84.209  1.00 23.34 ? 280  ARG   A CZ    1 
ATOM   1960  N  NH1   . ARG   A  1  282  ? -41.446 79.645  84.796  1.00 20.85 ? 280  ARG   A NH1   1 
ATOM   1961  N  NH2   . ARG   A  1  282  ? -42.685 79.946  82.888  1.00 22.03 ? 280  ARG   A NH2   1 
ATOM   1962  N  N     . VAL   A  1  283  ? -47.348 75.299  85.887  1.00 17.19 ? 281  VAL   A N     1 
ATOM   1963  C  CA    . VAL   A  1  283  ? -47.652 74.095  85.119  1.00 16.64 ? 281  VAL   A CA    1 
ATOM   1964  C  C     . VAL   A  1  283  ? -49.116 74.086  84.703  1.00 18.02 ? 281  VAL   A C     1 
ATOM   1965  O  O     . VAL   A  1  283  ? -49.453 73.854  83.537  1.00 17.74 ? 281  VAL   A O     1 
ATOM   1966  C  CB    . VAL   A  1  283  ? -47.287 72.843  85.930  1.00 16.33 ? 281  VAL   A CB    1 
ATOM   1967  C  CG1   . VAL   A  1  283  ? -47.881 71.598  85.282  1.00 20.14 ? 281  VAL   A CG1   1 
ATOM   1968  C  CG2   . VAL   A  1  283  ? -45.771 72.722  86.044  1.00 17.77 ? 281  VAL   A CG2   1 
ATOM   1969  N  N     . MET   A  1  284  ? -50.011 74.350  85.649  1.00 17.23 ? 282  MET   A N     1 
ATOM   1970  C  CA    . MET   A  1  284  ? -51.427 74.360  85.302  1.00 17.54 ? 282  MET   A CA    1 
ATOM   1971  C  C     . MET   A  1  284  ? -51.779 75.542  84.412  1.00 19.09 ? 282  MET   A C     1 
ATOM   1972  O  O     . MET   A  1  284  ? -52.683 75.441  83.574  1.00 22.05 ? 282  MET   A O     1 
ATOM   1973  C  CB    . MET   A  1  284  ? -52.260 74.377  86.577  1.00 18.80 ? 282  MET   A CB    1 
ATOM   1974  C  CG    . MET   A  1  284  ? -51.956 73.205  87.494  1.00 20.35 ? 282  MET   A CG    1 
ATOM   1975  S  SD    . MET   A  1  284  ? -52.191 71.576  86.766  1.00 23.58 ? 282  MET   A SD    1 
ATOM   1976  C  CE    . MET   A  1  284  ? -53.929 71.625  86.329  1.00 22.08 ? 282  MET   A CE    1 
ATOM   1977  N  N     . GLY   A  1  285  ? -51.084 76.666  84.571  1.00 17.20 ? 283  GLY   A N     1 
ATOM   1978  C  CA    . GLY   A  1  285  ? -51.430 77.843  83.801  1.00 18.54 ? 283  GLY   A CA    1 
ATOM   1979  C  C     . GLY   A  1  285  ? -50.854 77.834  82.406  1.00 19.69 ? 283  GLY   A C     1 
ATOM   1980  O  O     . GLY   A  1  285  ? -51.464 78.380  81.481  1.00 21.03 ? 283  GLY   A O     1 
ATOM   1981  N  N     . GLU   A  1  286  ? -49.693 77.219  82.225  1.00 18.79 ? 284  GLU   A N     1 
ATOM   1982  C  CA    . GLU   A  1  286  ? -48.924 77.354  80.995  1.00 17.88 ? 284  GLU   A CA    1 
ATOM   1983  C  C     . GLU   A  1  286  ? -48.712 76.043  80.275  1.00 18.72 ? 284  GLU   A C     1 
ATOM   1984  O  O     . GLU   A  1  286  ? -48.729 76.010  79.044  1.00 20.70 ? 284  GLU   A O     1 
ATOM   1985  C  CB    . GLU   A  1  286  ? -47.547 77.959  81.298  1.00 18.58 ? 284  GLU   A CB    1 
ATOM   1986  C  CG    . GLU   A  1  286  ? -47.609 79.335  81.919  1.00 24.61 ? 284  GLU   A CG    1 
ATOM   1987  C  CD    . GLU   A  1  286  ? -46.274 79.773  82.487  1.00 23.82 ? 284  GLU   A CD    1 
ATOM   1988  O  OE1   . GLU   A  1  286  ? -45.245 79.428  81.886  1.00 24.22 ? 284  GLU   A OE1   1 
ATOM   1989  O  OE2   . GLU   A  1  286  ? -46.257 80.467  83.531  1.00 26.80 ? 284  GLU   A OE2   1 
ATOM   1990  N  N     . LEU   A  1  287  ? -48.466 74.966  81.012  1.00 17.24 ? 285  LEU   A N     1 
ATOM   1991  C  CA    A LEU   A  1  287  ? -48.266 73.669  80.380  0.54 17.74 ? 285  LEU   A CA    1 
ATOM   1992  C  CA    B LEU   A  1  287  ? -48.268 73.670  80.383  0.46 17.75 ? 285  LEU   A CA    1 
ATOM   1993  C  C     . LEU   A  1  287  ? -49.598 73.052  79.978  1.00 18.03 ? 285  LEU   A C     1 
ATOM   1994  O  O     . LEU   A  1  287  ? -49.742 72.545  78.860  1.00 18.05 ? 285  LEU   A O     1 
ATOM   1995  C  CB    A LEU   A  1  287  ? -47.505 72.744  81.334  0.54 18.92 ? 285  LEU   A CB    1 
ATOM   1996  C  CB    B LEU   A  1  287  ? -47.513 72.753  81.344  0.46 18.91 ? 285  LEU   A CB    1 
ATOM   1997  C  CG    A LEU   A  1  287  ? -46.628 71.635  80.747  0.54 18.39 ? 285  LEU   A CG    1 
ATOM   1998  C  CG    B LEU   A  1  287  ? -47.503 71.277  80.972  0.46 18.52 ? 285  LEU   A CG    1 
ATOM   1999  C  CD1   A LEU   A  1  287  ? -45.826 70.965  81.849  0.54 18.32 ? 285  LEU   A CD1   1 
ATOM   2000  C  CD1   B LEU   A  1  287  ? -46.997 71.121  79.577  0.46 20.72 ? 285  LEU   A CD1   1 
ATOM   2001  C  CD2   A LEU   A  1  287  ? -47.438 70.598  80.017  0.54 21.06 ? 285  LEU   A CD2   1 
ATOM   2002  C  CD2   B LEU   A  1  287  ? -46.636 70.491  81.943  0.46 17.55 ? 285  LEU   A CD2   1 
ATOM   2003  N  N     . LEU   A  1  288  ? -50.568 73.063  80.886  1.00 17.72 ? 286  LEU   A N     1 
ATOM   2004  C  CA    . LEU   A  1  288  ? -51.870 72.462  80.610  1.00 17.72 ? 286  LEU   A CA    1 
ATOM   2005  C  C     . LEU   A  1  288  ? -52.503 72.941  79.308  1.00 18.34 ? 286  LEU   A C     1 
ATOM   2006  O  O     . LEU   A  1  288  ? -52.916 72.088  78.506  1.00 17.99 ? 286  LEU   A O     1 
ATOM   2007  C  CB    . LEU   A  1  288  ? -52.800 72.644  81.815  1.00 21.04 ? 286  LEU   A CB    1 
ATOM   2008  C  CG    . LEU   A  1  288  ? -54.262 72.297  81.546  1.00 25.61 ? 286  LEU   A CG    1 
ATOM   2009  C  CD1   . LEU   A  1  288  ? -54.410 70.793  81.372  1.00 21.45 ? 286  LEU   A CD1   1 
ATOM   2010  C  CD2   . LEU   A  1  288  ? -55.127 72.819  82.675  1.00 31.83 ? 286  LEU   A CD2   1 
ATOM   2011  N  N     . PRO   A  1  289  ? -52.575 74.241  79.009  1.00 17.06 ? 287  PRO   A N     1 
ATOM   2012  C  CA    . PRO   A  1  289  ? -53.169 74.649  77.725  1.00 17.34 ? 287  PRO   A CA    1 
ATOM   2013  C  C     . PRO   A  1  289  ? -52.442 74.091  76.523  1.00 17.81 ? 287  PRO   A C     1 
ATOM   2014  O  O     . PRO   A  1  289  ? -53.057 73.898  75.465  1.00 17.51 ? 287  PRO   A O     1 
ATOM   2015  C  CB    . PRO   A  1  289  ? -53.085 76.180  77.772  1.00 19.75 ? 287  PRO   A CB    1 
ATOM   2016  C  CG    . PRO   A  1  289  ? -53.085 76.506  79.226  1.00 24.16 ? 287  PRO   A CG    1 
ATOM   2017  C  CD    . PRO   A  1  289  ? -52.295 75.405  79.871  1.00 19.39 ? 287  PRO   A CD    1 
ATOM   2018  N  N     . ARG   A  1  290  ? -51.137 73.863  76.638  1.00 16.00 ? 288  ARG   A N     1 
ATOM   2019  C  CA    . ARG   A  1  290  ? -50.391 73.305  75.521  1.00 15.78 ? 288  ARG   A CA    1 
ATOM   2020  C  C     . ARG   A  1  290  ? -50.761 71.857  75.291  1.00 16.06 ? 288  ARG   A C     1 
ATOM   2021  O  O     . ARG   A  1  290  ? -50.977 71.438  74.148  1.00 16.85 ? 288  ARG   A O     1 
ATOM   2022  C  CB    . ARG   A  1  290  ? -48.890 73.449  75.762  1.00 16.84 ? 288  ARG   A CB    1 
ATOM   2023  C  CG    . ARG   A  1  290  ? -48.475 74.878  75.811  1.00 19.83 ? 288  ARG   A CG    1 
ATOM   2024  C  CD    . ARG   A  1  290  ? -47.031 75.005  76.244  1.00 21.64 ? 288  ARG   A CD    1 
ATOM   2025  N  NE    . ARG   A  1  290  ? -46.703 76.415  76.400  1.00 24.29 ? 288  ARG   A NE    1 
ATOM   2026  C  CZ    . ARG   A  1  290  ? -45.768 76.874  77.219  1.00 26.09 ? 288  ARG   A CZ    1 
ATOM   2027  N  NH1   . ARG   A  1  290  ? -45.016 76.055  77.937  1.00 21.99 ? 288  ARG   A NH1   1 
ATOM   2028  N  NH2   . ARG   A  1  290  ? -45.587 78.188  77.324  1.00 28.89 ? 288  ARG   A NH2   1 
ATOM   2029  N  N     . VAL   A  1  291  ? -50.843 71.074  76.366  1.00 15.64 ? 289  VAL   A N     1 
ATOM   2030  C  CA    . VAL   A  1  291  ? -51.305 69.699  76.222  1.00 15.16 ? 289  VAL   A CA    1 
ATOM   2031  C  C     . VAL   A  1  291  ? -52.712 69.679  75.655  1.00 15.50 ? 289  VAL   A C     1 
ATOM   2032  O  O     . VAL   A  1  291  ? -53.037 68.852  74.794  1.00 16.55 ? 289  VAL   A O     1 
ATOM   2033  C  CB    . VAL   A  1  291  ? -51.241 68.956  77.566  1.00 16.22 ? 289  VAL   A CB    1 
ATOM   2034  C  CG1   . VAL   A  1  291  ? -51.612 67.513  77.354  1.00 18.09 ? 289  VAL   A CG1   1 
ATOM   2035  C  CG2   . VAL   A  1  291  ? -49.860 69.051  78.129  1.00 19.02 ? 289  VAL   A CG2   1 
ATOM   2036  N  N     . LYS   A  1  292  ? -53.576 70.563  76.153  1.00 16.07 ? 290  LYS   A N     1 
ATOM   2037  C  CA    . LYS   A  1  292  ? -54.938 70.611  75.649  1.00 13.76 ? 290  LYS   A CA    1 
ATOM   2038  C  C     . LYS   A  1  292  ? -54.952 70.882  74.159  1.00 18.17 ? 290  LYS   A C     1 
ATOM   2039  O  O     . LYS   A  1  292  ? -55.714 70.258  73.414  1.00 15.08 ? 290  LYS   A O     1 
ATOM   2040  C  CB    . LYS   A  1  292  ? -55.743 71.676  76.382  1.00 16.78 ? 290  LYS   A CB    1 
ATOM   2041  C  CG    . LYS   A  1  292  ? -57.145 71.789  75.812  1.00 17.78 ? 290  LYS   A CG    1 
ATOM   2042  C  CD    . LYS   A  1  292  ? -57.995 72.791  76.528  1.00 19.30 ? 290  LYS   A CD    1 
ATOM   2043  C  CE    . LYS   A  1  292  ? -59.366 72.825  75.865  1.00 23.18 ? 290  LYS   A CE    1 
ATOM   2044  N  NZ    . LYS   A  1  292  ? -60.312 73.627  76.667  1.00 21.11 ? 290  LYS   A NZ    1 
ATOM   2045  N  N     . ALA   A  1  293  ? -54.114 71.810  73.700  1.00 14.45 ? 291  ALA   A N     1 
ATOM   2046  C  CA    . ALA   A  1  293  ? -54.108 72.115  72.274  1.00 15.50 ? 291  ALA   A CA    1 
ATOM   2047  C  C     . ALA   A  1  293  ? -53.664 70.905  71.459  1.00 15.35 ? 291  ALA   A C     1 
ATOM   2048  O  O     . ALA   A  1  293  ? -54.246 70.604  70.409  1.00 17.25 ? 291  ALA   A O     1 
ATOM   2049  C  CB    . ALA   A  1  293  ? -53.236 73.345  72.008  1.00 16.99 ? 291  ALA   A CB    1 
ATOM   2050  N  N     . LEU   A  1  294  ? -52.650 70.184  71.934  1.00 13.37 ? 292  LEU   A N     1 
ATOM   2051  C  CA    . LEU   A  1  294  ? -52.231 68.976  71.234  1.00 15.48 ? 292  LEU   A CA    1 
ATOM   2052  C  C     . LEU   A  1  294  ? -53.328 67.928  71.279  1.00 15.37 ? 292  LEU   A C     1 
ATOM   2053  O  O     . LEU   A  1  294  ? -53.586 67.238  70.284  1.00 14.59 ? 292  LEU   A O     1 
ATOM   2054  C  CB    . LEU   A  1  294  ? -50.958 68.427  71.869  1.00 16.79 ? 292  LEU   A CB    1 
ATOM   2055  C  CG    . LEU   A  1  294  ? -49.744 69.329  71.712  1.00 15.03 ? 292  LEU   A CG    1 
ATOM   2056  C  CD1   . LEU   A  1  294  ? -48.575 68.800  72.516  1.00 15.99 ? 292  LEU   A CD1   1 
ATOM   2057  C  CD2   . LEU   A  1  294  ? -49.355 69.461  70.244  1.00 17.16 ? 292  LEU   A CD2   1 
ATOM   2058  N  N     . ALA   A  1  295  ? -53.991 67.802  72.427  1.00 13.42 ? 293  ALA   A N     1 
ATOM   2059  C  CA    . ALA   A  1  295  ? -55.055 66.811  72.558  1.00 15.28 ? 293  ALA   A CA    1 
ATOM   2060  C  C     . ALA   A  1  295  ? -56.230 67.135  71.642  1.00 15.90 ? 293  ALA   A C     1 
ATOM   2061  O  O     . ALA   A  1  295  ? -56.827 66.231  71.055  1.00 15.72 ? 293  ALA   A O     1 
ATOM   2062  C  CB    . ALA   A  1  295  ? -55.509 66.714  74.014  1.00 15.37 ? 293  ALA   A CB    1 
ATOM   2063  N  N     . LEU   A  1  296  ? -56.571 68.417  71.504  1.00 14.23 ? 294  LEU   A N     1 
ATOM   2064  C  CA    . LEU   A  1  296  ? -57.642 68.798  70.585  1.00 14.10 ? 294  LEU   A CA    1 
ATOM   2065  C  C     . LEU   A  1  296  ? -57.322 68.371  69.161  1.00 15.62 ? 294  LEU   A C     1 
ATOM   2066  O  O     . LEU   A  1  296  ? -58.213 67.956  68.412  1.00 15.57 ? 294  LEU   A O     1 
ATOM   2067  C  CB    . LEU   A  1  296  ? -57.867 70.310  70.630  1.00 14.77 ? 294  LEU   A CB    1 
ATOM   2068  C  CG    . LEU   A  1  296  ? -58.573 70.824  71.882  1.00 17.68 ? 294  LEU   A CG    1 
ATOM   2069  C  CD1   . LEU   A  1  296  ? -58.470 72.345  71.950  1.00 18.19 ? 294  LEU   A CD1   1 
ATOM   2070  C  CD2   . LEU   A  1  296  ? -60.048 70.405  71.884  1.00 19.81 ? 294  LEU   A CD2   1 
ATOM   2071  N  N     . LEU   A  1  297  ? -56.056 68.471  68.766  1.00 15.15 ? 295  LEU   A N     1 
ATOM   2072  C  CA    . LEU   A  1  297  ? -55.689 68.053  67.422  1.00 16.58 ? 295  LEU   A CA    1 
ATOM   2073  C  C     . LEU   A  1  297  ? -55.728 66.537  67.300  1.00 15.48 ? 295  LEU   A C     1 
ATOM   2074  O  O     . LEU   A  1  297  ? -56.199 66.006  66.293  1.00 16.34 ? 295  LEU   A O     1 
ATOM   2075  C  CB    . LEU   A  1  297  ? -54.308 68.603  67.079  1.00 18.64 ? 295  LEU   A CB    1 
ATOM   2076  C  CG    . LEU   A  1  297  ? -53.896 68.534  65.612  1.00 22.37 ? 295  LEU   A CG    1 
ATOM   2077  C  CD1   . LEU   A  1  297  ? -54.839 69.355  64.722  1.00 25.31 ? 295  LEU   A CD1   1 
ATOM   2078  C  CD2   . LEU   A  1  297  ? -52.461 69.020  65.502  1.00 25.87 ? 295  LEU   A CD2   1 
ATOM   2079  N  N     . ALA   A  1  298  ? -55.242 65.822  68.322  1.00 14.13 ? 296  ALA   A N     1 
ATOM   2080  C  CA    . ALA   A  1  298  ? -55.344 64.367  68.308  1.00 15.40 ? 296  ALA   A CA    1 
ATOM   2081  C  C     . ALA   A  1  298  ? -56.798 63.930  68.236  1.00 15.66 ? 296  ALA   A C     1 
ATOM   2082  O  O     . ALA   A  1  298  ? -57.131 62.969  67.527  1.00 16.73 ? 296  ALA   A O     1 
ATOM   2083  C  CB    . ALA   A  1  298  ? -54.654 63.776  69.538  1.00 15.68 ? 296  ALA   A CB    1 
ATOM   2084  N  N     . LYS   A  1  299  ? -57.671 64.626  68.968  1.00 14.97 ? 297  LYS   A N     1 
ATOM   2085  C  CA    A LYS   A  1  299  ? -59.101 64.352  68.899  0.59 15.08 ? 297  LYS   A CA    1 
ATOM   2086  C  CA    B LYS   A  1  299  ? -59.098 64.347  68.899  0.41 15.11 ? 297  LYS   A CA    1 
ATOM   2087  C  C     . LYS   A  1  299  ? -59.630 64.526  67.483  1.00 18.00 ? 297  LYS   A C     1 
ATOM   2088  O  O     . LYS   A  1  299  ? -60.394 63.691  66.991  1.00 17.44 ? 297  LYS   A O     1 
ATOM   2089  C  CB    A LYS   A  1  299  ? -59.848 65.276  69.864  0.59 15.41 ? 297  LYS   A CB    1 
ATOM   2090  C  CB    B LYS   A  1  299  ? -59.838 65.258  69.879  0.41 15.44 ? 297  LYS   A CB    1 
ATOM   2091  C  CG    A LYS   A  1  299  ? -61.325 65.430  69.541  0.59 17.13 ? 297  LYS   A CG    1 
ATOM   2092  C  CG    B LYS   A  1  299  ? -61.329 65.346  69.647  0.41 17.18 ? 297  LYS   A CG    1 
ATOM   2093  C  CD    A LYS   A  1  299  ? -62.029 66.356  70.519  0.59 19.37 ? 297  LYS   A CD    1 
ATOM   2094  C  CD    B LYS   A  1  299  ? -62.008 66.054  70.803  0.41 18.75 ? 297  LYS   A CD    1 
ATOM   2095  C  CE    A LYS   A  1  299  ? -63.452 66.630  70.056  0.59 20.28 ? 297  LYS   A CE    1 
ATOM   2096  C  CE    B LYS   A  1  299  ? -63.438 66.403  70.449  0.41 21.01 ? 297  LYS   A CE    1 
ATOM   2097  N  NZ    A LYS   A  1  299  ? -64.250 67.353  71.079  0.59 20.58 ? 297  LYS   A NZ    1 
ATOM   2098  N  NZ    B LYS   A  1  299  ? -63.505 67.350  69.311  0.41 22.01 ? 297  LYS   A NZ    1 
ATOM   2099  N  N     . ASN   A  1  300  ? -59.226 65.595  66.802  1.00 17.39 ? 298  ASN   A N     1 
ATOM   2100  C  CA    . ASN   A  1  300  ? -59.804 65.810  65.483  1.00 16.67 ? 298  ASN   A CA    1 
ATOM   2101  C  C     . ASN   A  1  300  ? -59.398 64.717  64.503  1.00 18.33 ? 298  ASN   A C     1 
ATOM   2102  O  O     . ASN   A  1  300  ? -60.193 64.325  63.637  1.00 21.76 ? 298  ASN   A O     1 
ATOM   2103  C  CB    . ASN   A  1  300  ? -59.472 67.193  64.946  1.00 20.52 ? 298  ASN   A CB    1 
ATOM   2104  C  CG    . ASN   A  1  300  ? -60.300 67.526  63.725  1.00 31.11 ? 298  ASN   A CG    1 
ATOM   2105  O  OD1   . ASN   A  1  300  ? -61.453 67.969  63.835  1.00 33.99 ? 298  ASN   A OD1   1 
ATOM   2106  N  ND2   . ASN   A  1  300  ? -59.739 67.277  62.555  1.00 25.71 ? 298  ASN   A ND2   1 
ATOM   2107  N  N     . TYR   A  1  301  ? -58.173 64.210  64.614  1.00 17.03 ? 299  TYR   A N     1 
ATOM   2108  C  CA    . TYR   A  1  301  ? -57.760 63.098  63.777  1.00 16.62 ? 299  TYR   A CA    1 
ATOM   2109  C  C     . TYR   A  1  301  ? -58.139 61.746  64.357  1.00 17.01 ? 299  TYR   A C     1 
ATOM   2110  O  O     . TYR   A  1  301  ? -57.948 60.726  63.686  1.00 18.33 ? 299  TYR   A O     1 
ATOM   2111  C  CB    . TYR   A  1  301  ? -56.245 63.123  63.595  1.00 16.73 ? 299  TYR   A CB    1 
ATOM   2112  C  CG    . TYR   A  1  301  ? -55.723 64.208  62.695  1.00 17.12 ? 299  TYR   A CG    1 
ATOM   2113  C  CD1   . TYR   A  1  301  ? -55.924 64.155  61.321  1.00 19.13 ? 299  TYR   A CD1   1 
ATOM   2114  C  CD2   . TYR   A  1  301  ? -54.972 65.251  63.214  1.00 16.97 ? 299  TYR   A CD2   1 
ATOM   2115  C  CE1   . TYR   A  1  301  ? -55.394 65.130  60.482  1.00 19.90 ? 299  TYR   A CE1   1 
ATOM   2116  C  CE2   . TYR   A  1  301  ? -54.440 66.232  62.390  1.00 20.03 ? 299  TYR   A CE2   1 
ATOM   2117  C  CZ    . TYR   A  1  301  ? -54.666 66.173  61.024  1.00 21.41 ? 299  TYR   A CZ    1 
ATOM   2118  O  OH    . TYR   A  1  301  ? -54.130 67.147  60.206  1.00 21.25 ? 299  TYR   A OH    1 
ATOM   2119  N  N     . ASP   A  1  302  ? -58.646 61.713  65.591  1.00 15.68 ? 300  ASP   A N     1 
ATOM   2120  C  CA    . ASP   A  1  302  ? -58.981 60.476  66.290  1.00 16.26 ? 300  ASP   A CA    1 
ATOM   2121  C  C     . ASP   A  1  302  ? -57.779 59.534  66.376  1.00 16.65 ? 300  ASP   A C     1 
ATOM   2122  O  O     . ASP   A  1  302  ? -57.829 58.362  65.980  1.00 18.06 ? 300  ASP   A O     1 
ATOM   2123  C  CB    . ASP   A  1  302  ? -60.220 59.779  65.703  1.00 19.26 ? 300  ASP   A CB    1 
ATOM   2124  C  CG    . ASP   A  1  302  ? -60.877 58.841  66.697  1.00 23.21 ? 300  ASP   A CG    1 
ATOM   2125  O  OD1   . ASP   A  1  302  ? -60.805 59.124  67.919  1.00 22.49 ? 300  ASP   A OD1   1 
ATOM   2126  O  OD2   . ASP   A  1  302  ? -61.445 57.813  66.272  1.00 22.96 ? 300  ASP   A OD2   1 
ATOM   2127  N  N     . ILE   A  1  303  ? -56.694 60.064  66.932  1.00 15.41 ? 301  ILE   A N     1 
ATOM   2128  C  CA    . ILE   A  1  303  ? -55.502 59.273  67.223  1.00 14.91 ? 301  ILE   A CA    1 
ATOM   2129  C  C     . ILE   A  1  303  ? -55.247 59.269  68.728  1.00 18.48 ? 301  ILE   A C     1 
ATOM   2130  O  O     . ILE   A  1  303  ? -55.746 60.113  69.472  1.00 15.73 ? 301  ILE   A O     1 
ATOM   2131  C  CB    . ILE   A  1  303  ? -54.249 59.763  66.466  1.00 16.03 ? 301  ILE   A CB    1 
ATOM   2132  C  CG1   . ILE   A  1  303  ? -53.750 61.101  67.034  1.00 15.65 ? 301  ILE   A CG1   1 
ATOM   2133  C  CG2   . ILE   A  1  303  ? -54.566 59.907  64.973  1.00 19.36 ? 301  ILE   A CG2   1 
ATOM   2134  C  CD1   . ILE   A  1  303  ? -52.379 61.494  66.517  1.00 17.14 ? 301  ILE   A CD1   1 
ATOM   2135  N  N     . GLY   A  1  304  ? -54.449 58.302  69.172  1.00 16.93 ? 302  GLY   A N     1 
ATOM   2136  C  CA    . GLY   A  1  304  ? -54.060 58.266  70.573  1.00 16.30 ? 302  GLY   A CA    1 
ATOM   2137  C  C     . GLY   A  1  304  ? -53.024 59.336  70.875  1.00 16.35 ? 302  GLY   A C     1 
ATOM   2138  O  O     . GLY   A  1  304  ? -52.167 59.654  70.050  1.00 17.45 ? 302  GLY   A O     1 
ATOM   2139  N  N     . LEU   A  1  305  ? -53.138 59.929  72.063  1.00 16.28 ? 303  LEU   A N     1 
ATOM   2140  C  CA    . LEU   A  1  305  ? -52.134 60.844  72.591  1.00 15.59 ? 303  LEU   A CA    1 
ATOM   2141  C  C     . LEU   A  1  305  ? -51.810 60.370  73.997  1.00 17.19 ? 303  LEU   A C     1 
ATOM   2142  O  O     . LEU   A  1  305  ? -52.645 60.488  74.896  1.00 16.24 ? 303  LEU   A O     1 
ATOM   2143  C  CB    . LEU   A  1  305  ? -52.656 62.283  72.608  1.00 16.55 ? 303  LEU   A CB    1 
ATOM   2144  C  CG    . LEU   A  1  305  ? -51.583 63.316  72.967  1.00 19.48 ? 303  LEU   A CG    1 
ATOM   2145  C  CD1   . LEU   A  1  305  ? -51.850 64.629  72.256  1.00 22.08 ? 303  LEU   A CD1   1 
ATOM   2146  C  CD2   . LEU   A  1  305  ? -51.534 63.540  74.469  1.00 23.21 ? 303  LEU   A CD2   1 
ATOM   2147  N  N     . ASN   A  1  306  ? -50.604 59.853  74.195  1.00 15.91 ? 304  ASN   A N     1 
ATOM   2148  C  CA    . ASN   A  1  306  ? -50.227 59.233  75.455  1.00 16.43 ? 304  ASN   A CA    1 
ATOM   2149  C  C     . ASN   A  1  306  ? -49.255 60.137  76.198  1.00 16.85 ? 304  ASN   A C     1 
ATOM   2150  O  O     . ASN   A  1  306  ? -48.322 60.672  75.600  1.00 16.71 ? 304  ASN   A O     1 
ATOM   2151  C  CB    . ASN   A  1  306  ? -49.526 57.907  75.187  1.00 14.75 ? 304  ASN   A CB    1 
ATOM   2152  C  CG    . ASN   A  1  306  ? -48.888 57.344  76.431  1.00 18.68 ? 304  ASN   A CG    1 
ATOM   2153  O  OD1   . ASN   A  1  306  ? -47.687 57.520  76.676  1.00 21.87 ? 304  ASN   A OD1   1 
ATOM   2154  N  ND2   . ASN   A  1  306  ? -49.689 56.676  77.237  1.00 16.87 ? 304  ASN   A ND2   1 
ATOM   2155  N  N     . ILE   A  1  307  ? -49.474 60.297  77.499  1.00 14.83 ? 305  ILE   A N     1 
ATOM   2156  C  CA    . ILE   A  1  307  ? -48.558 61.036  78.361  1.00 15.99 ? 305  ILE   A CA    1 
ATOM   2157  C  C     . ILE   A  1  307  ? -47.590 60.049  78.995  1.00 13.73 ? 305  ILE   A C     1 
ATOM   2158  O  O     . ILE   A  1  307  ? -47.979 59.242  79.851  1.00 15.55 ? 305  ILE   A O     1 
ATOM   2159  C  CB    . ILE   A  1  307  ? -49.305 61.841  79.428  1.00 18.90 ? 305  ILE   A CB    1 
ATOM   2160  C  CG1   . ILE   A  1  307  ? -50.215 62.875  78.747  1.00 19.84 ? 305  ILE   A CG1   1 
ATOM   2161  C  CG2   . ILE   A  1  307  ? -48.279 62.488  80.393  1.00 18.65 ? 305  ILE   A CG2   1 
ATOM   2162  C  CD1   . ILE   A  1  307  ? -51.244 63.497  79.667  1.00 24.63 ? 305  ILE   A CD1   1 
ATOM   2163  N  N     . ASP   A  1  308  ? -46.319 60.118  78.582  1.00 14.83 ? 306  ASP   A N     1 
ATOM   2164  C  CA    . ASP   A  1  308  ? -45.292 59.248  79.132  1.00 15.19 ? 306  ASP   A CA    1 
ATOM   2165  C  C     . ASP   A  1  308  ? -45.053 59.582  80.603  1.00 17.09 ? 306  ASP   A C     1 
ATOM   2166  O  O     . ASP   A  1  308  ? -45.263 60.709  81.046  1.00 16.56 ? 306  ASP   A O     1 
ATOM   2167  C  CB    . ASP   A  1  308  ? -43.978 59.422  78.354  1.00 16.14 ? 306  ASP   A CB    1 
ATOM   2168  C  CG    . ASP   A  1  308  ? -44.031 58.838  76.949  1.00 22.69 ? 306  ASP   A CG    1 
ATOM   2169  O  OD1   . ASP   A  1  308  ? -44.938 58.030  76.650  1.00 19.18 ? 306  ASP   A OD1   1 
ATOM   2170  O  OD2   . ASP   A  1  308  ? -43.138 59.168  76.136  1.00 21.96 ? 306  ASP   A OD2   1 
ATOM   2171  N  N     . ALA   A  1  309  ? -44.646 58.577  81.378  1.00 14.23 ? 307  ALA   A N     1 
ATOM   2172  C  CA    . ALA   A  1  309  ? -44.366 58.784  82.792  1.00 14.06 ? 307  ALA   A CA    1 
ATOM   2173  C  C     . ALA   A  1  309  ? -42.883 59.037  83.012  1.00 16.00 ? 307  ALA   A C     1 
ATOM   2174  O  O     . ALA   A  1  309  ? -42.026 58.379  82.412  1.00 16.15 ? 307  ALA   A O     1 
ATOM   2175  C  CB    . ALA   A  1  309  ? -44.817 57.596  83.642  1.00 16.50 ? 307  ALA   A CB    1 
ATOM   2176  N  N     . GLU   A  1  310  ? -42.593 59.985  83.897  1.00 14.37 ? 308  GLU   A N     1 
ATOM   2177  C  CA    . GLU   A  1  310  ? -41.211 60.402  84.086  1.00 14.43 ? 308  GLU   A CA    1 
ATOM   2178  C  C     . GLU   A  1  310  ? -40.776 60.156  85.523  1.00 15.51 ? 308  GLU   A C     1 
ATOM   2179  O  O     . GLU   A  1  310  ? -41.040 59.074  86.062  1.00 15.60 ? 308  GLU   A O     1 
ATOM   2180  C  CB    . GLU   A  1  310  ? -41.033 61.845  83.612  1.00 15.27 ? 308  GLU   A CB    1 
ATOM   2181  C  CG    . GLU   A  1  310  ? -41.437 62.003  82.143  1.00 17.11 ? 308  GLU   A CG    1 
ATOM   2182  C  CD    . GLU   A  1  310  ? -41.170 63.399  81.607  1.00 19.56 ? 308  GLU   A CD    1 
ATOM   2183  O  OE1   . GLU   A  1  310  ? -39.979 63.730  81.414  1.00 20.51 ? 308  GLU   A OE1   1 
ATOM   2184  O  OE2   . GLU   A  1  310  ? -42.140 64.153  81.388  1.00 18.18 ? 308  GLU   A OE2   1 
ATOM   2185  N  N     . GLU   A  1  311  ? -40.107 61.116  86.146  1.00 16.18 ? 309  GLU   A N     1 
ATOM   2186  C  CA    . GLU   A  1  311  ? -39.567 60.881  87.480  1.00 16.68 ? 309  GLU   A CA    1 
ATOM   2187  C  C     . GLU   A  1  311  ? -40.685 60.766  88.508  1.00 13.35 ? 309  GLU   A C     1 
ATOM   2188  O  O     . GLU   A  1  311  ? -41.802 61.257  88.327  1.00 14.75 ? 309  GLU   A O     1 
ATOM   2189  C  CB    . GLU   A  1  311  ? -38.659 62.030  87.907  1.00 17.53 ? 309  GLU   A CB    1 
ATOM   2190  C  CG    . GLU   A  1  311  ? -37.361 62.128  87.110  1.00 18.49 ? 309  GLU   A CG    1 
ATOM   2191  C  CD    . GLU   A  1  311  ? -37.496 62.962  85.857  1.00 23.24 ? 309  GLU   A CD    1 
ATOM   2192  O  OE1   . GLU   A  1  311  ? -38.630 63.259  85.431  1.00 18.33 ? 309  GLU   A OE1   1 
ATOM   2193  O  OE2   . GLU   A  1  311  ? -36.451 63.333  85.287  1.00 26.21 ? 309  GLU   A OE2   1 
ATOM   2194  N  N     . ALA   A  1  312  ? -40.373 60.085  89.607  1.00 14.10 ? 310  ALA   A N     1 
ATOM   2195  C  CA    . ALA   A  1  312  ? -41.385 59.836  90.626  1.00 15.45 ? 310  ALA   A CA    1 
ATOM   2196  C  C     . ALA   A  1  312  ? -41.971 61.125  91.180  1.00 15.71 ? 310  ALA   A C     1 
ATOM   2197  O  O     . ALA   A  1  312  ? -43.156 61.162  91.520  1.00 16.58 ? 310  ALA   A O     1 
ATOM   2198  C  CB    . ALA   A  1  312  ? -40.788 58.992  91.752  1.00 15.63 ? 310  ALA   A CB    1 
ATOM   2199  N  N     . ASP   A  1  313  ? -41.176 62.191  91.277  1.00 16.10 ? 311  ASP   A N     1 
ATOM   2200  C  CA    . ASP   A  1  313  ? -41.690 63.441  91.834  1.00 16.35 ? 311  ASP   A CA    1 
ATOM   2201  C  C     . ASP   A  1  313  ? -42.583 64.215  90.874  1.00 16.21 ? 311  ASP   A C     1 
ATOM   2202  O  O     . ASP   A  1  313  ? -43.059 65.293  91.240  1.00 18.27 ? 311  ASP   A O     1 
ATOM   2203  C  CB    . ASP   A  1  313  ? -40.566 64.319  92.405  1.00 17.91 ? 311  ASP   A CB    1 
ATOM   2204  C  CG    . ASP   A  1  313  ? -39.613 64.850  91.342  1.00 24.52 ? 311  ASP   A CG    1 
ATOM   2205  O  OD1   . ASP   A  1  313  ? -39.795 64.571  90.135  1.00 21.88 ? 311  ASP   A OD1   1 
ATOM   2206  O  OD2   . ASP   A  1  313  ? -38.667 65.568  91.728  1.00 26.86 ? 311  ASP   A OD2   1 
ATOM   2207  N  N     . ARG   A  1  314  ? -42.815 63.692  89.674  1.00 15.29 ? 312  ARG   A N     1 
ATOM   2208  C  CA    . ARG   A  1  314  ? -43.722 64.298  88.715  1.00 14.69 ? 312  ARG   A CA    1 
ATOM   2209  C  C     . ARG   A  1  314  ? -45.008 63.514  88.560  1.00 16.72 ? 312  ARG   A C     1 
ATOM   2210  O  O     . ARG   A  1  314  ? -45.935 64.009  87.920  1.00 16.42 ? 312  ARG   A O     1 
ATOM   2211  C  CB    . ARG   A  1  314  ? -43.038 64.435  87.350  1.00 17.04 ? 312  ARG   A CB    1 
ATOM   2212  C  CG    . ARG   A  1  314  ? -42.038 65.554  87.365  1.00 20.70 ? 312  ARG   A CG    1 
ATOM   2213  C  CD    . ARG   A  1  314  ? -41.062 65.442  86.228  1.00 21.14 ? 312  ARG   A CD    1 
ATOM   2214  N  NE    . ARG   A  1  314  ? -40.492 66.752  85.958  1.00 19.88 ? 312  ARG   A NE    1 
ATOM   2215  C  CZ    . ARG   A  1  314  ? -39.499 66.969  85.110  1.00 18.77 ? 312  ARG   A CZ    1 
ATOM   2216  N  NH1   . ARG   A  1  314  ? -38.902 65.972  84.481  1.00 19.73 ? 312  ARG   A NH1   1 
ATOM   2217  N  NH2   . ARG   A  1  314  ? -39.107 68.221  84.878  1.00 20.40 ? 312  ARG   A NH2   1 
ATOM   2218  N  N     . LEU   A  1  315  ? -45.102 62.330  89.170  1.00 16.01 ? 313  LEU   A N     1 
ATOM   2219  C  CA    . LEU   A  1  315  ? -46.287 61.493  89.006  1.00 17.02 ? 313  LEU   A CA    1 
ATOM   2220  C  C     . LEU   A  1  315  ? -47.549 62.229  89.440  1.00 15.83 ? 313  LEU   A C     1 
ATOM   2221  O  O     . LEU   A  1  315  ? -48.500 62.375  88.666  1.00 16.06 ? 313  LEU   A O     1 
ATOM   2222  C  CB    . LEU   A  1  315  ? -46.112 60.205  89.812  1.00 16.39 ? 313  LEU   A CB    1 
ATOM   2223  C  CG    . LEU   A  1  315  ? -46.901 58.968  89.379  1.00 16.90 ? 313  LEU   A CG    1 
ATOM   2224  C  CD1   . LEU   A  1  315  ? -46.512 57.799  90.282  1.00 17.68 ? 313  LEU   A CD1   1 
ATOM   2225  C  CD2   . LEU   A  1  315  ? -48.399 59.179  89.447  1.00 19.35 ? 313  LEU   A CD2   1 
ATOM   2226  N  N     . GLU   A  1  316  ? -47.598 62.671  90.693  1.00 14.84 ? 314  GLU   A N     1 
ATOM   2227  C  CA    . GLU   A  1  316  ? -48.855 63.229  91.182  1.00 16.64 ? 314  GLU   A CA    1 
ATOM   2228  C  C     . GLU   A  1  316  ? -49.197 64.547  90.497  1.00 18.27 ? 314  GLU   A C     1 
ATOM   2229  O  O     . GLU   A  1  316  ? -50.376 64.820  90.235  1.00 18.48 ? 314  GLU   A O     1 
ATOM   2230  C  CB    . GLU   A  1  316  ? -48.840 63.312  92.707  1.00 18.88 ? 314  GLU   A CB    1 
ATOM   2231  C  CG    . GLU   A  1  316  ? -48.847 61.913  93.325  1.00 20.40 ? 314  GLU   A CG    1 
ATOM   2232  C  CD    . GLU   A  1  316  ? -48.868 61.916  94.825  1.00 20.56 ? 314  GLU   A CD    1 
ATOM   2233  O  OE1   . GLU   A  1  316  ? -49.620 62.721  95.400  1.00 22.75 ? 314  GLU   A OE1   1 
ATOM   2234  O  OE2   . GLU   A  1  316  ? -48.125 61.107  95.425  1.00 20.43 ? 314  GLU   A OE2   1 
ATOM   2235  N  N     . LEU   A  1  317  ? -48.189 65.348  90.151  1.00 17.39 ? 315  LEU   A N     1 
ATOM   2236  C  CA    . LEU   A  1  317  ? -48.457 66.553  89.378  1.00 18.67 ? 315  LEU   A CA    1 
ATOM   2237  C  C     . LEU   A  1  317  ? -49.114 66.213  88.045  1.00 18.52 ? 315  LEU   A C     1 
ATOM   2238  O  O     . LEU   A  1  317  ? -50.076 66.875  87.633  1.00 18.39 ? 315  LEU   A O     1 
ATOM   2239  C  CB    . LEU   A  1  317  ? -47.156 67.317  89.155  1.00 19.62 ? 315  LEU   A CB    1 
ATOM   2240  C  CG    . LEU   A  1  317  ? -47.286 68.618  88.363  1.00 21.10 ? 315  LEU   A CG    1 
ATOM   2241  C  CD1   . LEU   A  1  317  ? -48.294 69.571  89.007  1.00 22.54 ? 315  LEU   A CD1   1 
ATOM   2242  C  CD2   . LEU   A  1  317  ? -45.914 69.272  88.258  1.00 23.81 ? 315  LEU   A CD2   1 
ATOM   2243  N  N     . SER   A  1  318  ? -48.633 65.159  87.374  1.00 16.08 ? 316  SER   A N     1 
ATOM   2244  C  CA    . SER   A  1  318  ? -49.200 64.801  86.079  1.00 15.89 ? 316  SER   A CA    1 
ATOM   2245  C  C     . SER   A  1  318  ? -50.649 64.376  86.208  1.00 16.77 ? 316  SER   A C     1 
ATOM   2246  O  O     . SER   A  1  318  ? -51.416 64.519  85.252  1.00 16.95 ? 316  SER   A O     1 
ATOM   2247  C  CB    . SER   A  1  318  ? -48.388 63.699  85.396  1.00 15.05 ? 316  SER   A CB    1 
ATOM   2248  O  OG    . SER   A  1  318  ? -48.536 62.452  86.059  1.00 16.53 ? 316  SER   A OG    1 
ATOM   2249  N  N     . LEU   A  1  319  ? -51.032 63.839  87.369  1.00 15.64 ? 317  LEU   A N     1 
ATOM   2250  C  CA    . LEU   A  1  319  ? -52.432 63.495  87.609  1.00 17.46 ? 317  LEU   A CA    1 
ATOM   2251  C  C     . LEU   A  1  319  ? -53.327 64.720  87.606  1.00 17.04 ? 317  LEU   A C     1 
ATOM   2252  O  O     . LEU   A  1  319  ? -54.485 64.634  87.183  1.00 17.27 ? 317  LEU   A O     1 
ATOM   2253  C  CB    . LEU   A  1  319  ? -52.574 62.725  88.925  1.00 16.10 ? 317  LEU   A CB    1 
ATOM   2254  C  CG    . LEU   A  1  319  ? -51.885 61.365  88.944  1.00 19.77 ? 317  LEU   A CG    1 
ATOM   2255  C  CD1   . LEU   A  1  319  ? -52.064 60.740  90.331  1.00 19.28 ? 317  LEU   A CD1   1 
ATOM   2256  C  CD2   . LEU   A  1  319  ? -52.415 60.450  87.861  1.00 19.61 ? 317  LEU   A CD2   1 
ATOM   2257  N  N     . ASP   A  1  320  ? -52.834 65.863  88.079  1.00 17.38 ? 318  ASP   A N     1 
ATOM   2258  C  CA    . ASP   A  1  320  ? -53.646 67.075  88.017  1.00 18.95 ? 318  ASP   A CA    1 
ATOM   2259  C  C     . ASP   A  1  320  ? -53.907 67.494  86.579  1.00 19.98 ? 318  ASP   A C     1 
ATOM   2260  O  O     . ASP   A  1  320  ? -54.994 67.989  86.260  1.00 20.39 ? 318  ASP   A O     1 
ATOM   2261  C  CB    . ASP   A  1  320  ? -53.012 68.186  88.848  1.00 18.51 ? 318  ASP   A CB    1 
ATOM   2262  C  CG    . ASP   A  1  320  ? -53.177 67.937  90.325  1.00 24.14 ? 318  ASP   A CG    1 
ATOM   2263  O  OD1   . ASP   A  1  320  ? -54.344 67.777  90.756  1.00 24.88 ? 318  ASP   A OD1   1 
ATOM   2264  O  OD2   . ASP   A  1  320  ? -52.155 67.853  91.044  1.00 27.77 ? 318  ASP   A OD2   1 
ATOM   2265  N  N     . LEU   A  1  321  ? -52.936 67.282  85.690  1.00 17.90 ? 319  LEU   A N     1 
ATOM   2266  C  CA    . LEU   A  1  321  ? -53.176 67.582  84.285  1.00 17.69 ? 319  LEU   A CA    1 
ATOM   2267  C  C     . LEU   A  1  321  ? -54.138 66.582  83.678  1.00 17.52 ? 319  LEU   A C     1 
ATOM   2268  O  O     . LEU   A  1  321  ? -55.060 66.969  82.950  1.00 19.65 ? 319  LEU   A O     1 
ATOM   2269  C  CB    . LEU   A  1  321  ? -51.867 67.608  83.498  1.00 18.68 ? 319  LEU   A CB    1 
ATOM   2270  C  CG    . LEU   A  1  321  ? -51.092 68.900  83.706  1.00 21.73 ? 319  LEU   A CG    1 
ATOM   2271  C  CD1   . LEU   A  1  321  ? -50.189 68.763  84.903  1.00 24.32 ? 319  LEU   A CD1   1 
ATOM   2272  C  CD2   . LEU   A  1  321  ? -50.287 69.238  82.455  1.00 27.69 ? 319  LEU   A CD2   1 
ATOM   2273  N  N     . LEU   A  1  322  ? -53.935 65.292  83.959  1.00 17.00 ? 320  LEU   A N     1 
ATOM   2274  C  CA    . LEU   A  1  322  ? -54.837 64.275  83.432  1.00 16.84 ? 320  LEU   A CA    1 
ATOM   2275  C  C     . LEU   A  1  322  ? -56.265 64.544  83.871  1.00 16.85 ? 320  LEU   A C     1 
ATOM   2276  O  O     . LEU   A  1  322  ? -57.201 64.438  83.064  1.00 18.44 ? 320  LEU   A O     1 
ATOM   2277  C  CB    . LEU   A  1  322  ? -54.393 62.894  83.910  1.00 17.39 ? 320  LEU   A CB    1 
ATOM   2278  C  CG    . LEU   A  1  322  ? -55.237 61.729  83.388  1.00 18.95 ? 320  LEU   A CG    1 
ATOM   2279  C  CD1   . LEU   A  1  322  ? -55.026 61.570  81.886  1.00 16.11 ? 320  LEU   A CD1   1 
ATOM   2280  C  CD2   . LEU   A  1  322  ? -54.896 60.450  84.130  1.00 16.49 ? 320  LEU   A CD2   1 
ATOM   2281  N  N     . GLU   A  1  323  ? -56.447 64.927  85.136  1.00 17.18 ? 321  GLU   A N     1 
ATOM   2282  C  CA    . GLU   A  1  323  ? -57.786 65.203  85.655  1.00 18.68 ? 321  GLU   A CA    1 
ATOM   2283  C  C     . GLU   A  1  323  ? -58.450 66.330  84.875  1.00 21.20 ? 321  GLU   A C     1 
ATOM   2284  O  O     . GLU   A  1  323  ? -59.594 66.196  84.424  1.00 18.76 ? 321  GLU   A O     1 
ATOM   2285  C  CB    . GLU   A  1  323  ? -57.710 65.543  87.146  1.00 20.00 ? 321  GLU   A CB    1 
ATOM   2286  C  CG    . GLU   A  1  323  ? -59.010 66.121  87.731  1.00 26.06 ? 321  GLU   A CG    1 
ATOM   2287  C  CD    . GLU   A  1  323  ? -59.756 65.141  88.615  1.00 28.55 ? 321  GLU   A CD    1 
ATOM   2288  O  OE1   . GLU   A  1  323  ? -59.225 64.056  88.892  1.00 28.88 ? 321  GLU   A OE1   1 
ATOM   2289  O  OE2   . GLU   A  1  323  ? -60.902 65.446  89.024  1.00 30.72 ? 321  GLU   A OE2   1 
ATOM   2290  N  N     . VAL   A  1  324  ? -57.746 67.450  84.697  1.00 17.48 ? 322  VAL   A N     1 
ATOM   2291  C  CA    . VAL   A  1  324  ? -58.335 68.581  83.985  1.00 18.33 ? 322  VAL   A CA    1 
ATOM   2292  C  C     . VAL   A  1  324  ? -58.673 68.200  82.552  1.00 16.99 ? 322  VAL   A C     1 
ATOM   2293  O  O     . VAL   A  1  324  ? -59.756 68.524  82.049  1.00 19.25 ? 322  VAL   A O     1 
ATOM   2294  C  CB    . VAL   A  1  324  ? -57.422 69.816  84.049  1.00 22.38 ? 322  VAL   A CB    1 
ATOM   2295  C  CG1   . VAL   A  1  324  ? -58.043 70.962  83.243  1.00 21.63 ? 322  VAL   A CG1   1 
ATOM   2296  C  CG2   . VAL   A  1  324  ? -57.221 70.232  85.476  1.00 21.92 ? 322  VAL   A CG2   1 
ATOM   2297  N  N     . LEU   A  1  325  ? -57.749 67.516  81.869  1.00 16.11 ? 323  LEU   A N     1 
ATOM   2298  C  CA    . LEU   A  1  325  ? -57.983 67.167  80.471  1.00 17.97 ? 323  LEU   A CA    1 
ATOM   2299  C  C     . LEU   A  1  325  ? -59.179 66.239  80.334  1.00 17.58 ? 323  LEU   A C     1 
ATOM   2300  O  O     . LEU   A  1  325  ? -60.014 66.419  79.441  1.00 16.82 ? 323  LEU   A O     1 
ATOM   2301  C  CB    . LEU   A  1  325  ? -56.734 66.519  79.872  1.00 16.63 ? 323  LEU   A CB    1 
ATOM   2302  C  CG    . LEU   A  1  325  ? -55.527 67.456  79.805  1.00 19.88 ? 323  LEU   A CG    1 
ATOM   2303  C  CD1   . LEU   A  1  325  ? -54.248 66.671  79.604  1.00 19.11 ? 323  LEU   A CD1   1 
ATOM   2304  C  CD2   . LEU   A  1  325  ? -55.742 68.425  78.668  1.00 19.24 ? 323  LEU   A CD2   1 
ATOM   2305  N  N     . CYS   A  1  326  ? -59.291 65.247  81.218  1.00 18.11 ? 324  CYS   A N     1 
ATOM   2306  C  CA    . CYS   A  1  326  ? -60.388 64.295  81.073  1.00 15.82 ? 324  CYS   A CA    1 
ATOM   2307  C  C     . CYS   A  1  326  ? -61.731 64.906  81.422  1.00 18.81 ? 324  CYS   A C     1 
ATOM   2308  O  O     . CYS   A  1  326  ? -62.755 64.415  80.942  1.00 19.16 ? 324  CYS   A O     1 
ATOM   2309  C  CB    . CYS   A  1  326  ? -60.145 63.051  81.927  1.00 16.48 ? 324  CYS   A CB    1 
ATOM   2310  S  SG    . CYS   A  1  326  ? -58.784 62.048  81.282  1.00 22.35 ? 324  CYS   A SG    1 
ATOM   2311  N  N     . LEU   A  1  327  ? -61.747 65.966  82.221  1.00 17.45 ? 325  LEU   A N     1 
ATOM   2312  C  CA    . LEU   A  1  327  ? -62.982 66.656  82.568  1.00 18.00 ? 325  LEU   A CA    1 
ATOM   2313  C  C     . LEU   A  1  327  ? -63.298 67.817  81.629  1.00 18.57 ? 325  LEU   A C     1 
ATOM   2314  O  O     . LEU   A  1  327  ? -64.368 68.418  81.755  1.00 20.97 ? 325  LEU   A O     1 
ATOM   2315  C  CB    . LEU   A  1  327  ? -62.925 67.150  84.020  1.00 18.50 ? 325  LEU   A CB    1 
ATOM   2316  C  CG    . LEU   A  1  327  ? -62.789 66.033  85.064  1.00 24.75 ? 325  LEU   A CG    1 
ATOM   2317  C  CD1   . LEU   A  1  327  ? -62.632 66.619  86.458  1.00 23.53 ? 325  LEU   A CD1   1 
ATOM   2318  C  CD2   . LEU   A  1  327  ? -63.964 65.085  85.013  1.00 27.04 ? 325  LEU   A CD2   1 
ATOM   2319  N  N     . ASP   A  1  328  ? -62.413 68.130  80.687  1.00 18.50 ? 326  ASP   A N     1 
ATOM   2320  C  CA    . ASP   A  1  328  ? -62.599 69.266  79.792  1.00 16.58 ? 326  ASP   A CA    1 
ATOM   2321  C  C     . ASP   A  1  328  ? -63.546 68.886  78.663  1.00 17.05 ? 326  ASP   A C     1 
ATOM   2322  O  O     . ASP   A  1  328  ? -63.222 68.032  77.828  1.00 17.67 ? 326  ASP   A O     1 
ATOM   2323  C  CB    . ASP   A  1  328  ? -61.246 69.681  79.220  1.00 19.47 ? 326  ASP   A CB    1 
ATOM   2324  C  CG    . ASP   A  1  328  ? -61.303 71.007  78.487  1.00 22.60 ? 326  ASP   A CG    1 
ATOM   2325  O  OD1   . ASP   A  1  328  ? -62.280 71.258  77.759  1.00 23.13 ? 326  ASP   A OD1   1 
ATOM   2326  O  OD2   . ASP   A  1  328  ? -60.368 71.811  78.651  1.00 27.30 ? 326  ASP   A OD2   1 
ATOM   2327  N  N     . GLY   A  1  329  ? -64.705 69.540  78.618  1.00 16.84 ? 327  GLY   A N     1 
ATOM   2328  C  CA    . GLY   A  1  329  ? -65.707 69.193  77.625  1.00 18.12 ? 327  GLY   A CA    1 
ATOM   2329  C  C     . GLY   A  1  329  ? -65.247 69.383  76.195  1.00 20.11 ? 327  GLY   A C     1 
ATOM   2330  O  O     . GLY   A  1  329  ? -65.777 68.728  75.297  1.00 18.93 ? 327  GLY   A O     1 
ATOM   2331  N  N     . ASP   A  1  330  ? -64.262 70.255  75.960  1.00 18.48 ? 328  ASP   A N     1 
ATOM   2332  C  CA    . ASP   A  1  330  ? -63.775 70.460  74.598  1.00 18.57 ? 328  ASP   A CA    1 
ATOM   2333  C  C     . ASP   A  1  330  ? -63.136 69.202  74.030  1.00 17.58 ? 328  ASP   A C     1 
ATOM   2334  O  O     . ASP   A  1  330  ? -63.034 69.079  72.809  1.00 17.56 ? 328  ASP   A O     1 
ATOM   2335  C  CB    . ASP   A  1  330  ? -62.749 71.596  74.529  1.00 19.74 ? 328  ASP   A CB    1 
ATOM   2336  C  CG    . ASP   A  1  330  ? -63.357 72.958  74.793  1.00 25.39 ? 328  ASP   A CG    1 
ATOM   2337  O  OD1   . ASP   A  1  330  ? -64.587 73.112  74.638  1.00 28.67 ? 328  ASP   A OD1   1 
ATOM   2338  O  OD2   . ASP   A  1  330  ? -62.595 73.881  75.140  1.00 23.83 ? 328  ASP   A OD2   1 
ATOM   2339  N  N     . LEU   A  1  331  ? -62.716 68.272  74.884  1.00 15.97 ? 329  LEU   A N     1 
ATOM   2340  C  CA    . LEU   A  1  331  ? -62.089 67.034  74.449  1.00 16.88 ? 329  LEU   A CA    1 
ATOM   2341  C  C     . LEU   A  1  331  ? -63.054 65.862  74.432  1.00 18.18 ? 329  LEU   A C     1 
ATOM   2342  O  O     . LEU   A  1  331  ? -62.634 64.727  74.176  1.00 18.65 ? 329  LEU   A O     1 
ATOM   2343  C  CB    . LEU   A  1  331  ? -60.882 66.707  75.331  1.00 17.11 ? 329  LEU   A CB    1 
ATOM   2344  C  CG    . LEU   A  1  331  ? -59.686 67.638  75.124  1.00 17.08 ? 329  LEU   A CG    1 
ATOM   2345  C  CD1   . LEU   A  1  331  ? -58.657 67.403  76.212  1.00 18.25 ? 329  LEU   A CD1   1 
ATOM   2346  C  CD2   . LEU   A  1  331  ? -59.069 67.404  73.769  1.00 17.20 ? 329  LEU   A CD2   1 
ATOM   2347  N  N     . SER   A  1  332  ? -64.335 66.107  74.686  1.00 18.27 ? 330  SER   A N     1 
ATOM   2348  C  CA    . SER   A  1  332  ? -65.277 65.009  74.802  1.00 20.58 ? 330  SER   A CA    1 
ATOM   2349  C  C     . SER   A  1  332  ? -65.499 64.348  73.446  1.00 18.21 ? 330  SER   A C     1 
ATOM   2350  O  O     . SER   A  1  332  ? -65.337 64.964  72.391  1.00 22.49 ? 330  SER   A O     1 
ATOM   2351  C  CB    . SER   A  1  332  ? -66.602 65.500  75.390  1.00 21.03 ? 330  SER   A CB    1 
ATOM   2352  O  OG    . SER   A  1  332  ? -67.292 66.333  74.487  1.00 23.39 ? 330  SER   A OG    1 
ATOM   2353  N  N     . GLY   A  1  333  ? -65.852 63.070  73.485  1.00 18.47 ? 331  GLY   A N     1 
ATOM   2354  C  CA    . GLY   A  1  333  ? -66.065 62.312  72.275  1.00 19.00 ? 331  GLY   A CA    1 
ATOM   2355  C  C     . GLY   A  1  333  ? -64.828 61.624  71.758  1.00 20.10 ? 331  GLY   A C     1 
ATOM   2356  O  O     . GLY   A  1  333  ? -64.900 60.907  70.750  1.00 23.02 ? 331  GLY   A O     1 
ATOM   2357  N  N     . TRP   A  1  334  ? -63.700 61.802  72.427  1.00 17.73 ? 332  TRP   A N     1 
ATOM   2358  C  CA    . TRP   A  1  334  ? -62.436 61.222  72.015  1.00 20.01 ? 332  TRP   A CA    1 
ATOM   2359  C  C     . TRP   A  1  334  ? -61.897 60.403  73.171  1.00 16.98 ? 332  TRP   A C     1 
ATOM   2360  O  O     . TRP   A  1  334  ? -61.810 60.905  74.297  1.00 18.62 ? 332  TRP   A O     1 
ATOM   2361  C  CB    . TRP   A  1  334  ? -61.475 62.358  71.701  1.00 17.21 ? 332  TRP   A CB    1 
ATOM   2362  C  CG    . TRP   A  1  334  ? -60.048 61.980  71.485  1.00 16.10 ? 332  TRP   A CG    1 
ATOM   2363  C  CD1   . TRP   A  1  334  ? -59.531 61.220  70.472  1.00 15.48 ? 332  TRP   A CD1   1 
ATOM   2364  C  CD2   . TRP   A  1  334  ? -58.942 62.436  72.255  1.00 17.18 ? 332  TRP   A CD2   1 
ATOM   2365  N  NE1   . TRP   A  1  334  ? -58.163 61.146  70.595  1.00 15.68 ? 332  TRP   A NE1   1 
ATOM   2366  C  CE2   . TRP   A  1  334  ? -57.778 61.896  71.677  1.00 15.63 ? 332  TRP   A CE2   1 
ATOM   2367  C  CE3   . TRP   A  1  334  ? -58.822 63.240  73.396  1.00 17.36 ? 332  TRP   A CE3   1 
ATOM   2368  C  CZ2   . TRP   A  1  334  ? -56.503 62.129  72.206  1.00 14.99 ? 332  TRP   A CZ2   1 
ATOM   2369  C  CZ3   . TRP   A  1  334  ? -57.567 63.475  73.912  1.00 17.04 ? 332  TRP   A CZ3   1 
ATOM   2370  C  CH2   . TRP   A  1  334  ? -56.419 62.919  73.321  1.00 17.42 ? 332  TRP   A CH2   1 
ATOM   2371  N  N     . ASN   A  1  335  ? -61.555 59.142  72.897  1.00 16.34 ? 333  ASN   A N     1 
ATOM   2372  C  CA    . ASN   A  1  335  ? -61.021 58.231  73.903  1.00 15.98 ? 333  ASN   A CA    1 
ATOM   2373  C  C     . ASN   A  1  335  ? -59.525 58.015  73.737  1.00 16.39 ? 333  ASN   A C     1 
ATOM   2374  O  O     . ASN   A  1  335  ? -58.977 57.048  74.278  1.00 17.57 ? 333  ASN   A O     1 
ATOM   2375  C  CB    . ASN   A  1  335  ? -61.748 56.888  73.863  1.00 17.55 ? 333  ASN   A CB    1 
ATOM   2376  C  CG    . ASN   A  1  335  ? -63.099 56.948  74.531  1.00 20.39 ? 333  ASN   A CG    1 
ATOM   2377  O  OD1   . ASN   A  1  335  ? -63.324 57.747  75.436  1.00 17.86 ? 333  ASN   A OD1   1 
ATOM   2378  N  ND2   . ASN   A  1  335  ? -64.010 56.088  74.088  1.00 26.99 ? 333  ASN   A ND2   1 
ATOM   2379  N  N     . GLY   A  1  336  ? -58.862 58.885  72.985  1.00 16.79 ? 334  GLY   A N     1 
ATOM   2380  C  CA    . GLY   A  1  336  ? -57.461 58.674  72.699  1.00 14.82 ? 334  GLY   A CA    1 
ATOM   2381  C  C     . GLY   A  1  336  ? -56.493 59.127  73.768  1.00 14.53 ? 334  GLY   A C     1 
ATOM   2382  O  O     . GLY   A  1  336  ? -55.301 58.866  73.623  1.00 14.82 ? 334  GLY   A O     1 
ATOM   2383  N  N     . MET   A  1  337  ? -56.939 59.802  74.824  1.00 15.27 ? 335  MET   A N     1 
ATOM   2384  C  CA    A MET   A  1  337  ? -56.009 60.237  75.858  0.54 15.96 ? 335  MET   A CA    1 
ATOM   2385  C  CA    B MET   A  1  337  ? -55.997 60.232  75.846  0.46 15.97 ? 335  MET   A CA    1 
ATOM   2386  C  C     . MET   A  1  337  ? -55.434 59.028  76.587  1.00 15.88 ? 335  MET   A C     1 
ATOM   2387  O  O     . MET   A  1  337  ? -56.181 58.170  77.074  1.00 16.94 ? 335  MET   A O     1 
ATOM   2388  C  CB    A MET   A  1  337  ? -56.716 61.154  76.851  0.54 18.37 ? 335  MET   A CB    1 
ATOM   2389  C  CB    B MET   A  1  337  ? -56.656 61.190  76.826  0.46 18.34 ? 335  MET   A CB    1 
ATOM   2390  C  CG    A MET   A  1  337  ? -55.786 61.768  77.870  0.54 20.68 ? 335  MET   A CG    1 
ATOM   2391  C  CG    B MET   A  1  337  ? -55.753 61.550  77.980  0.46 20.82 ? 335  MET   A CG    1 
ATOM   2392  S  SD    A MET   A  1  337  ? -54.670 62.919  77.072  0.54 26.47 ? 335  MET   A SD    1 
ATOM   2393  S  SD    B MET   A  1  337  ? -55.847 63.300  78.324  0.46 23.34 ? 335  MET   A SD    1 
ATOM   2394  C  CE    A MET   A  1  337  ? -55.725 64.351  76.879  0.54 23.34 ? 335  MET   A CE    1 
ATOM   2395  C  CE    B MET   A  1  337  ? -55.174 63.953  76.796  0.46 20.11 ? 335  MET   A CE    1 
ATOM   2396  N  N     . GLY   A  1  338  ? -54.111 58.973  76.668  1.00 15.83 ? 336  GLY   A N     1 
ATOM   2397  C  CA    . GLY   A  1  338  ? -53.417 57.872  77.294  1.00 18.04 ? 336  GLY   A CA    1 
ATOM   2398  C  C     . GLY   A  1  338  ? -52.490 58.358  78.386  1.00 16.92 ? 336  GLY   A C     1 
ATOM   2399  O  O     . GLY   A  1  338  ? -52.126 59.534  78.428  1.00 15.88 ? 336  GLY   A O     1 
ATOM   2400  N  N     . PHE   A  1  339  ? -52.130 57.463  79.294  1.00 15.67 ? 337  PHE   A N     1 
ATOM   2401  C  CA    . PHE   A  1  339  ? -51.348 57.849  80.460  1.00 15.57 ? 337  PHE   A CA    1 
ATOM   2402  C  C     . PHE   A  1  339  ? -50.576 56.631  80.930  1.00 15.41 ? 337  PHE   A C     1 
ATOM   2403  O  O     . PHE   A  1  339  ? -51.144 55.545  81.055  1.00 15.91 ? 337  PHE   A O     1 
ATOM   2404  C  CB    . PHE   A  1  339  ? -52.308 58.321  81.554  1.00 15.09 ? 337  PHE   A CB    1 
ATOM   2405  C  CG    . PHE   A  1  339  ? -51.632 58.977  82.722  1.00 16.65 ? 337  PHE   A CG    1 
ATOM   2406  C  CD1   . PHE   A  1  339  ? -51.340 60.335  82.681  1.00 16.77 ? 337  PHE   A CD1   1 
ATOM   2407  C  CD2   . PHE   A  1  339  ? -51.327 58.257  83.866  1.00 17.21 ? 337  PHE   A CD2   1 
ATOM   2408  C  CE1   . PHE   A  1  339  ? -50.738 60.958  83.767  1.00 16.82 ? 337  PHE   A CE1   1 
ATOM   2409  C  CE2   . PHE   A  1  339  ? -50.717 58.883  84.960  1.00 17.99 ? 337  PHE   A CE2   1 
ATOM   2410  C  CZ    . PHE   A  1  339  ? -50.426 60.240  84.891  1.00 17.73 ? 337  PHE   A CZ    1 
ATOM   2411  N  N     . VAL   A  1  340  ? -49.279 56.798  81.160  1.00 14.55 ? 338  VAL   A N     1 
ATOM   2412  C  CA    . VAL   A  1  340  ? -48.427 55.703  81.594  1.00 16.54 ? 338  VAL   A CA    1 
ATOM   2413  C  C     . VAL   A  1  340  ? -48.424 55.628  83.110  1.00 14.02 ? 338  VAL   A C     1 
ATOM   2414  O  O     . VAL   A  1  340  ? -48.392 56.657  83.800  1.00 17.05 ? 338  VAL   A O     1 
ATOM   2415  C  CB    . VAL   A  1  340  ? -47.002 55.926  81.082  1.00 15.54 ? 338  VAL   A CB    1 
ATOM   2416  C  CG1   . VAL   A  1  340  ? -46.069 54.814  81.591  1.00 16.03 ? 338  VAL   A CG1   1 
ATOM   2417  C  CG2   . VAL   A  1  340  ? -47.014 55.999  79.571  1.00 15.77 ? 338  VAL   A CG2   1 
ATOM   2418  N  N     . VAL   A  1  341  ? -48.439 54.408  83.631  1.00 15.41 ? 339  VAL   A N     1 
ATOM   2419  C  CA    . VAL   A  1  341  ? -48.199 54.170  85.047  1.00 16.17 ? 339  VAL   A CA    1 
ATOM   2420  C  C     . VAL   A  1  341  ? -47.074 53.155  85.196  1.00 16.72 ? 339  VAL   A C     1 
ATOM   2421  O  O     . VAL   A  1  341  ? -47.014 52.159  84.463  1.00 16.21 ? 339  VAL   A O     1 
ATOM   2422  C  CB    . VAL   A  1  341  ? -49.456 53.716  85.807  1.00 18.15 ? 339  VAL   A CB    1 
ATOM   2423  C  CG1   . VAL   A  1  341  ? -49.187 53.763  87.280  1.00 23.05 ? 339  VAL   A CG1   1 
ATOM   2424  C  CG2   . VAL   A  1  341  ? -50.625 54.628  85.476  1.00 19.72 ? 339  VAL   A CG2   1 
ATOM   2425  N  N     . GLN   A  1  342  ? -46.176 53.422  86.144  1.00 15.63 ? 340  GLN   A N     1 
ATOM   2426  C  CA    . GLN   A  1  342  ? -44.929 52.681  86.302  1.00 16.56 ? 340  GLN   A CA    1 
ATOM   2427  C  C     . GLN   A  1  342  ? -45.077 51.693  87.447  1.00 15.07 ? 340  GLN   A C     1 
ATOM   2428  O  O     . GLN   A  1  342  ? -45.181 52.091  88.611  1.00 17.09 ? 340  GLN   A O     1 
ATOM   2429  C  CB    . GLN   A  1  342  ? -43.790 53.652  86.581  1.00 16.11 ? 340  GLN   A CB    1 
ATOM   2430  C  CG    . GLN   A  1  342  ? -43.476 54.594  85.408  1.00 15.82 ? 340  GLN   A CG    1 
ATOM   2431  C  CD    . GLN   A  1  342  ? -42.934 55.918  85.889  1.00 16.11 ? 340  GLN   A CD    1 
ATOM   2432  O  OE1   . GLN   A  1  342  ? -43.462 56.498  86.840  1.00 16.90 ? 340  GLN   A OE1   1 
ATOM   2433  N  NE2   . GLN   A  1  342  ? -41.876 56.410  85.233  1.00 15.92 ? 340  GLN   A NE2   1 
ATOM   2434  N  N     . ALA   A  1  343  ? -45.088 50.406  87.107  1.00 14.31 ? 341  ALA   A N     1 
ATOM   2435  C  CA    . ALA   A  1  343  ? -45.280 49.361  88.104  1.00 16.44 ? 341  ALA   A CA    1 
ATOM   2436  C  C     . ALA   A  1  343  ? -44.112 49.239  89.073  1.00 17.84 ? 341  ALA   A C     1 
ATOM   2437  O  O     . ALA   A  1  343  ? -44.266 48.608  90.129  1.00 17.64 ? 341  ALA   A O     1 
ATOM   2438  C  CB    . ALA   A  1  343  ? -45.495 48.024  87.411  1.00 18.39 ? 341  ALA   A CB    1 
ATOM   2439  N  N     . TYR   A  1  344  ? -42.954 49.816  88.755  1.00 16.33 ? 342  TYR   A N     1 
ATOM   2440  C  CA    . TYR   A  1  344  ? -41.888 49.815  89.748  1.00 16.51 ? 342  TYR   A CA    1 
ATOM   2441  C  C     . TYR   A  1  344  ? -42.159 50.786  90.879  1.00 19.31 ? 342  TYR   A C     1 
ATOM   2442  O  O     . TYR   A  1  344  ? -41.418 50.779  91.860  1.00 18.93 ? 342  TYR   A O     1 
ATOM   2443  C  CB    . TYR   A  1  344  ? -40.494 50.008  89.133  1.00 17.10 ? 342  TYR   A CB    1 
ATOM   2444  C  CG    . TYR   A  1  344  ? -40.077 51.389  88.631  1.00 14.35 ? 342  TYR   A CG    1 
ATOM   2445  C  CD1   . TYR   A  1  344  ? -40.935 52.489  88.614  1.00 15.80 ? 342  TYR   A CD1   1 
ATOM   2446  C  CD2   . TYR   A  1  344  ? -38.775 51.566  88.149  1.00 15.89 ? 342  TYR   A CD2   1 
ATOM   2447  C  CE1   . TYR   A  1  344  ? -40.497 53.716  88.117  1.00 15.37 ? 342  TYR   A CE1   1 
ATOM   2448  C  CE2   . TYR   A  1  344  ? -38.339 52.765  87.660  1.00 17.74 ? 342  TYR   A CE2   1 
ATOM   2449  C  CZ    . TYR   A  1  344  ? -39.182 53.840  87.654  1.00 16.73 ? 342  TYR   A CZ    1 
ATOM   2450  O  OH    . TYR   A  1  344  ? -38.703 55.024  87.161  1.00 15.68 ? 342  TYR   A OH    1 
ATOM   2451  N  N     . GLY   A  1  345  ? -43.215 51.586  90.774  1.00 16.36 ? 343  GLY   A N     1 
ATOM   2452  C  CA    . GLY   A  1  345  ? -43.530 52.591  91.770  1.00 16.76 ? 343  GLY   A CA    1 
ATOM   2453  C  C     . GLY   A  1  345  ? -44.522 52.054  92.788  1.00 18.83 ? 343  GLY   A C     1 
ATOM   2454  O  O     . GLY   A  1  345  ? -45.475 51.354  92.437  1.00 18.02 ? 343  GLY   A O     1 
ATOM   2455  N  N     . LYS   A  1  346  ? -44.283 52.409  94.048  1.00 18.06 ? 344  LYS   A N     1 
ATOM   2456  C  CA    . LYS   A  1  346  ? -45.112 51.909  95.132  1.00 17.72 ? 344  LYS   A CA    1 
ATOM   2457  C  C     . LYS   A  1  346  ? -46.534 52.434  95.061  1.00 20.07 ? 344  LYS   A C     1 
ATOM   2458  O  O     . LYS   A  1  346  ? -47.435 51.840  95.657  1.00 19.39 ? 344  LYS   A O     1 
ATOM   2459  C  CB    . LYS   A  1  346  ? -44.489 52.293  96.467  1.00 19.52 ? 344  LYS   A CB    1 
ATOM   2460  C  CG    . LYS   A  1  346  ? -43.111 51.726  96.631  1.00 20.79 ? 344  LYS   A CG    1 
ATOM   2461  C  CD    . LYS   A  1  346  ? -42.505 52.183  97.924  1.00 19.48 ? 344  LYS   A CD    1 
ATOM   2462  C  CE    . LYS   A  1  346  ? -41.247 51.385  98.204  1.00 19.83 ? 344  LYS   A CE    1 
ATOM   2463  N  NZ    . LYS   A  1  346  ? -40.517 51.971  99.364  1.00 21.86 ? 344  LYS   A NZ    1 
ATOM   2464  N  N     . ARG   A  1  347  ? -46.748 53.535  94.360  1.00 15.91 ? 345  ARG   A N     1 
ATOM   2465  C  CA    . ARG   A  1  347  ? -48.079 54.115  94.242  1.00 17.91 ? 345  ARG   A CA    1 
ATOM   2466  C  C     . ARG   A  1  347  ? -48.899 53.524  93.109  1.00 16.87 ? 345  ARG   A C     1 
ATOM   2467  O  O     . ARG   A  1  347  ? -50.100 53.800  93.039  1.00 18.10 ? 345  ARG   A O     1 
ATOM   2468  C  CB    . ARG   A  1  347  ? -47.975 55.634  94.070  1.00 17.01 ? 345  ARG   A CB    1 
ATOM   2469  C  CG    . ARG   A  1  347  ? -47.420 56.313  95.313  1.00 17.28 ? 345  ARG   A CG    1 
ATOM   2470  C  CD    . ARG   A  1  347  ? -47.024 57.745  95.025  1.00 16.56 ? 345  ARG   A CD    1 
ATOM   2471  N  NE    . ARG   A  1  347  ? -45.802 57.798  94.224  1.00 16.85 ? 345  ARG   A NE    1 
ATOM   2472  C  CZ    . ARG   A  1  347  ? -45.344 58.901  93.646  1.00 17.06 ? 345  ARG   A CZ    1 
ATOM   2473  N  NH1   . ARG   A  1  347  ? -45.956 60.063  93.796  1.00 18.19 ? 345  ARG   A NH1   1 
ATOM   2474  N  NH2   . ARG   A  1  347  ? -44.241 58.833  92.898  1.00 16.03 ? 345  ARG   A NH2   1 
ATOM   2475  N  N     . CYS   A  1  348  ? -48.307 52.708  92.249  1.00 16.82 ? 346  CYS   A N     1 
ATOM   2476  C  CA    . CYS   A  1  348  ? -48.948 52.224  91.028  1.00 17.81 ? 346  CYS   A CA    1 
ATOM   2477  C  C     . CYS   A  1  348  ? -50.398 51.763  91.200  1.00 17.94 ? 346  CYS   A C     1 
ATOM   2478  O  O     . CYS   A  1  348  ? -51.277 52.237  90.471  1.00 18.73 ? 346  CYS   A O     1 
ATOM   2479  C  CB    . CYS   A  1  348  ? -48.108 51.118  90.382  1.00 20.27 ? 346  CYS   A CB    1 
ATOM   2480  S  SG    . CYS   A  1  348  ? -48.591 50.816  88.673  1.00 24.31 ? 346  CYS   A SG    1 
ATOM   2481  N  N     . PRO   A  1  349  ? -50.699 50.830  92.108  1.00 18.82 ? 347  PRO   A N     1 
ATOM   2482  C  CA    . PRO   A  1  349  ? -52.092 50.371  92.204  1.00 18.15 ? 347  PRO   A CA    1 
ATOM   2483  C  C     . PRO   A  1  349  ? -53.052 51.468  92.615  1.00 17.27 ? 347  PRO   A C     1 
ATOM   2484  O  O     . PRO   A  1  349  ? -54.200 51.477  92.158  1.00 19.49 ? 347  PRO   A O     1 
ATOM   2485  C  CB    . PRO   A  1  349  ? -52.037 49.220  93.223  1.00 19.47 ? 347  PRO   A CB    1 
ATOM   2486  C  CG    . PRO   A  1  349  ? -50.774 49.419  93.971  1.00 20.87 ? 347  PRO   A CG    1 
ATOM   2487  C  CD    . PRO   A  1  349  ? -49.828 50.181  93.106  1.00 18.64 ? 347  PRO   A CD    1 
ATOM   2488  N  N     . PHE   A  1  350  ? -52.600 52.407  93.441  1.00 19.26 ? 348  PHE   A N     1 
ATOM   2489  C  CA    . PHE   A  1  350  ? -53.435 53.512  93.889  1.00 19.04 ? 348  PHE   A CA    1 
ATOM   2490  C  C     . PHE   A  1  350  ? -53.610 54.552  92.801  1.00 17.26 ? 348  PHE   A C     1 
ATOM   2491  O  O     . PHE   A  1  350  ? -54.684 55.151  92.677  1.00 17.80 ? 348  PHE   A O     1 
ATOM   2492  C  CB    . PHE   A  1  350  ? -52.809 54.107  95.143  1.00 18.65 ? 348  PHE   A CB    1 
ATOM   2493  C  CG    . PHE   A  1  350  ? -52.487 53.069  96.166  1.00 19.76 ? 348  PHE   A CG    1 
ATOM   2494  C  CD1   . PHE   A  1  350  ? -53.498 52.541  96.951  1.00 20.74 ? 348  PHE   A CD1   1 
ATOM   2495  C  CD2   . PHE   A  1  350  ? -51.203 52.581  96.312  1.00 20.74 ? 348  PHE   A CD2   1 
ATOM   2496  C  CE1   . PHE   A  1  350  ? -53.231 51.567  97.880  1.00 24.52 ? 348  PHE   A CE1   1 
ATOM   2497  C  CE2   . PHE   A  1  350  ? -50.928 51.583  97.244  1.00 23.15 ? 348  PHE   A CE2   1 
ATOM   2498  C  CZ    . PHE   A  1  350  ? -51.943 51.085  98.026  1.00 25.25 ? 348  PHE   A CZ    1 
ATOM   2499  N  N     . VAL   A  1  351  ? -52.578 54.741  91.987  1.00 16.32 ? 349  VAL   A N     1 
ATOM   2500  C  CA    . VAL   A  1  351  ? -52.706 55.572  90.800  1.00 17.05 ? 349  VAL   A CA    1 
ATOM   2501  C  C     . VAL   A  1  351  ? -53.724 54.963  89.849  1.00 17.86 ? 349  VAL   A C     1 
ATOM   2502  O  O     . VAL   A  1  351  ? -54.574 55.664  89.285  1.00 18.50 ? 349  VAL   A O     1 
ATOM   2503  C  CB    . VAL   A  1  351  ? -51.330 55.720  90.127  1.00 16.51 ? 349  VAL   A CB    1 
ATOM   2504  C  CG1   . VAL   A  1  351  ? -51.482 56.466  88.811  1.00 17.27 ? 349  VAL   A CG1   1 
ATOM   2505  C  CG2   . VAL   A  1  351  ? -50.359 56.454  91.040  1.00 18.71 ? 349  VAL   A CG2   1 
ATOM   2506  N  N     . LEU   A  1  352  ? -53.652 53.644  89.652  1.00 18.72 ? 350  LEU   A N     1 
ATOM   2507  C  CA    . LEU   A  1  352  ? -54.615 52.986  88.784  1.00 18.08 ? 350  LEU   A CA    1 
ATOM   2508  C  C     . LEU   A  1  352  ? -56.033 53.128  89.324  1.00 19.20 ? 350  LEU   A C     1 
ATOM   2509  O  O     . LEU   A  1  352  ? -56.975 53.356  88.554  1.00 19.46 ? 350  LEU   A O     1 
ATOM   2510  C  CB    . LEU   A  1  352  ? -54.249 51.515  88.609  1.00 17.70 ? 350  LEU   A CB    1 
ATOM   2511  C  CG    . LEU   A  1  352  ? -53.033 51.282  87.729  1.00 20.15 ? 350  LEU   A CG    1 
ATOM   2512  C  CD1   . LEU   A  1  352  ? -52.713 49.806  87.705  1.00 22.91 ? 350  LEU   A CD1   1 
ATOM   2513  C  CD2   . LEU   A  1  352  ? -53.273 51.808  86.323  1.00 21.03 ? 350  LEU   A CD2   1 
ATOM   2514  N  N     . ASP   A  1  353  ? -56.211 52.999  90.644  1.00 19.34 ? 351  ASP   A N     1 
ATOM   2515  C  CA    . ASP   A  1  353  ? -57.540 53.215  91.214  1.00 19.26 ? 351  ASP   A CA    1 
ATOM   2516  C  C     . ASP   A  1  353  ? -58.039 54.613  90.886  1.00 18.33 ? 351  ASP   A C     1 
ATOM   2517  O  O     . ASP   A  1  353  ? -59.211 54.803  90.530  1.00 18.70 ? 351  ASP   A O     1 
ATOM   2518  C  CB    . ASP   A  1  353  ? -57.510 53.038  92.729  1.00 18.89 ? 351  ASP   A CB    1 
ATOM   2519  C  CG    . ASP   A  1  353  ? -57.304 51.605  93.150  1.00 23.88 ? 351  ASP   A CG    1 
ATOM   2520  O  OD1   . ASP   A  1  353  ? -57.630 50.692  92.367  1.00 24.61 ? 351  ASP   A OD1   1 
ATOM   2521  O  OD2   . ASP   A  1  353  ? -56.810 51.398  94.276  1.00 27.49 ? 351  ASP   A OD2   1 
ATOM   2522  N  N     . PHE   A  1  354  ? -57.162 55.604  91.014  1.00 17.52 ? 352  PHE   A N     1 
ATOM   2523  C  CA    . PHE   A  1  354  ? -57.535 56.974  90.700  1.00 16.95 ? 352  PHE   A CA    1 
ATOM   2524  C  C     . PHE   A  1  354  ? -57.903 57.112  89.229  1.00 16.68 ? 352  PHE   A C     1 
ATOM   2525  O  O     . PHE   A  1  354  ? -58.914 57.729  88.890  1.00 18.15 ? 352  PHE   A O     1 
ATOM   2526  C  CB    . PHE   A  1  354  ? -56.383 57.922  91.056  1.00 16.74 ? 352  PHE   A CB    1 
ATOM   2527  C  CG    . PHE   A  1  354  ? -56.552 59.299  90.500  1.00 18.35 ? 352  PHE   A CG    1 
ATOM   2528  C  CD1   . PHE   A  1  354  ? -57.294 60.246  91.184  1.00 19.53 ? 352  PHE   A CD1   1 
ATOM   2529  C  CD2   . PHE   A  1  354  ? -55.991 59.638  89.281  1.00 21.07 ? 352  PHE   A CD2   1 
ATOM   2530  C  CE1   . PHE   A  1  354  ? -57.475 61.519  90.660  1.00 22.27 ? 352  PHE   A CE1   1 
ATOM   2531  C  CE2   . PHE   A  1  354  ? -56.160 60.899  88.751  1.00 20.40 ? 352  PHE   A CE2   1 
ATOM   2532  C  CZ    . PHE   A  1  354  ? -56.912 61.842  89.437  1.00 20.88 ? 352  PHE   A CZ    1 
ATOM   2533  N  N     . ILE   A  1  355  ? -57.079 56.560  88.339  1.00 15.93 ? 353  ILE   A N     1 
ATOM   2534  C  CA    . ILE   A  1  355  ? -57.338 56.696  86.907  1.00 16.06 ? 353  ILE   A CA    1 
ATOM   2535  C  C     . ILE   A  1  355  ? -58.623 55.989  86.517  1.00 18.12 ? 353  ILE   A C     1 
ATOM   2536  O  O     . ILE   A  1  355  ? -59.396 56.491  85.695  1.00 17.49 ? 353  ILE   A O     1 
ATOM   2537  C  CB    . ILE   A  1  355  ? -56.149 56.174  86.086  1.00 18.19 ? 353  ILE   A CB    1 
ATOM   2538  C  CG1   . ILE   A  1  355  ? -54.932 57.058  86.313  1.00 19.05 ? 353  ILE   A CG1   1 
ATOM   2539  C  CG2   . ILE   A  1  355  ? -56.514 56.122  84.606  1.00 17.58 ? 353  ILE   A CG2   1 
ATOM   2540  C  CD1   . ILE   A  1  355  ? -53.689 56.518  85.657  1.00 19.39 ? 353  ILE   A CD1   1 
ATOM   2541  N  N     . ILE   A  1  356  ? -58.831 54.780  87.035  1.00 20.03 ? 354  ILE   A N     1 
ATOM   2542  C  CA    . ILE   A  1  356  ? -60.047 54.051  86.717  1.00 17.46 ? 354  ILE   A CA    1 
ATOM   2543  C  C     . ILE   A  1  356  ? -61.259 54.837  87.171  1.00 18.58 ? 354  ILE   A C     1 
ATOM   2544  O  O     . ILE   A  1  356  ? -62.249 54.949  86.442  1.00 18.74 ? 354  ILE   A O     1 
ATOM   2545  C  CB    . ILE   A  1  356  ? -60.002 52.640  87.330  1.00 18.56 ? 354  ILE   A CB    1 
ATOM   2546  C  CG1   . ILE   A  1  356  ? -58.952 51.797  86.599  1.00 20.25 ? 354  ILE   A CG1   1 
ATOM   2547  C  CG2   . ILE   A  1  356  ? -61.387 52.003  87.297  1.00 21.73 ? 354  ILE   A CG2   1 
ATOM   2548  C  CD1   . ILE   A  1  356  ? -58.581 50.516  87.348  1.00 21.55 ? 354  ILE   A CD1   1 
ATOM   2549  N  N     . ASP   A  1  357  ? -61.183 55.429  88.361  1.00 16.76 ? 355  ASP   A N     1 
ATOM   2550  C  CA    . ASP   A  1  357  ? -62.289 56.250  88.832  1.00 17.96 ? 355  ASP   A CA    1 
ATOM   2551  C  C     . ASP   A  1  357  ? -62.452 57.500  87.976  1.00 18.54 ? 355  ASP   A C     1 
ATOM   2552  O  O     . ASP   A  1  357  ? -63.582 57.913  87.683  1.00 19.28 ? 355  ASP   A O     1 
ATOM   2553  C  CB    . ASP   A  1  357  ? -62.096 56.627  90.296  1.00 22.16 ? 355  ASP   A CB    1 
ATOM   2554  C  CG    . ASP   A  1  357  ? -63.137 57.618  90.771  1.00 21.00 ? 355  ASP   A CG    1 
ATOM   2555  O  OD1   . ASP   A  1  357  ? -64.265 57.184  91.093  1.00 25.56 ? 355  ASP   A OD1   1 
ATOM   2556  O  OD2   . ASP   A  1  357  ? -62.849 58.834  90.788  1.00 22.36 ? 355  ASP   A OD2   1 
ATOM   2557  N  N     . LEU   A  1  358  ? -61.338 58.105  87.555  1.00 18.12 ? 356  LEU   A N     1 
ATOM   2558  C  CA    . LEU   A  1  358  ? -61.429 59.271  86.683  1.00 16.30 ? 356  LEU   A CA    1 
ATOM   2559  C  C     . LEU   A  1  358  ? -62.061 58.900  85.350  1.00 17.66 ? 356  LEU   A C     1 
ATOM   2560  O  O     . LEU   A  1  358  ? -62.883 59.652  84.811  1.00 18.16 ? 356  LEU   A O     1 
ATOM   2561  C  CB    . LEU   A  1  358  ? -60.040 59.868  86.464  1.00 16.29 ? 356  LEU   A CB    1 
ATOM   2562  C  CG    . LEU   A  1  358  ? -59.964 61.005  85.449  1.00 17.19 ? 356  LEU   A CG    1 
ATOM   2563  C  CD1   . LEU   A  1  358  ? -60.831 62.192  85.859  1.00 21.56 ? 356  LEU   A CD1   1 
ATOM   2564  C  CD2   . LEU   A  1  358  ? -58.480 61.436  85.285  1.00 18.23 ? 356  LEU   A CD2   1 
ATOM   2565  N  N     . ALA   A  1  359  ? -61.717 57.723  84.825  1.00 18.70 ? 357  ALA   A N     1 
ATOM   2566  C  CA    . ALA   A  1  359  ? -62.332 57.260  83.590  1.00 17.76 ? 357  ALA   A CA    1 
ATOM   2567  C  C     . ALA   A  1  359  ? -63.832 57.107  83.764  1.00 18.22 ? 357  ALA   A C     1 
ATOM   2568  O  O     . ALA   A  1  359  ? -64.604 57.477  82.877  1.00 19.22 ? 357  ALA   A O     1 
ATOM   2569  C  CB    . ALA   A  1  359  ? -61.710 55.931  83.167  1.00 20.16 ? 357  ALA   A CB    1 
ATOM   2570  N  N     . ARG   A  1  360  ? -64.261 56.570  84.912  1.00 19.00 ? 358  ARG   A N     1 
ATOM   2571  C  CA    . ARG   A  1  360  ? -65.691 56.432  85.168  1.00 19.57 ? 358  ARG   A CA    1 
ATOM   2572  C  C     . ARG   A  1  360  ? -66.366 57.793  85.274  1.00 20.90 ? 358  ARG   A C     1 
ATOM   2573  O  O     . ARG   A  1  360  ? -67.438 58.016  84.696  1.00 23.56 ? 358  ARG   A O     1 
ATOM   2574  C  CB    . ARG   A  1  360  ? -65.925 55.625  86.446  1.00 22.43 ? 358  ARG   A CB    1 
ATOM   2575  C  CG    . ARG   A  1  360  ? -65.489 54.183  86.364  1.00 25.65 ? 358  ARG   A CG    1 
ATOM   2576  C  CD    . ARG   A  1  360  ? -66.007 53.397  87.566  1.00 28.68 ? 358  ARG   A CD    1 
ATOM   2577  N  NE    . ARG   A  1  360  ? -65.338 52.106  87.672  1.00 32.95 ? 358  ARG   A NE    1 
ATOM   2578  C  CZ    . ARG   A  1  360  ? -65.710 51.014  87.018  1.00 38.94 ? 358  ARG   A CZ    1 
ATOM   2579  N  NH1   . ARG   A  1  360  ? -66.793 51.000  86.254  1.00 39.74 ? 358  ARG   A NH1   1 
ATOM   2580  N  NH2   . ARG   A  1  360  ? -64.977 49.910  87.132  1.00 35.30 ? 358  ARG   A NH2   1 
ATOM   2581  N  N     . ARG   A  1  361  ? -65.759 58.715  86.022  1.00 20.23 ? 359  ARG   A N     1 
ATOM   2582  C  CA    . ARG   A  1  361  ? -66.354 60.038  86.207  1.00 19.53 ? 359  ARG   A CA    1 
ATOM   2583  C  C     . ARG   A  1  361  ? -66.448 60.792  84.889  1.00 20.78 ? 359  ARG   A C     1 
ATOM   2584  O  O     . ARG   A  1  361  ? -67.473 61.420  84.583  1.00 22.20 ? 359  ARG   A O     1 
ATOM   2585  C  CB    . ARG   A  1  361  ? -65.514 60.845  87.200  1.00 23.27 ? 359  ARG   A CB    1 
ATOM   2586  C  CG    . ARG   A  1  361  ? -65.639 60.393  88.640  1.00 25.13 ? 359  ARG   A CG    1 
ATOM   2587  C  CD    . ARG   A  1  361  ? -64.917 61.354  89.567  1.00 26.03 ? 359  ARG   A CD    1 
ATOM   2588  N  NE    . ARG   A  1  361  ? -63.462 61.232  89.499  1.00 24.34 ? 359  ARG   A NE    1 
ATOM   2589  C  CZ    . ARG   A  1  361  ? -62.637 62.231  89.217  1.00 23.65 ? 359  ARG   A CZ    1 
ATOM   2590  N  NH1   . ARG   A  1  361  ? -63.087 63.416  88.839  1.00 21.86 ? 359  ARG   A NH1   1 
ATOM   2591  N  NH2   . ARG   A  1  361  ? -61.326 62.044  89.337  1.00 22.92 ? 359  ARG   A NH2   1 
ATOM   2592  N  N     . SER   A  1  362  ? -65.376 60.771  84.109  1.00 19.21 ? 360  SER   A N     1 
ATOM   2593  C  CA    . SER   A  1  362  ? -65.337 61.552  82.886  1.00 18.80 ? 360  SER   A CA    1 
ATOM   2594  C  C     . SER   A  1  362  ? -66.031 60.859  81.726  1.00 19.77 ? 360  SER   A C     1 
ATOM   2595  O  O     . SER   A  1  362  ? -66.355 61.519  80.734  1.00 21.05 ? 360  SER   A O     1 
ATOM   2596  C  CB    . SER   A  1  362  ? -63.875 61.795  82.508  1.00 19.28 ? 360  SER   A CB    1 
ATOM   2597  O  OG    . SER   A  1  362  ? -63.238 60.559  82.212  1.00 18.34 ? 360  SER   A OG    1 
ATOM   2598  N  N     . GLY   A  1  363  ? -66.248 59.550  81.819  1.00 19.78 ? 361  GLY   A N     1 
ATOM   2599  C  CA    . GLY   A  1  363  ? -66.742 58.796  80.688  1.00 21.23 ? 361  GLY   A CA    1 
ATOM   2600  C  C     . GLY   A  1  363  ? -65.739 58.584  79.579  1.00 22.81 ? 361  GLY   A C     1 
ATOM   2601  O  O     . GLY   A  1  363  ? -66.124 58.144  78.488  1.00 23.01 ? 361  GLY   A O     1 
ATOM   2602  N  N     . ARG   A  1  364  ? -64.470 58.896  79.824  1.00 18.77 ? 362  ARG   A N     1 
ATOM   2603  C  CA    . ARG   A  1  364  ? -63.407 58.721  78.842  1.00 18.77 ? 362  ARG   A CA    1 
ATOM   2604  C  C     . ARG   A  1  364  ? -62.761 57.373  79.095  1.00 20.00 ? 362  ARG   A C     1 
ATOM   2605  O  O     . ARG   A  1  364  ? -62.392 57.067  80.232  1.00 21.64 ? 362  ARG   A O     1 
ATOM   2606  C  CB    . ARG   A  1  364  ? -62.327 59.785  79.034  1.00 21.90 ? 362  ARG   A CB    1 
ATOM   2607  C  CG    . ARG   A  1  364  ? -62.806 61.219  79.080  1.00 27.10 ? 362  ARG   A CG    1 
ATOM   2608  C  CD    . ARG   A  1  364  ? -62.746 61.891  77.727  1.00 19.53 ? 362  ARG   A CD    1 
ATOM   2609  N  NE    . ARG   A  1  364  ? -63.557 63.101  77.757  1.00 18.85 ? 362  ARG   A NE    1 
ATOM   2610  C  CZ    . ARG   A  1  364  ? -63.079 64.328  77.903  1.00 19.25 ? 362  ARG   A CZ    1 
ATOM   2611  N  NH1   . ARG   A  1  364  ? -61.776 64.570  77.896  1.00 16.36 ? 362  ARG   A NH1   1 
ATOM   2612  N  NH2   . ARG   A  1  364  ? -63.930 65.336  78.063  1.00 18.46 ? 362  ARG   A NH2   1 
ATOM   2613  N  N     . ARG   A  1  365  ? -62.604 56.576  78.044  1.00 18.04 ? 363  ARG   A N     1 
ATOM   2614  C  CA    . ARG   A  1  365  ? -61.939 55.287  78.200  1.00 17.59 ? 363  ARG   A CA    1 
ATOM   2615  C  C     . ARG   A  1  365  ? -60.438 55.536  78.126  1.00 18.86 ? 363  ARG   A C     1 
ATOM   2616  O  O     . ARG   A  1  365  ? -59.821 55.473  77.062  1.00 19.11 ? 363  ARG   A O     1 
ATOM   2617  C  CB    . ARG   A  1  365  ? -62.391 54.304  77.132  1.00 18.15 ? 363  ARG   A CB    1 
ATOM   2618  C  CG    . ARG   A  1  365  ? -61.803 52.926  77.319  1.00 19.64 ? 363  ARG   A CG    1 
ATOM   2619  C  CD    . ARG   A  1  365  ? -62.680 51.892  76.675  1.00 23.26 ? 363  ARG   A CD    1 
ATOM   2620  N  NE    . ARG   A  1  365  ? -62.187 50.554  76.972  1.00 21.44 ? 363  ARG   A NE    1 
ATOM   2621  C  CZ    . ARG   A  1  365  ? -61.473 49.831  76.121  1.00 21.48 ? 363  ARG   A CZ    1 
ATOM   2622  N  NH1   . ARG   A  1  365  ? -61.224 50.260  74.893  1.00 21.79 ? 363  ARG   A NH1   1 
ATOM   2623  N  NH2   . ARG   A  1  365  ? -61.005 48.651  76.509  1.00 19.99 ? 363  ARG   A NH2   1 
ATOM   2624  N  N     . ILE   A  1  366  ? -59.846 55.840  79.275  1.00 16.54 ? 364  ILE   A N     1 
ATOM   2625  C  CA    . ILE   A  1  366  ? -58.450 56.253  79.304  1.00 17.59 ? 364  ILE   A CA    1 
ATOM   2626  C  C     . ILE   A  1  366  ? -57.572 55.100  78.859  1.00 18.92 ? 364  ILE   A C     1 
ATOM   2627  O  O     . ILE   A  1  366  ? -57.735 53.961  79.312  1.00 16.47 ? 364  ILE   A O     1 
ATOM   2628  C  CB    . ILE   A  1  366  ? -58.072 56.760  80.701  1.00 16.61 ? 364  ILE   A CB    1 
ATOM   2629  C  CG1   . ILE   A  1  366  ? -58.927 57.989  81.040  1.00 17.96 ? 364  ILE   A CG1   1 
ATOM   2630  C  CG2   . ILE   A  1  366  ? -56.563 57.077  80.776  1.00 19.20 ? 364  ILE   A CG2   1 
ATOM   2631  C  CD1   . ILE   A  1  366  ? -58.785 58.471  82.479  1.00 18.98 ? 364  ILE   A CD1   1 
ATOM   2632  N  N     . MET   A  1  367  ? -56.647 55.386  77.952  1.00 16.49 ? 365  MET   A N     1 
ATOM   2633  C  CA    . MET   A  1  367  ? -55.674 54.388  77.533  1.00 16.62 ? 365  MET   A CA    1 
ATOM   2634  C  C     . MET   A  1  367  ? -54.565 54.372  78.568  1.00 17.89 ? 365  MET   A C     1 
ATOM   2635  O  O     . MET   A  1  367  ? -53.908 55.387  78.795  1.00 20.67 ? 365  MET   A O     1 
ATOM   2636  C  CB    . MET   A  1  367  ? -55.123 54.732  76.154  1.00 17.46 ? 365  MET   A CB    1 
ATOM   2637  C  CG    . MET   A  1  367  ? -56.229 54.997  75.130  1.00 18.19 ? 365  MET   A CG    1 
ATOM   2638  S  SD    . MET   A  1  367  ? -55.625 55.371  73.468  1.00 20.24 ? 365  MET   A SD    1 
ATOM   2639  C  CE    . MET   A  1  367  ? -55.489 53.766  72.682  1.00 22.05 ? 365  MET   A CE    1 
ATOM   2640  N  N     . VAL   A  1  368  ? -54.377 53.246  79.231  1.00 14.81 ? 366  VAL   A N     1 
ATOM   2641  C  CA    . VAL   A  1  368  ? -53.435 53.173  80.336  1.00 14.04 ? 366  VAL   A CA    1 
ATOM   2642  C  C     . VAL   A  1  368  ? -52.305 52.258  79.911  1.00 16.02 ? 366  VAL   A C     1 
ATOM   2643  O  O     . VAL   A  1  368  ? -52.504 51.045  79.747  1.00 16.83 ? 366  VAL   A O     1 
ATOM   2644  C  CB    . VAL   A  1  368  ? -54.096 52.664  81.622  1.00 16.25 ? 366  VAL   A CB    1 
ATOM   2645  C  CG1   . VAL   A  1  368  ? -53.043 52.529  82.711  1.00 18.57 ? 366  VAL   A CG1   1 
ATOM   2646  C  CG2   . VAL   A  1  368  ? -55.224 53.591  82.054  1.00 20.03 ? 366  VAL   A CG2   1 
ATOM   2647  N  N     . ARG   A  1  369  ? -51.116 52.825  79.746  1.00 15.14 ? 367  ARG   A N     1 
ATOM   2648  C  CA    . ARG   A  1  369  ? -49.940 52.034  79.415  1.00 16.70 ? 367  ARG   A CA    1 
ATOM   2649  C  C     . ARG   A  1  369  ? -49.265 51.637  80.715  1.00 17.75 ? 367  ARG   A C     1 
ATOM   2650  O  O     . ARG   A  1  369  ? -48.759 52.491  81.445  1.00 18.04 ? 367  ARG   A O     1 
ATOM   2651  C  CB    . ARG   A  1  369  ? -48.969 52.800  78.529  1.00 17.38 ? 367  ARG   A CB    1 
ATOM   2652  C  CG    . ARG   A  1  369  ? -47.777 51.924  78.168  1.00 17.89 ? 367  ARG   A CG    1 
ATOM   2653  C  CD    . ARG   A  1  369  ? -46.589 52.724  77.689  1.00 17.48 ? 367  ARG   A CD    1 
ATOM   2654  N  NE    . ARG   A  1  369  ? -46.904 53.402  76.444  1.00 16.64 ? 367  ARG   A NE    1 
ATOM   2655  C  CZ    . ARG   A  1  369  ? -46.352 54.545  76.065  1.00 17.98 ? 367  ARG   A CZ    1 
ATOM   2656  N  NH1   . ARG   A  1  369  ? -45.436 55.149  76.808  1.00 19.23 ? 367  ARG   A NH1   1 
ATOM   2657  N  NH2   . ARG   A  1  369  ? -46.741 55.103  74.921  1.00 17.17 ? 367  ARG   A NH2   1 
ATOM   2658  N  N     . LEU   A  1  370  ? -49.258 50.347  81.000  1.00 15.47 ? 368  LEU   A N     1 
ATOM   2659  C  CA    . LEU   A  1  370  ? -48.576 49.838  82.173  1.00 15.87 ? 368  LEU   A CA    1 
ATOM   2660  C  C     . LEU   A  1  370  ? -47.153 49.488  81.763  1.00 14.49 ? 368  LEU   A C     1 
ATOM   2661  O  O     . LEU   A  1  370  ? -46.943 48.685  80.849  1.00 16.28 ? 368  LEU   A O     1 
ATOM   2662  C  CB    . LEU   A  1  370  ? -49.300 48.604  82.703  1.00 17.37 ? 368  LEU   A CB    1 
ATOM   2663  C  CG    . LEU   A  1  370  ? -48.724 48.035  83.994  1.00 18.83 ? 368  LEU   A CG    1 
ATOM   2664  C  CD1   . LEU   A  1  370  ? -48.975 48.999  85.160  1.00 19.28 ? 368  LEU   A CD1   1 
ATOM   2665  C  CD2   . LEU   A  1  370  ? -49.339 46.669  84.263  1.00 19.20 ? 368  LEU   A CD2   1 
ATOM   2666  N  N     . VAL   A  1  371  ? -46.182 50.092  82.441  1.00 14.43 ? 369  VAL   A N     1 
ATOM   2667  C  CA    . VAL   A  1  371  ? -44.778 49.827  82.205  1.00 14.80 ? 369  VAL   A CA    1 
ATOM   2668  C  C     . VAL   A  1  371  ? -44.175 49.457  83.540  1.00 14.68 ? 369  VAL   A C     1 
ATOM   2669  O  O     . VAL   A  1  371  ? -44.786 49.631  84.589  1.00 17.81 ? 369  VAL   A O     1 
ATOM   2670  C  CB    . VAL   A  1  371  ? -44.050 51.053  81.627  1.00 15.32 ? 369  VAL   A CB    1 
ATOM   2671  C  CG1   . VAL   A  1  371  ? -44.741 51.542  80.380  1.00 15.46 ? 369  VAL   A CG1   1 
ATOM   2672  C  CG2   . VAL   A  1  371  ? -43.944 52.162  82.686  1.00 15.91 ? 369  VAL   A CG2   1 
ATOM   2673  N  N     . LYS   A  1  372  ? -42.929 48.987  83.495  1.00 16.24 ? 370  LYS   A N     1 
ATOM   2674  C  CA    . LYS   A  1  372  ? -42.216 48.808  84.754  1.00 18.24 ? 370  LYS   A CA    1 
ATOM   2675  C  C     . LYS   A  1  372  ? -41.602 50.121  85.233  1.00 16.86 ? 370  LYS   A C     1 
ATOM   2676  O  O     . LYS   A  1  372  ? -41.973 50.629  86.296  1.00 21.16 ? 370  LYS   A O     1 
ATOM   2677  C  CB    . LYS   A  1  372  ? -41.260 47.616  84.673  1.00 18.63 ? 370  LYS   A CB    1 
ATOM   2678  C  CG    . LYS   A  1  372  ? -42.079 46.316  84.562  1.00 18.06 ? 370  LYS   A CG    1 
ATOM   2679  C  CD    . LYS   A  1  372  ? -41.242 45.058  84.451  1.00 21.32 ? 370  LYS   A CD    1 
ATOM   2680  C  CE    . LYS   A  1  372  ? -42.176 43.890  84.152  1.00 22.04 ? 370  LYS   A CE    1 
ATOM   2681  N  NZ    . LYS   A  1  372  ? -41.437 42.628  83.886  1.00 21.21 ? 370  LYS   A NZ    1 
ATOM   2682  N  N     . GLY   A  1  373  ? -40.738 50.731  84.439  1.00 16.84 ? 371  GLY   A N     1 
ATOM   2683  C  CA    . GLY   A  1  373  ? -40.276 52.078  84.735  1.00 14.99 ? 371  GLY   A CA    1 
ATOM   2684  C  C     . GLY   A  1  373  ? -38.824 52.255  84.321  1.00 16.05 ? 371  GLY   A C     1 
ATOM   2685  O  O     . GLY   A  1  373  ? -38.012 51.351  84.402  1.00 17.86 ? 371  GLY   A O     1 
ATOM   2686  N  N     . ALA   A  1  374  ? -38.492 53.473  83.892  1.00 15.82 ? 372  ALA   A N     1 
ATOM   2687  C  CA    . ALA   A  1  374  ? -37.241 53.720  83.182  1.00 15.42 ? 372  ALA   A CA    1 
ATOM   2688  C  C     . ALA   A  1  374  ? -36.178 54.438  84.005  1.00 17.58 ? 372  ALA   A C     1 
ATOM   2689  O  O     . ALA   A  1  374  ? -35.052 54.599  83.516  1.00 19.38 ? 372  ALA   A O     1 
ATOM   2690  C  CB    . ALA   A  1  374  ? -37.504 54.522  81.907  1.00 17.99 ? 372  ALA   A CB    1 
ATOM   2691  N  N     . TYR   A  1  375  ? -36.491 54.884  85.222  1.00 16.75 ? 373  TYR   A N     1 
ATOM   2692  C  CA    . TYR   A  1  375  ? -35.619 55.790  85.961  1.00 16.51 ? 373  TYR   A CA    1 
ATOM   2693  C  C     . TYR   A  1  375  ? -35.111 55.174  87.254  1.00 14.43 ? 373  TYR   A C     1 
ATOM   2694  O  O     . TYR   A  1  375  ? -34.823 55.899  88.206  1.00 16.30 ? 373  TYR   A O     1 
ATOM   2695  C  CB    . TYR   A  1  375  ? -36.338 57.091  86.305  1.00 16.86 ? 373  TYR   A CB    1 
ATOM   2696  C  CG    . TYR   A  1  375  ? -36.906 57.833  85.127  1.00 16.26 ? 373  TYR   A CG    1 
ATOM   2697  C  CD1   . TYR   A  1  375  ? -38.111 57.433  84.542  1.00 16.87 ? 373  TYR   A CD1   1 
ATOM   2698  C  CD2   . TYR   A  1  375  ? -36.271 58.960  84.631  1.00 20.20 ? 373  TYR   A CD2   1 
ATOM   2699  C  CE1   . TYR   A  1  375  ? -38.644 58.128  83.471  1.00 18.40 ? 373  TYR   A CE1   1 
ATOM   2700  C  CE2   . TYR   A  1  375  ? -36.794 59.664  83.568  1.00 21.80 ? 373  TYR   A CE2   1 
ATOM   2701  C  CZ    . TYR   A  1  375  ? -37.980 59.244  82.993  1.00 21.35 ? 373  TYR   A CZ    1 
ATOM   2702  O  OH    . TYR   A  1  375  ? -38.503 59.959  81.940  1.00 22.43 ? 373  TYR   A OH    1 
ATOM   2703  N  N     . TRP   A  1  376  ? -35.007 53.847  87.301  1.00 15.27 ? 374  TRP   A N     1 
ATOM   2704  C  CA    . TRP   A  1  376  ? -34.803 53.165  88.574  1.00 16.64 ? 374  TRP   A CA    1 
ATOM   2705  C  C     . TRP   A  1  376  ? -33.545 53.642  89.286  1.00 16.64 ? 374  TRP   A C     1 
ATOM   2706  O  O     . TRP   A  1  376  ? -33.601 54.028  90.461  1.00 16.82 ? 374  TRP   A O     1 
ATOM   2707  C  CB    . TRP   A  1  376  ? -34.780 51.650  88.394  1.00 18.35 ? 374  TRP   A CB    1 
ATOM   2708  C  CG    . TRP   A  1  376  ? -34.621 50.951  89.706  1.00 18.40 ? 374  TRP   A CG    1 
ATOM   2709  C  CD1   . TRP   A  1  376  ? -35.596 50.720  90.624  1.00 19.01 ? 374  TRP   A CD1   1 
ATOM   2710  C  CD2   . TRP   A  1  376  ? -33.409 50.437  90.270  1.00 18.14 ? 374  TRP   A CD2   1 
ATOM   2711  N  NE1   . TRP   A  1  376  ? -35.075 50.073  91.720  1.00 17.70 ? 374  TRP   A NE1   1 
ATOM   2712  C  CE2   . TRP   A  1  376  ? -33.731 49.897  91.531  1.00 19.13 ? 374  TRP   A CE2   1 
ATOM   2713  C  CE3   . TRP   A  1  376  ? -32.088 50.377  89.832  1.00 21.54 ? 374  TRP   A CE3   1 
ATOM   2714  C  CZ2   . TRP   A  1  376  ? -32.784 49.294  92.354  1.00 21.95 ? 374  TRP   A CZ2   1 
ATOM   2715  C  CZ3   . TRP   A  1  376  ? -31.140 49.783  90.655  1.00 23.69 ? 374  TRP   A CZ3   1 
ATOM   2716  C  CH2   . TRP   A  1  376  ? -31.494 49.248  91.898  1.00 22.78 ? 374  TRP   A CH2   1 
ATOM   2717  N  N     . ASP   A  1  377  ? -32.388 53.586  88.609  1.00 18.60 ? 375  ASP   A N     1 
ATOM   2718  C  CA    A ASP   A  1  377  ? -31.125 53.999  89.229  0.47 18.75 ? 375  ASP   A CA    1 
ATOM   2719  C  CA    B ASP   A  1  377  ? -31.174 53.969  89.315  0.53 18.74 ? 375  ASP   A CA    1 
ATOM   2720  C  C     . ASP   A  1  377  ? -31.204 55.431  89.735  1.00 17.97 ? 375  ASP   A C     1 
ATOM   2721  O  O     . ASP   A  1  377  ? -30.685 55.761  90.805  1.00 18.73 ? 375  ASP   A O     1 
ATOM   2722  C  CB    A ASP   A  1  377  ? -29.988 53.921  88.206  0.47 22.96 ? 375  ASP   A CB    1 
ATOM   2723  C  CB    B ASP   A  1  377  ? -29.892 53.551  88.578  0.53 23.33 ? 375  ASP   A CB    1 
ATOM   2724  C  CG    A ASP   A  1  377  ? -29.692 52.510  87.747  0.47 24.33 ? 375  ASP   A CG    1 
ATOM   2725  C  CG    B ASP   A  1  377  ? -29.799 54.093  87.169  0.53 23.16 ? 375  ASP   A CG    1 
ATOM   2726  O  OD1   A ASP   A  1  377  ? -29.734 51.589  88.573  0.47 30.33 ? 375  ASP   A OD1   1 
ATOM   2727  O  OD1   B ASP   A  1  377  ? -30.480 55.083  86.849  0.53 26.03 ? 375  ASP   A OD1   1 
ATOM   2728  O  OD2   A ASP   A  1  377  ? -29.399 52.329  86.547  0.47 31.80 ? 375  ASP   A OD2   1 
ATOM   2729  O  OD2   B ASP   A  1  377  ? -29.027 53.513  86.376  0.53 26.69 ? 375  ASP   A OD2   1 
ATOM   2730  N  N     . ALA   A  1  378  ? -31.838 56.302  88.948  1.00 17.39 ? 376  ALA   A N     1 
ATOM   2731  C  CA    . ALA   A  1  378  ? -31.912 57.707  89.317  1.00 16.41 ? 376  ALA   A CA    1 
ATOM   2732  C  C     . ALA   A  1  378  ? -32.792 57.906  90.538  1.00 17.54 ? 376  ALA   A C     1 
ATOM   2733  O  O     . ALA   A  1  378  ? -32.523 58.787  91.362  1.00 17.16 ? 376  ALA   A O     1 
ATOM   2734  C  CB    . ALA   A  1  378  ? -32.435 58.537  88.144  1.00 17.95 ? 376  ALA   A CB    1 
ATOM   2735  N  N     . GLU   A  1  379  ? -33.868 57.120  90.652  1.00 16.62 ? 377  GLU   A N     1 
ATOM   2736  C  CA    . GLU   A  1  379  ? -34.735 57.238  91.819  1.00 15.48 ? 377  GLU   A CA    1 
ATOM   2737  C  C     . GLU   A  1  379  ? -34.011 56.802  93.082  1.00 16.07 ? 377  GLU   A C     1 
ATOM   2738  O  O     . GLU   A  1  379  ? -34.210 57.391  94.146  1.00 17.81 ? 377  GLU   A O     1 
ATOM   2739  C  CB    . GLU   A  1  379  ? -36.008 56.412  91.656  1.00 15.72 ? 377  GLU   A CB    1 
ATOM   2740  C  CG    . GLU   A  1  379  ? -36.902 56.789  90.473  1.00 18.12 ? 377  GLU   A CG    1 
ATOM   2741  C  CD    . GLU   A  1  379  ? -37.465 58.205  90.541  1.00 19.94 ? 377  GLU   A CD    1 
ATOM   2742  O  OE1   . GLU   A  1  379  ? -37.330 58.901  91.579  1.00 19.81 ? 377  GLU   A OE1   1 
ATOM   2743  O  OE2   . GLU   A  1  379  ? -38.086 58.613  89.539  1.00 18.72 ? 377  GLU   A OE2   1 
ATOM   2744  N  N     . ILE   A  1  380  ? -33.175 55.765  92.987  1.00 16.98 ? 378  ILE   A N     1 
ATOM   2745  C  CA    . ILE   A  1  380  ? -32.421 55.332  94.161  1.00 18.09 ? 378  ILE   A CA    1 
ATOM   2746  C  C     . ILE   A  1  380  ? -31.471 56.437  94.596  1.00 17.17 ? 378  ILE   A C     1 
ATOM   2747  O  O     . ILE   A  1  380  ? -31.400 56.797  95.781  1.00 16.91 ? 378  ILE   A O     1 
ATOM   2748  C  CB    . ILE   A  1  380  ? -31.662 54.025  93.866  1.00 19.42 ? 378  ILE   A CB    1 
ATOM   2749  C  CG1   . ILE   A  1  380  ? -32.619 52.908  93.451  1.00 19.58 ? 378  ILE   A CG1   1 
ATOM   2750  C  CG2   . ILE   A  1  380  ? -30.817 53.617  95.072  1.00 18.95 ? 378  ILE   A CG2   1 
ATOM   2751  C  CD1   . ILE   A  1  380  ? -33.719 52.573  94.462  1.00 19.39 ? 378  ILE   A CD1   1 
ATOM   2752  N  N     . LYS   A  1  381  ? -30.732 57.003  93.634  1.00 15.91 ? 379  LYS   A N     1 
ATOM   2753  C  CA    . LYS   A  1  381  ? -29.784 58.055  93.966  1.00 16.51 ? 379  LYS   A CA    1 
ATOM   2754  C  C     . LYS   A  1  381  ? -30.489 59.263  94.557  1.00 17.80 ? 379  LYS   A C     1 
ATOM   2755  O  O     . LYS   A  1  381  ? -30.034 59.828  95.557  1.00 16.78 ? 379  LYS   A O     1 
ATOM   2756  C  CB    . LYS   A  1  381  ? -28.968 58.461  92.742  1.00 16.55 ? 379  LYS   A CB    1 
ATOM   2757  C  CG    . LYS   A  1  381  ? -27.986 59.593  93.029  1.00 16.97 ? 379  LYS   A CG    1 
ATOM   2758  C  CD    . LYS   A  1  381  ? -27.089 59.868  91.810  1.00 17.60 ? 379  LYS   A CD    1 
ATOM   2759  C  CE    . LYS   A  1  381  ? -26.090 60.981  92.088  1.00 20.52 ? 379  LYS   A CE    1 
ATOM   2760  N  NZ    . LYS   A  1  381  ? -25.224 61.251  90.894  1.00 17.12 ? 379  LYS   A NZ    1 
ATOM   2761  N  N     . ARG   A  1  382  ? -31.621 59.658  93.968  1.00 16.84 ? 380  ARG   A N     1 
ATOM   2762  C  CA    . ARG   A  1  382  ? -32.297 60.868  94.413  1.00 17.69 ? 380  ARG   A CA    1 
ATOM   2763  C  C     . ARG   A  1  382  ? -32.770 60.728  95.846  1.00 17.35 ? 380  ARG   A C     1 
ATOM   2764  O  O     . ARG   A  1  382  ? -32.616 61.649  96.652  1.00 18.73 ? 380  ARG   A O     1 
ATOM   2765  C  CB    . ARG   A  1  382  ? -33.503 61.133  93.512  1.00 19.94 ? 380  ARG   A CB    1 
ATOM   2766  C  CG    . ARG   A  1  382  ? -34.207 62.433  93.798  1.00 25.83 ? 380  ARG   A CG    1 
ATOM   2767  C  CD    . ARG   A  1  382  ? -33.458 63.577  93.158  1.00 36.69 ? 380  ARG   A CD    1 
ATOM   2768  N  NE    . ARG   A  1  382  ? -32.717 64.345  94.149  1.00 39.26 ? 380  ARG   A NE    1 
ATOM   2769  C  CZ    . ARG   A  1  382  ? -31.703 65.155  93.874  1.00 40.88 ? 380  ARG   A CZ    1 
ATOM   2770  N  NH1   . ARG   A  1  382  ? -31.237 65.288  92.642  1.00 46.79 ? 380  ARG   A NH1   1 
ATOM   2771  N  NH2   . ARG   A  1  382  ? -31.145 65.852  94.863  1.00 34.16 ? 380  ARG   A NH2   1 
ATOM   2772  N  N     . ALA   A  1  383  ? -33.352 59.580  96.180  1.00 16.79 ? 381  ALA   A N     1 
ATOM   2773  C  CA    . ALA   A  1  383  ? -33.877 59.405  97.528  1.00 17.07 ? 381  ALA   A CA    1 
ATOM   2774  C  C     . ALA   A  1  383  ? -32.744 59.402  98.542  1.00 17.63 ? 381  ALA   A C     1 
ATOM   2775  O  O     . ALA   A  1  383  ? -32.890 59.928  99.655  1.00 18.38 ? 381  ALA   A O     1 
ATOM   2776  C  CB    . ALA   A  1  383  ? -34.689 58.111  97.598  1.00 17.25 ? 381  ALA   A CB    1 
ATOM   2777  N  N     . GLN   A  1  384  ? -31.607 58.812  98.174  1.00 16.97 ? 382  GLN   A N     1 
ATOM   2778  C  CA    . GLN   A  1  384  ? -30.452 58.831  99.065  1.00 17.68 ? 382  GLN   A CA    1 
ATOM   2779  C  C     . GLN   A  1  384  ? -29.936 60.249  99.247  1.00 17.75 ? 382  GLN   A C     1 
ATOM   2780  O  O     . GLN   A  1  384  ? -29.658 60.677  100.369 1.00 19.16 ? 382  GLN   A O     1 
ATOM   2781  C  CB    . GLN   A  1  384  ? -29.359 57.909  98.523  1.00 16.93 ? 382  GLN   A CB    1 
ATOM   2782  C  CG    . GLN   A  1  384  ? -29.715 56.439  98.642  1.00 15.97 ? 382  GLN   A CG    1 
ATOM   2783  C  CD    . GLN   A  1  384  ? -28.582 55.535  98.224  1.00 18.57 ? 382  GLN   A CD    1 
ATOM   2784  O  OE1   . GLN   A  1  384  ? -27.660 55.963  97.542  1.00 20.26 ? 382  GLN   A OE1   1 
ATOM   2785  N  NE2   . GLN   A  1  384  ? -28.647 54.277  98.628  1.00 19.85 ? 382  GLN   A NE2   1 
ATOM   2786  N  N     . LEU   A  1  385  ? -29.779 60.990  98.147  1.00 17.22 ? 383  LEU   A N     1 
ATOM   2787  C  CA    . LEU   A  1  385  ? -29.284 62.357  98.250  1.00 18.16 ? 383  LEU   A CA    1 
ATOM   2788  C  C     . LEU   A  1  385  ? -30.197 63.207  99.118  1.00 20.28 ? 383  LEU   A C     1 
ATOM   2789  O  O     . LEU   A  1  385  ? -29.728 64.041  99.899  1.00 20.26 ? 383  LEU   A O     1 
ATOM   2790  C  CB    . LEU   A  1  385  ? -29.188 62.984  96.864  1.00 18.40 ? 383  LEU   A CB    1 
ATOM   2791  C  CG    . LEU   A  1  385  ? -28.056 62.533  95.949  1.00 21.49 ? 383  LEU   A CG    1 
ATOM   2792  C  CD1   . LEU   A  1  385  ? -28.226 63.197  94.609  1.00 22.04 ? 383  LEU   A CD1   1 
ATOM   2793  C  CD2   . LEU   A  1  385  ? -26.725 62.905  96.548  1.00 22.28 ? 383  LEU   A CD2   1 
ATOM   2794  N  N     . ASP   A  1  386  ? -31.507 63.013  98.991  1.00 19.52 ? 384  ASP   A N     1 
ATOM   2795  C  CA    . ASP   A  1  386  ? -32.465 63.852  99.687  1.00 21.04 ? 384  ASP   A CA    1 
ATOM   2796  C  C     . ASP   A  1  386  ? -32.731 63.379  101.113 1.00 20.73 ? 384  ASP   A C     1 
ATOM   2797  O  O     . ASP   A  1  386  ? -33.487 64.033  101.838 1.00 21.54 ? 384  ASP   A O     1 
ATOM   2798  C  CB    . ASP   A  1  386  ? -33.758 63.948  98.867  1.00 21.36 ? 384  ASP   A CB    1 
ATOM   2799  C  CG    . ASP   A  1  386  ? -33.582 64.779  97.601  1.00 28.48 ? 384  ASP   A CG    1 
ATOM   2800  O  OD1   . ASP   A  1  386  ? -32.524 65.442  97.455  1.00 31.28 ? 384  ASP   A OD1   1 
ATOM   2801  O  OD2   . ASP   A  1  386  ? -34.490 64.768  96.735  1.00 30.44 ? 384  ASP   A OD2   1 
ATOM   2802  N  N     . GLY   A  1  387  ? -32.113 62.282  101.538 1.00 20.65 ? 385  GLY   A N     1 
ATOM   2803  C  CA    . GLY   A  1  387  ? -32.295 61.796  102.898 1.00 20.30 ? 385  GLY   A CA    1 
ATOM   2804  C  C     . GLY   A  1  387  ? -33.729 61.432  103.211 1.00 19.43 ? 385  GLY   A C     1 
ATOM   2805  O  O     . GLY   A  1  387  ? -34.214 61.708  104.314 1.00 20.45 ? 385  GLY   A O     1 
ATOM   2806  N  N     . LEU   A  1  388  ? -34.425 60.827  102.262 1.00 19.64 ? 386  LEU   A N     1 
ATOM   2807  C  CA    . LEU   A  1  388  ? -35.841 60.592  102.483 1.00 20.36 ? 386  LEU   A CA    1 
ATOM   2808  C  C     . LEU   A  1  388  ? -36.072 59.244  103.154 1.00 21.06 ? 386  LEU   A C     1 
ATOM   2809  O  O     . LEU   A  1  388  ? -35.162 58.432  103.326 1.00 23.17 ? 386  LEU   A O     1 
ATOM   2810  C  CB    . LEU   A  1  388  ? -36.619 60.757  101.178 1.00 20.46 ? 386  LEU   A CB    1 
ATOM   2811  C  CG    . LEU   A  1  388  ? -36.416 62.160  100.601 1.00 20.97 ? 386  LEU   A CG    1 
ATOM   2812  C  CD1   . LEU   A  1  388  ? -37.160 62.323  99.280  1.00 22.94 ? 386  LEU   A CD1   1 
ATOM   2813  C  CD2   . LEU   A  1  388  ? -36.819 63.256  101.579 1.00 22.95 ? 386  LEU   A CD2   1 
ATOM   2814  N  N     . ALA   A  1  389  ? -37.317 59.029  103.587 1.00 22.11 ? 387  ALA   A N     1 
ATOM   2815  C  CA    . ALA   A  1  389  ? -37.599 57.906  104.467 1.00 24.72 ? 387  ALA   A CA    1 
ATOM   2816  C  C     . ALA   A  1  389  ? -37.376 56.577  103.763 1.00 23.87 ? 387  ALA   A C     1 
ATOM   2817  O  O     . ALA   A  1  389  ? -36.933 55.603  104.381 1.00 23.97 ? 387  ALA   A O     1 
ATOM   2818  C  CB    . ALA   A  1  389  ? -39.033 58.011  104.977 1.00 25.75 ? 387  ALA   A CB    1 
ATOM   2819  N  N     . ASP   A  1  390  ? -37.678 56.516  102.473 1.00 21.02 ? 388  ASP   A N     1 
ATOM   2820  C  CA    . ASP   A  1  390  ? -37.625 55.267  101.729 1.00 21.81 ? 388  ASP   A CA    1 
ATOM   2821  C  C     . ASP   A  1  390  ? -37.639 55.634  100.255 1.00 19.82 ? 388  ASP   A C     1 
ATOM   2822  O  O     . ASP   A  1  390  ? -37.663 56.812  99.896  1.00 19.72 ? 388  ASP   A O     1 
ATOM   2823  C  CB    . ASP   A  1  390  ? -38.808 54.371  102.111 1.00 23.96 ? 388  ASP   A CB    1 
ATOM   2824  C  CG    . ASP   A  1  390  ? -38.532 52.890  101.893 1.00 24.02 ? 388  ASP   A CG    1 
ATOM   2825  O  OD1   . ASP   A  1  390  ? -37.907 52.528  100.873 1.00 25.02 ? 388  ASP   A OD1   1 
ATOM   2826  O  OD2   . ASP   A  1  390  ? -38.944 52.077  102.751 1.00 29.21 ? 388  ASP   A OD2   1 
ATOM   2827  N  N     . PHE   A  1  391  ? -37.580 54.649  99.431  1.00 20.07 ? 389  PHE   A N     1 
ATOM   2828  C  CA    . PHE   A  1  391  ? -37.600 54.904  98.005  1.00 19.32 ? 389  PHE   A CA    1 
ATOM   2829  C  C     . PHE   A  1  391  ? -39.035 54.933  97.498  1.00 19.21 ? 389  PHE   A C     1 
ATOM   2830  O  O     . PHE   A  1  391  ? -39.930 54.348  98.113  1.00 19.31 ? 389  PHE   A O     1 
ATOM   2831  C  CB    . PHE   A  1  391  ? -36.821 53.813  97.281  1.00 18.79 ? 389  PHE   A CB    1 
ATOM   2832  C  CG    . PHE   A  1  391  ? -35.410 53.713  97.756  1.00 16.85 ? 389  PHE   A CG    1 
ATOM   2833  C  CD1   . PHE   A  1  391  ? -34.500 54.667  97.383  1.00 18.17 ? 389  PHE   A CD1   1 
ATOM   2834  C  CD2   . PHE   A  1  391  ? -35.028 52.718  98.641  1.00 18.30 ? 389  PHE   A CD2   1 
ATOM   2835  C  CE1   . PHE   A  1  391  ? -33.200 54.626  97.844  1.00 20.25 ? 389  PHE   A CE1   1 
ATOM   2836  C  CE2   . PHE   A  1  391  ? -33.714 52.668  99.116  1.00 20.67 ? 389  PHE   A CE2   1 
ATOM   2837  C  CZ    . PHE   A  1  391  ? -32.809 53.622  98.717  1.00 21.10 ? 389  PHE   A CZ    1 
ATOM   2838  N  N     . PRO   A  1  392  ? -39.279 55.640  96.395  1.00 18.31 ? 390  PRO   A N     1 
ATOM   2839  C  CA    . PRO   A  1  392  ? -40.607 55.619  95.767  1.00 17.56 ? 390  PRO   A CA    1 
ATOM   2840  C  C     . PRO   A  1  392  ? -40.775 54.490  94.764  1.00 17.38 ? 390  PRO   A C     1 
ATOM   2841  O  O     . PRO   A  1  392  ? -41.818 54.407  94.098  1.00 19.18 ? 390  PRO   A O     1 
ATOM   2842  C  CB    . PRO   A  1  392  ? -40.629 56.966  95.045  1.00 16.36 ? 390  PRO   A CB    1 
ATOM   2843  C  CG    . PRO   A  1  392  ? -39.192 57.116  94.586  1.00 16.95 ? 390  PRO   A CG    1 
ATOM   2844  C  CD    . PRO   A  1  392  ? -38.353 56.562  95.714  1.00 16.61 ? 390  PRO   A CD    1 
ATOM   2845  N  N     . VAL   A  1  393  ? -39.746 53.658  94.613  1.00 18.84 ? 391  VAL   A N     1 
ATOM   2846  C  CA    . VAL   A  1  393  ? -39.763 52.507  93.734  1.00 17.41 ? 391  VAL   A CA    1 
ATOM   2847  C  C     . VAL   A  1  393  ? -39.320 51.300  94.542  1.00 18.01 ? 391  VAL   A C     1 
ATOM   2848  O  O     . VAL   A  1  393  ? -38.700 51.424  95.599  1.00 18.84 ? 391  VAL   A O     1 
ATOM   2849  C  CB    . VAL   A  1  393  ? -38.815 52.704  92.536  1.00 16.18 ? 391  VAL   A CB    1 
ATOM   2850  C  CG1   . VAL   A  1  393  ? -39.340 53.810  91.616  1.00 18.51 ? 391  VAL   A CG1   1 
ATOM   2851  C  CG2   . VAL   A  1  393  ? -37.412 53.057  93.017  1.00 18.11 ? 391  VAL   A CG2   1 
ATOM   2852  N  N     . PHE   A  1  394  ? -39.646 50.122  94.027  1.00 18.24 ? 392  PHE   A N     1 
ATOM   2853  C  CA    . PHE   A  1  394  ? -39.154 48.903  94.644  1.00 17.81 ? 392  PHE   A CA    1 
ATOM   2854  C  C     . PHE   A  1  394  ? -37.646 48.797  94.445  1.00 19.96 ? 392  PHE   A C     1 
ATOM   2855  O  O     . PHE   A  1  394  ? -37.059 49.470  93.597  1.00 19.56 ? 392  PHE   A O     1 
ATOM   2856  C  CB    . PHE   A  1  394  ? -39.875 47.704  94.047  1.00 18.40 ? 392  PHE   A CB    1 
ATOM   2857  C  CG    . PHE   A  1  394  ? -41.352 47.753  94.270  1.00 17.18 ? 392  PHE   A CG    1 
ATOM   2858  C  CD1   . PHE   A  1  394  ? -41.859 47.646  95.556  1.00 21.72 ? 392  PHE   A CD1   1 
ATOM   2859  C  CD2   . PHE   A  1  394  ? -42.220 47.944  93.217  1.00 19.61 ? 392  PHE   A CD2   1 
ATOM   2860  C  CE1   . PHE   A  1  394  ? -43.211 47.717  95.791  1.00 20.80 ? 392  PHE   A CE1   1 
ATOM   2861  C  CE2   . PHE   A  1  394  ? -43.594 48.006  93.441  1.00 18.06 ? 392  PHE   A CE2   1 
ATOM   2862  C  CZ    . PHE   A  1  394  ? -44.084 47.898  94.733  1.00 19.09 ? 392  PHE   A CZ    1 
ATOM   2863  N  N     . THR   A  1  395  ? -37.011 47.966  95.270  1.00 17.98 ? 393  THR   A N     1 
ATOM   2864  C  CA    . THR   A  1  395  ? -35.569 47.783  95.187  1.00 20.62 ? 393  THR   A CA    1 
ATOM   2865  C  C     . THR   A  1  395  ? -35.161 46.393  94.734  1.00 20.96 ? 393  THR   A C     1 
ATOM   2866  O  O     . THR   A  1  395  ? -33.972 46.172  94.469  1.00 21.39 ? 393  THR   A O     1 
ATOM   2867  C  CB    . THR   A  1  395  ? -34.882 48.097  96.523  1.00 20.25 ? 393  THR   A CB    1 
ATOM   2868  O  OG1   . THR   A  1  395  ? -35.415 47.248  97.544  1.00 21.78 ? 393  THR   A OG1   1 
ATOM   2869  C  CG2   . THR   A  1  395  ? -35.082 49.560  96.905  1.00 23.95 ? 393  THR   A CG2   1 
ATOM   2870  N  N     . ARG   A  1  396  ? -36.094 45.457  94.647  1.00 20.63 ? 394  ARG   A N     1 
ATOM   2871  C  CA    . ARG   A  1  396  ? -35.838 44.160  94.043  1.00 21.17 ? 394  ARG   A CA    1 
ATOM   2872  C  C     . ARG   A  1  396  ? -36.628 44.064  92.753  1.00 20.68 ? 394  ARG   A C     1 
ATOM   2873  O  O     . ARG   A  1  396  ? -37.824 44.379  92.725  1.00 20.70 ? 394  ARG   A O     1 
ATOM   2874  C  CB    . ARG   A  1  396  ? -36.221 43.017  94.973  1.00 22.03 ? 394  ARG   A CB    1 
ATOM   2875  C  CG    . ARG   A  1  396  ? -35.407 42.972  96.233  1.00 23.37 ? 394  ARG   A CG    1 
ATOM   2876  C  CD    . ARG   A  1  396  ? -35.769 41.732  97.028  1.00 29.04 ? 394  ARG   A CD    1 
ATOM   2877  N  NE    . ARG   A  1  396  ? -35.165 41.764  98.350  1.00 31.05 ? 394  ARG   A NE    1 
ATOM   2878  C  CZ    . ARG   A  1  396  ? -34.390 40.807  98.842  1.00 34.72 ? 394  ARG   A CZ    1 
ATOM   2879  N  NH1   . ARG   A  1  396  ? -34.149 39.696  98.163  1.00 36.57 ? 394  ARG   A NH1   1 
ATOM   2880  N  NH2   . ARG   A  1  396  ? -33.846 40.971  100.046 1.00 33.13 ? 394  ARG   A NH2   1 
ATOM   2881  N  N     . LYS   A  1  397  ? -35.948 43.655  91.687  1.00 20.94 ? 395  LYS   A N     1 
ATOM   2882  C  CA    . LYS   A  1  397  ? -36.591 43.571  90.382  1.00 19.86 ? 395  LYS   A CA    1 
ATOM   2883  C  C     . LYS   A  1  397  ? -37.830 42.690  90.431  1.00 20.97 ? 395  LYS   A C     1 
ATOM   2884  O  O     . LYS   A  1  397  ? -38.849 42.995  89.798  1.00 20.68 ? 395  LYS   A O     1 
ATOM   2885  C  CB    . LYS   A  1  397  ? -35.583 43.058  89.351  1.00 23.28 ? 395  LYS   A CB    1 
ATOM   2886  C  CG    . LYS   A  1  397  ? -35.968 43.354  87.912  1.00 23.69 ? 395  LYS   A CG    1 
ATOM   2887  C  CD    . LYS   A  1  397  ? -36.735 42.209  87.309  1.00 22.99 ? 395  LYS   A CD    1 
ATOM   2888  C  CE    . LYS   A  1  397  ? -37.095 42.487  85.863  1.00 25.40 ? 395  LYS   A CE    1 
ATOM   2889  N  NZ    . LYS   A  1  397  ? -37.801 41.335  85.246  1.00 26.50 ? 395  LYS   A NZ    1 
ATOM   2890  N  N     . ILE   A  1  398  ? -37.776 41.604  91.205  1.00 20.48 ? 396  ILE   A N     1 
ATOM   2891  C  CA    . ILE   A  1  398  ? -38.902 40.683  91.231  1.00 23.16 ? 396  ILE   A CA    1 
ATOM   2892  C  C     . ILE   A  1  398  ? -40.130 41.358  91.826  1.00 20.66 ? 396  ILE   A C     1 
ATOM   2893  O  O     . ILE   A  1  398  ? -41.272 41.004  91.496  1.00 22.20 ? 396  ILE   A O     1 
ATOM   2894  C  CB    . ILE   A  1  398  ? -38.500 39.390  91.965  1.00 23.65 ? 396  ILE   A CB    1 
ATOM   2895  C  CG1   . ILE   A  1  398  ? -39.535 38.304  91.729  1.00 28.66 ? 396  ILE   A CG1   1 
ATOM   2896  C  CG2   . ILE   A  1  398  ? -38.312 39.650  93.450  1.00 24.83 ? 396  ILE   A CG2   1 
ATOM   2897  C  CD1   . ILE   A  1  398  ? -39.027 36.925  92.064  1.00 32.76 ? 396  ILE   A CD1   1 
ATOM   2898  N  N     . HIS   A  1  399  ? -39.921 42.345  92.695  1.00 20.74 ? 397  HIS   A N     1 
ATOM   2899  C  CA    . HIS   A  1  399  ? -41.043 43.084  93.259  1.00 22.53 ? 397  HIS   A CA    1 
ATOM   2900  C  C     . HIS   A  1  399  ? -41.753 43.878  92.180  1.00 20.24 ? 397  HIS   A C     1 
ATOM   2901  O  O     . HIS   A  1  399  ? -42.987 43.898  92.124  1.00 20.17 ? 397  HIS   A O     1 
ATOM   2902  C  CB    . HIS   A  1  399  ? -40.551 44.020  94.357  1.00 22.04 ? 397  HIS   A CB    1 
ATOM   2903  C  CG    . HIS   A  1  399  ? -40.049 43.302  95.572  1.00 20.54 ? 397  HIS   A CG    1 
ATOM   2904  N  ND1   . HIS   A  1  399  ? -39.413 43.946  96.610  1.00 24.20 ? 397  HIS   A ND1   1 
ATOM   2905  C  CD2   . HIS   A  1  399  ? -40.088 41.990  95.908  1.00 27.38 ? 397  HIS   A CD2   1 
ATOM   2906  C  CE1   . HIS   A  1  399  ? -39.080 43.061  97.534  1.00 24.90 ? 397  HIS   A CE1   1 
ATOM   2907  N  NE2   . HIS   A  1  399  ? -39.474 41.867  97.130  1.00 24.22 ? 397  HIS   A NE2   1 
ATOM   2908  N  N     . THR   A  1  400  ? -40.983 44.524  91.308  1.00 19.57 ? 398  THR   A N     1 
ATOM   2909  C  CA    . THR   A  1  400  ? -41.590 45.219  90.183  1.00 18.48 ? 398  THR   A CA    1 
ATOM   2910  C  C     . THR   A  1  400  ? -42.376 44.258  89.300  1.00 18.85 ? 398  THR   A C     1 
ATOM   2911  O  O     . THR   A  1  400  ? -43.466 44.592  88.826  1.00 18.49 ? 398  THR   A O     1 
ATOM   2912  C  CB    . THR   A  1  400  ? -40.497 45.933  89.399  1.00 18.62 ? 398  THR   A CB    1 
ATOM   2913  O  OG1   . THR   A  1  400  ? -39.955 46.976  90.213  1.00 18.58 ? 398  THR   A OG1   1 
ATOM   2914  C  CG2   . THR   A  1  400  ? -41.056 46.527  88.119  1.00 16.45 ? 398  THR   A CG2   1 
ATOM   2915  N  N     . ASP   A  1  401  ? -41.857 43.048  89.086  1.00 18.87 ? 399  ASP   A N     1 
ATOM   2916  C  CA    . ASP   A  1  401  ? -42.589 42.092  88.258  1.00 21.72 ? 399  ASP   A CA    1 
ATOM   2917  C  C     . ASP   A  1  401  ? -43.917 41.713  88.899  1.00 19.19 ? 399  ASP   A C     1 
ATOM   2918  O  O     . ASP   A  1  401  ? -44.947 41.633  88.216  1.00 20.01 ? 399  ASP   A O     1 
ATOM   2919  C  CB    . ASP   A  1  401  ? -41.747 40.845  87.992  1.00 19.93 ? 399  ASP   A CB    1 
ATOM   2920  C  CG    . ASP   A  1  401  ? -40.561 41.122  87.099  1.00 24.74 ? 399  ASP   A CG    1 
ATOM   2921  O  OD1   . ASP   A  1  401  ? -40.629 42.081  86.308  1.00 25.98 ? 399  ASP   A OD1   1 
ATOM   2922  O  OD2   . ASP   A  1  401  ? -39.557 40.386  87.195  1.00 26.85 ? 399  ASP   A OD2   1 
ATOM   2923  N  N     . VAL   A  1  402  ? -43.911 41.480  90.215  1.00 20.50 ? 400  VAL   A N     1 
ATOM   2924  C  CA    . VAL   A  1  402  ? -45.154 41.161  90.909  1.00 21.38 ? 400  VAL   A CA    1 
ATOM   2925  C  C     . VAL   A  1  402  ? -46.111 42.339  90.841  1.00 17.41 ? 400  VAL   A C     1 
ATOM   2926  O  O     . VAL   A  1  402  ? -47.308 42.175  90.572  1.00 19.14 ? 400  VAL   A O     1 
ATOM   2927  C  CB    . VAL   A  1  402  ? -44.880 40.751  92.364  1.00 22.93 ? 400  VAL   A CB    1 
ATOM   2928  C  CG1   . VAL   A  1  402  ? -46.206 40.587  93.103  1.00 20.18 ? 400  VAL   A CG1   1 
ATOM   2929  C  CG2   . VAL   A  1  402  ? -44.079 39.466  92.407  1.00 24.66 ? 400  VAL   A CG2   1 
ATOM   2930  N  N     . SER   A  1  403  ? -45.593 43.544  91.106  1.00 20.48 ? 401  SER   A N     1 
ATOM   2931  C  CA    . SER   A  1  403  ? -46.401 44.753  91.019  1.00 20.41 ? 401  SER   A CA    1 
ATOM   2932  C  C     . SER   A  1  403  ? -47.047 44.862  89.649  1.00 20.64 ? 401  SER   A C     1 
ATOM   2933  O  O     . SER   A  1  403  ? -48.248 45.124  89.529  1.00 20.30 ? 401  SER   A O     1 
ATOM   2934  C  CB    . SER   A  1  403  ? -45.519 45.975  91.292  1.00 21.20 ? 401  SER   A CB    1 
ATOM   2935  O  OG    . SER   A  1  403  ? -46.241 47.181  91.079  1.00 19.87 ? 401  SER   A OG    1 
ATOM   2936  N  N     . TYR   A  1  404  ? -46.257 44.630  88.597  1.00 18.22 ? 402  TYR   A N     1 
ATOM   2937  C  CA    . TYR   A  1  404  ? -46.788 44.713  87.244  1.00 18.93 ? 402  TYR   A CA    1 
ATOM   2938  C  C     . TYR   A  1  404  ? -47.946 43.740  87.053  1.00 17.51 ? 402  TYR   A C     1 
ATOM   2939  O  O     . TYR   A  1  404  ? -49.009 44.112  86.548  1.00 19.52 ? 402  TYR   A O     1 
ATOM   2940  C  CB    . TYR   A  1  404  ? -45.655 44.441  86.249  1.00 17.69 ? 402  TYR   A CB    1 
ATOM   2941  C  CG    . TYR   A  1  404  ? -45.988 44.773  84.811  1.00 19.04 ? 402  TYR   A CG    1 
ATOM   2942  C  CD1   . TYR   A  1  404  ? -46.753 43.909  84.038  1.00 19.23 ? 402  TYR   A CD1   1 
ATOM   2943  C  CD2   . TYR   A  1  404  ? -45.528 45.946  84.226  1.00 18.19 ? 402  TYR   A CD2   1 
ATOM   2944  C  CE1   . TYR   A  1  404  ? -47.047 44.202  82.725  1.00 19.84 ? 402  TYR   A CE1   1 
ATOM   2945  C  CE2   . TYR   A  1  404  ? -45.823 46.247  82.903  1.00 17.50 ? 402  TYR   A CE2   1 
ATOM   2946  C  CZ    . TYR   A  1  404  ? -46.575 45.372  82.164  1.00 18.46 ? 402  TYR   A CZ    1 
ATOM   2947  O  OH    . TYR   A  1  404  ? -46.872 45.669  80.859  1.00 20.36 ? 402  TYR   A OH    1 
ATOM   2948  N  N     . ILE   A  1  405  ? -47.762 42.485  87.473  1.00 18.58 ? 403  ILE   A N     1 
ATOM   2949  C  CA    . ILE   A  1  405  ? -48.810 41.492  87.272  1.00 19.97 ? 403  ILE   A CA    1 
ATOM   2950  C  C     . ILE   A  1  405  ? -50.050 41.831  88.092  1.00 17.54 ? 403  ILE   A C     1 
ATOM   2951  O  O     . ILE   A  1  405  ? -51.176 41.725  87.599  1.00 20.74 ? 403  ILE   A O     1 
ATOM   2952  C  CB    . ILE   A  1  405  ? -48.270 40.082  87.550  1.00 19.71 ? 403  ILE   A CB    1 
ATOM   2953  C  CG1   . ILE   A  1  405  ? -47.128 39.793  86.571  1.00 25.39 ? 403  ILE   A CG1   1 
ATOM   2954  C  CG2   . ILE   A  1  405  ? -49.388 39.062  87.404  1.00 23.22 ? 403  ILE   A CG2   1 
ATOM   2955  C  CD1   . ILE   A  1  405  ? -46.320 38.555  86.889  1.00 32.10 ? 403  ILE   A CD1   1 
ATOM   2956  N  N     . ALA   A  1  406  ? -49.853 42.305  89.326  1.00 19.62 ? 404  ALA   A N     1 
ATOM   2957  C  CA    . ALA   A  1  406  ? -50.978 42.740  90.155  1.00 19.28 ? 404  ALA   A CA    1 
ATOM   2958  C  C     . ALA   A  1  406  ? -51.725 43.902  89.517  1.00 20.42 ? 404  ALA   A C     1 
ATOM   2959  O  O     . ALA   A  1  406  ? -52.962 43.941  89.529  1.00 21.62 ? 404  ALA   A O     1 
ATOM   2960  C  CB    . ALA   A  1  406  ? -50.468 43.169  91.524  1.00 21.51 ? 404  ALA   A CB    1 
ATOM   2961  N  N     . CYS   A  1  407  ? -50.992 44.876  88.978  1.00 21.40 ? 405  CYS   A N     1 
ATOM   2962  C  CA    . CYS   A  1  407  ? -51.638 46.013  88.341  1.00 19.74 ? 405  CYS   A CA    1 
ATOM   2963  C  C     . CYS   A  1  407  ? -52.344 45.604  87.057  1.00 20.22 ? 405  CYS   A C     1 
ATOM   2964  O  O     . CYS   A  1  407  ? -53.394 46.166  86.720  1.00 19.20 ? 405  CYS   A O     1 
ATOM   2965  C  CB    . CYS   A  1  407  ? -50.610 47.119  88.116  1.00 21.11 ? 405  CYS   A CB    1 
ATOM   2966  S  SG    . CYS   A  1  407  ? -50.112 47.853  89.699  1.00 26.51 ? 405  CYS   A SG    1 
ATOM   2967  N  N     . ALA   A  1  408  ? -51.801 44.609  86.345  1.00 19.22 ? 406  ALA   A N     1 
ATOM   2968  C  CA    . ALA   A  1  408  ? -52.481 44.108  85.161  1.00 19.68 ? 406  ALA   A CA    1 
ATOM   2969  C  C     . ALA   A  1  408  ? -53.801 43.449  85.530  1.00 19.26 ? 406  ALA   A C     1 
ATOM   2970  O  O     . ALA   A  1  408  ? -54.788 43.575  84.800  1.00 21.57 ? 406  ALA   A O     1 
ATOM   2971  C  CB    . ALA   A  1  408  ? -51.580 43.129  84.407  1.00 21.33 ? 406  ALA   A CB    1 
ATOM   2972  N  N     . ALA   A  1  409  ? -53.836 42.736  86.659  1.00 19.83 ? 407  ALA   A N     1 
ATOM   2973  C  CA    . ALA   A  1  409  ? -55.093 42.142  87.105  1.00 22.51 ? 407  ALA   A CA    1 
ATOM   2974  C  C     . ALA   A  1  409  ? -56.132 43.216  87.382  1.00 20.55 ? 407  ALA   A C     1 
ATOM   2975  O  O     . ALA   A  1  409  ? -57.310 43.050  87.051  1.00 21.66 ? 407  ALA   A O     1 
ATOM   2976  C  CB    . ALA   A  1  409  ? -54.866 41.270  88.343  1.00 22.99 ? 407  ALA   A CB    1 
ATOM   2977  N  N     . LYS   A  1  410  ? -55.703 44.339  87.969  1.00 21.04 ? 408  LYS   A N     1 
ATOM   2978  C  CA    . LYS   A  1  410  ? -56.624 45.444  88.218  1.00 20.17 ? 408  LYS   A CA    1 
ATOM   2979  C  C     . LYS   A  1  410  ? -57.112 46.055  86.908  1.00 18.45 ? 408  LYS   A C     1 
ATOM   2980  O  O     . LYS   A  1  410  ? -58.309 46.317  86.739  1.00 20.71 ? 408  LYS   A O     1 
ATOM   2981  C  CB    . LYS   A  1  410  ? -55.916 46.500  89.070  1.00 21.91 ? 408  LYS   A CB    1 
ATOM   2982  C  CG    . LYS   A  1  410  ? -56.775 47.712  89.429  1.00 23.87 ? 408  LYS   A CG    1 
ATOM   2983  C  CD    . LYS   A  1  410  ? -55.973 48.700  90.266  1.00 24.52 ? 408  LYS   A CD    1 
ATOM   2984  C  CE    . LYS   A  1  410  ? -55.600 48.138  91.628  1.00 24.88 ? 408  LYS   A CE    1 
ATOM   2985  N  NZ    . LYS   A  1  410  ? -56.781 48.121  92.517  1.00 27.76 ? 408  LYS   A NZ    1 
ATOM   2986  N  N     . LEU   A  1  411  ? -56.195 46.270  85.959  1.00 17.92 ? 409  LEU   A N     1 
ATOM   2987  C  CA    . LEU   A  1  411  ? -56.578 46.830  84.670  1.00 17.91 ? 409  LEU   A CA    1 
ATOM   2988  C  C     . LEU   A  1  411  ? -57.505 45.892  83.909  1.00 19.32 ? 409  LEU   A C     1 
ATOM   2989  O  O     . LEU   A  1  411  ? -58.474 46.341  83.290  1.00 17.99 ? 409  LEU   A O     1 
ATOM   2990  C  CB    . LEU   A  1  411  ? -55.322 47.130  83.846  1.00 17.93 ? 409  LEU   A CB    1 
ATOM   2991  C  CG    . LEU   A  1  411  ? -54.618 48.407  84.275  1.00 17.83 ? 409  LEU   A CG    1 
ATOM   2992  C  CD1   . LEU   A  1  411  ? -53.210 48.490  83.653  1.00 19.55 ? 409  LEU   A CD1   1 
ATOM   2993  C  CD2   . LEU   A  1  411  ? -55.421 49.647  83.916  1.00 18.38 ? 409  LEU   A CD2   1 
ATOM   2994  N  N     . LEU   A  1  412  ? -57.232 44.582  83.958  1.00 19.28 ? 410  LEU   A N     1 
ATOM   2995  C  CA    . LEU   A  1  412  ? -58.043 43.644  83.194  1.00 19.29 ? 410  LEU   A CA    1 
ATOM   2996  C  C     . LEU   A  1  412  ? -59.442 43.502  83.755  1.00 19.86 ? 410  LEU   A C     1 
ATOM   2997  O  O     . LEU   A  1  412  ? -60.343 43.083  83.026  1.00 23.65 ? 410  LEU   A O     1 
ATOM   2998  C  CB    . LEU   A  1  412  ? -57.347 42.289  83.075  1.00 23.28 ? 410  LEU   A CB    1 
ATOM   2999  C  CG    . LEU   A  1  412  ? -56.146 42.289  82.115  1.00 19.85 ? 410  LEU   A CG    1 
ATOM   3000  C  CD1   . LEU   A  1  412  ? -55.376 41.001  82.259  1.00 24.39 ? 410  LEU   A CD1   1 
ATOM   3001  C  CD2   . LEU   A  1  412  ? -56.615 42.466  80.687  1.00 22.46 ? 410  LEU   A CD2   1 
ATOM   3002  N  N     . ALA   A  1  413  ? -59.655 43.881  85.009  1.00 19.30 ? 411  ALA   A N     1 
ATOM   3003  C  CA    . ALA   A  1  413  ? -61.006 43.909  85.554  1.00 22.53 ? 411  ALA   A CA    1 
ATOM   3004  C  C     . ALA   A  1  413  ? -61.768 45.166  85.163  1.00 22.84 ? 411  ALA   A C     1 
ATOM   3005  O  O     . ALA   A  1  413  ? -62.956 45.282  85.477  1.00 24.75 ? 411  ALA   A O     1 
ATOM   3006  C  CB    . ALA   A  1  413  ? -60.953 43.794  87.081  1.00 22.73 ? 411  ALA   A CB    1 
ATOM   3007  N  N     . ALA   A  1  414  ? -61.125 46.108  84.478  1.00 22.28 ? 412  ALA   A N     1 
ATOM   3008  C  CA    . ALA   A  1  414  ? -61.730 47.403  84.203  1.00 21.63 ? 412  ALA   A CA    1 
ATOM   3009  C  C     . ALA   A  1  414  ? -61.674 47.748  82.722  1.00 23.08 ? 412  ALA   A C     1 
ATOM   3010  O  O     . ALA   A  1  414  ? -61.678 48.922  82.367  1.00 19.14 ? 412  ALA   A O     1 
ATOM   3011  C  CB    . ALA   A  1  414  ? -61.069 48.505  85.033  1.00 24.53 ? 412  ALA   A CB    1 
ATOM   3012  N  N     . THR   A  1  415  ? -61.629 46.740  81.842  1.00 22.17 ? 413  THR   A N     1 
ATOM   3013  C  CA    . THR   A  1  415  ? -61.529 47.015  80.410  1.00 22.18 ? 413  THR   A CA    1 
ATOM   3014  C  C     . THR   A  1  415  ? -62.753 47.730  79.854  1.00 22.27 ? 413  THR   A C     1 
ATOM   3015  O  O     . THR   A  1  415  ? -62.680 48.301  78.763  1.00 22.42 ? 413  THR   A O     1 
ATOM   3016  C  CB    . THR   A  1  415  ? -61.244 45.736  79.612  1.00 25.06 ? 413  THR   A CB    1 
ATOM   3017  O  OG1   . THR   A  1  415  ? -62.285 44.784  79.843  1.00 26.29 ? 413  THR   A OG1   1 
ATOM   3018  C  CG2   . THR   A  1  415  ? -59.927 45.127  80.038  1.00 22.75 ? 413  THR   A CG2   1 
ATOM   3019  N  N     . ASP   A  1  416  ? -63.878 47.722  80.567  1.00 23.04 ? 414  ASP   A N     1 
ATOM   3020  C  CA    . ASP   A  1  416  ? -65.009 48.498  80.081  1.00 21.59 ? 414  ASP   A CA    1 
ATOM   3021  C  C     . ASP   A  1  416  ? -64.764 49.997  80.211  1.00 20.77 ? 414  ASP   A C     1 
ATOM   3022  O  O     . ASP   A  1  416  ? -65.313 50.776  79.428  1.00 28.15 ? 414  ASP   A O     1 
ATOM   3023  C  CB    . ASP   A  1  416  ? -66.285 48.090  80.812  1.00 25.99 ? 414  ASP   A CB    1 
ATOM   3024  C  CG    . ASP   A  1  416  ? -66.178 48.292  82.303  1.00 32.21 ? 414  ASP   A CG    1 
ATOM   3025  O  OD1   . ASP   A  1  416  ? -65.138 47.902  82.887  1.00 32.69 ? 414  ASP   A OD1   1 
ATOM   3026  O  OD2   . ASP   A  1  416  ? -67.126 48.860  82.892  1.00 40.31 ? 414  ASP   A OD2   1 
ATOM   3027  N  N     . VAL   A  1  417  ? -63.922 50.425  81.153  1.00 20.37 ? 415  VAL   A N     1 
ATOM   3028  C  CA    . VAL   A  1  417  ? -63.723 51.850  81.388  1.00 22.55 ? 415  VAL   A CA    1 
ATOM   3029  C  C     . VAL   A  1  417  ? -62.317 52.350  81.070  1.00 20.95 ? 415  VAL   A C     1 
ATOM   3030  O  O     . VAL   A  1  417  ? -62.136 53.568  80.931  1.00 22.92 ? 415  VAL   A O     1 
ATOM   3031  C  CB    . VAL   A  1  417  ? -64.148 52.289  82.801  1.00 26.27 ? 415  VAL   A CB    1 
ATOM   3032  C  CG1   . VAL   A  1  417  ? -65.573 51.833  83.087  1.00 29.32 ? 415  VAL   A CG1   1 
ATOM   3033  C  CG2   . VAL   A  1  417  ? -63.192 51.752  83.820  1.00 24.93 ? 415  VAL   A CG2   1 
ATOM   3034  N  N     . VAL   A  1  418  ? -61.319 51.472  80.974  1.00 18.36 ? 416  VAL   A N     1 
ATOM   3035  C  CA    . VAL   A  1  418  ? -59.997 51.863  80.505  1.00 16.56 ? 416  VAL   A CA    1 
ATOM   3036  C  C     . VAL   A  1  418  ? -59.543 50.878  79.441  1.00 18.08 ? 416  VAL   A C     1 
ATOM   3037  O  O     . VAL   A  1  418  ? -60.050 49.763  79.334  1.00 19.32 ? 416  VAL   A O     1 
ATOM   3038  C  CB    . VAL   A  1  418  ? -58.938 51.957  81.631  1.00 15.84 ? 416  VAL   A CB    1 
ATOM   3039  C  CG1   . VAL   A  1  418  ? -59.284 53.094  82.602  1.00 19.78 ? 416  VAL   A CG1   1 
ATOM   3040  C  CG2   . VAL   A  1  418  ? -58.807 50.626  82.371  1.00 17.02 ? 416  VAL   A CG2   1 
ATOM   3041  N  N     . PHE   A  1  419  ? -58.560 51.304  78.658  1.00 15.46 ? 417  PHE   A N     1 
ATOM   3042  C  CA    . PHE   A  1  419  ? -57.952 50.452  77.644  1.00 18.06 ? 417  PHE   A CA    1 
ATOM   3043  C  C     . PHE   A  1  419  ? -56.549 50.107  78.121  1.00 16.12 ? 417  PHE   A C     1 
ATOM   3044  O  O     . PHE   A  1  419  ? -55.636 50.943  78.017  1.00 16.50 ? 417  PHE   A O     1 
ATOM   3045  C  CB    . PHE   A  1  419  ? -57.894 51.197  76.307  1.00 17.17 ? 417  PHE   A CB    1 
ATOM   3046  C  CG    . PHE   A  1  419  ? -57.167 50.445  75.215  1.00 18.24 ? 417  PHE   A CG    1 
ATOM   3047  C  CD1   . PHE   A  1  419  ? -57.607 49.196  74.806  1.00 20.31 ? 417  PHE   A CD1   1 
ATOM   3048  C  CD2   . PHE   A  1  419  ? -56.055 51.000  74.591  1.00 17.34 ? 417  PHE   A CD2   1 
ATOM   3049  C  CE1   . PHE   A  1  419  ? -56.968 48.510  73.799  1.00 18.37 ? 417  PHE   A CE1   1 
ATOM   3050  C  CE2   . PHE   A  1  419  ? -55.402 50.325  73.580  1.00 16.93 ? 417  PHE   A CE2   1 
ATOM   3051  C  CZ    . PHE   A  1  419  ? -55.851 49.076  73.175  1.00 17.37 ? 417  PHE   A CZ    1 
ATOM   3052  N  N     . PRO   A  1  420  ? -56.324 48.908  78.654  1.00 16.09 ? 418  PRO   A N     1 
ATOM   3053  C  CA    . PRO   A  1  420  ? -54.988 48.557  79.156  1.00 16.59 ? 418  PRO   A CA    1 
ATOM   3054  C  C     . PRO   A  1  420  ? -54.012 48.300  78.023  1.00 16.43 ? 418  PRO   A C     1 
ATOM   3055  O  O     . PRO   A  1  420  ? -54.350 47.690  77.008  1.00 17.90 ? 418  PRO   A O     1 
ATOM   3056  C  CB    . PRO   A  1  420  ? -55.233 47.270  79.953  1.00 15.71 ? 418  PRO   A CB    1 
ATOM   3057  C  CG    . PRO   A  1  420  ? -56.717 47.274  80.236  1.00 16.53 ? 418  PRO   A CG    1 
ATOM   3058  C  CD    . PRO   A  1  420  ? -57.319 47.881  79.002  1.00 16.62 ? 418  PRO   A CD    1 
ATOM   3059  N  N     . GLN   A  1  421  ? -52.776 48.741  78.231  1.00 15.36 ? 419  GLN   A N     1 
ATOM   3060  C  CA    . GLN   A  1  421  ? -51.715 48.626  77.238  1.00 17.16 ? 419  GLN   A CA    1 
ATOM   3061  C  C     . GLN   A  1  421  ? -50.506 48.093  77.984  1.00 16.98 ? 419  GLN   A C     1 
ATOM   3062  O  O     . GLN   A  1  421  ? -49.880 48.820  78.760  1.00 18.19 ? 419  GLN   A O     1 
ATOM   3063  C  CB    . GLN   A  1  421  ? -51.418 49.990  76.618  1.00 15.69 ? 419  GLN   A CB    1 
ATOM   3064  C  CG    . GLN   A  1  421  ? -52.641 50.581  75.926  1.00 15.86 ? 419  GLN   A CG    1 
ATOM   3065  C  CD    . GLN   A  1  421  ? -52.442 52.032  75.580  1.00 16.58 ? 419  GLN   A CD    1 
ATOM   3066  O  OE1   . GLN   A  1  421  ? -52.203 52.856  76.458  1.00 18.93 ? 419  GLN   A OE1   1 
ATOM   3067  N  NE2   . GLN   A  1  421  ? -52.516 52.352  74.288  1.00 17.26 ? 419  GLN   A NE2   1 
ATOM   3068  N  N     . PHE   A  1  422  ? -50.194 46.817  77.771  1.00 16.04 ? 420  PHE   A N     1 
ATOM   3069  C  CA    . PHE   A  1  422  ? -49.168 46.152  78.566  1.00 15.93 ? 420  PHE   A CA    1 
ATOM   3070  C  C     . PHE   A  1  422  ? -47.837 46.231  77.835  1.00 15.06 ? 420  PHE   A C     1 
ATOM   3071  O  O     . PHE   A  1  422  ? -47.543 45.412  76.962  1.00 17.35 ? 420  PHE   A O     1 
ATOM   3072  C  CB    . PHE   A  1  422  ? -49.578 44.723  78.877  1.00 17.48 ? 420  PHE   A CB    1 
ATOM   3073  C  CG    . PHE   A  1  422  ? -50.870 44.653  79.610  1.00 18.64 ? 420  PHE   A CG    1 
ATOM   3074  C  CD1   . PHE   A  1  422  ? -50.955 45.130  80.902  1.00 19.99 ? 420  PHE   A CD1   1 
ATOM   3075  C  CD2   . PHE   A  1  422  ? -52.008 44.175  78.992  1.00 17.27 ? 420  PHE   A CD2   1 
ATOM   3076  C  CE1   . PHE   A  1  422  ? -52.140 45.090  81.583  1.00 20.86 ? 420  PHE   A CE1   1 
ATOM   3077  C  CE2   . PHE   A  1  422  ? -53.209 44.129  79.673  1.00 20.97 ? 420  PHE   A CE2   1 
ATOM   3078  C  CZ    . PHE   A  1  422  ? -53.273 44.594  80.968  1.00 19.10 ? 420  PHE   A CZ    1 
ATOM   3079  N  N     . ALA   A  1  423  ? -47.036 47.218  78.215  1.00 16.03 ? 421  ALA   A N     1 
ATOM   3080  C  CA    . ALA   A  1  423  ? -45.731 47.448  77.609  1.00 16.26 ? 421  ALA   A CA    1 
ATOM   3081  C  C     . ALA   A  1  423  ? -44.706 46.595  78.345  1.00 19.44 ? 421  ALA   A C     1 
ATOM   3082  O  O     . ALA   A  1  423  ? -44.431 46.823  79.530  1.00 19.80 ? 421  ALA   A O     1 
ATOM   3083  C  CB    . ALA   A  1  423  ? -45.382 48.929  77.704  1.00 14.94 ? 421  ALA   A CB    1 
ATOM   3084  N  N     . THR   A  1  424  ? -44.151 45.605  77.655  1.00 17.46 ? 422  THR   A N     1 
ATOM   3085  C  CA    . THR   A  1  424  ? -43.109 44.790  78.263  1.00 18.00 ? 422  THR   A CA    1 
ATOM   3086  C  C     . THR   A  1  424  ? -42.415 43.973  77.184  1.00 19.26 ? 422  THR   A C     1 
ATOM   3087  O  O     . THR   A  1  424  ? -43.033 43.568  76.197  1.00 19.53 ? 422  THR   A O     1 
ATOM   3088  C  CB    . THR   A  1  424  ? -43.678 43.851  79.338  1.00 21.49 ? 422  THR   A CB    1 
ATOM   3089  O  OG1   . THR   A  1  424  ? -42.593 43.158  79.972  1.00 20.99 ? 422  THR   A OG1   1 
ATOM   3090  C  CG2   . THR   A  1  424  ? -44.661 42.844  78.725  1.00 22.23 ? 422  THR   A CG2   1 
ATOM   3091  N  N     . HIS   A  1  425  ? -41.123 43.746  77.385  1.00 17.74 ? 423  HIS   A N     1 
ATOM   3092  C  CA    . HIS   A  1  425  ? -40.370 42.813  76.569  1.00 17.43 ? 423  HIS   A CA    1 
ATOM   3093  C  C     . HIS   A  1  425  ? -40.146 41.491  77.267  1.00 20.50 ? 423  HIS   A C     1 
ATOM   3094  O  O     . HIS   A  1  425  ? -39.463 40.618  76.721  1.00 23.81 ? 423  HIS   A O     1 
ATOM   3095  C  CB    . HIS   A  1  425  ? -39.026 43.433  76.196  1.00 17.36 ? 423  HIS   A CB    1 
ATOM   3096  C  CG    . HIS   A  1  425  ? -39.168 44.698  75.423  1.00 20.15 ? 423  HIS   A CG    1 
ATOM   3097  N  ND1   . HIS   A  1  425  ? -38.425 45.826  75.692  1.00 22.20 ? 423  HIS   A ND1   1 
ATOM   3098  C  CD2   . HIS   A  1  425  ? -40.001 45.023  74.409  1.00 21.20 ? 423  HIS   A CD2   1 
ATOM   3099  C  CE1   . HIS   A  1  425  ? -38.783 46.788  74.859  1.00 23.07 ? 423  HIS   A CE1   1 
ATOM   3100  N  NE2   . HIS   A  1  425  ? -39.744 46.328  74.077  1.00 19.06 ? 423  HIS   A NE2   1 
ATOM   3101  N  N     . ASN   A  1  426  ? -40.708 41.317  78.451  1.00 20.59 ? 424  ASN   A N     1 
ATOM   3102  C  CA    . ASN   A  1  426  ? -40.456 40.130  79.255  1.00 23.43 ? 424  ASN   A CA    1 
ATOM   3103  C  C     . ASN   A  1  426  ? -41.487 39.067  78.888  1.00 22.15 ? 424  ASN   A C     1 
ATOM   3104  O  O     . ASN   A  1  426  ? -42.686 39.244  79.129  1.00 22.57 ? 424  ASN   A O     1 
ATOM   3105  C  CB    . ASN   A  1  426  ? -40.537 40.513  80.730  1.00 22.89 ? 424  ASN   A CB    1 
ATOM   3106  C  CG    . ASN   A  1  426  ? -40.175 39.371  81.650  1.00 23.22 ? 424  ASN   A CG    1 
ATOM   3107  O  OD1   . ASN   A  1  426  ? -40.582 38.241  81.427  1.00 24.05 ? 424  ASN   A OD1   1 
ATOM   3108  N  ND2   . ASN   A  1  426  ? -39.403 39.668  82.698  1.00 21.95 ? 424  ASN   A ND2   1 
ATOM   3109  N  N     . ALA   A  1  427  ? -41.021 37.955  78.311  1.00 20.07 ? 425  ALA   A N     1 
ATOM   3110  C  CA    . ALA   A  1  427  ? -41.933 36.920  77.839  1.00 23.21 ? 425  ALA   A CA    1 
ATOM   3111  C  C     . ALA   A  1  427  ? -42.706 36.269  78.982  1.00 21.30 ? 425  ALA   A C     1 
ATOM   3112  O  O     . ALA   A  1  427  ? -43.837 35.816  78.781  1.00 22.17 ? 425  ALA   A O     1 
ATOM   3113  C  CB    . ALA   A  1  427  ? -41.152 35.850  77.072  1.00 24.00 ? 425  ALA   A CB    1 
ATOM   3114  N  N     . GLN   A  1  428  ? -42.115 36.200  80.175  1.00 22.53 ? 426  GLN   A N     1 
ATOM   3115  C  CA    . GLN   A  1  428  ? -42.841 35.662  81.322  1.00 24.82 ? 426  GLN   A CA    1 
ATOM   3116  C  C     . GLN   A  1  428  ? -43.978 36.592  81.718  1.00 22.54 ? 426  GLN   A C     1 
ATOM   3117  O  O     . GLN   A  1  428  ? -45.106 36.145  81.959  1.00 23.94 ? 426  GLN   A O     1 
ATOM   3118  C  CB    . GLN   A  1  428  ? -41.882 35.460  82.496  1.00 23.51 ? 426  GLN   A CB    1 
ATOM   3119  C  CG    . GLN   A  1  428  ? -42.424 34.552  83.600  1.00 25.89 ? 426  GLN   A CG    1 
ATOM   3120  C  CD    . GLN   A  1  428  ? -43.502 35.206  84.453  1.00 29.98 ? 426  GLN   A CD    1 
ATOM   3121  O  OE1   . GLN   A  1  428  ? -43.452 36.406  84.729  1.00 31.34 ? 426  GLN   A OE1   1 
ATOM   3122  N  NE2   . GLN   A  1  428  ? -44.479 34.415  84.878  1.00 28.85 ? 426  GLN   A NE2   1 
ATOM   3123  N  N     . THR   A  1  429  ? -43.688 37.895  81.784  1.00 22.57 ? 427  THR   A N     1 
ATOM   3124  C  CA    . THR   A  1  429  ? -44.720 38.883  82.072  1.00 21.63 ? 427  THR   A CA    1 
ATOM   3125  C  C     . THR   A  1  429  ? -45.834 38.805  81.046  1.00 19.91 ? 427  THR   A C     1 
ATOM   3126  O  O     . THR   A  1  429  ? -47.020 38.764  81.396  1.00 22.84 ? 427  THR   A O     1 
ATOM   3127  C  CB    . THR   A  1  429  ? -44.107 40.282  82.036  1.00 22.14 ? 427  THR   A CB    1 
ATOM   3128  O  OG1   . THR   A  1  429  ? -42.938 40.320  82.858  1.00 23.90 ? 427  THR   A OG1   1 
ATOM   3129  C  CG2   . THR   A  1  429  ? -45.110 41.285  82.558  1.00 22.55 ? 427  THR   A CG2   1 
ATOM   3130  N  N     . LEU   A  1  430  ? -45.464 38.804  79.765  1.00 20.09 ? 428  LEU   A N     1 
ATOM   3131  C  CA    . LEU   A  1  430  ? -46.445 38.733  78.689  1.00 21.46 ? 428  LEU   A CA    1 
ATOM   3132  C  C     . LEU   A  1  430  ? -47.333 37.507  78.843  1.00 20.43 ? 428  LEU   A C     1 
ATOM   3133  O  O     . LEU   A  1  430  ? -48.567 37.604  78.797  1.00 21.58 ? 428  LEU   A O     1 
ATOM   3134  C  CB    . LEU   A  1  430  ? -45.706 38.676  77.354  1.00 20.98 ? 428  LEU   A CB    1 
ATOM   3135  C  CG    . LEU   A  1  430  ? -46.407 38.906  76.015  1.00 23.11 ? 428  LEU   A CG    1 
ATOM   3136  C  CD1   . LEU   A  1  430  ? -45.304 39.055  74.989  1.00 28.95 ? 428  LEU   A CD1   1 
ATOM   3137  C  CD2   . LEU   A  1  430  ? -47.310 37.754  75.616  1.00 27.46 ? 428  LEU   A CD2   1 
ATOM   3138  N  N     . ALA   A  1  431  ? -46.716 36.335  79.012  1.00 25.10 ? 429  ALA   A N     1 
ATOM   3139  C  CA    . ALA   A  1  431  ? -47.484 35.098  79.085  1.00 23.91 ? 429  ALA   A CA    1 
ATOM   3140  C  C     . ALA   A  1  431  ? -48.456 35.118  80.259  1.00 22.34 ? 429  ALA   A C     1 
ATOM   3141  O  O     . ALA   A  1  431  ? -49.614 34.707  80.124  1.00 21.78 ? 429  ALA   A O     1 
ATOM   3142  C  CB    . ALA   A  1  431  ? -46.535 33.905  79.204  1.00 23.40 ? 429  ALA   A CB    1 
ATOM   3143  N  N     . ALA   A  1  432  ? -48.004 35.623  81.408  1.00 23.63 ? 430  ALA   A N     1 
ATOM   3144  C  CA    . ALA   A  1  432  ? -48.871 35.714  82.577  1.00 24.76 ? 430  ALA   A CA    1 
ATOM   3145  C  C     . ALA   A  1  432  ? -50.108 36.549  82.284  1.00 23.44 ? 430  ALA   A C     1 
ATOM   3146  O  O     . ALA   A  1  432  ? -51.225 36.174  82.662  1.00 26.19 ? 430  ALA   A O     1 
ATOM   3147  C  CB    . ALA   A  1  432  ? -48.091 36.305  83.751  1.00 24.54 ? 430  ALA   A CB    1 
ATOM   3148  N  N     . ILE   A  1  433  ? -49.933 37.672  81.588  1.00 22.83 ? 431  ILE   A N     1 
ATOM   3149  C  CA    . ILE   A  1  433  ? -51.054 38.553  81.298  1.00 23.14 ? 431  ILE   A CA    1 
ATOM   3150  C  C     . ILE   A  1  433  ? -51.930 37.969  80.210  1.00 20.91 ? 431  ILE   A C     1 
ATOM   3151  O  O     . ILE   A  1  433  ? -53.157 38.045  80.284  1.00 22.90 ? 431  ILE   A O     1 
ATOM   3152  C  CB    . ILE   A  1  433  ? -50.516 39.941  80.927  1.00 22.02 ? 431  ILE   A CB    1 
ATOM   3153  C  CG1   . ILE   A  1  433  ? -49.825 40.536  82.149  1.00 24.91 ? 431  ILE   A CG1   1 
ATOM   3154  C  CG2   . ILE   A  1  433  ? -51.621 40.837  80.401  1.00 23.75 ? 431  ILE   A CG2   1 
ATOM   3155  C  CD1   . ILE   A  1  433  ? -49.270 41.870  81.903  1.00 27.08 ? 431  ILE   A CD1   1 
ATOM   3156  N  N     . TYR   A  1  434  ? -51.314 37.389  79.177  1.00 23.05 ? 432  TYR   A N     1 
ATOM   3157  C  CA    . TYR   A  1  434  ? -52.072 36.767  78.099  1.00 23.75 ? 432  TYR   A CA    1 
ATOM   3158  C  C     . TYR   A  1  434  ? -53.064 35.745  78.640  1.00 24.22 ? 432  TYR   A C     1 
ATOM   3159  O  O     . TYR   A  1  434  ? -54.231 35.710  78.228  1.00 25.34 ? 432  TYR   A O     1 
ATOM   3160  C  CB    . TYR   A  1  434  ? -51.087 36.107  77.136  1.00 23.31 ? 432  TYR   A CB    1 
ATOM   3161  C  CG    . TYR   A  1  434  ? -51.708 35.196  76.113  1.00 26.64 ? 432  TYR   A CG    1 
ATOM   3162  C  CD1   . TYR   A  1  434  ? -52.523 35.697  75.104  1.00 26.97 ? 432  TYR   A CD1   1 
ATOM   3163  C  CD2   . TYR   A  1  434  ? -51.468 33.824  76.149  1.00 27.11 ? 432  TYR   A CD2   1 
ATOM   3164  C  CE1   . TYR   A  1  434  ? -53.088 34.860  74.163  1.00 27.22 ? 432  TYR   A CE1   1 
ATOM   3165  C  CE2   . TYR   A  1  434  ? -52.024 32.980  75.216  1.00 30.65 ? 432  TYR   A CE2   1 
ATOM   3166  C  CZ    . TYR   A  1  434  ? -52.836 33.500  74.228  1.00 30.37 ? 432  TYR   A CZ    1 
ATOM   3167  O  OH    . TYR   A  1  434  ? -53.377 32.646  73.302  1.00 33.55 ? 432  TYR   A OH    1 
ATOM   3168  N  N     . HIS   A  1  435  ? -52.621 34.911  79.577  1.00 23.59 ? 433  HIS   A N     1 
ATOM   3169  C  CA    . HIS   A  1  435  ? -53.521 33.919  80.151  1.00 27.15 ? 433  HIS   A CA    1 
ATOM   3170  C  C     . HIS   A  1  435  ? -54.464 34.529  81.174  1.00 27.70 ? 433  HIS   A C     1 
ATOM   3171  O  O     . HIS   A  1  435  ? -55.620 34.103  81.271  1.00 27.26 ? 433  HIS   A O     1 
ATOM   3172  C  CB    . HIS   A  1  435  ? -52.723 32.755  80.729  1.00 30.54 ? 433  HIS   A CB    1 
ATOM   3173  C  CG    . HIS   A  1  435  ? -52.128 31.875  79.677  1.00 30.93 ? 433  HIS   A CG    1 
ATOM   3174  N  ND1   . HIS   A  1  435  ? -52.850 30.888  79.044  1.00 31.76 ? 433  HIS   A ND1   1 
ATOM   3175  C  CD2   . HIS   A  1  435  ? -50.899 31.866  79.108  1.00 28.28 ? 433  HIS   A CD2   1 
ATOM   3176  C  CE1   . HIS   A  1  435  ? -52.084 30.290  78.148  1.00 30.82 ? 433  HIS   A CE1   1 
ATOM   3177  N  NE2   . HIS   A  1  435  ? -50.895 30.864  78.168  1.00 30.04 ? 433  HIS   A NE2   1 
ATOM   3178  N  N     . MET   A  1  436  ? -54.003 35.541  81.915  1.00 25.83 ? 434  MET   A N     1 
ATOM   3179  C  CA    . MET   A  1  436  ? -54.890 36.242  82.838  1.00 24.34 ? 434  MET   A CA    1 
ATOM   3180  C  C     . MET   A  1  436  ? -56.061 36.879  82.103  1.00 24.65 ? 434  MET   A C     1 
ATOM   3181  O  O     . MET   A  1  436  ? -57.189 36.900  82.612  1.00 27.40 ? 434  MET   A O     1 
ATOM   3182  C  CB    . MET   A  1  436  ? -54.100 37.310  83.589  1.00 26.84 ? 434  MET   A CB    1 
ATOM   3183  C  CG    . MET   A  1  436  ? -54.923 38.058  84.606  1.00 27.30 ? 434  MET   A CG    1 
ATOM   3184  S  SD    . MET   A  1  436  ? -54.018 39.432  85.326  1.00 28.66 ? 434  MET   A SD    1 
ATOM   3185  C  CE    . MET   A  1  436  ? -52.780 38.563  86.285  1.00 28.06 ? 434  MET   A CE    1 
ATOM   3186  N  N     . ALA   A  1  437  ? -55.811 37.421  80.909  1.00 23.67 ? 435  ALA   A N     1 
ATOM   3187  C  CA    . ALA   A  1  437  ? -56.861 38.106  80.166  1.00 25.26 ? 435  ALA   A CA    1 
ATOM   3188  C  C     . ALA   A  1  437  ? -57.899 37.135  79.620  1.00 27.26 ? 435  ALA   A C     1 
ATOM   3189  O  O     . ALA   A  1  437  ? -59.052 37.520  79.402  1.00 27.29 ? 435  ALA   A O     1 
ATOM   3190  C  CB    . ALA   A  1  437  ? -56.243 38.921  79.033  1.00 27.09 ? 435  ALA   A CB    1 
ATOM   3191  N  N     . GLY   A  1  438  ? -57.516 35.887  79.388  1.00 30.27 ? 436  GLY   A N     1 
ATOM   3192  C  CA    . GLY   A  1  438  ? -58.464 34.881  78.955  1.00 33.25 ? 436  GLY   A CA    1 
ATOM   3193  C  C     . GLY   A  1  438  ? -58.692 34.854  77.460  1.00 31.22 ? 436  GLY   A C     1 
ATOM   3194  O  O     . GLY   A  1  438  ? -58.088 35.591  76.675  1.00 30.86 ? 436  GLY   A O     1 
ATOM   3195  N  N     . LYS   A  1  439  ? -59.633 33.984  77.070  1.00 36.65 ? 437  LYS   A N     1 
ATOM   3196  C  CA    . LYS   A  1  439  ? -59.869 33.654  75.668  1.00 37.34 ? 437  LYS   A CA    1 
ATOM   3197  C  C     . LYS   A  1  439  ? -60.756 34.660  74.945  1.00 34.58 ? 437  LYS   A C     1 
ATOM   3198  O  O     . LYS   A  1  439  ? -60.675 34.755  73.717  1.00 41.43 ? 437  LYS   A O     1 
ATOM   3199  C  CB    . LYS   A  1  439  ? -60.489 32.258  75.553  1.00 41.45 ? 437  LYS   A CB    1 
ATOM   3200  N  N     . ASP   A  1  440  ? -61.599 35.403  75.659  1.00 35.22 ? 438  ASP   A N     1 
ATOM   3201  C  CA    . ASP   A  1  440  ? -62.441 36.405  75.016  1.00 35.98 ? 438  ASP   A CA    1 
ATOM   3202  C  C     . ASP   A  1  440  ? -61.587 37.608  74.661  1.00 36.03 ? 438  ASP   A C     1 
ATOM   3203  O  O     . ASP   A  1  440  ? -61.110 38.321  75.550  1.00 36.43 ? 438  ASP   A O     1 
ATOM   3204  C  CB    . ASP   A  1  440  ? -63.574 36.827  75.946  1.00 37.91 ? 438  ASP   A CB    1 
ATOM   3205  C  CG    . ASP   A  1  440  ? -64.694 35.814  75.993  1.00 44.92 ? 438  ASP   A CG    1 
ATOM   3206  O  OD1   . ASP   A  1  440  ? -64.619 34.817  75.243  1.00 43.56 ? 438  ASP   A OD1   1 
ATOM   3207  O  OD2   . ASP   A  1  440  ? -65.646 36.017  76.777  1.00 48.41 ? 438  ASP   A OD2   1 
ATOM   3208  N  N     . PHE   A  1  441  ? -61.393 37.850  73.368  1.00 32.33 ? 439  PHE   A N     1 
ATOM   3209  C  CA    . PHE   A  1  441  ? -60.631 39.014  72.958  1.00 31.59 ? 439  PHE   A CA    1 
ATOM   3210  C  C     . PHE   A  1  441  ? -61.293 39.695  71.776  1.00 30.47 ? 439  PHE   A C     1 
ATOM   3211  O  O     . PHE   A  1  441  ? -61.859 39.041  70.899  1.00 30.44 ? 439  PHE   A O     1 
ATOM   3212  C  CB    . PHE   A  1  441  ? -59.165 38.701  72.600  1.00 28.01 ? 439  PHE   A CB    1 
ATOM   3213  C  CG    . PHE   A  1  441  ? -58.373 39.933  72.278  1.00 29.70 ? 439  PHE   A CG    1 
ATOM   3214  C  CD1   . PHE   A  1  441  ? -57.841 40.711  73.297  1.00 26.22 ? 439  PHE   A CD1   1 
ATOM   3215  C  CD2   . PHE   A  1  441  ? -58.212 40.351  70.967  1.00 26.90 ? 439  PHE   A CD2   1 
ATOM   3216  C  CE1   . PHE   A  1  441  ? -57.150 41.869  73.014  1.00 21.66 ? 439  PHE   A CE1   1 
ATOM   3217  C  CE2   . PHE   A  1  441  ? -57.521 41.515  70.680  1.00 25.89 ? 439  PHE   A CE2   1 
ATOM   3218  C  CZ    . PHE   A  1  441  ? -56.994 42.272  71.713  1.00 24.88 ? 439  PHE   A CZ    1 
ATOM   3219  N  N     . HIS   A  1  442  ? -61.202 41.018  71.762  1.00 26.19 ? 440  HIS   A N     1 
ATOM   3220  C  CA    . HIS   A  1  442  ? -61.545 41.815  70.601  1.00 26.65 ? 440  HIS   A CA    1 
ATOM   3221  C  C     . HIS   A  1  442  ? -60.575 42.982  70.558  1.00 29.45 ? 440  HIS   A C     1 
ATOM   3222  O  O     . HIS   A  1  442  ? -60.088 43.428  71.601  1.00 23.97 ? 440  HIS   A O     1 
ATOM   3223  C  CB    . HIS   A  1  442  ? -62.992 42.316  70.677  1.00 28.89 ? 440  HIS   A CB    1 
ATOM   3224  C  CG    . HIS   A  1  442  ? -63.267 43.208  71.848  1.00 22.77 ? 440  HIS   A CG    1 
ATOM   3225  N  ND1   . HIS   A  1  442  ? -63.657 42.725  73.079  1.00 28.66 ? 440  HIS   A ND1   1 
ATOM   3226  C  CD2   . HIS   A  1  442  ? -63.223 44.557  71.968  1.00 25.78 ? 440  HIS   A CD2   1 
ATOM   3227  C  CE1   . HIS   A  1  442  ? -63.836 43.738  73.908  1.00 27.43 ? 440  HIS   A CE1   1 
ATOM   3228  N  NE2   . HIS   A  1  442  ? -63.578 44.860  73.260  1.00 25.92 ? 440  HIS   A NE2   1 
ATOM   3229  N  N     . VAL   A  1  443  ? -60.275 43.459  69.346  1.00 30.88 ? 441  VAL   A N     1 
ATOM   3230  C  CA    . VAL   A  1  443  ? -59.428 44.637  69.227  1.00 31.01 ? 441  VAL   A CA    1 
ATOM   3231  C  C     . VAL   A  1  443  ? -60.115 45.795  69.927  1.00 25.74 ? 441  VAL   A C     1 
ATOM   3232  O  O     . VAL   A  1  443  ? -61.311 46.045  69.731  1.00 27.29 ? 441  VAL   A O     1 
ATOM   3233  C  CB    . VAL   A  1  443  ? -59.095 44.950  67.760  1.00 32.26 ? 441  VAL   A CB    1 
ATOM   3234  C  CG1   . VAL   A  1  443  ? -58.479 46.340  67.647  1.00 29.34 ? 441  VAL   A CG1   1 
ATOM   3235  C  CG2   . VAL   A  1  443  ? -58.125 43.919  67.210  1.00 35.32 ? 441  VAL   A CG2   1 
ATOM   3236  N  N     . GLY   A  1  444  ? -59.365 46.490  70.770  1.00 23.90 ? 442  GLY   A N     1 
ATOM   3237  C  CA    . GLY   A  1  444  ? -59.912 47.482  71.659  1.00 21.85 ? 442  GLY   A CA    1 
ATOM   3238  C  C     . GLY   A  1  444  ? -60.077 47.022  73.090  1.00 20.95 ? 442  GLY   A C     1 
ATOM   3239  O  O     . GLY   A  1  444  ? -60.312 47.856  73.963  1.00 21.70 ? 442  GLY   A O     1 
ATOM   3240  N  N     . LYS   A  1  445  ? -59.979 45.725  73.362  1.00 18.94 ? 443  LYS   A N     1 
ATOM   3241  C  CA    . LYS   A  1  445  ? -60.102 45.284  74.744  1.00 18.34 ? 443  LYS   A CA    1 
ATOM   3242  C  C     . LYS   A  1  445  ? -58.856 45.643  75.534  1.00 20.73 ? 443  LYS   A C     1 
ATOM   3243  O  O     . LYS   A  1  445  ? -58.937 46.280  76.591  1.00 20.18 ? 443  LYS   A O     1 
ATOM   3244  C  CB    . LYS   A  1  445  ? -60.360 43.787  74.826  1.00 20.92 ? 443  LYS   A CB    1 
ATOM   3245  C  CG    . LYS   A  1  445  ? -60.888 43.406  76.198  1.00 25.11 ? 443  LYS   A CG    1 
ATOM   3246  C  CD    . LYS   A  1  445  ? -61.112 41.927  76.351  1.00 31.40 ? 443  LYS   A CD    1 
ATOM   3247  C  CE    . LYS   A  1  445  ? -62.018 41.670  77.550  1.00 33.99 ? 443  LYS   A CE    1 
ATOM   3248  N  NZ    . LYS   A  1  445  ? -62.201 40.211  77.799  1.00 39.18 ? 443  LYS   A NZ    1 
ATOM   3249  N  N     . TYR   A  1  446  ? -57.697 45.223  75.039  1.00 19.82 ? 444  TYR   A N     1 
ATOM   3250  C  CA    . TYR   A  1  446  ? -56.400 45.631  75.561  1.00 20.25 ? 444  TYR   A CA    1 
ATOM   3251  C  C     . TYR   A  1  446  ? -55.403 45.389  74.442  1.00 18.92 ? 444  TYR   A C     1 
ATOM   3252  O  O     . TYR   A  1  446  ? -55.745 44.841  73.394  1.00 19.95 ? 444  TYR   A O     1 
ATOM   3253  C  CB    . TYR   A  1  446  ? -56.024 44.858  76.829  1.00 19.46 ? 444  TYR   A CB    1 
ATOM   3254  C  CG    . TYR   A  1  446  ? -55.761 43.386  76.601  1.00 22.33 ? 444  TYR   A CG    1 
ATOM   3255  C  CD1   . TYR   A  1  446  ? -56.798 42.457  76.658  1.00 27.09 ? 444  TYR   A CD1   1 
ATOM   3256  C  CD2   . TYR   A  1  446  ? -54.483 42.930  76.317  1.00 24.15 ? 444  TYR   A CD2   1 
ATOM   3257  C  CE1   . TYR   A  1  446  ? -56.559 41.118  76.444  1.00 27.17 ? 444  TYR   A CE1   1 
ATOM   3258  C  CE2   . TYR   A  1  446  ? -54.241 41.583  76.099  1.00 29.84 ? 444  TYR   A CE2   1 
ATOM   3259  C  CZ    . TYR   A  1  446  ? -55.285 40.692  76.165  1.00 29.39 ? 444  TYR   A CZ    1 
ATOM   3260  O  OH    . TYR   A  1  446  ? -55.043 39.356  75.950  1.00 43.81 ? 444  TYR   A OH    1 
ATOM   3261  N  N     . GLU   A  1  447  ? -54.162 45.798  74.668  1.00 17.34 ? 445  GLU   A N     1 
ATOM   3262  C  CA    . GLU   A  1  447  ? -53.112 45.500  73.708  1.00 17.24 ? 445  GLU   A CA    1 
ATOM   3263  C  C     . GLU   A  1  447  ? -51.822 45.331  74.479  1.00 19.02 ? 445  GLU   A C     1 
ATOM   3264  O  O     . GLU   A  1  447  ? -51.724 45.698  75.646  1.00 17.48 ? 445  GLU   A O     1 
ATOM   3265  C  CB    . GLU   A  1  447  ? -52.955 46.605  72.658  1.00 17.62 ? 445  GLU   A CB    1 
ATOM   3266  C  CG    . GLU   A  1  447  ? -52.485 47.920  73.258  1.00 19.00 ? 445  GLU   A CG    1 
ATOM   3267  C  CD    . GLU   A  1  447  ? -52.399 49.051  72.254  1.00 18.60 ? 445  GLU   A CD    1 
ATOM   3268  O  OE1   . GLU   A  1  447  ? -52.965 48.923  71.139  1.00 20.76 ? 445  GLU   A OE1   1 
ATOM   3269  O  OE2   . GLU   A  1  447  ? -51.765 50.081  72.587  1.00 18.42 ? 445  GLU   A OE2   1 
ATOM   3270  N  N     . PHE   A  1  448  ? -50.828 44.760  73.816  1.00 16.53 ? 446  PHE   A N     1 
ATOM   3271  C  CA    . PHE   A  1  448  ? -49.466 44.815  74.320  1.00 17.87 ? 446  PHE   A CA    1 
ATOM   3272  C  C     . PHE   A  1  448  ? -48.735 45.980  73.667  1.00 15.51 ? 446  PHE   A C     1 
ATOM   3273  O  O     . PHE   A  1  448  ? -49.207 46.569  72.694  1.00 17.37 ? 446  PHE   A O     1 
ATOM   3274  C  CB    . PHE   A  1  448  ? -48.748 43.507  74.011  1.00 19.37 ? 446  PHE   A CB    1 
ATOM   3275  C  CG    . PHE   A  1  448  ? -49.290 42.348  74.765  1.00 19.63 ? 446  PHE   A CG    1 
ATOM   3276  C  CD1   . PHE   A  1  448  ? -48.949 42.163  76.091  1.00 20.36 ? 446  PHE   A CD1   1 
ATOM   3277  C  CD2   . PHE   A  1  448  ? -50.154 41.451  74.155  1.00 22.21 ? 446  PHE   A CD2   1 
ATOM   3278  C  CE1   . PHE   A  1  448  ? -49.470 41.090  76.811  1.00 21.47 ? 446  PHE   A CE1   1 
ATOM   3279  C  CE2   . PHE   A  1  448  ? -50.671 40.370  74.860  1.00 24.21 ? 446  PHE   A CE2   1 
ATOM   3280  C  CZ    . PHE   A  1  448  ? -50.332 40.191  76.186  1.00 23.35 ? 446  PHE   A CZ    1 
ATOM   3281  N  N     . GLN   A  1  449  ? -47.584 46.330  74.232  1.00 15.68 ? 447  GLN   A N     1 
ATOM   3282  C  CA    . GLN   A  1  449  ? -46.730 47.338  73.627  1.00 16.39 ? 447  GLN   A CA    1 
ATOM   3283  C  C     . GLN   A  1  449  ? -45.278 46.927  73.757  1.00 18.01 ? 447  GLN   A C     1 
ATOM   3284  O  O     . GLN   A  1  449  ? -44.893 46.193  74.672  1.00 18.32 ? 447  GLN   A O     1 
ATOM   3285  C  CB    . GLN   A  1  449  ? -46.901 48.715  74.251  1.00 16.69 ? 447  GLN   A CB    1 
ATOM   3286  C  CG    . GLN   A  1  449  ? -48.310 49.237  74.126  1.00 16.41 ? 447  GLN   A CG    1 
ATOM   3287  C  CD    . GLN   A  1  449  ? -48.398 50.725  74.337  1.00 20.22 ? 447  GLN   A CD    1 
ATOM   3288  O  OE1   . GLN   A  1  449  ? -47.445 51.361  74.815  1.00 20.39 ? 447  GLN   A OE1   1 
ATOM   3289  N  NE2   . GLN   A  1  449  ? -49.537 51.298  73.984  1.00 17.20 ? 447  GLN   A NE2   1 
ATOM   3290  N  N     . CYS   A  1  450  ? -44.476 47.417  72.826  1.00 17.40 ? 448  CYS   A N     1 
ATOM   3291  C  CA    . CYS   A  1  450  ? -43.059 47.124  72.843  1.00 17.32 ? 448  CYS   A CA    1 
ATOM   3292  C  C     . CYS   A  1  450  ? -42.314 48.286  72.213  1.00 18.75 ? 448  CYS   A C     1 
ATOM   3293  O  O     . CYS   A  1  450  ? -42.908 49.194  71.622  1.00 18.50 ? 448  CYS   A O     1 
ATOM   3294  C  CB    . CYS   A  1  450  ? -42.759 45.822  72.108  1.00 18.79 ? 448  CYS   A CB    1 
ATOM   3295  S  SG    . CYS   A  1  450  ? -42.849 45.953  70.314  1.00 21.62 ? 448  CYS   A SG    1 
ATOM   3296  N  N     . LEU   A  1  451  ? -40.994 48.251  72.358  1.00 16.87 ? 449  LEU   A N     1 
ATOM   3297  C  CA    . LEU   A  1  451  ? -40.137 49.285  71.808  1.00 20.17 ? 449  LEU   A CA    1 
ATOM   3298  C  C     . LEU   A  1  451  ? -39.664 48.881  70.422  1.00 18.56 ? 449  LEU   A C     1 
ATOM   3299  O  O     . LEU   A  1  451  ? -39.337 47.717  70.176  1.00 21.48 ? 449  LEU   A O     1 
ATOM   3300  C  CB    . LEU   A  1  451  ? -38.926 49.497  72.717  1.00 20.51 ? 449  LEU   A CB    1 
ATOM   3301  C  CG    . LEU   A  1  451  ? -37.914 50.572  72.325  1.00 26.12 ? 449  LEU   A CG    1 
ATOM   3302  C  CD1   . LEU   A  1  451  ? -38.541 51.960  72.213  1.00 24.98 ? 449  LEU   A CD1   1 
ATOM   3303  C  CD2   . LEU   A  1  451  ? -36.774 50.573  73.341  1.00 24.57 ? 449  LEU   A CD2   1 
ATOM   3304  N  N     . HIS   A  1  452  ? -39.653 49.850  69.514  1.00 18.59 ? 450  HIS   A N     1 
ATOM   3305  C  CA    . HIS   A  1  452  ? -39.115 49.617  68.182  1.00 19.82 ? 450  HIS   A CA    1 
ATOM   3306  C  C     . HIS   A  1  452  ? -37.677 49.121  68.258  1.00 21.58 ? 450  HIS   A C     1 
ATOM   3307  O  O     . HIS   A  1  452  ? -36.888 49.585  69.082  1.00 23.62 ? 450  HIS   A O     1 
ATOM   3308  C  CB    . HIS   A  1  452  ? -39.129 50.922  67.397  1.00 19.64 ? 450  HIS   A CB    1 
ATOM   3309  C  CG    . HIS   A  1  452  ? -38.339 50.850  66.130  1.00 19.21 ? 450  HIS   A CG    1 
ATOM   3310  N  ND1   . HIS   A  1  452  ? -38.858 50.332  64.962  1.00 21.51 ? 450  HIS   A ND1   1 
ATOM   3311  C  CD2   . HIS   A  1  452  ? -37.058 51.196  65.856  1.00 24.05 ? 450  HIS   A CD2   1 
ATOM   3312  C  CE1   . HIS   A  1  452  ? -37.936 50.385  64.016  1.00 22.63 ? 450  HIS   A CE1   1 
ATOM   3313  N  NE2   . HIS   A  1  452  ? -36.834 50.900  64.535  1.00 22.66 ? 450  HIS   A NE2   1 
ATOM   3314  N  N     . GLY   A  1  453  ? -37.336 48.187  67.375  1.00 26.06 ? 451  GLY   A N     1 
ATOM   3315  C  CA    . GLY   A  1  453  ? -35.959 47.721  67.323  1.00 26.28 ? 451  GLY   A CA    1 
ATOM   3316  C  C     . GLY   A  1  453  ? -35.514 46.975  68.556  1.00 33.01 ? 451  GLY   A C     1 
ATOM   3317  O  O     . GLY   A  1  453  ? -34.311 46.867  68.813  1.00 34.95 ? 451  GLY   A O     1 
ATOM   3318  N  N     . MET   A  1  454  ? -36.460 46.465  69.338  1.00 25.27 ? 452  MET   A N     1 
ATOM   3319  C  CA    . MET   A  1  454  ? -36.148 45.696  70.531  1.00 23.02 ? 452  MET   A CA    1 
ATOM   3320  C  C     . MET   A  1  454  ? -37.210 44.628  70.737  1.00 24.92 ? 452  MET   A C     1 
ATOM   3321  O  O     . MET   A  1  454  ? -36.896 43.452  70.944  1.00 26.83 ? 452  MET   A O     1 
ATOM   3322  C  CB    . MET   A  1  454  ? -36.093 46.607  71.754  1.00 24.47 ? 452  MET   A CB    1 
ATOM   3323  C  CG    . MET   A  1  454  ? -35.932 45.839  73.043  1.00 27.27 ? 452  MET   A CG    1 
ATOM   3324  S  SD    . MET   A  1  454  ? -34.400 44.886  73.051  1.00 37.39 ? 452  MET   A SD    1 
ATOM   3325  C  CE    . MET   A  1  454  ? -33.211 46.221  73.185  1.00 34.05 ? 452  MET   A CE    1 
ATOM   3326  N  N     . GLY   A  1  455  ? -38.474 45.022  70.660  1.00 23.78 ? 453  GLY   A N     1 
ATOM   3327  C  CA    . GLY   A  1  455  ? -39.537 44.091  70.975  1.00 22.74 ? 453  GLY   A CA    1 
ATOM   3328  C  C     . GLY   A  1  455  ? -40.115 43.295  69.824  1.00 25.39 ? 453  GLY   A C     1 
ATOM   3329  O  O     . GLY   A  1  455  ? -40.894 42.369  70.069  1.00 25.44 ? 453  GLY   A O     1 
ATOM   3330  N  N     . GLU   A  1  456  ? -39.770 43.626  68.578  1.00 26.14 ? 454  GLU   A N     1 
ATOM   3331  C  CA    . GLU   A  1  456  ? -40.366 42.920  67.445  1.00 28.14 ? 454  GLU   A CA    1 
ATOM   3332  C  C     . GLU   A  1  456  ? -40.102 41.422  67.437  1.00 28.95 ? 454  GLU   A C     1 
ATOM   3333  O  O     . GLU   A  1  456  ? -41.033 40.670  67.100  1.00 29.17 ? 454  GLU   A O     1 
ATOM   3334  C  CB    . GLU   A  1  456  ? -39.958 43.546  66.105  1.00 29.48 ? 454  GLU   A CB    1 
ATOM   3335  C  CG    . GLU   A  1  456  ? -40.456 44.954  65.893  1.00 34.75 ? 454  GLU   A CG    1 
ATOM   3336  C  CD    . GLU   A  1  456  ? -39.434 45.974  66.311  1.00 33.40 ? 454  GLU   A CD    1 
ATOM   3337  O  OE1   . GLU   A  1  456  ? -38.535 45.612  67.104  1.00 30.58 ? 454  GLU   A OE1   1 
ATOM   3338  O  OE2   . GLU   A  1  456  ? -39.518 47.130  65.840  1.00 33.63 ? 454  GLU   A OE2   1 
ATOM   3339  N  N     . PRO   A  1  457  ? -38.900 40.922  67.751  1.00 25.70 ? 455  PRO   A N     1 
ATOM   3340  C  CA    . PRO   A  1  457  ? -38.729 39.461  67.760  1.00 27.56 ? 455  PRO   A CA    1 
ATOM   3341  C  C     . PRO   A  1  457  ? -39.704 38.751  68.680  1.00 29.40 ? 455  PRO   A C     1 
ATOM   3342  O  O     . PRO   A  1  457  ? -40.256 37.712  68.301  1.00 29.11 ? 455  PRO   A O     1 
ATOM   3343  C  CB    . PRO   A  1  457  ? -37.269 39.273  68.196  1.00 29.71 ? 455  PRO   A CB    1 
ATOM   3344  C  CG    . PRO   A  1  457  ? -36.599 40.529  67.814  1.00 30.27 ? 455  PRO   A CG    1 
ATOM   3345  C  CD    . PRO   A  1  457  ? -37.626 41.611  68.035  1.00 28.62 ? 455  PRO   A CD    1 
ATOM   3346  N  N     . LEU   A  1  458  ? -39.950 39.297  69.874  1.00 27.26 ? 456  LEU   A N     1 
ATOM   3347  C  CA    . LEU   A  1  458  ? -40.924 38.676  70.771  1.00 25.07 ? 456  LEU   A CA    1 
ATOM   3348  C  C     . LEU   A  1  458  ? -42.334 38.805  70.215  1.00 24.38 ? 456  LEU   A C     1 
ATOM   3349  O  O     . LEU   A  1  458  ? -43.087 37.828  70.160  1.00 22.46 ? 456  LEU   A O     1 
ATOM   3350  C  CB    . LEU   A  1  458  ? -40.843 39.318  72.154  1.00 24.13 ? 456  LEU   A CB    1 
ATOM   3351  C  CG    . LEU   A  1  458  ? -41.937 38.935  73.159  1.00 25.27 ? 456  LEU   A CG    1 
ATOM   3352  C  CD1   . LEU   A  1  458  ? -41.936 37.427  73.398  1.00 25.10 ? 456  LEU   A CD1   1 
ATOM   3353  C  CD2   . LEU   A  1  458  ? -41.725 39.692  74.462  1.00 25.18 ? 456  LEU   A CD2   1 
ATOM   3354  N  N     . TYR   A  1  459  ? -42.710 40.006  69.797  1.00 24.40 ? 457  TYR   A N     1 
ATOM   3355  C  CA    . TYR   A  1  459  ? -44.095 40.229  69.429  1.00 23.77 ? 457  TYR   A CA    1 
ATOM   3356  C  C     . TYR   A  1  459  ? -44.455 39.694  68.056  1.00 23.61 ? 457  TYR   A C     1 
ATOM   3357  O  O     . TYR   A  1  459  ? -45.644 39.519  67.773  1.00 25.83 ? 457  TYR   A O     1 
ATOM   3358  C  CB    . TYR   A  1  459  ? -44.467 41.692  69.640  1.00 21.27 ? 457  TYR   A CB    1 
ATOM   3359  C  CG    . TYR   A  1  459  ? -44.668 41.948  71.105  1.00 20.22 ? 457  TYR   A CG    1 
ATOM   3360  C  CD1   . TYR   A  1  459  ? -45.858 41.576  71.720  1.00 22.87 ? 457  TYR   A CD1   1 
ATOM   3361  C  CD2   . TYR   A  1  459  ? -43.664 42.499  71.889  1.00 21.42 ? 457  TYR   A CD2   1 
ATOM   3362  C  CE1   . TYR   A  1  459  ? -46.059 41.781  73.059  1.00 20.75 ? 457  TYR   A CE1   1 
ATOM   3363  C  CE2   . TYR   A  1  459  ? -43.863 42.711  73.251  1.00 21.17 ? 457  TYR   A CE2   1 
ATOM   3364  C  CZ    . TYR   A  1  459  ? -45.065 42.349  73.823  1.00 20.97 ? 457  TYR   A CZ    1 
ATOM   3365  O  OH    . TYR   A  1  459  ? -45.282 42.546  75.170  1.00 21.38 ? 457  TYR   A OH    1 
ATOM   3366  N  N     . GLU   A  1  460  ? -43.466 39.386  67.217  1.00 25.52 ? 458  GLU   A N     1 
ATOM   3367  C  CA    . GLU   A  1  460  ? -43.761 38.585  66.037  1.00 29.46 ? 458  GLU   A CA    1 
ATOM   3368  C  C     . GLU   A  1  460  ? -44.178 37.165  66.393  1.00 30.44 ? 458  GLU   A C     1 
ATOM   3369  O  O     . GLU   A  1  460  ? -44.727 36.461  65.538  1.00 31.85 ? 458  GLU   A O     1 
ATOM   3370  C  CB    . GLU   A  1  460  ? -42.591 38.609  65.055  1.00 33.72 ? 458  GLU   A CB    1 
ATOM   3371  C  CG    . GLU   A  1  460  ? -42.506 39.916  64.278  1.00 37.41 ? 458  GLU   A CG    1 
ATOM   3372  C  CD    . GLU   A  1  460  ? -41.417 39.907  63.225  1.00 49.64 ? 458  GLU   A CD    1 
ATOM   3373  O  OE1   . GLU   A  1  460  ? -40.677 38.902  63.145  1.00 52.00 ? 458  GLU   A OE1   1 
ATOM   3374  O  OE2   . GLU   A  1  460  ? -41.302 40.904  62.478  1.00 53.98 ? 458  GLU   A OE2   1 
ATOM   3375  N  N     . GLU   A  1  461  ? -43.949 36.736  67.631  1.00 27.44 ? 459  GLU   A N     1 
ATOM   3376  C  CA    . GLU   A  1  461  ? -44.487 35.479  68.132  1.00 31.20 ? 459  GLU   A CA    1 
ATOM   3377  C  C     . GLU   A  1  461  ? -45.824 35.663  68.834  1.00 30.20 ? 459  GLU   A C     1 
ATOM   3378  O  O     . GLU   A  1  461  ? -46.360 34.698  69.391  1.00 30.90 ? 459  GLU   A O     1 
ATOM   3379  C  CB    . GLU   A  1  461  ? -43.494 34.828  69.097  1.00 27.50 ? 459  GLU   A CB    1 
ATOM   3380  C  CG    . GLU   A  1  461  ? -42.088 34.710  68.548  1.00 31.20 ? 459  GLU   A CG    1 
ATOM   3381  C  CD    . GLU   A  1  461  ? -42.007 33.807  67.326  1.00 35.44 ? 459  GLU   A CD    1 
ATOM   3382  O  OE1   . GLU   A  1  461  ? -42.915 32.968  67.128  1.00 36.94 ? 459  GLU   A OE1   1 
ATOM   3383  O  OE2   . GLU   A  1  461  ? -41.025 33.936  66.564  1.00 39.00 ? 459  GLU   A OE2   1 
ATOM   3384  N  N     . VAL   A  1  462  ? -46.367 36.877  68.814  1.00 26.54 ? 460  VAL   A N     1 
ATOM   3385  C  CA    . VAL   A  1  462  ? -47.599 37.219  69.513  1.00 26.02 ? 460  VAL   A CA    1 
ATOM   3386  C  C     . VAL   A  1  462  ? -48.676 37.687  68.542  1.00 26.55 ? 460  VAL   A C     1 
ATOM   3387  O  O     . VAL   A  1  462  ? -49.803 37.174  68.543  1.00 28.41 ? 460  VAL   A O     1 
ATOM   3388  C  CB    . VAL   A  1  462  ? -47.344 38.284  70.604  1.00 26.14 ? 460  VAL   A CB    1 
ATOM   3389  C  CG1   . VAL   A  1  462  ? -48.650 38.693  71.263  1.00 24.99 ? 460  VAL   A CG1   1 
ATOM   3390  C  CG2   . VAL   A  1  462  ? -46.353 37.760  71.628  1.00 25.85 ? 460  VAL   A CG2   1 
ATOM   3391  N  N     . VAL   A  1  463  ? -48.341 38.655  67.691  1.00 25.67 ? 461  VAL   A N     1 
ATOM   3392  C  CA    . VAL   A  1  463  ? -49.328 39.282  66.824  1.00 26.93 ? 461  VAL   A CA    1 
ATOM   3393  C  C     . VAL   A  1  463  ? -49.715 38.332  65.700  1.00 32.18 ? 461  VAL   A C     1 
ATOM   3394  O  O     . VAL   A  1  463  ? -48.868 37.628  65.139  1.00 34.31 ? 461  VAL   A O     1 
ATOM   3395  C  CB    . VAL   A  1  463  ? -48.748 40.590  66.266  1.00 26.87 ? 461  VAL   A CB    1 
ATOM   3396  C  CG1   . VAL   A  1  463  ? -49.721 41.218  65.277  1.00 28.22 ? 461  VAL   A CG1   1 
ATOM   3397  C  CG2   . VAL   A  1  463  ? -48.426 41.551  67.405  1.00 27.27 ? 461  VAL   A CG2   1 
ATOM   3398  N  N     . GLY   A  1  464  ? -50.991 38.311  65.365  1.00 31.76 ? 462  GLY   A N     1 
ATOM   3399  C  CA    . GLY   A  1  464  ? -51.418 37.568  64.199  1.00 36.50 ? 462  GLY   A CA    1 
ATOM   3400  C  C     . GLY   A  1  464  ? -52.141 36.286  64.571  1.00 35.52 ? 462  GLY   A C     1 
ATOM   3401  O  O     . GLY   A  1  464  ? -51.880 35.669  65.613  1.00 33.08 ? 462  GLY   A O     1 
ATOM   3402  N  N     . ARG   A  1  465  ? -53.059 35.870  63.691  1.00 33.96 ? 463  ARG   A N     1 
ATOM   3403  C  CA    . ARG   A  1  465  ? -53.867 34.681  63.945  1.00 34.00 ? 463  ARG   A CA    1 
ATOM   3404  C  C     . ARG   A  1  465  ? -53.011 33.428  64.074  1.00 37.60 ? 463  ARG   A C     1 
ATOM   3405  O  O     . ARG   A  1  465  ? -53.385 32.492  64.787  1.00 41.08 ? 463  ARG   A O     1 
ATOM   3406  C  CB    . ARG   A  1  465  ? -54.904 34.510  62.834  1.00 38.19 ? 463  ARG   A CB    1 
ATOM   3407  N  N     . GLY   A  1  466  ? -51.868 33.389  63.407  1.00 33.71 ? 464  GLY   A N     1 
ATOM   3408  C  CA    . GLY   A  1  466  ? -50.998 32.241  63.539  1.00 34.10 ? 464  GLY   A CA    1 
ATOM   3409  C  C     . GLY   A  1  466  ? -50.198 32.184  64.818  1.00 37.83 ? 464  GLY   A C     1 
ATOM   3410  O  O     . GLY   A  1  466  ? -49.492 31.200  65.054  1.00 37.65 ? 464  GLY   A O     1 
ATOM   3411  N  N     . LYS   A  1  467  ? -50.283 33.223  65.657  1.00 35.90 ? 465  LYS   A N     1 
ATOM   3412  C  CA    . LYS   A  1  467  ? -49.522 33.281  66.899  1.00 31.51 ? 465  LYS   A CA    1 
ATOM   3413  C  C     . LYS   A  1  467  ? -50.516 33.324  68.053  1.00 35.23 ? 465  LYS   A C     1 
ATOM   3414  O  O     . LYS   A  1  467  ? -51.348 32.429  68.164  1.00 35.61 ? 465  LYS   A O     1 
ATOM   3415  C  CB    . LYS   A  1  467  ? -48.487 34.395  66.865  1.00 31.94 ? 465  LYS   A CB    1 
ATOM   3416  C  CG    . LYS   A  1  467  ? -47.494 34.276  65.724  1.00 33.96 ? 465  LYS   A CG    1 
ATOM   3417  C  CD    . LYS   A  1  467  ? -46.575 33.082  65.924  1.00 35.99 ? 465  LYS   A CD    1 
ATOM   3418  C  CE    . LYS   A  1  467  ? -45.432 33.095  64.917  1.00 38.48 ? 465  LYS   A CE    1 
ATOM   3419  N  NZ    . LYS   A  1  467  ? -44.423 32.039  65.220  1.00 38.51 ? 465  LYS   A NZ    1 
ATOM   3420  N  N     . LEU   A  1  468  ? -50.447 34.333  68.917  1.00 32.94 ? 466  LEU   A N     1 
ATOM   3421  C  CA    . LEU   A  1  468  ? -51.404 34.485  70.003  1.00 31.18 ? 466  LEU   A CA    1 
ATOM   3422  C  C     . LEU   A  1  468  ? -52.584 35.368  69.626  1.00 30.70 ? 466  LEU   A C     1 
ATOM   3423  O  O     . LEU   A  1  468  ? -53.536 35.475  70.408  1.00 29.29 ? 466  LEU   A O     1 
ATOM   3424  C  CB    . LEU   A  1  468  ? -50.708 35.048  71.244  1.00 30.60 ? 466  LEU   A CB    1 
ATOM   3425  C  CG    . LEU   A  1  468  ? -49.484 34.264  71.727  1.00 32.05 ? 466  LEU   A CG    1 
ATOM   3426  C  CD1   . LEU   A  1  468  ? -48.966 34.824  73.036  1.00 30.98 ? 466  LEU   A CD1   1 
ATOM   3427  C  CD2   . LEU   A  1  468  ? -49.814 32.779  71.864  1.00 36.52 ? 466  LEU   A CD2   1 
ATOM   3428  N  N     . ASP   A  1  469  ? -52.540 35.993  68.450  1.00 31.38 ? 467  ASP   A N     1 
ATOM   3429  C  CA    . ASP   A  1  469  ? -53.617 36.846  67.961  1.00 29.65 ? 467  ASP   A CA    1 
ATOM   3430  C  C     . ASP   A  1  469  ? -53.928 37.964  68.947  1.00 27.98 ? 467  ASP   A C     1 
ATOM   3431  O  O     . ASP   A  1  469  ? -55.087 38.233  69.265  1.00 24.97 ? 467  ASP   A O     1 
ATOM   3432  C  CB    . ASP   A  1  469  ? -54.872 36.047  67.605  1.00 31.41 ? 467  ASP   A CB    1 
ATOM   3433  C  CG    . ASP   A  1  469  ? -55.776 36.786  66.640  1.00 35.40 ? 467  ASP   A CG    1 
ATOM   3434  O  OD1   . ASP   A  1  469  ? -55.296 37.717  65.958  1.00 36.06 ? 467  ASP   A OD1   1 
ATOM   3435  O  OD2   . ASP   A  1  469  ? -56.973 36.440  66.569  1.00 42.90 ? 467  ASP   A OD2   1 
ATOM   3436  N  N     . ARG   A  1  470  ? -52.875 38.600  69.454  1.00 27.34 ? 468  ARG   A N     1 
ATOM   3437  C  CA    . ARG   A  1  470  ? -53.016 39.778  70.283  1.00 23.73 ? 468  ARG   A CA    1 
ATOM   3438  C  C     . ARG   A  1  470  ? -52.224 40.924  69.669  1.00 24.79 ? 468  ARG   A C     1 
ATOM   3439  O  O     . ARG   A  1  470  ? -51.106 40.717  69.185  1.00 25.17 ? 468  ARG   A O     1 
ATOM   3440  C  CB    . ARG   A  1  470  ? -52.505 39.517  71.710  1.00 23.51 ? 468  ARG   A CB    1 
ATOM   3441  C  CG    . ARG   A  1  470  ? -53.305 38.459  72.477  1.00 22.34 ? 468  ARG   A CG    1 
ATOM   3442  C  CD    . ARG   A  1  470  ? -54.766 38.853  72.680  1.00 25.44 ? 468  ARG   A CD    1 
ATOM   3443  N  NE    . ARG   A  1  470  ? -55.499 37.797  73.374  1.00 25.02 ? 468  ARG   A NE    1 
ATOM   3444  C  CZ    . ARG   A  1  470  ? -56.217 36.858  72.773  1.00 25.77 ? 468  ARG   A CZ    1 
ATOM   3445  N  NH1   . ARG   A  1  470  ? -56.357 36.829  71.456  1.00 27.11 ? 468  ARG   A NH1   1 
ATOM   3446  N  NH2   . ARG   A  1  470  ? -56.815 35.925  73.512  1.00 28.34 ? 468  ARG   A NH2   1 
ATOM   3447  N  N     . PRO   A  1  471  ? -52.778 42.130  69.659  1.00 22.75 ? 469  PRO   A N     1 
ATOM   3448  C  CA    . PRO   A  1  471  ? -52.104 43.256  69.012  1.00 19.69 ? 469  PRO   A CA    1 
ATOM   3449  C  C     . PRO   A  1  471  ? -50.986 43.804  69.878  1.00 21.97 ? 469  PRO   A C     1 
ATOM   3450  O  O     . PRO   A  1  471  ? -50.973 43.678  71.104  1.00 20.62 ? 469  PRO   A O     1 
ATOM   3451  C  CB    . PRO   A  1  471  ? -53.220 44.295  68.883  1.00 22.52 ? 469  PRO   A CB    1 
ATOM   3452  C  CG    . PRO   A  1  471  ? -54.083 44.019  70.072  1.00 22.69 ? 469  PRO   A CG    1 
ATOM   3453  C  CD    . PRO   A  1  471  ? -54.086 42.512  70.206  1.00 23.04 ? 469  PRO   A CD    1 
ATOM   3454  N  N     . CYS   A  1  472  ? -50.042 44.448  69.204  1.00 20.15 ? 470  CYS   A N     1 
ATOM   3455  C  CA    . CYS   A  1  472  ? -48.934 45.099  69.879  1.00 20.64 ? 470  CYS   A CA    1 
ATOM   3456  C  C     . CYS   A  1  472  ? -48.723 46.455  69.240  1.00 20.63 ? 470  CYS   A C     1 
ATOM   3457  O  O     . CYS   A  1  472  ? -48.670 46.567  68.010  1.00 22.54 ? 470  CYS   A O     1 
ATOM   3458  C  CB    . CYS   A  1  472  ? -47.648 44.282  69.757  1.00 20.93 ? 470  CYS   A CB    1 
ATOM   3459  S  SG    . CYS   A  1  472  ? -46.269 44.999  70.677  1.00 22.96 ? 470  CYS   A SG    1 
ATOM   3460  N  N     . ARG   A  1  473  ? -48.614 47.477  70.072  1.00 18.25 ? 471  ARG   A N     1 
ATOM   3461  C  CA    . ARG   A  1  473  ? -48.291 48.818  69.616  1.00 17.19 ? 471  ARG   A CA    1 
ATOM   3462  C  C     . ARG   A  1  473  ? -46.807 49.062  69.835  1.00 18.96 ? 471  ARG   A C     1 
ATOM   3463  O  O     . ARG   A  1  473  ? -46.296 48.886  70.948  1.00 17.27 ? 471  ARG   A O     1 
ATOM   3464  C  CB    . ARG   A  1  473  ? -49.109 49.869  70.360  1.00 18.96 ? 471  ARG   A CB    1 
ATOM   3465  C  CG    . ARG   A  1  473  ? -48.898 51.278  69.812  1.00 18.37 ? 471  ARG   A CG    1 
ATOM   3466  C  CD    . ARG   A  1  473  ? -49.813 52.261  70.503  1.00 17.41 ? 471  ARG   A CD    1 
ATOM   3467  N  NE    . ARG   A  1  473  ? -51.186 51.782  70.454  1.00 17.93 ? 471  ARG   A NE    1 
ATOM   3468  C  CZ    . ARG   A  1  473  ? -52.008 51.970  69.433  1.00 21.68 ? 471  ARG   A CZ    1 
ATOM   3469  N  NH1   . ARG   A  1  473  ? -51.658 52.708  68.393  1.00 20.13 ? 471  ARG   A NH1   1 
ATOM   3470  N  NH2   . ARG   A  1  473  ? -53.207 51.392  69.454  1.00 20.89 ? 471  ARG   A NH2   1 
ATOM   3471  N  N     . ILE   A  1  474  ? -46.131 49.476  68.775  1.00 19.02 ? 472  ILE   A N     1 
ATOM   3472  C  CA    . ILE   A  1  474  ? -44.689 49.673  68.791  1.00 17.02 ? 472  ILE   A CA    1 
ATOM   3473  C  C     . ILE   A  1  474  ? -44.419 51.121  69.145  1.00 18.72 ? 472  ILE   A C     1 
ATOM   3474  O  O     . ILE   A  1  474  ? -44.872 52.030  68.444  1.00 17.93 ? 472  ILE   A O     1 
ATOM   3475  C  CB    . ILE   A  1  474  ? -44.084 49.330  67.425  1.00 17.37 ? 472  ILE   A CB    1 
ATOM   3476  C  CG1   . ILE   A  1  474  ? -44.347 47.864  67.091  1.00 20.60 ? 472  ILE   A CG1   1 
ATOM   3477  C  CG2   . ILE   A  1  474  ? -42.588 49.655  67.411  1.00 18.76 ? 472  ILE   A CG2   1 
ATOM   3478  C  CD1   . ILE   A  1  474  ? -43.906 47.477  65.681  1.00 22.35 ? 472  ILE   A CD1   1 
ATOM   3479  N  N     . TYR   A  1  475  ? -43.686 51.336  70.235  1.00 19.26 ? 473  TYR   A N     1 
ATOM   3480  C  CA    . TYR   A  1  475  ? -43.252 52.675  70.609  1.00 19.36 ? 473  TYR   A CA    1 
ATOM   3481  C  C     . TYR   A  1  475  ? -42.078 53.048  69.712  1.00 18.08 ? 473  TYR   A C     1 
ATOM   3482  O  O     . TYR   A  1  475  ? -41.031 52.388  69.737  1.00 18.60 ? 473  TYR   A O     1 
ATOM   3483  C  CB    . TYR   A  1  475  ? -42.839 52.700  72.079  1.00 19.90 ? 473  TYR   A CB    1 
ATOM   3484  C  CG    . TYR   A  1  475  ? -42.566 54.075  72.658  1.00 18.69 ? 473  TYR   A CG    1 
ATOM   3485  C  CD1   . TYR   A  1  475  ? -41.297 54.641  72.594  1.00 23.65 ? 473  TYR   A CD1   1 
ATOM   3486  C  CD2   . TYR   A  1  475  ? -43.576 54.798  73.284  1.00 19.07 ? 473  TYR   A CD2   1 
ATOM   3487  C  CE1   . TYR   A  1  475  ? -41.043 55.901  73.135  1.00 21.85 ? 473  TYR   A CE1   1 
ATOM   3488  C  CE2   . TYR   A  1  475  ? -43.336 56.053  73.824  1.00 19.52 ? 473  TYR   A CE2   1 
ATOM   3489  C  CZ    . TYR   A  1  475  ? -42.068 56.596  73.747  1.00 23.88 ? 473  TYR   A CZ    1 
ATOM   3490  O  OH    . TYR   A  1  475  ? -41.830 57.842  74.274  1.00 26.10 ? 473  TYR   A OH    1 
ATOM   3491  N  N     . ALA   A  1  476  ? -42.254 54.101  68.924  1.00 17.69 ? 474  ALA   A N     1 
ATOM   3492  C  CA    . ALA   A  1  476  ? -41.395 54.361  67.770  1.00 18.87 ? 474  ALA   A CA    1 
ATOM   3493  C  C     . ALA   A  1  476  ? -40.694 55.694  67.940  1.00 17.77 ? 474  ALA   A C     1 
ATOM   3494  O  O     . ALA   A  1  476  ? -41.284 56.749  67.647  1.00 18.14 ? 474  ALA   A O     1 
ATOM   3495  C  CB    . ALA   A  1  476  ? -42.257 54.372  66.511  1.00 18.31 ? 474  ALA   A CB    1 
ATOM   3496  N  N     . PRO   A  1  477  ? -39.435 55.705  68.377  1.00 19.50 ? 475  PRO   A N     1 
ATOM   3497  C  CA    . PRO   A  1  477  ? -38.701 56.969  68.463  1.00 19.96 ? 475  PRO   A CA    1 
ATOM   3498  C  C     . PRO   A  1  477  ? -38.448 57.513  67.070  1.00 17.72 ? 475  PRO   A C     1 
ATOM   3499  O  O     . PRO   A  1  477  ? -38.225 56.767  66.115  1.00 18.33 ? 475  PRO   A O     1 
ATOM   3500  C  CB    . PRO   A  1  477  ? -37.379 56.575  69.139  1.00 22.38 ? 475  PRO   A CB    1 
ATOM   3501  C  CG    . PRO   A  1  477  ? -37.619 55.195  69.700  1.00 25.14 ? 475  PRO   A CG    1 
ATOM   3502  C  CD    . PRO   A  1  477  ? -38.604 54.558  68.769  1.00 21.89 ? 475  PRO   A CD    1 
ATOM   3503  N  N     . VAL   A  1  478  ? -38.504 58.827  66.959  1.00 17.12 ? 476  VAL   A N     1 
ATOM   3504  C  CA    . VAL   A  1  478  ? -38.323 59.500  65.683  1.00 18.20 ? 476  VAL   A CA    1 
ATOM   3505  C  C     . VAL   A  1  478  ? -37.406 60.682  65.924  1.00 21.65 ? 476  VAL   A C     1 
ATOM   3506  O  O     . VAL   A  1  478  ? -37.682 61.519  66.787  1.00 25.00 ? 476  VAL   A O     1 
ATOM   3507  C  CB    . VAL   A  1  478  ? -39.677 59.994  65.140  1.00 20.64 ? 476  VAL   A CB    1 
ATOM   3508  C  CG1   . VAL   A  1  478  ? -39.500 60.742  63.821  1.00 21.09 ? 476  VAL   A CG1   1 
ATOM   3509  C  CG2   . VAL   A  1  478  ? -40.645 58.832  64.967  1.00 20.88 ? 476  VAL   A CG2   1 
ATOM   3510  N  N     . GLY   A  1  479  ? -36.308 60.746  65.191  1.00 23.35 ? 477  GLY   A N     1 
ATOM   3511  C  CA    . GLY   A  1  479  ? -35.440 61.893  65.338  1.00 26.90 ? 477  GLY   A CA    1 
ATOM   3512  C  C     . GLY   A  1  479  ? -34.076 61.626  64.761  1.00 24.73 ? 477  GLY   A C     1 
ATOM   3513  O  O     . GLY   A  1  479  ? -33.752 60.515  64.334  1.00 23.72 ? 477  GLY   A O     1 
ATOM   3514  N  N     . THR   A  1  480  ? -33.271 62.683  64.768  1.00 28.79 ? 478  THR   A N     1 
ATOM   3515  C  CA    . THR   A  1  480  ? -31.953 62.670  64.157  1.00 30.81 ? 478  THR   A CA    1 
ATOM   3516  C  C     . THR   A  1  480  ? -30.947 61.992  65.083  1.00 35.41 ? 478  THR   A C     1 
ATOM   3517  O  O     . THR   A  1  480  ? -31.251 61.626  66.221  1.00 38.13 ? 478  THR   A O     1 
ATOM   3518  C  CB    . THR   A  1  480  ? -31.510 64.099  63.857  1.00 33.10 ? 478  THR   A CB    1 
ATOM   3519  O  OG1   . THR   A  1  480  ? -31.367 64.805  65.093  1.00 43.03 ? 478  THR   A OG1   1 
ATOM   3520  C  CG2   . THR   A  1  480  ? -32.543 64.805  63.003  1.00 31.91 ? 478  THR   A CG2   1 
ATOM   3521  N  N     . HIS   A  1  481  ? -29.720 61.839  64.581  1.00 34.25 ? 479  HIS   A N     1 
ATOM   3522  C  CA    . HIS   A  1  481  ? -28.652 61.242  65.378  1.00 42.53 ? 479  HIS   A CA    1 
ATOM   3523  C  C     . HIS   A  1  481  ? -28.388 62.047  66.645  1.00 44.06 ? 479  HIS   A C     1 
ATOM   3524  O  O     . HIS   A  1  481  ? -28.173 61.473  67.720  1.00 44.84 ? 479  HIS   A O     1 
ATOM   3525  C  CB    . HIS   A  1  481  ? -27.374 61.148  64.547  1.00 35.76 ? 479  HIS   A CB    1 
ATOM   3526  C  CG    . HIS   A  1  481  ? -27.516 60.334  63.298  1.00 39.59 ? 479  HIS   A CG    1 
ATOM   3527  N  ND1   . HIS   A  1  481  ? -26.509 60.232  62.361  1.00 40.07 ? 479  HIS   A ND1   1 
ATOM   3528  C  CD2   . HIS   A  1  481  ? -28.542 59.584  62.830  1.00 35.97 ? 479  HIS   A CD2   1 
ATOM   3529  C  CE1   . HIS   A  1  481  ? -26.911 59.459  61.368  1.00 37.69 ? 479  HIS   A CE1   1 
ATOM   3530  N  NE2   . HIS   A  1  481  ? -28.140 59.050  61.629  1.00 40.08 ? 479  HIS   A NE2   1 
ATOM   3531  N  N     . GLU   A  1  482  ? -28.393 63.379  66.537  1.00 44.04 ? 480  GLU   A N     1 
ATOM   3532  C  CA    . GLU   A  1  482  ? -28.162 64.219  67.708  1.00 46.07 ? 480  GLU   A CA    1 
ATOM   3533  C  C     . GLU   A  1  482  ? -29.215 63.973  68.779  1.00 45.14 ? 480  GLU   A C     1 
ATOM   3534  O  O     . GLU   A  1  482  ? -28.889 63.841  69.965  1.00 46.08 ? 480  GLU   A O     1 
ATOM   3535  C  CB    . GLU   A  1  482  ? -28.153 65.692  67.300  1.00 46.23 ? 480  GLU   A CB    1 
ATOM   3536  N  N     . THR   A  1  483  ? -30.485 63.886  68.375  1.00 41.06 ? 481  THR   A N     1 
ATOM   3537  C  CA    . THR   A  1  483  ? -31.565 63.724  69.342  1.00 44.68 ? 481  THR   A CA    1 
ATOM   3538  C  C     . THR   A  1  483  ? -31.576 62.321  69.942  1.00 40.89 ? 481  THR   A C     1 
ATOM   3539  O  O     . THR   A  1  483  ? -31.855 62.154  71.134  1.00 41.37 ? 481  THR   A O     1 
ATOM   3540  C  CB    . THR   A  1  483  ? -32.905 64.047  68.681  1.00 37.02 ? 481  THR   A CB    1 
ATOM   3541  N  N     . LEU   A  1  484  ? -31.273 61.302  69.133  1.00 38.47 ? 482  LEU   A N     1 
ATOM   3542  C  CA    . LEU   A  1  484  ? -31.347 59.923  69.609  1.00 37.10 ? 482  LEU   A CA    1 
ATOM   3543  C  C     . LEU   A  1  484  ? -30.307 59.641  70.689  1.00 39.04 ? 482  LEU   A C     1 
ATOM   3544  O  O     . LEU   A  1  484  ? -30.616 59.003  71.703  1.00 41.04 ? 482  LEU   A O     1 
ATOM   3545  C  CB    . LEU   A  1  484  ? -31.180 58.957  68.438  1.00 42.82 ? 482  LEU   A CB    1 
ATOM   3546  N  N     . LEU   A  1  485  ? -29.072 60.104  70.494  1.00 40.79 ? 483  LEU   A N     1 
ATOM   3547  C  CA    . LEU   A  1  485  ? -27.996 59.760  71.418  1.00 38.89 ? 483  LEU   A CA    1 
ATOM   3548  C  C     . LEU   A  1  485  ? -28.174 60.392  72.793  1.00 40.54 ? 483  LEU   A C     1 
ATOM   3549  O  O     . LEU   A  1  485  ? -27.547 59.931  73.754  1.00 39.34 ? 483  LEU   A O     1 
ATOM   3550  C  CB    . LEU   A  1  485  ? -26.644 60.163  70.824  1.00 36.67 ? 483  LEU   A CB    1 
ATOM   3551  C  CG    . LEU   A  1  485  ? -26.177 59.353  69.612  1.00 38.68 ? 483  LEU   A CG    1 
ATOM   3552  C  CD1   . LEU   A  1  485  ? -24.998 60.027  68.936  1.00 39.59 ? 483  LEU   A CD1   1 
ATOM   3553  C  CD2   . LEU   A  1  485  ? -25.824 57.930  70.017  1.00 35.62 ? 483  LEU   A CD2   1 
ATOM   3554  N  N     . ALA   A  1  486  ? -29.024 61.418  72.907  1.00 42.00 ? 484  ALA   A N     1 
ATOM   3555  C  CA    . ALA   A  1  486  ? -29.117 62.190  74.145  1.00 40.23 ? 484  ALA   A CA    1 
ATOM   3556  C  C     . ALA   A  1  486  ? -29.483 61.311  75.337  1.00 40.88 ? 484  ALA   A C     1 
ATOM   3557  O  O     . ALA   A  1  486  ? -28.822 61.359  76.382  1.00 41.71 ? 484  ALA   A O     1 
ATOM   3558  C  CB    . ALA   A  1  486  ? -30.118 63.334  73.976  1.00 40.10 ? 484  ALA   A CB    1 
ATOM   3559  N  N     . TYR   A  1  487  ? -30.538 60.501  75.204  1.00 41.75 ? 485  TYR   A N     1 
ATOM   3560  C  CA    . TYR   A  1  487  ? -30.990 59.628  76.286  1.00 37.35 ? 485  TYR   A CA    1 
ATOM   3561  C  C     . TYR   A  1  487  ? -30.936 58.150  75.907  1.00 39.29 ? 485  TYR   A C     1 
ATOM   3562  O  O     . TYR   A  1  487  ? -31.664 57.337  76.485  1.00 34.86 ? 485  TYR   A O     1 
ATOM   3563  C  CB    . TYR   A  1  487  ? -32.391 60.020  76.763  1.00 38.24 ? 485  TYR   A CB    1 
ATOM   3564  N  N     . LEU   A  1  488  ? -30.080 57.779  74.949  1.00 39.47 ? 486  LEU   A N     1 
ATOM   3565  C  CA    . LEU   A  1  488  ? -30.002 56.381  74.535  1.00 38.00 ? 486  LEU   A CA    1 
ATOM   3566  C  C     . LEU   A  1  488  ? -29.443 55.495  75.642  1.00 36.87 ? 486  LEU   A C     1 
ATOM   3567  O  O     . LEU   A  1  488  ? -29.787 54.306  75.722  1.00 29.94 ? 486  LEU   A O     1 
ATOM   3568  C  CB    . LEU   A  1  488  ? -29.157 56.254  73.267  1.00 37.80 ? 486  LEU   A CB    1 
ATOM   3569  C  CG    . LEU   A  1  488  ? -29.120 54.862  72.633  1.00 41.10 ? 486  LEU   A CG    1 
ATOM   3570  C  CD1   . LEU   A  1  488  ? -30.538 54.356  72.428  1.00 39.53 ? 486  LEU   A CD1   1 
ATOM   3571  C  CD2   . LEU   A  1  488  ? -28.360 54.880  71.317  1.00 33.88 ? 486  LEU   A CD2   1 
ATOM   3572  N  N     . VAL   A  1  489  ? -28.577 56.049  76.494  1.00 38.48 ? 487  VAL   A N     1 
ATOM   3573  C  CA    . VAL   A  1  489  ? -28.037 55.278  77.611  1.00 34.86 ? 487  VAL   A CA    1 
ATOM   3574  C  C     . VAL   A  1  489  ? -29.166 54.755  78.489  1.00 37.65 ? 487  VAL   A C     1 
ATOM   3575  O  O     . VAL   A  1  489  ? -29.215 53.566  78.822  1.00 37.28 ? 487  VAL   A O     1 
ATOM   3576  C  CB    . VAL   A  1  489  ? -27.025 56.114  78.411  1.00 36.94 ? 487  VAL   A CB    1 
ATOM   3577  C  CG1   . VAL   A  1  489  ? -26.739 55.447  79.745  1.00 37.96 ? 487  VAL   A CG1   1 
ATOM   3578  C  CG2   . VAL   A  1  489  ? -25.736 56.289  77.613  1.00 34.80 ? 487  VAL   A CG2   1 
ATOM   3579  N  N     . ARG   A  1  490  ? -30.090 55.637  78.880  1.00 37.27 ? 488  ARG   A N     1 
ATOM   3580  C  CA    . ARG   A  1  490  ? -31.226 55.203  79.690  1.00 39.03 ? 488  ARG   A CA    1 
ATOM   3581  C  C     . ARG   A  1  490  ? -32.038 54.134  78.966  1.00 39.52 ? 488  ARG   A C     1 
ATOM   3582  O  O     . ARG   A  1  490  ? -32.443 53.133  79.571  1.00 39.26 ? 488  ARG   A O     1 
ATOM   3583  C  CB    . ARG   A  1  490  ? -32.103 56.406  80.048  1.00 40.80 ? 488  ARG   A CB    1 
ATOM   3584  C  CG    . ARG   A  1  490  ? -33.314 56.072  80.918  1.00 35.48 ? 488  ARG   A CG    1 
ATOM   3585  C  CD    . ARG   A  1  490  ? -34.260 57.267  81.038  1.00 36.25 ? 488  ARG   A CD    1 
ATOM   3586  N  NE    . ARG   A  1  490  ? -34.931 57.573  79.776  1.00 37.98 ? 488  ARG   A NE    1 
ATOM   3587  C  CZ    . ARG   A  1  490  ? -35.343 58.785  79.427  1.00 36.00 ? 488  ARG   A CZ    1 
ATOM   3588  N  NH1   . ARG   A  1  490  ? -35.130 59.835  80.202  1.00 36.29 ? 488  ARG   A NH1   1 
ATOM   3589  N  NH2   . ARG   A  1  490  ? -35.975 58.948  78.267  1.00 32.59 ? 488  ARG   A NH2   1 
ATOM   3590  N  N     . ARG   A  1  491  ? -32.257 54.316  77.660  1.00 33.48 ? 489  ARG   A N     1 
ATOM   3591  C  CA    . ARG   A  1  491  ? -33.112 53.407  76.908  1.00 38.51 ? 489  ARG   A CA    1 
ATOM   3592  C  C     . ARG   A  1  491  ? -32.494 52.024  76.794  1.00 45.58 ? 489  ARG   A C     1 
ATOM   3593  O  O     . ARG   A  1  491  ? -33.221 51.031  76.693  1.00 42.16 ? 489  ARG   A O     1 
ATOM   3594  C  CB    . ARG   A  1  491  ? -33.382 53.979  75.516  1.00 42.01 ? 489  ARG   A CB    1 
ATOM   3595  N  N     . LEU   A  1  492  ? -31.160 51.940  76.818  1.00 43.29 ? 490  LEU   A N     1 
ATOM   3596  C  CA    . LEU   A  1  492  ? -30.487 50.656  76.652  1.00 44.56 ? 490  LEU   A CA    1 
ATOM   3597  C  C     . LEU   A  1  492  ? -30.453 49.855  77.952  1.00 44.55 ? 490  LEU   A C     1 
ATOM   3598  O  O     . LEU   A  1  492  ? -30.549 48.621  77.926  1.00 38.01 ? 490  LEU   A O     1 
ATOM   3599  C  CB    . LEU   A  1  492  ? -29.078 50.872  76.100  1.00 41.98 ? 490  LEU   A CB    1 
ATOM   3600  C  CG    . LEU   A  1  492  ? -28.984 51.403  74.667  1.00 44.27 ? 490  LEU   A CG    1 
ATOM   3601  C  CD1   . LEU   A  1  492  ? -27.589 51.943  74.376  1.00 42.19 ? 490  LEU   A CD1   1 
ATOM   3602  C  CD2   . LEU   A  1  492  ? -29.353 50.309  73.678  1.00 46.42 ? 490  LEU   A CD2   1 
ATOM   3603  N  N     . LEU   A  1  493  ? -30.311 50.526  79.092  1.00 39.73 ? 491  LEU   A N     1 
ATOM   3604  C  CA    . LEU   A  1  493  ? -30.379 49.832  80.372  1.00 37.41 ? 491  LEU   A CA    1 
ATOM   3605  C  C     . LEU   A  1  493  ? -31.774 49.241  80.573  1.00 40.92 ? 491  LEU   A C     1 
ATOM   3606  O  O     . LEU   A  1  493  ? -31.917 48.112  81.043  1.00 46.57 ? 491  LEU   A O     1 
ATOM   3607  C  CB    . LEU   A  1  493  ? -30.048 50.774  81.530  1.00 43.36 ? 491  LEU   A CB    1 
ATOM   3608  C  CG    . LEU   A  1  493  ? -28.715 51.512  81.467  1.00 44.22 ? 491  LEU   A CG    1 
ATOM   3609  C  CD1   . LEU   A  1  493  ? -28.373 52.127  82.823  1.00 40.00 ? 491  LEU   A CD1   1 
ATOM   3610  C  CD2   . LEU   A  1  493  ? -27.627 50.570  80.997  1.00 44.00 ? 491  LEU   A CD2   1 
ATOM   3611  N  N     . GLY   A  1  496  ? -30.885 46.295  79.341  1.00 44.19 ? 494  GLY   A N     1 
ATOM   3612  C  CA    . GLY   A  1  496  ? -29.557 45.740  79.134  1.00 44.09 ? 494  GLY   A CA    1 
ATOM   3613  C  C     . GLY   A  1  496  ? -28.770 45.513  80.414  1.00 47.30 ? 494  GLY   A C     1 
ATOM   3614  O  O     . GLY   A  1  496  ? -27.604 45.114  80.369  1.00 45.87 ? 494  GLY   A O     1 
ATOM   3615  N  N     . ALA   A  1  497  ? -29.402 45.780  81.556  1.00 45.65 ? 495  ALA   A N     1 
ATOM   3616  C  CA    . ALA   A  1  497  ? -28.808 45.490  82.852  1.00 41.44 ? 495  ALA   A CA    1 
ATOM   3617  C  C     . ALA   A  1  497  ? -28.869 43.992  83.127  1.00 35.91 ? 495  ALA   A C     1 
ATOM   3618  O  O     . ALA   A  1  497  ? -29.661 43.258  82.526  1.00 36.42 ? 495  ALA   A O     1 
ATOM   3619  C  CB    . ALA   A  1  497  ? -29.551 46.242  83.960  1.00 34.68 ? 495  ALA   A CB    1 
ATOM   3620  N  N     . ASN   A  1  498  ? -28.030 43.538  84.065  1.00 36.63 ? 496  ASN   A N     1 
ATOM   3621  C  CA    . ASN   A  1  498  ? -27.940 42.102  84.337  1.00 36.08 ? 496  ASN   A CA    1 
ATOM   3622  C  C     . ASN   A  1  498  ? -29.293 41.499  84.699  1.00 34.61 ? 496  ASN   A C     1 
ATOM   3623  O  O     . ASN   A  1  498  ? -29.536 40.316  84.431  1.00 37.99 ? 496  ASN   A O     1 
ATOM   3624  C  CB    . ASN   A  1  498  ? -26.918 41.825  85.440  1.00 39.53 ? 496  ASN   A CB    1 
ATOM   3625  N  N     . SER   A  1  499  ? -30.182 42.287  85.301  1.00 36.72 ? 497  SER   A N     1 
ATOM   3626  C  CA    . SER   A  1  499  ? -31.505 41.816  85.685  1.00 33.65 ? 497  SER   A CA    1 
ATOM   3627  C  C     . SER   A  1  499  ? -32.539 41.932  84.571  1.00 30.03 ? 497  SER   A C     1 
ATOM   3628  O  O     . SER   A  1  499  ? -33.643 41.399  84.722  1.00 30.51 ? 497  SER   A O     1 
ATOM   3629  C  CB    . SER   A  1  499  ? -31.999 42.585  86.919  1.00 35.02 ? 497  SER   A CB    1 
ATOM   3630  O  OG    . SER   A  1  499  ? -31.865 43.982  86.725  1.00 40.37 ? 497  SER   A OG    1 
ATOM   3631  N  N     . SER   A  1  500  ? -32.210 42.604  83.467  1.00 27.40 ? 498  SER   A N     1 
ATOM   3632  C  CA    . SER   A  1  500  ? -33.166 42.809  82.386  1.00 26.56 ? 498  SER   A CA    1 
ATOM   3633  C  C     . SER   A  1  500  ? -33.414 41.524  81.609  1.00 31.26 ? 498  SER   A C     1 
ATOM   3634  O  O     . SER   A  1  500  ? -32.483 40.775  81.298  1.00 29.89 ? 498  SER   A O     1 
ATOM   3635  C  CB    . SER   A  1  500  ? -32.646 43.869  81.420  1.00 33.00 ? 498  SER   A CB    1 
ATOM   3636  O  OG    . SER   A  1  500  ? -32.611 45.138  82.037  1.00 36.98 ? 498  SER   A OG    1 
ATOM   3637  N  N     . PHE   A  1  501  ? -34.685 41.294  81.264  1.00 26.08 ? 499  PHE   A N     1 
ATOM   3638  C  CA    . PHE   A  1  501  ? -35.046 40.129  80.463  1.00 27.13 ? 499  PHE   A CA    1 
ATOM   3639  C  C     . PHE   A  1  501  ? -34.274 40.083  79.151  1.00 31.37 ? 499  PHE   A C     1 
ATOM   3640  O  O     . PHE   A  1  501  ? -33.840 39.010  78.719  1.00 32.75 ? 499  PHE   A O     1 
ATOM   3641  C  CB    . PHE   A  1  501  ? -36.540 40.137  80.153  1.00 25.82 ? 499  PHE   A CB    1 
ATOM   3642  C  CG    . PHE   A  1  501  ? -36.970 39.000  79.277  1.00 25.93 ? 499  PHE   A CG    1 
ATOM   3643  C  CD1   . PHE   A  1  501  ? -37.304 37.786  79.832  1.00 27.15 ? 499  PHE   A CD1   1 
ATOM   3644  C  CD2   . PHE   A  1  501  ? -37.021 39.139  77.897  1.00 31.30 ? 499  PHE   A CD2   1 
ATOM   3645  C  CE1   . PHE   A  1  501  ? -37.696 36.729  79.037  1.00 28.13 ? 499  PHE   A CE1   1 
ATOM   3646  C  CE2   . PHE   A  1  501  ? -37.406 38.079  77.095  1.00 27.36 ? 499  PHE   A CE2   1 
ATOM   3647  C  CZ    . PHE   A  1  501  ? -37.744 36.877  77.668  1.00 28.71 ? 499  PHE   A CZ    1 
ATOM   3648  N  N     . VAL   A  1  502  ? -34.149 41.225  78.473  1.00 31.32 ? 500  VAL   A N     1 
ATOM   3649  C  CA    . VAL   A  1  502  ? -33.504 41.224  77.166  1.00 33.05 ? 500  VAL   A CA    1 
ATOM   3650  C  C     . VAL   A  1  502  ? -32.033 40.871  77.300  1.00 34.88 ? 500  VAL   A C     1 
ATOM   3651  O  O     . VAL   A  1  502  ? -31.462 40.211  76.425  1.00 41.51 ? 500  VAL   A O     1 
ATOM   3652  C  CB    . VAL   A  1  502  ? -33.728 42.560  76.440  1.00 34.38 ? 500  VAL   A CB    1 
ATOM   3653  N  N     . HIS   A  1  503  ? -31.395 41.289  78.391  1.00 32.50 ? 501  HIS   A N     1 
ATOM   3654  C  CA    . HIS   A  1  503  ? -30.036 40.833  78.653  1.00 32.73 ? 501  HIS   A CA    1 
ATOM   3655  C  C     . HIS   A  1  503  ? -30.020 39.343  78.959  1.00 36.41 ? 501  HIS   A C     1 
ATOM   3656  O  O     . HIS   A  1  503  ? -29.161 38.607  78.457  1.00 34.86 ? 501  HIS   A O     1 
ATOM   3657  C  CB    . HIS   A  1  503  ? -29.441 41.630  79.812  1.00 35.54 ? 501  HIS   A CB    1 
ATOM   3658  C  CG    . HIS   A  1  503  ? -28.093 41.151  80.253  1.00 37.71 ? 501  HIS   A CG    1 
ATOM   3659  N  ND1   . HIS   A  1  503  ? -27.922 40.274  81.303  1.00 38.23 ? 501  HIS   A ND1   1 
ATOM   3660  C  CD2   . HIS   A  1  503  ? -26.852 41.427  79.786  1.00 38.14 ? 501  HIS   A CD2   1 
ATOM   3661  C  CE1   . HIS   A  1  503  ? -26.633 40.032  81.467  1.00 38.30 ? 501  HIS   A CE1   1 
ATOM   3662  N  NE2   . HIS   A  1  503  ? -25.962 40.718  80.558  1.00 36.83 ? 501  HIS   A NE2   1 
ATOM   3663  N  N     . ARG   A  1  504  ? -30.982 38.878  79.756  1.00 30.97 ? 502  ARG   A N     1 
ATOM   3664  C  CA    . ARG   A  1  504  ? -30.975 37.491  80.202  1.00 31.90 ? 502  ARG   A CA    1 
ATOM   3665  C  C     . ARG   A  1  504  ? -31.326 36.526  79.078  1.00 35.01 ? 502  ARG   A C     1 
ATOM   3666  O  O     . ARG   A  1  504  ? -30.774 35.420  79.027  1.00 33.09 ? 502  ARG   A O     1 
ATOM   3667  C  CB    . ARG   A  1  504  ? -31.904 37.330  81.404  1.00 33.50 ? 502  ARG   A CB    1 
ATOM   3668  C  CG    . ARG   A  1  504  ? -31.371 38.017  82.657  1.00 34.95 ? 502  ARG   A CG    1 
ATOM   3669  C  CD    . ARG   A  1  504  ? -32.466 38.250  83.682  1.00 32.99 ? 502  ARG   A CD    1 
ATOM   3670  N  NE    . ARG   A  1  504  ? -33.222 37.035  83.955  1.00 34.33 ? 502  ARG   A NE    1 
ATOM   3671  C  CZ    . ARG   A  1  504  ? -32.811 36.057  84.750  1.00 38.13 ? 502  ARG   A CZ    1 
ATOM   3672  N  NH1   . ARG   A  1  504  ? -31.635 36.105  85.353  1.00 40.73 ? 502  ARG   A NH1   1 
ATOM   3673  N  NH2   . ARG   A  1  504  ? -33.598 35.003  84.942  1.00 37.75 ? 502  ARG   A NH2   1 
ATOM   3674  N  N     . ILE   A  1  505  ? -32.223 36.925  78.168  1.00 34.68 ? 503  ILE   A N     1 
ATOM   3675  C  CA    . ILE   A  1  505  ? -32.582 36.065  77.043  1.00 33.60 ? 503  ILE   A CA    1 
ATOM   3676  C  C     . ILE   A  1  505  ? -31.351 35.735  76.208  1.00 36.12 ? 503  ILE   A C     1 
ATOM   3677  O  O     . ILE   A  1  505  ? -31.249 34.640  75.640  1.00 40.78 ? 503  ILE   A O     1 
ATOM   3678  C  CB    . ILE   A  1  505  ? -33.709 36.702  76.200  1.00 34.00 ? 503  ILE   A CB    1 
ATOM   3679  C  CG1   . ILE   A  1  505  ? -34.195 35.749  75.114  1.00 38.09 ? 503  ILE   A CG1   1 
ATOM   3680  C  CG2   . ILE   A  1  505  ? -33.235 37.956  75.521  1.00 39.27 ? 503  ILE   A CG2   1 
ATOM   3681  C  CD1   . ILE   A  1  505  ? -35.150 34.718  75.611  1.00 30.82 ? 503  ILE   A CD1   1 
ATOM   3682  N  N     . ASN   A  1  506  ? -30.392 36.655  76.142  1.00 34.21 ? 504  ASN   A N     1 
ATOM   3683  C  CA    . ASN   A  1  506  ? -29.172 36.450  75.374  1.00 38.85 ? 504  ASN   A CA    1 
ATOM   3684  C  C     . ASN   A  1  506  ? -28.033 35.852  76.188  1.00 39.47 ? 504  ASN   A C     1 
ATOM   3685  O  O     . ASN   A  1  506  ? -26.974 35.567  75.619  1.00 43.14 ? 504  ASN   A O     1 
ATOM   3686  C  CB    . ASN   A  1  506  ? -28.712 37.767  74.748  1.00 41.10 ? 504  ASN   A CB    1 
ATOM   3687  C  CG    . ASN   A  1  506  ? -29.631 38.232  73.645  1.00 43.52 ? 504  ASN   A CG    1 
ATOM   3688  O  OD1   . ASN   A  1  506  ? -30.205 37.421  72.917  1.00 48.88 ? 504  ASN   A OD1   1 
ATOM   3689  N  ND2   . ASN   A  1  506  ? -29.779 39.544  73.513  1.00 50.03 ? 504  ASN   A ND2   1 
ATOM   3690  N  N     . ASP   A  1  507  ? -28.212 35.662  77.488  1.00 36.37 ? 505  ASP   A N     1 
ATOM   3691  C  CA    . ASP   A  1  507  ? -27.166 35.068  78.309  1.00 39.34 ? 505  ASP   A CA    1 
ATOM   3692  C  C     . ASP   A  1  507  ? -27.250 33.551  78.201  1.00 44.00 ? 505  ASP   A C     1 
ATOM   3693  O  O     . ASP   A  1  507  ? -28.263 32.969  78.601  1.00 38.90 ? 505  ASP   A O     1 
ATOM   3694  C  CB    . ASP   A  1  507  ? -27.331 35.493  79.763  1.00 36.48 ? 505  ASP   A CB    1 
ATOM   3695  C  CG    . ASP   A  1  507  ? -26.169 35.044  80.650  1.00 44.32 ? 505  ASP   A CG    1 
ATOM   3696  O  OD1   . ASP   A  1  507  ? -25.591 33.964  80.403  1.00 47.38 ? 505  ASP   A OD1   1 
ATOM   3697  O  OD2   . ASP   A  1  507  ? -25.835 35.771  81.608  1.00 42.31 ? 505  ASP   A OD2   1 
ATOM   3698  N  N     . PRO   A  1  508  ? -26.213 32.876  77.695  1.00 44.88 ? 506  PRO   A N     1 
ATOM   3699  C  CA    . PRO   A  1  508  ? -26.280 31.408  77.589  1.00 48.05 ? 506  PRO   A CA    1 
ATOM   3700  C  C     . PRO   A  1  508  ? -26.404 30.711  78.932  1.00 42.89 ? 506  PRO   A C     1 
ATOM   3701  O  O     . PRO   A  1  508  ? -26.976 29.615  79.003  1.00 48.20 ? 506  PRO   A O     1 
ATOM   3702  C  CB    . PRO   A  1  508  ? -24.961 31.038  76.889  1.00 46.86 ? 506  PRO   A CB    1 
ATOM   3703  C  CG    . PRO   A  1  508  ? -24.415 32.329  76.337  1.00 50.66 ? 506  PRO   A CG    1 
ATOM   3704  C  CD    . PRO   A  1  508  ? -24.925 33.414  77.227  1.00 43.88 ? 506  PRO   A CD    1 
ATOM   3705  N  N     . LYS   A  1  509  ? -25.888 31.315  79.999  1.00 41.74 ? 507  LYS   A N     1 
ATOM   3706  C  CA    . LYS   A  1  509  ? -25.900 30.711  81.324  1.00 42.68 ? 507  LYS   A CA    1 
ATOM   3707  C  C     . LYS   A  1  509  ? -27.258 30.791  82.009  1.00 42.56 ? 507  LYS   A C     1 
ATOM   3708  O  O     . LYS   A  1  509  ? -27.385 30.326  83.147  1.00 44.12 ? 507  LYS   A O     1 
ATOM   3709  C  CB    . LYS   A  1  509  ? -24.837 31.370  82.208  1.00 48.08 ? 507  LYS   A CB    1 
ATOM   3710  N  N     . VAL   A  1  510  ? -28.266 31.369  81.362  1.00 39.18 ? 508  VAL   A N     1 
ATOM   3711  C  CA    . VAL   A  1  510  ? -29.597 31.519  81.938  1.00 36.97 ? 508  VAL   A CA    1 
ATOM   3712  C  C     . VAL   A  1  510  ? -30.522 30.552  81.218  1.00 34.59 ? 508  VAL   A C     1 
ATOM   3713  O  O     . VAL   A  1  510  ? -30.745 30.679  80.009  1.00 39.25 ? 508  VAL   A O     1 
ATOM   3714  C  CB    . VAL   A  1  510  ? -30.103 32.964  81.821  1.00 36.97 ? 508  VAL   A CB    1 
ATOM   3715  C  CG1   . VAL   A  1  510  ? -31.524 33.079  82.368  1.00 34.46 ? 508  VAL   A CG1   1 
ATOM   3716  C  CG2   . VAL   A  1  510  ? -29.159 33.923  82.542  1.00 36.39 ? 508  VAL   A CG2   1 
ATOM   3717  N  N     . SER   A  1  511  ? -31.051 29.581  81.953  1.00 34.53 ? 509  SER   A N     1 
ATOM   3718  C  CA    . SER   A  1  511  ? -31.921 28.592  81.347  1.00 34.23 ? 509  SER   A CA    1 
ATOM   3719  C  C     . SER   A  1  511  ? -33.308 29.177  81.114  1.00 36.16 ? 509  SER   A C     1 
ATOM   3720  O  O     . SER   A  1  511  ? -33.681 30.213  81.677  1.00 35.56 ? 509  SER   A O     1 
ATOM   3721  C  CB    . SER   A  1  511  ? -32.043 27.364  82.245  1.00 38.61 ? 509  SER   A CB    1 
ATOM   3722  O  OG    . SER   A  1  511  ? -32.686 27.700  83.460  1.00 39.47 ? 509  SER   A OG    1 
ATOM   3723  N  N     . ILE   A  1  512  ? -34.070 28.496  80.260  1.00 33.92 ? 510  ILE   A N     1 
ATOM   3724  C  CA    . ILE   A  1  512  ? -35.461 28.877  80.046  1.00 35.20 ? 510  ILE   A CA    1 
ATOM   3725  C  C     . ILE   A  1  512  ? -36.255 28.734  81.337  1.00 38.68 ? 510  ILE   A C     1 
ATOM   3726  O  O     . ILE   A  1  512  ? -37.099 29.578  81.658  1.00 34.30 ? 510  ILE   A O     1 
ATOM   3727  C  CB    . ILE   A  1  512  ? -36.066 28.074  78.882  1.00 35.54 ? 510  ILE   A CB    1 
ATOM   3728  C  CG1   . ILE   A  1  512  ? -35.304 28.387  77.592  1.00 34.54 ? 510  ILE   A CG1   1 
ATOM   3729  C  CG2   . ILE   A  1  512  ? -37.547 28.389  78.716  1.00 36.77 ? 510  ILE   A CG2   1 
ATOM   3730  C  CD1   . ILE   A  1  512  ? -35.731 27.558  76.419  1.00 38.96 ? 510  ILE   A CD1   1 
ATOM   3731  N  N     . ASP   A  1  513  ? -35.982 27.680  82.110  1.00 37.01 ? 511  ASP   A N     1 
ATOM   3732  C  CA    . ASP   A  1  513  ? -36.676 27.506  83.383  1.00 37.46 ? 511  ASP   A CA    1 
ATOM   3733  C  C     . ASP   A  1  513  ? -36.461 28.704  84.300  1.00 38.07 ? 511  ASP   A C     1 
ATOM   3734  O  O     . ASP   A  1  513  ? -37.393 29.143  84.984  1.00 36.15 ? 511  ASP   A O     1 
ATOM   3735  C  CB    . ASP   A  1  513  ? -36.242 26.204  84.054  1.00 42.39 ? 511  ASP   A CB    1 
ATOM   3736  C  CG    . ASP   A  1  513  ? -36.692 24.979  83.283  1.00 47.31 ? 511  ASP   A CG    1 
ATOM   3737  O  OD1   . ASP   A  1  513  ? -37.808 25.001  82.721  1.00 48.52 ? 511  ASP   A OD1   1 
ATOM   3738  O  OD2   . ASP   A  1  513  ? -35.926 23.992  83.233  1.00 57.19 ? 511  ASP   A OD2   1 
ATOM   3739  N  N     . GLU   A  1  514  ? -35.247 29.261  84.311  1.00 35.31 ? 512  GLU   A N     1 
ATOM   3740  C  CA    . GLU   A  1  514  ? -34.999 30.485  85.068  1.00 34.17 ? 512  GLU   A CA    1 
ATOM   3741  C  C     . GLU   A  1  514  ? -35.805 31.652  84.510  1.00 33.84 ? 512  GLU   A C     1 
ATOM   3742  O  O     . GLU   A  1  514  ? -36.320 32.483  85.268  1.00 34.17 ? 512  GLU   A O     1 
ATOM   3743  C  CB    . GLU   A  1  514  ? -33.505 30.812  85.060  1.00 37.26 ? 512  GLU   A CB    1 
ATOM   3744  C  CG    . GLU   A  1  514  ? -32.666 29.923  85.965  1.00 42.94 ? 512  GLU   A CG    1 
ATOM   3745  C  CD    . GLU   A  1  514  ? -31.170 30.064  85.707  1.00 49.21 ? 512  GLU   A CD    1 
ATOM   3746  O  OE1   . GLU   A  1  514  ? -30.763 30.017  84.528  1.00 48.37 ? 512  GLU   A OE1   1 
ATOM   3747  O  OE2   . GLU   A  1  514  ? -30.402 30.223  86.680  1.00 59.29 ? 512  GLU   A OE2   1 
ATOM   3748  N  N     . LEU   A  1  515  ? -35.927 31.730  83.184  1.00 34.76 ? 513  LEU   A N     1 
ATOM   3749  C  CA    . LEU   A  1  515  ? -36.627 32.856  82.573  1.00 31.74 ? 513  LEU   A CA    1 
ATOM   3750  C  C     . LEU   A  1  515  ? -38.133 32.759  82.759  1.00 32.45 ? 513  LEU   A C     1 
ATOM   3751  O  O     . LEU   A  1  515  ? -38.816 33.788  82.777  1.00 30.31 ? 513  LEU   A O     1 
ATOM   3752  C  CB    . LEU   A  1  515  ? -36.287 32.942  81.089  1.00 29.72 ? 513  LEU   A CB    1 
ATOM   3753  C  CG    . LEU   A  1  515  ? -34.862 33.400  80.777  1.00 32.68 ? 513  LEU   A CG    1 
ATOM   3754  C  CD1   . LEU   A  1  515  ? -34.553 33.221  79.300  1.00 32.11 ? 513  LEU   A CD1   1 
ATOM   3755  C  CD2   . LEU   A  1  515  ? -34.663 34.846  81.200  1.00 30.74 ? 513  LEU   A CD2   1 
ATOM   3756  N  N     . ILE   A  1  516  ? -38.669 31.546  82.886  1.00 29.53 ? 514  ILE   A N     1 
ATOM   3757  C  CA    . ILE   A  1  516  ? -40.104 31.360  83.053  1.00 30.18 ? 514  ILE   A CA    1 
ATOM   3758  C  C     . ILE   A  1  516  ? -40.503 31.240  84.519  1.00 33.89 ? 514  ILE   A C     1 
ATOM   3759  O  O     . ILE   A  1  516  ? -41.675 30.970  84.818  1.00 34.22 ? 514  ILE   A O     1 
ATOM   3760  C  CB    . ILE   A  1  516  ? -40.634 30.174  82.225  1.00 31.95 ? 514  ILE   A CB    1 
ATOM   3761  C  CG1   . ILE   A  1  516  ? -40.097 28.859  82.793  1.00 37.13 ? 514  ILE   A CG1   1 
ATOM   3762  C  CG2   . ILE   A  1  516  ? -40.270 30.349  80.763  1.00 34.09 ? 514  ILE   A CG2   1 
ATOM   3763  C  CD1   . ILE   A  1  516  ? -40.643 27.622  82.105  1.00 37.01 ? 514  ILE   A CD1   1 
ATOM   3764  N  N     . ALA   A  1  517  ? -39.557 31.415  85.438  1.00 29.87 ? 515  ALA   A N     1 
ATOM   3765  C  CA    . ALA   A  1  517  ? -39.884 31.403  86.856  1.00 30.33 ? 515  ALA   A CA    1 
ATOM   3766  C  C     . ALA   A  1  517  ? -40.962 32.438  87.141  1.00 33.66 ? 515  ALA   A C     1 
ATOM   3767  O  O     . ALA   A  1  517  ? -40.932 33.550  86.612  1.00 29.95 ? 515  ALA   A O     1 
ATOM   3768  C  CB    . ALA   A  1  517  ? -38.638 31.718  87.686  1.00 35.36 ? 515  ALA   A CB    1 
ATOM   3769  N  N     . ASP   A  1  518  ? -41.931 32.052  87.961  1.00 31.92 ? 516  ASP   A N     1 
ATOM   3770  C  CA    . ASP   A  1  518  ? -43.074 32.896  88.269  1.00 31.74 ? 516  ASP   A CA    1 
ATOM   3771  C  C     . ASP   A  1  518  ? -42.713 33.836  89.409  1.00 28.09 ? 516  ASP   A C     1 
ATOM   3772  O  O     . ASP   A  1  518  ? -42.583 33.396  90.557  1.00 30.15 ? 516  ASP   A O     1 
ATOM   3773  C  CB    . ASP   A  1  518  ? -44.252 32.018  88.676  1.00 33.78 ? 516  ASP   A CB    1 
ATOM   3774  C  CG    . ASP   A  1  518  ? -45.514 32.812  88.922  1.00 32.17 ? 516  ASP   A CG    1 
ATOM   3775  O  OD1   . ASP   A  1  518  ? -45.492 34.058  88.813  1.00 30.67 ? 516  ASP   A OD1   1 
ATOM   3776  O  OD2   . ASP   A  1  518  ? -46.544 32.175  89.212  1.00 38.77 ? 516  ASP   A OD2   1 
ATOM   3777  N  N     . PRO   A  1  519  ? -42.566 35.135  89.143  1.00 30.13 ? 517  PRO   A N     1 
ATOM   3778  C  CA    . PRO   A  1  519  ? -42.174 36.050  90.223  1.00 29.03 ? 517  PRO   A CA    1 
ATOM   3779  C  C     . PRO   A  1  519  ? -43.163 36.070  91.373  1.00 25.57 ? 517  PRO   A C     1 
ATOM   3780  O  O     . PRO   A  1  519  ? -42.759 36.283  92.523  1.00 27.82 ? 517  PRO   A O     1 
ATOM   3781  C  CB    . PRO   A  1  519  ? -42.078 37.411  89.516  1.00 28.60 ? 517  PRO   A CB    1 
ATOM   3782  C  CG    . PRO   A  1  519  ? -42.927 37.275  88.308  1.00 31.60 ? 517  PRO   A CG    1 
ATOM   3783  C  CD    . PRO   A  1  519  ? -42.826 35.843  87.879  1.00 26.95 ? 517  PRO   A CD    1 
ATOM   3784  N  N     . VAL   A  1  520  ? -44.446 35.838  91.091  1.00 27.95 ? 518  VAL   A N     1 
ATOM   3785  C  CA    . VAL   A  1  520  ? -45.463 35.861  92.137  1.00 26.36 ? 518  VAL   A CA    1 
ATOM   3786  C  C     . VAL   A  1  520  ? -45.210 34.749  93.145  1.00 30.42 ? 518  VAL   A C     1 
ATOM   3787  O  O     . VAL   A  1  520  ? -45.210 34.975  94.360  1.00 30.69 ? 518  VAL   A O     1 
ATOM   3788  C  CB    . VAL   A  1  520  ? -46.865 35.748  91.517  1.00 28.57 ? 518  VAL   A CB    1 
ATOM   3789  C  CG1   . VAL   A  1  520  ? -47.931 35.755  92.607  1.00 30.72 ? 518  VAL   A CG1   1 
ATOM   3790  C  CG2   . VAL   A  1  520  ? -47.097 36.877  90.526  1.00 27.43 ? 518  VAL   A CG2   1 
ATOM   3791  N  N     . GLU   A  1  521  ? -44.983 33.532  92.652  1.00 32.78 ? 519  GLU   A N     1 
ATOM   3792  C  CA    . GLU   A  1  521  ? -44.741 32.414  93.558  1.00 30.99 ? 519  GLU   A CA    1 
ATOM   3793  C  C     . GLU   A  1  521  ? -43.376 32.505  94.227  1.00 32.77 ? 519  GLU   A C     1 
ATOM   3794  O  O     . GLU   A  1  521  ? -43.223 32.064  95.372  1.00 37.35 ? 519  GLU   A O     1 
ATOM   3795  C  CB    . GLU   A  1  521  ? -44.921 31.088  92.822  1.00 36.56 ? 519  GLU   A CB    1 
ATOM   3796  C  CG    . GLU   A  1  521  ? -46.353 30.866  92.367  1.00 38.94 ? 519  GLU   A CG    1 
ATOM   3797  C  CD    . GLU   A  1  521  ? -47.340 31.036  93.505  1.00 44.41 ? 519  GLU   A CD    1 
ATOM   3798  O  OE1   . GLU   A  1  521  ? -47.038 30.572  94.627  1.00 46.49 ? 519  GLU   A OE1   1 
ATOM   3799  O  OE2   . GLU   A  1  521  ? -48.414 31.636  93.285  1.00 45.07 ? 519  GLU   A OE2   1 
ATOM   3800  N  N     . VAL   A  1  522  ? -42.378 33.074  93.548  1.00 29.39 ? 520  VAL   A N     1 
ATOM   3801  C  CA    . VAL   A  1  522  ? -41.066 33.228  94.169  1.00 28.69 ? 520  VAL   A CA    1 
ATOM   3802  C  C     . VAL   A  1  522  ? -41.138 34.210  95.333  1.00 35.61 ? 520  VAL   A C     1 
ATOM   3803  O  O     . VAL   A  1  522  ? -40.610 33.952  96.420  1.00 32.92 ? 520  VAL   A O     1 
ATOM   3804  C  CB    . VAL   A  1  522  ? -40.005 33.629  93.128  1.00 33.14 ? 520  VAL   A CB    1 
ATOM   3805  C  CG1   . VAL   A  1  522  ? -38.670 33.894  93.809  1.00 34.56 ? 520  VAL   A CG1   1 
ATOM   3806  C  CG2   . VAL   A  1  522  ? -39.859 32.546  92.064  1.00 32.60 ? 520  VAL   A CG2   1 
ATOM   3807  N  N     . VAL   A  1  523  ? -41.800 35.349  95.125  1.00 30.31 ? 521  VAL   A N     1 
ATOM   3808  C  CA    . VAL   A  1  523  ? -41.931 36.335  96.194  1.00 28.36 ? 521  VAL   A CA    1 
ATOM   3809  C  C     . VAL   A  1  523  ? -42.756 35.776  97.344  1.00 31.87 ? 521  VAL   A C     1 
ATOM   3810  O  O     . VAL   A  1  523  ? -42.420 35.971  98.518  1.00 32.54 ? 521  VAL   A O     1 
ATOM   3811  C  CB    . VAL   A  1  523  ? -42.515 37.651  95.646  1.00 28.21 ? 521  VAL   A CB    1 
ATOM   3812  C  CG1   . VAL   A  1  523  ? -42.926 38.565  96.789  1.00 29.05 ? 521  VAL   A CG1   1 
ATOM   3813  C  CG2   . VAL   A  1  523  ? -41.495 38.343  94.766  1.00 27.68 ? 521  VAL   A CG2   1 
ATOM   3814  N  N     . ARG   A  1  524  ? -43.849 35.077  97.026  1.00 32.09 ? 522  ARG   A N     1 
ATOM   3815  C  CA    . ARG   A  1  524  ? -44.723 34.556  98.071  1.00 33.00 ? 522  ARG   A CA    1 
ATOM   3816  C  C     . ARG   A  1  524  ? -43.982 33.616  99.011  1.00 38.76 ? 522  ARG   A C     1 
ATOM   3817  O  O     . ARG   A  1  524  ? -44.308 33.546  100.202 1.00 41.76 ? 522  ARG   A O     1 
ATOM   3818  C  CB    . ARG   A  1  524  ? -45.911 33.827  97.451  1.00 36.17 ? 522  ARG   A CB    1 
ATOM   3819  C  CG    . ARG   A  1  524  ? -46.808 33.169  98.492  1.00 39.01 ? 522  ARG   A CG    1 
ATOM   3820  C  CD    . ARG   A  1  524  ? -47.658 32.082  97.882  1.00 43.02 ? 522  ARG   A CD    1 
ATOM   3821  N  NE    . ARG   A  1  524  ? -48.289 32.535  96.651  1.00 40.66 ? 522  ARG   A NE    1 
ATOM   3822  C  CZ    . ARG   A  1  524  ? -49.351 33.325  96.602  1.00 34.27 ? 522  ARG   A CZ    1 
ATOM   3823  N  NH1   . ARG   A  1  524  ? -49.912 33.798  97.704  1.00 41.73 ? 522  ARG   A NH1   1 
ATOM   3824  N  NH2   . ARG   A  1  524  ? -49.860 33.652  95.419  1.00 36.70 ? 522  ARG   A NH2   1 
ATOM   3825  N  N     . ALA   A  1  525  ? -42.977 32.906  98.504  1.00 35.73 ? 523  ALA   A N     1 
ATOM   3826  C  CA    . ALA   A  1  525  ? -42.255 31.905  99.277  1.00 39.69 ? 523  ALA   A CA    1 
ATOM   3827  C  C     . ALA   A  1  525  ? -41.018 32.455  99.974  1.00 40.47 ? 523  ALA   A C     1 
ATOM   3828  O  O     . ALA   A  1  525  ? -40.354 31.708  100.700 1.00 42.74 ? 523  ALA   A O     1 
ATOM   3829  C  CB    . ALA   A  1  525  ? -41.872 30.724  98.381  1.00 36.95 ? 523  ALA   A CB    1 
ATOM   3830  N  N     . MET   A  1  526  ? -40.688 33.728  99.776  1.00 38.68 ? 524  MET   A N     1 
ATOM   3831  C  CA    A MET   A  1  526  ? -39.542 34.322  100.447 0.43 39.23 ? 524  MET   A CA    1 
ATOM   3832  C  CA    B MET   A  1  526  ? -39.535 34.298  100.448 0.57 39.21 ? 524  MET   A CA    1 
ATOM   3833  C  C     . MET   A  1  526  ? -39.783 34.361  101.956 1.00 40.42 ? 524  MET   A C     1 
ATOM   3834  O  O     . MET   A  1  526  ? -40.930 34.422  102.405 1.00 37.67 ? 524  MET   A O     1 
ATOM   3835  C  CB    A MET   A  1  526  ? -39.322 35.745  99.936  0.43 41.16 ? 524  MET   A CB    1 
ATOM   3836  C  CB    B MET   A  1  526  ? -39.242 35.692  99.896  0.57 41.18 ? 524  MET   A CB    1 
ATOM   3837  C  CG    A MET   A  1  526  ? -38.845 35.828  98.499  0.43 39.25 ? 524  MET   A CG    1 
ATOM   3838  C  CG    B MET   A  1  526  ? -38.310 35.686  98.689  0.57 39.39 ? 524  MET   A CG    1 
ATOM   3839  S  SD    A MET   A  1  526  ? -37.204 35.120  98.281  0.43 44.96 ? 524  MET   A SD    1 
ATOM   3840  S  SD    B MET   A  1  526  ? -38.391 37.195  97.706  0.57 40.08 ? 524  MET   A SD    1 
ATOM   3841  C  CE    A MET   A  1  526  ? -36.231 36.154  99.376  0.43 36.88 ? 524  MET   A CE    1 
ATOM   3842  C  CE    B MET   A  1  526  ? -36.753 37.227  96.984  0.57 37.59 ? 524  MET   A CE    1 
ATOM   3843  N  N     . PRO   A  1  527  ? -38.715 34.332  102.767 1.00 44.18 ? 525  PRO   A N     1 
ATOM   3844  C  CA    . PRO   A  1  527  ? -38.924 34.338  104.228 1.00 44.50 ? 525  PRO   A CA    1 
ATOM   3845  C  C     . PRO   A  1  527  ? -39.594 35.601  104.736 1.00 42.05 ? 525  PRO   A C     1 
ATOM   3846  O  O     . PRO   A  1  527  ? -40.512 35.528  105.564 1.00 37.40 ? 525  PRO   A O     1 
ATOM   3847  C  CB    . PRO   A  1  527  ? -37.505 34.157  104.787 1.00 44.26 ? 525  PRO   A CB    1 
ATOM   3848  C  CG    . PRO   A  1  527  ? -36.610 34.660  103.706 1.00 44.10 ? 525  PRO   A CG    1 
ATOM   3849  C  CD    . PRO   A  1  527  ? -37.284 34.284  102.418 1.00 43.64 ? 525  PRO   A CD    1 
ATOM   3850  N  N     . VAL   A  1  528  ? -39.166 36.763  104.257 1.00 42.52 ? 526  VAL   A N     1 
ATOM   3851  C  CA    . VAL   A  1  528  ? -39.841 38.025  104.524 1.00 33.45 ? 526  VAL   A CA    1 
ATOM   3852  C  C     . VAL   A  1  528  ? -40.339 38.545  103.185 1.00 35.34 ? 526  VAL   A C     1 
ATOM   3853  O  O     . VAL   A  1  528  ? -39.536 38.947  102.331 1.00 37.32 ? 526  VAL   A O     1 
ATOM   3854  C  CB    . VAL   A  1  528  ? -38.915 39.045  105.196 1.00 36.26 ? 526  VAL   A CB    1 
ATOM   3855  C  CG1   . VAL   A  1  528  ? -39.639 40.372  105.369 1.00 38.64 ? 526  VAL   A CG1   1 
ATOM   3856  C  CG2   . VAL   A  1  528  ? -38.422 38.514  106.533 1.00 40.23 ? 526  VAL   A CG2   1 
ATOM   3857  N  N     . VAL   A  1  529  ? -41.654 38.533  102.991 1.00 32.96 ? 527  VAL   A N     1 
ATOM   3858  C  CA    . VAL   A  1  529  ? -42.220 38.993  101.729 1.00 32.43 ? 527  VAL   A CA    1 
ATOM   3859  C  C     . VAL   A  1  529  ? -41.958 40.488  101.582 1.00 34.01 ? 527  VAL   A C     1 
ATOM   3860  O  O     . VAL   A  1  529  ? -42.316 41.286  102.457 1.00 33.74 ? 527  VAL   A O     1 
ATOM   3861  C  CB    . VAL   A  1  529  ? -43.717 38.669  101.642 1.00 33.47 ? 527  VAL   A CB    1 
ATOM   3862  C  CG1   . VAL   A  1  529  ? -44.302 39.261  100.372 1.00 31.13 ? 527  VAL   A CG1   1 
ATOM   3863  C  CG2   . VAL   A  1  529  ? -43.933 37.161  101.672 1.00 37.24 ? 527  VAL   A CG2   1 
ATOM   3864  N  N     . GLY   A  1  530  ? -41.306 40.869  100.484 1.00 29.49 ? 528  GLY   A N     1 
ATOM   3865  C  CA    . GLY   A  1  530  ? -41.101 42.271  100.181 1.00 28.58 ? 528  GLY   A CA    1 
ATOM   3866  C  C     . GLY   A  1  530  ? -39.921 42.939  100.849 1.00 26.11 ? 528  GLY   A C     1 
ATOM   3867  O  O     . GLY   A  1  530  ? -39.874 44.169  100.890 1.00 28.61 ? 528  GLY   A O     1 
ATOM   3868  N  N     . ALA   A  1  531  ? -38.964 42.177  101.382 1.00 27.52 ? 529  ALA   A N     1 
ATOM   3869  C  CA    . ALA   A  1  531  ? -37.796 42.795  102.001 1.00 26.65 ? 529  ALA   A CA    1 
ATOM   3870  C  C     . ALA   A  1  531  ? -37.033 43.654  100.994 1.00 25.15 ? 529  ALA   A C     1 
ATOM   3871  O  O     . ALA   A  1  531  ? -36.917 43.304  99.815  1.00 29.29 ? 529  ALA   A O     1 
ATOM   3872  C  CB    . ALA   A  1  531  ? -36.860 41.723  102.564 1.00 29.48 ? 529  ALA   A CB    1 
ATOM   3873  N  N     . LYS   A  1  532  ? -36.522 44.793  101.472 1.00 26.53 ? 530  LYS   A N     1 
ATOM   3874  C  CA    . LYS   A  1  532  ? -35.642 45.649  100.682 1.00 26.52 ? 530  LYS   A CA    1 
ATOM   3875  C  C     . LYS   A  1  532  ? -34.451 44.846  100.175 1.00 28.07 ? 530  LYS   A C     1 
ATOM   3876  O  O     . LYS   A  1  532  ? -34.017 43.878  100.801 1.00 25.53 ? 530  LYS   A O     1 
ATOM   3877  C  CB    . LYS   A  1  532  ? -35.128 46.794  101.568 1.00 28.76 ? 530  LYS   A CB    1 
ATOM   3878  C  CG    . LYS   A  1  532  ? -34.086 47.717  100.920 1.00 34.08 ? 530  LYS   A CG    1 
ATOM   3879  C  CD    . LYS   A  1  532  ? -33.605 48.796  101.881 1.00 30.12 ? 530  LYS   A CD    1 
ATOM   3880  C  CE    . LYS   A  1  532  ? -32.788 48.207  103.030 1.00 31.51 ? 530  LYS   A CE    1 
ATOM   3881  N  NZ    . LYS   A  1  532  ? -31.550 47.527  102.550 1.00 29.04 ? 530  LYS   A NZ    1 
ATOM   3882  N  N     . HIS   A  1  533  ? -33.934 45.241  99.015  1.00 24.97 ? 531  HIS   A N     1 
ATOM   3883  C  CA    . HIS   A  1  533  ? -32.695 44.661  98.524  1.00 22.96 ? 531  HIS   A CA    1 
ATOM   3884  C  C     . HIS   A  1  533  ? -31.590 44.837  99.558  1.00 26.44 ? 531  HIS   A C     1 
ATOM   3885  O  O     . HIS   A  1  533  ? -31.398 45.927  100.105 1.00 25.40 ? 531  HIS   A O     1 
ATOM   3886  C  CB    . HIS   A  1  533  ? -32.289 45.350  97.232  1.00 25.03 ? 531  HIS   A CB    1 
ATOM   3887  C  CG    . HIS   A  1  533  ? -31.270 44.586  96.453  1.00 27.22 ? 531  HIS   A CG    1 
ATOM   3888  N  ND1   . HIS   A  1  533  ? -29.969 44.436  96.880  1.00 27.95 ? 531  HIS   A ND1   1 
ATOM   3889  C  CD2   . HIS   A  1  533  ? -31.366 43.907  95.286  1.00 31.85 ? 531  HIS   A CD2   1 
ATOM   3890  C  CE1   . HIS   A  1  533  ? -29.301 43.710  96.002  1.00 35.98 ? 531  HIS   A CE1   1 
ATOM   3891  N  NE2   . HIS   A  1  533  ? -30.127 43.372  95.027  1.00 37.04 ? 531  HIS   A NE2   1 
ATOM   3892  N  N     . ASP   A  1  534  ? -30.860 43.751  99.820  1.00 26.11 ? 532  ASP   A N     1 
ATOM   3893  C  CA    . ASP   A  1  534  ? -29.822 43.778  100.843 1.00 28.60 ? 532  ASP   A CA    1 
ATOM   3894  C  C     . ASP   A  1  534  ? -28.701 44.750  100.501 1.00 28.50 ? 532  ASP   A C     1 
ATOM   3895  O  O     . ASP   A  1  534  ? -28.059 45.298  101.404 1.00 31.88 ? 532  ASP   A O     1 
ATOM   3896  C  CB    . ASP   A  1  534  ? -29.258 42.370  101.033 1.00 31.11 ? 532  ASP   A CB    1 
ATOM   3897  N  N     . ARG   A  1  535  ? -28.442 44.980  99.217  1.00 26.06 ? 533  ARG   A N     1 
ATOM   3898  C  CA    . ARG   A  1  535  ? -27.288 45.767  98.813  1.00 26.49 ? 533  ARG   A CA    1 
ATOM   3899  C  C     . ARG   A  1  535  ? -27.628 47.218  98.484  1.00 25.25 ? 533  ARG   A C     1 
ATOM   3900  O  O     . ARG   A  1  535  ? -26.782 47.934  97.935  1.00 28.13 ? 533  ARG   A O     1 
ATOM   3901  C  CB    . ARG   A  1  535  ? -26.544 45.089  97.658  1.00 33.12 ? 533  ARG   A CB    1 
ATOM   3902  C  CG    . ARG   A  1  535  ? -26.132 43.647  97.969  1.00 40.18 ? 533  ARG   A CG    1 
ATOM   3903  C  CD    . ARG   A  1  535  ? -25.055 43.129  97.020  1.00 46.84 ? 533  ARG   A CD    1 
ATOM   3904  N  NE    . ARG   A  1  535  ? -25.363 43.402  95.620  1.00 51.34 ? 533  ARG   A NE    1 
ATOM   3905  C  CZ    . ARG   A  1  535  ? -26.060 42.597  94.829  1.00 53.16 ? 533  ARG   A CZ    1 
ATOM   3906  N  NH1   . ARG   A  1  535  ? -26.546 41.445  95.266  1.00 56.46 ? 533  ARG   A NH1   1 
ATOM   3907  N  NH2   . ARG   A  1  535  ? -26.279 42.958  93.567  1.00 52.20 ? 533  ARG   A NH2   1 
ATOM   3908  N  N     . ILE   A  1  536  ? -28.825 47.681  98.828  1.00 24.26 ? 534  ILE   A N     1 
ATOM   3909  C  CA    . ILE   A  1  536  ? -29.197 49.075  98.632  1.00 25.29 ? 534  ILE   A CA    1 
ATOM   3910  C  C     . ILE   A  1  536  ? -29.498 49.664  99.997  1.00 24.88 ? 534  ILE   A C     1 
ATOM   3911  O  O     . ILE   A  1  536  ? -30.357 49.152  100.722 1.00 27.16 ? 534  ILE   A O     1 
ATOM   3912  C  CB    . ILE   A  1  536  ? -30.397 49.212  97.688  1.00 24.21 ? 534  ILE   A CB    1 
ATOM   3913  C  CG1   . ILE   A  1  536  ? -30.036 48.643  96.320  1.00 27.04 ? 534  ILE   A CG1   1 
ATOM   3914  C  CG2   . ILE   A  1  536  ? -30.856 50.667  97.598  1.00 24.26 ? 534  ILE   A CG2   1 
ATOM   3915  C  CD1   . ILE   A  1  536  ? -31.187 48.640  95.375  1.00 27.94 ? 534  ILE   A CD1   1 
ATOM   3916  N  N     . ALA   A  1  537  ? -28.791 50.727  100.350 1.00 22.49 ? 535  ALA   A N     1 
ATOM   3917  C  CA    . ALA   A  1  537  ? -28.981 51.338  101.651 1.00 22.32 ? 535  ALA   A CA    1 
ATOM   3918  C  C     . ALA   A  1  537  ? -30.176 52.276  101.616 1.00 22.07 ? 535  ALA   A C     1 
ATOM   3919  O  O     . ALA   A  1  537  ? -30.347 53.048  100.672 1.00 22.76 ? 535  ALA   A O     1 
ATOM   3920  C  CB    . ALA   A  1  537  ? -27.729 52.122  102.044 1.00 23.56 ? 535  ALA   A CB    1 
ATOM   3921  N  N     . LEU   A  1  538  ? -31.010 52.203  102.650 1.00 21.85 ? 536  LEU   A N     1 
ATOM   3922  C  CA    . LEU   A  1  538  ? -31.970 53.267  102.865 1.00 23.79 ? 536  LEU   A CA    1 
ATOM   3923  C  C     . LEU   A  1  538  ? -31.204 54.571  103.082 1.00 21.79 ? 536  LEU   A C     1 
ATOM   3924  O  O     . LEU   A  1  538  ? -30.061 54.556  103.550 1.00 22.38 ? 536  LEU   A O     1 
ATOM   3925  C  CB    . LEU   A  1  538  ? -32.825 52.971  104.095 1.00 21.92 ? 536  LEU   A CB    1 
ATOM   3926  C  CG    . LEU   A  1  538  ? -33.921 51.912  103.950 1.00 23.44 ? 536  LEU   A CG    1 
ATOM   3927  C  CD1   . LEU   A  1  538  ? -34.601 51.673  105.292 1.00 28.64 ? 536  LEU   A CD1   1 
ATOM   3928  C  CD2   . LEU   A  1  538  ? -34.938 52.352  102.919 1.00 24.89 ? 536  LEU   A CD2   1 
ATOM   3929  N  N     . PRO   A  1  539  ? -31.789 55.710  102.722 1.00 20.92 ? 537  PRO   A N     1 
ATOM   3930  C  CA    . PRO   A  1  539  ? -31.056 56.977  102.879 1.00 21.41 ? 537  PRO   A CA    1 
ATOM   3931  C  C     . PRO   A  1  539  ? -30.522 57.214  104.281 1.00 20.42 ? 537  PRO   A C     1 
ATOM   3932  O  O     . PRO   A  1  539  ? -29.392 57.694  104.429 1.00 21.72 ? 537  PRO   A O     1 
ATOM   3933  C  CB    . PRO   A  1  539  ? -32.079 58.023  102.434 1.00 20.81 ? 537  PRO   A CB    1 
ATOM   3934  C  CG    . PRO   A  1  539  ? -32.888 57.289  101.410 1.00 20.94 ? 537  PRO   A CG    1 
ATOM   3935  C  CD    . PRO   A  1  539  ? -33.030 55.888  101.949 1.00 21.27 ? 537  PRO   A CD    1 
ATOM   3936  N  N     . ALA   A  1  540  ? -31.277 56.837  105.313 1.00 21.97 ? 538  ALA   A N     1 
ATOM   3937  C  CA    . ALA   A  1  540  ? -30.809 57.023  106.680 1.00 24.77 ? 538  ALA   A CA    1 
ATOM   3938  C  C     . ALA   A  1  540  ? -29.580 56.181  106.990 1.00 26.65 ? 538  ALA   A C     1 
ATOM   3939  O  O     . ALA   A  1  540  ? -28.881 56.467  107.967 1.00 26.30 ? 538  ALA   A O     1 
ATOM   3940  C  CB    . ALA   A  1  540  ? -31.916 56.676  107.673 1.00 25.21 ? 538  ALA   A CB    1 
ATOM   3941  N  N     . GLU   A  1  541  ? -29.297 55.157  106.189 1.00 23.63 ? 539  GLU   A N     1 
ATOM   3942  C  CA    . GLU   A  1  541  ? -28.259 54.188  106.522 1.00 25.22 ? 539  GLU   A CA    1 
ATOM   3943  C  C     . GLU   A  1  541  ? -27.037 54.307  105.617 1.00 24.39 ? 539  GLU   A C     1 
ATOM   3944  O  O     . GLU   A  1  541  ? -26.210 53.390  105.579 1.00 23.31 ? 539  GLU   A O     1 
ATOM   3945  C  CB    . GLU   A  1  541  ? -28.835 52.770  106.516 1.00 25.51 ? 539  GLU   A CB    1 
ATOM   3946  C  CG    . GLU   A  1  541  ? -30.004 52.620  107.482 1.00 30.99 ? 539  GLU   A CG    1 
ATOM   3947  C  CD    . GLU   A  1  541  ? -30.555 51.209  107.546 1.00 43.70 ? 539  GLU   A CD    1 
ATOM   3948  O  OE1   . GLU   A  1  541  ? -29.757 50.251  107.477 1.00 53.22 ? 539  GLU   A OE1   1 
ATOM   3949  O  OE2   . GLU   A  1  541  ? -31.791 51.059  107.664 1.00 49.69 ? 539  GLU   A OE2   1 
ATOM   3950  N  N     . LEU   A  1  542  ? -26.898 55.436  104.909 1.00 22.21 ? 540  LEU   A N     1 
ATOM   3951  C  CA    . LEU   A  1  542  ? -25.801 55.609  103.961 1.00 24.69 ? 540  LEU   A CA    1 
ATOM   3952  C  C     . LEU   A  1  542  ? -24.443 55.417  104.612 1.00 23.48 ? 540  LEU   A C     1 
ATOM   3953  O  O     . LEU   A  1  542  ? -23.491 55.003  103.946 1.00 25.62 ? 540  LEU   A O     1 
ATOM   3954  C  CB    . LEU   A  1  542  ? -25.839 57.016  103.369 1.00 25.37 ? 540  LEU   A CB    1 
ATOM   3955  C  CG    . LEU   A  1  542  ? -26.722 57.272  102.157 1.00 27.78 ? 540  LEU   A CG    1 
ATOM   3956  C  CD1   . LEU   A  1  542  ? -26.334 58.615  101.561 1.00 24.93 ? 540  LEU   A CD1   1 
ATOM   3957  C  CD2   . LEU   A  1  542  ? -26.570 56.162  101.130 1.00 27.32 ? 540  LEU   A CD2   1 
ATOM   3958  N  N     . PHE   A  1  543  ? -24.320 55.750  105.889 1.00 22.97 ? 541  PHE   A N     1 
ATOM   3959  C  CA    . PHE   A  1  543  ? -23.039 55.673  106.573 1.00 24.03 ? 541  PHE   A CA    1 
ATOM   3960  C  C     . PHE   A  1  543  ? -22.945 54.469  107.493 1.00 25.07 ? 541  PHE   A C     1 
ATOM   3961  O  O     . PHE   A  1  543  ? -21.959 54.337  108.228 1.00 26.49 ? 541  PHE   A O     1 
ATOM   3962  C  CB    . PHE   A  1  543  ? -22.778 56.972  107.324 1.00 21.53 ? 541  PHE   A CB    1 
ATOM   3963  C  CG    . PHE   A  1  543  ? -22.998 58.183  106.483 1.00 22.90 ? 541  PHE   A CG    1 
ATOM   3964  C  CD1   . PHE   A  1  543  ? -22.325 58.323  105.281 1.00 25.29 ? 541  PHE   A CD1   1 
ATOM   3965  C  CD2   . PHE   A  1  543  ? -23.893 59.167  106.868 1.00 22.16 ? 541  PHE   A CD2   1 
ATOM   3966  C  CE1   . PHE   A  1  543  ? -22.532 59.418  104.486 1.00 24.02 ? 541  PHE   A CE1   1 
ATOM   3967  C  CE2   . PHE   A  1  543  ? -24.098 60.272  106.076 1.00 21.45 ? 541  PHE   A CE2   1 
ATOM   3968  C  CZ    . PHE   A  1  543  ? -23.417 60.400  104.884 1.00 21.64 ? 541  PHE   A CZ    1 
ATOM   3969  N  N     . GLY   A  1  544  ? -23.952 53.600  107.470 1.00 23.99 ? 542  GLY   A N     1 
ATOM   3970  C  CA    . GLY   A  1  544  ? -23.881 52.364  108.224 1.00 26.88 ? 542  GLY   A CA    1 
ATOM   3971  C  C     . GLY   A  1  544  ? -23.705 52.620  109.707 1.00 28.94 ? 542  GLY   A C     1 
ATOM   3972  O  O     . GLY   A  1  544  ? -24.358 53.487  110.298 1.00 26.42 ? 542  GLY   A O     1 
ATOM   3973  N  N     . ASP   A  1  545  ? -22.788 51.864  110.318 1.00 28.80 ? 543  ASP   A N     1 
ATOM   3974  C  CA    . ASP   A  1  545  ? -22.619 51.917  111.768 1.00 32.96 ? 543  ASP   A CA    1 
ATOM   3975  C  C     . ASP   A  1  545  ? -21.976 53.213  112.244 1.00 30.93 ? 543  ASP   A C     1 
ATOM   3976  O  O     . ASP   A  1  545  ? -22.035 53.511  113.445 1.00 33.52 ? 543  ASP   A O     1 
ATOM   3977  C  CB    . ASP   A  1  545  ? -21.772 50.737  112.250 1.00 36.36 ? 543  ASP   A CB    1 
ATOM   3978  C  CG    . ASP   A  1  545  ? -22.420 49.393  111.964 1.00 45.00 ? 543  ASP   A CG    1 
ATOM   3979  O  OD1   . ASP   A  1  545  ? -23.659 49.343  111.806 1.00 44.41 ? 543  ASP   A OD1   1 
ATOM   3980  O  OD2   . ASP   A  1  545  ? -21.687 48.382  111.901 1.00 56.12 ? 543  ASP   A OD2   1 
ATOM   3981  N  N     . ALA   A  1  546  ? -21.367 53.984  111.343 1.00 26.21 ? 544  ALA   A N     1 
ATOM   3982  C  CA    . ALA   A  1  546  ? -20.629 55.171  111.764 1.00 29.38 ? 544  ALA   A CA    1 
ATOM   3983  C  C     . ALA   A  1  546  ? -21.557 56.215  112.367 1.00 29.66 ? 544  ALA   A C     1 
ATOM   3984  O  O     . ALA   A  1  546  ? -21.254 56.801  113.412 1.00 29.12 ? 544  ALA   A O     1 
ATOM   3985  C  CB    . ALA   A  1  546  ? -19.854 55.756  110.586 1.00 26.60 ? 544  ALA   A CB    1 
ATOM   3986  N  N     . ARG   A  1  547  ? -22.693 56.463  111.726 1.00 25.22 ? 545  ARG   A N     1 
ATOM   3987  C  CA    . ARG   A  1  547  ? -23.620 57.469  112.222 1.00 26.78 ? 545  ARG   A CA    1 
ATOM   3988  C  C     . ARG   A  1  547  ? -24.865 57.421  111.361 1.00 22.78 ? 545  ARG   A C     1 
ATOM   3989  O  O     . ARG   A  1  547  ? -24.885 56.813  110.289 1.00 22.61 ? 545  ARG   A O     1 
ATOM   3990  C  CB    . ARG   A  1  547  ? -23.037 58.881  112.194 1.00 27.07 ? 545  ARG   A CB    1 
ATOM   3991  C  CG    . ARG   A  1  547  ? -22.763 59.382  110.819 1.00 28.40 ? 545  ARG   A CG    1 
ATOM   3992  C  CD    . ARG   A  1  547  ? -22.114 60.742  110.860 1.00 28.88 ? 545  ARG   A CD    1 
ATOM   3993  N  NE    . ARG   A  1  547  ? -21.314 60.928  109.660 1.00 24.06 ? 545  ARG   A NE    1 
ATOM   3994  C  CZ    . ARG   A  1  547  ? -21.719 61.578  108.577 1.00 22.34 ? 545  ARG   A CZ    1 
ATOM   3995  N  NH1   . ARG   A  1  547  ? -22.888 62.202  108.540 1.00 23.18 ? 545  ARG   A NH1   1 
ATOM   3996  N  NH2   . ARG   A  1  547  ? -20.933 61.600  107.507 1.00 24.60 ? 545  ARG   A NH2   1 
ATOM   3997  N  N     . THR   A  1  548  ? -25.902 58.072  111.856 1.00 22.20 ? 546  THR   A N     1 
ATOM   3998  C  CA    . THR   A  1  548  ? -27.188 58.095  111.185 1.00 21.69 ? 546  THR   A CA    1 
ATOM   3999  C  C     . THR   A  1  548  ? -27.229 59.313  110.286 1.00 19.89 ? 546  THR   A C     1 
ATOM   4000  O  O     . THR   A  1  548  ? -26.922 60.426  110.720 1.00 20.47 ? 546  THR   A O     1 
ATOM   4001  C  CB    . THR   A  1  548  ? -28.299 58.186  112.224 1.00 25.15 ? 546  THR   A CB    1 
ATOM   4002  O  OG1   . THR   A  1  548  ? -28.208 57.057  113.102 1.00 29.41 ? 546  THR   A OG1   1 
ATOM   4003  C  CG2   . THR   A  1  548  ? -29.648 58.196  111.545 1.00 25.63 ? 546  THR   A CG2   1 
ATOM   4004  N  N     . ASN   A  1  549  ? -27.580 59.095  109.023 1.00 19.58 ? 547  ASN   A N     1 
ATOM   4005  C  CA    . ASN   A  1  549  ? -27.687 60.199  108.089 1.00 19.95 ? 547  ASN   A CA    1 
ATOM   4006  C  C     . ASN   A  1  549  ? -28.831 61.109  108.517 1.00 20.32 ? 547  ASN   A C     1 
ATOM   4007  O  O     . ASN   A  1  549  ? -29.824 60.659  109.091 1.00 21.84 ? 547  ASN   A O     1 
ATOM   4008  C  CB    . ASN   A  1  549  ? -27.937 59.638  106.686 1.00 20.04 ? 547  ASN   A CB    1 
ATOM   4009  C  CG    . ASN   A  1  549  ? -27.786 60.685  105.587 1.00 20.29 ? 547  ASN   A CG    1 
ATOM   4010  O  OD1   . ASN   A  1  549  ? -27.238 61.760  105.798 1.00 20.27 ? 547  ASN   A OD1   1 
ATOM   4011  N  ND2   . ASN   A  1  549  ? -28.274 60.361  104.399 1.00 19.87 ? 547  ASN   A ND2   1 
ATOM   4012  N  N     . SER   A  1  550  ? -28.664 62.407  108.289 1.00 20.94 ? 548  SER   A N     1 
ATOM   4013  C  CA    . SER   A  1  550  ? -29.765 63.328  108.526 1.00 20.56 ? 548  SER   A CA    1 
ATOM   4014  C  C     . SER   A  1  550  ? -30.880 63.034  107.536 1.00 19.13 ? 548  SER   A C     1 
ATOM   4015  O  O     . SER   A  1  550  ? -30.645 62.525  106.438 1.00 20.32 ? 548  SER   A O     1 
ATOM   4016  C  CB    . SER   A  1  550  ? -29.316 64.767  108.314 1.00 18.65 ? 548  SER   A CB    1 
ATOM   4017  O  OG    . SER   A  1  550  ? -28.813 64.937  107.006 1.00 19.99 ? 548  SER   A OG    1 
ATOM   4018  N  N     . ALA   A  1  551  ? -32.100 63.362  107.939 1.00 21.23 ? 549  ALA   A N     1 
ATOM   4019  C  CA    . ALA   A  1  551  ? -33.276 63.160  107.110 1.00 23.99 ? 549  ALA   A CA    1 
ATOM   4020  C  C     . ALA   A  1  551  ? -33.744 64.490  106.543 1.00 22.57 ? 549  ALA   A C     1 
ATOM   4021  O  O     . ALA   A  1  551  ? -33.726 65.518  107.225 1.00 22.33 ? 549  ALA   A O     1 
ATOM   4022  C  CB    . ALA   A  1  551  ? -34.404 62.529  107.923 1.00 24.84 ? 549  ALA   A CB    1 
ATOM   4023  N  N     . GLY   A  1  552  ? -34.153 64.465  105.281 1.00 21.36 ? 550  GLY   A N     1 
ATOM   4024  C  CA    . GLY   A  1  552  ? -34.747 65.610  104.649 1.00 21.75 ? 550  GLY   A CA    1 
ATOM   4025  C  C     . GLY   A  1  552  ? -36.255 65.519  104.637 1.00 22.71 ? 550  GLY   A C     1 
ATOM   4026  O  O     . GLY   A  1  552  ? -36.870 64.763  105.396 1.00 22.56 ? 550  GLY   A O     1 
ATOM   4027  N  N     . LEU   A  1  553  ? -36.856 66.300  103.752 1.00 22.81 ? 551  LEU   A N     1 
ATOM   4028  C  CA    . LEU   A  1  553  ? -38.297 66.350  103.608 1.00 20.44 ? 551  LEU   A CA    1 
ATOM   4029  C  C     . LEU   A  1  553  ? -38.610 66.338  102.128 1.00 22.46 ? 551  LEU   A C     1 
ATOM   4030  O  O     . LEU   A  1  553  ? -37.889 66.934  101.327 1.00 24.10 ? 551  LEU   A O     1 
ATOM   4031  C  CB    . LEU   A  1  553  ? -38.840 67.641  104.191 1.00 23.87 ? 551  LEU   A CB    1 
ATOM   4032  C  CG    . LEU   A  1  553  ? -38.775 67.754  105.708 1.00 24.00 ? 551  LEU   A CG    1 
ATOM   4033  C  CD1   . LEU   A  1  553  ? -39.291 69.113  106.127 1.00 29.37 ? 551  LEU   A CD1   1 
ATOM   4034  C  CD2   . LEU   A  1  553  ? -39.580 66.632  106.379 1.00 24.43 ? 551  LEU   A CD2   1 
ATOM   4035  N  N     . ASP   A  1  554  ? -39.701 65.671  101.774 1.00 19.92 ? 552  ASP   A N     1 
ATOM   4036  C  CA    . ASP   A  1  554  ? -40.067 65.512  100.365 1.00 21.88 ? 552  ASP   A CA    1 
ATOM   4037  C  C     . ASP   A  1  554  ? -41.019 66.641  99.983  1.00 20.16 ? 552  ASP   A C     1 
ATOM   4038  O  O     . ASP   A  1  554  ? -42.211 66.598  100.294 1.00 19.51 ? 552  ASP   A O     1 
ATOM   4039  C  CB    . ASP   A  1  554  ? -40.690 64.141  100.130 1.00 19.93 ? 552  ASP   A CB    1 
ATOM   4040  C  CG    . ASP   A  1  554  ? -41.004 63.888  98.661  1.00 21.61 ? 552  ASP   A CG    1 
ATOM   4041  O  OD1   . ASP   A  1  554  ? -40.762 64.793  97.835  1.00 23.49 ? 552  ASP   A OD1   1 
ATOM   4042  O  OD2   . ASP   A  1  554  ? -41.478 62.784  98.327  1.00 24.37 ? 552  ASP   A OD2   1 
ATOM   4043  N  N     . LEU   A  1  555  ? -40.499 67.660  99.294  1.00 19.55 ? 553  LEU   A N     1 
ATOM   4044  C  CA    . LEU   A  1  555  ? -41.344 68.789  98.920  1.00 19.93 ? 553  LEU   A CA    1 
ATOM   4045  C  C     . LEU   A  1  555  ? -42.238 68.495  97.721  1.00 19.68 ? 553  LEU   A C     1 
ATOM   4046  O  O     . LEU   A  1  555  ? -42.918 69.407  97.238  1.00 22.46 ? 553  LEU   A O     1 
ATOM   4047  C  CB    . LEU   A  1  555  ? -40.508 70.048  98.700  1.00 21.30 ? 553  LEU   A CB    1 
ATOM   4048  C  CG    . LEU   A  1  555  ? -39.686 70.430  99.931  1.00 21.64 ? 553  LEU   A CG    1 
ATOM   4049  C  CD1   . LEU   A  1  555  ? -38.982 71.758  99.716  1.00 27.33 ? 553  LEU   A CD1   1 
ATOM   4050  C  CD2   . LEU   A  1  555  ? -40.606 70.500  101.151 1.00 24.59 ? 553  LEU   A CD2   1 
ATOM   4051  N  N     . SER   A  1  556  ? -42.248 67.259  97.233  1.00 18.81 ? 554  SER   A N     1 
ATOM   4052  C  CA    . SER   A  1  556  ? -43.238 66.833  96.253  1.00 21.48 ? 554  SER   A CA    1 
ATOM   4053  C  C     . SER   A  1  556  ? -44.370 66.041  96.884  1.00 21.28 ? 554  SER   A C     1 
ATOM   4054  O  O     . SER   A  1  556  ? -45.293 65.632  96.177  1.00 23.08 ? 554  SER   A O     1 
ATOM   4055  C  CB    . SER   A  1  556  ? -42.586 65.990  95.149  1.00 21.71 ? 554  SER   A CB    1 
ATOM   4056  O  OG    . SER   A  1  556  ? -42.319 64.669  95.606  1.00 23.87 ? 554  SER   A OG    1 
ATOM   4057  N  N     . ASN   A  1  557  ? -44.320 65.818  98.191  1.00 20.18 ? 555  ASN   A N     1 
ATOM   4058  C  CA    . ASN   A  1  557  ? -45.316 65.023  98.897  1.00 19.76 ? 555  ASN   A CA    1 
ATOM   4059  C  C     . ASN   A  1  557  ? -46.358 65.972  99.472  1.00 20.53 ? 555  ASN   A C     1 
ATOM   4060  O  O     . ASN   A  1  557  ? -46.021 66.846  100.279 1.00 20.53 ? 555  ASN   A O     1 
ATOM   4061  C  CB    . ASN   A  1  557  ? -44.618 64.231  100.004 1.00 21.88 ? 555  ASN   A CB    1 
ATOM   4062  C  CG    . ASN   A  1  557  ? -45.564 63.319  100.765 1.00 20.89 ? 555  ASN   A CG    1 
ATOM   4063  O  OD1   . ASN   A  1  557  ? -46.608 63.750  101.232 1.00 23.98 ? 555  ASN   A OD1   1 
ATOM   4064  N  ND2   . ASN   A  1  557  ? -45.198 62.040  100.878 1.00 22.96 ? 555  ASN   A ND2   1 
ATOM   4065  N  N     . GLU   A  1  558  ? -47.622 65.803  99.050  1.00 20.16 ? 556  GLU   A N     1 
ATOM   4066  C  CA    . GLU   A  1  558  ? -48.664 66.736  99.474  1.00 23.02 ? 556  GLU   A CA    1 
ATOM   4067  C  C     . GLU   A  1  558  ? -48.884 66.695  100.978 1.00 21.76 ? 556  GLU   A C     1 
ATOM   4068  O  O     . GLU   A  1  558  ? -49.194 67.726  101.586 1.00 23.35 ? 556  GLU   A O     1 
ATOM   4069  C  CB    . GLU   A  1  558  ? -49.989 66.478  98.747  1.00 24.42 ? 556  GLU   A CB    1 
ATOM   4070  C  CG    . GLU   A  1  558  ? -49.967 66.779  97.276  1.00 24.31 ? 556  GLU   A CG    1 
ATOM   4071  C  CD    . GLU   A  1  558  ? -49.779 68.258  96.919  1.00 24.62 ? 556  GLU   A CD    1 
ATOM   4072  O  OE1   . GLU   A  1  558  ? -49.841 69.145  97.791  1.00 22.06 ? 556  GLU   A OE1   1 
ATOM   4073  O  OE2   . GLU   A  1  558  ? -49.575 68.530  95.716  1.00 23.84 ? 556  GLU   A OE2   1 
ATOM   4074  N  N     . GLU   A  1  559  ? -48.759 65.512  101.593 1.00 20.62 ? 557  GLU   A N     1 
ATOM   4075  C  CA    . GLU   A  1  559  ? -48.865 65.429  103.049 1.00 22.48 ? 557  GLU   A CA    1 
ATOM   4076  C  C     . GLU   A  1  559  ? -47.757 66.233  103.704 1.00 20.43 ? 557  GLU   A C     1 
ATOM   4077  O  O     . GLU   A  1  559  ? -47.997 66.982  104.656 1.00 23.70 ? 557  GLU   A O     1 
ATOM   4078  C  CB    . GLU   A  1  559  ? -48.767 63.976  103.517 1.00 26.58 ? 557  GLU   A CB    1 
ATOM   4079  C  CG    . GLU   A  1  559  ? -49.923 63.061  103.142 1.00 28.22 ? 557  GLU   A CG    1 
ATOM   4080  C  CD    . GLU   A  1  559  ? -49.623 61.591  103.473 1.00 38.03 ? 557  GLU   A CD    1 
ATOM   4081  O  OE1   . GLU   A  1  559  ? -48.556 61.309  104.071 1.00 41.01 ? 557  GLU   A OE1   1 
ATOM   4082  O  OE2   . GLU   A  1  559  ? -50.444 60.713  103.133 1.00 40.59 ? 557  GLU   A OE2   1 
ATOM   4083  N  N     . THR   A  1  560  ? -46.534 66.100  103.186 1.00 21.28 ? 558  THR   A N     1 
ATOM   4084  C  CA    . THR   A  1  560  ? -45.418 66.854  103.738 1.00 21.74 ? 558  THR   A CA    1 
ATOM   4085  C  C     . THR   A  1  560  ? -45.630 68.347  103.548 1.00 19.99 ? 558  THR   A C     1 
ATOM   4086  O  O     . THR   A  1  560  ? -45.407 69.136  104.472 1.00 23.24 ? 558  THR   A O     1 
ATOM   4087  C  CB    . THR   A  1  560  ? -44.130 66.394  103.064 1.00 21.76 ? 558  THR   A CB    1 
ATOM   4088  O  OG1   . THR   A  1  560  ? -43.965 64.992  103.307 1.00 24.79 ? 558  THR   A OG1   1 
ATOM   4089  C  CG2   . THR   A  1  560  ? -42.931 67.170  103.594 1.00 22.84 ? 558  THR   A CG2   1 
ATOM   4090  N  N     . LEU   A  1  561  ? -46.082 68.754  102.359 1.00 21.33 ? 559  LEU   A N     1 
ATOM   4091  C  CA    . LEU   A  1  561  ? -46.311 70.174  102.115 1.00 18.67 ? 559  LEU   A CA    1 
ATOM   4092  C  C     . LEU   A  1  561  ? -47.392 70.723  103.033 1.00 20.51 ? 559  LEU   A C     1 
ATOM   4093  O  O     . LEU   A  1  561  ? -47.276 71.847  103.535 1.00 23.02 ? 559  LEU   A O     1 
ATOM   4094  C  CB    . LEU   A  1  561  ? -46.679 70.402  100.650 1.00 18.87 ? 559  LEU   A CB    1 
ATOM   4095  C  CG    . LEU   A  1  561  ? -45.509 70.188  99.690  1.00 19.60 ? 559  LEU   A CG    1 
ATOM   4096  C  CD1   . LEU   A  1  561  ? -46.011 70.357  98.259  1.00 20.68 ? 559  LEU   A CD1   1 
ATOM   4097  C  CD2   . LEU   A  1  561  ? -44.364 71.172  99.980  1.00 20.44 ? 559  LEU   A CD2   1 
ATOM   4098  N  N     . ALA   A  1  562  ? -48.461 69.954  103.249 1.00 23.28 ? 560  ALA   A N     1 
ATOM   4099  C  CA    . ALA   A  1  562  ? -49.533 70.426  104.115 1.00 23.51 ? 560  ALA   A CA    1 
ATOM   4100  C  C     . ALA   A  1  562  ? -49.058 70.545  105.557 1.00 23.61 ? 560  ALA   A C     1 
ATOM   4101  O  O     . ALA   A  1  562  ? -49.327 71.546  106.235 1.00 23.68 ? 560  ALA   A O     1 
ATOM   4102  C  CB    . ALA   A  1  562  ? -50.740 69.493  104.013 1.00 24.18 ? 560  ALA   A CB    1 
ATOM   4103  N  N     . SER   A  1  563  ? -48.338 69.536  106.041 1.00 24.74 ? 561  SER   A N     1 
ATOM   4104  C  CA    A SER   A  1  563  ? -47.818 69.581  107.403 0.54 26.24 ? 561  SER   A CA    1 
ATOM   4105  C  CA    B SER   A  1  563  ? -47.838 69.600  107.408 0.46 26.24 ? 561  SER   A CA    1 
ATOM   4106  C  C     . SER   A  1  563  ? -46.761 70.667  107.548 1.00 24.70 ? 561  SER   A C     1 
ATOM   4107  O  O     . SER   A  1  563  ? -46.701 71.363  108.569 1.00 26.58 ? 561  SER   A O     1 
ATOM   4108  C  CB    A SER   A  1  563  ? -47.232 68.218  107.767 0.54 26.33 ? 561  SER   A CB    1 
ATOM   4109  C  CB    B SER   A  1  563  ? -47.326 68.231  107.853 0.46 26.39 ? 561  SER   A CB    1 
ATOM   4110  O  OG    A SER   A  1  563  ? -46.571 68.267  109.017 0.54 29.26 ? 561  SER   A OG    1 
ATOM   4111  O  OG    B SER   A  1  563  ? -46.211 67.832  107.084 0.46 29.52 ? 561  SER   A OG    1 
ATOM   4112  N  N     . LEU   A  1  564  ? -45.910 70.821  106.535 1.00 24.92 ? 562  LEU   A N     1 
ATOM   4113  C  CA    . LEU   A  1  564  ? -44.881 71.847  106.604 1.00 23.45 ? 562  LEU   A CA    1 
ATOM   4114  C  C     . LEU   A  1  564  ? -45.502 73.234  106.573 1.00 24.36 ? 562  LEU   A C     1 
ATOM   4115  O  O     . LEU   A  1  564  ? -45.060 74.131  107.297 1.00 25.59 ? 562  LEU   A O     1 
ATOM   4116  C  CB    . LEU   A  1  564  ? -43.883 71.661  105.463 1.00 23.22 ? 562  LEU   A CB    1 
ATOM   4117  C  CG    . LEU   A  1  564  ? -42.577 72.446  105.479 1.00 30.98 ? 562  LEU   A CG    1 
ATOM   4118  C  CD1   . LEU   A  1  564  ? -41.809 72.180  106.754 1.00 28.86 ? 562  LEU   A CD1   1 
ATOM   4119  C  CD2   . LEU   A  1  564  ? -41.742 72.057  104.269 1.00 26.69 ? 562  LEU   A CD2   1 
ATOM   4120  N  N     . THR   A  1  565  ? -46.549 73.425  105.764 1.00 22.23 ? 563  THR   A N     1 
ATOM   4121  C  CA    . THR   A  1  565  ? -47.218 74.721  105.735 1.00 23.24 ? 563  THR   A CA    1 
ATOM   4122  C  C     . THR   A  1  565  ? -47.650 75.140  107.131 1.00 22.80 ? 563  THR   A C     1 
ATOM   4123  O  O     . THR   A  1  565  ? -47.421 76.278  107.550 1.00 25.15 ? 563  THR   A O     1 
ATOM   4124  C  CB    . THR   A  1  565  ? -48.426 74.683  104.798 1.00 25.05 ? 563  THR   A CB    1 
ATOM   4125  O  OG1   . THR   A  1  565  ? -47.977 74.495  103.453 1.00 24.04 ? 563  THR   A OG1   1 
ATOM   4126  C  CG2   . THR   A  1  565  ? -49.203 75.996  104.884 1.00 28.58 ? 563  THR   A CG2   1 
ATOM   4127  N  N     . GLU   A  1  566  ? -48.257 74.219  107.877 1.00 24.37 ? 564  GLU   A N     1 
ATOM   4128  C  CA    . GLU   A  1  566  ? -48.710 74.559  109.220 1.00 24.83 ? 564  GLU   A CA    1 
ATOM   4129  C  C     . GLU   A  1  566  ? -47.533 74.852  110.139 1.00 25.06 ? 564  GLU   A C     1 
ATOM   4130  O  O     . GLU   A  1  566  ? -47.531 75.858  110.854 1.00 27.11 ? 564  GLU   A O     1 
ATOM   4131  C  CB    . GLU   A  1  566  ? -49.597 73.445  109.776 1.00 28.24 ? 564  GLU   A CB    1 
ATOM   4132  C  CG    . GLU   A  1  566  ? -50.868 73.244  108.966 1.00 36.22 ? 564  GLU   A CG    1 
ATOM   4133  C  CD    . GLU   A  1  566  ? -51.614 74.551  108.710 1.00 38.85 ? 564  GLU   A CD    1 
ATOM   4134  O  OE1   . GLU   A  1  566  ? -51.854 75.313  109.676 1.00 40.15 ? 564  GLU   A OE1   1 
ATOM   4135  O  OE2   . GLU   A  1  566  ? -51.958 74.821  107.536 1.00 41.47 ? 564  GLU   A OE2   1 
ATOM   4136  N  N     . ALA   A  1  567  ? -46.507 74.004  110.105 1.00 25.11 ? 565  ALA   A N     1 
ATOM   4137  C  CA    . ALA   A  1  567  ? -45.346 74.229  110.962 1.00 26.11 ? 565  ALA   A CA    1 
ATOM   4138  C  C     . ALA   A  1  567  ? -44.654 75.546  110.626 1.00 24.08 ? 565  ALA   A C     1 
ATOM   4139  O  O     . ALA   A  1  567  ? -44.199 76.267  111.527 1.00 25.52 ? 565  ALA   A O     1 
ATOM   4140  C  CB    . ALA   A  1  567  ? -44.376 73.055  110.841 1.00 26.95 ? 565  ALA   A CB    1 
ATOM   4141  N  N     . LEU   A  1  568  ? -44.555 75.869  109.333 1.00 23.23 ? 566  LEU   A N     1 
ATOM   4142  C  CA    . LEU   A  1  568  ? -43.929 77.119  108.916 1.00 22.32 ? 566  LEU   A CA    1 
ATOM   4143  C  C     . LEU   A  1  568  ? -44.728 78.317  109.400 1.00 23.66 ? 566  LEU   A C     1 
ATOM   4144  O  O     . LEU   A  1  568  ? -44.168 79.279  109.935 1.00 25.00 ? 566  LEU   A O     1 
ATOM   4145  C  CB    . LEU   A  1  568  ? -43.785 77.159  107.393 1.00 23.02 ? 566  LEU   A CB    1 
ATOM   4146  C  CG    . LEU   A  1  568  ? -42.816 76.142  106.797 1.00 22.31 ? 566  LEU   A CG    1 
ATOM   4147  C  CD1   . LEU   A  1  568  ? -42.812 76.227  105.279 1.00 21.38 ? 566  LEU   A CD1   1 
ATOM   4148  C  CD2   . LEU   A  1  568  ? -41.406 76.321  107.352 1.00 24.05 ? 566  LEU   A CD2   1 
ATOM   4149  N  N     . ARG   A  1  569  ? -46.050 78.276  109.217 1.00 23.84 ? 567  ARG   A N     1 
ATOM   4150  C  CA    . ARG   A  1  569  ? -46.889 79.345  109.747 1.00 25.96 ? 567  ARG   A CA    1 
ATOM   4151  C  C     . ARG   A  1  569  ? -46.719 79.471  111.254 1.00 26.35 ? 567  ARG   A C     1 
ATOM   4152  O  O     . ARG   A  1  569  ? -46.592 80.583  111.785 1.00 29.12 ? 567  ARG   A O     1 
ATOM   4153  C  CB    . ARG   A  1  569  ? -48.356 79.095  109.388 1.00 28.49 ? 567  ARG   A CB    1 
ATOM   4154  C  CG    . ARG   A  1  569  ? -48.674 79.306  107.911 1.00 29.57 ? 567  ARG   A CG    1 
ATOM   4155  C  CD    . ARG   A  1  569  ? -50.136 78.964  107.589 1.00 34.63 ? 567  ARG   A CD    1 
ATOM   4156  N  NE    . ARG   A  1  569  ? -50.388 78.990  106.151 1.00 37.25 ? 567  ARG   A NE    1 
ATOM   4157  C  CZ    . ARG   A  1  569  ? -51.486 78.519  105.574 1.00 41.97 ? 567  ARG   A CZ    1 
ATOM   4158  N  NH1   . ARG   A  1  569  ? -52.454 77.959  106.282 1.00 48.13 ? 567  ARG   A NH1   1 
ATOM   4159  N  NH2   . ARG   A  1  569  ? -51.615 78.607  104.252 1.00 46.26 ? 567  ARG   A NH2   1 
ATOM   4160  N  N     . GLU   A  1  570  ? -46.693 78.336  111.956 1.00 25.21 ? 568  GLU   A N     1 
ATOM   4161  C  CA    . GLU   A  1  570  ? -46.536 78.370  113.405 1.00 26.49 ? 568  GLU   A CA    1 
ATOM   4162  C  C     . GLU   A  1  570  ? -45.182 78.941  113.804 1.00 32.48 ? 568  GLU   A C     1 
ATOM   4163  O  O     . GLU   A  1  570  ? -45.077 79.627  114.828 1.00 30.84 ? 568  GLU   A O     1 
ATOM   4164  C  CB    . GLU   A  1  570  ? -46.744 76.968  113.981 1.00 29.87 ? 568  GLU   A CB    1 
ATOM   4165  C  CG    . GLU   A  1  570  ? -48.203 76.494  113.911 1.00 34.66 ? 568  GLU   A CG    1 
ATOM   4166  C  CD    . GLU   A  1  570  ? -48.366 75.019  114.226 1.00 41.64 ? 568  GLU   A CD    1 
ATOM   4167  O  OE1   . GLU   A  1  570  ? -47.360 74.281  114.166 1.00 48.22 ? 568  GLU   A OE1   1 
ATOM   4168  O  OE2   . GLU   A  1  570  ? -49.502 74.597  114.534 1.00 52.96 ? 568  GLU   A OE2   1 
ATOM   4169  N  N     . SER   A  1  571  ? -44.143 78.692  113.003 1.00 28.08 ? 569  SER   A N     1 
ATOM   4170  C  CA    . SER   A  1  571  ? -42.833 79.252  113.314 1.00 28.78 ? 569  SER   A CA    1 
ATOM   4171  C  C     . SER   A  1  571  ? -42.836 80.767  113.185 1.00 27.04 ? 569  SER   A C     1 
ATOM   4172  O  O     . SER   A  1  571  ? -42.121 81.453  113.922 1.00 29.06 ? 569  SER   A O     1 
ATOM   4173  C  CB    . SER   A  1  571  ? -41.772 78.658  112.395 1.00 25.10 ? 569  SER   A CB    1 
ATOM   4174  O  OG    . SER   A  1  571  ? -41.834 79.247  111.103 1.00 27.78 ? 569  SER   A OG    1 
ATOM   4175  N  N     . ALA   A  1  572  ? -43.636 81.309  112.266 1.00 28.25 ? 570  ALA   A N     1 
ATOM   4176  C  CA    . ALA   A  1  572  ? -43.694 82.756  112.110 1.00 29.40 ? 570  ALA   A CA    1 
ATOM   4177  C  C     . ALA   A  1  572  ? -44.480 83.431  113.225 1.00 32.43 ? 570  ALA   A C     1 
ATOM   4178  O  O     . ALA   A  1  572  ? -44.424 84.658  113.338 1.00 35.77 ? 570  ALA   A O     1 
ATOM   4179  C  CB    . ALA   A  1  572  ? -44.272 83.124  110.743 1.00 32.93 ? 570  ALA   A CB    1 
ATOM   4180  N  N     . ALA   A  1  573  ? -45.205 82.668  114.038 1.00 31.47 ? 571  ALA   A N     1 
ATOM   4181  C  CA    . ALA   A  1  573  ? -45.901 83.201  115.203 1.00 35.06 ? 571  ALA   A CA    1 
ATOM   4182  C  C     . ALA   A  1  573  ? -45.070 83.108  116.477 1.00 39.31 ? 571  ALA   A C     1 
ATOM   4183  O  O     . ALA   A  1  573  ? -45.536 83.529  117.540 1.00 39.65 ? 571  ALA   A O     1 
ATOM   4184  C  CB    . ALA   A  1  573  ? -47.243 82.485  115.404 1.00 33.58 ? 571  ALA   A CB    1 
ATOM   4185  N  N     . MET   A  1  574  ? -43.859 82.568  116.399 1.00 33.55 ? 572  MET   A N     1 
ATOM   4186  C  CA    . MET   A  1  574  ? -43.005 82.463  117.573 1.00 35.56 ? 572  MET   A CA    1 
ATOM   4187  C  C     . MET   A  1  574  ? -42.250 83.769  117.799 1.00 38.38 ? 572  MET   A C     1 
ATOM   4188  O  O     . MET   A  1  574  ? -41.948 84.509  116.859 1.00 32.34 ? 572  MET   A O     1 
ATOM   4189  C  CB    . MET   A  1  574  ? -42.046 81.283  117.427 1.00 37.09 ? 572  MET   A CB    1 
ATOM   4190  C  CG    . MET   A  1  574  ? -42.762 79.933  117.432 1.00 35.60 ? 572  MET   A CG    1 
ATOM   4191  S  SD    . MET   A  1  574  ? -41.703 78.522  117.098 1.00 38.00 ? 572  MET   A SD    1 
ATOM   4192  C  CE    . MET   A  1  574  ? -42.890 77.173  117.122 1.00 43.66 ? 572  MET   A CE    1 
ATOM   4193  N  N     . LYS   A  1  575  ? -41.980 84.066  119.073 1.00 37.65 ? 573  LYS   A N     1 
ATOM   4194  C  CA    . LYS   A  1  575  ? -41.312 85.310  119.461 1.00 35.87 ? 573  LYS   A CA    1 
ATOM   4195  C  C     . LYS   A  1  575  ? -39.809 85.051  119.547 1.00 35.13 ? 573  LYS   A C     1 
ATOM   4196  O  O     . LYS   A  1  575  ? -39.209 84.965  120.622 1.00 35.40 ? 573  LYS   A O     1 
ATOM   4197  C  CB    . LYS   A  1  575  ? -41.887 85.847  120.767 1.00 38.31 ? 573  LYS   A CB    1 
ATOM   4198  N  N     . TRP   A  1  576  ? -39.196 84.935  118.374 1.00 31.49 ? 574  TRP   A N     1 
ATOM   4199  C  CA    . TRP   A  1  576  ? -37.782 84.601  118.279 1.00 27.83 ? 574  TRP   A CA    1 
ATOM   4200  C  C     . TRP   A  1  576  ? -36.923 85.731  118.832 1.00 25.35 ? 574  TRP   A C     1 
ATOM   4201  O  O     . TRP   A  1  576  ? -37.105 86.898  118.473 1.00 28.62 ? 574  TRP   A O     1 
ATOM   4202  C  CB    . TRP   A  1  576  ? -37.413 84.380  116.818 1.00 27.97 ? 574  TRP   A CB    1 
ATOM   4203  C  CG    . TRP   A  1  576  ? -38.095 83.218  116.166 1.00 27.22 ? 574  TRP   A CG    1 
ATOM   4204  C  CD1   . TRP   A  1  576  ? -39.075 83.267  115.209 1.00 24.71 ? 574  TRP   A CD1   1 
ATOM   4205  C  CD2   . TRP   A  1  576  ? -37.846 81.834  116.416 1.00 25.43 ? 574  TRP   A CD2   1 
ATOM   4206  N  NE1   . TRP   A  1  576  ? -39.444 81.996  114.850 1.00 27.81 ? 574  TRP   A NE1   1 
ATOM   4207  C  CE2   . TRP   A  1  576  ? -38.703 81.097  115.574 1.00 25.20 ? 574  TRP   A CE2   1 
ATOM   4208  C  CE3   . TRP   A  1  576  ? -36.979 81.145  117.269 1.00 25.16 ? 574  TRP   A CE3   1 
ATOM   4209  C  CZ2   . TRP   A  1  576  ? -38.714 79.698  115.555 1.00 27.27 ? 574  TRP   A CZ2   1 
ATOM   4210  C  CZ3   . TRP   A  1  576  ? -36.988 79.758  117.249 1.00 26.00 ? 574  TRP   A CZ3   1 
ATOM   4211  C  CH2   . TRP   A  1  576  ? -37.854 79.049  116.399 1.00 30.48 ? 574  TRP   A CH2   1 
ATOM   4212  N  N     . THR   A  1  577  ? -35.976 85.386  119.698 1.00 26.26 ? 575  THR   A N     1 
ATOM   4213  C  CA    . THR   A  1  577  ? -35.021 86.363  120.199 1.00 28.47 ? 575  THR   A CA    1 
ATOM   4214  C  C     . THR   A  1  577  ? -33.627 85.756  120.235 1.00 29.82 ? 575  THR   A C     1 
ATOM   4215  O  O     . THR   A  1  577  ? -33.443 84.535  120.202 1.00 28.86 ? 575  THR   A O     1 
ATOM   4216  C  CB    . THR   A  1  577  ? -35.370 86.902  121.603 1.00 29.44 ? 575  THR   A CB    1 
ATOM   4217  O  OG1   . THR   A  1  577  ? -35.324 85.831  122.553 1.00 31.82 ? 575  THR   A OG1   1 
ATOM   4218  C  CG2   . THR   A  1  577  ? -36.748 87.543  121.613 1.00 31.64 ? 575  THR   A CG2   1 
ATOM   4219  N  N     . ALA   A  1  578  ? -32.640 86.644  120.283 1.00 27.93 ? 576  ALA   A N     1 
ATOM   4220  C  CA    . ALA   A  1  578  ? -31.246 86.290  120.488 1.00 25.76 ? 576  ALA   A CA    1 
ATOM   4221  C  C     . ALA   A  1  578  ? -30.700 87.242  121.534 1.00 30.46 ? 576  ALA   A C     1 
ATOM   4222  O  O     . ALA   A  1  578  ? -30.791 88.461  121.369 1.00 28.90 ? 576  ALA   A O     1 
ATOM   4223  C  CB    . ALA   A  1  578  ? -30.447 86.444  119.189 1.00 27.46 ? 576  ALA   A CB    1 
ATOM   4224  N  N     . LEU   A  1  579  ? -30.149 86.694  122.605 1.00 28.86 ? 577  LEU   A N     1 
ATOM   4225  C  CA    . LEU   A  1  579  ? -29.656 87.481  123.722 1.00 28.95 ? 577  LEU   A CA    1 
ATOM   4226  C  C     . LEU   A  1  579  ? -28.218 87.087  124.003 1.00 31.47 ? 577  LEU   A C     1 
ATOM   4227  O  O     . LEU   A  1  579  ? -27.790 85.978  123.661 1.00 28.58 ? 577  LEU   A O     1 
ATOM   4228  C  CB    . LEU   A  1  579  ? -30.494 87.237  124.988 1.00 28.86 ? 577  LEU   A CB    1 
ATOM   4229  C  CG    . LEU   A  1  579  ? -32.013 87.347  124.871 1.00 34.42 ? 577  LEU   A CG    1 
ATOM   4230  C  CD1   . LEU   A  1  579  ? -32.632 87.112  126.237 1.00 35.29 ? 577  LEU   A CD1   1 
ATOM   4231  C  CD2   . LEU   A  1  579  ? -32.421 88.701  124.318 1.00 37.35 ? 577  LEU   A CD2   1 
ATOM   4232  N  N     . PRO   A  1  580  ? -27.438 87.982  124.614 1.00 29.90 ? 578  PRO   A N     1 
ATOM   4233  C  CA    . PRO   A  1  580  ? -26.124 87.576  125.115 1.00 27.59 ? 578  PRO   A CA    1 
ATOM   4234  C  C     . PRO   A  1  580  ? -26.325 86.582  126.241 1.00 34.77 ? 578  PRO   A C     1 
ATOM   4235  O  O     . PRO   A  1  580  ? -26.757 86.949  127.338 1.00 35.26 ? 578  PRO   A O     1 
ATOM   4236  C  CB    . PRO   A  1  580  ? -25.512 88.889  125.622 1.00 34.73 ? 578  PRO   A CB    1 
ATOM   4237  C  CG    . PRO   A  1  580  ? -26.364 89.986  125.023 1.00 32.32 ? 578  PRO   A CG    1 
ATOM   4238  C  CD    . PRO   A  1  580  ? -27.725 89.397  124.899 1.00 31.52 ? 578  PRO   A CD    1 
ATOM   4239  N  N     . GLN   A  1  581  ? -26.061 85.311  125.957 1.00 27.12 ? 579  GLN   A N     1 
ATOM   4240  C  CA    . GLN   A  1  581  ? -26.266 84.233  126.916 1.00 29.86 ? 579  GLN   A CA    1 
ATOM   4241  C  C     . GLN   A  1  581  ? -24.917 83.924  127.551 1.00 31.10 ? 579  GLN   A C     1 
ATOM   4242  O  O     . GLN   A  1  581  ? -24.189 83.030  127.130 1.00 30.28 ? 579  GLN   A O     1 
ATOM   4243  C  CB    . GLN   A  1  581  ? -26.852 83.010  126.225 1.00 28.14 ? 579  GLN   A CB    1 
ATOM   4244  C  CG    . GLN   A  1  581  ? -28.212 83.240  125.599 1.00 29.45 ? 579  GLN   A CG    1 
ATOM   4245  C  CD    . GLN   A  1  581  ? -29.305 83.372  126.642 1.00 32.38 ? 579  GLN   A CD    1 
ATOM   4246  O  OE1   . GLN   A  1  581  ? -29.046 83.281  127.843 1.00 34.22 ? 579  GLN   A OE1   1 
ATOM   4247  N  NE2   . GLN   A  1  581  ? -30.540 83.586  126.189 1.00 31.50 ? 579  GLN   A NE2   1 
ATOM   4248  N  N     . LEU   A  1  582  ? -24.585 84.697  128.576 1.00 31.52 ? 580  LEU   A N     1 
ATOM   4249  C  CA    . LEU   A  1  582  ? -23.373 84.454  129.328 1.00 33.24 ? 580  LEU   A CA    1 
ATOM   4250  C  C     . LEU   A  1  582  ? -23.567 83.264  130.266 1.00 31.56 ? 580  LEU   A C     1 
ATOM   4251  O  O     . LEU   A  1  582  ? -24.679 82.761  130.458 1.00 35.34 ? 580  LEU   A O     1 
ATOM   4252  C  CB    . LEU   A  1  582  ? -22.955 85.712  130.090 1.00 31.11 ? 580  LEU   A CB    1 
ATOM   4253  C  CG    . LEU   A  1  582  ? -22.130 86.744  129.303 1.00 40.02 ? 580  LEU   A CG    1 
ATOM   4254  C  CD1   . LEU   A  1  582  ? -22.920 87.351  128.154 1.00 38.22 ? 580  LEU   A CD1   1 
ATOM   4255  C  CD2   . LEU   A  1  582  ? -21.625 87.844  130.221 1.00 42.93 ? 580  LEU   A CD2   1 
ATOM   4256  N  N     . ALA   A  1  583  ? -22.461 82.807  130.855 1.00 31.43 ? 581  ALA   A N     1 
ATOM   4257  C  CA    . ALA   A  1  583  ? -22.538 81.687  131.786 1.00 31.61 ? 581  ALA   A CA    1 
ATOM   4258  C  C     . ALA   A  1  583  ? -23.415 82.022  132.980 1.00 34.93 ? 581  ALA   A C     1 
ATOM   4259  O  O     . ALA   A  1  583  ? -23.981 81.122  133.609 1.00 42.84 ? 581  ALA   A O     1 
ATOM   4260  C  CB    . ALA   A  1  583  ? -21.138 81.310  132.265 1.00 31.54 ? 581  ALA   A CB    1 
ATOM   4261  N  N     . THR   A  1  584  ? -23.541 83.306  133.297 1.00 33.69 ? 582  THR   A N     1 
ATOM   4262  C  CA    . THR   A  1  584  ? -24.292 83.793  134.444 1.00 39.77 ? 582  THR   A CA    1 
ATOM   4263  C  C     . THR   A  1  584  ? -25.754 84.070  134.121 1.00 42.66 ? 582  THR   A C     1 
ATOM   4264  O  O     . THR   A  1  584  ? -26.509 84.465  135.019 1.00 42.97 ? 582  THR   A O     1 
ATOM   4265  C  CB    . THR   A  1  584  ? -23.638 85.074  134.969 1.00 41.32 ? 582  THR   A CB    1 
ATOM   4266  O  OG1   . THR   A  1  584  ? -23.432 85.979  133.877 1.00 43.10 ? 582  THR   A OG1   1 
ATOM   4267  C  CG2   . THR   A  1  584  ? -22.303 84.768  135.619 1.00 40.27 ? 582  THR   A CG2   1 
ATOM   4268  N  N     . GLY   A  1  585  ? -26.168 83.881  132.872 1.00 39.22 ? 583  GLY   A N     1 
ATOM   4269  C  CA    . GLY   A  1  585  ? -27.522 84.164  132.461 1.00 38.53 ? 583  GLY   A CA    1 
ATOM   4270  C  C     . GLY   A  1  585  ? -27.567 85.204  131.360 1.00 40.21 ? 583  GLY   A C     1 
ATOM   4271  O  O     . GLY   A  1  585  ? -26.540 85.773  130.975 1.00 39.51 ? 583  GLY   A O     1 
ATOM   4272  N  N     . PRO   A  1  586  ? -28.764 85.479  130.837 1.00 37.60 ? 584  PRO   A N     1 
ATOM   4273  C  CA    . PRO   A  1  586  ? -28.890 86.484  129.774 1.00 35.74 ? 584  PRO   A CA    1 
ATOM   4274  C  C     . PRO   A  1  586  ? -28.402 87.840  130.255 1.00 42.37 ? 584  PRO   A C     1 
ATOM   4275  O  O     . PRO   A  1  586  ? -28.592 88.212  131.413 1.00 39.77 ? 584  PRO   A O     1 
ATOM   4276  C  CB    . PRO   A  1  586  ? -30.397 86.516  129.488 1.00 41.60 ? 584  PRO   A CB    1 
ATOM   4277  C  CG    . PRO   A  1  586  ? -30.968 85.301  130.160 1.00 43.88 ? 584  PRO   A CG    1 
ATOM   4278  C  CD    . PRO   A  1  586  ? -30.073 84.987  131.299 1.00 40.02 ? 584  PRO   A CD    1 
ATOM   4279  N  N     . ALA   A  1  587  ? -27.764 88.580  129.356 1.00 37.19 ? 585  ALA   A N     1 
ATOM   4280  C  CA    . ALA   A  1  587  ? -27.224 89.890  129.679 1.00 39.71 ? 585  ALA   A CA    1 
ATOM   4281  C  C     . ALA   A  1  587  ? -27.994 90.963  128.926 1.00 41.57 ? 585  ALA   A C     1 
ATOM   4282  O  O     . ALA   A  1  587  ? -28.560 90.711  127.861 1.00 39.98 ? 585  ALA   A O     1 
ATOM   4283  C  CB    . ALA   A  1  587  ? -25.735 89.977  129.328 1.00 41.14 ? 585  ALA   A CB    1 
ATOM   4284  N  N     . ALA   A  1  588  ? -28.034 92.160  129.499 1.00 41.97 ? 586  ALA   A N     1 
ATOM   4285  C  CA    . ALA   A  1  588  ? -28.705 93.258  128.826 1.00 40.24 ? 586  ALA   A CA    1 
ATOM   4286  C  C     . ALA   A  1  588  ? -27.796 93.857  127.759 1.00 40.17 ? 586  ALA   A C     1 
ATOM   4287  O  O     . ALA   A  1  588  ? -26.580 93.644  127.744 1.00 44.25 ? 586  ALA   A O     1 
ATOM   4288  C  CB    . ALA   A  1  588  ? -29.101 94.339  129.828 1.00 38.41 ? 586  ALA   A CB    1 
ATOM   4289  N  N     . GLY   A  1  589  ? -28.402 94.628  126.865 1.00 38.70 ? 587  GLY   A N     1 
ATOM   4290  C  CA    . GLY   A  1  589  ? -27.649 95.262  125.805 1.00 38.32 ? 587  GLY   A CA    1 
ATOM   4291  C  C     . GLY   A  1  589  ? -28.582 95.986  124.858 1.00 41.23 ? 587  GLY   A C     1 
ATOM   4292  O  O     . GLY   A  1  589  ? -29.786 96.098  125.105 1.00 41.92 ? 587  GLY   A O     1 
ATOM   4293  N  N     . GLU   A  1  590  ? -27.997 96.478  123.768 1.00 41.12 ? 588  GLU   A N     1 
ATOM   4294  C  CA    . GLU   A  1  590  ? -28.774 97.184  122.758 1.00 40.49 ? 588  GLU   A CA    1 
ATOM   4295  C  C     . GLU   A  1  590  ? -29.631 96.192  121.982 1.00 38.45 ? 588  GLU   A C     1 
ATOM   4296  O  O     . GLU   A  1  590  ? -29.126 95.201  121.446 1.00 35.46 ? 588  GLU   A O     1 
ATOM   4297  C  CB    . GLU   A  1  590  ? -27.840 97.934  121.808 1.00 41.55 ? 588  GLU   A CB    1 
ATOM   4298  N  N     . THR   A  1  591  ? -30.931 96.463  121.922 1.00 35.82 ? 589  THR   A N     1 
ATOM   4299  C  CA    . THR   A  1  591  ? -31.896 95.566  121.303 1.00 34.28 ? 589  THR   A CA    1 
ATOM   4300  C  C     . THR   A  1  591  ? -32.440 96.193  120.027 1.00 34.85 ? 589  THR   A C     1 
ATOM   4301  O  O     . THR   A  1  591  ? -32.732 97.390  119.984 1.00 37.61 ? 589  THR   A O     1 
ATOM   4302  C  CB    . THR   A  1  591  ? -33.039 95.271  122.280 1.00 40.71 ? 589  THR   A CB    1 
ATOM   4303  O  OG1   . THR   A  1  591  ? -32.526 94.561  123.419 1.00 39.27 ? 589  THR   A OG1   1 
ATOM   4304  C  CG2   . THR   A  1  591  ? -34.117 94.442  121.615 1.00 35.41 ? 589  THR   A CG2   1 
ATOM   4305  N  N     . ARG   A  1  592  ? -32.554 95.383  118.975 1.00 31.74 ? 590  ARG   A N     1 
ATOM   4306  C  CA    . ARG   A  1  592  ? -33.142 95.848  117.729 1.00 35.58 ? 590  ARG   A CA    1 
ATOM   4307  C  C     . ARG   A  1  592  ? -33.882 94.687  117.090 1.00 34.43 ? 590  ARG   A C     1 
ATOM   4308  O  O     . ARG   A  1  592  ? -33.684 93.525  117.455 1.00 32.21 ? 590  ARG   A O     1 
ATOM   4309  C  CB    . ARG   A  1  592  ? -32.080 96.381  116.761 1.00 35.76 ? 590  ARG   A CB    1 
ATOM   4310  C  CG    . ARG   A  1  592  ? -31.150 95.305  116.240 1.00 35.59 ? 590  ARG   A CG    1 
ATOM   4311  C  CD    . ARG   A  1  592  ? -30.366 95.770  115.025 1.00 38.86 ? 590  ARG   A CD    1 
ATOM   4312  N  NE    . ARG   A  1  592  ? -29.320 94.813  114.685 1.00 41.11 ? 590  ARG   A NE    1 
ATOM   4313  C  CZ    . ARG   A  1  592  ? -29.517 93.716  113.967 1.00 39.70 ? 590  ARG   A CZ    1 
ATOM   4314  N  NH1   . ARG   A  1  592  ? -30.705 93.427  113.460 1.00 37.58 ? 590  ARG   A NH1   1 
ATOM   4315  N  NH2   . ARG   A  1  592  ? -28.498 92.886  113.758 1.00 37.53 ? 590  ARG   A NH2   1 
ATOM   4316  N  N     . THR   A  1  593  ? -34.740 95.013  116.128 1.00 33.67 ? 591  THR   A N     1 
ATOM   4317  C  CA    . THR   A  1  593  ? -35.474 93.978  115.427 1.00 34.32 ? 591  THR   A CA    1 
ATOM   4318  C  C     . THR   A  1  593  ? -34.604 93.332  114.352 1.00 33.38 ? 591  THR   A C     1 
ATOM   4319  O  O     . THR   A  1  593  ? -33.634 93.911  113.854 1.00 34.12 ? 591  THR   A O     1 
ATOM   4320  C  CB    . THR   A  1  593  ? -36.718 94.558  114.766 1.00 35.84 ? 591  THR   A CB    1 
ATOM   4321  O  OG1   . THR   A  1  593  ? -36.335 95.645  113.917 1.00 36.36 ? 591  THR   A OG1   1 
ATOM   4322  C  CG2   . THR   A  1  593  ? -37.707 95.041  115.817 1.00 34.37 ? 591  THR   A CG2   1 
ATOM   4323  N  N     . VAL   A  1  594  ? -34.964 92.103  114.010 1.00 28.41 ? 592  VAL   A N     1 
ATOM   4324  C  CA    . VAL   A  1  594  ? -34.387 91.386  112.883 1.00 27.83 ? 592  VAL   A CA    1 
ATOM   4325  C  C     . VAL   A  1  594  ? -35.469 91.344  111.814 1.00 29.57 ? 592  VAL   A C     1 
ATOM   4326  O  O     . VAL   A  1  594  ? -36.592 90.903  112.084 1.00 29.58 ? 592  VAL   A O     1 
ATOM   4327  C  CB    . VAL   A  1  594  ? -33.947 89.973  113.294 1.00 26.70 ? 592  VAL   A CB    1 
ATOM   4328  C  CG1   . VAL   A  1  594  ? -33.350 89.220  112.100 1.00 25.33 ? 592  VAL   A CG1   1 
ATOM   4329  C  CG2   . VAL   A  1  594  ? -32.928 90.038  114.435 1.00 30.89 ? 592  VAL   A CG2   1 
ATOM   4330  N  N     . LEU   A  1  595  ? -35.151 91.826  110.616 1.00 27.87 ? 593  LEU   A N     1 
ATOM   4331  C  CA    . LEU   A  1  595  ? -36.142 91.948  109.553 1.00 28.43 ? 593  LEU   A CA    1 
ATOM   4332  C  C     . LEU   A  1  595  ? -35.882 90.916  108.463 1.00 25.90 ? 593  LEU   A C     1 
ATOM   4333  O  O     . LEU   A  1  595  ? -34.735 90.545  108.194 1.00 29.78 ? 593  LEU   A O     1 
ATOM   4334  C  CB    . LEU   A  1  595  ? -36.133 93.356  108.942 1.00 28.48 ? 593  LEU   A CB    1 
ATOM   4335  C  CG    . LEU   A  1  595  ? -36.366 94.531  109.892 1.00 30.63 ? 593  LEU   A CG    1 
ATOM   4336  C  CD1   . LEU   A  1  595  ? -36.471 95.847  109.126 1.00 33.58 ? 593  LEU   A CD1   1 
ATOM   4337  C  CD2   . LEU   A  1  595  ? -37.608 94.294  110.734 1.00 30.75 ? 593  LEU   A CD2   1 
ATOM   4338  N  N     . ASN   A  1  596  ? -36.962 90.453  107.844 1.00 25.18 ? 594  ASN   A N     1 
ATOM   4339  C  CA    . ASN   A  1  596  ? -36.861 89.500  106.744 1.00 24.59 ? 594  ASN   A CA    1 
ATOM   4340  C  C     . ASN   A  1  596  ? -36.197 90.203  105.567 1.00 22.67 ? 594  ASN   A C     1 
ATOM   4341  O  O     . ASN   A  1  596  ? -36.705 91.236  105.114 1.00 25.14 ? 594  ASN   A O     1 
ATOM   4342  C  CB    . ASN   A  1  596  ? -38.282 89.064  106.371 1.00 24.56 ? 594  ASN   A CB    1 
ATOM   4343  C  CG    . ASN   A  1  596  ? -38.318 87.977  105.298 1.00 26.43 ? 594  ASN   A CG    1 
ATOM   4344  O  OD1   . ASN   A  1  596  ? -37.455 87.907  104.428 1.00 25.49 ? 594  ASN   A OD1   1 
ATOM   4345  N  ND2   . ASN   A  1  596  ? -39.340 87.131  105.361 1.00 26.75 ? 594  ASN   A ND2   1 
ATOM   4346  N  N     . PRO   A  1  597  ? -35.069 89.703  105.051 1.00 25.44 ? 595  PRO   A N     1 
ATOM   4347  C  CA    . PRO   A  1  597  ? -34.399 90.407  103.944 1.00 22.48 ? 595  PRO   A CA    1 
ATOM   4348  C  C     . PRO   A  1  597  ? -35.242 90.494  102.691 1.00 24.41 ? 595  PRO   A C     1 
ATOM   4349  O  O     . PRO   A  1  597  ? -35.008 91.380  101.857 1.00 23.65 ? 595  PRO   A O     1 
ATOM   4350  C  CB    . PRO   A  1  597  ? -33.128 89.579  103.711 1.00 24.70 ? 595  PRO   A CB    1 
ATOM   4351  C  CG    . PRO   A  1  597  ? -33.445 88.230  104.271 1.00 23.96 ? 595  PRO   A CG    1 
ATOM   4352  C  CD    . PRO   A  1  597  ? -34.350 88.480  105.446 1.00 22.35 ? 595  PRO   A CD    1 
ATOM   4353  N  N     . GLY   A  1  598  ? -36.224 89.617  102.538 1.00 21.02 ? 596  GLY   A N     1 
ATOM   4354  C  CA    . GLY   A  1  598  ? -37.093 89.658  101.380 1.00 20.50 ? 596  GLY   A CA    1 
ATOM   4355  C  C     . GLY   A  1  598  ? -38.291 90.558  101.533 1.00 25.02 ? 596  GLY   A C     1 
ATOM   4356  O  O     . GLY   A  1  598  ? -39.032 90.762  100.567 1.00 26.54 ? 596  GLY   A O     1 
ATOM   4357  N  N     . ASP   A  1  599  ? -38.482 91.114  102.725 1.00 24.22 ? 597  ASP   A N     1 
ATOM   4358  C  CA    . ASP   A  1  599  ? -39.610 91.993  103.000 1.00 25.78 ? 597  ASP   A CA    1 
ATOM   4359  C  C     . ASP   A  1  599  ? -39.389 92.594  104.374 1.00 25.78 ? 597  ASP   A C     1 
ATOM   4360  O  O     . ASP   A  1  599  ? -39.683 91.952  105.389 1.00 24.67 ? 597  ASP   A O     1 
ATOM   4361  C  CB    . ASP   A  1  599  ? -40.917 91.208  103.000 1.00 26.23 ? 597  ASP   A CB    1 
ATOM   4362  C  CG    . ASP   A  1  599  ? -42.139 92.102  103.048 1.00 30.74 ? 597  ASP   A CG    1 
ATOM   4363  O  OD1   . ASP   A  1  599  ? -42.012 93.278  103.454 1.00 28.72 ? 597  ASP   A OD1   1 
ATOM   4364  O  OD2   . ASP   A  1  599  ? -43.225 91.623  102.672 1.00 31.80 ? 597  ASP   A OD2   1 
ATOM   4365  N  N     . HIS   A  1  600  ? -38.879 93.821  104.414 1.00 24.61 ? 598  HIS   A N     1 
ATOM   4366  C  CA    . HIS   A  1  600  ? -38.521 94.430  105.688 1.00 28.92 ? 598  HIS   A CA    1 
ATOM   4367  C  C     . HIS   A  1  600  ? -39.727 94.689  106.585 1.00 31.04 ? 598  HIS   A C     1 
ATOM   4368  O  O     . HIS   A  1  600  ? -39.543 94.936  107.782 1.00 33.81 ? 598  HIS   A O     1 
ATOM   4369  C  CB    . HIS   A  1  600  ? -37.705 95.703  105.463 1.00 30.93 ? 598  HIS   A CB    1 
ATOM   4370  C  CG    . HIS   A  1  600  ? -36.315 95.442  104.967 1.00 32.23 ? 598  HIS   A CG    1 
ATOM   4371  N  ND1   . HIS   A  1  600  ? -35.417 96.453  104.699 1.00 35.45 ? 598  HIS   A ND1   1 
ATOM   4372  C  CD2   . HIS   A  1  600  ? -35.668 94.283  104.691 1.00 29.07 ? 598  HIS   A CD2   1 
ATOM   4373  C  CE1   . HIS   A  1  600  ? -34.278 95.930  104.281 1.00 32.72 ? 598  HIS   A CE1   1 
ATOM   4374  N  NE2   . HIS   A  1  600  ? -34.404 94.614  104.265 1.00 32.29 ? 598  HIS   A NE2   1 
ATOM   4375  N  N     . ARG   A  1  601  ? -40.942 94.621  106.043 1.00 27.75 ? 599  ARG   A N     1 
ATOM   4376  C  CA    . ARG   A  1  601  ? -42.144 94.731  106.858 1.00 28.63 ? 599  ARG   A CA    1 
ATOM   4377  C  C     . ARG   A  1  601  ? -42.368 93.500  107.723 1.00 33.23 ? 599  ARG   A C     1 
ATOM   4378  O  O     . ARG   A  1  601  ? -43.151 93.564  108.678 1.00 32.74 ? 599  ARG   A O     1 
ATOM   4379  C  CB    . ARG   A  1  601  ? -43.356 94.933  105.953 1.00 29.17 ? 599  ARG   A CB    1 
ATOM   4380  C  CG    . ARG   A  1  601  ? -43.259 96.155  105.063 1.00 31.86 ? 599  ARG   A CG    1 
ATOM   4381  C  CD    . ARG   A  1  601  ? -44.343 96.129  104.004 1.00 31.27 ? 599  ARG   A CD    1 
ATOM   4382  N  NE    . ARG   A  1  601  ? -44.314 94.881  103.252 1.00 31.76 ? 599  ARG   A NE    1 
ATOM   4383  C  CZ    . ARG   A  1  601  ? -45.215 94.533  102.345 1.00 35.86 ? 599  ARG   A CZ    1 
ATOM   4384  N  NH1   . ARG   A  1  601  ? -46.240 95.321  102.047 1.00 32.80 ? 599  ARG   A NH1   1 
ATOM   4385  N  NH2   . ARG   A  1  601  ? -45.087 93.364  101.723 1.00 33.31 ? 599  ARG   A NH2   1 
ATOM   4386  N  N     . ASP   A  1  602  ? -41.709 92.387  107.407 1.00 28.85 ? 600  ASP   A N     1 
ATOM   4387  C  CA    . ASP   A  1  602  ? -41.863 91.143  108.155 1.00 30.36 ? 600  ASP   A CA    1 
ATOM   4388  C  C     . ASP   A  1  602  ? -40.798 91.115  109.241 1.00 31.22 ? 600  ASP   A C     1 
ATOM   4389  O  O     . ASP   A  1  602  ? -39.641 90.783  108.985 1.00 28.59 ? 600  ASP   A O     1 
ATOM   4390  C  CB    . ASP   A  1  602  ? -41.729 89.942  107.226 1.00 29.11 ? 600  ASP   A CB    1 
ATOM   4391  C  CG    . ASP   A  1  602  ? -41.904 88.621  107.949 1.00 32.68 ? 600  ASP   A CG    1 
ATOM   4392  O  OD1   . ASP   A  1  602  ? -42.522 88.612  109.031 1.00 31.68 ? 600  ASP   A OD1   1 
ATOM   4393  O  OD2   . ASP   A  1  602  ? -41.408 87.589  107.446 1.00 29.65 ? 600  ASP   A OD2   1 
ATOM   4394  N  N     . VAL   A  1  603  ? -41.187 91.461  110.463 1.00 29.15 ? 601  VAL   A N     1 
ATOM   4395  C  CA    . VAL   A  1  603  ? -40.269 91.401  111.594 1.00 30.70 ? 601  VAL   A CA    1 
ATOM   4396  C  C     . VAL   A  1  603  ? -40.176 89.952  112.053 1.00 29.17 ? 601  VAL   A C     1 
ATOM   4397  O  O     . VAL   A  1  603  ? -41.191 89.329  112.385 1.00 31.45 ? 601  VAL   A O     1 
ATOM   4398  C  CB    . VAL   A  1  603  ? -40.738 92.319  112.730 1.00 31.05 ? 601  VAL   A CB    1 
ATOM   4399  C  CG1   . VAL   A  1  603  ? -39.768 92.263  113.893 1.00 31.76 ? 601  VAL   A CG1   1 
ATOM   4400  C  CG2   . VAL   A  1  603  ? -40.883 93.739  112.225 1.00 35.98 ? 601  VAL   A CG2   1 
ATOM   4401  N  N     . VAL   A  1  604  ? -38.961 89.411  112.063 1.00 26.49 ? 602  VAL   A N     1 
ATOM   4402  C  CA    . VAL   A  1  604  ? -38.749 88.006  112.397 1.00 25.66 ? 602  VAL   A CA    1 
ATOM   4403  C  C     . VAL   A  1  604  ? -38.495 87.828  113.883 1.00 27.40 ? 602  VAL   A C     1 
ATOM   4404  O  O     . VAL   A  1  604  ? -38.923 86.841  114.488 1.00 28.97 ? 602  VAL   A O     1 
ATOM   4405  C  CB    . VAL   A  1  604  ? -37.592 87.422  111.562 1.00 25.38 ? 602  VAL   A CB    1 
ATOM   4406  C  CG1   . VAL   A  1  604  ? -37.451 85.944  111.862 1.00 26.58 ? 602  VAL   A CG1   1 
ATOM   4407  C  CG2   . VAL   A  1  604  ? -37.832 87.654  110.075 1.00 25.32 ? 602  VAL   A CG2   1 
ATOM   4408  N  N     . GLY   A  1  605  ? -37.803 88.777  114.488 1.00 26.62 ? 603  GLY   A N     1 
ATOM   4409  C  CA    . GLY   A  1  605  ? -37.510 88.668  115.894 1.00 28.12 ? 603  GLY   A CA    1 
ATOM   4410  C  C     . GLY   A  1  605  ? -36.728 89.859  116.378 1.00 27.47 ? 603  GLY   A C     1 
ATOM   4411  O  O     . GLY   A  1  605  ? -36.690 90.907  115.732 1.00 30.84 ? 603  GLY   A O     1 
ATOM   4412  N  N     . SER   A  1  606  ? -36.086 89.676  117.526 1.00 28.57 ? 604  SER   A N     1 
ATOM   4413  C  CA    A SER   A  1  606  ? -35.336 90.744  118.161 0.56 28.80 ? 604  SER   A CA    1 
ATOM   4414  C  CA    B SER   A  1  606  ? -35.351 90.740  118.186 0.44 28.82 ? 604  SER   A CA    1 
ATOM   4415  C  C     . SER   A  1  606  ? -34.030 90.186  118.693 1.00 30.50 ? 604  SER   A C     1 
ATOM   4416  O  O     . SER   A  1  606  ? -33.990 89.085  119.250 1.00 33.30 ? 604  SER   A O     1 
ATOM   4417  C  CB    A SER   A  1  606  ? -36.135 91.375  119.306 0.56 28.50 ? 604  SER   A CB    1 
ATOM   4418  C  CB    B SER   A  1  606  ? -36.165 91.274  119.366 0.44 28.50 ? 604  SER   A CB    1 
ATOM   4419  O  OG    A SER   A  1  606  ? -37.291 92.020  118.804 0.56 28.03 ? 604  SER   A OG    1 
ATOM   4420  O  OG    B SER   A  1  606  ? -35.362 92.066  120.210 0.44 28.85 ? 604  SER   A OG    1 
ATOM   4421  N  N     . VAL   A  1  607  ? -32.956 90.941  118.496 1.00 27.29 ? 605  VAL   A N     1 
ATOM   4422  C  CA    . VAL   A  1  607  ? -31.637 90.561  118.984 1.00 28.48 ? 605  VAL   A CA    1 
ATOM   4423  C  C     . VAL   A  1  607  ? -31.160 91.610  119.974 1.00 30.44 ? 605  VAL   A C     1 
ATOM   4424  O  O     . VAL   A  1  607  ? -31.253 92.815  119.708 1.00 30.13 ? 605  VAL   A O     1 
ATOM   4425  C  CB    . VAL   A  1  607  ? -30.620 90.374  117.841 1.00 28.36 ? 605  VAL   A CB    1 
ATOM   4426  C  CG1   . VAL   A  1  607  ? -30.528 91.627  116.971 1.00 31.18 ? 605  VAL   A CG1   1 
ATOM   4427  C  CG2   . VAL   A  1  607  ? -29.248 90.010  118.406 1.00 28.21 ? 605  VAL   A CG2   1 
ATOM   4428  N  N     . THR   A  1  608  ? -30.665 91.152  121.116 1.00 27.58 ? 606  THR   A N     1 
ATOM   4429  C  CA    . THR   A  1  608  ? -29.957 92.004  122.056 1.00 31.04 ? 606  THR   A CA    1 
ATOM   4430  C  C     . THR   A  1  608  ? -28.472 91.754  121.838 1.00 29.06 ? 606  THR   A C     1 
ATOM   4431  O  O     . THR   A  1  608  ? -28.004 90.617  121.971 1.00 29.50 ? 606  THR   A O     1 
ATOM   4432  C  CB    . THR   A  1  608  ? -30.371 91.663  123.486 1.00 32.07 ? 606  THR   A CB    1 
ATOM   4433  O  OG1   . THR   A  1  608  ? -31.788 91.848  123.622 1.00 31.98 ? 606  THR   A OG1   1 
ATOM   4434  C  CG2   . THR   A  1  608  ? -29.660 92.569  124.480 1.00 34.34 ? 606  THR   A CG2   1 
ATOM   4435  N  N     . GLU   A  1  609  ? -27.743 92.796  121.460 1.00 30.05 ? 607  GLU   A N     1 
ATOM   4436  C  CA    . GLU   A  1  609  ? -26.339 92.632  121.118 1.00 31.91 ? 607  GLU   A CA    1 
ATOM   4437  C  C     . GLU   A  1  609  ? -25.429 92.792  122.335 1.00 33.46 ? 607  GLU   A C     1 
ATOM   4438  O  O     . GLU   A  1  609  ? -25.783 93.426  123.334 1.00 30.44 ? 607  GLU   A O     1 
ATOM   4439  C  CB    . GLU   A  1  609  ? -25.953 93.545  119.947 1.00 33.33 ? 607  GLU   A CB    1 
ATOM   4440  C  CG    . GLU   A  1  609  ? -26.633 93.062  118.649 1.00 37.47 ? 607  GLU   A CG    1 
ATOM   4441  C  CD    . GLU   A  1  609  ? -26.255 93.835  117.390 1.00 42.79 ? 607  GLU   A CD    1 
ATOM   4442  O  OE1   . GLU   A  1  609  ? -25.979 95.051  117.485 1.00 48.25 ? 607  GLU   A OE1   1 
ATOM   4443  O  OE2   . GLU   A  1  609  ? -26.256 93.216  116.295 1.00 41.30 ? 607  GLU   A OE2   1 
ATOM   4444  N  N     . THR   A  1  610  ? -24.263 92.169  122.251 1.00 31.66 ? 608  THR   A N     1 
ATOM   4445  C  CA    . THR   A  1  610  ? -23.350 92.047  123.377 1.00 32.05 ? 608  THR   A CA    1 
ATOM   4446  C  C     . THR   A  1  610  ? -22.460 93.277  123.457 1.00 35.43 ? 608  THR   A C     1 
ATOM   4447  O  O     . THR   A  1  610  ? -21.911 93.730  122.450 1.00 36.20 ? 608  THR   A O     1 
ATOM   4448  C  CB    . THR   A  1  610  ? -22.467 90.812  123.174 1.00 32.88 ? 608  THR   A CB    1 
ATOM   4449  O  OG1   . THR   A  1  610  ? -23.292 89.661  122.955 1.00 31.03 ? 608  THR   A OG1   1 
ATOM   4450  C  CG2   . THR   A  1  610  ? -21.573 90.564  124.380 1.00 32.25 ? 608  THR   A CG2   1 
ATOM   4451  N  N     . SER   A  1  611  ? -22.310 93.814  124.662 1.00 33.31 ? 609  SER   A N     1 
ATOM   4452  C  CA    . SER   A  1  611  ? -21.331 94.866  124.859 1.00 35.81 ? 609  SER   A CA    1 
ATOM   4453  C  C     . SER   A  1  611  ? -19.933 94.267  124.846 1.00 36.65 ? 609  SER   A C     1 
ATOM   4454  O  O     . SER   A  1  611  ? -19.732 93.093  125.171 1.00 35.51 ? 609  SER   A O     1 
ATOM   4455  C  CB    . SER   A  1  611  ? -21.566 95.562  126.197 1.00 38.45 ? 609  SER   A CB    1 
ATOM   4456  O  OG    . SER   A  1  611  ? -21.135 94.749  127.273 1.00 39.61 ? 609  SER   A OG    1 
ATOM   4457  N  N     . GLU   A  1  612  ? -18.958 95.084  124.448 1.00 37.40 ? 610  GLU   A N     1 
ATOM   4458  C  CA    . GLU   A  1  612  ? -17.577 94.620  124.465 1.00 37.94 ? 610  GLU   A CA    1 
ATOM   4459  C  C     . GLU   A  1  612  ? -17.133 94.239  125.872 1.00 38.00 ? 610  GLU   A C     1 
ATOM   4460  O  O     . GLU   A  1  612  ? -16.338 93.306  126.040 1.00 37.30 ? 610  GLU   A O     1 
ATOM   4461  C  CB    . GLU   A  1  612  ? -16.661 95.670  123.833 1.00 43.67 ? 610  GLU   A CB    1 
ATOM   4462  C  CG    . GLU   A  1  612  ? -16.588 95.577  122.308 1.00 47.69 ? 610  GLU   A CG    1 
ATOM   4463  C  CD    . GLU   A  1  612  ? -16.477 96.932  121.631 1.00 51.93 ? 610  GLU   A CD    1 
ATOM   4464  O  OE1   . GLU   A  1  612  ? -17.501 97.647  121.554 1.00 58.76 ? 610  GLU   A OE1   1 
ATOM   4465  O  OE2   . GLU   A  1  612  ? -15.367 97.287  121.179 1.00 56.24 ? 610  GLU   A OE2   1 
ATOM   4466  N  N     . GLU   A  1  613  ? -17.657 94.922  126.893 1.00 40.50 ? 611  GLU   A N     1 
ATOM   4467  C  CA    . GLU   A  1  613  ? -17.373 94.531  128.270 1.00 41.59 ? 611  GLU   A CA    1 
ATOM   4468  C  C     . GLU   A  1  613  ? -17.869 93.117  128.550 1.00 35.73 ? 611  GLU   A C     1 
ATOM   4469  O  O     . GLU   A  1  613  ? -17.146 92.296  129.123 1.00 33.16 ? 611  GLU   A O     1 
ATOM   4470  C  CB    . GLU   A  1  613  ? -17.999 95.529  129.245 1.00 43.91 ? 611  GLU   A CB    1 
ATOM   4471  N  N     . ASP   A  1  614  ? -19.104 92.810  128.138 1.00 34.99 ? 612  ASP   A N     1 
ATOM   4472  C  CA    . ASP   A  1  614  ? -19.659 91.485  128.397 1.00 31.66 ? 612  ASP   A CA    1 
ATOM   4473  C  C     . ASP   A  1  614  ? -18.992 90.416  127.541 1.00 32.93 ? 612  ASP   A C     1 
ATOM   4474  O  O     . ASP   A  1  614  ? -18.911 89.255  127.957 1.00 30.32 ? 612  ASP   A O     1 
ATOM   4475  C  CB    . ASP   A  1  614  ? -21.168 91.483  128.166 1.00 36.99 ? 612  ASP   A CB    1 
ATOM   4476  C  CG    . ASP   A  1  614  ? -21.926 92.244  129.244 1.00 37.13 ? 612  ASP   A CG    1 
ATOM   4477  O  OD1   . ASP   A  1  614  ? -21.461 92.268  130.406 1.00 41.63 ? 612  ASP   A OD1   1 
ATOM   4478  O  OD2   . ASP   A  1  614  ? -22.988 92.819  128.925 1.00 43.56 ? 612  ASP   A OD2   1 
ATOM   4479  N  N     . ALA   A  1  615  ? -18.525 90.779  126.347 1.00 30.88 ? 613  ALA   A N     1 
ATOM   4480  C  CA    . ALA   A  1  615  ? -17.758 89.829  125.550 1.00 29.06 ? 613  ALA   A CA    1 
ATOM   4481  C  C     . ALA   A  1  615  ? -16.490 89.418  126.282 1.00 30.28 ? 613  ALA   A C     1 
ATOM   4482  O  O     . ALA   A  1  615  ? -16.173 88.228  126.377 1.00 29.21 ? 613  ALA   A O     1 
ATOM   4483  C  CB    . ALA   A  1  615  ? -17.427 90.424  124.182 1.00 29.98 ? 613  ALA   A CB    1 
ATOM   4484  N  N     . ARG   A  1  616  ? -15.764 90.395  126.833 1.00 31.94 ? 614  ARG   A N     1 
ATOM   4485  C  CA    . ARG   A  1  616  ? -14.574 90.069  127.614 1.00 34.70 ? 614  ARG   A CA    1 
ATOM   4486  C  C     . ARG   A  1  616  ? -14.934 89.277  128.863 1.00 30.72 ? 614  ARG   A C     1 
ATOM   4487  O  O     . ARG   A  1  616  ? -14.241 88.317  129.219 1.00 29.50 ? 614  ARG   A O     1 
ATOM   4488  C  CB    . ARG   A  1  616  ? -13.803 91.341  127.961 1.00 38.16 ? 614  ARG   A CB    1 
ATOM   4489  C  CG    . ARG   A  1  616  ? -12.876 91.793  126.842 1.00 39.75 ? 614  ARG   A CG    1 
ATOM   4490  C  CD    . ARG   A  1  616  ? -12.060 93.016  127.219 1.00 45.10 ? 614  ARG   A CD    1 
ATOM   4491  N  NE    . ARG   A  1  616  ? -12.886 94.201  127.410 1.00 50.25 ? 614  ARG   A NE    1 
ATOM   4492  C  CZ    . ARG   A  1  616  ? -13.352 94.955  126.423 1.00 49.21 ? 614  ARG   A CZ    1 
ATOM   4493  N  NH1   . ARG   A  1  616  ? -13.130 94.649  125.155 1.00 49.80 ? 614  ARG   A NH1   1 
ATOM   4494  N  NH2   . ARG   A  1  616  ? -14.057 96.043  126.717 1.00 47.17 ? 614  ARG   A NH2   1 
ATOM   4495  N  N     . ARG   A  1  617  ? -16.040 89.637  129.515 1.00 29.36 ? 615  ARG   A N     1 
ATOM   4496  C  CA    . ARG   A  1  617  ? -16.477 88.876  130.679 1.00 30.24 ? 615  ARG   A CA    1 
ATOM   4497  C  C     . ARG   A  1  617  ? -16.798 87.434  130.306 1.00 32.56 ? 615  ARG   A C     1 
ATOM   4498  O  O     . ARG   A  1  617  ? -16.482 86.506  131.058 1.00 31.56 ? 615  ARG   A O     1 
ATOM   4499  C  CB    . ARG   A  1  617  ? -17.685 89.555  131.318 1.00 35.70 ? 615  ARG   A CB    1 
ATOM   4500  C  CG    . ARG   A  1  617  ? -18.096 88.945  132.630 1.00 41.08 ? 615  ARG   A CG    1 
ATOM   4501  C  CD    . ARG   A  1  617  ? -18.858 89.954  133.465 1.00 42.83 ? 615  ARG   A CD    1 
ATOM   4502  N  NE    . ARG   A  1  617  ? -20.063 90.437  132.801 1.00 41.30 ? 615  ARG   A NE    1 
ATOM   4503  C  CZ    . ARG   A  1  617  ? -21.263 89.888  132.941 1.00 48.61 ? 615  ARG   A CZ    1 
ATOM   4504  N  NH1   . ARG   A  1  617  ? -21.445 88.804  133.680 1.00 51.82 ? 615  ARG   A NH1   1 
ATOM   4505  N  NH2   . ARG   A  1  617  ? -22.307 90.443  132.330 1.00 47.43 ? 615  ARG   A NH2   1 
ATOM   4506  N  N     . ALA   A  1  618  ? -17.422 87.227  129.141 1.00 28.65 ? 616  ALA   A N     1 
ATOM   4507  C  CA    . ALA   A  1  618  ? -17.758 85.871  128.715 1.00 30.25 ? 616  ALA   A CA    1 
ATOM   4508  C  C     . ALA   A  1  618  ? -16.507 85.019  128.541 1.00 26.95 ? 616  ALA   A C     1 
ATOM   4509  O  O     . ALA   A  1  618  ? -16.489 83.841  128.922 1.00 27.87 ? 616  ALA   A O     1 
ATOM   4510  C  CB    . ALA   A  1  618  ? -18.578 85.907  127.424 1.00 29.26 ? 616  ALA   A CB    1 
ATOM   4511  N  N     . VAL   A  1  619  ? -15.444 85.597  127.982 1.00 27.35 ? 617  VAL   A N     1 
ATOM   4512  C  CA    . VAL   A  1  619  ? -14.207 84.840  127.819 1.00 28.13 ? 617  VAL   A CA    1 
ATOM   4513  C  C     . VAL   A  1  619  ? -13.633 84.460  129.176 1.00 28.33 ? 617  VAL   A C     1 
ATOM   4514  O  O     . VAL   A  1  619  ? -13.167 83.333  129.373 1.00 30.32 ? 617  VAL   A O     1 
ATOM   4515  C  CB    . VAL   A  1  619  ? -13.198 85.608  126.943 1.00 30.44 ? 617  VAL   A CB    1 
ATOM   4516  C  CG1   . VAL   A  1  619  ? -11.885 84.831  126.826 1.00 30.46 ? 617  VAL   A CG1   1 
ATOM   4517  C  CG2   . VAL   A  1  619  ? -13.785 85.851  125.562 1.00 27.43 ? 617  VAL   A CG2   1 
ATOM   4518  N  N     . ARG   A  1  620  ? -13.684 85.383  130.140 1.00 28.69 ? 618  ARG   A N     1 
ATOM   4519  C  CA    . ARG   A  1  620  ? -13.191 85.062  131.473 1.00 32.58 ? 618  ARG   A CA    1 
ATOM   4520  C  C     . ARG   A  1  620  ? -14.007 83.940  132.100 1.00 29.35 ? 618  ARG   A C     1 
ATOM   4521  O  O     . ARG   A  1  620  ? -13.445 83.021  132.708 1.00 34.30 ? 618  ARG   A O     1 
ATOM   4522  C  CB    . ARG   A  1  620  ? -13.185 86.313  132.353 1.00 34.60 ? 618  ARG   A CB    1 
ATOM   4523  C  CG    . ARG   A  1  620  ? -12.047 87.269  132.023 1.00 38.64 ? 618  ARG   A CG    1 
ATOM   4524  C  CD    . ARG   A  1  620  ? -12.007 88.479  132.960 1.00 46.11 ? 618  ARG   A CD    1 
ATOM   4525  N  NE    . ARG   A  1  620  ? -12.650 89.645  132.363 1.00 49.87 ? 618  ARG   A NE    1 
ATOM   4526  C  CZ    . ARG   A  1  620  ? -13.771 90.201  132.802 1.00 46.02 ? 618  ARG   A CZ    1 
ATOM   4527  N  NH1   . ARG   A  1  620  ? -14.388 89.756  133.887 1.00 49.21 ? 618  ARG   A NH1   1 
ATOM   4528  N  NH2   . ARG   A  1  620  ? -14.281 91.237  132.141 1.00 50.23 ? 618  ARG   A NH2   1 
ATOM   4529  N  N     . LEU   A  1  621  ? -15.330 83.977  131.925 1.00 27.41 ? 619  LEU   A N     1 
ATOM   4530  C  CA    . LEU   A  1  621  ? -16.179 82.911  132.448 1.00 29.97 ? 619  LEU   A CA    1 
ATOM   4531  C  C     . LEU   A  1  621  ? -15.896 81.587  131.749 1.00 30.67 ? 619  LEU   A C     1 
ATOM   4532  O  O     . LEU   A  1  621  ? -15.868 80.533  132.397 1.00 30.51 ? 619  LEU   A O     1 
ATOM   4533  C  CB    . LEU   A  1  621  ? -17.647 83.288  132.291 1.00 30.86 ? 619  LEU   A CB    1 
ATOM   4534  C  CG    . LEU   A  1  621  ? -18.155 84.472  133.110 1.00 34.08 ? 619  LEU   A CG    1 
ATOM   4535  C  CD1   . LEU   A  1  621  ? -19.498 84.954  132.574 1.00 32.20 ? 619  LEU   A CD1   1 
ATOM   4536  C  CD2   . LEU   A  1  621  ? -18.276 84.080  134.569 1.00 35.22 ? 619  LEU   A CD2   1 
ATOM   4537  N  N     . ALA   A  1  622  ? -15.699 81.620  130.427 1.00 29.29 ? 620  ALA   A N     1 
ATOM   4538  C  CA    . ALA   A  1  622  ? -15.313 80.413  129.701 1.00 27.97 ? 620  ALA   A CA    1 
ATOM   4539  C  C     . ALA   A  1  622  ? -14.013 79.840  130.244 1.00 27.86 ? 620  ALA   A C     1 
ATOM   4540  O  O     . ALA   A  1  622  ? -13.885 78.621  130.408 1.00 31.01 ? 620  ALA   A O     1 
ATOM   4541  C  CB    . ALA   A  1  622  ? -15.168 80.714  128.211 1.00 28.06 ? 620  ALA   A CB    1 
ATOM   4542  N  N     . ALA   A  1  623  ? -13.035 80.704  130.525 1.00 27.39 ? 621  ALA   A N     1 
ATOM   4543  C  CA    . ALA   A  1  623  ? -11.761 80.233  131.057 1.00 29.36 ? 621  ALA   A CA    1 
ATOM   4544  C  C     . ALA   A  1  623  ? -11.940 79.593  132.427 1.00 28.79 ? 621  ALA   A C     1 
ATOM   4545  O  O     . ALA   A  1  623  ? -11.365 78.535  132.705 1.00 32.20 ? 621  ALA   A O     1 
ATOM   4546  C  CB    . ALA   A  1  623  ? -10.761 81.386  131.123 1.00 31.35 ? 621  ALA   A CB    1 
ATOM   4547  N  N     . ASP   A  1  624  ? -12.746 80.213  133.293 1.00 29.76 ? 622  ASP   A N     1 
ATOM   4548  C  CA    . ASP   A  1  624  ? -12.983 79.637  134.613 1.00 36.01 ? 622  ASP   A CA    1 
ATOM   4549  C  C     . ASP   A  1  624  ? -13.709 78.304  134.510 1.00 33.18 ? 622  ASP   A C     1 
ATOM   4550  O  O     . ASP   A  1  624  ? -13.500 77.417  135.345 1.00 39.72 ? 622  ASP   A O     1 
ATOM   4551  C  CB    . ASP   A  1  624  ? -13.789 80.609  135.475 1.00 40.08 ? 622  ASP   A CB    1 
ATOM   4552  C  CG    . ASP   A  1  624  ? -13.034 81.896  135.764 1.00 45.75 ? 622  ASP   A CG    1 
ATOM   4553  O  OD1   . ASP   A  1  624  ? -11.787 81.853  135.851 1.00 52.18 ? 622  ASP   A OD1   1 
ATOM   4554  O  OD2   . ASP   A  1  624  ? -13.690 82.951  135.903 1.00 48.12 ? 622  ASP   A OD2   1 
ATOM   4555  N  N     . ALA   A  1  625  ? -14.543 78.142  133.487 1.00 36.00 ? 623  ALA   A N     1 
ATOM   4556  C  CA    . ALA   A  1  625  ? -15.330 76.937  133.288 1.00 38.51 ? 623  ALA   A CA    1 
ATOM   4557  C  C     . ALA   A  1  625  ? -14.601 75.864  132.501 1.00 36.96 ? 623  ALA   A C     1 
ATOM   4558  O  O     . ALA   A  1  625  ? -15.091 74.732  132.434 1.00 40.14 ? 623  ALA   A O     1 
ATOM   4559  C  CB    . ALA   A  1  625  ? -16.611 77.277  132.530 1.00 38.90 ? 623  ALA   A CB    1 
ATOM   4560  N  N     . ALA   A  1  626  ? -13.469 76.193  131.885 1.00 34.26 ? 624  ALA   A N     1 
ATOM   4561  C  CA    . ALA   A  1  626  ? -12.788 75.239  131.011 1.00 29.70 ? 624  ALA   A CA    1 
ATOM   4562  C  C     . ALA   A  1  626  ? -12.487 73.904  131.683 1.00 33.58 ? 624  ALA   A C     1 
ATOM   4563  O  O     . ALA   A  1  626  ? -12.789 72.861  131.081 1.00 33.05 ? 624  ALA   A O     1 
ATOM   4564  C  CB    . ALA   A  1  626  ? -11.555 75.896  130.375 1.00 31.97 ? 624  ALA   A CB    1 
ATOM   4565  N  N     . PRO   A  1  627  ? -11.916 73.850  132.897 1.00 35.13 ? 625  PRO   A N     1 
ATOM   4566  C  CA    . PRO   A  1  627  ? -11.639 72.534  133.506 1.00 35.91 ? 625  PRO   A CA    1 
ATOM   4567  C  C     . PRO   A  1  627  ? -12.865 71.651  133.649 1.00 35.62 ? 625  PRO   A C     1 
ATOM   4568  O  O     . PRO   A  1  627  ? -12.791 70.446  133.372 1.00 36.91 ? 625  PRO   A O     1 
ATOM   4569  C  CB    . PRO   A  1  627  ? -11.045 72.901  134.874 1.00 35.73 ? 625  PRO   A CB    1 
ATOM   4570  C  CG    . PRO   A  1  627  ? -10.468 74.263  134.677 1.00 37.89 ? 625  PRO   A CG    1 
ATOM   4571  C  CD    . PRO   A  1  627  ? -11.412 74.953  133.737 1.00 36.57 ? 625  PRO   A CD    1 
ATOM   4572  N  N     . ASP   A  1  628  ? -13.994 72.222  134.075 1.00 32.06 ? 626  ASP   A N     1 
ATOM   4573  C  CA    . ASP   A  1  628  ? -15.194 71.425  134.293 1.00 37.23 ? 626  ASP   A CA    1 
ATOM   4574  C  C     . ASP   A  1  628  ? -15.680 70.800  132.993 1.00 36.92 ? 626  ASP   A C     1 
ATOM   4575  O  O     . ASP   A  1  628  ? -16.175 69.667  132.986 1.00 36.66 ? 626  ASP   A O     1 
ATOM   4576  C  CB    . ASP   A  1  628  ? -16.291 72.303  134.892 1.00 35.65 ? 626  ASP   A CB    1 
ATOM   4577  C  CG    . ASP   A  1  628  ? -15.847 72.999  136.166 1.00 44.45 ? 626  ASP   A CG    1 
ATOM   4578  O  OD1   . ASP   A  1  628  ? -14.836 73.734  136.122 1.00 45.85 ? 626  ASP   A OD1   1 
ATOM   4579  O  OD2   . ASP   A  1  628  ? -16.513 72.813  137.202 1.00 51.76 ? 626  ASP   A OD2   1 
ATOM   4580  N  N     . TRP   A  1  629  ? -15.559 71.528  131.884 1.00 31.16 ? 627  TRP   A N     1 
ATOM   4581  C  CA    . TRP   A  1  629  ? -16.037 70.988  130.621 1.00 31.53 ? 627  TRP   A CA    1 
ATOM   4582  C  C     . TRP   A  1  629  ? -15.050 69.979  130.049 1.00 29.52 ? 627  TRP   A C     1 
ATOM   4583  O  O     . TRP   A  1  629  ? -15.460 68.943  129.518 1.00 29.94 ? 627  TRP   A O     1 
ATOM   4584  C  CB    . TRP   A  1  629  ? -16.322 72.122  129.638 1.00 30.27 ? 627  TRP   A CB    1 
ATOM   4585  C  CG    . TRP   A  1  629  ? -16.785 71.628  128.313 1.00 28.66 ? 627  TRP   A CG    1 
ATOM   4586  C  CD1   . TRP   A  1  629  ? -16.179 71.828  127.104 1.00 25.34 ? 627  TRP   A CD1   1 
ATOM   4587  C  CD2   . TRP   A  1  629  ? -17.926 70.804  128.058 1.00 26.38 ? 627  TRP   A CD2   1 
ATOM   4588  N  NE1   . TRP   A  1  629  ? -16.889 71.201  126.113 1.00 25.23 ? 627  TRP   A NE1   1 
ATOM   4589  C  CE2   . TRP   A  1  629  ? -17.968 70.568  126.670 1.00 24.61 ? 627  TRP   A CE2   1 
ATOM   4590  C  CE3   . TRP   A  1  629  ? -18.933 70.267  128.865 1.00 24.94 ? 627  TRP   A CE3   1 
ATOM   4591  C  CZ2   . TRP   A  1  629  ? -18.967 69.806  126.069 1.00 25.58 ? 627  TRP   A CZ2   1 
ATOM   4592  C  CZ3   . TRP   A  1  629  ? -19.924 69.508  128.265 1.00 28.29 ? 627  TRP   A CZ3   1 
ATOM   4593  C  CH2   . TRP   A  1  629  ? -19.930 69.283  126.881 1.00 26.81 ? 627  TRP   A CH2   1 
ATOM   4594  N  N     . ALA   A  1  630  ? -13.746 70.255  130.166 1.00 29.72 ? 628  ALA   A N     1 
ATOM   4595  C  CA    . ALA   A  1  630  ? -12.753 69.287  129.717 1.00 30.90 ? 628  ALA   A CA    1 
ATOM   4596  C  C     . ALA   A  1  630  ? -12.877 67.978  130.480 1.00 33.55 ? 628  ALA   A C     1 
ATOM   4597  O  O     . ALA   A  1  630  ? -12.505 66.916  129.963 1.00 33.64 ? 628  ALA   A O     1 
ATOM   4598  C  CB    . ALA   A  1  630  ? -11.343 69.860  129.878 1.00 29.49 ? 628  ALA   A CB    1 
ATOM   4599  N  N     . ALA   A  1  631  ? -13.405 68.034  131.703 1.00 31.86 ? 629  ALA   A N     1 
ATOM   4600  C  CA    . ALA   A  1  631  ? -13.539 66.844  132.531 1.00 34.81 ? 629  ALA   A CA    1 
ATOM   4601  C  C     . ALA   A  1  631  ? -14.713 65.967  132.124 1.00 35.41 ? 629  ALA   A C     1 
ATOM   4602  O  O     . ALA   A  1  631  ? -14.777 64.806  132.543 1.00 34.23 ? 629  ALA   A O     1 
ATOM   4603  C  CB    . ALA   A  1  631  ? -13.652 67.232  134.008 1.00 36.56 ? 629  ALA   A CB    1 
ATOM   4604  N  N     . VAL   A  1  632  ? -15.643 66.482  131.326 1.00 32.14 ? 630  VAL   A N     1 
ATOM   4605  C  CA    . VAL   A  1  632  ? -16.720 65.643  130.812 1.00 29.59 ? 630  VAL   A CA    1 
ATOM   4606  C  C     . VAL   A  1  632  ? -16.074 64.718  129.791 1.00 27.93 ? 630  VAL   A C     1 
ATOM   4607  O  O     . VAL   A  1  632  ? -15.441 65.210  128.851 1.00 28.51 ? 630  VAL   A O     1 
ATOM   4608  C  CB    . VAL   A  1  632  ? -17.847 66.490  130.204 1.00 31.39 ? 630  VAL   A CB    1 
ATOM   4609  C  CG1   . VAL   A  1  632  ? -18.926 65.603  129.578 1.00 29.08 ? 630  VAL   A CG1   1 
ATOM   4610  C  CG2   . VAL   A  1  632  ? -18.442 67.402  131.275 1.00 30.70 ? 630  VAL   A CG2   1 
ATOM   4611  N  N     . PRO   A  1  633  ? -16.175 63.397  129.947 1.00 29.25 ? 631  PRO   A N     1 
ATOM   4612  C  CA    . PRO   A  1  633  ? -15.435 62.501  129.061 1.00 26.79 ? 631  PRO   A CA    1 
ATOM   4613  C  C     . PRO   A  1  633  ? -15.851 62.719  127.615 1.00 27.85 ? 631  PRO   A C     1 
ATOM   4614  O  O     . PRO   A  1  633  ? -17.003 63.092  127.335 1.00 27.21 ? 631  PRO   A O     1 
ATOM   4615  C  CB    . PRO   A  1  633  ? -15.843 61.104  129.550 1.00 30.21 ? 631  PRO   A CB    1 
ATOM   4616  C  CG    . PRO   A  1  633  ? -16.351 61.310  130.934 1.00 33.43 ? 631  PRO   A CG    1 
ATOM   4617  C  CD    . PRO   A  1  633  ? -16.987 62.660  130.927 1.00 32.90 ? 631  PRO   A CD    1 
ATOM   4618  N  N     . PRO   A  1  634  ? -14.931 62.516  126.669 1.00 23.64 ? 632  PRO   A N     1 
ATOM   4619  C  CA    . PRO   A  1  634  ? -15.289 62.717  125.254 1.00 24.15 ? 632  PRO   A CA    1 
ATOM   4620  C  C     . PRO   A  1  634  ? -16.561 62.002  124.833 1.00 24.11 ? 632  PRO   A C     1 
ATOM   4621  O  O     . PRO   A  1  634  ? -17.342 62.564  124.062 1.00 24.14 ? 632  PRO   A O     1 
ATOM   4622  C  CB    . PRO   A  1  634  ? -14.063 62.187  124.495 1.00 25.91 ? 632  PRO   A CB    1 
ATOM   4623  C  CG    . PRO   A  1  634  ? -12.936 62.319  125.460 1.00 26.71 ? 632  PRO   A CG    1 
ATOM   4624  C  CD    . PRO   A  1  634  ? -13.515 62.146  126.847 1.00 25.94 ? 632  PRO   A CD    1 
ATOM   4625  N  N     . SER   A  1  635  ? -16.782 60.773  125.314 1.00 26.36 ? 633  SER   A N     1 
ATOM   4626  C  CA    . SER   A  1  635  ? -17.981 60.031  124.930 1.00 26.89 ? 633  SER   A CA    1 
ATOM   4627  C  C     . SER   A  1  635  ? -19.244 60.764  125.357 1.00 25.11 ? 633  SER   A C     1 
ATOM   4628  O  O     . SER   A  1  635  ? -20.232 60.801  124.610 1.00 24.77 ? 633  SER   A O     1 
ATOM   4629  C  CB    . SER   A  1  635  ? -17.946 58.625  125.530 1.00 34.45 ? 633  SER   A CB    1 
ATOM   4630  N  N     . GLU   A  1  636  ? -19.230 61.364  126.550 1.00 25.54 ? 634  GLU   A N     1 
ATOM   4631  C  CA    . GLU   A  1  636  ? -20.400 62.104  127.004 1.00 29.47 ? 634  GLU   A CA    1 
ATOM   4632  C  C     . GLU   A  1  636  ? -20.539 63.438  126.286 1.00 26.51 ? 634  GLU   A C     1 
ATOM   4633  O  O     . GLU   A  1  636  ? -21.662 63.869  126.011 1.00 27.42 ? 634  GLU   A O     1 
ATOM   4634  C  CB    . GLU   A  1  636  ? -20.385 62.288  128.522 1.00 31.37 ? 634  GLU   A CB    1 
ATOM   4635  C  CG    . GLU   A  1  636  ? -21.574 63.089  129.048 1.00 37.67 ? 634  GLU   A CG    1 
ATOM   4636  C  CD    . GLU   A  1  636  ? -22.916 62.555  128.549 1.00 42.86 ? 634  GLU   A CD    1 
ATOM   4637  O  OE1   . GLU   A  1  636  ? -23.135 61.327  128.637 1.00 45.22 ? 634  GLU   A OE1   1 
ATOM   4638  O  OE2   . GLU   A  1  636  ? -23.747 63.357  128.055 1.00 38.32 ? 634  GLU   A OE2   1 
ATOM   4639  N  N     . ARG   A  1  637  ? -19.427 64.097  125.961 1.00 26.43 ? 635  ARG   A N     1 
ATOM   4640  C  CA    . ARG   A  1  637  ? -19.508 65.271  125.099 1.00 22.11 ? 635  ARG   A CA    1 
ATOM   4641  C  C     . ARG   A  1  637  ? -20.125 64.914  123.752 1.00 23.21 ? 635  ARG   A C     1 
ATOM   4642  O  O     . ARG   A  1  637  ? -21.002 65.626  123.249 1.00 23.30 ? 635  ARG   A O     1 
ATOM   4643  C  CB    . ARG   A  1  637  ? -18.120 65.894  124.929 1.00 22.38 ? 635  ARG   A CB    1 
ATOM   4644  C  CG    . ARG   A  1  637  ? -17.488 66.249  126.276 1.00 25.58 ? 635  ARG   A CG    1 
ATOM   4645  C  CD    . ARG   A  1  637  ? -16.337 67.234  126.148 1.00 26.29 ? 635  ARG   A CD    1 
ATOM   4646  N  NE    . ARG   A  1  637  ? -15.281 66.761  125.271 1.00 25.59 ? 635  ARG   A NE    1 
ATOM   4647  C  CZ    . ARG   A  1  637  ? -14.082 66.352  125.667 1.00 28.94 ? 635  ARG   A CZ    1 
ATOM   4648  N  NH1   . ARG   A  1  637  ? -13.768 66.260  126.949 1.00 28.18 ? 635  ARG   A NH1   1 
ATOM   4649  N  NH2   . ARG   A  1  637  ? -13.170 66.040  124.752 1.00 24.48 ? 635  ARG   A NH2   1 
ATOM   4650  N  N     . ALA   A  1  638  ? -19.679 63.803  123.153 1.00 23.94 ? 636  ALA   A N     1 
ATOM   4651  C  CA    . ALA   A  1  638  ? -20.249 63.368  121.883 1.00 23.80 ? 636  ALA   A CA    1 
ATOM   4652  C  C     . ALA   A  1  638  ? -21.726 63.027  122.022 1.00 24.79 ? 636  ALA   A C     1 
ATOM   4653  O  O     . ALA   A  1  638  ? -22.504 63.245  121.088 1.00 22.20 ? 636  ALA   A O     1 
ATOM   4654  C  CB    . ALA   A  1  638  ? -19.479 62.160  121.347 1.00 23.32 ? 636  ALA   A CB    1 
ATOM   4655  N  N     . ALA   A  1  639  ? -22.129 62.487  123.174 1.00 22.32 ? 637  ALA   A N     1 
ATOM   4656  C  CA    . ALA   A  1  639  ? -23.543 62.200  123.392 1.00 23.70 ? 637  ALA   A CA    1 
ATOM   4657  C  C     . ALA   A  1  639  ? -24.374 63.478  123.384 1.00 24.39 ? 637  ALA   A C     1 
ATOM   4658  O  O     . ALA   A  1  639  ? -25.520 63.476  122.919 1.00 26.53 ? 637  ALA   A O     1 
ATOM   4659  C  CB    . ALA   A  1  639  ? -23.744 61.413  124.691 1.00 24.84 ? 637  ALA   A CB    1 
ATOM   4660  N  N     . CYS   A  1  640  ? -23.823 64.576  123.909 1.00 23.58 ? 638  CYS   A N     1 
ATOM   4661  C  CA    . CYS   A  1  640  ? -24.526 65.852  123.830 1.00 25.64 ? 638  CYS   A CA    1 
ATOM   4662  C  C     . CYS   A  1  640  ? -24.752 66.248  122.382 1.00 23.64 ? 638  CYS   A C     1 
ATOM   4663  O  O     . CYS   A  1  640  ? -25.845 66.688  122.007 1.00 23.98 ? 638  CYS   A O     1 
ATOM   4664  C  CB    . CYS   A  1  640  ? -23.739 66.951  124.535 1.00 25.82 ? 638  CYS   A CB    1 
ATOM   4665  S  SG    . CYS   A  1  640  ? -23.599 66.766  126.303 1.00 28.61 ? 638  CYS   A SG    1 
ATOM   4666  N  N     . LEU   A  1  641  ? -23.718 66.106  121.551 1.00 22.15 ? 639  LEU   A N     1 
ATOM   4667  C  CA    . LEU   A  1  641  ? -23.860 66.450  120.144 1.00 22.07 ? 639  LEU   A CA    1 
ATOM   4668  C  C     . LEU   A  1  641  ? -24.922 65.587  119.491 1.00 21.16 ? 639  LEU   A C     1 
ATOM   4669  O  O     . LEU   A  1  641  ? -25.757 66.089  118.728 1.00 22.29 ? 639  LEU   A O     1 
ATOM   4670  C  CB    . LEU   A  1  641  ? -22.525 66.277  119.422 1.00 21.61 ? 639  LEU   A CB    1 
ATOM   4671  C  CG    . LEU   A  1  641  ? -21.619 67.507  119.348 1.00 22.32 ? 639  LEU   A CG    1 
ATOM   4672  C  CD1   . LEU   A  1  641  ? -21.235 68.044  120.711 1.00 22.88 ? 639  LEU   A CD1   1 
ATOM   4673  C  CD2   . LEU   A  1  641  ? -20.382 67.186  118.540 1.00 21.46 ? 639  LEU   A CD2   1 
ATOM   4674  N  N     . ASP   A  1  642  ? -24.913 64.283  119.779 1.00 22.01 ? 640  ASP   A N     1 
ATOM   4675  C  CA    . ASP   A  1  642  ? -25.909 63.403  119.180 1.00 22.88 ? 640  ASP   A CA    1 
ATOM   4676  C  C     . ASP   A  1  642  ? -27.314 63.766  119.644 1.00 21.12 ? 640  ASP   A C     1 
ATOM   4677  O  O     . ASP   A  1  642  ? -28.263 63.719  118.855 1.00 22.51 ? 640  ASP   A O     1 
ATOM   4678  C  CB    . ASP   A  1  642  ? -25.595 61.942  119.489 1.00 23.67 ? 640  ASP   A CB    1 
ATOM   4679  C  CG    . ASP   A  1  642  ? -24.458 61.396  118.635 1.00 25.65 ? 640  ASP   A CG    1 
ATOM   4680  O  OD1   . ASP   A  1  642  ? -24.215 61.951  117.537 1.00 26.94 ? 640  ASP   A OD1   1 
ATOM   4681  O  OD2   . ASP   A  1  642  ? -23.826 60.411  119.061 1.00 28.08 ? 640  ASP   A OD2   1 
ATOM   4682  N  N     . ARG   A  1  643  ? -27.467 64.134  120.916 1.00 23.82 ? 641  ARG   A N     1 
ATOM   4683  C  CA    . ARG   A  1  643  ? -28.778 64.571  121.388 1.00 23.65 ? 641  ARG   A CA    1 
ATOM   4684  C  C     . ARG   A  1  643  ? -29.210 65.855  120.696 1.00 23.95 ? 641  ARG   A C     1 
ATOM   4685  O  O     . ARG   A  1  643  ? -30.390 66.022  120.360 1.00 24.75 ? 641  ARG   A O     1 
ATOM   4686  C  CB    . ARG   A  1  643  ? -28.772 64.750  122.905 1.00 24.71 ? 641  ARG   A CB    1 
ATOM   4687  C  CG    . ARG   A  1  643  ? -28.887 63.443  123.666 1.00 26.41 ? 641  ARG   A CG    1 
ATOM   4688  C  CD    . ARG   A  1  643  ? -29.093 63.687  125.155 1.00 28.95 ? 641  ARG   A CD    1 
ATOM   4689  N  NE    . ARG   A  1  643  ? -27.969 64.383  125.766 1.00 29.13 ? 641  ARG   A NE    1 
ATOM   4690  C  CZ    . ARG   A  1  643  ? -26.944 63.774  126.346 1.00 28.01 ? 641  ARG   A CZ    1 
ATOM   4691  N  NH1   . ARG   A  1  643  ? -26.848 62.455  126.368 1.00 29.41 ? 641  ARG   A NH1   1 
ATOM   4692  N  NH2   . ARG   A  1  643  ? -25.998 64.505  126.928 1.00 32.41 ? 641  ARG   A NH2   1 
ATOM   4693  N  N     . ALA   A  1  644  ? -28.274 66.781  120.483 1.00 21.53 ? 642  ALA   A N     1 
ATOM   4694  C  CA    . ALA   A  1  644  ? -28.609 68.000  119.759 1.00 22.95 ? 642  ALA   A CA    1 
ATOM   4695  C  C     . ALA   A  1  644  ? -29.048 67.687  118.339 1.00 21.82 ? 642  ALA   A C     1 
ATOM   4696  O  O     . ALA   A  1  644  ? -29.970 68.321  117.817 1.00 22.84 ? 642  ALA   A O     1 
ATOM   4697  C  CB    . ALA   A  1  644  ? -27.426 68.965  119.744 1.00 22.42 ? 642  ALA   A CB    1 
ATOM   4698  N  N     . ALA   A  1  645  ? -28.386 66.726  117.687 1.00 21.28 ? 643  ALA   A N     1 
ATOM   4699  C  CA    . ALA   A  1  645  ? -28.784 66.354  116.335 1.00 19.91 ? 643  ALA   A CA    1 
ATOM   4700  C  C     . ALA   A  1  645  ? -30.204 65.805  116.313 1.00 22.15 ? 643  ALA   A C     1 
ATOM   4701  O  O     . ALA   A  1  645  ? -30.993 66.133  115.415 1.00 21.96 ? 643  ALA   A O     1 
ATOM   4702  C  CB    . ALA   A  1  645  ? -27.802 65.332  115.764 1.00 20.60 ? 643  ALA   A CB    1 
ATOM   4703  N  N     . GLU   A  1  646  ? -30.539 64.952  117.282 1.00 22.92 ? 644  GLU   A N     1 
ATOM   4704  C  CA    . GLU   A  1  646  ? -31.905 64.449  117.379 1.00 24.31 ? 644  GLU   A CA    1 
ATOM   4705  C  C     . GLU   A  1  646  ? -32.891 65.589  117.573 1.00 24.33 ? 644  GLU   A C     1 
ATOM   4706  O  O     . GLU   A  1  646  ? -33.972 65.592  116.972 1.00 24.14 ? 644  GLU   A O     1 
ATOM   4707  C  CB    . GLU   A  1  646  ? -32.031 63.470  118.543 1.00 29.15 ? 644  GLU   A CB    1 
ATOM   4708  C  CG    . GLU   A  1  646  ? -31.350 62.133  118.351 1.00 34.35 ? 644  GLU   A CG    1 
ATOM   4709  C  CD    . GLU   A  1  646  ? -31.908 61.344  117.184 1.00 42.22 ? 644  GLU   A CD    1 
ATOM   4710  O  OE1   . GLU   A  1  646  ? -33.115 61.475  116.893 1.00 46.05 ? 644  GLU   A OE1   1 
ATOM   4711  O  OE2   . GLU   A  1  646  ? -31.133 60.593  116.555 1.00 43.52 ? 644  GLU   A OE2   1 
ATOM   4712  N  N     . LEU   A  1  647  ? -32.543 66.560  118.422 1.00 24.43 ? 645  LEU   A N     1 
ATOM   4713  C  CA    . LEU   A  1  647  ? -33.448 67.683  118.650 1.00 23.23 ? 645  LEU   A CA    1 
ATOM   4714  C  C     . LEU   A  1  647  ? -33.601 68.523  117.391 1.00 25.59 ? 645  LEU   A C     1 
ATOM   4715  O  O     . LEU   A  1  647  ? -34.705 68.980  117.069 1.00 27.05 ? 645  LEU   A O     1 
ATOM   4716  C  CB    . LEU   A  1  647  ? -32.944 68.535  119.811 1.00 25.78 ? 645  LEU   A CB    1 
ATOM   4717  C  CG    . LEU   A  1  647  ? -33.068 67.890  121.187 1.00 28.34 ? 645  LEU   A CG    1 
ATOM   4718  C  CD1   . LEU   A  1  647  ? -32.306 68.688  122.246 1.00 28.15 ? 645  LEU   A CD1   1 
ATOM   4719  C  CD2   . LEU   A  1  647  ? -34.546 67.761  121.567 1.00 31.07 ? 645  LEU   A CD2   1 
ATOM   4720  N  N     . MET   A  1  648  ? -32.506 68.739  116.663 1.00 24.13 ? 646  MET   A N     1 
ATOM   4721  C  CA    . MET   A  1  648  ? -32.605 69.510  115.432 1.00 22.66 ? 646  MET   A CA    1 
ATOM   4722  C  C     . MET   A  1  648  ? -33.423 68.774  114.387 1.00 22.97 ? 646  MET   A C     1 
ATOM   4723  O  O     . MET   A  1  648  ? -34.220 69.392  113.675 1.00 24.78 ? 646  MET   A O     1 
ATOM   4724  C  CB    . MET   A  1  648  ? -31.222 69.859  114.889 1.00 20.78 ? 646  MET   A CB    1 
ATOM   4725  C  CG    . MET   A  1  648  ? -30.573 70.992  115.625 1.00 27.35 ? 646  MET   A CG    1 
ATOM   4726  S  SD    . MET   A  1  648  ? -29.167 71.586  114.684 1.00 26.99 ? 646  MET   A SD    1 
ATOM   4727  C  CE    . MET   A  1  648  ? -28.473 72.723  115.868 1.00 28.75 ? 646  MET   A CE    1 
ATOM   4728  N  N     . GLN   A  1  649  ? -33.241 67.454  114.278 1.00 23.82 ? 647  GLN   A N     1 
ATOM   4729  C  CA    . GLN   A  1  649  ? -34.042 66.692  113.326 1.00 20.82 ? 647  GLN   A CA    1 
ATOM   4730  C  C     . GLN   A  1  649  ? -35.524 66.801  113.650 1.00 21.80 ? 647  GLN   A C     1 
ATOM   4731  O  O     . GLN   A  1  649  ? -36.353 66.986  112.749 1.00 25.91 ? 647  GLN   A O     1 
ATOM   4732  C  CB    . GLN   A  1  649  ? -33.615 65.226  113.327 1.00 23.91 ? 647  GLN   A CB    1 
ATOM   4733  C  CG    . GLN   A  1  649  ? -34.321 64.399  112.276 1.00 22.88 ? 647  GLN   A CG    1 
ATOM   4734  C  CD    . GLN   A  1  649  ? -33.768 64.633  110.889 1.00 22.36 ? 647  GLN   A CD    1 
ATOM   4735  O  OE1   . GLN   A  1  649  ? -32.665 64.190  110.565 1.00 23.06 ? 647  GLN   A OE1   1 
ATOM   4736  N  NE2   . GLN   A  1  649  ? -34.530 65.339  110.056 1.00 25.21 ? 647  GLN   A NE2   1 
ATOM   4737  N  N     . ALA   A  1  650  ? -35.872 66.702  114.930 1.00 23.39 ? 648  ALA   A N     1 
ATOM   4738  C  CA    . ALA   A  1  650  ? -37.274 66.777  115.322 1.00 24.46 ? 648  ALA   A CA    1 
ATOM   4739  C  C     . ALA   A  1  650  ? -37.837 68.166  115.074 1.00 28.10 ? 648  ALA   A C     1 
ATOM   4740  O  O     . ALA   A  1  650  ? -39.018 68.315  114.729 1.00 32.04 ? 648  ALA   A O     1 
ATOM   4741  C  CB    . ALA   A  1  650  ? -37.408 66.391  116.795 1.00 26.23 ? 648  ALA   A CB    1 
ATOM   4742  N  N     . ARG   A  1  651  ? -37.014 69.190  115.249 1.00 24.71 ? 649  ARG   A N     1 
ATOM   4743  C  CA    . ARG   A  1  651  ? -37.445 70.575  115.154 1.00 23.99 ? 649  ARG   A CA    1 
ATOM   4744  C  C     . ARG   A  1  651  ? -37.244 71.152  113.761 1.00 24.53 ? 649  ARG   A C     1 
ATOM   4745  O  O     . ARG   A  1  651  ? -37.509 72.340  113.551 1.00 25.40 ? 649  ARG   A O     1 
ATOM   4746  C  CB    . ARG   A  1  651  ? -36.703 71.419  116.197 1.00 26.90 ? 649  ARG   A CB    1 
ATOM   4747  C  CG    . ARG   A  1  651  ? -37.339 72.768  116.508 1.00 34.26 ? 649  ARG   A CG    1 
ATOM   4748  C  CD    . ARG   A  1  651  ? -37.133 73.163  117.969 1.00 32.23 ? 649  ARG   A CD    1 
ATOM   4749  N  NE    . ARG   A  1  651  ? -37.523 74.545  118.231 1.00 35.28 ? 649  ARG   A NE    1 
ATOM   4750  C  CZ    . ARG   A  1  651  ? -38.767 74.958  118.431 1.00 37.08 ? 649  ARG   A CZ    1 
ATOM   4751  N  NH1   . ARG   A  1  651  ? -39.795 74.132  118.330 1.00 38.87 ? 649  ARG   A NH1   1 
ATOM   4752  N  NH2   . ARG   A  1  651  ? -38.986 76.236  118.733 1.00 41.22 ? 649  ARG   A NH2   1 
ATOM   4753  N  N     . MET   A  1  652  ? -36.797 70.335  112.813 1.00 24.42 ? 650  MET   A N     1 
ATOM   4754  C  CA    . MET   A  1  652  ? -36.487 70.832  111.473 1.00 24.32 ? 650  MET   A CA    1 
ATOM   4755  C  C     . MET   A  1  652  ? -37.564 71.731  110.881 1.00 23.74 ? 650  MET   A C     1 
ATOM   4756  O  O     . MET   A  1  652  ? -37.221 72.825  110.413 1.00 23.00 ? 650  MET   A O     1 
ATOM   4757  C  CB    . MET   A  1  652  ? -36.107 69.689  110.524 1.00 25.11 ? 650  MET   A CB    1 
ATOM   4758  C  CG    . MET   A  1  652  ? -35.942 70.155  109.085 1.00 24.66 ? 650  MET   A CG    1 
ATOM   4759  S  SD    . MET   A  1  652  ? -35.465 68.829  107.965 1.00 26.63 ? 650  MET   A SD    1 
ATOM   4760  C  CE    . MET   A  1  652  ? -33.758 68.579  108.431 1.00 23.41 ? 650  MET   A CE    1 
ATOM   4761  N  N     . PRO   A  1  653  ? -38.856 71.365  110.882 1.00 24.83 ? 651  PRO   A N     1 
ATOM   4762  C  CA    . PRO   A  1  653  ? -39.850 72.251  110.252 1.00 27.26 ? 651  PRO   A CA    1 
ATOM   4763  C  C     . PRO   A  1  653  ? -39.865 73.651  110.835 1.00 25.06 ? 651  PRO   A C     1 
ATOM   4764  O  O     . PRO   A  1  653  ? -39.917 74.636  110.087 1.00 24.15 ? 651  PRO   A O     1 
ATOM   4765  C  CB    . PRO   A  1  653  ? -41.173 71.515  110.499 1.00 24.73 ? 651  PRO   A CB    1 
ATOM   4766  C  CG    . PRO   A  1  653  ? -40.781 70.076  110.549 1.00 29.10 ? 651  PRO   A CG    1 
ATOM   4767  C  CD    . PRO   A  1  653  ? -39.458 70.083  111.292 1.00 25.72 ? 651  PRO   A CD    1 
ATOM   4768  N  N     . THR   A  1  654  ? -39.805 73.761  112.160 1.00 22.86 ? 652  THR   A N     1 
ATOM   4769  C  CA    . THR   A  1  654  ? -39.740 75.073  112.788 1.00 23.32 ? 652  THR   A CA    1 
ATOM   4770  C  C     . THR   A  1  654  ? -38.447 75.790  112.425 1.00 25.44 ? 652  THR   A C     1 
ATOM   4771  O  O     . THR   A  1  654  ? -38.460 76.988  112.117 1.00 24.51 ? 652  THR   A O     1 
ATOM   4772  C  CB    . THR   A  1  654  ? -39.866 74.915  114.300 1.00 24.96 ? 652  THR   A CB    1 
ATOM   4773  O  OG1   . THR   A  1  654  ? -41.088 74.232  114.592 1.00 28.31 ? 652  THR   A OG1   1 
ATOM   4774  C  CG2   . THR   A  1  654  ? -39.855 76.275  114.983 1.00 27.34 ? 652  THR   A CG2   1 
ATOM   4775  N  N     . LEU   A  1  655  ? -37.320 75.072  112.443 1.00 23.06 ? 653  LEU   A N     1 
ATOM   4776  C  CA    . LEU   A  1  655  ? -36.057 75.688  112.060 1.00 23.28 ? 653  LEU   A CA    1 
ATOM   4777  C  C     . LEU   A  1  655  ? -36.094 76.187  110.620 1.00 26.82 ? 653  LEU   A C     1 
ATOM   4778  O  O     . LEU   A  1  655  ? -35.564 77.263  110.320 1.00 23.71 ? 653  LEU   A O     1 
ATOM   4779  C  CB    . LEU   A  1  655  ? -34.908 74.699  112.262 1.00 23.76 ? 653  LEU   A CB    1 
ATOM   4780  C  CG    . LEU   A  1  655  ? -34.705 74.226  113.699 1.00 23.55 ? 653  LEU   A CG    1 
ATOM   4781  C  CD1   . LEU   A  1  655  ? -33.598 73.190  113.786 1.00 26.68 ? 653  LEU   A CD1   1 
ATOM   4782  C  CD2   . LEU   A  1  655  ? -34.389 75.404  114.586 1.00 26.43 ? 653  LEU   A CD2   1 
ATOM   4783  N  N     . LEU   A  1  656  ? -36.713 75.418  109.713 1.00 24.33 ? 654  LEU   A N     1 
ATOM   4784  C  CA    . LEU   A  1  656  ? -36.833 75.862  108.326 1.00 22.84 ? 654  LEU   A CA    1 
ATOM   4785  C  C     . LEU   A  1  656  ? -37.502 77.225  108.247 1.00 26.25 ? 654  LEU   A C     1 
ATOM   4786  O  O     . LEU   A  1  656  ? -37.036 78.123  107.534 1.00 25.25 ? 654  LEU   A O     1 
ATOM   4787  C  CB    . LEU   A  1  656  ? -37.660 74.863  107.513 1.00 24.08 ? 654  LEU   A CB    1 
ATOM   4788  C  CG    . LEU   A  1  656  ? -37.171 73.426  107.400 1.00 25.76 ? 654  LEU   A CG    1 
ATOM   4789  C  CD1   . LEU   A  1  656  ? -38.038 72.685  106.409 1.00 25.90 ? 654  LEU   A CD1   1 
ATOM   4790  C  CD2   . LEU   A  1  656  ? -35.721 73.405  106.987 1.00 24.12 ? 654  LEU   A CD2   1 
ATOM   4791  N  N     . GLY   A  1  657  ? -38.616 77.388  108.958 1.00 24.70 ? 655  GLY   A N     1 
ATOM   4792  C  CA    . GLY   A  1  657  ? -39.343 78.637  108.868 1.00 26.54 ? 655  GLY   A CA    1 
ATOM   4793  C  C     . GLY   A  1  657  ? -38.511 79.814  109.321 1.00 22.56 ? 655  GLY   A C     1 
ATOM   4794  O  O     . GLY   A  1  657  ? -38.579 80.898  108.738 1.00 26.35 ? 655  GLY   A O     1 
ATOM   4795  N  N     . LEU   A  1  658  ? -37.723 79.621  110.381 1.00 23.19 ? 656  LEU   A N     1 
ATOM   4796  C  CA    . LEU   A  1  658  ? -36.886 80.705  110.868 1.00 23.09 ? 656  LEU   A CA    1 
ATOM   4797  C  C     . LEU   A  1  658  ? -35.797 81.032  109.854 1.00 22.59 ? 656  LEU   A C     1 
ATOM   4798  O  O     . LEU   A  1  658  ? -35.576 82.200  109.516 1.00 23.82 ? 656  LEU   A O     1 
ATOM   4799  C  CB    . LEU   A  1  658  ? -36.296 80.322  112.225 1.00 23.58 ? 656  LEU   A CB    1 
ATOM   4800  C  CG    . LEU   A  1  658  ? -35.374 81.352  112.871 1.00 25.61 ? 656  LEU   A CG    1 
ATOM   4801  C  CD1   . LEU   A  1  658  ? -36.081 82.690  113.003 1.00 26.32 ? 656  LEU   A CD1   1 
ATOM   4802  C  CD2   . LEU   A  1  658  ? -34.907 80.838  114.221 1.00 24.89 ? 656  LEU   A CD2   1 
ATOM   4803  N  N     . ILE   A  1  659  ? -35.139 80.001  109.329 1.00 23.16 ? 657  ILE   A N     1 
ATOM   4804  C  CA    . ILE   A  1  659  ? -34.090 80.206  108.341 1.00 21.01 ? 657  ILE   A CA    1 
ATOM   4805  C  C     . ILE   A  1  659  ? -34.651 80.870  107.089 1.00 22.07 ? 657  ILE   A C     1 
ATOM   4806  O  O     . ILE   A  1  659  ? -34.040 81.789  106.531 1.00 21.68 ? 657  ILE   A O     1 
ATOM   4807  C  CB    . ILE   A  1  659  ? -33.403 78.865  108.035 1.00 21.79 ? 657  ILE   A CB    1 
ATOM   4808  C  CG1   . ILE   A  1  659  ? -32.645 78.407  109.281 1.00 23.27 ? 657  ILE   A CG1   1 
ATOM   4809  C  CG2   . ILE   A  1  659  ? -32.488 78.993  106.841 1.00 21.60 ? 657  ILE   A CG2   1 
ATOM   4810  C  CD1   . ILE   A  1  659  ? -32.143 76.996  109.216 1.00 22.26 ? 657  ILE   A CD1   1 
ATOM   4811  N  N     . ILE   A  1  660  ? -35.820 80.414  106.631 1.00 21.75 ? 658  ILE   A N     1 
ATOM   4812  C  CA    . ILE   A  1  660  ? -36.436 80.999  105.443 1.00 21.96 ? 658  ILE   A CA    1 
ATOM   4813  C  C     . ILE   A  1  660  ? -36.632 82.501  105.626 1.00 24.62 ? 658  ILE   A C     1 
ATOM   4814  O  O     . ILE   A  1  660  ? -36.270 83.302  104.756 1.00 24.01 ? 658  ILE   A O     1 
ATOM   4815  C  CB    . ILE   A  1  660  ? -37.758 80.277  105.134 1.00 20.88 ? 658  ILE   A CB    1 
ATOM   4816  C  CG1   . ILE   A  1  660  ? -37.461 78.890  104.562 1.00 22.05 ? 658  ILE   A CG1   1 
ATOM   4817  C  CG2   . ILE   A  1  660  ? -38.632 81.113  104.205 1.00 23.49 ? 658  ILE   A CG2   1 
ATOM   4818  C  CD1   . ILE   A  1  660  ? -38.705 78.011  104.501 1.00 27.78 ? 658  ILE   A CD1   1 
ATOM   4819  N  N     . ARG   A  1  661  ? -37.177 82.905  106.774 1.00 22.59 ? 659  ARG   A N     1 
ATOM   4820  C  CA    . ARG   A  1  661  ? -37.518 84.308  106.971 1.00 24.36 ? 659  ARG   A CA    1 
ATOM   4821  C  C     . ARG   A  1  661  ? -36.328 85.154  107.402 1.00 26.31 ? 659  ARG   A C     1 
ATOM   4822  O  O     . ARG   A  1  661  ? -36.254 86.333  107.038 1.00 26.12 ? 659  ARG   A O     1 
ATOM   4823  C  CB    . ARG   A  1  661  ? -38.668 84.441  107.973 1.00 25.34 ? 659  ARG   A CB    1 
ATOM   4824  C  CG    . ARG   A  1  661  ? -40.001 83.973  107.398 1.00 25.90 ? 659  ARG   A CG    1 
ATOM   4825  C  CD    . ARG   A  1  661  ? -41.088 83.924  108.460 1.00 25.15 ? 659  ARG   A CD    1 
ATOM   4826  N  NE    . ARG   A  1  661  ? -41.341 85.225  109.064 1.00 26.77 ? 659  ARG   A NE    1 
ATOM   4827  C  CZ    . ARG   A  1  661  ? -41.280 85.474  110.365 1.00 29.41 ? 659  ARG   A CZ    1 
ATOM   4828  N  NH1   . ARG   A  1  661  ? -40.955 84.533  111.237 1.00 30.27 ? 659  ARG   A NH1   1 
ATOM   4829  N  NH2   . ARG   A  1  661  ? -41.570 86.692  110.805 1.00 27.69 ? 659  ARG   A NH2   1 
ATOM   4830  N  N     . GLU   A  1  662  ? -35.407 84.592  108.188 1.00 23.18 ? 660  GLU   A N     1 
ATOM   4831  C  CA    . GLU   A  1  662  ? -34.273 85.380  108.666 1.00 26.17 ? 660  GLU   A CA    1 
ATOM   4832  C  C     . GLU   A  1  662  ? -33.183 85.538  107.609 1.00 23.63 ? 660  GLU   A C     1 
ATOM   4833  O  O     . GLU   A  1  662  ? -32.600 86.619  107.482 1.00 26.35 ? 660  GLU   A O     1 
ATOM   4834  C  CB    . GLU   A  1  662  ? -33.698 84.778  109.950 1.00 27.53 ? 660  GLU   A CB    1 
ATOM   4835  C  CG    . GLU   A  1  662  ? -32.594 85.629  110.570 1.00 26.99 ? 660  GLU   A CG    1 
ATOM   4836  C  CD    . GLU   A  1  662  ? -32.028 85.054  111.860 1.00 27.53 ? 660  GLU   A CD    1 
ATOM   4837  O  OE1   . GLU   A  1  662  ? -32.014 83.814  112.033 1.00 26.86 ? 660  GLU   A OE1   1 
ATOM   4838  O  OE2   . GLU   A  1  662  ? -31.585 85.859  112.703 1.00 27.53 ? 660  GLU   A OE2   1 
ATOM   4839  N  N     . ALA   A  1  663  ? -32.894 84.490  106.835 1.00 21.70 ? 661  ALA   A N     1 
ATOM   4840  C  CA    . ALA   A  1  663  ? -31.697 84.462  106.000 1.00 20.11 ? 661  ALA   A CA    1 
ATOM   4841  C  C     . ALA   A  1  663  ? -31.991 84.477  104.502 1.00 24.79 ? 661  ALA   A C     1 
ATOM   4842  O  O     . ALA   A  1  663  ? -31.065 84.318  103.701 1.00 27.60 ? 661  ALA   A O     1 
ATOM   4843  C  CB    . ALA   A  1  663  ? -30.817 83.262  106.362 1.00 25.46 ? 661  ALA   A CB    1 
ATOM   4844  N  N     . GLY   A  1  664  ? -33.247 84.644  104.102 1.00 25.94 ? 662  GLY   A N     1 
ATOM   4845  C  CA    . GLY   A  1  664  ? -33.550 84.686  102.681 1.00 26.44 ? 662  GLY   A CA    1 
ATOM   4846  C  C     . GLY   A  1  664  ? -33.428 83.360  101.966 1.00 24.20 ? 662  GLY   A C     1 
ATOM   4847  O  O     . GLY   A  1  664  ? -33.200 83.334  100.755 1.00 28.71 ? 662  GLY   A O     1 
ATOM   4848  N  N     . LYS   A  1  665  ? -33.589 82.251  102.677 1.00 22.51 ? 663  LYS   A N     1 
ATOM   4849  C  CA    . LYS   A  1  665  ? -33.401 80.937  102.077 1.00 21.62 ? 663  LYS   A CA    1 
ATOM   4850  C  C     . LYS   A  1  665  ? -34.726 80.368  101.591 1.00 19.50 ? 663  LYS   A C     1 
ATOM   4851  O  O     . LYS   A  1  665  ? -35.768 80.562  102.221 1.00 20.56 ? 663  LYS   A O     1 
ATOM   4852  C  CB    . LYS   A  1  665  ? -32.809 79.972  103.100 1.00 23.09 ? 663  LYS   A CB    1 
ATOM   4853  C  CG    . LYS   A  1  665  ? -31.487 80.427  103.688 1.00 26.41 ? 663  LYS   A CG    1 
ATOM   4854  C  CD    . LYS   A  1  665  ? -30.440 80.631  102.620 1.00 27.29 ? 663  LYS   A CD    1 
ATOM   4855  C  CE    . LYS   A  1  665  ? -29.072 80.831  103.258 1.00 32.02 ? 663  LYS   A CE    1 
ATOM   4856  N  NZ    . LYS   A  1  665  ? -28.046 81.338  102.288 1.00 30.45 ? 663  LYS   A NZ    1 
ATOM   4857  N  N     . SER   A  1  666  ? -34.671 79.647  100.471 1.00 25.10 ? 664  SER   A N     1 
ATOM   4858  C  CA    . SER   A  1  666  ? -35.805 78.844  100.044 1.00 22.85 ? 664  SER   A CA    1 
ATOM   4859  C  C     . SER   A  1  666  ? -35.956 77.643  100.973 1.00 22.41 ? 664  SER   A C     1 
ATOM   4860  O  O     . SER   A  1  666  ? -35.046 77.294  101.727 1.00 22.27 ? 664  SER   A O     1 
ATOM   4861  C  CB    . SER   A  1  666  ? -35.555 78.319  98.633  1.00 26.15 ? 664  SER   A CB    1 
ATOM   4862  O  OG    . SER   A  1  666  ? -34.554 77.317  98.651  1.00 26.11 ? 664  SER   A OG    1 
ATOM   4863  N  N     . ALA   A  1  667  ? -37.126 77.002  100.917 1.00 22.69 ? 665  ALA   A N     1 
ATOM   4864  C  CA    . ALA   A  1  667  ? -37.341 75.816  101.743 1.00 21.02 ? 665  ALA   A CA    1 
ATOM   4865  C  C     . ALA   A  1  667  ? -36.307 74.728  101.449 1.00 24.24 ? 665  ALA   A C     1 
ATOM   4866  O  O     . ALA   A  1  667  ? -35.772 74.114  102.379 1.00 21.62 ? 665  ALA   A O     1 
ATOM   4867  C  CB    . ALA   A  1  667  ? -38.763 75.284  101.566 1.00 25.05 ? 665  ALA   A CB    1 
ATOM   4868  N  N     . LEU   A  1  668  ? -36.020 74.467  100.170 1.00 22.69 ? 666  LEU   A N     1 
ATOM   4869  C  CA    . LEU   A  1  668  ? -35.024 73.451  99.825  1.00 23.00 ? 666  LEU   A CA    1 
ATOM   4870  C  C     . LEU   A  1  668  ? -33.673 73.766  100.444 1.00 25.21 ? 666  LEU   A C     1 
ATOM   4871  O  O     . LEU   A  1  668  ? -33.004 72.876  100.984 1.00 24.85 ? 666  LEU   A O     1 
ATOM   4872  C  CB    . LEU   A  1  668  ? -34.869 73.345  98.306  1.00 26.28 ? 666  LEU   A CB    1 
ATOM   4873  C  CG    . LEU   A  1  668  ? -35.846 72.456  97.555  1.00 35.13 ? 666  LEU   A CG    1 
ATOM   4874  C  CD1   . LEU   A  1  668  ? -35.567 72.554  96.064  1.00 29.86 ? 666  LEU   A CD1   1 
ATOM   4875  C  CD2   . LEU   A  1  668  ? -35.705 71.022  98.043  1.00 36.02 ? 666  LEU   A CD2   1 
ATOM   4876  N  N     . ASN   A  1  669  ? -33.245 75.024  100.368 1.00 22.32 ? 667  ASN   A N     1 
ATOM   4877  C  CA    . ASN   A  1  669  ? -31.942 75.361  100.925 1.00 24.48 ? 667  ASN   A CA    1 
ATOM   4878  C  C     . ASN   A  1  669  ? -31.960 75.376  102.447 1.00 23.01 ? 667  ASN   A C     1 
ATOM   4879  O  O     . ASN   A  1  669  ? -30.927 75.110  103.071 1.00 22.07 ? 667  ASN   A O     1 
ATOM   4880  C  CB    . ASN   A  1  669  ? -31.460 76.693  100.365 1.00 29.66 ? 667  ASN   A CB    1 
ATOM   4881  C  CG    . ASN   A  1  669  ? -31.228 76.637  98.866  1.00 29.88 ? 667  ASN   A CG    1 
ATOM   4882  O  OD1   . ASN   A  1  669  ? -31.511 77.594  98.148  1.00 35.08 ? 667  ASN   A OD1   1 
ATOM   4883  N  ND2   . ASN   A  1  669  ? -30.707 75.506  98.386  1.00 36.17 ? 667  ASN   A ND2   1 
ATOM   4884  N  N     . ALA   A  1  670  ? -33.107 75.675  103.059 1.00 20.83 ? 668  ALA   A N     1 
ATOM   4885  C  CA    . ALA   A  1  670  ? -33.198 75.593  104.515 1.00 20.78 ? 668  ALA   A CA    1 
ATOM   4886  C  C     . ALA   A  1  670  ? -33.139 74.146  104.980 1.00 21.35 ? 668  ALA   A C     1 
ATOM   4887  O  O     . ALA   A  1  670  ? -32.530 73.843  106.017 1.00 21.29 ? 668  ALA   A O     1 
ATOM   4888  C  CB    . ALA   A  1  670  ? -34.475 76.269  105.014 1.00 21.61 ? 668  ALA   A CB    1 
ATOM   4889  N  N     . ILE   A  1  671  ? -33.769 73.239  104.235 1.00 20.76 ? 669  ILE   A N     1 
ATOM   4890  C  CA    . ILE   A  1  671  ? -33.670 71.822  104.563 1.00 20.84 ? 669  ILE   A CA    1 
ATOM   4891  C  C     . ILE   A  1  671  ? -32.216 71.389  104.552 1.00 21.43 ? 669  ILE   A C     1 
ATOM   4892  O  O     . ILE   A  1  671  ? -31.740 70.733  105.486 1.00 22.40 ? 669  ILE   A O     1 
ATOM   4893  C  CB    . ILE   A  1  671  ? -34.500 70.979  103.583 1.00 21.66 ? 669  ILE   A CB    1 
ATOM   4894  C  CG1   . ILE   A  1  671  ? -35.990 71.188  103.832 1.00 21.30 ? 669  ILE   A CG1   1 
ATOM   4895  C  CG2   . ILE   A  1  671  ? -34.112 69.514  103.716 1.00 23.63 ? 669  ILE   A CG2   1 
ATOM   4896  C  CD1   . ILE   A  1  671  ? -36.869 70.643  102.708 1.00 23.76 ? 669  ILE   A CD1   1 
ATOM   4897  N  N     . ALA   A  1  672  ? -31.495 71.747  103.480 1.00 21.54 ? 670  ALA   A N     1 
ATOM   4898  C  CA    . ALA   A  1  672  ? -30.083 71.402  103.373 1.00 21.09 ? 670  ALA   A CA    1 
ATOM   4899  C  C     . ALA   A  1  672  ? -29.295 71.990  104.529 1.00 19.73 ? 670  ALA   A C     1 
ATOM   4900  O  O     . ALA   A  1  672  ? -28.378 71.347  105.054 1.00 22.92 ? 670  ALA   A O     1 
ATOM   4901  C  CB    . ALA   A  1  672  ? -29.527 71.929  102.051 1.00 21.15 ? 670  ALA   A CB    1 
ATOM   4902  N  N     . GLU   A  1  673  ? -29.649 73.210  104.939 1.00 19.96 ? 671  GLU   A N     1 
ATOM   4903  C  CA    . GLU   A  1  673  ? -28.959 73.884  106.033 1.00 20.16 ? 671  GLU   A CA    1 
ATOM   4904  C  C     . GLU   A  1  673  ? -29.124 73.116  107.337 1.00 21.40 ? 671  GLU   A C     1 
ATOM   4905  O  O     . GLU   A  1  673  ? -28.153 72.881  108.063 1.00 20.93 ? 671  GLU   A O     1 
ATOM   4906  C  CB    . GLU   A  1  673  ? -29.528 75.296  106.172 1.00 22.20 ? 671  GLU   A CB    1 
ATOM   4907  C  CG    . GLU   A  1  673  ? -28.940 76.123  107.301 1.00 27.33 ? 671  GLU   A CG    1 
ATOM   4908  C  CD    . GLU   A  1  673  ? -27.620 76.753  106.917 1.00 28.28 ? 671  GLU   A CD    1 
ATOM   4909  O  OE1   . GLU   A  1  673  ? -27.302 76.805  105.702 1.00 30.96 ? 671  GLU   A OE1   1 
ATOM   4910  O  OE2   . GLU   A  1  673  ? -26.902 77.200  107.828 1.00 26.12 ? 671  GLU   A OE2   1 
ATOM   4911  N  N     . VAL   A  1  674  ? -30.352 72.709  107.648 1.00 19.08 ? 672  VAL   A N     1 
ATOM   4912  C  CA    . VAL   A  1  674  ? -30.598 71.990  108.889 1.00 20.22 ? 672  VAL   A CA    1 
ATOM   4913  C  C     . VAL   A  1  674  ? -30.000 70.593  108.821 1.00 20.73 ? 672  VAL   A C     1 
ATOM   4914  O  O     . VAL   A  1  674  ? -29.426 70.100  109.801 1.00 19.07 ? 672  VAL   A O     1 
ATOM   4915  C  CB    . VAL   A  1  674  ? -32.103 71.974  109.212 1.00 19.25 ? 672  VAL   A CB    1 
ATOM   4916  C  CG1   . VAL   A  1  674  ? -32.367 71.200  110.502 1.00 22.25 ? 672  VAL   A CG1   1 
ATOM   4917  C  CG2   . VAL   A  1  674  ? -32.651 73.404  109.311 1.00 20.35 ? 672  VAL   A CG2   1 
ATOM   4918  N  N     . ARG   A  1  675  ? -30.105 69.938  107.661 1.00 19.81 ? 673  ARG   A N     1 
ATOM   4919  C  CA    . ARG   A  1  675  ? -29.463 68.640  107.519 1.00 17.43 ? 673  ARG   A CA    1 
ATOM   4920  C  C     . ARG   A  1  675  ? -27.969 68.750  107.767 1.00 17.33 ? 673  ARG   A C     1 
ATOM   4921  O  O     . ARG   A  1  675  ? -27.384 67.895  108.440 1.00 19.02 ? 673  ARG   A O     1 
ATOM   4922  C  CB    . ARG   A  1  675  ? -29.715 68.066  106.134 1.00 17.64 ? 673  ARG   A CB    1 
ATOM   4923  C  CG    . ARG   A  1  675  ? -31.139 67.611  105.904 1.00 19.04 ? 673  ARG   A CG    1 
ATOM   4924  C  CD    . ARG   A  1  675  ? -31.180 66.845  104.594 1.00 21.79 ? 673  ARG   A CD    1 
ATOM   4925  N  NE    . ARG   A  1  675  ? -30.445 65.588  104.696 1.00 20.73 ? 673  ARG   A NE    1 
ATOM   4926  C  CZ    . ARG   A  1  675  ? -30.071 64.852  103.657 1.00 21.08 ? 673  ARG   A CZ    1 
ATOM   4927  N  NH1   . ARG   A  1  675  ? -30.347 65.223  102.416 1.00 18.65 ? 673  ARG   A NH1   1 
ATOM   4928  N  NH2   . ARG   A  1  675  ? -29.409 63.715  103.871 1.00 19.29 ? 673  ARG   A NH2   1 
ATOM   4929  N  N     . GLU   A  1  676  ? -27.336 69.790  107.219 1.00 18.25 ? 674  GLU   A N     1 
ATOM   4930  C  CA    . GLU   A  1  676  ? -25.894 69.951  107.397 1.00 18.53 ? 674  GLU   A CA    1 
ATOM   4931  C  C     . GLU   A  1  676  ? -25.550 70.121  108.870 1.00 18.97 ? 674  GLU   A C     1 
ATOM   4932  O  O     . GLU   A  1  676  ? -24.556 69.564  109.352 1.00 18.81 ? 674  GLU   A O     1 
ATOM   4933  C  CB    . GLU   A  1  676  ? -25.407 71.154  106.594 1.00 18.77 ? 674  GLU   A CB    1 
ATOM   4934  C  CG    . GLU   A  1  676  ? -23.887 71.311  106.542 1.00 21.72 ? 674  GLU   A CG    1 
ATOM   4935  C  CD    . GLU   A  1  676  ? -23.236 70.554  105.405 1.00 31.03 ? 674  GLU   A CD    1 
ATOM   4936  O  OE1   . GLU   A  1  676  ? -23.913 69.714  104.765 1.00 35.06 ? 674  GLU   A OE1   1 
ATOM   4937  O  OE2   . GLU   A  1  676  ? -22.034 70.799  105.157 1.00 31.81 ? 674  GLU   A OE2   1 
ATOM   4938  N  N     . ALA   A  1  677  ? -26.362 70.881  109.608 1.00 19.80 ? 675  ALA   A N     1 
ATOM   4939  C  CA    . ALA   A  1  677  ? -26.095 71.048  111.035 1.00 18.40 ? 675  ALA   A CA    1 
ATOM   4940  C  C     . ALA   A  1  677  ? -26.176 69.710  111.755 1.00 20.77 ? 675  ALA   A C     1 
ATOM   4941  O  O     . ALA   A  1  677  ? -25.300 69.364  112.559 1.00 19.79 ? 675  ALA   A O     1 
ATOM   4942  C  CB    . ALA   A  1  677  ? -27.068 72.061  111.647 1.00 17.98 ? 675  ALA   A CB    1 
ATOM   4943  N  N     . ILE   A  1  678  ? -27.231 68.946  111.470 1.00 18.53 ? 676  ILE   A N     1 
ATOM   4944  C  CA    . ILE   A  1  678  ? -27.397 67.621  112.053 1.00 17.40 ? 676  ILE   A CA    1 
ATOM   4945  C  C     . ILE   A  1  678  ? -26.196 66.748  111.725 1.00 18.48 ? 676  ILE   A C     1 
ATOM   4946  O  O     . ILE   A  1  678  ? -25.672 66.033  112.590 1.00 18.84 ? 676  ILE   A O     1 
ATOM   4947  C  CB    . ILE   A  1  678  ? -28.713 67.005  111.538 1.00 17.68 ? 676  ILE   A CB    1 
ATOM   4948  C  CG1   . ILE   A  1  678  ? -29.914 67.744  112.129 1.00 21.06 ? 676  ILE   A CG1   1 
ATOM   4949  C  CG2   . ILE   A  1  678  ? -28.780 65.509  111.831 1.00 22.17 ? 676  ILE   A CG2   1 
ATOM   4950  C  CD1   . ILE   A  1  678  ? -31.200 67.494  111.360 1.00 19.90 ? 676  ILE   A CD1   1 
ATOM   4951  N  N     . ASP   A  1  679  ? -25.748 66.788  110.465 1.00 17.93 ? 677  ASP   A N     1 
ATOM   4952  C  CA    . ASP   A  1  679  ? -24.620 65.960  110.041 1.00 17.12 ? 677  ASP   A CA    1 
ATOM   4953  C  C     . ASP   A  1  679  ? -23.321 66.388  110.716 1.00 20.02 ? 677  ASP   A C     1 
ATOM   4954  O  O     . ASP   A  1  679  ? -22.526 65.532  111.114 1.00 19.23 ? 677  ASP   A O     1 
ATOM   4955  C  CB    . ASP   A  1  679  ? -24.470 65.993  108.520 1.00 18.45 ? 677  ASP   A CB    1 
ATOM   4956  C  CG    . ASP   A  1  679  ? -25.647 65.360  107.794 1.00 23.27 ? 677  ASP   A CG    1 
ATOM   4957  O  OD1   . ASP   A  1  679  ? -26.242 64.408  108.325 1.00 23.38 ? 677  ASP   A OD1   1 
ATOM   4958  O  OD2   . ASP   A  1  679  ? -25.946 65.798  106.669 1.00 26.02 ? 677  ASP   A OD2   1 
ATOM   4959  N  N     . PHE   A  1  680  ? -23.079 67.698  110.850 1.00 17.97 ? 678  PHE   A N     1 
ATOM   4960  C  CA    . PHE   A  1  680  ? -21.919 68.152  111.620 1.00 17.99 ? 678  PHE   A CA    1 
ATOM   4961  C  C     . PHE   A  1  680  ? -21.944 67.580  113.030 1.00 17.63 ? 678  PHE   A C     1 
ATOM   4962  O  O     . PHE   A  1  680  ? -20.944 67.051  113.523 1.00 18.89 ? 678  PHE   A O     1 
ATOM   4963  C  CB    . PHE   A  1  680  ? -21.884 69.678  111.711 1.00 18.03 ? 678  PHE   A CB    1 
ATOM   4964  C  CG    . PHE   A  1  680  ? -21.240 70.360  110.531 1.00 17.15 ? 678  PHE   A CG    1 
ATOM   4965  C  CD1   . PHE   A  1  680  ? -20.011 69.945  110.026 1.00 18.85 ? 678  PHE   A CD1   1 
ATOM   4966  C  CD2   . PHE   A  1  680  ? -21.876 71.440  109.930 1.00 19.57 ? 678  PHE   A CD2   1 
ATOM   4967  C  CE1   . PHE   A  1  680  ? -19.435 70.596  108.950 1.00 21.07 ? 678  PHE   A CE1   1 
ATOM   4968  C  CE2   . PHE   A  1  680  ? -21.314 72.087  108.861 1.00 20.38 ? 678  PHE   A CE2   1 
ATOM   4969  C  CZ    . PHE   A  1  680  ? -20.088 71.679  108.364 1.00 18.61 ? 678  PHE   A CZ    1 
ATOM   4970  N  N     . LEU   A  1  681  ? -23.077 67.719  113.713 1.00 17.54 ? 679  LEU   A N     1 
ATOM   4971  C  CA    . LEU   A  1  681  ? -23.166 67.230  115.080 1.00 17.05 ? 679  LEU   A CA    1 
ATOM   4972  C  C     . LEU   A  1  681  ? -22.844 65.744  115.147 1.00 19.83 ? 679  LEU   A C     1 
ATOM   4973  O  O     . LEU   A  1  681  ? -22.057 65.304  115.992 1.00 19.63 ? 679  LEU   A O     1 
ATOM   4974  C  CB    . LEU   A  1  681  ? -24.566 67.505  115.638 1.00 20.31 ? 679  LEU   A CB    1 
ATOM   4975  C  CG    . LEU   A  1  681  ? -24.881 68.984  115.863 1.00 20.33 ? 679  LEU   A CG    1 
ATOM   4976  C  CD1   . LEU   A  1  681  ? -26.387 69.224  115.911 1.00 20.50 ? 679  LEU   A CD1   1 
ATOM   4977  C  CD2   . LEU   A  1  681  ? -24.247 69.476  117.142 1.00 19.96 ? 679  LEU   A CD2   1 
ATOM   4978  N  N     . ARG   A  1  682  ? -23.435 64.953  114.255 1.00 17.41 ? 680  ARG   A N     1 
ATOM   4979  C  CA    . ARG   A  1  682  ? -23.240 63.513  114.337 1.00 18.07 ? 680  ARG   A CA    1 
ATOM   4980  C  C     . ARG   A  1  682  ? -21.862 63.109  113.856 1.00 19.64 ? 680  ARG   A C     1 
ATOM   4981  O  O     . ARG   A  1  682  ? -21.283 62.153  114.381 1.00 19.73 ? 680  ARG   A O     1 
ATOM   4982  C  CB    . ARG   A  1  682  ? -24.316 62.788  113.542 1.00 17.55 ? 680  ARG   A CB    1 
ATOM   4983  C  CG    . ARG   A  1  682  ? -25.676 62.886  114.186 1.00 18.64 ? 680  ARG   A CG    1 
ATOM   4984  C  CD    . ARG   A  1  682  ? -26.721 62.319  113.276 1.00 21.30 ? 680  ARG   A CD    1 
ATOM   4985  N  NE    . ARG   A  1  682  ? -28.013 62.285  113.944 1.00 20.86 ? 680  ARG   A NE    1 
ATOM   4986  C  CZ    . ARG   A  1  682  ? -29.157 62.073  113.313 1.00 21.90 ? 680  ARG   A CZ    1 
ATOM   4987  N  NH1   . ARG   A  1  682  ? -29.194 61.852  112.010 1.00 22.15 ? 680  ARG   A NH1   1 
ATOM   4988  N  NH2   . ARG   A  1  682  ? -30.294 62.104  114.005 1.00 22.73 ? 680  ARG   A NH2   1 
ATOM   4989  N  N     . TYR   A  1  683  ? -21.323 63.842  112.889 1.00 17.03 ? 681  TYR   A N     1 
ATOM   4990  C  CA    . TYR   A  1  683  ? -19.996 63.520  112.382 1.00 16.13 ? 681  TYR   A CA    1 
ATOM   4991  C  C     . TYR   A  1  683  ? -18.940 63.825  113.428 1.00 19.94 ? 681  TYR   A C     1 
ATOM   4992  O  O     . TYR   A  1  683  ? -18.074 62.991  113.706 1.00 18.98 ? 681  TYR   A O     1 
ATOM   4993  C  CB    . TYR   A  1  683  ? -19.727 64.302  111.098 1.00 17.50 ? 681  TYR   A CB    1 
ATOM   4994  C  CG    . TYR   A  1  683  ? -18.346 64.073  110.545 1.00 17.22 ? 681  TYR   A CG    1 
ATOM   4995  C  CD1   . TYR   A  1  683  ? -18.044 62.908  109.863 1.00 17.91 ? 681  TYR   A CD1   1 
ATOM   4996  C  CD2   . TYR   A  1  683  ? -17.343 65.010  110.731 1.00 15.91 ? 681  TYR   A CD2   1 
ATOM   4997  C  CE1   . TYR   A  1  683  ? -16.778 62.692  109.359 1.00 17.65 ? 681  TYR   A CE1   1 
ATOM   4998  C  CE2   . TYR   A  1  683  ? -16.068 64.803  110.246 1.00 16.76 ? 681  TYR   A CE2   1 
ATOM   4999  C  CZ    . TYR   A  1  683  ? -15.796 63.640  109.556 1.00 19.36 ? 681  TYR   A CZ    1 
ATOM   5000  O  OH    . TYR   A  1  683  ? -14.530 63.426  109.073 1.00 20.11 ? 681  TYR   A OH    1 
ATOM   5001  N  N     . TYR   A  1  684  ? -19.000 65.013  114.033 1.00 18.72 ? 682  TYR   A N     1 
ATOM   5002  C  CA    . TYR   A  1  684  ? -17.994 65.322  115.043 1.00 18.13 ? 682  TYR   A CA    1 
ATOM   5003  C  C     . TYR   A  1  684  ? -18.152 64.434  116.268 1.00 19.10 ? 682  TYR   A C     1 
ATOM   5004  O  O     . TYR   A  1  684  ? -17.156 64.082  116.905 1.00 18.92 ? 682  TYR   A O     1 
ATOM   5005  C  CB    . TYR   A  1  684  ? -18.001 66.803  115.416 1.00 17.49 ? 682  TYR   A CB    1 
ATOM   5006  C  CG    . TYR   A  1  684  ? -17.625 67.703  114.263 1.00 16.38 ? 682  TYR   A CG    1 
ATOM   5007  C  CD1   . TYR   A  1  684  ? -16.560 67.392  113.423 1.00 17.11 ? 682  TYR   A CD1   1 
ATOM   5008  C  CD2   . TYR   A  1  684  ? -18.347 68.858  114.004 1.00 19.20 ? 682  TYR   A CD2   1 
ATOM   5009  C  CE1   . TYR   A  1  684  ? -16.221 68.211  112.362 1.00 20.10 ? 682  TYR   A CE1   1 
ATOM   5010  C  CE2   . TYR   A  1  684  ? -18.020 69.682  112.955 1.00 18.03 ? 682  TYR   A CE2   1 
ATOM   5011  C  CZ    . TYR   A  1  684  ? -16.956 69.361  112.129 1.00 19.80 ? 682  TYR   A CZ    1 
ATOM   5012  O  OH    . TYR   A  1  684  ? -16.643 70.190  111.079 1.00 18.90 ? 682  TYR   A OH    1 
ATOM   5013  N  N     . ALA   A  1  685  ? -19.380 64.039  116.598 1.00 18.39 ? 683  ALA   A N     1 
ATOM   5014  C  CA    . ALA   A  1  685  ? -19.575 63.087  117.683 1.00 18.75 ? 683  ALA   A CA    1 
ATOM   5015  C  C     . ALA   A  1  685  ? -18.878 61.769  117.369 1.00 22.23 ? 683  ALA   A C     1 
ATOM   5016  O  O     . ALA   A  1  685  ? -18.156 61.221  118.207 1.00 20.51 ? 683  ALA   A O     1 
ATOM   5017  C  CB    . ALA   A  1  685  ? -21.071 62.861  117.922 1.00 20.63 ? 683  ALA   A CB    1 
ATOM   5018  N  N     . GLU   A  1  686  ? -19.080 61.248  116.160 1.00 20.10 ? 684  GLU   A N     1 
ATOM   5019  C  CA    . GLU   A  1  686  ? -18.454 59.980  115.797 1.00 21.40 ? 684  GLU   A CA    1 
ATOM   5020  C  C     . GLU   A  1  686  ? -16.942 60.117  115.711 1.00 21.90 ? 684  GLU   A C     1 
ATOM   5021  O  O     . GLU   A  1  686  ? -16.208 59.242  116.191 1.00 20.75 ? 684  GLU   A O     1 
ATOM   5022  C  CB    . GLU   A  1  686  ? -19.018 59.459  114.477 1.00 24.19 ? 684  GLU   A CB    1 
ATOM   5023  C  CG    . GLU   A  1  686  ? -18.314 58.211  113.953 1.00 27.49 ? 684  GLU   A CG    1 
ATOM   5024  C  CD    . GLU   A  1  686  ? -18.451 56.984  114.867 1.00 32.69 ? 684  GLU   A CD    1 
ATOM   5025  O  OE1   . GLU   A  1  686  ? -19.328 56.960  115.769 1.00 32.28 ? 684  GLU   A OE1   1 
ATOM   5026  O  OE2   . GLU   A  1  686  ? -17.680 56.019  114.666 1.00 30.79 ? 684  GLU   A OE2   1 
ATOM   5027  N  N     . GLN   A  1  687  ? -16.459 61.217  115.129 1.00 19.26 ? 685  GLN   A N     1 
ATOM   5028  C  CA    . GLN   A  1  687  ? -15.016 61.426  115.053 1.00 18.80 ? 685  GLN   A CA    1 
ATOM   5029  C  C     . GLN   A  1  687  ? -14.417 61.501  116.448 1.00 20.85 ? 685  GLN   A C     1 
ATOM   5030  O  O     . GLN   A  1  687  ? -13.309 61.007  116.689 1.00 19.55 ? 685  GLN   A O     1 
ATOM   5031  C  CB    . GLN   A  1  687  ? -14.711 62.700  114.273 1.00 18.18 ? 685  GLN   A CB    1 
ATOM   5032  C  CG    . GLN   A  1  687  ? -15.004 62.586  112.774 1.00 18.98 ? 685  GLN   A CG    1 
ATOM   5033  C  CD    . GLN   A  1  687  ? -14.263 61.430  112.146 1.00 24.22 ? 685  GLN   A CD    1 
ATOM   5034  O  OE1   . GLN   A  1  687  ? -13.042 61.365  112.219 1.00 22.03 ? 685  GLN   A OE1   1 
ATOM   5035  N  NE2   . GLN   A  1  687  ? -14.997 60.496  111.555 1.00 25.31 ? 685  GLN   A NE2   1 
ATOM   5036  N  N     . THR   A  1  688  ? -15.143 62.106  117.386 1.00 18.36 ? 686  THR   A N     1 
ATOM   5037  C  CA    . THR   A  1  688  ? -14.669 62.136  118.765 1.00 17.16 ? 686  THR   A CA    1 
ATOM   5038  C  C     . THR   A  1  688  ? -14.580 60.728  119.338 1.00 18.80 ? 686  THR   A C     1 
ATOM   5039  O  O     . THR   A  1  688  ? -13.578 60.357  119.965 1.00 21.46 ? 686  THR   A O     1 
ATOM   5040  C  CB    . THR   A  1  688  ? -15.614 62.985  119.615 1.00 19.26 ? 686  THR   A CB    1 
ATOM   5041  O  OG1   . THR   A  1  688  ? -15.462 64.353  119.231 1.00 20.97 ? 686  THR   A OG1   1 
ATOM   5042  C  CG2   . THR   A  1  688  ? -15.271 62.835  121.098 1.00 19.78 ? 686  THR   A CG2   1 
ATOM   5043  N  N     . ARG   A  1  689  ? -15.621 59.929  119.126 1.00 20.00 ? 687  ARG   A N     1 
ATOM   5044  C  CA    . ARG   A  1  689  ? -15.631 58.562  119.626 1.00 20.69 ? 687  ARG   A CA    1 
ATOM   5045  C  C     . ARG   A  1  689  ? -14.531 57.722  119.007 1.00 21.32 ? 687  ARG   A C     1 
ATOM   5046  O  O     . ARG   A  1  689  ? -14.099 56.739  119.621 1.00 23.66 ? 687  ARG   A O     1 
ATOM   5047  C  CB    . ARG   A  1  689  ? -16.989 57.911  119.381 1.00 23.13 ? 687  ARG   A CB    1 
ATOM   5048  C  CG    . ARG   A  1  689  ? -18.069 58.403  120.332 1.00 24.62 ? 687  ARG   A CG    1 
ATOM   5049  C  CD    . ARG   A  1  689  ? -19.321 57.578  120.140 1.00 27.26 ? 687  ARG   A CD    1 
ATOM   5050  N  NE    . ARG   A  1  689  ? -19.843 57.718  118.790 1.00 27.09 ? 687  ARG   A NE    1 
ATOM   5051  C  CZ    . ARG   A  1  689  ? -20.827 58.544  118.461 1.00 30.13 ? 687  ARG   A CZ    1 
ATOM   5052  N  NH1   . ARG   A  1  689  ? -21.400 59.327  119.362 1.00 28.68 ? 687  ARG   A NH1   1 
ATOM   5053  N  NH2   . ARG   A  1  689  ? -21.247 58.585  117.200 1.00 27.95 ? 687  ARG   A NH2   1 
ATOM   5054  N  N     . ARG   A  1  690  ? -14.066 58.092  117.817 1.00 20.80 ? 688  ARG   A N     1 
ATOM   5055  C  CA    . ARG   A  1  690  ? -12.961 57.383  117.188 1.00 23.78 ? 688  ARG   A CA    1 
ATOM   5056  C  C     . ARG   A  1  690  ? -11.599 57.824  117.702 1.00 22.62 ? 688  ARG   A C     1 
ATOM   5057  O  O     . ARG   A  1  690  ? -10.633 57.072  117.544 1.00 22.12 ? 688  ARG   A O     1 
ATOM   5058  C  CB    . ARG   A  1  690  ? -12.970 57.601  115.674 1.00 21.30 ? 688  ARG   A CB    1 
ATOM   5059  C  CG    . ARG   A  1  690  ? -14.164 56.994  114.952 1.00 22.65 ? 688  ARG   A CG    1 
ATOM   5060  C  CD    . ARG   A  1  690  ? -14.113 55.471  114.914 1.00 24.88 ? 688  ARG   A CD    1 
ATOM   5061  N  NE    . ARG   A  1  690  ? -12.961 55.001  114.149 1.00 27.03 ? 688  ARG   A NE    1 
ATOM   5062  C  CZ    . ARG   A  1  690  ? -11.935 54.350  114.676 1.00 28.10 ? 688  ARG   A CZ    1 
ATOM   5063  N  NH1   . ARG   A  1  690  ? -11.898 54.044  115.965 1.00 26.78 ? 688  ARG   A NH1   1 
ATOM   5064  N  NH2   . ARG   A  1  690  ? -10.924 53.988  113.889 1.00 23.58 ? 688  ARG   A NH2   1 
ATOM   5065  N  N     . THR   A  1  691  ? -11.480 59.020  118.289 1.00 19.65 ? 689  THR   A N     1 
ATOM   5066  C  CA    . THR   A  1  691  ? -10.137 59.579  118.459 1.00 18.76 ? 689  THR   A CA    1 
ATOM   5067  C  C     . THR   A  1  691  ? -9.773  60.050  119.861 1.00 23.86 ? 689  THR   A C     1 
ATOM   5068  O  O     . THR   A  1  691  ? -8.688  59.732  120.355 1.00 26.17 ? 689  THR   A O     1 
ATOM   5069  C  CB    . THR   A  1  691  ? -9.869  60.727  117.474 1.00 21.62 ? 689  THR   A CB    1 
ATOM   5070  O  OG1   . THR   A  1  691  ? -10.833 61.770  117.665 1.00 23.83 ? 689  THR   A OG1   1 
ATOM   5071  C  CG2   . THR   A  1  691  ? -9.942  60.240  116.025 1.00 23.06 ? 689  THR   A CG2   1 
ATOM   5072  N  N     . LEU   A  1  692  ? -10.639 60.823  120.509 1.00 20.78 ? 690  LEU   A N     1 
ATOM   5073  C  CA    . LEU   A  1  692  ? -10.188 61.660  121.614 1.00 22.74 ? 690  LEU   A CA    1 
ATOM   5074  C  C     . LEU   A  1  692  ? -9.968  60.864  122.898 1.00 25.66 ? 690  LEU   A C     1 
ATOM   5075  O  O     . LEU   A  1  692  ? -10.826 60.082  123.325 1.00 26.83 ? 690  LEU   A O     1 
ATOM   5076  C  CB    . LEU   A  1  692  ? -11.156 62.819  121.841 1.00 22.37 ? 690  LEU   A CB    1 
ATOM   5077  C  CG    . LEU   A  1  692  ? -11.169 63.852  120.705 1.00 24.28 ? 690  LEU   A CG    1 
ATOM   5078  C  CD1   . LEU   A  1  692  ? -12.005 65.066  121.072 1.00 25.25 ? 690  LEU   A CD1   1 
ATOM   5079  C  CD2   . LEU   A  1  692  ? -9.758  64.281  120.310 1.00 25.43 ? 690  LEU   A CD2   1 
ATOM   5080  N  N     . GLY   A  1  693  ? -8.804  61.074  123.502 1.00 24.43 ? 691  GLY   A N     1 
ATOM   5081  C  CA    . GLY   A  1  693  ? -8.446  60.435  124.743 1.00 27.39 ? 691  GLY   A CA    1 
ATOM   5082  C  C     . GLY   A  1  693  ? -7.881  61.435  125.728 1.00 29.44 ? 691  GLY   A C     1 
ATOM   5083  O  O     . GLY   A  1  693  ? -7.823  62.643  125.469 1.00 30.93 ? 691  GLY   A O     1 
ATOM   5084  N  N     . PRO   A  1  694  ? -7.440  60.934  126.883 1.00 30.04 ? 692  PRO   A N     1 
ATOM   5085  C  CA    . PRO   A  1  694  ? -6.991  61.837  127.960 1.00 34.04 ? 692  PRO   A CA    1 
ATOM   5086  C  C     . PRO   A  1  694  ? -5.830  62.738  127.575 1.00 33.22 ? 692  PRO   A C     1 
ATOM   5087  O  O     . PRO   A  1  694  ? -5.728  63.859  128.092 1.00 35.08 ? 692  PRO   A O     1 
ATOM   5088  C  CB    . PRO   A  1  694  ? -6.614  60.873  129.094 1.00 37.17 ? 692  PRO   A CB    1 
ATOM   5089  C  CG    . PRO   A  1  694  ? -7.366  59.608  128.796 1.00 34.26 ? 692  PRO   A CG    1 
ATOM   5090  C  CD    . PRO   A  1  694  ? -7.485  59.523  127.299 1.00 29.80 ? 692  PRO   A CD    1 
ATOM   5091  N  N     . GLY   A  1  695  ? -4.952  62.288  126.683 1.00 28.50 ? 693  GLY   A N     1 
ATOM   5092  C  CA    . GLY   A  1  695  ? -3.815  63.077  126.273 1.00 32.45 ? 693  GLY   A CA    1 
ATOM   5093  C  C     . GLY   A  1  695  ? -4.085  64.125  125.224 1.00 32.49 ? 693  GLY   A C     1 
ATOM   5094  O  O     . GLY   A  1  695  ? -3.171  64.864  124.852 1.00 30.20 ? 693  GLY   A O     1 
ATOM   5095  N  N     . HIS   A  1  696  ? -5.312  64.215  124.712 1.00 27.86 ? 694  HIS   A N     1 
ATOM   5096  C  CA    . HIS   A  1  696  ? -5.650  65.219  123.708 1.00 27.51 ? 694  HIS   A CA    1 
ATOM   5097  C  C     . HIS   A  1  696  ? -6.372  66.342  124.441 1.00 30.97 ? 694  HIS   A C     1 
ATOM   5098  O  O     . HIS   A  1  696  ? -7.597  66.447  124.436 1.00 31.64 ? 694  HIS   A O     1 
ATOM   5099  C  CB    . HIS   A  1  696  ? -6.498  64.608  122.595 1.00 28.85 ? 694  HIS   A CB    1 
ATOM   5100  C  CG    . HIS   A  1  696  ? -5.923  63.344  122.032 1.00 23.74 ? 694  HIS   A CG    1 
ATOM   5101  N  ND1   . HIS   A  1  696  ? -6.526  62.115  122.196 1.00 28.22 ? 694  HIS   A ND1   1 
ATOM   5102  C  CD2   . HIS   A  1  696  ? -4.780  63.115  121.342 1.00 27.23 ? 694  HIS   A CD2   1 
ATOM   5103  C  CE1   . HIS   A  1  696  ? -5.793  61.187  121.606 1.00 25.73 ? 694  HIS   A CE1   1 
ATOM   5104  N  NE2   . HIS   A  1  696  ? -4.726  61.767  121.085 1.00 27.58 ? 694  HIS   A NE2   1 
ATOM   5105  N  N     . GLY   A  1  697  ? -5.584  67.183  125.098 1.00 29.56 ? 695  GLY   A N     1 
ATOM   5106  C  CA    . GLY   A  1  697  ? -6.140  68.210  125.945 1.00 30.27 ? 695  GLY   A CA    1 
ATOM   5107  C  C     . GLY   A  1  697  ? -6.732  69.342  125.134 1.00 25.89 ? 695  GLY   A C     1 
ATOM   5108  O  O     . GLY   A  1  697  ? -6.229  69.708  124.071 1.00 25.71 ? 695  GLY   A O     1 
ATOM   5109  N  N     . PRO   A  1  698  ? -7.816  69.925  125.621 1.00 26.72 ? 696  PRO   A N     1 
ATOM   5110  C  CA    . PRO   A  1  698  ? -8.428  71.039  124.894 1.00 28.59 ? 696  PRO   A CA    1 
ATOM   5111  C  C     . PRO   A  1  698  ? -7.507  72.250  124.881 1.00 26.29 ? 696  PRO   A C     1 
ATOM   5112  O  O     . PRO   A  1  698  ? -6.620  72.410  125.722 1.00 26.53 ? 696  PRO   A O     1 
ATOM   5113  C  CB    . PRO   A  1  698  ? -9.705  71.322  125.689 1.00 29.64 ? 696  PRO   A CB    1 
ATOM   5114  C  CG    . PRO   A  1  698  ? -9.424  70.818  127.044 1.00 32.86 ? 696  PRO   A CG    1 
ATOM   5115  C  CD    . PRO   A  1  698  ? -8.542  69.608  126.860 1.00 32.98 ? 696  PRO   A CD    1 
ATOM   5116  N  N     . LEU   A  1  699  ? -7.707  73.097  123.873 1.00 24.51 ? 697  LEU   A N     1 
ATOM   5117  C  CA    . LEU   A  1  699  ? -6.978  74.359  123.832 1.00 25.57 ? 697  LEU   A CA    1 
ATOM   5118  C  C     . LEU   A  1  699  ? -7.389  75.271  124.978 1.00 26.16 ? 697  LEU   A C     1 
ATOM   5119  O  O     . LEU   A  1  699  ? -6.546  75.944  125.578 1.00 25.39 ? 697  LEU   A O     1 
ATOM   5120  C  CB    . LEU   A  1  699  ? -7.237  75.066  122.507 1.00 22.47 ? 697  LEU   A CB    1 
ATOM   5121  C  CG    . LEU   A  1  699  ? -6.703  74.363  121.273 1.00 24.67 ? 697  LEU   A CG    1 
ATOM   5122  C  CD1   . LEU   A  1  699  ? -7.085  75.167  120.042 1.00 24.12 ? 697  LEU   A CD1   1 
ATOM   5123  C  CD2   . LEU   A  1  699  ? -5.191  74.197  121.378 1.00 26.67 ? 697  LEU   A CD2   1 
ATOM   5124  N  N     . GLY   A  1  700  ? -8.680  75.310  125.294 1.00 24.50 ? 698  GLY   A N     1 
ATOM   5125  C  CA    . GLY   A  1  700  ? -9.221  76.317  126.171 1.00 23.74 ? 698  GLY   A CA    1 
ATOM   5126  C  C     . GLY   A  1  700  ? -10.358 77.032  125.478 1.00 23.66 ? 698  GLY   A C     1 
ATOM   5127  O  O     . GLY   A  1  700  ? -10.917 76.527  124.497 1.00 25.66 ? 698  GLY   A O     1 
ATOM   5128  N  N     . PRO   A  1  701  ? -10.721 78.220  125.960 1.00 25.67 ? 699  PRO   A N     1 
ATOM   5129  C  CA    . PRO   A  1  701  ? -11.843 78.946  125.350 1.00 22.54 ? 699  PRO   A CA    1 
ATOM   5130  C  C     . PRO   A  1  701  ? -11.592 79.191  123.870 1.00 21.85 ? 699  PRO   A C     1 
ATOM   5131  O  O     . PRO   A  1  701  ? -10.551 79.721  123.477 1.00 23.73 ? 699  PRO   A O     1 
ATOM   5132  C  CB    . PRO   A  1  701  ? -11.879 80.262  126.134 1.00 26.54 ? 699  PRO   A CB    1 
ATOM   5133  C  CG    . PRO   A  1  701  ? -11.290 79.906  127.469 1.00 26.43 ? 699  PRO   A CG    1 
ATOM   5134  C  CD    . PRO   A  1  701  ? -10.220 78.894  127.172 1.00 26.59 ? 699  PRO   A CD    1 
ATOM   5135  N  N     . ILE   A  1  702  ? -12.551 78.785  123.044 1.00 24.61 ? 700  ILE   A N     1 
ATOM   5136  C  CA    A ILE   A  1  702  ? -12.467 78.968  121.604 0.56 22.69 ? 700  ILE   A CA    1 
ATOM   5137  C  CA    B ILE   A  1  702  ? -12.482 78.947  121.595 0.44 22.69 ? 700  ILE   A CA    1 
ATOM   5138  C  C     . ILE   A  1  702  ? -13.543 79.953  121.182 1.00 21.44 ? 700  ILE   A C     1 
ATOM   5139  O  O     . ILE   A  1  702  ? -14.709 79.824  121.571 1.00 22.63 ? 700  ILE   A O     1 
ATOM   5140  C  CB    A ILE   A  1  702  ? -12.576 77.633  120.848 0.56 21.50 ? 700  ILE   A CB    1 
ATOM   5141  C  CB    B ILE   A  1  702  ? -12.706 77.612  120.864 0.44 21.44 ? 700  ILE   A CB    1 
ATOM   5142  C  CG1   A ILE   A  1  702  ? -11.292 76.826  121.063 0.56 21.62 ? 700  ILE   A CG1   1 
ATOM   5143  C  CG1   B ILE   A  1  702  ? -11.663 76.579  121.288 0.44 22.43 ? 700  ILE   A CG1   1 
ATOM   5144  C  CG2   A ILE   A  1  702  ? -12.816 77.875  119.357 0.56 22.60 ? 700  ILE   A CG2   1 
ATOM   5145  C  CG2   B ILE   A  1  702  ? -12.653 77.817  119.350 0.44 22.53 ? 700  ILE   A CG2   1 
ATOM   5146  C  CD1   A ILE   A  1  702  ? -11.248 75.539  120.307 0.56 22.26 ? 700  ILE   A CD1   1 
ATOM   5147  C  CD1   B ILE   A  1  702  ? -10.284 76.875  120.795 0.44 22.94 ? 700  ILE   A CD1   1 
ATOM   5148  N  N     . VAL   A  1  703  ? -13.143 80.941  120.400 1.00 21.47 ? 701  VAL   A N     1 
ATOM   5149  C  CA    . VAL   A  1  703  ? -14.058 81.921  119.843 1.00 22.35 ? 701  VAL   A CA    1 
ATOM   5150  C  C     . VAL   A  1  703  ? -14.484 81.411  118.475 1.00 19.70 ? 701  VAL   A C     1 
ATOM   5151  O  O     . VAL   A  1  703  ? -13.646 81.189  117.600 1.00 21.04 ? 701  VAL   A O     1 
ATOM   5152  C  CB    . VAL   A  1  703  ? -13.372 83.289  119.744 1.00 25.13 ? 701  VAL   A CB    1 
ATOM   5153  C  CG1   . VAL   A  1  703  ? -14.213 84.246  118.951 1.00 24.11 ? 701  VAL   A CG1   1 
ATOM   5154  C  CG2   . VAL   A  1  703  ? -13.138 83.834  121.147 1.00 26.67 ? 701  VAL   A CG2   1 
ATOM   5155  N  N     . CYS   A  1  704  ? -15.783 81.183  118.303 1.00 19.93 ? 702  CYS   A N     1 
ATOM   5156  C  CA    . CYS   A  1  704  ? -16.348 80.701  117.049 1.00 20.71 ? 702  CYS   A CA    1 
ATOM   5157  C  C     . CYS   A  1  704  ? -17.097 81.857  116.411 1.00 22.70 ? 702  CYS   A C     1 
ATOM   5158  O  O     . CYS   A  1  704  ? -18.117 82.313  116.939 1.00 21.24 ? 702  CYS   A O     1 
ATOM   5159  C  CB    . CYS   A  1  704  ? -17.285 79.519  117.281 1.00 23.29 ? 702  CYS   A CB    1 
ATOM   5160  S  SG    . CYS   A  1  704  ? -16.459 78.096  118.009 1.00 22.23 ? 702  CYS   A SG    1 
ATOM   5161  N  N     . ILE   A  1  705  ? -16.586 82.325  115.277 1.00 20.72 ? 703  ILE   A N     1 
ATOM   5162  C  CA    . ILE   A  1  705  ? -17.161 83.447  114.554 1.00 21.35 ? 703  ILE   A CA    1 
ATOM   5163  C  C     . ILE   A  1  705  ? -17.665 82.906  113.223 1.00 19.42 ? 703  ILE   A C     1 
ATOM   5164  O  O     . ILE   A  1  705  ? -16.901 82.281  112.468 1.00 19.61 ? 703  ILE   A O     1 
ATOM   5165  C  CB    . ILE   A  1  705  ? -16.121 84.560  114.356 1.00 20.88 ? 703  ILE   A CB    1 
ATOM   5166  C  CG1   . ILE   A  1  705  ? -15.712 85.140  115.710 1.00 23.97 ? 703  ILE   A CG1   1 
ATOM   5167  C  CG2   . ILE   A  1  705  ? -16.660 85.642  113.468 1.00 19.69 ? 703  ILE   A CG2   1 
ATOM   5168  C  CD1   . ILE   A  1  705  ? -14.487 86.033  115.631 1.00 24.09 ? 703  ILE   A CD1   1 
ATOM   5169  N  N     . SER   A  1  706  ? -18.935 83.139  112.935 1.00 20.65 ? 704  SER   A N     1 
ATOM   5170  C  CA    . SER   A  1  706  ? -19.580 82.459  111.823 1.00 20.66 ? 704  SER   A CA    1 
ATOM   5171  C  C     . SER   A  1  706  ? -20.207 83.459  110.866 1.00 20.45 ? 704  SER   A C     1 
ATOM   5172  O  O     . SER   A  1  706  ? -20.494 84.599  111.241 1.00 21.25 ? 704  SER   A O     1 
ATOM   5173  C  CB    . SER   A  1  706  ? -20.642 81.475  112.332 1.00 22.16 ? 704  SER   A CB    1 
ATOM   5174  O  OG    . SER   A  1  706  ? -21.540 82.123  113.208 1.00 22.36 ? 704  SER   A OG    1 
ATOM   5175  N  N     . PRO   A  1  707  ? -20.434 83.056  109.622 1.00 22.14 ? 705  PRO   A N     1 
ATOM   5176  C  CA    . PRO   A  1  707  ? -20.983 83.962  108.612 1.00 21.82 ? 705  PRO   A CA    1 
ATOM   5177  C  C     . PRO   A  1  707  ? -22.508 83.901  108.613 1.00 19.50 ? 705  PRO   A C     1 
ATOM   5178  O  O     . PRO   A  1  707  ? -23.120 83.011  109.201 1.00 22.42 ? 705  PRO   A O     1 
ATOM   5179  C  CB    . PRO   A  1  707  ? -20.441 83.354  107.315 1.00 21.63 ? 705  PRO   A CB    1 
ATOM   5180  C  CG    . PRO   A  1  707  ? -20.437 81.893  107.588 1.00 21.29 ? 705  PRO   A CG    1 
ATOM   5181  C  CD    . PRO   A  1  707  ? -20.057 81.755  109.050 1.00 18.96 ? 705  PRO   A CD    1 
ATOM   5182  N  N     . TRP   A  1  708  ? -23.115 84.874  107.939 1.00 21.29 ? 706  TRP   A N     1 
ATOM   5183  C  CA    . TRP   A  1  708  ? -24.576 84.901  107.909 1.00 21.34 ? 706  TRP   A CA    1 
ATOM   5184  C  C     . TRP   A  1  708  ? -25.161 83.859  106.969 1.00 22.60 ? 706  TRP   A C     1 
ATOM   5185  O  O     . TRP   A  1  708  ? -26.301 83.433  107.168 1.00 23.53 ? 706  TRP   A O     1 
ATOM   5186  C  CB    . TRP   A  1  708  ? -25.105 86.290  107.517 1.00 20.73 ? 706  TRP   A CB    1 
ATOM   5187  C  CG    . TRP   A  1  708  ? -24.948 86.551  106.055 1.00 23.02 ? 706  TRP   A CG    1 
ATOM   5188  C  CD1   . TRP   A  1  708  ? -23.917 87.197  105.444 1.00 21.95 ? 706  TRP   A CD1   1 
ATOM   5189  C  CD2   . TRP   A  1  708  ? -25.841 86.140  105.010 1.00 21.98 ? 706  TRP   A CD2   1 
ATOM   5190  N  NE1   . TRP   A  1  708  ? -24.102 87.203  104.087 1.00 22.88 ? 706  TRP   A NE1   1 
ATOM   5191  C  CE2   . TRP   A  1  708  ? -25.273 86.558  103.791 1.00 21.90 ? 706  TRP   A CE2   1 
ATOM   5192  C  CE3   . TRP   A  1  708  ? -27.060 85.455  104.988 1.00 22.50 ? 706  TRP   A CE3   1 
ATOM   5193  C  CZ2   . TRP   A  1  708  ? -25.880 86.321  102.561 1.00 21.53 ? 706  TRP   A CZ2   1 
ATOM   5194  C  CZ3   . TRP   A  1  708  ? -27.654 85.203  103.763 1.00 23.01 ? 706  TRP   A CZ3   1 
ATOM   5195  C  CH2   . TRP   A  1  708  ? -27.064 85.642  102.566 1.00 22.71 ? 706  TRP   A CH2   1 
ATOM   5196  N  N     . ASN   A  1  709  ? -24.410 83.425  105.961 1.00 19.96 ? 707  ASN   A N     1 
ATOM   5197  C  CA    . ASN   A  1  709  ? -25.074 82.798  104.827 1.00 21.35 ? 707  ASN   A CA    1 
ATOM   5198  C  C     . ASN   A  1  709  ? -25.396 81.333  105.053 1.00 22.92 ? 707  ASN   A C     1 
ATOM   5199  O  O     . ASN   A  1  709  ? -26.282 80.801  104.384 1.00 23.23 ? 707  ASN   A O     1 
ATOM   5200  C  CB    . ASN   A  1  709  ? -24.233 82.977  103.576 1.00 20.32 ? 707  ASN   A CB    1 
ATOM   5201  C  CG    . ASN   A  1  709  ? -22.988 82.157  103.621 1.00 24.25 ? 707  ASN   A CG    1 
ATOM   5202  O  OD1   . ASN   A  1  709  ? -22.116 82.386  104.456 1.00 24.88 ? 707  ASN   A OD1   1 
ATOM   5203  N  ND2   . ASN   A  1  709  ? -22.893 81.178  102.731 1.00 20.62 ? 707  ASN   A ND2   1 
ATOM   5204  N  N     . PHE   A  1  710  ? -24.682 80.662  105.948 1.00 22.10 ? 708  PHE   A N     1 
ATOM   5205  C  CA    . PHE   A  1  710  ? -25.054 79.339  106.431 1.00 20.73 ? 708  PHE   A CA    1 
ATOM   5206  C  C     . PHE   A  1  710  ? -25.256 79.512  107.930 1.00 22.97 ? 708  PHE   A C     1 
ATOM   5207  O  O     . PHE   A  1  710  ? -24.415 79.108  108.745 1.00 22.27 ? 708  PHE   A O     1 
ATOM   5208  C  CB    . PHE   A  1  710  ? -23.978 78.302  106.115 1.00 20.73 ? 708  PHE   A CB    1 
ATOM   5209  C  CG    . PHE   A  1  710  ? -23.741 78.095  104.640 1.00 25.67 ? 708  PHE   A CG    1 
ATOM   5210  C  CD1   . PHE   A  1  710  ? -24.796 78.062  103.744 1.00 26.86 ? 708  PHE   A CD1   1 
ATOM   5211  C  CD2   . PHE   A  1  710  ? -22.451 77.920  104.157 1.00 25.08 ? 708  PHE   A CD2   1 
ATOM   5212  C  CE1   . PHE   A  1  710  ? -24.571 77.859  102.392 1.00 28.32 ? 708  PHE   A CE1   1 
ATOM   5213  C  CE2   . PHE   A  1  710  ? -22.215 77.718  102.809 1.00 24.79 ? 708  PHE   A CE2   1 
ATOM   5214  C  CZ    . PHE   A  1  710  ? -23.275 77.689  101.924 1.00 26.65 ? 708  PHE   A CZ    1 
ATOM   5215  N  N     . PRO   A  1  711  ? -26.369 80.135  108.323 1.00 22.28 ? 709  PRO   A N     1 
ATOM   5216  C  CA    . PRO   A  1  711  ? -26.474 80.691  109.678 1.00 22.50 ? 709  PRO   A CA    1 
ATOM   5217  C  C     . PRO   A  1  711  ? -26.705 79.657  110.751 1.00 22.52 ? 709  PRO   A C     1 
ATOM   5218  O  O     . PRO   A  1  711  ? -26.555 79.976  111.938 1.00 22.62 ? 709  PRO   A O     1 
ATOM   5219  C  CB    . PRO   A  1  711  ? -27.674 81.632  109.563 1.00 24.20 ? 709  PRO   A CB    1 
ATOM   5220  C  CG    . PRO   A  1  711  ? -28.536 80.981  108.540 1.00 22.20 ? 709  PRO   A CG    1 
ATOM   5221  C  CD    . PRO   A  1  711  ? -27.583 80.384  107.526 1.00 21.86 ? 709  PRO   A CD    1 
ATOM   5222  N  N     . LEU   A  1  712  ? -27.087 78.443  110.385 1.00 22.94 ? 710  LEU   A N     1 
ATOM   5223  C  CA    . LEU   A  1  712  ? -27.187 77.363  111.350 1.00 21.00 ? 710  LEU   A CA    1 
ATOM   5224  C  C     . LEU   A  1  712  ? -26.106 76.321  111.150 1.00 21.41 ? 710  LEU   A C     1 
ATOM   5225  O  O     . LEU   A  1  712  ? -25.478 75.899  112.118 1.00 19.67 ? 710  LEU   A O     1 
ATOM   5226  C  CB    . LEU   A  1  712  ? -28.569 76.698  111.277 1.00 20.90 ? 710  LEU   A CB    1 
ATOM   5227  C  CG    . LEU   A  1  712  ? -28.751 75.583  112.306 1.00 23.19 ? 710  LEU   A CG    1 
ATOM   5228  C  CD1   . LEU   A  1  712  ? -28.676 76.153  113.727 1.00 22.44 ? 710  LEU   A CD1   1 
ATOM   5229  C  CD2   . LEU   A  1  712  ? -30.046 74.812  112.072 1.00 24.50 ? 710  LEU   A CD2   1 
ATOM   5230  N  N     . ALA   A  1  713  ? -25.830 75.953  109.901 1.00 19.40 ? 711  ALA   A N     1 
ATOM   5231  C  CA    . ALA   A  1  713  ? -24.935 74.834  109.640 1.00 17.95 ? 711  ALA   A CA    1 
ATOM   5232  C  C     . ALA   A  1  713  ? -23.503 75.154  110.049 1.00 20.34 ? 711  ALA   A C     1 
ATOM   5233  O  O     . ALA   A  1  713  ? -22.902 74.436  110.849 1.00 21.13 ? 711  ALA   A O     1 
ATOM   5234  C  CB    . ALA   A  1  713  ? -24.993 74.442  108.165 1.00 18.74 ? 711  ALA   A CB    1 
ATOM   5235  N  N     . ILE   A  1  714  ? -22.923 76.213  109.489 1.00 18.62 ? 712  ILE   A N     1 
ATOM   5236  C  CA    . ILE   A  1  714  ? -21.533 76.514  109.823 1.00 17.25 ? 712  ILE   A CA    1 
ATOM   5237  C  C     . ILE   A  1  714  ? -21.420 76.926  111.277 1.00 20.71 ? 712  ILE   A C     1 
ATOM   5238  O  O     . ILE   A  1  714  ? -20.478 76.539  111.984 1.00 20.43 ? 712  ILE   A O     1 
ATOM   5239  C  CB    . ILE   A  1  714  ? -20.972 77.580  108.875 1.00 21.27 ? 712  ILE   A CB    1 
ATOM   5240  C  CG1   . ILE   A  1  714  ? -20.819 76.945  107.490 1.00 22.98 ? 712  ILE   A CG1   1 
ATOM   5241  C  CG2   . ILE   A  1  714  ? -19.643 78.143  109.417 1.00 21.59 ? 712  ILE   A CG2   1 
ATOM   5242  C  CD1   . ILE   A  1  714  ? -19.974 77.716  106.560 1.00 30.41 ? 712  ILE   A CD1   1 
ATOM   5243  N  N     . PHE   A  1  715  ? -22.382 77.719  111.743 1.00 21.03 ? 713  PHE   A N     1 
ATOM   5244  C  CA    . PHE   A  1  715  ? -22.455 78.079  113.150 1.00 19.75 ? 713  PHE   A CA    1 
ATOM   5245  C  C     . PHE   A  1  715  ? -22.390 76.838  114.035 1.00 23.83 ? 713  PHE   A C     1 
ATOM   5246  O  O     . PHE   A  1  715  ? -21.524 76.722  114.909 1.00 21.14 ? 713  PHE   A O     1 
ATOM   5247  C  CB    . PHE   A  1  715  ? -23.767 78.828  113.369 1.00 20.99 ? 713  PHE   A CB    1 
ATOM   5248  C  CG    . PHE   A  1  715  ? -24.005 79.210  114.780 1.00 23.24 ? 713  PHE   A CG    1 
ATOM   5249  C  CD1   . PHE   A  1  715  ? -23.381 80.320  115.308 1.00 23.42 ? 713  PHE   A CD1   1 
ATOM   5250  C  CD2   . PHE   A  1  715  ? -24.845 78.458  115.589 1.00 24.52 ? 713  PHE   A CD2   1 
ATOM   5251  C  CE1   . PHE   A  1  715  ? -23.599 80.687  116.616 1.00 26.00 ? 713  PHE   A CE1   1 
ATOM   5252  C  CE2   . PHE   A  1  715  ? -25.064 78.815  116.897 1.00 25.65 ? 713  PHE   A CE2   1 
ATOM   5253  C  CZ    . PHE   A  1  715  ? -24.445 79.936  117.412 1.00 25.83 ? 713  PHE   A CZ    1 
ATOM   5254  N  N     . THR   A  1  716  ? -23.289 75.882  113.795 1.00 20.63 ? 714  THR   A N     1 
ATOM   5255  C  CA    . THR   A  1  716  ? -23.318 74.662  114.599 1.00 20.68 ? 714  THR   A CA    1 
ATOM   5256  C  C     . THR   A  1  716  ? -22.042 73.854  114.433 1.00 20.41 ? 714  THR   A C     1 
ATOM   5257  O  O     . THR   A  1  716  ? -21.495 73.335  115.414 1.00 20.85 ? 714  THR   A O     1 
ATOM   5258  C  CB    . THR   A  1  716  ? -24.521 73.812  114.188 1.00 22.30 ? 714  THR   A CB    1 
ATOM   5259  O  OG1   . THR   A  1  716  ? -25.728 74.546  114.443 1.00 22.95 ? 714  THR   A OG1   1 
ATOM   5260  C  CG2   . THR   A  1  716  ? -24.552 72.515  114.969 1.00 22.58 ? 714  THR   A CG2   1 
ATOM   5261  N  N     . GLY   A  1  717  ? -21.553 73.738  113.196 1.00 18.77 ? 715  GLY   A N     1 
ATOM   5262  C  CA    . GLY   A  1  717  ? -20.368 72.929  112.949 1.00 20.15 ? 715  GLY   A CA    1 
ATOM   5263  C  C     . GLY   A  1  717  ? -19.169 73.389  113.758 1.00 21.62 ? 715  GLY   A C     1 
ATOM   5264  O  O     . GLY   A  1  717  ? -18.521 72.591  114.433 1.00 20.46 ? 715  GLY   A O     1 
ATOM   5265  N  N     . GLN   A  1  718  ? -18.869 74.689  113.720 1.00 17.93 ? 716  GLN   A N     1 
ATOM   5266  C  CA    . GLN   A  1  718  ? -17.684 75.168  114.435 1.00 19.72 ? 716  GLN   A CA    1 
ATOM   5267  C  C     . GLN   A  1  718  ? -17.840 74.954  115.929 1.00 21.60 ? 716  GLN   A C     1 
ATOM   5268  O  O     . GLN   A  1  718  ? -16.924 74.474  116.606 1.00 19.90 ? 716  GLN   A O     1 
ATOM   5269  C  CB    . GLN   A  1  718  ? -17.453 76.651  114.155 1.00 18.02 ? 716  GLN   A CB    1 
ATOM   5270  C  CG    . GLN   A  1  718  ? -17.112 76.945  112.708 1.00 18.92 ? 716  GLN   A CG    1 
ATOM   5271  C  CD    . GLN   A  1  718  ? -16.702 78.382  112.477 1.00 21.72 ? 716  GLN   A CD    1 
ATOM   5272  O  OE1   . GLN   A  1  718  ? -15.744 78.650  111.746 1.00 21.68 ? 716  GLN   A OE1   1 
ATOM   5273  N  NE2   . GLN   A  1  718  ? -17.398 79.314  113.113 1.00 22.30 ? 716  GLN   A NE2   1 
ATOM   5274  N  N     . ILE   A  1  719  ? -19.007 75.312  116.457 1.00 19.66 ? 717  ILE   A N     1 
ATOM   5275  C  CA    . ILE   A  1  719  ? -19.250 75.217  117.891 1.00 21.23 ? 717  ILE   A CA    1 
ATOM   5276  C  C     . ILE   A  1  719  ? -19.218 73.767  118.346 1.00 21.07 ? 717  ILE   A C     1 
ATOM   5277  O  O     . ILE   A  1  719  ? -18.612 73.433  119.370 1.00 22.22 ? 717  ILE   A O     1 
ATOM   5278  C  CB    . ILE   A  1  719  ? -20.587 75.886  118.233 1.00 24.79 ? 717  ILE   A CB    1 
ATOM   5279  C  CG1   . ILE   A  1  719  ? -20.443 77.390  118.080 1.00 22.66 ? 717  ILE   A CG1   1 
ATOM   5280  C  CG2   . ILE   A  1  719  ? -21.033 75.484  119.612 1.00 29.32 ? 717  ILE   A CG2   1 
ATOM   5281  C  CD1   . ILE   A  1  719  ? -21.755 78.034  117.834 1.00 28.96 ? 717  ILE   A CD1   1 
ATOM   5282  N  N     . ALA   A  1  720  ? -19.877 72.888  117.593 1.00 21.11 ? 718  ALA   A N     1 
ATOM   5283  C  CA    . ALA   A  1  720  ? -19.935 71.479  117.967 1.00 23.39 ? 718  ALA   A CA    1 
ATOM   5284  C  C     . ALA   A  1  720  ? -18.541 70.875  118.018 1.00 20.72 ? 718  ALA   A C     1 
ATOM   5285  O  O     . ALA   A  1  720  ? -18.204 70.157  118.965 1.00 20.14 ? 718  ALA   A O     1 
ATOM   5286  C  CB    . ALA   A  1  720  ? -20.804 70.712  116.967 1.00 21.06 ? 718  ALA   A CB    1 
ATOM   5287  N  N     . ALA   A  1  721  ? -17.725 71.163  117.005 1.00 19.05 ? 719  ALA   A N     1 
ATOM   5288  C  CA    . ALA   A  1  721  ? -16.363 70.650  116.966 1.00 18.84 ? 719  ALA   A CA    1 
ATOM   5289  C  C     . ALA   A  1  721  ? -15.572 71.127  118.179 1.00 20.13 ? 719  ALA   A C     1 
ATOM   5290  O  O     . ALA   A  1  721  ? -14.943 70.324  118.878 1.00 19.96 ? 719  ALA   A O     1 
ATOM   5291  C  CB    . ALA   A  1  721  ? -15.687 71.085  115.669 1.00 18.97 ? 719  ALA   A CB    1 
ATOM   5292  N  N     . ALA   A  1  722  ? -15.606 72.435  118.453 1.00 18.99 ? 720  ALA   A N     1 
ATOM   5293  C  CA    . ALA   A  1  722  ? -14.843 72.964  119.581 1.00 19.78 ? 720  ALA   A CA    1 
ATOM   5294  C  C     . ALA   A  1  722  ? -15.320 72.363  120.899 1.00 22.98 ? 720  ALA   A C     1 
ATOM   5295  O  O     . ALA   A  1  722  ? -14.512 71.933  121.729 1.00 21.45 ? 720  ALA   A O     1 
ATOM   5296  C  CB    . ALA   A  1  722  ? -14.927 74.491  119.606 1.00 19.82 ? 720  ALA   A CB    1 
ATOM   5297  N  N     . LEU   A  1  723  ? -16.638 72.316  121.102 1.00 19.48 ? 721  LEU   A N     1 
ATOM   5298  C  CA    . LEU   A  1  723  ? -17.189 71.754  122.327 1.00 19.81 ? 721  LEU   A CA    1 
ATOM   5299  C  C     . LEU   A  1  723  ? -16.806 70.292  122.495 1.00 21.13 ? 721  LEU   A C     1 
ATOM   5300  O  O     . LEU   A  1  723  ? -16.415 69.861  123.584 1.00 20.56 ? 721  LEU   A O     1 
ATOM   5301  C  CB    . LEU   A  1  723  ? -18.707 71.863  122.289 1.00 21.52 ? 721  LEU   A CB    1 
ATOM   5302  C  CG    . LEU   A  1  723  ? -19.300 73.248  122.450 1.00 19.48 ? 721  LEU   A CG    1 
ATOM   5303  C  CD1   . LEU   A  1  723  ? -20.790 73.115  122.196 1.00 23.05 ? 721  LEU   A CD1   1 
ATOM   5304  C  CD2   . LEU   A  1  723  ? -19.026 73.765  123.854 1.00 23.87 ? 721  LEU   A CD2   1 
ATOM   5305  N  N     . VAL   A  1  724  ? -16.957 69.496  121.439 1.00 22.24 ? 722  VAL   A N     1 
ATOM   5306  C  CA    . VAL   A  1  724  ? -16.741 68.071  121.629 1.00 20.37 ? 722  VAL   A CA    1 
ATOM   5307  C  C     . VAL   A  1  724  ? -15.264 67.781  121.855 1.00 20.04 ? 722  VAL   A C     1 
ATOM   5308  O  O     . VAL   A  1  724  ? -14.914 66.794  122.510 1.00 23.94 ? 722  VAL   A O     1 
ATOM   5309  C  CB    . VAL   A  1  724  ? -17.352 67.256  120.476 1.00 19.33 ? 722  VAL   A CB    1 
ATOM   5310  C  CG1   . VAL   A  1  724  ? -16.452 67.294  119.228 1.00 22.00 ? 722  VAL   A CG1   1 
ATOM   5311  C  CG2   . VAL   A  1  724  ? -17.670 65.839  120.939 1.00 22.19 ? 722  VAL   A CG2   1 
ATOM   5312  N  N     . ALA   A  1  725  ? -14.384 68.642  121.345 1.00 20.51 ? 723  ALA   A N     1 
ATOM   5313  C  CA    . ALA   A  1  725  ? -12.957 68.565  121.637 1.00 22.23 ? 723  ALA   A CA    1 
ATOM   5314  C  C     . ALA   A  1  725  ? -12.627 68.983  123.067 1.00 22.77 ? 723  ALA   A C     1 
ATOM   5315  O  O     . ALA   A  1  725  ? -11.450 68.949  123.453 1.00 24.42 ? 723  ALA   A O     1 
ATOM   5316  C  CB    . ALA   A  1  725  ? -12.169 69.416  120.644 1.00 20.89 ? 723  ALA   A CB    1 
ATOM   5317  N  N     . GLY   A  1  726  ? -13.619 69.381  123.854 1.00 22.56 ? 724  GLY   A N     1 
ATOM   5318  C  CA    . GLY   A  1  726  ? -13.402 69.716  125.243 1.00 24.40 ? 724  GLY   A CA    1 
ATOM   5319  C  C     . GLY   A  1  726  ? -13.184 71.180  125.536 1.00 24.34 ? 724  GLY   A C     1 
ATOM   5320  O  O     . GLY   A  1  726  ? -12.770 71.513  126.655 1.00 25.75 ? 724  GLY   A O     1 
ATOM   5321  N  N     . ASN   A  1  727  ? -13.453 72.061  124.580 1.00 24.06 ? 725  ASN   A N     1 
ATOM   5322  C  CA    . ASN   A  1  727  ? -13.247 73.488  124.765 1.00 22.65 ? 725  ASN   A CA    1 
ATOM   5323  C  C     . ASN   A  1  727  ? -14.563 74.193  125.046 1.00 24.31 ? 725  ASN   A C     1 
ATOM   5324  O  O     . ASN   A  1  727  ? -15.560 73.954  124.356 1.00 23.00 ? 725  ASN   A O     1 
ATOM   5325  C  CB    . ASN   A  1  727  ? -12.667 74.099  123.492 1.00 23.59 ? 725  ASN   A CB    1 
ATOM   5326  C  CG    . ASN   A  1  727  ? -11.429 73.404  123.027 1.00 22.63 ? 725  ASN   A CG    1 
ATOM   5327  O  OD1   . ASN   A  1  727  ? -10.355 73.591  123.589 1.00 24.00 ? 725  ASN   A OD1   1 
ATOM   5328  N  ND2   . ASN   A  1  727  ? -11.560 72.597  121.988 1.00 22.68 ? 725  ASN   A ND2   1 
ATOM   5329  N  N     . PRO   A  1  728  ? -14.601 75.106  126.003 1.00 22.82 ? 726  PRO   A N     1 
ATOM   5330  C  CA    . PRO   A  1  728  ? -15.758 75.993  126.102 1.00 22.99 ? 726  PRO   A CA    1 
ATOM   5331  C  C     . PRO   A  1  728  ? -15.721 76.972  124.944 1.00 23.28 ? 726  PRO   A C     1 
ATOM   5332  O  O     . PRO   A  1  728  ? -14.653 77.332  124.440 1.00 23.96 ? 726  PRO   A O     1 
ATOM   5333  C  CB    . PRO   A  1  728  ? -15.544 76.707  127.440 1.00 22.35 ? 726  PRO   A CB    1 
ATOM   5334  C  CG    . PRO   A  1  728  ? -14.061 76.716  127.613 1.00 25.36 ? 726  PRO   A CG    1 
ATOM   5335  C  CD    . PRO   A  1  728  ? -13.521 75.484  126.930 1.00 24.11 ? 726  PRO   A CD    1 
ATOM   5336  N  N     . VAL   A  1  729  ? -16.903 77.391  124.512 1.00 23.44 ? 727  VAL   A N     1 
ATOM   5337  C  CA    . VAL   A  1  729  ? -17.069 78.146  123.279 1.00 22.54 ? 727  VAL   A CA    1 
ATOM   5338  C  C     . VAL   A  1  729  ? -17.726 79.486  123.562 1.00 21.30 ? 727  VAL   A C     1 
ATOM   5339  O  O     . VAL   A  1  729  ? -18.684 79.580  124.341 1.00 24.70 ? 727  VAL   A O     1 
ATOM   5340  C  CB    . VAL   A  1  729  ? -17.884 77.340  122.247 1.00 22.94 ? 727  VAL   A CB    1 
ATOM   5341  C  CG1   . VAL   A  1  729  ? -18.350 78.227  121.088 1.00 23.64 ? 727  VAL   A CG1   1 
ATOM   5342  C  CG2   . VAL   A  1  729  ? -17.053 76.191  121.737 1.00 25.64 ? 727  VAL   A CG2   1 
ATOM   5343  N  N     . LEU   A  1  730  ? -17.205 80.518  122.914 1.00 22.26 ? 728  LEU   A N     1 
ATOM   5344  C  CA    . LEU   A  1  730  ? -17.870 81.803  122.782 1.00 24.62 ? 728  LEU   A CA    1 
ATOM   5345  C  C     . LEU   A  1  730  ? -18.359 81.854  121.343 1.00 21.78 ? 728  LEU   A C     1 
ATOM   5346  O  O     . LEU   A  1  730  ? -17.550 81.898  120.411 1.00 23.08 ? 728  LEU   A O     1 
ATOM   5347  C  CB    . LEU   A  1  730  ? -16.908 82.952  123.071 1.00 24.62 ? 728  LEU   A CB    1 
ATOM   5348  C  CG    . LEU   A  1  730  ? -16.262 82.998  124.464 1.00 24.86 ? 728  LEU   A CG    1 
ATOM   5349  C  CD1   . LEU   A  1  730  ? -17.286 82.713  125.549 1.00 25.18 ? 728  LEU   A CD1   1 
ATOM   5350  C  CD2   . LEU   A  1  730  ? -15.089 82.038  124.569 1.00 24.16 ? 728  LEU   A CD2   1 
ATOM   5351  N  N     . ALA   A  1  731  ? -19.678 81.811  121.163 1.00 23.74 ? 729  ALA   A N     1 
ATOM   5352  C  CA    . ALA   A  1  731  ? -20.295 81.748  119.845 1.00 22.49 ? 729  ALA   A CA    1 
ATOM   5353  C  C     . ALA   A  1  731  ? -20.707 83.157  119.440 1.00 23.94 ? 729  ALA   A C     1 
ATOM   5354  O  O     . ALA   A  1  731  ? -21.587 83.758  120.062 1.00 26.74 ? 729  ALA   A O     1 
ATOM   5355  C  CB    . ALA   A  1  731  ? -21.495 80.807  119.863 1.00 23.89 ? 729  ALA   A CB    1 
ATOM   5356  N  N     . LYS   A  1  732  ? -20.071 83.684  118.395 1.00 20.99 ? 730  LYS   A N     1 
ATOM   5357  C  CA    . LYS   A  1  732  ? -20.397 85.014  117.895 1.00 21.96 ? 730  LYS   A CA    1 
ATOM   5358  C  C     . LYS   A  1  732  ? -21.010 84.843  116.511 1.00 21.71 ? 730  LYS   A C     1 
ATOM   5359  O  O     . LYS   A  1  732  ? -20.287 84.769  115.508 1.00 22.13 ? 730  LYS   A O     1 
ATOM   5360  C  CB    . LYS   A  1  732  ? -19.139 85.881  117.835 1.00 26.14 ? 730  LYS   A CB    1 
ATOM   5361  C  CG    . LYS   A  1  732  ? -19.377 87.345  118.150 1.00 23.79 ? 730  LYS   A CG    1 
ATOM   5362  C  CD    . LYS   A  1  732  ? -20.371 87.984  117.172 1.00 23.91 ? 730  LYS   A CD    1 
ATOM   5363  C  CE    . LYS   A  1  732  ? -19.768 88.102  115.780 1.00 24.55 ? 730  LYS   A CE    1 
ATOM   5364  N  NZ    . LYS   A  1  732  ? -20.729 88.676  114.790 1.00 25.44 ? 730  LYS   A NZ    1 
ATOM   5365  N  N     . PRO   A  1  733  ? -22.332 84.777  116.397 1.00 21.56 ? 731  PRO   A N     1 
ATOM   5366  C  CA    . PRO   A  1  733  ? -22.950 84.627  115.080 1.00 23.20 ? 731  PRO   A CA    1 
ATOM   5367  C  C     . PRO   A  1  733  ? -22.934 85.946  114.331 1.00 22.32 ? 731  PRO   A C     1 
ATOM   5368  O  O     . PRO   A  1  733  ? -22.817 87.027  114.913 1.00 23.84 ? 731  PRO   A O     1 
ATOM   5369  C  CB    . PRO   A  1  733  ? -24.388 84.239  115.422 1.00 22.82 ? 731  PRO   A CB    1 
ATOM   5370  C  CG    . PRO   A  1  733  ? -24.646 84.954  116.715 1.00 25.47 ? 731  PRO   A CG    1 
ATOM   5371  C  CD    . PRO   A  1  733  ? -23.334 84.850  117.473 1.00 24.35 ? 731  PRO   A CD    1 
ATOM   5372  N  N     . ALA   A  1  734  ? -23.063 85.834  113.014 1.00 22.17 ? 732  ALA   A N     1 
ATOM   5373  C  CA    . ALA   A  1  734  ? -23.134 87.014  112.171 1.00 22.10 ? 732  ALA   A CA    1 
ATOM   5374  C  C     . ALA   A  1  734  ? -24.254 87.935  112.640 1.00 22.89 ? 732  ALA   A C     1 
ATOM   5375  O  O     . ALA   A  1  734  ? -25.313 87.490  113.101 1.00 25.28 ? 732  ALA   A O     1 
ATOM   5376  C  CB    . ALA   A  1  734  ? -23.413 86.587  110.734 1.00 21.21 ? 732  ALA   A CB    1 
ATOM   5377  N  N     . GLU   A  1  735  ? -24.018 89.238  112.511 1.00 25.12 ? 733  GLU   A N     1 
ATOM   5378  C  CA    . GLU   A  1  735  ? -25.020 90.203  112.946 1.00 27.78 ? 733  GLU   A CA    1 
ATOM   5379  C  C     . GLU   A  1  735  ? -26.318 90.091  112.154 1.00 25.63 ? 733  GLU   A C     1 
ATOM   5380  O  O     . GLU   A  1  735  ? -27.373 90.491  112.657 1.00 26.33 ? 733  GLU   A O     1 
ATOM   5381  C  CB    . GLU   A  1  735  ? -24.465 91.624  112.860 1.00 27.62 ? 733  GLU   A CB    1 
ATOM   5382  C  CG    . GLU   A  1  735  ? -23.945 92.015  111.481 1.00 27.80 ? 733  GLU   A CG    1 
ATOM   5383  C  CD    . GLU   A  1  735  ? -22.447 91.761  111.306 1.00 32.26 ? 733  GLU   A CD    1 
ATOM   5384  O  OE1   . GLU   A  1  735  ? -21.916 90.825  111.943 1.00 29.45 ? 733  GLU   A OE1   1 
ATOM   5385  O  OE2   . GLU   A  1  735  ? -21.806 92.502  110.529 1.00 31.95 ? 733  GLU   A OE2   1 
ATOM   5386  N  N     . GLU   A  1  736  ? -26.272 89.536  110.942 1.00 24.90 ? 734  GLU   A N     1 
ATOM   5387  C  CA    . GLU   A  1  736  ? -27.482 89.458  110.136 1.00 22.13 ? 734  GLU   A CA    1 
ATOM   5388  C  C     . GLU   A  1  736  ? -28.416 88.350  110.596 1.00 25.33 ? 734  GLU   A C     1 
ATOM   5389  O  O     . GLU   A  1  736  ? -29.632 88.468  110.417 1.00 27.12 ? 734  GLU   A O     1 
ATOM   5390  C  CB    . GLU   A  1  736  ? -27.131 89.242  108.662 1.00 24.65 ? 734  GLU   A CB    1 
ATOM   5391  C  CG    . GLU   A  1  736  ? -26.310 90.353  108.024 1.00 26.81 ? 734  GLU   A CG    1 
ATOM   5392  C  CD    . GLU   A  1  736  ? -24.814 90.126  108.138 1.00 31.12 ? 734  GLU   A CD    1 
ATOM   5393  O  OE1   . GLU   A  1  736  ? -24.386 89.322  108.999 1.00 26.72 ? 734  GLU   A OE1   1 
ATOM   5394  O  OE2   . GLU   A  1  736  ? -24.064 90.744  107.352 1.00 28.55 ? 734  GLU   A OE2   1 
ATOM   5395  N  N     . THR   A  1  737  ? -27.885 87.272  111.170 1.00 25.47 ? 735  THR   A N     1 
ATOM   5396  C  CA    . THR   A  1  737  ? -28.660 86.057  111.430 1.00 24.69 ? 735  THR   A CA    1 
ATOM   5397  C  C     . THR   A  1  737  ? -28.471 85.552  112.860 1.00 24.07 ? 735  THR   A C     1 
ATOM   5398  O  O     . THR   A  1  737  ? -28.099 84.395  113.082 1.00 24.17 ? 735  THR   A O     1 
ATOM   5399  C  CB    . THR   A  1  737  ? -28.296 84.980  110.410 1.00 23.67 ? 735  THR   A CB    1 
ATOM   5400  O  OG1   . THR   A  1  737  ? -26.866 84.786  110.400 1.00 23.57 ? 735  THR   A OG1   1 
ATOM   5401  C  CG2   . THR   A  1  737  ? -28.764 85.384  109.025 1.00 24.27 ? 735  THR   A CG2   1 
ATOM   5402  N  N     . PRO   A  1  738  ? -28.766 86.384  113.867 1.00 23.51 ? 736  PRO   A N     1 
ATOM   5403  C  CA    . PRO   A  1  738  ? -28.598 85.930  115.256 1.00 26.11 ? 736  PRO   A CA    1 
ATOM   5404  C  C     . PRO   A  1  738  ? -29.675 84.973  115.738 1.00 25.27 ? 736  PRO   A C     1 
ATOM   5405  O  O     . PRO   A  1  738  ? -29.416 84.209  116.679 1.00 24.90 ? 736  PRO   A O     1 
ATOM   5406  C  CB    . PRO   A  1  738  ? -28.668 87.238  116.053 1.00 26.69 ? 736  PRO   A CB    1 
ATOM   5407  C  CG    . PRO   A  1  738  ? -29.625 88.063  115.263 1.00 25.93 ? 736  PRO   A CG    1 
ATOM   5408  C  CD    . PRO   A  1  738  ? -29.314 87.753  113.813 1.00 25.98 ? 736  PRO   A CD    1 
ATOM   5409  N  N     . LEU   A  1  739  ? -30.875 84.995  115.151 1.00 23.66 ? 737  LEU   A N     1 
ATOM   5410  C  CA    . LEU   A  1  739  ? -31.991 84.261  115.744 1.00 23.90 ? 737  LEU   A CA    1 
ATOM   5411  C  C     . LEU   A  1  739  ? -31.810 82.755  115.599 1.00 23.33 ? 737  LEU   A C     1 
ATOM   5412  O  O     . LEU   A  1  739  ? -32.019 82.000  116.554 1.00 24.74 ? 737  LEU   A O     1 
ATOM   5413  C  CB    . LEU   A  1  739  ? -33.310 84.699  115.113 1.00 23.81 ? 737  LEU   A CB    1 
ATOM   5414  C  CG    . LEU   A  1  739  ? -33.654 86.179  115.214 1.00 26.60 ? 737  LEU   A CG    1 
ATOM   5415  C  CD1   . LEU   A  1  739  ? -34.897 86.467  114.377 1.00 22.25 ? 737  LEU   A CD1   1 
ATOM   5416  C  CD2   . LEU   A  1  739  ? -33.898 86.572  116.659 1.00 28.33 ? 737  LEU   A CD2   1 
ATOM   5417  N  N     . ILE   A  1  740  ? -31.466 82.292  114.402 1.00 21.45 ? 738  ILE   A N     1 
ATOM   5418  C  CA    . ILE   A  1  740  ? -31.287 80.856  114.227 1.00 21.55 ? 738  ILE   A CA    1 
ATOM   5419  C  C     . ILE   A  1  740  ? -30.079 80.380  115.026 1.00 22.07 ? 738  ILE   A C     1 
ATOM   5420  O  O     . ILE   A  1  740  ? -30.072 79.265  115.555 1.00 24.13 ? 738  ILE   A O     1 
ATOM   5421  C  CB    . ILE   A  1  740  ? -31.218 80.492  112.732 1.00 25.26 ? 738  ILE   A CB    1 
ATOM   5422  C  CG1   . ILE   A  1  740  ? -31.203 78.974  112.542 1.00 24.57 ? 738  ILE   A CG1   1 
ATOM   5423  C  CG2   . ILE   A  1  740  ? -29.983 81.092  112.104 1.00 24.35 ? 738  ILE   A CG2   1 
ATOM   5424  C  CD1   . ILE   A  1  740  ? -32.407 78.273  113.144 1.00 28.40 ? 738  ILE   A CD1   1 
ATOM   5425  N  N     . ALA   A  1  741  ? -29.067 81.232  115.170 1.00 24.74 ? 739  ALA   A N     1 
ATOM   5426  C  CA    . ALA   A  1  741  ? -27.939 80.905  116.034 1.00 24.34 ? 739  ALA   A CA    1 
ATOM   5427  C  C     . ALA   A  1  741  ? -28.388 80.754  117.481 1.00 22.86 ? 739  ALA   A C     1 
ATOM   5428  O  O     . ALA   A  1  741  ? -28.007 79.793  118.161 1.00 24.49 ? 739  ALA   A O     1 
ATOM   5429  C  CB    . ALA   A  1  741  ? -26.885 81.996  115.923 1.00 25.84 ? 739  ALA   A CB    1 
ATOM   5430  N  N     . ALA   A  1  742  ? -29.204 81.691  117.969 1.00 22.65 ? 740  ALA   A N     1 
ATOM   5431  C  CA    . ALA   A  1  742  ? -29.699 81.580  119.333 1.00 23.74 ? 740  ALA   A CA    1 
ATOM   5432  C  C     . ALA   A  1  742  ? -30.485 80.294  119.519 1.00 24.68 ? 740  ALA   A C     1 
ATOM   5433  O  O     . ALA   A  1  742  ? -30.387 79.646  120.567 1.00 26.14 ? 740  ALA   A O     1 
ATOM   5434  C  CB    . ALA   A  1  742  ? -30.557 82.794  119.694 1.00 24.51 ? 740  ALA   A CB    1 
ATOM   5435  N  N     . GLU   A  1  743  ? -31.266 79.905  118.509 1.00 23.83 ? 741  GLU   A N     1 
ATOM   5436  C  CA    . GLU   A  1  743  ? -32.021 78.663  118.608 1.00 26.34 ? 741  GLU   A CA    1 
ATOM   5437  C  C     . GLU   A  1  743  ? -31.093 77.452  118.603 1.00 23.51 ? 741  GLU   A C     1 
ATOM   5438  O  O     . GLU   A  1  743  ? -31.319 76.484  119.342 1.00 25.18 ? 741  GLU   A O     1 
ATOM   5439  C  CB    . GLU   A  1  743  ? -33.047 78.594  117.479 1.00 25.18 ? 741  GLU   A CB    1 
ATOM   5440  C  CG    . GLU   A  1  743  ? -33.808 77.288  117.388 1.00 28.54 ? 741  GLU   A CG    1 
ATOM   5441  C  CD    . GLU   A  1  743  ? -34.769 77.048  118.543 1.00 24.55 ? 741  GLU   A CD    1 
ATOM   5442  O  OE1   . GLU   A  1  743  ? -34.931 77.932  119.411 1.00 27.17 ? 741  GLU   A OE1   1 
ATOM   5443  O  OE2   . GLU   A  1  743  ? -35.350 75.944  118.585 1.00 33.24 ? 741  GLU   A OE2   1 
ATOM   5444  N  N     . GLY   A  1  744  ? -30.026 77.498  117.803 1.00 23.39 ? 742  GLY   A N     1 
ATOM   5445  C  CA    . GLY   A  1  744  ? -29.050 76.421  117.839 1.00 23.15 ? 742  GLY   A CA    1 
ATOM   5446  C  C     . GLY   A  1  744  ? -28.382 76.292  119.195 1.00 23.03 ? 742  GLY   A C     1 
ATOM   5447  O  O     . GLY   A  1  744  ? -28.212 75.185  119.712 1.00 24.43 ? 742  GLY   A O     1 
ATOM   5448  N  N     . VAL   A  1  745  ? -27.995 77.423  119.788 1.00 23.35 ? 743  VAL   A N     1 
ATOM   5449  C  CA    . VAL   A  1  745  ? -27.434 77.402  121.136 1.00 25.07 ? 743  VAL   A CA    1 
ATOM   5450  C  C     . VAL   A  1  745  ? -28.457 76.868  122.137 1.00 27.63 ? 743  VAL   A C     1 
ATOM   5451  O  O     . VAL   A  1  745  ? -28.120 76.085  123.035 1.00 27.92 ? 743  VAL   A O     1 
ATOM   5452  C  CB    . VAL   A  1  745  ? -26.914 78.801  121.515 1.00 27.09 ? 743  VAL   A CB    1 
ATOM   5453  C  CG1   . VAL   A  1  745  ? -26.663 78.901  123.019 1.00 29.78 ? 743  VAL   A CG1   1 
ATOM   5454  C  CG2   . VAL   A  1  745  ? -25.630 79.110  120.748 1.00 25.61 ? 743  VAL   A CG2   1 
ATOM   5455  N  N     . ARG   A  1  746  ? -29.725 77.268  121.991 1.00 26.08 ? 744  ARG   A N     1 
ATOM   5456  C  CA    . ARG   A  1  746  ? -30.752 76.747  122.890 1.00 26.11 ? 744  ARG   A CA    1 
ATOM   5457  C  C     . ARG   A  1  746  ? -30.841 75.227  122.785 1.00 24.89 ? 744  ARG   A C     1 
ATOM   5458  O  O     . ARG   A  1  746  ? -30.920 74.525  123.797 1.00 27.85 ? 744  ARG   A O     1 
ATOM   5459  C  CB    . ARG   A  1  746  ? -32.102 77.380  122.557 1.00 28.10 ? 744  ARG   A CB    1 
ATOM   5460  C  CG    . ARG   A  1  746  ? -33.179 77.096  123.591 1.00 29.35 ? 744  ARG   A CG    1 
ATOM   5461  C  CD    . ARG   A  1  746  ? -34.581 77.355  123.040 1.00 28.44 ? 744  ARG   A CD    1 
ATOM   5462  N  NE    . ARG   A  1  746  ? -34.901 76.459  121.935 1.00 30.42 ? 744  ARG   A NE    1 
ATOM   5463  C  CZ    . ARG   A  1  746  ? -35.249 75.188  122.080 1.00 32.25 ? 744  ARG   A CZ    1 
ATOM   5464  N  NH1   . ARG   A  1  746  ? -35.339 74.627  123.277 1.00 36.07 ? 744  ARG   A NH1   1 
ATOM   5465  N  NH2   . ARG   A  1  746  ? -35.508 74.458  120.998 1.00 31.04 ? 744  ARG   A NH2   1 
ATOM   5466  N  N     . ILE   A  1  747  ? -30.795 74.705  121.559 1.00 24.48 ? 745  ILE   A N     1 
ATOM   5467  C  CA    . ILE   A  1  747  ? -30.845 73.263  121.342 1.00 24.01 ? 745  ILE   A CA    1 
ATOM   5468  C  C     . ILE   A  1  747  ? -29.622 72.580  121.943 1.00 23.78 ? 745  ILE   A C     1 
ATOM   5469  O  O     . ILE   A  1  747  ? -29.735 71.546  122.611 1.00 23.82 ? 745  ILE   A O     1 
ATOM   5470  C  CB    . ILE   A  1  747  ? -30.997 72.973  119.840 1.00 23.78 ? 745  ILE   A CB    1 
ATOM   5471  C  CG1   . ILE   A  1  747  ? -32.423 73.336  119.412 1.00 24.31 ? 745  ILE   A CG1   1 
ATOM   5472  C  CG2   . ILE   A  1  747  ? -30.629 71.515  119.521 1.00 27.57 ? 745  ILE   A CG2   1 
ATOM   5473  C  CD1   . ILE   A  1  747  ? -32.614 73.471  117.925 1.00 25.61 ? 745  ILE   A CD1   1 
ATOM   5474  N  N     . LEU   A  1  748  ? -28.430 73.128  121.694 1.00 24.02 ? 746  LEU   A N     1 
ATOM   5475  C  CA    . LEU   A  1  748  ? -27.226 72.536  122.267 1.00 23.54 ? 746  LEU   A CA    1 
ATOM   5476  C  C     . LEU   A  1  748  ? -27.286 72.530  123.785 1.00 26.70 ? 746  LEU   A C     1 
ATOM   5477  O  O     . LEU   A  1  748  ? -26.912 71.543  124.426 1.00 25.43 ? 746  LEU   A O     1 
ATOM   5478  C  CB    . LEU   A  1  748  ? -25.987 73.278  121.774 1.00 23.42 ? 746  LEU   A CB    1 
ATOM   5479  C  CG    . LEU   A  1  748  ? -25.470 72.790  120.427 1.00 26.31 ? 746  LEU   A CG    1 
ATOM   5480  C  CD1   . LEU   A  1  748  ? -24.478 73.787  119.850 1.00 30.02 ? 746  LEU   A CD1   1 
ATOM   5481  C  CD2   . LEU   A  1  748  ? -24.822 71.429  120.590 1.00 28.17 ? 746  LEU   A CD2   1 
ATOM   5482  N  N     . ARG   A  1  749  ? -27.778 73.613  124.379 1.00 24.63 ? 747  ARG   A N     1 
ATOM   5483  C  CA    . ARG   A  1  749  ? -27.915 73.633  125.830 1.00 24.79 ? 747  ARG   A CA    1 
ATOM   5484  C  C     . ARG   A  1  749  ? -28.952 72.620  126.302 1.00 24.69 ? 747  ARG   A C     1 
ATOM   5485  O  O     . ARG   A  1  749  ? -28.746 71.940  127.317 1.00 28.03 ? 747  ARG   A O     1 
ATOM   5486  C  CB    . ARG   A  1  749  ? -28.221 75.052  126.309 1.00 27.97 ? 747  ARG   A CB    1 
ATOM   5487  C  CG    . ARG   A  1  749  ? -26.996 75.970  126.317 1.00 32.54 ? 747  ARG   A CG    1 
ATOM   5488  C  CD    . ARG   A  1  749  ? -27.357 77.356  126.826 1.00 37.91 ? 747  ARG   A CD    1 
ATOM   5489  N  NE    . ARG   A  1  749  ? -26.209 78.245  126.994 1.00 33.56 ? 747  ARG   A NE    1 
ATOM   5490  C  CZ    . ARG   A  1  749  ? -26.252 79.362  127.712 1.00 37.78 ? 747  ARG   A CZ    1 
ATOM   5491  N  NH1   . ARG   A  1  749  ? -27.357 79.736  128.333 1.00 35.36 ? 747  ARG   A NH1   1 
ATOM   5492  N  NH2   . ARG   A  1  749  ? -25.159 80.116  127.821 1.00 32.56 ? 747  ARG   A NH2   1 
ATOM   5493  N  N     . GLU   A  1  750  ? -30.068 72.493  125.579 1.00 24.98 ? 748  GLU   A N     1 
ATOM   5494  C  CA    . GLU   A  1  750  ? -31.050 71.476  125.943 1.00 28.45 ? 748  GLU   A CA    1 
ATOM   5495  C  C     . GLU   A  1  750  ? -30.456 70.075  125.860 1.00 25.60 ? 748  GLU   A C     1 
ATOM   5496  O  O     . GLU   A  1  750  ? -30.781 69.208  126.681 1.00 28.92 ? 748  GLU   A O     1 
ATOM   5497  C  CB    . GLU   A  1  750  ? -32.292 71.582  125.056 1.00 26.85 ? 748  GLU   A CB    1 
ATOM   5498  C  CG    . GLU   A  1  750  ? -33.350 70.574  125.436 1.00 30.74 ? 748  GLU   A CG    1 
ATOM   5499  C  CD    . GLU   A  1  750  ? -34.545 70.594  124.509 1.00 36.23 ? 748  GLU   A CD    1 
ATOM   5500  O  OE1   . GLU   A  1  750  ? -34.798 71.640  123.876 1.00 42.31 ? 748  GLU   A OE1   1 
ATOM   5501  O  OE2   . GLU   A  1  750  ? -35.221 69.552  124.410 1.00 37.34 ? 748  GLU   A OE2   1 
ATOM   5502  N  N     . ALA   A  1  751  ? -29.555 69.851  124.905 1.00 23.86 ? 749  ALA   A N     1 
ATOM   5503  C  CA    . ALA   A  1  751  ? -28.941 68.547  124.727 1.00 25.97 ? 749  ALA   A CA    1 
ATOM   5504  C  C     . ALA   A  1  751  ? -27.922 68.237  125.809 1.00 27.36 ? 749  ALA   A C     1 
ATOM   5505  O  O     . ALA   A  1  751  ? -27.419 67.111  125.858 1.00 29.48 ? 749  ALA   A O     1 
ATOM   5506  C  CB    . ALA   A  1  751  ? -28.295 68.462  123.343 1.00 25.10 ? 749  ALA   A CB    1 
ATOM   5507  N  N     . GLY   A  1  752  ? -27.604 69.200  126.668 1.00 26.49 ? 750  GLY   A N     1 
ATOM   5508  C  CA    . GLY   A  1  752  ? -26.743 68.953  127.809 1.00 28.34 ? 750  GLY   A CA    1 
ATOM   5509  C  C     . GLY   A  1  752  ? -25.467 69.770  127.842 1.00 28.87 ? 750  GLY   A C     1 
ATOM   5510  O  O     . GLY   A  1  752  ? -24.696 69.630  128.801 1.00 29.66 ? 750  GLY   A O     1 
ATOM   5511  N  N     . ILE   A  1  753  ? -25.186 70.615  126.853 1.00 28.43 ? 751  ILE   A N     1 
ATOM   5512  C  CA    . ILE   A  1  753  ? -24.008 71.477  126.917 1.00 28.16 ? 751  ILE   A CA    1 
ATOM   5513  C  C     . ILE   A  1  753  ? -24.265 72.499  128.014 1.00 28.54 ? 751  ILE   A C     1 
ATOM   5514  O  O     . ILE   A  1  753  ? -25.249 73.247  127.934 1.00 29.33 ? 751  ILE   A O     1 
ATOM   5515  C  CB    . ILE   A  1  753  ? -23.742 72.187  125.582 1.00 26.07 ? 751  ILE   A CB    1 
ATOM   5516  C  CG1   . ILE   A  1  753  ? -23.565 71.181  124.436 1.00 25.86 ? 751  ILE   A CG1   1 
ATOM   5517  C  CG2   . ILE   A  1  753  ? -22.496 73.058  125.704 1.00 28.29 ? 751  ILE   A CG2   1 
ATOM   5518  C  CD1   . ILE   A  1  753  ? -22.315 70.344  124.552 1.00 25.29 ? 751  ILE   A CD1   1 
ATOM   5519  N  N     . PRO   A  1  754  ? -23.427 72.575  129.043 1.00 29.67 ? 752  PRO   A N     1 
ATOM   5520  C  CA    . PRO   A  1  754  ? -23.682 73.542  130.115 1.00 30.58 ? 752  PRO   A CA    1 
ATOM   5521  C  C     . PRO   A  1  754  ? -23.558 74.970  129.608 1.00 28.23 ? 752  PRO   A C     1 
ATOM   5522  O  O     . PRO   A  1  754  ? -22.821 75.255  128.660 1.00 26.93 ? 752  PRO   A O     1 
ATOM   5523  C  CB    . PRO   A  1  754  ? -22.590 73.233  131.148 1.00 31.98 ? 752  PRO   A CB    1 
ATOM   5524  C  CG    . PRO   A  1  754  ? -21.993 71.921  130.743 1.00 29.93 ? 752  PRO   A CG    1 
ATOM   5525  C  CD    . PRO   A  1  754  ? -22.204 71.791  129.270 1.00 29.09 ? 752  PRO   A CD    1 
ATOM   5526  N  N     . ALA   A  1  755  ? -24.277 75.877  130.280 1.00 29.69 ? 753  ALA   A N     1 
ATOM   5527  C  CA    . ALA   A  1  755  ? -24.229 77.288  129.906 1.00 30.06 ? 753  ALA   A CA    1 
ATOM   5528  C  C     . ALA   A  1  755  ? -22.809 77.839  129.979 1.00 28.10 ? 753  ALA   A C     1 
ATOM   5529  O  O     . ALA   A  1  755  ? -22.433 78.703  129.178 1.00 29.89 ? 753  ALA   A O     1 
ATOM   5530  C  CB    . ALA   A  1  755  ? -25.158 78.102  130.811 1.00 33.99 ? 753  ALA   A CB    1 
ATOM   5531  N  N     . SER   A  1  756  ? -22.009 77.362  130.928 1.00 28.13 ? 754  SER   A N     1 
ATOM   5532  C  CA    . SER   A  1  756  ? -20.640 77.840  131.035 1.00 28.26 ? 754  SER   A CA    1 
ATOM   5533  C  C     . SER   A  1  756  ? -19.784 77.381  129.863 1.00 27.65 ? 754  SER   A C     1 
ATOM   5534  O  O     . SER   A  1  756  ? -18.805 78.052  129.527 1.00 31.77 ? 754  SER   A O     1 
ATOM   5535  C  CB    . SER   A  1  756  ? -20.035 77.368  132.351 1.00 31.26 ? 754  SER   A CB    1 
ATOM   5536  O  OG    . SER   A  1  756  ? -19.983 75.954  132.409 1.00 32.90 ? 754  SER   A OG    1 
ATOM   5537  N  N     . ALA   A  1  757  ? -20.147 76.266  129.224 1.00 28.85 ? 755  ALA   A N     1 
ATOM   5538  C  CA    . ALA   A  1  757  ? -19.393 75.740  128.093 1.00 25.92 ? 755  ALA   A CA    1 
ATOM   5539  C  C     . ALA   A  1  757  ? -19.796 76.363  126.767 1.00 26.47 ? 755  ALA   A C     1 
ATOM   5540  O  O     . ALA   A  1  757  ? -19.031 76.276  125.804 1.00 25.68 ? 755  ALA   A O     1 
ATOM   5541  C  CB    . ALA   A  1  757  ? -19.575 74.224  127.984 1.00 25.81 ? 755  ALA   A CB    1 
ATOM   5542  N  N     . LEU   A  1  758  ? -20.977 76.972  126.683 1.00 23.56 ? 756  LEU   A N     1 
ATOM   5543  C  CA    . LEU   A  1  758  ? -21.461 77.521  125.418 1.00 22.64 ? 756  LEU   A CA    1 
ATOM   5544  C  C     . LEU   A  1  758  ? -22.183 78.828  125.710 1.00 27.26 ? 756  LEU   A C     1 
ATOM   5545  O  O     . LEU   A  1  758  ? -23.320 78.828  126.189 1.00 28.63 ? 756  LEU   A O     1 
ATOM   5546  C  CB    . LEU   A  1  758  ? -22.370 76.539  124.697 1.00 25.01 ? 756  LEU   A CB    1 
ATOM   5547  C  CG    . LEU   A  1  758  ? -22.961 77.046  123.382 1.00 27.81 ? 756  LEU   A CG    1 
ATOM   5548  C  CD1   . LEU   A  1  758  ? -21.866 77.520  122.427 1.00 25.32 ? 756  LEU   A CD1   1 
ATOM   5549  C  CD2   . LEU   A  1  758  ? -23.781 75.942  122.752 1.00 28.63 ? 756  LEU   A CD2   1 
ATOM   5550  N  N     . GLN   A  1  759  ? -21.521 79.934  125.412 1.00 25.14 ? 757  GLN   A N     1 
ATOM   5551  C  CA    . GLN   A  1  759  ? -22.083 81.260  125.580 1.00 26.70 ? 757  GLN   A CA    1 
ATOM   5552  C  C     . GLN   A  1  759  ? -22.349 81.867  124.212 1.00 27.14 ? 757  GLN   A C     1 
ATOM   5553  O  O     . GLN   A  1  759  ? -21.501 81.794  123.317 1.00 27.92 ? 757  GLN   A O     1 
ATOM   5554  C  CB    . GLN   A  1  759  ? -21.125 82.137  126.383 1.00 26.25 ? 757  GLN   A CB    1 
ATOM   5555  C  CG    . GLN   A  1  759  ? -21.003 81.693  127.819 1.00 28.57 ? 757  GLN   A CG    1 
ATOM   5556  C  CD    . GLN   A  1  759  ? -19.957 82.479  128.569 1.00 27.27 ? 757  GLN   A CD    1 
ATOM   5557  O  OE1   . GLN   A  1  759  ? -20.268 83.466  129.238 1.00 27.20 ? 757  GLN   A OE1   1 
ATOM   5558  N  NE2   . GLN   A  1  759  ? -18.701 82.057  128.448 1.00 26.55 ? 757  GLN   A NE2   1 
ATOM   5559  N  N     . LEU   A  1  760  ? -23.527 82.447  124.045 1.00 28.15 ? 758  LEU   A N     1 
ATOM   5560  C  CA    . LEU   A  1  760  ? -23.903 83.092  122.796 1.00 28.42 ? 758  LEU   A CA    1 
ATOM   5561  C  C     . LEU   A  1  760  ? -23.724 84.590  122.963 1.00 27.02 ? 758  LEU   A C     1 
ATOM   5562  O  O     . LEU   A  1  760  ? -24.218 85.171  123.929 1.00 27.27 ? 758  LEU   A O     1 
ATOM   5563  C  CB    . LEU   A  1  760  ? -25.355 82.783  122.444 1.00 25.48 ? 758  LEU   A CB    1 
ATOM   5564  C  CG    . LEU   A  1  760  ? -25.877 83.466  121.179 1.00 25.65 ? 758  LEU   A CG    1 
ATOM   5565  C  CD1   . LEU   A  1  760  ? -25.442 82.735  119.922 1.00 27.64 ? 758  LEU   A CD1   1 
ATOM   5566  C  CD2   . LEU   A  1  760  ? -27.383 83.575  121.230 1.00 26.98 ? 758  LEU   A CD2   1 
ATOM   5567  N  N     . LEU   A  1  761  ? -22.993 85.205  122.039 1.00 25.11 ? 759  LEU   A N     1 
ATOM   5568  C  CA    A LEU   A  1  761  ? -22.671 86.629  122.101 0.44 27.88 ? 759  LEU   A CA    1 
ATOM   5569  C  CA    B LEU   A  1  761  ? -22.665 86.630  122.100 0.56 27.89 ? 759  LEU   A CA    1 
ATOM   5570  C  C     . LEU   A  1  761  ? -23.067 87.274  120.781 1.00 26.85 ? 759  LEU   A C     1 
ATOM   5571  O  O     . LEU   A  1  761  ? -22.237 87.456  119.885 1.00 25.89 ? 759  LEU   A O     1 
ATOM   5572  C  CB    A LEU   A  1  761  ? -21.191 86.832  122.424 0.44 27.48 ? 759  LEU   A CB    1 
ATOM   5573  C  CB    B LEU   A  1  761  ? -21.177 86.857  122.376 0.56 27.48 ? 759  LEU   A CB    1 
ATOM   5574  C  CG    A LEU   A  1  761  ? -20.782 86.072  123.690 0.44 28.02 ? 759  LEU   A CG    1 
ATOM   5575  C  CG    B LEU   A  1  761  ? -20.556 86.349  123.683 0.56 27.91 ? 759  LEU   A CG    1 
ATOM   5576  C  CD1   A LEU   A  1  761  ? -19.288 85.883  123.776 0.44 27.34 ? 759  LEU   A CD1   1 
ATOM   5577  C  CD1   B LEU   A  1  761  ? -21.470 86.629  124.862 0.56 27.68 ? 759  LEU   A CD1   1 
ATOM   5578  C  CD2   A LEU   A  1  761  ? -21.302 86.788  124.921 0.44 27.84 ? 759  LEU   A CD2   1 
ATOM   5579  C  CD2   B LEU   A  1  761  ? -20.205 84.871  123.602 0.56 28.03 ? 759  LEU   A CD2   1 
ATOM   5580  N  N     . PRO   A  1  762  ? -24.335 87.631  120.625 1.00 26.55 ? 760  PRO   A N     1 
ATOM   5581  C  CA    . PRO   A  1  762  ? -24.756 88.275  119.379 1.00 26.29 ? 760  PRO   A CA    1 
ATOM   5582  C  C     . PRO   A  1  762  ? -24.132 89.651  119.238 1.00 30.99 ? 760  PRO   A C     1 
ATOM   5583  O  O     . PRO   A  1  762  ? -23.785 90.310  120.220 1.00 30.55 ? 760  PRO   A O     1 
ATOM   5584  C  CB    . PRO   A  1  762  ? -26.281 88.378  119.527 1.00 25.55 ? 760  PRO   A CB    1 
ATOM   5585  C  CG    . PRO   A  1  762  ? -26.640 87.437  120.618 1.00 27.27 ? 760  PRO   A CG    1 
ATOM   5586  C  CD    . PRO   A  1  762  ? -25.467 87.407  121.540 1.00 25.41 ? 760  PRO   A CD    1 
ATOM   5587  N  N     . GLY   A  1  763  ? -23.991 90.083  118.000 1.00 26.37 ? 761  GLY   A N     1 
ATOM   5588  C  CA    . GLY   A  1  763  ? -23.489 91.411  117.719 1.00 28.45 ? 761  GLY   A CA    1 
ATOM   5589  C  C     . GLY   A  1  763  ? -22.663 91.382  116.456 1.00 31.64 ? 761  GLY   A C     1 
ATOM   5590  O  O     . GLY   A  1  763  ? -22.590 90.365  115.774 1.00 26.25 ? 761  GLY   A O     1 
ATOM   5591  N  N     . ASP   A  1  764  ? -22.049 92.517  116.166 1.00 31.10 ? 762  ASP   A N     1 
ATOM   5592  C  CA    . ASP   A  1  764  ? -21.351 92.708  114.905 1.00 32.16 ? 762  ASP   A CA    1 
ATOM   5593  C  C     . ASP   A  1  764  ? -19.864 92.362  115.055 1.00 31.39 ? 762  ASP   A C     1 
ATOM   5594  O  O     . ASP   A  1  764  ? -19.467 91.659  115.989 1.00 26.66 ? 762  ASP   A O     1 
ATOM   5595  C  CB    . ASP   A  1  764  ? -21.619 94.125  114.374 1.00 35.32 ? 762  ASP   A CB    1 
ATOM   5596  C  CG    . ASP   A  1  764  ? -21.170 95.213  115.340 1.00 35.52 ? 762  ASP   A CG    1 
ATOM   5597  O  OD1   . ASP   A  1  764  ? -20.265 94.958  116.162 1.00 35.97 ? 762  ASP   A OD1   1 
ATOM   5598  O  OD2   . ASP   A  1  764  ? -21.738 96.327  115.289 1.00 43.50 ? 762  ASP   A OD2   1 
ATOM   5599  N  N     . GLY   A  1  765  ? -19.035 92.852  114.130 1.00 28.21 ? 763  GLY   A N     1 
ATOM   5600  C  CA    . GLY   A  1  765  ? -17.618 92.527  114.143 1.00 29.08 ? 763  GLY   A CA    1 
ATOM   5601  C  C     . GLY   A  1  765  ? -16.890 93.016  115.376 1.00 28.47 ? 763  GLY   A C     1 
ATOM   5602  O  O     . GLY   A  1  765  ? -15.855 92.447  115.745 1.00 28.62 ? 763  GLY   A O     1 
ATOM   5603  N  N     . ARG   A  1  766  ? -17.415 94.054  116.030 1.00 30.15 ? 764  ARG   A N     1 
ATOM   5604  C  CA    . ARG   A  1  766  ? -16.812 94.530  117.269 1.00 32.41 ? 764  ARG   A CA    1 
ATOM   5605  C  C     . ARG   A  1  766  ? -16.850 93.458  118.344 1.00 30.99 ? 764  ARG   A C     1 
ATOM   5606  O  O     . ARG   A  1  766  ? -15.912 93.333  119.141 1.00 29.52 ? 764  ARG   A O     1 
ATOM   5607  C  CB    . ARG   A  1  766  ? -17.570 95.749  117.785 1.00 35.30 ? 764  ARG   A CB    1 
ATOM   5608  C  CG    . ARG   A  1  766  ? -17.307 97.030  117.060 1.00 42.42 ? 764  ARG   A CG    1 
ATOM   5609  C  CD    . ARG   A  1  766  ? -18.233 98.071  117.636 1.00 39.69 ? 764  ARG   A CD    1 
ATOM   5610  N  NE    . ARG   A  1  766  ? -19.623 97.703  117.403 1.00 41.49 ? 764  ARG   A NE    1 
ATOM   5611  C  CZ    . ARG   A  1  766  ? -20.620 97.973  118.232 1.00 41.85 ? 764  ARG   A CZ    1 
ATOM   5612  N  NH1   . ARG   A  1  766  ? -20.411 98.578  119.390 1.00 48.05 ? 764  ARG   A NH1   1 
ATOM   5613  N  NH2   . ARG   A  1  766  ? -21.858 97.627  117.890 1.00 45.27 ? 764  ARG   A NH2   1 
ATOM   5614  N  N     . VAL   A  1  767  ? -17.953 92.713  118.418 1.00 27.42 ? 765  VAL   A N     1 
ATOM   5615  C  CA    . VAL   A  1  767  ? -18.045 91.630  119.387 1.00 30.57 ? 765  VAL   A CA    1 
ATOM   5616  C  C     . VAL   A  1  767  ? -17.071 90.530  119.022 1.00 26.34 ? 765  VAL   A C     1 
ATOM   5617  O  O     . VAL   A  1  767  ? -16.377 89.986  119.887 1.00 27.66 ? 765  VAL   A O     1 
ATOM   5618  C  CB    . VAL   A  1  767  ? -19.490 91.107  119.488 1.00 27.37 ? 765  VAL   A CB    1 
ATOM   5619  C  CG1   . VAL   A  1  767  ? -19.586 90.018  120.555 1.00 29.77 ? 765  VAL   A CG1   1 
ATOM   5620  C  CG2   . VAL   A  1  767  ? -20.449 92.247  119.784 1.00 32.02 ? 765  VAL   A CG2   1 
ATOM   5621  N  N     . GLY   A  1  768  ? -17.006 90.183  117.732 1.00 27.06 ? 766  GLY   A N     1 
ATOM   5622  C  CA    . GLY   A  1  768  ? -16.013 89.224  117.289 1.00 25.88 ? 766  GLY   A CA    1 
ATOM   5623  C  C     . GLY   A  1  768  ? -14.607 89.665  117.644 1.00 24.05 ? 766  GLY   A C     1 
ATOM   5624  O  O     . GLY   A  1  768  ? -13.819 88.894  118.188 1.00 25.27 ? 766  GLY   A O     1 
ATOM   5625  N  N     . ALA   A  1  769  ? -14.288 90.930  117.367 1.00 26.28 ? 767  ALA   A N     1 
ATOM   5626  C  CA    . ALA   A  1  769  ? -12.923 91.398  117.585 1.00 25.88 ? 767  ALA   A CA    1 
ATOM   5627  C  C     . ALA   A  1  769  ? -12.593 91.443  119.069 1.00 26.32 ? 767  ALA   A C     1 
ATOM   5628  O  O     . ALA   A  1  769  ? -11.467 91.133  119.469 1.00 28.58 ? 767  ALA   A O     1 
ATOM   5629  C  CB    . ALA   A  1  769  ? -12.725 92.773  116.947 1.00 27.36 ? 767  ALA   A CB    1 
ATOM   5630  N  N     . ALA   A  1  770  ? -13.568 91.812  119.899 1.00 28.43 ? 768  ALA   A N     1 
ATOM   5631  C  CA    . ALA   A  1  770  ? -13.318 91.848  121.336 1.00 29.45 ? 768  ALA   A CA    1 
ATOM   5632  C  C     . ALA   A  1  770  ? -13.059 90.448  121.866 1.00 27.77 ? 768  ALA   A C     1 
ATOM   5633  O  O     . ALA   A  1  770  ? -12.231 90.258  122.764 1.00 29.46 ? 768  ALA   A O     1 
ATOM   5634  C  CB    . ALA   A  1  770  ? -14.502 92.485  122.061 1.00 28.84 ? 768  ALA   A CB    1 
ATOM   5635  N  N     . LEU   A  1  771  ? -13.754 89.458  121.311 1.00 27.07 ? 769  LEU   A N     1 
ATOM   5636  C  CA    . LEU   A  1  771  ? -13.545 88.073  121.714 1.00 25.95 ? 769  LEU   A CA    1 
ATOM   5637  C  C     . LEU   A  1  771  ? -12.172 87.581  121.285 1.00 27.93 ? 769  LEU   A C     1 
ATOM   5638  O  O     . LEU   A  1  771  ? -11.448 86.960  122.072 1.00 28.94 ? 769  LEU   A O     1 
ATOM   5639  C  CB    . LEU   A  1  771  ? -14.640 87.198  121.098 1.00 24.90 ? 769  LEU   A CB    1 
ATOM   5640  C  CG    . LEU   A  1  771  ? -16.045 87.405  121.665 1.00 25.62 ? 769  LEU   A CG    1 
ATOM   5641  C  CD1   . LEU   A  1  771  ? -17.080 86.611  120.879 1.00 26.15 ? 769  LEU   A CD1   1 
ATOM   5642  C  CD2   . LEU   A  1  771  ? -16.076 87.019  123.125 1.00 27.84 ? 769  LEU   A CD2   1 
ATOM   5643  N  N     . VAL   A  1  772  ? -11.808 87.838  120.026 1.00 25.73 ? 770  VAL   A N     1 
ATOM   5644  C  CA    . VAL   A  1  772  ? -10.492 87.457  119.525 1.00 25.22 ? 770  VAL   A CA    1 
ATOM   5645  C  C     . VAL   A  1  772  ? -9.392  88.066  120.386 1.00 29.21 ? 770  VAL   A C     1 
ATOM   5646  O  O     . VAL   A  1  772  ? -8.400  87.405  120.706 1.00 31.61 ? 770  VAL   A O     1 
ATOM   5647  C  CB    . VAL   A  1  772  ? -10.357 87.850  118.042 1.00 24.15 ? 770  VAL   A CB    1 
ATOM   5648  C  CG1   . VAL   A  1  772  ? -8.928  87.678  117.568 1.00 29.62 ? 770  VAL   A CG1   1 
ATOM   5649  C  CG2   . VAL   A  1  772  ? -11.301 87.004  117.188 1.00 25.18 ? 770  VAL   A CG2   1 
ATOM   5650  N  N     . ALA   A  1  773  ? -9.554  89.329  120.775 1.00 30.81 ? 771  ALA   A N     1 
ATOM   5651  C  CA    . ALA   A  1  773  ? -8.521  90.049  121.511 1.00 27.62 ? 771  ALA   A CA    1 
ATOM   5652  C  C     . ALA   A  1  773  ? -8.452  89.670  122.984 1.00 33.50 ? 771  ALA   A C     1 
ATOM   5653  O  O     . ALA   A  1  773  ? -7.477  90.037  123.651 1.00 35.92 ? 771  ALA   A O     1 
ATOM   5654  C  CB    . ALA   A  1  773  ? -8.747  91.556  121.383 1.00 30.12 ? 771  ALA   A CB    1 
ATOM   5655  N  N     . ALA   A  1  774  ? -9.444  88.951  123.507 1.00 33.82 ? 772  ALA   A N     1 
ATOM   5656  C  CA    . ALA   A  1  774  ? -9.478  88.666  124.939 1.00 33.83 ? 772  ALA   A CA    1 
ATOM   5657  C  C     . ALA   A  1  774  ? -8.341  87.728  125.337 1.00 32.42 ? 772  ALA   A C     1 
ATOM   5658  O  O     . ALA   A  1  774  ? -8.016  86.773  124.629 1.00 30.09 ? 772  ALA   A O     1 
ATOM   5659  C  CB    . ALA   A  1  774  ? -10.831 88.079  125.341 1.00 29.69 ? 772  ALA   A CB    1 
ATOM   5660  N  N     . ALA   A  1  775  ? -7.735  88.005  126.495 1.00 37.19 ? 773  ALA   A N     1 
ATOM   5661  C  CA    . ALA   A  1  775  ? -6.480  87.346  126.839 1.00 35.58 ? 773  ALA   A CA    1 
ATOM   5662  C  C     . ALA   A  1  775  ? -6.628  85.835  126.980 1.00 30.51 ? 773  ALA   A C     1 
ATOM   5663  O  O     . ALA   A  1  775  ? -5.698  85.094  126.651 1.00 33.23 ? 773  ALA   A O     1 
ATOM   5664  C  CB    . ALA   A  1  775  ? -5.883  87.962  128.106 1.00 36.96 ? 773  ALA   A CB    1 
ATOM   5665  N  N     . GLU   A  1  776  ? -7.779  85.353  127.440 1.00 29.52 ? 774  GLU   A N     1 
ATOM   5666  C  CA    . GLU   A  1  776  ? -7.955  83.923  127.671 1.00 25.84 ? 774  GLU   A CA    1 
ATOM   5667  C  C     . GLU   A  1  776  ? -8.398  83.155  126.424 1.00 26.66 ? 774  GLU   A C     1 
ATOM   5668  O  O     . GLU   A  1  776  ? -8.530  81.927  126.481 1.00 29.51 ? 774  GLU   A O     1 
ATOM   5669  C  CB    . GLU   A  1  776  ? -8.939  83.678  128.817 1.00 32.82 ? 774  GLU   A CB    1 
ATOM   5670  C  CG    . GLU   A  1  776  ? -8.522  84.329  130.124 1.00 36.67 ? 774  GLU   A CG    1 
ATOM   5671  C  CD    . GLU   A  1  776  ? -9.104  85.723  130.311 1.00 40.65 ? 774  GLU   A CD    1 
ATOM   5672  O  OE1   . GLU   A  1  776  ? -9.591  86.326  129.324 1.00 33.53 ? 774  GLU   A OE1   1 
ATOM   5673  O  OE2   . GLU   A  1  776  ? -9.073  86.215  131.458 1.00 46.76 ? 774  GLU   A OE2   1 
ATOM   5674  N  N     . THR   A  1  777  ? -8.609  83.834  125.306 1.00 25.68 ? 775  THR   A N     1 
ATOM   5675  C  CA    . THR   A  1  777  ? -8.970  83.143  124.073 1.00 27.13 ? 775  THR   A CA    1 
ATOM   5676  C  C     . THR   A  1  777  ? -7.825  82.257  123.607 1.00 26.57 ? 775  THR   A C     1 
ATOM   5677  O  O     . THR   A  1  777  ? -6.711  82.733  123.360 1.00 29.16 ? 775  THR   A O     1 
ATOM   5678  C  CB    . THR   A  1  777  ? -9.312  84.170  123.008 1.00 26.63 ? 775  THR   A CB    1 
ATOM   5679  O  OG1   . THR   A  1  777  ? -10.517 84.836  123.393 1.00 25.97 ? 775  THR   A OG1   1 
ATOM   5680  C  CG2   . THR   A  1  777  ? -9.519  83.479  121.658 1.00 24.03 ? 775  THR   A CG2   1 
ATOM   5681  N  N     . ALA   A  1  778  ? -8.102  80.962  123.500 1.00 24.28 ? 776  ALA   A N     1 
ATOM   5682  C  CA    . ALA   A  1  778  ? -7.082  79.970  123.213 1.00 22.30 ? 776  ALA   A CA    1 
ATOM   5683  C  C     . ALA   A  1  778  ? -7.108  79.501  121.768 1.00 23.37 ? 776  ALA   A C     1 
ATOM   5684  O  O     . ALA   A  1  778  ? -6.196  78.788  121.344 1.00 25.03 ? 776  ALA   A O     1 
ATOM   5685  C  CB    . ALA   A  1  778  ? -7.253  78.762  124.139 1.00 24.12 ? 776  ALA   A CB    1 
ATOM   5686  N  N     . GLY   A  1  779  ? -8.128  79.875  121.018 1.00 22.80 ? 777  GLY   A N     1 
ATOM   5687  C  CA    . GLY   A  1  779  ? -8.207  79.501  119.630 1.00 21.86 ? 777  GLY   A CA    1 
ATOM   5688  C  C     . GLY   A  1  779  ? -9.393  80.191  119.011 1.00 20.42 ? 777  GLY   A C     1 
ATOM   5689  O  O     . GLY   A  1  779  ? -10.342 80.578  119.700 1.00 21.61 ? 777  GLY   A O     1 
ATOM   5690  N  N     . VAL   A  1  780  ? -9.318  80.363  117.699 1.00 21.29 ? 778  VAL   A N     1 
ATOM   5691  C  CA    . VAL   A  1  780  ? -10.357 81.057  116.961 1.00 20.52 ? 778  VAL   A CA    1 
ATOM   5692  C  C     . VAL   A  1  780  ? -10.753 80.193  115.780 1.00 19.77 ? 778  VAL   A C     1 
ATOM   5693  O  O     . VAL   A  1  780  ? -9.892  79.711  115.035 1.00 20.54 ? 778  VAL   A O     1 
ATOM   5694  C  CB    . VAL   A  1  780  ? -9.892  82.448  116.500 1.00 22.03 ? 778  VAL   A CB    1 
ATOM   5695  C  CG1   . VAL   A  1  780  ? -10.986 83.142  115.729 1.00 21.29 ? 778  VAL   A CG1   1 
ATOM   5696  C  CG2   . VAL   A  1  780  ? -9.468  83.292  117.694 1.00 23.15 ? 778  VAL   A CG2   1 
ATOM   5697  N  N     . MET   A  1  781  ? -12.052 79.978  115.625 1.00 18.30 ? 779  MET   A N     1 
ATOM   5698  C  CA    . MET   A  1  781  ? -12.598 79.345  114.434 1.00 18.31 ? 779  MET   A CA    1 
ATOM   5699  C  C     . MET   A  1  781  ? -13.407 80.409  113.716 1.00 20.64 ? 779  MET   A C     1 
ATOM   5700  O  O     . MET   A  1  781  ? -14.389 80.923  114.262 1.00 20.64 ? 779  MET   A O     1 
ATOM   5701  C  CB    . MET   A  1  781  ? -13.465 78.142  114.797 1.00 21.28 ? 779  MET   A CB    1 
ATOM   5702  C  CG    . MET   A  1  781  ? -12.740 77.138  115.677 1.00 20.58 ? 779  MET   A CG    1 
ATOM   5703  S  SD    . MET   A  1  781  ? -13.818 75.840  116.276 1.00 21.45 ? 779  MET   A SD    1 
ATOM   5704  C  CE    . MET   A  1  781  ? -14.000 74.874  114.787 1.00 21.58 ? 779  MET   A CE    1 
ATOM   5705  N  N     . PHE   A  1  782  ? -12.966 80.763  112.515 1.00 20.68 ? 780  PHE   A N     1 
ATOM   5706  C  CA    . PHE   A  1  782  ? -13.575 81.827  111.743 1.00 21.20 ? 780  PHE   A CA    1 
ATOM   5707  C  C     . PHE   A  1  782  ? -14.007 81.282  110.396 1.00 20.23 ? 780  PHE   A C     1 
ATOM   5708  O  O     . PHE   A  1  782  ? -13.212 80.653  109.690 1.00 19.06 ? 780  PHE   A O     1 
ATOM   5709  C  CB    . PHE   A  1  782  ? -12.589 82.964  111.482 1.00 20.90 ? 780  PHE   A CB    1 
ATOM   5710  C  CG    . PHE   A  1  782  ? -13.146 84.026  110.594 1.00 20.23 ? 780  PHE   A CG    1 
ATOM   5711  C  CD1   . PHE   A  1  782  ? -14.011 84.981  111.106 1.00 22.22 ? 780  PHE   A CD1   1 
ATOM   5712  C  CD2   . PHE   A  1  782  ? -12.850 84.048  109.237 1.00 19.43 ? 780  PHE   A CD2   1 
ATOM   5713  C  CE1   . PHE   A  1  782  ? -14.553 85.960  110.301 1.00 23.22 ? 780  PHE   A CE1   1 
ATOM   5714  C  CE2   . PHE   A  1  782  ? -13.384 85.017  108.427 1.00 20.37 ? 780  PHE   A CE2   1 
ATOM   5715  C  CZ    . PHE   A  1  782  ? -14.238 85.981  108.955 1.00 20.56 ? 780  PHE   A CZ    1 
ATOM   5716  N  N     . THR   A  1  783  ? -15.252 81.554  110.035 1.00 18.06 ? 781  THR   A N     1 
ATOM   5717  C  CA    . THR   A  1  783  ? -15.706 81.370  108.667 1.00 20.78 ? 781  THR   A CA    1 
ATOM   5718  C  C     . THR   A  1  783  ? -16.354 82.673  108.239 1.00 20.73 ? 781  THR   A C     1 
ATOM   5719  O  O     . THR   A  1  783  ? -17.203 83.209  108.956 1.00 20.28 ? 781  THR   A O     1 
ATOM   5720  C  CB    . THR   A  1  783  ? -16.670 80.185  108.559 1.00 21.27 ? 781  THR   A CB    1 
ATOM   5721  O  OG1   . THR   A  1  783  ? -16.004 78.990  109.000 1.00 19.93 ? 781  THR   A OG1   1 
ATOM   5722  C  CG2   . THR   A  1  783  ? -17.097 79.995  107.113 1.00 21.40 ? 781  THR   A CG2   1 
ATOM   5723  N  N     . GLY   A  1  784  ? -15.918 83.200  107.101 1.00 19.78 ? 782  GLY   A N     1 
ATOM   5724  C  CA    . GLY   A  1  784  ? -16.318 84.534  106.701 1.00 20.26 ? 782  GLY   A CA    1 
ATOM   5725  C  C     . GLY   A  1  784  ? -15.451 84.999  105.552 1.00 19.86 ? 782  GLY   A C     1 
ATOM   5726  O  O     . GLY   A  1  784  ? -14.803 84.190  104.887 1.00 20.01 ? 782  GLY   A O     1 
ATOM   5727  N  N     . SER   A  1  785  ? -15.453 86.308  105.328 1.00 20.61 ? 783  SER   A N     1 
ATOM   5728  C  CA    . SER   A  1  785  ? -14.701 86.872  104.215 1.00 20.95 ? 783  SER   A CA    1 
ATOM   5729  C  C     . SER   A  1  785  ? -13.199 86.833  104.475 1.00 22.83 ? 783  SER   A C     1 
ATOM   5730  O  O     . SER   A  1  785  ? -12.735 86.888  105.615 1.00 21.40 ? 783  SER   A O     1 
ATOM   5731  C  CB    . SER   A  1  785  ? -15.120 88.319  103.971 1.00 23.38 ? 783  SER   A CB    1 
ATOM   5732  O  OG    . SER   A  1  785  ? -14.825 89.129  105.094 1.00 23.24 ? 783  SER   A OG    1 
ATOM   5733  N  N     . THR   A  1  786  ? -12.436 86.750  103.383 1.00 18.66 ? 784  THR   A N     1 
ATOM   5734  C  CA    . THR   A  1  786  ? -10.982 86.770  103.486 1.00 20.16 ? 784  THR   A CA    1 
ATOM   5735  C  C     . THR   A  1  786  ? -10.475 88.049  104.151 1.00 20.13 ? 784  THR   A C     1 
ATOM   5736  O  O     . THR   A  1  786  ? -9.506  88.021  104.923 1.00 21.36 ? 784  THR   A O     1 
ATOM   5737  C  CB    . THR   A  1  786  ? -10.387 86.585  102.091 1.00 21.98 ? 784  THR   A CB    1 
ATOM   5738  O  OG1   . THR   A  1  786  ? -10.887 85.362  101.538 1.00 23.65 ? 784  THR   A OG1   1 
ATOM   5739  C  CG2   . THR   A  1  786  ? -8.865  86.540  102.158 1.00 23.63 ? 784  THR   A CG2   1 
ATOM   5740  N  N     . GLU   A  1  787  ? -11.109 89.185  103.861 1.00 24.54 ? 785  GLU   A N     1 
ATOM   5741  C  CA    . GLU   A  1  787  ? -10.637 90.450  104.412 1.00 23.43 ? 785  GLU   A CA    1 
ATOM   5742  C  C     . GLU   A  1  787  ? -10.811 90.494  105.926 1.00 22.02 ? 785  GLU   A C     1 
ATOM   5743  O  O     . GLU   A  1  787  ? -9.940  90.998  106.645 1.00 22.90 ? 785  GLU   A O     1 
ATOM   5744  C  CB    . GLU   A  1  787  ? -11.362 91.620  103.745 1.00 27.39 ? 785  GLU   A CB    1 
ATOM   5745  N  N     . VAL   A  1  788  ? -11.920 89.957  106.430 1.00 23.52 ? 786  VAL   A N     1 
ATOM   5746  C  CA    . VAL   A  1  788  ? -12.101 89.926  107.877 1.00 22.02 ? 786  VAL   A CA    1 
ATOM   5747  C  C     . VAL   A  1  788  ? -11.136 88.939  108.512 1.00 22.18 ? 786  VAL   A C     1 
ATOM   5748  O  O     . VAL   A  1  788  ? -10.522 89.223  109.548 1.00 21.94 ? 786  VAL   A O     1 
ATOM   5749  C  CB    . VAL   A  1  788  ? -13.568 89.634  108.240 1.00 22.32 ? 786  VAL   A CB    1 
ATOM   5750  C  CG1   . VAL   A  1  788  ? -13.701 89.369  109.731 1.00 24.67 ? 786  VAL   A CG1   1 
ATOM   5751  C  CG2   . VAL   A  1  788  ? -14.435 90.817  107.853 1.00 24.09 ? 786  VAL   A CG2   1 
ATOM   5752  N  N     . ALA   A  1  789  ? -10.964 87.770  107.897 1.00 21.02 ? 787  ALA   A N     1 
ATOM   5753  C  CA    . ALA   A  1  789  ? -9.996  86.820  108.430 1.00 19.95 ? 787  ALA   A CA    1 
ATOM   5754  C  C     . ALA   A  1  789  ? -8.616  87.452  108.527 1.00 18.72 ? 787  ALA   A C     1 
ATOM   5755  O  O     . ALA   A  1  789  ? -7.876  87.209  109.485 1.00 20.06 ? 787  ALA   A O     1 
ATOM   5756  C  CB    . ALA   A  1  789  ? -9.962  85.563  107.559 1.00 17.78 ? 787  ALA   A CB    1 
ATOM   5757  N  N     . ARG   A  1  790  ? -8.261  88.296  107.554 1.00 19.35 ? 788  ARG   A N     1 
ATOM   5758  C  CA    . ARG   A  1  790  ? -6.963  88.960  107.595 1.00 21.30 ? 788  ARG   A CA    1 
ATOM   5759  C  C     . ARG   A  1  790  ? -6.861  89.905  108.789 1.00 21.04 ? 788  ARG   A C     1 
ATOM   5760  O  O     . ARG   A  1  790  ? -5.796  90.027  109.406 1.00 22.22 ? 788  ARG   A O     1 
ATOM   5761  C  CB    . ARG   A  1  790  ? -6.742  89.703  106.276 1.00 24.43 ? 788  ARG   A CB    1 
ATOM   5762  C  CG    . ARG   A  1  790  ? -5.350  90.275  106.092 1.00 22.84 ? 788  ARG   A CG    1 
ATOM   5763  C  CD    . ARG   A  1  790  ? -5.163  90.817  104.667 1.00 24.46 ? 788  ARG   A CD    1 
ATOM   5764  N  NE    . ARG   A  1  790  ? -5.098  89.743  103.681 1.00 23.75 ? 788  ARG   A NE    1 
ATOM   5765  C  CZ    . ARG   A  1  790  ? -5.936  89.579  102.663 1.00 22.27 ? 788  ARG   A CZ    1 
ATOM   5766  N  NH1   . ARG   A  1  790  ? -6.931  90.420  102.436 1.00 26.45 ? 788  ARG   A NH1   1 
ATOM   5767  N  NH2   . ARG   A  1  790  ? -5.763  88.546  101.842 1.00 26.40 ? 788  ARG   A NH2   1 
ATOM   5768  N  N     . LEU   A  1  791  ? -7.970  90.570  109.143 1.00 22.20 ? 789  LEU   A N     1 
ATOM   5769  C  CA    . LEU   A  1  791  ? -7.993  91.395  110.347 1.00 23.82 ? 789  LEU   A CA    1 
ATOM   5770  C  C     . LEU   A  1  791  ? -7.814  90.547  111.600 1.00 25.06 ? 789  LEU   A C     1 
ATOM   5771  O  O     . LEU   A  1  791  ? -7.103  90.942  112.530 1.00 23.65 ? 789  LEU   A O     1 
ATOM   5772  C  CB    . LEU   A  1  791  ? -9.313  92.160  110.421 1.00 23.54 ? 789  LEU   A CB    1 
ATOM   5773  C  CG    . LEU   A  1  791  ? -9.558  93.184  109.311 1.00 29.52 ? 789  LEU   A CG    1 
ATOM   5774  C  CD1   . LEU   A  1  791  ? -10.969 93.735  109.388 1.00 32.57 ? 789  LEU   A CD1   1 
ATOM   5775  C  CD2   . LEU   A  1  791  ? -8.537  94.297  109.410 1.00 29.60 ? 789  LEU   A CD2   1 
ATOM   5776  N  N     . ILE   A  1  792  ? -8.463  89.383  111.647 1.00 22.62 ? 790  ILE   A N     1 
ATOM   5777  C  CA    . ILE   A  1  792  ? -8.305  88.498  112.798 1.00 24.23 ? 790  ILE   A CA    1 
ATOM   5778  C  C     . ILE   A  1  792  ? -6.884  87.964  112.877 1.00 24.74 ? 790  ILE   A C     1 
ATOM   5779  O  O     . ILE   A  1  792  ? -6.284  87.905  113.960 1.00 24.42 ? 790  ILE   A O     1 
ATOM   5780  C  CB    . ILE   A  1  792  ? -9.360  87.381  112.754 1.00 22.40 ? 790  ILE   A CB    1 
ATOM   5781  C  CG1   . ILE   A  1  792  ? -10.727 87.988  113.012 1.00 22.94 ? 790  ILE   A CG1   1 
ATOM   5782  C  CG2   . ILE   A  1  792  ? -9.048  86.281  113.779 1.00 24.23 ? 790  ILE   A CG2   1 
ATOM   5783  C  CD1   . ILE   A  1  792  ? -11.868 87.101  112.615 1.00 22.15 ? 790  ILE   A CD1   1 
ATOM   5784  N  N     . GLN   A  1  793  ? -6.322  87.578  111.731 1.00 19.77 ? 791  GLN   A N     1 
ATOM   5785  C  CA    . GLN   A  1  793  ? -4.935  87.137  111.678 1.00 20.18 ? 791  GLN   A CA    1 
ATOM   5786  C  C     . GLN   A  1  793  ? -4.007  88.192  112.264 1.00 21.66 ? 791  GLN   A C     1 
ATOM   5787  O  O     . GLN   A  1  793  ? -3.093  87.869  113.025 1.00 23.32 ? 791  GLN   A O     1 
ATOM   5788  C  CB    . GLN   A  1  793  ? -4.566  86.832  110.227 1.00 22.67 ? 791  GLN   A CB    1 
ATOM   5789  C  CG    . GLN   A  1  793  ? -3.125  86.431  110.011 1.00 21.07 ? 791  GLN   A CG    1 
ATOM   5790  C  CD    . GLN   A  1  793  ? -2.739  86.487  108.540 1.00 24.05 ? 791  GLN   A CD    1 
ATOM   5791  O  OE1   . GLN   A  1  793  ? -3.159  87.389  107.809 1.00 27.10 ? 791  GLN   A OE1   1 
ATOM   5792  N  NE2   . GLN   A  1  793  ? -1.962  85.508  108.092 1.00 26.15 ? 791  GLN   A NE2   1 
ATOM   5793  N  N     . ALA   A  1  794  ? -4.246  89.466  111.934 1.00 23.69 ? 792  ALA   A N     1 
ATOM   5794  C  CA    . ALA   A  1  794  ? -3.421  90.544  112.467 1.00 26.28 ? 792  ALA   A CA    1 
ATOM   5795  C  C     . ALA   A  1  794  ? -3.591  90.676  113.975 1.00 25.04 ? 792  ALA   A C     1 
ATOM   5796  O  O     . ALA   A  1  794  ? -2.605  90.865  114.695 1.00 28.09 ? 792  ALA   A O     1 
ATOM   5797  C  CB    . ALA   A  1  794  ? -3.779  91.860  111.781 1.00 25.52 ? 792  ALA   A CB    1 
ATOM   5798  N  N     . GLN   A  1  795  ? -4.831  90.578  114.465 1.00 26.77 ? 793  GLN   A N     1 
ATOM   5799  C  CA    . GLN   A  1  795  ? -5.082  90.623  115.905 1.00 26.28 ? 793  GLN   A CA    1 
ATOM   5800  C  C     . GLN   A  1  795  ? -4.304  89.535  116.627 1.00 27.68 ? 793  GLN   A C     1 
ATOM   5801  O  O     . GLN   A  1  795  ? -3.675  89.783  117.663 1.00 29.29 ? 793  GLN   A O     1 
ATOM   5802  C  CB    . GLN   A  1  795  ? -6.572  90.404  116.169 1.00 28.88 ? 793  GLN   A CB    1 
ATOM   5803  C  CG    . GLN   A  1  795  ? -7.428  91.624  116.365 1.00 37.68 ? 793  GLN   A CG    1 
ATOM   5804  C  CD    . GLN   A  1  795  ? -8.860  91.244  116.741 1.00 35.89 ? 793  GLN   A CD    1 
ATOM   5805  O  OE1   . GLN   A  1  795  ? -9.548  90.539  115.994 1.00 37.46 ? 793  GLN   A OE1   1 
ATOM   5806  N  NE2   . GLN   A  1  795  ? -9.306  91.696  117.902 1.00 29.67 ? 793  GLN   A NE2   1 
ATOM   5807  N  N     . LEU   A  1  796  ? -4.355  88.309  116.099 1.00 23.83 ? 794  LEU   A N     1 
ATOM   5808  C  CA    . LEU   A  1  796  ? -3.716  87.177  116.758 1.00 27.22 ? 794  LEU   A CA    1 
ATOM   5809  C  C     . LEU   A  1  796  ? -2.202  87.208  116.645 1.00 25.98 ? 794  LEU   A C     1 
ATOM   5810  O  O     . LEU   A  1  796  ? -1.523  86.537  117.430 1.00 30.39 ? 794  LEU   A O     1 
ATOM   5811  C  CB    . LEU   A  1  796  ? -4.246  85.865  116.179 1.00 25.38 ? 794  LEU   A CB    1 
ATOM   5812  C  CG    . LEU   A  1  796  ? -5.705  85.560  116.508 1.00 23.92 ? 794  LEU   A CG    1 
ATOM   5813  C  CD1   . LEU   A  1  796  ? -6.147  84.235  115.886 1.00 23.97 ? 794  LEU   A CD1   1 
ATOM   5814  C  CD2   . LEU   A  1  796  ? -5.896  85.557  118.023 1.00 27.14 ? 794  LEU   A CD2   1 
ATOM   5815  N  N     . ALA   A  1  797  ? -1.651  87.949  115.686 1.00 26.75 ? 795  ALA   A N     1 
ATOM   5816  C  CA    . ALA   A  1  797  ? -0.202  87.959  115.544 1.00 28.73 ? 795  ALA   A CA    1 
ATOM   5817  C  C     . ALA   A  1  797  ? 0.472   88.571  116.764 1.00 30.27 ? 795  ALA   A C     1 
ATOM   5818  O  O     . ALA   A  1  797  ? 1.630   88.251  117.049 1.00 39.99 ? 795  ALA   A O     1 
ATOM   5819  C  CB    . ALA   A  1  797  ? 0.203   88.685  114.260 1.00 30.09 ? 795  ALA   A CB    1 
ATOM   5820  N  N     . ASP   A  1  798  ? -0.246  89.419  117.504 1.00 33.97 ? 796  ASP   A N     1 
ATOM   5821  C  CA    . ASP   A  1  798  ? 0.271   90.002  118.737 1.00 37.82 ? 796  ASP   A CA    1 
ATOM   5822  C  C     . ASP   A  1  798  ? 0.301   89.008  119.882 1.00 37.64 ? 796  ASP   A C     1 
ATOM   5823  O  O     . ASP   A  1  798  ? 0.967   89.269  120.890 1.00 38.88 ? 796  ASP   A O     1 
ATOM   5824  C  CB    . ASP   A  1  798  ? -0.670  91.113  119.212 1.00 35.63 ? 796  ASP   A CB    1 
ATOM   5825  C  CG    . ASP   A  1  798  ? -0.742  92.277  118.255 1.00 47.76 ? 796  ASP   A CG    1 
ATOM   5826  O  OD1   . ASP   A  1  798  ? 0.222   92.471  117.486 1.00 52.01 ? 796  ASP   A OD1   1 
ATOM   5827  O  OD2   . ASP   A  1  798  ? -1.762  93.002  118.278 1.00 49.27 ? 796  ASP   A OD2   1 
ATOM   5828  N  N     . ARG   A  1  799  ? -0.393  87.884  119.754 1.00 32.47 ? 797  ARG   A N     1 
ATOM   5829  C  CA    A ARG   A  1  799  ? -0.767  87.048  120.883 0.55 31.94 ? 797  ARG   A CA    1 
ATOM   5830  C  CA    B ARG   A  1  799  ? -0.735  87.066  120.904 0.45 31.95 ? 797  ARG   A CA    1 
ATOM   5831  C  C     . ARG   A  1  799  ? 0.033   85.752  120.910 1.00 27.94 ? 797  ARG   A C     1 
ATOM   5832  O  O     . ARG   A  1  799  ? 0.386   85.201  119.865 1.00 26.96 ? 797  ARG   A O     1 
ATOM   5833  C  CB    A ARG   A  1  799  ? -2.248  86.700  120.770 0.55 33.68 ? 797  ARG   A CB    1 
ATOM   5834  C  CB    B ARG   A  1  799  ? -2.239  86.782  120.953 0.45 33.69 ? 797  ARG   A CB    1 
ATOM   5835  C  CG    A ARG   A  1  799  ? -3.101  87.906  120.439 0.55 31.72 ? 797  ARG   A CG    1 
ATOM   5836  C  CG    B ARG   A  1  799  ? -3.101  87.995  121.289 0.45 32.62 ? 797  ARG   A CG    1 
ATOM   5837  C  CD    A ARG   A  1  799  ? -3.351  88.708  121.690 0.55 33.13 ? 797  ARG   A CD    1 
ATOM   5838  C  CD    B ARG   A  1  799  ? -4.529  87.559  121.565 0.45 32.82 ? 797  ARG   A CD    1 
ATOM   5839  N  NE    A ARG   A  1  799  ? -4.047  87.890  122.673 0.55 33.35 ? 797  ARG   A NE    1 
ATOM   5840  N  NE    B ARG   A  1  799  ? -4.559  86.549  122.615 0.45 33.28 ? 797  ARG   A NE    1 
ATOM   5841  C  CZ    A ARG   A  1  799  ? -5.314  87.519  122.565 0.55 31.18 ? 797  ARG   A CZ    1 
ATOM   5842  C  CZ    B ARG   A  1  799  ? -5.409  85.533  122.659 0.45 31.41 ? 797  ARG   A CZ    1 
ATOM   5843  N  NH1   A ARG   A  1  799  ? -6.062  87.901  121.542 0.55 34.30 ? 797  ARG   A NH1   1 
ATOM   5844  N  NH1   B ARG   A  1  799  ? -6.340  85.368  121.732 0.45 28.76 ? 797  ARG   A NH1   1 
ATOM   5845  N  NH2   A ARG   A  1  799  ? -5.845  86.743  123.504 0.55 33.85 ? 797  ARG   A NH2   1 
ATOM   5846  N  NH2   B ARG   A  1  799  ? -5.313  84.652  123.650 0.45 31.14 ? 797  ARG   A NH2   1 
ATOM   5847  N  N     . LEU   A  1  800  ? 0.293   85.265  122.121 1.00 30.03 ? 798  LEU   A N     1 
ATOM   5848  C  CA    . LEU   A  1  800  ? 0.836   83.936  122.342 1.00 28.41 ? 798  LEU   A CA    1 
ATOM   5849  C  C     . LEU   A  1  800  ? 0.044   83.283  123.465 1.00 27.11 ? 798  LEU   A C     1 
ATOM   5850  O  O     . LEU   A  1  800  ? -0.495  83.964  124.340 1.00 31.27 ? 798  LEU   A O     1 
ATOM   5851  C  CB    . LEU   A  1  800  ? 2.312   83.967  122.752 1.00 30.78 ? 798  LEU   A CB    1 
ATOM   5852  C  CG    . LEU   A  1  800  ? 3.323   84.371  121.685 1.00 27.79 ? 798  LEU   A CG    1 
ATOM   5853  C  CD1   . LEU   A  1  800  ? 4.711   84.459  122.301 1.00 30.38 ? 798  LEU   A CD1   1 
ATOM   5854  C  CD2   . LEU   A  1  800  ? 3.298   83.389  120.535 1.00 29.24 ? 798  LEU   A CD2   1 
ATOM   5855  N  N     . SER   A  1  801  ? -0.029  81.957  123.421 1.00 29.78 ? 799  SER   A N     1 
ATOM   5856  C  CA    . SER   A  1  801  ? -0.624  81.187  124.497 1.00 31.74 ? 799  SER   A CA    1 
ATOM   5857  C  C     . SER   A  1  801  ? 0.256   81.294  125.738 1.00 35.06 ? 799  SER   A C     1 
ATOM   5858  O  O     . SER   A  1  801  ? 1.401   81.751  125.665 1.00 33.70 ? 799  SER   A O     1 
ATOM   5859  C  CB    . SER   A  1  801  ? -0.711  79.721  124.077 1.00 32.96 ? 799  SER   A CB    1 
ATOM   5860  O  OG    . SER   A  1  801  ? 0.591   79.160  123.981 1.00 32.42 ? 799  SER   A OG    1 
ATOM   5861  N  N     . PRO   A  1  802  ? -0.252  80.875  126.901 1.00 33.52 ? 800  PRO   A N     1 
ATOM   5862  C  CA    . PRO   A  1  802  ? 0.606   80.830  128.098 1.00 36.40 ? 800  PRO   A CA    1 
ATOM   5863  C  C     . PRO   A  1  802  ? 1.849   79.982  127.926 1.00 35.82 ? 800  PRO   A C     1 
ATOM   5864  O  O     . PRO   A  1  802  ? 2.844   80.226  128.617 1.00 41.69 ? 800  PRO   A O     1 
ATOM   5865  C  CB    . PRO   A  1  802  ? -0.324  80.261  129.175 1.00 38.81 ? 800  PRO   A CB    1 
ATOM   5866  C  CG    . PRO   A  1  802  ? -1.684  80.682  128.731 1.00 40.06 ? 800  PRO   A CG    1 
ATOM   5867  C  CD    . PRO   A  1  802  ? -1.659  80.582  127.231 1.00 34.40 ? 800  PRO   A CD    1 
ATOM   5868  N  N     . ALA   A  1  803  ? 1.829   78.997  127.033 1.00 35.74 ? 801  ALA   A N     1 
ATOM   5869  C  CA    . ALA   A  1  803  ? 3.028   78.247  126.691 1.00 36.32 ? 801  ALA   A CA    1 
ATOM   5870  C  C     . ALA   A  1  803  ? 3.922   78.983  125.702 1.00 40.42 ? 801  ALA   A C     1 
ATOM   5871  O  O     . ALA   A  1  803  ? 4.955   78.435  125.303 1.00 41.77 ? 801  ALA   A O     1 
ATOM   5872  C  CB    . ALA   A  1  803  ? 2.648   76.878  126.120 1.00 40.11 ? 801  ALA   A CB    1 
ATOM   5873  N  N     . GLY   A  1  804  ? 3.551   80.191  125.289 1.00 38.63 ? 802  GLY   A N     1 
ATOM   5874  C  CA    . GLY   A  1  804  ? 4.331   80.929  124.306 1.00 32.66 ? 802  GLY   A CA    1 
ATOM   5875  C  C     . GLY   A  1  804  ? 4.251   80.418  122.881 1.00 32.78 ? 802  GLY   A C     1 
ATOM   5876  O  O     . GLY   A  1  804  ? 5.260   80.436  122.166 1.00 33.98 ? 802  GLY   A O     1 
ATOM   5877  N  N     . ARG   A  1  805  ? 3.078   79.983  122.436 1.00 31.89 ? 803  ARG   A N     1 
ATOM   5878  C  CA    . ARG   A  1  805  ? 2.893   79.476  121.086 1.00 32.59 ? 803  ARG   A CA    1 
ATOM   5879  C  C     . ARG   A  1  805  ? 1.728   80.199  120.423 1.00 26.50 ? 803  ARG   A C     1 
ATOM   5880  O  O     . ARG   A  1  805  ? 0.883   80.780  121.111 1.00 25.98 ? 803  ARG   A O     1 
ATOM   5881  C  CB    . ARG   A  1  805  ? 2.643   77.960  121.101 1.00 32.71 ? 803  ARG   A CB    1 
ATOM   5882  C  CG    . ARG   A  1  805  ? 3.807   77.151  121.677 1.00 31.40 ? 803  ARG   A CG    1 
ATOM   5883  C  CD    . ARG   A  1  805  ? 5.124   77.480  120.974 1.00 35.29 ? 803  ARG   A CD    1 
ATOM   5884  N  NE    . ARG   A  1  805  ? 6.249   76.714  121.507 1.00 32.94 ? 803  ARG   A NE    1 
ATOM   5885  C  CZ    . ARG   A  1  805  ? 7.175   77.192  122.331 1.00 38.23 ? 803  ARG   A CZ    1 
ATOM   5886  N  NH1   . ARG   A  1  805  ? 7.155   78.449  122.747 1.00 36.75 ? 803  ARG   A NH1   1 
ATOM   5887  N  NH2   . ARG   A  1  805  ? 8.145   76.385  122.752 1.00 42.94 ? 803  ARG   A NH2   1 
ATOM   5888  N  N     . PRO   A  1  806  ? 1.681   80.229  119.086 1.00 28.28 ? 804  PRO   A N     1 
ATOM   5889  C  CA    . PRO   A  1  806  ? 0.615   80.981  118.409 1.00 26.72 ? 804  PRO   A CA    1 
ATOM   5890  C  C     . PRO   A  1  806  ? -0.763  80.432  118.743 1.00 27.91 ? 804  PRO   A C     1 
ATOM   5891  O  O     . PRO   A  1  806  ? -0.945  79.230  118.946 1.00 25.89 ? 804  PRO   A O     1 
ATOM   5892  C  CB    . PRO   A  1  806  ? 0.935   80.786  116.923 1.00 27.41 ? 804  PRO   A CB    1 
ATOM   5893  C  CG    . PRO   A  1  806  ? 2.393   80.544  116.890 1.00 31.02 ? 804  PRO   A CG    1 
ATOM   5894  C  CD    . PRO   A  1  806  ? 2.694   79.750  118.130 1.00 29.39 ? 804  PRO   A CD    1 
ATOM   5895  N  N     . ILE   A  1  807  ? -1.738  81.336  118.789 1.00 22.30 ? 805  ILE   A N     1 
ATOM   5896  C  CA    . ILE   A  1  807  ? -3.137  80.970  119.008 1.00 23.29 ? 805  ILE   A CA    1 
ATOM   5897  C  C     . ILE   A  1  807  ? -3.670  80.337  117.728 1.00 24.20 ? 805  ILE   A C     1 
ATOM   5898  O  O     . ILE   A  1  807  ? -3.649  80.979  116.672 1.00 23.57 ? 805  ILE   A O     1 
ATOM   5899  C  CB    . ILE   A  1  807  ? -3.971  82.200  119.384 1.00 23.95 ? 805  ILE   A CB    1 
ATOM   5900  C  CG1   . ILE   A  1  807  ? -3.407  82.865  120.642 1.00 27.49 ? 805  ILE   A CG1   1 
ATOM   5901  C  CG2   . ILE   A  1  807  ? -5.437  81.819  119.568 1.00 25.42 ? 805  ILE   A CG2   1 
ATOM   5902  C  CD1   . ILE   A  1  807  ? -3.417  81.988  121.869 1.00 29.36 ? 805  ILE   A CD1   1 
ATOM   5903  N  N     . PRO   A  1  808  ? -4.139  79.091  117.764 1.00 23.39 ? 806  PRO   A N     1 
ATOM   5904  C  CA    . PRO   A  1  808  ? -4.606  78.450  116.529 1.00 22.26 ? 806  PRO   A CA    1 
ATOM   5905  C  C     . PRO   A  1  808  ? -5.791  79.185  115.921 1.00 21.49 ? 806  PRO   A C     1 
ATOM   5906  O  O     . PRO   A  1  808  ? -6.732  79.585  116.615 1.00 22.85 ? 806  PRO   A O     1 
ATOM   5907  C  CB    . PRO   A  1  808  ? -5.009  77.046  116.992 1.00 22.53 ? 806  PRO   A CB    1 
ATOM   5908  C  CG    . PRO   A  1  808  ? -4.200  76.814  118.215 1.00 25.23 ? 806  PRO   A CG    1 
ATOM   5909  C  CD    . PRO   A  1  808  ? -4.134  78.157  118.897 1.00 23.19 ? 806  PRO   A CD    1 
ATOM   5910  N  N     . LEU   A  1  809  ? -5.731  79.358  114.604 1.00 22.20 ? 807  LEU   A N     1 
ATOM   5911  C  CA    . LEU   A  1  809  ? -6.797  79.999  113.848 1.00 20.95 ? 807  LEU   A CA    1 
ATOM   5912  C  C     . LEU   A  1  809  ? -7.183  79.087  112.698 1.00 21.81 ? 807  LEU   A C     1 
ATOM   5913  O  O     . LEU   A  1  809  ? -6.343  78.757  111.851 1.00 21.29 ? 807  LEU   A O     1 
ATOM   5914  C  CB    . LEU   A  1  809  ? -6.334  81.343  113.284 1.00 21.42 ? 807  LEU   A CB    1 
ATOM   5915  C  CG    . LEU   A  1  809  ? -7.301  81.991  112.291 1.00 21.40 ? 807  LEU   A CG    1 
ATOM   5916  C  CD1   . LEU   A  1  809  ? -8.590  82.387  112.979 1.00 21.52 ? 807  LEU   A CD1   1 
ATOM   5917  C  CD2   . LEU   A  1  809  ? -6.647  83.195  111.644 1.00 25.63 ? 807  LEU   A CD2   1 
ATOM   5918  N  N     . ILE   A  1  810  ? -8.447  78.680  112.668 1.00 19.23 ? 808  ILE   A N     1 
ATOM   5919  C  CA    . ILE   A  1  810  ? -9.037  78.087  111.481 1.00 20.87 ? 808  ILE   A CA    1 
ATOM   5920  C  C     . ILE   A  1  810  ? -9.807  79.202  110.809 1.00 21.47 ? 808  ILE   A C     1 
ATOM   5921  O  O     . ILE   A  1  810  ? -10.710 79.787  111.414 1.00 21.34 ? 808  ILE   A O     1 
ATOM   5922  C  CB    . ILE   A  1  810  ? -9.966  76.918  111.828 1.00 19.97 ? 808  ILE   A CB    1 
ATOM   5923  C  CG1   . ILE   A  1  810  ? -9.227  75.871  112.651 1.00 21.47 ? 808  ILE   A CG1   1 
ATOM   5924  C  CG2   . ILE   A  1  810  ? -10.509 76.302  110.543 1.00 20.54 ? 808  ILE   A CG2   1 
ATOM   5925  C  CD1   . ILE   A  1  810  ? -10.065 74.634  112.936 1.00 25.27 ? 808  ILE   A CD1   1 
ATOM   5926  N  N     . ALA   A  1  811  ? -9.424  79.529  109.582 1.00 19.32 ? 809  ALA   A N     1 
ATOM   5927  C  CA    . ALA   A  1  811  ? -10.019 80.648  108.857 1.00 20.06 ? 809  ALA   A CA    1 
ATOM   5928  C  C     . ALA   A  1  811  ? -10.457 80.116  107.503 1.00 21.08 ? 809  ALA   A C     1 
ATOM   5929  O  O     . ALA   A  1  811  ? -9.633  79.876  106.616 1.00 20.18 ? 809  ALA   A O     1 
ATOM   5930  C  CB    . ALA   A  1  811  ? -9.045  81.805  108.718 1.00 21.98 ? 809  ALA   A CB    1 
ATOM   5931  N  N     . GLU   A  1  812  ? -11.755 79.918  107.359 1.00 18.38 ? 810  GLU   A N     1 
ATOM   5932  C  CA    . GLU   A  1  812  ? -12.339 79.375  106.142 1.00 19.49 ? 810  GLU   A CA    1 
ATOM   5933  C  C     . GLU   A  1  812  ? -13.035 80.522  105.428 1.00 18.74 ? 810  GLU   A C     1 
ATOM   5934  O  O     . GLU   A  1  812  ? -13.975 81.119  105.967 1.00 18.75 ? 810  GLU   A O     1 
ATOM   5935  C  CB    . GLU   A  1  812  ? -13.271 78.216  106.483 1.00 21.64 ? 810  GLU   A CB    1 
ATOM   5936  C  CG    . GLU   A  1  812  ? -12.519 77.077  107.204 1.00 20.09 ? 810  GLU   A CG    1 
ATOM   5937  C  CD    . GLU   A  1  812  ? -11.343 76.521  106.388 1.00 25.77 ? 810  GLU   A CD    1 
ATOM   5938  O  OE1   . GLU   A  1  812  ? -11.584 75.729  105.451 1.00 24.93 ? 810  GLU   A OE1   1 
ATOM   5939  O  OE2   . GLU   A  1  812  ? -10.174 76.877  106.681 1.00 25.57 ? 810  GLU   A OE2   1 
ATOM   5940  N  N     . THR   A  1  813  ? -12.533 80.864  104.242 1.00 18.87 ? 811  THR   A N     1 
ATOM   5941  C  CA    . THR   A  1  813  ? -12.838 82.158  103.653 1.00 19.32 ? 811  THR   A CA    1 
ATOM   5942  C  C     . THR   A  1  813  ? -13.434 82.036  102.252 1.00 20.14 ? 811  THR   A C     1 
ATOM   5943  O  O     . THR   A  1  813  ? -14.006 80.998  101.914 1.00 21.18 ? 811  THR   A O     1 
ATOM   5944  C  CB    . THR   A  1  813  ? -11.610 83.075  103.736 1.00 19.79 ? 811  THR   A CB    1 
ATOM   5945  O  OG1   . THR   A  1  813  ? -10.448 82.413  103.212 1.00 22.60 ? 811  THR   A OG1   1 
ATOM   5946  C  CG2   . THR   A  1  813  ? -11.334 83.418  105.198 1.00 19.33 ? 811  THR   A CG2   1 
ATOM   5947  N  N     . GLY   A  1  814  ? -13.326 83.089  101.443 1.00 20.24 ? 812  GLY   A N     1 
ATOM   5948  C  CA    . GLY   A  1  814  ? -14.111 83.185  100.228 1.00 19.55 ? 812  GLY   A CA    1 
ATOM   5949  C  C     . GLY   A  1  814  ? -13.561 82.355  99.085  1.00 21.35 ? 812  GLY   A C     1 
ATOM   5950  O  O     . GLY   A  1  814  ? -12.494 81.750  99.165  1.00 21.64 ? 812  GLY   A O     1 
ATOM   5951  N  N     . GLY   A  1  815  ? -14.321 82.340  97.987  1.00 20.33 ? 813  GLY   A N     1 
ATOM   5952  C  CA    . GLY   A  1  815  ? -13.914 81.642  96.790  1.00 19.59 ? 813  GLY   A CA    1 
ATOM   5953  C  C     . GLY   A  1  815  ? -14.094 82.514  95.563  1.00 18.83 ? 813  GLY   A C     1 
ATOM   5954  O  O     . GLY   A  1  815  ? -14.757 83.550  95.591  1.00 23.39 ? 813  GLY   A O     1 
ATOM   5955  N  N     . GLN   A  1  816  ? -13.454 82.095  94.485  1.00 18.04 ? 814  GLN   A N     1 
ATOM   5956  C  CA    . GLN   A  1  816  ? -13.678 82.673  93.164  1.00 19.62 ? 814  GLN   A CA    1 
ATOM   5957  C  C     . GLN   A  1  816  ? -13.823 81.476  92.241  1.00 18.17 ? 814  GLN   A C     1 
ATOM   5958  O  O     . GLN   A  1  816  ? -12.968 81.187  91.405  1.00 20.42 ? 814  GLN   A O     1 
ATOM   5959  C  CB    . GLN   A  1  816  ? -12.531 83.582  92.743  1.00 20.20 ? 814  GLN   A CB    1 
ATOM   5960  C  CG    . GLN   A  1  816  ? -12.804 84.382  91.484  1.00 23.31 ? 814  GLN   A CG    1 
ATOM   5961  C  CD    . GLN   A  1  816  ? -13.876 85.431  91.687  1.00 27.18 ? 814  GLN   A CD    1 
ATOM   5962  O  OE1   . GLN   A  1  816  ? -15.066 85.117  91.724  1.00 24.22 ? 814  GLN   A OE1   1 
ATOM   5963  N  NE2   . GLN   A  1  816  ? -13.457 86.690  91.828  1.00 26.73 ? 814  GLN   A NE2   1 
ATOM   5964  N  N     . ASN   A  1  817  ? -14.922 80.770  92.428  1.00 17.07 ? 815  ASN   A N     1 
ATOM   5965  C  CA    . ASN   A  1  817  ? -15.027 79.391  91.996  1.00 15.59 ? 815  ASN   A CA    1 
ATOM   5966  C  C     . ASN   A  1  817  ? -15.376 79.318  90.522  1.00 16.57 ? 815  ASN   A C     1 
ATOM   5967  O  O     . ASN   A  1  817  ? -16.289 80.004  90.049  1.00 17.74 ? 815  ASN   A O     1 
ATOM   5968  C  CB    . ASN   A  1  817  ? -16.085 78.694  92.842  1.00 16.54 ? 815  ASN   A CB    1 
ATOM   5969  C  CG    . ASN   A  1  817  ? -15.867 78.938  94.313  1.00 17.09 ? 815  ASN   A CG    1 
ATOM   5970  O  OD1   . ASN   A  1  817  ? -14.770 78.709  94.827  1.00 15.12 ? 815  ASN   A OD1   1 
ATOM   5971  N  ND2   . ASN   A  1  817  ? -16.889 79.447  94.996  1.00 17.28 ? 815  ASN   A ND2   1 
ATOM   5972  N  N     . ALA   A  1  818  ? -14.646 78.474  89.803  1.00 15.93 ? 816  ALA   A N     1 
ATOM   5973  C  CA    . ALA   A  1  818  ? -14.804 78.302  88.372  1.00 17.27 ? 816  ALA   A CA    1 
ATOM   5974  C  C     . ALA   A  1  818  ? -15.389 76.933  88.067  1.00 15.77 ? 816  ALA   A C     1 
ATOM   5975  O  O     . ALA   A  1  818  ? -15.245 75.982  88.841  1.00 15.70 ? 816  ALA   A O     1 
ATOM   5976  C  CB    . ALA   A  1  818  ? -13.439 78.393  87.692  1.00 15.30 ? 816  ALA   A CB    1 
ATOM   5977  N  N     . MET   A  1  819  ? -16.063 76.850  86.925  1.00 16.59 ? 817  MET   A N     1 
ATOM   5978  C  CA    . MET   A  1  819  ? -16.418 75.578  86.324  1.00 16.04 ? 817  MET   A CA    1 
ATOM   5979  C  C     . MET   A  1  819  ? -15.943 75.609  84.885  1.00 16.59 ? 817  MET   A C     1 
ATOM   5980  O  O     . MET   A  1  819  ? -16.182 76.587  84.169  1.00 17.22 ? 817  MET   A O     1 
ATOM   5981  C  CB    . MET   A  1  819  ? -17.924 75.353  86.343  1.00 17.67 ? 817  MET   A CB    1 
ATOM   5982  C  CG    . MET   A  1  819  ? -18.323 74.033  85.713  1.00 18.57 ? 817  MET   A CG    1 
ATOM   5983  S  SD    . MET   A  1  819  ? -20.121 73.959  85.514  1.00 20.69 ? 817  MET   A SD    1 
ATOM   5984  C  CE    . MET   A  1  819  ? -20.608 73.782  87.224  1.00 21.86 ? 817  MET   A CE    1 
ATOM   5985  N  N     . ILE   A  1  820  ? -15.265 74.551  84.468  1.00 14.93 ? 818  ILE   A N     1 
ATOM   5986  C  CA    . ILE   A  1  820  ? -14.789 74.427  83.101  1.00 16.22 ? 818  ILE   A CA    1 
ATOM   5987  C  C     . ILE   A  1  820  ? -15.668 73.417  82.395  1.00 14.61 ? 818  ILE   A C     1 
ATOM   5988  O  O     . ILE   A  1  820  ? -15.923 72.326  82.924  1.00 15.88 ? 818  ILE   A O     1 
ATOM   5989  C  CB    . ILE   A  1  820  ? -13.312 74.018  83.064  1.00 16.42 ? 818  ILE   A CB    1 
ATOM   5990  C  CG1   . ILE   A  1  820  ? -12.472 75.121  83.690  1.00 16.41 ? 818  ILE   A CG1   1 
ATOM   5991  C  CG2   . ILE   A  1  820  ? -12.884 73.755  81.623  1.00 19.43 ? 818  ILE   A CG2   1 
ATOM   5992  C  CD1   . ILE   A  1  820  ? -10.998 74.798  83.714  1.00 16.48 ? 818  ILE   A CD1   1 
ATOM   5993  N  N     . VAL   A  1  821  ? -16.150 73.791  81.213  1.00 15.58 ? 819  VAL   A N     1 
ATOM   5994  C  CA    . VAL   A  1  821  ? -17.053 72.963  80.428  1.00 16.84 ? 819  VAL   A CA    1 
ATOM   5995  C  C     . VAL   A  1  821  ? -16.426 72.790  79.060  1.00 17.33 ? 819  VAL   A C     1 
ATOM   5996  O  O     . VAL   A  1  821  ? -16.108 73.779  78.393  1.00 19.14 ? 819  VAL   A O     1 
ATOM   5997  C  CB    . VAL   A  1  821  ? -18.432 73.631  80.293  1.00 18.84 ? 819  VAL   A CB    1 
ATOM   5998  C  CG1   . VAL   A  1  821  ? -19.361 72.773  79.465  1.00 18.70 ? 819  VAL   A CG1   1 
ATOM   5999  C  CG2   . VAL   A  1  821  ? -19.009 73.905  81.676  1.00 18.01 ? 819  VAL   A CG2   1 
ATOM   6000  N  N     . ASP   A  1  822  ? -16.233 71.547  78.644  1.00 18.01 ? 820  ASP   A N     1 
ATOM   6001  C  CA    . ASP   A  1  822  ? -15.717 71.315  77.304  1.00 20.00 ? 820  ASP   A CA    1 
ATOM   6002  C  C     . ASP   A  1  822  ? -16.840 70.891  76.363  1.00 18.33 ? 820  ASP   A C     1 
ATOM   6003  O  O     . ASP   A  1  822  ? -18.009 70.795  76.742  1.00 18.54 ? 820  ASP   A O     1 
ATOM   6004  C  CB    . ASP   A  1  822  ? -14.493 70.394  77.306  1.00 21.44 ? 820  ASP   A CB    1 
ATOM   6005  C  CG    . ASP   A  1  822  ? -14.830 68.928  77.532  1.00 21.28 ? 820  ASP   A CG    1 
ATOM   6006  O  OD1   . ASP   A  1  822  ? -16.022 68.522  77.504  1.00 21.48 ? 820  ASP   A OD1   1 
ATOM   6007  O  OD2   . ASP   A  1  822  ? -13.856 68.164  77.741  1.00 21.80 ? 820  ASP   A OD2   1 
ATOM   6008  N  N     . SER   A  1  823  ? -16.472 70.649  75.104  1.00 20.22 ? 821  SER   A N     1 
ATOM   6009  C  CA    . SER   A  1  823  ? -17.474 70.347  74.093  1.00 21.46 ? 821  SER   A CA    1 
ATOM   6010  C  C     . SER   A  1  823  ? -18.045 68.941  74.213  1.00 21.36 ? 821  SER   A C     1 
ATOM   6011  O  O     . SER   A  1  823  ? -18.959 68.604  73.455  1.00 25.18 ? 821  SER   A O     1 
ATOM   6012  C  CB    . SER   A  1  823  ? -16.886 70.567  72.698  1.00 21.46 ? 821  SER   A CB    1 
ATOM   6013  O  OG    . SER   A  1  823  ? -15.723 69.777  72.523  1.00 26.11 ? 821  SER   A OG    1 
ATOM   6014  N  N     . SER   A  1  824  ? -17.551 68.115  75.133  1.00 20.62 ? 822  SER   A N     1 
ATOM   6015  C  CA    . SER   A  1  824  ? -18.126 66.797  75.336  1.00 21.02 ? 822  SER   A CA    1 
ATOM   6016  C  C     . SER   A  1  824  ? -19.254 66.806  76.359  1.00 22.00 ? 822  SER   A C     1 
ATOM   6017  O  O     . SER   A  1  824  ? -19.967 65.806  76.492  1.00 21.08 ? 822  SER   A O     1 
ATOM   6018  C  CB    . SER   A  1  824  ? -17.046 65.803  75.780  1.00 22.56 ? 822  SER   A CB    1 
ATOM   6019  O  OG    . SER   A  1  824  ? -16.662 66.053  77.120  1.00 21.15 ? 822  SER   A OG    1 
ATOM   6020  N  N     . ALA   A  1  825  ? -19.422 67.906  77.089  1.00 20.36 ? 823  ALA   A N     1 
ATOM   6021  C  CA    . ALA   A  1  825  ? -20.430 67.954  78.130  1.00 19.86 ? 823  ALA   A CA    1 
ATOM   6022  C  C     . ALA   A  1  825  ? -21.822 68.056  77.514  1.00 21.93 ? 823  ALA   A C     1 
ATOM   6023  O  O     . ALA   A  1  825  ? -21.997 68.550  76.400  1.00 23.26 ? 823  ALA   A O     1 
ATOM   6024  C  CB    . ALA   A  1  825  ? -20.175 69.158  79.034  1.00 20.48 ? 823  ALA   A CB    1 
ATOM   6025  N  N     . LEU   A  1  826  ? -22.813 67.553  78.241  1.00 20.88 ? 824  LEU   A N     1 
ATOM   6026  C  CA    . LEU   A  1  826  ? -24.206 67.656  77.818  1.00 23.28 ? 824  LEU   A CA    1 
ATOM   6027  C  C     . LEU   A  1  826  ? -24.752 69.008  78.267  1.00 23.56 ? 824  LEU   A C     1 
ATOM   6028  O  O     . LEU   A  1  826  ? -24.785 69.303  79.469  1.00 22.37 ? 824  LEU   A O     1 
ATOM   6029  C  CB    . LEU   A  1  826  ? -25.020 66.520  78.432  1.00 26.70 ? 824  LEU   A CB    1 
ATOM   6030  N  N     . ALA   A  1  827  ? -25.165 69.835  77.301  1.00 22.28 ? 825  ALA   A N     1 
ATOM   6031  C  CA    . ALA   A  1  827  ? -25.520 71.218  77.610  1.00 20.67 ? 825  ALA   A CA    1 
ATOM   6032  C  C     . ALA   A  1  827  ? -26.609 71.308  78.676  1.00 21.72 ? 825  ALA   A C     1 
ATOM   6033  O  O     . ALA   A  1  827  ? -26.495 72.111  79.611  1.00 20.16 ? 825  ALA   A O     1 
ATOM   6034  C  CB    . ALA   A  1  827  ? -25.933 71.960  76.339  1.00 25.51 ? 825  ALA   A CB    1 
ATOM   6035  N  N     . GLU   A  1  828  ? -27.664 70.491  78.558  1.00 22.07 ? 826  GLU   A N     1 
ATOM   6036  C  CA    . GLU   A  1  828  ? -28.771 70.564  79.511  1.00 22.59 ? 826  GLU   A CA    1 
ATOM   6037  C  C     . GLU   A  1  828  ? -28.295 70.257  80.923  1.00 21.62 ? 826  GLU   A C     1 
ATOM   6038  O  O     . GLU   A  1  828  ? -28.754 70.872  81.896  1.00 22.04 ? 826  GLU   A O     1 
ATOM   6039  C  CB    . GLU   A  1  828  ? -29.881 69.583  79.121  1.00 26.19 ? 826  GLU   A CB    1 
ATOM   6040  C  CG    . GLU   A  1  828  ? -30.699 69.986  77.895  1.00 29.27 ? 826  GLU   A CG    1 
ATOM   6041  C  CD    . GLU   A  1  828  ? -29.956 69.799  76.575  1.00 37.43 ? 826  GLU   A CD    1 
ATOM   6042  O  OE1   . GLU   A  1  828  ? -28.881 69.156  76.564  1.00 33.99 ? 826  GLU   A OE1   1 
ATOM   6043  O  OE2   . GLU   A  1  828  ? -30.455 70.301  75.543  1.00 42.83 ? 826  GLU   A OE2   1 
ATOM   6044  N  N     . GLN   A  1  829  ? -27.381 69.297  81.051  1.00 22.01 ? 827  GLN   A N     1 
ATOM   6045  C  CA    . GLN   A  1  829  ? -26.807 68.975  82.353  1.00 21.30 ? 827  GLN   A CA    1 
ATOM   6046  C  C     . GLN   A  1  829  ? -25.980 70.138  82.883  1.00 20.69 ? 827  GLN   A C     1 
ATOM   6047  O  O     . GLN   A  1  829  ? -26.100 70.528  84.053  1.00 21.16 ? 827  GLN   A O     1 
ATOM   6048  C  CB    . GLN   A  1  829  ? -25.947 67.723  82.206  1.00 23.02 ? 827  GLN   A CB    1 
ATOM   6049  C  CG    . GLN   A  1  829  ? -25.450 67.152  83.489  1.00 29.25 ? 827  GLN   A CG    1 
ATOM   6050  C  CD    . GLN   A  1  829  ? -24.786 65.807  83.274  1.00 33.61 ? 827  GLN   A CD    1 
ATOM   6051  O  OE1   . GLN   A  1  829  ? -24.202 65.548  82.214  1.00 32.88 ? 827  GLN   A OE1   1 
ATOM   6052  N  NE2   . GLN   A  1  829  ? -24.886 64.935  84.269  1.00 39.15 ? 827  GLN   A NE2   1 
ATOM   6053  N  N     . VAL   A  1  830  ? -25.123 70.698  82.027  1.00 17.92 ? 828  VAL   A N     1 
ATOM   6054  C  CA    . VAL   A  1  830  ? -24.329 71.859  82.404  1.00 19.26 ? 828  VAL   A CA    1 
ATOM   6055  C  C     . VAL   A  1  830  ? -25.228 72.987  82.879  1.00 19.24 ? 828  VAL   A C     1 
ATOM   6056  O  O     . VAL   A  1  830  ? -24.996 73.585  83.932  1.00 17.56 ? 828  VAL   A O     1 
ATOM   6057  C  CB    . VAL   A  1  830  ? -23.463 72.317  81.223  1.00 19.26 ? 828  VAL   A CB    1 
ATOM   6058  C  CG1   . VAL   A  1  830  ? -22.833 73.667  81.520  1.00 19.69 ? 828  VAL   A CG1   1 
ATOM   6059  C  CG2   . VAL   A  1  830  ? -22.386 71.275  80.916  1.00 22.01 ? 828  VAL   A CG2   1 
ATOM   6060  N  N     . VAL   A  1  831  ? -26.255 73.316  82.089  1.00 17.50 ? 829  VAL   A N     1 
ATOM   6061  C  CA    . VAL   A  1  831  ? -27.074 74.475  82.426  1.00 16.87 ? 829  VAL   A CA    1 
ATOM   6062  C  C     . VAL   A  1  831  ? -27.738 74.289  83.779  1.00 18.13 ? 829  VAL   A C     1 
ATOM   6063  O  O     . VAL   A  1  831  ? -27.756 75.210  84.602  1.00 18.63 ? 829  VAL   A O     1 
ATOM   6064  C  CB    . VAL   A  1  831  ? -28.086 74.779  81.312  1.00 18.87 ? 829  VAL   A CB    1 
ATOM   6065  C  CG1   . VAL   A  1  831  ? -29.062 75.849  81.775  1.00 19.99 ? 829  VAL   A CG1   1 
ATOM   6066  C  CG2   . VAL   A  1  831  ? -27.343 75.255  80.085  1.00 22.23 ? 829  VAL   A CG2   1 
ATOM   6067  N  N     . GLY   A  1  832  ? -28.284 73.098  84.033  1.00 18.77 ? 830  GLY   A N     1 
ATOM   6068  C  CA    . GLY   A  1  832  ? -28.896 72.848  85.328  1.00 17.56 ? 830  GLY   A CA    1 
ATOM   6069  C  C     . GLY   A  1  832  ? -27.907 73.028  86.465  1.00 17.24 ? 830  GLY   A C     1 
ATOM   6070  O  O     . GLY   A  1  832  ? -28.200 73.684  87.468  1.00 18.66 ? 830  GLY   A O     1 
ATOM   6071  N  N     . ASP   A  1  833  ? -26.707 72.472  86.304  1.00 18.23 ? 831  ASP   A N     1 
ATOM   6072  C  CA    . ASP   A  1  833  ? -25.707 72.586  87.363  1.00 19.24 ? 831  ASP   A CA    1 
ATOM   6073  C  C     . ASP   A  1  833  ? -25.198 74.012  87.524  1.00 17.12 ? 831  ASP   A C     1 
ATOM   6074  O  O     . ASP   A  1  833  ? -24.826 74.416  88.630  1.00 17.06 ? 831  ASP   A O     1 
ATOM   6075  C  CB    . ASP   A  1  833  ? -24.546 71.637  87.082  1.00 17.74 ? 831  ASP   A CB    1 
ATOM   6076  C  CG    . ASP   A  1  833  ? -24.938 70.202  87.255  1.00 20.29 ? 831  ASP   A CG    1 
ATOM   6077  O  OD1   . ASP   A  1  833  ? -25.975 69.964  87.906  1.00 23.25 ? 831  ASP   A OD1   1 
ATOM   6078  O  OD2   . ASP   A  1  833  ? -24.236 69.310  86.735  1.00 20.79 ? 831  ASP   A OD2   1 
ATOM   6079  N  N     . VAL   A  1  834  ? -25.136 74.770  86.431  1.00 16.02 ? 832  VAL   A N     1 
ATOM   6080  C  CA    . VAL   A  1  834  ? -24.707 76.163  86.492  1.00 16.14 ? 832  VAL   A CA    1 
ATOM   6081  C  C     . VAL   A  1  834  ? -25.766 77.018  87.173  1.00 18.36 ? 832  VAL   A C     1 
ATOM   6082  O  O     . VAL   A  1  834  ? -25.461 77.842  88.045  1.00 18.48 ? 832  VAL   A O     1 
ATOM   6083  C  CB    . VAL   A  1  834  ? -24.391 76.674  85.075  1.00 17.28 ? 832  VAL   A CB    1 
ATOM   6084  C  CG1   . VAL   A  1  834  ? -24.266 78.179  85.060  1.00 18.51 ? 832  VAL   A CG1   1 
ATOM   6085  C  CG2   . VAL   A  1  834  ? -23.117 76.012  84.548  1.00 17.12 ? 832  VAL   A CG2   1 
ATOM   6086  N  N     . ILE   A  1  835  ? -27.026 76.856  86.762  1.00 17.55 ? 833  ILE   A N     1 
ATOM   6087  C  CA    . ILE   A  1  835  ? -28.107 77.616  87.375  1.00 18.24 ? 833  ILE   A CA    1 
ATOM   6088  C  C     . ILE   A  1  835  ? -28.129 77.374  88.876  1.00 19.61 ? 833  ILE   A C     1 
ATOM   6089  O  O     . ILE   A  1  835  ? -28.203 78.314  89.676  1.00 20.54 ? 833  ILE   A O     1 
ATOM   6090  C  CB    . ILE   A  1  835  ? -29.451 77.274  86.711  1.00 18.96 ? 833  ILE   A CB    1 
ATOM   6091  C  CG1   . ILE   A  1  835  ? -29.512 77.839  85.284  1.00 22.73 ? 833  ILE   A CG1   1 
ATOM   6092  C  CG2   . ILE   A  1  835  ? -30.607 77.792  87.572  1.00 23.47 ? 833  ILE   A CG2   1 
ATOM   6093  C  CD1   . ILE   A  1  835  ? -29.691 79.335  85.213  1.00 26.50 ? 833  ILE   A CD1   1 
ATOM   6094  N  N     . THR   A  1  836  ? -28.020 76.110  89.280  1.00 17.80 ? 834  THR   A N     1 
ATOM   6095  C  CA    . THR   A  1  836  ? -28.001 75.792  90.704  1.00 19.41 ? 834  THR   A CA    1 
ATOM   6096  C  C     . THR   A  1  836  ? -26.761 76.369  91.371  1.00 18.16 ? 834  THR   A C     1 
ATOM   6097  O  O     . THR   A  1  836  ? -26.855 77.053  92.392  1.00 21.16 ? 834  THR   A O     1 
ATOM   6098  C  CB    . THR   A  1  836  ? -28.057 74.274  90.893  1.00 23.00 ? 834  THR   A CB    1 
ATOM   6099  O  OG1   . THR   A  1  836  ? -29.308 73.789  90.398  1.00 27.56 ? 834  THR   A OG1   1 
ATOM   6100  C  CG2   . THR   A  1  836  ? -27.940 73.918  92.357  1.00 26.39 ? 834  THR   A CG2   1 
ATOM   6101  N  N     . SER   A  1  837  ? -25.588 76.132  90.789  1.00 17.09 ? 835  SER   A N     1 
ATOM   6102  C  CA    . SER   A  1  837  ? -24.356 76.520  91.465  1.00 17.53 ? 835  SER   A CA    1 
ATOM   6103  C  C     . SER   A  1  837  ? -24.221 78.030  91.561  1.00 16.72 ? 835  SER   A C     1 
ATOM   6104  O  O     . SER   A  1  837  ? -23.691 78.546  92.545  1.00 18.11 ? 835  SER   A O     1 
ATOM   6105  C  CB    . SER   A  1  837  ? -23.141 75.925  90.749  1.00 16.75 ? 835  SER   A CB    1 
ATOM   6106  O  OG    . SER   A  1  837  ? -23.206 74.516  90.784  1.00 18.21 ? 835  SER   A OG    1 
ATOM   6107  N  N     . ALA   A  1  838  ? -24.681 78.755  90.551  1.00 16.63 ? 836  ALA   A N     1 
ATOM   6108  C  CA    . ALA   A  1  838  ? -24.458 80.189  90.533  1.00 17.26 ? 836  ALA   A CA    1 
ATOM   6109  C  C     . ALA   A  1  838  ? -25.541 80.952  91.269  1.00 20.95 ? 836  ALA   A C     1 
ATOM   6110  O  O     . ALA   A  1  838  ? -25.254 81.982  91.876  1.00 19.18 ? 836  ALA   A O     1 
ATOM   6111  C  CB    . ALA   A  1  838  ? -24.373 80.696  89.091  1.00 18.82 ? 836  ALA   A CB    1 
ATOM   6112  N  N     . PHE   A  1  839  ? -26.782 80.485  91.210  1.00 19.35 ? 837  PHE   A N     1 
ATOM   6113  C  CA    . PHE   A  1  839  ? -27.900 81.309  91.644  1.00 20.14 ? 837  PHE   A CA    1 
ATOM   6114  C  C     . PHE   A  1  839  ? -28.707 80.761  92.804  1.00 21.14 ? 837  PHE   A C     1 
ATOM   6115  O  O     . PHE   A  1  839  ? -29.497 81.517  93.381  1.00 21.29 ? 837  PHE   A O     1 
ATOM   6116  C  CB    . PHE   A  1  839  ? -28.826 81.638  90.467  1.00 20.82 ? 837  PHE   A CB    1 
ATOM   6117  C  CG    . PHE   A  1  839  ? -28.105 82.244  89.317  1.00 18.11 ? 837  PHE   A CG    1 
ATOM   6118  C  CD1   . PHE   A  1  839  ? -27.434 83.440  89.463  1.00 20.52 ? 837  PHE   A CD1   1 
ATOM   6119  C  CD2   . PHE   A  1  839  ? -28.085 81.616  88.088  1.00 21.05 ? 837  PHE   A CD2   1 
ATOM   6120  C  CE1   . PHE   A  1  839  ? -26.763 84.003  88.406  1.00 19.71 ? 837  PHE   A CE1   1 
ATOM   6121  C  CE2   . PHE   A  1  839  ? -27.408 82.171  87.023  1.00 21.77 ? 837  PHE   A CE2   1 
ATOM   6122  C  CZ    . PHE   A  1  839  ? -26.751 83.369  87.177  1.00 21.23 ? 837  PHE   A CZ    1 
ATOM   6123  N  N     . ASP   A  1  840  ? -28.531 79.496  93.173  1.00 22.13 ? 838  ASP   A N     1 
ATOM   6124  C  CA    . ASP   A  1  840  ? -29.094 79.008  94.421  1.00 22.97 ? 838  ASP   A CA    1 
ATOM   6125  C  C     . ASP   A  1  840  ? -28.688 79.947  95.545  1.00 23.81 ? 838  ASP   A C     1 
ATOM   6126  O  O     . ASP   A  1  840  ? -27.549 80.425  95.595  1.00 21.60 ? 838  ASP   A O     1 
ATOM   6127  C  CB    . ASP   A  1  840  ? -28.550 77.606  94.698  1.00 25.13 ? 838  ASP   A CB    1 
ATOM   6128  C  CG    . ASP   A  1  840  ? -29.103 76.993  95.958  1.00 32.11 ? 838  ASP   A CG    1 
ATOM   6129  O  OD1   . ASP   A  1  840  ? -28.558 77.271  97.050  1.00 31.27 ? 838  ASP   A OD1   1 
ATOM   6130  O  OD2   . ASP   A  1  840  ? -30.083 76.225  95.845  1.00 38.05 ? 838  ASP   A OD2   1 
ATOM   6131  N  N     . SER   A  1  841  ? -29.639 80.249  96.428  1.00 21.26 ? 839  SER   A N     1 
ATOM   6132  C  CA    . SER   A  1  841  ? -29.395 81.165  97.540  1.00 22.47 ? 839  SER   A CA    1 
ATOM   6133  C  C     . SER   A  1  841  ? -28.908 82.528  97.062  1.00 20.16 ? 839  SER   A C     1 
ATOM   6134  O  O     . SER   A  1  841  ? -28.181 83.222  97.778  1.00 20.16 ? 839  SER   A O     1 
ATOM   6135  C  CB    . SER   A  1  841  ? -28.427 80.566  98.566  1.00 25.28 ? 839  SER   A CB    1 
ATOM   6136  O  OG    . SER   A  1  841  ? -28.834 79.258  98.924  1.00 29.02 ? 839  SER   A OG    1 
ATOM   6137  N  N     . ALA   A  1  842  ? -29.295 82.911  95.846  1.00 20.21 ? 840  ALA   A N     1 
ATOM   6138  C  CA    . ALA   A  1  842  ? -28.872 84.172  95.241  1.00 18.09 ? 840  ALA   A CA    1 
ATOM   6139  C  C     . ALA   A  1  842  ? -27.350 84.283  95.193  1.00 17.87 ? 840  ALA   A C     1 
ATOM   6140  O  O     . ALA   A  1  842  ? -26.778 85.357  95.377  1.00 20.60 ? 840  ALA   A O     1 
ATOM   6141  C  CB    . ALA   A  1  842  ? -29.514 85.388  95.920  1.00 20.02 ? 840  ALA   A CB    1 
ATOM   6142  N  N     . GLY   A  1  843  ? -26.691 83.156  94.929  1.00 18.48 ? 841  GLY   A N     1 
ATOM   6143  C  CA    . GLY   A  1  843  ? -25.246 83.148  94.865  1.00 17.82 ? 841  GLY   A CA    1 
ATOM   6144  C  C     . GLY   A  1  843  ? -24.571 83.371  96.189  1.00 18.37 ? 841  GLY   A C     1 
ATOM   6145  O  O     . GLY   A  1  843  ? -23.353 83.553  96.225  1.00 19.49 ? 841  GLY   A O     1 
ATOM   6146  N  N     . GLN   A  1  844  ? -25.320 83.340  97.284  1.00 17.54 ? 842  GLN   A N     1 
ATOM   6147  C  CA    . GLN   A  1  844  ? -24.736 83.588  98.596  1.00 17.20 ? 842  GLN   A CA    1 
ATOM   6148  C  C     . GLN   A  1  844  ? -24.322 82.294  99.285  1.00 20.49 ? 842  GLN   A C     1 
ATOM   6149  O  O     . GLN   A  1  844  ? -24.693 81.999  100.418 1.00 21.37 ? 842  GLN   A O     1 
ATOM   6150  C  CB    . GLN   A  1  844  ? -25.692 84.421  99.435  1.00 17.79 ? 842  GLN   A CB    1 
ATOM   6151  C  CG    . GLN   A  1  844  ? -25.901 85.791  98.817  1.00 19.16 ? 842  GLN   A CG    1 
ATOM   6152  C  CD    . GLN   A  1  844  ? -27.122 86.478  99.366  1.00 20.67 ? 842  GLN   A CD    1 
ATOM   6153  O  OE1   . GLN   A  1  844  ? -27.032 87.572  99.907  1.00 19.85 ? 842  GLN   A OE1   1 
ATOM   6154  N  NE2   . GLN   A  1  844  ? -28.284 85.841  99.218  1.00 22.74 ? 842  GLN   A NE2   1 
ATOM   6155  N  N     . ARG   A  1  845  ? -23.544 81.500  98.556  1.00 19.34 ? 843  ARG   A N     1 
ATOM   6156  C  CA    . ARG   A  1  845  ? -22.830 80.363  99.099  1.00 19.50 ? 843  ARG   A CA    1 
ATOM   6157  C  C     . ARG   A  1  845  ? -21.363 80.612  98.812  1.00 18.64 ? 843  ARG   A C     1 
ATOM   6158  O  O     . ARG   A  1  845  ? -21.013 81.114  97.742  1.00 19.81 ? 843  ARG   A O     1 
ATOM   6159  C  CB    . ARG   A  1  845  ? -23.239 79.061  98.406  1.00 21.58 ? 843  ARG   A CB    1 
ATOM   6160  C  CG    . ARG   A  1  845  ? -24.687 78.616  98.633  1.00 20.22 ? 843  ARG   A CG    1 
ATOM   6161  C  CD    . ARG   A  1  845  ? -24.926 77.307  97.894  1.00 26.18 ? 843  ARG   A CD    1 
ATOM   6162  N  NE    . ARG   A  1  845  ? -26.219 76.720  98.219  1.00 32.36 ? 843  ARG   A NE    1 
ATOM   6163  C  CZ    . ARG   A  1  845  ? -26.402 75.797  99.153  1.00 34.85 ? 843  ARG   A CZ    1 
ATOM   6164  N  NH1   . ARG   A  1  845  ? -25.390 75.314  99.858  1.00 30.90 ? 843  ARG   A NH1   1 
ATOM   6165  N  NH2   . ARG   A  1  845  ? -27.631 75.342  99.383  1.00 39.72 ? 843  ARG   A NH2   1 
ATOM   6166  N  N     . CYS   A  1  846  ? -20.497 80.273  99.764  1.00 17.01 ? 844  CYS   A N     1 
ATOM   6167  C  CA    . CYS   A  1  846  ? -19.078 80.446  99.502  1.00 18.82 ? 844  CYS   A CA    1 
ATOM   6168  C  C     . CYS   A  1  846  ? -18.638 79.581  98.335  1.00 16.59 ? 844  CYS   A C     1 
ATOM   6169  O  O     . CYS   A  1  846  ? -17.687 79.924  97.632  1.00 17.65 ? 844  CYS   A O     1 
ATOM   6170  C  CB    . CYS   A  1  846  ? -18.286 80.077  100.749 1.00 18.92 ? 844  CYS   A CB    1 
ATOM   6171  S  SG    . CYS   A  1  846  ? -18.691 78.466  101.417 1.00 22.37 ? 844  CYS   A SG    1 
ATOM   6172  N  N     . SER   A  1  847  ? -19.332 78.473  98.118  1.00 17.22 ? 845  SER   A N     1 
ATOM   6173  C  CA    . SER   A  1  847  ? -19.053 77.511  97.064  1.00 15.19 ? 845  SER   A CA    1 
ATOM   6174  C  C     . SER   A  1  847  ? -19.653 77.902  95.727  1.00 16.14 ? 845  SER   A C     1 
ATOM   6175  O  O     . SER   A  1  847  ? -19.444 77.174  94.752  1.00 16.80 ? 845  SER   A O     1 
ATOM   6176  C  CB    . SER   A  1  847  ? -19.658 76.174  97.467  1.00 16.18 ? 845  SER   A CB    1 
ATOM   6177  O  OG    . SER   A  1  847  ? -21.034 76.361  97.767  1.00 18.89 ? 845  SER   A OG    1 
ATOM   6178  N  N     . ALA   A  1  848  ? -20.371 79.021  95.654  1.00 17.69 ? 846  ALA   A N     1 
ATOM   6179  C  CA    . ALA   A  1  848  ? -21.158 79.314  94.464  1.00 16.17 ? 846  ALA   A CA    1 
ATOM   6180  C  C     . ALA   A  1  848  ? -20.264 79.498  93.246  1.00 16.21 ? 846  ALA   A C     1 
ATOM   6181  O  O     . ALA   A  1  848  ? -19.128 79.964  93.334  1.00 17.06 ? 846  ALA   A O     1 
ATOM   6182  C  CB    . ALA   A  1  848  ? -21.993 80.580  94.676  1.00 17.92 ? 846  ALA   A CB    1 
ATOM   6183  N  N     . LEU   A  1  849  ? -20.801 79.120  92.098  1.00 17.57 ? 847  LEU   A N     1 
ATOM   6184  C  CA    . LEU   A  1  849  ? -20.079 79.271  90.848  1.00 15.41 ? 847  LEU   A CA    1 
ATOM   6185  C  C     . LEU   A  1  849  ? -20.025 80.747  90.474  1.00 16.04 ? 847  LEU   A C     1 
ATOM   6186  O  O     . LEU   A  1  849  ? -21.068 81.399  90.344  1.00 18.89 ? 847  LEU   A O     1 
ATOM   6187  C  CB    . LEU   A  1  849  ? -20.810 78.492  89.771  1.00 17.42 ? 847  LEU   A CB    1 
ATOM   6188  C  CG    . LEU   A  1  849  ? -20.222 78.684  88.372  1.00 15.87 ? 847  LEU   A CG    1 
ATOM   6189  C  CD1   . LEU   A  1  849  ? -18.774 78.209  88.296  1.00 17.12 ? 847  LEU   A CD1   1 
ATOM   6190  C  CD2   . LEU   A  1  849  ? -21.104 77.960  87.373  1.00 18.68 ? 847  LEU   A CD2   1 
ATOM   6191  N  N     . ARG   A  1  850  ? -18.810 81.265  90.305  1.00 15.53 ? 848  ARG   A N     1 
ATOM   6192  C  CA    . ARG   A  1  850  ? -18.583 82.660  89.964  1.00 18.89 ? 848  ARG   A CA    1 
ATOM   6193  C  C     . ARG   A  1  850  ? -18.126 82.846  88.533  1.00 19.50 ? 848  ARG   A C     1 
ATOM   6194  O  O     . ARG   A  1  850  ? -18.394 83.892  87.943  1.00 19.14 ? 848  ARG   A O     1 
ATOM   6195  C  CB    . ARG   A  1  850  ? -17.499 83.254  90.873  1.00 17.85 ? 848  ARG   A CB    1 
ATOM   6196  C  CG    . ARG   A  1  850  ? -17.760 83.047  92.339  1.00 19.35 ? 848  ARG   A CG    1 
ATOM   6197  C  CD    . ARG   A  1  850  ? -19.128 83.580  92.720  1.00 21.83 ? 848  ARG   A CD    1 
ATOM   6198  N  NE    . ARG   A  1  850  ? -19.296 83.543  94.164  1.00 20.00 ? 848  ARG   A NE    1 
ATOM   6199  C  CZ    . ARG   A  1  850  ? -20.446 83.770  94.784  1.00 19.87 ? 848  ARG   A CZ    1 
ATOM   6200  N  NH1   . ARG   A  1  850  ? -21.544 84.082  94.111  1.00 20.52 ? 848  ARG   A NH1   1 
ATOM   6201  N  NH2   . ARG   A  1  850  ? -20.493 83.681  96.110  1.00 20.98 ? 848  ARG   A NH2   1 
ATOM   6202  N  N     . VAL   A  1  851  ? -17.410 81.870  87.978  1.00 17.83 ? 849  VAL   A N     1 
ATOM   6203  C  CA    . VAL   A  1  851  ? -16.802 82.004  86.659  1.00 19.19 ? 849  VAL   A CA    1 
ATOM   6204  C  C     . VAL   A  1  851  ? -17.057 80.711  85.902  1.00 17.71 ? 849  VAL   A C     1 
ATOM   6205  O  O     . VAL   A  1  851  ? -16.504 79.666  86.254  1.00 18.44 ? 849  VAL   A O     1 
ATOM   6206  C  CB    . VAL   A  1  851  ? -15.293 82.279  86.713  1.00 22.11 ? 849  VAL   A CB    1 
ATOM   6207  C  CG1   . VAL   A  1  851  ? -14.782 82.509  85.294  1.00 25.17 ? 849  VAL   A CG1   1 
ATOM   6208  C  CG2   . VAL   A  1  851  ? -14.969 83.474  87.597  1.00 26.89 ? 849  VAL   A CG2   1 
ATOM   6209  N  N     . LEU   A  1  852  ? -17.891 80.776  84.874  1.00 17.63 ? 850  LEU   A N     1 
ATOM   6210  C  CA    . LEU   A  1  852  ? -18.151 79.642  83.999  1.00 16.63 ? 850  LEU   A CA    1 
ATOM   6211  C  C     . LEU   A  1  852  ? -17.268 79.777  82.768  1.00 15.65 ? 850  LEU   A C     1 
ATOM   6212  O  O     . LEU   A  1  852  ? -17.272 80.827  82.110  1.00 17.17 ? 850  LEU   A O     1 
ATOM   6213  C  CB    . LEU   A  1  852  ? -19.616 79.653  83.574  1.00 16.62 ? 850  LEU   A CB    1 
ATOM   6214  C  CG    . LEU   A  1  852  ? -20.046 78.597  82.565  1.00 16.60 ? 850  LEU   A CG    1 
ATOM   6215  C  CD1   . LEU   A  1  852  ? -19.904 77.216  83.174  1.00 15.70 ? 850  LEU   A CD1   1 
ATOM   6216  C  CD2   . LEU   A  1  852  ? -21.510 78.862  82.141  1.00 16.38 ? 850  LEU   A CD2   1 
ATOM   6217  N  N     . CYS   A  1  853  ? -16.519 78.719  82.458  1.00 17.28 ? 851  CYS   A N     1 
ATOM   6218  C  CA    . CYS   A  1  853  ? -15.543 78.732  81.374  1.00 18.00 ? 851  CYS   A CA    1 
ATOM   6219  C  C     . CYS   A  1  853  ? -16.004 77.733  80.329  1.00 15.12 ? 851  CYS   A C     1 
ATOM   6220  O  O     . CYS   A  1  853  ? -16.047 76.528  80.589  1.00 17.42 ? 851  CYS   A O     1 
ATOM   6221  C  CB    . CYS   A  1  853  ? -14.149 78.371  81.879  1.00 19.56 ? 851  CYS   A CB    1 
ATOM   6222  S  SG    . CYS   A  1  853  ? -13.622 79.317  83.304  1.00 21.48 ? 851  CYS   A SG    1 
ATOM   6223  N  N     . LEU   A  1  854  ? -16.350 78.242  79.156  1.00 17.31 ? 852  LEU   A N     1 
ATOM   6224  C  CA    . LEU   A  1  854  ? -17.001 77.471  78.112  1.00 17.66 ? 852  LEU   A CA    1 
ATOM   6225  C  C     . LEU   A  1  854  ? -16.052 77.332  76.938  1.00 17.18 ? 852  LEU   A C     1 
ATOM   6226  O  O     . LEU   A  1  854  ? -15.532 78.331  76.430  1.00 18.55 ? 852  LEU   A O     1 
ATOM   6227  C  CB    . LEU   A  1  854  ? -18.266 78.187  77.643  1.00 17.29 ? 852  LEU   A CB    1 
ATOM   6228  C  CG    . LEU   A  1  854  ? -19.367 78.364  78.695  1.00 16.16 ? 852  LEU   A CG    1 
ATOM   6229  C  CD1   . LEU   A  1  854  ? -20.592 79.043  78.052  1.00 18.19 ? 852  LEU   A CD1   1 
ATOM   6230  C  CD2   . LEU   A  1  854  ? -19.739 77.015  79.287  1.00 17.96 ? 852  LEU   A CD2   1 
ATOM   6231  N  N     . GLN   A  1  855  ? -15.844 76.099  76.501  1.00 17.34 ? 853  GLN   A N     1 
ATOM   6232  C  CA    . GLN   A  1  855  ? -15.034 75.894  75.316  1.00 18.26 ? 853  GLN   A CA    1 
ATOM   6233  C  C     . GLN   A  1  855  ? -15.691 76.605  74.141  1.00 19.33 ? 853  GLN   A C     1 
ATOM   6234  O  O     . GLN   A  1  855  ? -16.915 76.586  73.992  1.00 20.36 ? 853  GLN   A O     1 
ATOM   6235  C  CB    . GLN   A  1  855  ? -14.887 74.405  75.032  1.00 18.52 ? 853  GLN   A CB    1 
ATOM   6236  C  CG    . GLN   A  1  855  ? -13.853 74.162  73.960  1.00 18.72 ? 853  GLN   A CG    1 
ATOM   6237  C  CD    . GLN   A  1  855  ? -13.720 72.713  73.567  1.00 23.02 ? 853  GLN   A CD    1 
ATOM   6238  O  OE1   . GLN   A  1  855  ? -13.760 71.819  74.404  1.00 23.38 ? 853  GLN   A OE1   1 
ATOM   6239  N  NE2   . GLN   A  1  855  ? -13.540 72.474  72.268  1.00 27.78 ? 853  GLN   A NE2   1 
ATOM   6240  N  N     . GLU   A  1  856  ? -14.861 77.257  73.323  1.00 20.13 ? 854  GLU   A N     1 
ATOM   6241  C  CA    . GLU   A  1  856  ? -15.371 78.200  72.332  1.00 23.47 ? 854  GLU   A CA    1 
ATOM   6242  C  C     . GLU   A  1  856  ? -16.424 77.572  71.425  1.00 25.87 ? 854  GLU   A C     1 
ATOM   6243  O  O     . GLU   A  1  856  ? -17.433 78.210  71.102  1.00 24.70 ? 854  GLU   A O     1 
ATOM   6244  C  CB    . GLU   A  1  856  ? -14.202 78.769  71.528  1.00 23.19 ? 854  GLU   A CB    1 
ATOM   6245  C  CG    . GLU   A  1  856  ? -14.625 79.653  70.367  1.00 28.83 ? 854  GLU   A CG    1 
ATOM   6246  C  CD    . GLU   A  1  856  ? -15.444 80.854  70.804  1.00 37.44 ? 854  GLU   A CD    1 
ATOM   6247  O  OE1   . GLU   A  1  856  ? -15.151 81.423  71.879  1.00 36.29 ? 854  GLU   A OE1   1 
ATOM   6248  O  OE2   . GLU   A  1  856  ? -16.384 81.229  70.068  1.00 38.71 ? 854  GLU   A OE2   1 
ATOM   6249  N  N     . ASP   A  1  857  ? -16.231 76.305  71.043  1.00 24.42 ? 855  ASP   A N     1 
ATOM   6250  C  CA    . ASP   A  1  857  ? -17.081 75.670  70.041  1.00 25.12 ? 855  ASP   A CA    1 
ATOM   6251  C  C     . ASP   A  1  857  ? -18.505 75.441  70.531  1.00 25.10 ? 855  ASP   A C     1 
ATOM   6252  O  O     . ASP   A  1  857  ? -19.419 75.285  69.710  1.00 28.35 ? 855  ASP   A O     1 
ATOM   6253  C  CB    . ASP   A  1  857  ? -16.470 74.335  69.616  1.00 31.21 ? 855  ASP   A CB    1 
ATOM   6254  N  N     . VAL   A  1  858  ? -18.718 75.404  71.842  1.00 20.32 ? 856  VAL   A N     1 
ATOM   6255  C  CA    . VAL   A  1  858  ? -20.041 75.173  72.404  1.00 21.71 ? 856  VAL   A CA    1 
ATOM   6256  C  C     . VAL   A  1  858  ? -20.548 76.357  73.201  1.00 21.50 ? 856  VAL   A C     1 
ATOM   6257  O  O     . VAL   A  1  858  ? -21.668 76.304  73.722  1.00 21.16 ? 856  VAL   A O     1 
ATOM   6258  C  CB    . VAL   A  1  858  ? -20.094 73.887  73.251  1.00 22.59 ? 856  VAL   A CB    1 
ATOM   6259  C  CG1   . VAL   A  1  858  ? -19.875 72.670  72.364  1.00 24.80 ? 856  VAL   A CG1   1 
ATOM   6260  C  CG2   . VAL   A  1  858  ? -19.057 73.948  74.387  1.00 21.39 ? 856  VAL   A CG2   1 
ATOM   6261  N  N     . ALA   A  1  859  ? -19.763 77.431  73.294  1.00 19.82 ? 857  ALA   A N     1 
ATOM   6262  C  CA    . ALA   A  1  859  ? -20.086 78.518  74.209  1.00 19.94 ? 857  ALA   A CA    1 
ATOM   6263  C  C     . ALA   A  1  859  ? -21.395 79.192  73.834  1.00 23.61 ? 857  ALA   A C     1 
ATOM   6264  O  O     . ALA   A  1  859  ? -22.214 79.495  74.706  1.00 20.01 ? 857  ALA   A O     1 
ATOM   6265  C  CB    . ALA   A  1  859  ? -18.952 79.537  74.238  1.00 22.05 ? 857  ALA   A CB    1 
ATOM   6266  N  N     . ASP   A  1  860  ? -21.612 79.438  72.541  1.00 23.68 ? 858  ASP   A N     1 
ATOM   6267  C  CA    . ASP   A  1  860  ? -22.813 80.160  72.144  1.00 25.17 ? 858  ASP   A CA    1 
ATOM   6268  C  C     . ASP   A  1  860  ? -24.068 79.357  72.446  1.00 23.88 ? 858  ASP   A C     1 
ATOM   6269  O  O     . ASP   A  1  860  ? -25.046 79.900  72.974  1.00 22.72 ? 858  ASP   A O     1 
ATOM   6270  C  CB    . ASP   A  1  860  ? -22.737 80.526  70.668  1.00 23.97 ? 858  ASP   A CB    1 
ATOM   6271  C  CG    . ASP   A  1  860  ? -21.774 81.662  70.409  1.00 30.07 ? 858  ASP   A CG    1 
ATOM   6272  O  OD1   . ASP   A  1  860  ? -21.706 82.588  71.248  1.00 36.70 ? 858  ASP   A OD1   1 
ATOM   6273  O  OD2   . ASP   A  1  860  ? -21.084 81.627  69.369  1.00 44.22 ? 858  ASP   A OD2   1 
ATOM   6274  N  N     . ARG   A  1  861  ? -24.055 78.061  72.132  1.00 20.89 ? 859  ARG   A N     1 
ATOM   6275  C  CA    . ARG   A  1  861  ? -25.216 77.224  72.392  1.00 22.14 ? 859  ARG   A CA    1 
ATOM   6276  C  C     . ARG   A  1  861  ? -25.496 77.116  73.887  1.00 19.81 ? 859  ARG   A C     1 
ATOM   6277  O  O     . ARG   A  1  861  ? -26.651 77.222  74.319  1.00 22.31 ? 859  ARG   A O     1 
ATOM   6278  C  CB    . ARG   A  1  861  ? -25.013 75.840  71.783  1.00 28.87 ? 859  ARG   A CB    1 
ATOM   6279  C  CG    . ARG   A  1  861  ? -26.095 74.872  72.182  1.00 32.90 ? 859  ARG   A CG    1 
ATOM   6280  C  CD    . ARG   A  1  861  ? -26.163 73.661  71.281  1.00 41.85 ? 859  ARG   A CD    1 
ATOM   6281  N  NE    . ARG   A  1  861  ? -27.313 72.840  71.642  1.00 50.83 ? 859  ARG   A NE    1 
ATOM   6282  C  CZ    . ARG   A  1  861  ? -27.279 71.857  72.529  1.00 42.82 ? 859  ARG   A CZ    1 
ATOM   6283  N  NH1   . ARG   A  1  861  ? -26.155 71.513  73.135  1.00 44.07 ? 859  ARG   A NH1   1 
ATOM   6284  N  NH2   . ARG   A  1  861  ? -28.399 71.199  72.812  1.00 43.21 ? 859  ARG   A NH2   1 
ATOM   6285  N  N     . ILE   A  1  862  ? -24.454 76.910  74.693  1.00 18.22 ? 860  ILE   A N     1 
ATOM   6286  C  CA    . ILE   A  1  862  ? -24.661 76.800  76.134  1.00 19.72 ? 860  ILE   A CA    1 
ATOM   6287  C  C     . ILE   A  1  862  ? -25.124 78.129  76.712  1.00 19.98 ? 860  ILE   A C     1 
ATOM   6288  O  O     . ILE   A  1  862  ? -26.026 78.172  77.556  1.00 18.67 ? 860  ILE   A O     1 
ATOM   6289  C  CB    . ILE   A  1  862  ? -23.390 76.275  76.820  1.00 18.78 ? 860  ILE   A CB    1 
ATOM   6290  C  CG1   . ILE   A  1  862  ? -23.210 74.792  76.475  1.00 21.03 ? 860  ILE   A CG1   1 
ATOM   6291  C  CG2   . ILE   A  1  862  ? -23.475 76.477  78.333  1.00 20.05 ? 860  ILE   A CG2   1 
ATOM   6292  C  CD1   . ILE   A  1  862  ? -21.890 74.210  76.980  1.00 23.94 ? 860  ILE   A CD1   1 
ATOM   6293  N  N     . LEU   A  1  863  ? -24.528 79.230  76.259  1.00 18.18 ? 861  LEU   A N     1 
ATOM   6294  C  CA    A LEU   A  1  863  ? -24.913 80.546  76.763  0.44 19.90 ? 861  LEU   A CA    1 
ATOM   6295  C  CA    B LEU   A  1  863  ? -24.913 80.541  76.766  0.56 19.88 ? 861  LEU   A CA    1 
ATOM   6296  C  C     . LEU   A  1  863  ? -26.366 80.857  76.442  1.00 20.05 ? 861  LEU   A C     1 
ATOM   6297  O  O     . LEU   A  1  863  ? -27.093 81.390  77.287  1.00 18.26 ? 861  LEU   A O     1 
ATOM   6298  C  CB    A LEU   A  1  863  ? -24.003 81.625  76.180  0.44 22.10 ? 861  LEU   A CB    1 
ATOM   6299  C  CB    B LEU   A  1  863  ? -23.989 81.602  76.183  0.56 22.10 ? 861  LEU   A CB    1 
ATOM   6300  C  CG    A LEU   A  1  863  ? -22.833 82.095  77.042  0.44 23.59 ? 861  LEU   A CG    1 
ATOM   6301  C  CG    B LEU   A  1  863  ? -24.075 82.995  76.782  0.56 24.30 ? 861  LEU   A CG    1 
ATOM   6302  C  CD1   A LEU   A  1  863  ? -21.920 82.989  76.224  0.44 23.88 ? 861  LEU   A CD1   1 
ATOM   6303  C  CD1   B LEU   A  1  863  ? -23.989 82.932  78.299  0.56 23.47 ? 861  LEU   A CD1   1 
ATOM   6304  C  CD2   A LEU   A  1  863  ? -23.351 82.833  78.266  0.44 24.68 ? 861  LEU   A CD2   1 
ATOM   6305  C  CD2   B LEU   A  1  863  ? -22.945 83.818  76.203  0.56 25.66 ? 861  LEU   A CD2   1 
ATOM   6306  N  N     . THR   A  1  864  ? -26.803 80.545  75.222  1.00 19.21 ? 862  THR   A N     1 
ATOM   6307  C  CA    . THR   A  1  864  ? -28.207 80.744  74.873  1.00 21.04 ? 862  THR   A CA    1 
ATOM   6308  C  C     . THR   A  1  864  ? -29.105 79.930  75.792  1.00 19.06 ? 862  THR   A C     1 
ATOM   6309  O  O     . THR   A  1  864  ? -30.109 80.433  76.305  1.00 18.21 ? 862  THR   A O     1 
ATOM   6310  C  CB    . THR   A  1  864  ? -28.439 80.339  73.420  1.00 21.36 ? 862  THR   A CB    1 
ATOM   6311  O  OG1   . THR   A  1  864  ? -27.715 81.232  72.572  1.00 23.58 ? 862  THR   A OG1   1 
ATOM   6312  C  CG2   . THR   A  1  864  ? -29.936 80.384  73.067  1.00 19.73 ? 862  THR   A CG2   1 
ATOM   6313  N  N     . MET   A  1  865  ? -28.753 78.664  76.016  1.00 18.03 ? 863  MET   A N     1 
ATOM   6314  C  CA    . MET   A  1  865  ? -29.560 77.838  76.905  1.00 16.85 ? 863  MET   A CA    1 
ATOM   6315  C  C     . MET   A  1  865  ? -29.540 78.378  78.326  1.00 17.00 ? 863  MET   A C     1 
ATOM   6316  O  O     . MET   A  1  865  ? -30.571 78.400  79.009  1.00 16.07 ? 863  MET   A O     1 
ATOM   6317  C  CB    . MET   A  1  865  ? -29.057 76.399  76.872  1.00 19.27 ? 863  MET   A CB    1 
ATOM   6318  C  CG    . MET   A  1  865  ? -29.902 75.427  77.665  1.00 23.44 ? 863  MET   A CG    1 
ATOM   6319  S  SD    . MET   A  1  865  ? -29.256 73.758  77.435  1.00 26.14 ? 863  MET   A SD    1 
ATOM   6320  C  CE    . MET   A  1  865  ? -28.899 73.889  75.668  1.00 23.04 ? 863  MET   A CE    1 
ATOM   6321  N  N     . LEU   A  1  866  ? -28.374 78.825  78.784  1.00 17.29 ? 864  LEU   A N     1 
ATOM   6322  C  CA    . LEU   A  1  866  ? -28.262 79.342  80.141  1.00 16.77 ? 864  LEU   A CA    1 
ATOM   6323  C  C     . LEU   A  1  866  ? -29.119 80.588  80.328  1.00 16.07 ? 864  LEU   A C     1 
ATOM   6324  O  O     . LEU   A  1  866  ? -29.781 80.748  81.363  1.00 18.35 ? 864  LEU   A O     1 
ATOM   6325  C  CB    . LEU   A  1  866  ? -26.794 79.663  80.407  1.00 16.84 ? 864  LEU   A CB    1 
ATOM   6326  C  CG    . LEU   A  1  866  ? -26.506 80.280  81.769  1.00 22.92 ? 864  LEU   A CG    1 
ATOM   6327  C  CD1   . LEU   A  1  866  ? -26.929 79.302  82.854  1.00 22.27 ? 864  LEU   A CD1   1 
ATOM   6328  C  CD2   . LEU   A  1  866  ? -25.028 80.629  81.873  1.00 23.25 ? 864  LEU   A CD2   1 
ATOM   6329  N  N     . LYS   A  1  867  ? -29.084 81.506  79.358  1.00 18.09 ? 865  LYS   A N     1 
ATOM   6330  C  CA    . LYS   A  1  867  ? -29.911 82.701  79.463  1.00 18.31 ? 865  LYS   A CA    1 
ATOM   6331  C  C     . LYS   A  1  867  ? -31.386 82.337  79.456  1.00 18.59 ? 865  LYS   A C     1 
ATOM   6332  O  O     . LYS   A  1  867  ? -32.178 82.919  80.204  1.00 18.34 ? 865  LYS   A O     1 
ATOM   6333  C  CB    . LYS   A  1  867  ? -29.579 83.683  78.338  1.00 21.37 ? 865  LYS   A CB    1 
ATOM   6334  C  CG    . LYS   A  1  867  ? -28.168 84.269  78.457  1.00 22.76 ? 865  LYS   A CG    1 
ATOM   6335  C  CD    . LYS   A  1  867  ? -27.810 85.136  77.247  1.00 23.46 ? 865  LYS   A CD    1 
ATOM   6336  C  CE    . LYS   A  1  867  ? -26.385 85.669  77.363  1.00 30.66 ? 865  LYS   A CE    1 
ATOM   6337  N  NZ    . LYS   A  1  867  ? -25.942 86.408  76.140  1.00 33.98 ? 865  LYS   A NZ    1 
ATOM   6338  N  N     . GLY   A  1  868  ? -31.773 81.375  78.616  1.00 18.09 ? 866  GLY   A N     1 
ATOM   6339  C  CA    . GLY   A  1  868  ? -33.154 80.925  78.620  1.00 19.12 ? 866  GLY   A CA    1 
ATOM   6340  C  C     . GLY   A  1  868  ? -33.562 80.350  79.962  1.00 17.46 ? 866  GLY   A C     1 
ATOM   6341  O  O     . GLY   A  1  868  ? -34.668 80.604  80.452  1.00 18.57 ? 866  GLY   A O     1 
ATOM   6342  N  N     . ALA   A  1  869  ? -32.665 79.591  80.583  1.00 16.29 ? 867  ALA   A N     1 
ATOM   6343  C  CA    . ALA   A  1  869  ? -32.964 79.007  81.883  1.00 16.52 ? 867  ALA   A CA    1 
ATOM   6344  C  C     . ALA   A  1  869  ? -33.010 80.080  82.960  1.00 17.90 ? 867  ALA   A C     1 
ATOM   6345  O  O     . ALA   A  1  869  ? -33.831 80.007  83.878  1.00 18.04 ? 867  ALA   A O     1 
ATOM   6346  C  CB    . ALA   A  1  869  ? -31.909 77.963  82.233  1.00 17.45 ? 867  ALA   A CB    1 
ATOM   6347  N  N     . LEU   A  1  870  ? -32.129 81.077  82.863  1.00 17.40 ? 868  LEU   A N     1 
ATOM   6348  C  CA    . LEU   A  1  870  ? -32.126 82.176  83.823  1.00 19.36 ? 868  LEU   A CA    1 
ATOM   6349  C  C     . LEU   A  1  870  ? -33.497 82.822  83.906  1.00 19.56 ? 868  LEU   A C     1 
ATOM   6350  O  O     . LEU   A  1  870  ? -33.974 83.160  84.993  1.00 20.67 ? 868  LEU   A O     1 
ATOM   6351  C  CB    . LEU   A  1  870  ? -31.100 83.220  83.384  1.00 19.32 ? 868  LEU   A CB    1 
ATOM   6352  C  CG    . LEU   A  1  870  ? -30.782 84.398  84.310  1.00 23.95 ? 868  LEU   A CG    1 
ATOM   6353  C  CD1   . LEU   A  1  870  ? -29.778 83.984  85.361  1.00 26.35 ? 868  LEU   A CD1   1 
ATOM   6354  C  CD2   . LEU   A  1  870  ? -30.254 85.595  83.526  1.00 26.50 ? 868  LEU   A CD2   1 
ATOM   6355  N  N     . HIS   A  1  871  ? -34.148 83.004  82.762  1.00 17.66 ? 869  HIS   A N     1 
ATOM   6356  C  CA    . HIS   A  1  871  ? -35.410 83.726  82.746  1.00 21.20 ? 869  HIS   A CA    1 
ATOM   6357  C  C     . HIS   A  1  871  ? -36.577 82.906  83.263  1.00 21.88 ? 869  HIS   A C     1 
ATOM   6358  O  O     . HIS   A  1  871  ? -37.674 83.452  83.413  1.00 23.33 ? 869  HIS   A O     1 
ATOM   6359  C  CB    . HIS   A  1  871  ? -35.684 84.285  81.358  1.00 24.95 ? 869  HIS   A CB    1 
ATOM   6360  C  CG    . HIS   A  1  871  ? -34.785 85.426  81.017  1.00 26.39 ? 869  HIS   A CG    1 
ATOM   6361  N  ND1   . HIS   A  1  871  ? -34.905 86.663  81.614  1.00 27.11 ? 869  HIS   A ND1   1 
ATOM   6362  C  CD2   . HIS   A  1  871  ? -33.720 85.507  80.186  1.00 25.98 ? 869  HIS   A CD2   1 
ATOM   6363  C  CE1   . HIS   A  1  871  ? -33.964 87.465  81.147  1.00 30.16 ? 869  HIS   A CE1   1 
ATOM   6364  N  NE2   . HIS   A  1  871  ? -33.233 86.789  80.278  1.00 29.95 ? 869  HIS   A NE2   1 
ATOM   6365  N  N     . GLU   A  1  872  ? -36.364 81.634  83.559  1.00 18.12 ? 870  GLU   A N     1 
ATOM   6366  C  CA    . GLU   A  1  872  ? -37.406 80.815  84.149  1.00 21.51 ? 870  GLU   A CA    1 
ATOM   6367  C  C     . GLU   A  1  872  ? -37.371 80.830  85.666  1.00 20.42 ? 870  GLU   A C     1 
ATOM   6368  O  O     . GLU   A  1  872  ? -38.199 80.161  86.290  1.00 20.26 ? 870  GLU   A O     1 
ATOM   6369  C  CB    . GLU   A  1  872  ? -37.295 79.375  83.642  1.00 18.83 ? 870  GLU   A CB    1 
ATOM   6370  C  CG    . GLU   A  1  872  ? -37.489 79.268  82.143  1.00 19.98 ? 870  GLU   A CG    1 
ATOM   6371  C  CD    . GLU   A  1  872  ? -38.876 79.701  81.710  1.00 23.84 ? 870  GLU   A CD    1 
ATOM   6372  O  OE1   . GLU   A  1  872  ? -39.813 79.622  82.541  1.00 24.48 ? 870  GLU   A OE1   1 
ATOM   6373  O  OE2   . GLU   A  1  872  ? -39.035 80.120  80.539  1.00 23.00 ? 870  GLU   A OE2   1 
ATOM   6374  N  N     . LEU   A  1  873  ? -36.440 81.570  86.272  1.00 18.94 ? 871  LEU   A N     1 
ATOM   6375  C  CA    . LEU   A  1  873  ? -36.314 81.589  87.721  1.00 17.12 ? 871  LEU   A CA    1 
ATOM   6376  C  C     . LEU   A  1  873  ? -37.285 82.585  88.328  1.00 18.31 ? 871  LEU   A C     1 
ATOM   6377  O  O     . LEU   A  1  873  ? -37.480 83.688  87.808  1.00 22.06 ? 871  LEU   A O     1 
ATOM   6378  C  CB    . LEU   A  1  873  ? -34.899 81.990  88.126  1.00 19.32 ? 871  LEU   A CB    1 
ATOM   6379  C  CG    . LEU   A  1  873  ? -33.815 81.054  87.608  1.00 21.28 ? 871  LEU   A CG    1 
ATOM   6380  C  CD1   . LEU   A  1  873  ? -32.454 81.617  87.995  1.00 21.81 ? 871  LEU   A CD1   1 
ATOM   6381  C  CD2   . LEU   A  1  873  ? -34.016 79.652  88.168  1.00 23.31 ? 871  LEU   A CD2   1 
ATOM   6382  N  N     . HIS   A  1  874  ? -37.873 82.195  89.451  1.00 19.83 ? 872  HIS   A N     1 
ATOM   6383  C  CA    . HIS   A  1  874  ? -38.780 83.042  90.202  1.00 20.13 ? 872  HIS   A CA    1 
ATOM   6384  C  C     . HIS   A  1  874  ? -38.014 83.618  91.388  1.00 20.11 ? 872  HIS   A C     1 
ATOM   6385  O  O     . HIS   A  1  874  ? -37.518 82.869  92.233  1.00 19.60 ? 872  HIS   A O     1 
ATOM   6386  C  CB    . HIS   A  1  874  ? -39.974 82.213  90.675  1.00 21.27 ? 872  HIS   A CB    1 
ATOM   6387  C  CG    . HIS   A  1  874  ? -41.003 82.995  91.429  1.00 24.57 ? 872  HIS   A CG    1 
ATOM   6388  N  ND1   . HIS   A  1  874  ? -42.178 82.428  91.877  1.00 31.06 ? 872  HIS   A ND1   1 
ATOM   6389  C  CD2   . HIS   A  1  874  ? -41.045 84.294  91.805  1.00 29.56 ? 872  HIS   A CD2   1 
ATOM   6390  C  CE1   . HIS   A  1  874  ? -42.894 83.342  92.506  1.00 30.14 ? 872  HIS   A CE1   1 
ATOM   6391  N  NE2   . HIS   A  1  874  ? -42.228 84.484  92.477  1.00 26.65 ? 872  HIS   A NE2   1 
ATOM   6392  N  N     . ILE   A  1  875  ? -37.926 84.944  91.441  1.00 21.53 ? 873  ILE   A N     1 
ATOM   6393  C  CA    . ILE   A  1  875  ? -37.216 85.662  92.491  1.00 21.04 ? 873  ILE   A CA    1 
ATOM   6394  C  C     . ILE   A  1  875  ? -38.256 86.332  93.379  1.00 23.78 ? 873  ILE   A C     1 
ATOM   6395  O  O     . ILE   A  1  875  ? -39.178 86.992  92.882  1.00 22.49 ? 873  ILE   A O     1 
ATOM   6396  C  CB    . ILE   A  1  875  ? -36.242 86.700  91.904  1.00 21.62 ? 873  ILE   A CB    1 
ATOM   6397  C  CG1   . ILE   A  1  875  ? -34.987 86.043  91.324  1.00 26.78 ? 873  ILE   A CG1   1 
ATOM   6398  C  CG2   . ILE   A  1  875  ? -35.762 87.660  92.980  1.00 24.20 ? 873  ILE   A CG2   1 
ATOM   6399  C  CD1   . ILE   A  1  875  ? -35.184 85.197  90.088  1.00 26.77 ? 873  ILE   A CD1   1 
ATOM   6400  N  N     . GLY   A  1  876  ? -38.121 86.163  94.687  1.00 21.47 ? 874  GLY   A N     1 
ATOM   6401  C  CA    . GLY   A  1  876  ? -39.063 86.810  95.576  1.00 21.47 ? 874  GLY   A CA    1 
ATOM   6402  C  C     . GLY   A  1  876  ? -38.860 86.379  97.013  1.00 23.35 ? 874  GLY   A C     1 
ATOM   6403  O  O     . GLY   A  1  876  ? -37.903 85.674  97.350  1.00 21.37 ? 874  GLY   A O     1 
ATOM   6404  N  N     . ARG   A  1  877  ? -39.784 86.837  97.856  1.00 21.46 ? 875  ARG   A N     1 
ATOM   6405  C  CA    . ARG   A  1  877  ? -39.776 86.438  99.253  1.00 22.97 ? 875  ARG   A CA    1 
ATOM   6406  C  C     . ARG   A  1  877  ? -39.921 84.926  99.338  1.00 22.54 ? 875  ARG   A C     1 
ATOM   6407  O  O     . ARG   A  1  877  ? -40.755 84.333  98.654  1.00 22.14 ? 875  ARG   A O     1 
ATOM   6408  C  CB    . ARG   A  1  877  ? -40.929 87.125  99.978  1.00 26.64 ? 875  ARG   A CB    1 
ATOM   6409  C  CG    . ARG   A  1  877  ? -40.737 87.198  101.465 1.00 27.30 ? 875  ARG   A CG    1 
ATOM   6410  C  CD    . ARG   A  1  877  ? -41.846 88.001  102.076 1.00 31.80 ? 875  ARG   A CD    1 
ATOM   6411  N  NE    . ARG   A  1  877  ? -43.011 87.188  102.386 1.00 29.86 ? 875  ARG   A NE    1 
ATOM   6412  C  CZ    . ARG   A  1  877  ? -44.058 87.643  103.060 1.00 36.48 ? 875  ARG   A CZ    1 
ATOM   6413  N  NH1   . ARG   A  1  877  ? -44.111 88.895  103.482 1.00 33.13 ? 875  ARG   A NH1   1 
ATOM   6414  N  NH2   . ARG   A  1  877  ? -45.073 86.821  103.316 1.00 35.20 ? 875  ARG   A NH2   1 
ATOM   6415  N  N     . THR   A  1  878  ? -39.104 84.301  100.176 1.00 22.17 ? 876  THR   A N     1 
ATOM   6416  C  CA    . THR   A  1  878  ? -38.878 82.866  100.066 1.00 20.51 ? 876  THR   A CA    1 
ATOM   6417  C  C     . THR   A  1  878  ? -39.894 82.021  100.821 1.00 21.62 ? 876  THR   A C     1 
ATOM   6418  O  O     . THR   A  1  878  ? -39.725 80.799  100.879 1.00 23.13 ? 876  THR   A O     1 
ATOM   6419  C  CB    . THR   A  1  878  ? -37.463 82.521  100.539 1.00 22.19 ? 876  THR   A CB    1 
ATOM   6420  O  OG1   . THR   A  1  878  ? -37.228 83.134  101.809 1.00 24.80 ? 876  THR   A OG1   1 
ATOM   6421  C  CG2   . THR   A  1  878  ? -36.447 83.029  99.557  1.00 25.84 ? 876  THR   A CG2   1 
ATOM   6422  N  N     . ASP   A  1  879  ? -40.943 82.624  101.378 1.00 20.68 ? 877  ASP   A N     1 
ATOM   6423  C  CA    . ASP   A  1  879  ? -41.972 81.849  102.061 1.00 24.19 ? 877  ASP   A CA    1 
ATOM   6424  C  C     . ASP   A  1  879  ? -43.022 81.324  101.081 1.00 22.81 ? 877  ASP   A C     1 
ATOM   6425  O  O     . ASP   A  1  879  ? -44.179 81.084  101.456 1.00 21.84 ? 877  ASP   A O     1 
ATOM   6426  C  CB    . ASP   A  1  879  ? -42.600 82.667  103.193 1.00 22.15 ? 877  ASP   A CB    1 
ATOM   6427  C  CG    . ASP   A  1  879  ? -43.384 83.862  102.681 1.00 30.37 ? 877  ASP   A CG    1 
ATOM   6428  O  OD1   . ASP   A  1  879  ? -43.000 84.436  101.636 1.00 32.83 ? 877  ASP   A OD1   1 
ATOM   6429  O  OD2   . ASP   A  1  879  ? -44.398 84.219  103.315 1.00 29.60 ? 877  ASP   A OD2   1 
ATOM   6430  N  N     . ARG   A  1  880  ? -42.616 81.132  99.827  1.00 22.93 ? 878  ARG   A N     1 
ATOM   6431  C  CA    . ARG   A  1  880  ? -43.419 80.468  98.814  1.00 22.64 ? 878  ARG   A CA    1 
ATOM   6432  C  C     . ARG   A  1  880  ? -42.553 79.399  98.173  1.00 19.73 ? 878  ARG   A C     1 
ATOM   6433  O  O     . ARG   A  1  880  ? -41.420 79.681  97.775  1.00 20.94 ? 878  ARG   A O     1 
ATOM   6434  C  CB    . ARG   A  1  880  ? -43.873 81.442  97.723  1.00 25.88 ? 878  ARG   A CB    1 
ATOM   6435  C  CG    . ARG   A  1  880  ? -44.943 82.426  98.157  1.00 30.19 ? 878  ARG   A CG    1 
ATOM   6436  C  CD    . ARG   A  1  880  ? -45.310 83.357  97.005  1.00 32.95 ? 878  ARG   A CD    1 
ATOM   6437  N  NE    . ARG   A  1  880  ? -46.318 84.335  97.394  1.00 48.34 ? 878  ARG   A NE    1 
ATOM   6438  C  CZ    . ARG   A  1  880  ? -47.536 84.397  96.874  1.00 48.54 ? 878  ARG   A CZ    1 
ATOM   6439  N  NH1   . ARG   A  1  880  ? -47.922 83.566  95.919  1.00 49.01 ? 878  ARG   A NH1   1 
ATOM   6440  N  NH2   . ARG   A  1  880  ? -48.386 85.321  97.316  1.00 51.49 ? 878  ARG   A NH2   1 
ATOM   6441  N  N     . LEU   A  1  881  ? -43.091 78.179  98.077  1.00 19.61 ? 879  LEU   A N     1 
ATOM   6442  C  CA    . LEU   A  1  881  ? -42.371 77.080  97.438  1.00 17.77 ? 879  LEU   A CA    1 
ATOM   6443  C  C     . LEU   A  1  881  ? -41.966 77.414  96.008  1.00 18.36 ? 879  LEU   A C     1 
ATOM   6444  O  O     . LEU   A  1  881  ? -40.935 76.929  95.516  1.00 19.72 ? 879  LEU   A O     1 
ATOM   6445  C  CB    . LEU   A  1  881  ? -43.241 75.827  97.460  1.00 20.46 ? 879  LEU   A CB    1 
ATOM   6446  C  CG    . LEU   A  1  881  ? -42.592 74.546  96.949  1.00 23.01 ? 879  LEU   A CG    1 
ATOM   6447  C  CD1   . LEU   A  1  881  ? -41.422 74.137  97.851  1.00 25.11 ? 879  LEU   A CD1   1 
ATOM   6448  C  CD2   . LEU   A  1  881  ? -43.637 73.443  96.846  1.00 24.36 ? 879  LEU   A CD2   1 
ATOM   6449  N  N     . SER   A  1  882  ? -42.754 78.240  95.323  1.00 18.49 ? 880  SER   A N     1 
ATOM   6450  C  CA    . SER   A  1  882  ? -42.456 78.545  93.929  1.00 19.62 ? 880  SER   A CA    1 
ATOM   6451  C  C     . SER   A  1  882  ? -41.266 79.479  93.761  1.00 22.78 ? 880  SER   A C     1 
ATOM   6452  O  O     . SER   A  1  882  ? -40.841 79.709  92.623  1.00 21.85 ? 880  SER   A O     1 
ATOM   6453  C  CB    . SER   A  1  882  ? -43.688 79.173  93.281  1.00 20.57 ? 880  SER   A CB    1 
ATOM   6454  O  OG    . SER   A  1  882  ? -44.013 80.394  93.925  1.00 25.06 ? 880  SER   A OG    1 
ATOM   6455  N  N     . VAL   A  1  883  ? -40.708 80.012  94.844  1.00 20.88 ? 881  VAL   A N     1 
ATOM   6456  C  CA    . VAL   A  1  883  ? -39.598 80.951  94.723  1.00 20.90 ? 881  VAL   A CA    1 
ATOM   6457  C  C     . VAL   A  1  883  ? -38.293 80.180  94.593  1.00 20.30 ? 881  VAL   A C     1 
ATOM   6458  O  O     . VAL   A  1  883  ? -37.983 79.304  95.410  1.00 24.32 ? 881  VAL   A O     1 
ATOM   6459  C  CB    . VAL   A  1  883  ? -39.556 81.921  95.915  1.00 22.77 ? 881  VAL   A CB    1 
ATOM   6460  C  CG1   . VAL   A  1  883  ? -38.200 82.648  95.954  1.00 21.51 ? 881  VAL   A CG1   1 
ATOM   6461  C  CG2   . VAL   A  1  883  ? -40.691 82.919  95.803  1.00 24.57 ? 881  VAL   A CG2   1 
ATOM   6462  N  N     . ASP   A  1  884  ? -37.521 80.508  93.563  1.00 19.30 ? 882  ASP   A N     1 
ATOM   6463  C  CA    . ASP   A  1  884  ? -36.246 79.842  93.346  1.00 19.83 ? 882  ASP   A CA    1 
ATOM   6464  C  C     . ASP   A  1  884  ? -35.099 80.586  93.990  1.00 24.34 ? 882  ASP   A C     1 
ATOM   6465  O  O     . ASP   A  1  884  ? -34.181 79.960  94.531  1.00 26.83 ? 882  ASP   A O     1 
ATOM   6466  C  CB    . ASP   A  1  884  ? -35.971 79.732  91.853  1.00 21.57 ? 882  ASP   A CB    1 
ATOM   6467  C  CG    . ASP   A  1  884  ? -37.043 78.963  91.151  1.00 18.71 ? 882  ASP   A CG    1 
ATOM   6468  O  OD1   . ASP   A  1  884  ? -37.235 77.790  91.523  1.00 23.11 ? 882  ASP   A OD1   1 
ATOM   6469  O  OD2   . ASP   A  1  884  ? -37.702 79.541  90.271  1.00 20.70 ? 882  ASP   A OD2   1 
ATOM   6470  N  N     . VAL   A  1  885  ? -35.133 81.912  93.922  1.00 19.75 ? 883  VAL   A N     1 
ATOM   6471  C  CA    . VAL   A  1  885  ? -34.009 82.745  94.317  1.00 21.58 ? 883  VAL   A CA    1 
ATOM   6472  C  C     . VAL   A  1  885  ? -34.560 83.800  95.254  1.00 20.66 ? 883  VAL   A C     1 
ATOM   6473  O  O     . VAL   A  1  885  ? -35.497 84.524  94.895  1.00 20.81 ? 883  VAL   A O     1 
ATOM   6474  C  CB    . VAL   A  1  885  ? -33.329 83.406  93.105  1.00 23.82 ? 883  VAL   A CB    1 
ATOM   6475  C  CG1   . VAL   A  1  885  ? -32.172 84.278  93.564  1.00 23.22 ? 883  VAL   A CG1   1 
ATOM   6476  C  CG2   . VAL   A  1  885  ? -32.823 82.361  92.116  1.00 23.72 ? 883  VAL   A CG2   1 
ATOM   6477  N  N     . GLY   A  1  886  ? -34.002 83.869  96.456  1.00 21.11 ? 884  GLY   A N     1 
ATOM   6478  C  CA    . GLY   A  1  886  ? -34.443 84.834  97.424  1.00 19.48 ? 884  GLY   A CA    1 
ATOM   6479  C  C     . GLY   A  1  886  ? -33.624 86.101  97.378  1.00 21.63 ? 884  GLY   A C     1 
ATOM   6480  O  O     . GLY   A  1  886  ? -32.893 86.378  96.418  1.00 20.49 ? 884  GLY   A O     1 
ATOM   6481  N  N     . PRO   A  1  887  ? -33.743 86.896  98.431  1.00 21.00 ? 885  PRO   A N     1 
ATOM   6482  C  CA    . PRO   A  1  887  ? -33.081 88.200  98.469  1.00 20.31 ? 885  PRO   A CA    1 
ATOM   6483  C  C     . PRO   A  1  887  ? -31.606 88.058  98.811  1.00 19.85 ? 885  PRO   A C     1 
ATOM   6484  O  O     . PRO   A  1  887  ? -31.129 87.013  99.255  1.00 20.73 ? 885  PRO   A O     1 
ATOM   6485  C  CB    . PRO   A  1  887  ? -33.813 88.902  99.614  1.00 21.06 ? 885  PRO   A CB    1 
ATOM   6486  C  CG    . PRO   A  1  887  ? -34.155 87.775  100.562 1.00 22.60 ? 885  PRO   A CG    1 
ATOM   6487  C  CD    . PRO   A  1  887  ? -34.513 86.618  99.657  1.00 23.25 ? 885  PRO   A CD    1 
ATOM   6488  N  N     . VAL   A  1  888  ? -30.887 89.154  98.609  1.00 19.65 ? 886  VAL   A N     1 
ATOM   6489  C  CA    . VAL   A  1  888  ? -29.592 89.291  99.249  1.00 18.37 ? 886  VAL   A CA    1 
ATOM   6490  C  C     . VAL   A  1  888  ? -29.789 89.814  100.669 1.00 21.25 ? 886  VAL   A C     1 
ATOM   6491  O  O     . VAL   A  1  888  ? -30.811 90.409  101.003 1.00 22.65 ? 886  VAL   A O     1 
ATOM   6492  C  CB    . VAL   A  1  888  ? -28.621 90.155  98.428  1.00 22.61 ? 886  VAL   A CB    1 
ATOM   6493  C  CG1   . VAL   A  1  888  ? -28.417 89.530  97.047  1.00 23.91 ? 886  VAL   A CG1   1 
ATOM   6494  C  CG2   . VAL   A  1  888  ? -29.125 91.559  98.296  1.00 23.48 ? 886  VAL   A CG2   1 
ATOM   6495  N  N     . ILE   A  1  889  ? -28.796 89.564  101.524 1.00 21.63 ? 887  ILE   A N     1 
ATOM   6496  C  CA    . ILE   A  1  889  ? -29.031 89.630  102.967 1.00 23.28 ? 887  ILE   A CA    1 
ATOM   6497  C  C     . ILE   A  1  889  ? -29.320 91.054  103.441 1.00 25.28 ? 887  ILE   A C     1 
ATOM   6498  O  O     . ILE   A  1  889  ? -30.128 91.259  104.357 1.00 23.83 ? 887  ILE   A O     1 
ATOM   6499  C  CB    . ILE   A  1  889  ? -27.878 88.957  103.739 1.00 22.18 ? 887  ILE   A CB    1 
ATOM   6500  C  CG1   . ILE   A  1  889  ? -28.231 88.840  105.226 1.00 24.00 ? 887  ILE   A CG1   1 
ATOM   6501  C  CG2   . ILE   A  1  889  ? -26.560 89.712  103.534 1.00 22.78 ? 887  ILE   A CG2   1 
ATOM   6502  C  CD1   . ILE   A  1  889  ? -29.479 88.028  105.493 1.00 21.86 ? 887  ILE   A CD1   1 
ATOM   6503  N  N     . THR   A  1  890  ? -28.670 92.054  102.850 1.00 20.79 ? 888  THR   A N     1 
ATOM   6504  C  CA    . THR   A  1  890  ? -28.823 93.426  103.318 1.00 21.51 ? 888  THR   A CA    1 
ATOM   6505  C  C     . THR   A  1  890  ? -28.739 94.387  102.147 1.00 21.78 ? 888  THR   A C     1 
ATOM   6506  O  O     . THR   A  1  890  ? -28.261 94.048  101.059 1.00 22.86 ? 888  THR   A O     1 
ATOM   6507  C  CB    . THR   A  1  890  ? -27.702 93.842  104.283 1.00 25.77 ? 888  THR   A CB    1 
ATOM   6508  O  OG1   . THR   A  1  890  ? -26.447 93.769  103.598 1.00 26.02 ? 888  THR   A OG1   1 
ATOM   6509  C  CG2   . THR   A  1  890  ? -27.661 92.969  105.533 1.00 26.26 ? 888  THR   A CG2   1 
ATOM   6510  N  N     . SER   A  1  891  ? -29.150 95.628  102.419 1.00 24.06 ? 889  SER   A N     1 
ATOM   6511  C  CA    A SER   A  1  891  ? -29.041 96.696  101.428 0.45 26.77 ? 889  SER   A CA    1 
ATOM   6512  C  CA    B SER   A  1  891  ? -29.043 96.672  101.407 0.55 26.76 ? 889  SER   A CA    1 
ATOM   6513  C  C     . SER   A  1  891  ? -27.590 96.954  101.049 1.00 25.71 ? 889  SER   A C     1 
ATOM   6514  O  O     . SER   A  1  891  ? -27.295 97.297  99.900  1.00 27.91 ? 889  SER   A O     1 
ATOM   6515  C  CB    A SER   A  1  891  ? -29.659 97.983  101.978 0.45 28.49 ? 889  SER   A CB    1 
ATOM   6516  C  CB    B SER   A  1  891  ? -29.731 97.946  101.895 0.55 28.50 ? 889  SER   A CB    1 
ATOM   6517  O  OG    A SER   A  1  891  ? -31.058 97.865  102.132 0.45 27.55 ? 889  SER   A OG    1 
ATOM   6518  O  OG    B SER   A  1  891  ? -29.156 98.391  103.107 0.55 30.81 ? 889  SER   A OG    1 
ATOM   6519  N  N     . GLU   A  1  892  ? -26.674 96.820  102.013 1.00 25.27 ? 890  GLU   A N     1 
ATOM   6520  C  CA    . GLU   A  1  892  ? -25.261 97.057  101.722 1.00 26.82 ? 890  GLU   A CA    1 
ATOM   6521  C  C     . GLU   A  1  892  ? -24.706 95.972  100.816 1.00 27.27 ? 890  GLU   A C     1 
ATOM   6522  O  O     . GLU   A  1  892  ? -23.905 96.252  99.916  1.00 28.50 ? 890  GLU   A O     1 
ATOM   6523  C  CB    . GLU   A  1  892  ? -24.446 97.141  103.011 1.00 28.70 ? 890  GLU   A CB    1 
ATOM   6524  C  CG    . GLU   A  1  892  ? -25.044 98.061  104.058 1.00 38.28 ? 890  GLU   A CG    1 
ATOM   6525  C  CD    . GLU   A  1  892  ? -25.886 97.295  105.061 1.00 42.61 ? 890  GLU   A CD    1 
ATOM   6526  O  OE1   . GLU   A  1  892  ? -25.295 96.627  105.940 1.00 51.88 ? 890  GLU   A OE1   1 
ATOM   6527  O  OE2   . GLU   A  1  892  ? -27.129 97.337  104.955 1.00 37.23 ? 890  GLU   A OE2   1 
ATOM   6528  N  N     . ALA   A  1  893  ? -25.111 94.723  101.046 1.00 25.92 ? 891  ALA   A N     1 
ATOM   6529  C  CA    . ALA   A  1  893  ? -24.713 93.657  100.136 1.00 26.78 ? 891  ALA   A CA    1 
ATOM   6530  C  C     . ALA   A  1  893  ? -25.258 93.916  98.739  1.00 26.35 ? 891  ALA   A C     1 
ATOM   6531  O  O     . ALA   A  1  893  ? -24.523 93.830  97.749  1.00 26.31 ? 891  ALA   A O     1 
ATOM   6532  C  CB    . ALA   A  1  893  ? -25.169 92.303  100.677 1.00 21.84 ? 891  ALA   A CB    1 
ATOM   6533  N  N     . LYS   A  1  894  ? -26.545 94.266  98.648  1.00 24.31 ? 892  LYS   A N     1 
ATOM   6534  C  CA    . LYS   A  1  894  ? -27.141 94.642  97.371  1.00 27.79 ? 892  LYS   A CA    1 
ATOM   6535  C  C     . LYS   A  1  894  ? -26.362 95.766  96.699  1.00 29.04 ? 892  LYS   A C     1 
ATOM   6536  O  O     . LYS   A  1  894  ? -26.048 95.695  95.507  1.00 28.24 ? 892  LYS   A O     1 
ATOM   6537  C  CB    . LYS   A  1  894  ? -28.596 95.061  97.586  1.00 23.46 ? 892  LYS   A CB    1 
ATOM   6538  C  CG    . LYS   A  1  894  ? -29.298 95.537  96.321  1.00 26.69 ? 892  LYS   A CG    1 
ATOM   6539  C  CD    . LYS   A  1  894  ? -30.752 95.892  96.599  1.00 29.10 ? 892  LYS   A CD    1 
ATOM   6540  C  CE    . LYS   A  1  894  ? -31.435 96.460  95.361  1.00 31.81 ? 892  LYS   A CE    1 
ATOM   6541  N  NZ    . LYS   A  1  894  ? -32.802 96.959  95.659  1.00 42.79 ? 892  LYS   A NZ    1 
ATOM   6542  N  N     . ASP   A  1  895  ? -26.040 96.818  97.456  1.00 27.35 ? 893  ASP   A N     1 
ATOM   6543  C  CA    . ASP   A  1  895  ? -25.287 97.930  96.887  1.00 32.07 ? 893  ASP   A CA    1 
ATOM   6544  C  C     . ASP   A  1  895  ? -23.931 97.474  96.372  1.00 27.94 ? 893  ASP   A C     1 
ATOM   6545  O  O     . ASP   A  1  895  ? -23.492 97.897  95.297  1.00 30.76 ? 893  ASP   A O     1 
ATOM   6546  C  CB    . ASP   A  1  895  ? -25.096 99.029  97.932  1.00 30.09 ? 893  ASP   A CB    1 
ATOM   6547  C  CG    . ASP   A  1  895  ? -26.368 99.807  98.209  1.00 39.22 ? 893  ASP   A CG    1 
ATOM   6548  O  OD1   . ASP   A  1  895  ? -27.314 99.734  97.390  1.00 47.51 ? 893  ASP   A OD1   1 
ATOM   6549  O  OD2   . ASP   A  1  895  ? -26.417 100.507 99.246  1.00 40.70 ? 893  ASP   A OD2   1 
ATOM   6550  N  N     . ASN   A  1  896  ? -23.240 96.630  97.139  1.00 26.92 ? 894  ASN   A N     1 
ATOM   6551  C  CA    . ASN   A  1  896  ? -21.924 96.166  96.720  1.00 29.78 ? 894  ASN   A CA    1 
ATOM   6552  C  C     . ASN   A  1  896  ? -22.019 95.338  95.447  1.00 28.93 ? 894  ASN   A C     1 
ATOM   6553  O  O     . ASN   A  1  896  ? -21.210 95.502  94.525  1.00 27.46 ? 894  ASN   A O     1 
ATOM   6554  C  CB    . ASN   A  1  896  ? -21.279 95.353  97.842  1.00 30.49 ? 894  ASN   A CB    1 
ATOM   6555  C  CG    . ASN   A  1  896  ? -19.987 94.693  97.412  1.00 38.22 ? 894  ASN   A CG    1 
ATOM   6556  O  OD1   . ASN   A  1  896  ? -19.964 93.510  97.052  1.00 39.46 ? 894  ASN   A OD1   1 
ATOM   6557  N  ND2   . ASN   A  1  896  ? -18.902 95.455  97.439  1.00 39.19 ? 894  ASN   A ND2   1 
ATOM   6558  N  N     . ILE   A  1  897  ? -23.006 94.446  95.375  1.00 26.57 ? 895  ILE   A N     1 
ATOM   6559  C  CA    . ILE   A  1  897  ? -23.170 93.620  94.184  1.00 25.47 ? 895  ILE   A CA    1 
ATOM   6560  C  C     . ILE   A  1  897  ? -23.523 94.488  92.984  1.00 29.03 ? 895  ILE   A C     1 
ATOM   6561  O  O     . ILE   A  1  897  ? -22.968 94.329  91.891  1.00 27.34 ? 895  ILE   A O     1 
ATOM   6562  C  CB    . ILE   A  1  897  ? -24.232 92.538  94.430  1.00 23.04 ? 895  ILE   A CB    1 
ATOM   6563  C  CG1   . ILE   A  1  897  ? -23.802 91.609  95.566  1.00 23.32 ? 895  ILE   A CG1   1 
ATOM   6564  C  CG2   . ILE   A  1  897  ? -24.475 91.747  93.154  1.00 24.93 ? 895  ILE   A CG2   1 
ATOM   6565  C  CD1   . ILE   A  1  897  ? -24.994 90.907  96.237  1.00 22.23 ? 895  ILE   A CD1   1 
ATOM   6566  N  N     . GLU   A  1  898  ? -24.456 95.422  93.165  1.00 26.96 ? 896  GLU   A N     1 
ATOM   6567  C  CA    . GLU   A  1  898  ? -24.884 96.227  92.029  1.00 28.76 ? 896  GLU   A CA    1 
ATOM   6568  C  C     . GLU   A  1  898  ? -23.773 97.145  91.538  1.00 27.48 ? 896  GLU   A C     1 
ATOM   6569  O  O     . GLU   A  1  898  ? -23.679 97.410  90.335  1.00 30.98 ? 896  GLU   A O     1 
ATOM   6570  C  CB    . GLU   A  1  898  ? -26.171 96.979  92.366  1.00 30.51 ? 896  GLU   A CB    1 
ATOM   6571  C  CG    . GLU   A  1  898  ? -27.337 96.023  92.582  1.00 33.01 ? 896  GLU   A CG    1 
ATOM   6572  C  CD    . GLU   A  1  898  ? -28.644 96.714  92.922  1.00 37.29 ? 896  GLU   A CD    1 
ATOM   6573  O  OE1   . GLU   A  1  898  ? -28.616 97.819  93.504  1.00 40.74 ? 896  GLU   A OE1   1 
ATOM   6574  O  OE2   . GLU   A  1  898  ? -29.705 96.134  92.608  1.00 47.27 ? 896  GLU   A OE2   1 
ATOM   6575  N  N     . LYS   A  1  899  ? -22.919 97.626  92.445  1.00 28.92 ? 897  LYS   A N     1 
ATOM   6576  C  CA    . LYS   A  1  899  ? -21.770 98.417  92.021  1.00 29.55 ? 897  LYS   A CA    1 
ATOM   6577  C  C     . LYS   A  1  899  ? -20.849 97.596  91.129  1.00 31.09 ? 897  LYS   A C     1 
ATOM   6578  O  O     . LYS   A  1  899  ? -20.281 98.117  90.162  1.00 30.93 ? 897  LYS   A O     1 
ATOM   6579  C  CB    . LYS   A  1  899  ? -21.008 98.938  93.241  1.00 33.06 ? 897  LYS   A CB    1 
ATOM   6580  N  N     . HIS   A  1  900  ? -20.692 96.307  91.436  1.00 25.30 ? 898  HIS   A N     1 
ATOM   6581  C  CA    . HIS   A  1  900  ? -19.883 95.451  90.578  1.00 28.80 ? 898  HIS   A CA    1 
ATOM   6582  C  C     . HIS   A  1  900  ? -20.542 95.258  89.218  1.00 25.73 ? 898  HIS   A C     1 
ATOM   6583  O  O     . HIS   A  1  900  ? -19.882 95.354  88.179  1.00 31.41 ? 898  HIS   A O     1 
ATOM   6584  C  CB    . HIS   A  1  900  ? -19.652 94.102  91.249  1.00 26.06 ? 898  HIS   A CB    1 
ATOM   6585  C  CG    . HIS   A  1  900  ? -19.052 93.087  90.334  1.00 26.70 ? 898  HIS   A CG    1 
ATOM   6586  N  ND1   . HIS   A  1  900  ? -17.722 93.107  89.975  1.00 27.37 ? 898  HIS   A ND1   1 
ATOM   6587  C  CD2   . HIS   A  1  900  ? -19.609 92.048  89.668  1.00 27.45 ? 898  HIS   A CD2   1 
ATOM   6588  C  CE1   . HIS   A  1  900  ? -17.478 92.100  89.153  1.00 27.40 ? 898  HIS   A CE1   1 
ATOM   6589  N  NE2   . HIS   A  1  900  ? -18.607 91.447  88.946  1.00 25.28 ? 898  HIS   A NE2   1 
ATOM   6590  N  N     . ILE   A  1  901  ? -21.843 94.970  89.210  1.00 25.06 ? 899  ILE   A N     1 
ATOM   6591  C  CA    . ILE   A  1  901  ? -22.563 94.798  87.953  1.00 28.64 ? 899  ILE   A CA    1 
ATOM   6592  C  C     . ILE   A  1  901  ? -22.429 96.041  87.090  1.00 31.65 ? 899  ILE   A C     1 
ATOM   6593  O  O     . ILE   A  1  901  ? -22.205 95.951  85.877  1.00 32.55 ? 899  ILE   A O     1 
ATOM   6594  C  CB    . ILE   A  1  901  ? -24.035 94.455  88.230  1.00 26.42 ? 899  ILE   A CB    1 
ATOM   6595  C  CG1   . ILE   A  1  901  ? -24.137 93.102  88.941  1.00 26.46 ? 899  ILE   A CG1   1 
ATOM   6596  C  CG2   . ILE   A  1  901  ? -24.842 94.469  86.937  1.00 30.29 ? 899  ILE   A CG2   1 
ATOM   6597  C  CD1   . ILE   A  1  901  ? -25.543 92.769  89.417  1.00 26.64 ? 899  ILE   A CD1   1 
ATOM   6598  N  N     . GLU   A  1  902  ? -22.548 97.220  87.701  1.00 31.57 ? 900  GLU   A N     1 
ATOM   6599  C  CA    . GLU   A  1  902  ? -22.506 98.451  86.918  1.00 34.07 ? 900  GLU   A CA    1 
ATOM   6600  C  C     . GLU   A  1  902  ? -21.109 98.732  86.384  1.00 32.52 ? 900  GLU   A C     1 
ATOM   6601  O  O     . GLU   A  1  902  ? -20.963 99.213  85.254  1.00 37.42 ? 900  GLU   A O     1 
ATOM   6602  C  CB    . GLU   A  1  902  ? -23.045 99.624  87.734  1.00 36.61 ? 900  GLU   A CB    1 
ATOM   6603  C  CG    . GLU   A  1  902  ? -24.549 99.588  87.847  1.00 40.34 ? 900  GLU   A CG    1 
ATOM   6604  C  CD    . GLU   A  1  902  ? -25.204 99.337  86.504  1.00 43.97 ? 900  GLU   A CD    1 
ATOM   6605  O  OE1   . GLU   A  1  902  ? -25.014 100.165 85.587  1.00 48.25 ? 900  GLU   A OE1   1 
ATOM   6606  O  OE2   . GLU   A  1  902  ? -25.890 98.300  86.362  1.00 46.43 ? 900  GLU   A OE2   1 
ATOM   6607  N  N     . ARG   A  1  903  ? -20.074 98.455  87.179  1.00 33.17 ? 901  ARG   A N     1 
ATOM   6608  C  CA    . ARG   A  1  903  ? -18.707 98.550  86.676  1.00 36.16 ? 901  ARG   A CA    1 
ATOM   6609  C  C     . ARG   A  1  903  ? -18.525 97.678  85.439  1.00 40.65 ? 901  ARG   A C     1 
ATOM   6610  O  O     . ARG   A  1  903  ? -18.012 98.137  84.412  1.00 38.95 ? 901  ARG   A O     1 
ATOM   6611  C  CB    . ARG   A  1  903  ? -17.716 98.150  87.768  1.00 38.63 ? 901  ARG   A CB    1 
ATOM   6612  N  N     . MET   A  1  904  ? -18.959 96.417  85.517  1.00 36.96 ? 902  MET   A N     1 
ATOM   6613  C  CA    . MET   A  1  904  ? -18.868 95.519  84.368  1.00 36.86 ? 902  MET   A CA    1 
ATOM   6614  C  C     . MET   A  1  904  ? -19.664 96.056  83.188  1.00 35.92 ? 902  MET   A C     1 
ATOM   6615  O  O     . MET   A  1  904  ? -19.182 96.065  82.050  1.00 37.35 ? 902  MET   A O     1 
ATOM   6616  C  CB    . MET   A  1  904  ? -19.376 94.125  84.745  1.00 31.81 ? 902  MET   A CB    1 
ATOM   6617  C  CG    . MET   A  1  904  ? -18.582 93.425  85.819  1.00 31.62 ? 902  MET   A CG    1 
ATOM   6618  S  SD    . MET   A  1  904  ? -16.875 93.126  85.331  1.00 44.18 ? 902  MET   A SD    1 
ATOM   6619  C  CE    . MET   A  1  904  ? -16.021 94.444  86.200  1.00 42.67 ? 902  MET   A CE    1 
ATOM   6620  N  N     . ARG   A  1  905  ? -20.900 96.492  83.439  1.00 34.37 ? 903  ARG   A N     1 
ATOM   6621  C  CA    . ARG   A  1  905  ? -21.707 97.043  82.360  1.00 34.29 ? 903  ARG   A CA    1 
ATOM   6622  C  C     . ARG   A  1  905  ? -21.054 98.291  81.787  1.00 42.20 ? 903  ARG   A C     1 
ATOM   6623  O  O     . ARG   A  1  905  ? -21.086 98.516  80.573  1.00 37.53 ? 903  ARG   A O     1 
ATOM   6624  C  CB    . ARG   A  1  905  ? -23.114 97.357  82.859  1.00 37.52 ? 903  ARG   A CB    1 
ATOM   6625  C  CG    . ARG   A  1  905  ? -24.120 97.561  81.744  1.00 40.64 ? 903  ARG   A CG    1 
ATOM   6626  C  CD    . ARG   A  1  905  ? -25.401 98.170  82.262  1.00 39.66 ? 903  ARG   A CD    1 
ATOM   6627  N  NE    . ARG   A  1  905  ? -25.947 97.438  83.398  1.00 38.84 ? 903  ARG   A NE    1 
ATOM   6628  C  CZ    . ARG   A  1  905  ? -26.800 96.430  83.296  1.00 40.08 ? 903  ARG   A CZ    1 
ATOM   6629  N  NH1   . ARG   A  1  905  ? -27.186 95.965  82.117  1.00 37.14 ? 903  ARG   A NH1   1 
ATOM   6630  N  NH2   . ARG   A  1  905  ? -27.283 95.876  84.404  1.00 39.77 ? 903  ARG   A NH2   1 
ATOM   6631  N  N     . GLY   A  1  906  ? -20.435 99.101  82.650  1.00 37.96 ? 904  GLY   A N     1 
ATOM   6632  C  CA    . GLY   A  1  906  ? -19.773 100.313 82.205  1.00 44.49 ? 904  GLY   A CA    1 
ATOM   6633  C  C     . GLY   A  1  906  ? -18.524 100.068 81.388  1.00 45.26 ? 904  GLY   A C     1 
ATOM   6634  O  O     . GLY   A  1  906  ? -18.040 100.991 80.725  1.00 49.50 ? 904  GLY   A O     1 
ATOM   6635  N  N     . LEU   A  1  907  ? -17.990 98.851  81.421  1.00 43.11 ? 905  LEU   A N     1 
ATOM   6636  C  CA    . LEU   A  1  907  ? -16.844 98.483  80.602  1.00 41.98 ? 905  LEU   A CA    1 
ATOM   6637  C  C     . LEU   A  1  907  ? -17.245 97.882  79.262  1.00 42.13 ? 905  LEU   A C     1 
ATOM   6638  O  O     . LEU   A  1  907  ? -16.366 97.514  78.478  1.00 44.88 ? 905  LEU   A O     1 
ATOM   6639  C  CB    . LEU   A  1  907  ? -15.940 97.507  81.360  1.00 43.63 ? 905  LEU   A CB    1 
ATOM   6640  C  CG    . LEU   A  1  907  ? -15.343 98.078  82.645  1.00 48.19 ? 905  LEU   A CG    1 
ATOM   6641  C  CD1   . LEU   A  1  907  ? -14.436 97.064  83.319  1.00 50.69 ? 905  LEU   A CD1   1 
ATOM   6642  C  CD2   . LEU   A  1  907  ? -14.599 99.372  82.349  1.00 50.24 ? 905  LEU   A CD2   1 
ATOM   6643  N  N     . GLY   A  1  908  ? -18.542 97.771  78.986  1.00 40.07 ? 906  GLY   A N     1 
ATOM   6644  C  CA    . GLY   A  1  908  ? -19.017 97.212  77.742  1.00 42.00 ? 906  GLY   A CA    1 
ATOM   6645  C  C     . GLY   A  1  908  ? -19.340 95.736  77.782  1.00 33.18 ? 906  GLY   A C     1 
ATOM   6646  O  O     . GLY   A  1  908  ? -19.746 95.181  76.754  1.00 37.29 ? 906  GLY   A O     1 
ATOM   6647  N  N     . ARG   A  1  909  ? -19.191 95.085  78.930  1.00 35.14 ? 907  ARG   A N     1 
ATOM   6648  C  CA    . ARG   A  1  909  ? -19.466 93.659  79.013  1.00 31.09 ? 907  ARG   A CA    1 
ATOM   6649  C  C     . ARG   A  1  909  ? -20.962 93.405  78.880  1.00 32.43 ? 907  ARG   A C     1 
ATOM   6650  O  O     . ARG   A  1  909  ? -21.790 94.179  79.375  1.00 34.08 ? 907  ARG   A O     1 
ATOM   6651  C  CB    . ARG   A  1  909  ? -18.959 93.108  80.344  1.00 32.80 ? 907  ARG   A CB    1 
ATOM   6652  C  CG    . ARG   A  1  909  ? -17.521 93.477  80.675  1.00 33.40 ? 907  ARG   A CG    1 
ATOM   6653  C  CD    . ARG   A  1  909  ? -16.532 92.813  79.730  1.00 37.19 ? 907  ARG   A CD    1 
ATOM   6654  N  NE    . ARG   A  1  909  ? -15.161 92.898  80.226  1.00 38.77 ? 907  ARG   A NE    1 
ATOM   6655  C  CZ    . ARG   A  1  909  ? -14.268 93.793  79.825  1.00 49.55 ? 907  ARG   A CZ    1 
ATOM   6656  N  NH1   . ARG   A  1  909  ? -14.564 94.708  78.915  1.00 46.80 ? 907  ARG   A NH1   1 
ATOM   6657  N  NH2   . ARG   A  1  909  ? -13.044 93.770  80.351  1.00 45.75 ? 907  ARG   A NH2   1 
ATOM   6658  N  N     . LYS   A  1  910  ? -21.308 92.315  78.198  1.00 26.85 ? 908  LYS   A N     1 
ATOM   6659  C  CA    . LYS   A  1  910  ? -22.707 91.957  78.021  1.00 28.62 ? 908  LYS   A CA    1 
ATOM   6660  C  C     . LYS   A  1  910  ? -23.286 91.457  79.336  1.00 30.63 ? 908  LYS   A C     1 
ATOM   6661  O  O     . LYS   A  1  910  ? -22.729 90.557  79.972  1.00 27.14 ? 908  LYS   A O     1 
ATOM   6662  C  CB    . LYS   A  1  910  ? -22.846 90.883  76.945  1.00 33.36 ? 908  LYS   A CB    1 
ATOM   6663  C  CG    . LYS   A  1  910  ? -22.733 91.418  75.525  1.00 35.54 ? 908  LYS   A CG    1 
ATOM   6664  C  CD    . LYS   A  1  910  ? -23.069 90.342  74.501  1.00 40.54 ? 908  LYS   A CD    1 
ATOM   6665  C  CE    . LYS   A  1  910  ? -24.432 89.727  74.762  1.00 39.03 ? 908  LYS   A CE    1 
ATOM   6666  N  NZ    . LYS   A  1  910  ? -24.849 88.858  73.624  1.00 46.57 ? 908  LYS   A NZ    1 
ATOM   6667  N  N     . VAL   A  1  911  ? -24.418 92.032  79.735  1.00 27.91 ? 909  VAL   A N     1 
ATOM   6668  C  CA    . VAL   A  1  911  ? -25.033 91.756  81.026  1.00 26.04 ? 909  VAL   A CA    1 
ATOM   6669  C  C     . VAL   A  1  911  ? -26.471 91.324  80.782  1.00 27.34 ? 909  VAL   A C     1 
ATOM   6670  O  O     . VAL   A  1  911  ? -27.258 92.076  80.194  1.00 29.07 ? 909  VAL   A O     1 
ATOM   6671  C  CB    . VAL   A  1  911  ? -24.984 92.982  81.954  1.00 29.29 ? 909  VAL   A CB    1 
ATOM   6672  C  CG1   . VAL   A  1  911  ? -25.763 92.711  83.235  1.00 31.17 ? 909  VAL   A CG1   1 
ATOM   6673  C  CG2   . VAL   A  1  911  ? -23.539 93.369  82.268  1.00 30.10 ? 909  VAL   A CG2   1 
ATOM   6674  N  N     . GLU   A  1  912  ? -26.803 90.114  81.217  1.00 26.57 ? 910  GLU   A N     1 
ATOM   6675  C  CA    . GLU   A  1  912  ? -28.147 89.563  81.143  1.00 26.68 ? 910  GLU   A CA    1 
ATOM   6676  C  C     . GLU   A  1  912  ? -28.704 89.495  82.559  1.00 28.45 ? 910  GLU   A C     1 
ATOM   6677  O  O     . GLU   A  1  912  ? -28.043 88.968  83.461  1.00 25.55 ? 910  GLU   A O     1 
ATOM   6678  C  CB    . GLU   A  1  912  ? -28.095 88.148  80.558  1.00 27.19 ? 910  GLU   A CB    1 
ATOM   6679  C  CG    . GLU   A  1  912  ? -29.460 87.527  80.291  1.00 28.64 ? 910  GLU   A CG    1 
ATOM   6680  C  CD    . GLU   A  1  912  ? -30.087 88.052  79.015  1.00 33.22 ? 910  GLU   A CD    1 
ATOM   6681  O  OE1   . GLU   A  1  912  ? -29.359 88.660  78.207  1.00 32.31 ? 910  GLU   A OE1   1 
ATOM   6682  O  OE2   . GLU   A  1  912  ? -31.307 87.859  78.815  1.00 31.05 ? 910  GLU   A OE2   1 
ATOM   6683  N  N     . GLN   A  1  913  ? -29.904 90.044  82.761  1.00 27.24 ? 911  GLN   A N     1 
ATOM   6684  C  CA    . GLN   A  1  913  ? -30.524 90.044  84.079  1.00 24.44 ? 911  GLN   A CA    1 
ATOM   6685  C  C     . GLN   A  1  913  ? -31.998 89.703  83.961  1.00 30.67 ? 911  GLN   A C     1 
ATOM   6686  O  O     . GLN   A  1  913  ? -32.675 90.159  83.035  1.00 30.67 ? 911  GLN   A O     1 
ATOM   6687  C  CB    . GLN   A  1  913  ? -30.397 91.418  84.759  1.00 26.65 ? 911  GLN   A CB    1 
ATOM   6688  C  CG    . GLN   A  1  913  ? -28.979 91.811  85.093  1.00 27.39 ? 911  GLN   A CG    1 
ATOM   6689  C  CD    . GLN   A  1  913  ? -28.910 93.063  85.947  1.00 30.62 ? 911  GLN   A CD    1 
ATOM   6690  O  OE1   . GLN   A  1  913  ? -29.390 94.125  85.551  1.00 34.59 ? 911  GLN   A OE1   1 
ATOM   6691  N  NE2   . GLN   A  1  913  ? -28.321 92.942  87.126  1.00 28.15 ? 911  GLN   A NE2   1 
ATOM   6692  N  N     . ILE   A  1  914  ? -32.489 88.905  84.911  1.00 28.86 ? 912  ILE   A N     1 
ATOM   6693  C  CA    . ILE   A  1  914  ? -33.917 88.635  84.994  1.00 27.61 ? 912  ILE   A CA    1 
ATOM   6694  C  C     . ILE   A  1  914  ? -34.639 89.884  85.481  1.00 30.59 ? 912  ILE   A C     1 
ATOM   6695  O  O     . ILE   A  1  914  ? -34.105 90.681  86.268  1.00 29.76 ? 912  ILE   A O     1 
ATOM   6696  C  CB    . ILE   A  1  914  ? -34.173 87.435  85.926  1.00 35.10 ? 912  ILE   A CB    1 
ATOM   6697  N  N     . GLY   A  1  915  ? -35.858 90.081  84.986  1.00 30.98 ? 913  GLY   A N     1 
ATOM   6698  C  CA    . GLY   A  1  915  ? -36.676 91.183  85.462  1.00 33.38 ? 913  GLY   A CA    1 
ATOM   6699  C  C     . GLY   A  1  915  ? -37.303 90.817  86.790  1.00 33.31 ? 913  GLY   A C     1 
ATOM   6700  O  O     . GLY   A  1  915  ? -37.841 89.717  86.953  1.00 36.45 ? 913  GLY   A O     1 
ATOM   6701  N  N     . LEU   A  1  916  ? -37.225 91.733  87.749  1.00 30.25 ? 914  LEU   A N     1 
ATOM   6702  C  CA    . LEU   A  1  916  ? -37.743 91.494  89.088  1.00 33.29 ? 914  LEU   A CA    1 
ATOM   6703  C  C     . LEU   A  1  916  ? -39.177 91.984  89.201  1.00 35.68 ? 914  LEU   A C     1 
ATOM   6704  O  O     . LEU   A  1  916  ? -39.545 93.014  88.627  1.00 35.44 ? 914  LEU   A O     1 
ATOM   6705  C  CB    . LEU   A  1  916  ? -36.887 92.216  90.126  1.00 32.64 ? 914  LEU   A CB    1 
ATOM   6706  C  CG    . LEU   A  1  916  ? -35.447 91.717  90.226  1.00 31.74 ? 914  LEU   A CG    1 
ATOM   6707  C  CD1   . LEU   A  1  916  ? -34.755 92.381  91.398  1.00 33.80 ? 914  LEU   A CD1   1 
ATOM   6708  C  CD2   . LEU   A  1  916  ? -35.429 90.205  90.359  1.00 34.80 ? 914  LEU   A CD2   1 
ATOM   6709  N  N     . ALA   A  1  917  ? -39.983 91.240  89.951  1.00 30.79 ? 915  ALA   A N     1 
ATOM   6710  C  CA    . ALA   A  1  917  ? -41.355 91.654  90.202  1.00 33.96 ? 915  ALA   A CA    1 
ATOM   6711  C  C     . ALA   A  1  917  ? -41.366 92.867  91.121  1.00 33.32 ? 915  ALA   A C     1 
ATOM   6712  O  O     . ALA   A  1  917  ? -40.443 93.082  91.913  1.00 33.73 ? 915  ALA   A O     1 
ATOM   6713  C  CB    . ALA   A  1  917  ? -42.138 90.514  90.851  1.00 35.09 ? 915  ALA   A CB    1 
ATOM   6714  N  N     . SER   A  1  918  ? -42.431 93.669  91.013  1.00 34.09 ? 916  SER   A N     1 
ATOM   6715  C  CA    . SER   A  1  918  ? -42.536 94.864  91.845  1.00 35.57 ? 916  SER   A CA    1 
ATOM   6716  C  C     . SER   A  1  918  ? -42.544 94.518  93.329  1.00 34.62 ? 916  SER   A C     1 
ATOM   6717  O  O     . SER   A  1  918  ? -42.118 95.333  94.154  1.00 33.57 ? 916  SER   A O     1 
ATOM   6718  C  CB    . SER   A  1  918  ? -43.788 95.662  91.476  1.00 33.68 ? 916  SER   A CB    1 
ATOM   6719  O  OG    . SER   A  1  918  ? -44.957 94.887  91.690  1.00 42.62 ? 916  SER   A OG    1 
ATOM   6720  N  N     . GLU   A  1  919  ? -43.005 93.314  93.683  1.00 33.64 ? 917  GLU   A N     1 
ATOM   6721  C  CA    . GLU   A  1  919  ? -43.055 92.891  95.080  1.00 32.19 ? 917  GLU   A CA    1 
ATOM   6722  C  C     . GLU   A  1  919  ? -41.675 92.824  95.724  1.00 32.87 ? 917  GLU   A C     1 
ATOM   6723  O  O     . GLU   A  1  919  ? -41.579 92.847  96.956  1.00 33.15 ? 917  GLU   A O     1 
ATOM   6724  C  CB    . GLU   A  1  919  ? -43.736 91.525  95.198  1.00 33.39 ? 917  GLU   A CB    1 
ATOM   6725  C  CG    . GLU   A  1  919  ? -45.253 91.548  95.033  1.00 40.49 ? 917  GLU   A CG    1 
ATOM   6726  C  CD    . GLU   A  1  919  ? -45.701 91.457  93.584  1.00 48.03 ? 917  GLU   A CD    1 
ATOM   6727  O  OE1   . GLU   A  1  919  ? -44.865 91.657  92.675  1.00 45.48 ? 917  GLU   A OE1   1 
ATOM   6728  O  OE2   . GLU   A  1  919  ? -46.897 91.178  93.354  1.00 55.59 ? 917  GLU   A OE2   1 
ATOM   6729  N  N     . THR   A  1  920  ? -40.609 92.736  94.933  1.00 31.82 ? 918  THR   A N     1 
ATOM   6730  C  CA    . THR   A  1  920  ? -39.273 92.707  95.512  1.00 31.57 ? 918  THR   A CA    1 
ATOM   6731  C  C     . THR   A  1  920  ? -38.867 94.043  96.122  1.00 29.51 ? 918  THR   A C     1 
ATOM   6732  O  O     . THR   A  1  920  ? -37.900 94.085  96.892  1.00 27.89 ? 918  THR   A O     1 
ATOM   6733  C  CB    . THR   A  1  920  ? -38.263 92.274  94.448  1.00 28.28 ? 918  THR   A CB    1 
ATOM   6734  O  OG1   . THR   A  1  920  ? -38.294 93.198  93.356  1.00 30.95 ? 918  THR   A OG1   1 
ATOM   6735  C  CG2   . THR   A  1  920  ? -38.607 90.888  93.937  1.00 27.18 ? 918  THR   A CG2   1 
ATOM   6736  N  N     . GLY   A  1  921  ? -39.583 95.126  95.806  1.00 31.99 ? 919  GLY   A N     1 
ATOM   6737  C  CA    . GLY   A  1  921  ? -39.241 96.439  96.324  1.00 32.07 ? 919  GLY   A CA    1 
ATOM   6738  C  C     . GLY   A  1  921  ? -39.246 96.545  97.837  1.00 30.12 ? 919  GLY   A C     1 
ATOM   6739  O  O     . GLY   A  1  921  ? -38.554 97.405  98.388  1.00 33.67 ? 919  GLY   A O     1 
ATOM   6740  N  N     . VAL   A  1  922  ? -40.011 95.694  98.527  1.00 31.38 ? 920  VAL   A N     1 
ATOM   6741  C  CA    . VAL   A  1  922  ? -40.031 95.734  99.989  1.00 26.96 ? 920  VAL   A CA    1 
ATOM   6742  C  C     . VAL   A  1  922  ? -38.844 95.023  100.618 1.00 29.64 ? 920  VAL   A C     1 
ATOM   6743  O  O     . VAL   A  1  922  ? -38.652 95.124  101.837 1.00 29.98 ? 920  VAL   A O     1 
ATOM   6744  C  CB    . VAL   A  1  922  ? -41.346 95.173  100.561 1.00 28.31 ? 920  VAL   A CB    1 
ATOM   6745  C  CG1   . VAL   A  1  922  ? -42.508 96.083  100.194 1.00 31.83 ? 920  VAL   A CG1   1 
ATOM   6746  C  CG2   . VAL   A  1  922  ? -41.576 93.765  100.046 1.00 29.28 ? 920  VAL   A CG2   1 
ATOM   6747  N  N     . GLY   A  1  923  ? -38.050 94.303  99.826  1.00 25.75 ? 921  GLY   A N     1 
ATOM   6748  C  CA    . GLY   A  1  923  ? -36.853 93.648  100.317 1.00 26.81 ? 921  GLY   A CA    1 
ATOM   6749  C  C     . GLY   A  1  923  ? -35.612 94.085  99.565  1.00 24.14 ? 921  GLY   A C     1 
ATOM   6750  O  O     . GLY   A  1  923  ? -35.645 95.078  98.833  1.00 27.26 ? 921  GLY   A O     1 
ATOM   6751  N  N     . THR   A  1  924  ? -34.508 93.366  99.744  1.00 23.81 ? 922  THR   A N     1 
ATOM   6752  C  CA    . THR   A  1  924  ? -33.243 93.689  99.083  1.00 24.34 ? 922  THR   A CA    1 
ATOM   6753  C  C     . THR   A  1  924  ? -32.903 92.550  98.133  1.00 24.81 ? 922  THR   A C     1 
ATOM   6754  O  O     . THR   A  1  924  ? -32.361 91.526  98.551  1.00 24.30 ? 922  THR   A O     1 
ATOM   6755  C  CB    . THR   A  1  924  ? -32.123 93.934  100.093 1.00 23.07 ? 922  THR   A CB    1 
ATOM   6756  O  OG1   . THR   A  1  924  ? -32.074 92.860  101.040 1.00 22.90 ? 922  THR   A OG1   1 
ATOM   6757  C  CG2   . THR   A  1  924  ? -32.382 95.233  100.836 1.00 27.11 ? 922  THR   A CG2   1 
ATOM   6758  N  N     . PHE   A  1  925  ? -33.222 92.735  96.859  1.00 23.06 ? 923  PHE   A N     1 
ATOM   6759  C  CA    . PHE   A  1  925  ? -33.015 91.704  95.859  1.00 21.54 ? 923  PHE   A CA    1 
ATOM   6760  C  C     . PHE   A  1  925  ? -32.056 92.199  94.790  1.00 21.65 ? 923  PHE   A C     1 
ATOM   6761  O  O     . PHE   A  1  925  ? -32.038 93.383  94.431  1.00 25.80 ? 923  PHE   A O     1 
ATOM   6762  C  CB    . PHE   A  1  925  ? -34.328 91.315  95.178  1.00 19.46 ? 923  PHE   A CB    1 
ATOM   6763  C  CG    . PHE   A  1  925  ? -35.292 90.603  96.077  1.00 22.31 ? 923  PHE   A CG    1 
ATOM   6764  C  CD1   . PHE   A  1  925  ? -36.127 91.318  96.921  1.00 22.38 ? 923  PHE   A CD1   1 
ATOM   6765  C  CD2   . PHE   A  1  925  ? -35.377 89.223  96.072  1.00 20.78 ? 923  PHE   A CD2   1 
ATOM   6766  C  CE1   . PHE   A  1  925  ? -37.027 90.669  97.743  1.00 23.10 ? 923  PHE   A CE1   1 
ATOM   6767  C  CE2   . PHE   A  1  925  ? -36.285 88.567  96.897  1.00 21.17 ? 923  PHE   A CE2   1 
ATOM   6768  C  CZ    . PHE   A  1  925  ? -37.106 89.293  97.730  1.00 20.51 ? 923  PHE   A CZ    1 
ATOM   6769  N  N     . VAL   A  1  926  ? -31.278 91.257  94.272  1.00 20.96 ? 924  VAL   A N     1 
ATOM   6770  C  CA    . VAL   A  1  926  ? -30.446 91.458  93.099  1.00 21.55 ? 924  VAL   A CA    1 
ATOM   6771  C  C     . VAL   A  1  926  ? -30.867 90.395  92.095  1.00 21.57 ? 924  VAL   A C     1 
ATOM   6772  O  O     . VAL   A  1  926  ? -30.891 89.213  92.440  1.00 22.85 ? 924  VAL   A O     1 
ATOM   6773  C  CB    . VAL   A  1  926  ? -28.946 91.327  93.419  1.00 22.59 ? 924  VAL   A CB    1 
ATOM   6774  C  CG1   . VAL   A  1  926  ? -28.121 91.345  92.138  1.00 23.79 ? 924  VAL   A CG1   1 
ATOM   6775  C  CG2   . VAL   A  1  926  ? -28.513 92.458  94.344  1.00 24.22 ? 924  VAL   A CG2   1 
ATOM   6776  N  N     . PRO   A  1  927  ? -31.236 90.757  90.876  1.00 22.23 ? 925  PRO   A N     1 
ATOM   6777  C  CA    . PRO   A  1  927  ? -31.638 89.743  89.908  1.00 23.68 ? 925  PRO   A CA    1 
ATOM   6778  C  C     . PRO   A  1  927  ? -30.452 88.880  89.531  1.00 23.34 ? 925  PRO   A C     1 
ATOM   6779  O  O     . PRO   A  1  927  ? -29.327 89.383  89.391  1.00 23.30 ? 925  PRO   A O     1 
ATOM   6780  C  CB    . PRO   A  1  927  ? -32.111 90.571  88.708  1.00 27.92 ? 925  PRO   A CB    1 
ATOM   6781  C  CG    . PRO   A  1  927  ? -31.361 91.845  88.816  1.00 28.69 ? 925  PRO   A CG    1 
ATOM   6782  C  CD    . PRO   A  1  927  ? -31.218 92.108  90.290  1.00 27.57 ? 925  PRO   A CD    1 
ATOM   6783  N  N     . PRO   A  1  928  ? -30.658 87.574  89.401  1.00 23.55 ? 926  PRO   A N     1 
ATOM   6784  C  CA    . PRO   A  1  928  ? -29.620 86.721  88.824  1.00 22.31 ? 926  PRO   A CA    1 
ATOM   6785  C  C     . PRO   A  1  928  ? -29.097 87.346  87.545  1.00 20.84 ? 926  PRO   A C     1 
ATOM   6786  O  O     . PRO   A  1  928  ? -29.863 87.829  86.705  1.00 22.14 ? 926  PRO   A O     1 
ATOM   6787  C  CB    . PRO   A  1  928  ? -30.363 85.410  88.561  1.00 20.79 ? 926  PRO   A CB    1 
ATOM   6788  C  CG    . PRO   A  1  928  ? -31.347 85.363  89.684  1.00 23.08 ? 926  PRO   A CG    1 
ATOM   6789  C  CD    . PRO   A  1  928  ? -31.826 86.793  89.843  1.00 23.20 ? 926  PRO   A CD    1 
ATOM   6790  N  N     . THR   A  1  929  ? -27.780 87.351  87.414  1.00 21.94 ? 927  THR   A N     1 
ATOM   6791  C  CA    . THR   A  1  929  ? -27.094 88.152  86.419  1.00 22.74 ? 927  THR   A CA    1 
ATOM   6792  C  C     . THR   A  1  929  ? -26.012 87.300  85.787  1.00 23.46 ? 927  THR   A C     1 
ATOM   6793  O  O     . THR   A  1  929  ? -25.288 86.598  86.491  1.00 21.15 ? 927  THR   A O     1 
ATOM   6794  C  CB    . THR   A  1  929  ? -26.449 89.373  87.089  1.00 24.39 ? 927  THR   A CB    1 
ATOM   6795  O  OG1   . THR   A  1  929  ? -27.477 90.187  87.676  1.00 24.11 ? 927  THR   A OG1   1 
ATOM   6796  C  CG2   . THR   A  1  929  ? -25.670 90.202  86.075  1.00 23.20 ? 927  THR   A CG2   1 
ATOM   6797  N  N     . ILE   A  1  930  ? -25.916 87.364  84.463  1.00 21.87 ? 928  ILE   A N     1 
ATOM   6798  C  CA    . ILE   A  1  930  ? -24.839 86.733  83.712  1.00 22.88 ? 928  ILE   A CA    1 
ATOM   6799  C  C     . ILE   A  1  930  ? -24.039 87.845  83.062  1.00 23.15 ? 928  ILE   A C     1 
ATOM   6800  O  O     . ILE   A  1  930  ? -24.609 88.710  82.387  1.00 26.68 ? 928  ILE   A O     1 
ATOM   6801  C  CB    . ILE   A  1  930  ? -25.386 85.765  82.650  1.00 19.57 ? 928  ILE   A CB    1 
ATOM   6802  C  CG1   . ILE   A  1  930  ? -26.150 84.623  83.313  1.00 23.26 ? 928  ILE   A CG1   1 
ATOM   6803  C  CG2   . ILE   A  1  930  ? -24.242 85.229  81.781  1.00 25.95 ? 928  ILE   A CG2   1 
ATOM   6804  C  CD1   . ILE   A  1  930  ? -26.966 83.782  82.326  1.00 25.08 ? 928  ILE   A CD1   1 
ATOM   6805  N  N     . ILE   A  1  931  ? -22.728 87.828  83.274  1.00 21.67 ? 929  ILE   A N     1 
ATOM   6806  C  CA    . ILE   A  1  931  ? -21.812 88.834  82.758  1.00 24.23 ? 929  ILE   A CA    1 
ATOM   6807  C  C     . ILE   A  1  931  ? -20.774 88.109  81.921  1.00 26.71 ? 929  ILE   A C     1 
ATOM   6808  O  O     . ILE   A  1  931  ? -20.067 87.232  82.427  1.00 25.65 ? 929  ILE   A O     1 
ATOM   6809  C  CB    . ILE   A  1  931  ? -21.127 89.611  83.892  1.00 26.13 ? 929  ILE   A CB    1 
ATOM   6810  C  CG1   . ILE   A  1  931  ? -22.166 90.335  84.758  1.00 25.60 ? 929  ILE   A CG1   1 
ATOM   6811  C  CG2   . ILE   A  1  931  ? -20.118 90.591  83.326  1.00 26.20 ? 929  ILE   A CG2   1 
ATOM   6812  C  CD1   . ILE   A  1  931  ? -21.551 91.223  85.813  1.00 27.35 ? 929  ILE   A CD1   1 
ATOM   6813  N  N     . GLU   A  1  932  ? -20.676 88.470  80.651  1.00 26.09 ? 930  GLU   A N     1 
ATOM   6814  C  CA    . GLU   A  1  932  ? -19.708 87.847  79.756  1.00 27.00 ? 930  GLU   A CA    1 
ATOM   6815  C  C     . GLU   A  1  932  ? -18.402 88.624  79.816  1.00 23.68 ? 930  GLU   A C     1 
ATOM   6816  O  O     . GLU   A  1  932  ? -18.352 89.808  79.460  1.00 27.90 ? 930  GLU   A O     1 
ATOM   6817  C  CB    . GLU   A  1  932  ? -20.278 87.789  78.346  1.00 25.61 ? 930  GLU   A CB    1 
ATOM   6818  C  CG    . GLU   A  1  932  ? -21.416 86.803  78.264  1.00 28.05 ? 930  GLU   A CG    1 
ATOM   6819  C  CD    . GLU   A  1  932  ? -22.201 86.929  76.991  1.00 34.61 ? 930  GLU   A CD    1 
ATOM   6820  O  OE1   . GLU   A  1  932  ? -21.582 86.851  75.909  1.00 30.74 ? 930  GLU   A OE1   1 
ATOM   6821  O  OE2   . GLU   A  1  932  ? -23.437 87.102  77.077  1.00 33.55 ? 930  GLU   A OE2   1 
ATOM   6822  N  N     . LEU   A  1  933  ? -17.355 87.974  80.304  1.00 25.15 ? 931  LEU   A N     1 
ATOM   6823  C  CA    . LEU   A  1  933  ? -16.050 88.591  80.468  1.00 25.54 ? 931  LEU   A CA    1 
ATOM   6824  C  C     . LEU   A  1  933  ? -15.138 88.254  79.298  1.00 34.34 ? 931  LEU   A C     1 
ATOM   6825  O  O     . LEU   A  1  933  ? -15.329 87.261  78.592  1.00 32.48 ? 931  LEU   A O     1 
ATOM   6826  C  CB    . LEU   A  1  933  ? -15.379 88.115  81.755  1.00 28.14 ? 931  LEU   A CB    1 
ATOM   6827  C  CG    . LEU   A  1  933  ? -16.080 88.433  83.076  1.00 33.63 ? 931  LEU   A CG    1 
ATOM   6828  C  CD1   . LEU   A  1  933  ? -15.193 87.992  84.220  1.00 34.69 ? 931  LEU   A CD1   1 
ATOM   6829  C  CD2   . LEU   A  1  933  ? -16.386 89.911  83.175  1.00 33.34 ? 931  LEU   A CD2   1 
ATOM   6830  N  N     . GLU   A  1  934  ? -14.119 89.096  79.123  1.00 32.29 ? 932  GLU   A N     1 
ATOM   6831  C  CA    . GLU   A  1  934  ? -13.061 88.865  78.149  1.00 39.55 ? 932  GLU   A CA    1 
ATOM   6832  C  C     . GLU   A  1  934  ? -11.962 87.966  78.711  1.00 43.22 ? 932  GLU   A C     1 
ATOM   6833  O  O     . GLU   A  1  934  ? -11.546 87.007  78.053  1.00 44.57 ? 932  GLU   A O     1 
ATOM   6834  C  CB    . GLU   A  1  934  ? -12.483 90.203  77.674  1.00 41.79 ? 932  GLU   A CB    1 
ATOM   6835  N  N     . LYS   A  1  935  ? -11.492 88.253  79.924  1.00 40.38 ? 933  LYS   A N     1 
ATOM   6836  C  CA    . LYS   A  1  935  ? -10.459 87.455  80.573  1.00 44.41 ? 933  LYS   A CA    1 
ATOM   6837  C  C     . LYS   A  1  935  ? -10.787 87.309  82.052  1.00 47.06 ? 933  LYS   A C     1 
ATOM   6838  O  O     . LYS   A  1  935  ? -11.501 88.130  82.633  1.00 45.28 ? 933  LYS   A O     1 
ATOM   6839  C  CB    . LYS   A  1  935  ? -9.070  88.087  80.419  1.00 47.06 ? 933  LYS   A CB    1 
ATOM   6840  N  N     . LEU   A  1  936  ? -10.245 86.250  82.661  1.00 44.13 ? 934  LEU   A N     1 
ATOM   6841  C  CA    . LEU   A  1  936  ? -10.481 86.000  84.079  1.00 45.94 ? 934  LEU   A CA    1 
ATOM   6842  C  C     . LEU   A  1  936  ? -9.902  87.098  84.957  1.00 48.01 ? 934  LEU   A C     1 
ATOM   6843  O  O     . LEU   A  1  936  ? -10.367 87.286  86.086  1.00 46.24 ? 934  LEU   A O     1 
ATOM   6844  C  CB    . LEU   A  1  936  ? -9.899  84.644  84.486  1.00 44.08 ? 934  LEU   A CB    1 
ATOM   6845  C  CG    . LEU   A  1  936  ? -10.812 83.715  85.293  1.00 47.72 ? 934  LEU   A CG    1 
ATOM   6846  C  CD1   . LEU   A  1  936  ? -10.188 82.334  85.432  1.00 40.16 ? 934  LEU   A CD1   1 
ATOM   6847  C  CD2   . LEU   A  1  936  ? -11.126 84.296  86.664  1.00 42.19 ? 934  LEU   A CD2   1 
ATOM   6848  N  N     . SER   A  1  937  ? -8.906  87.833  84.461  1.00 50.12 ? 935  SER   A N     1 
ATOM   6849  C  CA    . SER   A  1  937  ? -8.340  88.953  85.199  1.00 48.45 ? 935  SER   A CA    1 
ATOM   6850  C  C     . SER   A  1  937  ? -9.305  90.124  85.337  1.00 46.82 ? 935  SER   A C     1 
ATOM   6851  O  O     . SER   A  1  937  ? -9.006  91.065  86.080  1.00 50.44 ? 935  SER   A O     1 
ATOM   6852  C  CB    . SER   A  1  937  ? -7.037  89.406  84.536  1.00 50.30 ? 935  SER   A CB    1 
ATOM   6853  O  OG    . SER   A  1  937  ? -7.197  89.499  83.131  1.00 49.11 ? 935  SER   A OG    1 
ATOM   6854  N  N     . ASP   A  1  938  ? -10.445 90.099  84.641  1.00 47.78 ? 936  ASP   A N     1 
ATOM   6855  C  CA    . ASP   A  1  938  ? -11.455 91.135  84.826  1.00 47.70 ? 936  ASP   A CA    1 
ATOM   6856  C  C     . ASP   A  1  938  ? -12.044 91.127  86.229  1.00 49.08 ? 936  ASP   A C     1 
ATOM   6857  O  O     . ASP   A  1  938  ? -12.599 92.142  86.660  1.00 47.79 ? 936  ASP   A O     1 
ATOM   6858  C  CB    . ASP   A  1  938  ? -12.583 90.971  83.807  1.00 50.36 ? 936  ASP   A CB    1 
ATOM   6859  C  CG    . ASP   A  1  938  ? -12.105 91.128  82.380  1.00 52.28 ? 936  ASP   A CG    1 
ATOM   6860  O  OD1   . ASP   A  1  938  ? -10.910 91.446  82.189  1.00 52.61 ? 936  ASP   A OD1   1 
ATOM   6861  O  OD2   . ASP   A  1  938  ? -12.922 90.926  81.453  1.00 48.60 ? 936  ASP   A OD2   1 
ATOM   6862  N  N     . LEU   A  1  939  ? -11.948 90.010  86.945  1.00 44.47 ? 937  LEU   A N     1 
ATOM   6863  C  CA    . LEU   A  1  939  ? -12.470 89.922  88.299  1.00 44.15 ? 937  LEU   A CA    1 
ATOM   6864  C  C     . LEU   A  1  939  ? -11.386 90.252  89.312  1.00 45.79 ? 937  LEU   A C     1 
ATOM   6865  O  O     . LEU   A  1  939  ? -10.239 89.811  89.185  1.00 48.08 ? 937  LEU   A O     1 
ATOM   6866  C  CB    . LEU   A  1  939  ? -12.999 88.519  88.576  1.00 42.43 ? 937  LEU   A CB    1 
ATOM   6867  C  CG    . LEU   A  1  939  ? -14.202 88.091  87.747  1.00 38.66 ? 937  LEU   A CG    1 
ATOM   6868  C  CD1   . LEU   A  1  939  ? -14.821 86.866  88.376  1.00 37.78 ? 937  LEU   A CD1   1 
ATOM   6869  C  CD2   . LEU   A  1  939  ? -15.212 89.223  87.657  1.00 39.02 ? 937  LEU   A CD2   1 
ATOM   6870  N  N     . GLN   A  1  940  ? -11.760 91.028  90.326  1.00 42.12 ? 938  GLN   A N     1 
ATOM   6871  C  CA    . GLN   A  1  940  ? -10.844 91.358  91.408  1.00 41.34 ? 938  GLN   A CA    1 
ATOM   6872  C  C     . GLN   A  1  940  ? -11.093 90.436  92.593  1.00 43.53 ? 938  GLN   A C     1 
ATOM   6873  O  O     . GLN   A  1  940  ? -10.393 89.432  92.762  1.00 49.09 ? 938  GLN   A O     1 
ATOM   6874  C  CB    . GLN   A  1  940  ? -11.003 92.823  91.819  1.00 46.15 ? 938  GLN   A CB    1 
ATOM   6875  N  N     . ARG   A  1  941  ? -12.093 90.753  93.406  1.00 41.89 ? 939  ARG   A N     1 
ATOM   6876  C  CA    . ARG   A  1  941  ? -12.415 89.982  94.597  1.00 36.23 ? 939  ARG   A CA    1 
ATOM   6877  C  C     . ARG   A  1  941  ? -13.732 89.236  94.409  1.00 30.07 ? 939  ARG   A C     1 
ATOM   6878  O  O     . ARG   A  1  941  ? -14.486 89.471  93.462  1.00 33.33 ? 939  ARG   A O     1 
ATOM   6879  C  CB    . ARG   A  1  941  ? -12.499 90.894  95.826  1.00 36.70 ? 939  ARG   A CB    1 
ATOM   6880  N  N     . GLU   A  1  942  ? -13.983 88.313  95.336  1.00 27.90 ? 940  GLU   A N     1 
ATOM   6881  C  CA    . GLU   A  1  942  ? -15.242 87.585  95.376  1.00 29.40 ? 940  GLU   A CA    1 
ATOM   6882  C  C     . GLU   A  1  942  ? -16.407 88.562  95.423  1.00 25.09 ? 940  GLU   A C     1 
ATOM   6883  O  O     . GLU   A  1  942  ? -16.401 89.512  96.211  1.00 27.36 ? 940  GLU   A O     1 
ATOM   6884  C  CB    . GLU   A  1  942  ? -15.252 86.713  96.631  1.00 24.83 ? 940  GLU   A CB    1 
ATOM   6885  C  CG    . GLU   A  1  942  ? -16.581 86.067  96.967  1.00 23.79 ? 940  GLU   A CG    1 
ATOM   6886  C  CD    . GLU   A  1  942  ? -16.560 85.441  98.346  1.00 23.75 ? 940  GLU   A CD    1 
ATOM   6887  O  OE1   . GLU   A  1  942  ? -16.311 86.184  99.322  1.00 27.95 ? 940  GLU   A OE1   1 
ATOM   6888  O  OE2   . GLU   A  1  942  ? -16.776 84.218  98.456  1.00 21.66 ? 940  GLU   A OE2   1 
ATOM   6889  N  N     . VAL   A  1  943  ? -17.396 88.342  94.558  1.00 25.68 ? 941  VAL   A N     1 
ATOM   6890  C  CA    . VAL   A  1  943  ? -18.644 89.101  94.552  1.00 23.37 ? 941  VAL   A CA    1 
ATOM   6891  C  C     . VAL   A  1  943  ? -19.731 88.163  95.056  1.00 24.94 ? 941  VAL   A C     1 
ATOM   6892  O  O     . VAL   A  1  943  ? -20.153 87.233  94.355  1.00 22.55 ? 941  VAL   A O     1 
ATOM   6893  C  CB    . VAL   A  1  943  ? -18.976 89.665  93.165  1.00 25.67 ? 941  VAL   A CB    1 
ATOM   6894  C  CG1   . VAL   A  1  943  ? -20.317 90.373  93.178  1.00 25.77 ? 941  VAL   A CG1   1 
ATOM   6895  C  CG2   . VAL   A  1  943  ? -17.873 90.607  92.710  1.00 27.85 ? 941  VAL   A CG2   1 
ATOM   6896  N  N     . PHE   A  1  944  ? -20.164 88.391  96.291  1.00 23.82 ? 942  PHE   A N     1 
ATOM   6897  C  CA    . PHE   A  1  944  ? -20.983 87.423  97.012  1.00 22.61 ? 942  PHE   A CA    1 
ATOM   6898  C  C     . PHE   A  1  944  ? -22.453 87.701  96.713  1.00 23.24 ? 942  PHE   A C     1 
ATOM   6899  O  O     . PHE   A  1  944  ? -23.205 88.250  97.518  1.00 24.62 ? 942  PHE   A O     1 
ATOM   6900  C  CB    . PHE   A  1  944  ? -20.672 87.494  98.502  1.00 21.21 ? 942  PHE   A CB    1 
ATOM   6901  C  CG    . PHE   A  1  944  ? -21.045 86.258  99.251  1.00 20.09 ? 942  PHE   A CG    1 
ATOM   6902  C  CD1   . PHE   A  1  944  ? -20.365 85.075  99.033  1.00 20.15 ? 942  PHE   A CD1   1 
ATOM   6903  C  CD2   . PHE   A  1  944  ? -22.068 86.275  100.183 1.00 19.93 ? 942  PHE   A CD2   1 
ATOM   6904  C  CE1   . PHE   A  1  944  ? -20.716 83.928  99.729  1.00 17.69 ? 942  PHE   A CE1   1 
ATOM   6905  C  CE2   . PHE   A  1  944  ? -22.403 85.127  100.886 1.00 20.98 ? 942  PHE   A CE2   1 
ATOM   6906  C  CZ    . PHE   A  1  944  ? -21.734 83.959  100.650 1.00 19.08 ? 942  PHE   A CZ    1 
ATOM   6907  N  N     . GLY   A  1  945  ? -22.851 87.331  95.502  1.00 21.22 ? 943  GLY   A N     1 
ATOM   6908  C  CA    . GLY   A  1  945  ? -24.202 87.570  95.060  1.00 21.26 ? 943  GLY   A CA    1 
ATOM   6909  C  C     . GLY   A  1  945  ? -24.512 86.762  93.825  1.00 23.28 ? 943  GLY   A C     1 
ATOM   6910  O  O     . GLY   A  1  945  ? -23.714 85.929  93.386  1.00 21.10 ? 943  GLY   A O     1 
ATOM   6911  N  N     . PRO   A  1  946  ? -25.687 86.979  93.242  1.00 20.08 ? 944  PRO   A N     1 
ATOM   6912  C  CA    . PRO   A  1  946  ? -26.128 86.124  92.130  1.00 20.07 ? 944  PRO   A CA    1 
ATOM   6913  C  C     . PRO   A  1  946  ? -25.580 86.610  90.795  1.00 19.73 ? 944  PRO   A C     1 
ATOM   6914  O  O     . PRO   A  1  946  ? -26.318 87.037  89.910  1.00 21.63 ? 944  PRO   A O     1 
ATOM   6915  C  CB    . PRO   A  1  946  ? -27.653 86.242  92.225  1.00 18.37 ? 944  PRO   A CB    1 
ATOM   6916  C  CG    . PRO   A  1  946  ? -27.867 87.643  92.702  1.00 24.74 ? 944  PRO   A CG    1 
ATOM   6917  C  CD    . PRO   A  1  946  ? -26.717 87.961  93.634  1.00 21.91 ? 944  PRO   A CD    1 
ATOM   6918  N  N     . VAL   A  1  947  ? -24.257 86.560  90.656  1.00 21.50 ? 945  VAL   A N     1 
ATOM   6919  C  CA    . VAL   A  1  947  ? -23.574 87.143  89.510  1.00 23.55 ? 945  VAL   A CA    1 
ATOM   6920  C  C     . VAL   A  1  947  ? -22.636 86.105  88.920  1.00 21.02 ? 945  VAL   A C     1 
ATOM   6921  O  O     . VAL   A  1  947  ? -21.574 85.822  89.488  1.00 21.18 ? 945  VAL   A O     1 
ATOM   6922  C  CB    . VAL   A  1  947  ? -22.818 88.431  89.856  1.00 24.22 ? 945  VAL   A CB    1 
ATOM   6923  C  CG1   . VAL   A  1  947  ? -22.215 89.011  88.600  1.00 23.74 ? 945  VAL   A CG1   1 
ATOM   6924  C  CG2   . VAL   A  1  947  ? -23.755 89.436  90.527  1.00 22.79 ? 945  VAL   A CG2   1 
ATOM   6925  N  N     . LEU   A  1  948  ? -23.008 85.571  87.769  1.00 22.40 ? 946  LEU   A N     1 
ATOM   6926  C  CA    . LEU   A  1  948  ? -22.210 84.581  87.075  1.00 21.09 ? 946  LEU   A CA    1 
ATOM   6927  C  C     . LEU   A  1  948  ? -21.411 85.280  85.989  1.00 21.55 ? 946  LEU   A C     1 
ATOM   6928  O  O     . LEU   A  1  948  ? -21.967 86.043  85.193  1.00 23.88 ? 946  LEU   A O     1 
ATOM   6929  C  CB    . LEU   A  1  948  ? -23.125 83.545  86.441  1.00 19.07 ? 946  LEU   A CB    1 
ATOM   6930  C  CG    . LEU   A  1  948  ? -22.354 82.498  85.643  1.00 20.00 ? 946  LEU   A CG    1 
ATOM   6931  C  CD1   . LEU   A  1  948  ? -21.367 81.758  86.552  1.00 19.95 ? 946  LEU   A CD1   1 
ATOM   6932  C  CD2   . LEU   A  1  948  ? -23.349 81.568  85.003  1.00 23.40 ? 946  LEU   A CD2   1 
ATOM   6933  N  N     . HIS   A  1  949  ? -20.115 85.022  85.960  1.00 18.20 ? 947  HIS   A N     1 
ATOM   6934  C  CA    . HIS   A  1  949  ? -19.267 85.536  84.900  1.00 20.30 ? 947  HIS   A CA    1 
ATOM   6935  C  C     . HIS   A  1  949  ? -18.954 84.401  83.946  1.00 20.82 ? 947  HIS   A C     1 
ATOM   6936  O  O     . HIS   A  1  949  ? -18.794 83.256  84.369  1.00 21.56 ? 947  HIS   A O     1 
ATOM   6937  C  CB    . HIS   A  1  949  ? -17.991 86.117  85.482  1.00 20.67 ? 947  HIS   A CB    1 
ATOM   6938  C  CG    . HIS   A  1  949  ? -18.253 87.156  86.518  1.00 22.39 ? 947  HIS   A CG    1 
ATOM   6939  N  ND1   . HIS   A  1  949  ? -18.466 86.842  87.842  1.00 22.94 ? 947  HIS   A ND1   1 
ATOM   6940  C  CD2   . HIS   A  1  949  ? -18.390 88.498  86.417  1.00 26.57 ? 947  HIS   A CD2   1 
ATOM   6941  C  CE1   . HIS   A  1  949  ? -18.692 87.955  88.519  1.00 27.10 ? 947  HIS   A CE1   1 
ATOM   6942  N  NE2   . HIS   A  1  949  ? -18.655 88.971  87.676  1.00 25.07 ? 947  HIS   A NE2   1 
ATOM   6943  N  N     . VAL   A  1  950  ? -18.903 84.714  82.654  1.00 19.38 ? 948  VAL   A N     1 
ATOM   6944  C  CA    . VAL   A  1  950  ? -18.711 83.704  81.621  1.00 22.22 ? 948  VAL   A CA    1 
ATOM   6945  C  C     . VAL   A  1  950  ? -17.487 84.070  80.804  1.00 24.22 ? 948  VAL   A C     1 
ATOM   6946  O  O     . VAL   A  1  950  ? -17.389 85.192  80.290  1.00 24.76 ? 948  VAL   A O     1 
ATOM   6947  C  CB    . VAL   A  1  950  ? -19.951 83.552  80.723  1.00 20.88 ? 948  VAL   A CB    1 
ATOM   6948  C  CG1   . VAL   A  1  950  ? -19.693 82.498  79.628  1.00 22.18 ? 948  VAL   A CG1   1 
ATOM   6949  C  CG2   . VAL   A  1  950  ? -21.153 83.162  81.554  1.00 22.69 ? 948  VAL   A CG2   1 
ATOM   6950  N  N     . ILE   A  1  951  ? -16.558 83.125  80.692  1.00 21.36 ? 949  ILE   A N     1 
ATOM   6951  C  CA    . ILE   A  1  951  ? -15.371 83.259  79.859  1.00 22.61 ? 949  ILE   A CA    1 
ATOM   6952  C  C     . ILE   A  1  951  ? -15.393 82.129  78.840  1.00 25.18 ? 949  ILE   A C     1 
ATOM   6953  O  O     . ILE   A  1  951  ? -15.922 81.044  79.101  1.00 21.17 ? 949  ILE   A O     1 
ATOM   6954  C  CB    . ILE   A  1  951  ? -14.075 83.226  80.695  1.00 25.93 ? 949  ILE   A CB    1 
ATOM   6955  N  N     . ARG   A  1  952  ? -14.826 82.389  77.668  1.00 22.84 ? 950  ARG   A N     1 
ATOM   6956  C  CA    . ARG   A  1  952  ? -14.734 81.400  76.605  1.00 19.92 ? 950  ARG   A CA    1 
ATOM   6957  C  C     . ARG   A  1  952  ? -13.267 81.046  76.423  1.00 21.74 ? 950  ARG   A C     1 
ATOM   6958  O  O     . ARG   A  1  952  ? -12.389 81.885  76.626  1.00 24.96 ? 950  ARG   A O     1 
ATOM   6959  C  CB    . ARG   A  1  952  ? -15.268 81.973  75.292  1.00 23.23 ? 950  ARG   A CB    1 
ATOM   6960  C  CG    . ARG   A  1  952  ? -16.644 82.594  75.413  1.00 25.74 ? 950  ARG   A CG    1 
ATOM   6961  C  CD    . ARG   A  1  952  ? -16.902 83.538  74.258  1.00 32.71 ? 950  ARG   A CD    1 
ATOM   6962  N  NE    . ARG   A  1  952  ? -17.287 82.827  73.047  1.00 33.50 ? 950  ARG   A NE    1 
ATOM   6963  C  CZ    . ARG   A  1  952  ? -18.537 82.706  72.619  1.00 30.73 ? 950  ARG   A CZ    1 
ATOM   6964  N  NH1   . ARG   A  1  952  ? -19.550 83.238  73.284  1.00 32.67 ? 950  ARG   A NH1   1 
ATOM   6965  N  NH2   . ARG   A  1  952  ? -18.776 82.035  71.497  1.00 30.85 ? 950  ARG   A NH2   1 
ATOM   6966  N  N     . TYR   A  1  953  ? -12.997 79.797  76.052  1.00 19.59 ? 951  TYR   A N     1 
ATOM   6967  C  CA    . TYR   A  1  953  ? -11.613 79.390  75.860  1.00 20.77 ? 951  TYR   A CA    1 
ATOM   6968  C  C     . TYR   A  1  953  ? -11.516 78.426  74.688  1.00 19.39 ? 951  TYR   A C     1 
ATOM   6969  O  O     . TYR   A  1  953  ? -12.446 77.667  74.407  1.00 21.02 ? 951  TYR   A O     1 
ATOM   6970  C  CB    . TYR   A  1  953  ? -11.019 78.763  77.134  1.00 21.59 ? 951  TYR   A CB    1 
ATOM   6971  C  CG    . TYR   A  1  953  ? -11.551 77.381  77.420  1.00 20.73 ? 951  TYR   A CG    1 
ATOM   6972  C  CD1   . TYR   A  1  953  ? -12.777 77.202  78.059  1.00 19.27 ? 951  TYR   A CD1   1 
ATOM   6973  C  CD2   . TYR   A  1  953  ? -10.841 76.251  77.020  1.00 19.14 ? 951  TYR   A CD2   1 
ATOM   6974  C  CE1   . TYR   A  1  953  ? -13.270 75.937  78.312  1.00 19.86 ? 951  TYR   A CE1   1 
ATOM   6975  C  CE2   . TYR   A  1  953  ? -11.326 74.980  77.265  1.00 18.15 ? 951  TYR   A CE2   1 
ATOM   6976  C  CZ    . TYR   A  1  953  ? -12.550 74.826  77.904  1.00 18.59 ? 951  TYR   A CZ    1 
ATOM   6977  O  OH    . TYR   A  1  953  ? -13.038 73.563  78.153  1.00 19.14 ? 951  TYR   A OH    1 
ATOM   6978  N  N     . ARG   A  1  954  ? -10.377 78.483  73.996  1.00 23.18 ? 952  ARG   A N     1 
ATOM   6979  C  CA    . ARG   A  1  954  ? -10.063 77.507  72.963  1.00 24.06 ? 952  ARG   A CA    1 
ATOM   6980  C  C     . ARG   A  1  954  ? -9.452  76.270  73.607  1.00 21.88 ? 952  ARG   A C     1 
ATOM   6981  O  O     . ARG   A  1  954  ? -8.698  76.372  74.581  1.00 21.93 ? 952  ARG   A O     1 
ATOM   6982  C  CB    . ARG   A  1  954  ? -9.084  78.106  71.954  1.00 27.97 ? 952  ARG   A CB    1 
ATOM   6983  N  N     . ARG   A  1  955  ? -9.786  75.096  73.061  1.00 22.35 ? 953  ARG   A N     1 
ATOM   6984  C  CA    . ARG   A  1  955  ? -9.419  73.845  73.720  1.00 23.27 ? 953  ARG   A CA    1 
ATOM   6985  C  C     . ARG   A  1  955  ? -7.917  73.752  73.958  1.00 21.01 ? 953  ARG   A C     1 
ATOM   6986  O  O     . ARG   A  1  955  ? -7.477  73.259  75.005  1.00 24.10 ? 953  ARG   A O     1 
ATOM   6987  C  CB    . ARG   A  1  955  ? -9.906  72.642  72.916  1.00 26.24 ? 953  ARG   A CB    1 
ATOM   6988  C  CG    . ARG   A  1  955  ? -9.559  71.285  73.560  1.00 31.68 ? 953  ARG   A CG    1 
ATOM   6989  C  CD    . ARG   A  1  955  ? -9.911  71.257  75.051  1.00 35.34 ? 953  ARG   A CD    1 
ATOM   6990  N  NE    . ARG   A  1  955  ? -9.566  70.001  75.713  1.00 36.98 ? 953  ARG   A NE    1 
ATOM   6991  C  CZ    . ARG   A  1  955  ? -8.353  69.685  76.153  1.00 36.69 ? 953  ARG   A CZ    1 
ATOM   6992  N  NH1   . ARG   A  1  955  ? -7.320  70.497  75.983  1.00 32.34 ? 953  ARG   A NH1   1 
ATOM   6993  N  NH2   . ARG   A  1  955  ? -8.171  68.523  76.778  1.00 35.52 ? 953  ARG   A NH2   1 
ATOM   6994  N  N     . ASP   A  1  956  ? -7.112  74.225  73.005  1.00 22.81 ? 954  ASP   A N     1 
ATOM   6995  C  CA    . ASP   A  1  956  ? -5.666  74.157  73.195  1.00 23.90 ? 954  ASP   A CA    1 
ATOM   6996  C  C     . ASP   A  1  956  ? -5.198  75.014  74.357  1.00 26.18 ? 954  ASP   A C     1 
ATOM   6997  O  O     . ASP   A  1  956  ? -4.110  74.773  74.887  1.00 26.77 ? 954  ASP   A O     1 
ATOM   6998  C  CB    . ASP   A  1  956  ? -4.926  74.572  71.923  1.00 25.09 ? 954  ASP   A CB    1 
ATOM   6999  C  CG    . ASP   A  1  956  ? -5.047  73.543  70.816  1.00 31.12 ? 954  ASP   A CG    1 
ATOM   7000  O  OD1   . ASP   A  1  956  ? -5.390  72.380  71.117  1.00 31.84 ? 954  ASP   A OD1   1 
ATOM   7001  O  OD2   . ASP   A  1  956  ? -4.788  73.899  69.647  1.00 35.40 ? 954  ASP   A OD2   1 
ATOM   7002  N  N     . ASP   A  1  957  ? -5.995  75.996  74.770  1.00 22.45 ? 955  ASP   A N     1 
ATOM   7003  C  CA    . ASP   A  1  957  ? -5.643  76.869  75.874  1.00 23.27 ? 955  ASP   A CA    1 
ATOM   7004  C  C     . ASP   A  1  957  ? -6.178  76.378  77.209  1.00 22.58 ? 955  ASP   A C     1 
ATOM   7005  O  O     . ASP   A  1  957  ? -6.177  77.146  78.175  1.00 23.78 ? 955  ASP   A O     1 
ATOM   7006  C  CB    . ASP   A  1  957  ? -6.150  78.287  75.609  1.00 26.33 ? 955  ASP   A CB    1 
ATOM   7007  C  CG    . ASP   A  1  957  ? -5.446  78.946  74.445  1.00 33.87 ? 955  ASP   A CG    1 
ATOM   7008  O  OD1   . ASP   A  1  957  ? -4.277  78.596  74.181  1.00 35.10 ? 955  ASP   A OD1   1 
ATOM   7009  O  OD2   . ASP   A  1  957  ? -6.063  79.815  73.794  1.00 35.93 ? 955  ASP   A OD2   1 
ATOM   7010  N  N     . LEU   A  1  958  ? -6.621  75.121  77.290  1.00 19.39 ? 956  LEU   A N     1 
ATOM   7011  C  CA    . LEU   A  1  958  ? -7.182  74.617  78.541  1.00 19.43 ? 956  LEU   A CA    1 
ATOM   7012  C  C     . LEU   A  1  958  ? -6.182  74.737  79.685  1.00 21.73 ? 956  LEU   A C     1 
ATOM   7013  O  O     . LEU   A  1  958  ? -6.529  75.181  80.786  1.00 20.49 ? 956  LEU   A O     1 
ATOM   7014  C  CB    . LEU   A  1  958  ? -7.610  73.162  78.372  1.00 20.00 ? 956  LEU   A CB    1 
ATOM   7015  C  CG    . LEU   A  1  958  ? -8.133  72.500  79.649  1.00 21.12 ? 956  LEU   A CG    1 
ATOM   7016  C  CD1   . LEU   A  1  958  ? -9.290  73.303  80.262  1.00 19.85 ? 956  LEU   A CD1   1 
ATOM   7017  C  CD2   . LEU   A  1  958  ? -8.554  71.064  79.376  1.00 25.09 ? 956  LEU   A CD2   1 
ATOM   7018  N  N     . ASP   A  1  959  ? -4.926  74.347  79.446  1.00 19.26 ? 957  ASP   A N     1 
ATOM   7019  C  CA    . ASP   A  1  959  ? -3.951  74.389  80.529  1.00 19.87 ? 957  ASP   A CA    1 
ATOM   7020  C  C     . ASP   A  1  959  ? -3.706  75.817  80.994  1.00 20.76 ? 957  ASP   A C     1 
ATOM   7021  O  O     . ASP   A  1  959  ? -3.598  76.075  82.196  1.00 19.49 ? 957  ASP   A O     1 
ATOM   7022  C  CB    . ASP   A  1  959  ? -2.639  73.729  80.110  1.00 23.01 ? 957  ASP   A CB    1 
ATOM   7023  C  CG    . ASP   A  1  959  ? -1.747  73.432  81.300  1.00 27.23 ? 957  ASP   A CG    1 
ATOM   7024  O  OD1   . ASP   A  1  959  ? -2.216  72.760  82.245  1.00 23.70 ? 957  ASP   A OD1   1 
ATOM   7025  O  OD2   . ASP   A  1  959  ? -0.580  73.873  81.304  1.00 29.57 ? 957  ASP   A OD2   1 
ATOM   7026  N  N     . ARG   A  1  960  ? -3.621  76.757  80.055  1.00 20.24 ? 958  ARG   A N     1 
ATOM   7027  C  CA    . ARG   A  1  960  ? -3.479  78.162  80.418  1.00 22.61 ? 958  ARG   A CA    1 
ATOM   7028  C  C     . ARG   A  1  960  ? -4.684  78.633  81.220  1.00 22.62 ? 958  ARG   A C     1 
ATOM   7029  O  O     . ARG   A  1  960  ? -4.539  79.400  82.178  1.00 25.04 ? 958  ARG   A O     1 
ATOM   7030  C  CB    . ARG   A  1  960  ? -3.324  78.997  79.142  1.00 22.83 ? 958  ARG   A CB    1 
ATOM   7031  C  CG    . ARG   A  1  960  ? -3.053  80.493  79.346  1.00 26.27 ? 958  ARG   A CG    1 
ATOM   7032  C  CD    . ARG   A  1  960  ? -4.347  81.311  79.410  1.00 38.41 ? 958  ARG   A CD    1 
ATOM   7033  N  NE    . ARG   A  1  960  ? -5.360  80.814  78.484  1.00 41.27 ? 958  ARG   A NE    1 
ATOM   7034  C  CZ    . ARG   A  1  960  ? -6.665  81.012  78.620  1.00 37.84 ? 958  ARG   A CZ    1 
ATOM   7035  N  NH1   . ARG   A  1  960  ? -7.159  81.716  79.626  1.00 43.04 ? 958  ARG   A NH1   1 
ATOM   7036  N  NH2   . ARG   A  1  960  ? -7.498  80.475  77.734  1.00 41.85 ? 958  ARG   A NH2   1 
ATOM   7037  N  N     . LEU   A  1  961  ? -5.881  78.193  80.831  1.00 20.18 ? 959  LEU   A N     1 
ATOM   7038  C  CA    . LEU   A  1  961  ? -7.082  78.573  81.566  1.00 22.06 ? 959  LEU   A CA    1 
ATOM   7039  C  C     . LEU   A  1  961  ? -7.016  78.086  83.005  1.00 22.67 ? 959  LEU   A C     1 
ATOM   7040  O  O     . LEU   A  1  961  ? -7.339  78.829  83.938  1.00 20.98 ? 959  LEU   A O     1 
ATOM   7041  C  CB    . LEU   A  1  961  ? -8.312  78.008  80.872  1.00 19.07 ? 959  LEU   A CB    1 
ATOM   7042  C  CG    . LEU   A  1  961  ? -9.610  78.137  81.674  1.00 18.65 ? 959  LEU   A CG    1 
ATOM   7043  C  CD1   . LEU   A  1  961  ? -9.963  79.608  81.867  1.00 25.65 ? 959  LEU   A CD1   1 
ATOM   7044  C  CD2   . LEU   A  1  961  ? -10.712 77.384  80.968  1.00 21.73 ? 959  LEU   A CD2   1 
ATOM   7045  N  N     . VAL   A  1  962  ? -6.618  76.829  83.206  1.00 19.07 ? 960  VAL   A N     1 
ATOM   7046  C  CA    . VAL   A  1  962  ? -6.463  76.327  84.568  1.00 20.48 ? 960  VAL   A CA    1 
ATOM   7047  C  C     . VAL   A  1  962  ? -5.478  77.188  85.350  1.00 25.07 ? 960  VAL   A C     1 
ATOM   7048  O  O     . VAL   A  1  962  ? -5.696  77.486  86.532  1.00 21.48 ? 960  VAL   A O     1 
ATOM   7049  C  CB    . VAL   A  1  962  ? -6.068  74.839  84.562  1.00 22.65 ? 960  VAL   A CB    1 
ATOM   7050  C  CG1   . VAL   A  1  962  ? -5.778  74.360  85.986  1.00 24.48 ? 960  VAL   A CG1   1 
ATOM   7051  C  CG2   . VAL   A  1  962  ? -7.173  74.011  83.933  1.00 22.08 ? 960  VAL   A CG2   1 
ATOM   7052  N  N     . ASP   A  1  963  ? -4.389  77.611  84.702  1.00 23.01 ? 961  ASP   A N     1 
ATOM   7053  C  CA    . ASP   A  1  963  ? -3.467  78.543  85.344  1.00 25.03 ? 961  ASP   A CA    1 
ATOM   7054  C  C     . ASP   A  1  963  ? -4.191  79.816  85.753  1.00 23.65 ? 961  ASP   A C     1 
ATOM   7055  O  O     . ASP   A  1  963  ? -4.003  80.321  86.865  1.00 27.69 ? 961  ASP   A O     1 
ATOM   7056  C  CB    . ASP   A  1  963  ? -2.325  78.899  84.394  1.00 25.91 ? 961  ASP   A CB    1 
ATOM   7057  C  CG    . ASP   A  1  963  ? -1.330  77.787  84.230  1.00 31.46 ? 961  ASP   A CG    1 
ATOM   7058  O  OD1   . ASP   A  1  963  ? -1.305  76.871  85.073  1.00 37.20 ? 961  ASP   A OD1   1 
ATOM   7059  O  OD2   . ASP   A  1  963  ? -0.559  77.839  83.245  1.00 41.14 ? 961  ASP   A OD2   1 
ATOM   7060  N  N     . ASP   A  1  964  ? -5.018  80.354  84.853  1.00 22.56 ? 962  ASP   A N     1 
ATOM   7061  C  CA    . ASP   A  1  964  ? -5.736  81.589  85.152  1.00 26.02 ? 962  ASP   A CA    1 
ATOM   7062  C  C     . ASP   A  1  964  ? -6.685  81.413  86.331  1.00 28.43 ? 962  ASP   A C     1 
ATOM   7063  O  O     . ASP   A  1  964  ? -6.830  82.319  87.161  1.00 25.57 ? 962  ASP   A O     1 
ATOM   7064  C  CB    . ASP   A  1  964  ? -6.500  82.053  83.916  1.00 26.87 ? 962  ASP   A CB    1 
ATOM   7065  C  CG    . ASP   A  1  964  ? -5.576  82.493  82.798  1.00 30.76 ? 962  ASP   A CG    1 
ATOM   7066  O  OD1   . ASP   A  1  964  ? -4.362  82.665  83.061  1.00 34.11 ? 962  ASP   A OD1   1 
ATOM   7067  O  OD2   . ASP   A  1  964  ? -6.065  82.654  81.661  1.00 37.68 ? 962  ASP   A OD2   1 
ATOM   7068  N  N     . VAL   A  1  965  ? -7.358  80.264  86.412  1.00 23.54 ? 963  VAL   A N     1 
ATOM   7069  C  CA    . VAL   A  1  965  ? -8.208  80.000  87.570  1.00 23.21 ? 963  VAL   A CA    1 
ATOM   7070  C  C     . VAL   A  1  965  ? -7.370  79.979  88.842  1.00 24.70 ? 963  VAL   A C     1 
ATOM   7071  O  O     . VAL   A  1  965  ? -7.725  80.600  89.854  1.00 24.01 ? 963  VAL   A O     1 
ATOM   7072  C  CB    . VAL   A  1  965  ? -8.986  78.686  87.385  1.00 21.77 ? 963  VAL   A CB    1 
ATOM   7073  C  CG1   . VAL   A  1  965  ? -9.785  78.369  88.647  1.00 19.92 ? 963  VAL   A CG1   1 
ATOM   7074  C  CG2   . VAL   A  1  965  ? -9.913  78.790  86.194  1.00 22.10 ? 963  VAL   A CG2   1 
ATOM   7075  N  N     . ASN   A  1  966  ? -6.248  79.255  88.808  1.00 20.88 ? 964  ASN   A N     1 
ATOM   7076  C  CA    . ASN   A  1  966  ? -5.362  79.194  89.965  1.00 23.00 ? 964  ASN   A CA    1 
ATOM   7077  C  C     . ASN   A  1  966  ? -4.812  80.569  90.308  1.00 25.45 ? 964  ASN   A C     1 
ATOM   7078  O  O     . ASN   A  1  966  ? -4.565  80.864  91.483  1.00 24.39 ? 964  ASN   A O     1 
ATOM   7079  C  CB    . ASN   A  1  966  ? -4.199  78.234  89.696  1.00 23.89 ? 964  ASN   A CB    1 
ATOM   7080  C  CG    . ASN   A  1  966  ? -4.620  76.776  89.701  1.00 22.38 ? 964  ASN   A CG    1 
ATOM   7081  O  OD1   . ASN   A  1  966  ? -5.660  76.415  90.262  1.00 21.52 ? 964  ASN   A OD1   1 
ATOM   7082  N  ND2   . ASN   A  1  966  ? -3.811  75.924  89.068  1.00 21.63 ? 964  ASN   A ND2   1 
ATOM   7083  N  N     . ALA   A  1  967  ? -4.633  81.425  89.297  1.00 24.14 ? 965  ALA   A N     1 
ATOM   7084  C  CA    . ALA   A  1  967  ? -3.948  82.701  89.488  1.00 26.95 ? 965  ALA   A CA    1 
ATOM   7085  C  C     . ALA   A  1  967  ? -4.737  83.691  90.330  1.00 28.20 ? 965  ALA   A C     1 
ATOM   7086  O  O     . ALA   A  1  967  ? -4.159  84.683  90.787  1.00 30.08 ? 965  ALA   A O     1 
ATOM   7087  C  CB    . ALA   A  1  967  ? -3.597  83.334  88.138  1.00 30.24 ? 965  ALA   A CB    1 
ATOM   7088  N  N     . THR   A  1  968  ? -6.034  83.466  90.540  1.00 23.50 ? 966  THR   A N     1 
ATOM   7089  C  CA    . THR   A  1  968  ? -6.772  84.370  91.413  1.00 24.66 ? 966  THR   A CA    1 
ATOM   7090  C  C     . THR   A  1  968  ? -6.259  84.314  92.844  1.00 24.50 ? 966  THR   A C     1 
ATOM   7091  O  O     . THR   A  1  968  ? -6.449  85.277  93.595  1.00 25.85 ? 966  THR   A O     1 
ATOM   7092  C  CB    . THR   A  1  968  ? -8.254  84.023  91.433  1.00 23.55 ? 966  THR   A CB    1 
ATOM   7093  O  OG1   . THR   A  1  968  ? -8.426  82.753  92.078  1.00 23.82 ? 966  THR   A OG1   1 
ATOM   7094  C  CG2   . THR   A  1  968  ? -8.826  83.968  90.014  1.00 23.55 ? 966  THR   A CG2   1 
ATOM   7095  N  N     . GLY   A  1  969  ? -5.629  83.211  93.238  1.00 23.10 ? 967  GLY   A N     1 
ATOM   7096  C  CA    . GLY   A  1  969  ? -5.239  82.993  94.612  1.00 23.90 ? 967  GLY   A CA    1 
ATOM   7097  C  C     . GLY   A  1  969  ? -6.279  82.284  95.452  1.00 19.57 ? 967  GLY   A C     1 
ATOM   7098  O  O     . GLY   A  1  969  ? -5.950  81.808  96.545  1.00 20.35 ? 967  GLY   A O     1 
ATOM   7099  N  N     . TYR   A  1  970  ? -7.521  82.204  94.979  1.00 20.21 ? 968  TYR   A N     1 
ATOM   7100  C  CA    . TYR   A  1  970  ? -8.535  81.439  95.677  1.00 18.49 ? 968  TYR   A CA    1 
ATOM   7101  C  C     . TYR   A  1  970  ? -8.359  79.958  95.360  1.00 17.87 ? 968  TYR   A C     1 
ATOM   7102  O  O     . TYR   A  1  970  ? -7.555  79.575  94.508  1.00 21.95 ? 968  TYR   A O     1 
ATOM   7103  C  CB    . TYR   A  1  970  ? -9.930  81.908  95.267  1.00 18.43 ? 968  TYR   A CB    1 
ATOM   7104  C  CG    . TYR   A  1  970  ? -10.246 83.316  95.717  1.00 21.05 ? 968  TYR   A CG    1 
ATOM   7105  C  CD1   . TYR   A  1  970  ? -10.764 83.558  96.983  1.00 20.84 ? 968  TYR   A CD1   1 
ATOM   7106  C  CD2   . TYR   A  1  970  ? -10.033 84.397  94.876  1.00 24.24 ? 968  TYR   A CD2   1 
ATOM   7107  C  CE1   . TYR   A  1  970  ? -11.068 84.844  97.394  1.00 23.07 ? 968  TYR   A CE1   1 
ATOM   7108  C  CE2   . TYR   A  1  970  ? -10.332 85.678  95.276  1.00 23.27 ? 968  TYR   A CE2   1 
ATOM   7109  C  CZ    . TYR   A  1  970  ? -10.845 85.897  96.538  1.00 26.45 ? 968  TYR   A CZ    1 
ATOM   7110  O  OH    . TYR   A  1  970  ? -11.146 87.183  96.936  1.00 33.38 ? 968  TYR   A OH    1 
ATOM   7111  N  N     . GLY   A  1  971  ? -9.115  79.121  96.055  1.00 15.17 ? 969  GLY   A N     1 
ATOM   7112  C  CA    . GLY   A  1  971  ? -9.000  77.688  95.861  1.00 17.11 ? 969  GLY   A CA    1 
ATOM   7113  C  C     . GLY   A  1  971  ? -10.052 76.937  96.640  1.00 15.50 ? 969  GLY   A C     1 
ATOM   7114  O  O     . GLY   A  1  971  ? -9.735  76.022  97.408  1.00 16.69 ? 969  GLY   A O     1 
ATOM   7115  N  N     . LEU   A  1  972  ? -11.317 77.312  96.442  1.00 14.40 ? 970  LEU   A N     1 
ATOM   7116  C  CA    . LEU   A  1  972  ? -12.385 76.715  97.233  1.00 15.82 ? 970  LEU   A CA    1 
ATOM   7117  C  C     . LEU   A  1  972  ? -13.056 75.598  96.451  1.00 17.38 ? 970  LEU   A C     1 
ATOM   7118  O  O     . LEU   A  1  972  ? -12.657 74.441  96.572  1.00 17.12 ? 970  LEU   A O     1 
ATOM   7119  C  CB    . LEU   A  1  972  ? -13.382 77.773  97.706  1.00 16.34 ? 970  LEU   A CB    1 
ATOM   7120  C  CG    . LEU   A  1  972  ? -14.398 77.294  98.741  1.00 18.80 ? 970  LEU   A CG    1 
ATOM   7121  C  CD1   . LEU   A  1  972  ? -13.728 76.591  99.920  1.00 16.11 ? 970  LEU   A CD1   1 
ATOM   7122  C  CD2   . LEU   A  1  972  ? -15.209 78.485  99.244  1.00 19.63 ? 970  LEU   A CD2   1 
ATOM   7123  N  N     . THR   A  1  973  ? -14.074 75.912  95.657  1.00 15.80 ? 971  THR   A N     1 
ATOM   7124  C  CA    . THR   A  1  973  ? -14.706 74.886  94.843  1.00 15.10 ? 971  THR   A CA    1 
ATOM   7125  C  C     . THR   A  1  973  ? -14.325 75.061  93.381  1.00 15.56 ? 971  THR   A C     1 
ATOM   7126  O  O     . THR   A  1  973  ? -13.975 76.148  92.924  1.00 16.25 ? 971  THR   A O     1 
ATOM   7127  C  CB    . THR   A  1  973  ? -16.230 74.899  94.979  1.00 13.69 ? 971  THR   A CB    1 
ATOM   7128  O  OG1   . THR   A  1  973  ? -16.725 76.183  94.588  1.00 16.10 ? 971  THR   A OG1   1 
ATOM   7129  C  CG2   . THR   A  1  973  ? -16.643 74.582  96.420  1.00 15.63 ? 971  THR   A CG2   1 
ATOM   7130  N  N     . PHE   A  1  974  ? -14.406 73.959  92.651  1.00 15.05 ? 972  PHE   A N     1 
ATOM   7131  C  CA    . PHE   A  1  974  ? -14.094 73.951  91.236  1.00 14.58 ? 972  PHE   A CA    1 
ATOM   7132  C  C     . PHE   A  1  974  ? -14.879 72.826  90.589  1.00 13.37 ? 972  PHE   A C     1 
ATOM   7133  O  O     . PHE   A  1  974  ? -14.940 71.717  91.119  1.00 16.59 ? 972  PHE   A O     1 
ATOM   7134  C  CB    . PHE   A  1  974  ? -12.604 73.684  91.022  1.00 16.21 ? 972  PHE   A CB    1 
ATOM   7135  C  CG    . PHE   A  1  974  ? -12.252 73.493  89.588  1.00 15.22 ? 972  PHE   A CG    1 
ATOM   7136  C  CD1   . PHE   A  1  974  ? -12.082 74.580  88.769  1.00 15.31 ? 972  PHE   A CD1   1 
ATOM   7137  C  CD2   . PHE   A  1  974  ? -12.174 72.221  89.042  1.00 16.45 ? 972  PHE   A CD2   1 
ATOM   7138  C  CE1   . PHE   A  1  974  ? -11.788 74.421  87.428  1.00 18.42 ? 972  PHE   A CE1   1 
ATOM   7139  C  CE2   . PHE   A  1  974  ? -11.882 72.049  87.697  1.00 15.77 ? 972  PHE   A CE2   1 
ATOM   7140  C  CZ    . PHE   A  1  974  ? -11.687 73.154  86.895  1.00 17.34 ? 972  PHE   A CZ    1 
ATOM   7141  N  N     . GLY   A  1  975  ? -15.453 73.108  89.427  1.00 15.89 ? 973  GLY   A N     1 
ATOM   7142  C  CA    . GLY   A  1  975  ? -16.222 72.127  88.698  1.00 17.10 ? 973  GLY   A CA    1 
ATOM   7143  C  C     . GLY   A  1  975  ? -15.656 71.887  87.317  1.00 13.40 ? 973  GLY   A C     1 
ATOM   7144  O  O     . GLY   A  1  975  ? -15.107 72.789  86.682  1.00 14.23 ? 973  GLY   A O     1 
ATOM   7145  N  N     . LEU   A  1  976  ? -15.811 70.656  86.853  1.00 14.61 ? 974  LEU   A N     1 
ATOM   7146  C  CA    . LEU   A  1  976  ? -15.422 70.301  85.505  1.00 14.52 ? 974  LEU   A CA    1 
ATOM   7147  C  C     . LEU   A  1  976  ? -16.525 69.449  84.913  1.00 14.42 ? 974  LEU   A C     1 
ATOM   7148  O  O     . LEU   A  1  976  ? -16.930 68.447  85.509  1.00 15.87 ? 974  LEU   A O     1 
ATOM   7149  C  CB    . LEU   A  1  976  ? -14.112 69.512  85.531  1.00 15.09 ? 974  LEU   A CB    1 
ATOM   7150  C  CG    . LEU   A  1  976  ? -13.710 68.894  84.201  1.00 16.26 ? 974  LEU   A CG    1 
ATOM   7151  C  CD1   . LEU   A  1  976  ? -13.392 70.014  83.218  1.00 19.93 ? 974  LEU   A CD1   1 
ATOM   7152  C  CD2   . LEU   A  1  976  ? -12.504 68.028  84.450  1.00 21.09 ? 974  LEU   A CD2   1 
ATOM   7153  N  N     . HIS   A  1  977  ? -16.995 69.846  83.734  1.00 15.77 ? 975  HIS   A N     1 
ATOM   7154  C  CA    . HIS   A  1  977  ? -17.981 69.080  82.990  1.00 16.96 ? 975  HIS   A CA    1 
ATOM   7155  C  C     . HIS   A  1  977  ? -17.300 68.583  81.726  1.00 16.23 ? 975  HIS   A C     1 
ATOM   7156  O  O     . HIS   A  1  977  ? -16.979 69.368  80.824  1.00 15.95 ? 975  HIS   A O     1 
ATOM   7157  C  CB    . HIS   A  1  977  ? -19.209 69.923  82.670  1.00 16.44 ? 975  HIS   A CB    1 
ATOM   7158  C  CG    . HIS   A  1  977  ? -20.292 69.797  83.688  1.00 18.82 ? 975  HIS   A CG    1 
ATOM   7159  N  ND1   . HIS   A  1  977  ? -21.416 69.027  83.483  1.00 25.01 ? 975  HIS   A ND1   1 
ATOM   7160  C  CD2   . HIS   A  1  977  ? -20.402 70.304  84.938  1.00 24.43 ? 975  HIS   A CD2   1 
ATOM   7161  C  CE1   . HIS   A  1  977  ? -22.188 69.092  84.552  1.00 21.55 ? 975  HIS   A CE1   1 
ATOM   7162  N  NE2   . HIS   A  1  977  ? -21.600 69.865  85.445  1.00 22.87 ? 975  HIS   A NE2   1 
ATOM   7163  N  N     . THR   A  1  978  ? -17.072 67.279  81.681  1.00 15.07 ? 976  THR   A N     1 
ATOM   7164  C  CA    . THR   A  1  978  ? -16.481 66.640  80.521  1.00 15.80 ? 976  THR   A CA    1 
ATOM   7165  C  C     . THR   A  1  978  ? -16.760 65.157  80.636  1.00 15.93 ? 976  THR   A C     1 
ATOM   7166  O  O     . THR   A  1  978  ? -16.926 64.627  81.733  1.00 17.67 ? 976  THR   A O     1 
ATOM   7167  C  CB    . THR   A  1  978  ? -14.960 66.859  80.455  1.00 16.58 ? 976  THR   A CB    1 
ATOM   7168  O  OG1   . THR   A  1  978  ? -14.433 66.171  79.313  1.00 17.69 ? 976  THR   A OG1   1 
ATOM   7169  C  CG2   . THR   A  1  978  ? -14.279 66.291  81.665  1.00 18.37 ? 976  THR   A CG2   1 
ATOM   7170  N  N     . ARG   A  1  979  ? -16.788 64.490  79.494  1.00 17.10 ? 977  ARG   A N     1 
ATOM   7171  C  CA    . ARG   A  1  979  ? -16.862 63.041  79.471  1.00 18.50 ? 977  ARG   A CA    1 
ATOM   7172  C  C     . ARG   A  1  979  ? -15.504 62.395  79.262  1.00 17.52 ? 977  ARG   A C     1 
ATOM   7173  O  O     . ARG   A  1  979  ? -15.416 61.164  79.254  1.00 21.41 ? 977  ARG   A O     1 
ATOM   7174  C  CB    . ARG   A  1  979  ? -17.808 62.599  78.363  1.00 17.88 ? 977  ARG   A CB    1 
ATOM   7175  C  CG    . ARG   A  1  979  ? -19.218 63.079  78.592  1.00 24.41 ? 977  ARG   A CG    1 
ATOM   7176  C  CD    . ARG   A  1  979  ? -20.090 62.758  77.425  1.00 32.50 ? 977  ARG   A CD    1 
ATOM   7177  N  NE    . ARG   A  1  979  ? -21.493 62.927  77.768  1.00 34.55 ? 977  ARG   A NE    1 
ATOM   7178  C  CZ    . ARG   A  1  979  ? -22.494 62.670  76.940  1.00 38.07 ? 977  ARG   A CZ    1 
ATOM   7179  N  NH1   . ARG   A  1  979  ? -22.275 62.238  75.707  1.00 33.11 ? 977  ARG   A NH1   1 
ATOM   7180  N  NH2   . ARG   A  1  979  ? -23.745 62.847  77.359  1.00 34.31 ? 977  ARG   A NH2   1 
ATOM   7181  N  N     . LEU   A  1  980  ? -14.451 63.186  79.128  1.00 14.44 ? 978  LEU   A N     1 
ATOM   7182  C  CA    . LEU   A  1  980  ? -13.184 62.694  78.594  1.00 15.75 ? 978  LEU   A CA    1 
ATOM   7183  C  C     . LEU   A  1  980  ? -12.174 62.494  79.719  1.00 16.38 ? 978  LEU   A C     1 
ATOM   7184  O  O     . LEU   A  1  980  ? -11.791 63.455  80.389  1.00 17.02 ? 978  LEU   A O     1 
ATOM   7185  C  CB    . LEU   A  1  980  ? -12.633 63.689  77.578  1.00 16.28 ? 978  LEU   A CB    1 
ATOM   7186  C  CG    . LEU   A  1  980  ? -13.586 63.990  76.419  1.00 16.49 ? 978  LEU   A CG    1 
ATOM   7187  C  CD1   . LEU   A  1  980  ? -12.966 65.027  75.498  1.00 19.80 ? 978  LEU   A CD1   1 
ATOM   7188  C  CD2   . LEU   A  1  980  ? -13.917 62.698  75.671  1.00 19.60 ? 978  LEU   A CD2   1 
ATOM   7189  N  N     . ASP   A  1  981  ? -11.709 61.254  79.888  1.00 17.96 ? 979  ASP   A N     1 
ATOM   7190  C  CA    . ASP   A  1  981  ? -10.769 60.958  80.973  1.00 17.39 ? 979  ASP   A CA    1 
ATOM   7191  C  C     . ASP   A  1  981  ? -9.486  61.766  80.864  1.00 16.83 ? 979  ASP   A C     1 
ATOM   7192  O  O     . ASP   A  1  981  ? -8.909  62.154  81.888  1.00 18.01 ? 979  ASP   A O     1 
ATOM   7193  C  CB    . ASP   A  1  981  ? -10.417 59.474  80.989  1.00 18.22 ? 979  ASP   A CB    1 
ATOM   7194  C  CG    . ASP   A  1  981  ? -11.550 58.612  81.477  1.00 21.39 ? 979  ASP   A CG    1 
ATOM   7195  O  OD1   . ASP   A  1  981  ? -12.474 59.148  82.115  1.00 24.71 ? 979  ASP   A OD1   1 
ATOM   7196  O  OD2   . ASP   A  1  981  ? -11.501 57.387  81.221  1.00 23.51 ? 979  ASP   A OD2   1 
ATOM   7197  N  N     . GLU   A  1  982  ? -8.982  61.974  79.645  1.00 16.88 ? 980  GLU   A N     1 
ATOM   7198  C  CA    . GLU   A  1  982  ? -7.763  62.754  79.502  1.00 17.25 ? 980  GLU   A CA    1 
ATOM   7199  C  C     . GLU   A  1  982  ? -7.957  64.153  80.067  1.00 17.21 ? 980  GLU   A C     1 
ATOM   7200  O  O     . GLU   A  1  982  ? -7.072  64.693  80.738  1.00 18.02 ? 980  GLU   A O     1 
ATOM   7201  C  CB    . GLU   A  1  982  ? -7.352  62.847  78.040  1.00 19.99 ? 980  GLU   A CB    1 
ATOM   7202  C  CG    . GLU   A  1  982  ? -6.052  63.628  77.881  1.00 21.90 ? 980  GLU   A CG    1 
ATOM   7203  C  CD    . GLU   A  1  982  ? -5.792  64.083  76.458  1.00 29.66 ? 980  GLU   A CD    1 
ATOM   7204  O  OE1   . GLU   A  1  982  ? -6.723  64.625  75.821  1.00 33.07 ? 980  GLU   A OE1   1 
ATOM   7205  O  OE2   . GLU   A  1  982  ? -4.650  63.907  75.984  1.00 27.05 ? 980  GLU   A OE2   1 
ATOM   7206  N  N     . THR   A  1  983  ? -9.126  64.740  79.823  1.00 16.02 ? 981  THR   A N     1 
ATOM   7207  C  CA    . THR   A  1  983  ? -9.371  66.093  80.293  1.00 15.46 ? 981  THR   A CA    1 
ATOM   7208  C  C     . THR   A  1  983  ? -9.559  66.110  81.799  1.00 16.53 ? 981  THR   A C     1 
ATOM   7209  O  O     . THR   A  1  983  ? -9.068  67.021  82.480  1.00 17.18 ? 981  THR   A O     1 
ATOM   7210  C  CB    . THR   A  1  983  ? -10.595 66.654  79.572  1.00 16.97 ? 981  THR   A CB    1 
ATOM   7211  O  OG1   . THR   A  1  983  ? -10.308 66.738  78.169  1.00 19.54 ? 981  THR   A OG1   1 
ATOM   7212  C  CG2   . THR   A  1  983  ? -10.937 68.044  80.102  1.00 18.22 ? 981  THR   A CG2   1 
ATOM   7213  N  N     . ILE   A  1  984  ? -10.245 65.096  82.338  1.00 15.55 ? 982  ILE   A N     1 
ATOM   7214  C  CA    . ILE   A  1  984  ? -10.381 64.984  83.789  1.00 16.46 ? 982  ILE   A CA    1 
ATOM   7215  C  C     . ILE   A  1  984  ? -9.011  64.865  84.437  1.00 17.17 ? 982  ILE   A C     1 
ATOM   7216  O  O     . ILE   A  1  984  ? -8.717  65.546  85.423  1.00 16.89 ? 982  ILE   A O     1 
ATOM   7217  C  CB    . ILE   A  1  984  ? -11.279 63.797  84.170  1.00 16.52 ? 982  ILE   A CB    1 
ATOM   7218  C  CG1   . ILE   A  1  984  ? -12.708 64.052  83.699  1.00 21.53 ? 982  ILE   A CG1   1 
ATOM   7219  C  CG2   . ILE   A  1  984  ? -11.241 63.566  85.678  1.00 18.54 ? 982  ILE   A CG2   1 
ATOM   7220  C  CD1   . ILE   A  1  984  ? -13.606 62.833  83.756  1.00 20.59 ? 982  ILE   A CD1   1 
ATOM   7221  N  N     . ALA   A  1  985  ? -8.164  63.975  83.910  1.00 15.04 ? 983  ALA   A N     1 
ATOM   7222  C  CA    . ALA   A  1  985  ? -6.851  63.774  84.519  1.00 17.44 ? 983  ALA   A CA    1 
ATOM   7223  C  C     . ALA   A  1  985  ? -6.044  65.062  84.474  1.00 16.27 ? 983  ALA   A C     1 
ATOM   7224  O  O     . ALA   A  1  985  ? -5.454  65.473  85.482  1.00 19.14 ? 983  ALA   A O     1 
ATOM   7225  C  CB    . ALA   A  1  985  ? -6.113  62.635  83.811  1.00 19.65 ? 983  ALA   A CB    1 
ATOM   7226  N  N     . HIS   A  1  986  ? -6.028  65.722  83.315  1.00 17.18 ? 984  HIS   A N     1 
ATOM   7227  C  CA    . HIS   A  1  986  ? -5.281  66.963  83.156  1.00 18.36 ? 984  HIS   A CA    1 
ATOM   7228  C  C     . HIS   A  1  986  ? -5.783  68.028  84.118  1.00 18.69 ? 984  HIS   A C     1 
ATOM   7229  O  O     . HIS   A  1  986  ? -5.028  68.540  84.949  1.00 18.25 ? 984  HIS   A O     1 
ATOM   7230  C  CB    . HIS   A  1  986  ? -5.417  67.424  81.709  1.00 17.72 ? 984  HIS   A CB    1 
ATOM   7231  C  CG    . HIS   A  1  986  ? -4.895  68.800  81.436  1.00 19.68 ? 984  HIS   A CG    1 
ATOM   7232  N  ND1   . HIS   A  1  986  ? -5.156  69.458  80.256  1.00 25.94 ? 984  HIS   A ND1   1 
ATOM   7233  C  CD2   . HIS   A  1  986  ? -4.122  69.637  82.169  1.00 20.90 ? 984  HIS   A CD2   1 
ATOM   7234  C  CE1   . HIS   A  1  986  ? -4.578  70.646  80.276  1.00 29.46 ? 984  HIS   A CE1   1 
ATOM   7235  N  NE2   . HIS   A  1  986  ? -3.953  70.784  81.432  1.00 23.20 ? 984  HIS   A NE2   1 
ATOM   7236  N  N     . VAL   A  1  987  ? -7.076  68.348  84.043  1.00 17.85 ? 985  VAL   A N     1 
ATOM   7237  C  CA    . VAL   A  1  987  ? -7.604  69.463  84.820  1.00 18.14 ? 985  VAL   A CA    1 
ATOM   7238  C  C     . VAL   A  1  987  ? -7.486  69.193  86.314  1.00 18.47 ? 985  VAL   A C     1 
ATOM   7239  O  O     . VAL   A  1  987  ? -7.080  70.072  87.086  1.00 18.62 ? 985  VAL   A O     1 
ATOM   7240  C  CB    . VAL   A  1  987  ? -9.050  69.773  84.400  1.00 14.58 ? 985  VAL   A CB    1 
ATOM   7241  C  CG1   . VAL   A  1  987  ? -9.653  70.806  85.345  1.00 15.83 ? 985  VAL   A CG1   1 
ATOM   7242  C  CG2   . VAL   A  1  987  ? -9.077  70.295  82.976  1.00 18.96 ? 985  VAL   A CG2   1 
ATOM   7243  N  N     . THR   A  1  988  ? -7.846  67.987  86.757  1.00 17.75 ? 986  THR   A N     1 
ATOM   7244  C  CA    . THR   A  1  988  ? -7.842  67.759  88.200  1.00 18.95 ? 986  THR   A CA    1 
ATOM   7245  C  C     . THR   A  1  988  ? -6.427  67.718  88.753  1.00 23.32 ? 986  THR   A C     1 
ATOM   7246  O  O     . THR   A  1  988  ? -6.218  68.011  89.938  1.00 23.08 ? 986  THR   A O     1 
ATOM   7247  C  CB    . THR   A  1  988  ? -8.622  66.498  88.583  1.00 21.19 ? 986  THR   A CB    1 
ATOM   7248  O  OG1   . THR   A  1  988  ? -8.010  65.360  87.980  1.00 22.14 ? 986  THR   A OG1   1 
ATOM   7249  C  CG2   . THR   A  1  988  ? -10.079 66.600  88.132  1.00 19.96 ? 986  THR   A CG2   1 
ATOM   7250  N  N     . SER   A  1  989  ? -5.449  67.369  87.922  1.00 19.66 ? 987  SER   A N     1 
ATOM   7251  C  CA    . SER   A  1  989  ? -4.067  67.351  88.380  1.00 22.85 ? 987  SER   A CA    1 
ATOM   7252  C  C     . SER   A  1  989  ? -3.480  68.751  88.480  1.00 25.86 ? 987  SER   A C     1 
ATOM   7253  O  O     . SER   A  1  989  ? -2.542  68.962  89.256  1.00 31.11 ? 987  SER   A O     1 
ATOM   7254  C  CB    . SER   A  1  989  ? -3.202  66.455  87.477  1.00 24.10 ? 987  SER   A CB    1 
ATOM   7255  O  OG    . SER   A  1  989  ? -3.006  67.020  86.194  1.00 29.39 ? 987  SER   A OG    1 
ATOM   7256  N  N     . ARG   A  1  990  ? -4.025  69.711  87.738  1.00 18.43 ? 988  ARG   A N     1 
ATOM   7257  C  CA    . ARG   A  1  990  ? -3.442  71.041  87.656  1.00 20.80 ? 988  ARG   A CA    1 
ATOM   7258  C  C     . ARG   A  1  990  ? -4.190  72.077  88.474  1.00 19.43 ? 988  ARG   A C     1 
ATOM   7259  O  O     . ARG   A  1  990  ? -3.588  73.071  88.897  1.00 21.14 ? 988  ARG   A O     1 
ATOM   7260  C  CB    . ARG   A  1  990  ? -3.378  71.494  86.196  1.00 21.34 ? 988  ARG   A CB    1 
ATOM   7261  C  CG    . ARG   A  1  990  ? -2.622  70.522  85.307  1.00 29.78 ? 988  ARG   A CG    1 
ATOM   7262  C  CD    . ARG   A  1  990  ? -1.124  70.728  85.388  1.00 32.31 ? 988  ARG   A CD    1 
ATOM   7263  N  NE    . ARG   A  1  990  ? -0.671  71.692  84.392  1.00 29.77 ? 988  ARG   A NE    1 
ATOM   7264  C  CZ    . ARG   A  1  990  ? 0.572   72.144  84.304  1.00 31.06 ? 988  ARG   A CZ    1 
ATOM   7265  N  NH1   . ARG   A  1  990  ? 1.496   71.798  85.186  1.00 31.40 ? 988  ARG   A NH1   1 
ATOM   7266  N  NH2   . ARG   A  1  990  ? 0.892   72.970  83.310  1.00 30.52 ? 988  ARG   A NH2   1 
ATOM   7267  N  N     . ILE   A  1  991  ? -5.491  71.878  88.684  1.00 18.17 ? 989  ILE   A N     1 
ATOM   7268  C  CA    . ILE   A  1  991  ? -6.264  72.821  89.471  1.00 17.16 ? 989  ILE   A CA    1 
ATOM   7269  C  C     . ILE   A  1  991  ? -5.828  72.725  90.925  1.00 19.07 ? 989  ILE   A C     1 
ATOM   7270  O  O     . ILE   A  1  991  ? -5.432  71.659  91.413  1.00 20.55 ? 989  ILE   A O     1 
ATOM   7271  C  CB    . ILE   A  1  991  ? -7.769  72.530  89.304  1.00 17.70 ? 989  ILE   A CB    1 
ATOM   7272  C  CG1   . ILE   A  1  991  ? -8.599  73.695  89.851  1.00 20.37 ? 989  ILE   A CG1   1 
ATOM   7273  C  CG2   . ILE   A  1  991  ? -8.145  71.229  89.977  1.00 18.98 ? 989  ILE   A CG2   1 
ATOM   7274  C  CD1   . ILE   A  1  991  ? -8.515  74.922  88.977  1.00 22.37 ? 989  ILE   A CD1   1 
ATOM   7275  N  N     . LYS   A  1  992  ? -5.866  73.855  91.619  1.00 17.25 ? 990  LYS   A N     1 
ATOM   7276  C  CA    . LYS   A  1  992  ? -5.502  73.918  93.030  1.00 19.01 ? 990  LYS   A CA    1 
ATOM   7277  C  C     . LYS   A  1  992  ? -6.711  74.434  93.800  1.00 18.31 ? 990  LYS   A C     1 
ATOM   7278  O  O     . LYS   A  1  992  ? -6.837  75.636  94.041  1.00 20.82 ? 990  LYS   A O     1 
ATOM   7279  C  CB    . LYS   A  1  992  ? -4.306  74.818  93.231  1.00 19.37 ? 990  LYS   A CB    1 
ATOM   7280  C  CG    . LYS   A  1  992  ? -3.062  74.393  92.461  1.00 24.55 ? 990  LYS   A CG    1 
ATOM   7281  C  CD    . LYS   A  1  992  ? -1.962  75.447  92.602  1.00 33.46 ? 990  LYS   A CD    1 
ATOM   7282  C  CE    . LYS   A  1  992  ? -0.713  75.079  91.809  1.00 37.72 ? 990  LYS   A CE    1 
ATOM   7283  N  NZ    . LYS   A  1  992  ? 0.239   76.229  91.710  1.00 49.17 ? 990  LYS   A NZ    1 
ATOM   7284  N  N     . ALA   A  1  993  ? -7.595  73.524  94.184  1.00 18.39 ? 991  ALA   A N     1 
ATOM   7285  C  CA    . ALA   A  1  993  ? -8.778  73.898  94.945  1.00 17.28 ? 991  ALA   A CA    1 
ATOM   7286  C  C     . ALA   A  1  993  ? -9.107  72.760  95.887  1.00 16.62 ? 991  ALA   A C     1 
ATOM   7287  O  O     . ALA   A  1  993  ? -8.759  71.606  95.635  1.00 19.26 ? 991  ALA   A O     1 
ATOM   7288  C  CB    . ALA   A  1  993  ? -9.968  74.173  94.028  1.00 17.21 ? 991  ALA   A CB    1 
ATOM   7289  N  N     . GLY   A  1  994  ? -9.829  73.092  96.963  1.00 15.55 ? 992  GLY   A N     1 
ATOM   7290  C  CA    . GLY   A  1  994  ? -10.064 72.110  98.002  1.00 18.05 ? 992  GLY   A CA    1 
ATOM   7291  C  C     . GLY   A  1  994  ? -11.198 71.154  97.705  1.00 15.74 ? 992  GLY   A C     1 
ATOM   7292  O  O     . GLY   A  1  994  ? -11.198 70.025  98.203  1.00 16.34 ? 992  GLY   A O     1 
ATOM   7293  N  N     . ASN   A  1  995  ? -12.166 71.574  96.899  1.00 16.03 ? 993  ASN   A N     1 
ATOM   7294  C  CA    . ASN   A  1  995  ? -13.351 70.769  96.625  1.00 15.97 ? 993  ASN   A CA    1 
ATOM   7295  C  C     . ASN   A  1  995  ? -13.577 70.759  95.126  1.00 16.36 ? 993  ASN   A C     1 
ATOM   7296  O  O     . ASN   A  1  995  ? -13.879 71.799  94.534  1.00 15.30 ? 993  ASN   A O     1 
ATOM   7297  C  CB    . ASN   A  1  995  ? -14.572 71.316  97.363  1.00 16.17 ? 993  ASN   A CB    1 
ATOM   7298  C  CG    . ASN   A  1  995  ? -14.588 70.896  98.806  1.00 17.03 ? 993  ASN   A CG    1 
ATOM   7299  O  OD1   . ASN   A  1  995  ? -13.956 71.523  99.649  1.00 17.73 ? 993  ASN   A OD1   1 
ATOM   7300  N  ND2   . ASN   A  1  995  ? -15.288 69.807  99.095  1.00 16.78 ? 993  ASN   A ND2   1 
ATOM   7301  N  N     . LEU   A  1  996  ? -13.387 69.602  94.515  1.00 14.65 ? 994  LEU   A N     1 
ATOM   7302  C  CA    . LEU   A  1  996  ? -13.577 69.440  93.084  1.00 16.18 ? 994  LEU   A CA    1 
ATOM   7303  C  C     . LEU   A  1  996  ? -14.851 68.658  92.824  1.00 14.05 ? 994  LEU   A C     1 
ATOM   7304  O  O     . LEU   A  1  996  ? -15.224 67.773  93.597  1.00 14.71 ? 994  LEU   A O     1 
ATOM   7305  C  CB    . LEU   A  1  996  ? -12.415 68.673  92.456  1.00 15.45 ? 994  LEU   A CB    1 
ATOM   7306  C  CG    . LEU   A  1  996  ? -11.032 69.092  92.942  1.00 16.40 ? 994  LEU   A CG    1 
ATOM   7307  C  CD1   . LEU   A  1  996  ? -9.970  68.213  92.292  1.00 21.04 ? 994  LEU   A CD1   1 
ATOM   7308  C  CD2   . LEU   A  1  996  ? -10.786 70.550  92.641  1.00 18.37 ? 994  LEU   A CD2   1 
ATOM   7309  N  N     . TYR   A  1  997  ? -15.512 68.992  91.717  1.00 13.51 ? 995  TYR   A N     1 
ATOM   7310  C  CA    . TYR   A  1  997  ? -16.776 68.364  91.367  1.00 15.00 ? 995  TYR   A CA    1 
ATOM   7311  C  C     . TYR   A  1  997  ? -16.751 68.081  89.883  1.00 14.90 ? 995  TYR   A C     1 
ATOM   7312  O  O     . TYR   A  1  997  ? -16.459 68.973  89.085  1.00 16.28 ? 995  TYR   A O     1 
ATOM   7313  C  CB    . TYR   A  1  997  ? -17.957 69.273  91.691  1.00 14.41 ? 995  TYR   A CB    1 
ATOM   7314  C  CG    . TYR   A  1  997  ? -17.975 69.715  93.126  1.00 15.27 ? 995  TYR   A CG    1 
ATOM   7315  C  CD1   . TYR   A  1  997  ? -17.269 70.839  93.520  1.00 16.88 ? 995  TYR   A CD1   1 
ATOM   7316  C  CD2   . TYR   A  1  997  ? -18.685 69.004  94.080  1.00 18.12 ? 995  TYR   A CD2   1 
ATOM   7317  C  CE1   . TYR   A  1  997  ? -17.266 71.256  94.825  1.00 19.38 ? 995  TYR   A CE1   1 
ATOM   7318  C  CE2   . TYR   A  1  997  ? -18.698 69.420  95.403  1.00 18.63 ? 995  TYR   A CE2   1 
ATOM   7319  C  CZ    . TYR   A  1  997  ? -17.984 70.545  95.759  1.00 18.49 ? 995  TYR   A CZ    1 
ATOM   7320  O  OH    . TYR   A  1  997  ? -17.992 70.966  97.075  1.00 22.51 ? 995  TYR   A OH    1 
ATOM   7321  N  N     . ILE   A  1  998  ? -17.028 66.837  89.520  1.00 14.28 ? 996  ILE   A N     1 
ATOM   7322  C  CA    A ILE   A  1  998  ? -16.970 66.389  88.135  0.47 15.56 ? 996  ILE   A CA    1 
ATOM   7323  C  CA    B ILE   A  1  998  ? -16.973 66.399  88.134  0.53 15.55 ? 996  ILE   A CA    1 
ATOM   7324  C  C     . ILE   A  1  998  ? -18.382 66.029  87.697  1.00 15.45 ? 996  ILE   A C     1 
ATOM   7325  O  O     . ILE   A  1  998  ? -19.002 65.131  88.271  1.00 14.92 ? 996  ILE   A O     1 
ATOM   7326  C  CB    A ILE   A  1  998  ? -16.034 65.185  87.975  0.47 16.60 ? 996  ILE   A CB    1 
ATOM   7327  C  CB    B ILE   A  1  998  ? -15.999 65.230  87.950  0.53 16.61 ? 996  ILE   A CB    1 
ATOM   7328  C  CG1   A ILE   A  1  998  ? -14.687 65.461  88.646  0.47 17.69 ? 996  ILE   A CG1   1 
ATOM   7329  C  CG1   B ILE   A  1  998  ? -14.572 65.699  88.250  0.53 17.27 ? 996  ILE   A CG1   1 
ATOM   7330  C  CG2   A ILE   A  1  998  ? -15.856 64.862  86.492  0.47 16.76 ? 996  ILE   A CG2   1 
ATOM   7331  C  CG2   B ILE   A  1  998  ? -16.118 64.665  86.533  0.53 16.51 ? 996  ILE   A CG2   1 
ATOM   7332  C  CD1   A ILE   A  1  998  ? -13.871 66.528  87.959  0.47 16.87 ? 996  ILE   A CD1   1 
ATOM   7333  C  CD1   B ILE   A  1  998  ? -13.534 64.603  88.199  0.53 19.02 ? 996  ILE   A CD1   1 
ATOM   7334  N  N     . ASN   A  1  999  ? -18.876 66.724  86.676  1.00 14.74 ? 997  ASN   A N     1 
ATOM   7335  C  CA    . ASN   A  1  999  ? -20.168 66.421  86.049  1.00 15.24 ? 997  ASN   A CA    1 
ATOM   7336  C  C     . ASN   A  1  999  ? -21.344 66.587  87.006  1.00 14.29 ? 997  ASN   A C     1 
ATOM   7337  O  O     . ASN   A  1  999  ? -22.335 65.853  86.950  1.00 16.11 ? 997  ASN   A O     1 
ATOM   7338  C  CB    . ASN   A  1  999  ? -20.152 65.056  85.369  1.00 14.15 ? 997  ASN   A CB    1 
ATOM   7339  C  CG    . ASN   A  1  999  ? -19.197 65.035  84.205  1.00 15.03 ? 997  ASN   A CG    1 
ATOM   7340  O  OD1   . ASN   A  1  999  ? -19.009 66.059  83.553  1.00 17.26 ? 997  ASN   A OD1   1 
ATOM   7341  N  ND2   . ASN   A  1  999  ? -18.595 63.888  83.937  1.00 16.97 ? 997  ASN   A ND2   1 
ATOM   7342  N  N     . ARG   A  1  1000 ? -21.247 67.587  87.870  1.00 15.99 ? 998  ARG   A N     1 
ATOM   7343  C  CA    . ARG   A  1  1000 ? -22.299 67.875  88.833  1.00 15.97 ? 998  ARG   A CA    1 
ATOM   7344  C  C     . ARG   A  1  1000 ? -22.159 69.331  89.247  1.00 17.07 ? 998  ARG   A C     1 
ATOM   7345  O  O     . ARG   A  1  1000 ? -21.244 70.032  88.816  1.00 17.43 ? 998  ARG   A O     1 
ATOM   7346  C  CB    . ARG   A  1  1000 ? -22.217 66.944  90.041  1.00 16.43 ? 998  ARG   A CB    1 
ATOM   7347  C  CG    . ARG   A  1  1000 ? -20.817 66.877  90.650  1.00 15.20 ? 998  ARG   A CG    1 
ATOM   7348  C  CD    . ARG   A  1  1000 ? -20.898 66.491  92.107  1.00 16.75 ? 998  ARG   A CD    1 
ATOM   7349  N  NE    . ARG   A  1  1000 ? -21.575 67.528  92.870  1.00 16.31 ? 998  ARG   A NE    1 
ATOM   7350  C  CZ    . ARG   A  1  1000 ? -21.920 67.420  94.144  1.00 18.70 ? 998  ARG   A CZ    1 
ATOM   7351  N  NH1   . ARG   A  1  1000 ? -21.660 66.322  94.845  1.00 18.99 ? 998  ARG   A NH1   1 
ATOM   7352  N  NH2   . ARG   A  1  1000 ? -22.524 68.444  94.737  1.00 17.70 ? 998  ARG   A NH2   1 
ATOM   7353  N  N     . ASN   A  1  1001 ? -23.071 69.783  90.101  1.00 16.49 ? 999  ASN   A N     1 
ATOM   7354  C  CA    . ASN   A  1  1001 ? -22.934 71.132  90.629  1.00 17.31 ? 999  ASN   A CA    1 
ATOM   7355  C  C     . ASN   A  1  1001 ? -21.745 71.196  91.594  1.00 18.33 ? 999  ASN   A C     1 
ATOM   7356  O  O     . ASN   A  1  1001 ? -21.186 70.179  91.994  1.00 16.20 ? 999  ASN   A O     1 
ATOM   7357  C  CB    . ASN   A  1  1001 ? -24.251 71.601  91.259  1.00 18.52 ? 999  ASN   A CB    1 
ATOM   7358  C  CG    . ASN   A  1  1001 ? -24.586 70.883  92.554  1.00 21.44 ? 999  ASN   A CG    1 
ATOM   7359  O  OD1   . ASN   A  1  1001 ? -23.742 70.697  93.424  1.00 20.06 ? 999  ASN   A OD1   1 
ATOM   7360  N  ND2   . ASN   A  1  1001 ? -25.850 70.503  92.697  1.00 27.22 ? 999  ASN   A ND2   1 
ATOM   7361  N  N     . ILE   A  1  1002 ? -21.369 72.411  91.973  1.00 15.14 ? 1000 ILE   A N     1 
ATOM   7362  C  CA    . ILE   A  1  1002 ? -20.176 72.625  92.785  1.00 16.13 ? 1000 ILE   A CA    1 
ATOM   7363  C  C     . ILE   A  1  1002 ? -20.529 73.091  94.189  1.00 17.29 ? 1000 ILE   A C     1 
ATOM   7364  O  O     . ILE   A  1  1002 ? -19.685 73.650  94.883  1.00 18.36 ? 1000 ILE   A O     1 
ATOM   7365  C  CB    . ILE   A  1  1002 ? -19.162 73.563  92.108  1.00 15.57 ? 1000 ILE   A CB    1 
ATOM   7366  C  CG1   . ILE   A  1  1002 ? -19.676 75.012  92.049  1.00 17.76 ? 1000 ILE   A CG1   1 
ATOM   7367  C  CG2   . ILE   A  1  1002 ? -18.796 73.019  90.738  1.00 16.49 ? 1000 ILE   A CG2   1 
ATOM   7368  C  CD1   . ILE   A  1  1002 ? -18.622 75.999  91.573  1.00 17.19 ? 1000 ILE   A CD1   1 
ATOM   7369  N  N     . ILE   A  1  1003 ? -21.760 72.871  94.625  1.00 16.73 ? 1001 ILE   A N     1 
ATOM   7370  C  CA    . ILE   A  1  1003 ? -22.174 73.389  95.919  1.00 19.83 ? 1001 ILE   A CA    1 
ATOM   7371  C  C     . ILE   A  1  1003 ? -22.324 72.273  96.951  1.00 29.16 ? 1001 ILE   A C     1 
ATOM   7372  O  O     . ILE   A  1  1003 ? -22.926 72.473  98.015  1.00 26.74 ? 1001 ILE   A O     1 
ATOM   7373  C  CB    . ILE   A  1  1003 ? -23.393 74.316  95.812  1.00 18.47 ? 1001 ILE   A CB    1 
ATOM   7374  C  CG1   . ILE   A  1  1003 ? -24.590 73.609  95.172  1.00 22.79 ? 1001 ILE   A CG1   1 
ATOM   7375  C  CG2   . ILE   A  1  1003 ? -23.010 75.573  95.021  1.00 18.45 ? 1001 ILE   A CG2   1 
ATOM   7376  C  CD1   . ILE   A  1  1003 ? -25.870 74.427  95.256  1.00 27.23 ? 1001 ILE   A CD1   1 
ATOM   7377  N  N     . GLY   A  1  1004 ? -21.710 71.122  96.669  1.00 29.06 ? 1002 GLY   A N     1 
ATOM   7378  C  CA    . GLY   A  1  1004 ? -21.788 69.982  97.563  1.00 22.88 ? 1002 GLY   A CA    1 
ATOM   7379  C  C     . GLY   A  1  1004 ? -20.840 70.134  98.728  1.00 26.73 ? 1002 GLY   A C     1 
ATOM   7380  O  O     . GLY   A  1  1004 ? -19.646 70.399  98.554  1.00 27.26 ? 1002 GLY   A O     1 
ATOM   7381  N  N     . ALA   A  1  1005 ? -21.373 69.989  99.926  1.00 20.69 ? 1003 ALA   A N     1 
ATOM   7382  C  CA    . ALA   A  1  1005 ? -20.547 70.016  101.118 1.00 26.94 ? 1003 ALA   A CA    1 
ATOM   7383  C  C     . ALA   A  1  1005 ? -21.040 68.974  102.097 1.00 26.85 ? 1003 ALA   A C     1 
ATOM   7384  O  O     . ALA   A  1  1005 ? -21.077 69.211  103.309 1.00 29.10 ? 1003 ALA   A O     1 
ATOM   7385  C  CB    . ALA   A  1  1005 ? -20.542 71.401  101.764 1.00 25.49 ? 1003 ALA   A CB    1 
ATOM   7386  N  N     . VAL   A  1  1006 ? -21.425 67.802  101.589 1.00 21.57 ? 1004 VAL   A N     1 
ATOM   7387  C  CA    . VAL   A  1  1006 ? -21.997 66.795  102.473 1.00 19.43 ? 1004 VAL   A CA    1 
ATOM   7388  C  C     . VAL   A  1  1006 ? -20.951 66.404  103.501 1.00 18.76 ? 1004 VAL   A C     1 
ATOM   7389  O  O     . VAL   A  1  1006 ? -19.849 65.962  103.156 1.00 18.33 ? 1004 VAL   A O     1 
ATOM   7390  C  CB    . VAL   A  1  1006 ? -22.523 65.591  101.691 1.00 19.46 ? 1004 VAL   A CB    1 
ATOM   7391  C  CG1   . VAL   A  1  1006 ? -22.966 64.504  102.651 1.00 20.91 ? 1004 VAL   A CG1   1 
ATOM   7392  C  CG2   . VAL   A  1  1006 ? -23.695 66.023  100.815 1.00 18.15 ? 1004 VAL   A CG2   1 
ATOM   7393  N  N     . VAL   A  1  1007 ? -21.288 66.603  104.773 1.00 17.60 ? 1005 VAL   A N     1 
ATOM   7394  C  CA    . VAL   A  1  1007 ? -20.347 66.366  105.856 1.00 16.67 ? 1005 VAL   A CA    1 
ATOM   7395  C  C     . VAL   A  1  1007 ? -19.855 64.931  105.793 1.00 17.91 ? 1005 VAL   A C     1 
ATOM   7396  O  O     . VAL   A  1  1007 ? -20.646 63.996  105.633 1.00 19.54 ? 1005 VAL   A O     1 
ATOM   7397  C  CB    . VAL   A  1  1007 ? -21.041 66.674  107.192 1.00 17.29 ? 1005 VAL   A CB    1 
ATOM   7398  C  CG1   . VAL   A  1  1007 ? -20.158 66.277  108.358 1.00 19.97 ? 1005 VAL   A CG1   1 
ATOM   7399  C  CG2   . VAL   A  1  1007 ? -21.370 68.138  107.272 1.00 20.32 ? 1005 VAL   A CG2   1 
ATOM   7400  N  N     . GLY   A  1  1008 ? -18.537 64.747  105.913 1.00 17.83 ? 1006 GLY   A N     1 
ATOM   7401  C  CA    . GLY   A  1  1008 ? -17.964 63.415  105.888 1.00 17.20 ? 1006 GLY   A CA    1 
ATOM   7402  C  C     . GLY   A  1  1008 ? -17.987 62.746  104.532 1.00 18.66 ? 1006 GLY   A C     1 
ATOM   7403  O  O     . GLY   A  1  1008 ? -17.532 61.605  104.409 1.00 20.47 ? 1006 GLY   A O     1 
ATOM   7404  N  N     . VAL   A  1  1009 ? -18.497 63.418  103.509 1.00 17.73 ? 1007 VAL   A N     1 
ATOM   7405  C  CA    . VAL   A  1  1009 ? -18.583 62.875  102.160 1.00 19.44 ? 1007 VAL   A CA    1 
ATOM   7406  C  C     . VAL   A  1  1009 ? -17.854 63.767  101.169 1.00 17.01 ? 1007 VAL   A C     1 
ATOM   7407  O  O     . VAL   A  1  1009 ? -17.030 63.295  100.378 1.00 18.27 ? 1007 VAL   A O     1 
ATOM   7408  C  CB    . VAL   A  1  1009 ? -20.048 62.657  101.734 1.00 19.02 ? 1007 VAL   A CB    1 
ATOM   7409  C  CG1   . VAL   A  1  1009 ? -20.100 62.083  100.339 1.00 18.67 ? 1007 VAL   A CG1   1 
ATOM   7410  C  CG2   . VAL   A  1  1009 ? -20.747 61.714  102.704 1.00 17.26 ? 1007 VAL   A CG2   1 
ATOM   7411  N  N     . GLN   A  1  1010 ? -18.116 65.075  101.224 1.00 18.19 ? 1008 GLN   A N     1 
ATOM   7412  C  CA    . GLN   A  1  1010 ? -17.254 66.091  100.626 1.00 17.80 ? 1008 GLN   A CA    1 
ATOM   7413  C  C     . GLN   A  1  1010 ? -16.817 66.983  101.778 1.00 17.82 ? 1008 GLN   A C     1 
ATOM   7414  O  O     . GLN   A  1  1010 ? -17.363 68.076  101.968 1.00 21.58 ? 1008 GLN   A O     1 
ATOM   7415  C  CB    . GLN   A  1  1010 ? -17.974 66.922  99.567  1.00 18.92 ? 1008 GLN   A CB    1 
ATOM   7416  C  CG    . GLN   A  1  1010 ? -18.487 66.117  98.383  1.00 19.68 ? 1008 GLN   A CG    1 
ATOM   7417  C  CD    . GLN   A  1  1010 ? -19.982 65.871  98.453  1.00 21.15 ? 1008 GLN   A CD    1 
ATOM   7418  O  OE1   . GLN   A  1  1010 ? -20.742 66.700  98.972  1.00 20.30 ? 1008 GLN   A OE1   1 
ATOM   7419  N  NE2   . GLN   A  1  1010 ? -20.415 64.725  97.936  1.00 19.42 ? 1008 GLN   A NE2   1 
ATOM   7420  N  N     . PRO   A  1  1011 ? -15.867 66.531  102.593 1.00 18.54 ? 1009 PRO   A N     1 
ATOM   7421  C  CA    . PRO   A  1  1011 ? -15.249 67.439  103.567 1.00 19.11 ? 1009 PRO   A CA    1 
ATOM   7422  C  C     . PRO   A  1  1011 ? -14.882 68.720  102.847 1.00 15.59 ? 1009 PRO   A C     1 
ATOM   7423  O  O     . PRO   A  1  1011 ? -14.339 68.695  101.747 1.00 16.24 ? 1009 PRO   A O     1 
ATOM   7424  C  CB    . PRO   A  1  1011 ? -14.002 66.679  104.008 1.00 17.67 ? 1009 PRO   A CB    1 
ATOM   7425  C  CG    . PRO   A  1  1011 ? -14.366 65.242  103.829 1.00 18.27 ? 1009 PRO   A CG    1 
ATOM   7426  C  CD    . PRO   A  1  1011 ? -15.243 65.201  102.592 1.00 18.00 ? 1009 PRO   A CD    1 
ATOM   7427  N  N     . PHE   A  1  1012 ? -15.238 69.845  103.439 1.00 16.35 ? 1010 PHE   A N     1 
ATOM   7428  C  CA    . PHE   A  1  1012 ? -15.324 71.084  102.695 1.00 16.54 ? 1010 PHE   A CA    1 
ATOM   7429  C  C     . PHE   A  1  1012 ? -14.308 72.085  103.202 1.00 17.67 ? 1010 PHE   A C     1 
ATOM   7430  O  O     . PHE   A  1  1012 ? -14.199 72.312  104.414 1.00 18.19 ? 1010 PHE   A O     1 
ATOM   7431  C  CB    . PHE   A  1  1012 ? -16.723 71.700  102.806 1.00 16.96 ? 1010 PHE   A CB    1 
ATOM   7432  C  CG    . PHE   A  1  1012 ? -16.891 72.895  101.936 1.00 16.03 ? 1010 PHE   A CG    1 
ATOM   7433  C  CD1   . PHE   A  1  1012 ? -17.167 72.740  100.589 1.00 19.88 ? 1010 PHE   A CD1   1 
ATOM   7434  C  CD2   . PHE   A  1  1012 ? -16.702 74.177  102.440 1.00 19.15 ? 1010 PHE   A CD2   1 
ATOM   7435  C  CE1   . PHE   A  1  1012 ? -17.283 73.842  99.764  1.00 16.23 ? 1010 PHE   A CE1   1 
ATOM   7436  C  CE2   . PHE   A  1  1012 ? -16.829 75.286  101.622 1.00 19.42 ? 1010 PHE   A CE2   1 
ATOM   7437  C  CZ    . PHE   A  1  1012 ? -17.114 75.122  100.282 1.00 16.58 ? 1010 PHE   A CZ    1 
ATOM   7438  N  N     . GLY   A  1  1013 ? -13.614 72.717  102.282 1.00 15.96 ? 1011 GLY   A N     1 
ATOM   7439  C  CA    . GLY   A  1  1013 ? -12.709 73.779  102.657 1.00 17.40 ? 1011 GLY   A CA    1 
ATOM   7440  C  C     . GLY   A  1  1013 ? -11.612 73.874  101.634 1.00 16.89 ? 1011 GLY   A C     1 
ATOM   7441  O  O     . GLY   A  1  1013 ? -11.192 72.877  101.043 1.00 17.54 ? 1011 GLY   A O     1 
ATOM   7442  N  N     . GLY   A  1  1014 ? -11.134 75.095  101.448 1.00 18.87 ? 1012 GLY   A N     1 
ATOM   7443  C  CA    . GLY   A  1  1014 ? -10.170 75.380  100.419 1.00 18.95 ? 1012 GLY   A CA    1 
ATOM   7444  C  C     . GLY   A  1  1014 ? -8.815  75.837  100.908 1.00 18.09 ? 1012 GLY   A C     1 
ATOM   7445  O  O     . GLY   A  1  1014 ? -8.472  75.740  102.092 1.00 20.19 ? 1012 GLY   A O     1 
ATOM   7446  N  N     . ARG   A  1  1015 ? -8.050  76.374  99.974  1.00 16.13 ? 1013 ARG   A N     1 
ATOM   7447  C  CA    . ARG   A  1  1015 ? -6.659  76.721  100.179 1.00 17.45 ? 1013 ARG   A CA    1 
ATOM   7448  C  C     . ARG   A  1  1015 ? -6.442  78.115  99.629  1.00 17.35 ? 1013 ARG   A C     1 
ATOM   7449  O  O     . ARG   A  1  1015 ? -7.353  78.727  99.070  1.00 17.28 ? 1013 ARG   A O     1 
ATOM   7450  C  CB    . ARG   A  1  1015 ? -5.764  75.746  99.414  1.00 20.08 ? 1013 ARG   A CB    1 
ATOM   7451  C  CG    . ARG   A  1  1015 ? -6.039  75.770  97.914  1.00 20.36 ? 1013 ARG   A CG    1 
ATOM   7452  C  CD    . ARG   A  1  1015 ? -4.962  75.046  97.106  1.00 24.27 ? 1013 ARG   A CD    1 
ATOM   7453  N  NE    . ARG   A  1  1015 ? -3.634  75.246  97.662  1.00 27.93 ? 1013 ARG   A NE    1 
ATOM   7454  C  CZ    . ARG   A  1  1015 ? -2.918  76.350  97.518  1.00 29.58 ? 1013 ARG   A CZ    1 
ATOM   7455  N  NH1   . ARG   A  1  1015 ? -3.367  77.375  96.813  1.00 28.18 ? 1013 ARG   A NH1   1 
ATOM   7456  N  NH2   . ARG   A  1  1015 ? -1.727  76.429  98.108  1.00 26.52 ? 1013 ARG   A NH2   1 
ATOM   7457  N  N     . GLY   A  1  1016 ? -5.216  78.609  99.766  1.00 19.45 ? 1014 GLY   A N     1 
ATOM   7458  C  CA    . GLY   A  1  1016 ? -4.957  79.949  99.283  1.00 18.68 ? 1014 GLY   A CA    1 
ATOM   7459  C  C     . GLY   A  1  1016 ? -5.793  80.960  100.041 1.00 19.97 ? 1014 GLY   A C     1 
ATOM   7460  O  O     . GLY   A  1  1016 ? -5.955  80.885  101.264 1.00 20.07 ? 1014 GLY   A O     1 
ATOM   7461  N  N     . LEU   A  1  1017 ? -6.355  81.914  99.299  1.00 18.64 ? 1015 LEU   A N     1 
ATOM   7462  C  CA    . LEU   A  1  1017 ? -7.232  82.919  99.889  1.00 18.78 ? 1015 LEU   A CA    1 
ATOM   7463  C  C     . LEU   A  1  1017 ? -8.528  82.331  100.413 1.00 17.69 ? 1015 LEU   A C     1 
ATOM   7464  O  O     . LEU   A  1  1017 ? -9.321  83.062  101.016 1.00 18.35 ? 1015 LEU   A O     1 
ATOM   7465  C  CB    . LEU   A  1  1017 ? -7.560  83.985  98.838  1.00 19.52 ? 1015 LEU   A CB    1 
ATOM   7466  C  CG    . LEU   A  1  1017 ? -6.356  84.778  98.337  1.00 21.59 ? 1015 LEU   A CG    1 
ATOM   7467  C  CD1   . LEU   A  1  1017 ? -6.775  85.653  97.153  1.00 21.98 ? 1015 LEU   A CD1   1 
ATOM   7468  C  CD2   . LEU   A  1  1017 ? -5.754  85.629  99.477  1.00 21.40 ? 1015 LEU   A CD2   1 
ATOM   7469  N  N     . SER   A  1  1018 ? -8.764  81.036  100.194 1.00 15.69 ? 1016 SER   A N     1 
ATOM   7470  C  CA    . SER   A  1  1018 ? -10.029 80.416  100.552 1.00 16.90 ? 1016 SER   A CA    1 
ATOM   7471  C  C     . SER   A  1  1018 ? -9.989  79.679  101.878 1.00 17.08 ? 1016 SER   A C     1 
ATOM   7472  O  O     . SER   A  1  1018 ? -11.043 79.265  102.358 1.00 18.22 ? 1016 SER   A O     1 
ATOM   7473  C  CB    . SER   A  1  1018 ? -10.464 79.428  99.468  1.00 18.48 ? 1016 SER   A CB    1 
ATOM   7474  O  OG    . SER   A  1  1018 ? -10.687 80.119  98.253  1.00 17.32 ? 1016 SER   A OG    1 
ATOM   7475  N  N     . GLY   A  1  1019 ? -8.824  79.499  102.485 1.00 17.23 ? 1017 GLY   A N     1 
ATOM   7476  C  CA    . GLY   A  1  1019 ? -8.819  78.774  103.733 1.00 18.58 ? 1017 GLY   A CA    1 
ATOM   7477  C  C     . GLY   A  1  1019 ? -7.440  78.434  104.236 1.00 17.48 ? 1017 GLY   A C     1 
ATOM   7478  O  O     . GLY   A  1  1019 ? -6.475  78.350  103.468 1.00 21.68 ? 1017 GLY   A O     1 
ATOM   7479  N  N     . THR   A  1  1020 ? -7.347  78.267  105.546 1.00 18.39 ? 1018 THR   A N     1 
ATOM   7480  C  CA    . THR   A  1  1020 ? -6.176  77.688  106.171 1.00 20.60 ? 1018 THR   A CA    1 
ATOM   7481  C  C     . THR   A  1  1020 ? -6.297  76.187  106.307 1.00 19.18 ? 1018 THR   A C     1 
ATOM   7482  O  O     . THR   A  1  1020 ? -5.280  75.508  106.460 1.00 21.18 ? 1018 THR   A O     1 
ATOM   7483  C  CB    . THR   A  1  1020 ? -6.038  78.240  107.594 1.00 19.78 ? 1018 THR   A CB    1 
ATOM   7484  O  OG1   . THR   A  1  1020 ? -7.218  77.932  108.369 1.00 19.78 ? 1018 THR   A OG1   1 
ATOM   7485  C  CG2   . THR   A  1  1020 ? -5.845  79.751  107.551 1.00 23.23 ? 1018 THR   A CG2   1 
ATOM   7486  N  N     . GLY   A  1  1021 ? -7.522  75.672  106.325 1.00 21.02 ? 1019 GLY   A N     1 
ATOM   7487  C  CA    . GLY   A  1  1021 ? -7.746  74.321  106.757 1.00 20.97 ? 1019 GLY   A CA    1 
ATOM   7488  C  C     . GLY   A  1  1021 ? -7.548  74.216  108.256 1.00 20.84 ? 1019 GLY   A C     1 
ATOM   7489  O  O     . GLY   A  1  1021 ? -7.244  75.202  108.938 1.00 20.60 ? 1019 GLY   A O     1 
ATOM   7490  N  N     . PRO   A  1  1022 ? -7.763  73.024  108.805 1.00 19.70 ? 1020 PRO   A N     1 
ATOM   7491  C  CA    . PRO   A  1  1022 ? -8.235  71.816  108.122 1.00 19.78 ? 1020 PRO   A CA    1 
ATOM   7492  C  C     . PRO   A  1  1022 ? -9.702  71.943  107.697 1.00 21.14 ? 1020 PRO   A C     1 
ATOM   7493  O  O     . PRO   A  1  1022 ? -10.410 72.861  108.102 1.00 21.40 ? 1020 PRO   A O     1 
ATOM   7494  C  CB    . PRO   A  1  1022 ? -8.065  70.732  109.192 1.00 19.03 ? 1020 PRO   A CB    1 
ATOM   7495  C  CG    . PRO   A  1  1022 ? -8.264  71.470  110.484 1.00 20.25 ? 1020 PRO   A CG    1 
ATOM   7496  C  CD    . PRO   A  1  1022 ? -7.609  72.808  110.256 1.00 20.01 ? 1020 PRO   A CD    1 
ATOM   7497  N  N     . LYS   A  1  1023 ? -10.162 71.021  106.860 1.00 18.61 ? 1021 LYS   A N     1 
ATOM   7498  C  CA    . LYS   A  1  1023 ? -11.523 71.074  106.340 1.00 18.01 ? 1021 LYS   A CA    1 
ATOM   7499  C  C     . LYS   A  1  1023 ? -12.553 70.785  107.422 1.00 19.25 ? 1021 LYS   A C     1 
ATOM   7500  O  O     . LYS   A  1  1023 ? -12.438 69.810  108.165 1.00 18.37 ? 1021 LYS   A O     1 
ATOM   7501  C  CB    . LYS   A  1  1023 ? -11.694 70.013  105.261 1.00 16.68 ? 1021 LYS   A CB    1 
ATOM   7502  C  CG    . LYS   A  1  1023 ? -11.069 70.334  103.925 1.00 15.59 ? 1021 LYS   A CG    1 
ATOM   7503  C  CD    . LYS   A  1  1023 ? -11.244 69.105  103.050 1.00 16.26 ? 1021 LYS   A CD    1 
ATOM   7504  C  CE    . LYS   A  1  1023 ? -10.854 69.344  101.596 1.00 16.53 ? 1021 LYS   A CE    1 
ATOM   7505  N  NZ    . LYS   A  1  1023 ? -11.898 70.123  100.890 1.00 18.10 ? 1021 LYS   A NZ    1 
ATOM   7506  N  N     . ALA   A  1  1024 ? -13.588 71.615  107.477 1.00 20.13 ? 1022 ALA   A N     1 
ATOM   7507  C  CA    . ALA   A  1  1024 ? -14.778 71.267  108.234 1.00 21.19 ? 1022 ALA   A CA    1 
ATOM   7508  C  C     . ALA   A  1  1024 ? -15.431 70.033  107.624 1.00 21.03 ? 1022 ALA   A C     1 
ATOM   7509  O  O     . ALA   A  1  1024 ? -15.391 69.815  106.405 1.00 20.78 ? 1022 ALA   A O     1 
ATOM   7510  C  CB    . ALA   A  1  1024 ? -15.760 72.434  108.208 1.00 19.31 ? 1022 ALA   A CB    1 
ATOM   7511  N  N     . GLY   A  1  1025 ? -16.034 69.218  108.485 1.00 19.36 ? 1023 GLY   A N     1 
ATOM   7512  C  CA    . GLY   A  1  1025 ? -16.675 68.012  108.007 1.00 19.21 ? 1023 GLY   A CA    1 
ATOM   7513  C  C     . GLY   A  1  1025 ? -15.705 66.969  107.522 1.00 19.98 ? 1023 GLY   A C     1 
ATOM   7514  O  O     . GLY   A  1  1025 ? -16.097 66.059  106.780 1.00 18.36 ? 1023 GLY   A O     1 
ATOM   7515  N  N     . GLY   A  1  1026 ? -14.440 67.089  107.914 1.00 17.63 ? 1024 GLY   A N     1 
ATOM   7516  C  CA    . GLY   A  1  1026 ? -13.431 66.111  107.597 1.00 17.18 ? 1024 GLY   A CA    1 
ATOM   7517  C  C     . GLY   A  1  1026 ? -12.677 65.690  108.842 1.00 17.43 ? 1024 GLY   A C     1 
ATOM   7518  O  O     . GLY   A  1  1026 ? -12.848 66.243  109.931 1.00 17.13 ? 1024 GLY   A O     1 
ATOM   7519  N  N     . PRO   A  1  1027 ? -11.786 64.712  108.681 1.00 16.04 ? 1025 PRO   A N     1 
ATOM   7520  C  CA    . PRO   A  1  1027 ? -11.235 64.011  109.838 1.00 17.22 ? 1025 PRO   A CA    1 
ATOM   7521  C  C     . PRO   A  1  1027 ? -10.056 64.706  110.492 1.00 15.86 ? 1025 PRO   A C     1 
ATOM   7522  O  O     . PRO   A  1  1027 ? -9.632  64.260  111.561 1.00 17.50 ? 1025 PRO   A O     1 
ATOM   7523  C  CB    . PRO   A  1  1027 ? -10.831 62.656  109.251 1.00 19.35 ? 1025 PRO   A CB    1 
ATOM   7524  C  CG    . PRO   A  1  1027 ? -10.498 62.972  107.818 1.00 20.41 ? 1025 PRO   A CG    1 
ATOM   7525  C  CD    . PRO   A  1  1027 ? -11.477 64.038  107.408 1.00 16.41 ? 1025 PRO   A CD    1 
ATOM   7526  N  N     . LEU   A  1  1028 ? -9.510  65.768  109.902 1.00 17.58 ? 1026 LEU   A N     1 
ATOM   7527  C  CA    . LEU   A  1  1028 ? -8.433  66.513  110.543 1.00 17.99 ? 1026 LEU   A CA    1 
ATOM   7528  C  C     . LEU   A  1  1028 ? -8.936  67.648  111.414 1.00 16.43 ? 1026 LEU   A C     1 
ATOM   7529  O  O     . LEU   A  1  1028 ? -8.138  68.280  112.113 1.00 18.76 ? 1026 LEU   A O     1 
ATOM   7530  C  CB    . LEU   A  1  1028 ? -7.472  67.088  109.495 1.00 17.19 ? 1026 LEU   A CB    1 
ATOM   7531  C  CG    . LEU   A  1  1028 ? -6.706  66.044  108.686 1.00 20.66 ? 1026 LEU   A CG    1 
ATOM   7532  C  CD1   . LEU   A  1  1028 ? -5.842  66.723  107.639 1.00 21.19 ? 1026 LEU   A CD1   1 
ATOM   7533  C  CD2   . LEU   A  1  1028 ? -5.881  65.206  109.618 1.00 27.30 ? 1026 LEU   A CD2   1 
ATOM   7534  N  N     . TYR   A  1  1029 ? -10.246 67.897  111.410 1.00 16.74 ? 1027 TYR   A N     1 
ATOM   7535  C  CA    . TYR   A  1  1029 ? -10.775 69.124  111.993 1.00 18.74 ? 1027 TYR   A CA    1 
ATOM   7536  C  C     . TYR   A  1  1029 ? -10.613 69.131  113.501 1.00 19.58 ? 1027 TYR   A C     1 
ATOM   7537  O  O     . TYR   A  1  1029 ? -10.073 70.089  114.071 1.00 19.08 ? 1027 TYR   A O     1 
ATOM   7538  C  CB    . TYR   A  1  1029 ? -12.243 69.217  111.618 1.00 17.53 ? 1027 TYR   A CB    1 
ATOM   7539  C  CG    . TYR   A  1  1029 ? -12.885 70.567  111.708 1.00 16.68 ? 1027 TYR   A CG    1 
ATOM   7540  C  CD1   . TYR   A  1  1029 ? -12.519 71.604  110.849 1.00 18.11 ? 1027 TYR   A CD1   1 
ATOM   7541  C  CD2   . TYR   A  1  1029 ? -13.938 70.779  112.590 1.00 18.00 ? 1027 TYR   A CD2   1 
ATOM   7542  C  CE1   . TYR   A  1  1029 ? -13.163 72.835  110.897 1.00 17.79 ? 1027 TYR   A CE1   1 
ATOM   7543  C  CE2   . TYR   A  1  1029 ? -14.579 72.000  112.642 1.00 19.93 ? 1027 TYR   A CE2   1 
ATOM   7544  C  CZ    . TYR   A  1  1029 ? -14.194 73.018  111.794 1.00 18.25 ? 1027 TYR   A CZ    1 
ATOM   7545  O  OH    . TYR   A  1  1029 ? -14.862 74.221  111.853 1.00 20.84 ? 1027 TYR   A OH    1 
ATOM   7546  N  N     . LEU   A  1  1030 ? -11.085 68.075  114.173 1.00 17.99 ? 1028 LEU   A N     1 
ATOM   7547  C  CA    . LEU   A  1  1030 ? -11.053 68.090  115.635 1.00 17.79 ? 1028 LEU   A CA    1 
ATOM   7548  C  C     . LEU   A  1  1030 ? -9.632  68.190  116.151 1.00 20.00 ? 1028 LEU   A C     1 
ATOM   7549  O  O     . LEU   A  1  1030 ? -9.392  68.822  117.184 1.00 21.16 ? 1028 LEU   A O     1 
ATOM   7550  C  CB    . LEU   A  1  1030 ? -11.722 66.848  116.216 1.00 20.04 ? 1028 LEU   A CB    1 
ATOM   7551  C  CG    . LEU   A  1  1030 ? -13.214 66.671  115.950 1.00 22.42 ? 1028 LEU   A CG    1 
ATOM   7552  C  CD1   . LEU   A  1  1030 ? -13.700 65.390  116.618 1.00 23.49 ? 1028 LEU   A CD1   1 
ATOM   7553  C  CD2   . LEU   A  1  1030 ? -13.993 67.864  116.484 1.00 23.64 ? 1028 LEU   A CD2   1 
ATOM   7554  N  N     . GLY   A  1  1031 ? -8.677  67.594  115.437 1.00 18.80 ? 1029 GLY   A N     1 
ATOM   7555  C  CA    . GLY   A  1  1031 ? -7.303  67.599  115.896 1.00 18.19 ? 1029 GLY   A CA    1 
ATOM   7556  C  C     . GLY   A  1  1031 ? -6.699  68.978  116.019 1.00 20.12 ? 1029 GLY   A C     1 
ATOM   7557  O  O     . GLY   A  1  1031 ? -5.710  69.152  116.737 1.00 21.61 ? 1029 GLY   A O     1 
ATOM   7558  N  N     . ARG   A  1  1032 ? -7.267  69.962  115.331 1.00 18.78 ? 1030 ARG   A N     1 
ATOM   7559  C  CA    . ARG   A  1  1032 ? -6.787  71.325  115.433 1.00 18.05 ? 1030 ARG   A CA    1 
ATOM   7560  C  C     . ARG   A  1  1032 ? -7.264  71.999  116.709 1.00 20.82 ? 1030 ARG   A C     1 
ATOM   7561  O  O     . ARG   A  1  1032 ? -6.703  73.024  117.107 1.00 21.22 ? 1030 ARG   A O     1 
ATOM   7562  C  CB    . ARG   A  1  1032 ? -7.262  72.110  114.211 1.00 21.24 ? 1030 ARG   A CB    1 
ATOM   7563  C  CG    . ARG   A  1  1032 ? -6.626  73.472  114.049 1.00 19.25 ? 1030 ARG   A CG    1 
ATOM   7564  C  CD    . ARG   A  1  1032 ? -5.166  73.345  113.618 1.00 19.96 ? 1030 ARG   A CD    1 
ATOM   7565  N  NE    . ARG   A  1  1032 ? -4.647  74.644  113.218 1.00 21.59 ? 1030 ARG   A NE    1 
ATOM   7566  C  CZ    . ARG   A  1  1032 ? -3.607  75.254  113.771 1.00 24.41 ? 1030 ARG   A CZ    1 
ATOM   7567  N  NH1   . ARG   A  1  1032 ? -2.940  74.714  114.780 1.00 26.64 ? 1030 ARG   A NH1   1 
ATOM   7568  N  NH2   . ARG   A  1  1032 ? -3.229  76.438  113.300 1.00 26.91 ? 1030 ARG   A NH2   1 
ATOM   7569  N  N     . LEU   A  1  1033 ? -8.279  71.437  117.359 1.00 18.54 ? 1031 LEU   A N     1 
ATOM   7570  C  CA    . LEU   A  1  1033 ? -8.902  72.054  118.516 1.00 19.15 ? 1031 LEU   A CA    1 
ATOM   7571  C  C     . LEU   A  1  1033 ? -8.415  71.458  119.827 1.00 22.51 ? 1031 LEU   A C     1 
ATOM   7572  O  O     . LEU   A  1  1033 ? -9.031  71.695  120.868 1.00 21.95 ? 1031 LEU   A O     1 
ATOM   7573  C  CB    . LEU   A  1  1033 ? -10.421 71.936  118.405 1.00 20.01 ? 1031 LEU   A CB    1 
ATOM   7574  C  CG    . LEU   A  1  1033 ? -10.908 72.365  117.024 1.00 18.87 ? 1031 LEU   A CG    1 
ATOM   7575  C  CD1   . LEU   A  1  1033 ? -12.425 72.164  116.881 1.00 18.13 ? 1031 LEU   A CD1   1 
ATOM   7576  C  CD2   . LEU   A  1  1033 ? -10.537 73.814  116.773 1.00 22.91 ? 1031 LEU   A CD2   1 
ATOM   7577  N  N     . VAL   A  1  1034 ? -7.329  70.685  119.794 1.00 20.95 ? 1032 VAL   A N     1 
ATOM   7578  C  CA    . VAL   A  1  1034 ? -6.711  70.124  120.984 1.00 20.24 ? 1032 VAL   A CA    1 
ATOM   7579  C  C     . VAL   A  1  1034 ? -5.221  70.411  120.904 1.00 22.92 ? 1032 VAL   A C     1 
ATOM   7580  O  O     . VAL   A  1  1034 ? -4.677  70.692  119.834 1.00 23.41 ? 1032 VAL   A O     1 
ATOM   7581  C  CB    . VAL   A  1  1034 ? -6.965  68.610  121.129 1.00 21.22 ? 1032 VAL   A CB    1 
ATOM   7582  C  CG1   . VAL   A  1  1034 ? -8.453  68.337  121.375 1.00 23.68 ? 1032 VAL   A CG1   1 
ATOM   7583  C  CG2   . VAL   A  1  1034 ? -6.470  67.869  119.873 1.00 20.44 ? 1032 VAL   A CG2   1 
ATOM   7584  N  N     . THR   A  1  1035 ? -4.553  70.325  122.059 1.00 24.06 ? 1033 THR   A N     1 
ATOM   7585  C  CA    . THR   A  1  1035 ? -3.142  70.684  122.098 1.00 24.66 ? 1033 THR   A CA    1 
ATOM   7586  C  C     . THR   A  1  1035 ? -2.264  69.632  121.429 1.00 29.75 ? 1033 THR   A C     1 
ATOM   7587  O  O     . THR   A  1  1035 ? -1.259  69.982  120.802 1.00 32.44 ? 1033 THR   A O     1 
ATOM   7588  C  CB    . THR   A  1  1035 ? -2.711  70.971  123.536 1.00 28.54 ? 1033 THR   A CB    1 
ATOM   7589  O  OG1   . THR   A  1  1035 ? -3.006  69.842  124.364 1.00 37.69 ? 1033 THR   A OG1   1 
ATOM   7590  C  CG2   . THR   A  1  1035 ? -3.461  72.163  124.065 1.00 28.37 ? 1033 THR   A CG2   1 
ATOM   7591  N  N     . THR   A  1  1036 ? -2.632  68.357  121.528 1.00 25.10 ? 1034 THR   A N     1 
ATOM   7592  C  CA    . THR   A  1  1036 ? -1.914  67.266  120.878 1.00 25.83 ? 1034 THR   A CA    1 
ATOM   7593  C  C     . THR   A  1  1036 ? -2.894  66.561  119.958 1.00 24.93 ? 1034 THR   A C     1 
ATOM   7594  O  O     . THR   A  1  1036 ? -3.876  65.978  120.428 1.00 27.60 ? 1034 THR   A O     1 
ATOM   7595  C  CB    . THR   A  1  1036 ? -1.375  66.282  121.916 1.00 31.09 ? 1034 THR   A CB    1 
ATOM   7596  O  OG1   . THR   A  1  1036 ? -0.542  66.983  122.846 1.00 34.37 ? 1034 THR   A OG1   1 
ATOM   7597  C  CG2   . THR   A  1  1036 ? -0.555  65.196  121.236 1.00 35.97 ? 1034 THR   A CG2   1 
ATOM   7598  N  N     . ALA   A  1  1037 ? -2.631  66.616  118.662 1.00 25.73 ? 1035 ALA   A N     1 
ATOM   7599  C  CA    . ALA   A  1  1037 ? -3.597  66.109  117.695 1.00 24.86 ? 1035 ALA   A CA    1 
ATOM   7600  C  C     . ALA   A  1  1037 ? -3.650  64.588  117.770 1.00 24.99 ? 1035 ALA   A C     1 
ATOM   7601  O  O     . ALA   A  1  1037 ? -2.599  63.940  117.827 1.00 24.96 ? 1035 ALA   A O     1 
ATOM   7602  C  CB    . ALA   A  1  1037 ? -3.210  66.549  116.285 1.00 28.24 ? 1035 ALA   A CB    1 
ATOM   7603  N  N     . PRO   A  1  1038 ? -4.834  63.986  117.783 1.00 21.14 ? 1036 PRO   A N     1 
ATOM   7604  C  CA    . PRO   A  1  1038 ? -4.922  62.528  117.678 1.00 20.62 ? 1036 PRO   A CA    1 
ATOM   7605  C  C     . PRO   A  1  1038 ? -4.642  62.094  116.250 1.00 21.54 ? 1036 PRO   A C     1 
ATOM   7606  O  O     . PRO   A  1  1038 ? -4.528  62.901  115.330 1.00 21.57 ? 1036 PRO   A O     1 
ATOM   7607  C  CB    . PRO   A  1  1038 ? -6.385  62.247  118.029 1.00 22.51 ? 1036 PRO   A CB    1 
ATOM   7608  C  CG    . PRO   A  1  1038 ? -7.099  63.445  117.512 1.00 24.95 ? 1036 PRO   A CG    1 
ATOM   7609  C  CD    . PRO   A  1  1038 ? -6.170  64.614  117.784 1.00 22.34 ? 1036 PRO   A CD    1 
ATOM   7610  N  N     . VAL   A  1  1039 ? -4.562  60.780  116.073 1.00 21.25 ? 1037 VAL   A N     1 
ATOM   7611  C  CA    . VAL   A  1  1039 ? -4.443  60.172  114.752 1.00 19.98 ? 1037 VAL   A CA    1 
ATOM   7612  C  C     . VAL   A  1  1039 ? -5.859  59.992  114.208 1.00 18.39 ? 1037 VAL   A C     1 
ATOM   7613  O  O     . VAL   A  1  1039 ? -6.624  59.197  114.774 1.00 20.21 ? 1037 VAL   A O     1 
ATOM   7614  C  CB    . VAL   A  1  1039 ? -3.716  58.823  114.834 1.00 21.63 ? 1037 VAL   A CB    1 
ATOM   7615  C  CG1   . VAL   A  1  1039 ? -3.721  58.136  113.479 1.00 21.82 ? 1037 VAL   A CG1   1 
ATOM   7616  C  CG2   . VAL   A  1  1039 ? -2.287  59.014  115.363 1.00 23.58 ? 1037 VAL   A CG2   1 
ATOM   7617  N  N     . PRO   A  1  1040 ? -6.247  60.694  113.151 1.00 18.69 ? 1038 PRO   A N     1 
ATOM   7618  C  CA    . PRO   A  1  1040 ? -7.615  60.561  112.656 1.00 19.60 ? 1038 PRO   A CA    1 
ATOM   7619  C  C     . PRO   A  1  1040 ? -7.872  59.158  112.138 1.00 18.32 ? 1038 PRO   A C     1 
ATOM   7620  O  O     . PRO   A  1  1040 ? -6.931  58.440  111.771 1.00 19.26 ? 1038 PRO   A O     1 
ATOM   7621  C  CB    . PRO   A  1  1040 ? -7.684  61.585  111.512 1.00 19.36 ? 1038 PRO   A CB    1 
ATOM   7622  C  CG    . PRO   A  1  1040 ? -6.585  62.533  111.789 1.00 23.14 ? 1038 PRO   A CG    1 
ATOM   7623  C  CD    . PRO   A  1  1040 ? -5.492  61.713  112.409 1.00 21.79 ? 1038 PRO   A CD    1 
ATOM   7624  N  N     . PRO   A  1  1041 ? -9.133  58.736  112.072 1.00 19.45 ? 1039 PRO   A N     1 
ATOM   7625  C  CA    . PRO   A  1  1041 ? -9.434  57.456  111.425 1.00 18.44 ? 1039 PRO   A CA    1 
ATOM   7626  C  C     . PRO   A  1  1041 ? -8.922  57.455  109.994 1.00 18.65 ? 1039 PRO   A C     1 
ATOM   7627  O  O     . PRO   A  1  1041 ? -8.960  58.473  109.297 1.00 19.47 ? 1039 PRO   A O     1 
ATOM   7628  C  CB    . PRO   A  1  1041 ? -10.969 57.389  111.457 1.00 23.14 ? 1039 PRO   A CB    1 
ATOM   7629  C  CG    . PRO   A  1  1041 ? -11.380 58.376  112.489 1.00 24.70 ? 1039 PRO   A CG    1 
ATOM   7630  C  CD    . PRO   A  1  1041 ? -10.357 59.451  112.484 1.00 20.47 ? 1039 PRO   A CD    1 
ATOM   7631  N  N     . GLN   A  1  1042 ? -8.417  56.297  109.570 1.00 18.32 ? 1040 GLN   A N     1 
ATOM   7632  C  CA    . GLN   A  1  1042 ? -7.934  56.036  108.215 1.00 19.22 ? 1040 GLN   A CA    1 
ATOM   7633  C  C     . GLN   A  1  1042 ? -6.760  56.910  107.797 1.00 19.88 ? 1040 GLN   A C     1 
ATOM   7634  O  O     . GLN   A  1  1042 ? -6.409  56.924  106.618 1.00 19.49 ? 1040 GLN   A O     1 
ATOM   7635  C  CB    . GLN   A  1  1042 ? -9.051  56.143  107.167 1.00 21.98 ? 1040 GLN   A CB    1 
ATOM   7636  C  CG    . GLN   A  1  1042 ? -10.269 55.311  107.495 1.00 30.03 ? 1040 GLN   A CG    1 
ATOM   7637  C  CD    . GLN   A  1  1042 ? -11.332 55.416  106.414 1.00 32.85 ? 1040 GLN   A CD    1 
ATOM   7638  O  OE1   . GLN   A  1  1042 ? -11.352 54.626  105.474 1.00 41.77 ? 1040 GLN   A OE1   1 
ATOM   7639  N  NE2   . GLN   A  1  1042 ? -12.205 56.407  106.535 1.00 38.24 ? 1040 GLN   A NE2   1 
ATOM   7640  N  N     . HIS   A  1  1043 ? -6.130  57.629  108.723 1.00 17.50 ? 1041 HIS   A N     1 
ATOM   7641  C  CA    . HIS   A  1  1043 ? -5.153  58.654  108.373 1.00 18.05 ? 1041 HIS   A CA    1 
ATOM   7642  C  C     . HIS   A  1  1043 ? -3.754  58.054  108.425 1.00 16.96 ? 1041 HIS   A C     1 
ATOM   7643  O  O     . HIS   A  1  1043 ? -3.131  57.992  109.488 1.00 19.00 ? 1041 HIS   A O     1 
ATOM   7644  C  CB    . HIS   A  1  1043 ? -5.271  59.831  109.328 1.00 17.05 ? 1041 HIS   A CB    1 
ATOM   7645  C  CG    . HIS   A  1  1043 ? -4.294  60.932  109.057 1.00 18.22 ? 1041 HIS   A CG    1 
ATOM   7646  N  ND1   . HIS   A  1  1043 ? -4.562  61.977  108.201 1.00 18.34 ? 1041 HIS   A ND1   1 
ATOM   7647  C  CD2   . HIS   A  1  1043 ? -3.055  61.161  109.554 1.00 18.14 ? 1041 HIS   A CD2   1 
ATOM   7648  C  CE1   . HIS   A  1  1043 ? -3.529  62.799  108.171 1.00 19.23 ? 1041 HIS   A CE1   1 
ATOM   7649  N  NE2   . HIS   A  1  1043 ? -2.603  62.331  108.991 1.00 19.44 ? 1041 HIS   A NE2   1 
ATOM   7650  N  N     . SER   A  1  1044 ? -3.272  57.611  107.271 1.00 16.17 ? 1042 SER   A N     1 
ATOM   7651  C  CA    . SER   A  1  1044 ? -1.920  57.084  107.133 1.00 16.33 ? 1042 SER   A CA    1 
ATOM   7652  C  C     . SER   A  1  1044 ? -1.645  57.025  105.645 1.00 17.25 ? 1042 SER   A C     1 
ATOM   7653  O  O     . SER   A  1  1044 ? -2.551  57.159  104.819 1.00 19.20 ? 1042 SER   A O     1 
ATOM   7654  C  CB    . SER   A  1  1044 ? -1.796  55.679  107.728 1.00 18.43 ? 1042 SER   A CB    1 
ATOM   7655  O  OG    . SER   A  1  1044 ? -2.583  54.764  106.988 1.00 19.17 ? 1042 SER   A OG    1 
ATOM   7656  N  N     . SER   A  1  1045 ? -0.383  56.800  105.309 1.00 15.76 ? 1043 SER   A N     1 
ATOM   7657  C  CA    . SER   A  1  1045 ? -0.020  56.595  103.919 1.00 17.61 ? 1043 SER   A CA    1 
ATOM   7658  C  C     . SER   A  1  1045 ? 1.192   55.685  103.862 1.00 15.60 ? 1043 SER   A C     1 
ATOM   7659  O  O     . SER   A  1  1045 ? 2.131   55.838  104.648 1.00 16.80 ? 1043 SER   A O     1 
ATOM   7660  C  CB    . SER   A  1  1045 ? 0.313   57.928  103.248 1.00 18.35 ? 1043 SER   A CB    1 
ATOM   7661  O  OG    . SER   A  1  1045 ? 0.814   57.703  101.937 1.00 19.01 ? 1043 SER   A OG    1 
ATOM   7662  N  N     . VAL   A  1  1046 ? 1.170   54.730  102.927 1.00 17.79 ? 1044 VAL   A N     1 
ATOM   7663  C  CA    . VAL   A  1  1046 ? 2.334   53.868  102.743 1.00 18.61 ? 1044 VAL   A CA    1 
ATOM   7664  C  C     . VAL   A  1  1046 ? 3.390   54.517  101.877 1.00 18.92 ? 1044 VAL   A C     1 
ATOM   7665  O  O     . VAL   A  1  1046 ? 4.469   53.943  101.698 1.00 21.16 ? 1044 VAL   A O     1 
ATOM   7666  C  CB    . VAL   A  1  1046 ? 1.988   52.476  102.179 1.00 20.59 ? 1044 VAL   A CB    1 
ATOM   7667  C  CG1   . VAL   A  1  1046 ? 1.034   51.754  103.124 1.00 22.67 ? 1044 VAL   A CG1   1 
ATOM   7668  C  CG2   . VAL   A  1  1046 ? 1.391   52.594  100.796 1.00 19.38 ? 1044 VAL   A CG2   1 
ATOM   7669  N  N     . HIS   A  1  1047 ? 3.119   55.697  101.347 1.00 17.65 ? 1045 HIS   A N     1 
ATOM   7670  C  CA    . HIS   A  1  1047 ? 4.017   56.341  100.407 1.00 21.27 ? 1045 HIS   A CA    1 
ATOM   7671  C  C     . HIS   A  1  1047 ? 4.970   57.256  101.149 1.00 18.27 ? 1045 HIS   A C     1 
ATOM   7672  O  O     . HIS   A  1  1047 ? 4.600   57.890  102.140 1.00 19.61 ? 1045 HIS   A O     1 
ATOM   7673  C  CB    . HIS   A  1  1047 ? 3.185   57.100  99.383  1.00 22.97 ? 1045 HIS   A CB    1 
ATOM   7674  C  CG    . HIS   A  1  1047 ? 2.202   56.217  98.682  1.00 26.86 ? 1045 HIS   A CG    1 
ATOM   7675  N  ND1   . HIS   A  1  1047 ? 2.593   55.215  97.817  1.00 30.09 ? 1045 HIS   A ND1   1 
ATOM   7676  C  CD2   . HIS   A  1  1047 ? 0.851   56.148  98.752  1.00 28.53 ? 1045 HIS   A CD2   1 
ATOM   7677  C  CE1   . HIS   A  1  1047 ? 1.523   54.586  97.364  1.00 30.81 ? 1045 HIS   A CE1   1 
ATOM   7678  N  NE2   . HIS   A  1  1047 ? 0.453   55.132  97.918  1.00 28.38 ? 1045 HIS   A NE2   1 
ATOM   7679  N  N     . THR   A  1  1048 ? 6.212   57.287  100.692 1.00 18.29 ? 1046 THR   A N     1 
ATOM   7680  C  CA    . THR   A  1  1048 ? 7.238   58.113  101.302 1.00 19.72 ? 1046 THR   A CA    1 
ATOM   7681  C  C     . THR   A  1  1048 ? 7.748   59.085  100.253 1.00 19.31 ? 1046 THR   A C     1 
ATOM   7682  O  O     . THR   A  1  1048 ? 8.114   58.677  99.147  1.00 20.37 ? 1046 THR   A O     1 
ATOM   7683  C  CB    . THR   A  1  1048 ? 8.390   57.262  101.810 1.00 18.64 ? 1046 THR   A CB    1 
ATOM   7684  O  OG1   . THR   A  1  1048 ? 7.880   56.239  102.674 1.00 21.23 ? 1046 THR   A OG1   1 
ATOM   7685  C  CG2   . THR   A  1  1048 ? 9.368   58.140  102.595 1.00 20.68 ? 1046 THR   A CG2   1 
ATOM   7686  N  N     . ASP   A  1  1049 ? 7.755   60.357  100.599 1.00 18.13 ? 1047 ASP   A N     1 
ATOM   7687  C  CA    . ASP   A  1  1049 ? 8.193   61.362  99.658  1.00 16.17 ? 1047 ASP   A CA    1 
ATOM   7688  C  C     . ASP   A  1  1049 ? 9.653   61.102  99.293  1.00 16.97 ? 1047 ASP   A C     1 
ATOM   7689  O  O     . ASP   A  1  1049 ? 10.490  60.907  100.182 1.00 17.18 ? 1047 ASP   A O     1 
ATOM   7690  C  CB    . ASP   A  1  1049 ? 8.022   62.748  100.269 1.00 14.67 ? 1047 ASP   A CB    1 
ATOM   7691  C  CG    . ASP   A  1  1049 ? 8.440   63.839  99.326  1.00 19.96 ? 1047 ASP   A CG    1 
ATOM   7692  O  OD1   . ASP   A  1  1049 ? 9.656   64.082  99.232  1.00 19.67 ? 1047 ASP   A OD1   1 
ATOM   7693  O  OD2   . ASP   A  1  1049 ? 7.559   64.423  98.643  1.00 19.88 ? 1047 ASP   A OD2   1 
ATOM   7694  N  N     . PRO   A  1  1050 ? 9.984   61.044  98.005  1.00 16.31 ? 1048 PRO   A N     1 
ATOM   7695  C  CA    . PRO   A  1  1050 ? 11.343  60.658  97.617  1.00 18.13 ? 1048 PRO   A CA    1 
ATOM   7696  C  C     . PRO   A  1  1050 ? 12.353  61.753  97.870  1.00 17.19 ? 1048 PRO   A C     1 
ATOM   7697  O  O     . PRO   A  1  1050 ? 13.543  61.461  98.055  1.00 18.03 ? 1048 PRO   A O     1 
ATOM   7698  C  CB    . PRO   A  1  1050 ? 11.202  60.337  96.123  1.00 20.01 ? 1048 PRO   A CB    1 
ATOM   7699  C  CG    . PRO   A  1  1050 ? 10.028  61.173  95.682  1.00 19.62 ? 1048 PRO   A CG    1 
ATOM   7700  C  CD    . PRO   A  1  1050 ? 9.093   61.244  96.856  1.00 17.35 ? 1048 PRO   A CD    1 
ATOM   7701  N  N     . VAL   A  1  1051 ? 11.917  63.010  97.874  1.00 17.44 ? 1049 VAL   A N     1 
ATOM   7702  C  CA    . VAL   A  1  1051 ? 12.826  64.093  98.212  1.00 17.53 ? 1049 VAL   A CA    1 
ATOM   7703  C  C     . VAL   A  1  1051 ? 13.155  64.047  99.692  1.00 16.04 ? 1049 VAL   A C     1 
ATOM   7704  O  O     . VAL   A  1  1051 ? 14.301  64.287  100.093 1.00 16.49 ? 1049 VAL   A O     1 
ATOM   7705  C  CB    . VAL   A  1  1051 ? 12.246  65.447  97.775  1.00 18.90 ? 1049 VAL   A CB    1 
ATOM   7706  C  CG1   . VAL   A  1  1051 ? 13.181  66.571  98.175  1.00 22.87 ? 1049 VAL   A CG1   1 
ATOM   7707  C  CG2   . VAL   A  1  1051 ? 12.028  65.448  96.267  1.00 19.37 ? 1049 VAL   A CG2   1 
ATOM   7708  N  N     . LEU   A  1  1052 ? 12.163  63.720  100.525 1.00 15.27 ? 1050 LEU   A N     1 
ATOM   7709  C  CA    . LEU   A  1  1052 ? 12.447  63.464  101.932 1.00 15.97 ? 1050 LEU   A CA    1 
ATOM   7710  C  C     . LEU   A  1  1052 ? 13.502  62.378  102.075 1.00 16.95 ? 1050 LEU   A C     1 
ATOM   7711  O  O     . LEU   A  1  1052 ? 14.463  62.524  102.840 1.00 15.01 ? 1050 LEU   A O     1 
ATOM   7712  C  CB    . LEU   A  1  1052 ? 11.163  63.065  102.652 1.00 16.56 ? 1050 LEU   A CB    1 
ATOM   7713  C  CG    . LEU   A  1  1052 ? 11.237  62.676  104.141 1.00 15.88 ? 1050 LEU   A CG    1 
ATOM   7714  C  CD1   . LEU   A  1  1052 ? 11.769  61.244  104.386 1.00 17.22 ? 1050 LEU   A CD1   1 
ATOM   7715  C  CD2   . LEU   A  1  1052 ? 12.032  63.711  104.975 1.00 17.87 ? 1050 LEU   A CD2   1 
ATOM   7716  N  N     . LEU   A  1  1053 ? 13.340  61.269  101.341 1.00 16.79 ? 1051 LEU   A N     1 
ATOM   7717  C  CA    . LEU   A  1  1053 ? 14.317  60.189  101.435 1.00 17.41 ? 1051 LEU   A CA    1 
ATOM   7718  C  C     . LEU   A  1  1053 ? 15.702  60.663  101.015 1.00 15.87 ? 1051 LEU   A C     1 
ATOM   7719  O  O     . LEU   A  1  1053 ? 16.695  60.326  101.664 1.00 18.11 ? 1051 LEU   A O     1 
ATOM   7720  C  CB    . LEU   A  1  1053 ? 13.872  58.994  100.588 1.00 16.51 ? 1051 LEU   A CB    1 
ATOM   7721  C  CG    . LEU   A  1  1053 ? 12.670  58.229  101.137 1.00 20.58 ? 1051 LEU   A CG    1 
ATOM   7722  C  CD1   . LEU   A  1  1053 ? 12.216  57.163  100.144 1.00 22.04 ? 1051 LEU   A CD1   1 
ATOM   7723  C  CD2   . LEU   A  1  1053 ? 13.004  57.619  102.478 1.00 20.96 ? 1051 LEU   A CD2   1 
ATOM   7724  N  N     . ASP   A  1  1054 ? 15.785  61.462  99.943  1.00 17.37 ? 1052 ASP   A N     1 
ATOM   7725  C  CA    . ASP   A  1  1054 ? 17.081  61.989  99.519  1.00 18.32 ? 1052 ASP   A CA    1 
ATOM   7726  C  C     . ASP   A  1  1054 ? 17.660  62.916  100.574 1.00 15.65 ? 1052 ASP   A C     1 
ATOM   7727  O  O     . ASP   A  1  1054 ? 18.869  62.915  100.818 1.00 17.68 ? 1052 ASP   A O     1 
ATOM   7728  C  CB    . ASP   A  1  1054 ? 16.948  62.754  98.206  1.00 16.59 ? 1052 ASP   A CB    1 
ATOM   7729  C  CG    . ASP   A  1  1054 ? 16.669  61.848  97.026  1.00 23.17 ? 1052 ASP   A CG    1 
ATOM   7730  O  OD1   . ASP   A  1  1054 ? 16.762  60.611  97.183  1.00 21.61 ? 1052 ASP   A OD1   1 
ATOM   7731  O  OD2   . ASP   A  1  1054 ? 16.358  62.387  95.948  1.00 26.11 ? 1052 ASP   A OD2   1 
ATOM   7732  N  N     . PHE   A  1  1055 ? 16.810  63.712  101.211 1.00 16.52 ? 1053 PHE   A N     1 
ATOM   7733  C  CA    . PHE   A  1  1055 ? 17.284  64.592  102.271 1.00 16.66 ? 1053 PHE   A CA    1 
ATOM   7734  C  C     . PHE   A  1  1055 ? 17.797  63.795  103.460 1.00 16.32 ? 1053 PHE   A C     1 
ATOM   7735  O  O     . PHE   A  1  1055 ? 18.844  64.128  104.030 1.00 17.78 ? 1053 PHE   A O     1 
ATOM   7736  C  CB    . PHE   A  1  1055 ? 16.158  65.541  102.676 1.00 16.39 ? 1053 PHE   A CB    1 
ATOM   7737  C  CG    . PHE   A  1  1055 ? 16.535  66.495  103.766 1.00 16.69 ? 1053 PHE   A CG    1 
ATOM   7738  C  CD1   . PHE   A  1  1055 ? 17.611  67.351  103.601 1.00 20.03 ? 1053 PHE   A CD1   1 
ATOM   7739  C  CD2   . PHE   A  1  1055 ? 15.808  66.547  104.941 1.00 17.51 ? 1053 PHE   A CD2   1 
ATOM   7740  C  CE1   . PHE   A  1  1055 ? 17.959  68.252  104.602 1.00 21.52 ? 1053 PHE   A CE1   1 
ATOM   7741  C  CE2   . PHE   A  1  1055 ? 16.163  67.449  105.947 1.00 19.58 ? 1053 PHE   A CE2   1 
ATOM   7742  C  CZ    . PHE   A  1  1055 ? 17.236  68.287  105.767 1.00 18.96 ? 1053 PHE   A CZ    1 
ATOM   7743  N  N     . ALA   A  1  1056 ? 17.080  62.737  103.848 1.00 16.54 ? 1054 ALA   A N     1 
ATOM   7744  C  CA    . ALA   A  1  1056 ? 17.549  61.892  104.941 1.00 17.50 ? 1054 ALA   A CA    1 
ATOM   7745  C  C     . ALA   A  1  1056 ? 18.924  61.304  104.637 1.00 18.73 ? 1054 ALA   A C     1 
ATOM   7746  O  O     . ALA   A  1  1056 ? 19.786  61.244  105.517 1.00 18.91 ? 1054 ALA   A O     1 
ATOM   7747  C  CB    . ALA   A  1  1056 ? 16.535  60.788  105.232 1.00 20.31 ? 1054 ALA   A CB    1 
ATOM   7748  N  N     . LYS   A  1  1057 ? 19.150  60.858  103.398 1.00 18.47 ? 1055 LYS   A N     1 
ATOM   7749  C  CA    . LYS   A  1  1057 ? 20.466  60.325  103.053 1.00 21.22 ? 1055 LYS   A CA    1 
ATOM   7750  C  C     . LYS   A  1  1057 ? 21.524  61.413  103.092 1.00 19.02 ? 1055 LYS   A C     1 
ATOM   7751  O  O     . LYS   A  1  1057 ? 22.666  61.169  103.512 1.00 20.94 ? 1055 LYS   A O     1 
ATOM   7752  C  CB    . LYS   A  1  1057 ? 20.429  59.695  101.662 1.00 22.25 ? 1055 LYS   A CB    1 
ATOM   7753  C  CG    . LYS   A  1  1057 ? 19.730  58.368  101.636 1.00 23.91 ? 1055 LYS   A CG    1 
ATOM   7754  C  CD    . LYS   A  1  1057 ? 19.952  57.669  100.309 1.00 22.62 ? 1055 LYS   A CD    1 
ATOM   7755  C  CE    . LYS   A  1  1057 ? 19.333  58.453  99.164  1.00 23.19 ? 1055 LYS   A CE    1 
ATOM   7756  N  NZ    . LYS   A  1  1057 ? 19.098  57.549  98.005  1.00 26.33 ? 1055 LYS   A NZ    1 
ATOM   7757  N  N     . TRP   A  1  1058 ? 21.175  62.605  102.613 1.00 18.82 ? 1056 TRP   A N     1 
ATOM   7758  C  CA    . TRP   A  1  1058 ? 22.096  63.729  102.680 1.00 21.29 ? 1056 TRP   A CA    1 
ATOM   7759  C  C     . TRP   A  1  1058 ? 22.451  64.051  104.124 1.00 20.06 ? 1056 TRP   A C     1 
ATOM   7760  O  O     . TRP   A  1  1058 ? 23.622  64.259  104.446 1.00 20.91 ? 1056 TRP   A O     1 
ATOM   7761  C  CB    . TRP   A  1  1058 ? 21.483  64.938  101.975 1.00 20.43 ? 1056 TRP   A CB    1 
ATOM   7762  C  CG    . TRP   A  1  1058 ? 22.313  66.196  102.050 1.00 20.75 ? 1056 TRP   A CG    1 
ATOM   7763  C  CD1   . TRP   A  1  1058 ? 23.311  66.580  101.189 1.00 26.46 ? 1056 TRP   A CD1   1 
ATOM   7764  C  CD2   . TRP   A  1  1058 ? 22.208  67.237  103.028 1.00 23.16 ? 1056 TRP   A CD2   1 
ATOM   7765  N  NE1   . TRP   A  1  1058 ? 23.828  67.795  101.578 1.00 26.26 ? 1056 TRP   A NE1   1 
ATOM   7766  C  CE2   . TRP   A  1  1058 ? 23.169  68.219  102.703 1.00 27.30 ? 1056 TRP   A CE2   1 
ATOM   7767  C  CE3   . TRP   A  1  1058 ? 21.394  67.433  104.149 1.00 22.13 ? 1056 TRP   A CE3   1 
ATOM   7768  C  CZ2   . TRP   A  1  1058 ? 23.337  69.381  103.459 1.00 26.90 ? 1056 TRP   A CZ2   1 
ATOM   7769  C  CZ3   . TRP   A  1  1058 ? 21.561  68.588  104.901 1.00 23.96 ? 1056 TRP   A CZ3   1 
ATOM   7770  C  CH2   . TRP   A  1  1058 ? 22.531  69.545  104.555 1.00 26.08 ? 1056 TRP   A CH2   1 
ATOM   7771  N  N     . LEU   A  1  1059 ? 21.455  64.055  105.013 1.00 18.39 ? 1057 LEU   A N     1 
ATOM   7772  C  CA    . LEU   A  1  1059 ? 21.720  64.322  106.424 1.00 21.06 ? 1057 LEU   A CA    1 
ATOM   7773  C  C     . LEU   A  1  1059 ? 22.703  63.319  106.992 1.00 21.54 ? 1057 LEU   A C     1 
ATOM   7774  O  O     . LEU   A  1  1059 ? 23.623  63.691  107.728 1.00 22.20 ? 1057 LEU   A O     1 
ATOM   7775  C  CB    . LEU   A  1  1059 ? 20.420  64.257  107.223 1.00 18.34 ? 1057 LEU   A CB    1 
ATOM   7776  C  CG    . LEU   A  1  1059 ? 19.535  65.483  107.071 1.00 19.33 ? 1057 LEU   A CG    1 
ATOM   7777  C  CD1   . LEU   A  1  1059 ? 18.169  65.217  107.712 1.00 18.36 ? 1057 LEU   A CD1   1 
ATOM   7778  C  CD2   . LEU   A  1  1059 ? 20.196  66.698  107.716 1.00 22.13 ? 1057 LEU   A CD2   1 
ATOM   7779  N  N     . ASP   A  1  1060 ? 22.519  62.036  106.674 1.00 20.22 ? 1058 ASP   A N     1 
ATOM   7780  C  CA    . ASP   A  1  1060 ? 23.447  61.026  107.164 1.00 25.12 ? 1058 ASP   A CA    1 
ATOM   7781  C  C     . ASP   A  1  1060 ? 24.842  61.260  106.611 1.00 24.19 ? 1058 ASP   A C     1 
ATOM   7782  O  O     . ASP   A  1  1060 ? 25.831  61.154  107.346 1.00 27.46 ? 1058 ASP   A O     1 
ATOM   7783  C  CB    . ASP   A  1  1060 ? 22.953  59.631  106.805 1.00 24.62 ? 1058 ASP   A CB    1 
ATOM   7784  C  CG    . ASP   A  1  1060 ? 22.131  59.006  107.909 1.00 25.56 ? 1058 ASP   A CG    1 
ATOM   7785  O  OD1   . ASP   A  1  1060 ? 22.424  59.271  109.099 1.00 29.64 ? 1058 ASP   A OD1   1 
ATOM   7786  O  OD2   . ASP   A  1  1060 ? 21.199  58.247  107.590 1.00 28.57 ? 1058 ASP   A OD2   1 
ATOM   7787  N  N     . GLY   A  1  1061 ? 24.945  61.606  105.326 1.00 25.33 ? 1059 GLY   A N     1 
ATOM   7788  C  CA    . GLY   A  1  1061 ? 26.250  61.905  104.754 1.00 24.63 ? 1059 GLY   A CA    1 
ATOM   7789  C  C     . GLY   A  1  1061 ? 26.930  63.099  105.399 1.00 28.73 ? 1059 GLY   A C     1 
ATOM   7790  O  O     . GLY   A  1  1061 ? 28.166  63.156  105.469 1.00 26.71 ? 1059 GLY   A O     1 
ATOM   7791  N  N     . LYS   A  1  1062 ? 26.144  64.065  105.879 1.00 23.37 ? 1060 LYS   A N     1 
ATOM   7792  C  CA    . LYS   A  1  1062 ? 26.674  65.239  106.563 1.00 26.47 ? 1060 LYS   A CA    1 
ATOM   7793  C  C     . LYS   A  1  1062 ? 27.010  64.970  108.022 1.00 27.41 ? 1060 LYS   A C     1 
ATOM   7794  O  O     . LYS   A  1  1062 ? 27.570  65.852  108.684 1.00 30.85 ? 1060 LYS   A O     1 
ATOM   7795  C  CB    . LYS   A  1  1062 ? 25.676  66.398  106.486 1.00 27.22 ? 1060 LYS   A CB    1 
ATOM   7796  C  CG    . LYS   A  1  1062 ? 25.549  67.034  105.109 1.00 27.37 ? 1060 LYS   A CG    1 
ATOM   7797  C  CD    . LYS   A  1  1062 ? 26.858  67.702  104.706 1.00 33.82 ? 1060 LYS   A CD    1 
ATOM   7798  C  CE    . LYS   A  1  1062 ? 26.791  68.259  103.300 1.00 36.25 ? 1060 LYS   A CE    1 
ATOM   7799  N  NZ    . LYS   A  1  1062 ? 28.071  68.935  102.933 1.00 37.35 ? 1060 LYS   A NZ    1 
ATOM   7800  N  N     . GLY   A  1  1063 ? 26.676  63.787  108.534 1.00 25.58 ? 1061 GLY   A N     1 
ATOM   7801  C  CA    . GLY   A  1  1063 ? 26.886  63.444  109.923 1.00 29.21 ? 1061 GLY   A CA    1 
ATOM   7802  C  C     . GLY   A  1  1063 ? 25.770  63.832  110.866 1.00 29.93 ? 1061 GLY   A C     1 
ATOM   7803  O  O     . GLY   A  1  1063 ? 25.929  63.663  112.082 1.00 30.76 ? 1061 GLY   A O     1 
ATOM   7804  N  N     . ALA   A  1  1064 ? 24.647  64.343  110.349 1.00 25.91 ? 1062 ALA   A N     1 
ATOM   7805  C  CA    . ALA   A  1  1064 ? 23.490  64.721  111.169 1.00 23.77 ? 1062 ALA   A CA    1 
ATOM   7806  C  C     . ALA   A  1  1064 ? 22.628  63.477  111.386 1.00 23.42 ? 1062 ALA   A C     1 
ATOM   7807  O  O     . ALA   A  1  1064 ? 21.523  63.333  110.857 1.00 22.26 ? 1062 ALA   A O     1 
ATOM   7808  C  CB    . ALA   A  1  1064 ? 22.712  65.842  110.492 1.00 25.08 ? 1062 ALA   A CB    1 
ATOM   7809  N  N     . ARG   A  1  1065 ? 23.157  62.569  112.206 1.00 20.95 ? 1063 ARG   A N     1 
ATOM   7810  C  CA    A ARG   A  1  1065 ? 22.568  61.239  112.326 0.53 22.88 ? 1063 ARG   A CA    1 
ATOM   7811  C  CA    B ARG   A  1  1065 ? 22.566  61.240  112.322 0.47 22.89 ? 1063 ARG   A CA    1 
ATOM   7812  C  C     . ARG   A  1  1065 ? 21.185  61.297  112.963 1.00 22.62 ? 1063 ARG   A C     1 
ATOM   7813  O  O     . ARG   A  1  1065 ? 20.233  60.689  112.465 1.00 23.45 ? 1063 ARG   A O     1 
ATOM   7814  C  CB    A ARG   A  1  1065 ? 23.500  60.333  113.127 0.53 25.88 ? 1063 ARG   A CB    1 
ATOM   7815  C  CB    B ARG   A  1  1065 ? 23.495  60.317  113.108 0.47 25.87 ? 1063 ARG   A CB    1 
ATOM   7816  C  CG    A ARG   A  1  1065 ? 24.950  60.387  112.670 0.53 28.82 ? 1063 ARG   A CG    1 
ATOM   7817  C  CG    B ARG   A  1  1065 ? 24.958  60.416  112.704 0.47 28.80 ? 1063 ARG   A CG    1 
ATOM   7818  C  CD    A ARG   A  1  1065 ? 25.106  59.865  111.251 0.53 29.02 ? 1063 ARG   A CD    1 
ATOM   7819  C  CD    B ARG   A  1  1065 ? 25.163  60.160  111.218 0.47 28.96 ? 1063 ARG   A CD    1 
ATOM   7820  N  NE    A ARG   A  1  1065 ? 26.491  59.924  110.797 0.53 28.97 ? 1063 ARG   A NE    1 
ATOM   7821  N  NE    B ARG   A  1  1065 ? 24.782  58.808  110.825 0.47 29.43 ? 1063 ARG   A NE    1 
ATOM   7822  C  CZ    A ARG   A  1  1065 ? 26.963  59.251  109.758 0.53 28.51 ? 1063 ARG   A CZ    1 
ATOM   7823  C  CZ    B ARG   A  1  1065 ? 25.092  58.260  109.659 0.47 28.15 ? 1063 ARG   A CZ    1 
ATOM   7824  N  NH1   A ARG   A  1  1065 ? 26.189  58.452  109.042 0.53 33.00 ? 1063 ARG   A NH1   1 
ATOM   7825  N  NH1   B ARG   A  1  1065 ? 25.804  58.914  108.758 0.47 32.17 ? 1063 ARG   A NH1   1 
ATOM   7826  N  NH2   A ARG   A  1  1065 ? 28.246  59.378  109.431 0.53 28.61 ? 1063 ARG   A NH2   1 
ATOM   7827  N  NH2   B ARG   A  1  1065 ? 24.675  57.027  109.390 0.47 31.03 ? 1063 ARG   A NH2   1 
ATOM   7828  N  N     . ALA   A  1  1066 ? 21.052  62.018  114.078 1.00 23.12 ? 1064 ALA   A N     1 
ATOM   7829  C  CA    . ALA   A  1  1066 ? 19.751  62.079  114.731 1.00 22.46 ? 1064 ALA   A CA    1 
ATOM   7830  C  C     . ALA   A  1  1066 ? 18.724  62.749  113.830 1.00 20.59 ? 1064 ALA   A C     1 
ATOM   7831  O  O     . ALA   A  1  1066 ? 17.558  62.342  113.797 1.00 21.61 ? 1064 ALA   A O     1 
ATOM   7832  C  CB    . ALA   A  1  1066 ? 19.852  62.806  116.071 1.00 22.56 ? 1064 ALA   A CB    1 
ATOM   7833  N  N     . GLU   A  1  1067 ? 19.148  63.770  113.081 1.00 19.93 ? 1065 GLU   A N     1 
ATOM   7834  C  CA    . GLU   A  1  1067 ? 18.218  64.456  112.193 1.00 20.21 ? 1065 GLU   A CA    1 
ATOM   7835  C  C     . GLU   A  1  1067 ? 17.804  63.557  111.041 1.00 19.73 ? 1065 GLU   A C     1 
ATOM   7836  O  O     . GLU   A  1  1067 ? 16.642  63.583  110.618 1.00 19.84 ? 1065 GLU   A O     1 
ATOM   7837  C  CB    . GLU   A  1  1067 ? 18.840  65.748  111.673 1.00 22.20 ? 1065 GLU   A CB    1 
ATOM   7838  C  CG    . GLU   A  1  1067 ? 18.944  66.854  112.723 1.00 22.59 ? 1065 GLU   A CG    1 
ATOM   7839  C  CD    . GLU   A  1  1067 ? 20.146  66.709  113.655 1.00 29.83 ? 1065 GLU   A CD    1 
ATOM   7840  O  OE1   . GLU   A  1  1067 ? 21.012  65.827  113.436 1.00 23.71 ? 1065 GLU   A OE1   1 
ATOM   7841  O  OE2   . GLU   A  1  1067 ? 20.217  67.493  114.627 1.00 32.39 ? 1065 GLU   A OE2   1 
ATOM   7842  N  N     . ALA   A  1  1068 ? 18.745  62.771  110.513 1.00 21.86 ? 1066 ALA   A N     1 
ATOM   7843  C  CA    . ALA   A  1  1068 ? 18.406  61.808  109.469 1.00 18.18 ? 1066 ALA   A CA    1 
ATOM   7844  C  C     . ALA   A  1  1068 ? 17.364  60.818  109.961 1.00 19.69 ? 1066 ALA   A C     1 
ATOM   7845  O  O     . ALA   A  1  1068 ? 16.413  60.493  109.238 1.00 19.41 ? 1066 ALA   A O     1 
ATOM   7846  C  CB    . ALA   A  1  1068 ? 19.665  61.067  109.025 1.00 21.23 ? 1066 ALA   A CB    1 
ATOM   7847  N  N     . GLU   A  1  1069 ? 17.527  60.320  111.188 1.00 21.30 ? 1067 GLU   A N     1 
ATOM   7848  C  CA    . GLU   A  1  1069 ? 16.523  59.437  111.766 1.00 20.24 ? 1067 GLU   A CA    1 
ATOM   7849  C  C     . GLU   A  1  1069 ? 15.179  60.142  111.899 1.00 20.20 ? 1067 GLU   A C     1 
ATOM   7850  O  O     . GLU   A  1  1069 ? 14.130  59.562  111.593 1.00 21.34 ? 1067 GLU   A O     1 
ATOM   7851  C  CB    . GLU   A  1  1069 ? 16.994  58.939  113.132 1.00 23.56 ? 1067 GLU   A CB    1 
ATOM   7852  C  CG    . GLU   A  1  1069 ? 15.955  58.155  113.908 1.00 28.68 ? 1067 GLU   A CG    1 
ATOM   7853  C  CD    . GLU   A  1  1069 ? 15.790  56.734  113.401 1.00 34.08 ? 1067 GLU   A CD    1 
ATOM   7854  O  OE1   . GLU   A  1  1069 ? 16.465  56.363  112.414 1.00 40.83 ? 1067 GLU   A OE1   1 
ATOM   7855  O  OE2   . GLU   A  1  1069 ? 14.986  55.984  113.995 1.00 42.83 ? 1067 GLU   A OE2   1 
ATOM   7856  N  N     . ALA   A  1  1070 ? 15.189  61.391  112.365 1.00 21.73 ? 1068 ALA   A N     1 
ATOM   7857  C  CA    . ALA   A  1  1070 ? 13.939  62.129  112.481 1.00 19.88 ? 1068 ALA   A CA    1 
ATOM   7858  C  C     . ALA   A  1  1070 ? 13.321  62.356  111.111 1.00 19.44 ? 1068 ALA   A C     1 
ATOM   7859  O  O     . ALA   A  1  1070 ? 12.093  62.335  110.963 1.00 19.09 ? 1068 ALA   A O     1 
ATOM   7860  C  CB    . ALA   A  1  1070 ? 14.180  63.466  113.183 1.00 20.54 ? 1068 ALA   A CB    1 
ATOM   7861  N  N     . ALA   A  1  1071 ? 14.161  62.583  110.099 1.00 18.21 ? 1069 ALA   A N     1 
ATOM   7862  C  CA    . ALA   A  1  1071 ? 13.658  62.760  108.740 1.00 16.58 ? 1069 ALA   A CA    1 
ATOM   7863  C  C     . ALA   A  1  1071 ? 12.993  61.483  108.250 1.00 18.57 ? 1069 ALA   A C     1 
ATOM   7864  O  O     . ALA   A  1  1071 ? 11.875  61.516  107.726 1.00 15.93 ? 1069 ALA   A O     1 
ATOM   7865  C  CB    . ALA   A  1  1071 ? 14.792  63.177  107.799 1.00 17.44 ? 1069 ALA   A CB    1 
ATOM   7866  N  N     . ARG   A  1  1072 ? 13.648  60.337  108.453 1.00 18.26 ? 1070 ARG   A N     1 
ATOM   7867  C  CA    . ARG   A  1  1072 ? 13.016  59.075  108.082 1.00 18.63 ? 1070 ARG   A CA    1 
ATOM   7868  C  C     . ARG   A  1  1072 ? 11.699  58.882  108.822 1.00 18.80 ? 1070 ARG   A C     1 
ATOM   7869  O  O     . ARG   A  1  1072 ? 10.701  58.462  108.227 1.00 20.03 ? 1070 ARG   A O     1 
ATOM   7870  C  CB    . ARG   A  1  1072 ? 13.964  57.904  108.335 1.00 19.42 ? 1070 ARG   A CB    1 
ATOM   7871  C  CG    . ARG   A  1  1072 ? 15.081  57.800  107.296 1.00 21.58 ? 1070 ARG   A CG    1 
ATOM   7872  C  CD    . ARG   A  1  1072 ? 15.910  56.549  107.518 1.00 24.87 ? 1070 ARG   A CD    1 
ATOM   7873  N  NE    . ARG   A  1  1072 ? 16.649  56.603  108.772 1.00 25.28 ? 1070 ARG   A NE    1 
ATOM   7874  C  CZ    . ARG   A  1  1072 ? 17.874  57.095  108.894 1.00 25.84 ? 1070 ARG   A CZ    1 
ATOM   7875  N  NH1   . ARG   A  1  1072 ? 18.530  57.592  107.854 1.00 24.71 ? 1070 ARG   A NH1   1 
ATOM   7876  N  NH2   . ARG   A  1  1072 ? 18.453  57.093  110.090 1.00 27.66 ? 1070 ARG   A NH2   1 
ATOM   7877  N  N     . ASN   A  1  1073 ? 11.675  59.207  110.116 1.00 18.20 ? 1071 ASN   A N     1 
ATOM   7878  C  CA    . ASN   A  1  1073 ? 10.443  59.104  110.884 1.00 18.30 ? 1071 ASN   A CA    1 
ATOM   7879  C  C     . ASN   A  1  1073 ? 9.357   60.002  110.311 1.00 19.06 ? 1071 ASN   A C     1 
ATOM   7880  O  O     . ASN   A  1  1073 ? 8.195   59.589  110.210 1.00 20.78 ? 1071 ASN   A O     1 
ATOM   7881  C  CB    . ASN   A  1  1073 ? 10.708  59.428  112.354 1.00 20.40 ? 1071 ASN   A CB    1 
ATOM   7882  C  CG    . ASN   A  1  1073 ? 11.471  58.329  113.043 1.00 26.01 ? 1071 ASN   A CG    1 
ATOM   7883  O  OD1   . ASN   A  1  1073 ? 11.495  57.194  112.566 1.00 28.07 ? 1071 ASN   A OD1   1 
ATOM   7884  N  ND2   . ASN   A  1  1073 ? 12.106  58.653  114.160 1.00 28.82 ? 1071 ASN   A ND2   1 
ATOM   7885  N  N     . ALA   A  1  1074 ? 9.716   61.231  109.916 1.00 17.18 ? 1072 ALA   A N     1 
ATOM   7886  C  CA    . ALA   A  1  1074 ? 8.726   62.126  109.328 1.00 18.50 ? 1072 ALA   A CA    1 
ATOM   7887  C  C     . ALA   A  1  1074 ? 8.213   61.565  108.016 1.00 18.69 ? 1072 ALA   A C     1 
ATOM   7888  O  O     . ALA   A  1  1074 ? 7.017   61.653  107.724 1.00 17.22 ? 1072 ALA   A O     1 
ATOM   7889  C  CB    . ALA   A  1  1074 ? 9.319   63.521  109.122 1.00 19.77 ? 1072 ALA   A CB    1 
ATOM   7890  N  N     . GLY   A  1  1075 ? 9.101   60.959  107.229 1.00 17.36 ? 1073 GLY   A N     1 
ATOM   7891  C  CA    . GLY   A  1  1075 ? 8.671   60.367  105.975 1.00 17.58 ? 1073 GLY   A CA    1 
ATOM   7892  C  C     . GLY   A  1  1075 ? 7.612   59.304  106.182 1.00 17.02 ? 1073 GLY   A C     1 
ATOM   7893  O  O     . GLY   A  1  1075 ? 6.641   59.229  105.427 1.00 18.70 ? 1073 GLY   A O     1 
ATOM   7894  N  N     . SER   A  1  1076 ? 7.782   58.478  107.220 1.00 18.28 ? 1074 SER   A N     1 
ATOM   7895  C  CA    . SER   A  1  1076 ? 6.817   57.425  107.529 1.00 20.30 ? 1074 SER   A CA    1 
ATOM   7896  C  C     . SER   A  1  1076 ? 5.549   57.988  108.144 1.00 22.03 ? 1074 SER   A C     1 
ATOM   7897  O  O     . SER   A  1  1076 ? 4.444   57.523  107.836 1.00 21.82 ? 1074 SER   A O     1 
ATOM   7898  C  CB    . SER   A  1  1076 ? 7.439   56.431  108.511 1.00 23.84 ? 1074 SER   A CB    1 
ATOM   7899  O  OG    . SER   A  1  1076 ? 8.425   55.650  107.879 1.00 31.35 ? 1074 SER   A OG    1 
ATOM   7900  N  N     . SER   A  1  1077 ? 5.691   58.981  109.025 1.00 18.08 ? 1075 SER   A N     1 
ATOM   7901  C  CA    A SER   A  1  1077 ? 4.533   59.515  109.731 0.52 20.38 ? 1075 SER   A CA    1 
ATOM   7902  C  CA    B SER   A  1  1077 ? 4.549   59.543  109.743 0.48 20.38 ? 1075 SER   A CA    1 
ATOM   7903  C  C     . SER   A  1  1077 ? 3.648   60.364  108.829 1.00 18.71 ? 1075 SER   A C     1 
ATOM   7904  O  O     . SER   A  1  1077 ? 2.444   60.501  109.094 1.00 20.04 ? 1075 SER   A O     1 
ATOM   7905  C  CB    A SER   A  1  1077 ? 4.995   60.314  110.946 0.52 21.54 ? 1075 SER   A CB    1 
ATOM   7906  C  CB    B SER   A  1  1077 ? 5.060   60.414  110.895 0.48 21.50 ? 1075 SER   A CB    1 
ATOM   7907  O  OG    A SER   A  1  1077 ? 5.514   59.441  111.930 0.52 24.83 ? 1075 SER   A OG    1 
ATOM   7908  O  OG    B SER   A  1  1077 ? 4.004   61.114  111.535 0.48 25.63 ? 1075 SER   A OG    1 
ATOM   7909  N  N     . SER   A  1  1078 ? 4.211   60.936  107.777 1.00 17.07 ? 1076 SER   A N     1 
ATOM   7910  C  CA    . SER   A  1  1078 ? 3.436   61.754  106.864 1.00 19.74 ? 1076 SER   A CA    1 
ATOM   7911  C  C     . SER   A  1  1078 ? 2.304   60.938  106.258 1.00 17.46 ? 1076 SER   A C     1 
ATOM   7912  O  O     . SER   A  1  1078 ? 2.475   59.767  105.908 1.00 18.04 ? 1076 SER   A O     1 
ATOM   7913  C  CB    . SER   A  1  1078 ? 4.353   62.218  105.743 1.00 17.51 ? 1076 SER   A CB    1 
ATOM   7914  O  OG    . SER   A  1  1078 ? 3.601   62.911  104.768 1.00 16.36 ? 1076 SER   A OG    1 
ATOM   7915  N  N     . ALA   A  1  1079 ? 1.134   61.557  106.134 1.00 15.67 ? 1077 ALA   A N     1 
ATOM   7916  C  CA    . ALA   A  1  1079 ? 0.015   60.929  105.449 1.00 14.80 ? 1077 ALA   A CA    1 
ATOM   7917  C  C     . ALA   A  1  1079 ? -0.129  61.425  104.026 1.00 17.68 ? 1077 ALA   A C     1 
ATOM   7918  O  O     . ALA   A  1  1079 ? -1.153  61.162  103.392 1.00 15.72 ? 1077 ALA   A O     1 
ATOM   7919  C  CB    . ALA   A  1  1079 ? -1.289  61.124  106.224 1.00 16.33 ? 1077 ALA   A CB    1 
ATOM   7920  N  N     . LEU   A  1  1080 ? 0.866   62.148  103.516 1.00 16.14 ? 1078 LEU   A N     1 
ATOM   7921  C  CA    . LEU   A  1  1080 ? 0.887   62.535  102.111 1.00 16.15 ? 1078 LEU   A CA    1 
ATOM   7922  C  C     . LEU   A  1  1080 ? 0.658   61.316  101.236 1.00 16.12 ? 1078 LEU   A C     1 
ATOM   7923  O  O     . LEU   A  1  1080 ? 1.295   60.277  101.423 1.00 17.15 ? 1078 LEU   A O     1 
ATOM   7924  C  CB    . LEU   A  1  1080 ? 2.266   63.103  101.778 1.00 15.74 ? 1078 LEU   A CB    1 
ATOM   7925  C  CG    . LEU   A  1  1080 ? 2.469   63.422  100.296 1.00 16.01 ? 1078 LEU   A CG    1 
ATOM   7926  C  CD1   . LEU   A  1  1080 ? 1.660   64.661  99.913  1.00 19.31 ? 1078 LEU   A CD1   1 
ATOM   7927  C  CD2   . LEU   A  1  1080 ? 3.950   63.647  100.028 1.00 17.24 ? 1078 LEU   A CD2   1 
ATOM   7928  N  N     . GLY   A  1  1081 ? -0.271  61.435  100.287 1.00 15.95 ? 1079 GLY   A N     1 
ATOM   7929  C  CA    . GLY   A  1  1081 ? -0.584  60.313  99.429  1.00 17.96 ? 1079 GLY   A CA    1 
ATOM   7930  C  C     . GLY   A  1  1081 ? -1.781  59.502  99.875  1.00 17.82 ? 1079 GLY   A C     1 
ATOM   7931  O  O     . GLY   A  1  1081 ? -2.181  58.572  99.162  1.00 18.96 ? 1079 GLY   A O     1 
ATOM   7932  N  N     . LEU   A  1  1082 ? -2.336  59.796  101.046 1.00 15.04 ? 1080 LEU   A N     1 
ATOM   7933  C  CA    A LEU   A  1  1082 ? -3.594  59.183  101.439 0.62 15.20 ? 1080 LEU   A CA    1 
ATOM   7934  C  CA    B LEU   A  1  1082 ? -3.597  59.188  101.442 0.38 15.26 ? 1080 LEU   A CA    1 
ATOM   7935  C  C     . LEU   A  1  1082 ? -4.626  59.403  100.340 1.00 17.56 ? 1080 LEU   A C     1 
ATOM   7936  O  O     . LEU   A  1  1082 ? -4.729  60.492  99.772  1.00 16.96 ? 1080 LEU   A O     1 
ATOM   7937  C  CB    A LEU   A  1  1082 ? -4.074  59.821  102.742 0.62 16.74 ? 1080 LEU   A CB    1 
ATOM   7938  C  CB    B LEU   A  1  1082 ? -4.077  59.831  102.746 0.38 16.74 ? 1080 LEU   A CB    1 
ATOM   7939  C  CG    A LEU   A  1  1082 ? -5.418  59.340  103.274 0.62 16.66 ? 1080 LEU   A CG    1 
ATOM   7940  C  CG    B LEU   A  1  1082 ? -5.396  59.370  103.365 0.38 16.68 ? 1080 LEU   A CG    1 
ATOM   7941  C  CD1   A LEU   A  1  1082 ? -5.414  57.834  103.418 0.62 17.21 ? 1080 LEU   A CD1   1 
ATOM   7942  C  CD1   B LEU   A  1  1082 ? -5.356  59.561  104.864 0.38 17.80 ? 1080 LEU   A CD1   1 
ATOM   7943  C  CD2   A LEU   A  1  1082 ? -5.714  59.998  104.603 0.62 17.71 ? 1080 LEU   A CD2   1 
ATOM   7944  C  CD2   B LEU   A  1  1082 ? -6.575  60.129  102.784 0.38 16.83 ? 1080 LEU   A CD2   1 
ATOM   7945  N  N     . ASP   A  1  1083 ? -5.378  58.353  100.027 1.00 16.35 ? 1081 ASP   A N     1 
ATOM   7946  C  CA    . ASP   A  1  1083 ? -6.295  58.404  98.890  1.00 20.55 ? 1081 ASP   A CA    1 
ATOM   7947  C  C     . ASP   A  1  1083 ? -7.457  57.470  99.212  1.00 20.51 ? 1081 ASP   A C     1 
ATOM   7948  O  O     . ASP   A  1  1083 ? -7.328  56.251  99.075  1.00 23.16 ? 1081 ASP   A O     1 
ATOM   7949  C  CB    . ASP   A  1  1083 ? -5.559  57.967  97.633  1.00 21.22 ? 1081 ASP   A CB    1 
ATOM   7950  C  CG    . ASP   A  1  1083 ? -6.397  58.102  96.385  1.00 31.62 ? 1081 ASP   A CG    1 
ATOM   7951  O  OD1   . ASP   A  1  1083 ? -7.472  58.731  96.455  1.00 31.41 ? 1081 ASP   A OD1   1 
ATOM   7952  O  OD2   . ASP   A  1  1083 ? -5.972  57.573  95.333  1.00 34.49 ? 1081 ASP   A OD2   1 
ATOM   7953  N  N     . LEU   A  1  1084 ? -8.574  58.045  99.653  1.00 19.29 ? 1082 LEU   A N     1 
ATOM   7954  C  CA    . LEU   A  1  1084 ? -9.692  57.267  100.157 1.00 18.91 ? 1082 LEU   A CA    1 
ATOM   7955  C  C     . LEU   A  1  1084 ? -10.945 57.576  99.364  1.00 18.32 ? 1082 LEU   A C     1 
ATOM   7956  O  O     . LEU   A  1  1084 ? -11.105 58.670  98.816  1.00 19.73 ? 1082 LEU   A O     1 
ATOM   7957  C  CB    . LEU   A  1  1084 ? -10.007 57.607  101.607 1.00 21.82 ? 1082 LEU   A CB    1 
ATOM   7958  C  CG    . LEU   A  1  1084 ? -8.904  57.431  102.632 1.00 22.30 ? 1082 LEU   A CG    1 
ATOM   7959  C  CD1   . LEU   A  1  1084 ? -9.369  58.054  103.942 1.00 23.29 ? 1082 LEU   A CD1   1 
ATOM   7960  C  CD2   . LEU   A  1  1084 ? -8.577  55.956  102.800 1.00 24.89 ? 1082 LEU   A CD2   1 
ATOM   7961  N  N     . GLU   A  1  1085 ? -11.829 56.593  99.311  1.00 19.05 ? 1083 GLU   A N     1 
ATOM   7962  C  CA    . GLU   A  1  1085 ? -13.186 56.811  98.846  1.00 16.63 ? 1083 GLU   A CA    1 
ATOM   7963  C  C     . GLU   A  1  1085 ? -14.096 56.806  100.063 1.00 19.47 ? 1083 GLU   A C     1 
ATOM   7964  O  O     . GLU   A  1  1085 ? -14.043 55.879  100.880 1.00 22.16 ? 1083 GLU   A O     1 
ATOM   7965  C  CB    . GLU   A  1  1085 ? -13.623 55.750  97.840  1.00 19.54 ? 1083 GLU   A CB    1 
ATOM   7966  C  CG    . GLU   A  1  1085 ? -15.087 55.967  97.458  1.00 23.06 ? 1083 GLU   A CG    1 
ATOM   7967  C  CD    . GLU   A  1  1085 ? -15.545 55.249  96.204  1.00 30.32 ? 1083 GLU   A CD    1 
ATOM   7968  O  OE1   . GLU   A  1  1085 ? -14.711 54.650  95.492  1.00 32.29 ? 1083 GLU   A OE1   1 
ATOM   7969  O  OE2   . GLU   A  1  1085 ? -16.770 55.294  95.938  1.00 31.65 ? 1083 GLU   A OE2   1 
ATOM   7970  N  N     . LEU   A  1  1086 ? -14.877 57.863  100.208 1.00 19.78 ? 1084 LEU   A N     1 
ATOM   7971  C  CA    . LEU   A  1  1086 ? -15.752 58.014  101.359 1.00 18.99 ? 1084 LEU   A CA    1 
ATOM   7972  C  C     . LEU   A  1  1086 ? -17.142 57.480  101.029 1.00 22.85 ? 1084 LEU   A C     1 
ATOM   7973  O  O     . LEU   A  1  1086 ? -17.647 57.708  99.929  1.00 20.57 ? 1084 LEU   A O     1 
ATOM   7974  C  CB    . LEU   A  1  1086 ? -15.858 59.486  101.740 1.00 20.71 ? 1084 LEU   A CB    1 
ATOM   7975  C  CG    . LEU   A  1  1086 ? -14.505 60.157  101.997 1.00 24.36 ? 1084 LEU   A CG    1 
ATOM   7976  C  CD1   . LEU   A  1  1086 ? -14.709 61.597  102.434 1.00 21.49 ? 1084 LEU   A CD1   1 
ATOM   7977  C  CD2   . LEU   A  1  1086 ? -13.708 59.384  103.046 1.00 25.60 ? 1084 LEU   A CD2   1 
ATOM   7978  N  N     . PRO   A  1  1087 ? -17.756 56.761  101.967 1.00 22.36 ? 1085 PRO   A N     1 
ATOM   7979  C  CA    . PRO   A  1  1087 ? -19.100 56.227  101.722 1.00 25.24 ? 1085 PRO   A CA    1 
ATOM   7980  C  C     . PRO   A  1  1087 ? -20.084 57.351  101.460 1.00 22.23 ? 1085 PRO   A C     1 
ATOM   7981  O  O     . PRO   A  1  1087 ? -20.040 58.405  102.094 1.00 25.33 ? 1085 PRO   A O     1 
ATOM   7982  C  CB    . PRO   A  1  1087 ? -19.446 55.505  103.029 1.00 27.48 ? 1085 PRO   A CB    1 
ATOM   7983  C  CG    . PRO   A  1  1087 ? -18.149 55.276  103.718 1.00 29.04 ? 1085 PRO   A CG    1 
ATOM   7984  C  CD    . PRO   A  1  1087 ? -17.201 56.348  103.266 1.00 23.02 ? 1085 PRO   A CD    1 
ATOM   7985  N  N     . GLY   A  1  1088 ? -20.978 57.117  100.511 1.00 23.26 ? 1086 GLY   A N     1 
ATOM   7986  C  CA    . GLY   A  1  1088 ? -21.964 58.101  100.161 1.00 23.29 ? 1086 GLY   A CA    1 
ATOM   7987  C  C     . GLY   A  1  1088 ? -23.064 57.501  99.316  1.00 17.39 ? 1086 GLY   A C     1 
ATOM   7988  O  O     . GLY   A  1  1088 ? -23.270 56.286  99.277  1.00 20.54 ? 1086 GLY   A O     1 
ATOM   7989  N  N     . PRO   A  1  1089 ? -23.779 58.356  98.602  1.00 19.66 ? 1087 PRO   A N     1 
ATOM   7990  C  CA    . PRO   A  1  1089 ? -24.887 57.876  97.778  1.00 18.99 ? 1087 PRO   A CA    1 
ATOM   7991  C  C     . PRO   A  1  1089 ? -24.383 57.100  96.572  1.00 22.30 ? 1087 PRO   A C     1 
ATOM   7992  O  O     . PRO   A  1  1089 ? -23.244 57.250  96.119  1.00 20.10 ? 1087 PRO   A O     1 
ATOM   7993  C  CB    . PRO   A  1  1089 ? -25.565 59.173  97.329  1.00 22.37 ? 1087 PRO   A CB    1 
ATOM   7994  C  CG    . PRO   A  1  1089 ? -24.433 60.173  97.310  1.00 25.34 ? 1087 PRO   A CG    1 
ATOM   7995  C  CD    . PRO   A  1  1089 ? -23.581 59.810  98.493  1.00 20.41 ? 1087 PRO   A CD    1 
ATOM   7996  N  N     . VAL   A  1  1090 ? -25.263 56.244  96.056  1.00 19.40 ? 1088 VAL   A N     1 
ATOM   7997  C  CA    . VAL   A  1  1090 ? -24.992 55.597  94.784  1.00 16.88 ? 1088 VAL   A CA    1 
ATOM   7998  C  C     . VAL   A  1  1090 ? -24.874 56.645  93.684  1.00 18.58 ? 1088 VAL   A C     1 
ATOM   7999  O  O     . VAL   A  1  1090 ? -25.358 57.781  93.797  1.00 18.66 ? 1088 VAL   A O     1 
ATOM   8000  C  CB    . VAL   A  1  1090 ? -26.056 54.550  94.425  1.00 19.83 ? 1088 VAL   A CB    1 
ATOM   8001  C  CG1   . VAL   A  1  1090 ? -26.133 53.483  95.513  1.00 21.34 ? 1088 VAL   A CG1   1 
ATOM   8002  C  CG2   . VAL   A  1  1090 ? -27.408 55.222  94.216  1.00 21.05 ? 1088 VAL   A CG2   1 
ATOM   8003  N  N     . GLY   A  1  1091 ? -24.219 56.248  92.598  1.00 17.99 ? 1089 GLY   A N     1 
ATOM   8004  C  CA    . GLY   A  1  1091 ? -24.117 57.135  91.455  1.00 21.90 ? 1089 GLY   A CA    1 
ATOM   8005  C  C     . GLY   A  1  1091 ? -23.162 58.282  91.659  1.00 17.64 ? 1089 GLY   A C     1 
ATOM   8006  O  O     . GLY   A  1  1091 ? -23.185 59.246  90.895  1.00 18.33 ? 1089 GLY   A O     1 
ATOM   8007  N  N     . GLU   A  1  1092 ? -22.309 58.193  92.672  1.00 17.30 ? 1090 GLU   A N     1 
ATOM   8008  C  CA    . GLU   A  1  1092 ? -21.328 59.224  92.941  1.00 20.01 ? 1090 GLU   A CA    1 
ATOM   8009  C  C     . GLU   A  1  1092 ? -20.110 58.531  93.525  1.00 18.62 ? 1090 GLU   A C     1 
ATOM   8010  O  O     . GLU   A  1  1092 ? -20.238 57.533  94.241  1.00 20.25 ? 1090 GLU   A O     1 
ATOM   8011  C  CB    . GLU   A  1  1092 ? -21.895 60.200  93.974  1.00 21.77 ? 1090 GLU   A CB    1 
ATOM   8012  C  CG    . GLU   A  1  1092 ? -21.400 61.626  93.873  1.00 26.20 ? 1090 GLU   A CG    1 
ATOM   8013  C  CD    . GLU   A  1  1092 ? -22.206 62.550  94.776  1.00 28.37 ? 1090 GLU   A CD    1 
ATOM   8014  O  OE1   . GLU   A  1  1092 ? -21.979 62.509  96.003  1.00 24.10 ? 1090 GLU   A OE1   1 
ATOM   8015  O  OE2   . GLU   A  1  1092 ? -23.089 63.282  94.263  1.00 29.67 ? 1090 GLU   A OE2   1 
ATOM   8016  N  N     . ARG   A  1  1093 ? -18.930 59.034  93.195  1.00 16.20 ? 1091 ARG   A N     1 
ATOM   8017  C  CA    . ARG   A  1  1093 ? -17.706 58.613  93.863  1.00 19.41 ? 1091 ARG   A CA    1 
ATOM   8018  C  C     . ARG   A  1  1093 ? -17.135 59.826  94.570  1.00 17.64 ? 1091 ARG   A C     1 
ATOM   8019  O  O     . ARG   A  1  1093 ? -16.926 60.875  93.953  1.00 17.92 ? 1091 ARG   A O     1 
ATOM   8020  C  CB    . ARG   A  1  1093 ? -16.694 58.008  92.889  1.00 21.38 ? 1091 ARG   A CB    1 
ATOM   8021  C  CG    . ARG   A  1  1093 ? -16.916 56.527  92.618  1.00 31.85 ? 1091 ARG   A CG    1 
ATOM   8022  C  CD    . ARG   A  1  1093 ? -15.634 55.845  92.135  1.00 40.96 ? 1091 ARG   A CD    1 
ATOM   8023  N  NE    . ARG   A  1  1093 ? -15.050 56.558  91.007  1.00 45.55 ? 1091 ARG   A NE    1 
ATOM   8024  C  CZ    . ARG   A  1  1093 ? -15.399 56.374  89.740  1.00 46.31 ? 1091 ARG   A CZ    1 
ATOM   8025  N  NH1   . ARG   A  1  1093 ? -16.313 55.479  89.398  1.00 43.77 ? 1091 ARG   A NH1   1 
ATOM   8026  N  NH2   . ARG   A  1  1093 ? -14.820 57.109  88.793  1.00 47.06 ? 1091 ARG   A NH2   1 
ATOM   8027  N  N     . ASN   A  1  1094 ? -16.941 59.703  95.870  1.00 16.68 ? 1092 ASN   A N     1 
ATOM   8028  C  CA    . ASN   A  1  1094 ? -16.468 60.817  96.669  1.00 15.05 ? 1092 ASN   A CA    1 
ATOM   8029  C  C     . ASN   A  1  1094 ? -15.108 60.462  97.226  1.00 15.52 ? 1092 ASN   A C     1 
ATOM   8030  O  O     . ASN   A  1  1094 ? -14.983 59.514  98.006  1.00 17.50 ? 1092 ASN   A O     1 
ATOM   8031  C  CB    . ASN   A  1  1094 ? -17.485 61.138  97.752  1.00 14.97 ? 1092 ASN   A CB    1 
ATOM   8032  C  CG    . ASN   A  1  1094 ? -18.703 61.777  97.173  1.00 17.17 ? 1092 ASN   A CG    1 
ATOM   8033  O  OD1   . ASN   A  1  1094 ? -18.631 62.906  96.698  1.00 17.79 ? 1092 ASN   A OD1   1 
ATOM   8034  N  ND2   . ASN   A  1  1094 ? -19.831 61.056  97.175  1.00 19.42 ? 1092 ASN   A ND2   1 
ATOM   8035  N  N     . LEU   A  1  1095 ? -14.098 61.202  96.791  1.00 16.05 ? 1093 LEU   A N     1 
ATOM   8036  C  CA    . LEU   A  1  1095 ? -12.711 60.876  97.063  1.00 16.97 ? 1093 LEU   A CA    1 
ATOM   8037  C  C     . LEU   A  1  1095 ? -12.116 61.923  97.982  1.00 18.03 ? 1093 LEU   A C     1 
ATOM   8038  O  O     . LEU   A  1  1095 ? -12.493 63.096  97.956  1.00 17.83 ? 1093 LEU   A O     1 
ATOM   8039  C  CB    . LEU   A  1  1095 ? -11.918 60.849  95.759  1.00 19.05 ? 1093 LEU   A CB    1 
ATOM   8040  C  CG    . LEU   A  1  1095 ? -12.566 59.924  94.720  1.00 22.18 ? 1093 LEU   A CG    1 
ATOM   8041  C  CD1   . LEU   A  1  1095 ? -11.808 59.987  93.415  1.00 27.02 ? 1093 LEU   A CD1   1 
ATOM   8042  C  CD2   . LEU   A  1  1095 ? -12.664 58.487  95.234  1.00 25.15 ? 1093 LEU   A CD2   1 
ATOM   8043  N  N     . TYR   A  1  1096 ? -11.155 61.489  98.782  1.00 16.83 ? 1094 TYR   A N     1 
ATOM   8044  C  CA    . TYR   A  1  1096 ? -10.529 62.363  99.757  1.00 15.89 ? 1094 TYR   A CA    1 
ATOM   8045  C  C     . TYR   A  1  1096 ? -9.057  62.027  99.717  1.00 16.49 ? 1094 TYR   A C     1 
ATOM   8046  O  O     . TYR   A  1  1096 ? -8.688  60.860  99.889  1.00 18.59 ? 1094 TYR   A O     1 
ATOM   8047  C  CB    . TYR   A  1  1096 ? -11.092 62.065  101.138 1.00 16.48 ? 1094 TYR   A CB    1 
ATOM   8048  C  CG    . TYR   A  1  1096 ? -10.389 62.741  102.283 1.00 18.18 ? 1094 TYR   A CG    1 
ATOM   8049  C  CD1   . TYR   A  1  1096 ? -10.748 64.019  102.678 1.00 17.19 ? 1094 TYR   A CD1   1 
ATOM   8050  C  CD2   . TYR   A  1  1096 ? -9.386  62.090  102.986 1.00 17.34 ? 1094 TYR   A CD2   1 
ATOM   8051  C  CE1   . TYR   A  1  1096 ? -10.124 64.636  103.749 1.00 19.81 ? 1094 TYR   A CE1   1 
ATOM   8052  C  CE2   . TYR   A  1  1096 ? -8.749  62.696  104.058 1.00 18.47 ? 1094 TYR   A CE2   1 
ATOM   8053  C  CZ    . TYR   A  1  1096 ? -9.118  63.973  104.430 1.00 16.89 ? 1094 TYR   A CZ    1 
ATOM   8054  O  OH    . TYR   A  1  1096 ? -8.528  64.585  105.505 1.00 19.70 ? 1094 TYR   A OH    1 
ATOM   8055  N  N     . THR   A  1  1097 ? -8.235  63.035  99.456  1.00 16.54 ? 1095 THR   A N     1 
ATOM   8056  C  CA    . THR   A  1  1097 ? -6.820  62.803  99.214  1.00 15.77 ? 1095 THR   A CA    1 
ATOM   8057  C  C     . THR   A  1  1097 ? -6.003  63.855  99.946  1.00 17.28 ? 1095 THR   A C     1 
ATOM   8058  O  O     . THR   A  1  1097 ? -6.455  64.982  100.150 1.00 17.46 ? 1095 THR   A O     1 
ATOM   8059  C  CB    . THR   A  1  1097 ? -6.480  62.841  97.713  1.00 22.12 ? 1095 THR   A CB    1 
ATOM   8060  O  OG1   . THR   A  1  1097 ? -6.813  64.123  97.170  1.00 24.55 ? 1095 THR   A OG1   1 
ATOM   8061  C  CG2   . THR   A  1  1097 ? -7.251  61.789  96.962  1.00 19.95 ? 1095 THR   A CG2   1 
ATOM   8062  N  N     . LEU   A  1  1098 ? -4.791  63.477  100.349 1.00 16.21 ? 1096 LEU   A N     1 
ATOM   8063  C  CA    . LEU   A  1  1098 ? -3.871  64.392  101.010 1.00 17.76 ? 1096 LEU   A CA    1 
ATOM   8064  C  C     . LEU   A  1  1098 ? -2.712  64.684  100.074 1.00 14.93 ? 1096 LEU   A C     1 
ATOM   8065  O  O     . LEU   A  1  1098 ? -2.000  63.767  99.649  1.00 15.56 ? 1096 LEU   A O     1 
ATOM   8066  C  CB    . LEU   A  1  1098 ? -3.357  63.822  102.331 1.00 16.65 ? 1096 LEU   A CB    1 
ATOM   8067  C  CG    . LEU   A  1  1098 ? -4.463  63.631  103.365 1.00 15.49 ? 1096 LEU   A CG    1 
ATOM   8068  C  CD1   . LEU   A  1  1098 ? -3.831  63.137  104.651 1.00 17.20 ? 1096 LEU   A CD1   1 
ATOM   8069  C  CD2   . LEU   A  1  1098 ? -5.199  64.941  103.592 1.00 17.06 ? 1096 LEU   A CD2   1 
ATOM   8070  N  N     . HIS   A  1  1099 ? -2.526  65.962  99.778  1.00 15.30 ? 1097 HIS   A N     1 
ATOM   8071  C  CA    . HIS   A  1  1099 ? -1.491  66.458  98.883  1.00 15.80 ? 1097 HIS   A CA    1 
ATOM   8072  C  C     . HIS   A  1  1099 ? -0.563  67.392  99.642  1.00 17.06 ? 1097 HIS   A C     1 
ATOM   8073  O  O     . HIS   A  1  1099 ? -0.820  67.774  100.782 1.00 17.01 ? 1097 HIS   A O     1 
ATOM   8074  C  CB    . HIS   A  1  1099 ? -2.122  67.246  97.736  1.00 18.72 ? 1097 HIS   A CB    1 
ATOM   8075  C  CG    . HIS   A  1  1099 ? -3.070  66.447  96.910  1.00 21.18 ? 1097 HIS   A CG    1 
ATOM   8076  N  ND1   . HIS   A  1  1099 ? -2.731  65.941  95.674  1.00 25.00 ? 1097 HIS   A ND1   1 
ATOM   8077  C  CD2   . HIS   A  1  1099 ? -4.342  66.049  97.147  1.00 22.59 ? 1097 HIS   A CD2   1 
ATOM   8078  C  CE1   . HIS   A  1  1099 ? -3.760  65.277  95.178  1.00 25.67 ? 1097 HIS   A CE1   1 
ATOM   8079  N  NE2   . HIS   A  1  1099 ? -4.748  65.324  96.053  1.00 24.57 ? 1097 HIS   A NE2   1 
ATOM   8080  N  N     . ALA   A  1  1100 ? 0.532   67.768  98.986  1.00 17.89 ? 1098 ALA   A N     1 
ATOM   8081  C  CA    . ALA   A  1  1100 ? 1.371   68.818  99.534  1.00 17.75 ? 1098 ALA   A CA    1 
ATOM   8082  C  C     . ALA   A  1  1100 ? 0.587   70.123  99.580  1.00 19.00 ? 1098 ALA   A C     1 
ATOM   8083  O  O     . ALA   A  1  1100 ? -0.334  70.351  98.791  1.00 20.08 ? 1098 ALA   A O     1 
ATOM   8084  C  CB    . ALA   A  1  1100 ? 2.607   68.995  98.654  1.00 18.47 ? 1098 ALA   A CB    1 
ATOM   8085  N  N     . ARG   A  1  1101 ? 0.943   70.980  100.531 1.00 18.09 ? 1099 ARG   A N     1 
ATOM   8086  C  CA    A ARG   A  1  1101 ? 0.313   72.295  100.602 0.55 19.76 ? 1099 ARG   A CA    1 
ATOM   8087  C  CA    B ARG   A  1  1101 ? 0.315   72.293  100.603 0.45 19.76 ? 1099 ARG   A CA    1 
ATOM   8088  C  C     . ARG   A  1  1101 ? 0.873   73.240  99.552  1.00 18.49 ? 1099 ARG   A C     1 
ATOM   8089  O  O     . ARG   A  1  1101 ? 0.132   74.038  98.975  1.00 20.26 ? 1099 ARG   A O     1 
ATOM   8090  C  CB    A ARG   A  1  1101 ? 0.505   72.911  101.987 0.55 20.06 ? 1099 ARG   A CB    1 
ATOM   8091  C  CB    B ARG   A  1  1101 ? 0.521   72.893  101.990 0.45 20.06 ? 1099 ARG   A CB    1 
ATOM   8092  C  CG    A ARG   A  1  1101 ? -0.207  72.180  103.102 0.55 21.20 ? 1099 ARG   A CG    1 
ATOM   8093  C  CG    B ARG   A  1  1101 ? -0.387  72.320  103.046 0.45 21.52 ? 1099 ARG   A CG    1 
ATOM   8094  C  CD    A ARG   A  1  1101 ? -0.114  72.931  104.426 0.55 20.24 ? 1099 ARG   A CD    1 
ATOM   8095  C  CD    B ARG   A  1  1101 ? -1.080  73.440  103.792 0.45 22.23 ? 1099 ARG   A CD    1 
ATOM   8096  N  NE    A ARG   A  1  1101 ? -1.000  74.088  104.511 0.55 20.16 ? 1099 ARG   A NE    1 
ATOM   8097  N  NE    B ARG   A  1  1101 ? -2.194  72.964  104.602 0.45 21.06 ? 1099 ARG   A NE    1 
ATOM   8098  C  CZ    A ARG   A  1  1101 ? -2.251  74.045  104.955 0.55 21.73 ? 1099 ARG   A CZ    1 
ATOM   8099  C  CZ    B ARG   A  1  1101 ? -2.919  73.738  105.399 0.45 22.60 ? 1099 ARG   A CZ    1 
ATOM   8100  N  NH1   A ARG   A  1  1101 ? -2.815  72.906  105.332 0.55 21.99 ? 1099 ARG   A NH1   1 
ATOM   8101  N  NH1   B ARG   A  1  1101 ? -2.672  75.035  105.518 0.45 22.68 ? 1099 ARG   A NH1   1 
ATOM   8102  N  NH2   A ARG   A  1  1101 ? -2.956  75.172  105.020 0.55 22.72 ? 1099 ARG   A NH2   1 
ATOM   8103  N  NH2   B ARG   A  1  1101 ? -3.913  73.199  106.097 0.45 21.97 ? 1099 ARG   A NH2   1 
ATOM   8104  N  N     . GLY   A  1  1102 ? 2.171   73.178  99.308  1.00 17.96 ? 1100 GLY   A N     1 
ATOM   8105  C  CA    . GLY   A  1  1102 ? 2.794   74.095  98.380  1.00 20.91 ? 1100 GLY   A CA    1 
ATOM   8106  C  C     . GLY   A  1  1102 ? 4.175   74.468  98.860  1.00 18.08 ? 1100 GLY   A C     1 
ATOM   8107  O  O     . GLY   A  1  1102 ? 4.991   73.588  99.152  1.00 20.12 ? 1100 GLY   A O     1 
ATOM   8108  N  N     . ARG   A  1  1103 ? 4.464   75.761  98.944  1.00 18.58 ? 1101 ARG   A N     1 
ATOM   8109  C  CA    . ARG   A  1  1103 ? 5.759   76.214  99.429  1.00 16.43 ? 1101 ARG   A CA    1 
ATOM   8110  C  C     . ARG   A  1  1103 ? 5.588   76.683  100.866 1.00 16.63 ? 1101 ARG   A C     1 
ATOM   8111  O  O     . ARG   A  1  1103 ? 4.770   77.571  101.142 1.00 19.03 ? 1101 ARG   A O     1 
ATOM   8112  C  CB    . ARG   A  1  1103 ? 6.338   77.337  98.567  1.00 20.13 ? 1101 ARG   A CB    1 
ATOM   8113  C  CG    . ARG   A  1  1103 ? 7.803   77.647  98.937  1.00 20.51 ? 1101 ARG   A CG    1 
ATOM   8114  C  CD    . ARG   A  1  1103 ? 8.512   78.530  97.909  1.00 23.85 ? 1101 ARG   A CD    1 
ATOM   8115  N  NE    . ARG   A  1  1103 ? 8.533   77.910  96.588  1.00 26.51 ? 1101 ARG   A NE    1 
ATOM   8116  C  CZ    . ARG   A  1  1103 ? 9.529   77.182  96.091  1.00 30.18 ? 1101 ARG   A CZ    1 
ATOM   8117  N  NH1   . ARG   A  1  1103 ? 10.624  76.906  96.798  1.00 24.85 ? 1101 ARG   A NH1   1 
ATOM   8118  N  NH2   . ARG   A  1  1103 ? 9.427   76.717  94.850  1.00 32.59 ? 1101 ARG   A NH2   1 
ATOM   8119  N  N     . ILE   A  1  1104 ? 6.336   76.065  101.776 1.00 16.62 ? 1102 ILE   A N     1 
ATOM   8120  C  CA    . ILE   A  1  1104 ? 6.263   76.388  103.191 1.00 17.00 ? 1102 ILE   A CA    1 
ATOM   8121  C  C     . ILE   A  1  1104 ? 7.393   77.349  103.509 1.00 15.06 ? 1102 ILE   A C     1 
ATOM   8122  O  O     . ILE   A  1  1104 ? 8.547   77.103  103.138 1.00 17.12 ? 1102 ILE   A O     1 
ATOM   8123  C  CB    . ILE   A  1  1104 ? 6.390   75.118  104.044 1.00 18.21 ? 1102 ILE   A CB    1 
ATOM   8124  C  CG1   . ILE   A  1  1104 ? 5.390   74.056  103.585 1.00 17.45 ? 1102 ILE   A CG1   1 
ATOM   8125  C  CG2   . ILE   A  1  1104 ? 6.211   75.468  105.526 1.00 18.34 ? 1102 ILE   A CG2   1 
ATOM   8126  C  CD1   . ILE   A  1  1104 ? 3.935   74.459  103.756 1.00 19.12 ? 1102 ILE   A CD1   1 
ATOM   8127  N  N     . LEU   A  1  1105 ? 7.065   78.443  104.191 1.00 16.21 ? 1103 LEU   A N     1 
ATOM   8128  C  CA    . LEU   A  1  1105 ? 8.079   79.353  104.701 1.00 17.66 ? 1103 LEU   A CA    1 
ATOM   8129  C  C     . LEU   A  1  1105 ? 8.715   78.744  105.940 1.00 17.82 ? 1103 LEU   A C     1 
ATOM   8130  O  O     . LEU   A  1  1105 ? 8.016   78.430  106.906 1.00 19.03 ? 1103 LEU   A O     1 
ATOM   8131  C  CB    . LEU   A  1  1105 ? 7.436   80.686  105.063 1.00 19.46 ? 1103 LEU   A CB    1 
ATOM   8132  C  CG    . LEU   A  1  1105 ? 8.382   81.704  105.710 1.00 20.11 ? 1103 LEU   A CG    1 
ATOM   8133  C  CD1   . LEU   A  1  1105 ? 9.460   82.137  104.722 1.00 20.91 ? 1103 LEU   A CD1   1 
ATOM   8134  C  CD2   . LEU   A  1  1105 ? 7.579   82.912  106.182 1.00 20.54 ? 1103 LEU   A CD2   1 
ATOM   8135  N  N     . LEU   A  1  1106 ? 10.028  78.580  105.917 1.00 16.89 ? 1104 LEU   A N     1 
ATOM   8136  C  CA    . LEU   A  1  1106 ? 10.771  78.072  107.060 1.00 17.94 ? 1104 LEU   A CA    1 
ATOM   8137  C  C     . LEU   A  1  1106 ? 11.519  79.229  107.698 1.00 19.71 ? 1104 LEU   A C     1 
ATOM   8138  O  O     . LEU   A  1  1106 ? 12.287  79.927  107.026 1.00 19.49 ? 1104 LEU   A O     1 
ATOM   8139  C  CB    . LEU   A  1  1106 ? 11.774  76.996  106.653 1.00 18.12 ? 1104 LEU   A CB    1 
ATOM   8140  C  CG    . LEU   A  1  1106 ? 11.245  75.753  105.943 1.00 24.97 ? 1104 LEU   A CG    1 
ATOM   8141  C  CD1   . LEU   A  1  1106 ? 12.301  74.660  105.958 1.00 19.66 ? 1104 LEU   A CD1   1 
ATOM   8142  C  CD2   . LEU   A  1  1106 ? 9.937   75.233  106.512 1.00 20.87 ? 1104 LEU   A CD2   1 
ATOM   8143  N  N     . VAL   A  1  1107 ? 11.295  79.425  108.989 1.00 18.10 ? 1105 VAL   A N     1 
ATOM   8144  C  CA    . VAL   A  1  1107 ? 12.003  80.454  109.733 1.00 20.19 ? 1105 VAL   A CA    1 
ATOM   8145  C  C     . VAL   A  1  1107 ? 12.767  79.742  110.839 1.00 18.92 ? 1105 VAL   A C     1 
ATOM   8146  O  O     . VAL   A  1  1107 ? 12.291  79.666  111.978 1.00 20.55 ? 1105 VAL   A O     1 
ATOM   8147  C  CB    . VAL   A  1  1107 ? 11.035  81.520  110.264 1.00 18.70 ? 1105 VAL   A CB    1 
ATOM   8148  C  CG1   . VAL   A  1  1107 ? 11.813  82.691  110.824 1.00 21.07 ? 1105 VAL   A CG1   1 
ATOM   8149  C  CG2   . VAL   A  1  1107 ? 10.094  81.982  109.136 1.00 20.51 ? 1105 VAL   A CG2   1 
ATOM   8150  N  N     . PRO   A  1  1108 ? 13.940  79.192  110.554 1.00 18.01 ? 1106 PRO   A N     1 
ATOM   8151  C  CA    . PRO   A  1  1108 ? 14.685  78.456  111.574 1.00 20.25 ? 1106 PRO   A CA    1 
ATOM   8152  C  C     . PRO   A  1  1108 ? 15.545  79.391  112.410 1.00 23.28 ? 1106 PRO   A C     1 
ATOM   8153  O  O     . PRO   A  1  1108 ? 15.803  80.540  112.051 1.00 23.03 ? 1106 PRO   A O     1 
ATOM   8154  C  CB    . PRO   A  1  1108 ? 15.591  77.554  110.730 1.00 20.38 ? 1106 PRO   A CB    1 
ATOM   8155  C  CG    . PRO   A  1  1108 ? 15.876  78.381  109.521 1.00 21.05 ? 1106 PRO   A CG    1 
ATOM   8156  C  CD    . PRO   A  1  1108 ? 14.599  79.134  109.237 1.00 20.39 ? 1106 PRO   A CD    1 
ATOM   8157  N  N     . ALA   A  1  1109 ? 15.986  78.865  113.547 1.00 19.09 ? 1107 ALA   A N     1 
ATOM   8158  C  CA    . ALA   A  1  1109 ? 16.949  79.548  114.400 1.00 20.78 ? 1107 ALA   A CA    1 
ATOM   8159  C  C     . ALA   A  1  1109 ? 18.270  78.816  114.494 1.00 25.15 ? 1107 ALA   A C     1 
ATOM   8160  O  O     . ALA   A  1  1109 ? 19.318  79.457  114.602 1.00 27.18 ? 1107 ALA   A O     1 
ATOM   8161  C  CB    . ALA   A  1  1109 ? 16.381  79.734  115.815 1.00 22.11 ? 1107 ALA   A CB    1 
ATOM   8162  N  N     . THR   A  1  1110 ? 18.244  77.491  114.443 1.00 22.05 ? 1108 THR   A N     1 
ATOM   8163  C  CA    . THR   A  1  1110 ? 19.439  76.688  114.591 1.00 20.89 ? 1108 THR   A CA    1 
ATOM   8164  C  C     . THR   A  1  1110 ? 19.520  75.730  113.416 1.00 20.78 ? 1108 THR   A C     1 
ATOM   8165  O  O     . THR   A  1  1110 ? 18.533  75.473  112.722 1.00 19.46 ? 1108 THR   A O     1 
ATOM   8166  C  CB    . THR   A  1  1110 ? 19.418  75.869  115.887 1.00 23.74 ? 1108 THR   A CB    1 
ATOM   8167  O  OG1   . THR   A  1  1110 ? 18.316  74.955  115.863 1.00 21.87 ? 1108 THR   A OG1   1 
ATOM   8168  C  CG2   . THR   A  1  1110 ? 19.287  76.785  117.112 1.00 23.71 ? 1108 THR   A CG2   1 
ATOM   8169  N  N     . GLU   A  1  1111 ? 20.716  75.190  113.209 1.00 20.73 ? 1109 GLU   A N     1 
ATOM   8170  C  CA    . GLU   A  1  1111 ? 20.887  74.203  112.147 1.00 19.44 ? 1109 GLU   A CA    1 
ATOM   8171  C  C     . GLU   A  1  1111 ? 19.978  72.999  112.361 1.00 21.28 ? 1109 GLU   A C     1 
ATOM   8172  O  O     . GLU   A  1  1111 ? 19.299  72.544  111.429 1.00 19.66 ? 1109 GLU   A O     1 
ATOM   8173  C  CB    . GLU   A  1  1111 ? 22.346  73.771  112.072 1.00 22.56 ? 1109 GLU   A CB    1 
ATOM   8174  C  CG    . GLU   A  1  1111 ? 22.532  72.593  111.150 1.00 23.47 ? 1109 GLU   A CG    1 
ATOM   8175  C  CD    . GLU   A  1  1111 ? 23.989  72.250  110.953 1.00 28.16 ? 1109 GLU   A CD    1 
ATOM   8176  O  OE1   . GLU   A  1  1111 ? 24.671  73.027  110.258 1.00 28.05 ? 1109 GLU   A OE1   1 
ATOM   8177  O  OE2   . GLU   A  1  1111 ? 24.440  71.220  111.502 1.00 29.29 ? 1109 GLU   A OE2   1 
ATOM   8178  N  N     . SER   A  1  1112 ? 19.954  72.463  113.583 1.00 21.23 ? 1110 SER   A N     1 
ATOM   8179  C  CA    . SER   A  1  1112 ? 19.115  71.300  113.844 1.00 21.10 ? 1110 SER   A CA    1 
ATOM   8180  C  C     . SER   A  1  1112 ? 17.646  71.633  113.642 1.00 21.30 ? 1110 SER   A C     1 
ATOM   8181  O  O     . SER   A  1  1112 ? 16.897  70.842  113.058 1.00 20.95 ? 1110 SER   A O     1 
ATOM   8182  C  CB    . SER   A  1  1112 ? 19.348  70.759  115.248 1.00 25.49 ? 1110 SER   A CB    1 
ATOM   8183  O  OG    . SER   A  1  1112 ? 18.563  69.600  115.448 1.00 25.64 ? 1110 SER   A OG    1 
ATOM   8184  N  N     . GLY   A  1  1113 ? 17.217  72.810  114.097 1.00 21.75 ? 1111 GLY   A N     1 
ATOM   8185  C  CA    . GLY   A  1  1113 ? 15.842  73.205  113.856 1.00 17.66 ? 1111 GLY   A CA    1 
ATOM   8186  C  C     . GLY   A  1  1113 ? 15.526  73.283  112.376 1.00 17.21 ? 1111 GLY   A C     1 
ATOM   8187  O  O     . GLY   A  1  1113 ? 14.453  72.863  111.937 1.00 17.94 ? 1111 GLY   A O     1 
ATOM   8188  N  N     . LEU   A  1  1114 ? 16.458  73.819  111.584 1.00 18.75 ? 1112 LEU   A N     1 
ATOM   8189  C  CA    . LEU   A  1  1114 ? 16.248  73.868  110.143 1.00 19.08 ? 1112 LEU   A CA    1 
ATOM   8190  C  C     . LEU   A  1  1114 ? 16.094  72.469  109.568 1.00 17.58 ? 1112 LEU   A C     1 
ATOM   8191  O  O     . LEU   A  1  1114 ? 15.205  72.227  108.742 1.00 18.17 ? 1112 LEU   A O     1 
ATOM   8192  C  CB    . LEU   A  1  1114 ? 17.408  74.590  109.461 1.00 18.21 ? 1112 LEU   A CB    1 
ATOM   8193  C  CG    . LEU   A  1  1114 ? 17.403  74.531  107.931 1.00 20.62 ? 1112 LEU   A CG    1 
ATOM   8194  C  CD1   . LEU   A  1  1114 ? 16.097  75.115  107.368 1.00 19.48 ? 1112 LEU   A CD1   1 
ATOM   8195  C  CD2   . LEU   A  1  1114 ? 18.612  75.239  107.334 1.00 23.81 ? 1112 LEU   A CD2   1 
ATOM   8196  N  N     . TYR   A  1  1115 ? 16.949  71.538  109.992 1.00 18.53 ? 1113 TYR   A N     1 
ATOM   8197  C  CA    . TYR   A  1  1115 ? 16.865  70.185  109.449 1.00 17.89 ? 1113 TYR   A CA    1 
ATOM   8198  C  C     . TYR   A  1  1115 ? 15.533  69.533  109.807 1.00 17.96 ? 1113 TYR   A C     1 
ATOM   8199  O  O     . TYR   A  1  1115 ? 14.944  68.824  108.984 1.00 19.08 ? 1113 TYR   A O     1 
ATOM   8200  C  CB    . TYR   A  1  1115 ? 18.033  69.338  109.946 1.00 17.94 ? 1113 TYR   A CB    1 
ATOM   8201  C  CG    . TYR   A  1  1115 ? 19.399  69.759  109.440 1.00 17.18 ? 1113 TYR   A CG    1 
ATOM   8202  C  CD1   . TYR   A  1  1115 ? 19.542  70.630  108.370 1.00 17.13 ? 1113 TYR   A CD1   1 
ATOM   8203  C  CD2   . TYR   A  1  1115 ? 20.543  69.276  110.045 1.00 21.55 ? 1113 TYR   A CD2   1 
ATOM   8204  C  CE1   . TYR   A  1  1115 ? 20.809  70.996  107.907 1.00 20.50 ? 1113 TYR   A CE1   1 
ATOM   8205  C  CE2   . TYR   A  1  1115 ? 21.798  69.626  109.591 1.00 21.04 ? 1113 TYR   A CE2   1 
ATOM   8206  C  CZ    . TYR   A  1  1115 ? 21.919  70.496  108.528 1.00 24.12 ? 1113 TYR   A CZ    1 
ATOM   8207  O  OH    . TYR   A  1  1115 ? 23.173  70.860  108.092 1.00 23.60 ? 1113 TYR   A OH    1 
ATOM   8208  N  N     . HIS   A  1  1116 ? 15.063  69.733  111.042 1.00 17.10 ? 1114 HIS   A N     1 
ATOM   8209  C  CA    . HIS   A  1  1116 ? 13.755  69.216  111.430 1.00 18.63 ? 1114 HIS   A CA    1 
ATOM   8210  C  C     . HIS   A  1  1116 ? 12.643  69.892  110.643 1.00 18.15 ? 1114 HIS   A C     1 
ATOM   8211  O  O     . HIS   A  1  1116 ? 11.682  69.237  110.222 1.00 18.09 ? 1114 HIS   A O     1 
ATOM   8212  C  CB    . HIS   A  1  1116 ? 13.535  69.427  112.924 1.00 19.35 ? 1114 HIS   A CB    1 
ATOM   8213  C  CG    . HIS   A  1  1116 ? 14.176  68.386  113.786 1.00 21.23 ? 1114 HIS   A CG    1 
ATOM   8214  N  ND1   . HIS   A  1  1116 ? 15.483  68.473  114.219 1.00 24.35 ? 1114 HIS   A ND1   1 
ATOM   8215  C  CD2   . HIS   A  1  1116 ? 13.687  67.231  114.296 1.00 21.74 ? 1114 HIS   A CD2   1 
ATOM   8216  C  CE1   . HIS   A  1  1116 ? 15.766  67.420  114.967 1.00 24.59 ? 1114 HIS   A CE1   1 
ATOM   8217  N  NE2   . HIS   A  1  1116 ? 14.696  66.649  115.022 1.00 27.21 ? 1114 HIS   A NE2   1 
ATOM   8218  N  N     . GLN   A  1  1117 ? 12.734  71.211  110.461 1.00 16.52 ? 1115 GLN   A N     1 
ATOM   8219  C  CA    . GLN   A  1  1117 ? 11.714  71.902  109.683 1.00 16.75 ? 1115 GLN   A CA    1 
ATOM   8220  C  C     . GLN   A  1  1117 ? 11.687  71.396  108.252 1.00 15.23 ? 1115 GLN   A C     1 
ATOM   8221  O  O     . GLN   A  1  1117 ? 10.614  71.187  107.676 1.00 15.97 ? 1115 GLN   A O     1 
ATOM   8222  C  CB    . GLN   A  1  1117 ? 11.986  73.398  109.684 1.00 17.72 ? 1115 GLN   A CB    1 
ATOM   8223  C  CG    . GLN   A  1  1117 ? 11.741  74.081  110.996 1.00 18.14 ? 1115 GLN   A CG    1 
ATOM   8224  C  CD    . GLN   A  1  1117 ? 12.000  75.559  110.907 1.00 23.06 ? 1115 GLN   A CD    1 
ATOM   8225  O  OE1   . GLN   A  1  1117 ? 12.590  76.039  109.935 1.00 19.47 ? 1115 GLN   A OE1   1 
ATOM   8226  N  NE2   . GLN   A  1  1117 ? 11.559  76.297  111.919 1.00 18.80 ? 1115 GLN   A NE2   1 
ATOM   8227  N  N     . LEU   A  1  1118 ? 12.869  71.251  107.645 1.00 16.13 ? 1116 LEU   A N     1 
ATOM   8228  C  CA    . LEU   A  1  1118 ? 12.960  70.751  106.283 1.00 16.72 ? 1116 LEU   A CA    1 
ATOM   8229  C  C     . LEU   A  1  1118 ? 12.412  69.341  106.186 1.00 16.39 ? 1116 LEU   A C     1 
ATOM   8230  O  O     . LEU   A  1  1118 ? 11.691  69.010  105.236 1.00 17.27 ? 1116 LEU   A O     1 
ATOM   8231  C  CB    . LEU   A  1  1118 ? 14.416  70.753  105.846 1.00 19.35 ? 1116 LEU   A CB    1 
ATOM   8232  C  CG    . LEU   A  1  1118 ? 14.866  72.011  105.145 1.00 25.47 ? 1116 LEU   A CG    1 
ATOM   8233  C  CD1   . LEU   A  1  1118 ? 16.379  71.940  105.022 1.00 26.59 ? 1116 LEU   A CD1   1 
ATOM   8234  C  CD2   . LEU   A  1  1118 ? 14.182  72.103  103.778 1.00 27.24 ? 1116 LEU   A CD2   1 
ATOM   8235  N  N     . ALA   A  1  1119 ? 12.749  68.492  107.151 1.00 17.62 ? 1117 ALA   A N     1 
ATOM   8236  C  CA    . ALA   A  1  1119 ? 12.242  67.126  107.122 1.00 18.79 ? 1117 ALA   A CA    1 
ATOM   8237  C  C     . ALA   A  1  1119 ? 10.722  67.120  107.174 1.00 18.45 ? 1117 ALA   A C     1 
ATOM   8238  O  O     . ALA   A  1  1119 ? 10.069  66.428  106.389 1.00 18.17 ? 1117 ALA   A O     1 
ATOM   8239  C  CB    . ALA   A  1  1119 ? 12.830  66.319  108.273 1.00 19.45 ? 1117 ALA   A CB    1 
ATOM   8240  N  N     . ALA   A  1  1120 ? 10.134  67.920  108.065 1.00 15.58 ? 1118 ALA   A N     1 
ATOM   8241  C  CA    . ALA   A  1  1120 ? 8.676   67.959  108.154 1.00 14.43 ? 1118 ALA   A CA    1 
ATOM   8242  C  C     . ALA   A  1  1120 ? 8.071   68.415  106.836 1.00 18.14 ? 1118 ALA   A C     1 
ATOM   8243  O  O     . ALA   A  1  1120 ? 7.106   67.822  106.335 1.00 16.85 ? 1118 ALA   A O     1 
ATOM   8244  C  CB    . ALA   A  1  1120 ? 8.246   68.884  109.294 1.00 16.05 ? 1118 ALA   A CB    1 
ATOM   8245  N  N     . ALA   A  1  1121 ? 8.641   69.462  106.246 1.00 17.08 ? 1119 ALA   A N     1 
ATOM   8246  C  CA    . ALA   A  1  1121 ? 8.070   70.022  105.030 1.00 16.17 ? 1119 ALA   A CA    1 
ATOM   8247  C  C     . ALA   A  1  1121 ? 8.233   69.075  103.843 1.00 13.92 ? 1119 ALA   A C     1 
ATOM   8248  O  O     . ALA   A  1  1121 ? 7.299   68.898  103.048 1.00 14.97 ? 1119 ALA   A O     1 
ATOM   8249  C  CB    . ALA   A  1  1121 ? 8.713   71.374  104.732 1.00 19.35 ? 1119 ALA   A CB    1 
ATOM   8250  N  N     . LEU   A  1  1122 ? 9.423   68.500  103.680 1.00 15.74 ? 1120 LEU   A N     1 
ATOM   8251  C  CA    . LEU   A  1  1122 ? 9.657   67.587  102.561 1.00 14.19 ? 1120 LEU   A CA    1 
ATOM   8252  C  C     . LEU   A  1  1122 ? 8.865   66.299  102.711 1.00 15.82 ? 1120 LEU   A C     1 
ATOM   8253  O  O     . LEU   A  1  1122 ? 8.380   65.752  101.718 1.00 15.75 ? 1120 LEU   A O     1 
ATOM   8254  C  CB    . LEU   A  1  1122 ? 11.138  67.259  102.449 1.00 16.07 ? 1120 LEU   A CB    1 
ATOM   8255  C  CG    . LEU   A  1  1122 ? 12.046  68.446  102.129 1.00 17.72 ? 1120 LEU   A CG    1 
ATOM   8256  C  CD1   . LEU   A  1  1122 ? 13.488  68.012  102.207 1.00 19.64 ? 1120 LEU   A CD1   1 
ATOM   8257  C  CD2   . LEU   A  1  1122 ? 11.699  69.037  100.765 1.00 16.80 ? 1120 LEU   A CD2   1 
ATOM   8258  N  N     . ALA   A  1  1123 ? 8.731   65.794  103.938 1.00 15.85 ? 1121 ALA   A N     1 
ATOM   8259  C  CA    . ALA   A  1  1123 ? 7.979   64.561  104.150 1.00 15.34 ? 1121 ALA   A CA    1 
ATOM   8260  C  C     . ALA   A  1  1123 ? 6.528   64.713  103.745 1.00 15.60 ? 1121 ALA   A C     1 
ATOM   8261  O  O     . ALA   A  1  1123 ? 5.867   63.715  103.448 1.00 16.48 ? 1121 ALA   A O     1 
ATOM   8262  C  CB    . ALA   A  1  1123 ? 8.038   64.158  105.627 1.00 15.28 ? 1121 ALA   A CB    1 
ATOM   8263  N  N     . THR   A  1  1124 ? 6.029   65.943  103.717 1.00 13.83 ? 1122 THR   A N     1 
ATOM   8264  C  CA    . THR   A  1  1124 ? 4.659   66.226  103.333 1.00 13.06 ? 1122 THR   A CA    1 
ATOM   8265  C  C     . THR   A  1  1124 ? 4.579   66.786  101.921 1.00 15.75 ? 1122 THR   A C     1 
ATOM   8266  O  O     . THR   A  1  1124 ? 3.537   67.309  101.521 1.00 15.29 ? 1122 THR   A O     1 
ATOM   8267  C  CB    . THR   A  1  1124 ? 4.001   67.136  104.379 1.00 17.65 ? 1122 THR   A CB    1 
ATOM   8268  O  OG1   . THR   A  1  1124 ? 4.878   68.221  104.681 1.00 16.64 ? 1122 THR   A OG1   1 
ATOM   8269  C  CG2   . THR   A  1  1124 ? 3.735   66.349  105.678 1.00 16.93 ? 1122 THR   A CG2   1 
ATOM   8270  N  N     . GLY   A  1  1125 ? 5.654   66.650  101.151 1.00 14.92 ? 1123 GLY   A N     1 
ATOM   8271  C  CA    . GLY   A  1  1125 ? 5.631   66.894  99.724  1.00 15.19 ? 1123 GLY   A CA    1 
ATOM   8272  C  C     . GLY   A  1  1125 ? 5.849   68.329  99.319  1.00 16.76 ? 1123 GLY   A C     1 
ATOM   8273  O  O     . GLY   A  1  1125 ? 5.772   68.641  98.121  1.00 17.62 ? 1123 GLY   A O     1 
ATOM   8274  N  N     . ASN   A  1  1126 ? 6.133   69.206  100.270 1.00 16.31 ? 1124 ASN   A N     1 
ATOM   8275  C  CA    . ASN   A  1  1126 ? 6.198   70.633  100.012 1.00 15.97 ? 1124 ASN   A CA    1 
ATOM   8276  C  C     . ASN   A  1  1126 ? 7.577   71.045  99.530  1.00 15.52 ? 1124 ASN   A C     1 
ATOM   8277  O  O     . ASN   A  1  1126 ? 8.580   70.363  99.765  1.00 17.79 ? 1124 ASN   A O     1 
ATOM   8278  C  CB    . ASN   A  1  1126 ? 5.916   71.387  101.307 1.00 14.69 ? 1124 ASN   A CB    1 
ATOM   8279  C  CG    . ASN   A  1  1126 ? 4.544   71.103  101.835 1.00 15.60 ? 1124 ASN   A CG    1 
ATOM   8280  O  OD1   . ASN   A  1  1126 ? 3.558   71.469  101.213 1.00 17.05 ? 1124 ASN   A OD1   1 
ATOM   8281  N  ND2   . ASN   A  1  1126 ? 4.468   70.417  102.968 1.00 14.57 ? 1124 ASN   A ND2   1 
ATOM   8282  N  N     . SER   A  1  1127 ? 7.617   72.205  98.878  1.00 16.17 ? 1125 SER   A N     1 
ATOM   8283  C  CA    . SER   A  1  1127 ? 8.860   72.937  98.723  1.00 16.49 ? 1125 SER   A CA    1 
ATOM   8284  C  C     . SER   A  1  1127 ? 8.966   73.923  99.872  1.00 15.72 ? 1125 SER   A C     1 
ATOM   8285  O  O     . SER   A  1  1127 ? 8.036   74.088  100.659 1.00 17.41 ? 1125 SER   A O     1 
ATOM   8286  C  CB    . SER   A  1  1127 ? 8.880   73.686  97.393  1.00 17.41 ? 1125 SER   A CB    1 
ATOM   8287  O  OG    . SER   A  1  1127 ? 7.772   74.547  97.279  1.00 22.68 ? 1125 SER   A OG    1 
ATOM   8288  N  N     . VAL   A  1  1128 ? 10.120  74.570  99.987  1.00 18.47 ? 1126 VAL   A N     1 
ATOM   8289  C  CA    . VAL   A  1  1128 ? 10.326  75.490  101.094 1.00 18.35 ? 1126 VAL   A CA    1 
ATOM   8290  C  C     . VAL   A  1  1128 ? 10.964  76.771  100.597 1.00 19.66 ? 1126 VAL   A C     1 
ATOM   8291  O  O     . VAL   A  1  1128 ? 11.693  76.790  99.601  1.00 19.53 ? 1126 VAL   A O     1 
ATOM   8292  C  CB    . VAL   A  1  1128 ? 11.177  74.877  102.220 1.00 17.74 ? 1126 VAL   A CB    1 
ATOM   8293  C  CG1   . VAL   A  1  1128 ? 10.519  73.640  102.756 1.00 19.46 ? 1126 VAL   A CG1   1 
ATOM   8294  C  CG2   . VAL   A  1  1128 ? 12.583  74.572  101.702 1.00 20.35 ? 1126 VAL   A CG2   1 
ATOM   8295  N  N     . ALA   A  1  1129 ? 10.685  77.849  101.312 1.00 19.25 ? 1127 ALA   A N     1 
ATOM   8296  C  CA    . ALA   A  1  1129 ? 11.477  79.064  101.230 1.00 20.66 ? 1127 ALA   A CA    1 
ATOM   8297  C  C     . ALA   A  1  1129 ? 12.040  79.300  102.620 1.00 17.43 ? 1127 ALA   A C     1 
ATOM   8298  O  O     . ALA   A  1  1129 ? 11.278  79.425  103.584 1.00 20.77 ? 1127 ALA   A O     1 
ATOM   8299  C  CB    . ALA   A  1  1129 ? 10.625  80.247  100.777 1.00 23.67 ? 1127 ALA   A CB    1 
ATOM   8300  N  N     . ILE   A  1  1130 ? 13.365  79.312  102.731 1.00 17.69 ? 1128 ILE   A N     1 
ATOM   8301  C  CA    . ILE   A  1  1130 ? 14.034  79.401  104.024 1.00 19.77 ? 1128 ILE   A CA    1 
ATOM   8302  C  C     . ILE   A  1  1130 ? 14.453  80.840  104.248 1.00 22.35 ? 1128 ILE   A C     1 
ATOM   8303  O  O     . ILE   A  1  1130 ? 15.062  81.459  103.370 1.00 22.77 ? 1128 ILE   A O     1 
ATOM   8304  C  CB    . ILE   A  1  1130 ? 15.261  78.481  104.111 1.00 18.47 ? 1128 ILE   A CB    1 
ATOM   8305  C  CG1   . ILE   A  1  1130 ? 14.920  77.062  103.659 1.00 21.01 ? 1128 ILE   A CG1   1 
ATOM   8306  C  CG2   . ILE   A  1  1130 ? 15.804  78.486  105.542 1.00 19.66 ? 1128 ILE   A CG2   1 
ATOM   8307  C  CD1   . ILE   A  1  1130 ? 16.138  76.187  103.543 1.00 21.26 ? 1128 ILE   A CD1   1 
ATOM   8308  N  N     . ASP   A  1  1131 ? 14.160  81.357  105.437 1.00 20.86 ? 1129 ASP   A N     1 
ATOM   8309  C  CA    . ASP   A  1  1131 ? 14.538  82.715  105.797 1.00 19.52 ? 1129 ASP   A CA    1 
ATOM   8310  C  C     . ASP   A  1  1131 ? 16.042  82.911  105.667 1.00 21.72 ? 1129 ASP   A C     1 
ATOM   8311  O  O     . ASP   A  1  1131 ? 16.817  82.282  106.390 1.00 23.14 ? 1129 ASP   A O     1 
ATOM   8312  C  CB    . ASP   A  1  1131 ? 14.097  82.999  107.227 1.00 20.50 ? 1129 ASP   A CB    1 
ATOM   8313  C  CG    . ASP   A  1  1131 ? 14.453  84.386  107.670 1.00 28.50 ? 1129 ASP   A CG    1 
ATOM   8314  O  OD1   . ASP   A  1  1131 ? 14.568  85.269  106.797 1.00 25.28 ? 1129 ASP   A OD1   1 
ATOM   8315  O  OD2   . ASP   A  1  1131 ? 14.613  84.585  108.889 1.00 26.64 ? 1129 ASP   A OD2   1 
ATOM   8316  N  N     . ALA   A  1  1132 ? 16.455  83.769  104.730 1.00 22.80 ? 1130 ALA   A N     1 
ATOM   8317  C  CA    . ALA   A  1  1132 ? 17.873  84.036  104.528 1.00 25.80 ? 1130 ALA   A CA    1 
ATOM   8318  C  C     . ALA   A  1  1132 ? 18.475  84.761  105.721 1.00 29.41 ? 1130 ALA   A C     1 
ATOM   8319  O  O     . ALA   A  1  1132 ? 19.680  84.643  105.977 1.00 29.69 ? 1130 ALA   A O     1 
ATOM   8320  C  CB    . ALA   A  1  1132 ? 18.066  84.851  103.245 1.00 26.01 ? 1130 ALA   A CB    1 
ATOM   8321  N  N     . ALA   A  1  1133 ? 17.659  85.501  106.469 1.00 28.00 ? 1131 ALA   A N     1 
ATOM   8322  C  CA    . ALA   A  1  1133 ? 18.169  86.220  107.631 1.00 31.34 ? 1131 ALA   A CA    1 
ATOM   8323  C  C     . ALA   A  1  1133 ? 18.553  85.294  108.776 1.00 28.85 ? 1131 ALA   A C     1 
ATOM   8324  O  O     . ALA   A  1  1133 ? 19.129  85.758  109.763 1.00 30.85 ? 1131 ALA   A O     1 
ATOM   8325  C  CB    . ALA   A  1  1133 ? 17.156  87.263  108.104 1.00 29.09 ? 1131 ALA   A CB    1 
ATOM   8326  N  N     . SER   A  1  1134 ? 18.246  84.002  108.673 1.00 27.26 ? 1132 SER   A N     1 
ATOM   8327  C  CA    . SER   A  1  1134 ? 18.667  83.058  109.695 1.00 24.80 ? 1132 SER   A CA    1 
ATOM   8328  C  C     . SER   A  1  1134 ? 20.171  82.845  109.696 1.00 24.23 ? 1132 SER   A C     1 
ATOM   8329  O  O     . SER   A  1  1134 ? 20.708  82.350  110.690 1.00 25.53 ? 1132 SER   A O     1 
ATOM   8330  C  CB    . SER   A  1  1134 ? 18.007  81.704  109.447 1.00 25.35 ? 1132 SER   A CB    1 
ATOM   8331  O  OG    . SER   A  1  1134 ? 18.494  81.141  108.240 1.00 25.31 ? 1132 SER   A OG    1 
ATOM   8332  N  N     . GLY   A  1  1135 ? 20.854  83.185  108.606 1.00 24.95 ? 1133 GLY   A N     1 
ATOM   8333  C  CA    . GLY   A  1  1135 ? 22.280  82.940  108.517 1.00 25.78 ? 1133 GLY   A CA    1 
ATOM   8334  C  C     . GLY   A  1  1135 ? 22.673  81.483  108.450 1.00 25.93 ? 1133 GLY   A C     1 
ATOM   8335  O  O     . GLY   A  1  1135 ? 23.826  81.149  108.721 1.00 28.88 ? 1133 GLY   A O     1 
ATOM   8336  N  N     . LEU   A  1  1136 ? 21.748  80.593  108.087 1.00 23.06 ? 1134 LEU   A N     1 
ATOM   8337  C  CA    . LEU   A  1  1136 ? 22.011  79.161  108.116 1.00 24.85 ? 1134 LEU   A CA    1 
ATOM   8338  C  C     . LEU   A  1  1136 ? 22.353  78.593  106.745 1.00 24.96 ? 1134 LEU   A C     1 
ATOM   8339  O  O     . LEU   A  1  1136 ? 22.341  77.370  106.577 1.00 24.24 ? 1134 LEU   A O     1 
ATOM   8340  C  CB    . LEU   A  1  1136 ? 20.834  78.406  108.738 1.00 23.97 ? 1134 LEU   A CB    1 
ATOM   8341  C  CG    . LEU   A  1  1136 ? 20.616  78.643  110.233 1.00 23.42 ? 1134 LEU   A CG    1 
ATOM   8342  C  CD1   . LEU   A  1  1136 ? 19.317  77.974  110.707 1.00 23.60 ? 1134 LEU   A CD1   1 
ATOM   8343  C  CD2   . LEU   A  1  1136 ? 21.809  78.165  111.044 1.00 27.02 ? 1134 LEU   A CD2   1 
ATOM   8344  N  N     . GLN   A  1  1137 ? 22.672  79.455  105.773 1.00 25.78 ? 1135 GLN   A N     1 
ATOM   8345  C  CA    . GLN   A  1  1137 ? 22.997  78.987  104.427 1.00 28.34 ? 1135 GLN   A CA    1 
ATOM   8346  C  C     . GLN   A  1  1137 ? 24.070  77.903  104.440 1.00 25.82 ? 1135 GLN   A C     1 
ATOM   8347  O  O     . GLN   A  1  1137 ? 23.956  76.899  103.725 1.00 26.52 ? 1135 GLN   A O     1 
ATOM   8348  C  CB    . GLN   A  1  1137 ? 23.422  80.161  103.540 1.00 28.35 ? 1135 GLN   A CB    1 
ATOM   8349  C  CG    . GLN   A  1  1137 ? 22.273  81.048  103.080 1.00 27.93 ? 1135 GLN   A CG    1 
ATOM   8350  C  CD    . GLN   A  1  1137 ? 21.932  82.138  104.081 1.00 26.00 ? 1135 GLN   A CD    1 
ATOM   8351  O  OE1   . GLN   A  1  1137 ? 22.400  82.123  105.221 1.00 28.96 ? 1135 GLN   A OE1   1 
ATOM   8352  N  NE2   . GLN   A  1  1137 ? 21.131  83.104  103.649 1.00 30.85 ? 1135 GLN   A NE2   1 
ATOM   8353  N  N     . ALA   A  1  1138 ? 25.107  78.066  105.262 1.00 26.08 ? 1136 ALA   A N     1 
ATOM   8354  C  CA    . ALA   A  1  1138 ? 26.182  77.076  105.259 1.00 25.92 ? 1136 ALA   A CA    1 
ATOM   8355  C  C     . ALA   A  1  1138 ? 25.742  75.707  105.763 1.00 31.13 ? 1136 ALA   A C     1 
ATOM   8356  O  O     . ALA   A  1  1138 ? 26.499  74.741  105.626 1.00 32.18 ? 1136 ALA   A O     1 
ATOM   8357  C  CB    . ALA   A  1  1138 ? 27.388  77.576  106.061 1.00 31.67 ? 1136 ALA   A CB    1 
ATOM   8358  N  N     . SER   A  1  1139 ? 24.539  75.592  106.327 1.00 26.24 ? 1137 SER   A N     1 
ATOM   8359  C  CA    . SER   A  1  1139 ? 24.061  74.309  106.816 1.00 28.52 ? 1137 SER   A CA    1 
ATOM   8360  C  C     . SER   A  1  1139 ? 23.451  73.444  105.723 1.00 24.48 ? 1137 SER   A C     1 
ATOM   8361  O  O     . SER   A  1  1139 ? 23.157  72.275  105.984 1.00 27.11 ? 1137 SER   A O     1 
ATOM   8362  C  CB    . SER   A  1  1139 ? 23.033  74.514  107.938 1.00 24.74 ? 1137 SER   A CB    1 
ATOM   8363  O  OG    . SER   A  1  1139 ? 23.627  75.118  109.066 1.00 30.33 ? 1137 SER   A OG    1 
ATOM   8364  N  N     . LEU   A  1  1140 ? 23.248  73.981  104.524 1.00 24.18 ? 1138 LEU   A N     1 
ATOM   8365  C  CA    . LEU   A  1  1140 ? 22.620  73.254  103.425 1.00 25.67 ? 1138 LEU   A CA    1 
ATOM   8366  C  C     . LEU   A  1  1140 ? 23.520  73.195  102.201 1.00 27.62 ? 1138 LEU   A C     1 
ATOM   8367  O  O     . LEU   A  1  1140 ? 23.061  73.333  101.064 1.00 33.79 ? 1138 LEU   A O     1 
ATOM   8368  C  CB    . LEU   A  1  1140 ? 21.261  73.847  103.058 1.00 27.23 ? 1138 LEU   A CB    1 
ATOM   8369  C  CG    . LEU   A  1  1140 ? 20.035  73.546  103.911 1.00 29.85 ? 1138 LEU   A CG    1 
ATOM   8370  C  CD1   . LEU   A  1  1140 ? 18.815  73.976  103.121 1.00 28.99 ? 1138 LEU   A CD1   1 
ATOM   8371  C  CD2   . LEU   A  1  1140 ? 19.933  72.076  104.291 1.00 25.05 ? 1138 LEU   A CD2   1 
ATOM   8372  N  N     . LYS   A  1  1141 ? 24.815  72.978  102.414 1.00 26.21 ? 1139 LYS   A N     1 
ATOM   8373  C  CA    . LYS   A  1  1141 ? 25.755  72.866  101.307 1.00 31.26 ? 1139 LYS   A CA    1 
ATOM   8374  C  C     . LYS   A  1  1141 ? 25.659  71.493  100.650 1.00 30.12 ? 1139 LYS   A C     1 
ATOM   8375  O  O     . LYS   A  1  1141 ? 25.486  70.473  101.322 1.00 27.88 ? 1139 LYS   A O     1 
ATOM   8376  C  CB    . LYS   A  1  1141 ? 27.183  73.081  101.813 1.00 31.79 ? 1139 LYS   A CB    1 
ATOM   8377  N  N     . ASN   A  1  1142 ? 25.779  71.473  99.324  1.00 29.45 ? 1140 ASN   A N     1 
ATOM   8378  C  CA    . ASN   A  1  1142 ? 25.893  70.230  98.558  1.00 29.15 ? 1140 ASN   A CA    1 
ATOM   8379  C  C     . ASN   A  1  1142 ? 24.616  69.387  98.602  1.00 28.33 ? 1140 ASN   A C     1 
ATOM   8380  O  O     . ASN   A  1  1142 ? 24.675  68.158  98.663  1.00 27.27 ? 1140 ASN   A O     1 
ATOM   8381  C  CB    . ASN   A  1  1142 ? 27.109  69.400  98.976  1.00 34.20 ? 1140 ASN   A CB    1 
ATOM   8382  C  CG    . ASN   A  1  1142 ? 28.348  70.246  99.186  1.00 38.72 ? 1140 ASN   A CG    1 
ATOM   8383  O  OD1   . ASN   A  1  1142 ? 28.917  70.273  100.281 1.00 39.06 ? 1140 ASN   A OD1   1 
ATOM   8384  N  ND2   . ASN   A  1  1142 ? 28.770  70.951  98.140  1.00 38.34 ? 1140 ASN   A ND2   1 
ATOM   8385  N  N     . LEU   A  1  1143 ? 23.456  70.035  98.565  1.00 28.45 ? 1141 LEU   A N     1 
ATOM   8386  C  CA    . LEU   A  1  1143 ? 22.225  69.266  98.566  1.00 29.32 ? 1141 LEU   A CA    1 
ATOM   8387  C  C     . LEU   A  1  1143 ? 22.103  68.456  97.279  1.00 28.44 ? 1141 LEU   A C     1 
ATOM   8388  O  O     . LEU   A  1  1143 ? 22.547  68.892  96.213  1.00 26.60 ? 1141 LEU   A O     1 
ATOM   8389  C  CB    . LEU   A  1  1143 ? 21.011  70.179  98.664  1.00 25.86 ? 1141 LEU   A CB    1 
ATOM   8390  C  CG    . LEU   A  1  1143 ? 20.634  70.710  100.032 1.00 27.09 ? 1141 LEU   A CG    1 
ATOM   8391  C  CD1   . LEU   A  1  1143 ? 19.490  71.678  99.844  1.00 26.12 ? 1141 LEU   A CD1   1 
ATOM   8392  C  CD2   . LEU   A  1  1143 ? 20.243  69.566  100.965 1.00 25.43 ? 1141 LEU   A CD2   1 
ATOM   8393  N  N     . PRO   A  1  1144 ? 21.494  67.278  97.351  1.00 27.46 ? 1142 PRO   A N     1 
ATOM   8394  C  CA    . PRO   A  1  1144 ? 21.108  66.584  96.120  1.00 29.61 ? 1142 PRO   A CA    1 
ATOM   8395  C  C     . PRO   A  1  1144 ? 20.242  67.512  95.287  1.00 26.72 ? 1142 PRO   A C     1 
ATOM   8396  O  O     . PRO   A  1  1144 ? 19.462  68.307  95.820  1.00 25.15 ? 1142 PRO   A O     1 
ATOM   8397  C  CB    . PRO   A  1  1144 ? 20.290  65.391  96.629  1.00 30.13 ? 1142 PRO   A CB    1 
ATOM   8398  C  CG    . PRO   A  1  1144 ? 20.642  65.255  98.081  1.00 30.10 ? 1142 PRO   A CG    1 
ATOM   8399  C  CD    . PRO   A  1  1144 ? 20.959  66.627  98.557  1.00 27.15 ? 1142 PRO   A CD    1 
ATOM   8400  N  N     . GLN   A  1  1145 ? 20.396  67.417  93.965  1.00 25.21 ? 1143 GLN   A N     1 
ATOM   8401  C  CA    . GLN   A  1  1145 ? 19.588  68.240  93.070  1.00 25.39 ? 1143 GLN   A CA    1 
ATOM   8402  C  C     . GLN   A  1  1145 ? 18.091  68.083  93.331  1.00 24.74 ? 1143 GLN   A C     1 
ATOM   8403  O  O     . GLN   A  1  1145 ? 17.336  69.050  93.183  1.00 23.64 ? 1143 GLN   A O     1 
ATOM   8404  C  CB    . GLN   A  1  1145 ? 19.909  67.904  91.612  1.00 31.15 ? 1143 GLN   A CB    1 
ATOM   8405  N  N     . THR   A  1  1146 ? 17.638  66.885  93.714  1.00 23.77 ? 1144 THR   A N     1 
ATOM   8406  C  CA    . THR   A  1  1146 ? 16.212  66.702  93.975  1.00 25.42 ? 1144 THR   A CA    1 
ATOM   8407  C  C     . THR   A  1  1146 ? 15.755  67.555  95.143  1.00 23.35 ? 1144 THR   A C     1 
ATOM   8408  O  O     . THR   A  1  1146 ? 14.633  68.075  95.141  1.00 22.53 ? 1144 THR   A O     1 
ATOM   8409  C  CB    . THR   A  1  1146 ? 15.911  65.243  94.294  1.00 26.30 ? 1144 THR   A CB    1 
ATOM   8410  O  OG1   . THR   A  1  1146 ? 16.806  64.796  95.321  1.00 26.11 ? 1144 THR   A OG1   1 
ATOM   8411  C  CG2   . THR   A  1  1146 ? 16.058  64.386  93.058  1.00 24.16 ? 1144 THR   A CG2   1 
ATOM   8412  N  N     . VAL   A  1  1147 ? 16.597  67.677  96.167  1.00 22.76 ? 1145 VAL   A N     1 
ATOM   8413  C  CA    . VAL   A  1  1147 ? 16.247  68.497  97.318  1.00 19.99 ? 1145 VAL   A CA    1 
ATOM   8414  C  C     . VAL   A  1  1147 ? 16.429  69.973  96.990  1.00 21.36 ? 1145 VAL   A C     1 
ATOM   8415  O  O     . VAL   A  1  1147 ? 15.564  70.798  97.294  1.00 21.53 ? 1145 VAL   A O     1 
ATOM   8416  C  CB    . VAL   A  1  1147 ? 17.067  68.076  98.553  1.00 20.20 ? 1145 VAL   A CB    1 
ATOM   8417  C  CG1   . VAL   A  1  1147 ? 16.624  68.870  99.770  1.00 20.31 ? 1145 VAL   A CG1   1 
ATOM   8418  C  CG2   . VAL   A  1  1147 ? 16.937  66.575  98.820  1.00 21.92 ? 1145 VAL   A CG2   1 
ATOM   8419  N  N     . GLY   A  1  1148 ? 17.550  70.320  96.350  1.00 21.09 ? 1146 GLY   A N     1 
ATOM   8420  C  CA    . GLY   A  1  1148 ? 17.755  71.699  95.940  1.00 21.78 ? 1146 GLY   A CA    1 
ATOM   8421  C  C     . GLY   A  1  1148 ? 16.601  72.259  95.129  1.00 23.99 ? 1146 GLY   A C     1 
ATOM   8422  O  O     . GLY   A  1  1148 ? 16.263  73.439  95.252  1.00 23.68 ? 1146 GLY   A O     1 
ATOM   8423  N  N     . LEU   A  1  1149 ? 15.972  71.420  94.294  1.00 20.34 ? 1147 LEU   A N     1 
ATOM   8424  C  CA    . LEU   A  1  1149 ? 14.836  71.874  93.497  1.00 24.12 ? 1147 LEU   A CA    1 
ATOM   8425  C  C     . LEU   A  1  1149 ? 13.679  72.326  94.372  1.00 20.98 ? 1147 LEU   A C     1 
ATOM   8426  O  O     . LEU   A  1  1149 ? 12.870  73.158  93.946  1.00 26.50 ? 1147 LEU   A O     1 
ATOM   8427  C  CB    . LEU   A  1  1149 ? 14.359  70.763  92.564  1.00 25.19 ? 1147 LEU   A CB    1 
ATOM   8428  C  CG    . LEU   A  1  1149 ? 15.193  70.507  91.311  1.00 30.27 ? 1147 LEU   A CG    1 
ATOM   8429  C  CD1   . LEU   A  1  1149 ? 14.590  69.355  90.528  1.00 32.63 ? 1147 LEU   A CD1   1 
ATOM   8430  C  CD2   . LEU   A  1  1149 ? 15.254  71.770  90.461  1.00 33.49 ? 1147 LEU   A CD2   1 
ATOM   8431  N  N     . ARG   A  1  1150 ? 13.577  71.780  95.585  1.00 20.72 ? 1148 ARG   A N     1 
ATOM   8432  C  CA    . ARG   A  1  1150 ? 12.515  72.149  96.505  1.00 20.39 ? 1148 ARG   A CA    1 
ATOM   8433  C  C     . ARG   A  1  1150 ? 12.904  73.285  97.429  1.00 21.31 ? 1148 ARG   A C     1 
ATOM   8434  O  O     . ARG   A  1  1150 ? 12.048  73.755  98.173  1.00 21.46 ? 1148 ARG   A O     1 
ATOM   8435  C  CB    . ARG   A  1  1150 ? 12.132  70.957  97.385  1.00 20.19 ? 1148 ARG   A CB    1 
ATOM   8436  C  CG    . ARG   A  1  1150 ? 11.486  69.808  96.637  1.00 24.61 ? 1148 ARG   A CG    1 
ATOM   8437  C  CD    . ARG   A  1  1150 ? 10.127  69.513  97.207  1.00 24.56 ? 1148 ARG   A CD    1 
ATOM   8438  N  NE    . ARG   A  1  1150 ? 9.596   68.260  96.696  1.00 23.44 ? 1148 ARG   A NE    1 
ATOM   8439  C  CZ    . ARG   A  1  1150 ? 9.119   67.287  97.459  1.00 21.38 ? 1148 ARG   A CZ    1 
ATOM   8440  N  NH1   . ARG   A  1  1150 ? 9.035   67.416  98.777  1.00 19.67 ? 1148 ARG   A NH1   1 
ATOM   8441  N  NH2   . ARG   A  1  1150 ? 8.711   66.158  96.884  1.00 20.57 ? 1148 ARG   A NH2   1 
ATOM   8442  N  N     . VAL   A  1  1151 ? 14.162  73.715  97.422  1.00 18.03 ? 1149 VAL   A N     1 
ATOM   8443  C  CA    . VAL   A  1  1151 ? 14.671  74.662  98.409  1.00 20.06 ? 1149 VAL   A CA    1 
ATOM   8444  C  C     . VAL   A  1  1151 ? 14.972  75.993  97.738  1.00 24.28 ? 1149 VAL   A C     1 
ATOM   8445  O  O     . VAL   A  1  1151 ? 15.713  76.052  96.749  1.00 26.21 ? 1149 VAL   A O     1 
ATOM   8446  C  CB    . VAL   A  1  1151 ? 15.910  74.117  99.137  1.00 20.65 ? 1149 VAL   A CB    1 
ATOM   8447  C  CG1   . VAL   A  1  1151 ? 16.489  75.184  100.062 1.00 24.52 ? 1149 VAL   A CG1   1 
ATOM   8448  C  CG2   . VAL   A  1  1151 ? 15.556  72.872  99.934  1.00 21.20 ? 1149 VAL   A CG2   1 
ATOM   8449  N  N     . SER   A  1  1152 ? 14.406  77.057  98.281  1.00 21.06 ? 1150 SER   A N     1 
ATOM   8450  C  CA    . SER   A  1  1152 ? 14.785  78.410  97.927  1.00 25.17 ? 1150 SER   A CA    1 
ATOM   8451  C  C     . SER   A  1  1152 ? 15.100  79.156  99.213  1.00 26.68 ? 1150 SER   A C     1 
ATOM   8452  O  O     . SER   A  1  1152 ? 14.652  78.780  100.301 1.00 23.60 ? 1150 SER   A O     1 
ATOM   8453  C  CB    . SER   A  1  1152 ? 13.671  79.135  97.167  1.00 25.73 ? 1150 SER   A CB    1 
ATOM   8454  O  OG    . SER   A  1  1152 ? 12.505  79.263  97.961  1.00 28.67 ? 1150 SER   A OG    1 
ATOM   8455  N  N     . TRP   A  1  1153 ? 15.893  80.209  99.079  1.00 22.71 ? 1151 TRP   A N     1 
ATOM   8456  C  CA    . TRP   A  1  1153 ? 16.211  81.086  100.192 1.00 25.73 ? 1151 TRP   A CA    1 
ATOM   8457  C  C     . TRP   A  1  1153 ? 15.557  82.435  99.952  1.00 26.30 ? 1151 TRP   A C     1 
ATOM   8458  O  O     . TRP   A  1  1153 ? 15.575  82.954  98.832  1.00 29.60 ? 1151 TRP   A O     1 
ATOM   8459  C  CB    . TRP   A  1  1153 ? 17.720  81.249  100.331 1.00 26.08 ? 1151 TRP   A CB    1 
ATOM   8460  C  CG    . TRP   A  1  1153 ? 18.369  80.023  100.858 1.00 26.52 ? 1151 TRP   A CG    1 
ATOM   8461  C  CD1   . TRP   A  1  1153 ? 18.815  78.954  100.134 1.00 28.57 ? 1151 TRP   A CD1   1 
ATOM   8462  C  CD2   . TRP   A  1  1153 ? 18.632  79.717  102.231 1.00 24.48 ? 1151 TRP   A CD2   1 
ATOM   8463  N  NE1   . TRP   A  1  1153 ? 19.348  78.009  100.974 1.00 30.66 ? 1151 TRP   A NE1   1 
ATOM   8464  C  CE2   . TRP   A  1  1153 ? 19.243  78.449  102.267 1.00 25.97 ? 1151 TRP   A CE2   1 
ATOM   8465  C  CE3   . TRP   A  1  1153 ? 18.414  80.396  103.434 1.00 26.03 ? 1151 TRP   A CE3   1 
ATOM   8466  C  CZ2   . TRP   A  1  1153 ? 19.644  77.846  103.459 1.00 24.81 ? 1151 TRP   A CZ2   1 
ATOM   8467  C  CZ3   . TRP   A  1  1153 ? 18.817  79.795  104.621 1.00 25.44 ? 1151 TRP   A CZ3   1 
ATOM   8468  C  CH2   . TRP   A  1  1153 ? 19.424  78.533  104.623 1.00 27.78 ? 1151 TRP   A CH2   1 
ATOM   8469  N  N     . SER   A  1  1154 ? 14.972  83.002  101.002 1.00 25.34 ? 1152 SER   A N     1 
ATOM   8470  C  CA    . SER   A  1  1154 ? 14.150  84.192  100.852 1.00 24.70 ? 1152 SER   A CA    1 
ATOM   8471  C  C     . SER   A  1  1154 ? 14.658  85.279  101.781 1.00 28.08 ? 1152 SER   A C     1 
ATOM   8472  O  O     . SER   A  1  1154 ? 14.638  85.111  103.004 1.00 24.30 ? 1152 SER   A O     1 
ATOM   8473  C  CB    . SER   A  1  1154 ? 12.684  83.889  101.160 1.00 24.16 ? 1152 SER   A CB    1 
ATOM   8474  O  OG    . SER   A  1  1154 ? 11.915  85.067  101.037 1.00 26.80 ? 1152 SER   A OG    1 
ATOM   8475  N  N     . LYS   A  1  1155 ? 15.103  86.393  101.202 1.00 26.51 ? 1153 LYS   A N     1 
ATOM   8476  C  CA    . LYS   A  1  1155 ? 15.390  87.585  101.990 1.00 29.71 ? 1153 LYS   A CA    1 
ATOM   8477  C  C     . LYS   A  1  1155 ? 14.164  88.471  102.159 1.00 32.80 ? 1153 LYS   A C     1 
ATOM   8478  O  O     . LYS   A  1  1155 ? 13.997  89.099  103.211 1.00 40.00 ? 1153 LYS   A O     1 
ATOM   8479  C  CB    . LYS   A  1  1155 ? 16.527  88.384  101.341 1.00 32.75 ? 1153 LYS   A CB    1 
ATOM   8480  N  N     . ASP   A  1  1156 ? 13.296  88.522  101.155 1.00 32.29 ? 1154 ASP   A N     1 
ATOM   8481  C  CA    . ASP   A  1  1156 ? 12.091  89.340  101.172 1.00 32.30 ? 1154 ASP   A CA    1 
ATOM   8482  C  C     . ASP   A  1  1156 ? 10.932  88.353  101.074 1.00 28.80 ? 1154 ASP   A C     1 
ATOM   8483  O  O     . ASP   A  1  1156 ? 10.534  87.963  99.976  1.00 27.64 ? 1154 ASP   A O     1 
ATOM   8484  C  CB    . ASP   A  1  1156 ? 12.115  90.319  99.986  1.00 34.23 ? 1154 ASP   A CB    1 
ATOM   8485  C  CG    . ASP   A  1  1156 ? 10.903  91.239  99.948  1.00 40.35 ? 1154 ASP   A CG    1 
ATOM   8486  O  OD1   . ASP   A  1  1156 ? 9.969   91.063  100.762 1.00 42.07 ? 1154 ASP   A OD1   1 
ATOM   8487  O  OD2   . ASP   A  1  1156 ? 10.888  92.156  99.098  1.00 42.65 ? 1154 ASP   A OD2   1 
ATOM   8488  N  N     . TRP   A  1  1157 ? 10.400  87.942  102.230 1.00 26.41 ? 1155 TRP   A N     1 
ATOM   8489  C  CA    . TRP   A  1  1157 ? 9.375   86.900  102.234 1.00 24.92 ? 1155 TRP   A CA    1 
ATOM   8490  C  C     . TRP   A  1  1157 ? 8.170   87.304  101.401 1.00 26.75 ? 1155 TRP   A C     1 
ATOM   8491  O  O     . TRP   A  1  1157 ? 7.565   86.465  100.727 1.00 28.62 ? 1155 TRP   A O     1 
ATOM   8492  C  CB    . TRP   A  1  1157 ? 8.920   86.600  103.659 1.00 24.17 ? 1155 TRP   A CB    1 
ATOM   8493  C  CG    . TRP   A  1  1157 ? 9.981   86.199  104.620 1.00 22.54 ? 1155 TRP   A CG    1 
ATOM   8494  C  CD1   . TRP   A  1  1157 ? 11.262  85.840  104.344 1.00 24.36 ? 1155 TRP   A CD1   1 
ATOM   8495  C  CD2   . TRP   A  1  1157 ? 9.832   86.116  106.036 1.00 21.82 ? 1155 TRP   A CD2   1 
ATOM   8496  N  NE1   . TRP   A  1  1157 ? 11.932  85.537  105.512 1.00 24.30 ? 1155 TRP   A NE1   1 
ATOM   8497  C  CE2   . TRP   A  1  1157 ? 11.069  85.703  106.564 1.00 23.63 ? 1155 TRP   A CE2   1 
ATOM   8498  C  CE3   . TRP   A  1  1157 ? 8.766   86.361  106.913 1.00 23.48 ? 1155 TRP   A CE3   1 
ATOM   8499  C  CZ2   . TRP   A  1  1157 ? 11.271  85.519  107.932 1.00 25.01 ? 1155 TRP   A CZ2   1 
ATOM   8500  C  CZ3   . TRP   A  1  1157 ? 8.968   86.180  108.271 1.00 22.98 ? 1155 TRP   A CZ3   1 
ATOM   8501  C  CH2   . TRP   A  1  1157 ? 10.211  85.772  108.766 1.00 24.46 ? 1155 TRP   A CH2   1 
ATOM   8502  N  N     . ALA   A  1  1158 ? 7.799   88.582  101.441 1.00 26.78 ? 1156 ALA   A N     1 
ATOM   8503  C  CA    . ALA   A  1  1158 ? 6.617   89.028  100.715 1.00 28.89 ? 1156 ALA   A CA    1 
ATOM   8504  C  C     . ALA   A  1  1158 ? 6.794   88.932  99.207  1.00 33.85 ? 1156 ALA   A C     1 
ATOM   8505  O  O     . ALA   A  1  1158 ? 5.796   88.849  98.482  1.00 40.17 ? 1156 ALA   A O     1 
ATOM   8506  C  CB    . ALA   A  1  1158 ? 6.254   90.457  101.119 1.00 31.21 ? 1156 ALA   A CB    1 
ATOM   8507  N  N     . ALA   A  1  1159 ? 8.036   88.937  98.724  1.00 30.27 ? 1157 ALA   A N     1 
ATOM   8508  C  CA    . ALA   A  1  1159 ? 8.296   88.822  97.296  1.00 33.93 ? 1157 ALA   A CA    1 
ATOM   8509  C  C     . ALA   A  1  1159 ? 8.264   87.383  96.807  1.00 33.83 ? 1157 ALA   A C     1 
ATOM   8510  O  O     . ALA   A  1  1159 ? 8.043   87.150  95.615  1.00 35.49 ? 1157 ALA   A O     1 
ATOM   8511  C  CB    . ALA   A  1  1159 ? 9.659   89.435  96.964  1.00 33.73 ? 1157 ALA   A CB    1 
ATOM   8512  N  N     . ASP   A  1  1160 ? 8.463   86.415  97.696  1.00 32.18 ? 1158 ASP   A N     1 
ATOM   8513  C  CA    . ASP   A  1  1160 ? 8.646   85.024  97.309  1.00 31.80 ? 1158 ASP   A CA    1 
ATOM   8514  C  C     . ASP   A  1  1160 ? 7.428   84.158  97.597  1.00 27.21 ? 1158 ASP   A C     1 
ATOM   8515  O  O     . ASP   A  1  1160 ? 7.491   82.937  97.420  1.00 29.57 ? 1158 ASP   A O     1 
ATOM   8516  C  CB    . ASP   A  1  1160 ? 9.901   84.463  97.974  1.00 31.22 ? 1158 ASP   A CB    1 
ATOM   8517  C  CG    . ASP   A  1  1160 ? 11.126  85.288  97.655  1.00 35.02 ? 1158 ASP   A CG    1 
ATOM   8518  O  OD1   . ASP   A  1  1160 ? 11.096  86.004  96.627  1.00 39.77 ? 1158 ASP   A OD1   1 
ATOM   8519  O  OD2   . ASP   A  1  1160 ? 12.109  85.234  98.425  1.00 34.26 ? 1158 ASP   A OD2   1 
ATOM   8520  N  N     . GLY   A  1  1161 ? 6.322   84.758  98.026  1.00 28.26 ? 1159 GLY   A N     1 
ATOM   8521  C  CA    . GLY   A  1  1161 ? 5.100   84.029  98.239  1.00 27.87 ? 1159 GLY   A CA    1 
ATOM   8522  C  C     . GLY   A  1  1161 ? 4.324   83.834  96.948  1.00 29.47 ? 1159 GLY   A C     1 
ATOM   8523  O  O     . GLY   A  1  1161 ? 4.824   84.100  95.854  1.00 32.11 ? 1159 GLY   A O     1 
ATOM   8524  N  N     . PRO   A  1  1162 ? 3.077   83.365  97.056  1.00 28.18 ? 1160 PRO   A N     1 
ATOM   8525  C  CA    . PRO   A  1  1162 ? 2.372   83.026  98.292  1.00 25.17 ? 1160 PRO   A CA    1 
ATOM   8526  C  C     . PRO   A  1  1162 ? 2.905   81.741  98.891  1.00 26.85 ? 1160 PRO   A C     1 
ATOM   8527  O  O     . PRO   A  1  1162 ? 3.288   80.800  98.200  1.00 25.94 ? 1160 PRO   A O     1 
ATOM   8528  C  CB    . PRO   A  1  1162 ? 0.914   82.878  97.833  1.00 26.46 ? 1160 PRO   A CB    1 
ATOM   8529  C  CG    . PRO   A  1  1162 ? 1.036   82.389  96.419  1.00 32.46 ? 1160 PRO   A CG    1 
ATOM   8530  C  CD    . PRO   A  1  1162 ? 2.240   83.119  95.867  1.00 30.04 ? 1160 PRO   A CD    1 
ATOM   8531  N  N     . PHE   A  1  1163 ? 2.958   81.700  100.209 1.00 21.64 ? 1161 PHE   A N     1 
ATOM   8532  C  CA    . PHE   A  1  1163 ? 3.278   80.461  100.880 1.00 18.45 ? 1161 PHE   A CA    1 
ATOM   8533  C  C     . PHE   A  1  1163 ? 1.990   79.740  101.245 1.00 21.25 ? 1161 PHE   A C     1 
ATOM   8534  O  O     . PHE   A  1  1163 ? 0.888   80.286  101.141 1.00 23.65 ? 1161 PHE   A O     1 
ATOM   8535  C  CB    . PHE   A  1  1163 ? 4.148   80.742  102.101 1.00 18.42 ? 1161 PHE   A CB    1 
ATOM   8536  C  CG    . PHE   A  1  1163 ? 5.381   81.507  101.771 1.00 20.39 ? 1161 PHE   A CG    1 
ATOM   8537  C  CD1   . PHE   A  1  1163 ? 6.354   80.940  100.963 1.00 23.44 ? 1161 PHE   A CD1   1 
ATOM   8538  C  CD2   . PHE   A  1  1163 ? 5.564   82.799  102.231 1.00 19.78 ? 1161 PHE   A CD2   1 
ATOM   8539  C  CE1   . PHE   A  1  1163 ? 7.498   81.639  100.631 1.00 25.90 ? 1161 PHE   A CE1   1 
ATOM   8540  C  CE2   . PHE   A  1  1163 ? 6.716   83.502  101.905 1.00 24.15 ? 1161 PHE   A CE2   1 
ATOM   8541  C  CZ    . PHE   A  1  1163 ? 7.679   82.923  101.102 1.00 22.85 ? 1161 PHE   A CZ    1 
ATOM   8542  N  N     . ALA   A  1  1164 ? 2.134   78.479  101.637 1.00 19.24 ? 1162 ALA   A N     1 
ATOM   8543  C  CA    . ALA   A  1  1164 ? 0.991   77.663  102.017 1.00 19.80 ? 1162 ALA   A CA    1 
ATOM   8544  C  C     . ALA   A  1  1164 ? 1.048   77.255  103.478 1.00 20.19 ? 1162 ALA   A C     1 
ATOM   8545  O  O     . ALA   A  1  1164 ? 0.216   76.463  103.928 1.00 21.62 ? 1162 ALA   A O     1 
ATOM   8546  C  CB    . ALA   A  1  1164 ? 0.901   76.432  101.110 1.00 21.62 ? 1162 ALA   A CB    1 
ATOM   8547  N  N     . GLY   A  1  1165 ? 2.025   77.759  104.213 1.00 17.91 ? 1163 GLY   A N     1 
ATOM   8548  C  CA    . GLY   A  1  1165 ? 2.153   77.506  105.631 1.00 18.97 ? 1163 GLY   A CA    1 
ATOM   8549  C  C     . GLY   A  1  1165 ? 3.517   77.994  106.053 1.00 19.05 ? 1163 GLY   A C     1 
ATOM   8550  O  O     . GLY   A  1  1165 ? 4.294   78.480  105.233 1.00 17.76 ? 1163 GLY   A O     1 
ATOM   8551  N  N     . ALA   A  1  1166 ? 3.804   77.849  107.342 1.00 17.87 ? 1164 ALA   A N     1 
ATOM   8552  C  CA    . ALA   A  1  1166 ? 5.101   78.287  107.831 1.00 17.57 ? 1164 ALA   A CA    1 
ATOM   8553  C  C     . ALA   A  1  1166 ? 5.478   77.460  109.046 1.00 17.59 ? 1164 ALA   A C     1 
ATOM   8554  O  O     . ALA   A  1  1166 ? 4.615   76.996  109.795 1.00 20.45 ? 1164 ALA   A O     1 
ATOM   8555  C  CB    . ALA   A  1  1166 ? 5.100   79.774  108.199 1.00 17.86 ? 1164 ALA   A CB    1 
ATOM   8556  N  N     . LEU   A  1  1167 ? 6.780   77.265  109.211 1.00 17.00 ? 1165 LEU   A N     1 
ATOM   8557  C  CA    . LEU   A  1  1167 ? 7.359   76.627  110.382 1.00 16.91 ? 1165 LEU   A CA    1 
ATOM   8558  C  C     . LEU   A  1  1167 ? 8.375   77.596  110.960 1.00 18.83 ? 1165 LEU   A C     1 
ATOM   8559  O  O     . LEU   A  1  1167 ? 9.225   78.117  110.230 1.00 18.88 ? 1165 LEU   A O     1 
ATOM   8560  C  CB    . LEU   A  1  1167 ? 8.051   75.320  110.010 1.00 17.62 ? 1165 LEU   A CB    1 
ATOM   8561  C  CG    . LEU   A  1  1167 ? 7.148   74.285  109.334 1.00 17.06 ? 1165 LEU   A CG    1 
ATOM   8562  C  CD1   . LEU   A  1  1167 ? 7.969   73.083  108.873 1.00 18.70 ? 1165 LEU   A CD1   1 
ATOM   8563  C  CD2   . LEU   A  1  1167 ? 6.019   73.862  110.271 1.00 18.82 ? 1165 LEU   A CD2   1 
ATOM   8564  N  N     . VAL   A  1  1168 ? 8.272   77.843  112.258 1.00 19.13 ? 1166 VAL   A N     1 
ATOM   8565  C  CA    . VAL   A  1  1168 ? 9.062   78.855  112.939 1.00 19.35 ? 1166 VAL   A CA    1 
ATOM   8566  C  C     . VAL   A  1  1168 ? 9.735   78.203  114.125 1.00 18.94 ? 1166 VAL   A C     1 
ATOM   8567  O  O     . VAL   A  1  1168 ? 9.120   77.399  114.836 1.00 18.13 ? 1166 VAL   A O     1 
ATOM   8568  C  CB    . VAL   A  1  1168 ? 8.169   80.025  113.403 1.00 19.77 ? 1166 VAL   A CB    1 
ATOM   8569  C  CG1   . VAL   A  1  1168 ? 9.008   81.098  114.111 1.00 21.23 ? 1166 VAL   A CG1   1 
ATOM   8570  C  CG2   . VAL   A  1  1168 ? 7.398   80.607  112.210 1.00 19.07 ? 1166 VAL   A CG2   1 
ATOM   8571  N  N     . GLU   A  1  1169 ? 11.005  78.528  114.325 1.00 17.23 ? 1167 GLU   A N     1 
ATOM   8572  C  CA    . GLU   A  1  1169 ? 11.750  78.084  115.491 1.00 18.81 ? 1167 GLU   A CA    1 
ATOM   8573  C  C     . GLU   A  1  1169 ? 12.218  79.317  116.244 1.00 21.90 ? 1167 GLU   A C     1 
ATOM   8574  O  O     . GLU   A  1  1169 ? 12.742  80.257  115.636 1.00 20.82 ? 1167 GLU   A O     1 
ATOM   8575  C  CB    . GLU   A  1  1169 ? 12.965  77.270  115.065 1.00 19.42 ? 1167 GLU   A CB    1 
ATOM   8576  C  CG    . GLU   A  1  1169 ? 13.854  76.855  116.228 1.00 19.67 ? 1167 GLU   A CG    1 
ATOM   8577  C  CD    . GLU   A  1  1169 ? 15.183  76.310  115.761 1.00 20.07 ? 1167 GLU   A CD    1 
ATOM   8578  O  OE1   . GLU   A  1  1169 ? 15.498  76.408  114.547 1.00 20.60 ? 1167 GLU   A OE1   1 
ATOM   8579  O  OE2   . GLU   A  1  1169 ? 15.919  75.779  116.611 1.00 20.21 ? 1167 GLU   A OE2   1 
ATOM   8580  N  N     . GLY   A  1  1170 ? 12.033  79.316  117.549 1.00 19.39 ? 1168 GLY   A N     1 
ATOM   8581  C  CA    . GLY   A  1  1170 ? 12.597  80.394  118.338 1.00 22.53 ? 1168 GLY   A CA    1 
ATOM   8582  C  C     . GLY   A  1  1170 ? 12.000  80.429  119.719 1.00 21.67 ? 1168 GLY   A C     1 
ATOM   8583  O  O     . GLY   A  1  1170 ? 11.068  79.690  120.046 1.00 24.52 ? 1168 GLY   A O     1 
ATOM   8584  N  N     . ASP   A  1  1171 ? 12.541  81.334  120.530 1.00 23.01 ? 1169 ASP   A N     1 
ATOM   8585  C  CA    . ASP   A  1  1171 ? 11.921  81.596  121.816 1.00 24.41 ? 1169 ASP   A CA    1 
ATOM   8586  C  C     . ASP   A  1  1171 ? 10.612  82.365  121.621 1.00 26.73 ? 1169 ASP   A C     1 
ATOM   8587  O  O     . ASP   A  1  1171 ? 10.239  82.747  120.505 1.00 23.67 ? 1169 ASP   A O     1 
ATOM   8588  C  CB    . ASP   A  1  1171 ? 12.917  82.243  122.790 1.00 26.28 ? 1169 ASP   A CB    1 
ATOM   8589  C  CG    . ASP   A  1  1171 ? 13.384  83.641  122.359 1.00 30.15 ? 1169 ASP   A CG    1 
ATOM   8590  O  OD1   . ASP   A  1  1171 ? 12.738  84.295  121.517 1.00 28.02 ? 1169 ASP   A OD1   1 
ATOM   8591  O  OD2   . ASP   A  1  1171 ? 14.424  84.097  122.893 1.00 38.16 ? 1169 ASP   A OD2   1 
ATOM   8592  N  N     . ALA   A  1  1172 ? 9.899   82.587  122.728 1.00 25.23 ? 1170 ALA   A N     1 
ATOM   8593  C  CA    . ALA   A  1  1172 ? 8.562   83.163  122.646 1.00 25.07 ? 1170 ALA   A CA    1 
ATOM   8594  C  C     . ALA   A  1  1172 ? 8.563   84.505  121.920 1.00 25.86 ? 1170 ALA   A C     1 
ATOM   8595  O  O     . ALA   A  1  1172 ? 7.700   84.760  121.076 1.00 24.67 ? 1170 ALA   A O     1 
ATOM   8596  C  CB    . ALA   A  1  1172 ? 7.960   83.309  124.043 1.00 27.71 ? 1170 ALA   A CB    1 
ATOM   8597  N  N     . GLU   A  1  1173 ? 9.511   85.385  122.241 1.00 27.32 ? 1171 GLU   A N     1 
ATOM   8598  C  CA    . GLU   A  1  1173 ? 9.494   86.699  121.606 1.00 28.80 ? 1171 GLU   A CA    1 
ATOM   8599  C  C     . GLU   A  1  1173 ? 9.904   86.631  120.138 1.00 26.04 ? 1171 GLU   A C     1 
ATOM   8600  O  O     . GLU   A  1  1173 ? 9.380   87.396  119.319 1.00 26.95 ? 1171 GLU   A O     1 
ATOM   8601  C  CB    . GLU   A  1  1173 ? 10.330  87.703  122.399 1.00 32.80 ? 1171 GLU   A CB    1 
ATOM   8602  C  CG    . GLU   A  1  1173 ? 9.691   88.071  123.729 1.00 36.59 ? 1171 GLU   A CG    1 
ATOM   8603  C  CD    . GLU   A  1  1173 ? 8.216   88.459  123.596 1.00 42.02 ? 1171 GLU   A CD    1 
ATOM   8604  O  OE1   . GLU   A  1  1173 ? 7.856   89.169  122.627 1.00 39.50 ? 1171 GLU   A OE1   1 
ATOM   8605  O  OE2   . GLU   A  1  1173 ? 7.410   88.049  124.462 1.00 39.73 ? 1171 GLU   A OE2   1 
ATOM   8606  N  N     . ARG   A  1  1174 ? 10.817  85.723  119.787 1.00 23.84 ? 1172 ARG   A N     1 
ATOM   8607  C  CA    . ARG   A  1  1174 ? 11.123  85.499  118.377 1.00 22.37 ? 1172 ARG   A CA    1 
ATOM   8608  C  C     . ARG   A  1  1174 ? 9.898   84.993  117.632 1.00 24.52 ? 1172 ARG   A C     1 
ATOM   8609  O  O     . ARG   A  1  1174 ? 9.594   85.459  116.529 1.00 21.05 ? 1172 ARG   A O     1 
ATOM   8610  C  CB    . ARG   A  1  1174 ? 12.272  84.502  118.248 1.00 24.03 ? 1172 ARG   A CB    1 
ATOM   8611  C  CG    . ARG   A  1  1174 ? 12.582  84.084  116.818 1.00 23.42 ? 1172 ARG   A CG    1 
ATOM   8612  C  CD    . ARG   A  1  1174 ? 13.010  85.272  115.976 1.00 28.36 ? 1172 ARG   A CD    1 
ATOM   8613  N  NE    . ARG   A  1  1174 ? 13.331  84.884  114.605 1.00 24.28 ? 1172 ARG   A NE    1 
ATOM   8614  C  CZ    . ARG   A  1  1174 ? 13.445  85.743  113.601 1.00 26.90 ? 1172 ARG   A CZ    1 
ATOM   8615  N  NH1   . ARG   A  1  1174 ? 13.264  87.042  113.779 1.00 26.33 ? 1172 ARG   A NH1   1 
ATOM   8616  N  NH2   . ARG   A  1  1174 ? 13.735  85.286  112.387 1.00 24.26 ? 1172 ARG   A NH2   1 
ATOM   8617  N  N     . ILE   A  1  1175 ? 9.171   84.045  118.226 1.00 21.75 ? 1173 ILE   A N     1 
ATOM   8618  C  CA    . ILE   A  1  1175 ? 7.956   83.535  117.597 1.00 22.06 ? 1173 ILE   A CA    1 
ATOM   8619  C  C     . ILE   A  1  1175 ? 6.953   84.660  117.393 1.00 21.55 ? 1173 ILE   A C     1 
ATOM   8620  O  O     . ILE   A  1  1175 ? 6.340   84.786  116.325 1.00 24.58 ? 1173 ILE   A O     1 
ATOM   8621  C  CB    . ILE   A  1  1175 ? 7.357   82.394  118.436 1.00 23.14 ? 1173 ILE   A CB    1 
ATOM   8622  C  CG1   . ILE   A  1  1175 ? 8.254   81.161  118.360 1.00 22.17 ? 1173 ILE   A CG1   1 
ATOM   8623  C  CG2   . ILE   A  1  1175 ? 5.942   82.079  117.959 1.00 22.50 ? 1173 ILE   A CG2   1 
ATOM   8624  C  CD1   . ILE   A  1  1175 ? 7.948   80.112  119.420 1.00 24.51 ? 1173 ILE   A CD1   1 
ATOM   8625  N  N     . ARG   A  1  1176 ? 6.777   85.502  118.416 1.00 23.87 ? 1174 ARG   A N     1 
ATOM   8626  C  CA    . ARG   A  1  1176 ? 5.833   86.605  118.295 1.00 23.27 ? 1174 ARG   A CA    1 
ATOM   8627  C  C     . ARG   A  1  1176 ? 6.234   87.538  117.159 1.00 22.93 ? 1174 ARG   A C     1 
ATOM   8628  O  O     . ARG   A  1  1176 ? 5.396   87.918  116.331 1.00 25.40 ? 1174 ARG   A O     1 
ATOM   8629  C  CB    . ARG   A  1  1176 ? 5.726   87.363  119.619 1.00 22.93 ? 1174 ARG   A CB    1 
ATOM   8630  C  CG    . ARG   A  1  1176 ? 4.450   88.180  119.712 1.00 31.23 ? 1174 ARG   A CG    1 
ATOM   8631  C  CD    . ARG   A  1  1176 ? 4.498   89.178  120.863 1.00 33.88 ? 1174 ARG   A CD    1 
ATOM   8632  N  NE    . ARG   A  1  1176 ? 4.829   88.544  122.133 1.00 31.43 ? 1174 ARG   A NE    1 
ATOM   8633  C  CZ    . ARG   A  1  1176 ? 3.931   88.103  123.006 1.00 37.02 ? 1174 ARG   A CZ    1 
ATOM   8634  N  NH1   . ARG   A  1  1176 ? 2.634   88.144  122.743 1.00 35.22 ? 1174 ARG   A NH1   1 
ATOM   8635  N  NH2   . ARG   A  1  1176 ? 4.344   87.620  124.175 1.00 35.80 ? 1174 ARG   A NH2   1 
ATOM   8636  N  N     . ALA   A  1  1177 ? 7.520   87.882  117.080 1.00 23.07 ? 1175 ALA   A N     1 
ATOM   8637  C  CA    . ALA   A  1  1177 ? 7.979   88.792  116.035 1.00 25.47 ? 1175 ALA   A CA    1 
ATOM   8638  C  C     . ALA   A  1  1177 ? 7.809   88.174  114.658 1.00 22.91 ? 1175 ALA   A C     1 
ATOM   8639  O  O     . ALA   A  1  1177 ? 7.370   88.844  113.719 1.00 24.55 ? 1175 ALA   A O     1 
ATOM   8640  C  CB    . ALA   A  1  1177 ? 9.436   89.175  116.268 1.00 23.83 ? 1175 ALA   A CB    1 
ATOM   8641  N  N     . VAL   A  1  1178 ? 8.146   86.894  114.524 1.00 20.76 ? 1176 VAL   A N     1 
ATOM   8642  C  CA    . VAL   A  1  1178 ? 7.991   86.223  113.238 1.00 20.04 ? 1176 VAL   A CA    1 
ATOM   8643  C  C     . VAL   A  1  1178 ? 6.522   86.137  112.857 1.00 21.54 ? 1176 VAL   A C     1 
ATOM   8644  O  O     . VAL   A  1  1178 ? 6.154   86.355  111.695 1.00 22.90 ? 1176 VAL   A O     1 
ATOM   8645  C  CB    . VAL   A  1  1178 ? 8.671   84.842  113.266 1.00 19.32 ? 1176 VAL   A CB    1 
ATOM   8646  C  CG1   . VAL   A  1  1178 ? 8.332   84.067  112.003 1.00 19.89 ? 1176 VAL   A CG1   1 
ATOM   8647  C  CG2   . VAL   A  1  1178 ? 10.169  85.002  113.377 1.00 20.96 ? 1176 VAL   A CG2   1 
ATOM   8648  N  N     . ASN   A  1  1179 ? 5.657   85.831  113.829 1.00 21.27 ? 1177 ASN   A N     1 
ATOM   8649  C  CA    . ASN   A  1  1179 ? 4.227   85.733  113.559 1.00 21.98 ? 1177 ASN   A CA    1 
ATOM   8650  C  C     . ASN   A  1  1179 ? 3.683   87.057  113.036 1.00 25.63 ? 1177 ASN   A C     1 
ATOM   8651  O  O     . ASN   A  1  1179 ? 2.853   87.078  112.121 1.00 24.17 ? 1177 ASN   A O     1 
ATOM   8652  C  CB    . ASN   A  1  1179 ? 3.501   85.328  114.845 1.00 28.29 ? 1177 ASN   A CB    1 
ATOM   8653  C  CG    . ASN   A  1  1179 ? 2.302   84.441  114.597 1.00 30.03 ? 1177 ASN   A CG    1 
ATOM   8654  O  OD1   . ASN   A  1  1179 ? 2.118   83.900  113.502 1.00 35.62 ? 1177 ASN   A OD1   1 
ATOM   8655  N  ND2   . ASN   A  1  1179 ? 1.472   84.277  115.629 1.00 34.81 ? 1177 ASN   A ND2   1 
ATOM   8656  N  N     . LYS   A  1  1180 ? 4.146   88.173  113.604 1.00 24.34 ? 1178 LYS   A N     1 
ATOM   8657  C  CA    . LYS   A  1  1180 ? 3.739   89.482  113.104 1.00 24.83 ? 1178 LYS   A CA    1 
ATOM   8658  C  C     . LYS   A  1  1180 ? 4.211   89.696  111.673 1.00 22.93 ? 1178 LYS   A C     1 
ATOM   8659  O  O     . LYS   A  1  1180 ? 3.452   90.184  110.827 1.00 24.41 ? 1178 LYS   A O     1 
ATOM   8660  C  CB    . LYS   A  1  1180 ? 4.276   90.579  114.022 1.00 27.31 ? 1178 LYS   A CB    1 
ATOM   8661  C  CG    . LYS   A  1  1180 ? 3.586   90.610  115.381 1.00 29.17 ? 1178 LYS   A CG    1 
ATOM   8662  C  CD    . LYS   A  1  1180 ? 4.399   91.401  116.413 1.00 29.63 ? 1178 LYS   A CD    1 
ATOM   8663  C  CE    . LYS   A  1  1180 ? 4.588   92.858  115.994 1.00 39.27 ? 1178 LYS   A CE    1 
ATOM   8664  N  NZ    . LYS   A  1  1180 ? 5.313   93.663  117.032 1.00 41.45 ? 1178 LYS   A NZ    1 
ATOM   8665  N  N     . ALA   A  1  1181 ? 5.457   89.328  111.378 1.00 24.17 ? 1179 ALA   A N     1 
ATOM   8666  C  CA    . ALA   A  1  1181 ? 5.967   89.476  110.018 1.00 23.19 ? 1179 ALA   A CA    1 
ATOM   8667  C  C     . ALA   A  1  1181 ? 5.213   88.584  109.038 1.00 23.44 ? 1179 ALA   A C     1 
ATOM   8668  O  O     . ALA   A  1  1181 ? 4.926   88.996  107.908 1.00 22.22 ? 1179 ALA   A O     1 
ATOM   8669  C  CB    . ALA   A  1  1181 ? 7.465   89.177  109.982 1.00 23.35 ? 1179 ALA   A CB    1 
ATOM   8670  N  N     . ILE   A  1  1182 ? 4.871   87.361  109.451 1.00 22.21 ? 1180 ILE   A N     1 
ATOM   8671  C  CA    . ILE   A  1  1182 ? 4.129   86.476  108.559 1.00 21.84 ? 1180 ILE   A CA    1 
ATOM   8672  C  C     . ILE   A  1  1182 ? 2.735   87.023  108.302 1.00 20.86 ? 1180 ILE   A C     1 
ATOM   8673  O  O     . ILE   A  1  1182 ? 2.231   86.974  107.172 1.00 22.94 ? 1180 ILE   A O     1 
ATOM   8674  C  CB    . ILE   A  1  1182 ? 4.084   85.051  109.134 1.00 22.85 ? 1180 ILE   A CB    1 
ATOM   8675  C  CG1   . ILE   A  1  1182 ? 5.475   84.433  109.083 1.00 20.30 ? 1180 ILE   A CG1   1 
ATOM   8676  C  CG2   . ILE   A  1  1182 ? 3.047   84.212  108.396 1.00 23.43 ? 1180 ILE   A CG2   1 
ATOM   8677  C  CD1   . ILE   A  1  1182 ? 5.570   83.069  109.760 1.00 23.23 ? 1180 ILE   A CD1   1 
ATOM   8678  N  N     . ALA   A  1  1183 ? 2.084   87.546  109.343 1.00 21.90 ? 1181 ALA   A N     1 
ATOM   8679  C  CA    . ALA   A  1  1183 ? 0.737   88.072  109.169 1.00 23.02 ? 1181 ALA   A CA    1 
ATOM   8680  C  C     . ALA   A  1  1183 ? 0.731   89.231  108.189 1.00 24.02 ? 1181 ALA   A C     1 
ATOM   8681  O  O     . ALA   A  1  1183 ? -0.282  89.479  107.518 1.00 23.50 ? 1181 ALA   A O     1 
ATOM   8682  C  CB    . ALA   A  1  1183 ? 0.159   88.514  110.516 1.00 24.94 ? 1181 ALA   A CB    1 
ATOM   8683  N  N     . ALA   A  1  1184 ? 1.851   89.941  108.087 1.00 23.22 ? 1182 ALA   A N     1 
ATOM   8684  C  CA    . ALA   A  1  1184 ? 1.954   91.090  107.202 1.00 24.89 ? 1182 ALA   A CA    1 
ATOM   8685  C  C     . ALA   A  1  1184 ? 2.190   90.696  105.756 1.00 23.69 ? 1182 ALA   A C     1 
ATOM   8686  O  O     . ALA   A  1  1184 ? 2.125   91.564  104.880 1.00 24.66 ? 1182 ALA   A O     1 
ATOM   8687  C  CB    . ALA   A  1  1184 ? 3.080   92.021  107.662 1.00 25.22 ? 1182 ALA   A CB    1 
ATOM   8688  N  N     . LEU   A  1  1185 ? 2.466   89.427  105.483 1.00 21.74 ? 1183 LEU   A N     1 
ATOM   8689  C  CA    . LEU   A  1  1185 ? 2.667   89.018  104.103 1.00 23.57 ? 1183 LEU   A CA    1 
ATOM   8690  C  C     . LEU   A  1  1185 ? 1.366   89.178  103.323 1.00 22.48 ? 1183 LEU   A C     1 
ATOM   8691  O  O     . LEU   A  1  1185 ? 0.284   88.906  103.850 1.00 23.69 ? 1183 LEU   A O     1 
ATOM   8692  C  CB    . LEU   A  1  1185 ? 3.129   87.566  104.027 1.00 20.26 ? 1183 LEU   A CB    1 
ATOM   8693  C  CG    . LEU   A  1  1185 ? 4.451   87.279  104.736 1.00 22.68 ? 1183 LEU   A CG    1 
ATOM   8694  C  CD1   . LEU   A  1  1185 ? 4.750   85.794  104.708 1.00 22.40 ? 1183 LEU   A CD1   1 
ATOM   8695  C  CD2   . LEU   A  1  1185 ? 5.609   88.093  104.146 1.00 24.26 ? 1183 LEU   A CD2   1 
ATOM   8696  N  N     . PRO   A  1  1186 ? 1.434   89.618  102.072 1.00 25.50 ? 1184 PRO   A N     1 
ATOM   8697  C  CA    . PRO   A  1  1186 ? 0.212   89.728  101.271 1.00 23.83 ? 1184 PRO   A CA    1 
ATOM   8698  C  C     . PRO   A  1  1186 ? -0.382  88.360  100.982 1.00 21.26 ? 1184 PRO   A C     1 
ATOM   8699  O  O     . PRO   A  1  1186 ? 0.315   87.343  100.968 1.00 22.71 ? 1184 PRO   A O     1 
ATOM   8700  C  CB    . PRO   A  1  1186 ? 0.703   90.377  99.972  1.00 26.76 ? 1184 PRO   A CB    1 
ATOM   8701  C  CG    . PRO   A  1  1186 ? 2.139   89.981  99.874  1.00 29.76 ? 1184 PRO   A CG    1 
ATOM   8702  C  CD    . PRO   A  1  1186 ? 2.647   89.920  101.295 1.00 26.41 ? 1184 PRO   A CD    1 
ATOM   8703  N  N     . GLY   A  1  1187 ? -1.693  88.349  100.749 1.00 22.02 ? 1185 GLY   A N     1 
ATOM   8704  C  CA    . GLY   A  1  1187 ? -2.338  87.171  100.223 1.00 24.83 ? 1185 GLY   A CA    1 
ATOM   8705  C  C     . GLY   A  1  1187 ? -2.909  86.267  101.295 1.00 20.23 ? 1185 GLY   A C     1 
ATOM   8706  O  O     . GLY   A  1  1187 ? -3.599  86.712  102.213 1.00 23.59 ? 1185 GLY   A O     1 
ATOM   8707  N  N     . PRO   A  1  1188 ? -2.637  84.970  101.184 1.00 20.08 ? 1186 PRO   A N     1 
ATOM   8708  C  CA    . PRO   A  1  1188 ? -3.365  84.000  102.004 1.00 19.43 ? 1186 PRO   A CA    1 
ATOM   8709  C  C     . PRO   A  1  1188 ? -2.930  84.044  103.454 1.00 19.99 ? 1186 PRO   A C     1 
ATOM   8710  O  O     . PRO   A  1  1188 ? -1.782  84.353  103.781 1.00 20.96 ? 1186 PRO   A O     1 
ATOM   8711  C  CB    . PRO   A  1  1188 ? -2.995  82.656  101.371 1.00 22.79 ? 1186 PRO   A CB    1 
ATOM   8712  C  CG    . PRO   A  1  1188 ? -1.637  82.886  100.806 1.00 24.79 ? 1186 PRO   A CG    1 
ATOM   8713  C  CD    . PRO   A  1  1188 ? -1.664  84.319  100.294 1.00 22.34 ? 1186 PRO   A CD    1 
ATOM   8714  N  N     . LEU   A  1  1189 ? -3.869  83.716  104.331 1.00 19.59 ? 1187 LEU   A N     1 
ATOM   8715  C  CA    . LEU   A  1  1189 ? -3.497  83.464  105.715 1.00 20.21 ? 1187 LEU   A CA    1 
ATOM   8716  C  C     . LEU   A  1  1189 ? -2.649  82.200  105.752 1.00 20.76 ? 1187 LEU   A C     1 
ATOM   8717  O  O     . LEU   A  1  1189 ? -2.934  81.226  105.051 1.00 24.44 ? 1187 LEU   A O     1 
ATOM   8718  C  CB    . LEU   A  1  1189 ? -4.747  83.288  106.572 1.00 19.81 ? 1187 LEU   A CB    1 
ATOM   8719  C  CG    . LEU   A  1  1189 ? -5.471  84.560  107.037 1.00 22.14 ? 1187 LEU   A CG    1 
ATOM   8720  C  CD1   . LEU   A  1  1189 ? -6.167  85.292  105.879 1.00 23.88 ? 1187 LEU   A CD1   1 
ATOM   8721  C  CD2   . LEU   A  1  1189 ? -6.473  84.230  108.122 1.00 27.33 ? 1187 LEU   A CD2   1 
ATOM   8722  N  N     . LEU   A  1  1190 ? -1.559  82.238  106.512 1.00 20.26 ? 1188 LEU   A N     1 
ATOM   8723  C  CA    . LEU   A  1  1190 ? -0.658  81.098  106.604 1.00 20.37 ? 1188 LEU   A CA    1 
ATOM   8724  C  C     . LEU   A  1  1190 ? -0.919  80.354  107.899 1.00 19.86 ? 1188 LEU   A C     1 
ATOM   8725  O  O     . LEU   A  1  1190 ? -0.984  80.965  108.970 1.00 22.56 ? 1188 LEU   A O     1 
ATOM   8726  C  CB    . LEU   A  1  1190 ? 0.812   81.518  106.544 1.00 20.98 ? 1188 LEU   A CB    1 
ATOM   8727  C  CG    . LEU   A  1  1190 ? 1.230   82.248  105.272 1.00 22.27 ? 1188 LEU   A CG    1 
ATOM   8728  C  CD1   . LEU   A  1  1190 ? 2.748   82.306  105.229 1.00 25.26 ? 1188 LEU   A CD1   1 
ATOM   8729  C  CD2   . LEU   A  1  1190 ? 0.691   81.507  104.059 1.00 24.29 ? 1188 LEU   A CD2   1 
ATOM   8730  N  N     . LEU   A  1  1191 ? -1.071  79.041  107.797 1.00 19.91 ? 1189 LEU   A N     1 
ATOM   8731  C  CA    . LEU   A  1  1191 ? -1.088  78.207  108.990 1.00 21.49 ? 1189 LEU   A CA    1 
ATOM   8732  C  C     . LEU   A  1  1191 ? 0.347   78.081  109.479 1.00 19.22 ? 1189 LEU   A C     1 
ATOM   8733  O  O     . LEU   A  1  1191 ? 1.176   77.414  108.844 1.00 20.36 ? 1189 LEU   A O     1 
ATOM   8734  C  CB    . LEU   A  1  1191 ? -1.705  76.850  108.668 1.00 19.68 ? 1189 LEU   A CB    1 
ATOM   8735  C  CG    . LEU   A  1  1191 ? -2.251  76.022  109.832 1.00 20.16 ? 1189 LEU   A CG    1 
ATOM   8736  C  CD1   . LEU   A  1  1191 ? -3.073  74.871  109.287 1.00 20.79 ? 1189 LEU   A CD1   1 
ATOM   8737  C  CD2   . LEU   A  1  1191 ? -1.110  75.486  110.697 1.00 20.47 ? 1189 LEU   A CD2   1 
ATOM   8738  N  N     . VAL   A  1  1192 ? 0.635   78.754  110.593 1.00 19.84 ? 1190 VAL   A N     1 
ATOM   8739  C  CA    . VAL   A  1  1192 ? 1.968   78.831  111.175 1.00 19.20 ? 1190 VAL   A CA    1 
ATOM   8740  C  C     . VAL   A  1  1192 ? 2.050   77.848  112.334 1.00 19.71 ? 1190 VAL   A C     1 
ATOM   8741  O  O     . VAL   A  1  1192 ? 1.156   77.803  113.191 1.00 21.99 ? 1190 VAL   A O     1 
ATOM   8742  C  CB    . VAL   A  1  1192 ? 2.256   80.256  111.674 1.00 23.80 ? 1190 VAL   A CB    1 
ATOM   8743  C  CG1   . VAL   A  1  1192 ? 3.667   80.337  112.221 1.00 23.39 ? 1190 VAL   A CG1   1 
ATOM   8744  C  CG2   . VAL   A  1  1192 ? 2.057   81.260  110.560 1.00 25.90 ? 1190 VAL   A CG2   1 
ATOM   8745  N  N     . GLN   A  1  1193 ? 3.132   77.084  112.381 1.00 18.90 ? 1191 GLN   A N     1 
ATOM   8746  C  CA    . GLN   A  1  1193 ? 3.462   76.264  113.534 1.00 15.44 ? 1191 GLN   A CA    1 
ATOM   8747  C  C     . GLN   A  1  1193 ? 4.805   76.720  114.065 1.00 17.97 ? 1191 GLN   A C     1 
ATOM   8748  O  O     . GLN   A  1  1193 ? 5.761   76.869  113.297 1.00 18.42 ? 1191 GLN   A O     1 
ATOM   8749  C  CB    . GLN   A  1  1193 ? 3.582   74.801  113.154 1.00 17.96 ? 1191 GLN   A CB    1 
ATOM   8750  C  CG    . GLN   A  1  1193 ? 2.338   74.226  112.531 1.00 19.70 ? 1191 GLN   A CG    1 
ATOM   8751  C  CD    . GLN   A  1  1193 ? 2.401   72.723  112.472 1.00 19.30 ? 1191 GLN   A CD    1 
ATOM   8752  O  OE1   . GLN   A  1  1193 ? 2.329   72.051  113.500 1.00 21.13 ? 1191 GLN   A OE1   1 
ATOM   8753  N  NE2   . GLN   A  1  1193 ? 2.545   72.187  111.274 1.00 19.70 ? 1191 GLN   A NE2   1 
ATOM   8754  N  N     . ALA   A  1  1194 ? 4.882   76.923  115.373 1.00 17.29 ? 1192 ALA   A N     1 
ATOM   8755  C  CA    . ALA   A  1  1194 ? 6.112   77.384  115.981 1.00 17.62 ? 1192 ALA   A CA    1 
ATOM   8756  C  C     . ALA   A  1  1194 ? 6.547   76.414  117.066 1.00 19.22 ? 1192 ALA   A C     1 
ATOM   8757  O  O     . ALA   A  1  1194 ? 5.728   75.732  117.686 1.00 19.70 ? 1192 ALA   A O     1 
ATOM   8758  C  CB    . ALA   A  1  1194 ? 5.906   78.761  116.603 1.00 18.64 ? 1192 ALA   A CB    1 
ATOM   8759  N  N     . ALA   A  1  1195 ? 7.848   76.378  117.300 1.00 18.69 ? 1193 ALA   A N     1 
ATOM   8760  C  CA    . ALA   A  1  1195 ? 8.400   75.555  118.358 1.00 22.37 ? 1193 ALA   A CA    1 
ATOM   8761  C  C     . ALA   A  1  1195 ? 9.699   76.195  118.800 1.00 21.25 ? 1193 ALA   A C     1 
ATOM   8762  O  O     . ALA   A  1  1195 ? 10.370  76.863  118.012 1.00 21.65 ? 1193 ALA   A O     1 
ATOM   8763  C  CB    . ALA   A  1  1195 ? 8.662   74.139  117.842 1.00 19.54 ? 1193 ALA   A CB    1 
ATOM   8764  N  N     . SER   A  1  1196 ? 10.048  75.999  120.066 1.00 20.05 ? 1194 SER   A N     1 
ATOM   8765  C  CA    . SER   A  1  1196 ? 11.364  76.415  120.512 1.00 22.54 ? 1194 SER   A CA    1 
ATOM   8766  C  C     . SER   A  1  1196 ? 12.400  75.381  120.089 1.00 21.15 ? 1194 SER   A C     1 
ATOM   8767  O  O     . SER   A  1  1196 ? 12.073  74.260  119.697 1.00 21.64 ? 1194 SER   A O     1 
ATOM   8768  C  CB    . SER   A  1  1196 ? 11.388  76.539  122.030 1.00 26.20 ? 1194 SER   A CB    1 
ATOM   8769  O  OG    . SER   A  1  1196 ? 11.251  75.258  122.619 1.00 24.21 ? 1194 SER   A OG    1 
ATOM   8770  N  N     . SER   A  1  1197 ? 13.675  75.762  120.178 1.00 21.40 ? 1195 SER   A N     1 
ATOM   8771  C  CA    . SER   A  1  1197 ? 14.730  74.800  119.880 1.00 21.08 ? 1195 SER   A CA    1 
ATOM   8772  C  C     . SER   A  1  1197 ? 14.650  73.602  120.820 1.00 21.25 ? 1195 SER   A C     1 
ATOM   8773  O  O     . SER   A  1  1197 ? 14.815  72.452  120.394 1.00 22.27 ? 1195 SER   A O     1 
ATOM   8774  C  CB    . SER   A  1  1197 ? 16.096  75.479  119.979 1.00 23.80 ? 1195 SER   A CB    1 
ATOM   8775  O  OG    . SER   A  1  1197 ? 16.208  76.550  119.051 1.00 24.03 ? 1195 SER   A OG    1 
ATOM   8776  N  N     . GLY   A  1  1198 ? 14.388  73.855  122.099 1.00 23.63 ? 1196 GLY   A N     1 
ATOM   8777  C  CA    . GLY   A  1  1198 ? 14.260  72.760  123.050 1.00 23.81 ? 1196 GLY   A CA    1 
ATOM   8778  C  C     . GLY   A  1  1198 ? 13.067  71.870  122.764 1.00 27.29 ? 1196 GLY   A C     1 
ATOM   8779  O  O     . GLY   A  1  1198 ? 13.143  70.647  122.912 1.00 24.97 ? 1196 GLY   A O     1 
ATOM   8780  N  N     . GLU   A  1  1199 ? 11.950  72.469  122.341 1.00 24.39 ? 1197 GLU   A N     1 
ATOM   8781  C  CA    . GLU   A  1  1199 ? 10.787  71.673  121.975 1.00 25.18 ? 1197 GLU   A CA    1 
ATOM   8782  C  C     . GLU   A  1  1199 ? 11.100  70.758  120.800 1.00 24.53 ? 1197 GLU   A C     1 
ATOM   8783  O  O     . GLU   A  1  1199 ? 10.705  69.587  120.791 1.00 23.01 ? 1197 GLU   A O     1 
ATOM   8784  C  CB    . GLU   A  1  1199 ? 9.624   72.600  121.648 1.00 23.48 ? 1197 GLU   A CB    1 
ATOM   8785  C  CG    . GLU   A  1  1199 ? 8.318   71.908  121.414 1.00 30.56 ? 1197 GLU   A CG    1 
ATOM   8786  C  CD    . GLU   A  1  1199 ? 7.205   72.908  121.229 1.00 38.62 ? 1197 GLU   A CD    1 
ATOM   8787  O  OE1   . GLU   A  1  1199 ? 7.491   74.129  121.333 1.00 35.28 ? 1197 GLU   A OE1   1 
ATOM   8788  O  OE2   . GLU   A  1  1199 ? 6.056   72.478  120.986 1.00 43.82 ? 1197 GLU   A OE2   1 
ATOM   8789  N  N     . ILE   A  1  1200 ? 11.815  71.273  119.798 1.00 21.44 ? 1198 ILE   A N     1 
ATOM   8790  C  CA    . ILE   A  1  1200 ? 12.215  70.439  118.669 1.00 22.86 ? 1198 ILE   A CA    1 
ATOM   8791  C  C     . ILE   A  1  1200 ? 13.062  69.268  119.149 1.00 24.81 ? 1198 ILE   A C     1 
ATOM   8792  O  O     . ILE   A  1  1200 ? 12.918  68.140  118.668 1.00 23.56 ? 1198 ILE   A O     1 
ATOM   8793  C  CB    . ILE   A  1  1200 ? 12.954  71.289  117.622 1.00 20.84 ? 1198 ILE   A CB    1 
ATOM   8794  C  CG1   . ILE   A  1  1200 ? 11.997  72.302  116.991 1.00 21.96 ? 1198 ILE   A CG1   1 
ATOM   8795  C  CG2   . ILE   A  1  1200 ? 13.617  70.392  116.555 1.00 21.98 ? 1198 ILE   A CG2   1 
ATOM   8796  C  CD1   . ILE   A  1  1200 ? 12.692  73.307  116.124 1.00 21.15 ? 1198 ILE   A CD1   1 
ATOM   8797  N  N     . ALA   A  1  1201 ? 13.941  69.514  120.122 1.00 23.63 ? 1199 ALA   A N     1 
ATOM   8798  C  CA    . ALA   A  1  1201 ? 14.792  68.446  120.628 1.00 25.41 ? 1199 ALA   A CA    1 
ATOM   8799  C  C     . ALA   A  1  1201 ? 13.984  67.422  121.415 1.00 25.66 ? 1199 ALA   A C     1 
ATOM   8800  O  O     . ALA   A  1  1201 ? 14.270  66.220  121.359 1.00 26.68 ? 1199 ALA   A O     1 
ATOM   8801  C  CB    . ALA   A  1  1201 ? 15.903  69.037  121.494 1.00 24.88 ? 1199 ALA   A CB    1 
ATOM   8802  N  N     . ARG   A  1  1202 ? 12.973  67.876  122.154 1.00 23.57 ? 1200 ARG   A N     1 
ATOM   8803  C  CA    . ARG   A  1  1202 ? 12.237  66.984  123.037 1.00 24.32 ? 1200 ARG   A CA    1 
ATOM   8804  C  C     . ARG   A  1  1202 ? 11.068  66.286  122.358 1.00 27.46 ? 1200 ARG   A C     1 
ATOM   8805  O  O     . ARG   A  1  1202 ? 10.753  65.141  122.707 1.00 27.99 ? 1200 ARG   A O     1 
ATOM   8806  C  CB    . ARG   A  1  1202 ? 11.718  67.749  124.261 1.00 22.23 ? 1200 ARG   A CB    1 
ATOM   8807  C  CG    . ARG   A  1  1202 ? 12.822  68.253  125.185 1.00 23.51 ? 1200 ARG   A CG    1 
ATOM   8808  C  CD    . ARG   A  1  1202 ? 12.220  68.915  126.416 1.00 26.79 ? 1200 ARG   A CD    1 
ATOM   8809  N  NE    . ARG   A  1  1202 ? 11.365  70.032  126.043 1.00 29.98 ? 1200 ARG   A NE    1 
ATOM   8810  C  CZ    . ARG   A  1  1202 ? 11.728  71.307  126.077 1.00 30.68 ? 1200 ARG   A CZ    1 
ATOM   8811  N  NH1   . ARG   A  1  1202 ? 12.900  71.683  126.568 1.00 28.10 ? 1200 ARG   A NH1   1 
ATOM   8812  N  NH2   . ARG   A  1  1202 ? 10.895  72.228  125.599 1.00 30.59 ? 1200 ARG   A NH2   1 
ATOM   8813  N  N     . ASN   A  1  1203 ? 10.417  66.931  121.402 1.00 23.60 ? 1201 ASN   A N     1 
ATOM   8814  C  CA    . ASN   A  1  1203 ? 9.145   66.427  120.889 1.00 24.54 ? 1201 ASN   A CA    1 
ATOM   8815  C  C     . ASN   A  1  1203 ? 9.257   66.109  119.409 1.00 28.10 ? 1201 ASN   A C     1 
ATOM   8816  O  O     . ASN   A  1  1203 ? 9.340   67.037  118.582 1.00 26.49 ? 1201 ASN   A O     1 
ATOM   8817  C  CB    . ASN   A  1  1203 ? 8.030   67.444  121.128 1.00 25.32 ? 1201 ASN   A CB    1 
ATOM   8818  C  CG    . ASN   A  1  1203 ? 6.675   66.946  120.659 1.00 29.97 ? 1201 ASN   A CG    1 
ATOM   8819  O  OD1   . ASN   A  1  1203 ? 6.534   65.802  120.232 1.00 30.08 ? 1201 ASN   A OD1   1 
ATOM   8820  N  ND2   . ASN   A  1  1203 ? 5.666   67.811  120.739 1.00 31.65 ? 1201 ASN   A ND2   1 
ATOM   8821  N  N     . PRO   A  1  1204 ? 9.234   64.834  119.024 1.00 27.58 ? 1202 PRO   A N     1 
ATOM   8822  C  CA    . PRO   A  1  1204 ? 9.282   64.497  117.595 1.00 31.68 ? 1202 PRO   A CA    1 
ATOM   8823  C  C     . PRO   A  1  1204 ? 8.157   65.116  116.791 1.00 28.30 ? 1202 PRO   A C     1 
ATOM   8824  O  O     . PRO   A  1  1204 ? 8.297   65.275  115.575 1.00 29.45 ? 1202 PRO   A O     1 
ATOM   8825  C  CB    . PRO   A  1  1204 ? 9.193   62.964  117.594 1.00 33.18 ? 1202 PRO   A CB    1 
ATOM   8826  C  CG    . PRO   A  1  1204 ? 9.695   62.561  118.941 1.00 35.47 ? 1202 PRO   A CG    1 
ATOM   8827  C  CD    . PRO   A  1  1204 ? 9.202   63.633  119.875 1.00 30.35 ? 1202 PRO   A CD    1 
ATOM   8828  N  N     . ASP   A  1  1205 ? 7.051   65.480  117.434 1.00 28.11 ? 1203 ASP   A N     1 
ATOM   8829  C  CA    . ASP   A  1  1205 ? 5.915   66.090  116.757 1.00 28.26 ? 1203 ASP   A CA    1 
ATOM   8830  C  C     . ASP   A  1  1205 ? 5.804   67.578  117.063 1.00 26.01 ? 1203 ASP   A C     1 
ATOM   8831  O  O     . ASP   A  1  1205 ? 4.706   68.142  117.026 1.00 29.15 ? 1203 ASP   A O     1 
ATOM   8832  C  CB    . ASP   A  1  1205 ? 4.623   65.363  117.120 1.00 33.14 ? 1203 ASP   A CB    1 
ATOM   8833  C  CG    . ASP   A  1  1205 ? 4.683   63.880  116.809 1.00 38.93 ? 1203 ASP   A CG    1 
ATOM   8834  O  OD1   . ASP   A  1  1205 ? 5.448   63.485  115.905 1.00 37.35 ? 1203 ASP   A OD1   1 
ATOM   8835  O  OD2   . ASP   A  1  1205 ? 3.967   63.107  117.477 1.00 43.48 ? 1203 ASP   A OD2   1 
ATOM   8836  N  N     . ALA   A  1  1206 ? 6.930   68.215  117.403 1.00 25.02 ? 1204 ALA   A N     1 
ATOM   8837  C  CA    . ALA   A  1  1206 ? 6.941   69.662  117.604 1.00 26.34 ? 1204 ALA   A CA    1 
ATOM   8838  C  C     . ALA   A  1  1206 ? 6.221   70.373  116.467 1.00 25.07 ? 1204 ALA   A C     1 
ATOM   8839  O  O     . ALA   A  1  1206 ? 5.427   71.292  116.702 1.00 28.25 ? 1204 ALA   A O     1 
ATOM   8840  C  CB    . ALA   A  1  1206 ? 8.381   70.164  117.711 1.00 25.26 ? 1204 ALA   A CB    1 
ATOM   8841  N  N     . TYR   A  1  1207 ? 6.475   69.948  115.231 1.00 20.66 ? 1205 TYR   A N     1 
ATOM   8842  C  CA    . TYR   A  1  1207 ? 5.718   70.387  114.067 1.00 22.00 ? 1205 TYR   A CA    1 
ATOM   8843  C  C     . TYR   A  1  1207 ? 4.824   69.238  113.634 1.00 22.21 ? 1205 TYR   A C     1 
ATOM   8844  O  O     . TYR   A  1  1207 ? 5.312   68.154  113.302 1.00 30.39 ? 1205 TYR   A O     1 
ATOM   8845  C  CB    . TYR   A  1  1207 ? 6.641   70.796  112.923 1.00 21.95 ? 1205 TYR   A CB    1 
ATOM   8846  C  CG    . TYR   A  1  1207 ? 7.587   71.907  113.298 1.00 20.80 ? 1205 TYR   A CG    1 
ATOM   8847  C  CD1   . TYR   A  1  1207 ? 7.099   73.156  113.670 1.00 20.49 ? 1205 TYR   A CD1   1 
ATOM   8848  C  CD2   . TYR   A  1  1207 ? 8.965   71.711  113.289 1.00 20.40 ? 1205 TYR   A CD2   1 
ATOM   8849  C  CE1   . TYR   A  1  1207 ? 7.952   74.176  114.012 1.00 20.03 ? 1205 TYR   A CE1   1 
ATOM   8850  C  CE2   . TYR   A  1  1207 ? 9.832   72.739  113.637 1.00 21.39 ? 1205 TYR   A CE2   1 
ATOM   8851  C  CZ    . TYR   A  1  1207 ? 9.312   73.967  113.998 1.00 19.37 ? 1205 TYR   A CZ    1 
ATOM   8852  O  OH    . TYR   A  1  1207 ? 10.137  75.001  114.347 1.00 21.17 ? 1205 TYR   A OH    1 
ATOM   8853  N  N     . CYS   A  1  1208 ? 3.528   69.484  113.609 1.00 20.95 ? 1206 CYS   A N     1 
ATOM   8854  C  CA    . CYS   A  1  1208 ? 2.564   68.437  113.330 1.00 21.26 ? 1206 CYS   A CA    1 
ATOM   8855  C  C     . CYS   A  1  1208 ? 2.367   68.323  111.825 1.00 20.76 ? 1206 CYS   A C     1 
ATOM   8856  O  O     . CYS   A  1  1208 ? 2.090   69.320  111.145 1.00 20.19 ? 1206 CYS   A O     1 
ATOM   8857  C  CB    . CYS   A  1  1208 ? 1.257   68.765  114.043 1.00 25.28 ? 1206 CYS   A CB    1 
ATOM   8858  S  SG    . CYS   A  1  1208 ? -0.072  67.607  113.710 1.00 28.11 ? 1206 CYS   A SG    1 
ATOM   8859  N  N     . LEU   A  1  1209 ? 2.539   67.107  111.303 1.00 17.49 ? 1207 LEU   A N     1 
ATOM   8860  C  CA    . LEU   A  1  1209 ? 2.436   66.913  109.866 1.00 17.75 ? 1207 LEU   A CA    1 
ATOM   8861  C  C     . LEU   A  1  1209 ? 1.005   67.009  109.350 1.00 18.22 ? 1207 LEU   A C     1 
ATOM   8862  O  O     . LEU   A  1  1209 ? 0.828   67.163  108.140 1.00 19.20 ? 1207 LEU   A O     1 
ATOM   8863  C  CB    . LEU   A  1  1209 ? 3.053   65.569  109.473 1.00 18.15 ? 1207 LEU   A CB    1 
ATOM   8864  C  CG    . LEU   A  1  1209 ? 4.486   65.337  109.942 1.00 18.66 ? 1207 LEU   A CG    1 
ATOM   8865  C  CD1   . LEU   A  1  1209 ? 4.968   63.992  109.427 1.00 20.44 ? 1207 LEU   A CD1   1 
ATOM   8866  C  CD2   . LEU   A  1  1209 ? 5.399   66.461  109.464 1.00 20.91 ? 1207 LEU   A CD2   1 
ATOM   8867  N  N     . ASN   A  1  1210 ? -0.002  66.945  110.233 1.00 19.97 ? 1208 ASN   A N     1 
ATOM   8868  C  CA    . ASN   A  1  1210 ? -1.386  67.125  109.800 1.00 20.17 ? 1208 ASN   A CA    1 
ATOM   8869  C  C     . ASN   A  1  1210 ? -1.561  68.453  109.075 1.00 18.47 ? 1208 ASN   A C     1 
ATOM   8870  O  O     . ASN   A  1  1210 ? -2.344  68.554  108.129 1.00 21.49 ? 1208 ASN   A O     1 
ATOM   8871  C  CB    . ASN   A  1  1210 ? -2.340  67.129  111.005 1.00 22.15 ? 1208 ASN   A CB    1 
ATOM   8872  C  CG    . ASN   A  1  1210 ? -2.438  65.784  111.710 1.00 26.29 ? 1208 ASN   A CG    1 
ATOM   8873  O  OD1   . ASN   A  1  1210 ? -1.671  64.859  111.450 1.00 31.27 ? 1208 ASN   A OD1   1 
ATOM   8874  N  ND2   . ASN   A  1  1210 ? -3.386  65.688  112.636 1.00 32.01 ? 1208 ASN   A ND2   1 
ATOM   8875  N  N     . TRP   A  1  1211 ? -0.864  69.491  109.530 1.00 18.24 ? 1209 TRP   A N     1 
ATOM   8876  C  CA    . TRP   A  1  1211 ? -1.086  70.832  109.015 1.00 19.36 ? 1209 TRP   A CA    1 
ATOM   8877  C  C     . TRP   A  1  1211 ? -0.147  71.188  107.878 1.00 19.18 ? 1209 TRP   A C     1 
ATOM   8878  O  O     . TRP   A  1  1211 ? -0.180  72.323  107.399 1.00 21.34 ? 1209 TRP   A O     1 
ATOM   8879  C  CB    . TRP   A  1  1211 ? -0.997  71.865  110.150 1.00 19.70 ? 1209 TRP   A CB    1 
ATOM   8880  C  CG    . TRP   A  1  1211 ? -1.572  71.348  111.441 1.00 21.04 ? 1209 TRP   A CG    1 
ATOM   8881  C  CD1   . TRP   A  1  1211 ? -0.942  71.289  112.659 1.00 20.20 ? 1209 TRP   A CD1   1 
ATOM   8882  C  CD2   . TRP   A  1  1211 ? -2.869  70.768  111.635 1.00 21.29 ? 1209 TRP   A CD2   1 
ATOM   8883  N  NE1   . TRP   A  1  1211 ? -1.773  70.719  113.595 1.00 22.81 ? 1209 TRP   A NE1   1 
ATOM   8884  C  CE2   . TRP   A  1  1211 ? -2.962  70.398  112.994 1.00 21.30 ? 1209 TRP   A CE2   1 
ATOM   8885  C  CE3   . TRP   A  1  1211 ? -3.964  70.534  110.794 1.00 21.78 ? 1209 TRP   A CE3   1 
ATOM   8886  C  CZ2   . TRP   A  1  1211 ? -4.103  69.796  113.531 1.00 21.69 ? 1209 TRP   A CZ2   1 
ATOM   8887  C  CZ3   . TRP   A  1  1211 ? -5.107  69.949  111.337 1.00 21.81 ? 1209 TRP   A CZ3   1 
ATOM   8888  C  CH2   . TRP   A  1  1211 ? -5.161  69.581  112.686 1.00 21.36 ? 1209 TRP   A CH2   1 
ATOM   8889  N  N     . LEU   A  1  1212 ? 0.685   70.246  107.436 1.00 17.06 ? 1210 LEU   A N     1 
ATOM   8890  C  CA    . LEU   A  1  1212 ? 1.596   70.462  106.325 1.00 16.52 ? 1210 LEU   A CA    1 
ATOM   8891  C  C     . LEU   A  1  1212 ? 1.139   69.761  105.056 1.00 16.54 ? 1210 LEU   A C     1 
ATOM   8892  O  O     . LEU   A  1  1212 ? 1.818   69.847  104.032 1.00 16.86 ? 1210 LEU   A O     1 
ATOM   8893  C  CB    . LEU   A  1  1212 ? 3.003   70.007  106.714 1.00 15.28 ? 1210 LEU   A CB    1 
ATOM   8894  C  CG    . LEU   A  1  1212 ? 3.666   70.981  107.677 1.00 16.17 ? 1210 LEU   A CG    1 
ATOM   8895  C  CD1   . LEU   A  1  1212 ? 4.814   70.298  108.392 1.00 17.81 ? 1210 LEU   A CD1   1 
ATOM   8896  C  CD2   . LEU   A  1  1212 ? 4.158   72.201  106.899 1.00 18.78 ? 1210 LEU   A CD2   1 
ATOM   8897  N  N     . VAL   A  1  1213 ? 0.009   69.068  105.104 1.00 17.14 ? 1211 VAL   A N     1 
ATOM   8898  C  CA    . VAL   A  1  1213 ? -0.621  68.526  103.912 1.00 17.04 ? 1211 VAL   A CA    1 
ATOM   8899  C  C     . VAL   A  1  1213 ? -1.895  69.308  103.664 1.00 16.85 ? 1211 VAL   A C     1 
ATOM   8900  O  O     . VAL   A  1  1213 ? -2.397  70.039  104.526 1.00 18.72 ? 1211 VAL   A O     1 
ATOM   8901  C  CB    . VAL   A  1  1213 ? -0.922  67.015  104.012 1.00 17.39 ? 1211 VAL   A CB    1 
ATOM   8902  C  CG1   . VAL   A  1  1213 ? 0.368   66.220  104.081 1.00 17.93 ? 1211 VAL   A CG1   1 
ATOM   8903  C  CG2   . VAL   A  1  1213 ? -1.791  66.716  105.215 1.00 18.70 ? 1211 VAL   A CG2   1 
ATOM   8904  N  N     . GLU   A  1  1214 ? -2.406  69.162  102.450 1.00 17.72 ? 1212 GLU   A N     1 
ATOM   8905  C  CA    . GLU   A  1  1214 ? -3.612  69.835  102.004 1.00 20.13 ? 1212 GLU   A CA    1 
ATOM   8906  C  C     . GLU   A  1  1214 ? -4.621  68.761  101.650 1.00 16.97 ? 1212 GLU   A C     1 
ATOM   8907  O  O     . GLU   A  1  1214 ? -4.317  67.853  100.873 1.00 16.71 ? 1212 GLU   A O     1 
ATOM   8908  C  CB    . GLU   A  1  1214 ? -3.282  70.625  100.750 1.00 22.43 ? 1212 GLU   A CB    1 
ATOM   8909  C  CG    . GLU   A  1  1214 ? -4.301  71.655  100.358 1.00 32.09 ? 1212 GLU   A CG    1 
ATOM   8910  C  CD    . GLU   A  1  1214 ? -3.789  72.492  99.203  1.00 33.66 ? 1212 GLU   A CD    1 
ATOM   8911  O  OE1   . GLU   A  1  1214 ? -4.004  72.084  98.045  1.00 35.80 ? 1212 GLU   A OE1   1 
ATOM   8912  O  OE2   . GLU   A  1  1214 ? -3.142  73.534  99.461  1.00 34.88 ? 1212 GLU   A OE2   1 
ATOM   8913  N  N     . GLU   A  1  1215 ? -5.815  68.869  102.211 1.00 16.49 ? 1213 GLU   A N     1 
ATOM   8914  C  CA    . GLU   A  1  1215 ? -6.877  67.941  101.884 1.00 14.93 ? 1213 GLU   A CA    1 
ATOM   8915  C  C     . GLU   A  1  1215 ? -7.548  68.384  100.597 1.00 16.56 ? 1213 GLU   A C     1 
ATOM   8916  O  O     . GLU   A  1  1215 ? -7.786  69.573  100.376 1.00 16.54 ? 1213 GLU   A O     1 
ATOM   8917  C  CB    . GLU   A  1  1215 ? -7.927  67.953  102.985 1.00 15.84 ? 1213 GLU   A CB    1 
ATOM   8918  C  CG    . GLU   A  1  1215 ? -7.403  67.584  104.340 1.00 16.63 ? 1213 GLU   A CG    1 
ATOM   8919  C  CD    . GLU   A  1  1215 ? -8.356  67.985  105.431 1.00 20.30 ? 1213 GLU   A CD    1 
ATOM   8920  O  OE1   . GLU   A  1  1215 ? -8.346  69.176  105.803 1.00 18.95 ? 1213 GLU   A OE1   1 
ATOM   8921  O  OE2   . GLU   A  1  1215 ? -9.111  67.118  105.903 1.00 18.87 ? 1213 GLU   A OE2   1 
ATOM   8922  N  N     . VAL   A  1  1216 ? -7.859  67.418  99.754  1.00 15.65 ? 1214 VAL   A N     1 
ATOM   8923  C  CA    . VAL   A  1  1216 ? -8.631  67.674  98.549  1.00 16.32 ? 1214 VAL   A CA    1 
ATOM   8924  C  C     . VAL   A  1  1216 ? -9.775  66.682  98.508  1.00 16.47 ? 1214 VAL   A C     1 
ATOM   8925  O  O     . VAL   A  1  1216 ? -9.570  65.474  98.665  1.00 16.98 ? 1214 VAL   A O     1 
ATOM   8926  C  CB    . VAL   A  1  1216 ? -7.785  67.587  97.270  1.00 17.63 ? 1214 VAL   A CB    1 
ATOM   8927  C  CG1   . VAL   A  1  1216 ? -8.678  67.790  96.063  1.00 16.87 ? 1214 VAL   A CG1   1 
ATOM   8928  C  CG2   . VAL   A  1  1216 ? -6.680  68.639  97.298  1.00 19.31 ? 1214 VAL   A CG2   1 
ATOM   8929  N  N     . SER   A  1  1217 ? -10.977 67.193  98.313  1.00 17.13 ? 1215 SER   A N     1 
ATOM   8930  C  CA    . SER   A  1  1217 ? -12.168 66.380  98.154  1.00 17.01 ? 1215 SER   A CA    1 
ATOM   8931  C  C     . SER   A  1  1217 ? -12.580 66.463  96.696  1.00 15.39 ? 1215 SER   A C     1 
ATOM   8932  O  O     . SER   A  1  1217 ? -12.560 67.545  96.104  1.00 16.68 ? 1215 SER   A O     1 
ATOM   8933  C  CB    . SER   A  1  1217 ? -13.291 66.926  99.029  1.00 20.11 ? 1215 SER   A CB    1 
ATOM   8934  O  OG    . SER   A  1  1217 ? -14.547 66.436  98.599  1.00 22.11 ? 1215 SER   A OG    1 
ATOM   8935  N  N     . ALA   A  1  1218 ? -12.914 65.321  96.116  1.00 15.37 ? 1216 ALA   A N     1 
ATOM   8936  C  CA    . ALA   A  1  1218 ? -13.387 65.282  94.739  1.00 16.70 ? 1216 ALA   A CA    1 
ATOM   8937  C  C     . ALA   A  1  1218 ? -14.660 64.458  94.688  1.00 16.44 ? 1216 ALA   A C     1 
ATOM   8938  O  O     . ALA   A  1  1218 ? -14.692 63.319  95.170  1.00 19.10 ? 1216 ALA   A O     1 
ATOM   8939  C  CB    . ALA   A  1  1218 ? -12.336 64.699  93.793  1.00 16.47 ? 1216 ALA   A CB    1 
ATOM   8940  N  N     . SER   A  1  1219 ? -15.705 65.035  94.108  1.00 15.12 ? 1217 SER   A N     1 
ATOM   8941  C  CA    . SER   A  1  1219 ? -17.001 64.384  94.006  1.00 16.12 ? 1217 SER   A CA    1 
ATOM   8942  C  C     . SER   A  1  1219 ? -17.322 64.215  92.534  1.00 15.62 ? 1217 SER   A C     1 
ATOM   8943  O  O     . SER   A  1  1219 ? -17.463 65.201  91.807  1.00 15.80 ? 1217 SER   A O     1 
ATOM   8944  C  CB    . SER   A  1  1219 ? -18.088 65.198  94.702  1.00 17.58 ? 1217 SER   A CB    1 
ATOM   8945  O  OG    . SER   A  1  1219 ? -19.326 64.518  94.587  1.00 18.02 ? 1217 SER   A OG    1 
ATOM   8946  N  N     . ILE   A  1  1220 ? -17.434 62.970  92.104  1.00 15.07 ? 1218 ILE   A N     1 
ATOM   8947  C  CA    . ILE   A  1  1220 ? -17.620 62.630  90.703  1.00 17.14 ? 1218 ILE   A CA    1 
ATOM   8948  C  C     . ILE   A  1  1220 ? -19.011 62.039  90.544  1.00 15.60 ? 1218 ILE   A C     1 
ATOM   8949  O  O     . ILE   A  1  1220 ? -19.340 61.033  91.181  1.00 16.21 ? 1218 ILE   A O     1 
ATOM   8950  C  CB    . ILE   A  1  1220 ? -16.558 61.628  90.237  1.00 16.90 ? 1218 ILE   A CB    1 
ATOM   8951  C  CG1   . ILE   A  1  1220 ? -15.155 62.184  90.496  1.00 23.60 ? 1218 ILE   A CG1   1 
ATOM   8952  C  CG2   . ILE   A  1  1220 ? -16.761 61.332  88.763  1.00 19.92 ? 1218 ILE   A CG2   1 
ATOM   8953  C  CD1   . ILE   A  1  1220 ? -14.091 61.126  90.655  1.00 31.56 ? 1218 ILE   A CD1   1 
ATOM   8954  N  N     . ASN   A  1  1221 ? -19.817 62.645  89.682  1.00 15.61 ? 1219 ASN   A N     1 
ATOM   8955  C  CA    . ASN   A  1  1221 ? -21.140 62.118  89.364  1.00 17.41 ? 1219 ASN   A CA    1 
ATOM   8956  C  C     . ASN   A  1  1221 ? -20.956 60.989  88.355  1.00 18.28 ? 1219 ASN   A C     1 
ATOM   8957  O  O     . ASN   A  1  1221 ? -20.720 61.231  87.176  1.00 19.90 ? 1219 ASN   A O     1 
ATOM   8958  C  CB    . ASN   A  1  1221 ? -22.014 63.236  88.809  1.00 18.59 ? 1219 ASN   A CB    1 
ATOM   8959  C  CG    . ASN   A  1  1221 ? -23.358 62.737  88.321  1.00 19.67 ? 1219 ASN   A CG    1 
ATOM   8960  O  OD1   . ASN   A  1  1221 ? -23.744 61.593  88.566  1.00 17.72 ? 1219 ASN   A OD1   1 
ATOM   8961  N  ND2   . ASN   A  1  1221 ? -24.079 63.603  87.618  1.00 22.91 ? 1219 ASN   A ND2   1 
ATOM   8962  N  N     . THR   A  1  1222 ? -21.078 59.749  88.815  1.00 16.78 ? 1220 THR   A N     1 
ATOM   8963  C  CA    . THR   A  1  1222 ? -20.871 58.596  87.954  1.00 19.61 ? 1220 THR   A CA    1 
ATOM   8964  C  C     . THR   A  1  1222 ? -22.152 58.145  87.279  1.00 23.54 ? 1220 THR   A C     1 
ATOM   8965  O  O     . THR   A  1  1222 ? -22.144 57.134  86.570  1.00 25.94 ? 1220 THR   A O     1 
ATOM   8966  C  CB    . THR   A  1  1222 ? -20.250 57.449  88.750  1.00 22.06 ? 1220 THR   A CB    1 
ATOM   8967  O  OG1   . THR   A  1  1222 ? -21.127 57.083  89.820  1.00 20.67 ? 1220 THR   A OG1   1 
ATOM   8968  C  CG2   . THR   A  1  1222 ? -18.906 57.886  89.323  1.00 21.53 ? 1220 THR   A CG2   1 
ATOM   8969  N  N     . ALA   A  1  1223 ? -23.249 58.855  87.504  1.00 20.07 ? 1221 ALA   A N     1 
ATOM   8970  C  CA    . ALA   A  1  1223 ? -24.486 58.634  86.777  1.00 24.14 ? 1221 ALA   A CA    1 
ATOM   8971  C  C     . ALA   A  1  1223 ? -24.667 59.619  85.630  1.00 28.59 ? 1221 ALA   A C     1 
ATOM   8972  O  O     . ALA   A  1  1223 ? -25.723 59.617  84.992  1.00 33.46 ? 1221 ALA   A O     1 
ATOM   8973  C  CB    . ALA   A  1  1223 ? -25.674 58.737  87.733  1.00 24.91 ? 1221 ALA   A CB    1 
ATOM   8974  N  N     . ALA   A  1  1224 ? -23.665 60.464  85.359  1.00 29.01 ? 1222 ALA   A N     1 
ATOM   8975  C  CA    . ALA   A  1  1224 ? -23.830 61.547  84.394  1.00 29.83 ? 1222 ALA   A CA    1 
ATOM   8976  C  C     . ALA   A  1  1224 ? -23.995 61.049  82.963  1.00 33.42 ? 1222 ALA   A C     1 
ATOM   8977  O  O     . ALA   A  1  1224 ? -24.589 61.757  82.145  1.00 39.84 ? 1222 ALA   A O     1 
ATOM   8978  C  CB    . ALA   A  1  1224 ? -22.659 62.527  84.489  1.00 30.14 ? 1222 ALA   A CB    1 
ATOM   8979  N  N     . ALA   A  1  1225 ? -23.496 59.852  82.643  1.00 32.96 ? 1223 ALA   A N     1 
ATOM   8980  C  CA    . ALA   A  1  1225 ? -23.669 59.321  81.294  1.00 39.15 ? 1223 ALA   A CA    1 
ATOM   8981  C  C     . ALA   A  1  1225 ? -25.099 58.877  81.010  1.00 42.37 ? 1223 ALA   A C     1 
ATOM   8982  O  O     . ALA   A  1  1225 ? -25.409 58.556  79.857  1.00 41.55 ? 1223 ALA   A O     1 
ATOM   8983  C  CB    . ALA   A  1  1225 ? -22.692 58.171  81.029  1.00 39.64 ? 1223 ALA   A CB    1 
ATOM   8984  N  N     . GLY   A  1  1226 ? -25.967 58.848  82.017  1.00 35.95 ? 1224 GLY   A N     1 
ATOM   8985  C  CA    . GLY   A  1  1226 ? -27.362 58.482  81.829  1.00 41.50 ? 1224 GLY   A CA    1 
ATOM   8986  C  C     . GLY   A  1  1226 ? -27.815 57.284  82.635  1.00 45.18 ? 1224 GLY   A C     1 
ATOM   8987  O  O     . GLY   A  1  1226 ? -29.004 56.936  82.579  1.00 39.65 ? 1224 GLY   A O     1 
ATOM   8988  N  N     . GLY   A  1  1227 ? -26.929 56.637  83.381  1.00 33.06 ? 1225 GLY   A N     1 
ATOM   8989  C  CA    . GLY   A  1  1227 ? -27.310 55.484  84.171  1.00 37.61 ? 1225 GLY   A CA    1 
ATOM   8990  C  C     . GLY   A  1  1227 ? -26.209 55.153  85.151  1.00 35.34 ? 1225 GLY   A C     1 
ATOM   8991  O  O     . GLY   A  1  1227 ? -25.140 55.772  85.155  1.00 37.12 ? 1225 GLY   A O     1 
ATOM   8992  N  N     . ASN   A  1  1228 ? -26.483 54.154  85.983  1.00 27.11 ? 1226 ASN   A N     1 
ATOM   8993  C  CA    . ASN   A  1  1228 ? -25.581 53.740  87.052  1.00 33.28 ? 1226 ASN   A CA    1 
ATOM   8994  C  C     . ASN   A  1  1228 ? -25.076 52.335  86.731  1.00 35.35 ? 1226 ASN   A C     1 
ATOM   8995  O  O     . ASN   A  1  1228 ? -25.844 51.367  86.770  1.00 36.85 ? 1226 ASN   A O     1 
ATOM   8996  C  CB    . ASN   A  1  1228 ? -26.321 53.782  88.390  1.00 34.37 ? 1226 ASN   A CB    1 
ATOM   8997  C  CG    . ASN   A  1  1228 ? -25.403 53.588  89.585  1.00 37.08 ? 1226 ASN   A CG    1 
ATOM   8998  O  OD1   . ASN   A  1  1228 ? -24.418 52.847  89.522  1.00 37.40 ? 1226 ASN   A OD1   1 
ATOM   8999  N  ND2   . ASN   A  1  1228 ? -25.738 54.243  90.696  1.00 35.09 ? 1226 ASN   A ND2   1 
ATOM   9000  N  N     . ALA   A  1  1229 ? -23.779 52.230  86.416  1.00 35.73 ? 1227 ALA   A N     1 
ATOM   9001  C  CA    . ALA   A  1  1229 ? -23.193 50.937  86.072  1.00 37.11 ? 1227 ALA   A CA    1 
ATOM   9002  C  C     . ALA   A  1  1229 ? -23.208 49.981  87.259  1.00 41.32 ? 1227 ALA   A C     1 
ATOM   9003  O  O     . ALA   A  1  1229 ? -23.552 48.802  87.109  1.00 39.71 ? 1227 ALA   A O     1 
ATOM   9004  C  CB    . ALA   A  1  1229 ? -21.764 51.132  85.566  1.00 34.09 ? 1227 ALA   A CB    1 
ATOM   9005  N  N     . SER   A  1  1230 ? -22.828 50.465  88.446  1.00 37.45 ? 1228 SER   A N     1 
ATOM   9006  C  CA    . SER   A  1  1230 ? -22.787 49.594  89.618  1.00 40.31 ? 1228 SER   A CA    1 
ATOM   9007  C  C     . SER   A  1  1230 ? -24.166 49.026  89.933  1.00 44.55 ? 1228 SER   A C     1 
ATOM   9008  O  O     . SER   A  1  1230 ? -24.293 47.853  90.309  1.00 46.35 ? 1228 SER   A O     1 
ATOM   9009  C  CB    . SER   A  1  1230 ? -22.226 50.356  90.819  1.00 41.02 ? 1228 SER   A CB    1 
ATOM   9010  N  N     . LEU   A  1  1231 ? -25.214 49.834  89.767  1.00 36.48 ? 1229 LEU   A N     1 
ATOM   9011  C  CA    . LEU   A  1  1231 ? -26.568 49.377  90.047  1.00 42.48 ? 1229 LEU   A CA    1 
ATOM   9012  C  C     . LEU   A  1  1231 ? -27.150 48.505  88.939  1.00 42.60 ? 1229 LEU   A C     1 
ATOM   9013  O  O     . LEU   A  1  1231 ? -28.197 47.882  89.150  1.00 43.05 ? 1229 LEU   A O     1 
ATOM   9014  C  CB    . LEU   A  1  1231 ? -27.488 50.566  90.342  1.00 37.15 ? 1229 LEU   A CB    1 
ATOM   9015  C  CG    . LEU   A  1  1231 ? -27.421 51.174  91.748  1.00 37.55 ? 1229 LEU   A CG    1 
ATOM   9016  C  CD1   . LEU   A  1  1231 ? -28.538 52.185  91.955  1.00 30.19 ? 1229 LEU   A CD1   1 
ATOM   9017  C  CD2   . LEU   A  1  1231 ? -27.492 50.100  92.812  1.00 41.64 ? 1229 LEU   A CD2   1 
ATOM   9018  N  N     . MET   A  1  1232 ? -26.502 48.437  87.772  1.00 43.81 ? 1230 MET   A N     1 
ATOM   9019  C  CA    . MET   A  1  1232 ? -26.941 47.491  86.749  1.00 45.73 ? 1230 MET   A CA    1 
ATOM   9020  C  C     . MET   A  1  1232 ? -26.812 46.050  87.229  1.00 44.02 ? 1230 MET   A C     1 
ATOM   9021  O  O     . MET   A  1  1232 ? -27.543 45.171  86.760  1.00 42.26 ? 1230 MET   A O     1 
ATOM   9022  C  CB    . MET   A  1  1232 ? -26.148 47.696  85.455  1.00 41.64 ? 1230 MET   A CB    1 
ATOM   9023  C  CG    . MET   A  1  1232 ? -26.502 48.961  84.686  1.00 41.52 ? 1230 MET   A CG    1 
ATOM   9024  S  SD    . MET   A  1  1232 ? -25.423 49.171  83.243  1.00 47.01 ? 1230 MET   A SD    1 
ATOM   9025  C  CE    . MET   A  1  1232 ? -25.845 47.708  82.273  1.00 41.55 ? 1230 MET   A CE    1 
ATOM   9026  N  N     . ALA   A  1  1233 ? -25.895 45.790  88.162  1.00 49.71 ? 1231 ALA   A N     1 
ATOM   9027  C  CA    . ALA   A  1  1233 ? -25.719 44.465  88.742  1.00 51.36 ? 1231 ALA   A CA    1 
ATOM   9028  C  C     . ALA   A  1  1233 ? -26.625 44.213  89.940  1.00 55.11 ? 1231 ALA   A C     1 
ATOM   9029  O  O     . ALA   A  1  1233 ? -26.651 43.088  90.453  1.00 54.81 ? 1231 ALA   A O     1 
ATOM   9030  C  CB    . ALA   A  1  1233 ? -24.258 44.256  89.155  1.00 51.28 ? 1231 ALA   A CB    1 
ATOM   9031  N  N     . ILE   A  1  1234 ? -27.365 45.219  90.395  1.00 54.94 ? 1232 ILE   A N     1 
ATOM   9032  C  CA    . ILE   A  1  1234 ? -28.239 45.090  91.555  1.00 54.45 ? 1232 ILE   A CA    1 
ATOM   9033  C  C     . ILE   A  1  1234 ? -29.664 44.870  91.062  1.00 53.30 ? 1232 ILE   A C     1 
ATOM   9034  O  O     . ILE   A  1  1234 ? -30.281 45.765  90.471  1.00 50.74 ? 1232 ILE   A O     1 
ATOM   9035  C  CB    . ILE   A  1  1234 ? -28.129 46.300  92.494  1.00 46.92 ? 1232 ILE   A CB    1 
ATOM   9036  C  CG1   . ILE   A  1  1234 ? -26.750 46.316  93.162  1.00 49.33 ? 1232 ILE   A CG1   1 
ATOM   9037  C  CG2   . ILE   A  1  1234 ? -29.230 46.263  93.534  1.00 39.23 ? 1232 ILE   A CG2   1 
ATOM   9038  C  CD1   . ILE   A  1  1234 ? -26.685 47.112  94.444  1.00 42.76 ? 1232 ILE   A CD1   1 
ATOM   9039  N  N     . GLY   A  1  1235 ? -30.181 43.670  91.297  1.00 48.70 ? 1233 GLY   A N     1 
ATOM   9040  C  CA    . GLY   A  1  1235 ? -31.549 43.339  90.959  1.00 41.73 ? 1233 GLY   A CA    1 
ATOM   9041  C  C     . GLY   A  1  1235 ? -32.160 42.483  92.049  1.00 40.63 ? 1233 GLY   A C     1 
ATOM   9042  O  O     . GLY   A  1  1235 ? -31.463 41.707  92.707  1.00 44.79 ? 1233 GLY   A O     1 
ATOM   9043  O  OXT   . GLY   A  1  1235 ? -33.356 42.541  92.305  1.00 27.74 ? 1233 GLY   A OXT   1 
ATOM   9044  N  N     . ALA   B  1  16   ? 30.110  4.977   80.986  1.00 42.06 ? 14   ALA   B N     1 
ATOM   9045  C  CA    . ALA   B  1  16   ? 29.143  6.028   81.293  1.00 42.44 ? 14   ALA   B CA    1 
ATOM   9046  C  C     . ALA   B  1  16   ? 27.733  5.465   81.248  1.00 40.63 ? 14   ALA   B C     1 
ATOM   9047  O  O     . ALA   B  1  16   ? 27.386  4.744   80.313  1.00 43.47 ? 14   ALA   B O     1 
ATOM   9048  C  CB    . ALA   B  1  16   ? 29.278  7.189   80.309  1.00 37.11 ? 14   ALA   B CB    1 
ATOM   9049  N  N     . PRO   B  1  17   ? 26.921  5.794   82.254  1.00 41.25 ? 15   PRO   B N     1 
ATOM   9050  C  CA    . PRO   B  1  17   ? 25.536  5.305   82.265  1.00 37.94 ? 15   PRO   B CA    1 
ATOM   9051  C  C     . PRO   B  1  17   ? 24.778  5.784   81.036  1.00 36.26 ? 15   PRO   B C     1 
ATOM   9052  O  O     . PRO   B  1  17   ? 24.934  6.925   80.593  1.00 36.18 ? 15   PRO   B O     1 
ATOM   9053  C  CB    . PRO   B  1  17   ? 24.957  5.903   83.553  1.00 40.30 ? 15   PRO   B CB    1 
ATOM   9054  C  CG    . PRO   B  1  17   ? 25.852  7.056   83.881  1.00 42.29 ? 15   PRO   B CG    1 
ATOM   9055  C  CD    . PRO   B  1  17   ? 27.216  6.658   83.409  1.00 38.43 ? 15   PRO   B CD    1 
ATOM   9056  N  N     . ALA   B  1  18   ? 23.973  4.885   80.475  1.00 32.98 ? 16   ALA   B N     1 
ATOM   9057  C  CA    . ALA   B  1  18   ? 23.184  5.224   79.303  1.00 30.22 ? 16   ALA   B CA    1 
ATOM   9058  C  C     . ALA   B  1  18   ? 22.265  6.397   79.635  1.00 26.52 ? 16   ALA   B C     1 
ATOM   9059  O  O     . ALA   B  1  18   ? 21.726  6.465   80.746  1.00 27.76 ? 16   ALA   B O     1 
ATOM   9060  C  CB    . ALA   B  1  18   ? 22.336  4.031   78.867  1.00 31.85 ? 16   ALA   B CB    1 
ATOM   9061  N  N     . PRO   B  1  19   ? 22.086  7.339   78.715  1.00 25.15 ? 17   PRO   B N     1 
ATOM   9062  C  CA    . PRO   B  1  19   ? 21.258  8.511   79.013  1.00 24.95 ? 17   PRO   B CA    1 
ATOM   9063  C  C     . PRO   B  1  19   ? 19.840  8.100   79.377  1.00 22.78 ? 17   PRO   B C     1 
ATOM   9064  O  O     . PRO   B  1  19   ? 19.216  7.279   78.698  1.00 23.83 ? 17   PRO   B O     1 
ATOM   9065  C  CB    . PRO   B  1  19   ? 21.297  9.311   77.704  1.00 24.02 ? 17   PRO   B CB    1 
ATOM   9066  C  CG    . PRO   B  1  19   ? 22.565  8.910   77.061  1.00 27.95 ? 17   PRO   B CG    1 
ATOM   9067  C  CD    . PRO   B  1  19   ? 22.738  7.448   77.400  1.00 28.20 ? 17   PRO   B CD    1 
ATOM   9068  N  N     . PHE   B  1  20   ? 19.348  8.654   80.483  1.00 23.18 ? 18   PHE   B N     1 
ATOM   9069  C  CA    . PHE   B  1  20   ? 17.970  8.486   80.935  1.00 21.62 ? 18   PHE   B CA    1 
ATOM   9070  C  C     . PHE   B  1  20   ? 17.635  7.068   81.374  1.00 25.69 ? 18   PHE   B C     1 
ATOM   9071  O  O     . PHE   B  1  20   ? 16.458  6.758   81.568  1.00 25.83 ? 18   PHE   B O     1 
ATOM   9072  C  CB    . PHE   B  1  20   ? 16.955  8.966   79.895  1.00 21.43 ? 18   PHE   B CB    1 
ATOM   9073  C  CG    . PHE   B  1  20   ? 17.140  10.395  79.496  1.00 19.17 ? 18   PHE   B CG    1 
ATOM   9074  C  CD1   . PHE   B  1  20   ? 16.788  11.413  80.363  1.00 18.65 ? 18   PHE   B CD1   1 
ATOM   9075  C  CD2   . PHE   B  1  20   ? 17.673  10.719  78.257  1.00 20.00 ? 18   PHE   B CD2   1 
ATOM   9076  C  CE1   . PHE   B  1  20   ? 16.946  12.742  80.003  1.00 21.12 ? 18   PHE   B CE1   1 
ATOM   9077  C  CE2   . PHE   B  1  20   ? 17.836  12.041  77.894  1.00 20.79 ? 18   PHE   B CE2   1 
ATOM   9078  C  CZ    . PHE   B  1  20   ? 17.471  13.052  78.769  1.00 20.45 ? 18   PHE   B CZ    1 
ATOM   9079  N  N     . ALA   B  1  21   ? 18.633  6.200   81.539  1.00 27.70 ? 19   ALA   B N     1 
ATOM   9080  C  CA    . ALA   B  1  21   ? 18.358  4.817   81.918  1.00 29.45 ? 19   ALA   B CA    1 
ATOM   9081  C  C     . ALA   B  1  21   ? 17.770  4.710   83.319  1.00 31.24 ? 19   ALA   B C     1 
ATOM   9082  O  O     . ALA   B  1  21   ? 17.092  3.723   83.625  1.00 35.41 ? 19   ALA   B O     1 
ATOM   9083  C  CB    . ALA   B  1  21   ? 19.632  3.979   81.801  1.00 32.34 ? 19   ALA   B CB    1 
ATOM   9084  N  N     . ASP   B  1  22   ? 17.999  5.702   84.170  1.00 24.80 ? 20   ASP   B N     1 
ATOM   9085  C  CA    . ASP   B  1  22   ? 17.443  5.716   85.515  1.00 27.91 ? 20   ASP   B CA    1 
ATOM   9086  C  C     . ASP   B  1  22   ? 16.750  7.038   85.774  1.00 22.14 ? 20   ASP   B C     1 
ATOM   9087  O  O     . ASP   B  1  22   ? 16.882  7.632   86.852  1.00 25.01 ? 20   ASP   B O     1 
ATOM   9088  C  CB    . ASP   B  1  22   ? 18.523  5.446   86.559  1.00 29.58 ? 20   ASP   B CB    1 
ATOM   9089  N  N     . PHE   B  1  23   ? 15.998  7.526   84.784  1.00 19.00 ? 21   PHE   B N     1 
ATOM   9090  C  CA    . PHE   B  1  23   ? 15.463  8.882   84.885  1.00 18.57 ? 21   PHE   B CA    1 
ATOM   9091  C  C     . PHE   B  1  23   ? 14.499  9.021   86.062  1.00 18.72 ? 21   PHE   B C     1 
ATOM   9092  O  O     . PHE   B  1  23   ? 14.655  9.911   86.907  1.00 18.92 ? 21   PHE   B O     1 
ATOM   9093  C  CB    . PHE   B  1  23   ? 14.781  9.272   83.576  1.00 20.12 ? 21   PHE   B CB    1 
ATOM   9094  C  CG    . PHE   B  1  23   ? 14.093  10.587  83.648  1.00 18.42 ? 21   PHE   B CG    1 
ATOM   9095  C  CD1   . PHE   B  1  23   ? 14.824  11.746  83.787  1.00 18.84 ? 21   PHE   B CD1   1 
ATOM   9096  C  CD2   . PHE   B  1  23   ? 12.704  10.662  83.597  1.00 19.71 ? 21   PHE   B CD2   1 
ATOM   9097  C  CE1   . PHE   B  1  23   ? 14.177  12.981  83.890  1.00 18.23 ? 21   PHE   B CE1   1 
ATOM   9098  C  CE2   . PHE   B  1  23   ? 12.062  11.882  83.696  1.00 20.65 ? 21   PHE   B CE2   1 
ATOM   9099  C  CZ    . PHE   B  1  23   ? 12.796  13.035  83.843  1.00 19.16 ? 21   PHE   B CZ    1 
ATOM   9100  N  N     . ALA   B  1  24   ? 13.481  8.171   86.116  1.00 19.47 ? 22   ALA   B N     1 
ATOM   9101  C  CA    . ALA   B  1  24   ? 12.496  8.275   87.190  1.00 18.18 ? 22   ALA   B CA    1 
ATOM   9102  C  C     . ALA   B  1  24   ? 11.785  6.946   87.411  1.00 19.45 ? 22   ALA   B C     1 
ATOM   9103  O  O     . ALA   B  1  24   ? 10.556  6.874   87.294  1.00 20.93 ? 22   ALA   B O     1 
ATOM   9104  C  CB    . ALA   B  1  24   ? 11.473  9.359   86.852  1.00 22.12 ? 22   ALA   B CB    1 
ATOM   9105  N  N     . PRO   B  1  25   ? 12.502  5.887   87.759  1.00 20.01 ? 23   PRO   B N     1 
ATOM   9106  C  CA    . PRO   B  1  25   ? 11.853  4.585   87.945  1.00 23.23 ? 23   PRO   B CA    1 
ATOM   9107  C  C     . PRO   B  1  25   ? 10.855  4.656   89.086  1.00 23.48 ? 23   PRO   B C     1 
ATOM   9108  O  O     . PRO   B  1  25   ? 11.138  5.279   90.117  1.00 22.76 ? 23   PRO   B O     1 
ATOM   9109  C  CB    . PRO   B  1  25   ? 13.028  3.659   88.294  1.00 24.46 ? 23   PRO   B CB    1 
ATOM   9110  C  CG    . PRO   B  1  25   ? 14.062  4.552   88.844  1.00 24.64 ? 23   PRO   B CG    1 
ATOM   9111  C  CD    . PRO   B  1  25   ? 13.930  5.854   88.113  1.00 21.80 ? 23   PRO   B CD    1 
ATOM   9112  N  N     . PRO   B  1  26   ? 9.675   4.058   88.937  1.00 21.98 ? 24   PRO   B N     1 
ATOM   9113  C  CA    . PRO   B  1  26   ? 8.691   4.105   90.023  1.00 22.36 ? 24   PRO   B CA    1 
ATOM   9114  C  C     . PRO   B  1  26   ? 9.164   3.293   91.218  1.00 22.73 ? 24   PRO   B C     1 
ATOM   9115  O  O     . PRO   B  1  26   ? 9.991   2.387   91.103  1.00 23.54 ? 24   PRO   B O     1 
ATOM   9116  C  CB    . PRO   B  1  26   ? 7.441   3.478   89.399  1.00 25.79 ? 24   PRO   B CB    1 
ATOM   9117  C  CG    . PRO   B  1  26   ? 7.964   2.581   88.346  1.00 24.79 ? 24   PRO   B CG    1 
ATOM   9118  C  CD    . PRO   B  1  26   ? 9.197   3.262   87.793  1.00 22.71 ? 24   PRO   B CD    1 
ATOM   9119  N  N     . VAL   B  1  27   ? 8.622   3.643   92.386  1.00 22.31 ? 25   VAL   B N     1 
ATOM   9120  C  CA    . VAL   B  1  27   ? 8.959   2.912   93.605  1.00 21.79 ? 25   VAL   B CA    1 
ATOM   9121  C  C     . VAL   B  1  27   ? 8.624   1.437   93.450  1.00 22.27 ? 25   VAL   B C     1 
ATOM   9122  O  O     . VAL   B  1  27   ? 9.379   0.563   93.892  1.00 26.19 ? 25   VAL   B O     1 
ATOM   9123  C  CB    . VAL   B  1  27   ? 8.246   3.538   94.817  1.00 22.41 ? 25   VAL   B CB    1 
ATOM   9124  C  CG1   . VAL   B  1  27   ? 8.372   2.624   96.032  1.00 25.15 ? 25   VAL   B CG1   1 
ATOM   9125  C  CG2   . VAL   B  1  27   ? 8.824   4.901   95.108  1.00 21.36 ? 25   VAL   B CG2   1 
ATOM   9126  N  N     . ARG   B  1  28   ? 7.508   1.136   92.800  1.00 22.44 ? 26   ARG   B N     1 
ATOM   9127  C  CA    . ARG   B  1  28   ? 7.061   -0.236  92.628  1.00 22.93 ? 26   ARG   B CA    1 
ATOM   9128  C  C     . ARG   B  1  28   ? 6.276   -0.319  91.332  1.00 25.86 ? 26   ARG   B C     1 
ATOM   9129  O  O     . ARG   B  1  28   ? 5.806   0.705   90.822  1.00 25.00 ? 26   ARG   B O     1 
ATOM   9130  C  CB    . ARG   B  1  28   ? 6.183   -0.669  93.810  1.00 26.80 ? 26   ARG   B CB    1 
ATOM   9131  C  CG    . ARG   B  1  28   ? 4.841   0.058   93.873  1.00 27.07 ? 26   ARG   B CG    1 
ATOM   9132  C  CD    . ARG   B  1  28   ? 4.039   -0.330  95.109  1.00 30.29 ? 26   ARG   B CD    1 
ATOM   9133  N  NE    . ARG   B  1  28   ? 4.611   0.256   96.314  1.00 30.21 ? 26   ARG   B NE    1 
ATOM   9134  C  CZ    . ARG   B  1  28   ? 5.349   -0.406  97.194  1.00 34.33 ? 26   ARG   B CZ    1 
ATOM   9135  N  NH1   . ARG   B  1  28   ? 5.599   -1.699  97.056  1.00 33.16 ? 26   ARG   B NH1   1 
ATOM   9136  N  NH2   . ARG   B  1  28   ? 5.851   0.246   98.239  1.00 33.00 ? 26   ARG   B NH2   1 
ATOM   9137  N  N     . PRO   B  1  29   ? 6.146   -1.510  90.752  1.00 25.34 ? 27   PRO   B N     1 
ATOM   9138  C  CA    . PRO   B  1  29   ? 5.249   -1.658  89.603  1.00 25.78 ? 27   PRO   B CA    1 
ATOM   9139  C  C     . PRO   B  1  29   ? 3.841   -1.230  89.984  1.00 26.46 ? 27   PRO   B C     1 
ATOM   9140  O  O     . PRO   B  1  29   ? 3.352   -1.535  91.075  1.00 25.87 ? 27   PRO   B O     1 
ATOM   9141  C  CB    . PRO   B  1  29   ? 5.314   -3.156  89.289  1.00 29.15 ? 27   PRO   B CB    1 
ATOM   9142  C  CG    . PRO   B  1  29   ? 6.626   -3.601  89.853  1.00 29.82 ? 27   PRO   B CG    1 
ATOM   9143  C  CD    . PRO   B  1  29   ? 6.823   -2.776  91.089  1.00 27.41 ? 27   PRO   B CD    1 
ATOM   9144  N  N     . GLN   B  1  30   ? 3.195   -0.508  89.075  1.00 24.28 ? 28   GLN   B N     1 
ATOM   9145  C  CA    . GLN   B  1  30   ? 1.896   0.089   89.362  1.00 26.73 ? 28   GLN   B CA    1 
ATOM   9146  C  C     . GLN   B  1  30   ? 0.796   -0.938  89.133  1.00 24.28 ? 28   GLN   B C     1 
ATOM   9147  O  O     . GLN   B  1  30   ? 0.598   -1.414  88.007  1.00 24.30 ? 28   GLN   B O     1 
ATOM   9148  C  CB    . GLN   B  1  30   ? 1.680   1.327   88.493  1.00 24.23 ? 28   GLN   B CB    1 
ATOM   9149  C  CG    . GLN   B  1  30   ? 2.775   2.376   88.654  1.00 22.43 ? 28   GLN   B CG    1 
ATOM   9150  C  CD    . GLN   B  1  30   ? 2.742   3.040   90.012  1.00 24.58 ? 28   GLN   B CD    1 
ATOM   9151  O  OE1   . GLN   B  1  30   ? 1.853   3.841   90.298  1.00 25.44 ? 28   GLN   B OE1   1 
ATOM   9152  N  NE2   . GLN   B  1  30   ? 3.709   2.705   90.866  1.00 23.39 ? 28   GLN   B NE2   1 
ATOM   9153  N  N     . SER   B  1  31   ? 0.084   -1.277  90.206  1.00 24.66 ? 29   SER   B N     1 
ATOM   9154  C  CA    . SER   B  1  31   ? -1.013  -2.222  90.150  1.00 23.10 ? 29   SER   B CA    1 
ATOM   9155  C  C     . SER   B  1  31   ? -2.189  -1.616  89.385  1.00 22.32 ? 29   SER   B C     1 
ATOM   9156  O  O     . SER   B  1  31   ? -2.223  -0.418  89.087  1.00 22.98 ? 29   SER   B O     1 
ATOM   9157  C  CB    . SER   B  1  31   ? -1.484  -2.554  91.561  1.00 23.96 ? 29   SER   B CB    1 
ATOM   9158  O  OG    . SER   B  1  31   ? -2.121  -1.427  92.141  1.00 23.20 ? 29   SER   B OG    1 
ATOM   9159  N  N     . THR   B  1  32   ? -3.164  -2.468  89.062  1.00 23.90 ? 30   THR   B N     1 
ATOM   9160  C  CA    . THR   B  1  32   ? -4.382  -1.987  88.416  1.00 24.30 ? 30   THR   B CA    1 
ATOM   9161  C  C     . THR   B  1  32   ? -5.030  -0.871  89.229  1.00 23.21 ? 30   THR   B C     1 
ATOM   9162  O  O     . THR   B  1  32   ? -5.412  0.167   88.683  1.00 23.38 ? 30   THR   B O     1 
ATOM   9163  C  CB    . THR   B  1  32   ? -5.343  -3.157  88.215  1.00 26.43 ? 30   THR   B CB    1 
ATOM   9164  O  OG1   . THR   B  1  32   ? -4.790  -4.040  87.234  1.00 30.15 ? 30   THR   B OG1   1 
ATOM   9165  C  CG2   . THR   B  1  32   ? -6.729  -2.674  87.770  1.00 31.51 ? 30   THR   B CG2   1 
ATOM   9166  N  N     . LEU   B  1  33   ? -5.128  -1.054  90.546  1.00 23.01 ? 31   LEU   B N     1 
ATOM   9167  C  CA    . LEU   B  1  33   ? -5.724  -0.018  91.387  1.00 24.52 ? 31   LEU   B CA    1 
ATOM   9168  C  C     . LEU   B  1  33   ? -4.888  1.257   91.403  1.00 21.87 ? 31   LEU   B C     1 
ATOM   9169  O  O     . LEU   B  1  33   ? -5.437  2.364   91.382  1.00 20.81 ? 31   LEU   B O     1 
ATOM   9170  C  CB    . LEU   B  1  33   ? -5.945  -0.553  92.799  1.00 21.96 ? 31   LEU   B CB    1 
ATOM   9171  C  CG    . LEU   B  1  33   ? -6.984  -1.668  92.782  1.00 27.20 ? 31   LEU   B CG    1 
ATOM   9172  C  CD1   . LEU   B  1  33   ? -7.059  -2.343  94.131  1.00 25.31 ? 31   LEU   B CD1   1 
ATOM   9173  C  CD2   . LEU   B  1  33   ? -8.343  -1.121  92.372  1.00 27.59 ? 31   LEU   B CD2   1 
ATOM   9174  N  N     . ARG   B  1  34   ? -3.557  1.132   91.460  1.00 19.89 ? 32   ARG   B N     1 
ATOM   9175  C  CA    . ARG   B  1  34   ? -2.728  2.330   91.435  1.00 20.51 ? 32   ARG   B CA    1 
ATOM   9176  C  C     . ARG   B  1  34   ? -2.864  3.049   90.102  1.00 18.80 ? 32   ARG   B C     1 
ATOM   9177  O  O     . ARG   B  1  34   ? -2.900  4.285   90.054  1.00 18.76 ? 32   ARG   B O     1 
ATOM   9178  C  CB    . ARG   B  1  34   ? -1.267  1.980   91.711  1.00 20.43 ? 32   ARG   B CB    1 
ATOM   9179  C  CG    . ARG   B  1  34   ? -0.982  1.539   93.131  1.00 21.51 ? 32   ARG   B CG    1 
ATOM   9180  C  CD    . ARG   B  1  34   ? -1.041  2.712   94.109  1.00 22.25 ? 32   ARG   B CD    1 
ATOM   9181  N  NE    . ARG   B  1  34   ? -0.023  3.715   93.820  1.00 22.75 ? 32   ARG   B NE    1 
ATOM   9182  C  CZ    . ARG   B  1  34   ? 1.180   3.741   94.379  1.00 23.47 ? 32   ARG   B CZ    1 
ATOM   9183  N  NH1   . ARG   B  1  34   ? 1.546   2.835   95.276  1.00 23.50 ? 32   ARG   B NH1   1 
ATOM   9184  N  NH2   . ARG   B  1  34   ? 2.031   4.703   94.039  1.00 21.81 ? 32   ARG   B NH2   1 
ATOM   9185  N  N     . ARG   B  1  35   ? -2.949  2.291   89.007  1.00 21.45 ? 33   ARG   B N     1 
ATOM   9186  C  CA    . ARG   B  1  35   ? -3.094  2.914   87.699  1.00 20.37 ? 33   ARG   B CA    1 
ATOM   9187  C  C     . ARG   B  1  35   ? -4.419  3.646   87.577  1.00 19.56 ? 33   ARG   B C     1 
ATOM   9188  O  O     . ARG   B  1  35   ? -4.486  4.688   86.920  1.00 20.20 ? 33   ARG   B O     1 
ATOM   9189  C  CB    . ARG   B  1  35   ? -2.968  1.858   86.601  1.00 22.65 ? 33   ARG   B CB    1 
ATOM   9190  C  CG    . ARG   B  1  35   ? -1.542  1.362   86.425  1.00 25.00 ? 33   ARG   B CG    1 
ATOM   9191  C  CD    . ARG   B  1  35   ? -1.430  0.320   85.318  1.00 30.65 ? 33   ARG   B CD    1 
ATOM   9192  N  NE    . ARG   B  1  35   ? -0.081  -0.230  85.277  1.00 37.66 ? 33   ARG   B NE    1 
ATOM   9193  C  CZ    . ARG   B  1  35   ? 0.953   0.368   84.700  1.00 41.02 ? 33   ARG   B CZ    1 
ATOM   9194  N  NH1   . ARG   B  1  35   ? 0.814   1.513   84.050  1.00 45.85 ? 33   ARG   B NH1   1 
ATOM   9195  N  NH2   . ARG   B  1  35   ? 2.159   -0.188  84.787  1.00 37.72 ? 33   ARG   B NH2   1 
ATOM   9196  N  N     . ALA   B  1  36   ? -5.476  3.122   88.199  1.00 20.02 ? 34   ALA   B N     1 
ATOM   9197  C  CA    . ALA   B  1  36   ? -6.763  3.803   88.139  1.00 21.63 ? 34   ALA   B CA    1 
ATOM   9198  C  C     . ALA   B  1  36   ? -6.715  5.124   88.888  1.00 19.81 ? 34   ALA   B C     1 
ATOM   9199  O  O     . ALA   B  1  36   ? -7.380  6.086   88.497  1.00 22.68 ? 34   ALA   B O     1 
ATOM   9200  C  CB    . ALA   B  1  36   ? -7.867  2.906   88.699  1.00 22.60 ? 34   ALA   B CB    1 
ATOM   9201  N  N     . ILE   B  1  37   ? -5.931  5.185   89.963  1.00 20.42 ? 35   ILE   B N     1 
ATOM   9202  C  CA    . ILE   B  1  37   ? -5.703  6.452   90.643  1.00 17.26 ? 35   ILE   B CA    1 
ATOM   9203  C  C     . ILE   B  1  37   ? -5.035  7.438   89.700  1.00 21.09 ? 35   ILE   B C     1 
ATOM   9204  O  O     . ILE   B  1  37   ? -5.525  8.550   89.479  1.00 18.75 ? 35   ILE   B O     1 
ATOM   9205  C  CB    . ILE   B  1  37   ? -4.856  6.223   91.906  1.00 17.67 ? 35   ILE   B CB    1 
ATOM   9206  C  CG1   . ILE   B  1  37   ? -5.663  5.425   92.936  1.00 17.85 ? 35   ILE   B CG1   1 
ATOM   9207  C  CG2   . ILE   B  1  37   ? -4.336  7.550   92.475  1.00 18.39 ? 35   ILE   B CG2   1 
ATOM   9208  C  CD1   . ILE   B  1  37   ? -4.803  4.831   94.049  1.00 19.95 ? 35   ILE   B CD1   1 
ATOM   9209  N  N     . THR   B  1  38   ? -3.889  7.040   89.135  1.00 18.06 ? 36   THR   B N     1 
ATOM   9210  C  CA    . THR   B  1  38   ? -3.144  7.942   88.266  1.00 18.89 ? 36   THR   B CA    1 
ATOM   9211  C  C     . THR   B  1  38   ? -3.989  8.402   87.087  1.00 19.62 ? 36   THR   B C     1 
ATOM   9212  O  O     . THR   B  1  38   ? -3.908  9.567   86.677  1.00 18.33 ? 36   THR   B O     1 
ATOM   9213  C  CB    . THR   B  1  38   ? -1.868  7.253   87.789  1.00 19.69 ? 36   THR   B CB    1 
ATOM   9214  O  OG1   . THR   B  1  38   ? -1.172  6.738   88.930  1.00 18.18 ? 36   THR   B OG1   1 
ATOM   9215  C  CG2   . THR   B  1  38   ? -0.971  8.230   87.030  1.00 23.28 ? 36   THR   B CG2   1 
ATOM   9216  N  N     . ALA   B  1  39   ? -4.812  7.503   86.541  1.00 19.08 ? 37   ALA   B N     1 
ATOM   9217  C  CA    . ALA   B  1  39   ? -5.632  7.849   85.385  1.00 21.79 ? 37   ALA   B CA    1 
ATOM   9218  C  C     . ALA   B  1  39   ? -6.611  8.973   85.703  1.00 21.06 ? 37   ALA   B C     1 
ATOM   9219  O  O     . ALA   B  1  39   ? -7.008  9.718   84.802  1.00 21.75 ? 37   ALA   B O     1 
ATOM   9220  C  CB    . ALA   B  1  39   ? -6.382  6.614   84.880  1.00 22.00 ? 37   ALA   B CB    1 
ATOM   9221  N  N     . ALA   B  1  40   ? -6.993  9.124   86.969  1.00 18.40 ? 38   ALA   B N     1 
ATOM   9222  C  CA    . ALA   B  1  40   ? -7.982  10.119  87.361  1.00 20.78 ? 38   ALA   B CA    1 
ATOM   9223  C  C     . ALA   B  1  40   ? -7.367  11.466  87.720  1.00 18.78 ? 38   ALA   B C     1 
ATOM   9224  O  O     . ALA   B  1  40   ? -8.112  12.416  87.982  1.00 18.59 ? 38   ALA   B O     1 
ATOM   9225  C  CB    . ALA   B  1  40   ? -8.816  9.593   88.539  1.00 19.30 ? 38   ALA   B CB    1 
ATOM   9226  N  N     . TYR   B  1  41   ? -6.031  11.565  87.728  1.00 18.79 ? 39   TYR   B N     1 
ATOM   9227  C  CA    . TYR   B  1  41   ? -5.336  12.690  88.349  1.00 17.47 ? 39   TYR   B CA    1 
ATOM   9228  C  C     . TYR   B  1  41   ? -5.916  14.028  87.900  1.00 18.63 ? 39   TYR   B C     1 
ATOM   9229  O  O     . TYR   B  1  41   ? -6.246  14.888  88.726  1.00 18.19 ? 39   TYR   B O     1 
ATOM   9230  C  CB    . TYR   B  1  41   ? -3.859  12.580  87.967  1.00 16.92 ? 39   TYR   B CB    1 
ATOM   9231  C  CG    . TYR   B  1  41   ? -2.859  13.276  88.852  1.00 19.34 ? 39   TYR   B CG    1 
ATOM   9232  C  CD1   . TYR   B  1  41   ? -3.185  14.413  89.583  1.00 18.35 ? 39   TYR   B CD1   1 
ATOM   9233  C  CD2   . TYR   B  1  41   ? -1.559  12.807  88.918  1.00 19.33 ? 39   TYR   B CD2   1 
ATOM   9234  C  CE1   . TYR   B  1  41   ? -2.233  15.046  90.374  1.00 18.15 ? 39   TYR   B CE1   1 
ATOM   9235  C  CE2   . TYR   B  1  41   ? -0.611  13.423  89.702  1.00 19.05 ? 39   TYR   B CE2   1 
ATOM   9236  C  CZ    . TYR   B  1  41   ? -0.945  14.545  90.420  1.00 19.24 ? 39   TYR   B CZ    1 
ATOM   9237  O  OH    . TYR   B  1  41   ? 0.014   15.148  91.196  1.00 19.78 ? 39   TYR   B OH    1 
ATOM   9238  N  N     . ARG   B  1  42   ? -6.062  14.216  86.587  1.00 19.63 ? 40   ARG   B N     1 
ATOM   9239  C  CA    . ARG   B  1  42   ? -6.569  15.476  86.058  1.00 18.95 ? 40   ARG   B CA    1 
ATOM   9240  C  C     . ARG   B  1  42   ? -7.770  15.264  85.153  1.00 19.10 ? 40   ARG   B C     1 
ATOM   9241  O  O     . ARG   B  1  42   ? -7.961  16.002  84.186  1.00 22.09 ? 40   ARG   B O     1 
ATOM   9242  C  CB    . ARG   B  1  42   ? -5.465  16.283  85.381  1.00 20.11 ? 40   ARG   B CB    1 
ATOM   9243  C  CG    . ARG   B  1  42   ? -4.390  16.651  86.392  1.00 21.83 ? 40   ARG   B CG    1 
ATOM   9244  C  CD    . ARG   B  1  42   ? -3.179  17.275  85.785  1.00 19.35 ? 40   ARG   B CD    1 
ATOM   9245  N  NE    . ARG   B  1  42   ? -2.096  17.216  86.755  1.00 19.01 ? 40   ARG   B NE    1 
ATOM   9246  C  CZ    . ARG   B  1  42   ? -1.910  18.090  87.733  1.00 17.59 ? 40   ARG   B CZ    1 
ATOM   9247  N  NH1   . ARG   B  1  42   ? -2.676  19.165  87.863  1.00 18.82 ? 40   ARG   B NH1   1 
ATOM   9248  N  NH2   . ARG   B  1  42   ? -0.932  17.878  88.608  1.00 18.68 ? 40   ARG   B NH2   1 
ATOM   9249  N  N     . ARG   B  1  43   ? -8.594  14.278  85.482  1.00 18.75 ? 41   ARG   B N     1 
ATOM   9250  C  CA    . ARG   B  1  43   ? -9.752  13.954  84.664  1.00 19.44 ? 41   ARG   B CA    1 
ATOM   9251  C  C     . ARG   B  1  43   ? -10.690 15.158  84.581  1.00 21.49 ? 41   ARG   B C     1 
ATOM   9252  O  O     . ARG   B  1  43   ? -10.896 15.858  85.578  1.00 20.29 ? 41   ARG   B O     1 
ATOM   9253  C  CB    . ARG   B  1  43   ? -10.486 12.767  85.293  1.00 19.96 ? 41   ARG   B CB    1 
ATOM   9254  C  CG    . ARG   B  1  43   ? -11.727 12.306  84.551  1.00 18.83 ? 41   ARG   B CG    1 
ATOM   9255  C  CD    . ARG   B  1  43   ? -12.127 10.937  85.060  1.00 22.79 ? 41   ARG   B CD    1 
ATOM   9256  N  NE    . ARG   B  1  43   ? -11.136 9.938   84.683  1.00 23.59 ? 41   ARG   B NE    1 
ATOM   9257  C  CZ    . ARG   B  1  43   ? -10.882 8.834   85.373  1.00 27.38 ? 41   ARG   B CZ    1 
ATOM   9258  N  NH1   . ARG   B  1  43   ? -11.517 8.562   86.498  1.00 23.56 ? 41   ARG   B NH1   1 
ATOM   9259  N  NH2   . ARG   B  1  43   ? -9.968  7.981   84.921  1.00 24.02 ? 41   ARG   B NH2   1 
ATOM   9260  N  N     . PRO   B  1  44   ? -11.257 15.443  83.412  1.00 21.87 ? 42   PRO   B N     1 
ATOM   9261  C  CA    . PRO   B  1  44   ? -12.175 16.581  83.305  1.00 21.25 ? 42   PRO   B CA    1 
ATOM   9262  C  C     . PRO   B  1  44   ? -13.284 16.501  84.343  1.00 20.77 ? 42   PRO   B C     1 
ATOM   9263  O  O     . PRO   B  1  44   ? -13.799 15.427  84.664  1.00 19.74 ? 42   PRO   B O     1 
ATOM   9264  C  CB    . PRO   B  1  44   ? -12.721 16.453  81.879  1.00 23.21 ? 42   PRO   B CB    1 
ATOM   9265  C  CG    . PRO   B  1  44   ? -11.546 15.866  81.124  1.00 24.94 ? 42   PRO   B CG    1 
ATOM   9266  C  CD    . PRO   B  1  44   ? -10.928 14.873  82.093  1.00 23.80 ? 42   PRO   B CD    1 
ATOM   9267  N  N     . GLU   B  1  45   ? -13.636 17.664  84.885  1.00 19.72 ? 43   GLU   B N     1 
ATOM   9268  C  CA    . GLU   B  1  45   ? -14.643 17.715  85.932  1.00 20.88 ? 43   GLU   B CA    1 
ATOM   9269  C  C     . GLU   B  1  45   ? -15.980 17.151  85.461  1.00 22.98 ? 43   GLU   B C     1 
ATOM   9270  O  O     . GLU   B  1  45   ? -16.686 16.509  86.240  1.00 23.73 ? 43   GLU   B O     1 
ATOM   9271  C  CB    . GLU   B  1  45   ? -14.761 19.153  86.417  1.00 24.90 ? 43   GLU   B CB    1 
ATOM   9272  C  CG    . GLU   B  1  45   ? -14.981 19.259  87.884  1.00 29.10 ? 43   GLU   B CG    1 
ATOM   9273  C  CD    . GLU   B  1  45   ? -14.606 20.611  88.442  1.00 20.68 ? 43   GLU   B CD    1 
ATOM   9274  O  OE1   . GLU   B  1  45   ? -13.851 21.375  87.800  1.00 21.77 ? 43   GLU   B OE1   1 
ATOM   9275  O  OE2   . GLU   B  1  45   ? -15.086 20.897  89.540  1.00 22.05 ? 43   GLU   B OE2   1 
ATOM   9276  N  N     . THR   B  1  46   ? -16.332 17.349  84.187  1.00 21.67 ? 44   THR   B N     1 
ATOM   9277  C  CA    . THR   B  1  46   ? -17.578 16.797  83.668  1.00 22.27 ? 44   THR   B CA    1 
ATOM   9278  C  C     . THR   B  1  46   ? -17.548 15.279  83.587  1.00 21.58 ? 44   THR   B C     1 
ATOM   9279  O  O     . THR   B  1  46   ? -18.608 14.654  83.509  1.00 25.32 ? 44   THR   B O     1 
ATOM   9280  C  CB    . THR   B  1  46   ? -17.862 17.367  82.282  1.00 23.13 ? 44   THR   B CB    1 
ATOM   9281  O  OG1   . THR   B  1  46   ? -16.716 17.157  81.439  1.00 24.28 ? 44   THR   B OG1   1 
ATOM   9282  C  CG2   . THR   B  1  46   ? -18.159 18.856  82.374  1.00 24.49 ? 44   THR   B CG2   1 
ATOM   9283  N  N     . GLU   B  1  47   ? -16.364 14.674  83.579  1.00 23.40 ? 45   GLU   B N     1 
ATOM   9284  C  CA    . GLU   B  1  47   ? -16.277 13.221  83.638  1.00 23.29 ? 45   GLU   B CA    1 
ATOM   9285  C  C     . GLU   B  1  47   ? -16.274 12.698  85.068  1.00 21.56 ? 45   GLU   B C     1 
ATOM   9286  O  O     . GLU   B  1  47   ? -16.786 11.601  85.323  1.00 24.53 ? 45   GLU   B O     1 
ATOM   9287  C  CB    . GLU   B  1  47   ? -15.029 12.733  82.894  1.00 23.10 ? 45   GLU   B CB    1 
ATOM   9288  C  CG    . GLU   B  1  47   ? -15.031 13.042  81.402  1.00 28.25 ? 45   GLU   B CG    1 
ATOM   9289  C  CD    . GLU   B  1  47   ? -13.730 12.641  80.733  1.00 33.24 ? 45   GLU   B CD    1 
ATOM   9290  O  OE1   . GLU   B  1  47   ? -13.056 11.718  81.247  1.00 35.68 ? 45   GLU   B OE1   1 
ATOM   9291  O  OE2   . GLU   B  1  47   ? -13.379 13.255  79.705  1.00 37.39 ? 45   GLU   B OE2   1 
ATOM   9292  N  N     . CYS   B  1  48   ? -15.734 13.472  86.012  1.00 20.68 ? 46   CYS   B N     1 
ATOM   9293  C  CA    . CYS   B  1  48   ? -15.670 13.013  87.394  1.00 22.05 ? 46   CYS   B CA    1 
ATOM   9294  C  C     . CYS   B  1  48   ? -17.041 13.017  88.044  1.00 22.91 ? 46   CYS   B C     1 
ATOM   9295  O  O     . CYS   B  1  48   ? -17.355 12.130  88.843  1.00 21.64 ? 46   CYS   B O     1 
ATOM   9296  C  CB    . CYS   B  1  48   ? -14.747 13.916  88.204  1.00 20.73 ? 46   CYS   B CB    1 
ATOM   9297  S  SG    . CYS   B  1  48   ? -13.038 13.916  87.702  1.00 22.22 ? 46   CYS   B SG    1 
ATOM   9298  N  N     . LEU   B  1  49   ? -17.856 14.012  87.737  1.00 21.70 ? 47   LEU   B N     1 
ATOM   9299  C  CA    . LEU   B  1  49   ? -19.054 14.237  88.543  1.00 22.02 ? 47   LEU   B CA    1 
ATOM   9300  C  C     . LEU   B  1  49   ? -20.158 13.189  88.406  1.00 21.96 ? 47   LEU   B C     1 
ATOM   9301  O  O     . LEU   B  1  49   ? -20.723 12.783  89.425  1.00 22.13 ? 47   LEU   B O     1 
ATOM   9302  C  CB    . LEU   B  1  49   ? -19.579 15.671  88.404  1.00 21.47 ? 47   LEU   B CB    1 
ATOM   9303  C  CG    . LEU   B  1  49   ? -19.088 16.611  89.516  1.00 21.32 ? 47   LEU   B CG    1 
ATOM   9304  C  CD1   . LEU   B  1  49   ? -19.609 16.133  90.875  1.00 22.36 ? 47   LEU   B CD1   1 
ATOM   9305  C  CD2   . LEU   B  1  49   ? -17.569 16.688  89.533  1.00 22.27 ? 47   LEU   B CD2   1 
ATOM   9306  N  N     . PRO   B  1  50   ? -20.510 12.725  87.206  1.00 24.00 ? 48   PRO   B N     1 
ATOM   9307  C  CA    . PRO   B  1  50   ? -21.674 11.827  87.082  1.00 25.29 ? 48   PRO   B CA    1 
ATOM   9308  C  C     . PRO   B  1  50   ? -21.558 10.574  87.940  1.00 25.70 ? 48   PRO   B C     1 
ATOM   9309  O  O     . PRO   B  1  50   ? -22.524 10.223  88.629  1.00 27.11 ? 48   PRO   B O     1 
ATOM   9310  C  CB    . PRO   B  1  50   ? -21.721 11.506  85.579  1.00 24.37 ? 48   PRO   B CB    1 
ATOM   9311  C  CG    . PRO   B  1  50   ? -21.172 12.721  84.953  1.00 24.82 ? 48   PRO   B CG    1 
ATOM   9312  C  CD    . PRO   B  1  50   ? -20.074 13.206  85.885  1.00 24.41 ? 48   PRO   B CD    1 
ATOM   9313  N  N     . PRO   B  1  51   ? -20.415 9.873   87.971  1.00 25.38 ? 49   PRO   B N     1 
ATOM   9314  C  CA    . PRO   B  1  51   ? -20.352 8.715   88.881  1.00 25.21 ? 49   PRO   B CA    1 
ATOM   9315  C  C     . PRO   B  1  51   ? -20.437 9.093   90.350  1.00 24.50 ? 49   PRO   B C     1 
ATOM   9316  O  O     . PRO   B  1  51   ? -20.973 8.312   91.148  1.00 25.35 ? 49   PRO   B O     1 
ATOM   9317  C  CB    . PRO   B  1  51   ? -19.016 8.044   88.538  1.00 26.95 ? 49   PRO   B CB    1 
ATOM   9318  C  CG    . PRO   B  1  51   ? -18.212 9.103   87.874  1.00 28.04 ? 49   PRO   B CG    1 
ATOM   9319  C  CD    . PRO   B  1  51   ? -19.206 9.940   87.122  1.00 24.78 ? 49   PRO   B CD    1 
ATOM   9320  N  N     . LEU   B  1  52   ? -19.939 10.271  90.729  1.00 25.24 ? 50   LEU   B N     1 
ATOM   9321  C  CA    . LEU   B  1  52   ? -20.051 10.700  92.121  1.00 21.04 ? 50   LEU   B CA    1 
ATOM   9322  C  C     . LEU   B  1  52   ? -21.497 11.024  92.476  1.00 25.57 ? 50   LEU   B C     1 
ATOM   9323  O  O     . LEU   B  1  52   ? -21.976 10.650  93.551  1.00 23.88 ? 50   LEU   B O     1 
ATOM   9324  C  CB    . LEU   B  1  52   ? -19.156 11.913  92.372  1.00 21.33 ? 50   LEU   B CB    1 
ATOM   9325  C  CG    . LEU   B  1  52   ? -17.668 11.706  92.112  1.00 22.03 ? 50   LEU   B CG    1 
ATOM   9326  C  CD1   . LEU   B  1  52   ? -16.946 13.042  92.190  1.00 21.31 ? 50   LEU   B CD1   1 
ATOM   9327  C  CD2   . LEU   B  1  52   ? -17.092 10.714  93.101  1.00 24.57 ? 50   LEU   B CD2   1 
ATOM   9328  N  N     . VAL   B  1  53   ? -22.203 11.724  91.583  1.00 22.38 ? 51   VAL   B N     1 
ATOM   9329  C  CA    . VAL   B  1  53   ? -23.629 11.982  91.792  1.00 22.38 ? 51   VAL   B CA    1 
ATOM   9330  C  C     . VAL   B  1  53   ? -24.375 10.673  92.005  1.00 29.12 ? 51   VAL   B C     1 
ATOM   9331  O  O     . VAL   B  1  53   ? -25.180 10.535  92.936  1.00 26.39 ? 51   VAL   B O     1 
ATOM   9332  C  CB    . VAL   B  1  53   ? -24.208 12.775  90.605  1.00 24.28 ? 51   VAL   B CB    1 
ATOM   9333  C  CG1   . VAL   B  1  53   ? -25.742 12.748  90.638  1.00 28.38 ? 51   VAL   B CG1   1 
ATOM   9334  C  CG2   . VAL   B  1  53   ? -23.707 14.203  90.619  1.00 24.01 ? 51   VAL   B CG2   1 
ATOM   9335  N  N     . GLU   B  1  54   ? -24.107 9.684   91.148  1.00 25.56 ? 52   GLU   B N     1 
ATOM   9336  C  CA    . GLU   B  1  54   ? -24.773 8.393   91.283  1.00 28.28 ? 52   GLU   B CA    1 
ATOM   9337  C  C     . GLU   B  1  54   ? -24.467 7.749   92.627  1.00 30.25 ? 52   GLU   B C     1 
ATOM   9338  O  O     . GLU   B  1  54   ? -25.375 7.252   93.306  1.00 29.92 ? 52   GLU   B O     1 
ATOM   9339  C  CB    . GLU   B  1  54   ? -24.370 7.472   90.131  1.00 29.04 ? 52   GLU   B CB    1 
ATOM   9340  N  N     . ALA   B  1  55   ? -23.192 7.762   93.039  1.00 27.17 ? 53   ALA   B N     1 
ATOM   9341  C  CA    . ALA   B  1  55   ? -22.810 7.135   94.302  1.00 27.43 ? 53   ALA   B CA    1 
ATOM   9342  C  C     . ALA   B  1  55   ? -23.360 7.891   95.507  1.00 26.75 ? 53   ALA   B C     1 
ATOM   9343  O  O     . ALA   B  1  55   ? -23.631 7.281   96.546  1.00 30.29 ? 53   ALA   B O     1 
ATOM   9344  C  CB    . ALA   B  1  55   ? -21.286 7.035   94.394  1.00 28.94 ? 53   ALA   B CB    1 
ATOM   9345  N  N     . ALA   B  1  56   ? -23.517 9.208   95.396  1.00 27.23 ? 54   ALA   B N     1 
ATOM   9346  C  CA    . ALA   B  1  56   ? -24.005 10.032  96.496  1.00 26.08 ? 54   ALA   B CA    1 
ATOM   9347  C  C     . ALA   B  1  56   ? -25.526 10.083  96.582  1.00 28.39 ? 54   ALA   B C     1 
ATOM   9348  O  O     . ALA   B  1  56   ? -26.059 10.705  97.507  1.00 31.37 ? 54   ALA   B O     1 
ATOM   9349  C  CB    . ALA   B  1  56   ? -23.458 11.453  96.367  1.00 27.50 ? 54   ALA   B CB    1 
ATOM   9350  N  N     . THR   B  1  57   ? -26.236 9.450   95.653  1.00 27.72 ? 55   THR   B N     1 
ATOM   9351  C  CA    . THR   B  1  57   ? -27.687 9.564   95.629  1.00 31.81 ? 55   THR   B CA    1 
ATOM   9352  C  C     . THR   B  1  57   ? -28.311 8.814   96.800  1.00 32.74 ? 55   THR   B C     1 
ATOM   9353  O  O     . THR   B  1  57   ? -27.909 7.695   97.127  1.00 33.74 ? 55   THR   B O     1 
ATOM   9354  C  CB    . THR   B  1  57   ? -28.219 9.023   94.304  1.00 32.13 ? 55   THR   B CB    1 
ATOM   9355  O  OG1   . THR   B  1  57   ? -27.827 9.908   93.251  1.00 32.38 ? 55   THR   B OG1   1 
ATOM   9356  C  CG2   . THR   B  1  57   ? -29.740 8.918   94.334  1.00 32.62 ? 55   THR   B CG2   1 
ATOM   9357  N  N     . GLN   B  1  58   ? -29.292 9.448   97.442  1.00 37.65 ? 56   GLN   B N     1 
ATOM   9358  C  CA    . GLN   B  1  58   ? -30.042 8.832   98.526  1.00 32.85 ? 56   GLN   B CA    1 
ATOM   9359  C  C     . GLN   B  1  58   ? -31.536 9.003   98.263  1.00 34.56 ? 56   GLN   B C     1 
ATOM   9360  O  O     . GLN   B  1  58   ? -31.958 9.876   97.499  1.00 35.36 ? 56   GLN   B O     1 
ATOM   9361  C  CB    . GLN   B  1  58   ? -29.666 9.424   99.896  1.00 36.70 ? 56   GLN   B CB    1 
ATOM   9362  C  CG    . GLN   B  1  58   ? -28.164 9.593   100.124 1.00 35.26 ? 56   GLN   B CG    1 
ATOM   9363  C  CD    . GLN   B  1  58   ? -27.795 9.592   101.598 1.00 38.91 ? 56   GLN   B CD    1 
ATOM   9364  O  OE1   . GLN   B  1  58   ? -28.042 8.615   102.304 1.00 41.42 ? 56   GLN   B OE1   1 
ATOM   9365  N  NE2   . GLN   B  1  58   ? -27.209 10.687  102.069 1.00 39.14 ? 56   GLN   B NE2   1 
ATOM   9366  N  N     . SER   B  1  59   ? -32.332 8.157   98.913  1.00 39.10 ? 57   SER   B N     1 
ATOM   9367  C  CA    . SER   B  1  59   ? -33.776 8.173   98.729  1.00 39.68 ? 57   SER   B CA    1 
ATOM   9368  C  C     . SER   B  1  59   ? -34.369 9.478   99.249  1.00 38.94 ? 57   SER   B C     1 
ATOM   9369  O  O     . SER   B  1  59   ? -33.746 10.218  100.014 1.00 39.15 ? 57   SER   B O     1 
ATOM   9370  C  CB    . SER   B  1  59   ? -34.410 7.030   99.513  1.00 43.24 ? 57   SER   B CB    1 
ATOM   9371  O  OG    . SER   B  1  59   ? -34.207 7.225   100.903 1.00 41.93 ? 57   SER   B OG    1 
ATOM   9372  N  N     . LYS   B  1  60   ? -35.603 9.756   98.824  1.00 38.80 ? 58   LYS   B N     1 
ATOM   9373  C  CA    . LYS   B  1  60   ? -36.307 10.928  99.334  1.00 42.20 ? 58   LYS   B CA    1 
ATOM   9374  C  C     . LYS   B  1  60   ? -36.427 10.872  100.850 1.00 38.36 ? 58   LYS   B C     1 
ATOM   9375  O  O     . LYS   B  1  60   ? -36.294 11.898  101.528 1.00 41.05 ? 58   LYS   B O     1 
ATOM   9376  C  CB    . LYS   B  1  60   ? -37.694 11.037  98.694  1.00 37.62 ? 58   LYS   B CB    1 
ATOM   9377  N  N     . GLU   B  1  61   ? -36.673 9.679   101.400 1.00 38.86 ? 59   GLU   B N     1 
ATOM   9378  C  CA    . GLU   B  1  61   ? -36.834 9.541   102.845 1.00 37.71 ? 59   GLU   B CA    1 
ATOM   9379  C  C     . GLU   B  1  61   ? -35.568 9.965   103.578 1.00 39.74 ? 59   GLU   B C     1 
ATOM   9380  O  O     . GLU   B  1  61   ? -35.613 10.800  104.490 1.00 39.75 ? 59   GLU   B O     1 
ATOM   9381  C  CB    . GLU   B  1  61   ? -37.206 8.099   103.199 1.00 42.08 ? 59   GLU   B CB    1 
ATOM   9382  N  N     . ILE   B  1  62   ? -34.422 9.407   103.183 1.00 40.33 ? 60   ILE   B N     1 
ATOM   9383  C  CA    . ILE   B  1  62   ? -33.161 9.769   103.828 1.00 38.55 ? 60   ILE   B CA    1 
ATOM   9384  C  C     . ILE   B  1  62   ? -32.837 11.242  103.594 1.00 37.36 ? 60   ILE   B C     1 
ATOM   9385  O  O     . ILE   B  1  62   ? -32.342 11.932  104.494 1.00 39.44 ? 60   ILE   B O     1 
ATOM   9386  C  CB    . ILE   B  1  62   ? -32.030 8.832   103.365 1.00 39.26 ? 60   ILE   B CB    1 
ATOM   9387  N  N     . ARG   B  1  63   ? -33.124 11.752  102.392 1.00 36.57 ? 61   ARG   B N     1 
ATOM   9388  C  CA    . ARG   B  1  63   ? -32.824 13.149  102.092 1.00 35.63 ? 61   ARG   B CA    1 
ATOM   9389  C  C     . ARG   B  1  63   ? -33.649 14.103  102.946 1.00 40.22 ? 61   ARG   B C     1 
ATOM   9390  O  O     . ARG   B  1  63   ? -33.117 15.087  103.470 1.00 38.81 ? 61   ARG   B O     1 
ATOM   9391  C  CB    . ARG   B  1  63   ? -33.007 13.435  100.602 1.00 39.31 ? 61   ARG   B CB    1 
ATOM   9392  C  CG    . ARG   B  1  63   ? -31.878 12.881  99.759  1.00 39.51 ? 61   ARG   B CG    1 
ATOM   9393  C  CD    . ARG   B  1  63   ? -31.972 13.313  98.310  1.00 42.23 ? 61   ARG   B CD    1 
ATOM   9394  N  NE    . ARG   B  1  63   ? -33.019 12.609  97.579  1.00 40.21 ? 61   ARG   B NE    1 
ATOM   9395  C  CZ    . ARG   B  1  63   ? -34.071 13.197  97.025  1.00 43.30 ? 61   ARG   B CZ    1 
ATOM   9396  N  NH1   . ARG   B  1  63   ? -34.277 14.499  97.144  1.00 46.18 ? 61   ARG   B NH1   1 
ATOM   9397  N  NH2   . ARG   B  1  63   ? -34.928 12.464  96.321  1.00 40.95 ? 61   ARG   B NH2   1 
ATOM   9398  N  N     . ASP   B  1  64   ? -34.953 13.841  103.083 1.00 35.57 ? 62   ASP   B N     1 
ATOM   9399  C  CA    . ASP   B  1  64   ? -35.770 14.661  103.972 1.00 38.39 ? 62   ASP   B CA    1 
ATOM   9400  C  C     . ASP   B  1  64   ? -35.261 14.582  105.404 1.00 32.13 ? 62   ASP   B C     1 
ATOM   9401  O  O     . ASP   B  1  64   ? -35.147 15.606  106.087 1.00 39.93 ? 62   ASP   B O     1 
ATOM   9402  C  CB    . ASP   B  1  64   ? -37.233 14.224  103.908 1.00 36.86 ? 62   ASP   B CB    1 
ATOM   9403  C  CG    . ASP   B  1  64   ? -37.868 14.495  102.556 1.00 47.65 ? 62   ASP   B CG    1 
ATOM   9404  O  OD1   . ASP   B  1  64   ? -37.216 15.132  101.702 1.00 45.21 ? 62   ASP   B OD1   1 
ATOM   9405  O  OD2   . ASP   B  1  64   ? -39.026 14.067  102.349 1.00 46.91 ? 62   ASP   B OD2   1 
ATOM   9406  N  N     . ALA   B  1  65   ? -34.949 13.373  105.874 1.00 33.43 ? 63   ALA   B N     1 
ATOM   9407  C  CA    . ALA   B  1  65   ? -34.464 13.208  107.240 1.00 33.83 ? 63   ALA   B CA    1 
ATOM   9408  C  C     . ALA   B  1  65   ? -33.157 13.959  107.457 1.00 38.31 ? 63   ALA   B C     1 
ATOM   9409  O  O     . ALA   B  1  65   ? -32.953 14.575  108.510 1.00 38.11 ? 63   ALA   B O     1 
ATOM   9410  C  CB    . ALA   B  1  65   ? -34.297 11.722  107.561 1.00 35.40 ? 63   ALA   B CB    1 
ATOM   9411  N  N     . ALA   B  1  66   ? -32.265 13.930  106.465 1.00 38.03 ? 64   ALA   B N     1 
ATOM   9412  C  CA    . ALA   B  1  66   ? -30.995 14.637  106.596 1.00 34.68 ? 64   ALA   B CA    1 
ATOM   9413  C  C     . ALA   B  1  66   ? -31.200 16.145  106.600 1.00 32.63 ? 64   ALA   B C     1 
ATOM   9414  O  O     . ALA   B  1  66   ? -30.535 16.866  107.351 1.00 35.60 ? 64   ALA   B O     1 
ATOM   9415  C  CB    . ALA   B  1  66   ? -30.045 14.215  105.478 1.00 33.96 ? 64   ALA   B CB    1 
ATOM   9416  N  N     . ALA   B  1  67   ? -32.127 16.642  105.783 1.00 34.34 ? 65   ALA   B N     1 
ATOM   9417  C  CA    . ALA   B  1  67   ? -32.406 18.073  105.788 1.00 35.44 ? 65   ALA   B CA    1 
ATOM   9418  C  C     . ALA   B  1  67   ? -32.968 18.521  107.132 1.00 38.17 ? 65   ALA   B C     1 
ATOM   9419  O  O     . ALA   B  1  67   ? -32.672 19.632  107.587 1.00 37.21 ? 65   ALA   B O     1 
ATOM   9420  C  CB    . ALA   B  1  67   ? -33.373 18.424  104.658 1.00 35.90 ? 65   ALA   B CB    1 
ATOM   9421  N  N     . SER   B  1  68   ? -33.772 17.670  107.778 1.00 37.59 ? 66   SER   B N     1 
ATOM   9422  C  CA    . SER   B  1  68   ? -34.289 17.986  109.108 1.00 34.81 ? 66   SER   B CA    1 
ATOM   9423  C  C     . SER   B  1  68   ? -33.182 17.943  110.156 1.00 38.96 ? 66   SER   B C     1 
ATOM   9424  O  O     . SER   B  1  68   ? -33.127 18.801  111.047 1.00 39.54 ? 66   SER   B O     1 
ATOM   9425  C  CB    . SER   B  1  68   ? -35.417 17.021  109.479 1.00 41.70 ? 66   SER   B CB    1 
ATOM   9426  N  N     . THR   B  1  69   ? -32.297 16.947  110.076 1.00 36.49 ? 67   THR   B N     1 
ATOM   9427  C  CA    . THR   B  1  69   ? -31.179 16.886  111.012 1.00 34.13 ? 67   THR   B CA    1 
ATOM   9428  C  C     . THR   B  1  69   ? -30.246 18.077  110.832 1.00 37.57 ? 67   THR   B C     1 
ATOM   9429  O  O     . THR   B  1  69   ? -29.794 18.676  111.818 1.00 33.92 ? 67   THR   B O     1 
ATOM   9430  C  CB    . THR   B  1  69   ? -30.409 15.580  110.830 1.00 39.45 ? 67   THR   B CB    1 
ATOM   9431  O  OG1   . THR   B  1  69   ? -31.230 14.478  111.227 1.00 39.04 ? 67   THR   B OG1   1 
ATOM   9432  C  CG2   . THR   B  1  69   ? -29.136 15.586  111.673 1.00 35.13 ? 67   THR   B CG2   1 
ATOM   9433  N  N     . ALA   B  1  70   ? -29.932 18.423  109.579 1.00 33.38 ? 68   ALA   B N     1 
ATOM   9434  C  CA    . ALA   B  1  70   ? -29.076 19.574  109.319 1.00 34.45 ? 68   ALA   B CA    1 
ATOM   9435  C  C     . ALA   B  1  70   ? -29.709 20.860  109.832 1.00 36.79 ? 68   ALA   B C     1 
ATOM   9436  O  O     . ALA   B  1  70   ? -29.013 21.731  110.367 1.00 33.54 ? 68   ALA   B O     1 
ATOM   9437  C  CB    . ALA   B  1  70   ? -28.770 19.678  107.823 1.00 32.97 ? 68   ALA   B CB    1 
ATOM   9438  N  N     . ARG   B  1  71   ? -31.029 20.998  109.674 1.00 36.83 ? 69   ARG   B N     1 
ATOM   9439  C  CA    . ARG   B  1  71   ? -31.711 22.174  110.200 1.00 40.15 ? 69   ARG   B CA    1 
ATOM   9440  C  C     . ARG   B  1  71   ? -31.593 22.239  111.715 1.00 31.64 ? 69   ARG   B C     1 
ATOM   9441  O  O     . ARG   B  1  71   ? -31.308 23.301  112.278 1.00 36.35 ? 69   ARG   B O     1 
ATOM   9442  C  CB    . ARG   B  1  71   ? -33.182 22.165  109.782 1.00 40.65 ? 69   ARG   B CB    1 
ATOM   9443  C  CG    . ARG   B  1  71   ? -33.972 23.325  110.366 1.00 41.06 ? 69   ARG   B CG    1 
ATOM   9444  C  CD    . ARG   B  1  71   ? -35.402 23.353  109.859 1.00 48.79 ? 69   ARG   B CD    1 
ATOM   9445  N  NE    . ARG   B  1  71   ? -35.495 23.635  108.431 1.00 47.24 ? 69   ARG   B NE    1 
ATOM   9446  C  CZ    . ARG   B  1  71   ? -35.412 24.847  107.898 1.00 49.99 ? 69   ARG   B CZ    1 
ATOM   9447  N  NH1   . ARG   B  1  71   ? -35.156 25.914  108.640 1.00 53.23 ? 69   ARG   B NH1   1 
ATOM   9448  N  NH2   . ARG   B  1  71   ? -35.592 24.991  106.588 1.00 54.92 ? 69   ARG   B NH2   1 
ATOM   9449  N  N     . LYS   B  1  72   ? -31.780 21.101  112.385 1.00 35.17 ? 70   LYS   B N     1 
ATOM   9450  C  CA    . LYS   B  1  72   ? -31.671 21.056  113.839 1.00 36.67 ? 70   LYS   B CA    1 
ATOM   9451  C  C     . LYS   B  1  72   ? -30.269 21.444  114.299 1.00 37.86 ? 70   LYS   B C     1 
ATOM   9452  O  O     . LYS   B  1  72   ? -30.104 22.097  115.335 1.00 37.99 ? 70   LYS   B O     1 
ATOM   9453  C  CB    . LYS   B  1  72   ? -32.043 19.656  114.330 1.00 34.56 ? 70   LYS   B CB    1 
ATOM   9454  C  CG    . LYS   B  1  72   ? -31.935 19.450  115.833 1.00 39.42 ? 70   LYS   B CG    1 
ATOM   9455  C  CD    . LYS   B  1  72   ? -32.413 18.050  116.222 1.00 36.89 ? 70   LYS   B CD    1 
ATOM   9456  C  CE    . LYS   B  1  72   ? -32.208 17.769  117.703 1.00 41.59 ? 70   LYS   B CE    1 
ATOM   9457  N  NZ    . LYS   B  1  72   ? -33.082 18.606  118.563 1.00 38.13 ? 70   LYS   B NZ    1 
ATOM   9458  N  N     . LEU   B  1  73   ? -29.243 21.063  113.533 1.00 36.01 ? 71   LEU   B N     1 
ATOM   9459  C  CA    . LEU   B  1  73   ? -27.877 21.404  113.918 1.00 34.78 ? 71   LEU   B CA    1 
ATOM   9460  C  C     . LEU   B  1  73   ? -27.589 22.883  113.701 1.00 32.94 ? 71   LEU   B C     1 
ATOM   9461  O  O     . LEU   B  1  73   ? -26.921 23.518  114.525 1.00 36.93 ? 71   LEU   B O     1 
ATOM   9462  C  CB    . LEU   B  1  73   ? -26.888 20.550  113.125 1.00 32.00 ? 71   LEU   B CB    1 
ATOM   9463  C  CG    . LEU   B  1  73   ? -26.972 19.048  113.379 1.00 31.23 ? 71   LEU   B CG    1 
ATOM   9464  C  CD1   . LEU   B  1  73   ? -26.171 18.277  112.322 1.00 30.54 ? 71   LEU   B CD1   1 
ATOM   9465  C  CD2   . LEU   B  1  73   ? -26.484 18.727  114.783 1.00 35.13 ? 71   LEU   B CD2   1 
ATOM   9466  N  N     . ILE   B  1  74   ? -28.078 23.445  112.595 1.00 33.04 ? 72   ILE   B N     1 
ATOM   9467  C  CA    . ILE   B  1  74   ? -27.750 24.822  112.241 1.00 36.16 ? 72   ILE   B CA    1 
ATOM   9468  C  C     . ILE   B  1  74   ? -28.464 25.804  113.164 1.00 38.89 ? 72   ILE   B C     1 
ATOM   9469  O  O     . ILE   B  1  74   ? -27.866 26.770  113.654 1.00 36.86 ? 72   ILE   B O     1 
ATOM   9470  C  CB    . ILE   B  1  74   ? -28.062 25.078  110.757 1.00 36.29 ? 72   ILE   B CB    1 
ATOM   9471  C  CG1   . ILE   B  1  74   ? -27.061 24.314  109.882 1.00 34.23 ? 72   ILE   B CG1   1 
ATOM   9472  C  CG2   . ILE   B  1  74   ? -28.006 26.562  110.446 1.00 36.37 ? 72   ILE   B CG2   1 
ATOM   9473  C  CD1   . ILE   B  1  74   ? -27.583 23.996  108.510 1.00 37.37 ? 72   ILE   B CD1   1 
ATOM   9474  N  N     . GLU   B  1  75   ? -29.757 25.580  113.400 1.00 38.46 ? 73   GLU   B N     1 
ATOM   9475  C  CA    . GLU   B  1  75   ? -30.479 26.397  114.372 1.00 40.59 ? 73   GLU   B CA    1 
ATOM   9476  C  C     . GLU   B  1  75   ? -29.789 26.368  115.732 1.00 42.65 ? 73   GLU   B C     1 
ATOM   9477  O  O     . GLU   B  1  75   ? -29.605 27.415  116.365 1.00 40.81 ? 73   GLU   B O     1 
ATOM   9478  C  CB    . GLU   B  1  75   ? -31.932 25.934  114.467 1.00 39.67 ? 73   GLU   B CB    1 
ATOM   9479  C  CG    . GLU   B  1  75   ? -32.701 26.103  113.161 1.00 42.39 ? 73   GLU   B CG    1 
ATOM   9480  C  CD    . GLU   B  1  75   ? -34.157 25.683  113.261 1.00 45.21 ? 73   GLU   B CD    1 
ATOM   9481  O  OE1   . GLU   B  1  75   ? -34.508 24.962  114.221 1.00 49.51 ? 73   GLU   B OE1   1 
ATOM   9482  O  OE2   . GLU   B  1  75   ? -34.948 26.074  112.375 1.00 45.60 ? 73   GLU   B OE2   1 
ATOM   9483  N  N     . ALA   B  1  76   ? -29.371 25.180  116.178 1.00 36.64 ? 74   ALA   B N     1 
ATOM   9484  C  CA    . ALA   B  1  76   ? -28.600 25.073  117.413 1.00 38.71 ? 74   ALA   B CA    1 
ATOM   9485  C  C     . ALA   B  1  76   ? -27.334 25.924  117.356 1.00 38.41 ? 74   ALA   B C     1 
ATOM   9486  O  O     . ALA   B  1  76   ? -27.012 26.639  118.311 1.00 40.72 ? 74   ALA   B O     1 
ATOM   9487  C  CB    . ALA   B  1  76   ? -28.265 23.609  117.696 1.00 37.26 ? 74   ALA   B CB    1 
ATOM   9488  N  N     . LEU   B  1  77   ? -26.603 25.866  116.238 1.00 37.99 ? 75   LEU   B N     1 
ATOM   9489  C  CA    . LEU   B  1  77   ? -25.375 26.647  116.116 1.00 38.20 ? 75   LEU   B CA    1 
ATOM   9490  C  C     . LEU   B  1  77   ? -25.668 28.143  116.129 1.00 38.80 ? 75   LEU   B C     1 
ATOM   9491  O  O     . LEU   B  1  77   ? -24.981 28.918  116.806 1.00 38.75 ? 75   LEU   B O     1 
ATOM   9492  C  CB    . LEU   B  1  77   ? -24.633 26.262  114.831 1.00 35.62 ? 75   LEU   B CB    1 
ATOM   9493  C  CG    . LEU   B  1  77   ? -23.941 24.900  114.795 1.00 38.82 ? 75   LEU   B CG    1 
ATOM   9494  C  CD1   . LEU   B  1  77   ? -23.474 24.557  113.385 1.00 33.93 ? 75   LEU   B CD1   1 
ATOM   9495  C  CD2   . LEU   B  1  77   ? -22.765 24.909  115.733 1.00 38.33 ? 75   LEU   B CD2   1 
ATOM   9496  N  N     . ARG   B  1  78   ? -26.675 28.571  115.368 1.00 34.65 ? 76   ARG   B N     1 
ATOM   9497  C  CA    . ARG   B  1  78   ? -26.983 29.991  115.255 1.00 38.10 ? 76   ARG   B CA    1 
ATOM   9498  C  C     . ARG   B  1  78   ? -27.646 30.549  116.502 1.00 41.18 ? 76   ARG   B C     1 
ATOM   9499  O  O     . ARG   B  1  78   ? -27.734 31.774  116.642 1.00 41.67 ? 76   ARG   B O     1 
ATOM   9500  C  CB    . ARG   B  1  78   ? -27.886 30.240  114.050 1.00 43.02 ? 76   ARG   B CB    1 
ATOM   9501  C  CG    . ARG   B  1  78   ? -27.213 29.918  112.739 1.00 43.90 ? 76   ARG   B CG    1 
ATOM   9502  C  CD    . ARG   B  1  78   ? -27.959 30.495  111.557 1.00 44.06 ? 76   ARG   B CD    1 
ATOM   9503  N  NE    . ARG   B  1  78   ? -27.028 30.977  110.544 1.00 43.83 ? 76   ARG   B NE    1 
ATOM   9504  C  CZ    . ARG   B  1  78   ? -27.381 31.412  109.342 1.00 45.76 ? 76   ARG   B CZ    1 
ATOM   9505  N  NH1   . ARG   B  1  78   ? -28.643 31.398  108.944 1.00 50.47 ? 76   ARG   B NH1   1 
ATOM   9506  N  NH2   . ARG   B  1  78   ? -26.443 31.873  108.519 1.00 45.58 ? 76   ARG   B NH2   1 
ATOM   9507  N  N     . GLY   B  1  79   ? -28.106 29.688  117.395 1.00 37.82 ? 77   GLY   B N     1 
ATOM   9508  C  CA    . GLY   B  1  79   ? -28.785 30.103  118.601 1.00 39.81 ? 77   GLY   B CA    1 
ATOM   9509  C  C     . GLY   B  1  79   ? -27.905 30.264  119.812 1.00 43.54 ? 77   GLY   B C     1 
ATOM   9510  O  O     . GLY   B  1  79   ? -28.413 30.584  120.889 1.00 40.42 ? 77   GLY   B O     1 
ATOM   9511  N  N     . LYS   B  1  80   ? -26.597 30.068  119.677 1.00 42.67 ? 78   LYS   B N     1 
ATOM   9512  C  CA    . LYS   B  1  80   ? -25.699 30.133  120.820 1.00 41.13 ? 78   LYS   B CA    1 
ATOM   9513  C  C     . LYS   B  1  80   ? -24.407 30.865  120.468 1.00 38.80 ? 78   LYS   B C     1 
ATOM   9514  O  O     . LYS   B  1  80   ? -24.249 31.363  119.352 1.00 43.77 ? 78   LYS   B O     1 
ATOM   9515  C  CB    . LYS   B  1  80   ? -25.393 28.723  121.329 1.00 43.00 ? 78   LYS   B CB    1 
ATOM   9516  C  CG    . LYS   B  1  80   ? -24.654 27.852  120.326 1.00 40.58 ? 78   LYS   B CG    1 
ATOM   9517  C  CD    . LYS   B  1  80   ? -24.627 26.394  120.759 1.00 40.66 ? 78   LYS   B CD    1 
ATOM   9518  C  CE    . LYS   B  1  80   ? -23.770 25.557  119.806 1.00 36.13 ? 78   LYS   B CE    1 
ATOM   9519  N  NZ    . LYS   B  1  80   ? -23.737 24.113  120.188 1.00 40.16 ? 78   LYS   B NZ    1 
ATOM   9520  N  N     . GLY   B  1  85   ? -15.206 36.014  121.016 1.00 45.06 ? 83   GLY   B N     1 
ATOM   9521  C  CA    . GLY   B  1  85   ? -14.305 36.680  121.935 1.00 40.79 ? 83   GLY   B CA    1 
ATOM   9522  C  C     . GLY   B  1  85   ? -13.785 38.003  121.405 1.00 41.24 ? 83   GLY   B C     1 
ATOM   9523  O  O     . GLY   B  1  85   ? -13.911 39.037  122.063 1.00 41.69 ? 83   GLY   B O     1 
ATOM   9524  N  N     . VAL   B  1  86   ? -13.188 37.968  120.210 1.00 42.60 ? 84   VAL   B N     1 
ATOM   9525  C  CA    . VAL   B  1  86   ? -12.686 39.195  119.598 1.00 41.49 ? 84   VAL   B CA    1 
ATOM   9526  C  C     . VAL   B  1  86   ? -13.835 40.146  119.282 1.00 39.93 ? 84   VAL   B C     1 
ATOM   9527  O  O     . VAL   B  1  86   ? -13.703 41.370  119.414 1.00 39.62 ? 84   VAL   B O     1 
ATOM   9528  C  CB    . VAL   B  1  86   ? -11.825 38.871  118.362 1.00 43.10 ? 84   VAL   B CB    1 
ATOM   9529  C  CG1   . VAL   B  1  86   ? -11.594 40.118  117.521 1.00 43.47 ? 84   VAL   B CG1   1 
ATOM   9530  C  CG2   . VAL   B  1  86   ? -10.497 38.295  118.797 1.00 45.21 ? 84   VAL   B CG2   1 
ATOM   9531  N  N     . GLU   B  1  87   ? -14.984 39.598  118.878 1.00 41.23 ? 85   GLU   B N     1 
ATOM   9532  C  CA    . GLU   B  1  87   ? -16.150 40.430  118.594 1.00 45.15 ? 85   GLU   B CA    1 
ATOM   9533  C  C     . GLU   B  1  87   ? -16.536 41.276  119.803 1.00 40.25 ? 85   GLU   B C     1 
ATOM   9534  O  O     . GLU   B  1  87   ? -16.805 42.477  119.679 1.00 38.46 ? 85   GLU   B O     1 
ATOM   9535  C  CB    . GLU   B  1  87   ? -17.321 39.549  118.152 1.00 48.89 ? 85   GLU   B CB    1 
ATOM   9536  N  N     . GLY   B  1  88   ? -16.565 40.664  120.988 1.00 39.73 ? 86   GLY   B N     1 
ATOM   9537  C  CA    . GLY   B  1  88   ? -16.927 41.410  122.181 1.00 40.46 ? 86   GLY   B CA    1 
ATOM   9538  C  C     . GLY   B  1  88   ? -15.902 42.469  122.538 1.00 37.87 ? 86   GLY   B C     1 
ATOM   9539  O  O     . GLY   B  1  88   ? -16.253 43.544  123.031 1.00 38.03 ? 86   GLY   B O     1 
ATOM   9540  N  N     . LEU   B  1  89   ? -14.623 42.180  122.296 1.00 36.24 ? 87   LEU   B N     1 
ATOM   9541  C  CA    . LEU   B  1  89   ? -13.581 43.168  122.547 1.00 36.95 ? 87   LEU   B CA    1 
ATOM   9542  C  C     . LEU   B  1  89   ? -13.721 44.353  121.602 1.00 31.42 ? 87   LEU   B C     1 
ATOM   9543  O  O     . LEU   B  1  89   ? -13.621 45.510  122.027 1.00 31.63 ? 87   LEU   B O     1 
ATOM   9544  C  CB    . LEU   B  1  89   ? -12.212 42.511  122.389 1.00 34.95 ? 87   LEU   B CB    1 
ATOM   9545  C  CG    . LEU   B  1  89   ? -10.978 43.400  122.510 1.00 37.87 ? 87   LEU   B CG    1 
ATOM   9546  C  CD1   . LEU   B  1  89   ? -10.888 43.991  123.895 1.00 39.92 ? 87   LEU   B CD1   1 
ATOM   9547  C  CD2   . LEU   B  1  89   ? -9.723  42.602  122.172 1.00 42.31 ? 87   LEU   B CD2   1 
ATOM   9548  N  N     . VAL   B  1  90   ? -13.965 44.076  120.320 1.00 33.98 ? 88   VAL   B N     1 
ATOM   9549  C  CA    . VAL   B  1  90   ? -14.169 45.136  119.336 1.00 33.91 ? 88   VAL   B CA    1 
ATOM   9550  C  C     . VAL   B  1  90   ? -15.370 45.996  119.708 1.00 36.46 ? 88   VAL   B C     1 
ATOM   9551  O  O     . VAL   B  1  90   ? -15.327 47.227  119.597 1.00 34.39 ? 88   VAL   B O     1 
ATOM   9552  C  CB    . VAL   B  1  90   ? -14.302 44.534  117.925 1.00 34.27 ? 88   VAL   B CB    1 
ATOM   9553  C  CG1   . VAL   B  1  90   ? -14.765 45.590  116.933 1.00 35.04 ? 88   VAL   B CG1   1 
ATOM   9554  C  CG2   . VAL   B  1  90   ? -12.981 43.916  117.479 1.00 31.32 ? 88   VAL   B CG2   1 
ATOM   9555  N  N     . GLN   B  1  91   ? -16.455 45.368  120.169 1.00 35.42 ? 89   GLN   B N     1 
ATOM   9556  C  CA    . GLN   B  1  91   ? -17.635 46.143  120.546 1.00 38.56 ? 89   GLN   B CA    1 
ATOM   9557  C  C     . GLN   B  1  91   ? -17.397 46.952  121.818 1.00 35.35 ? 89   GLN   B C     1 
ATOM   9558  O  O     . GLN   B  1  91   ? -17.811 48.114  121.905 1.00 40.20 ? 89   GLN   B O     1 
ATOM   9559  C  CB    . GLN   B  1  91   ? -18.852 45.228  120.693 1.00 44.78 ? 89   GLN   B CB    1 
ATOM   9560  N  N     . GLU   B  1  92   ? -16.729 46.363  122.814 1.00 35.09 ? 90   GLU   B N     1 
ATOM   9561  C  CA    . GLU   B  1  92   ? -16.543 47.055  124.087 1.00 37.04 ? 90   GLU   B CA    1 
ATOM   9562  C  C     . GLU   B  1  92   ? -15.705 48.316  123.927 1.00 33.34 ? 90   GLU   B C     1 
ATOM   9563  O  O     . GLU   B  1  92   ? -16.002 49.349  124.535 1.00 34.62 ? 90   GLU   B O     1 
ATOM   9564  C  CB    . GLU   B  1  92   ? -15.914 46.126  125.127 1.00 39.24 ? 90   GLU   B CB    1 
ATOM   9565  C  CG    . GLU   B  1  92   ? -15.602 46.832  126.442 1.00 41.53 ? 90   GLU   B CG    1 
ATOM   9566  C  CD    . GLU   B  1  92   ? -15.083 45.902  127.527 1.00 41.60 ? 90   GLU   B CD    1 
ATOM   9567  O  OE1   . GLU   B  1  92   ? -14.880 44.700  127.248 1.00 47.86 ? 90   GLU   B OE1   1 
ATOM   9568  O  OE2   . GLU   B  1  92   ? -14.881 46.382  128.663 1.00 40.59 ? 90   GLU   B OE2   1 
ATOM   9569  N  N     . TYR   B  1  93   ? -14.656 48.260  123.111 1.00 33.90 ? 91   TYR   B N     1 
ATOM   9570  C  CA    . TYR   B  1  93   ? -13.781 49.410  122.944 1.00 33.96 ? 91   TYR   B CA    1 
ATOM   9571  C  C     . TYR   B  1  93   ? -14.013 50.140  121.634 1.00 32.54 ? 91   TYR   B C     1 
ATOM   9572  O  O     . TYR   B  1  93   ? -13.207 51.004  121.270 1.00 31.97 ? 91   TYR   B O     1 
ATOM   9573  C  CB    . TYR   B  1  93   ? -12.318 49.005  123.114 1.00 28.51 ? 91   TYR   B CB    1 
ATOM   9574  C  CG    . TYR   B  1  93   ? -12.026 48.636  124.542 1.00 27.59 ? 91   TYR   B CG    1 
ATOM   9575  C  CD1   . TYR   B  1  93   ? -11.714 49.613  125.478 1.00 28.85 ? 91   TYR   B CD1   1 
ATOM   9576  C  CD2   . TYR   B  1  93   ? -12.093 47.318  124.963 1.00 31.10 ? 91   TYR   B CD2   1 
ATOM   9577  C  CE1   . TYR   B  1  93   ? -11.462 49.288  126.793 1.00 32.23 ? 91   TYR   B CE1   1 
ATOM   9578  C  CE2   . TYR   B  1  93   ? -11.840 46.981  126.278 1.00 33.57 ? 91   TYR   B CE2   1 
ATOM   9579  C  CZ    . TYR   B  1  93   ? -11.528 47.973  127.188 1.00 34.53 ? 91   TYR   B CZ    1 
ATOM   9580  O  OH    . TYR   B  1  93   ? -11.277 47.648  128.499 1.00 35.22 ? 91   TYR   B OH    1 
ATOM   9581  N  N     . SER   B  1  94   ? -15.092 49.810  120.928 1.00 28.12 ? 92   SER   B N     1 
ATOM   9582  C  CA    . SER   B  1  94   ? -15.452 50.465  119.675 1.00 29.67 ? 92   SER   B CA    1 
ATOM   9583  C  C     . SER   B  1  94   ? -14.265 50.510  118.725 1.00 28.31 ? 92   SER   B C     1 
ATOM   9584  O  O     . SER   B  1  94   ? -13.904 51.560  118.192 1.00 28.40 ? 92   SER   B O     1 
ATOM   9585  C  CB    . SER   B  1  94   ? -16.015 51.861  119.920 1.00 30.33 ? 92   SER   B CB    1 
ATOM   9586  O  OG    . SER   B  1  94   ? -17.099 51.800  120.829 1.00 33.87 ? 92   SER   B OG    1 
ATOM   9587  N  N     . LEU   B  1  95   ? -13.640 49.355  118.531 1.00 24.26 ? 93   LEU   B N     1 
ATOM   9588  C  CA    . LEU   B  1  95   ? -12.463 49.290  117.684 1.00 24.60 ? 93   LEU   B CA    1 
ATOM   9589  C  C     . LEU   B  1  95   ? -12.876 49.218  116.226 1.00 27.00 ? 93   LEU   B C     1 
ATOM   9590  O  O     . LEU   B  1  95   ? -13.841 48.539  115.868 1.00 27.72 ? 93   LEU   B O     1 
ATOM   9591  C  CB    . LEU   B  1  95   ? -11.633 48.050  118.008 1.00 24.83 ? 93   LEU   B CB    1 
ATOM   9592  C  CG    . LEU   B  1  95   ? -11.140 47.944  119.445 1.00 25.27 ? 93   LEU   B CG    1 
ATOM   9593  C  CD1   . LEU   B  1  95   ? -10.203 46.762  119.599 1.00 25.44 ? 93   LEU   B CD1   1 
ATOM   9594  C  CD2   . LEU   B  1  95   ? -10.459 49.236  119.882 1.00 27.92 ? 93   LEU   B CD2   1 
ATOM   9595  N  N     . SER   B  1  96   ? -12.133 49.922  115.382 1.00 23.38 ? 94   SER   B N     1 
ATOM   9596  C  CA    . SER   B  1  96   ? -12.196 49.628  113.971 1.00 24.69 ? 94   SER   B CA    1 
ATOM   9597  C  C     . SER   B  1  96   ? -11.525 48.279  113.724 1.00 25.69 ? 94   SER   B C     1 
ATOM   9598  O  O     . SER   B  1  96   ? -10.854 47.725  114.601 1.00 22.94 ? 94   SER   B O     1 
ATOM   9599  C  CB    . SER   B  1  96   ? -11.457 50.708  113.189 1.00 26.49 ? 94   SER   B CB    1 
ATOM   9600  O  OG    . SER   B  1  96   ? -10.066 50.667  113.479 1.00 21.99 ? 94   SER   B OG    1 
ATOM   9601  N  N     . SER   B  1  97   ? -11.702 47.749  112.514 1.00 22.20 ? 95   SER   B N     1 
ATOM   9602  C  CA    . SER   B  1  97   ? -11.046 46.493  112.166 1.00 22.03 ? 95   SER   B CA    1 
ATOM   9603  C  C     . SER   B  1  97   ? -9.534  46.615  112.285 1.00 21.36 ? 95   SER   B C     1 
ATOM   9604  O  O     . SER   B  1  97   ? -8.881  45.761  112.894 1.00 21.41 ? 95   SER   B O     1 
ATOM   9605  C  CB    . SER   B  1  97   ? -11.445 46.040  110.761 1.00 26.85 ? 95   SER   B CB    1 
ATOM   9606  O  OG    . SER   B  1  97   ? -12.803 45.635  110.758 1.00 33.96 ? 95   SER   B OG    1 
ATOM   9607  N  N     . GLN   B  1  98   ? -8.962  47.684  111.724 1.00 20.93 ? 96   GLN   B N     1 
ATOM   9608  C  CA    . GLN   B  1  98   ? -7.514  47.868  111.788 1.00 19.81 ? 96   GLN   B CA    1 
ATOM   9609  C  C     . GLN   B  1  98   ? -7.047  48.012  113.232 1.00 18.23 ? 96   GLN   B C     1 
ATOM   9610  O  O     . GLN   B  1  98   ? -5.958  47.550  113.590 1.00 18.42 ? 96   GLN   B O     1 
ATOM   9611  C  CB    . GLN   B  1  98   ? -7.092  49.090  110.960 1.00 20.25 ? 96   GLN   B CB    1 
ATOM   9612  C  CG    . GLN   B  1  98   ? -7.148  48.878  109.463 1.00 20.20 ? 96   GLN   B CG    1 
ATOM   9613  C  CD    . GLN   B  1  98   ? -6.179  47.825  109.010 1.00 23.69 ? 96   GLN   B CD    1 
ATOM   9614  O  OE1   . GLN   B  1  98   ? -6.464  46.629  109.064 1.00 24.75 ? 96   GLN   B OE1   1 
ATOM   9615  N  NE2   . GLN   B  1  98   ? -5.006  48.260  108.575 1.00 21.17 ? 96   GLN   B NE2   1 
ATOM   9616  N  N     . GLU   B  1  99   ? -7.859  48.648  114.079 1.00 18.92 ? 97   GLU   B N     1 
ATOM   9617  C  CA    . GLU   B  1  99   ? -7.495  48.743  115.488 1.00 20.09 ? 97   GLU   B CA    1 
ATOM   9618  C  C     . GLU   B  1  99   ? -7.525  47.376  116.150 1.00 22.12 ? 97   GLU   B C     1 
ATOM   9619  O  O     . GLU   B  1  99   ? -6.628  47.040  116.931 1.00 22.54 ? 97   GLU   B O     1 
ATOM   9620  C  CB    . GLU   B  1  99   ? -8.410  49.723  116.213 1.00 21.77 ? 97   GLU   B CB    1 
ATOM   9621  C  CG    . GLU   B  1  99   ? -8.110  51.173  115.871 1.00 21.94 ? 97   GLU   B CG    1 
ATOM   9622  C  CD    . GLU   B  1  99   ? -9.201  52.111  116.340 1.00 22.85 ? 97   GLU   B CD    1 
ATOM   9623  O  OE1   . GLU   B  1  99   ? -10.234 51.627  116.859 1.00 24.48 ? 97   GLU   B OE1   1 
ATOM   9624  O  OE2   . GLU   B  1  99   ? -9.031  53.341  116.210 1.00 23.30 ? 97   GLU   B OE2   1 
ATOM   9625  N  N     . GLY   B  1  100  ? -8.541  46.569  115.837 1.00 21.12 ? 98   GLY   B N     1 
ATOM   9626  C  CA    . GLY   B  1  100  ? -8.575  45.216  116.365 1.00 20.71 ? 98   GLY   B CA    1 
ATOM   9627  C  C     . GLY   B  1  100  ? -7.371  44.406  115.937 1.00 21.61 ? 98   GLY   B C     1 
ATOM   9628  O  O     . GLY   B  1  100  ? -6.766  43.703  116.750 1.00 20.53 ? 98   GLY   B O     1 
ATOM   9629  N  N     . VAL   B  1  101  ? -6.993  44.510  114.659 1.00 19.31 ? 99   VAL   B N     1 
ATOM   9630  C  CA    . VAL   B  1  101  ? -5.825  43.784  114.171 1.00 19.71 ? 99   VAL   B CA    1 
ATOM   9631  C  C     . VAL   B  1  101  ? -4.570  44.276  114.879 1.00 19.91 ? 99   VAL   B C     1 
ATOM   9632  O  O     . VAL   B  1  101  ? -3.752  43.484  115.368 1.00 18.50 ? 99   VAL   B O     1 
ATOM   9633  C  CB    . VAL   B  1  101  ? -5.707  43.932  112.644 1.00 19.15 ? 99   VAL   B CB    1 
ATOM   9634  C  CG1   . VAL   B  1  101  ? -4.393  43.361  112.157 1.00 19.87 ? 99   VAL   B CG1   1 
ATOM   9635  C  CG2   . VAL   B  1  101  ? -6.890  43.255  111.954 1.00 21.70 ? 99   VAL   B CG2   1 
ATOM   9636  N  N     . ALA   B  1  102  ? -4.401  45.601  114.938 1.00 18.20 ? 100  ALA   B N     1 
ATOM   9637  C  CA    . ALA   B  1  102  ? -3.211  46.175  115.553 1.00 19.36 ? 100  ALA   B CA    1 
ATOM   9638  C  C     . ALA   B  1  102  ? -3.113  45.782  117.017 1.00 20.29 ? 100  ALA   B C     1 
ATOM   9639  O  O     . ALA   B  1  102  ? -2.019  45.500  117.520 1.00 20.32 ? 100  ALA   B O     1 
ATOM   9640  C  CB    . ALA   B  1  102  ? -3.257  47.700  115.440 1.00 18.59 ? 100  ALA   B CB    1 
ATOM   9641  N  N     . LEU   B  1  103  ? -4.248  45.770  117.715 1.00 18.14 ? 101  LEU   B N     1 
ATOM   9642  C  CA    . LEU   B  1  103  ? -4.256  45.398  119.126 1.00 19.65 ? 101  LEU   B CA    1 
ATOM   9643  C  C     . LEU   B  1  103  ? -3.820  43.951  119.307 1.00 22.07 ? 101  LEU   B C     1 
ATOM   9644  O  O     . LEU   B  1  103  ? -3.045  43.634  120.220 1.00 21.77 ? 101  LEU   B O     1 
ATOM   9645  C  CB    . LEU   B  1  103  ? -5.653  45.613  119.708 1.00 21.62 ? 101  LEU   B CB    1 
ATOM   9646  C  CG    . LEU   B  1  103  ? -5.832  45.183  121.153 1.00 23.25 ? 101  LEU   B CG    1 
ATOM   9647  C  CD1   . LEU   B  1  103  ? -4.948  46.033  122.058 1.00 23.48 ? 101  LEU   B CD1   1 
ATOM   9648  C  CD2   . LEU   B  1  103  ? -7.290  45.303  121.554 1.00 22.16 ? 101  LEU   B CD2   1 
ATOM   9649  N  N     . MET   B  1  104  ? -4.314  43.054  118.455 1.00 19.66 ? 102  MET   B N     1 
ATOM   9650  C  CA    . MET   B  1  104  ? -3.914  41.660  118.588 1.00 22.67 ? 102  MET   B CA    1 
ATOM   9651  C  C     . MET   B  1  104  ? -2.441  41.483  118.270 1.00 23.94 ? 102  MET   B C     1 
ATOM   9652  O  O     . MET   B  1  104  ? -1.763  40.674  118.911 1.00 22.17 ? 102  MET   B O     1 
ATOM   9653  C  CB    . MET   B  1  104  ? -4.782  40.762  117.714 1.00 21.26 ? 102  MET   B CB    1 
ATOM   9654  C  CG    . MET   B  1  104  ? -6.267  40.802  118.082 1.00 20.46 ? 102  MET   B CG    1 
ATOM   9655  S  SD    . MET   B  1  104  ? -6.590  40.496  119.848 1.00 33.63 ? 102  MET   B SD    1 
ATOM   9656  C  CE    . MET   B  1  104  ? -6.205  38.752  119.922 1.00 36.79 ? 102  MET   B CE    1 
ATOM   9657  N  N     . CYS   B  1  105  ? -1.919  42.250  117.315 1.00 19.43 ? 103  CYS   B N     1 
ATOM   9658  C  CA    . CYS   B  1  105  ? -0.487  42.194  117.051 1.00 20.18 ? 103  CYS   B CA    1 
ATOM   9659  C  C     . CYS   B  1  105  ? 0.301   42.633  118.273 1.00 21.38 ? 103  CYS   B C     1 
ATOM   9660  O  O     . CYS   B  1  105  ? 1.299   42.002  118.641 1.00 23.36 ? 103  CYS   B O     1 
ATOM   9661  C  CB    . CYS   B  1  105  ? -0.125  43.081  115.863 1.00 19.45 ? 103  CYS   B CB    1 
ATOM   9662  S  SG    . CYS   B  1  105  ? -0.726  42.477  114.293 1.00 21.23 ? 103  CYS   B SG    1 
ATOM   9663  N  N     . LEU   B  1  106  ? -0.110  43.745  118.891 1.00 20.21 ? 104  LEU   B N     1 
ATOM   9664  C  CA    . LEU   B  1  106  ? 0.544   44.194  120.112 1.00 18.68 ? 104  LEU   B CA    1 
ATOM   9665  C  C     . LEU   B  1  106  ? 0.432   43.140  121.197 1.00 22.65 ? 104  LEU   B C     1 
ATOM   9666  O  O     . LEU   B  1  106  ? 1.399   42.877  121.924 1.00 22.99 ? 104  LEU   B O     1 
ATOM   9667  C  CB    . LEU   B  1  106  ? -0.084  45.504  120.592 1.00 21.17 ? 104  LEU   B CB    1 
ATOM   9668  C  CG    . LEU   B  1  106  ? 0.371   46.007  121.964 1.00 23.20 ? 104  LEU   B CG    1 
ATOM   9669  C  CD1   . LEU   B  1  106  ? 1.827   46.417  121.924 1.00 26.30 ? 104  LEU   B CD1   1 
ATOM   9670  C  CD2   . LEU   B  1  106  ? -0.503  47.158  122.442 1.00 23.27 ? 104  LEU   B CD2   1 
ATOM   9671  N  N     . ALA   B  1  107  ? -0.746  42.526  121.321 1.00 21.45 ? 105  ALA   B N     1 
ATOM   9672  C  CA    . ALA   B  1  107  ? -0.941  41.502  122.341 1.00 21.97 ? 105  ALA   B CA    1 
ATOM   9673  C  C     . ALA   B  1  107  ? -0.038  40.304  122.081 1.00 24.44 ? 105  ALA   B C     1 
ATOM   9674  O  O     . ALA   B  1  107  ? 0.600   39.788  123.007 1.00 26.11 ? 105  ALA   B O     1 
ATOM   9675  C  CB    . ALA   B  1  107  ? -2.407  41.079  122.377 1.00 22.47 ? 105  ALA   B CB    1 
ATOM   9676  N  N     . GLU   B  1  108  ? 0.049   39.871  120.820 1.00 22.94 ? 106  GLU   B N     1 
ATOM   9677  C  CA    . GLU   B  1  108  ? 0.962   38.791  120.456 1.00 24.33 ? 106  GLU   B CA    1 
ATOM   9678  C  C     . GLU   B  1  108  ? 2.389   39.118  120.869 1.00 26.91 ? 106  GLU   B C     1 
ATOM   9679  O  O     . GLU   B  1  108  ? 3.090   38.273  121.439 1.00 27.52 ? 106  GLU   B O     1 
ATOM   9680  C  CB    . GLU   B  1  108  ? 0.890   38.542  118.949 1.00 26.46 ? 106  GLU   B CB    1 
ATOM   9681  C  CG    . GLU   B  1  108  ? 1.985   37.627  118.399 1.00 28.92 ? 106  GLU   B CG    1 
ATOM   9682  C  CD    . GLU   B  1  108  ? 2.122   37.708  116.881 1.00 34.11 ? 106  GLU   B CD    1 
ATOM   9683  O  OE1   . GLU   B  1  108  ? 1.182   38.192  116.213 1.00 31.84 ? 106  GLU   B OE1   1 
ATOM   9684  O  OE2   . GLU   B  1  108  ? 3.182   37.297  116.351 1.00 37.47 ? 106  GLU   B OE2   1 
ATOM   9685  N  N     . ALA   B  1  109  ? 2.836   40.346  120.599 1.00 24.83 ? 107  ALA   B N     1 
ATOM   9686  C  CA    . ALA   B  1  109  ? 4.189   40.733  120.981 1.00 27.16 ? 107  ALA   B CA    1 
ATOM   9687  C  C     . ALA   B  1  109  ? 4.356   40.748  122.497 1.00 26.87 ? 107  ALA   B C     1 
ATOM   9688  O  O     . ALA   B  1  109  ? 5.373   40.275  123.019 1.00 25.56 ? 107  ALA   B O     1 
ATOM   9689  C  CB    . ALA   B  1  109  ? 4.548   42.084  120.362 1.00 27.95 ? 107  ALA   B CB    1 
ATOM   9690  N  N     . LEU   B  1  110  ? 3.365   41.270  123.225 1.00 22.90 ? 108  LEU   B N     1 
ATOM   9691  C  CA    . LEU   B  1  110  ? 3.473   41.301  124.681 1.00 24.06 ? 108  LEU   B CA    1 
ATOM   9692  C  C     . LEU   B  1  110  ? 3.514   39.901  125.272 1.00 27.38 ? 108  LEU   B C     1 
ATOM   9693  O  O     . LEU   B  1  110  ? 4.141   39.690  126.319 1.00 29.03 ? 108  LEU   B O     1 
ATOM   9694  C  CB    . LEU   B  1  110  ? 2.315   42.093  125.286 1.00 22.36 ? 108  LEU   B CB    1 
ATOM   9695  C  CG    . LEU   B  1  110  ? 2.453   43.595  125.037 1.00 24.09 ? 108  LEU   B CG    1 
ATOM   9696  C  CD1   . LEU   B  1  110  ? 1.162   44.302  125.381 1.00 25.20 ? 108  LEU   B CD1   1 
ATOM   9697  C  CD2   . LEU   B  1  110  ? 3.610   44.162  125.856 1.00 27.10 ? 108  LEU   B CD2   1 
ATOM   9698  N  N     . LEU   B  1  111  ? 2.864   38.938  124.622 1.00 25.50 ? 109  LEU   B N     1 
ATOM   9699  C  CA    . LEU   B  1  111  ? 2.883   37.568  125.116 1.00 30.15 ? 109  LEU   B CA    1 
ATOM   9700  C  C     . LEU   B  1  111  ? 4.206   36.864  124.862 1.00 32.97 ? 109  LEU   B C     1 
ATOM   9701  O  O     . LEU   B  1  111  ? 4.456   35.820  125.471 1.00 34.00 ? 109  LEU   B O     1 
ATOM   9702  C  CB    . LEU   B  1  111  ? 1.733   36.765  124.517 1.00 31.55 ? 109  LEU   B CB    1 
ATOM   9703  C  CG    . LEU   B  1  111  ? 0.373   37.207  125.043 1.00 28.13 ? 109  LEU   B CG    1 
ATOM   9704  C  CD1   . LEU   B  1  111  ? -0.725  36.550  124.245 1.00 31.94 ? 109  LEU   B CD1   1 
ATOM   9705  C  CD2   . LEU   B  1  111  ? 0.251   36.872  126.523 1.00 34.27 ? 109  LEU   B CD2   1 
ATOM   9706  N  N     . ARG   B  1  112  ? 5.062   37.410  123.998 1.00 30.71 ? 110  ARG   B N     1 
ATOM   9707  C  CA    . ARG   B  1  112  ? 6.409   36.871  123.874 1.00 34.49 ? 110  ARG   B CA    1 
ATOM   9708  C  C     . ARG   B  1  112  ? 7.253   37.185  125.102 1.00 35.36 ? 110  ARG   B C     1 
ATOM   9709  O  O     . ARG   B  1  112  ? 8.307   36.570  125.290 1.00 37.58 ? 110  ARG   B O     1 
ATOM   9710  C  CB    . ARG   B  1  112  ? 7.077   37.361  122.585 1.00 31.96 ? 110  ARG   B CB    1 
ATOM   9711  C  CG    . ARG   B  1  112  ? 6.312   36.976  121.318 1.00 34.80 ? 110  ARG   B CG    1 
ATOM   9712  C  CD    . ARG   B  1  112  ? 7.135   37.147  120.036 1.00 43.73 ? 110  ARG   B CD    1 
ATOM   9713  N  NE    . ARG   B  1  112  ? 7.207   38.529  119.574 1.00 44.57 ? 110  ARG   B NE    1 
ATOM   9714  C  CZ    . ARG   B  1  112  ? 6.408   39.063  118.658 1.00 42.46 ? 110  ARG   B CZ    1 
ATOM   9715  N  NH1   . ARG   B  1  112  ? 5.445   38.361  118.083 1.00 44.75 ? 110  ARG   B NH1   1 
ATOM   9716  N  NH2   . ARG   B  1  112  ? 6.579   40.336  118.309 1.00 49.49 ? 110  ARG   B NH2   1 
ATOM   9717  N  N     . ILE   B  1  113  ? 6.812   38.120  125.938 1.00 32.77 ? 111  ILE   B N     1 
ATOM   9718  C  CA    . ILE   B  1  113  ? 7.431   38.362  127.237 1.00 33.46 ? 111  ILE   B CA    1 
ATOM   9719  C  C     . ILE   B  1  113  ? 6.908   37.297  128.190 1.00 35.65 ? 111  ILE   B C     1 
ATOM   9720  O  O     . ILE   B  1  113  ? 5.730   37.333  128.571 1.00 36.64 ? 111  ILE   B O     1 
ATOM   9721  C  CB    . ILE   B  1  113  ? 7.116   39.774  127.755 1.00 35.80 ? 111  ILE   B CB    1 
ATOM   9722  C  CG1   . ILE   B  1  113  ? 7.658   40.827  126.790 1.00 33.32 ? 111  ILE   B CG1   1 
ATOM   9723  C  CG2   . ILE   B  1  113  ? 7.680   39.967  129.160 1.00 36.15 ? 111  ILE   B CG2   1 
ATOM   9724  C  CD1   . ILE   B  1  113  ? 7.179   42.231  127.096 1.00 32.37 ? 111  ILE   B CD1   1 
ATOM   9725  N  N     . PRO   B  1  114  ? 7.738   36.333  128.598 1.00 41.91 ? 112  PRO   B N     1 
ATOM   9726  C  CA    . PRO   B  1  114  ? 7.207   35.208  129.385 1.00 37.39 ? 112  PRO   B CA    1 
ATOM   9727  C  C     . PRO   B  1  114  ? 6.814   35.575  130.805 1.00 36.14 ? 112  PRO   B C     1 
ATOM   9728  O  O     . PRO   B  1  114  ? 5.866   34.986  131.339 1.00 41.05 ? 112  PRO   B O     1 
ATOM   9729  C  CB    . PRO   B  1  114  ? 8.346   34.176  129.343 1.00 32.78 ? 112  PRO   B CB    1 
ATOM   9730  C  CG    . PRO   B  1  114  ? 9.568   34.978  129.096 1.00 36.95 ? 112  PRO   B CG    1 
ATOM   9731  C  CD    . PRO   B  1  114  ? 9.169   36.176  128.287 1.00 37.84 ? 112  PRO   B CD    1 
ATOM   9732  N  N     . ASP   B  1  115  ? 7.500   36.527  131.431 1.00 38.37 ? 113  ASP   B N     1 
ATOM   9733  C  CA    . ASP   B  1  115  ? 7.236   36.870  132.824 1.00 42.97 ? 113  ASP   B CA    1 
ATOM   9734  C  C     . ASP   B  1  115  ? 6.049   37.824  132.907 1.00 43.01 ? 113  ASP   B C     1 
ATOM   9735  O  O     . ASP   B  1  115  ? 6.100   38.935  132.367 1.00 42.25 ? 113  ASP   B O     1 
ATOM   9736  C  CB    . ASP   B  1  115  ? 8.476   37.504  133.452 1.00 40.06 ? 113  ASP   B CB    1 
ATOM   9737  C  CG    . ASP   B  1  115  ? 8.262   37.892  134.906 1.00 45.81 ? 113  ASP   B CG    1 
ATOM   9738  O  OD1   . ASP   B  1  115  ? 7.925   37.009  135.722 1.00 53.23 ? 113  ASP   B OD1   1 
ATOM   9739  O  OD2   . ASP   B  1  115  ? 8.436   39.082  135.237 1.00 49.24 ? 113  ASP   B OD2   1 
ATOM   9740  N  N     . THR   B  1  116  ? 4.990   37.391  133.596 1.00 42.54 ? 114  THR   B N     1 
ATOM   9741  C  CA    . THR   B  1  116  ? 3.788   38.212  133.724 1.00 46.22 ? 114  THR   B CA    1 
ATOM   9742  C  C     . THR   B  1  116  ? 4.097   39.559  134.368 1.00 46.61 ? 114  THR   B C     1 
ATOM   9743  O  O     . THR   B  1  116  ? 3.570   40.595  133.944 1.00 43.14 ? 114  THR   B O     1 
ATOM   9744  C  CB    . THR   B  1  116  ? 2.726   37.455  134.525 1.00 46.10 ? 114  THR   B CB    1 
ATOM   9745  O  OG1   . THR   B  1  116  ? 2.318   36.291  133.797 1.00 52.72 ? 114  THR   B OG1   1 
ATOM   9746  C  CG2   . THR   B  1  116  ? 1.507   38.335  134.783 1.00 47.54 ? 114  THR   B CG2   1 
ATOM   9747  N  N     . ALA   B  1  117  ? 4.953   39.568  135.391 1.00 46.71 ? 115  ALA   B N     1 
ATOM   9748  C  CA    . ALA   B  1  117  ? 5.275   40.824  136.059 1.00 44.97 ? 115  ALA   B CA    1 
ATOM   9749  C  C     . ALA   B  1  117  ? 6.008   41.771  135.122 1.00 41.13 ? 115  ALA   B C     1 
ATOM   9750  O  O     . ALA   B  1  117  ? 5.699   42.968  135.070 1.00 44.49 ? 115  ALA   B O     1 
ATOM   9751  C  CB    . ALA   B  1  117  ? 6.102   40.556  137.317 1.00 45.23 ? 115  ALA   B CB    1 
ATOM   9752  N  N     . THR   B  1  118  ? 6.985   41.256  134.373 1.00 43.96 ? 116  THR   B N     1 
ATOM   9753  C  CA    . THR   B  1  118  ? 7.706   42.099  133.428 1.00 40.69 ? 116  THR   B CA    1 
ATOM   9754  C  C     . THR   B  1  118  ? 6.769   42.621  132.351 1.00 42.23 ? 116  THR   B C     1 
ATOM   9755  O  O     . THR   B  1  118  ? 6.897   43.766  131.903 1.00 40.73 ? 116  THR   B O     1 
ATOM   9756  C  CB    . THR   B  1  118  ? 8.855   41.309  132.801 1.00 41.94 ? 116  THR   B CB    1 
ATOM   9757  O  OG1   . THR   B  1  118  ? 9.747   40.868  133.833 1.00 47.22 ? 116  THR   B OG1   1 
ATOM   9758  C  CG2   . THR   B  1  118  ? 9.623   42.172  131.817 1.00 40.79 ? 116  THR   B CG2   1 
ATOM   9759  N  N     . ARG   B  1  119  ? 5.809   41.795  131.935 1.00 40.51 ? 117  ARG   B N     1 
ATOM   9760  C  CA    . ARG   B  1  119  ? 4.887   42.198  130.882 1.00 38.16 ? 117  ARG   B CA    1 
ATOM   9761  C  C     . ARG   B  1  119  ? 3.929   43.270  131.381 1.00 38.82 ? 117  ARG   B C     1 
ATOM   9762  O  O     . ARG   B  1  119  ? 3.775   44.324  130.749 1.00 36.43 ? 117  ARG   B O     1 
ATOM   9763  C  CB    . ARG   B  1  119  ? 4.119   40.978  130.381 1.00 33.18 ? 117  ARG   B CB    1 
ATOM   9764  C  CG    . ARG   B  1  119  ? 3.218   41.266  129.191 1.00 33.74 ? 117  ARG   B CG    1 
ATOM   9765  C  CD    . ARG   B  1  119  ? 2.254   40.128  128.944 1.00 33.43 ? 117  ARG   B CD    1 
ATOM   9766  N  NE    . ARG   B  1  119  ? 2.935   38.847  128.792 1.00 35.35 ? 117  ARG   B NE    1 
ATOM   9767  C  CZ    . ARG   B  1  119  ? 2.611   37.743  129.454 1.00 39.98 ? 117  ARG   B CZ    1 
ATOM   9768  N  NH1   . ARG   B  1  119  ? 1.611   37.725  130.322 1.00 36.52 ? 117  ARG   B NH1   1 
ATOM   9769  N  NH2   . ARG   B  1  119  ? 3.294   36.626  129.227 1.00 40.32 ? 117  ARG   B NH2   1 
ATOM   9770  N  N     . ASP   B  1  120  ? 3.282   43.022  132.524 1.00 38.35 ? 118  ASP   B N     1 
ATOM   9771  C  CA    . ASP   B  1  120  ? 2.353   44.001  133.080 1.00 41.22 ? 118  ASP   B CA    1 
ATOM   9772  C  C     . ASP   B  1  120  ? 3.051   45.311  133.413 1.00 42.76 ? 118  ASP   B C     1 
ATOM   9773  O  O     . ASP   B  1  120  ? 2.440   46.380  133.312 1.00 39.52 ? 118  ASP   B O     1 
ATOM   9774  C  CB    . ASP   B  1  120  ? 1.649   43.425  134.306 1.00 40.26 ? 118  ASP   B CB    1 
ATOM   9775  C  CG    . ASP   B  1  120  ? 0.787   42.224  133.969 1.00 47.79 ? 118  ASP   B CG    1 
ATOM   9776  O  OD1   . ASP   B  1  120  ? 0.569   41.965  132.763 1.00 49.77 ? 118  ASP   B OD1   1 
ATOM   9777  O  OD2   . ASP   B  1  120  ? 0.334   41.531  134.905 1.00 52.83 ? 118  ASP   B OD2   1 
ATOM   9778  N  N     . ALA   B  1  121  ? 4.331   45.252  133.794 1.00 41.06 ? 119  ALA   B N     1 
ATOM   9779  C  CA    . ALA   B  1  121  ? 5.074   46.479  134.056 1.00 43.97 ? 119  ALA   B CA    1 
ATOM   9780  C  C     . ALA   B  1  121  ? 5.312   47.266  132.774 1.00 40.82 ? 119  ALA   B C     1 
ATOM   9781  O  O     . ALA   B  1  121  ? 5.158   48.492  132.756 1.00 42.30 ? 119  ALA   B O     1 
ATOM   9782  C  CB    . ALA   B  1  121  ? 6.396   46.164  134.758 1.00 43.62 ? 119  ALA   B CB    1 
ATOM   9783  N  N     . LEU   B  1  122  ? 5.688   46.582  131.689 1.00 39.77 ? 120  LEU   B N     1 
ATOM   9784  C  CA    . LEU   B  1  122  ? 5.893   47.278  130.423 1.00 37.59 ? 120  LEU   B CA    1 
ATOM   9785  C  C     . LEU   B  1  122  ? 4.594   47.903  129.930 1.00 37.16 ? 120  LEU   B C     1 
ATOM   9786  O  O     . LEU   B  1  122  ? 4.600   48.997  129.354 1.00 37.71 ? 120  LEU   B O     1 
ATOM   9787  C  CB    . LEU   B  1  122  ? 6.453   46.315  129.374 1.00 37.86 ? 120  LEU   B CB    1 
ATOM   9788  C  CG    . LEU   B  1  122  ? 6.802   46.967  128.034 1.00 39.41 ? 120  LEU   B CG    1 
ATOM   9789  C  CD1   . LEU   B  1  122  ? 8.041   47.852  128.167 1.00 42.48 ? 120  LEU   B CD1   1 
ATOM   9790  C  CD2   . LEU   B  1  122  ? 6.983   45.928  126.942 1.00 36.09 ? 120  LEU   B CD2   1 
ATOM   9791  N  N     . ILE   B  1  123  ? 3.472   47.217  130.149 1.00 33.77 ? 121  ILE   B N     1 
ATOM   9792  C  CA    . ILE   B  1  123  ? 2.178   47.724  129.704 1.00 37.77 ? 121  ILE   B CA    1 
ATOM   9793  C  C     . ILE   B  1  123  ? 1.823   49.006  130.445 1.00 41.13 ? 121  ILE   B C     1 
ATOM   9794  O  O     . ILE   B  1  123  ? 1.529   50.039  129.829 1.00 39.12 ? 121  ILE   B O     1 
ATOM   9795  C  CB    . ILE   B  1  123  ? 1.098   46.643  129.881 1.00 34.83 ? 121  ILE   B CB    1 
ATOM   9796  C  CG1   . ILE   B  1  123  ? 1.315   45.501  128.890 1.00 28.47 ? 121  ILE   B CG1   1 
ATOM   9797  C  CG2   . ILE   B  1  123  ? -0.295  47.238  129.728 1.00 35.73 ? 121  ILE   B CG2   1 
ATOM   9798  C  CD1   . ILE   B  1  123  ? 0.475   44.302  129.202 1.00 27.11 ? 121  ILE   B CD1   1 
ATOM   9799  N  N     . ARG   B  1  124  ? 1.852   48.959  131.779 1.00 37.56 ? 122  ARG   B N     1 
ATOM   9800  C  CA    . ARG   B  1  124  ? 1.423   50.104  132.575 1.00 43.20 ? 122  ARG   B CA    1 
ATOM   9801  C  C     . ARG   B  1  124  ? 2.372   51.287  132.437 1.00 45.55 ? 122  ARG   B C     1 
ATOM   9802  O  O     . ARG   B  1  124  ? 1.925   52.439  132.469 1.00 49.64 ? 122  ARG   B O     1 
ATOM   9803  C  CB    . ARG   B  1  124  ? 1.281   49.702  134.043 1.00 43.83 ? 122  ARG   B CB    1 
ATOM   9804  N  N     . ASP   B  1  125  ? 3.669   51.034  132.261 1.00 43.24 ? 123  ASP   B N     1 
ATOM   9805  C  CA    . ASP   B  1  125  ? 4.666   52.091  132.352 1.00 47.18 ? 123  ASP   B CA    1 
ATOM   9806  C  C     . ASP   B  1  125  ? 5.192   52.572  131.008 1.00 47.63 ? 123  ASP   B C     1 
ATOM   9807  O  O     . ASP   B  1  125  ? 5.668   53.708  130.926 1.00 51.90 ? 123  ASP   B O     1 
ATOM   9808  C  CB    . ASP   B  1  125  ? 5.842   51.645  133.230 1.00 53.62 ? 123  ASP   B CB    1 
ATOM   9809  C  CG    . ASP   B  1  125  ? 5.398   51.211  134.613 1.00 56.95 ? 123  ASP   B CG    1 
ATOM   9810  O  OD1   . ASP   B  1  125  ? 4.424   51.795  135.132 1.00 58.80 ? 123  ASP   B OD1   1 
ATOM   9811  O  OD2   . ASP   B  1  125  ? 6.014   50.284  135.179 1.00 62.24 ? 123  ASP   B OD2   1 
ATOM   9812  N  N     . LYS   B  1  126  ? 5.123   51.761  129.961 1.00 43.46 ? 124  LYS   B N     1 
ATOM   9813  C  CA    . LYS   B  1  126  ? 5.696   52.154  128.682 1.00 42.93 ? 124  LYS   B CA    1 
ATOM   9814  C  C     . LYS   B  1  126  ? 4.714   52.090  127.522 1.00 45.70 ? 124  LYS   B C     1 
ATOM   9815  O  O     . LYS   B  1  126  ? 4.765   52.946  126.634 1.00 48.15 ? 124  LYS   B O     1 
ATOM   9816  C  CB    . LYS   B  1  126  ? 6.934   51.301  128.365 1.00 46.08 ? 124  LYS   B CB    1 
ATOM   9817  N  N     . ILE   B  1  127  ? 3.821   51.105  127.497 1.00 42.04 ? 125  ILE   B N     1 
ATOM   9818  C  CA    . ILE   B  1  127  ? 2.896   50.951  126.374 1.00 39.22 ? 125  ILE   B CA    1 
ATOM   9819  C  C     . ILE   B  1  127  ? 1.665   51.836  126.537 1.00 41.70 ? 125  ILE   B C     1 
ATOM   9820  O  O     . ILE   B  1  127  ? 1.253   52.525  125.600 1.00 42.22 ? 125  ILE   B O     1 
ATOM   9821  C  CB    . ILE   B  1  127  ? 2.510   49.471  126.171 1.00 34.37 ? 125  ILE   B CB    1 
ATOM   9822  C  CG1   . ILE   B  1  127  ? 3.750   48.570  126.167 1.00 39.03 ? 125  ILE   B CG1   1 
ATOM   9823  C  CG2   . ILE   B  1  127  ? 1.746   49.303  124.864 1.00 33.94 ? 125  ILE   B CG2   1 
ATOM   9824  C  CD1   . ILE   B  1  127  ? 4.725   48.882  125.064 1.00 40.95 ? 125  ILE   B CD1   1 
ATOM   9825  N  N     . ALA   B  1  128  ? 1.053   51.823  127.726 1.00 36.24 ? 126  ALA   B N     1 
ATOM   9826  C  CA    . ALA   B  1  128  ? -0.175  52.583  127.941 1.00 37.47 ? 126  ALA   B CA    1 
ATOM   9827  C  C     . ALA   B  1  128  ? 0.049   54.080  127.782 1.00 42.55 ? 126  ALA   B C     1 
ATOM   9828  O  O     . ALA   B  1  128  ? -0.884  54.812  127.432 1.00 44.11 ? 126  ALA   B O     1 
ATOM   9829  C  CB    . ALA   B  1  128  ? -0.759  52.269  129.317 1.00 37.88 ? 126  ALA   B CB    1 
ATOM   9830  N  N     . ASP   B  1  129  ? 1.266   54.552  128.034 1.00 46.58 ? 127  ASP   B N     1 
ATOM   9831  C  CA    . ASP   B  1  129  ? 1.615   55.949  127.834 1.00 53.19 ? 127  ASP   B CA    1 
ATOM   9832  C  C     . ASP   B  1  129  ? 1.838   56.295  126.364 1.00 57.31 ? 127  ASP   B C     1 
ATOM   9833  O  O     . ASP   B  1  129  ? 2.328   57.388  126.068 1.00 64.70 ? 127  ASP   B O     1 
ATOM   9834  C  CB    . ASP   B  1  129  ? 2.849   56.314  128.667 1.00 55.45 ? 127  ASP   B CB    1 
ATOM   9835  N  N     . GLY   B  1  130  ? 1.500   55.389  125.449 1.00 55.73 ? 128  GLY   B N     1 
ATOM   9836  C  CA    . GLY   B  1  130  ? 1.625   55.621  124.032 1.00 56.77 ? 128  GLY   B CA    1 
ATOM   9837  C  C     . GLY   B  1  130  ? 2.948   55.195  123.431 1.00 57.14 ? 128  GLY   B C     1 
ATOM   9838  O  O     . GLY   B  1  130  ? 2.977   54.738  122.287 1.00 54.76 ? 128  GLY   B O     1 
ATOM   9839  N  N     . ASN   B  1  131  ? 4.045   55.328  124.177 1.00 63.13 ? 129  ASN   B N     1 
ATOM   9840  C  CA    . ASN   B  1  131  ? 5.369   55.009  123.650 1.00 61.53 ? 129  ASN   B CA    1 
ATOM   9841  C  C     . ASN   B  1  131  ? 5.509   53.519  123.357 1.00 60.95 ? 129  ASN   B C     1 
ATOM   9842  O  O     . ASN   B  1  131  ? 6.306   52.827  123.999 1.00 66.51 ? 129  ASN   B O     1 
ATOM   9843  C  CB    . ASN   B  1  131  ? 6.450   55.458  124.635 1.00 63.48 ? 129  ASN   B CB    1 
ATOM   9844  N  N     . TRP   B  1  132  ? 4.750   53.017  122.381 1.00 51.66 ? 130  TRP   B N     1 
ATOM   9845  C  CA    . TRP   B  1  132  ? 4.798   51.600  122.048 1.00 46.03 ? 130  TRP   B CA    1 
ATOM   9846  C  C     . TRP   B  1  132  ? 5.814   51.283  120.962 1.00 47.93 ? 130  TRP   B C     1 
ATOM   9847  O  O     . TRP   B  1  132  ? 6.310   50.153  120.900 1.00 52.36 ? 130  TRP   B O     1 
ATOM   9848  C  CB    . TRP   B  1  132  ? 3.410   51.085  121.635 1.00 42.29 ? 130  TRP   B CB    1 
ATOM   9849  C  CG    . TRP   B  1  132  ? 2.879   51.654  120.339 1.00 36.46 ? 130  TRP   B CG    1 
ATOM   9850  C  CD1   . TRP   B  1  132  ? 1.998   52.684  120.197 1.00 34.78 ? 130  TRP   B CD1   1 
ATOM   9851  C  CD2   . TRP   B  1  132  ? 3.200   51.217  119.012 1.00 32.39 ? 130  TRP   B CD2   1 
ATOM   9852  N  NE1   . TRP   B  1  132  ? 1.746   52.917  118.867 1.00 33.01 ? 130  TRP   B NE1   1 
ATOM   9853  C  CE2   . TRP   B  1  132  ? 2.473   52.031  118.117 1.00 27.61 ? 130  TRP   B CE2   1 
ATOM   9854  C  CE3   . TRP   B  1  132  ? 4.022   50.214  118.495 1.00 30.26 ? 130  TRP   B CE3   1 
ATOM   9855  C  CZ2   . TRP   B  1  132  ? 2.550   51.874  116.733 1.00 26.22 ? 130  TRP   B CZ2   1 
ATOM   9856  C  CZ3   . TRP   B  1  132  ? 4.104   50.063  117.128 1.00 27.45 ? 130  TRP   B CZ3   1 
ATOM   9857  C  CH2   . TRP   B  1  132  ? 3.367   50.886  116.260 1.00 27.63 ? 130  TRP   B CH2   1 
ATOM   9858  N  N     . LYS   B  1  133  ? 6.128   52.251  120.100 1.00 49.55 ? 131  LYS   B N     1 
ATOM   9859  C  CA    . LYS   B  1  133  ? 7.063   52.002  119.009 1.00 52.05 ? 131  LYS   B CA    1 
ATOM   9860  C  C     . LYS   B  1  133  ? 8.443   51.640  119.547 1.00 61.24 ? 131  LYS   B C     1 
ATOM   9861  O  O     . LYS   B  1  133  ? 8.946   50.532  119.321 1.00 64.28 ? 131  LYS   B O     1 
ATOM   9862  C  CB    . LYS   B  1  133  ? 7.131   53.229  118.097 1.00 50.78 ? 131  LYS   B CB    1 
ATOM   9863  N  N     . SER   B  1  134  ? 9.065   52.563  120.280 1.00 65.33 ? 132  SER   B N     1 
ATOM   9864  C  CA    . SER   B  1  134  ? 10.382  52.332  120.870 1.00 65.62 ? 132  SER   B CA    1 
ATOM   9865  C  C     . SER   B  1  134  ? 10.252  51.556  122.183 1.00 65.13 ? 132  SER   B C     1 
ATOM   9866  O  O     . SER   B  1  134  ? 10.572  52.043  123.268 1.00 68.87 ? 132  SER   B O     1 
ATOM   9867  C  CB    . SER   B  1  134  ? 11.110  53.656  121.067 1.00 67.28 ? 132  SER   B CB    1 
ATOM   9868  N  N     . HIS   B  1  135  ? 9.764   50.320  122.063 1.00 62.78 ? 133  HIS   B N     1 
ATOM   9869  C  CA    . HIS   B  1  135  ? 9.574   49.457  123.224 1.00 62.56 ? 133  HIS   B CA    1 
ATOM   9870  C  C     . HIS   B  1  135  ? 9.330   48.013  122.801 1.00 62.94 ? 133  HIS   B C     1 
ATOM   9871  O  O     . HIS   B  1  135  ? 9.535   47.087  123.593 1.00 62.36 ? 133  HIS   B O     1 
ATOM   9872  C  CB    . HIS   B  1  135  ? 8.416   49.960  124.090 1.00 57.34 ? 133  HIS   B CB    1 
ATOM   9873  N  N     . LEU   B  1  136  ? 8.884   47.813  121.564 1.00 59.32 ? 134  LEU   B N     1 
ATOM   9874  C  CA    . LEU   B  1  136  ? 8.645   46.474  121.036 1.00 54.75 ? 134  LEU   B CA    1 
ATOM   9875  C  C     . LEU   B  1  136  ? 9.036   46.399  119.563 1.00 48.91 ? 134  LEU   B C     1 
ATOM   9876  O  O     . LEU   B  1  136  ? 8.934   45.344  118.940 1.00 47.54 ? 134  LEU   B O     1 
ATOM   9877  C  CB    . LEU   B  1  136  ? 7.177   46.074  121.208 1.00 50.99 ? 134  LEU   B CB    1 
ATOM   9878  C  CG    . LEU   B  1  136  ? 6.668   45.804  122.624 1.00 47.14 ? 134  LEU   B CG    1 
ATOM   9879  C  CD1   . LEU   B  1  136  ? 5.182   45.535  122.597 1.00 38.54 ? 134  LEU   B CD1   1 
ATOM   9880  C  CD2   . LEU   B  1  136  ? 7.411   44.630  123.250 1.00 48.42 ? 134  LEU   B CD2   1 
ATOM   9881  N  N     . ARG   B  1  140  ? 12.111  44.445  114.215 1.00 45.22 ? 138  ARG   B N     1 
ATOM   9882  C  CA    . ARG   B  1  140  ? 11.034  43.596  113.712 1.00 48.70 ? 138  ARG   B CA    1 
ATOM   9883  C  C     . ARG   B  1  140  ? 9.667   44.231  113.973 1.00 44.09 ? 138  ARG   B C     1 
ATOM   9884  O  O     . ARG   B  1  140  ? 9.311   44.519  115.118 1.00 36.22 ? 138  ARG   B O     1 
ATOM   9885  C  CB    . ARG   B  1  140  ? 11.106  42.200  114.342 1.00 48.17 ? 138  ARG   B CB    1 
ATOM   9886  C  CG    . ARG   B  1  140  ? 9.978   41.253  113.931 1.00 44.57 ? 138  ARG   B CG    1 
ATOM   9887  C  CD    . ARG   B  1  140  ? 10.110  39.914  114.650 1.00 54.13 ? 138  ARG   B CD    1 
ATOM   9888  N  NE    . ARG   B  1  140  ? 8.954   39.044  114.467 1.00 52.30 ? 138  ARG   B NE    1 
ATOM   9889  C  CZ    . ARG   B  1  140  ? 8.912   38.013  113.631 1.00 57.01 ? 138  ARG   B CZ    1 
ATOM   9890  N  NH1   . ARG   B  1  140  ? 9.942   37.703  112.861 1.00 57.60 ? 138  ARG   B NH1   1 
ATOM   9891  N  NH2   . ARG   B  1  140  ? 7.808   37.271  113.570 1.00 57.77 ? 138  ARG   B NH2   1 
ATOM   9892  N  N     . SER   B  1  141  ? 8.907   44.433  112.898 1.00 37.67 ? 139  SER   B N     1 
ATOM   9893  C  CA    . SER   B  1  141  ? 7.622   45.105  113.005 1.00 28.86 ? 139  SER   B CA    1 
ATOM   9894  C  C     . SER   B  1  141  ? 6.692   44.349  113.950 1.00 30.78 ? 139  SER   B C     1 
ATOM   9895  O  O     . SER   B  1  141  ? 6.648   43.115  113.972 1.00 29.54 ? 139  SER   B O     1 
ATOM   9896  C  CB    . SER   B  1  141  ? 6.979   45.216  111.619 1.00 32.35 ? 139  SER   B CB    1 
ATOM   9897  O  OG    . SER   B  1  141  ? 5.672   45.787  111.678 1.00 30.70 ? 139  SER   B OG    1 
ATOM   9898  N  N     . LEU   B  1  142  ? 5.942   45.109  114.741 1.00 25.55 ? 140  LEU   B N     1 
ATOM   9899  C  CA    . LEU   B  1  142  ? 4.872   44.528  115.530 1.00 23.76 ? 140  LEU   B CA    1 
ATOM   9900  C  C     . LEU   B  1  142  ? 3.853   43.803  114.664 1.00 21.39 ? 140  LEU   B C     1 
ATOM   9901  O  O     . LEU   B  1  142  ? 3.117   42.946  115.163 1.00 22.33 ? 140  LEU   B O     1 
ATOM   9902  C  CB    . LEU   B  1  142  ? 4.153   45.662  116.254 1.00 23.64 ? 140  LEU   B CB    1 
ATOM   9903  C  CG    . LEU   B  1  142  ? 3.566   45.278  117.595 1.00 27.60 ? 140  LEU   B CG    1 
ATOM   9904  C  CD1   . LEU   B  1  142  ? 4.701   45.113  118.572 1.00 27.51 ? 140  LEU   B CD1   1 
ATOM   9905  C  CD2   . LEU   B  1  142  ? 2.603   46.333  118.059 1.00 28.01 ? 140  LEU   B CD2   1 
ATOM   9906  N  N     . PHE   B  1  143  ? 3.777   44.143  113.381 1.00 21.35 ? 141  PHE   B N     1 
ATOM   9907  C  CA    . PHE   B  1  143  ? 2.676   43.735  112.529 1.00 18.32 ? 141  PHE   B CA    1 
ATOM   9908  C  C     . PHE   B  1  143  ? 3.051   42.616  111.568 1.00 20.67 ? 141  PHE   B C     1 
ATOM   9909  O  O     . PHE   B  1  143  ? 2.303   42.347  110.626 1.00 21.78 ? 141  PHE   B O     1 
ATOM   9910  C  CB    . PHE   B  1  143  ? 2.128   44.965  111.805 1.00 18.95 ? 141  PHE   B CB    1 
ATOM   9911  C  CG    . PHE   B  1  143  ? 1.828   46.100  112.735 1.00 18.40 ? 141  PHE   B CG    1 
ATOM   9912  C  CD1   . PHE   B  1  143  ? 0.918   45.935  113.769 1.00 19.25 ? 141  PHE   B CD1   1 
ATOM   9913  C  CD2   . PHE   B  1  143  ? 2.445   47.329  112.584 1.00 18.07 ? 141  PHE   B CD2   1 
ATOM   9914  C  CE1   . PHE   B  1  143  ? 0.638   46.956  114.625 1.00 19.34 ? 141  PHE   B CE1   1 
ATOM   9915  C  CE2   . PHE   B  1  143  ? 2.172   48.365  113.456 1.00 19.05 ? 141  PHE   B CE2   1 
ATOM   9916  C  CZ    . PHE   B  1  143  ? 1.261   48.184  114.469 1.00 19.65 ? 141  PHE   B CZ    1 
ATOM   9917  N  N     . VAL   B  1  144  ? 4.182   41.943  111.812 1.00 21.85 ? 142  VAL   B N     1 
ATOM   9918  C  CA    . VAL   B  1  144  ? 4.612   40.832  110.960 1.00 22.42 ? 142  VAL   B CA    1 
ATOM   9919  C  C     . VAL   B  1  144  ? 3.479   39.841  110.708 1.00 24.53 ? 142  VAL   B C     1 
ATOM   9920  O  O     . VAL   B  1  144  ? 3.292   39.364  109.582 1.00 23.30 ? 142  VAL   B O     1 
ATOM   9921  C  CB    . VAL   B  1  144  ? 5.865   40.155  111.548 1.00 29.60 ? 142  VAL   B CB    1 
ATOM   9922  C  CG1   . VAL   B  1  144  ? 6.216   38.896  110.767 1.00 30.22 ? 142  VAL   B CG1   1 
ATOM   9923  C  CG2   . VAL   B  1  144  ? 7.031   41.122  111.532 1.00 29.66 ? 142  VAL   B CG2   1 
ATOM   9924  N  N     . ASN   B  1  145  ? 2.692   39.527  111.739 1.00 23.06 ? 143  ASN   B N     1 
ATOM   9925  C  CA    . ASN   B  1  145  ? 1.645   38.523  111.611 1.00 24.45 ? 143  ASN   B CA    1 
ATOM   9926  C  C     . ASN   B  1  145  ? 0.252   39.122  111.472 1.00 24.93 ? 143  ASN   B C     1 
ATOM   9927  O  O     . ASN   B  1  145  ? -0.740  38.447  111.763 1.00 23.17 ? 143  ASN   B O     1 
ATOM   9928  C  CB    . ASN   B  1  145  ? 1.712   37.532  112.770 1.00 29.62 ? 143  ASN   B CB    1 
ATOM   9929  C  CG    . ASN   B  1  145  ? 2.862   36.569  112.622 1.00 34.79 ? 143  ASN   B CG    1 
ATOM   9930  O  OD1   . ASN   B  1  145  ? 3.120   36.064  111.524 1.00 35.77 ? 143  ASN   B OD1   1 
ATOM   9931  N  ND2   . ASN   B  1  145  ? 3.568   36.313  113.716 1.00 34.55 ? 143  ASN   B ND2   1 
ATOM   9932  N  N     . ALA   B  1  146  ? 0.158   40.370  111.013 1.00 21.84 ? 144  ALA   B N     1 
ATOM   9933  C  CA    . ALA   B  1  146  ? -1.134  41.040  110.968 1.00 22.33 ? 144  ALA   B CA    1 
ATOM   9934  C  C     . ALA   B  1  146  ? -2.076  40.423  109.941 1.00 21.42 ? 144  ALA   B C     1 
ATOM   9935  O  O     . ALA   B  1  146  ? -3.297  40.561  110.069 1.00 23.03 ? 144  ALA   B O     1 
ATOM   9936  C  CB    . ALA   B  1  146  ? -0.940  42.531  110.694 1.00 22.62 ? 144  ALA   B CB    1 
ATOM   9937  N  N     . ALA   B  1  147  ? -1.547  39.778  108.896 1.00 23.10 ? 145  ALA   B N     1 
ATOM   9938  C  CA    . ALA   B  1  147  ? -2.438  39.102  107.958 1.00 25.30 ? 145  ALA   B CA    1 
ATOM   9939  C  C     . ALA   B  1  147  ? -3.234  38.016  108.665 1.00 24.37 ? 145  ALA   B C     1 
ATOM   9940  O  O     . ALA   B  1  147  ? -4.441  37.866  108.436 1.00 25.41 ? 145  ALA   B O     1 
ATOM   9941  C  CB    . ALA   B  1  147  ? -1.641  38.519  106.793 1.00 26.52 ? 145  ALA   B CB    1 
ATOM   9942  N  N     . THR   B  1  148  ? -2.580  37.279  109.560 1.00 25.08 ? 146  THR   B N     1 
ATOM   9943  C  CA    . THR   B  1  148  ? -3.272  36.265  110.342 1.00 24.14 ? 146  THR   B CA    1 
ATOM   9944  C  C     . THR   B  1  148  ? -4.300  36.901  111.267 1.00 23.93 ? 146  THR   B C     1 
ATOM   9945  O  O     . THR   B  1  148  ? -5.449  36.454  111.332 1.00 26.47 ? 146  THR   B O     1 
ATOM   9946  C  CB    . THR   B  1  148  ? -2.253  35.450  111.138 1.00 33.30 ? 146  THR   B CB    1 
ATOM   9947  O  OG1   . THR   B  1  148  ? -1.292  34.885  110.238 1.00 34.32 ? 146  THR   B OG1   1 
ATOM   9948  C  CG2   . THR   B  1  148  ? -2.941  34.334  111.897 1.00 36.90 ? 146  THR   B CG2   1 
ATOM   9949  N  N     . TRP   B  1  149  ? -3.911  37.958  111.985 1.00 22.79 ? 147  TRP   B N     1 
ATOM   9950  C  CA    . TRP   B  1  149  ? -4.869  38.625  112.855 1.00 23.39 ? 147  TRP   B CA    1 
ATOM   9951  C  C     . TRP   B  1  149  ? -5.961  39.317  112.056 1.00 22.14 ? 147  TRP   B C     1 
ATOM   9952  O  O     . TRP   B  1  149  ? -7.101  39.397  112.517 1.00 22.92 ? 147  TRP   B O     1 
ATOM   9953  C  CB    . TRP   B  1  149  ? -4.169  39.602  113.795 1.00 23.23 ? 147  TRP   B CB    1 
ATOM   9954  C  CG    . TRP   B  1  149  ? -3.296  38.911  114.789 1.00 23.38 ? 147  TRP   B CG    1 
ATOM   9955  C  CD1   . TRP   B  1  149  ? -1.941  38.960  114.853 1.00 24.84 ? 147  TRP   B CD1   1 
ATOM   9956  C  CD2   . TRP   B  1  149  ? -3.721  38.037  115.842 1.00 25.52 ? 147  TRP   B CD2   1 
ATOM   9957  N  NE1   . TRP   B  1  149  ? -1.488  38.185  115.894 1.00 26.00 ? 147  TRP   B NE1   1 
ATOM   9958  C  CE2   . TRP   B  1  149  ? -2.561  37.604  116.515 1.00 27.32 ? 147  TRP   B CE2   1 
ATOM   9959  C  CE3   . TRP   B  1  149  ? -4.968  37.584  116.284 1.00 28.67 ? 147  TRP   B CE3   1 
ATOM   9960  C  CZ2   . TRP   B  1  149  ? -2.610  36.743  117.613 1.00 29.71 ? 147  TRP   B CZ2   1 
ATOM   9961  C  CZ3   . TRP   B  1  149  ? -5.015  36.728  117.384 1.00 29.83 ? 147  TRP   B CZ3   1 
ATOM   9962  C  CH2   . TRP   B  1  149  ? -3.842  36.317  118.029 1.00 33.36 ? 147  TRP   B CH2   1 
ATOM   9963  N  N     . GLY   B  1  150  ? -5.637  39.806  110.856 1.00 22.28 ? 148  GLY   B N     1 
ATOM   9964  C  CA    . GLY   B  1  150  ? -6.675  40.344  109.996 1.00 23.67 ? 148  GLY   B CA    1 
ATOM   9965  C  C     . GLY   B  1  150  ? -7.739  39.312  109.695 1.00 24.77 ? 148  GLY   B C     1 
ATOM   9966  O  O     . GLY   B  1  150  ? -8.937  39.612  109.699 1.00 25.50 ? 148  GLY   B O     1 
ATOM   9967  N  N     . LEU   B  1  151  ? -7.318  38.074  109.450 1.00 24.49 ? 149  LEU   B N     1 
ATOM   9968  C  CA    . LEU   B  1  151  ? -8.284  37.015  109.203 1.00 28.48 ? 149  LEU   B CA    1 
ATOM   9969  C  C     . LEU   B  1  151  ? -9.117  36.745  110.451 1.00 27.71 ? 149  LEU   B C     1 
ATOM   9970  O  O     . LEU   B  1  151  ? -10.336 36.554  110.367 1.00 29.03 ? 149  LEU   B O     1 
ATOM   9971  C  CB    . LEU   B  1  151  ? -7.546  35.763  108.731 1.00 29.71 ? 149  LEU   B CB    1 
ATOM   9972  C  CG    . LEU   B  1  151  ? -8.382  34.632  108.143 1.00 37.69 ? 149  LEU   B CG    1 
ATOM   9973  C  CD1   . LEU   B  1  151  ? -9.226  35.153  106.993 1.00 34.39 ? 149  LEU   B CD1   1 
ATOM   9974  C  CD2   . LEU   B  1  151  ? -7.465  33.518  107.672 1.00 41.67 ? 149  LEU   B CD2   1 
ATOM   9975  N  N     . VAL   B  1  152  ? -8.479  36.759  111.625 1.00 27.12 ? 150  VAL   B N     1 
ATOM   9976  C  CA    . VAL   B  1  152  ? -9.200  36.547  112.877 1.00 29.59 ? 150  VAL   B CA    1 
ATOM   9977  C  C     . VAL   B  1  152  ? -10.234 37.643  113.104 1.00 30.18 ? 150  VAL   B C     1 
ATOM   9978  O  O     . VAL   B  1  152  ? -11.368 37.374  113.515 1.00 29.90 ? 150  VAL   B O     1 
ATOM   9979  C  CB    . VAL   B  1  152  ? -8.209  36.463  114.052 1.00 26.19 ? 150  VAL   B CB    1 
ATOM   9980  C  CG1   . VAL   B  1  152  ? -8.962  36.503  115.377 1.00 32.24 ? 150  VAL   B CG1   1 
ATOM   9981  C  CG2   . VAL   B  1  152  ? -7.370  35.215  113.942 1.00 31.85 ? 150  VAL   B CG2   1 
ATOM   9982  N  N     . VAL   B  1  153  ? -9.858  38.892  112.844 1.00 25.75 ? 151  VAL   B N     1 
ATOM   9983  C  CA    . VAL   B  1  153  ? -10.698 40.029  113.203 1.00 27.23 ? 151  VAL   B CA    1 
ATOM   9984  C  C     . VAL   B  1  153  ? -11.788 40.267  112.163 1.00 27.07 ? 151  VAL   B C     1 
ATOM   9985  O  O     . VAL   B  1  153  ? -12.939 40.544  112.511 1.00 30.76 ? 151  VAL   B O     1 
ATOM   9986  C  CB    . VAL   B  1  153  ? -9.807  41.269  113.399 1.00 28.06 ? 151  VAL   B CB    1 
ATOM   9987  C  CG1   . VAL   B  1  153  ? -10.648 42.535  113.540 1.00 27.67 ? 151  VAL   B CG1   1 
ATOM   9988  C  CG2   . VAL   B  1  153  ? -8.896  41.072  114.600 1.00 24.53 ? 151  VAL   B CG2   1 
ATOM   9989  N  N     . THR   B  1  154  ? -11.441 40.189  110.879 1.00 26.21 ? 152  THR   B N     1 
ATOM   9990  C  CA    . THR   B  1  154  ? -12.334 40.591  109.800 1.00 29.32 ? 152  THR   B CA    1 
ATOM   9991  C  C     . THR   B  1  154  ? -12.809 39.435  108.940 1.00 31.75 ? 152  THR   B C     1 
ATOM   9992  O  O     . THR   B  1  154  ? -13.704 39.632  108.116 1.00 35.12 ? 152  THR   B O     1 
ATOM   9993  C  CB    . THR   B  1  154  ? -11.627 41.582  108.866 1.00 30.14 ? 152  THR   B CB    1 
ATOM   9994  O  OG1   . THR   B  1  154  ? -10.719 40.860  108.023 1.00 30.99 ? 152  THR   B OG1   1 
ATOM   9995  C  CG2   . THR   B  1  154  ? -10.857 42.616  109.659 1.00 32.08 ? 152  THR   B CG2   1 
ATOM   9996  N  N     . GLY   B  1  155  ? -12.215 38.257  109.075 1.00 28.54 ? 153  GLY   B N     1 
ATOM   9997  C  CA    . GLY   B  1  155  ? -12.547 37.153  108.202 1.00 31.46 ? 153  GLY   B CA    1 
ATOM   9998  C  C     . GLY   B  1  155  ? -11.978 37.257  106.809 1.00 33.12 ? 153  GLY   B C     1 
ATOM   9999  O  O     . GLY   B  1  155  ? -12.252 36.380  105.979 1.00 34.78 ? 153  GLY   B O     1 
ATOM   10000 N  N     . LYS   B  1  156  ? -11.202 38.292  106.518 1.00 30.16 ? 154  LYS   B N     1 
ATOM   10001 C  CA    . LYS   B  1  156  ? -10.598 38.474  105.209 1.00 32.65 ? 154  LYS   B CA    1 
ATOM   10002 C  C     . LYS   B  1  156  ? -9.088  38.349  105.332 1.00 33.08 ? 154  LYS   B C     1 
ATOM   10003 O  O     . LYS   B  1  156  ? -8.496  38.734  106.344 1.00 30.36 ? 154  LYS   B O     1 
ATOM   10004 C  CB    . LYS   B  1  156  ? -10.954 39.845  104.628 1.00 36.44 ? 154  LYS   B CB    1 
ATOM   10005 N  N     . LEU   B  1  157  ? -8.468  37.802  104.293 1.00 29.84 ? 155  LEU   B N     1 
ATOM   10006 C  CA    . LEU   B  1  157  ? -7.030  37.609  104.251 1.00 30.41 ? 155  LEU   B CA    1 
ATOM   10007 C  C     . LEU   B  1  157  ? -6.445  38.536  103.200 1.00 37.81 ? 155  LEU   B C     1 
ATOM   10008 O  O     . LEU   B  1  157  ? -6.940  38.591  102.071 1.00 42.64 ? 155  LEU   B O     1 
ATOM   10009 C  CB    . LEU   B  1  157  ? -6.687  36.160  103.900 1.00 34.65 ? 155  LEU   B CB    1 
ATOM   10010 N  N     . THR   B  1  158  ? -5.412  39.276  103.575 1.00 41.30 ? 156  THR   B N     1 
ATOM   10011 C  CA    . THR   B  1  158  ? -4.573  39.970  102.613 1.00 39.50 ? 156  THR   B CA    1 
ATOM   10012 C  C     . THR   B  1  158  ? -3.196  39.325  102.621 1.00 36.85 ? 156  THR   B C     1 
ATOM   10013 O  O     . THR   B  1  158  ? -2.793  38.681  103.594 1.00 39.51 ? 156  THR   B O     1 
ATOM   10014 C  CB    . THR   B  1  158  ? -4.442  41.454  102.957 1.00 42.31 ? 156  THR   B CB    1 
ATOM   10015 O  OG1   . THR   B  1  158  ? -3.671  41.593  104.158 1.00 45.84 ? 156  THR   B OG1   1 
ATOM   10016 C  CG2   . THR   B  1  158  ? -5.814  42.077  103.159 1.00 44.39 ? 156  THR   B CG2   1 
ATOM   10017 N  N     . SER   B  1  159  ? -2.472  39.498  101.520 1.00 32.64 ? 157  SER   B N     1 
ATOM   10018 C  CA    . SER   B  1  159  ? -1.146  38.904  101.430 1.00 33.53 ? 157  SER   B CA    1 
ATOM   10019 C  C     . SER   B  1  159  ? -0.104  39.748  102.147 1.00 33.84 ? 157  SER   B C     1 
ATOM   10020 O  O     . SER   B  1  159  ? 0.861   39.210  102.701 1.00 32.20 ? 157  SER   B O     1 
ATOM   10021 C  CB    . SER   B  1  159  ? -0.754  38.727  99.964  1.00 36.96 ? 157  SER   B CB    1 
ATOM   10022 O  OG    . SER   B  1  159  ? -1.321  39.761  99.176  1.00 42.62 ? 157  SER   B OG    1 
ATOM   10023 N  N     . THR   B  1  160  ? -0.281  41.060  102.145 1.00 29.81 ? 158  THR   B N     1 
ATOM   10024 C  CA    . THR   B  1  160  ? 0.638   41.966  102.802 1.00 22.96 ? 158  THR   B CA    1 
ATOM   10025 C  C     . THR   B  1  160  ? -0.154  42.882  103.720 1.00 22.64 ? 158  THR   B C     1 
ATOM   10026 O  O     . THR   B  1  160  ? -1.384  42.954  103.662 1.00 27.68 ? 158  THR   B O     1 
ATOM   10027 C  CB    . THR   B  1  160  ? 1.438   42.788  101.780 1.00 25.13 ? 158  THR   B CB    1 
ATOM   10028 O  OG1   . THR   B  1  160  ? 0.527   43.531  100.967 1.00 31.94 ? 158  THR   B OG1   1 
ATOM   10029 C  CG2   . THR   B  1  160  ? 2.292   41.881  100.907 1.00 28.43 ? 158  THR   B CG2   1 
ATOM   10030 N  N     . VAL   B  1  161  ? 0.587   43.605  104.551 1.00 18.37 ? 159  VAL   B N     1 
ATOM   10031 C  CA    . VAL   B  1  161  ? 0.079   44.292  105.724 1.00 21.36 ? 159  VAL   B CA    1 
ATOM   10032 C  C     . VAL   B  1  161  ? 0.281   45.780  105.498 1.00 20.90 ? 159  VAL   B C     1 
ATOM   10033 O  O     . VAL   B  1  161  ? 1.370   46.203  105.093 1.00 18.85 ? 159  VAL   B O     1 
ATOM   10034 C  CB    . VAL   B  1  161  ? 0.872   43.807  106.954 1.00 24.50 ? 159  VAL   B CB    1 
ATOM   10035 C  CG1   . VAL   B  1  161  ? 0.797   44.776  108.088 1.00 29.37 ? 159  VAL   B CG1   1 
ATOM   10036 C  CG2   . VAL   B  1  161  ? 0.389   42.414  107.361 1.00 32.19 ? 159  VAL   B CG2   1 
ATOM   10037 N  N     . ASN   B  1  162  ? -0.765  46.572  105.727 1.00 18.01 ? 160  ASN   B N     1 
ATOM   10038 C  CA    . ASN   B  1  162  ? -0.578  48.020  105.678 1.00 18.95 ? 160  ASN   B CA    1 
ATOM   10039 C  C     . ASN   B  1  162  ? -0.084  48.457  107.050 1.00 18.96 ? 160  ASN   B C     1 
ATOM   10040 O  O     . ASN   B  1  162  ? -0.858  48.777  107.954 1.00 18.67 ? 160  ASN   B O     1 
ATOM   10041 C  CB    . ASN   B  1  162  ? -1.838  48.753  105.250 1.00 21.52 ? 160  ASN   B CB    1 
ATOM   10042 C  CG    . ASN   B  1  162  ? -1.616  50.252  105.130 1.00 20.77 ? 160  ASN   B CG    1 
ATOM   10043 O  OD1   . ASN   B  1  162  ? -0.684  50.795  105.719 1.00 19.60 ? 160  ASN   B OD1   1 
ATOM   10044 N  ND2   . ASN   B  1  162  ? -2.469  50.924  104.375 1.00 22.09 ? 160  ASN   B ND2   1 
ATOM   10045 N  N     . ASP   B  1  163  ? 1.242   48.459  107.201 1.00 18.74 ? 161  ASP   B N     1 
ATOM   10046 C  CA    . ASP   B  1  163  ? 1.840   48.733  108.498 1.00 15.79 ? 161  ASP   B CA    1 
ATOM   10047 C  C     . ASP   B  1  163  ? 1.703   50.182  108.917 1.00 17.16 ? 161  ASP   B C     1 
ATOM   10048 O  O     . ASP   B  1  163  ? 1.722   50.469  110.113 1.00 18.17 ? 161  ASP   B O     1 
ATOM   10049 C  CB    . ASP   B  1  163  ? 3.302   48.283  108.535 1.00 17.58 ? 161  ASP   B CB    1 
ATOM   10050 C  CG    . ASP   B  1  163  ? 4.113   48.774  107.345 1.00 22.80 ? 161  ASP   B CG    1 
ATOM   10051 O  OD1   . ASP   B  1  163  ? 3.634   48.706  106.197 1.00 19.65 ? 161  ASP   B OD1   1 
ATOM   10052 O  OD2   . ASP   B  1  163  ? 5.261   49.207  107.577 1.00 24.30 ? 161  ASP   B OD2   1 
ATOM   10053 N  N     . ARG   B  1  164  ? 1.561   51.107  107.969 1.00 17.33 ? 162  ARG   B N     1 
ATOM   10054 C  CA    . ARG   B  1  164  ? 1.298   52.479  108.370 1.00 15.37 ? 162  ARG   B CA    1 
ATOM   10055 C  C     . ARG   B  1  164  ? -0.110  52.631  108.932 1.00 16.00 ? 162  ARG   B C     1 
ATOM   10056 O  O     . ARG   B  1  164  ? -0.318  53.348  109.918 1.00 16.44 ? 162  ARG   B O     1 
ATOM   10057 C  CB    . ARG   B  1  164  ? 1.528   53.424  107.193 1.00 17.37 ? 162  ARG   B CB    1 
ATOM   10058 C  CG    . ARG   B  1  164  ? 2.979   53.464  106.721 1.00 17.81 ? 162  ARG   B CG    1 
ATOM   10059 C  CD    . ARG   B  1  164  ? 3.956   53.553  107.874 1.00 22.83 ? 162  ARG   B CD    1 
ATOM   10060 N  NE    . ARG   B  1  164  ? 3.681   54.696  108.728 1.00 30.53 ? 162  ARG   B NE    1 
ATOM   10061 C  CZ    . ARG   B  1  164  ? 4.075   54.798  109.989 1.00 33.14 ? 162  ARG   B CZ    1 
ATOM   10062 N  NH1   . ARG   B  1  164  ? 4.769   53.834  110.579 1.00 36.65 ? 162  ARG   B NH1   1 
ATOM   10063 N  NH2   . ARG   B  1  164  ? 3.765   55.893  110.675 1.00 31.91 ? 162  ARG   B NH2   1 
ATOM   10064 N  N     . SER   B  1  165  ? -1.088  51.973  108.303 1.00 16.21 ? 163  SER   B N     1 
ATOM   10065 C  CA    . SER   B  1  165  ? -2.455  52.002  108.815 1.00 15.89 ? 163  SER   B CA    1 
ATOM   10066 C  C     . SER   B  1  165  ? -2.539  51.339  110.185 1.00 17.17 ? 163  SER   B C     1 
ATOM   10067 O  O     . SER   B  1  165  ? -3.251  51.815  111.077 1.00 16.48 ? 163  SER   B O     1 
ATOM   10068 C  CB    . SER   B  1  165  ? -3.363  51.268  107.832 1.00 16.74 ? 163  SER   B CB    1 
ATOM   10069 O  OG    . SER   B  1  165  ? -4.666  51.091  108.355 1.00 18.97 ? 163  SER   B OG    1 
ATOM   10070 N  N     . LEU   B  1  166  ? -1.829  50.226  110.357 1.00 17.36 ? 164  LEU   B N     1 
ATOM   10071 C  CA    . LEU   B  1  166  ? -1.848  49.533  111.639 1.00 17.72 ? 164  LEU   B CA    1 
ATOM   10072 C  C     . LEU   B  1  166  ? -1.148  50.346  112.716 1.00 18.95 ? 164  LEU   B C     1 
ATOM   10073 O  O     . LEU   B  1  166  ? -1.607  50.381  113.859 1.00 17.48 ? 164  LEU   B O     1 
ATOM   10074 C  CB    . LEU   B  1  166  ? -1.196  48.164  111.488 1.00 17.24 ? 164  LEU   B CB    1 
ATOM   10075 C  CG    . LEU   B  1  166  ? -2.112  47.229  110.716 1.00 17.60 ? 164  LEU   B CG    1 
ATOM   10076 C  CD1   . LEU   B  1  166  ? -1.378  45.964  110.398 1.00 20.97 ? 164  LEU   B CD1   1 
ATOM   10077 C  CD2   . LEU   B  1  166  ? -3.386  46.936  111.525 1.00 16.80 ? 164  LEU   B CD2   1 
ATOM   10078 N  N     . ALA   B  1  167  ? -0.014  50.971  112.381 1.00 16.49 ? 165  ALA   B N     1 
ATOM   10079 C  CA    . ALA   B  1  167  ? 0.670   51.822  113.349 1.00 17.05 ? 165  ALA   B CA    1 
ATOM   10080 C  C     . ALA   B  1  167  ? -0.229  52.969  113.789 1.00 19.35 ? 165  ALA   B C     1 
ATOM   10081 O  O     . ALA   B  1  167  ? -0.337  53.271  114.977 1.00 18.73 ? 165  ALA   B O     1 
ATOM   10082 C  CB    . ALA   B  1  167  ? 1.969   52.352  112.744 1.00 20.63 ? 165  ALA   B CB    1 
ATOM   10083 N  N     . ALA   B  1  168  ? -0.906  53.606  112.827 1.00 18.17 ? 166  ALA   B N     1 
ATOM   10084 C  CA    . ALA   B  1  168  ? -1.853  54.663  113.141 1.00 18.31 ? 166  ALA   B CA    1 
ATOM   10085 C  C     . ALA   B  1  168  ? -2.980  54.144  114.022 1.00 16.79 ? 166  ALA   B C     1 
ATOM   10086 O  O     . ALA   B  1  168  ? -3.376  54.798  114.984 1.00 17.36 ? 166  ALA   B O     1 
ATOM   10087 C  CB    . ALA   B  1  168  ? -2.436  55.194  111.832 1.00 19.15 ? 166  ALA   B CB    1 
ATOM   10088 N  N     . ALA   B  1  169  ? -3.508  52.963  113.691 1.00 17.34 ? 167  ALA   B N     1 
ATOM   10089 C  CA    . ALA   B  1  169  ? -4.613  52.402  114.461 1.00 17.21 ? 167  ALA   B CA    1 
ATOM   10090 C  C     . ALA   B  1  169  ? -4.182  52.082  115.885 1.00 19.02 ? 167  ALA   B C     1 
ATOM   10091 O  O     . ALA   B  1  169  ? -4.931  52.317  116.835 1.00 17.85 ? 167  ALA   B O     1 
ATOM   10092 C  CB    . ALA   B  1  169  ? -5.113  51.135  113.771 1.00 18.06 ? 167  ALA   B CB    1 
ATOM   10093 N  N     . LEU   B  1  170  ? -2.974  51.549  116.053 1.00 18.38 ? 168  LEU   B N     1 
ATOM   10094 C  CA    . LEU   B  1  170  ? -2.524  51.204  117.398 1.00 17.83 ? 168  LEU   B CA    1 
ATOM   10095 C  C     . LEU   B  1  170  ? -2.292  52.451  118.236 1.00 19.53 ? 168  LEU   B C     1 
ATOM   10096 O  O     . LEU   B  1  170  ? -2.690  52.507  119.405 1.00 19.00 ? 168  LEU   B O     1 
ATOM   10097 C  CB    . LEU   B  1  170  ? -1.255  50.368  117.322 1.00 18.76 ? 168  LEU   B CB    1 
ATOM   10098 C  CG    . LEU   B  1  170  ? -0.734  49.852  118.658 1.00 19.07 ? 168  LEU   B CG    1 
ATOM   10099 C  CD1   . LEU   B  1  170  ? -1.785  49.011  119.365 1.00 20.75 ? 168  LEU   B CD1   1 
ATOM   10100 C  CD2   . LEU   B  1  170  ? 0.509   49.059  118.383 1.00 22.53 ? 168  LEU   B CD2   1 
ATOM   10101 N  N     . THR   B  1  171  ? -1.649  53.463  117.658 1.00 18.90 ? 169  THR   B N     1 
ATOM   10102 C  CA    . THR   B  1  171  ? -1.525  54.733  118.359 1.00 19.12 ? 169  THR   B CA    1 
ATOM   10103 C  C     . THR   B  1  171  ? -2.890  55.286  118.744 1.00 20.63 ? 169  THR   B C     1 
ATOM   10104 O  O     . THR   B  1  171  ? -3.092  55.757  119.870 1.00 20.05 ? 169  THR   B O     1 
ATOM   10105 C  CB    . THR   B  1  171  ? -0.791  55.730  117.474 1.00 20.18 ? 169  THR   B CB    1 
ATOM   10106 O  OG1   . THR   B  1  171  ? 0.533   55.244  117.223 1.00 23.42 ? 169  THR   B OG1   1 
ATOM   10107 C  CG2   . THR   B  1  171  ? -0.720  57.082  118.146 1.00 22.73 ? 169  THR   B CG2   1 
ATOM   10108 N  N     . ARG   B  1  172  ? -3.844  55.230  117.815 1.00 19.34 ? 170  ARG   B N     1 
ATOM   10109 C  CA    . ARG   B  1  172  ? -5.154  55.796  118.080 1.00 19.53 ? 170  ARG   B CA    1 
ATOM   10110 C  C     . ARG   B  1  172  ? -5.847  55.046  119.205 1.00 20.29 ? 170  ARG   B C     1 
ATOM   10111 O  O     . ARG   B  1  172  ? -6.407  55.650  120.120 1.00 20.29 ? 170  ARG   B O     1 
ATOM   10112 C  CB    . ARG   B  1  172  ? -5.999  55.755  116.812 1.00 19.40 ? 170  ARG   B CB    1 
ATOM   10113 C  CG    . ARG   B  1  172  ? -7.278  56.552  116.932 1.00 18.83 ? 170  ARG   B CG    1 
ATOM   10114 C  CD    . ARG   B  1  172  ? -8.161  56.421  115.687 1.00 21.04 ? 170  ARG   B CD    1 
ATOM   10115 N  NE    . ARG   B  1  172  ? -7.417  56.525  114.438 1.00 18.21 ? 170  ARG   B NE    1 
ATOM   10116 C  CZ    . ARG   B  1  172  ? -7.115  55.495  113.660 1.00 17.74 ? 170  ARG   B CZ    1 
ATOM   10117 N  NH1   . ARG   B  1  172  ? -7.439  54.254  113.991 1.00 19.47 ? 170  ARG   B NH1   1 
ATOM   10118 N  NH2   . ARG   B  1  172  ? -6.461  55.710  112.522 1.00 17.39 ? 170  ARG   B NH2   1 
ATOM   10119 N  N     . LEU   B  1  173  ? -5.795  53.717  119.167 1.00 19.16 ? 171  LEU   B N     1 
ATOM   10120 C  CA    . LEU   B  1  173  ? -6.530  52.966  120.175 1.00 20.36 ? 171  LEU   B CA    1 
ATOM   10121 C  C     . LEU   B  1  173  ? -5.895  53.108  121.550 1.00 20.29 ? 171  LEU   B C     1 
ATOM   10122 O  O     . LEU   B  1  173  ? -6.604  53.191  122.552 1.00 21.36 ? 171  LEU   B O     1 
ATOM   10123 C  CB    . LEU   B  1  173  ? -6.671  51.502  119.755 1.00 20.51 ? 171  LEU   B CB    1 
ATOM   10124 C  CG    . LEU   B  1  173  ? -5.487  50.542  119.850 1.00 22.42 ? 171  LEU   B CG    1 
ATOM   10125 C  CD1   . LEU   B  1  173  ? -5.443  49.893  121.239 1.00 25.43 ? 171  LEU   B CD1   1 
ATOM   10126 C  CD2   . LEU   B  1  173  ? -5.593  49.485  118.769 1.00 22.89 ? 171  LEU   B CD2   1 
ATOM   10127 N  N     . ILE   B  1  174  ? -4.564  53.134  121.621 1.00 19.83 ? 172  ILE   B N     1 
ATOM   10128 C  CA    . ILE   B  1  174  ? -3.931  53.279  122.925 1.00 19.32 ? 172  ILE   B CA    1 
ATOM   10129 C  C     . ILE   B  1  174  ? -4.186  54.667  123.482 1.00 22.37 ? 172  ILE   B C     1 
ATOM   10130 O  O     . ILE   B  1  174  ? -4.508  54.827  124.665 1.00 23.38 ? 172  ILE   B O     1 
ATOM   10131 C  CB    . ILE   B  1  174  ? -2.430  52.960  122.839 1.00 20.63 ? 172  ILE   B CB    1 
ATOM   10132 C  CG1   . ILE   B  1  174  ? -2.214  51.490  122.481 1.00 21.09 ? 172  ILE   B CG1   1 
ATOM   10133 C  CG2   . ILE   B  1  174  ? -1.745  53.337  124.151 1.00 23.25 ? 172  ILE   B CG2   1 
ATOM   10134 C  CD1   . ILE   B  1  174  ? -0.775  51.150  122.170 1.00 24.45 ? 172  ILE   B CD1   1 
ATOM   10135 N  N     . SER   B  1  175  ? -4.056  55.692  122.637 1.00 21.17 ? 173  SER   B N     1 
ATOM   10136 C  CA    . SER   B  1  175  ? -4.299  57.048  123.104 1.00 21.22 ? 173  SER   B CA    1 
ATOM   10137 C  C     . SER   B  1  175  ? -5.757  57.258  123.490 1.00 22.96 ? 173  SER   B C     1 
ATOM   10138 O  O     . SER   B  1  175  ? -6.053  58.130  124.303 1.00 27.21 ? 173  SER   B O     1 
ATOM   10139 C  CB    . SER   B  1  175  ? -3.891  58.062  122.038 1.00 24.84 ? 173  SER   B CB    1 
ATOM   10140 O  OG    . SER   B  1  175  ? -2.496  58.025  121.803 1.00 30.59 ? 173  SER   B OG    1 
ATOM   10141 N  N     . ARG   B  1  176  ? -6.675  56.487  122.909 1.00 21.61 ? 174  ARG   B N     1 
ATOM   10142 C  CA    . ARG   B  1  176  ? -8.087  56.633  123.247 1.00 22.33 ? 174  ARG   B CA    1 
ATOM   10143 C  C     . ARG   B  1  176  ? -8.466  55.811  124.480 1.00 23.30 ? 174  ARG   B C     1 
ATOM   10144 O  O     . ARG   B  1  176  ? -9.199  56.294  125.350 1.00 25.50 ? 174  ARG   B O     1 
ATOM   10145 C  CB    . ARG   B  1  176  ? -8.938  56.223  122.036 1.00 24.28 ? 174  ARG   B CB    1 
ATOM   10146 C  CG    . ARG   B  1  176  ? -10.435 56.522  122.155 1.00 23.03 ? 174  ARG   B CG    1 
ATOM   10147 C  CD    . ARG   B  1  176  ? -11.143 56.181  120.837 1.00 23.31 ? 174  ARG   B CD    1 
ATOM   10148 N  NE    . ARG   B  1  176  ? -11.280 54.742  120.623 1.00 23.25 ? 174  ARG   B NE    1 
ATOM   10149 C  CZ    . ARG   B  1  176  ? -10.709 54.044  119.650 1.00 26.02 ? 174  ARG   B CZ    1 
ATOM   10150 N  NH1   . ARG   B  1  176  ? -9.960  54.621  118.709 1.00 23.50 ? 174  ARG   B NH1   1 
ATOM   10151 N  NH2   . ARG   B  1  176  ? -10.903 52.727  119.604 1.00 29.51 ? 174  ARG   B NH2   1 
ATOM   10152 N  N     . CYS   B  1  177  ? -7.982  54.567  124.571 1.00 24.37 ? 175  CYS   B N     1 
ATOM   10153 C  CA    . CYS   B  1  177  ? -8.477  53.626  125.569 1.00 24.61 ? 175  CYS   B CA    1 
ATOM   10154 C  C     . CYS   B  1  177  ? -7.453  53.203  126.609 1.00 28.96 ? 175  CYS   B C     1 
ATOM   10155 O  O     . CYS   B  1  177  ? -7.849  52.639  127.634 1.00 30.37 ? 175  CYS   B O     1 
ATOM   10156 C  CB    . CYS   B  1  177  ? -9.032  52.367  124.893 1.00 26.96 ? 175  CYS   B CB    1 
ATOM   10157 S  SG    . CYS   B  1  177  ? -10.335 52.696  123.674 1.00 34.08 ? 175  CYS   B SG    1 
ATOM   10158 N  N     . GLY   B  1  178  ? -6.164  53.422  126.367 1.00 25.67 ? 176  GLY   B N     1 
ATOM   10159 C  CA    . GLY   B  1  178  ? -5.196  53.253  127.442 1.00 27.37 ? 176  GLY   B CA    1 
ATOM   10160 C  C     . GLY   B  1  178  ? -4.943  51.806  127.841 1.00 25.97 ? 176  GLY   B C     1 
ATOM   10161 O  O     . GLY   B  1  178  ? -5.182  50.857  127.091 1.00 26.25 ? 176  GLY   B O     1 
ATOM   10162 N  N     . GLU   B  1  179  ? -4.430  51.657  129.061 1.00 29.32 ? 177  GLU   B N     1 
ATOM   10163 C  CA    . GLU   B  1  179  ? -4.108  50.333  129.585 1.00 31.75 ? 177  GLU   B CA    1 
ATOM   10164 C  C     . GLU   B  1  179  ? -5.266  49.337  129.558 1.00 25.43 ? 177  GLU   B C     1 
ATOM   10165 O  O     . GLU   B  1  179  ? -5.019  48.166  129.221 1.00 28.04 ? 177  GLU   B O     1 
ATOM   10166 C  CB    . GLU   B  1  179  ? -3.494  50.445  130.989 1.00 31.82 ? 177  GLU   B CB    1 
ATOM   10167 C  CG    . GLU   B  1  179  ? -2.915  49.128  131.476 1.00 34.99 ? 177  GLU   B CG    1 
ATOM   10168 C  CD    . GLU   B  1  179  ? -2.529  49.141  132.939 1.00 46.58 ? 177  GLU   B CD    1 
ATOM   10169 O  OE1   . GLU   B  1  179  ? -2.262  50.233  133.487 1.00 49.72 ? 177  GLU   B OE1   1 
ATOM   10170 O  OE2   . GLU   B  1  179  ? -2.500  48.048  133.541 1.00 51.22 ? 177  GLU   B OE2   1 
ATOM   10171 N  N     . PRO   B  1  180  ? -6.515  49.702  129.883 1.00 26.09 ? 178  PRO   B N     1 
ATOM   10172 C  CA    . PRO   B  1  180  ? -7.579  48.682  129.876 1.00 28.36 ? 178  PRO   B CA    1 
ATOM   10173 C  C     . PRO   B  1  180  ? -7.739  47.937  128.557 1.00 29.93 ? 178  PRO   B C     1 
ATOM   10174 O  O     . PRO   B  1  180  ? -8.000  46.729  128.577 1.00 30.37 ? 178  PRO   B O     1 
ATOM   10175 C  CB    . PRO   B  1  180  ? -8.835  49.474  130.266 1.00 32.23 ? 178  PRO   B CB    1 
ATOM   10176 C  CG    . PRO   B  1  180  ? -8.313  50.591  131.093 1.00 29.81 ? 178  PRO   B CG    1 
ATOM   10177 C  CD    . PRO   B  1  180  ? -7.006  50.976  130.439 1.00 28.59 ? 178  PRO   B CD    1 
ATOM   10178 N  N     . VAL   B  1  181  ? -7.589  48.603  127.407 1.00 25.08 ? 179  VAL   B N     1 
ATOM   10179 C  CA    . VAL   B  1  181  ? -7.755  47.866  126.163 1.00 24.30 ? 179  VAL   B CA    1 
ATOM   10180 C  C     . VAL   B  1  181  ? -6.559  46.961  125.904 1.00 24.95 ? 179  VAL   B C     1 
ATOM   10181 O  O     . VAL   B  1  181  ? -6.708  45.881  125.320 1.00 26.27 ? 179  VAL   B O     1 
ATOM   10182 C  CB    . VAL   B  1  181  ? -8.058  48.793  124.966 1.00 24.08 ? 179  VAL   B CB    1 
ATOM   10183 C  CG1   . VAL   B  1  181  ? -6.827  49.597  124.571 1.00 25.90 ? 179  VAL   B CG1   1 
ATOM   10184 C  CG2   . VAL   B  1  181  ? -8.545  47.973  123.782 1.00 26.77 ? 179  VAL   B CG2   1 
ATOM   10185 N  N     . ILE   B  1  182  ? -5.359  47.383  126.313 1.00 24.10 ? 180  ILE   B N     1 
ATOM   10186 C  CA    . ILE   B  1  182  ? -4.178  46.543  126.141 1.00 24.84 ? 180  ILE   B CA    1 
ATOM   10187 C  C     . ILE   B  1  182  ? -4.313  45.282  126.978 1.00 27.68 ? 180  ILE   B C     1 
ATOM   10188 O  O     . ILE   B  1  182  ? -4.054  44.167  126.503 1.00 25.62 ? 180  ILE   B O     1 
ATOM   10189 C  CB    . ILE   B  1  182  ? -2.900  47.322  126.500 1.00 26.33 ? 180  ILE   B CB    1 
ATOM   10190 C  CG1   . ILE   B  1  182  ? -2.757  48.563  125.622 1.00 24.38 ? 180  ILE   B CG1   1 
ATOM   10191 C  CG2   . ILE   B  1  182  ? -1.675  46.424  126.327 1.00 24.52 ? 180  ILE   B CG2   1 
ATOM   10192 C  CD1   . ILE   B  1  182  ? -1.716  49.542  126.141 1.00 27.90 ? 180  ILE   B CD1   1 
ATOM   10193 N  N     . ARG   B  1  183  ? -4.724  45.446  128.240 1.00 30.07 ? 181  ARG   B N     1 
ATOM   10194 C  CA    . ARG   B  1  183  ? -4.946  44.303  129.120 1.00 30.83 ? 181  ARG   B CA    1 
ATOM   10195 C  C     . ARG   B  1  183  ? -5.964  43.338  128.523 1.00 30.70 ? 181  ARG   B C     1 
ATOM   10196 O  O     . ARG   B  1  183  ? -5.727  42.126  128.470 1.00 32.19 ? 181  ARG   B O     1 
ATOM   10197 C  CB    . ARG   B  1  183  ? -5.384  44.798  130.500 1.00 30.62 ? 181  ARG   B CB    1 
ATOM   10198 C  CG    . ARG   B  1  183  ? -6.160  43.783  131.327 1.00 39.99 ? 181  ARG   B CG    1 
ATOM   10199 C  CD    . ARG   B  1  183  ? -5.251  42.925  132.199 1.00 46.54 ? 181  ARG   B CD    1 
ATOM   10200 N  NE    . ARG   B  1  183  ? -4.362  42.064  131.428 1.00 44.90 ? 181  ARG   B NE    1 
ATOM   10201 C  CZ    . ARG   B  1  183  ? -3.039  42.162  131.430 1.00 44.47 ? 181  ARG   B CZ    1 
ATOM   10202 N  NH1   . ARG   B  1  183  ? -2.415  43.079  132.150 1.00 47.56 ? 181  ARG   B NH1   1 
ATOM   10203 N  NH2   . ARG   B  1  183  ? -2.325  41.312  130.699 1.00 41.70 ? 181  ARG   B NH2   1 
ATOM   10204 N  N     . ARG   B  1  184  ? -7.097  43.862  128.046 1.00 29.83 ? 182  ARG   B N     1 
ATOM   10205 C  CA    . ARG   B  1  184  ? -8.112  43.007  127.429 1.00 31.09 ? 182  ARG   B CA    1 
ATOM   10206 C  C     . ARG   B  1  184  ? -7.582  42.318  126.177 1.00 32.24 ? 182  ARG   B C     1 
ATOM   10207 O  O     . ARG   B  1  184  ? -7.884  41.144  125.931 1.00 30.83 ? 182  ARG   B O     1 
ATOM   10208 C  CB    . ARG   B  1  184  ? -9.363  43.823  127.099 1.00 32.77 ? 182  ARG   B CB    1 
ATOM   10209 C  CG    . ARG   B  1  184  ? -10.278 44.080  128.287 1.00 38.16 ? 182  ARG   B CG    1 
ATOM   10210 C  CD    . ARG   B  1  184  ? -11.264 42.936  128.504 1.00 39.18 ? 182  ARG   B CD    1 
ATOM   10211 N  NE    . ARG   B  1  184  ? -12.469 43.072  127.690 1.00 40.17 ? 182  ARG   B NE    1 
ATOM   10212 C  CZ    . ARG   B  1  184  ? -12.908 42.167  126.823 1.00 40.43 ? 182  ARG   B CZ    1 
ATOM   10213 N  NH1   . ARG   B  1  184  ? -12.265 41.025  126.624 1.00 40.80 ? 182  ARG   B NH1   1 
ATOM   10214 N  NH2   . ARG   B  1  184  ? -14.022 42.413  126.138 1.00 43.35 ? 182  ARG   B NH2   1 
ATOM   10215 N  N     . GLY   B  1  185  ? -6.807  43.035  125.360 1.00 28.88 ? 183  GLY   B N     1 
ATOM   10216 C  CA    . GLY   B  1  185  ? -6.233  42.413  124.181 1.00 24.94 ? 183  GLY   B CA    1 
ATOM   10217 C  C     . GLY   B  1  185  ? -5.265  41.299  124.528 1.00 28.16 ? 183  GLY   B C     1 
ATOM   10218 O  O     . GLY   B  1  185  ? -5.280  40.234  123.905 1.00 27.63 ? 183  GLY   B O     1 
ATOM   10219 N  N     . VAL   B  1  186  ? -4.417  41.527  125.532 1.00 24.24 ? 184  VAL   B N     1 
ATOM   10220 C  CA    . VAL   B  1  186  ? -3.457  40.506  125.943 1.00 28.53 ? 184  VAL   B CA    1 
ATOM   10221 C  C     . VAL   B  1  186  ? -4.183  39.271  126.459 1.00 29.18 ? 184  VAL   B C     1 
ATOM   10222 O  O     . VAL   B  1  186  ? -3.864  38.136  126.082 1.00 29.63 ? 184  VAL   B O     1 
ATOM   10223 C  CB    . VAL   B  1  186  ? -2.478  41.080  126.979 1.00 26.11 ? 184  VAL   B CB    1 
ATOM   10224 C  CG1   . VAL   B  1  186  ? -1.721  39.956  127.687 1.00 27.53 ? 184  VAL   B CG1   1 
ATOM   10225 C  CG2   . VAL   B  1  186  ? -1.512  42.037  126.302 1.00 29.52 ? 184  VAL   B CG2   1 
ATOM   10226 N  N     . ASP   B  1  187  ? -5.173  39.475  127.329 1.00 30.45 ? 185  ASP   B N     1 
ATOM   10227 C  CA    . ASP   B  1  187  ? -5.947  38.349  127.843 1.00 32.00 ? 185  ASP   B CA    1 
ATOM   10228 C  C     . ASP   B  1  187  ? -6.645  37.603  126.717 1.00 35.09 ? 185  ASP   B C     1 
ATOM   10229 O  O     . ASP   B  1  187  ? -6.664  36.367  126.702 1.00 29.85 ? 185  ASP   B O     1 
ATOM   10230 C  CB    . ASP   B  1  187  ? -6.947  38.836  128.889 1.00 33.78 ? 185  ASP   B CB    1 
ATOM   10231 C  CG    . ASP   B  1  187  ? -6.261  39.312  130.158 1.00 41.96 ? 185  ASP   B CG    1 
ATOM   10232 O  OD1   . ASP   B  1  187  ? -5.123  38.861  130.414 1.00 46.25 ? 185  ASP   B OD1   1 
ATOM   10233 O  OD2   . ASP   B  1  187  ? -6.847  40.134  130.892 1.00 41.44 ? 185  ASP   B OD2   1 
ATOM   10234 N  N     . MET   B  1  188  ? -7.202  38.339  125.753 1.00 32.80 ? 186  MET   B N     1 
ATOM   10235 C  CA    . MET   B  1  188  ? -7.850  37.711  124.606 1.00 31.71 ? 186  MET   B CA    1 
ATOM   10236 C  C     . MET   B  1  188  ? -6.858  36.878  123.803 1.00 31.93 ? 186  MET   B C     1 
ATOM   10237 O  O     . MET   B  1  188  ? -7.126  35.717  123.471 1.00 34.33 ? 186  MET   B O     1 
ATOM   10238 C  CB    . MET   B  1  188  ? -8.461  38.796  123.723 1.00 35.54 ? 186  MET   B CB    1 
ATOM   10239 C  CG    . MET   B  1  188  ? -9.268  38.277  122.558 1.00 39.33 ? 186  MET   B CG    1 
ATOM   10240 S  SD    . MET   B  1  188  ? -10.708 37.372  123.134 1.00 55.37 ? 186  MET   B SD    1 
ATOM   10241 C  CE    . MET   B  1  188  ? -11.365 38.516  124.355 1.00 45.45 ? 186  MET   B CE    1 
ATOM   10242 N  N     . ALA   B  1  189  ? -5.710  37.463  123.464 1.00 30.58 ? 187  ALA   B N     1 
ATOM   10243 C  CA    . ALA   B  1  189  ? -4.731  36.743  122.654 1.00 31.75 ? 187  ALA   B CA    1 
ATOM   10244 C  C     . ALA   B  1  189  ? -4.198  35.523  123.392 1.00 34.98 ? 187  ALA   B C     1 
ATOM   10245 O  O     . ALA   B  1  189  ? -3.978  34.467  122.786 1.00 31.35 ? 187  ALA   B O     1 
ATOM   10246 C  CB    . ALA   B  1  189  ? -3.587  37.675  122.265 1.00 32.32 ? 187  ALA   B CB    1 
ATOM   10247 N  N     . MET   B  1  190  ? -3.975  35.656  124.701 1.00 32.82 ? 188  MET   B N     1 
ATOM   10248 C  CA    . MET   B  1  190  ? -3.531  34.523  125.510 1.00 32.23 ? 188  MET   B CA    1 
ATOM   10249 C  C     . MET   B  1  190  ? -4.519  33.366  125.418 1.00 34.41 ? 188  MET   B C     1 
ATOM   10250 O  O     . MET   B  1  190  ? -4.126  32.211  125.212 1.00 34.91 ? 188  MET   B O     1 
ATOM   10251 C  CB    . MET   B  1  190  ? -3.369  34.968  126.964 1.00 33.21 ? 188  MET   B CB    1 
ATOM   10252 C  CG    . MET   B  1  190  ? -2.493  34.057  127.794 1.00 38.88 ? 188  MET   B CG    1 
ATOM   10253 S  SD    . MET   B  1  190  ? -2.473  34.558  129.524 1.00 50.71 ? 188  MET   B SD    1 
ATOM   10254 C  CE    . MET   B  1  190  ? -2.400  36.345  129.375 1.00 40.87 ? 188  MET   B CE    1 
ATOM   10255 N  N     . ARG   B  1  191  ? -5.813  33.659  125.560 1.00 32.03 ? 189  ARG   B N     1 
ATOM   10256 C  CA    . ARG   B  1  191  ? -6.823  32.607  125.487 1.00 36.79 ? 189  ARG   B CA    1 
ATOM   10257 C  C     . ARG   B  1  191  ? -6.864  31.986  124.097 1.00 37.49 ? 189  ARG   B C     1 
ATOM   10258 O  O     . ARG   B  1  191  ? -6.879  30.757  123.950 1.00 34.42 ? 189  ARG   B O     1 
ATOM   10259 C  CB    . ARG   B  1  191  ? -8.193  33.168  125.869 1.00 29.28 ? 189  ARG   B CB    1 
ATOM   10260 N  N     . MET   B  1  192  ? -6.872  32.823  123.060 1.00 33.79 ? 190  MET   B N     1 
ATOM   10261 C  CA    . MET   B  1  192  ? -6.960  32.304  121.702 1.00 33.53 ? 190  MET   B CA    1 
ATOM   10262 C  C     . MET   B  1  192  ? -5.749  31.447  121.362 1.00 35.27 ? 190  MET   B C     1 
ATOM   10263 O  O     . MET   B  1  192  ? -5.888  30.319  120.872 1.00 33.75 ? 190  MET   B O     1 
ATOM   10264 C  CB    . MET   B  1  192  ? -7.096  33.459  120.711 1.00 35.46 ? 190  MET   B CB    1 
ATOM   10265 C  CG    . MET   B  1  192  ? -8.340  34.304  120.911 1.00 36.26 ? 190  MET   B CG    1 
ATOM   10266 S  SD    . MET   B  1  192  ? -8.540  35.461  119.541 1.00 49.81 ? 190  MET   B SD    1 
ATOM   10267 C  CE    . MET   B  1  192  ? -8.987  34.319  118.239 1.00 38.89 ? 190  MET   B CE    1 
ATOM   10268 N  N     . MET   B  1  193  ? -4.549  31.963  121.617 1.00 33.21 ? 191  MET   B N     1 
ATOM   10269 C  CA    A MET   B  1  193  ? -3.332  31.256  121.238 0.50 34.91 ? 191  MET   B CA    1 
ATOM   10270 C  CA    B MET   B  1  193  ? -3.349  31.238  121.226 0.50 34.91 ? 191  MET   B CA    1 
ATOM   10271 C  C     . MET   B  1  193  ? -2.999  30.109  122.180 1.00 36.93 ? 191  MET   B C     1 
ATOM   10272 O  O     . MET   B  1  193  ? -2.255  29.203  121.792 1.00 34.56 ? 191  MET   B O     1 
ATOM   10273 C  CB    A MET   B  1  193  ? -2.146  32.223  121.194 0.50 34.95 ? 191  MET   B CB    1 
ATOM   10274 C  CB    B MET   B  1  193  ? -2.167  32.195  121.083 0.50 34.95 ? 191  MET   B CB    1 
ATOM   10275 C  CG    A MET   B  1  193  ? -2.370  33.453  120.335 0.50 33.60 ? 191  MET   B CG    1 
ATOM   10276 C  CG    B MET   B  1  193  ? -2.288  33.112  119.889 0.50 34.13 ? 191  MET   B CG    1 
ATOM   10277 S  SD    A MET   B  1  193  ? -1.025  34.643  120.499 0.50 32.74 ? 191  MET   B SD    1 
ATOM   10278 S  SD    B MET   B  1  193  ? -0.730  33.911  119.495 0.50 35.92 ? 191  MET   B SD    1 
ATOM   10279 C  CE    A MET   B  1  193  ? 0.144   34.000  119.305 0.50 38.45 ? 191  MET   B CE    1 
ATOM   10280 C  CE    B MET   B  1  193  ? -0.501  34.943  120.942 0.50 33.32 ? 191  MET   B CE    1 
ATOM   10281 N  N     . GLY   B  1  194  ? -3.520  30.130  123.401 1.00 33.46 ? 192  GLY   B N     1 
ATOM   10282 C  CA    . GLY   B  1  194  ? -3.189  29.098  124.360 1.00 33.30 ? 192  GLY   B CA    1 
ATOM   10283 C  C     . GLY   B  1  194  ? -4.240  28.019  124.510 1.00 34.20 ? 192  GLY   B C     1 
ATOM   10284 O  O     . GLY   B  1  194  ? -3.926  26.904  124.943 1.00 33.78 ? 192  GLY   B O     1 
ATOM   10285 N  N     . GLU   B  1  195  ? -5.491  28.329  124.159 1.00 31.61 ? 193  GLU   B N     1 
ATOM   10286 C  CA    . GLU   B  1  195  ? -6.600  27.422  124.431 1.00 33.98 ? 193  GLU   B CA    1 
ATOM   10287 C  C     . GLU   B  1  195  ? -7.519  27.157  123.247 1.00 35.30 ? 193  GLU   B C     1 
ATOM   10288 O  O     . GLU   B  1  195  ? -8.255  26.165  123.282 1.00 32.68 ? 193  GLU   B O     1 
ATOM   10289 C  CB    . GLU   B  1  195  ? -7.437  27.919  125.624 1.00 34.53 ? 193  GLU   B CB    1 
ATOM   10290 N  N     . GLN   B  1  196  ? -7.500  27.983  122.204 1.00 36.44 ? 194  GLN   B N     1 
ATOM   10291 C  CA    . GLN   B  1  196  ? -8.367  27.782  121.049 1.00 34.44 ? 194  GLN   B CA    1 
ATOM   10292 C  C     . GLN   B  1  196  ? -7.604  27.382  119.795 1.00 33.88 ? 194  GLN   B C     1 
ATOM   10293 O  O     . GLN   B  1  196  ? -7.974  26.410  119.131 1.00 37.74 ? 194  GLN   B O     1 
ATOM   10294 C  CB    . GLN   B  1  196  ? -9.203  29.040  120.785 1.00 35.27 ? 194  GLN   B CB    1 
ATOM   10295 C  CG    . GLN   B  1  196  ? -9.971  29.006  119.475 1.00 44.69 ? 194  GLN   B CG    1 
ATOM   10296 C  CD    . GLN   B  1  196  ? -10.651 30.323  119.174 1.00 46.00 ? 194  GLN   B CD    1 
ATOM   10297 O  OE1   . GLN   B  1  196  ? -10.703 31.216  120.023 1.00 52.99 ? 194  GLN   B OE1   1 
ATOM   10298 N  NE2   . GLN   B  1  196  ? -11.174 30.455  117.961 1.00 52.30 ? 194  GLN   B NE2   1 
ATOM   10299 N  N     . PHE   B  1  197  ? -6.550  28.114  119.442 1.00 33.98 ? 195  PHE   B N     1 
ATOM   10300 C  CA    . PHE   B  1  197  ? -5.737  27.711  118.302 1.00 33.98 ? 195  PHE   B CA    1 
ATOM   10301 C  C     . PHE   B  1  197  ? -4.999  26.412  118.580 1.00 36.28 ? 195  PHE   B C     1 
ATOM   10302 O  O     . PHE   B  1  197  ? -4.688  25.663  117.646 1.00 35.99 ? 195  PHE   B O     1 
ATOM   10303 C  CB    . PHE   B  1  197  ? -4.751  28.818  117.937 1.00 33.61 ? 195  PHE   B CB    1 
ATOM   10304 C  CG    . PHE   B  1  197  ? -5.411  30.084  117.463 1.00 34.70 ? 195  PHE   B CG    1 
ATOM   10305 C  CD1   . PHE   B  1  197  ? -6.632  30.040  116.810 1.00 39.13 ? 195  PHE   B CD1   1 
ATOM   10306 C  CD2   . PHE   B  1  197  ? -4.815  31.314  117.684 1.00 38.05 ? 195  PHE   B CD2   1 
ATOM   10307 C  CE1   . PHE   B  1  197  ? -7.242  31.201  116.375 1.00 42.23 ? 195  PHE   B CE1   1 
ATOM   10308 C  CE2   . PHE   B  1  197  ? -5.418  32.481  117.251 1.00 39.78 ? 195  PHE   B CE2   1 
ATOM   10309 C  CZ    . PHE   B  1  197  ? -6.632  32.423  116.598 1.00 40.41 ? 195  PHE   B CZ    1 
ATOM   10310 N  N     . VAL   B  1  198  ? -4.696  26.137  119.846 1.00 32.36 ? 196  VAL   B N     1 
ATOM   10311 C  CA    . VAL   B  1  198  ? -4.068  24.888  120.249 1.00 30.61 ? 196  VAL   B CA    1 
ATOM   10312 C  C     . VAL   B  1  198  ? -4.796  24.364  121.476 1.00 28.81 ? 196  VAL   B C     1 
ATOM   10313 O  O     . VAL   B  1  198  ? -5.408  25.122  122.236 1.00 29.57 ? 196  VAL   B O     1 
ATOM   10314 C  CB    . VAL   B  1  198  ? -2.553  25.035  120.544 1.00 25.32 ? 196  VAL   B CB    1 
ATOM   10315 C  CG1   . VAL   B  1  198  ? -1.799  25.517  119.320 1.00 32.33 ? 196  VAL   B CG1   1 
ATOM   10316 C  CG2   . VAL   B  1  198  ? -2.329  25.965  121.728 1.00 34.64 ? 196  VAL   B CG2   1 
ATOM   10317 N  N     . THR   B  1  199  ? -4.746  23.048  121.655 1.00 28.26 ? 197  THR   B N     1 
ATOM   10318 C  CA    A THR   B  1  199  ? -5.279  22.455  122.869 0.71 27.07 ? 197  THR   B CA    1 
ATOM   10319 C  CA    B THR   B  1  199  ? -5.270  22.446  122.877 0.29 27.10 ? 197  THR   B CA    1 
ATOM   10320 C  C     . THR   B  1  199  ? -4.359  22.691  124.061 1.00 29.64 ? 197  THR   B C     1 
ATOM   10321 O  O     . THR   B  1  199  ? -4.821  22.659  125.203 1.00 33.20 ? 197  THR   B O     1 
ATOM   10322 C  CB    A THR   B  1  199  ? -5.517  20.970  122.614 0.71 25.68 ? 197  THR   B CB    1 
ATOM   10323 C  CB    B THR   B  1  199  ? -5.423  20.933  122.736 0.29 25.70 ? 197  THR   B CB    1 
ATOM   10324 O  OG1   A THR   B  1  199  ? -6.285  20.831  121.408 0.71 27.11 ? 197  THR   B OG1   1 
ATOM   10325 O  OG1   B THR   B  1  199  ? -4.293  20.392  122.040 0.29 23.13 ? 197  THR   B OG1   1 
ATOM   10326 C  CG2   A THR   B  1  199  ? -6.273  20.332  123.770 0.71 25.22 ? 197  THR   B CG2   1 
ATOM   10327 C  CG2   B THR   B  1  199  ? -6.695  20.593  122.016 0.29 26.75 ? 197  THR   B CG2   1 
ATOM   10328 N  N     . GLY   B  1  200  ? -3.084  22.921  123.813 1.00 24.62 ? 198  GLY   B N     1 
ATOM   10329 C  CA    . GLY   B  1  200  ? -2.140  23.204  124.871 1.00 28.61 ? 198  GLY   B CA    1 
ATOM   10330 C  C     . GLY   B  1  200  ? -0.796  23.469  124.237 1.00 27.85 ? 198  GLY   B C     1 
ATOM   10331 O  O     . GLY   B  1  200  ? -0.587  23.210  123.048 1.00 25.43 ? 198  GLY   B O     1 
ATOM   10332 N  N     . GLU   B  1  201  ? 0.113   24.006  125.053 1.00 30.01 ? 199  GLU   B N     1 
ATOM   10333 C  CA    . GLU   B  1  201  ? 1.462   24.302  124.581 1.00 31.37 ? 199  GLU   B CA    1 
ATOM   10334 C  C     . GLU   B  1  201  ? 2.365   23.081  124.605 1.00 29.17 ? 199  GLU   B C     1 
ATOM   10335 O  O     . GLU   B  1  201  ? 3.368   23.044  123.886 1.00 32.42 ? 199  GLU   B O     1 
ATOM   10336 C  CB    . GLU   B  1  201  ? 2.100   25.386  125.449 1.00 33.57 ? 199  GLU   B CB    1 
ATOM   10337 C  CG    . GLU   B  1  201  ? 1.585   26.785  125.187 1.00 44.73 ? 199  GLU   B CG    1 
ATOM   10338 C  CD    . GLU   B  1  201  ? 2.436   27.842  125.866 1.00 53.55 ? 199  GLU   B CD    1 
ATOM   10339 O  OE1   . GLU   B  1  201  ? 3.119   27.508  126.859 1.00 49.86 ? 199  GLU   B OE1   1 
ATOM   10340 O  OE2   . GLU   B  1  201  ? 2.430   29.002  125.400 1.00 52.56 ? 199  GLU   B OE2   1 
ATOM   10341 N  N     . THR   B  1  202  ? 2.062   22.105  125.451 1.00 23.11 ? 200  THR   B N     1 
ATOM   10342 C  CA    . THR   B  1  202  ? 2.812   20.865  125.541 1.00 26.01 ? 200  THR   B CA    1 
ATOM   10343 C  C     . THR   B  1  202  ? 1.827   19.712  125.466 1.00 22.69 ? 200  THR   B C     1 
ATOM   10344 O  O     . THR   B  1  202  ? 0.625   19.889  125.683 1.00 23.10 ? 200  THR   B O     1 
ATOM   10345 C  CB    . THR   B  1  202  ? 3.527   20.753  126.882 1.00 27.02 ? 200  THR   B CB    1 
ATOM   10346 O  OG1   . THR   B  1  202  ? 2.551   20.600  127.917 1.00 26.86 ? 200  THR   B OG1   1 
ATOM   10347 C  CG2   . THR   B  1  202  ? 4.355   21.997  127.154 1.00 31.40 ? 200  THR   B CG2   1 
ATOM   10348 N  N     . ILE   B  1  203  ? 2.348   18.521  125.172 1.00 22.12 ? 201  ILE   B N     1 
ATOM   10349 C  CA    . ILE   B  1  203  ? 1.467   17.368  125.029 1.00 23.04 ? 201  ILE   B CA    1 
ATOM   10350 C  C     . ILE   B  1  203  ? 0.852   16.989  126.372 1.00 22.72 ? 201  ILE   B C     1 
ATOM   10351 O  O     . ILE   B  1  203  ? -0.323  16.612  126.447 1.00 23.23 ? 201  ILE   B O     1 
ATOM   10352 C  CB    . ILE   B  1  203  ? 2.171   16.191  124.326 1.00 22.34 ? 201  ILE   B CB    1 
ATOM   10353 C  CG1   . ILE   B  1  203  ? 1.165   15.074  124.019 1.00 22.45 ? 201  ILE   B CG1   1 
ATOM   10354 C  CG2   . ILE   B  1  203  ? 3.324   15.654  125.177 1.00 25.08 ? 201  ILE   B CG2   1 
ATOM   10355 C  CD1   . ILE   B  1  203  ? 0.006   15.516  123.115 1.00 22.14 ? 201  ILE   B CD1   1 
ATOM   10356 N  N     . ARG   B  1  204  ? 1.603   17.123  127.467 1.00 26.15 ? 202  ARG   B N     1 
ATOM   10357 C  CA    . ARG   B  1  204  ? 0.991   16.787  128.747 1.00 27.62 ? 202  ARG   B CA    1 
ATOM   10358 C  C     . ARG   B  1  204  ? -0.118  17.771  129.125 1.00 24.51 ? 202  ARG   B C     1 
ATOM   10359 O  O     . ARG   B  1  204  ? -1.115  17.367  129.732 1.00 26.80 ? 202  ARG   B O     1 
ATOM   10360 C  CB    . ARG   B  1  204  ? 2.043   16.628  129.844 1.00 30.15 ? 202  ARG   B CB    1 
ATOM   10361 C  CG    . ARG   B  1  204  ? 2.659   17.918  130.274 1.00 26.34 ? 202  ARG   B CG    1 
ATOM   10362 C  CD    . ARG   B  1  204  ? 3.612   17.699  131.442 1.00 33.08 ? 202  ARG   B CD    1 
ATOM   10363 N  NE    . ARG   B  1  204  ? 3.883   18.966  132.107 1.00 28.38 ? 202  ARG   B NE    1 
ATOM   10364 C  CZ    . ARG   B  1  204  ? 3.228   19.406  133.169 1.00 34.56 ? 202  ARG   B CZ    1 
ATOM   10365 N  NH1   . ARG   B  1  204  ? 2.287   18.678  133.752 1.00 33.89 ? 202  ARG   B NH1   1 
ATOM   10366 N  NH2   . ARG   B  1  204  ? 3.529   20.602  133.665 1.00 32.72 ? 202  ARG   B NH2   1 
ATOM   10367 N  N     . GLU   B  1  205  ? 0.009   19.046  128.746 1.00 24.36 ? 203  GLU   B N     1 
ATOM   10368 C  CA    . GLU   B  1  205  ? -1.077  19.990  128.998 1.00 26.76 ? 203  GLU   B CA    1 
ATOM   10369 C  C     . GLU   B  1  205  ? -2.282  19.688  128.116 1.00 26.31 ? 203  GLU   B C     1 
ATOM   10370 O  O     . GLU   B  1  205  ? -3.427  19.704  128.585 1.00 26.56 ? 203  GLU   B O     1 
ATOM   10371 C  CB    . GLU   B  1  205  ? -0.604  21.422  128.762 1.00 27.81 ? 203  GLU   B CB    1 
ATOM   10372 C  CG    . GLU   B  1  205  ? -1.726  22.457  128.838 1.00 28.59 ? 203  GLU   B CG    1 
ATOM   10373 C  CD    . GLU   B  1  205  ? -1.220  23.895  128.772 1.00 40.68 ? 203  GLU   B CD    1 
ATOM   10374 O  OE1   . GLU   B  1  205  ? -0.737  24.324  127.700 1.00 39.32 ? 203  GLU   B OE1   1 
ATOM   10375 O  OE2   . GLU   B  1  205  ? -1.300  24.599  129.803 1.00 52.36 ? 203  GLU   B OE2   1 
ATOM   10376 N  N     . ALA   B  1  206  ? -2.039  19.405  126.839 1.00 21.87 ? 204  ALA   B N     1 
ATOM   10377 C  CA    . ALA   B  1  206  ? -3.129  19.048  125.939 1.00 21.50 ? 204  ALA   B CA    1 
ATOM   10378 C  C     . ALA   B  1  206  ? -3.838  17.793  126.421 1.00 25.99 ? 204  ALA   B C     1 
ATOM   10379 O  O     . ALA   B  1  206  ? -5.073  17.728  126.413 1.00 24.98 ? 204  ALA   B O     1 
ATOM   10380 C  CB    . ALA   B  1  206  ? -2.595  18.857  124.520 1.00 23.64 ? 204  ALA   B CB    1 
ATOM   10381 N  N     . LEU   B  1  207  ? -3.074  16.792  126.864 1.00 21.38 ? 205  LEU   B N     1 
ATOM   10382 C  CA    . LEU   B  1  207  ? -3.687  15.575  127.394 1.00 23.63 ? 205  LEU   B CA    1 
ATOM   10383 C  C     . LEU   B  1  207  ? -4.525  15.863  128.632 1.00 27.10 ? 205  LEU   B C     1 
ATOM   10384 O  O     . LEU   B  1  207  ? -5.620  15.307  128.786 1.00 26.83 ? 205  LEU   B O     1 
ATOM   10385 C  CB    . LEU   B  1  207  ? -2.616  14.522  127.691 1.00 24.94 ? 205  LEU   B CB    1 
ATOM   10386 C  CG    . LEU   B  1  207  ? -1.997  13.880  126.445 1.00 25.45 ? 205  LEU   B CG    1 
ATOM   10387 C  CD1   . LEU   B  1  207  ? -0.685  13.171  126.796 1.00 28.22 ? 205  LEU   B CD1   1 
ATOM   10388 C  CD2   . LEU   B  1  207  ? -2.971  12.917  125.790 1.00 23.55 ? 205  LEU   B CD2   1 
ATOM   10389 N  N     . LYS   B  1  208  ? -4.031  16.721  129.530 1.00 22.66 ? 206  LYS   B N     1 
ATOM   10390 C  CA    . LYS   B  1  208  ? -4.810  17.063  130.717 1.00 26.36 ? 206  LYS   B CA    1 
ATOM   10391 C  C     . LYS   B  1  208  ? -6.108  17.769  130.339 1.00 27.83 ? 206  LYS   B C     1 
ATOM   10392 O  O     . LYS   B  1  208  ? -7.162  17.516  130.936 1.00 31.63 ? 206  LYS   B O     1 
ATOM   10393 C  CB    . LYS   B  1  208  ? -3.977  17.922  131.673 1.00 29.91 ? 206  LYS   B CB    1 
ATOM   10394 N  N     . ARG   B  1  209  ? -6.055  18.650  129.343 1.00 27.50 ? 207  ARG   B N     1 
ATOM   10395 C  CA    . ARG   B  1  209  ? -7.243  19.388  128.941 1.00 29.60 ? 207  ARG   B CA    1 
ATOM   10396 C  C     . ARG   B  1  209  ? -8.221  18.532  128.156 1.00 31.71 ? 207  ARG   B C     1 
ATOM   10397 O  O     . ARG   B  1  209  ? -9.379  18.934  127.985 1.00 32.12 ? 207  ARG   B O     1 
ATOM   10398 C  CB    . ARG   B  1  209  ? -6.853  20.611  128.122 1.00 28.63 ? 207  ARG   B CB    1 
ATOM   10399 C  CG    . ARG   B  1  209  ? -6.106  21.661  128.931 1.00 28.61 ? 207  ARG   B CG    1 
ATOM   10400 C  CD    . ARG   B  1  209  ? -5.860  22.874  128.075 1.00 31.49 ? 207  ARG   B CD    1 
ATOM   10401 N  NE    . ARG   B  1  209  ? -5.102  23.915  128.752 1.00 39.99 ? 207  ARG   B NE    1 
ATOM   10402 C  CZ    . ARG   B  1  209  ? -4.607  24.981  128.137 1.00 41.84 ? 207  ARG   B CZ    1 
ATOM   10403 N  NH1   . ARG   B  1  209  ? -4.760  25.158  126.834 1.00 32.83 ? 207  ARG   B NH1   1 
ATOM   10404 N  NH2   . ARG   B  1  209  ? -3.946  25.892  128.846 1.00 45.19 ? 207  ARG   B NH2   1 
ATOM   10405 N  N     . SER   B  1  210  ? -7.796  17.360  127.704 1.00 25.74 ? 208  SER   B N     1 
ATOM   10406 C  CA    . SER   B  1  210  ? -8.662  16.508  126.907 1.00 27.45 ? 208  SER   B CA    1 
ATOM   10407 C  C     . SER   B  1  210  ? -9.648  15.707  127.751 1.00 27.82 ? 208  SER   B C     1 
ATOM   10408 O  O     . SER   B  1  210  ? -10.624 15.184  127.203 1.00 27.20 ? 208  SER   B O     1 
ATOM   10409 C  CB    . SER   B  1  210  ? -7.794  15.574  126.070 1.00 21.64 ? 208  SER   B CB    1 
ATOM   10410 O  OG    . SER   B  1  210  ? -7.029  16.328  125.129 1.00 27.70 ? 208  SER   B OG    1 
ATOM   10411 N  N     . LYS   B  1  211  ? -9.429  15.615  129.064 1.00 27.64 ? 209  LYS   B N     1 
ATOM   10412 C  CA    . LYS   B  1  211  ? -10.274 14.771  129.900 1.00 29.26 ? 209  LYS   B CA    1 
ATOM   10413 C  C     . LYS   B  1  211  ? -11.734 15.200  129.830 1.00 29.16 ? 209  LYS   B C     1 
ATOM   10414 O  O     . LYS   B  1  211  ? -12.633 14.354  129.795 1.00 33.87 ? 209  LYS   B O     1 
ATOM   10415 C  CB    . LYS   B  1  211  ? -9.782  14.815  131.345 1.00 30.45 ? 209  LYS   B CB    1 
ATOM   10416 N  N     . GLU   B  1  212  ? -11.985 16.511  129.793 1.00 30.19 ? 210  GLU   B N     1 
ATOM   10417 C  CA    . GLU   B  1  212  ? -13.350 17.019  129.902 1.00 31.00 ? 210  GLU   B CA    1 
ATOM   10418 C  C     . GLU   B  1  212  ? -14.224 16.519  128.758 1.00 30.30 ? 210  GLU   B C     1 
ATOM   10419 O  O     . GLU   B  1  212  ? -15.321 15.994  128.986 1.00 30.09 ? 210  GLU   B O     1 
ATOM   10420 C  CB    . GLU   B  1  212  ? -13.327 18.546  129.933 1.00 37.52 ? 210  GLU   B CB    1 
ATOM   10421 C  CG    . GLU   B  1  212  ? -14.702 19.192  129.887 1.00 44.79 ? 210  GLU   B CG    1 
ATOM   10422 C  CD    . GLU   B  1  212  ? -14.636 20.649  129.475 1.00 47.56 ? 210  GLU   B CD    1 
ATOM   10423 O  OE1   . GLU   B  1  212  ? -13.510 21.180  129.350 1.00 56.08 ? 210  GLU   B OE1   1 
ATOM   10424 O  OE2   . GLU   B  1  212  ? -15.705 21.262  129.265 1.00 57.57 ? 210  GLU   B OE2   1 
ATOM   10425 N  N     . LEU   B  1  213  ? -13.758 16.679  127.518 1.00 27.39 ? 211  LEU   B N     1 
ATOM   10426 C  CA    . LEU   B  1  213  ? -14.540 16.217  126.376 1.00 29.88 ? 211  LEU   B CA    1 
ATOM   10427 C  C     . LEU   B  1  213  ? -14.466 14.705  126.195 1.00 28.41 ? 211  LEU   B C     1 
ATOM   10428 O  O     . LEU   B  1  213  ? -15.419 14.104  125.688 1.00 26.91 ? 211  LEU   B O     1 
ATOM   10429 C  CB    . LEU   B  1  213  ? -14.169 16.981  125.101 1.00 23.81 ? 211  LEU   B CB    1 
ATOM   10430 C  CG    . LEU   B  1  213  ? -14.613 18.449  125.100 1.00 27.81 ? 211  LEU   B CG    1 
ATOM   10431 C  CD1   . LEU   B  1  213  ? -14.376 19.117  123.759 1.00 29.65 ? 211  LEU   B CD1   1 
ATOM   10432 C  CD2   . LEU   B  1  213  ? -16.081 18.561  125.502 1.00 32.93 ? 211  LEU   B CD2   1 
ATOM   10433 N  N     . GLU   B  1  214  ? -13.367 14.070  126.611 1.00 25.70 ? 212  GLU   B N     1 
ATOM   10434 C  CA    . GLU   B  1  214  ? -13.308 12.613  126.544 1.00 25.77 ? 212  GLU   B CA    1 
ATOM   10435 C  C     . GLU   B  1  214  ? -14.384 11.975  127.408 1.00 29.23 ? 212  GLU   B C     1 
ATOM   10436 O  O     . GLU   B  1  214  ? -15.037 11.018  126.982 1.00 29.34 ? 212  GLU   B O     1 
ATOM   10437 C  CB    . GLU   B  1  214  ? -11.920 12.098  126.918 1.00 28.04 ? 212  GLU   B CB    1 
ATOM   10438 C  CG    . GLU   B  1  214  ? -10.901 12.274  125.795 1.00 26.58 ? 212  GLU   B CG    1 
ATOM   10439 C  CD    . GLU   B  1  214  ? -9.561  11.646  126.117 1.00 28.42 ? 212  GLU   B CD    1 
ATOM   10440 O  OE1   . GLU   B  1  214  ? -9.315  11.325  127.293 1.00 32.10 ? 212  GLU   B OE1   1 
ATOM   10441 O  OE2   . GLU   B  1  214  ? -8.746  11.480  125.186 1.00 26.79 ? 212  GLU   B OE2   1 
ATOM   10442 N  N     . GLU   B  1  215  ? -14.597 12.506  128.617 1.00 27.78 ? 213  GLU   B N     1 
ATOM   10443 C  CA    . GLU   B  1  215  ? -15.664 11.997  129.473 1.00 27.55 ? 213  GLU   B CA    1 
ATOM   10444 C  C     . GLU   B  1  215  ? -17.038 12.141  128.829 1.00 30.48 ? 213  GLU   B C     1 
ATOM   10445 O  O     . GLU   B  1  215  ? -17.951 11.387  129.175 1.00 31.75 ? 213  GLU   B O     1 
ATOM   10446 C  CB    . GLU   B  1  215  ? -15.629 12.684  130.842 1.00 34.54 ? 213  GLU   B CB    1 
ATOM   10447 C  CG    . GLU   B  1  215  ? -14.391 12.340  131.671 1.00 36.76 ? 213  GLU   B CG    1 
ATOM   10448 C  CD    . GLU   B  1  215  ? -14.408 12.966  133.056 1.00 51.29 ? 213  GLU   B CD    1 
ATOM   10449 O  OE1   . GLU   B  1  215  ? -15.473 12.941  133.713 1.00 56.42 ? 213  GLU   B OE1   1 
ATOM   10450 O  OE2   . GLU   B  1  215  ? -13.351 13.480  133.488 1.00 53.56 ? 213  GLU   B OE2   1 
ATOM   10451 N  N     . LYS   B  1  216  ? -17.202 13.084  127.898 1.00 28.92 ? 214  LYS   B N     1 
ATOM   10452 C  CA    . LYS   B  1  216  ? -18.459 13.227  127.175 1.00 31.59 ? 214  LYS   B CA    1 
ATOM   10453 C  C     . LYS   B  1  216  ? -18.555 12.307  125.966 1.00 32.95 ? 214  LYS   B C     1 
ATOM   10454 O  O     . LYS   B  1  216  ? -19.637 12.200  125.379 1.00 31.48 ? 214  LYS   B O     1 
ATOM   10455 C  CB    . LYS   B  1  216  ? -18.664 14.676  126.726 1.00 32.75 ? 214  LYS   B CB    1 
ATOM   10456 C  CG    . LYS   B  1  216  ? -18.827 15.680  127.864 1.00 36.11 ? 214  LYS   B CG    1 
ATOM   10457 C  CD    . LYS   B  1  216  ? -18.957 17.096  127.306 1.00 41.81 ? 214  LYS   B CD    1 
ATOM   10458 C  CE    . LYS   B  1  216  ? -18.951 18.138  128.412 1.00 49.17 ? 214  LYS   B CE    1 
ATOM   10459 N  NZ    . LYS   B  1  216  ? -18.114 19.318  128.033 1.00 48.23 ? 214  LYS   B NZ    1 
ATOM   10460 N  N     . GLY   B  1  217  ? -17.465 11.648  125.577 1.00 29.90 ? 215  GLY   B N     1 
ATOM   10461 C  CA    . GLY   B  1  217  ? -17.477 10.742  124.448 1.00 25.02 ? 215  GLY   B CA    1 
ATOM   10462 C  C     . GLY   B  1  217  ? -16.688 11.214  123.249 1.00 29.44 ? 215  GLY   B C     1 
ATOM   10463 O  O     . GLY   B  1  217  ? -16.713 10.539  122.213 1.00 27.96 ? 215  GLY   B O     1 
ATOM   10464 N  N     . PHE   B  1  218  ? -16.019 12.359  123.336 1.00 26.21 ? 216  PHE   B N     1 
ATOM   10465 C  CA    . PHE   B  1  218  ? -15.075 12.728  122.295 1.00 24.32 ? 216  PHE   B CA    1 
ATOM   10466 C  C     . PHE   B  1  218  ? -13.798 11.916  122.448 1.00 24.63 ? 216  PHE   B C     1 
ATOM   10467 O  O     . PHE   B  1  218  ? -13.512 11.340  123.500 1.00 25.21 ? 216  PHE   B O     1 
ATOM   10468 C  CB    . PHE   B  1  218  ? -14.708 14.211  122.384 1.00 23.89 ? 216  PHE   B CB    1 
ATOM   10469 C  CG    . PHE   B  1  218  ? -15.821 15.145  121.997 1.00 26.65 ? 216  PHE   B CG    1 
ATOM   10470 C  CD1   . PHE   B  1  218  ? -16.835 15.445  122.900 1.00 27.35 ? 216  PHE   B CD1   1 
ATOM   10471 C  CD2   . PHE   B  1  218  ? -15.847 15.736  120.743 1.00 26.90 ? 216  PHE   B CD2   1 
ATOM   10472 C  CE1   . PHE   B  1  218  ? -17.855 16.309  122.551 1.00 28.64 ? 216  PHE   B CE1   1 
ATOM   10473 C  CE2   . PHE   B  1  218  ? -16.868 16.602  120.388 1.00 29.63 ? 216  PHE   B CE2   1 
ATOM   10474 C  CZ    . PHE   B  1  218  ? -17.873 16.888  121.302 1.00 26.31 ? 216  PHE   B CZ    1 
ATOM   10475 N  N     . SER   B  1  219  ? -13.036 11.858  121.363 1.00 24.13 ? 217  SER   B N     1 
ATOM   10476 C  CA    . SER   B  1  219  ? -11.680 11.346  121.388 1.00 23.56 ? 217  SER   B CA    1 
ATOM   10477 C  C     . SER   B  1  219  ? -10.781 12.408  120.775 1.00 21.74 ? 217  SER   B C     1 
ATOM   10478 O  O     . SER   B  1  219  ? -11.245 13.468  120.344 1.00 20.91 ? 217  SER   B O     1 
ATOM   10479 C  CB    . SER   B  1  219  ? -11.561 10.021  120.631 1.00 23.34 ? 217  SER   B CB    1 
ATOM   10480 O  OG    . SER   B  1  219  ? -11.934 10.195  119.271 1.00 25.81 ? 217  SER   B OG    1 
ATOM   10481 N  N     . TYR   B  1  220  ? -9.483  12.122  120.717 1.00 21.81 ? 218  TYR   B N     1 
ATOM   10482 C  CA    . TYR   B  1  220  ? -8.523  13.117  120.273 1.00 20.68 ? 218  TYR   B CA    1 
ATOM   10483 C  C     . TYR   B  1  220  ? -7.501  12.516  119.326 1.00 18.21 ? 218  TYR   B C     1 
ATOM   10484 O  O     . TYR   B  1  220  ? -7.171  11.332  119.394 1.00 21.88 ? 218  TYR   B O     1 
ATOM   10485 C  CB    . TYR   B  1  220  ? -7.774  13.731  121.463 1.00 19.30 ? 218  TYR   B CB    1 
ATOM   10486 C  CG    . TYR   B  1  220  ? -8.553  14.834  122.124 1.00 20.74 ? 218  TYR   B CG    1 
ATOM   10487 C  CD1   . TYR   B  1  220  ? -9.522  14.550  123.071 1.00 22.68 ? 218  TYR   B CD1   1 
ATOM   10488 C  CD2   . TYR   B  1  220  ? -8.350  16.158  121.758 1.00 18.87 ? 218  TYR   B CD2   1 
ATOM   10489 C  CE1   . TYR   B  1  220  ? -10.250 15.558  123.670 1.00 22.58 ? 218  TYR   B CE1   1 
ATOM   10490 C  CE2   . TYR   B  1  220  ? -9.072  17.176  122.339 1.00 21.79 ? 218  TYR   B CE2   1 
ATOM   10491 C  CZ    . TYR   B  1  220  ? -10.026 16.864  123.295 1.00 20.26 ? 218  TYR   B CZ    1 
ATOM   10492 O  OH    . TYR   B  1  220  ? -10.756 17.861  123.901 1.00 26.73 ? 218  TYR   B OH    1 
ATOM   10493 N  N     . SER   B  1  221  ? -6.986  13.369  118.456 1.00 17.51 ? 219  SER   B N     1 
ATOM   10494 C  CA    . SER   B  1  221  ? -5.822  13.060  117.638 1.00 17.98 ? 219  SER   B CA    1 
ATOM   10495 C  C     . SER   B  1  221  ? -4.933  14.286  117.705 1.00 19.71 ? 219  SER   B C     1 
ATOM   10496 O  O     . SER   B  1  221  ? -5.340  15.362  117.260 1.00 21.55 ? 219  SER   B O     1 
ATOM   10497 C  CB    . SER   B  1  221  ? -6.227  12.781  116.193 1.00 20.90 ? 219  SER   B CB    1 
ATOM   10498 O  OG    . SER   B  1  221  ? -5.075  12.504  115.409 1.00 20.52 ? 219  SER   B OG    1 
ATOM   10499 N  N     . TYR   B  1  222  ? -3.734  14.132  118.272 1.00 18.44 ? 220  TYR   B N     1 
ATOM   10500 C  CA    . TYR   B  1  222  ? -2.862  15.272  118.535 1.00 18.59 ? 220  TYR   B CA    1 
ATOM   10501 C  C     . TYR   B  1  222  ? -1.935  15.562  117.366 1.00 18.64 ? 220  TYR   B C     1 
ATOM   10502 O  O     . TYR   B  1  222  ? -1.380  14.647  116.757 1.00 20.50 ? 220  TYR   B O     1 
ATOM   10503 C  CB    . TYR   B  1  222  ? -2.047  15.025  119.803 1.00 17.44 ? 220  TYR   B CB    1 
ATOM   10504 C  CG    . TYR   B  1  222  ? -2.965  14.898  120.976 1.00 17.48 ? 220  TYR   B CG    1 
ATOM   10505 C  CD1   . TYR   B  1  222  ? -3.531  16.026  121.547 1.00 18.90 ? 220  TYR   B CD1   1 
ATOM   10506 C  CD2   . TYR   B  1  222  ? -3.318  13.654  121.479 1.00 19.07 ? 220  TYR   B CD2   1 
ATOM   10507 C  CE1   . TYR   B  1  222  ? -4.411  15.924  122.598 1.00 18.72 ? 220  TYR   B CE1   1 
ATOM   10508 C  CE2   . TYR   B  1  222  ? -4.191  13.542  122.547 1.00 19.90 ? 220  TYR   B CE2   1 
ATOM   10509 C  CZ    . TYR   B  1  222  ? -4.734  14.683  123.097 1.00 19.76 ? 220  TYR   B CZ    1 
ATOM   10510 O  OH    . TYR   B  1  222  ? -5.616  14.591  124.135 1.00 21.36 ? 220  TYR   B OH    1 
ATOM   10511 N  N     . ASP   B  1  223  ? -1.768  16.853  117.073 1.00 18.92 ? 221  ASP   B N     1 
ATOM   10512 C  CA    . ASP   B  1  223  ? -0.928  17.348  115.988 1.00 21.22 ? 221  ASP   B CA    1 
ATOM   10513 C  C     . ASP   B  1  223  ? 0.173   18.190  116.619 1.00 23.32 ? 221  ASP   B C     1 
ATOM   10514 O  O     . ASP   B  1  223  ? -0.096  19.278  117.139 1.00 25.12 ? 221  ASP   B O     1 
ATOM   10515 C  CB    . ASP   B  1  223  ? -1.767  18.197  115.040 1.00 23.63 ? 221  ASP   B CB    1 
ATOM   10516 C  CG    . ASP   B  1  223  ? -0.921  19.011  114.065 1.00 26.12 ? 221  ASP   B CG    1 
ATOM   10517 O  OD1   . ASP   B  1  223  ? 0.227   18.625  113.772 1.00 26.73 ? 221  ASP   B OD1   1 
ATOM   10518 O  OD2   . ASP   B  1  223  ? -1.417  20.050  113.599 1.00 29.74 ? 221  ASP   B OD2   1 
ATOM   10519 N  N     . MET   B  1  224  ? 1.405   17.689  116.579 1.00 19.75 ? 222  MET   B N     1 
ATOM   10520 C  CA    . MET   B  1  224  ? 2.537   18.377  117.186 1.00 24.11 ? 222  MET   B CA    1 
ATOM   10521 C  C     . MET   B  1  224  ? 3.106   19.477  116.309 1.00 27.32 ? 222  MET   B C     1 
ATOM   10522 O  O     . MET   B  1  224  ? 4.166   20.021  116.638 1.00 29.70 ? 222  MET   B O     1 
ATOM   10523 C  CB    . MET   B  1  224  ? 3.635   17.380  117.559 1.00 26.52 ? 222  MET   B CB    1 
ATOM   10524 C  CG    . MET   B  1  224  ? 3.178   16.314  118.542 1.00 22.95 ? 222  MET   B CG    1 
ATOM   10525 S  SD    . MET   B  1  224  ? 2.316   17.025  119.953 1.00 27.19 ? 222  MET   B SD    1 
ATOM   10526 C  CE    . MET   B  1  224  ? 3.663   17.934  120.706 1.00 28.74 ? 222  MET   B CE    1 
ATOM   10527 N  N     . LEU   B  1  225  ? 2.441   19.785  115.205 1.00 25.85 ? 223  LEU   B N     1 
ATOM   10528 C  CA    . LEU   B  1  225  ? 2.647   20.950  114.343 1.00 25.22 ? 223  LEU   B CA    1 
ATOM   10529 C  C     . LEU   B  1  225  ? 3.803   20.808  113.360 1.00 30.75 ? 223  LEU   B C     1 
ATOM   10530 O  O     . LEU   B  1  225  ? 4.031   21.747  112.583 1.00 32.67 ? 223  LEU   B O     1 
ATOM   10531 C  CB    . LEU   B  1  225  ? 2.791   22.276  115.105 1.00 28.14 ? 223  LEU   B CB    1 
ATOM   10532 C  CG    . LEU   B  1  225  ? 1.654   22.605  116.065 1.00 32.45 ? 223  LEU   B CG    1 
ATOM   10533 C  CD1   . LEU   B  1  225  ? 1.955   23.886  116.815 1.00 34.06 ? 223  LEU   B CD1   1 
ATOM   10534 C  CD2   . LEU   B  1  225  ? 0.337   22.695  115.316 1.00 31.37 ? 223  LEU   B CD2   1 
ATOM   10535 N  N     . GLY   B  1  226  ? 4.539   19.699  113.362 1.00 25.67 ? 224  GLY   B N     1 
ATOM   10536 C  CA    . GLY   B  1  226  ? 5.591   19.511  112.381 1.00 27.59 ? 224  GLY   B CA    1 
ATOM   10537 C  C     . GLY   B  1  226  ? 5.048   19.528  110.969 1.00 24.87 ? 224  GLY   B C     1 
ATOM   10538 O  O     . GLY   B  1  226  ? 4.021   18.905  110.688 1.00 24.03 ? 224  GLY   B O     1 
ATOM   10539 N  N     . GLU   B  1  227  ? 5.709   20.254  110.072 1.00 21.79 ? 225  GLU   B N     1 
ATOM   10540 C  CA    . GLU   B  1  227  ? 5.256   20.278  108.689 1.00 21.94 ? 225  GLU   B CA    1 
ATOM   10541 C  C     . GLU   B  1  227  ? 6.368   20.860  107.834 1.00 19.71 ? 225  GLU   B C     1 
ATOM   10542 O  O     . GLU   B  1  227  ? 7.066   21.775  108.270 1.00 24.03 ? 225  GLU   B O     1 
ATOM   10543 C  CB    . GLU   B  1  227  ? 3.990   21.134  108.549 1.00 24.42 ? 225  GLU   B CB    1 
ATOM   10544 C  CG    . GLU   B  1  227  ? 3.403   21.151  107.172 1.00 26.60 ? 225  GLU   B CG    1 
ATOM   10545 C  CD    . GLU   B  1  227  ? 2.065   21.852  107.138 1.00 29.44 ? 225  GLU   B CD    1 
ATOM   10546 O  OE1   . GLU   B  1  227  ? 1.486   22.083  108.223 1.00 28.37 ? 225  GLU   B OE1   1 
ATOM   10547 O  OE2   . GLU   B  1  227  ? 1.604   22.174  106.029 1.00 33.44 ? 225  GLU   B OE2   1 
ATOM   10548 N  N     . ALA   B  1  228  ? 6.532   20.313  106.628 1.00 18.12 ? 226  ALA   B N     1 
ATOM   10549 C  CA    . ALA   B  1  228  ? 7.383   20.916  105.609 1.00 19.92 ? 226  ALA   B CA    1 
ATOM   10550 C  C     . ALA   B  1  228  ? 8.778   21.238  106.146 1.00 19.55 ? 226  ALA   B C     1 
ATOM   10551 O  O     . ALA   B  1  228  ? 9.217   22.388  106.164 1.00 21.89 ? 226  ALA   B O     1 
ATOM   10552 C  CB    . ALA   B  1  228  ? 6.713   22.158  105.019 1.00 21.49 ? 226  ALA   B CB    1 
ATOM   10553 N  N     . ALA   B  1  229  ? 9.457   20.198  106.632 1.00 17.44 ? 227  ALA   B N     1 
ATOM   10554 C  CA    . ALA   B  1  229  ? 10.853  20.340  107.024 1.00 18.15 ? 227  ALA   B CA    1 
ATOM   10555 C  C     . ALA   B  1  229  ? 11.645  20.957  105.877 1.00 16.73 ? 227  ALA   B C     1 
ATOM   10556 O  O     . ALA   B  1  229  ? 11.484  20.567  104.717 1.00 18.74 ? 227  ALA   B O     1 
ATOM   10557 C  CB    . ALA   B  1  229  ? 11.428  18.965  107.353 1.00 18.16 ? 227  ALA   B CB    1 
ATOM   10558 N  N     . THR   B  1  230  ? 12.482  21.938  106.211 1.00 18.04 ? 228  THR   B N     1 
ATOM   10559 C  CA    . THR   B  1  230  ? 13.369  22.570  105.244 1.00 19.18 ? 228  THR   B CA    1 
ATOM   10560 C  C     . THR   B  1  230  ? 14.773  22.007  105.319 1.00 19.29 ? 228  THR   B C     1 
ATOM   10561 O  O     . THR   B  1  230  ? 15.473  21.943  104.302 1.00 18.90 ? 228  THR   B O     1 
ATOM   10562 C  CB    . THR   B  1  230  ? 13.412  24.080  105.515 1.00 19.20 ? 228  THR   B CB    1 
ATOM   10563 O  OG1   . THR   B  1  230  ? 12.068  24.574  105.558 1.00 23.96 ? 228  THR   B OG1   1 
ATOM   10564 C  CG2   . THR   B  1  230  ? 14.180  24.835  104.431 1.00 18.29 ? 228  THR   B CG2   1 
ATOM   10565 N  N     . THR   B  1  231  ? 15.196  21.582  106.499 1.00 17.39 ? 229  THR   B N     1 
ATOM   10566 C  CA    . THR   B  1  231  ? 16.533  21.059  106.684 1.00 15.80 ? 229  THR   B CA    1 
ATOM   10567 C  C     . THR   B  1  231  ? 16.430  19.703  107.356 1.00 15.13 ? 229  THR   B C     1 
ATOM   10568 O  O     . THR   B  1  231  ? 15.390  19.338  107.909 1.00 16.65 ? 229  THR   B O     1 
ATOM   10569 C  CB    . THR   B  1  231  ? 17.373  21.973  107.574 1.00 17.51 ? 229  THR   B CB    1 
ATOM   10570 O  OG1   . THR   B  1  231  ? 16.859  21.932  108.912 1.00 19.39 ? 229  THR   B OG1   1 
ATOM   10571 C  CG2   . THR   B  1  231  ? 17.345  23.409  107.059 1.00 17.59 ? 229  THR   B CG2   1 
ATOM   10572 N  N     . ALA   B  1  232  ? 17.548  18.978  107.319 1.00 16.56 ? 230  ALA   B N     1 
ATOM   10573 C  CA    . ALA   B  1  232  ? 17.632  17.715  108.046 1.00 17.83 ? 230  ALA   B CA    1 
ATOM   10574 C  C     . ALA   B  1  232  ? 17.359  17.920  109.527 1.00 18.78 ? 230  ALA   B C     1 
ATOM   10575 O  O     . ALA   B  1  232  ? 16.696  17.091  110.163 1.00 19.98 ? 230  ALA   B O     1 
ATOM   10576 C  CB    . ALA   B  1  232  ? 19.012  17.092  107.833 1.00 18.03 ? 230  ALA   B CB    1 
ATOM   10577 N  N     . ALA   B  1  233  ? 17.856  19.023  110.096 1.00 17.85 ? 231  ALA   B N     1 
ATOM   10578 C  CA    . ALA   B  1  233  ? 17.640  19.281  111.518 1.00 18.63 ? 231  ALA   B CA    1 
ATOM   10579 C  C     . ALA   B  1  233  ? 16.163  19.491  111.819 1.00 19.85 ? 231  ALA   B C     1 
ATOM   10580 O  O     . ALA   B  1  233  ? 15.677  19.096  112.887 1.00 18.29 ? 231  ALA   B O     1 
ATOM   10581 C  CB    . ALA   B  1  233  ? 18.451  20.496  111.967 1.00 20.03 ? 231  ALA   B CB    1 
ATOM   10582 N  N     . ASP   B  1  234  ? 15.440  20.144  110.906 1.00 16.76 ? 232  ASP   B N     1 
ATOM   10583 C  CA    . ASP   B  1  234  ? 13.997  20.290  111.079 1.00 17.57 ? 232  ASP   B CA    1 
ATOM   10584 C  C     . ASP   B  1  234  ? 13.336  18.925  111.162 1.00 17.58 ? 232  ASP   B C     1 
ATOM   10585 O  O     . ASP   B  1  234  ? 12.530  18.656  112.065 1.00 16.93 ? 232  ASP   B O     1 
ATOM   10586 C  CB    . ASP   B  1  234  ? 13.389  21.005  109.872 1.00 19.90 ? 232  ASP   B CB    1 
ATOM   10587 C  CG    . ASP   B  1  234  ? 13.705  22.469  109.825 1.00 23.11 ? 232  ASP   B CG    1 
ATOM   10588 O  OD1   . ASP   B  1  234  ? 14.018  23.066  110.874 1.00 23.89 ? 232  ASP   B OD1   1 
ATOM   10589 O  OD2   . ASP   B  1  234  ? 13.602  23.027  108.714 1.00 24.19 ? 232  ASP   B OD2   1 
ATOM   10590 N  N     . ALA   B  1  235  ? 13.649  18.061  110.197 1.00 16.93 ? 233  ALA   B N     1 
ATOM   10591 C  CA    . ALA   B  1  235  ? 13.009  16.758  110.126 1.00 16.77 ? 233  ALA   B CA    1 
ATOM   10592 C  C     . ALA   B  1  235  ? 13.327  15.932  111.357 1.00 16.61 ? 233  ALA   B C     1 
ATOM   10593 O  O     . ALA   B  1  235  ? 12.460  15.232  111.887 1.00 17.97 ? 233  ALA   B O     1 
ATOM   10594 C  CB    . ALA   B  1  235  ? 13.446  16.027  108.855 1.00 17.63 ? 233  ALA   B CB    1 
ATOM   10595 N  N     . GLU   B  1  236  ? 14.576  15.992  111.817 1.00 16.46 ? 234  GLU   B N     1 
ATOM   10596 C  CA    . GLU   B  1  236  ? 14.958  15.247  113.007 1.00 18.87 ? 234  GLU   B CA    1 
ATOM   10597 C  C     . GLU   B  1  236  ? 14.225  15.766  114.234 1.00 20.43 ? 234  GLU   B C     1 
ATOM   10598 O  O     . GLU   B  1  236  ? 13.746  14.979  115.060 1.00 18.81 ? 234  GLU   B O     1 
ATOM   10599 C  CB    . GLU   B  1  236  ? 16.473  15.317  113.195 1.00 19.36 ? 234  GLU   B CB    1 
ATOM   10600 C  CG    . GLU   B  1  236  ? 16.977  14.356  114.235 1.00 23.50 ? 234  GLU   B CG    1 
ATOM   10601 C  CD    . GLU   B  1  236  ? 18.486  14.393  114.363 1.00 31.06 ? 234  GLU   B CD    1 
ATOM   10602 O  OE1   . GLU   B  1  236  ? 19.127  15.208  113.665 1.00 38.19 ? 234  GLU   B OE1   1 
ATOM   10603 O  OE2   . GLU   B  1  236  ? 19.026  13.600  115.160 1.00 35.37 ? 234  GLU   B OE2   1 
ATOM   10604 N  N     . ARG   B  1  237  ? 14.120  17.087  114.369 1.00 16.92 ? 235  ARG   B N     1 
ATOM   10605 C  CA    . ARG   B  1  237  ? 13.378  17.646  115.489 1.00 19.51 ? 235  ARG   B CA    1 
ATOM   10606 C  C     . ARG   B  1  237  ? 11.919  17.215  115.451 1.00 19.29 ? 235  ARG   B C     1 
ATOM   10607 O  O     . ARG   B  1  237  ? 11.365  16.778  116.467 1.00 19.38 ? 235  ARG   B O     1 
ATOM   10608 C  CB    . ARG   B  1  237  ? 13.480  19.169  115.482 1.00 22.51 ? 235  ARG   B CB    1 
ATOM   10609 C  CG    . ARG   B  1  237  ? 12.753  19.795  116.651 1.00 24.93 ? 235  ARG   B CG    1 
ATOM   10610 C  CD    . ARG   B  1  237  ? 12.692  21.299  116.547 1.00 31.79 ? 235  ARG   B CD    1 
ATOM   10611 N  NE    . ARG   B  1  237  ? 12.018  21.840  117.721 1.00 34.91 ? 235  ARG   B NE    1 
ATOM   10612 C  CZ    . ARG   B  1  237  ? 12.131  23.090  118.139 1.00 36.40 ? 235  ARG   B CZ    1 
ATOM   10613 N  NH1   . ARG   B  1  237  ? 12.891  23.965  117.501 1.00 40.26 ? 235  ARG   B NH1   1 
ATOM   10614 N  NH2   . ARG   B  1  237  ? 11.481  23.467  119.237 1.00 36.03 ? 235  ARG   B NH2   1 
ATOM   10615 N  N     . TYR   B  1  238  ? 11.278  17.323  114.283 1.00 17.48 ? 236  TYR   B N     1 
ATOM   10616 C  CA    . TYR   B  1  238  ? 9.871   16.940  114.188 1.00 17.09 ? 236  TYR   B CA    1 
ATOM   10617 C  C     . TYR   B  1  238  ? 9.691   15.464  114.497 1.00 18.43 ? 236  TYR   B C     1 
ATOM   10618 O  O     . TYR   B  1  238  ? 8.707   15.071  115.139 1.00 17.61 ? 236  TYR   B O     1 
ATOM   10619 C  CB    . TYR   B  1  238  ? 9.322   17.233  112.795 1.00 17.58 ? 236  TYR   B CB    1 
ATOM   10620 C  CG    . TYR   B  1  238  ? 9.212   18.700  112.464 1.00 18.37 ? 236  TYR   B CG    1 
ATOM   10621 C  CD1   . TYR   B  1  238  ? 8.999   19.650  113.452 1.00 21.94 ? 236  TYR   B CD1   1 
ATOM   10622 C  CD2   . TYR   B  1  238  ? 9.331   19.132  111.154 1.00 18.57 ? 236  TYR   B CD2   1 
ATOM   10623 C  CE1   . TYR   B  1  238  ? 8.907   21.003  113.139 1.00 27.01 ? 236  TYR   B CE1   1 
ATOM   10624 C  CE2   . TYR   B  1  238  ? 9.242   20.468  110.831 1.00 20.79 ? 236  TYR   B CE2   1 
ATOM   10625 C  CZ    . TYR   B  1  238  ? 9.029   21.397  111.817 1.00 27.57 ? 236  TYR   B CZ    1 
ATOM   10626 O  OH    . TYR   B  1  238  ? 8.950   22.727  111.463 1.00 29.74 ? 236  TYR   B OH    1 
ATOM   10627 N  N     . TYR   B  1  239  ? 10.621  14.632  114.032 1.00 17.00 ? 237  TYR   B N     1 
ATOM   10628 C  CA    . TYR   B  1  239  ? 10.569  13.218  114.378 1.00 18.99 ? 237  TYR   B CA    1 
ATOM   10629 C  C     . TYR   B  1  239  ? 10.606  13.030  115.887 1.00 19.31 ? 237  TYR   B C     1 
ATOM   10630 O  O     . TYR   B  1  239  ? 9.783   12.299  116.461 1.00 18.60 ? 237  TYR   B O     1 
ATOM   10631 C  CB    . TYR   B  1  239  ? 11.745  12.478  113.747 1.00 16.86 ? 237  TYR   B CB    1 
ATOM   10632 C  CG    . TYR   B  1  239  ? 11.804  11.038  114.197 1.00 20.24 ? 237  TYR   B CG    1 
ATOM   10633 C  CD1   . TYR   B  1  239  ? 11.072  10.067  113.544 1.00 19.99 ? 237  TYR   B CD1   1 
ATOM   10634 C  CD2   . TYR   B  1  239  ? 12.573  10.652  115.292 1.00 26.66 ? 237  TYR   B CD2   1 
ATOM   10635 C  CE1   . TYR   B  1  239  ? 11.109  8.761   113.954 1.00 17.54 ? 237  TYR   B CE1   1 
ATOM   10636 C  CE2   . TYR   B  1  239  ? 12.606  9.332   115.711 1.00 27.22 ? 237  TYR   B CE2   1 
ATOM   10637 C  CZ    . TYR   B  1  239  ? 11.872  8.395   115.030 1.00 23.67 ? 237  TYR   B CZ    1 
ATOM   10638 O  OH    . TYR   B  1  239  ? 11.887  7.076   115.418 1.00 29.65 ? 237  TYR   B OH    1 
ATOM   10639 N  N     . ARG   B  1  240  ? 11.578  13.665  116.548 1.00 18.59 ? 238  ARG   B N     1 
ATOM   10640 C  CA    . ARG   B  1  240  ? 11.700  13.514  117.992 1.00 20.54 ? 238  ARG   B CA    1 
ATOM   10641 C  C     . ARG   B  1  240  ? 10.466  14.040  118.710 1.00 21.73 ? 238  ARG   B C     1 
ATOM   10642 O  O     . ARG   B  1  240  ? 10.056  13.486  119.739 1.00 22.37 ? 238  ARG   B O     1 
ATOM   10643 C  CB    . ARG   B  1  240  ? 12.953  14.226  118.494 1.00 20.57 ? 238  ARG   B CB    1 
ATOM   10644 C  CG    . ARG   B  1  240  ? 14.233  13.591  118.032 1.00 22.49 ? 238  ARG   B CG    1 
ATOM   10645 C  CD    . ARG   B  1  240  ? 14.338  12.137  118.464 1.00 24.99 ? 238  ARG   B CD    1 
ATOM   10646 N  NE    . ARG   B  1  240  ? 15.559  11.537  117.944 1.00 26.43 ? 238  ARG   B NE    1 
ATOM   10647 C  CZ    . ARG   B  1  240  ? 15.821  10.239  117.954 1.00 36.38 ? 238  ARG   B CZ    1 
ATOM   10648 N  NH1   . ARG   B  1  240  ? 14.967  9.365   118.465 1.00 31.34 ? 238  ARG   B NH1   1 
ATOM   10649 N  NH2   . ARG   B  1  240  ? 16.970  9.806   117.442 1.00 37.49 ? 238  ARG   B NH2   1 
ATOM   10650 N  N     . ASP   B  1  241  ? 9.862   15.112  118.185 1.00 21.30 ? 239  ASP   B N     1 
ATOM   10651 C  CA    . ASP   B  1  241  ? 8.642   15.641  118.784 1.00 23.04 ? 239  ASP   B CA    1 
ATOM   10652 C  C     . ASP   B  1  241  ? 7.496   14.643  118.670 1.00 20.41 ? 239  ASP   B C     1 
ATOM   10653 O  O     . ASP   B  1  241  ? 6.734   14.456  119.619 1.00 19.91 ? 239  ASP   B O     1 
ATOM   10654 C  CB    . ASP   B  1  241  ? 8.262   16.982  118.153 1.00 25.10 ? 239  ASP   B CB    1 
ATOM   10655 C  CG    . ASP   B  1  241  ? 9.239   18.103  118.507 1.00 31.12 ? 239  ASP   B CG    1 
ATOM   10656 O  OD1   . ASP   B  1  241  ? 10.018  17.957  119.479 1.00 35.01 ? 239  ASP   B OD1   1 
ATOM   10657 O  OD2   . ASP   B  1  241  ? 9.220   19.135  117.804 1.00 37.96 ? 239  ASP   B OD2   1 
ATOM   10658 N  N     . TYR   B  1  242  ? 7.357   13.992  117.512 1.00 19.15 ? 240  TYR   B N     1 
ATOM   10659 C  CA    . TYR   B  1  242  ? 6.332   12.965  117.371 1.00 17.81 ? 240  TYR   B CA    1 
ATOM   10660 C  C     . TYR   B  1  242  ? 6.610   11.793  118.292 1.00 18.59 ? 240  TYR   B C     1 
ATOM   10661 O  O     . TYR   B  1  242  ? 5.695   11.261  118.928 1.00 17.34 ? 240  TYR   B O     1 
ATOM   10662 C  CB    . TYR   B  1  242  ? 6.321   12.438  115.948 1.00 18.39 ? 240  TYR   B CB    1 
ATOM   10663 C  CG    . TYR   B  1  242  ? 5.742   13.349  114.885 1.00 15.37 ? 240  TYR   B CG    1 
ATOM   10664 C  CD1   . TYR   B  1  242  ? 4.657   14.184  115.138 1.00 18.92 ? 240  TYR   B CD1   1 
ATOM   10665 C  CD2   . TYR   B  1  242  ? 6.274   13.341  113.615 1.00 17.26 ? 240  TYR   B CD2   1 
ATOM   10666 C  CE1   . TYR   B  1  242  ? 4.122   14.988  114.136 1.00 19.20 ? 240  TYR   B CE1   1 
ATOM   10667 C  CE2   . TYR   B  1  242  ? 5.759   14.132  112.622 1.00 19.64 ? 240  TYR   B CE2   1 
ATOM   10668 C  CZ    . TYR   B  1  242  ? 4.689   14.953  112.878 1.00 20.95 ? 240  TYR   B CZ    1 
ATOM   10669 O  OH    . TYR   B  1  242  ? 4.189   15.721  111.846 1.00 20.29 ? 240  TYR   B OH    1 
ATOM   10670 N  N     . GLU   B  1  243  ? 7.872   11.367  118.360 1.00 19.13 ? 241  GLU   B N     1 
ATOM   10671 C  CA    . GLU   B  1  243  ? 8.228   10.238  119.211 1.00 18.67 ? 241  GLU   B CA    1 
ATOM   10672 C  C     . GLU   B  1  243  ? 7.876   10.532  120.659 1.00 20.48 ? 241  GLU   B C     1 
ATOM   10673 O  O     . GLU   B  1  243  ? 7.280   9.701   121.358 1.00 17.57 ? 241  GLU   B O     1 
ATOM   10674 C  CB    . GLU   B  1  243  ? 9.727   9.981   119.080 1.00 17.39 ? 241  GLU   B CB    1 
ATOM   10675 C  CG    . GLU   B  1  243  ? 10.245  8.865   119.961 1.00 23.07 ? 241  GLU   B CG    1 
ATOM   10676 C  CD    . GLU   B  1  243  ? 11.764  8.780   119.937 1.00 27.17 ? 241  GLU   B CD    1 
ATOM   10677 O  OE1   . GLU   B  1  243  ? 12.422  9.831   119.778 1.00 28.76 ? 241  GLU   B OE1   1 
ATOM   10678 O  OE2   . GLU   B  1  243  ? 12.298  7.660   120.066 1.00 30.79 ? 241  GLU   B OE2   1 
ATOM   10679 N  N     . SER   B  1  244  ? 8.261   11.717  121.132 1.00 17.93 ? 242  SER   B N     1 
ATOM   10680 C  CA    A SER   B  1  244  ? 7.969   12.105  122.504 0.52 18.71 ? 242  SER   B CA    1 
ATOM   10681 C  CA    B SER   B  1  244  ? 7.967   12.087  122.509 0.48 18.71 ? 242  SER   B CA    1 
ATOM   10682 C  C     . SER   B  1  244  ? 6.467   12.164  122.741 1.00 18.06 ? 242  SER   B C     1 
ATOM   10683 O  O     . SER   B  1  244  ? 5.972   11.725  123.786 1.00 18.07 ? 242  SER   B O     1 
ATOM   10684 C  CB    A SER   B  1  244  ? 8.598   13.471  122.766 0.52 20.67 ? 242  SER   B CB    1 
ATOM   10685 C  CB    B SER   B  1  244  ? 8.626   13.424  122.839 0.48 20.69 ? 242  SER   B CB    1 
ATOM   10686 O  OG    A SER   B  1  244  ? 8.303   13.936  124.063 0.52 22.10 ? 242  SER   B OG    1 
ATOM   10687 O  OG    B SER   B  1  244  ? 10.034  13.286  122.893 0.48 21.16 ? 242  SER   B OG    1 
ATOM   10688 N  N     . ALA   B  1  245  ? 5.730   12.707  121.773 1.00 19.36 ? 243  ALA   B N     1 
ATOM   10689 C  CA    . ALA   B  1  245  ? 4.283   12.783  121.904 1.00 19.95 ? 243  ALA   B CA    1 
ATOM   10690 C  C     . ALA   B  1  245  ? 3.651   11.395  121.935 1.00 20.91 ? 243  ALA   B C     1 
ATOM   10691 O  O     . ALA   B  1  245  ? 2.718   11.152  122.709 1.00 20.27 ? 243  ALA   B O     1 
ATOM   10692 C  CB    . ALA   B  1  245  ? 3.701   13.606  120.759 1.00 19.89 ? 243  ALA   B CB    1 
ATOM   10693 N  N     . ILE   B  1  246  ? 4.136   10.473  121.099 1.00 18.90 ? 244  ILE   B N     1 
ATOM   10694 C  CA    . ILE   B  1  246  ? 3.573   9.122   121.106 1.00 17.60 ? 244  ILE   B CA    1 
ATOM   10695 C  C     . ILE   B  1  246  ? 3.710   8.488   122.480 1.00 19.10 ? 244  ILE   B C     1 
ATOM   10696 O  O     . ILE   B  1  246  ? 2.775   7.868   122.986 1.00 20.35 ? 244  ILE   B O     1 
ATOM   10697 C  CB    . ILE   B  1  246  ? 4.195   8.252   120.003 1.00 17.45 ? 244  ILE   B CB    1 
ATOM   10698 C  CG1   . ILE   B  1  246  ? 3.719   8.735   118.646 1.00 20.41 ? 244  ILE   B CG1   1 
ATOM   10699 C  CG2   . ILE   B  1  246  ? 3.790   6.791   120.194 1.00 20.39 ? 244  ILE   B CG2   1 
ATOM   10700 C  CD1   . ILE   B  1  246  ? 4.431   8.059   117.490 1.00 21.05 ? 244  ILE   B CD1   1 
ATOM   10701 N  N     . HIS   B  1  247  ? 4.883   8.616   123.097 1.00 19.62 ? 245  HIS   B N     1 
ATOM   10702 C  CA    . HIS   B  1  247  ? 5.040   8.080   124.445 1.00 20.00 ? 245  HIS   B CA    1 
ATOM   10703 C  C     . HIS   B  1  247  ? 4.040   8.692   125.412 1.00 18.54 ? 245  HIS   B C     1 
ATOM   10704 O  O     . HIS   B  1  247  ? 3.446   7.980   126.225 1.00 21.40 ? 245  HIS   B O     1 
ATOM   10705 C  CB    . HIS   B  1  247  ? 6.469   8.275   124.943 1.00 19.91 ? 245  HIS   B CB    1 
ATOM   10706 C  CG    . HIS   B  1  247  ? 7.441   7.350   124.290 1.00 19.88 ? 245  HIS   B CG    1 
ATOM   10707 N  ND1   . HIS   B  1  247  ? 7.427   5.991   124.510 1.00 20.91 ? 245  HIS   B ND1   1 
ATOM   10708 C  CD2   . HIS   B  1  247  ? 8.439   7.582   123.406 1.00 23.09 ? 245  HIS   B CD2   1 
ATOM   10709 C  CE1   . HIS   B  1  247  ? 8.382   5.425   123.795 1.00 22.45 ? 245  HIS   B CE1   1 
ATOM   10710 N  NE2   . HIS   B  1  247  ? 9.007   6.368   123.111 1.00 24.65 ? 245  HIS   B NE2   1 
ATOM   10711 N  N     . ALA   B  1  248  ? 3.840   10.008  125.340 1.00 19.13 ? 246  ALA   B N     1 
ATOM   10712 C  CA    . ALA   B  1  248  ? 2.908   10.649  126.260 1.00 18.66 ? 246  ALA   B CA    1 
ATOM   10713 C  C     . ALA   B  1  248  ? 1.473   10.241  125.950 1.00 18.82 ? 246  ALA   B C     1 
ATOM   10714 O  O     . ALA   B  1  248  ? 0.696   9.919   126.857 1.00 22.27 ? 246  ALA   B O     1 
ATOM   10715 C  CB    . ALA   B  1  248  ? 3.064   12.170  126.173 1.00 22.57 ? 246  ALA   B CB    1 
ATOM   10716 N  N     . ILE   B  1  249  ? 1.107   10.258  124.666 1.00 19.14 ? 247  ILE   B N     1 
ATOM   10717 C  CA    . ILE   B  1  249  ? -0.254  9.903   124.275 1.00 18.55 ? 247  ILE   B CA    1 
ATOM   10718 C  C     . ILE   B  1  249  ? -0.522  8.438   124.563 1.00 21.34 ? 247  ILE   B C     1 
ATOM   10719 O  O     . ILE   B  1  249  ? -1.605  8.067   125.037 1.00 22.15 ? 247  ILE   B O     1 
ATOM   10720 C  CB    . ILE   B  1  249  ? -0.474  10.232  122.793 1.00 18.04 ? 247  ILE   B CB    1 
ATOM   10721 C  CG1   . ILE   B  1  249  ? -0.403  11.734  122.563 1.00 17.58 ? 247  ILE   B CG1   1 
ATOM   10722 C  CG2   . ILE   B  1  249  ? -1.813  9.647   122.306 1.00 20.83 ? 247  ILE   B CG2   1 
ATOM   10723 C  CD1   . ILE   B  1  249  ? -0.083  12.098  121.120 1.00 20.22 ? 247  ILE   B CD1   1 
ATOM   10724 N  N     . GLY   B  1  250  ? 0.464   7.584   124.292 1.00 20.65 ? 248  GLY   B N     1 
ATOM   10725 C  CA    . GLY   B  1  250  ? 0.288   6.165   124.534 1.00 20.12 ? 248  GLY   B CA    1 
ATOM   10726 C  C     . GLY   B  1  250  ? 0.137   5.846   126.004 1.00 23.67 ? 248  GLY   B C     1 
ATOM   10727 O  O     . GLY   B  1  250  ? -0.675  5.002   126.388 1.00 23.50 ? 248  GLY   B O     1 
ATOM   10728 N  N     . LYS   B  1  251  ? 0.916   6.512   126.850 1.00 21.91 ? 249  LYS   B N     1 
ATOM   10729 C  CA    . LYS   B  1  251  ? 0.766   6.269   128.277 1.00 25.24 ? 249  LYS   B CA    1 
ATOM   10730 C  C     . LYS   B  1  251  ? -0.577  6.791   128.775 1.00 24.47 ? 249  LYS   B C     1 
ATOM   10731 O  O     . LYS   B  1  251  ? -1.249  6.130   129.575 1.00 24.84 ? 249  LYS   B O     1 
ATOM   10732 C  CB    . LYS   B  1  251  ? 1.940   6.880   129.043 1.00 26.08 ? 249  LYS   B CB    1 
ATOM   10733 N  N     . ALA   B  1  252  ? -0.996  7.960   128.282 1.00 24.45 ? 250  ALA   B N     1 
ATOM   10734 C  CA    . ALA   B  1  252  ? -2.297  8.507   128.660 1.00 24.86 ? 250  ALA   B CA    1 
ATOM   10735 C  C     . ALA   B  1  252  ? -3.439  7.643   128.141 1.00 23.84 ? 250  ALA   B C     1 
ATOM   10736 O  O     . ALA   B  1  252  ? -4.480  7.526   128.796 1.00 26.34 ? 250  ALA   B O     1 
ATOM   10737 C  CB    . ALA   B  1  252  ? -2.440  9.932   128.131 1.00 26.51 ? 250  ALA   B CB    1 
ATOM   10738 N  N     . SER   B  1  253  ? -3.276  7.059   126.955 1.00 23.05 ? 251  SER   B N     1 
ATOM   10739 C  CA    . SER   B  1  253  ? -4.309  6.177   126.422 1.00 25.03 ? 251  SER   B CA    1 
ATOM   10740 C  C     . SER   B  1  253  ? -4.599  5.040   127.388 1.00 26.19 ? 251  SER   B C     1 
ATOM   10741 O  O     . SER   B  1  253  ? -5.764  4.688   127.620 1.00 27.84 ? 251  SER   B O     1 
ATOM   10742 C  CB    . SER   B  1  253  ? -3.867  5.610   125.081 1.00 22.93 ? 251  SER   B CB    1 
ATOM   10743 O  OG    . SER   B  1  253  ? -4.836  4.698   124.591 1.00 23.96 ? 251  SER   B OG    1 
ATOM   10744 N  N     . ALA   B  1  254  ? -3.544  4.447   127.953 1.00 25.10 ? 252  ALA   B N     1 
ATOM   10745 C  CA    . ALA   B  1  254  ? -3.663  3.451   129.019 1.00 27.08 ? 252  ALA   B CA    1 
ATOM   10746 C  C     . ALA   B  1  254  ? -4.550  2.275   128.612 1.00 29.04 ? 252  ALA   B C     1 
ATOM   10747 O  O     . ALA   B  1  254  ? -5.391  1.809   129.383 1.00 30.54 ? 252  ALA   B O     1 
ATOM   10748 C  CB    . ALA   B  1  254  ? -4.101  4.080   130.344 1.00 26.47 ? 252  ALA   B CB    1 
ATOM   10749 N  N     . GLY   B  1  255  ? -4.367  1.803   127.380 1.00 30.74 ? 253  GLY   B N     1 
ATOM   10750 C  CA    . GLY   B  1  255  ? -5.076  0.637   126.895 1.00 29.63 ? 253  GLY   B CA    1 
ATOM   10751 C  C     . GLY   B  1  255  ? -6.488  0.886   126.421 1.00 28.92 ? 253  GLY   B C     1 
ATOM   10752 O  O     . GLY   B  1  255  ? -7.220  -0.080  126.189 1.00 30.65 ? 253  GLY   B O     1 
ATOM   10753 N  N     . ARG   B  1  256  ? -6.902  2.146   126.279 1.00 24.90 ? 254  ARG   B N     1 
ATOM   10754 C  CA    . ARG   B  1  256  ? -8.241  2.431   125.776 1.00 27.71 ? 254  ARG   B CA    1 
ATOM   10755 C  C     . ARG   B  1  256  ? -8.438  2.015   124.325 1.00 26.75 ? 254  ARG   B C     1 
ATOM   10756 O  O     . ARG   B  1  256  ? -9.585  1.938   123.871 1.00 28.94 ? 254  ARG   B O     1 
ATOM   10757 C  CB    . ARG   B  1  256  ? -8.586  3.908   125.948 1.00 27.82 ? 254  ARG   B CB    1 
ATOM   10758 C  CG    . ARG   B  1  256  ? -9.080  4.242   127.341 1.00 27.65 ? 254  ARG   B CG    1 
ATOM   10759 C  CD    . ARG   B  1  256  ? -9.371  5.716   127.459 1.00 29.83 ? 254  ARG   B CD    1 
ATOM   10760 N  NE    . ARG   B  1  256  ? -8.136  6.484   127.539 1.00 28.99 ? 254  ARG   B NE    1 
ATOM   10761 C  CZ    . ARG   B  1  256  ? -8.056  7.792   127.354 1.00 26.17 ? 254  ARG   B CZ    1 
ATOM   10762 N  NH1   . ARG   B  1  256  ? -9.114  8.504   127.004 1.00 28.57 ? 254  ARG   B NH1   1 
ATOM   10763 N  NH2   . ARG   B  1  256  ? -6.884  8.403   127.526 1.00 28.60 ? 254  ARG   B NH2   1 
ATOM   10764 N  N     . GLY   B  1  257  ? -7.364  1.749   123.589 1.00 27.84 ? 255  GLY   B N     1 
ATOM   10765 C  CA    . GLY   B  1  257  ? -7.494  1.313   122.215 1.00 26.35 ? 255  GLY   B CA    1 
ATOM   10766 C  C     . GLY   B  1  257  ? -7.616  2.467   121.244 1.00 23.39 ? 255  GLY   B C     1 
ATOM   10767 O  O     . GLY   B  1  257  ? -7.687  3.642   121.604 1.00 24.30 ? 255  GLY   B O     1 
ATOM   10768 N  N     . ILE   B  1  258  ? -7.665  2.111   119.963 1.00 24.33 ? 256  ILE   B N     1 
ATOM   10769 C  CA    . ILE   B  1  258  ? -7.578  3.121   118.919 1.00 25.52 ? 256  ILE   B CA    1 
ATOM   10770 C  C     . ILE   B  1  258  ? -8.867  3.911   118.718 1.00 23.13 ? 256  ILE   B C     1 
ATOM   10771 O  O     . ILE   B  1  258  ? -8.820  4.993   118.119 1.00 23.38 ? 256  ILE   B O     1 
ATOM   10772 C  CB    . ILE   B  1  258  ? -7.110  2.478   117.610 1.00 27.58 ? 256  ILE   B CB    1 
ATOM   10773 C  CG1   . ILE   B  1  258  ? -8.114  1.418   117.176 1.00 27.74 ? 256  ILE   B CG1   1 
ATOM   10774 C  CG2   . ILE   B  1  258  ? -5.736  1.858   117.794 1.00 25.84 ? 256  ILE   B CG2   1 
ATOM   10775 C  CD1   . ILE   B  1  258  ? -7.752  0.756   115.875 1.00 30.54 ? 256  ILE   B CD1   1 
ATOM   10776 N  N     . TYR   B  1  259  ? -10.009 3.426   119.207 1.00 24.79 ? 257  TYR   B N     1 
ATOM   10777 C  CA    . TYR   B  1  259  ? -11.271 4.131   118.988 1.00 24.85 ? 257  TYR   B CA    1 
ATOM   10778 C  C     . TYR   B  1  259  ? -11.617 5.065   120.140 1.00 25.90 ? 257  TYR   B C     1 
ATOM   10779 O  O     . TYR   B  1  259  ? -11.835 6.261   119.928 1.00 25.52 ? 257  TYR   B O     1 
ATOM   10780 C  CB    . TYR   B  1  259  ? -12.409 3.131   118.725 1.00 25.64 ? 257  TYR   B CB    1 
ATOM   10781 C  CG    . TYR   B  1  259  ? -12.042 2.160   117.631 1.00 26.33 ? 257  TYR   B CG    1 
ATOM   10782 C  CD1   . TYR   B  1  259  ? -11.930 2.588   116.319 1.00 27.87 ? 257  TYR   B CD1   1 
ATOM   10783 C  CD2   . TYR   B  1  259  ? -11.768 0.828   117.912 1.00 28.46 ? 257  TYR   B CD2   1 
ATOM   10784 C  CE1   . TYR   B  1  259  ? -11.571 1.720   115.310 1.00 30.03 ? 257  TYR   B CE1   1 
ATOM   10785 C  CE2   . TYR   B  1  259  ? -11.409 -0.051  116.901 1.00 27.24 ? 257  TYR   B CE2   1 
ATOM   10786 C  CZ    . TYR   B  1  259  ? -11.311 0.405   115.606 1.00 28.92 ? 257  TYR   B CZ    1 
ATOM   10787 O  OH    . TYR   B  1  259  ? -10.950 -0.452  114.593 1.00 31.05 ? 257  TYR   B OH    1 
ATOM   10788 N  N     . GLU   B  1  260  ? -11.668 4.539   121.362 1.00 25.55 ? 258  GLU   B N     1 
ATOM   10789 C  CA    . GLU   B  1  260  ? -11.935 5.395   122.510 1.00 26.38 ? 258  GLU   B CA    1 
ATOM   10790 C  C     . GLU   B  1  260  ? -10.735 6.274   122.828 1.00 29.66 ? 258  GLU   B C     1 
ATOM   10791 O  O     . GLU   B  1  260  ? -10.889 7.451   123.181 1.00 31.33 ? 258  GLU   B O     1 
ATOM   10792 C  CB    . GLU   B  1  260  ? -12.300 4.543   123.723 1.00 29.98 ? 258  GLU   B CB    1 
ATOM   10793 C  CG    . GLU   B  1  260  ? -12.503 5.359   124.984 1.00 39.24 ? 258  GLU   B CG    1 
ATOM   10794 C  CD    . GLU   B  1  260  ? -12.766 4.502   126.210 1.00 38.30 ? 258  GLU   B CD    1 
ATOM   10795 O  OE1   . GLU   B  1  260  ? -12.929 3.271   126.058 1.00 43.79 ? 258  GLU   B OE1   1 
ATOM   10796 O  OE2   . GLU   B  1  260  ? -12.804 5.066   127.326 1.00 43.12 ? 258  GLU   B OE2   1 
ATOM   10797 N  N     . GLY   B  1  261  ? -9.536  5.725   122.691 1.00 24.36 ? 259  GLY   B N     1 
ATOM   10798 C  CA    . GLY   B  1  261  ? -8.345  6.383   123.163 1.00 24.59 ? 259  GLY   B CA    1 
ATOM   10799 C  C     . GLY   B  1  261  ? -7.775  7.340   122.141 1.00 24.89 ? 259  GLY   B C     1 
ATOM   10800 O  O     . GLY   B  1  261  ? -8.126  7.316   120.958 1.00 22.29 ? 259  GLY   B O     1 
ATOM   10801 N  N     . PRO   B  1  262  ? -6.865  8.195   122.589 1.00 21.18 ? 260  PRO   B N     1 
ATOM   10802 C  CA    . PRO   B  1  262  ? -6.305  9.218   121.701 1.00 22.49 ? 260  PRO   B CA    1 
ATOM   10803 C  C     . PRO   B  1  262  ? -5.313  8.635   120.710 1.00 23.32 ? 260  PRO   B C     1 
ATOM   10804 O  O     . PRO   B  1  262  ? -4.753  7.549   120.890 1.00 22.83 ? 260  PRO   B O     1 
ATOM   10805 C  CB    . PRO   B  1  262  ? -5.592  10.167  122.670 1.00 22.10 ? 260  PRO   B CB    1 
ATOM   10806 C  CG    . PRO   B  1  262  ? -5.230  9.286   123.845 1.00 23.76 ? 260  PRO   B CG    1 
ATOM   10807 C  CD    . PRO   B  1  262  ? -6.406  8.352   123.979 1.00 22.33 ? 260  PRO   B CD    1 
ATOM   10808 N  N     . GLY   B  1  263  ? -5.098  9.402   119.644 1.00 20.31 ? 261  GLY   B N     1 
ATOM   10809 C  CA    . GLY   B  1  263  ? -4.117  9.064   118.634 1.00 19.80 ? 261  GLY   B CA    1 
ATOM   10810 C  C     . GLY   B  1  263  ? -3.252  10.264  118.286 1.00 20.32 ? 261  GLY   B C     1 
ATOM   10811 O  O     . GLY   B  1  263  ? -3.343  11.331  118.902 1.00 20.98 ? 261  GLY   B O     1 
ATOM   10812 N  N     . ILE   B  1  264  ? -2.405  10.057  117.294 1.00 19.27 ? 262  ILE   B N     1 
ATOM   10813 C  CA    . ILE   B  1  264  ? -1.522  11.112  116.826 1.00 18.67 ? 262  ILE   B CA    1 
ATOM   10814 C  C     . ILE   B  1  264  ? -1.667  11.239  115.319 1.00 18.57 ? 262  ILE   B C     1 
ATOM   10815 O  O     . ILE   B  1  264  ? -1.987  10.269  114.625 1.00 19.97 ? 262  ILE   B O     1 
ATOM   10816 C  CB    . ILE   B  1  264  ? -0.058  10.840  117.236 1.00 17.91 ? 262  ILE   B CB    1 
ATOM   10817 C  CG1   . ILE   B  1  264  ? 0.767   12.118  117.084 1.00 18.31 ? 262  ILE   B CG1   1 
ATOM   10818 C  CG2   . ILE   B  1  264  ? 0.520   9.694   116.431 1.00 21.60 ? 262  ILE   B CG2   1 
ATOM   10819 C  CD1   . ILE   B  1  264  ? 2.229   11.992  117.545 1.00 20.86 ? 262  ILE   B CD1   1 
ATOM   10820 N  N     . SER   B  1  265  ? -1.483  12.458  114.816 1.00 15.93 ? 263  SER   B N     1 
ATOM   10821 C  CA    . SER   B  1  265  ? -1.493  12.728  113.386 1.00 18.04 ? 263  SER   B CA    1 
ATOM   10822 C  C     . SER   B  1  265  ? -0.128  13.272  113.001 1.00 19.22 ? 263  SER   B C     1 
ATOM   10823 O  O     . SER   B  1  265  ? 0.425   14.124  113.702 1.00 20.91 ? 263  SER   B O     1 
ATOM   10824 C  CB    . SER   B  1  265  ? -2.541  13.774  113.027 1.00 21.64 ? 263  SER   B CB    1 
ATOM   10825 O  OG    . SER   B  1  265  ? -3.841  13.213  113.000 1.00 21.00 ? 263  SER   B OG    1 
ATOM   10826 N  N     . ILE   B  1  266  ? 0.422   12.777  111.898 1.00 16.15 ? 264  ILE   B N     1 
ATOM   10827 C  CA    . ILE   B  1  266  ? 1.730   13.218  111.436 1.00 17.75 ? 264  ILE   B CA    1 
ATOM   10828 C  C     . ILE   B  1  266  ? 1.624   13.686  109.997 1.00 17.10 ? 264  ILE   B C     1 
ATOM   10829 O  O     . ILE   B  1  266  ? 0.683   13.352  109.275 1.00 17.42 ? 264  ILE   B O     1 
ATOM   10830 C  CB    . ILE   B  1  266  ? 2.811   12.126  111.556 1.00 17.57 ? 264  ILE   B CB    1 
ATOM   10831 C  CG1   . ILE   B  1  266  ? 2.493   10.958  110.628 1.00 19.54 ? 264  ILE   B CG1   1 
ATOM   10832 C  CG2   . ILE   B  1  266  ? 2.915   11.646  112.991 1.00 19.08 ? 264  ILE   B CG2   1 
ATOM   10833 C  CD1   . ILE   B  1  266  ? 3.583   9.906   110.559 1.00 24.07 ? 264  ILE   B CD1   1 
ATOM   10834 N  N     . LYS   B  1  267  ? 2.619   14.464  109.583 1.00 17.62 ? 265  LYS   B N     1 
ATOM   10835 C  CA    . LYS   B  1  267  ? 2.753   14.873  108.192 1.00 15.27 ? 265  LYS   B CA    1 
ATOM   10836 C  C     . LYS   B  1  267  ? 4.072   14.335  107.674 1.00 15.79 ? 265  LYS   B C     1 
ATOM   10837 O  O     . LYS   B  1  267  ? 5.118   14.551  108.294 1.00 17.20 ? 265  LYS   B O     1 
ATOM   10838 C  CB    . LYS   B  1  267  ? 2.709   16.398  108.063 1.00 18.21 ? 265  LYS   B CB    1 
ATOM   10839 C  CG    . LYS   B  1  267  ? 1.327   16.973  108.367 1.00 18.80 ? 265  LYS   B CG    1 
ATOM   10840 C  CD    . LYS   B  1  267  ? 1.342   18.489  108.427 1.00 26.61 ? 265  LYS   B CD    1 
ATOM   10841 C  CE    . LYS   B  1  267  ? -0.053  19.038  108.750 1.00 26.94 ? 265  LYS   B CE    1 
ATOM   10842 N  NZ    . LYS   B  1  267  ? -0.640  18.416  109.972 1.00 27.83 ? 265  LYS   B NZ    1 
ATOM   10843 N  N     . LEU   B  1  268  ? 4.014   13.604  106.561 1.00 14.99 ? 266  LEU   B N     1 
ATOM   10844 C  CA    . LEU   B  1  268  ? 5.242   13.077  105.983 1.00 16.60 ? 266  LEU   B CA    1 
ATOM   10845 C  C     . LEU   B  1  268  ? 6.214   14.191  105.619 1.00 17.69 ? 266  LEU   B C     1 
ATOM   10846 O  O     . LEU   B  1  268  ? 7.432   14.008  105.741 1.00 17.02 ? 266  LEU   B O     1 
ATOM   10847 C  CB    . LEU   B  1  268  ? 4.938   12.197  104.773 1.00 16.61 ? 266  LEU   B CB    1 
ATOM   10848 C  CG    . LEU   B  1  268  ? 4.041   10.993  105.072 1.00 17.89 ? 266  LEU   B CG    1 
ATOM   10849 C  CD1   . LEU   B  1  268  ? 3.993   10.099  103.856 1.00 19.71 ? 266  LEU   B CD1   1 
ATOM   10850 C  CD2   . LEU   B  1  268  ? 4.547   10.208  106.262 1.00 20.47 ? 266  LEU   B CD2   1 
ATOM   10851 N  N     . SER   B  1  269  ? 5.710   15.364  105.220 1.00 15.79 ? 267  SER   B N     1 
ATOM   10852 C  CA    . SER   B  1  269  ? 6.619   16.462  104.906 1.00 17.49 ? 267  SER   B CA    1 
ATOM   10853 C  C     . SER   B  1  269  ? 7.390   16.943  106.127 1.00 17.22 ? 267  SER   B C     1 
ATOM   10854 O  O     . SER   B  1  269  ? 8.443   17.567  105.968 1.00 17.75 ? 267  SER   B O     1 
ATOM   10855 C  CB    . SER   B  1  269  ? 5.872   17.641  104.284 1.00 17.17 ? 267  SER   B CB    1 
ATOM   10856 O  OG    . SER   B  1  269  ? 5.062   18.303  105.254 1.00 18.04 ? 267  SER   B OG    1 
ATOM   10857 N  N     . ALA   B  1  270  ? 6.907   16.659  107.337 1.00 13.72 ? 268  ALA   B N     1 
ATOM   10858 C  CA    . ALA   B  1  270  ? 7.662   17.012  108.527 1.00 15.41 ? 268  ALA   B CA    1 
ATOM   10859 C  C     . ALA   B  1  270  ? 8.893   16.141  108.687 1.00 18.64 ? 268  ALA   B C     1 
ATOM   10860 O  O     . ALA   B  1  270  ? 9.832   16.532  109.383 1.00 17.39 ? 268  ALA   B O     1 
ATOM   10861 C  CB    . ALA   B  1  270  ? 6.787   16.835  109.771 1.00 17.78 ? 268  ALA   B CB    1 
ATOM   10862 N  N     . LEU   B  1  271  ? 8.902   14.959  108.079 1.00 16.24 ? 269  LEU   B N     1 
ATOM   10863 C  CA    . LEU   B  1  271  ? 9.879   13.940  108.427 1.00 18.15 ? 269  LEU   B CA    1 
ATOM   10864 C  C     . LEU   B  1  271  ? 11.022  13.840  107.437 1.00 16.61 ? 269  LEU   B C     1 
ATOM   10865 O  O     . LEU   B  1  271  ? 11.927  13.027  107.641 1.00 18.08 ? 269  LEU   B O     1 
ATOM   10866 C  CB    . LEU   B  1  271  ? 9.205   12.582  108.573 1.00 17.05 ? 269  LEU   B CB    1 
ATOM   10867 C  CG    . LEU   B  1  271  ? 8.227   12.493  109.748 1.00 17.39 ? 269  LEU   B CG    1 
ATOM   10868 C  CD1   . LEU   B  1  271  ? 7.523   11.154  109.692 1.00 23.48 ? 269  LEU   B CD1   1 
ATOM   10869 C  CD2   . LEU   B  1  271  ? 8.983   12.640  111.047 1.00 17.94 ? 269  LEU   B CD2   1 
ATOM   10870 N  N     . HIS   B  1  272  ? 11.012  14.656  106.387 1.00 16.78 ? 270  HIS   B N     1 
ATOM   10871 C  CA    . HIS   B  1  272  ? 12.126  14.637  105.460 1.00 17.14 ? 270  HIS   B CA    1 
ATOM   10872 C  C     . HIS   B  1  272  ? 12.101  15.942  104.694 1.00 16.56 ? 270  HIS   B C     1 
ATOM   10873 O  O     . HIS   B  1  272  ? 11.018  16.372  104.276 1.00 18.14 ? 270  HIS   B O     1 
ATOM   10874 C  CB    . HIS   B  1  272  ? 11.994  13.475  104.482 1.00 17.93 ? 270  HIS   B CB    1 
ATOM   10875 C  CG    . HIS   B  1  272  ? 13.274  13.161  103.792 1.00 18.71 ? 270  HIS   B CG    1 
ATOM   10876 N  ND1   . HIS   B  1  272  ? 13.757  13.923  102.751 1.00 21.61 ? 270  HIS   B ND1   1 
ATOM   10877 C  CD2   . HIS   B  1  272  ? 14.201  12.200  104.024 1.00 24.69 ? 270  HIS   B CD2   1 
ATOM   10878 C  CE1   . HIS   B  1  272  ? 14.924  13.440  102.364 1.00 20.84 ? 270  HIS   B CE1   1 
ATOM   10879 N  NE2   . HIS   B  1  272  ? 15.210  12.387  103.111 1.00 23.51 ? 270  HIS   B NE2   1 
ATOM   10880 N  N     . PRO   B  1  273  ? 13.250  16.588  104.479 1.00 16.52 ? 271  PRO   B N     1 
ATOM   10881 C  CA    . PRO   B  1  273  ? 13.249  17.883  103.782 1.00 16.86 ? 271  PRO   B CA    1 
ATOM   10882 C  C     . PRO   B  1  273  ? 13.059  17.774  102.278 1.00 16.86 ? 271  PRO   B C     1 
ATOM   10883 O  O     . PRO   B  1  273  ? 12.883  18.808  101.628 1.00 17.85 ? 271  PRO   B O     1 
ATOM   10884 C  CB    . PRO   B  1  273  ? 14.621  18.472  104.135 1.00 19.13 ? 271  PRO   B CB    1 
ATOM   10885 C  CG    . PRO   B  1  273  ? 15.480  17.283  104.408 1.00 18.79 ? 271  PRO   B CG    1 
ATOM   10886 C  CD    . PRO   B  1  273  ? 14.566  16.261  105.051 1.00 18.20 ? 271  PRO   B CD    1 
ATOM   10887 N  N     . ARG   B  1  274  ? 13.077  16.571  101.707 1.00 16.10 ? 272  ARG   B N     1 
ATOM   10888 C  CA    . ARG   B  1  274  ? 12.889  16.362  100.274 1.00 18.78 ? 272  ARG   B CA    1 
ATOM   10889 C  C     . ARG   B  1  274  ? 11.786  15.351  100.038 1.00 18.58 ? 272  ARG   B C     1 
ATOM   10890 O  O     . ARG   B  1  274  ? 11.952  14.348  99.338  1.00 18.05 ? 272  ARG   B O     1 
ATOM   10891 C  CB    . ARG   B  1  274  ? 14.174  15.930  99.567  1.00 18.55 ? 272  ARG   B CB    1 
ATOM   10892 C  CG    . ARG   B  1  274  ? 15.304  16.936  99.662  1.00 19.92 ? 272  ARG   B CG    1 
ATOM   10893 C  CD    . ARG   B  1  274  ? 14.910  18.293  99.078  1.00 20.16 ? 272  ARG   B CD    1 
ATOM   10894 N  NE    . ARG   B  1  274  ? 14.428  18.206  97.701  1.00 19.59 ? 272  ARG   B NE    1 
ATOM   10895 C  CZ    . ARG   B  1  274  ? 15.216  18.113  96.637  1.00 17.54 ? 272  ARG   B CZ    1 
ATOM   10896 N  NH1   . ARG   B  1  274  ? 16.532  18.008  96.758  1.00 19.54 ? 272  ARG   B NH1   1 
ATOM   10897 N  NH2   . ARG   B  1  274  ? 14.672  18.118  95.423  1.00 19.19 ? 272  ARG   B NH2   1 
ATOM   10898 N  N     . TYR   B  1  275  ? 10.631  15.590  100.650 1.00 17.33 ? 273  TYR   B N     1 
ATOM   10899 C  CA    . TYR   B  1  275  ? 9.498   14.687  100.488 1.00 18.06 ? 273  TYR   B CA    1 
ATOM   10900 C  C     . TYR   B  1  275  ? 8.803   15.040  99.176  1.00 18.13 ? 273  TYR   B C     1 
ATOM   10901 O  O     . TYR   B  1  275  ? 7.967   15.940  99.099  1.00 18.04 ? 273  TYR   B O     1 
ATOM   10902 C  CB    . TYR   B  1  275  ? 8.575   14.780  101.693 1.00 17.60 ? 273  TYR   B CB    1 
ATOM   10903 C  CG    . TYR   B  1  275  ? 7.307   14.001  101.521 1.00 16.13 ? 273  TYR   B CG    1 
ATOM   10904 C  CD1   . TYR   B  1  275  ? 7.336   12.664  101.130 1.00 18.21 ? 273  TYR   B CD1   1 
ATOM   10905 C  CD2   . TYR   B  1  275  ? 6.083   14.593  101.753 1.00 15.82 ? 273  TYR   B CD2   1 
ATOM   10906 C  CE1   . TYR   B  1  275  ? 6.169   11.946  100.957 1.00 18.04 ? 273  TYR   B CE1   1 
ATOM   10907 C  CE2   . TYR   B  1  275  ? 4.918   13.886  101.603 1.00 16.25 ? 273  TYR   B CE2   1 
ATOM   10908 C  CZ    . TYR   B  1  275  ? 4.963   12.561  101.197 1.00 18.08 ? 273  TYR   B CZ    1 
ATOM   10909 O  OH    . TYR   B  1  275  ? 3.808   11.854  101.033 1.00 19.26 ? 273  TYR   B OH    1 
ATOM   10910 N  N     . SER   B  1  276  ? 9.184   14.337  98.113  1.00 16.14 ? 274  SER   B N     1 
ATOM   10911 C  CA    . SER   B  1  276  ? 8.650   14.631  96.789  1.00 17.69 ? 274  SER   B CA    1 
ATOM   10912 C  C     . SER   B  1  276  ? 8.898   13.435  95.887  1.00 16.89 ? 274  SER   B C     1 
ATOM   10913 O  O     . SER   B  1  276  ? 9.810   12.637  96.116  1.00 17.02 ? 274  SER   B O     1 
ATOM   10914 C  CB    . SER   B  1  276  ? 9.315   15.859  96.171  1.00 21.96 ? 274  SER   B CB    1 
ATOM   10915 O  OG    . SER   B  1  276  ? 10.654  15.575  95.843  1.00 24.84 ? 274  SER   B OG    1 
ATOM   10916 N  N     . ARG   B  1  277  ? 8.077   13.335  94.843  1.00 15.64 ? 275  ARG   B N     1 
ATOM   10917 C  CA    . ARG   B  1  277  ? 8.247   12.245  93.894  1.00 16.34 ? 275  ARG   B CA    1 
ATOM   10918 C  C     . ARG   B  1  277  ? 9.620   12.290  93.242  1.00 16.67 ? 275  ARG   B C     1 
ATOM   10919 O  O     . ARG   B  1  277  ? 10.205  11.242  92.964  1.00 17.33 ? 275  ARG   B O     1 
ATOM   10920 C  CB    . ARG   B  1  277  ? 7.132   12.286  92.852  1.00 16.55 ? 275  ARG   B CB    1 
ATOM   10921 C  CG    . ARG   B  1  277  ? 7.302   11.321  91.676  1.00 19.07 ? 275  ARG   B CG    1 
ATOM   10922 C  CD    . ARG   B  1  277  ? 7.373   9.888   92.154  1.00 18.99 ? 275  ARG   B CD    1 
ATOM   10923 N  NE    . ARG   B  1  277  ? 7.532   8.955   91.046  1.00 18.23 ? 275  ARG   B NE    1 
ATOM   10924 C  CZ    . ARG   B  1  277  ? 8.700   8.579   90.541  1.00 19.02 ? 275  ARG   B CZ    1 
ATOM   10925 N  NH1   . ARG   B  1  277  ? 9.842   9.092   90.976  1.00 20.47 ? 275  ARG   B NH1   1 
ATOM   10926 N  NH2   . ARG   B  1  277  ? 8.721   7.649   89.585  1.00 18.22 ? 275  ARG   B NH2   1 
ATOM   10927 N  N     . ALA   B  1  278  ? 10.151  13.489  93.003  1.00 17.75 ? 276  ALA   B N     1 
ATOM   10928 C  CA    . ALA   B  1  278  ? 11.469  13.583  92.385  1.00 17.98 ? 276  ALA   B CA    1 
ATOM   10929 C  C     . ALA   B  1  278  ? 12.536  12.942  93.252  1.00 18.27 ? 276  ALA   B C     1 
ATOM   10930 O  O     . ALA   B  1  278  ? 13.577  12.517  92.737  1.00 19.66 ? 276  ALA   B O     1 
ATOM   10931 C  CB    . ALA   B  1  278  ? 11.827  15.040  92.118  1.00 19.22 ? 276  ALA   B CB    1 
ATOM   10932 N  N     . GLN   B  1  279  ? 12.312  12.874  94.561  1.00 15.98 ? 277  GLN   B N     1 
ATOM   10933 C  CA    . GLN   B  1  279  ? 13.264  12.262  95.480  1.00 15.77 ? 277  GLN   B CA    1 
ATOM   10934 C  C     . GLN   B  1  279  ? 12.706  10.983  96.090  1.00 17.29 ? 277  GLN   B C     1 
ATOM   10935 O  O     . GLN   B  1  279  ? 12.975  10.669  97.250  1.00 17.53 ? 277  GLN   B O     1 
ATOM   10936 C  CB    . GLN   B  1  279  ? 13.692  13.243  96.575  1.00 19.96 ? 277  GLN   B CB    1 
ATOM   10937 C  CG    . GLN   B  1  279  ? 14.299  14.518  96.027  1.00 19.34 ? 277  GLN   B CG    1 
ATOM   10938 C  CD    . GLN   B  1  279  ? 15.598  14.242  95.291  1.00 20.36 ? 277  GLN   B CD    1 
ATOM   10939 O  OE1   . GLN   B  1  279  ? 16.271  13.237  95.547  1.00 23.01 ? 277  GLN   B OE1   1 
ATOM   10940 N  NE2   . GLN   B  1  279  ? 15.943  15.116  94.351  1.00 19.94 ? 277  GLN   B NE2   1 
ATOM   10941 N  N     . ALA   B  1  280  ? 11.940  10.226  95.299  1.00 17.16 ? 278  ALA   B N     1 
ATOM   10942 C  CA    . ALA   B  1  280  ? 11.248  9.059   95.834  1.00 17.78 ? 278  ALA   B CA    1 
ATOM   10943 C  C     . ALA   B  1  280  ? 12.215  8.074   96.473  1.00 18.73 ? 278  ALA   B C     1 
ATOM   10944 O  O     . ALA   B  1  280  ? 11.888  7.453   97.487  1.00 17.33 ? 278  ALA   B O     1 
ATOM   10945 C  CB    . ALA   B  1  280  ? 10.437  8.367   94.737  1.00 20.00 ? 278  ALA   B CB    1 
ATOM   10946 N  N     . ALA   B  1  281  ? 13.403  7.899   95.887  1.00 18.69 ? 279  ALA   B N     1 
ATOM   10947 C  CA    . ALA   B  1  281  ? 14.360  6.958   96.464  1.00 20.62 ? 279  ALA   B CA    1 
ATOM   10948 C  C     . ALA   B  1  281  ? 14.759  7.376   97.873  1.00 17.60 ? 279  ALA   B C     1 
ATOM   10949 O  O     . ALA   B  1  281  ? 14.816  6.542   98.784  1.00 19.32 ? 279  ALA   B O     1 
ATOM   10950 C  CB    . ALA   B  1  281  ? 15.590  6.812   95.561  1.00 22.54 ? 279  ALA   B CB    1 
ATOM   10951 N  N     . ARG   B  1  282  ? 15.020  8.664   98.078  1.00 17.74 ? 280  ARG   B N     1 
ATOM   10952 C  CA    . ARG   B  1  282  ? 15.345  9.134   99.419  1.00 17.61 ? 280  ARG   B CA    1 
ATOM   10953 C  C     . ARG   B  1  282  ? 14.143  9.051   100.339 1.00 18.68 ? 280  ARG   B C     1 
ATOM   10954 O  O     . ARG   B  1  282  ? 14.298  8.796   101.533 1.00 19.93 ? 280  ARG   B O     1 
ATOM   10955 C  CB    . ARG   B  1  282  ? 15.841  10.575  99.362  1.00 19.56 ? 280  ARG   B CB    1 
ATOM   10956 C  CG    . ARG   B  1  282  ? 17.205  10.729  98.707  1.00 20.82 ? 280  ARG   B CG    1 
ATOM   10957 C  CD    . ARG   B  1  282  ? 17.738  12.131  98.945  1.00 20.92 ? 280  ARG   B CD    1 
ATOM   10958 N  NE    . ARG   B  1  282  ? 18.072  12.307  100.350 1.00 22.51 ? 280  ARG   B NE    1 
ATOM   10959 C  CZ    . ARG   B  1  282  ? 18.260  13.481  100.934 1.00 19.75 ? 280  ARG   B CZ    1 
ATOM   10960 N  NH1   . ARG   B  1  282  ? 18.162  14.616  100.255 1.00 22.23 ? 280  ARG   B NH1   1 
ATOM   10961 N  NH2   . ARG   B  1  282  ? 18.552  13.519  102.231 1.00 22.85 ? 280  ARG   B NH2   1 
ATOM   10962 N  N     . VAL   B  1  283  ? 12.943  9.255   99.806  1.00 16.75 ? 281  VAL   B N     1 
ATOM   10963 C  CA    . VAL   B  1  283  ? 11.753  9.124   100.636 1.00 17.81 ? 281  VAL   B CA    1 
ATOM   10964 C  C     . VAL   B  1  283  ? 11.630  7.701   101.156 1.00 17.78 ? 281  VAL   B C     1 
ATOM   10965 O  O     . VAL   B  1  283  ? 11.476  7.472   102.362 1.00 19.77 ? 281  VAL   B O     1 
ATOM   10966 C  CB    . VAL   B  1  283  ? 10.514  9.572   99.850  1.00 15.98 ? 281  VAL   B CB    1 
ATOM   10967 C  CG1   . VAL   B  1  283  ? 9.243   9.168   100.583 1.00 17.78 ? 281  VAL   B CG1   1 
ATOM   10968 C  CG2   . VAL   B  1  283  ? 10.572  11.096  99.670  1.00 17.28 ? 281  VAL   B CG2   1 
ATOM   10969 N  N     . MET   B  1  284  ? 11.731  6.719   100.256 1.00 17.01 ? 282  MET   B N     1 
ATOM   10970 C  CA    . MET   B  1  284  ? 11.595  5.330   100.682 1.00 18.18 ? 282  MET   B CA    1 
ATOM   10971 C  C     . MET   B  1  284  ? 12.762  4.898   101.554 1.00 20.89 ? 282  MET   B C     1 
ATOM   10972 O  O     . MET   B  1  284  ? 12.590  4.071   102.456 1.00 22.44 ? 282  MET   B O     1 
ATOM   10973 C  CB    . MET   B  1  284  ? 11.469  4.411   99.467  1.00 17.60 ? 282  MET   B CB    1 
ATOM   10974 C  CG    . MET   B  1  284  ? 10.267  4.706   98.584  1.00 19.30 ? 282  MET   B CG    1 
ATOM   10975 S  SD    . MET   B  1  284  ? 8.693   4.661   99.460  1.00 24.75 ? 282  MET   B SD    1 
ATOM   10976 C  CE    . MET   B  1  284  ? 8.515   2.901   99.729  1.00 24.95 ? 282  MET   B CE    1 
ATOM   10977 N  N     . GLY   B  1  285  ? 13.949  5.448   101.308 1.00 18.13 ? 283  GLY   B N     1 
ATOM   10978 C  CA    . GLY   B  1  285  ? 15.124  5.009   102.041 1.00 21.39 ? 283  GLY   B CA    1 
ATOM   10979 C  C     . GLY   B  1  285  ? 15.307  5.677   103.384 1.00 21.20 ? 283  GLY   B C     1 
ATOM   10980 O  O     . GLY   B  1  285  ? 15.864  5.071   104.305 1.00 23.86 ? 283  GLY   B O     1 
ATOM   10981 N  N     . GLU   B  1  286  ? 14.863  6.919   103.519 1.00 19.00 ? 284  GLU   B N     1 
ATOM   10982 C  CA    . GLU   B  1  286  ? 15.122  7.727   104.705 1.00 18.66 ? 284  GLU   B CA    1 
ATOM   10983 C  C     . GLU   B  1  286  ? 13.865  8.136   105.450 1.00 20.47 ? 284  GLU   B C     1 
ATOM   10984 O  O     . GLU   B  1  286  ? 13.861  8.129   106.684 1.00 24.39 ? 284  GLU   B O     1 
ATOM   10985 C  CB    . GLU   B  1  286  ? 15.914  8.987   104.319 1.00 22.02 ? 284  GLU   B CB    1 
ATOM   10986 C  CG    . GLU   B  1  286  ? 17.185  8.670   103.524 1.00 21.13 ? 284  GLU   B CG    1 
ATOM   10987 C  CD    . GLU   B  1  286  ? 17.793  9.899   102.870 1.00 25.35 ? 284  GLU   B CD    1 
ATOM   10988 O  OE1   . GLU   B  1  286  ? 17.572  11.015  103.377 1.00 25.03 ? 284  GLU   B OE1   1 
ATOM   10989 O  OE2   . GLU   B  1  286  ? 18.492  9.744   101.843 1.00 29.81 ? 284  GLU   B OE2   1 
ATOM   10990 N  N     . LEU   B  1  287  ? 12.799  8.498   104.736 1.00 19.24 ? 285  LEU   B N     1 
ATOM   10991 C  CA    . LEU   B  1  287  ? 11.566  8.908   105.395 1.00 19.97 ? 285  LEU   B CA    1 
ATOM   10992 C  C     . LEU   B  1  287  ? 10.796  7.697   105.904 1.00 20.44 ? 285  LEU   B C     1 
ATOM   10993 O  O     . LEU   B  1  287  ? 10.380  7.663   107.064 1.00 19.42 ? 285  LEU   B O     1 
ATOM   10994 C  CB    . LEU   B  1  287  ? 10.711  9.720   104.422 1.00 18.57 ? 285  LEU   B CB    1 
ATOM   10995 C  CG    . LEU   B  1  287  ? 9.685   10.704  105.008 1.00 21.82 ? 285  LEU   B CG    1 
ATOM   10996 C  CD1   . LEU   B  1  287  ? 9.125   11.566  103.899 1.00 20.23 ? 285  LEU   B CD1   1 
ATOM   10997 C  CD2   . LEU   B  1  287  ? 8.553   10.002  105.715 1.00 21.24 ? 285  LEU   B CD2   1 
ATOM   10998 N  N     . LEU   B  1  288  ? 10.588  6.704   105.041 1.00 20.26 ? 286  LEU   B N     1 
ATOM   10999 C  CA    . LEU   B  1  288  ? 9.835   5.511   105.426 1.00 19.75 ? 286  LEU   B CA    1 
ATOM   11000 C  C     . LEU   B  1  288  ? 10.306  4.866   106.725 1.00 21.71 ? 286  LEU   B C     1 
ATOM   11001 O  O     . LEU   B  1  288  ? 9.454   4.561   107.573 1.00 19.07 ? 286  LEU   B O     1 
ATOM   11002 C  CB    . LEU   B  1  288  ? 9.770   4.527   104.250 1.00 21.60 ? 286  LEU   B CB    1 
ATOM   11003 C  CG    . LEU   B  1  288  ? 9.206   3.162   104.630 1.00 25.28 ? 286  LEU   B CG    1 
ATOM   11004 C  CD1   . LEU   B  1  288  ? 7.747   3.279   105.063 1.00 25.01 ? 286  LEU   B CD1   1 
ATOM   11005 C  CD2   . LEU   B  1  288  ? 9.351   2.198   103.475 1.00 28.00 ? 286  LEU   B CD2   1 
ATOM   11006 N  N     . PRO   B  1  289  ? 11.604  4.646   106.961 1.00 20.11 ? 287  PRO   B N     1 
ATOM   11007 C  CA    . PRO   B  1  289  ? 12.005  4.059   108.252 1.00 21.40 ? 287  PRO   B CA    1 
ATOM   11008 C  C     . PRO   B  1  289  ? 11.595  4.897   109.452 1.00 19.49 ? 287  PRO   B C     1 
ATOM   11009 O  O     . PRO   B  1  289  ? 11.312  4.345   110.523 1.00 21.48 ? 287  PRO   B O     1 
ATOM   11010 C  CB    . PRO   B  1  289  ? 13.530  3.948   108.123 1.00 26.32 ? 287  PRO   B CB    1 
ATOM   11011 C  CG    . PRO   B  1  289  ? 13.755  3.812   106.643 1.00 24.95 ? 287  PRO   B CG    1 
ATOM   11012 C  CD    . PRO   B  1  289  ? 12.745  4.736   106.029 1.00 21.54 ? 287  PRO   B CD    1 
ATOM   11013 N  N     . ARG   B  1  290  ? 11.554  6.220   109.305 1.00 18.81 ? 288  ARG   B N     1 
ATOM   11014 C  CA    A ARG   B  1  290  ? 11.115  7.068   110.408 0.53 20.55 ? 288  ARG   B CA    1 
ATOM   11015 C  CA    B ARG   B  1  290  ? 11.116  7.067   110.408 0.47 20.55 ? 288  ARG   B CA    1 
ATOM   11016 C  C     . ARG   B  1  290  ? 9.631   6.881   110.687 1.00 17.18 ? 288  ARG   B C     1 
ATOM   11017 O  O     . ARG   B  1  290  ? 9.220   6.785   111.850 1.00 18.30 ? 288  ARG   B O     1 
ATOM   11018 C  CB    A ARG   B  1  290  ? 11.440  8.527   110.098 0.53 21.20 ? 288  ARG   B CB    1 
ATOM   11019 C  CB    B ARG   B  1  290  ? 11.456  8.524   110.102 0.47 21.21 ? 288  ARG   B CB    1 
ATOM   11020 C  CG    A ARG   B  1  290  ? 12.941  8.786   110.077 0.53 22.51 ? 288  ARG   B CG    1 
ATOM   11021 C  CG    B ARG   B  1  290  ? 12.964  8.750   109.987 0.47 22.52 ? 288  ARG   B CG    1 
ATOM   11022 C  CD    A ARG   B  1  290  ? 13.289  10.013  109.262 0.53 25.78 ? 288  ARG   B CD    1 
ATOM   11023 C  CD    B ARG   B  1  290  ? 13.283  10.091  109.359 0.47 25.79 ? 288  ARG   B CD    1 
ATOM   11024 N  NE    A ARG   B  1  290  ? 14.723  10.113  109.023 0.53 23.71 ? 288  ARG   B NE    1 
ATOM   11025 N  NE    B ARG   B  1  290  ? 14.061  10.948  110.246 0.47 24.08 ? 288  ARG   B NE    1 
ATOM   11026 C  CZ    A ARG   B  1  290  ? 15.274  10.938  108.144 0.53 26.59 ? 288  ARG   B CZ    1 
ATOM   11027 C  CZ    B ARG   B  1  290  ? 15.170  11.586  109.895 0.47 25.64 ? 288  ARG   B CZ    1 
ATOM   11028 N  NH1   A ARG   B  1  290  ? 14.537  11.760  107.416 0.53 21.44 ? 288  ARG   B NH1   1 
ATOM   11029 N  NH1   B ARG   B  1  290  ? 15.695  11.447  108.690 0.47 30.62 ? 288  ARG   B NH1   1 
ATOM   11030 N  NH2   A ARG   B  1  290  ? 16.596  10.936  107.991 0.53 26.03 ? 288  ARG   B NH2   1 
ATOM   11031 N  NH2   B ARG   B  1  290  ? 15.753  12.401  110.769 0.47 23.95 ? 288  ARG   B NH2   1 
ATOM   11032 N  N     . VAL   B  1  291  ? 8.812   6.810   109.636 1.00 18.55 ? 289  VAL   B N     1 
ATOM   11033 C  CA    . VAL   B  1  291  ? 7.395   6.554   109.858 1.00 18.18 ? 289  VAL   B CA    1 
ATOM   11034 C  C     . VAL   B  1  291  ? 7.207   5.181   110.475 1.00 18.18 ? 289  VAL   B C     1 
ATOM   11035 O  O     . VAL   B  1  291  ? 6.380   4.999   111.381 1.00 19.51 ? 289  VAL   B O     1 
ATOM   11036 C  CB    . VAL   B  1  291  ? 6.601   6.685   108.550 1.00 18.22 ? 289  VAL   B CB    1 
ATOM   11037 C  CG1   . VAL   B  1  291  ? 5.111   6.498   108.834 1.00 22.02 ? 289  VAL   B CG1   1 
ATOM   11038 C  CG2   . VAL   B  1  291  ? 6.860   8.021   107.923 1.00 21.99 ? 289  VAL   B CG2   1 
ATOM   11039 N  N     . LYS   B  1  292  ? 7.958   4.188   109.989 1.00 17.39 ? 290  LYS   B N     1 
ATOM   11040 C  CA    . LYS   B  1  292  ? 7.813   2.851   110.554 1.00 18.99 ? 290  LYS   B CA    1 
ATOM   11041 C  C     . LYS   B  1  292  ? 8.131   2.859   112.043 1.00 21.85 ? 290  LYS   B C     1 
ATOM   11042 O  O     . LYS   B  1  292  ? 7.423   2.238   112.842 1.00 20.83 ? 290  LYS   B O     1 
ATOM   11043 C  CB    . LYS   B  1  292  ? 8.688   1.844   109.803 1.00 21.40 ? 290  LYS   B CB    1 
ATOM   11044 C  CG    . LYS   B  1  292  ? 8.470   0.394   110.237 1.00 26.27 ? 290  LYS   B CG    1 
ATOM   11045 C  CD    . LYS   B  1  292  ? 9.467   -0.026  111.284 1.00 31.94 ? 290  LYS   B CD    1 
ATOM   11046 C  CE    . LYS   B  1  292  ? 9.193   -1.458  111.759 1.00 31.14 ? 290  LYS   B CE    1 
ATOM   11047 N  NZ    . LYS   B  1  292  ? 9.541   -2.471  110.728 1.00 32.50 ? 290  LYS   B NZ    1 
ATOM   11048 N  N     . ALA   B  1  293  ? 9.180   3.583   112.438 1.00 19.39 ? 291  ALA   B N     1 
ATOM   11049 C  CA    . ALA   B  1  293  ? 9.549   3.629   113.848 1.00 21.19 ? 291  ALA   B CA    1 
ATOM   11050 C  C     . ALA   B  1  293  ? 8.446   4.259   114.688 1.00 21.81 ? 291  ALA   B C     1 
ATOM   11051 O  O     . ALA   B  1  293  ? 8.144   3.781   115.790 1.00 20.54 ? 291  ALA   B O     1 
ATOM   11052 C  CB    . ALA   B  1  293  ? 10.854  4.396   114.016 1.00 21.02 ? 291  ALA   B CB    1 
ATOM   11053 N  N     . LEU   B  1  294  ? 7.841   5.337   114.190 1.00 20.22 ? 292  LEU   B N     1 
ATOM   11054 C  CA    . LEU   B  1  294  ? 6.736   5.954   114.916 1.00 20.42 ? 292  LEU   B CA    1 
ATOM   11055 C  C     . LEU   B  1  294  ? 5.524   5.037   114.948 1.00 19.78 ? 292  LEU   B C     1 
ATOM   11056 O  O     . LEU   B  1  294  ? 4.854   4.918   115.981 1.00 20.87 ? 292  LEU   B O     1 
ATOM   11057 C  CB    . LEU   B  1  294  ? 6.369   7.292   114.277 1.00 19.52 ? 292  LEU   B CB    1 
ATOM   11058 C  CG    . LEU   B  1  294  ? 7.493   8.330   114.251 1.00 19.46 ? 292  LEU   B CG    1 
ATOM   11059 C  CD1   . LEU   B  1  294  ? 7.070   9.512   113.410 1.00 21.11 ? 292  LEU   B CD1   1 
ATOM   11060 C  CD2   . LEU   B  1  294  ? 7.863   8.777   115.667 1.00 20.53 ? 292  LEU   B CD2   1 
ATOM   11061 N  N     . ALA   B  1  295  ? 5.218   4.388   113.823 1.00 20.20 ? 293  ALA   B N     1 
ATOM   11062 C  CA    . ALA   B  1  295  ? 4.090   3.467   113.794 1.00 19.77 ? 293  ALA   B CA    1 
ATOM   11063 C  C     . ALA   B  1  295  ? 4.312   2.309   114.755 1.00 21.93 ? 293  ALA   B C     1 
ATOM   11064 O  O     . ALA   B  1  295  ? 3.376   1.858   115.422 1.00 20.81 ? 293  ALA   B O     1 
ATOM   11065 C  CB    . ALA   B  1  295  ? 3.867   2.966   112.364 1.00 20.68 ? 293  ALA   B CB    1 
ATOM   11066 N  N     . LEU   B  1  296  ? 5.553   1.839   114.867 1.00 20.21 ? 294  LEU   B N     1 
ATOM   11067 C  CA    . LEU   B  1  296  ? 5.842   0.760   115.809 1.00 20.04 ? 294  LEU   B CA    1 
ATOM   11068 C  C     . LEU   B  1  296  ? 5.591   1.198   117.247 1.00 22.27 ? 294  LEU   B C     1 
ATOM   11069 O  O     . LEU   B  1  296  ? 5.024   0.441   118.047 1.00 23.25 ? 294  LEU   B O     1 
ATOM   11070 C  CB    . LEU   B  1  296  ? 7.283   0.294   115.621 1.00 24.05 ? 294  LEU   B CB    1 
ATOM   11071 C  CG    . LEU   B  1  296  ? 7.743   -0.903  116.448 1.00 29.21 ? 294  LEU   B CG    1 
ATOM   11072 C  CD1   . LEU   B  1  296  ? 6.788   -2.078  116.274 1.00 31.39 ? 294  LEU   B CD1   1 
ATOM   11073 C  CD2   . LEU   B  1  296  ? 9.158   -1.288  116.031 1.00 34.94 ? 294  LEU   B CD2   1 
ATOM   11074 N  N     . LEU   B  1  297  ? 6.011   2.415   117.602 1.00 20.85 ? 295  LEU   B N     1 
ATOM   11075 C  CA    . LEU   B  1  297  ? 5.669   2.941   118.922 1.00 21.11 ? 295  LEU   B CA    1 
ATOM   11076 C  C     . LEU   B  1  297  ? 4.159   3.041   119.100 1.00 21.36 ? 295  LEU   B C     1 
ATOM   11077 O  O     . LEU   B  1  297  ? 3.624   2.684   120.155 1.00 22.54 ? 295  LEU   B O     1 
ATOM   11078 C  CB    . LEU   B  1  297  ? 6.305   4.312   119.125 1.00 20.27 ? 295  LEU   B CB    1 
ATOM   11079 C  CG    . LEU   B  1  297  ? 7.803   4.406   119.407 1.00 27.70 ? 295  LEU   B CG    1 
ATOM   11080 C  CD1   . LEU   B  1  297  ? 8.219   5.875   119.439 1.00 24.92 ? 295  LEU   B CD1   1 
ATOM   11081 C  CD2   . LEU   B  1  297  ? 8.149   3.734   120.715 1.00 27.41 ? 295  LEU   B CD2   1 
ATOM   11082 N  N     . ALA   B  1  298  ? 3.449   3.539   118.083 1.00 19.01 ? 296  ALA   B N     1 
ATOM   11083 C  CA    . ALA   B  1  298  ? 2.000   3.669   118.212 1.00 19.29 ? 296  ALA   B CA    1 
ATOM   11084 C  C     . ALA   B  1  298  ? 1.352   2.308   118.388 1.00 22.53 ? 296  ALA   B C     1 
ATOM   11085 O  O     . ALA   B  1  298  ? 0.424   2.144   119.191 1.00 23.24 ? 296  ALA   B O     1 
ATOM   11086 C  CB    . ALA   B  1  298  ? 1.423   4.357   116.978 1.00 20.79 ? 296  ALA   B CB    1 
ATOM   11087 N  N     . LYS   B  1  299  ? 1.834   1.315   117.642 1.00 21.17 ? 297  LYS   B N     1 
ATOM   11088 C  CA    . LYS   B  1  299  ? 1.311   -0.032  117.794 1.00 23.32 ? 297  LYS   B CA    1 
ATOM   11089 C  C     . LYS   B  1  299  ? 1.580   -0.565  119.193 1.00 26.07 ? 297  LYS   B C     1 
ATOM   11090 O  O     . LYS   B  1  299  ? 0.709   -1.198  119.799 1.00 26.38 ? 297  LYS   B O     1 
ATOM   11091 C  CB    . LYS   B  1  299  ? 1.920   -0.952  116.739 1.00 24.83 ? 297  LYS   B CB    1 
ATOM   11092 C  CG    . LYS   B  1  299  ? 1.646   -2.423  117.017 1.00 28.71 ? 297  LYS   B CG    1 
ATOM   11093 C  CD    . LYS   B  1  299  ? 2.731   -3.304  116.452 1.00 35.83 ? 297  LYS   B CD    1 
ATOM   11094 C  CE    . LYS   B  1  299  ? 2.376   -4.775  116.617 1.00 34.04 ? 297  LYS   B CE    1 
ATOM   11095 N  NZ    . LYS   B  1  299  ? 2.384   -5.199  118.032 1.00 39.19 ? 297  LYS   B NZ    1 
ATOM   11096 N  N     . ASN   B  1  300  ? 2.774   -0.306  119.733 1.00 23.11 ? 298  ASN   B N     1 
ATOM   11097 C  CA    . ASN   B  1  300  ? 3.086   -0.834  121.057 1.00 25.70 ? 298  ASN   B CA    1 
ATOM   11098 C  C     . ASN   B  1  300  ? 2.168   -0.252  122.122 1.00 24.02 ? 298  ASN   B C     1 
ATOM   11099 O  O     . ASN   B  1  300  ? 1.843   -0.935  123.097 1.00 25.86 ? 298  ASN   B O     1 
ATOM   11100 C  CB    . ASN   B  1  300  ? 4.555   -0.595  121.406 1.00 26.72 ? 298  ASN   B CB    1 
ATOM   11101 C  CG    . ASN   B  1  300  ? 5.502   -1.470  120.587 1.00 28.35 ? 298  ASN   B CG    1 
ATOM   11102 O  OD1   . ASN   B  1  300  ? 5.119   -2.534  120.100 1.00 34.96 ? 298  ASN   B OD1   1 
ATOM   11103 N  ND2   . ASN   B  1  300  ? 6.745   -1.021  120.441 1.00 35.02 ? 298  ASN   B ND2   1 
ATOM   11104 N  N     . TYR   B  1  301  ? 1.729   0.992   121.954 1.00 21.99 ? 299  TYR   B N     1 
ATOM   11105 C  CA    . TYR   B  1  301  ? 0.767   1.582   122.874 1.00 22.32 ? 299  TYR   B CA    1 
ATOM   11106 C  C     . TYR   B  1  301  ? -0.672  1.363   122.440 1.00 21.31 ? 299  TYR   B C     1 
ATOM   11107 O  O     . TYR   B  1  301  ? -1.587  1.765   123.165 1.00 23.14 ? 299  TYR   B O     1 
ATOM   11108 C  CB    . TYR   B  1  301  ? 1.004   3.088   122.997 1.00 20.16 ? 299  TYR   B CB    1 
ATOM   11109 C  CG    . TYR   B  1  301  ? 2.251   3.468   123.761 1.00 22.89 ? 299  TYR   B CG    1 
ATOM   11110 C  CD1   . TYR   B  1  301  ? 2.331   3.269   125.134 1.00 22.85 ? 299  TYR   B CD1   1 
ATOM   11111 C  CD2   . TYR   B  1  301  ? 3.333   4.051   123.116 1.00 20.95 ? 299  TYR   B CD2   1 
ATOM   11112 C  CE1   . TYR   B  1  301  ? 3.463   3.625   125.840 1.00 22.77 ? 299  TYR   B CE1   1 
ATOM   11113 C  CE2   . TYR   B  1  301  ? 4.473   4.417   123.819 1.00 23.98 ? 299  TYR   B CE2   1 
ATOM   11114 C  CZ    . TYR   B  1  301  ? 4.522   4.201   125.175 1.00 23.06 ? 299  TYR   B CZ    1 
ATOM   11115 O  OH    . TYR   B  1  301  ? 5.635   4.554   125.873 1.00 24.38 ? 299  TYR   B OH    1 
ATOM   11116 N  N     . ASP   B  1  302  ? -0.882  0.756   121.273 1.00 20.88 ? 300  ASP   B N     1 
ATOM   11117 C  CA    . ASP   B  1  302  ? -2.200  0.577   120.672 1.00 23.67 ? 300  ASP   B CA    1 
ATOM   11118 C  C     . ASP   B  1  302  ? -2.969  1.892   120.570 1.00 21.44 ? 300  ASP   B C     1 
ATOM   11119 O  O     . ASP   B  1  302  ? -4.098  2.029   121.048 1.00 23.59 ? 300  ASP   B O     1 
ATOM   11120 C  CB    . ASP   B  1  302  ? -3.021  -0.514  121.355 1.00 24.82 ? 300  ASP   B CB    1 
ATOM   11121 C  CG    . ASP   B  1  302  ? -4.127  -1.016  120.455 1.00 28.94 ? 300  ASP   B CG    1 
ATOM   11122 O  OD1   . ASP   B  1  302  ? -3.930  -0.978  119.217 1.00 31.85 ? 300  ASP   B OD1   1 
ATOM   11123 O  OD2   . ASP   B  1  302  ? -5.189  -1.412  120.967 1.00 32.61 ? 300  ASP   B OD2   1 
ATOM   11124 N  N     . ILE   B  1  303  ? -2.337  2.870   119.932 1.00 21.12 ? 301  ILE   B N     1 
ATOM   11125 C  CA    . ILE   B  1  303  ? -2.976  4.136   119.618 1.00 21.11 ? 301  ILE   B CA    1 
ATOM   11126 C  C     . ILE   B  1  303  ? -3.010  4.282   118.104 1.00 22.38 ? 301  ILE   B C     1 
ATOM   11127 O  O     . ILE   B  1  303  ? -2.283  3.606   117.369 1.00 21.48 ? 301  ILE   B O     1 
ATOM   11128 C  CB    . ILE   B  1  303  ? -2.258  5.338   120.269 1.00 19.27 ? 301  ILE   B CB    1 
ATOM   11129 C  CG1   . ILE   B  1  303  ? -0.892  5.556   119.618 1.00 21.78 ? 301  ILE   B CG1   1 
ATOM   11130 C  CG2   . ILE   B  1  303  ? -2.090  5.118   121.759 1.00 20.52 ? 301  ILE   B CG2   1 
ATOM   11131 C  CD1   . ILE   B  1  303  ? -0.269  6.899   119.956 1.00 22.74 ? 301  ILE   B CD1   1 
ATOM   11132 N  N     . GLY   B  1  304  ? -3.858  5.195   117.640 1.00 19.61 ? 302  GLY   B N     1 
ATOM   11133 C  CA    . GLY   B  1  304  ? -3.903  5.492   116.215 1.00 19.30 ? 302  GLY   B CA    1 
ATOM   11134 C  C     . GLY   B  1  304  ? -2.765  6.415   115.805 1.00 22.98 ? 302  GLY   B C     1 
ATOM   11135 O  O     . GLY   B  1  304  ? -2.359  7.311   116.545 1.00 22.19 ? 302  GLY   B O     1 
ATOM   11136 N  N     . LEU   B  1  305  ? -2.238  6.179   114.608 1.00 18.39 ? 303  LEU   B N     1 
ATOM   11137 C  CA    . LEU   B  1  305  ? -1.255  7.073   114.010 1.00 19.41 ? 303  LEU   B CA    1 
ATOM   11138 C  C     . LEU   B  1  305  ? -1.741  7.386   112.612 1.00 18.88 ? 303  LEU   B C     1 
ATOM   11139 O  O     . LEU   B  1  305  ? -1.807  6.490   111.766 1.00 20.39 ? 303  LEU   B O     1 
ATOM   11140 C  CB    . LEU   B  1  305  ? 0.131   6.433   113.968 1.00 20.69 ? 303  LEU   B CB    1 
ATOM   11141 C  CG    . LEU   B  1  305  ? 1.231   7.338   113.403 1.00 22.35 ? 303  LEU   B CG    1 
ATOM   11142 C  CD1   . LEU   B  1  305  ? 2.529   7.163   114.167 1.00 24.94 ? 303  LEU   B CD1   1 
ATOM   11143 C  CD2   . LEU   B  1  305  ? 1.449   7.048   111.932 1.00 26.76 ? 303  LEU   B CD2   1 
ATOM   11144 N  N     . ASN   B  1  306  ? -2.066  8.645   112.369 1.00 18.16 ? 304  ASN   B N     1 
ATOM   11145 C  CA    . ASN   B  1  306  ? -2.697  9.052   111.127 1.00 18.86 ? 304  ASN   B CA    1 
ATOM   11146 C  C     . ASN   B  1  306  ? -1.720  9.855   110.286 1.00 18.27 ? 304  ASN   B C     1 
ATOM   11147 O  O     . ASN   B  1  306  ? -1.034  10.741  110.799 1.00 18.69 ? 304  ASN   B O     1 
ATOM   11148 C  CB    . ASN   B  1  306  ? -3.901  9.936   111.418 1.00 19.47 ? 304  ASN   B CB    1 
ATOM   11149 C  CG    . ASN   B  1  306  ? -4.488  10.500  110.169 1.00 20.90 ? 304  ASN   B CG    1 
ATOM   11150 O  OD1   . ASN   B  1  306  ? -5.200  9.803   109.452 1.00 23.30 ? 304  ASN   B OD1   1 
ATOM   11151 N  ND2   . ASN   B  1  306  ? -4.169  11.755  109.871 1.00 19.27 ? 304  ASN   B ND2   1 
ATOM   11152 N  N     . ILE   B  1  307  ? -1.675  9.559   108.994 1.00 17.86 ? 305  ILE   B N     1 
ATOM   11153 C  CA    . ILE   B  1  307  ? -0.873  10.324  108.049 1.00 18.00 ? 305  ILE   B CA    1 
ATOM   11154 C  C     . ILE   B  1  307  ? -1.775  11.363  107.404 1.00 19.21 ? 305  ILE   B C     1 
ATOM   11155 O  O     . ILE   B  1  307  ? -2.678  11.021  106.628 1.00 16.83 ? 305  ILE   B O     1 
ATOM   11156 C  CB    . ILE   B  1  307  ? -0.231  9.427   106.985 1.00 18.84 ? 305  ILE   B CB    1 
ATOM   11157 C  CG1   . ILE   B  1  307  ? 0.752   8.451   107.642 1.00 21.18 ? 305  ILE   B CG1   1 
ATOM   11158 C  CG2   . ILE   B  1  307  ? 0.418   10.292  105.890 1.00 19.94 ? 305  ILE   B CG2   1 
ATOM   11159 C  CD1   . ILE   B  1  307  ? 1.313   7.423   106.674 1.00 24.61 ? 305  ILE   B CD1   1 
ATOM   11160 N  N     . ASP   B  1  308  ? -1.520  12.632  107.712 1.00 17.78 ? 306  ASP   B N     1 
ATOM   11161 C  CA    . ASP   B  1  308  ? -2.287  13.717  107.124 1.00 18.56 ? 306  ASP   B CA    1 
ATOM   11162 C  C     . ASP   B  1  308  ? -1.996  13.799  105.634 1.00 17.35 ? 306  ASP   B C     1 
ATOM   11163 O  O     . ASP   B  1  308  ? -0.924  13.409  105.165 1.00 18.95 ? 306  ASP   B O     1 
ATOM   11164 C  CB    . ASP   B  1  308  ? -1.923  15.049  107.784 1.00 17.04 ? 306  ASP   B CB    1 
ATOM   11165 C  CG    . ASP   B  1  308  ? -2.397  15.147  109.240 1.00 21.81 ? 306  ASP   B CG    1 
ATOM   11166 O  OD1   . ASP   B  1  308  ? -3.275  14.369  109.649 1.00 20.35 ? 306  ASP   B OD1   1 
ATOM   11167 O  OD2   . ASP   B  1  308  ? -1.886  16.022  109.980 1.00 20.79 ? 306  ASP   B OD2   1 
ATOM   11168 N  N     . ALA   B  1  309  ? -2.971  14.293  104.883 1.00 15.85 ? 307  ALA   B N     1 
ATOM   11169 C  CA    . ALA   B  1  309  ? -2.823  14.422  103.445 1.00 14.87 ? 307  ALA   B CA    1 
ATOM   11170 C  C     . ALA   B  1  309  ? -2.418  15.840  103.093 1.00 17.70 ? 307  ALA   B C     1 
ATOM   11171 O  O     . ALA   B  1  309  ? -2.931  16.807  103.660 1.00 17.21 ? 307  ALA   B O     1 
ATOM   11172 C  CB    . ALA   B  1  309  ? -4.122  14.067  102.727 1.00 16.97 ? 307  ALA   B CB    1 
ATOM   11173 N  N     . GLU   B  1  310  ? -1.470  15.957  102.167 1.00 15.22 ? 308  GLU   B N     1 
ATOM   11174 C  CA    . GLU   B  1  310  ? -0.900  17.262  101.872 1.00 15.95 ? 308  GLU   B CA    1 
ATOM   11175 C  C     . GLU   B  1  310  ? -1.175  17.625  100.420 1.00 14.08 ? 308  GLU   B C     1 
ATOM   11176 O  O     . GLU   B  1  310  ? -2.295  17.417  99.944  1.00 15.41 ? 308  GLU   B O     1 
ATOM   11177 C  CB    . GLU   B  1  310  ? 0.589   17.282  102.251 1.00 14.48 ? 308  GLU   B CB    1 
ATOM   11178 C  CG    . GLU   B  1  310  ? 0.767   16.978  103.745 1.00 16.97 ? 308  GLU   B CG    1 
ATOM   11179 C  CD    . GLU   B  1  310  ? 2.216   17.057  104.212 1.00 18.43 ? 308  GLU   B CD    1 
ATOM   11180 O  OE1   . GLU   B  1  310  ? 2.717   18.186  104.368 1.00 20.01 ? 308  GLU   B OE1   1 
ATOM   11181 O  OE2   . GLU   B  1  310  ? 2.828   15.989  104.441 1.00 18.05 ? 308  GLU   B OE2   1 
ATOM   11182 N  N     . GLU   B  1  311  ? -0.186  18.150  99.709  1.00 16.41 ? 309  GLU   B N     1 
ATOM   11183 C  CA    . GLU   B  1  311  ? -0.416  18.616  98.351  1.00 14.47 ? 309  GLU   B CA    1 
ATOM   11184 C  C     . GLU   B  1  311  ? -0.728  17.451  97.416  1.00 15.31 ? 309  GLU   B C     1 
ATOM   11185 O  O     . GLU   B  1  311  ? -0.369  16.296  97.663  1.00 15.89 ? 309  GLU   B O     1 
ATOM   11186 C  CB    . GLU   B  1  311  ? 0.811   19.364  97.833  1.00 15.43 ? 309  GLU   B CB    1 
ATOM   11187 C  CG    . GLU   B  1  311  ? 1.074   20.665  98.574  1.00 19.49 ? 309  GLU   B CG    1 
ATOM   11188 C  CD    . GLU   B  1  311  ? 1.997   20.510  99.779  1.00 24.50 ? 309  GLU   B CD    1 
ATOM   11189 O  OE1   . GLU   B  1  311  ? 2.217   19.372  100.274 1.00 17.95 ? 309  GLU   B OE1   1 
ATOM   11190 O  OE2   . GLU   B  1  311  ? 2.502   21.559  100.238 1.00 26.31 ? 309  GLU   B OE2   1 
ATOM   11191 N  N     . ALA   B  1  312  ? -1.415  17.776  96.315  1.00 14.98 ? 310  ALA   B N     1 
ATOM   11192 C  CA    . ALA   B  1  312  ? -1.850  16.742  95.390  1.00 14.84 ? 310  ALA   B CA    1 
ATOM   11193 C  C     . ALA   B  1  312  ? -0.678  15.956  94.822  1.00 14.50 ? 310  ALA   B C     1 
ATOM   11194 O  O     . ALA   B  1  312  ? -0.818  14.757  94.558  1.00 15.95 ? 310  ALA   B O     1 
ATOM   11195 C  CB    . ALA   B  1  312  ? -2.654  17.366  94.245  1.00 16.33 ? 310  ALA   B CB    1 
ATOM   11196 N  N     . ASP   B  1  313  ? 0.486   16.598  94.652  1.00 15.24 ? 311  ASP   B N     1 
ATOM   11197 C  CA    . ASP   B  1  313  ? 1.627   15.890  94.084  1.00 17.02 ? 311  ASP   B CA    1 
ATOM   11198 C  C     . ASP   B  1  313  ? 2.326   14.977  95.078  1.00 17.60 ? 311  ASP   B C     1 
ATOM   11199 O  O     . ASP   B  1  313  ? 3.287   14.306  94.699  1.00 17.53 ? 311  ASP   B O     1 
ATOM   11200 C  CB    . ASP   B  1  313  ? 2.597   16.833  93.353  1.00 18.44 ? 311  ASP   B CB    1 
ATOM   11201 C  CG    . ASP   B  1  313  ? 3.297   17.825  94.260  1.00 22.54 ? 311  ASP   B CG    1 
ATOM   11202 O  OD1   . ASP   B  1  313  ? 3.136   17.778  95.494  1.00 20.95 ? 311  ASP   B OD1   1 
ATOM   11203 O  OD2   . ASP   B  1  313  ? 4.057   18.663  93.717  1.00 23.20 ? 311  ASP   B OD2   1 
ATOM   11204 N  N     . ARG   B  1  314  ? 1.838   14.904  96.313  1.00 15.65 ? 312  ARG   B N     1 
ATOM   11205 C  CA    . ARG   B  1  314  ? 2.351   13.961  97.291  1.00 17.39 ? 312  ARG   B CA    1 
ATOM   11206 C  C     . ARG   B  1  314  ? 1.412   12.795  97.542  1.00 16.25 ? 312  ARG   B C     1 
ATOM   11207 O  O     . ARG   B  1  314  ? 1.801   11.854  98.233  1.00 16.95 ? 312  ARG   B O     1 
ATOM   11208 C  CB    . ARG   B  1  314  ? 2.648   14.691  98.603  1.00 15.52 ? 312  ARG   B CB    1 
ATOM   11209 C  CG    . ARG   B  1  314  ? 3.924   15.479  98.493  1.00 15.87 ? 312  ARG   B CG    1 
ATOM   11210 C  CD    . ARG   B  1  314  ? 3.995   16.570  99.538  1.00 17.57 ? 312  ARG   B CD    1 
ATOM   11211 N  NE    . ARG   B  1  314  ? 5.357   17.075  99.639  1.00 16.59 ? 312  ARG   B NE    1 
ATOM   11212 C  CZ    . ARG   B  1  314  ? 5.715   18.080  100.425 1.00 18.13 ? 312  ARG   B CZ    1 
ATOM   11213 N  NH1   . ARG   B  1  314  ? 4.817   18.810  101.072 1.00 18.89 ? 312  ARG   B NH1   1 
ATOM   11214 N  NH2   . ARG   B  1  314  ? 7.006   18.345  100.587 1.00 18.92 ? 312  ARG   B NH2   1 
ATOM   11215 N  N     . LEU   B  1  315  ? 0.205   12.821  96.977  1.00 15.70 ? 313  LEU   B N     1 
ATOM   11216 C  CA    . LEU   B  1  315  ? -0.784  11.799  97.290  1.00 15.72 ? 313  LEU   B CA    1 
ATOM   11217 C  C     . LEU   B  1  315  ? -0.262  10.415  96.939  1.00 16.78 ? 313  LEU   B C     1 
ATOM   11218 O  O     . LEU   B  1  315  ? -0.219  9.517   97.787  1.00 16.94 ? 313  LEU   B O     1 
ATOM   11219 C  CB    . LEU   B  1  315  ? -2.078  12.083  96.529  1.00 17.50 ? 313  LEU   B CB    1 
ATOM   11220 C  CG    . LEU   B  1  315  ? -3.379  11.446  97.026  1.00 16.94 ? 313  LEU   B CG    1 
ATOM   11221 C  CD1   . LEU   B  1  315  ? -4.517  11.914  96.142  1.00 18.44 ? 313  LEU   B CD1   1 
ATOM   11222 C  CD2   . LEU   B  1  315  ? -3.348  9.911   97.046  1.00 20.49 ? 313  LEU   B CD2   1 
ATOM   11223 N  N     . GLU   B  1  316  ? 0.116   10.210  95.680  1.00 17.43 ? 314  GLU   B N     1 
ATOM   11224 C  CA    . GLU   B  1  316  ? 0.448   8.854   95.268  1.00 18.50 ? 314  GLU   B CA    1 
ATOM   11225 C  C     . GLU   B  1  316  ? 1.747   8.388   95.912  1.00 18.20 ? 314  GLU   B C     1 
ATOM   11226 O  O     . GLU   B  1  316  ? 1.871   7.216   96.285  1.00 18.52 ? 314  GLU   B O     1 
ATOM   11227 C  CB    . GLU   B  1  316  ? 0.458   8.746   93.744  1.00 20.48 ? 314  GLU   B CB    1 
ATOM   11228 C  CG    . GLU   B  1  316  ? -0.956  8.919   93.187  1.00 18.81 ? 314  GLU   B CG    1 
ATOM   11229 C  CD    . GLU   B  1  316  ? -1.027  8.823   91.671  1.00 22.71 ? 314  GLU   B CD    1 
ATOM   11230 O  OE1   . GLU   B  1  316  ? -0.370  7.930   91.094  1.00 22.28 ? 314  GLU   B OE1   1 
ATOM   11231 O  OE2   . GLU   B  1  316  ? -1.749  9.640   91.062  1.00 21.54 ? 314  GLU   B OE2   1 
ATOM   11232 N  N     . LEU   B  1  317  ? 2.707   9.298   96.085  1.00 20.13 ? 315  LEU   B N     1 
ATOM   11233 C  CA    . LEU   B  1  317  ? 3.918   8.959   96.822  1.00 20.48 ? 315  LEU   B CA    1 
ATOM   11234 C  C     . LEU   B  1  317  ? 3.589   8.440   98.214  1.00 20.60 ? 315  LEU   B C     1 
ATOM   11235 O  O     . LEU   B  1  317  ? 4.158   7.439   98.666  1.00 20.34 ? 315  LEU   B O     1 
ATOM   11236 C  CB    . LEU   B  1  317  ? 4.821   10.182  96.919  1.00 20.72 ? 315  LEU   B CB    1 
ATOM   11237 C  CG    . LEU   B  1  317  ? 6.162   9.938   97.614  1.00 22.16 ? 315  LEU   B CG    1 
ATOM   11238 C  CD1   . LEU   B  1  317  ? 6.885   8.769   96.963  1.00 24.39 ? 315  LEU   B CD1   1 
ATOM   11239 C  CD2   . LEU   B  1  317  ? 6.994   11.185  97.513  1.00 23.74 ? 315  LEU   B CD2   1 
ATOM   11240 N  N     . SER   B  1  318  ? 2.652   9.089   98.909  1.00 18.70 ? 316  SER   B N     1 
ATOM   11241 C  CA    . SER   B  1  318  ? 2.327   8.629   100.255 1.00 18.47 ? 316  SER   B CA    1 
ATOM   11242 C  C     . SER   B  1  318  ? 1.746   7.220   100.239 1.00 18.37 ? 316  SER   B C     1 
ATOM   11243 O  O     . SER   B  1  318  ? 1.901   6.477   101.212 1.00 20.16 ? 316  SER   B O     1 
ATOM   11244 C  CB    . SER   B  1  318  ? 1.372   9.595   100.964 1.00 18.25 ? 316  SER   B CB    1 
ATOM   11245 O  OG    . SER   B  1  318  ? 0.070   9.535   100.396 1.00 18.16 ? 316  SER   B OG    1 
ATOM   11246 N  N     . LEU   B  1  319  ? 1.079   6.835   99.148  1.00 16.26 ? 317  LEU   B N     1 
ATOM   11247 C  CA    . LEU   B  1  319  ? 0.519   5.492   99.067  1.00 17.87 ? 317  LEU   B CA    1 
ATOM   11248 C  C     . LEU   B  1  319  ? 1.603   4.427   99.057  1.00 20.47 ? 317  LEU   B C     1 
ATOM   11249 O  O     . LEU   B  1  319  ? 1.383   3.317   99.548  1.00 20.82 ? 317  LEU   B O     1 
ATOM   11250 C  CB    . LEU   B  1  319  ? -0.344  5.353   97.815  1.00 19.22 ? 317  LEU   B CB    1 
ATOM   11251 C  CG    . LEU   B  1  319  ? -1.601  6.220   97.762  1.00 19.27 ? 317  LEU   B CG    1 
ATOM   11252 C  CD1   . LEU   B  1  319  ? -2.233  6.076   96.381  1.00 19.86 ? 317  LEU   B CD1   1 
ATOM   11253 C  CD2   . LEU   B  1  319  ? -2.583  5.846   98.863  1.00 21.56 ? 317  LEU   B CD2   1 
ATOM   11254 N  N     . ASP   B  1  320  ? 2.765   4.729   98.482  1.00 20.12 ? 318  ASP   B N     1 
ATOM   11255 C  CA    . ASP   B  1  320  ? 3.859   3.767   98.515  1.00 21.92 ? 318  ASP   B CA    1 
ATOM   11256 C  C     . ASP   B  1  320  ? 4.348   3.517   99.931  1.00 20.71 ? 318  ASP   B C     1 
ATOM   11257 O  O     . ASP   B  1  320  ? 4.772   2.404   100.253 1.00 24.49 ? 318  ASP   B O     1 
ATOM   11258 C  CB    . ASP   B  1  320  ? 4.988   4.256   97.626  1.00 20.58 ? 318  ASP   B CB    1 
ATOM   11259 C  CG    . ASP   B  1  320  ? 4.686   4.025   96.175  1.00 22.36 ? 318  ASP   B CG    1 
ATOM   11260 O  OD1   . ASP   B  1  320  ? 4.395   2.864   95.830  1.00 25.05 ? 318  ASP   B OD1   1 
ATOM   11261 O  OD2   . ASP   B  1  320  ? 4.699   4.994   95.397  1.00 23.16 ? 318  ASP   B OD2   1 
ATOM   11262 N  N     . LEU   B  1  321  ? 4.286   4.527   100.793 1.00 17.78 ? 319  LEU   B N     1 
ATOM   11263 C  CA    . LEU   B  1  321  ? 4.625   4.293   102.191 1.00 19.66 ? 319  LEU   B CA    1 
ATOM   11264 C  C     . LEU   B  1  321  ? 3.517   3.534   102.901 1.00 21.05 ? 319  LEU   B C     1 
ATOM   11265 O  O     . LEU   B  1  321  ? 3.783   2.608   103.680 1.00 22.15 ? 319  LEU   B O     1 
ATOM   11266 C  CB    . LEU   B  1  321  ? 4.913   5.615   102.901 1.00 20.57 ? 319  LEU   B CB    1 
ATOM   11267 C  CG    . LEU   B  1  321  ? 6.273   6.222   102.587 1.00 20.20 ? 319  LEU   B CG    1 
ATOM   11268 C  CD1   . LEU   B  1  321  ? 6.194   7.073   101.344 1.00 22.00 ? 319  LEU   B CD1   1 
ATOM   11269 C  CD2   . LEU   B  1  321  ? 6.748   7.039   103.771 1.00 22.60 ? 319  LEU   B CD2   1 
ATOM   11270 N  N     . LEU   B  1  322  ? 2.265   3.897   102.639 1.00 19.42 ? 320  LEU   B N     1 
ATOM   11271 C  CA    . LEU   B  1  322  ? 1.164   3.190   103.279 1.00 18.94 ? 320  LEU   B CA    1 
ATOM   11272 C  C     . LEU   B  1  322  ? 1.220   1.709   102.951 1.00 19.90 ? 320  LEU   B C     1 
ATOM   11273 O  O     . LEU   B  1  322  ? 0.994   0.860   103.823 1.00 22.43 ? 320  LEU   B O     1 
ATOM   11274 C  CB    . LEU   B  1  322  ? -0.164  3.775   102.806 1.00 19.25 ? 320  LEU   B CB    1 
ATOM   11275 C  CG    . LEU   B  1  322  ? -1.396  3.099   103.399 1.00 21.49 ? 320  LEU   B CG    1 
ATOM   11276 C  CD1   . LEU   B  1  322  ? -1.400  3.290   104.907 1.00 20.97 ? 320  LEU   B CD1   1 
ATOM   11277 C  CD2   . LEU   B  1  322  ? -2.662  3.646   102.760 1.00 21.11 ? 320  LEU   B CD2   1 
ATOM   11278 N  N     . GLU   B  1  323  ? 1.545   1.383   101.698 1.00 19.37 ? 321  GLU   B N     1 
ATOM   11279 C  CA    . GLU   B  1  323  ? 1.635   -0.011  101.277 1.00 22.21 ? 321  GLU   B CA    1 
ATOM   11280 C  C     . GLU   B  1  323  ? 2.662   -0.773  102.104 1.00 24.19 ? 321  GLU   B C     1 
ATOM   11281 O  O     . GLU   B  1  323  ? 2.382   -1.869  102.606 1.00 25.40 ? 321  GLU   B O     1 
ATOM   11282 C  CB    . GLU   B  1  323  ? 2.003   -0.071  99.795  1.00 24.51 ? 321  GLU   B CB    1 
ATOM   11283 C  CG    . GLU   B  1  323  ? 2.322   -1.469  99.279  1.00 30.26 ? 321  GLU   B CG    1 
ATOM   11284 C  CD    . GLU   B  1  323  ? 1.127   -2.149  98.642  1.00 32.19 ? 321  GLU   B CD    1 
ATOM   11285 O  OE1   . GLU   B  1  323  ? 0.144   -1.451  98.328  1.00 30.16 ? 321  GLU   B OE1   1 
ATOM   11286 O  OE2   . GLU   B  1  323  ? 1.165   -3.383  98.462  1.00 29.65 ? 321  GLU   B OE2   1 
ATOM   11287 N  N     . VAL   B  1  324  ? 3.866   -0.213  102.246 1.00 21.25 ? 322  VAL   B N     1 
ATOM   11288 C  CA    . VAL   B  1  324  ? 4.912   -0.891  103.007 1.00 23.35 ? 322  VAL   B CA    1 
ATOM   11289 C  C     . VAL   B  1  324  ? 4.486   -1.083  104.458 1.00 22.00 ? 322  VAL   B C     1 
ATOM   11290 O  O     . VAL   B  1  324  ? 4.654   -2.164  105.037 1.00 24.83 ? 322  VAL   B O     1 
ATOM   11291 C  CB    . VAL   B  1  324  ? 6.251   -0.134  102.890 1.00 23.71 ? 322  VAL   B CB    1 
ATOM   11292 C  CG1   . VAL   B  1  324  ? 7.295   -0.746  103.812 1.00 23.41 ? 322  VAL   B CG1   1 
ATOM   11293 C  CG2   . VAL   B  1  324  ? 6.737   -0.127  101.443 1.00 28.52 ? 322  VAL   B CG2   1 
ATOM   11294 N  N     . LEU   B  1  325  ? 3.917   -0.046  105.068 1.00 19.85 ? 323  LEU   B N     1 
ATOM   11295 C  CA    . LEU   B  1  325  ? 3.537   -0.142  106.474 1.00 23.59 ? 323  LEU   B CA    1 
ATOM   11296 C  C     . LEU   B  1  325  ? 2.481   -1.213  106.699 1.00 22.51 ? 323  LEU   B C     1 
ATOM   11297 O  O     . LEU   B  1  325  ? 2.546   -1.961  107.681 1.00 23.33 ? 323  LEU   B O     1 
ATOM   11298 C  CB    . LEU   B  1  325  ? 3.048   1.214   106.970 1.00 21.64 ? 323  LEU   B CB    1 
ATOM   11299 C  CG    . LEU   B  1  325  ? 4.168   2.246   106.950 1.00 21.39 ? 323  LEU   B CG    1 
ATOM   11300 C  CD1   . LEU   B  1  325  ? 3.594   3.648   107.027 1.00 25.72 ? 323  LEU   B CD1   1 
ATOM   11301 C  CD2   . LEU   B  1  325  ? 5.115   1.993   108.103 1.00 21.07 ? 323  LEU   B CD2   1 
ATOM   11302 N  N     . CYS   B  1  326  ? 1.494   -1.300  105.803 1.00 21.76 ? 324  CYS   B N     1 
ATOM   11303 C  CA    . CYS   B  1  326  ? 0.429   -2.280  105.971 1.00 22.14 ? 324  CYS   B CA    1 
ATOM   11304 C  C     . CYS   B  1  326  ? 0.917   -3.709  105.779 1.00 23.31 ? 324  CYS   B C     1 
ATOM   11305 O  O     . CYS   B  1  326  ? 0.297   -4.636  106.308 1.00 22.49 ? 324  CYS   B O     1 
ATOM   11306 C  CB    . CYS   B  1  326  ? -0.715  -1.973  105.007 1.00 24.34 ? 324  CYS   B CB    1 
ATOM   11307 S  SG    . CYS   B  1  326  ? -1.600  -0.490  105.485 1.00 28.24 ? 324  CYS   B SG    1 
ATOM   11308 N  N     . LEU   B  1  327  ? 2.013   -3.903  105.049 1.00 22.57 ? 325  LEU   B N     1 
ATOM   11309 C  CA    . LEU   B  1  327  ? 2.591   -5.226  104.852 1.00 25.40 ? 325  LEU   B CA    1 
ATOM   11310 C  C     . LEU   B  1  327  ? 3.743   -5.519  105.803 1.00 29.14 ? 325  LEU   B C     1 
ATOM   11311 O  O     . LEU   B  1  327  ? 4.359   -6.584  105.697 1.00 29.19 ? 325  LEU   B O     1 
ATOM   11312 C  CB    . LEU   B  1  327  ? 3.056   -5.383  103.403 1.00 22.04 ? 325  LEU   B CB    1 
ATOM   11313 C  CG    . LEU   B  1  327  ? 1.958   -5.179  102.358 1.00 29.05 ? 325  LEU   B CG    1 
ATOM   11314 C  CD1   . LEU   B  1  327  ? 2.539   -5.269  100.957 1.00 33.25 ? 325  LEU   B CD1   1 
ATOM   11315 C  CD2   . LEU   B  1  327  ? 0.840   -6.172  102.538 1.00 34.05 ? 325  LEU   B CD2   1 
ATOM   11316 N  N     . ASP   B  1  328  ? 4.039   -4.615  106.735 1.00 25.65 ? 326  ASP   B N     1 
ATOM   11317 C  CA    . ASP   B  1  328  ? 5.155   -4.800  107.660 1.00 26.05 ? 326  ASP   B CA    1 
ATOM   11318 C  C     . ASP   B  1  328  ? 4.699   -5.656  108.839 1.00 26.59 ? 326  ASP   B C     1 
ATOM   11319 O  O     . ASP   B  1  328  ? 3.890   -5.216  109.661 1.00 27.04 ? 326  ASP   B O     1 
ATOM   11320 C  CB    . ASP   B  1  328  ? 5.648   -3.436  108.135 1.00 24.95 ? 326  ASP   B CB    1 
ATOM   11321 C  CG    . ASP   B  1  328  ? 6.959   -3.519  108.910 1.00 31.87 ? 326  ASP   B CG    1 
ATOM   11322 O  OD1   . ASP   B  1  328  ? 7.235   -4.564  109.534 1.00 30.39 ? 326  ASP   B OD1   1 
ATOM   11323 O  OD2   . ASP   B  1  328  ? 7.712   -2.526  108.901 1.00 33.61 ? 326  ASP   B OD2   1 
ATOM   11324 N  N     . GLY   B  1  329  ? 5.234   -6.874  108.940 1.00 27.44 ? 327  GLY   B N     1 
ATOM   11325 C  CA    . GLY   B  1  329  ? 4.850   -7.770  110.019 1.00 27.02 ? 327  GLY   B CA    1 
ATOM   11326 C  C     . GLY   B  1  329  ? 5.138   -7.244  111.411 1.00 27.96 ? 327  GLY   B C     1 
ATOM   11327 O  O     . GLY   B  1  329  ? 4.502   -7.686  112.373 1.00 28.30 ? 327  GLY   B O     1 
ATOM   11328 N  N     . ASP   B  1  330  ? 6.081   -6.310  111.548 1.00 27.86 ? 328  ASP   B N     1 
ATOM   11329 C  CA    . ASP   B  1  330  ? 6.296   -5.688  112.851 1.00 23.92 ? 328  ASP   B CA    1 
ATOM   11330 C  C     . ASP   B  1  330  ? 5.045   -4.988  113.358 1.00 30.60 ? 328  ASP   B C     1 
ATOM   11331 O  O     . ASP   B  1  330  ? 4.898   -4.810  114.571 1.00 29.31 ? 328  ASP   B O     1 
ATOM   11332 C  CB    . ASP   B  1  330  ? 7.468   -4.697  112.799 1.00 29.45 ? 328  ASP   B CB    1 
ATOM   11333 C  CG    . ASP   B  1  330  ? 8.813   -5.388  112.625 1.00 34.27 ? 328  ASP   B CG    1 
ATOM   11334 O  OD1   . ASP   B  1  330  ? 8.890   -6.614  112.860 1.00 35.49 ? 328  ASP   B OD1   1 
ATOM   11335 O  OD2   . ASP   B  1  330  ? 9.800   -4.707  112.266 1.00 33.84 ? 328  ASP   B OD2   1 
ATOM   11336 N  N     . LEU   B  1  331  ? 4.138   -4.596  112.461 1.00 25.56 ? 329  LEU   B N     1 
ATOM   11337 C  CA    . LEU   B  1  331  ? 2.913   -3.906  112.831 1.00 26.38 ? 329  LEU   B CA    1 
ATOM   11338 C  C     . LEU   B  1  331  ? 1.714   -4.839  112.879 1.00 23.48 ? 329  LEU   B C     1 
ATOM   11339 O  O     . LEU   B  1  331  ? 0.576   -4.367  112.923 1.00 26.28 ? 329  LEU   B O     1 
ATOM   11340 C  CB    . LEU   B  1  331  ? 2.652   -2.749  111.868 1.00 22.75 ? 329  LEU   B CB    1 
ATOM   11341 C  CG    . LEU   B  1  331  ? 3.827   -1.776  111.792 1.00 24.49 ? 329  LEU   B CG    1 
ATOM   11342 C  CD1   . LEU   B  1  331  ? 3.544   -0.680  110.779 1.00 23.58 ? 329  LEU   B CD1   1 
ATOM   11343 C  CD2   . LEU   B  1  331  ? 4.093   -1.198  113.178 1.00 22.57 ? 329  LEU   B CD2   1 
ATOM   11344 N  N     . SER   B  1  332  ? 1.959   -6.148  112.904 1.00 27.90 ? 330  SER   B N     1 
ATOM   11345 C  CA    . SER   B  1  332  ? 0.912   -7.159  112.808 1.00 26.55 ? 330  SER   B CA    1 
ATOM   11346 C  C     . SER   B  1  332  ? -0.237  -6.903  113.776 1.00 27.54 ? 330  SER   B C     1 
ATOM   11347 O  O     . SER   B  1  332  ? -0.025  -6.660  114.966 1.00 30.67 ? 330  SER   B O     1 
ATOM   11348 C  CB    . SER   B  1  332  ? 1.528   -8.520  113.123 1.00 32.33 ? 330  SER   B CB    1 
ATOM   11349 O  OG    . SER   B  1  332  ? 0.541   -9.533  113.090 1.00 37.86 ? 330  SER   B OG    1 
ATOM   11350 N  N     . GLY   B  1  333  ? -1.461  -6.970  113.257 1.00 24.93 ? 331  GLY   B N     1 
ATOM   11351 C  CA    . GLY   B  1  333  ? -2.641  -6.892  114.096 1.00 29.31 ? 331  GLY   B CA    1 
ATOM   11352 C  C     . GLY   B  1  333  ? -3.009  -5.501  114.567 1.00 29.03 ? 331  GLY   B C     1 
ATOM   11353 O  O     . GLY   B  1  333  ? -4.035  -5.342  115.242 1.00 30.88 ? 331  GLY   B O     1 
ATOM   11354 N  N     . TRP   B  1  334  ? -2.217  -4.493  114.231 1.00 28.32 ? 332  TRP   B N     1 
ATOM   11355 C  CA    . TRP   B  1  334  ? -2.478  -3.125  114.658 1.00 25.39 ? 332  TRP   B CA    1 
ATOM   11356 C  C     . TRP   B  1  334  ? -3.440  -2.473  113.676 1.00 24.38 ? 332  TRP   B C     1 
ATOM   11357 O  O     . TRP   B  1  334  ? -3.145  -2.357  112.482 1.00 25.52 ? 332  TRP   B O     1 
ATOM   11358 C  CB    . TRP   B  1  334  ? -1.163  -2.358  114.730 1.00 26.12 ? 332  TRP   B CB    1 
ATOM   11359 C  CG    . TRP   B  1  334  ? -1.280  -0.894  115.049 1.00 24.20 ? 332  TRP   B CG    1 
ATOM   11360 C  CD1   . TRP   B  1  334  ? -1.864  -0.332  116.151 1.00 25.98 ? 332  TRP   B CD1   1 
ATOM   11361 C  CD2   . TRP   B  1  334  ? -0.743  0.183   114.285 1.00 25.51 ? 332  TRP   B CD2   1 
ATOM   11362 N  NE1   . TRP   B  1  334  ? -1.733  1.038   116.107 1.00 21.41 ? 332  TRP   B NE1   1 
ATOM   11363 C  CE2   . TRP   B  1  334  ? -1.053  1.378   114.967 1.00 20.58 ? 332  TRP   B CE2   1 
ATOM   11364 C  CE3   . TRP   B  1  334  ? -0.042  0.259   113.079 1.00 22.55 ? 332  TRP   B CE3   1 
ATOM   11365 C  CZ2   . TRP   B  1  334  ? -0.681  2.629   114.480 1.00 22.74 ? 332  TRP   B CZ2   1 
ATOM   11366 C  CZ3   . TRP   B  1  334  ? 0.327   1.497   112.602 1.00 27.44 ? 332  TRP   B CZ3   1 
ATOM   11367 C  CH2   . TRP   B  1  334  ? 0.007   2.668   113.303 1.00 25.51 ? 332  TRP   B CH2   1 
ATOM   11368 N  N     . ASN   B  1  335  ? -4.597  -2.056  114.170 1.00 24.88 ? 333  ASN   B N     1 
ATOM   11369 C  CA    . ASN   B  1  335  ? -5.583  -1.412  113.320 1.00 24.60 ? 333  ASN   B CA    1 
ATOM   11370 C  C     . ASN   B  1  335  ? -5.534  0.103   113.426 1.00 22.35 ? 333  ASN   B C     1 
ATOM   11371 O  O     . ASN   B  1  335  ? -6.466  0.784   112.989 1.00 24.31 ? 333  ASN   B O     1 
ATOM   11372 C  CB    . ASN   B  1  335  ? -6.974  -1.966  113.605 1.00 25.61 ? 333  ASN   B CB    1 
ATOM   11373 C  CG    . ASN   B  1  335  ? -7.090  -3.417  113.204 1.00 30.90 ? 333  ASN   B CG    1 
ATOM   11374 O  OD1   . ASN   B  1  335  ? -6.446  -3.845  112.243 1.00 26.47 ? 333  ASN   B OD1   1 
ATOM   11375 N  ND2   . ASN   B  1  335  ? -7.896  -4.186  113.936 1.00 30.89 ? 333  ASN   B ND2   1 
ATOM   11376 N  N     . GLY   B  1  336  ? -4.459  0.641   113.985 1.00 21.82 ? 334  GLY   B N     1 
ATOM   11377 C  CA    . GLY   B  1  336  ? -4.382  2.068   114.192 1.00 22.43 ? 334  GLY   B CA    1 
ATOM   11378 C  C     . GLY   B  1  336  ? -3.726  2.869   113.097 1.00 20.47 ? 334  GLY   B C     1 
ATOM   11379 O  O     . GLY   B  1  336  ? -3.601  4.089   113.245 1.00 20.45 ? 334  GLY   B O     1 
ATOM   11380 N  N     . MET   B  1  337  ? -3.302  2.251   111.997 1.00 20.57 ? 335  MET   B N     1 
ATOM   11381 C  CA    . MET   B  1  337  ? -2.750  3.035   110.899 1.00 21.00 ? 335  MET   B CA    1 
ATOM   11382 C  C     . MET   B  1  337  ? -3.864  3.864   110.277 1.00 20.92 ? 335  MET   B C     1 
ATOM   11383 O  O     . MET   B  1  337  ? -4.894  3.321   109.868 1.00 21.86 ? 335  MET   B O     1 
ATOM   11384 C  CB    . MET   B  1  337  ? -2.136  2.123   109.844 1.00 23.87 ? 335  MET   B CB    1 
ATOM   11385 C  CG    . MET   B  1  337  ? -1.459  2.875   108.712 1.00 26.72 ? 335  MET   B CG    1 
ATOM   11386 S  SD    . MET   B  1  337  ? 0.132   3.535   109.232 1.00 37.48 ? 335  MET   B SD    1 
ATOM   11387 C  CE    . MET   B  1  337  ? -0.201  5.290   109.137 1.00 30.37 ? 335  MET   B CE    1 
ATOM   11388 N  N     . GLY   B  1  338  ? -3.659  5.174   110.210 1.00 19.12 ? 336  GLY   B N     1 
ATOM   11389 C  CA    . GLY   B  1  338  ? -4.647  6.080   109.669 1.00 20.94 ? 336  GLY   B CA    1 
ATOM   11390 C  C     . GLY   B  1  338  ? -4.106  6.786   108.444 1.00 20.53 ? 336  GLY   B C     1 
ATOM   11391 O  O     . GLY   B  1  338  ? -2.905  7.014   108.319 1.00 19.19 ? 336  GLY   B O     1 
ATOM   11392 N  N     . PHE   B  1  339  ? -5.008  7.128   107.535 1.00 19.18 ? 337  PHE   B N     1 
ATOM   11393 C  CA    . PHE   B  1  339  ? -4.597  7.746   106.285 1.00 18.65 ? 337  PHE   B CA    1 
ATOM   11394 C  C     . PHE   B  1  339  ? -5.712  8.670   105.832 1.00 18.93 ? 337  PHE   B C     1 
ATOM   11395 O  O     . PHE   B  1  339  ? -6.875  8.265   105.798 1.00 19.50 ? 337  PHE   B O     1 
ATOM   11396 C  CB    . PHE   B  1  339  ? -4.357  6.659   105.236 1.00 19.22 ? 337  PHE   B CB    1 
ATOM   11397 C  CG    . PHE   B  1  339  ? -3.662  7.145   104.002 1.00 18.92 ? 337  PHE   B CG    1 
ATOM   11398 C  CD1   . PHE   B  1  339  ? -2.280  7.191   103.935 1.00 19.84 ? 337  PHE   B CD1   1 
ATOM   11399 C  CD2   . PHE   B  1  339  ? -4.394  7.531   102.897 1.00 18.92 ? 337  PHE   B CD2   1 
ATOM   11400 C  CE1   . PHE   B  1  339  ? -1.632  7.641   102.770 1.00 19.73 ? 337  PHE   B CE1   1 
ATOM   11401 C  CE2   . PHE   B  1  339  ? -3.764  7.966   101.734 1.00 20.08 ? 337  PHE   B CE2   1 
ATOM   11402 C  CZ    . PHE   B  1  339  ? -2.386  8.026   101.673 1.00 20.26 ? 337  PHE   B CZ    1 
ATOM   11403 N  N     . VAL   B  1  340  ? -5.365  9.900   105.505 1.00 18.24 ? 338  VAL   B N     1 
ATOM   11404 C  CA    . VAL   B  1  340  ? -6.346  10.894  105.086 1.00 17.75 ? 338  VAL   B CA    1 
ATOM   11405 C  C     . VAL   B  1  340  ? -6.520  10.810  103.581 1.00 18.88 ? 338  VAL   B C     1 
ATOM   11406 O  O     . VAL   B  1  340  ? -5.548  10.660  102.839 1.00 18.21 ? 338  VAL   B O     1 
ATOM   11407 C  CB    . VAL   B  1  340  ? -5.889  12.304  105.496 1.00 18.43 ? 338  VAL   B CB    1 
ATOM   11408 C  CG1   . VAL   B  1  340  ? -6.857  13.347  104.973 1.00 20.08 ? 338  VAL   B CG1   1 
ATOM   11409 C  CG2   . VAL   B  1  340  ? -5.763  12.396  107.008 1.00 18.63 ? 338  VAL   B CG2   1 
ATOM   11410 N  N     . VAL   B  1  341  ? -7.755  10.928  103.121 1.00 18.37 ? 339  VAL   B N     1 
ATOM   11411 C  CA    . VAL   B  1  341  ? -8.033  11.101  101.703 1.00 18.40 ? 339  VAL   B CA    1 
ATOM   11412 C  C     . VAL   B  1  341  ? -8.889  12.343  101.529 1.00 17.52 ? 339  VAL   B C     1 
ATOM   11413 O  O     . VAL   B  1  341  ? -9.847  12.560  102.285 1.00 18.35 ? 339  VAL   B O     1 
ATOM   11414 C  CB    . VAL   B  1  341  ? -8.682  9.856   101.062 1.00 22.48 ? 339  VAL   B CB    1 
ATOM   11415 C  CG1   . VAL   B  1  341  ? -8.685  9.998   99.546  1.00 25.99 ? 339  VAL   B CG1   1 
ATOM   11416 C  CG2   . VAL   B  1  341  ? -7.908  8.617   101.429 1.00 23.72 ? 339  VAL   B CG2   1 
ATOM   11417 N  N     . GLN   B  1  342  ? -8.547  13.144  100.524 1.00 16.48 ? 340  GLN   B N     1 
ATOM   11418 C  CA    . GLN   B  1  342  ? -9.123  14.470  100.306 1.00 16.45 ? 340  GLN   B CA    1 
ATOM   11419 C  C     . GLN   B  1  342  ? -10.185 14.378  99.220  1.00 17.36 ? 340  GLN   B C     1 
ATOM   11420 O  O     . GLN   B  1  342  ? -9.876  14.127  98.047  1.00 17.31 ? 340  GLN   B O     1 
ATOM   11421 C  CB    . GLN   B  1  342  ? -8.031  15.459  99.911  1.00 15.22 ? 340  GLN   B CB    1 
ATOM   11422 C  CG    . GLN   B  1  342  ? -6.976  15.617  100.973 1.00 14.20 ? 340  GLN   B CG    1 
ATOM   11423 C  CD    . GLN   B  1  342  ? -5.616  15.978  100.384 1.00 15.99 ? 340  GLN   B CD    1 
ATOM   11424 O  OE1   . GLN   B  1  342  ? -5.154  15.352  99.426  1.00 17.32 ? 340  GLN   B OE1   1 
ATOM   11425 N  NE2   . GLN   B  1  342  ? -4.978  16.996  100.944 1.00 15.22 ? 340  GLN   B NE2   1 
ATOM   11426 N  N     . ALA   B  1  343  ? -11.434 14.598  99.615  1.00 16.03 ? 341  ALA   B N     1 
ATOM   11427 C  CA    . ALA   B  1  343  ? -12.541 14.464  98.682  1.00 17.31 ? 341  ALA   B CA    1 
ATOM   11428 C  C     . ALA   B  1  343  ? -12.583 15.580  97.651  1.00 17.81 ? 341  ALA   B C     1 
ATOM   11429 O  O     . ALA   B  1  343  ? -13.285 15.438  96.643  1.00 18.45 ? 341  ALA   B O     1 
ATOM   11430 C  CB    . ALA   B  1  343  ? -13.858 14.395  99.452  1.00 19.58 ? 341  ALA   B CB    1 
ATOM   11431 N  N     . TYR   B  1  344  ? -11.857 16.686  97.865  1.00 17.27 ? 342  TYR   B N     1 
ATOM   11432 C  CA    . TYR   B  1  344  ? -11.772 17.673  96.798  1.00 18.63 ? 342  TYR   B CA    1 
ATOM   11433 C  C     . TYR   B  1  344  ? -10.903 17.196  95.648  1.00 17.62 ? 342  TYR   B C     1 
ATOM   11434 O  O     . TYR   B  1  344  ? -10.826 17.877  94.623  1.00 18.18 ? 342  TYR   B O     1 
ATOM   11435 C  CB    . TYR   B  1  344  ? -11.351 19.075  97.289  1.00 17.03 ? 342  TYR   B CB    1 
ATOM   11436 C  CG    . TYR   B  1  344  ? -9.906  19.333  97.700  1.00 18.96 ? 342  TYR   B CG    1 
ATOM   11437 C  CD1   . TYR   B  1  344  ? -8.944  18.328  97.744  1.00 15.34 ? 342  TYR   B CD1   1 
ATOM   11438 C  CD2   . TYR   B  1  344  ? -9.523  20.623  98.065  1.00 16.41 ? 342  TYR   B CD2   1 
ATOM   11439 C  CE1   . TYR   B  1  344  ? -7.623  18.611  98.138  1.00 14.95 ? 342  TYR   B CE1   1 
ATOM   11440 C  CE2   . TYR   B  1  344  ? -8.221  20.915  98.463  1.00 17.76 ? 342  TYR   B CE2   1 
ATOM   11441 C  CZ    . TYR   B  1  344  ? -7.283  19.914  98.499  1.00 16.50 ? 342  TYR   B CZ    1 
ATOM   11442 O  OH    . TYR   B  1  344  ? -6.009  20.229  98.912  1.00 16.41 ? 342  TYR   B OH    1 
ATOM   11443 N  N     . GLY   B  1  345  ? -10.247 16.049  95.797  1.00 16.91 ? 343  GLY   B N     1 
ATOM   11444 C  CA    . GLY   B  1  345  ? -9.365  15.544  94.773  1.00 17.27 ? 343  GLY   B CA    1 
ATOM   11445 C  C     . GLY   B  1  345  ? -10.100 14.572  93.867  1.00 18.16 ? 343  GLY   B C     1 
ATOM   11446 O  O     . GLY   B  1  345  ? -10.900 13.758  94.319  1.00 17.88 ? 343  GLY   B O     1 
ATOM   11447 N  N     . LYS   B  1  346  ? -9.788  14.661  92.578  1.00 16.70 ? 344  LYS   B N     1 
ATOM   11448 C  CA    . LYS   B  1  346  ? -10.440 13.815  91.591  1.00 17.80 ? 344  LYS   B CA    1 
ATOM   11449 C  C     . LYS   B  1  346  ? -10.095 12.348  91.768  1.00 17.27 ? 344  LYS   B C     1 
ATOM   11450 O  O     . LYS   B  1  346  ? -10.835 11.488  91.283  1.00 19.26 ? 344  LYS   B O     1 
ATOM   11451 C  CB    . LYS   B  1  346  ? -10.032 14.279  90.202  1.00 19.89 ? 344  LYS   B CB    1 
ATOM   11452 C  CG    . LYS   B  1  346  ? -10.545 15.661  89.895  1.00 18.34 ? 344  LYS   B CG    1 
ATOM   11453 C  CD    . LYS   B  1  346  ? -9.990  16.176  88.615  1.00 18.97 ? 344  LYS   B CD    1 
ATOM   11454 C  CE    . LYS   B  1  346  ? -10.652 17.498  88.282  1.00 18.92 ? 344  LYS   B CE    1 
ATOM   11455 N  NZ    . LYS   B  1  346  ? -10.047 18.087  87.042  1.00 18.45 ? 344  LYS   B NZ    1 
ATOM   11456 N  N     . ARG   B  1  347  ? -8.981  12.041  92.421  1.00 16.70 ? 345  ARG   B N     1 
ATOM   11457 C  CA    . ARG   B  1  347  ? -8.583  10.652  92.576  1.00 18.45 ? 345  ARG   B CA    1 
ATOM   11458 C  C     . ARG   B  1  347  ? -9.218  9.991   93.786  1.00 19.03 ? 345  ARG   B C     1 
ATOM   11459 O  O     . ARG   B  1  347  ? -9.073  8.776   93.952  1.00 19.00 ? 345  ARG   B O     1 
ATOM   11460 C  CB    . ARG   B  1  347  ? -7.059  10.561  92.644  1.00 16.40 ? 345  ARG   B CB    1 
ATOM   11461 C  CG    . ARG   B  1  347  ? -6.407  10.950  91.337  1.00 16.13 ? 345  ARG   B CG    1 
ATOM   11462 C  CD    . ARG   B  1  347  ? -4.937  11.196  91.549  1.00 16.78 ? 345  ARG   B CD    1 
ATOM   11463 N  NE    . ARG   B  1  347  ? -4.685  12.442  92.261  1.00 16.19 ? 345  ARG   B NE    1 
ATOM   11464 C  CZ    . ARG   B  1  347  ? -3.501  12.775  92.745  1.00 17.42 ? 345  ARG   B CZ    1 
ATOM   11465 N  NH1   . ARG   B  1  347  ? -2.449  11.994  92.580  1.00 17.06 ? 345  ARG   B NH1   1 
ATOM   11466 N  NH2   . ARG   B  1  347  ? -3.368  13.923  93.406  1.00 15.36 ? 345  ARG   B NH2   1 
ATOM   11467 N  N     . CYS   B  1  348  ? -9.927  10.759  94.611  1.00 18.91 ? 346  CYS   B N     1 
ATOM   11468 C  CA    . CYS   B  1  348  ? -10.401 10.272  95.907  1.00 18.82 ? 346  CYS   B CA    1 
ATOM   11469 C  C     . CYS   B  1  348  ? -11.086 8.908   95.870  1.00 20.24 ? 346  CYS   B C     1 
ATOM   11470 O  O     . CYS   B  1  348  ? -10.671 8.017   96.630  1.00 19.77 ? 346  CYS   B O     1 
ATOM   11471 C  CB    . CYS   B  1  348  ? -11.274 11.347  96.563  1.00 18.89 ? 346  CYS   B CB    1 
ATOM   11472 S  SG    . CYS   B  1  348  ? -11.605 10.983  98.297  1.00 25.16 ? 346  CYS   B SG    1 
ATOM   11473 N  N     . PRO   B  1  349  ? -12.116 8.667   95.049  1.00 19.43 ? 347  PRO   B N     1 
ATOM   11474 C  CA    . PRO   B  1  349  ? -12.743 7.339   95.073  1.00 20.50 ? 347  PRO   B CA    1 
ATOM   11475 C  C     . PRO   B  1  349  ? -11.799 6.227   94.668  1.00 19.09 ? 347  PRO   B C     1 
ATOM   11476 O  O     . PRO   B  1  349  ? -11.909 5.116   95.201  1.00 20.04 ? 347  PRO   B O     1 
ATOM   11477 C  CB    . PRO   B  1  349  ? -13.929 7.470   94.107  1.00 22.20 ? 347  PRO   B CB    1 
ATOM   11478 C  CG    . PRO   B  1  349  ? -13.632 8.640   93.277  1.00 21.75 ? 347  PRO   B CG    1 
ATOM   11479 C  CD    . PRO   B  1  349  ? -12.727 9.552   94.042  1.00 19.90 ? 347  PRO   B CD    1 
ATOM   11480 N  N     . PHE   B  1  350  ? -10.861 6.502   93.762  1.00 19.92 ? 348  PHE   B N     1 
ATOM   11481 C  CA    . PHE   B  1  350  ? -9.924  5.475   93.331  1.00 20.46 ? 348  PHE   B CA    1 
ATOM   11482 C  C     . PHE   B  1  350  ? -8.870  5.220   94.387  1.00 19.66 ? 348  PHE   B C     1 
ATOM   11483 O  O     . PHE   B  1  350  ? -8.443  4.071   94.569  1.00 19.90 ? 348  PHE   B O     1 
ATOM   11484 C  CB    . PHE   B  1  350  ? -9.319  5.873   91.991  1.00 19.33 ? 348  PHE   B CB    1 
ATOM   11485 C  CG    . PHE   B  1  350  ? -10.355 6.273   91.007  1.00 20.92 ? 348  PHE   B CG    1 
ATOM   11486 C  CD1   . PHE   B  1  350  ? -11.041 5.311   90.294  1.00 23.68 ? 348  PHE   B CD1   1 
ATOM   11487 C  CD2   . PHE   B  1  350  ? -10.694 7.606   90.837  1.00 20.44 ? 348  PHE   B CD2   1 
ATOM   11488 C  CE1   . PHE   B  1  350  ? -12.037 5.671   89.403  1.00 25.75 ? 348  PHE   B CE1   1 
ATOM   11489 C  CE2   . PHE   B  1  350  ? -11.690 7.970   89.948  1.00 22.19 ? 348  PHE   B CE2   1 
ATOM   11490 C  CZ    . PHE   B  1  350  ? -12.354 7.005   89.231  1.00 21.30 ? 348  PHE   B CZ    1 
ATOM   11491 N  N     . VAL   B  1  351  ? -8.483  6.268   95.118  1.00 17.89 ? 349  VAL   B N     1 
ATOM   11492 C  CA    . VAL   B  1  351  ? -7.595  6.082   96.262  1.00 17.75 ? 349  VAL   B CA    1 
ATOM   11493 C  C     . VAL   B  1  351  ? -8.281  5.232   97.325  1.00 20.00 ? 349  VAL   B C     1 
ATOM   11494 O  O     . VAL   B  1  351  ? -7.673  4.325   97.902  1.00 20.13 ? 349  VAL   B O     1 
ATOM   11495 C  CB    . VAL   B  1  351  ? -7.146  7.442   96.823  1.00 17.41 ? 349  VAL   B CB    1 
ATOM   11496 C  CG1   . VAL   B  1  351  ? -6.305  7.239   98.098  1.00 18.97 ? 349  VAL   B CG1   1 
ATOM   11497 C  CG2   . VAL   B  1  351  ? -6.344  8.202   95.777  1.00 18.56 ? 349  VAL   B CG2   1 
ATOM   11498 N  N     . LEU   B  1  352  ? -9.568  5.497   97.584  1.00 17.89 ? 350  LEU   B N     1 
ATOM   11499 C  CA    . LEU   B  1  352  ? -10.312 4.683   98.536  1.00 19.01 ? 350  LEU   B CA    1 
ATOM   11500 C  C     . LEU   B  1  352  ? -10.379 3.229   98.084  1.00 20.48 ? 350  LEU   B C     1 
ATOM   11501 O  O     . LEU   B  1  352  ? -10.210 2.314   98.898  1.00 22.08 ? 350  LEU   B O     1 
ATOM   11502 C  CB    . LEU   B  1  352  ? -11.710 5.257   98.734  1.00 19.41 ? 350  LEU   B CB    1 
ATOM   11503 C  CG    . LEU   B  1  352  ? -11.746 6.594   99.471  1.00 21.51 ? 350  LEU   B CG    1 
ATOM   11504 C  CD1   . LEU   B  1  352  ? -13.175 7.080   99.528  1.00 23.77 ? 350  LEU   B CD1   1 
ATOM   11505 C  CD2   . LEU   B  1  352  ? -11.187 6.442   100.889 1.00 23.52 ? 350  LEU   B CD2   1 
ATOM   11506 N  N     . ASP   B  1  353  ? -10.621 2.994   96.790  1.00 22.55 ? 351  ASP   B N     1 
ATOM   11507 C  CA    . ASP   B  1  353  ? -10.599 1.625   96.277  1.00 22.29 ? 351  ASP   B CA    1 
ATOM   11508 C  C     . ASP   B  1  353  ? -9.261  0.968   96.575  1.00 19.89 ? 351  ASP   B C     1 
ATOM   11509 O  O     . ASP   B  1  353  ? -9.208  -0.187  97.019  1.00 22.21 ? 351  ASP   B O     1 
ATOM   11510 C  CB    . ASP   B  1  353  ? -10.840 1.607   94.763  1.00 22.25 ? 351  ASP   B CB    1 
ATOM   11511 C  CG    . ASP   B  1  353  ? -12.254 1.980   94.380  1.00 27.31 ? 351  ASP   B CG    1 
ATOM   11512 O  OD1   . ASP   B  1  353  ? -13.164 1.827   95.219  1.00 30.19 ? 351  ASP   B OD1   1 
ATOM   11513 O  OD2   . ASP   B  1  353  ? -12.444 2.432   93.223  1.00 30.75 ? 351  ASP   B OD2   1 
ATOM   11514 N  N     . PHE   B  1  354  ? -8.167  1.687   96.315  1.00 20.64 ? 352  PHE   B N     1 
ATOM   11515 C  CA    . PHE   B  1  354  ? -6.840  1.168   96.620  1.00 20.64 ? 352  PHE   B CA    1 
ATOM   11516 C  C     . PHE   B  1  354  ? -6.695  0.849   98.105  1.00 21.40 ? 352  PHE   B C     1 
ATOM   11517 O  O     . PHE   B  1  354  ? -6.186  -0.217  98.472  1.00 21.55 ? 352  PHE   B O     1 
ATOM   11518 C  CB    . PHE   B  1  354  ? -5.769  2.169   96.178  1.00 19.22 ? 352  PHE   B CB    1 
ATOM   11519 C  CG    . PHE   B  1  354  ? -4.392  1.811   96.662  1.00 21.36 ? 352  PHE   B CG    1 
ATOM   11520 C  CD1   . PHE   B  1  354  ? -3.627  0.884   95.977  1.00 22.50 ? 352  PHE   B CD1   1 
ATOM   11521 C  CD2   . PHE   B  1  354  ? -3.889  2.355   97.830  1.00 22.04 ? 352  PHE   B CD2   1 
ATOM   11522 C  CE1   . PHE   B  1  354  ? -2.363  0.526   96.441  1.00 21.68 ? 352  PHE   B CE1   1 
ATOM   11523 C  CE2   . PHE   B  1  354  ? -2.639  2.001   98.297  1.00 22.61 ? 352  PHE   B CE2   1 
ATOM   11524 C  CZ    . PHE   B  1  354  ? -1.876  1.089   97.604  1.00 21.60 ? 352  PHE   B CZ    1 
ATOM   11525 N  N     . ILE   B  1  355  ? -7.125  1.769   98.979  1.00 19.17 ? 353  ILE   B N     1 
ATOM   11526 C  CA    . ILE   B  1  355  ? -6.950  1.570   100.418 1.00 19.57 ? 353  ILE   B CA    1 
ATOM   11527 C  C     . ILE   B  1  355  ? -7.812  0.419   100.919 1.00 18.42 ? 353  ILE   B C     1 
ATOM   11528 O  O     . ILE   B  1  355  ? -7.372  -0.398  101.736 1.00 22.43 ? 353  ILE   B O     1 
ATOM   11529 C  CB    . ILE   B  1  355  ? -7.239  2.876   101.180 1.00 20.06 ? 353  ILE   B CB    1 
ATOM   11530 C  CG1   . ILE   B  1  355  ? -6.212  3.944   100.804 1.00 23.55 ? 353  ILE   B CG1   1 
ATOM   11531 C  CG2   . ILE   B  1  355  ? -7.307  2.625   102.707 1.00 20.96 ? 353  ILE   B CG2   1 
ATOM   11532 C  CD1   . ILE   B  1  355  ? -6.547  5.298   101.346 1.00 21.66 ? 353  ILE   B CD1   1 
ATOM   11533 N  N     . ILE   B  1  356  ? -9.061  0.346   100.457 1.00 20.34 ? 354  ILE   B N     1 
ATOM   11534 C  CA    . ILE   B  1  356  ? -9.930  -0.745  100.876 1.00 22.32 ? 354  ILE   B CA    1 
ATOM   11535 C  C     . ILE   B  1  356  ? -9.342  -2.084  100.462 1.00 22.57 ? 354  ILE   B C     1 
ATOM   11536 O  O     . ILE   B  1  356  ? -9.376  -3.057  101.224 1.00 21.92 ? 354  ILE   B O     1 
ATOM   11537 C  CB    . ILE   B  1  356  ? -11.345 -0.536  100.313 1.00 22.77 ? 354  ILE   B CB    1 
ATOM   11538 C  CG1   . ILE   B  1  356  ? -11.988 0.678   100.980 1.00 25.08 ? 354  ILE   B CG1   1 
ATOM   11539 C  CG2   . ILE   B  1  356  ? -12.183 -1.767  100.548 1.00 26.21 ? 354  ILE   B CG2   1 
ATOM   11540 C  CD1   . ILE   B  1  356  ? -13.244 1.164   100.275 1.00 24.88 ? 354  ILE   B CD1   1 
ATOM   11541 N  N     . ASP   B  1  357  ? -8.800  -2.156  99.245  1.00 22.02 ? 355  ASP   B N     1 
ATOM   11542 C  CA    . ASP   B  1  357  ? -8.180  -3.394  98.795  1.00 23.58 ? 355  ASP   B CA    1 
ATOM   11543 C  C     . ASP   B  1  357  ? -6.928  -3.698  99.605  1.00 22.18 ? 355  ASP   B C     1 
ATOM   11544 O  O     . ASP   B  1  357  ? -6.702  -4.851  99.994  1.00 21.73 ? 355  ASP   B O     1 
ATOM   11545 C  CB    . ASP   B  1  357  ? -7.842  -3.300  97.315  1.00 22.36 ? 355  ASP   B CB    1 
ATOM   11546 C  CG    . ASP   B  1  357  ? -6.979  -4.448  96.852  1.00 25.71 ? 355  ASP   B CG    1 
ATOM   11547 O  OD1   . ASP   B  1  357  ? -7.530  -5.553  96.682  1.00 26.54 ? 355  ASP   B OD1   1 
ATOM   11548 O  OD2   . ASP   B  1  357  ? -5.757  -4.251  96.672  1.00 24.50 ? 355  ASP   B OD2   1 
ATOM   11549 N  N     . LEU   B  1  358  ? -6.111  -2.675  99.875  1.00 21.07 ? 356  LEU   B N     1 
ATOM   11550 C  CA    . LEU   B  1  358  ? -4.933  -2.864  100.713 1.00 19.93 ? 356  LEU   B CA    1 
ATOM   11551 C  C     . LEU   B  1  358  ? -5.325  -3.396  102.083 1.00 20.15 ? 356  LEU   B C     1 
ATOM   11552 O  O     . LEU   B  1  358  ? -4.698  -4.330  102.599 1.00 21.17 ? 356  LEU   B O     1 
ATOM   11553 C  CB    . LEU   B  1  358  ? -4.183  -1.544  100.856 1.00 18.14 ? 356  LEU   B CB    1 
ATOM   11554 C  CG    . LEU   B  1  358  ? -2.945  -1.562  101.762 1.00 22.12 ? 356  LEU   B CG    1 
ATOM   11555 C  CD1   . LEU   B  1  358  ? -1.935  -2.630  101.334 1.00 22.60 ? 356  LEU   B CD1   1 
ATOM   11556 C  CD2   . LEU   B  1  358  ? -2.312  -0.180  101.758 1.00 21.52 ? 356  LEU   B CD2   1 
ATOM   11557 N  N     . ALA   B  1  359  ? -6.374  -2.827  102.680 1.00 20.74 ? 357  ALA   B N     1 
ATOM   11558 C  CA    . ALA   B  1  359  ? -6.825  -3.306  103.978 1.00 21.78 ? 357  ALA   B CA    1 
ATOM   11559 C  C     . ALA   B  1  359  ? -7.216  -4.774  103.902 1.00 24.88 ? 357  ALA   B C     1 
ATOM   11560 O  O     . ALA   B  1  359  ? -6.808  -5.579  104.743 1.00 23.08 ? 357  ALA   B O     1 
ATOM   11561 C  CB    . ALA   B  1  359  ? -8.005  -2.463  104.461 1.00 24.92 ? 357  ALA   B CB    1 
ATOM   11562 N  N     . ARG   B  1  360  ? -7.992  -5.138  102.874 1.00 21.41 ? 358  ARG   B N     1 
ATOM   11563 C  CA    . ARG   B  1  360  ? -8.443  -6.518  102.708 1.00 24.82 ? 358  ARG   B CA    1 
ATOM   11564 C  C     . ARG   B  1  360  ? -7.270  -7.474  102.578 1.00 21.76 ? 358  ARG   B C     1 
ATOM   11565 O  O     . ARG   B  1  360  ? -7.241  -8.530  103.219 1.00 24.70 ? 358  ARG   B O     1 
ATOM   11566 C  CB    . ARG   B  1  360  ? -9.325  -6.628  101.464 1.00 24.84 ? 358  ARG   B CB    1 
ATOM   11567 C  CG    . ARG   B  1  360  ? -10.721 -6.133  101.682 1.00 31.69 ? 358  ARG   B CG    1 
ATOM   11568 C  CD    . ARG   B  1  360  ? -11.648 -6.542  100.553 1.00 31.93 ? 358  ARG   B CD    1 
ATOM   11569 N  NE    . ARG   B  1  360  ? -13.029 -6.298  100.940 1.00 36.78 ? 358  ARG   B NE    1 
ATOM   11570 C  CZ    . ARG   B  1  360  ? -13.797 -5.344  100.435 1.00 39.52 ? 358  ARG   B CZ    1 
ATOM   11571 N  NH1   . ARG   B  1  360  ? -13.377 -4.570  99.451  1.00 42.90 ? 358  ARG   B NH1   1 
ATOM   11572 N  NH2   . ARG   B  1  360  ? -15.026 -5.177  100.920 1.00 47.70 ? 358  ARG   B NH2   1 
ATOM   11573 N  N     . ARG   B  1  361  ? -6.295  -7.134  101.738 1.00 24.53 ? 359  ARG   B N     1 
ATOM   11574 C  CA    . ARG   B  1  361  ? -5.243  -8.104  101.475 1.00 23.47 ? 359  ARG   B CA    1 
ATOM   11575 C  C     . ARG   B  1  361  ? -4.156  -8.108  102.538 1.00 22.22 ? 359  ARG   B C     1 
ATOM   11576 O  O     . ARG   B  1  361  ? -3.421  -9.092  102.635 1.00 25.19 ? 359  ARG   B O     1 
ATOM   11577 C  CB    . ARG   B  1  361  ? -4.664  -7.931  100.073 1.00 29.42 ? 359  ARG   B CB    1 
ATOM   11578 C  CG    . ARG   B  1  361  ? -3.930  -6.647  99.867  1.00 26.66 ? 359  ARG   B CG    1 
ATOM   11579 C  CD    . ARG   B  1  361  ? -3.547  -6.501  98.395  1.00 23.77 ? 359  ARG   B CD    1 
ATOM   11580 N  NE    . ARG   B  1  361  ? -3.345  -5.099  98.058  1.00 24.14 ? 359  ARG   B NE    1 
ATOM   11581 C  CZ    . ARG   B  1  361  ? -2.181  -4.472  98.147  1.00 21.68 ? 359  ARG   B CZ    1 
ATOM   11582 N  NH1   . ARG   B  1  361  ? -1.091  -5.098  98.557  1.00 24.92 ? 359  ARG   B NH1   1 
ATOM   11583 N  NH2   . ARG   B  1  361  ? -2.109  -3.184  97.813  1.00 22.68 ? 359  ARG   B NH2   1 
ATOM   11584 N  N     . SER   B  1  362  ? -4.054  -7.058  103.353 1.00 24.43 ? 360  SER   B N     1 
ATOM   11585 C  CA    . SER   B  1  362  ? -3.043  -7.011  104.403 1.00 23.36 ? 360  SER   B CA    1 
ATOM   11586 C  C     . SER   B  1  362  ? -3.566  -7.441  105.768 1.00 24.02 ? 360  SER   B C     1 
ATOM   11587 O  O     . SER   B  1  362  ? -2.764  -7.624  106.690 1.00 24.46 ? 360  SER   B O     1 
ATOM   11588 C  CB    . SER   B  1  362  ? -2.450  -5.601  104.509 1.00 24.12 ? 360  SER   B CB    1 
ATOM   11589 O  OG    . SER   B  1  362  ? -3.419  -4.688  104.982 1.00 23.59 ? 360  SER   B OG    1 
ATOM   11590 N  N     . GLY   B  1  363  ? -4.875  -7.590  105.930 1.00 22.33 ? 361  GLY   B N     1 
ATOM   11591 C  CA    . GLY   B  1  363  ? -5.402  -7.956  107.231 1.00 24.54 ? 361  GLY   B CA    1 
ATOM   11592 C  C     . GLY   B  1  363  ? -5.280  -6.846  108.251 1.00 24.38 ? 361  GLY   B C     1 
ATOM   11593 O  O     . GLY   B  1  363  ? -5.064  -7.112  109.438 1.00 26.09 ? 361  GLY   B O     1 
ATOM   11594 N  N     . ARG   B  1  364  ? -5.397  -5.602  107.806 1.00 23.23 ? 362  ARG   B N     1 
ATOM   11595 C  CA    . ARG   B  1  364  ? -5.326  -4.428  108.663 1.00 26.25 ? 362  ARG   B CA    1 
ATOM   11596 C  C     . ARG   B  1  364  ? -6.605  -3.649  108.439 1.00 27.80 ? 362  ARG   B C     1 
ATOM   11597 O  O     . ARG   B  1  364  ? -6.962  -3.367  107.294 1.00 28.37 ? 362  ARG   B O     1 
ATOM   11598 C  CB    . ARG   B  1  364  ? -4.177  -3.510  108.232 1.00 26.73 ? 362  ARG   B CB    1 
ATOM   11599 C  CG    . ARG   B  1  364  ? -2.803  -4.120  108.295 1.00 25.16 ? 362  ARG   B CG    1 
ATOM   11600 C  CD    . ARG   B  1  364  ? -2.275  -4.137  109.713 1.00 25.00 ? 362  ARG   B CD    1 
ATOM   11601 N  NE    . ARG   B  1  364  ? -1.020  -4.874  109.761 1.00 25.67 ? 362  ARG   B NE    1 
ATOM   11602 C  CZ    . ARG   B  1  364  ? 0.175   -4.341  109.553 1.00 24.18 ? 362  ARG   B CZ    1 
ATOM   11603 N  NH1   . ARG   B  1  364  ? 0.331   -3.038  109.353 1.00 23.87 ? 362  ARG   B NH1   1 
ATOM   11604 N  NH2   . ARG   B  1  364  ? 1.242   -5.132  109.546 1.00 26.61 ? 362  ARG   B NH2   1 
ATOM   11605 N  N     . ARG   B  1  365  ? -7.300  -3.300  109.507 1.00 23.97 ? 363  ARG   B N     1 
ATOM   11606 C  CA    . ARG   B  1  365  ? -8.326  -2.288  109.355 1.00 24.11 ? 363  ARG   B CA    1 
ATOM   11607 C  C     . ARG   B  1  365  ? -7.614  -0.951  109.323 1.00 24.68 ? 363  ARG   B C     1 
ATOM   11608 O  O     . ARG   B  1  365  ? -6.864  -0.623  110.244 1.00 25.89 ? 363  ARG   B O     1 
ATOM   11609 C  CB    . ARG   B  1  365  ? -9.341  -2.341  110.487 1.00 24.58 ? 363  ARG   B CB    1 
ATOM   11610 C  CG    . ARG   B  1  365  ? -10.583 -1.526  110.193 1.00 25.86 ? 363  ARG   B CG    1 
ATOM   11611 C  CD    . ARG   B  1  365  ? -11.683 -1.899  111.171 1.00 29.23 ? 363  ARG   B CD    1 
ATOM   11612 N  NE    . ARG   B  1  365  ? -12.954 -1.256  110.861 1.00 29.85 ? 363  ARG   B NE    1 
ATOM   11613 C  CZ    . ARG   B  1  365  ? -13.642 -0.515  111.719 1.00 26.44 ? 363  ARG   B CZ    1 
ATOM   11614 N  NH1   . ARG   B  1  365  ? -13.204 -0.297  112.950 1.00 28.29 ? 363  ARG   B NH1   1 
ATOM   11615 N  NH2   . ARG   B  1  365  ? -14.801 0.013   111.337 1.00 27.20 ? 363  ARG   B NH2   1 
ATOM   11616 N  N     . ILE   B  1  366  ? -7.773  -0.220  108.237 1.00 22.20 ? 364  ILE   B N     1 
ATOM   11617 C  CA    . ILE   B  1  366  ? -7.116  1.064   108.069 1.00 21.76 ? 364  ILE   B CA    1 
ATOM   11618 C  C     . ILE   B  1  366  ? -8.109  2.146   108.454 1.00 22.24 ? 364  ILE   B C     1 
ATOM   11619 O  O     . ILE   B  1  366  ? -9.265  2.126   108.004 1.00 21.17 ? 364  ILE   B O     1 
ATOM   11620 C  CB    . ILE   B  1  366  ? -6.617  1.233   106.623 1.00 20.11 ? 364  ILE   B CB    1 
ATOM   11621 C  CG1   . ILE   B  1  366  ? -5.571  0.157   106.313 1.00 24.34 ? 364  ILE   B CG1   1 
ATOM   11622 C  CG2   . ILE   B  1  366  ? -6.096  2.655   106.396 1.00 18.65 ? 364  ILE   B CG2   1 
ATOM   11623 C  CD1   . ILE   B  1  366  ? -5.178  0.032   104.841 1.00 23.90 ? 364  ILE   B CD1   1 
ATOM   11624 N  N     . MET   B  1  367  ? -7.678  3.067   109.314 1.00 20.57 ? 365  MET   B N     1 
ATOM   11625 C  CA    . MET   B  1  367  ? -8.510  4.207   109.665 1.00 24.02 ? 365  MET   B CA    1 
ATOM   11626 C  C     . MET   B  1  367  ? -8.406  5.210   108.529 1.00 22.35 ? 365  MET   B C     1 
ATOM   11627 O  O     . MET   B  1  367  ? -7.302  5.606   108.148 1.00 21.98 ? 365  MET   B O     1 
ATOM   11628 C  CB    . MET   B  1  367  ? -8.023  4.819   110.973 1.00 21.47 ? 365  MET   B CB    1 
ATOM   11629 C  CG    . MET   B  1  367  ? -7.811  3.773   112.042 1.00 21.88 ? 365  MET   B CG    1 
ATOM   11630 S  SD    . MET   B  1  367  ? -7.336  4.490   113.628 1.00 25.55 ? 365  MET   B SD    1 
ATOM   11631 C  CE    . MET   B  1  367  ? -8.888  4.866   114.422 1.00 34.55 ? 365  MET   B CE    1 
ATOM   11632 N  N     . VAL   B  1  368  ? -9.536  5.587   107.951 1.00 18.34 ? 366  VAL   B N     1 
ATOM   11633 C  CA    . VAL   B  1  368  ? -9.534  6.468   106.791 1.00 19.38 ? 366  VAL   B CA    1 
ATOM   11634 C  C     . VAL   B  1  368  ? -10.238 7.759   107.156 1.00 22.01 ? 366  VAL   B C     1 
ATOM   11635 O  O     . VAL   B  1  368  ? -11.465 7.780   107.330 1.00 21.27 ? 366  VAL   B O     1 
ATOM   11636 C  CB    . VAL   B  1  368  ? -10.196 5.828   105.566 1.00 20.32 ? 366  VAL   B CB    1 
ATOM   11637 C  CG1   . VAL   B  1  368  ? -10.139 6.807   104.415 1.00 23.87 ? 366  VAL   B CG1   1 
ATOM   11638 C  CG2   . VAL   B  1  368  ? -9.503  4.526   105.206 1.00 22.12 ? 366  VAL   B CG2   1 
ATOM   11639 N  N     . ARG   B  1  369  ? -9.485  8.848   107.215 1.00 19.82 ? 367  ARG   B N     1 
ATOM   11640 C  CA    . ARG   B  1  369  ? -10.079 10.145  107.487 1.00 18.97 ? 367  ARG   B CA    1 
ATOM   11641 C  C     . ARG   B  1  369  ? -10.459 10.760  106.156 1.00 19.31 ? 367  ARG   B C     1 
ATOM   11642 O  O     . ARG   B  1  369  ? -9.590  11.074  105.338 1.00 20.67 ? 367  ARG   B O     1 
ATOM   11643 C  CB    . ARG   B  1  369  ? -9.131  11.064  108.256 1.00 18.82 ? 367  ARG   B CB    1 
ATOM   11644 C  CG    . ARG   B  1  369  ? -9.795  12.392  108.619 1.00 21.12 ? 367  ARG   B CG    1 
ATOM   11645 C  CD    . ARG   B  1  369  ? -8.784  13.446  108.955 1.00 20.46 ? 367  ARG   B CD    1 
ATOM   11646 N  NE    . ARG   B  1  369  ? -8.107  13.129  110.202 1.00 19.68 ? 367  ARG   B NE    1 
ATOM   11647 C  CZ    . ARG   B  1  369  ? -6.883  13.527  110.503 1.00 20.14 ? 367  ARG   B CZ    1 
ATOM   11648 N  NH1   . ARG   B  1  369  ? -6.176  14.276  109.669 1.00 18.93 ? 367  ARG   B NH1   1 
ATOM   11649 N  NH2   . ARG   B  1  369  ? -6.347  13.139  111.658 1.00 21.58 ? 367  ARG   B NH2   1 
ATOM   11650 N  N     . LEU   B  1  370  ? -11.755 10.927  105.938 1.00 18.07 ? 368  LEU   B N     1 
ATOM   11651 C  CA    . LEU   B  1  370  ? -12.239 11.610  104.757 1.00 18.04 ? 368  LEU   B CA    1 
ATOM   11652 C  C     . LEU   B  1  370  ? -12.362 13.087  105.090 1.00 18.96 ? 368  LEU   B C     1 
ATOM   11653 O  O     . LEU   B  1  370  ? -13.075 13.466  106.028 1.00 19.98 ? 368  LEU   B O     1 
ATOM   11654 C  CB    . LEU   B  1  370  ? -13.584 11.035  104.330 1.00 19.49 ? 368  LEU   B CB    1 
ATOM   11655 C  CG    . LEU   B  1  370  ? -14.128 11.604  103.028 1.00 20.28 ? 368  LEU   B CG    1 
ATOM   11656 C  CD1   . LEU   B  1  370  ? -13.260 11.176  101.866 1.00 20.37 ? 368  LEU   B CD1   1 
ATOM   11657 C  CD2   . LEU   B  1  370  ? -15.561 11.136  102.827 1.00 21.01 ? 368  LEU   B CD2   1 
ATOM   11658 N  N     . VAL   B  1  371  ? -11.641 13.908  104.348 1.00 16.41 ? 369  VAL   B N     1 
ATOM   11659 C  CA    . VAL   B  1  371  ? -11.694 15.350  104.477 1.00 16.43 ? 369  VAL   B CA    1 
ATOM   11660 C  C     . VAL   B  1  371  ? -12.066 15.895  103.119 1.00 18.90 ? 369  VAL   B C     1 
ATOM   11661 O  O     . VAL   B  1  371  ? -12.022 15.193  102.110 1.00 19.07 ? 369  VAL   B O     1 
ATOM   11662 C  CB    . VAL   B  1  371  ? -10.347 15.933  104.934 1.00 15.99 ? 369  VAL   B CB    1 
ATOM   11663 C  CG1   . VAL   B  1  371  ? -9.895  15.238  106.193 1.00 17.53 ? 369  VAL   B CG1   1 
ATOM   11664 C  CG2   . VAL   B  1  371  ? -9.288  15.769  103.846 1.00 17.81 ? 369  VAL   B CG2   1 
ATOM   11665 N  N     . LYS   B  1  372  ? -12.400 17.178  103.090 1.00 17.42 ? 370  LYS   B N     1 
ATOM   11666 C  CA    . LYS   B  1  372  ? -12.514 17.826  101.792 1.00 17.39 ? 370  LYS   B CA    1 
ATOM   11667 C  C     . LYS   B  1  372  ? -11.134 18.179  101.247 1.00 16.57 ? 370  LYS   B C     1 
ATOM   11668 O  O     . LYS   B  1  372  ? -10.694 17.611  100.245 1.00 19.45 ? 370  LYS   B O     1 
ATOM   11669 C  CB    . LYS   B  1  372  ? -13.518 18.982  101.859 1.00 18.97 ? 370  LYS   B CB    1 
ATOM   11670 C  CG    . LYS   B  1  372  ? -14.915 18.411  102.135 1.00 19.91 ? 370  LYS   B CG    1 
ATOM   11671 C  CD    . LYS   B  1  372  ? -16.003 19.454  102.265 1.00 20.04 ? 370  LYS   B CD    1 
ATOM   11672 C  CE    . LYS   B  1  372  ? -17.286 18.779  102.745 1.00 21.55 ? 370  LYS   B CE    1 
ATOM   11673 N  NZ    . LYS   B  1  372  ? -18.382 19.771  102.985 1.00 23.15 ? 370  LYS   B NZ    1 
ATOM   11674 N  N     . GLY   B  1  373  ? -10.412 19.049  101.922 1.00 18.64 ? 371  GLY   B N     1 
ATOM   11675 C  CA    . GLY   B  1  373  ? -9.019  19.270  101.573 1.00 17.22 ? 371  GLY   B CA    1 
ATOM   11676 C  C     . GLY   B  1  373  ? -8.617  20.701  101.877 1.00 17.78 ? 371  GLY   B C     1 
ATOM   11677 O  O     . GLY   B  1  373  ? -9.396  21.636  101.758 1.00 20.15 ? 371  GLY   B O     1 
ATOM   11678 N  N     . ALA   B  1  374  ? -7.349  20.870  102.265 1.00 15.76 ? 372  ALA   B N     1 
ATOM   11679 C  CA    . ALA   B  1  374  ? -6.893  22.120  102.863 1.00 16.46 ? 372  ALA   B CA    1 
ATOM   11680 C  C     . ALA   B  1  374  ? -6.083  22.996  101.921 1.00 15.45 ? 372  ALA   B C     1 
ATOM   11681 O  O     . ALA   B  1  374  ? -5.744  24.119  102.298 1.00 17.81 ? 372  ALA   B O     1 
ATOM   11682 C  CB    . ALA   B  1  374  ? -6.066  21.853  104.127 1.00 18.16 ? 372  ALA   B CB    1 
ATOM   11683 N  N     . TYR   B  1  375  ? -5.785  22.531  100.707 1.00 16.48 ? 373  TYR   B N     1 
ATOM   11684 C  CA    . TYR   B  1  375  ? -4.842  23.225  99.839  1.00 16.92 ? 373  TYR   B CA    1 
ATOM   11685 C  C     . TYR   B  1  375  ? -5.495  23.770  98.579  1.00 16.92 ? 373  TYR   B C     1 
ATOM   11686 O  O     . TYR   B  1  375  ? -4.804  23.959  97.581  1.00 16.47 ? 373  TYR   B O     1 
ATOM   11687 C  CB    . TYR   B  1  375  ? -3.687  22.307  99.449  1.00 17.93 ? 373  TYR   B CB    1 
ATOM   11688 C  CG    . TYR   B  1  375  ? -2.948  21.726  100.623 1.00 17.27 ? 373  TYR   B CG    1 
ATOM   11689 C  CD1   . TYR   B  1  375  ? -3.483  20.674  101.361 1.00 18.68 ? 373  TYR   B CD1   1 
ATOM   11690 C  CD2   . TYR   B  1  375  ? -1.695  22.203  100.970 1.00 19.50 ? 373  TYR   B CD2   1 
ATOM   11691 C  CE1   . TYR   B  1  375  ? -2.800  20.141  102.436 1.00 17.50 ? 373  TYR   B CE1   1 
ATOM   11692 C  CE2   . TYR   B  1  375  ? -0.998  21.675  102.022 1.00 21.28 ? 373  TYR   B CE2   1 
ATOM   11693 C  CZ    . TYR   B  1  375  ? -1.554  20.644  102.756 1.00 20.43 ? 373  TYR   B CZ    1 
ATOM   11694 O  OH    . TYR   B  1  375  ? -0.849  20.113  103.801 1.00 21.97 ? 373  TYR   B OH    1 
ATOM   11695 N  N     . TRP   B  1  376  ? -6.802  24.030  98.601  1.00 17.00 ? 374  TRP   B N     1 
ATOM   11696 C  CA    . TRP   B  1  376  ? -7.525  24.275  97.357  1.00 16.20 ? 374  TRP   B CA    1 
ATOM   11697 C  C     . TRP   B  1  376  ? -6.927  25.424  96.549  1.00 16.23 ? 374  TRP   B C     1 
ATOM   11698 O  O     . TRP   B  1  376  ? -6.616  25.257  95.367  1.00 17.48 ? 374  TRP   B O     1 
ATOM   11699 C  CB    . TRP   B  1  376  ? -9.006  24.500  97.628  1.00 15.87 ? 374  TRP   B CB    1 
ATOM   11700 C  CG    . TRP   B  1  376  ? -9.743  24.661  96.348  1.00 16.41 ? 374  TRP   B CG    1 
ATOM   11701 C  CD1   . TRP   B  1  376  ? -10.137 23.667  95.497  1.00 14.55 ? 374  TRP   B CD1   1 
ATOM   11702 C  CD2   . TRP   B  1  376  ? -10.141 25.888  95.748  1.00 17.53 ? 374  TRP   B CD2   1 
ATOM   11703 N  NE1   . TRP   B  1  376  ? -10.777 24.206  94.412  1.00 16.19 ? 374  TRP   B NE1   1 
ATOM   11704 C  CE2   . TRP   B  1  376  ? -10.793 25.569  94.538  1.00 17.68 ? 374  TRP   B CE2   1 
ATOM   11705 C  CE3   . TRP   B  1  376  ? -10.030 27.231  96.123  1.00 20.22 ? 374  TRP   B CE3   1 
ATOM   11706 C  CZ2   . TRP   B  1  376  ? -11.308 26.540  93.691  1.00 18.32 ? 374  TRP   B CZ2   1 
ATOM   11707 C  CZ3   . TRP   B  1  376  ? -10.551 28.195  95.290  1.00 21.85 ? 374  TRP   B CZ3   1 
ATOM   11708 C  CH2   . TRP   B  1  376  ? -11.189 27.847  94.086  1.00 22.81 ? 374  TRP   B CH2   1 
ATOM   11709 N  N     . ASP   B  1  377  ? -6.794  26.608  97.158  1.00 17.55 ? 375  ASP   B N     1 
ATOM   11710 C  CA    . ASP   B  1  377  ? -6.287  27.761  96.416  1.00 18.08 ? 375  ASP   B CA    1 
ATOM   11711 C  C     . ASP   B  1  377  ? -4.924  27.461  95.831  1.00 17.02 ? 375  ASP   B C     1 
ATOM   11712 O  O     . ASP   B  1  377  ? -4.622  27.858  94.697  1.00 17.94 ? 375  ASP   B O     1 
ATOM   11713 C  CB    . ASP   B  1  377  ? -6.140  28.971  97.341  1.00 25.14 ? 375  ASP   B CB    1 
ATOM   11714 C  CG    . ASP   B  1  377  ? -7.457  29.475  97.878  1.00 34.79 ? 375  ASP   B CG    1 
ATOM   11715 O  OD1   . ASP   B  1  377  ? -8.387  29.676  97.082  1.00 41.87 ? 375  ASP   B OD1   1 
ATOM   11716 O  OD2   . ASP   B  1  377  ? -7.548  29.696  99.102  1.00 46.20 ? 375  ASP   B OD2   1 
ATOM   11717 N  N     . ALA   B  1  378  ? -4.072  26.791  96.609  1.00 16.93 ? 376  ALA   B N     1 
ATOM   11718 C  CA    . ALA   B  1  378  ? -2.723  26.506  96.148  1.00 15.62 ? 376  ALA   B CA    1 
ATOM   11719 C  C     . ALA   B  1  378  ? -2.733  25.511  94.998  1.00 15.40 ? 376  ALA   B C     1 
ATOM   11720 O  O     . ALA   B  1  378  ? -1.873  25.583  94.110  1.00 16.31 ? 376  ALA   B O     1 
ATOM   11721 C  CB    . ALA   B  1  378  ? -1.870  25.975  97.302  1.00 18.04 ? 376  ALA   B CB    1 
ATOM   11722 N  N     . GLU   B  1  379  ? -3.683  24.574  95.003  1.00 14.74 ? 377  GLU   B N     1 
ATOM   11723 C  CA    . GLU   B  1  379  ? -3.730  23.597  93.917  1.00 16.04 ? 377  GLU   B CA    1 
ATOM   11724 C  C     . GLU   B  1  379  ? -4.175  24.252  92.621  1.00 17.48 ? 377  GLU   B C     1 
ATOM   11725 O  O     . GLU   B  1  379  ? -3.688  23.894  91.540  1.00 15.56 ? 377  GLU   B O     1 
ATOM   11726 C  CB    . GLU   B  1  379  ? -4.648  22.422  94.258  1.00 16.70 ? 377  GLU   B CB    1 
ATOM   11727 C  CG    . GLU   B  1  379  ? -4.243  21.586  95.473  1.00 18.57 ? 377  GLU   B CG    1 
ATOM   11728 C  CD    . GLU   B  1  379  ? -2.939  20.813  95.327  1.00 20.34 ? 377  GLU   B CD    1 
ATOM   11729 O  OE1   . GLU   B  1  379  ? -2.320  20.791  94.235  1.00 20.05 ? 377  GLU   B OE1   1 
ATOM   11730 O  OE2   . GLU   B  1  379  ? -2.529  20.207  96.344  1.00 20.22 ? 377  GLU   B OE2   1 
ATOM   11731 N  N     . ILE   B  1  380  ? -5.104  25.211  92.699  1.00 17.12 ? 378  ILE   B N     1 
ATOM   11732 C  CA    . ILE   B  1  380  ? -5.503  25.933  91.491  1.00 16.73 ? 378  ILE   B CA    1 
ATOM   11733 C  C     . ILE   B  1  380  ? -4.316  26.694  90.925  1.00 15.78 ? 378  ILE   B C     1 
ATOM   11734 O  O     . ILE   B  1  380  ? -4.024  26.636  89.724  1.00 15.54 ? 378  ILE   B O     1 
ATOM   11735 C  CB    . ILE   B  1  380  ? -6.670  26.886  91.794  1.00 16.06 ? 378  ILE   B CB    1 
ATOM   11736 C  CG1   . ILE   B  1  380  ? -7.866  26.122  92.362  1.00 15.97 ? 378  ILE   B CG1   1 
ATOM   11737 C  CG2   . ILE   B  1  380  ? -7.042  27.688  90.552  1.00 16.45 ? 378  ILE   B CG2   1 
ATOM   11738 C  CD1   . ILE   B  1  380  ? -8.372  24.990  91.451  1.00 18.68 ? 378  ILE   B CD1   1 
ATOM   11739 N  N     . LYS   B  1  381  ? -3.629  27.443  91.789  1.00 15.53 ? 379  LYS   B N     1 
ATOM   11740 C  CA    . LYS   B  1  381  ? -2.498  28.229  91.324  1.00 15.02 ? 379  LYS   B CA    1 
ATOM   11741 C  C     . LYS   B  1  381  ? -1.424  27.339  90.728  1.00 16.48 ? 379  LYS   B C     1 
ATOM   11742 O  O     . LYS   B  1  381  ? -0.895  27.634  89.654  1.00 16.29 ? 379  LYS   B O     1 
ATOM   11743 C  CB    . LYS   B  1  381  ? -1.929  29.060  92.466  1.00 17.12 ? 379  LYS   B CB    1 
ATOM   11744 C  CG    . LYS   B  1  381  ? -0.677  29.811  92.066  1.00 17.98 ? 379  LYS   B CG    1 
ATOM   11745 C  CD    . LYS   B  1  381  ? -0.259  30.774  93.170  1.00 16.46 ? 379  LYS   B CD    1 
ATOM   11746 C  CE    . LYS   B  1  381  ? 0.898   31.631  92.696  1.00 18.25 ? 379  LYS   B CE    1 
ATOM   11747 N  NZ    . LYS   B  1  381  ? 1.352   32.538  93.799  1.00 17.61 ? 379  LYS   B NZ    1 
ATOM   11748 N  N     . ARG   B  1  382  ? -1.120  26.215  91.390  1.00 15.06 ? 380  ARG   B N     1 
ATOM   11749 C  CA    . ARG   B  1  382  ? -0.001  25.398  90.931  1.00 16.03 ? 380  ARG   B CA    1 
ATOM   11750 C  C     . ARG   B  1  382  ? -0.289  24.804  89.559  1.00 16.13 ? 380  ARG   B C     1 
ATOM   11751 O  O     . ARG   B  1  382  ? 0.578   24.799  88.675  1.00 15.85 ? 380  ARG   B O     1 
ATOM   11752 C  CB    . ARG   B  1  382  ? 0.279   24.293  91.949  1.00 17.65 ? 380  ARG   B CB    1 
ATOM   11753 C  CG    . ARG   B  1  382  ? 1.423   23.383  91.559  1.00 23.24 ? 380  ARG   B CG    1 
ATOM   11754 C  CD    . ARG   B  1  382  ? 2.719   24.157  91.351  1.00 25.24 ? 380  ARG   B CD    1 
ATOM   11755 N  NE    . ARG   B  1  382  ? 3.830   23.248  91.096  1.00 34.83 ? 380  ARG   B NE    1 
ATOM   11756 C  CZ    . ARG   B  1  382  ? 4.549   22.665  92.046  1.00 41.24 ? 380  ARG   B CZ    1 
ATOM   11757 N  NH1   . ARG   B  1  382  ? 4.310   22.888  93.331  1.00 36.32 ? 380  ARG   B NH1   1 
ATOM   11758 N  NH2   . ARG   B  1  382  ? 5.533   21.838  91.701  1.00 38.59 ? 380  ARG   B NH2   1 
ATOM   11759 N  N     . ALA   B  1  383  ? -1.514  24.346  89.346  1.00 14.10 ? 381  ALA   B N     1 
ATOM   11760 C  CA    . ALA   B  1  383  ? -1.851  23.761  88.051  1.00 13.53 ? 381  ALA   B CA    1 
ATOM   11761 C  C     . ALA   B  1  383  ? -1.796  24.815  86.960  1.00 14.72 ? 381  ALA   B C     1 
ATOM   11762 O  O     . ALA   B  1  383  ? -1.341  24.537  85.842  1.00 15.79 ? 381  ALA   B O     1 
ATOM   11763 C  CB    . ALA   B  1  383  ? -3.234  23.112  88.109  1.00 15.66 ? 381  ALA   B CB    1 
ATOM   11764 N  N     . GLN   B  1  384  ? -2.232  26.039  87.275  1.00 13.51 ? 382  GLN   B N     1 
ATOM   11765 C  CA    . GLN   B  1  384  ? -2.150  27.114  86.291  1.00 15.98 ? 382  GLN   B CA    1 
ATOM   11766 C  C     . GLN   B  1  384  ? -0.706  27.467  85.976  1.00 14.96 ? 382  GLN   B C     1 
ATOM   11767 O  O     . GLN   B  1  384  ? -0.340  27.584  84.802  1.00 16.85 ? 382  GLN   B O     1 
ATOM   11768 C  CB    . GLN   B  1  384  ? -2.919  28.341  86.762  1.00 14.30 ? 382  GLN   B CB    1 
ATOM   11769 C  CG    . GLN   B  1  384  ? -4.409  28.127  86.745  1.00 14.99 ? 382  GLN   B CG    1 
ATOM   11770 C  CD    . GLN   B  1  384  ? -5.136  29.356  87.151  1.00 14.81 ? 382  GLN   B CD    1 
ATOM   11771 O  OE1   . GLN   B  1  384  ? -4.560  30.234  87.782  1.00 19.53 ? 382  GLN   B OE1   1 
ATOM   11772 N  NE2   . GLN   B  1  384  ? -6.424  29.432  86.817  1.00 14.68 ? 382  GLN   B NE2   1 
ATOM   11773 N  N     . LEU   B  1  385  ? 0.129   27.644  87.011  1.00 14.95 ? 383  LEU   B N     1 
ATOM   11774 C  CA    . LEU   B  1  385  ? 1.547   27.927  86.793  1.00 15.54 ? 383  LEU   B CA    1 
ATOM   11775 C  C     . LEU   B  1  385  ? 2.200   26.859  85.939  1.00 15.61 ? 383  LEU   B C     1 
ATOM   11776 O  O     . LEU   B  1  385  ? 3.041   27.166  85.084  1.00 15.78 ? 383  LEU   B O     1 
ATOM   11777 C  CB    . LEU   B  1  385  ? 2.277   27.992  88.132  1.00 16.75 ? 383  LEU   B CB    1 
ATOM   11778 C  CG    . LEU   B  1  385  ? 1.936   29.195  88.992  1.00 19.37 ? 383  LEU   B CG    1 
ATOM   11779 C  CD1   . LEU   B  1  385  ? 2.710   29.089  90.274  1.00 19.74 ? 383  LEU   B CD1   1 
ATOM   11780 C  CD2   . LEU   B  1  385  ? 2.315   30.454  88.259  1.00 21.92 ? 383  LEU   B CD2   1 
ATOM   11781 N  N     . ASP   B  1  386  ? 1.847   25.598  86.167  1.00 16.32 ? 384  ASP   B N     1 
ATOM   11782 C  CA    . ASP   B  1  386  ? 2.531   24.504  85.499  1.00 16.27 ? 384  ASP   B CA    1 
ATOM   11783 C  C     . ASP   B  1  386  ? 1.937   24.170  84.141  1.00 17.35 ? 384  ASP   B C     1 
ATOM   11784 O  O     . ASP   B  1  386  ? 2.467   23.295  83.449  1.00 18.29 ? 384  ASP   B O     1 
ATOM   11785 C  CB    . ASP   B  1  386  ? 2.580   23.272  86.412  1.00 18.65 ? 384  ASP   B CB    1 
ATOM   11786 C  CG    . ASP   B  1  386  ? 3.482   23.482  87.627  1.00 24.87 ? 384  ASP   B CG    1 
ATOM   11787 O  OD1   . ASP   B  1  386  ? 4.213   24.506  87.679  1.00 25.51 ? 384  ASP   B OD1   1 
ATOM   11788 O  OD2   . ASP   B  1  386  ? 3.464   22.625  88.539  1.00 25.62 ? 384  ASP   B OD2   1 
ATOM   11789 N  N     . GLY   B  1  387  ? 0.865   24.845  83.738  1.00 16.07 ? 385  GLY   B N     1 
ATOM   11790 C  CA    . GLY   B  1  387  ? 0.278   24.608  82.434  1.00 18.16 ? 385  GLY   B CA    1 
ATOM   11791 C  C     . GLY   B  1  387  ? -0.232  23.196  82.276  1.00 19.63 ? 385  GLY   B C     1 
ATOM   11792 O  O     . GLY   B  1  387  ? -0.109  22.607  81.196  1.00 19.21 ? 385  GLY   B O     1 
ATOM   11793 N  N     . LEU   B  1  388  ? -0.805  22.632  83.333  1.00 17.03 ? 386  LEU   B N     1 
ATOM   11794 C  CA    . LEU   B  1  388  ? -1.174  21.231  83.249  1.00 17.16 ? 386  LEU   B CA    1 
ATOM   11795 C  C     . LEU   B  1  388  ? -2.578  21.077  82.669  1.00 18.12 ? 386  LEU   B C     1 
ATOM   11796 O  O     . LEU   B  1  388  ? -3.318  22.048  82.490  1.00 18.42 ? 386  LEU   B O     1 
ATOM   11797 C  CB    . LEU   B  1  388  ? -0.992  20.551  84.601  1.00 17.66 ? 386  LEU   B CB    1 
ATOM   11798 C  CG    . LEU   B  1  388  ? 0.477   20.601  85.028  1.00 16.36 ? 386  LEU   B CG    1 
ATOM   11799 C  CD1   . LEU   B  1  388  ? 0.725   19.913  86.371  1.00 21.56 ? 386  LEU   B CD1   1 
ATOM   11800 C  CD2   . LEU   B  1  388  ? 1.424   20.052  83.946  1.00 19.49 ? 386  LEU   B CD2   1 
ATOM   11801 N  N     . ALA   B  1  389  ? -2.925  19.833  82.331  1.00 18.81 ? 387  ALA   B N     1 
ATOM   11802 C  CA    . ALA   B  1  389  ? -4.123  19.594  81.529  1.00 19.69 ? 387  ALA   B CA    1 
ATOM   11803 C  C     . ALA   B  1  389  ? -5.382  20.035  82.258  1.00 19.99 ? 387  ALA   B C     1 
ATOM   11804 O  O     . ALA   B  1  389  ? -6.333  20.542  81.644  1.00 21.75 ? 387  ALA   B O     1 
ATOM   11805 C  CB    . ALA   B  1  389  ? -4.212  18.112  81.160  1.00 21.19 ? 387  ALA   B CB    1 
ATOM   11806 N  N     . ASP   B  1  390  ? -5.408  19.853  83.566  1.00 18.02 ? 388  ASP   B N     1 
ATOM   11807 C  CA    . ASP   B  1  390  ? -6.573  20.219  84.354  1.00 18.71 ? 388  ASP   B CA    1 
ATOM   11808 C  C     . ASP   B  1  390  ? -6.105  20.316  85.796  1.00 13.96 ? 388  ASP   B C     1 
ATOM   11809 O  O     . ASP   B  1  390  ? -4.923  20.131  86.101  1.00 16.34 ? 388  ASP   B O     1 
ATOM   11810 C  CB    . ASP   B  1  390  ? -7.687  19.183  84.174  1.00 19.81 ? 388  ASP   B CB    1 
ATOM   11811 C  CG    . ASP   B  1  390  ? -9.079  19.765  84.348  1.00 21.49 ? 388  ASP   B CG    1 
ATOM   11812 O  OD1   . ASP   B  1  390  ? -9.305  20.542  85.299  1.00 20.72 ? 388  ASP   B OD1   1 
ATOM   11813 O  OD2   . ASP   B  1  390  ? -9.953  19.433  83.516  1.00 26.19 ? 388  ASP   B OD2   1 
ATOM   11814 N  N     . PHE   B  1  391  ? -7.032  20.627  86.667  1.00 16.92 ? 389  PHE   B N     1 
ATOM   11815 C  CA    . PHE   B  1  391  ? -6.729  20.658  88.079  1.00 15.88 ? 389  PHE   B CA    1 
ATOM   11816 C  C     . PHE   B  1  391  ? -6.833  19.255  88.663  1.00 15.26 ? 389  PHE   B C     1 
ATOM   11817 O  O     . PHE   B  1  391  ? -7.535  18.400  88.127  1.00 17.95 ? 389  PHE   B O     1 
ATOM   11818 C  CB    . PHE   B  1  391  ? -7.723  21.578  88.776  1.00 17.35 ? 389  PHE   B CB    1 
ATOM   11819 C  CG    . PHE   B  1  391  ? -7.704  22.960  88.215  1.00 16.07 ? 389  PHE   B CG    1 
ATOM   11820 C  CD1   . PHE   B  1  391  ? -6.653  23.818  88.520  1.00 16.27 ? 389  PHE   B CD1   1 
ATOM   11821 C  CD2   . PHE   B  1  391  ? -8.677  23.379  87.332  1.00 17.45 ? 389  PHE   B CD2   1 
ATOM   11822 C  CE1   . PHE   B  1  391  ? -6.604  25.091  87.978  1.00 17.06 ? 389  PHE   B CE1   1 
ATOM   11823 C  CE2   . PHE   B  1  391  ? -8.644  24.655  86.801  1.00 17.19 ? 389  PHE   B CE2   1 
ATOM   11824 C  CZ    . PHE   B  1  391  ? -7.612  25.500  87.107  1.00 16.10 ? 389  PHE   B CZ    1 
ATOM   11825 N  N     . PRO   B  1  392  ? -6.115  18.990  89.749  1.00 15.35 ? 390  PRO   B N     1 
ATOM   11826 C  CA    . PRO   B  1  392  ? -6.262  17.713  90.446  1.00 14.48 ? 390  PRO   B CA    1 
ATOM   11827 C  C     . PRO   B  1  392  ? -7.324  17.780  91.525  1.00 16.40 ? 390  PRO   B C     1 
ATOM   11828 O  O     . PRO   B  1  392  ? -7.489  16.825  92.285  1.00 16.74 ? 390  PRO   B O     1 
ATOM   11829 C  CB    . PRO   B  1  392  ? -4.879  17.566  91.083  1.00 16.21 ? 390  PRO   B CB    1 
ATOM   11830 C  CG    . PRO   B  1  392  ? -4.516  18.981  91.466  1.00 17.84 ? 390  PRO   B CG    1 
ATOM   11831 C  CD    . PRO   B  1  392  ? -5.029  19.816  90.317  1.00 13.13 ? 390  PRO   B CD    1 
ATOM   11832 N  N     . VAL   B  1  393  ? -7.980  18.926  91.633  1.00 16.00 ? 391  VAL   B N     1 
ATOM   11833 C  CA    . VAL   B  1  393  ? -9.081  19.131  92.556  1.00 16.06 ? 391  VAL   B CA    1 
ATOM   11834 C  C     . VAL   B  1  393  ? -10.247 19.679  91.756  1.00 17.39 ? 391  VAL   B C     1 
ATOM   11835 O  O     . VAL   B  1  393  ? -10.085 20.178  90.642  1.00 17.17 ? 391  VAL   B O     1 
ATOM   11836 C  CB    . VAL   B  1  393  ? -8.711  20.106  93.697  1.00 16.11 ? 391  VAL   B CB    1 
ATOM   11837 C  CG1   . VAL   B  1  393  ? -7.584  19.531  94.552  1.00 17.62 ? 391  VAL   B CG1   1 
ATOM   11838 C  CG2   . VAL   B  1  393  ? -8.317  21.464  93.128  1.00 16.53 ? 391  VAL   B CG2   1 
ATOM   11839 N  N     . PHE   B  1  394  ? -11.435 19.583  92.348  1.00 17.29 ? 392  PHE   B N     1 
ATOM   11840 C  CA    . PHE   B  1  394  ? -12.610 20.214  91.771  1.00 16.48 ? 392  PHE   B CA    1 
ATOM   11841 C  C     . PHE   B  1  394  ? -12.505 21.731  91.866  1.00 16.65 ? 392  PHE   B C     1 
ATOM   11842 O  O     . PHE   B  1  394  ? -11.715 22.280  92.641  1.00 17.88 ? 392  PHE   B O     1 
ATOM   11843 C  CB    . PHE   B  1  394  ? -13.883 19.699  92.450  1.00 17.10 ? 392  PHE   B CB    1 
ATOM   11844 C  CG    . PHE   B  1  394  ? -14.024 18.220  92.333  1.00 16.89 ? 392  PHE   B CG    1 
ATOM   11845 C  CD1   . PHE   B  1  394  ? -14.257 17.651  91.089  1.00 19.03 ? 392  PHE   B CD1   1 
ATOM   11846 C  CD2   . PHE   B  1  394  ? -13.841 17.399  93.420  1.00 17.60 ? 392  PHE   B CD2   1 
ATOM   11847 C  CE1   . PHE   B  1  394  ? -14.337 16.290  90.938  1.00 18.77 ? 392  PHE   B CE1   1 
ATOM   11848 C  CE2   . PHE   B  1  394  ? -13.932 16.035  93.282  1.00 18.19 ? 392  PHE   B CE2   1 
ATOM   11849 C  CZ    . PHE   B  1  394  ? -14.169 15.478  92.035  1.00 17.69 ? 392  PHE   B CZ    1 
ATOM   11850 N  N     . THR   B  1  395  ? -13.291 22.408  91.029  1.00 17.48 ? 393  THR   B N     1 
ATOM   11851 C  CA    . THR   B  1  395  ? -13.285 23.863  90.968  1.00 18.22 ? 393  THR   B CA    1 
ATOM   11852 C  C     . THR   B  1  395  ? -14.577 24.501  91.451  1.00 17.02 ? 393  THR   B C     1 
ATOM   11853 O  O     . THR   B  1  395  ? -14.589 25.718  91.653  1.00 18.51 ? 393  THR   B O     1 
ATOM   11854 C  CB    . THR   B  1  395  ? -12.983 24.377  89.554  1.00 18.13 ? 393  THR   B CB    1 
ATOM   11855 O  OG1   . THR   B  1  395  ? -14.007 23.939  88.653  1.00 18.21 ? 393  THR   B OG1   1 
ATOM   11856 C  CG2   . THR   B  1  395  ? -11.624 23.896  89.077  1.00 18.89 ? 393  THR   B CG2   1 
ATOM   11857 N  N     . ARG   B  1  396  ? -15.652 23.734  91.626  1.00 17.88 ? 394  ARG   B N     1 
ATOM   11858 C  CA    . ARG   B  1  396  ? -16.864 24.212  92.285  1.00 17.84 ? 394  ARG   B CA    1 
ATOM   11859 C  C     . ARG   B  1  396  ? -16.958 23.550  93.643  1.00 19.59 ? 394  ARG   B C     1 
ATOM   11860 O  O     . ARG   B  1  396  ? -16.802 22.329  93.757  1.00 18.73 ? 394  ARG   B O     1 
ATOM   11861 C  CB    . ARG   B  1  396  ? -18.132 23.896  91.487  1.00 18.20 ? 394  ARG   B CB    1 
ATOM   11862 C  CG    . ARG   B  1  396  ? -18.142 24.531  90.117  1.00 22.00 ? 394  ARG   B CG    1 
ATOM   11863 C  CD    . ARG   B  1  396  ? -19.507 24.345  89.438  1.00 23.57 ? 394  ARG   B CD    1 
ATOM   11864 N  NE    . ARG   B  1  396  ? -19.450 24.843  88.070  1.00 27.08 ? 394  ARG   B NE    1 
ATOM   11865 C  CZ    . ARG   B  1  396  ? -20.258 25.762  87.562  1.00 31.17 ? 394  ARG   B CZ    1 
ATOM   11866 N  NH1   . ARG   B  1  396  ? -21.293 26.229  88.245  1.00 30.47 ? 394  ARG   B NH1   1 
ATOM   11867 N  NH2   . ARG   B  1  396  ? -20.029 26.217  86.332  1.00 29.16 ? 394  ARG   B NH2   1 
ATOM   11868 N  N     . LYS   B  1  397  ? -17.238 24.352  94.669  1.00 20.75 ? 395  LYS   B N     1 
ATOM   11869 C  CA    . LYS   B  1  397  ? -17.279 23.802  96.016  1.00 22.22 ? 395  LYS   B CA    1 
ATOM   11870 C  C     . LYS   B  1  397  ? -18.342 22.719  96.134  1.00 21.73 ? 395  LYS   B C     1 
ATOM   11871 O  O     . LYS   B  1  397  ? -18.144 21.707  96.816  1.00 22.23 ? 395  LYS   B O     1 
ATOM   11872 C  CB    . LYS   B  1  397  ? -17.494 24.934  97.013  1.00 21.14 ? 395  LYS   B CB    1 
ATOM   11873 C  CG    . LYS   B  1  397  ? -17.138 24.566  98.417  1.00 22.73 ? 395  LYS   B CG    1 
ATOM   11874 C  CD    . LYS   B  1  397  ? -18.377 24.185  99.156  1.00 26.86 ? 395  LYS   B CD    1 
ATOM   11875 C  CE    . LYS   B  1  397  ? -18.049 23.835  100.579 1.00 24.68 ? 395  LYS   B CE    1 
ATOM   11876 N  NZ    . LYS   B  1  397  ? -19.265 23.327  101.238 1.00 24.10 ? 395  LYS   B NZ    1 
ATOM   11877 N  N     . ILE   B  1  398  ? -19.463 22.890  95.432  1.00 19.94 ? 396  ILE   B N     1 
ATOM   11878 C  CA    . ILE   B  1  398  ? -20.514 21.885  95.482  1.00 26.20 ? 396  ILE   B CA    1 
ATOM   11879 C  C     . ILE   B  1  398  ? -20.026 20.546  94.936  1.00 20.55 ? 396  ILE   B C     1 
ATOM   11880 O  O     . ILE   B  1  398  ? -20.524 19.485  95.337  1.00 22.49 ? 396  ILE   B O     1 
ATOM   11881 C  CB    . ILE   B  1  398  ? -21.762 22.413  94.749  1.00 27.20 ? 396  ILE   B CB    1 
ATOM   11882 C  CG1   . ILE   B  1  398  ? -22.962 21.553  95.084  1.00 31.73 ? 396  ILE   B CG1   1 
ATOM   11883 C  CG2   . ILE   B  1  398  ? -21.529 22.469  93.237  1.00 24.81 ? 396  ILE   B CG2   1 
ATOM   11884 C  CD1   . ILE   B  1  398  ? -24.241 22.125  94.579  1.00 32.92 ? 396  ILE   B CD1   1 
ATOM   11885 N  N     . HIS   B  1  399  ? -19.038 20.563  94.034  1.00 20.17 ? 397  HIS   B N     1 
ATOM   11886 C  CA    . HIS   B  1  399  ? -18.506 19.306  93.518  1.00 19.75 ? 397  HIS   B CA    1 
ATOM   11887 C  C     . HIS   B  1  399  ? -17.733 18.562  94.591  1.00 19.54 ? 397  HIS   B C     1 
ATOM   11888 O  O     . HIS   B  1  399  ? -17.841 17.337  94.710  1.00 21.10 ? 397  HIS   B O     1 
ATOM   11889 C  CB    . HIS   B  1  399  ? -17.623 19.568  92.310  1.00 17.99 ? 397  HIS   B CB    1 
ATOM   11890 C  CG    . HIS   B  1  399  ? -18.385 20.063  91.123  1.00 20.87 ? 397  HIS   B CG    1 
ATOM   11891 N  ND1   . HIS   B  1  399  ? -17.766 20.576  90.008  1.00 22.09 ? 397  HIS   B ND1   1 
ATOM   11892 C  CD2   . HIS   B  1  399  ? -19.716 20.126  90.882  1.00 22.98 ? 397  HIS   B CD2   1 
ATOM   11893 C  CE1   . HIS   B  1  399  ? -18.681 20.933  89.124  1.00 22.82 ? 397  HIS   B CE1   1 
ATOM   11894 N  NE2   . HIS   B  1  399  ? -19.872 20.669  89.628  1.00 22.51 ? 397  HIS   B NE2   1 
ATOM   11895 N  N     . THR   B  1  400  ? -16.949 19.289  95.378  1.00 18.85 ? 398  THR   B N     1 
ATOM   11896 C  CA    . THR   B  1  400  ? -16.258 18.660  96.492  1.00 19.88 ? 398  THR   B CA    1 
ATOM   11897 C  C     . THR   B  1  400  ? -17.249 18.066  97.480  1.00 17.20 ? 398  THR   B C     1 
ATOM   11898 O  O     . THR   B  1  400  ? -17.037 16.963  97.994  1.00 19.15 ? 398  THR   B O     1 
ATOM   11899 C  CB    . THR   B  1  400  ? -15.348 19.683  97.155  1.00 18.65 ? 398  THR   B CB    1 
ATOM   11900 O  OG1   . THR   B  1  400  ? -14.256 19.940  96.268  1.00 18.09 ? 398  THR   B OG1   1 
ATOM   11901 C  CG2   . THR   B  1  400  ? -14.822 19.150  98.472  1.00 20.34 ? 398  THR   B CG2   1 
ATOM   11902 N  N     . ASP   B  1  401  ? -18.370 18.759  97.707  1.00 20.99 ? 399  ASP   B N     1 
ATOM   11903 C  CA    . ASP   B  1  401  ? -19.376 18.262  98.639  1.00 23.43 ? 399  ASP   B CA    1 
ATOM   11904 C  C     . ASP   B  1  401  ? -19.993 16.966  98.136  1.00 18.91 ? 399  ASP   B C     1 
ATOM   11905 O  O     . ASP   B  1  401  ? -20.173 16.013  98.904  1.00 21.04 ? 399  ASP   B O     1 
ATOM   11906 C  CB    . ASP   B  1  401  ? -20.463 19.316  98.843  1.00 24.10 ? 399  ASP   B CB    1 
ATOM   11907 C  CG    . ASP   B  1  401  ? -19.995 20.483  99.698  1.00 30.25 ? 399  ASP   B CG    1 
ATOM   11908 O  OD1   . ASP   B  1  401  ? -19.024 20.322  100.478 1.00 26.46 ? 399  ASP   B OD1   1 
ATOM   11909 O  OD2   . ASP   B  1  401  ? -20.609 21.566  99.596  1.00 26.88 ? 399  ASP   B OD2   1 
ATOM   11910 N  N     . VAL   B  1  402  ? -20.305 16.912  96.840  1.00 20.18 ? 400  VAL   B N     1 
ATOM   11911 C  CA    . VAL   B  1  402  ? -20.829 15.689  96.243  1.00 21.46 ? 400  VAL   B CA    1 
ATOM   11912 C  C     . VAL   B  1  402  ? -19.792 14.581  96.321  1.00 19.54 ? 400  VAL   B C     1 
ATOM   11913 O  O     . VAL   B  1  402  ? -20.102 13.441  96.693  1.00 22.13 ? 400  VAL   B O     1 
ATOM   11914 C  CB    . VAL   B  1  402  ? -21.261 15.957  94.795  1.00 23.25 ? 400  VAL   B CB    1 
ATOM   11915 C  CG1   . VAL   B  1  402  ? -21.610 14.646  94.093  1.00 25.86 ? 400  VAL   B CG1   1 
ATOM   11916 C  CG2   . VAL   B  1  402  ? -22.427 16.950  94.776  1.00 23.23 ? 400  VAL   B CG2   1 
ATOM   11917 N  N     . SER   B  1  403  ? -18.546 14.898  95.954  1.00 20.08 ? 401  SER   B N     1 
ATOM   11918 C  CA    . SER   B  1  403  ? -17.470 13.916  96.043  1.00 21.21 ? 401  SER   B CA    1 
ATOM   11919 C  C     . SER   B  1  403  ? -17.341 13.366  97.457  1.00 17.72 ? 401  SER   B C     1 
ATOM   11920 O  O     . SER   B  1  403  ? -17.198 12.152  97.653  1.00 20.50 ? 401  SER   B O     1 
ATOM   11921 C  CB    . SER   B  1  403  ? -16.157 14.558  95.604  1.00 19.30 ? 401  SER   B CB    1 
ATOM   11922 O  OG    . SER   B  1  403  ? -15.069 13.680  95.838  1.00 20.17 ? 401  SER   B OG    1 
ATOM   11923 N  N     . TYR   B  1  404  ? -17.417 14.245  98.456  1.00 20.11 ? 402  TYR   B N     1 
ATOM   11924 C  CA    . TYR   B  1  404  ? -17.346 13.808  99.848  1.00 23.84 ? 402  TYR   B CA    1 
ATOM   11925 C  C     . TYR   B  1  404  ? -18.457 12.819  100.170 1.00 20.53 ? 402  TYR   B C     1 
ATOM   11926 O  O     . TYR   B  1  404  ? -18.215 11.757  100.753 1.00 20.79 ? 402  TYR   B O     1 
ATOM   11927 C  CB    . TYR   B  1  404  ? -17.426 15.026  100.767 1.00 20.19 ? 402  TYR   B CB    1 
ATOM   11928 C  CG    . TYR   B  1  404  ? -17.064 14.735  102.205 1.00 20.10 ? 402  TYR   B CG    1 
ATOM   11929 C  CD1   . TYR   B  1  404  ? -17.992 14.203  103.085 1.00 24.75 ? 402  TYR   B CD1   1 
ATOM   11930 C  CD2   . TYR   B  1  404  ? -15.785 15.001  102.673 1.00 22.17 ? 402  TYR   B CD2   1 
ATOM   11931 C  CE1   . TYR   B  1  404  ? -17.654 13.949  104.400 1.00 23.53 ? 402  TYR   B CE1   1 
ATOM   11932 C  CE2   . TYR   B  1  404  ? -15.434 14.753  103.979 1.00 20.31 ? 402  TYR   B CE2   1 
ATOM   11933 C  CZ    . TYR   B  1  404  ? -16.375 14.219  104.840 1.00 23.52 ? 402  TYR   B CZ    1 
ATOM   11934 O  OH    . TYR   B  1  404  ? -16.051 13.961  106.153 1.00 25.31 ? 402  TYR   B OH    1 
ATOM   11935 N  N     . ILE   B  1  405  ? -19.689 13.147  99.781  1.00 21.80 ? 403  ILE   B N     1 
ATOM   11936 C  CA    . ILE   B  1  405  ? -20.818 12.276  100.082 1.00 24.86 ? 403  ILE   B CA    1 
ATOM   11937 C  C     . ILE   B  1  405  ? -20.697 10.954  99.331  1.00 21.38 ? 403  ILE   B C     1 
ATOM   11938 O  O     . ILE   B  1  405  ? -20.963 9.884   99.888  1.00 24.18 ? 403  ILE   B O     1 
ATOM   11939 C  CB    . ILE   B  1  405  ? -22.139 13.018  99.807  1.00 25.92 ? 403  ILE   B CB    1 
ATOM   11940 C  CG1   . ILE   B  1  405  ? -22.265 14.210  100.761 1.00 27.85 ? 403  ILE   B CG1   1 
ATOM   11941 C  CG2   . ILE   B  1  405  ? -23.320 12.090  99.977  1.00 24.86 ? 403  ILE   B CG2   1 
ATOM   11942 C  CD1   . ILE   B  1  405  ? -23.423 15.127  100.475 1.00 37.01 ? 403  ILE   B CD1   1 
ATOM   11943 N  N     . ALA   B  1  406  ? -20.250 11.001  98.069  1.00 24.54 ? 404  ALA   B N     1 
ATOM   11944 C  CA    . ALA   B  1  406  ? -20.051 9.769   97.308  1.00 23.93 ? 404  ALA   B CA    1 
ATOM   11945 C  C     . ALA   B  1  406  ? -18.966 8.905   97.930  1.00 24.26 ? 404  ALA   B C     1 
ATOM   11946 O  O     . ALA   B  1  406  ? -19.082 7.675   97.974  1.00 25.36 ? 404  ALA   B O     1 
ATOM   11947 C  CB    . ALA   B  1  406  ? -19.686 10.106  95.859  1.00 25.14 ? 404  ALA   B CB    1 
ATOM   11948 N  N     . CYS   B  1  407  ? -17.888 9.531   98.398  1.00 22.27 ? 405  CYS   B N     1 
ATOM   11949 C  CA    . CYS   B  1  407  ? -16.822 8.767   99.026  1.00 25.41 ? 405  CYS   B CA    1 
ATOM   11950 C  C     . CYS   B  1  407  ? -17.245 8.256   100.395 1.00 21.39 ? 405  CYS   B C     1 
ATOM   11951 O  O     . CYS   B  1  407  ? -16.833 7.165   100.805 1.00 23.90 ? 405  CYS   B O     1 
ATOM   11952 C  CB    . CYS   B  1  407  ? -15.562 9.618   99.093  1.00 21.26 ? 405  CYS   B CB    1 
ATOM   11953 S  SG    . CYS   B  1  407  ? -14.860 9.899   97.408  1.00 27.76 ? 405  CYS   B SG    1 
ATOM   11954 N  N     . ALA   B  1  408  ? -18.095 9.012   101.097 1.00 21.81 ? 406  ALA   B N     1 
ATOM   11955 C  CA    . ALA   B  1  408  ? -18.647 8.515   102.350 1.00 24.64 ? 406  ALA   B CA    1 
ATOM   11956 C  C     . ALA   B  1  408  ? -19.500 7.281   102.105 1.00 22.88 ? 406  ALA   B C     1 
ATOM   11957 O  O     . ALA   B  1  408  ? -19.459 6.326   102.886 1.00 27.49 ? 406  ALA   B O     1 
ATOM   11958 C  CB    . ALA   B  1  408  ? -19.464 9.611   103.027 1.00 26.99 ? 406  ALA   B CB    1 
ATOM   11959 N  N     . ALA   B  1  409  ? -20.247 7.269   100.997 1.00 24.68 ? 407  ALA   B N     1 
ATOM   11960 C  CA    . ALA   B  1  409  ? -21.035 6.092   100.658 1.00 29.70 ? 407  ALA   B CA    1 
ATOM   11961 C  C     . ALA   B  1  409  ? -20.141 4.881   100.447 1.00 25.27 ? 407  ALA   B C     1 
ATOM   11962 O  O     . ALA   B  1  409  ? -20.451 3.781   100.920 1.00 28.38 ? 407  ALA   B O     1 
ATOM   11963 C  CB    . ALA   B  1  409  ? -21.886 6.367   99.418  1.00 24.92 ? 407  ALA   B CB    1 
ATOM   11964 N  N     . LYS   B  1  410  ? -19.011 5.072   99.764  1.00 26.16 ? 408  LYS   B N     1 
ATOM   11965 C  CA    . LYS   B  1  410  ? -18.072 3.977   99.569  1.00 22.92 ? 408  LYS   B CA    1 
ATOM   11966 C  C     . LYS   B  1  410  ? -17.493 3.517   100.898 1.00 27.81 ? 408  LYS   B C     1 
ATOM   11967 O  O     . LYS   B  1  410  ? -17.402 2.314   101.162 1.00 26.88 ? 408  LYS   B O     1 
ATOM   11968 C  CB    . LYS   B  1  410  ? -16.957 4.416   98.621  1.00 24.95 ? 408  LYS   B CB    1 
ATOM   11969 C  CG    . LYS   B  1  410  ? -15.950 3.322   98.302  1.00 26.25 ? 408  LYS   B CG    1 
ATOM   11970 C  CD    . LYS   B  1  410  ? -14.780 3.843   97.465  1.00 28.13 ? 408  LYS   B CD    1 
ATOM   11971 C  CE    . LYS   B  1  410  ? -15.202 4.330   96.084  1.00 31.48 ? 408  LYS   B CE    1 
ATOM   11972 N  NZ    . LYS   B  1  410  ? -15.491 3.205   95.132  1.00 30.32 ? 408  LYS   B NZ    1 
ATOM   11973 N  N     . LEU   B  1  411  ? -17.093 4.467   101.748 1.00 25.82 ? 409  LEU   B N     1 
ATOM   11974 C  CA    . LEU   B  1  411  ? -16.542 4.101   103.050 1.00 26.99 ? 409  LEU   B CA    1 
ATOM   11975 C  C     . LEU   B  1  411  ? -17.581 3.416   103.923 1.00 25.42 ? 409  LEU   B C     1 
ATOM   11976 O  O     . LEU   B  1  411  ? -17.283 2.400   104.555 1.00 26.97 ? 409  LEU   B O     1 
ATOM   11977 C  CB    . LEU   B  1  411  ? -15.976 5.330   103.748 1.00 24.34 ? 409  LEU   B CB    1 
ATOM   11978 C  CG    . LEU   B  1  411  ? -14.634 5.781   103.190 1.00 24.79 ? 409  LEU   B CG    1 
ATOM   11979 C  CD1   . LEU   B  1  411  ? -14.323 7.179   103.688 1.00 25.12 ? 409  LEU   B CD1   1 
ATOM   11980 C  CD2   . LEU   B  1  411  ? -13.535 4.807   103.591 1.00 25.37 ? 409  LEU   B CD2   1 
ATOM   11981 N  N     . LEU   B  1  412  ? -18.806 3.952   103.965 1.00 27.68 ? 410  LEU   B N     1 
ATOM   11982 C  CA    . LEU   B  1  412  ? -19.833 3.381   104.830 1.00 27.52 ? 410  LEU   B CA    1 
ATOM   11983 C  C     . LEU   B  1  412  ? -20.224 1.977   104.407 1.00 30.63 ? 410  LEU   B C     1 
ATOM   11984 O  O     . LEU   B  1  412  ? -20.698 1.202   105.243 1.00 33.16 ? 410  LEU   B O     1 
ATOM   11985 C  CB    . LEU   B  1  412  ? -21.064 4.284   104.879 1.00 31.84 ? 410  LEU   B CB    1 
ATOM   11986 C  CG    . LEU   B  1  412  ? -20.892 5.540   105.737 1.00 31.98 ? 410  LEU   B CG    1 
ATOM   11987 C  CD1   . LEU   B  1  412  ? -22.052 6.497   105.536 1.00 32.85 ? 410  LEU   B CD1   1 
ATOM   11988 C  CD2   . LEU   B  1  412  ? -20.753 5.152   107.204 1.00 35.06 ? 410  LEU   B CD2   1 
ATOM   11989 N  N     . ALA   B  1  413  ? -20.032 1.631   103.136 1.00 30.17 ? 411  ALA   B N     1 
ATOM   11990 C  CA    . ALA   B  1  413  ? -20.249 0.260   102.701 1.00 35.19 ? 411  ALA   B CA    1 
ATOM   11991 C  C     . ALA   B  1  413  ? -19.063 -0.638  103.005 1.00 31.57 ? 411  ALA   B C     1 
ATOM   11992 O  O     . ALA   B  1  413  ? -19.155 -1.849  102.791 1.00 34.69 ? 411  ALA   B O     1 
ATOM   11993 C  CB    . ALA   B  1  413  ? -20.565 0.218   101.205 1.00 31.41 ? 411  ALA   B CB    1 
ATOM   11994 N  N     . ALA   B  1  414  ? -17.960 -0.085  103.517 1.00 28.01 ? 412  ALA   B N     1 
ATOM   11995 C  CA    . ALA   B  1  414  ? -16.763 -0.869  103.780 1.00 27.00 ? 412  ALA   B CA    1 
ATOM   11996 C  C     . ALA   B  1  414  ? -16.342 -0.814  105.247 1.00 30.53 ? 412  ALA   B C     1 
ATOM   11997 O  O     . ALA   B  1  414  ? -15.164 -1.033  105.550 1.00 29.42 ? 412  ALA   B O     1 
ATOM   11998 C  CB    . ALA   B  1  414  ? -15.616 -0.404  102.880 1.00 28.02 ? 412  ALA   B CB    1 
ATOM   11999 N  N     . THR   B  1  415  ? -17.275 -0.530  106.165 1.00 28.30 ? 413  THR   B N     1 
ATOM   12000 C  CA    . THR   B  1  415  ? -16.903 -0.387  107.573 1.00 30.33 ? 413  THR   B CA    1 
ATOM   12001 C  C     . THR   B  1  415  ? -16.378 -1.683  108.166 1.00 29.23 ? 413  THR   B C     1 
ATOM   12002 O  O     . THR   B  1  415  ? -15.705 -1.656  109.204 1.00 31.81 ? 413  THR   B O     1 
ATOM   12003 C  CB    . THR   B  1  415  ? -18.074 0.128   108.414 1.00 29.42 ? 413  THR   B CB    1 
ATOM   12004 O  OG1   . THR   B  1  415  ? -19.162 -0.802  108.351 1.00 32.56 ? 413  THR   B OG1   1 
ATOM   12005 C  CG2   . THR   B  1  415  ? -18.530 1.490   107.931 1.00 30.91 ? 413  THR   B CG2   1 
ATOM   12006 N  N     . ASP   B  1  416  ? -16.672 -2.819  107.536 1.00 33.72 ? 414  ASP   B N     1 
ATOM   12007 C  CA    . ASP   B  1  416  ? -16.068 -4.076  107.945 1.00 32.78 ? 414  ASP   B CA    1 
ATOM   12008 C  C     . ASP   B  1  416  ? -14.582 -4.141  107.619 1.00 29.56 ? 414  ASP   B C     1 
ATOM   12009 O  O     . ASP   B  1  416  ? -13.885 -5.008  108.154 1.00 35.40 ? 414  ASP   B O     1 
ATOM   12010 C  CB    . ASP   B  1  416  ? -16.813 -5.238  107.273 1.00 32.78 ? 414  ASP   B CB    1 
ATOM   12011 C  CG    . ASP   B  1  416  ? -17.046 -5.005  105.781 1.00 43.65 ? 414  ASP   B CG    1 
ATOM   12012 O  OD1   . ASP   B  1  416  ? -17.526 -3.912  105.402 1.00 42.62 ? 414  ASP   B OD1   1 
ATOM   12013 O  OD2   . ASP   B  1  416  ? -16.746 -5.920  104.980 1.00 49.84 ? 414  ASP   B OD2   1 
ATOM   12014 N  N     . VAL   B  1  417  ? -14.075 -3.229  106.788 1.00 29.81 ? 415  VAL   B N     1 
ATOM   12015 C  CA    . VAL   B  1  417  ? -12.737 -3.338  106.212 1.00 27.28 ? 415  VAL   B CA    1 
ATOM   12016 C  C     . VAL   B  1  417  ? -11.886 -2.128  106.586 1.00 27.99 ? 415  VAL   B C     1 
ATOM   12017 O  O     . VAL   B  1  417  ? -10.663 -2.223  106.730 1.00 26.41 ? 415  VAL   B O     1 
ATOM   12018 C  CB    . VAL   B  1  417  ? -12.855 -3.475  104.683 1.00 33.82 ? 415  VAL   B CB    1 
ATOM   12019 C  CG1   . VAL   B  1  417  ? -11.491 -3.519  104.028 1.00 27.39 ? 415  VAL   B CG1   1 
ATOM   12020 C  CG2   . VAL   B  1  417  ? -13.678 -4.716  104.329 1.00 32.22 ? 415  VAL   B CG2   1 
ATOM   12021 N  N     . VAL   B  1  418  ? -12.521 -0.971  106.722 1.00 26.20 ? 416  VAL   B N     1 
ATOM   12022 C  CA    . VAL   B  1  418  ? -11.825 0.244   107.104 1.00 22.94 ? 416  VAL   B CA    1 
ATOM   12023 C  C     . VAL   B  1  418  ? -12.648 0.925   108.178 1.00 25.96 ? 416  VAL   B C     1 
ATOM   12024 O  O     . VAL   B  1  418  ? -13.829 0.629   108.372 1.00 25.77 ? 416  VAL   B O     1 
ATOM   12025 C  CB    . VAL   B  1  418  ? -11.603 1.201   105.916 1.00 26.19 ? 416  VAL   B CB    1 
ATOM   12026 C  CG1   . VAL   B  1  418  ? -10.628 0.591   104.921 1.00 24.13 ? 416  VAL   B CG1   1 
ATOM   12027 C  CG2   . VAL   B  1  418  ? -12.941 1.525   105.245 1.00 23.50 ? 416  VAL   B CG2   1 
ATOM   12028 N  N     . PHE   B  1  419  ? -12.001 1.845   108.883 1.00 23.42 ? 417  PHE   B N     1 
ATOM   12029 C  CA    . PHE   B  1  419  ? -12.679 2.638   109.899 1.00 23.01 ? 417  PHE   B CA    1 
ATOM   12030 C  C     . PHE   B  1  419  ? -12.849 4.048   109.356 1.00 20.96 ? 417  PHE   B C     1 
ATOM   12031 O  O     . PHE   B  1  419  ? -11.892 4.839   109.359 1.00 21.80 ? 417  PHE   B O     1 
ATOM   12032 C  CB    . PHE   B  1  419  ? -11.865 2.649   111.192 1.00 23.68 ? 417  PHE   B CB    1 
ATOM   12033 C  CG    . PHE   B  1  419  ? -12.467 3.488   112.274 1.00 25.74 ? 417  PHE   B CG    1 
ATOM   12034 C  CD1   . PHE   B  1  419  ? -13.741 3.229   112.746 1.00 26.30 ? 417  PHE   B CD1   1 
ATOM   12035 C  CD2   . PHE   B  1  419  ? -11.754 4.536   112.824 1.00 23.44 ? 417  PHE   B CD2   1 
ATOM   12036 C  CE1   . PHE   B  1  419  ? -14.293 4.002   113.753 1.00 27.02 ? 417  PHE   B CE1   1 
ATOM   12037 C  CE2   . PHE   B  1  419  ? -12.297 5.308   113.838 1.00 21.41 ? 417  PHE   B CE2   1 
ATOM   12038 C  CZ    . PHE   B  1  419  ? -13.567 5.046   114.299 1.00 24.31 ? 417  PHE   B CZ    1 
ATOM   12039 N  N     . PRO   B  1  420  ? -14.035 4.409   108.883 1.00 22.10 ? 418  PRO   B N     1 
ATOM   12040 C  CA    . PRO   B  1  420  ? -14.223 5.730   108.283 1.00 20.80 ? 418  PRO   B CA    1 
ATOM   12041 C  C     . PRO   B  1  420  ? -14.316 6.807   109.346 1.00 21.13 ? 418  PRO   B C     1 
ATOM   12042 O  O     . PRO   B  1  420  ? -14.966 6.639   110.379 1.00 20.83 ? 418  PRO   B O     1 
ATOM   12043 C  CB    . PRO   B  1  420  ? -15.554 5.584   107.533 1.00 23.27 ? 418  PRO   B CB    1 
ATOM   12044 C  CG    . PRO   B  1  420  ? -15.761 4.096   107.392 1.00 23.37 ? 418  PRO   B CG    1 
ATOM   12045 C  CD    . PRO   B  1  420  ? -15.187 3.529   108.647 1.00 23.13 ? 418  PRO   B CD    1 
ATOM   12046 N  N     . GLN   B  1  421  ? -13.628 7.915   109.092 1.00 21.46 ? 419  GLN   B N     1 
ATOM   12047 C  CA    . GLN   B  1  421  ? -13.583 9.048   110.004 1.00 21.94 ? 419  GLN   B CA    1 
ATOM   12048 C  C     . GLN   B  1  421  ? -13.964 10.266  109.185 1.00 21.66 ? 419  GLN   B C     1 
ATOM   12049 O  O     . GLN   B  1  421  ? -13.200 10.700  108.320 1.00 20.79 ? 419  GLN   B O     1 
ATOM   12050 C  CB    . GLN   B  1  421  ? -12.183 9.193   110.602 1.00 20.04 ? 419  GLN   B CB    1 
ATOM   12051 C  CG    . GLN   B  1  421  ? -11.718 7.922   111.281 1.00 20.58 ? 419  GLN   B CG    1 
ATOM   12052 C  CD    . GLN   B  1  421  ? -10.222 7.893   111.479 1.00 21.52 ? 419  GLN   B CD    1 
ATOM   12053 O  OE1   . GLN   B  1  421  ? -9.459  7.994   110.527 1.00 22.44 ? 419  GLN   B OE1   1 
ATOM   12054 N  NE2   . GLN   B  1  421  ? -9.796  7.771   112.727 1.00 21.07 ? 419  GLN   B NE2   1 
ATOM   12055 N  N     . PHE   B  1  422  ? -15.150 10.804  109.432 1.00 22.72 ? 420  PHE   B N     1 
ATOM   12056 C  CA    . PHE   B  1  422  ? -15.701 11.858  108.586 1.00 21.05 ? 420  PHE   B CA    1 
ATOM   12057 C  C     . PHE   B  1  422  ? -15.391 13.203  109.222 1.00 20.97 ? 420  PHE   B C     1 
ATOM   12058 O  O     . PHE   B  1  422  ? -16.105 13.679  110.106 1.00 21.55 ? 420  PHE   B O     1 
ATOM   12059 C  CB    . PHE   B  1  422  ? -17.192 11.628  108.366 1.00 18.44 ? 420  PHE   B CB    1 
ATOM   12060 C  CG    . PHE   B  1  422  ? -17.490 10.311  107.710 1.00 20.98 ? 420  PHE   B CG    1 
ATOM   12061 C  CD1   . PHE   B  1  422  ? -17.094 10.075  106.405 1.00 23.21 ? 420  PHE   B CD1   1 
ATOM   12062 C  CD2   . PHE   B  1  422  ? -18.144 9.304   108.400 1.00 23.44 ? 420  PHE   B CD2   1 
ATOM   12063 C  CE1   . PHE   B  1  422  ? -17.353 8.863   105.800 1.00 24.30 ? 420  PHE   B CE1   1 
ATOM   12064 C  CE2   . PHE   B  1  422  ? -18.414 8.087   107.792 1.00 24.89 ? 420  PHE   B CE2   1 
ATOM   12065 C  CZ    . PHE   B  1  422  ? -18.018 7.875   106.483 1.00 26.38 ? 420  PHE   B CZ    1 
ATOM   12066 N  N     . ALA   B  1  423  ? -14.295 13.808  108.768 1.00 19.90 ? 421  ALA   B N     1 
ATOM   12067 C  CA    . ALA   B  1  423  ? -13.869 15.113  109.248 1.00 22.30 ? 421  ALA   B CA    1 
ATOM   12068 C  C     . ALA   B  1  423  ? -14.609 16.183  108.462 1.00 22.31 ? 421  ALA   B C     1 
ATOM   12069 O  O     . ALA   B  1  423  ? -14.382 16.352  107.257 1.00 23.08 ? 421  ALA   B O     1 
ATOM   12070 C  CB    . ALA   B  1  423  ? -12.365 15.257  109.045 1.00 18.72 ? 421  ALA   B CB    1 
ATOM   12071 N  N     . THR   B  1  424  ? -15.468 16.934  109.143 1.00 23.45 ? 422  THR   B N     1 
ATOM   12072 C  CA    . THR   B  1  424  ? -16.170 18.027  108.487 1.00 21.96 ? 422  THR   B CA    1 
ATOM   12073 C  C     . THR   B  1  424  ? -16.783 18.913  109.557 1.00 20.55 ? 422  THR   B C     1 
ATOM   12074 O  O     . THR   B  1  424  ? -17.194 18.422  110.615 1.00 24.79 ? 422  THR   B O     1 
ATOM   12075 C  CB    . THR   B  1  424  ? -17.266 17.507  107.536 1.00 24.33 ? 422  THR   B CB    1 
ATOM   12076 O  OG1   . THR   B  1  424  ? -17.914 18.620  106.912 1.00 25.11 ? 422  THR   B OG1   1 
ATOM   12077 C  CG2   . THR   B  1  424  ? -18.305 16.651  108.285 1.00 24.90 ? 422  THR   B CG2   1 
ATOM   12078 N  N     . HIS   B  1  425  ? -16.812 20.216  109.292 1.00 21.74 ? 423  HIS   B N     1 
ATOM   12079 C  CA    . HIS   B  1  425  ? -17.545 21.147  110.142 1.00 20.71 ? 423  HIS   B CA    1 
ATOM   12080 C  C     . HIS   B  1  425  ? -18.890 21.532  109.544 1.00 25.29 ? 423  HIS   B C     1 
ATOM   12081 O  O     . HIS   B  1  425  ? -19.592 22.376  110.108 1.00 28.25 ? 423  HIS   B O     1 
ATOM   12082 C  CB    . HIS   B  1  425  ? -16.704 22.394  110.390 1.00 22.30 ? 423  HIS   B CB    1 
ATOM   12083 C  CG    . HIS   B  1  425  ? -15.425 22.108  111.102 1.00 24.60 ? 423  HIS   B CG    1 
ATOM   12084 N  ND1   . HIS   B  1  425  ? -14.215 22.630  110.701 1.00 29.36 ? 423  HIS   B ND1   1 
ATOM   12085 C  CD2   . HIS   B  1  425  ? -15.165 21.343  112.189 1.00 23.78 ? 423  HIS   B CD2   1 
ATOM   12086 C  CE1   . HIS   B  1  425  ? -13.263 22.200  111.512 1.00 25.76 ? 423  HIS   B CE1   1 
ATOM   12087 N  NE2   . HIS   B  1  425  ? -13.814 21.417  112.422 1.00 23.45 ? 423  HIS   B NE2   1 
ATOM   12088 N  N     . ASN   B  1  426  ? -19.260 20.925  108.424 1.00 25.82 ? 424  ASN   B N     1 
ATOM   12089 C  CA    . ASN   B  1  426  ? -20.454 21.304  107.679 1.00 25.73 ? 424  ASN   B CA    1 
ATOM   12090 C  C     . ASN   B  1  426  ? -21.624 20.452  108.160 1.00 26.70 ? 424  ASN   B C     1 
ATOM   12091 O  O     . ASN   B  1  426  ? -21.624 19.231  107.982 1.00 24.12 ? 424  ASN   B O     1 
ATOM   12092 C  CB    . ASN   B  1  426  ? -20.180 21.082  106.195 1.00 25.27 ? 424  ASN   B CB    1 
ATOM   12093 C  CG    . ASN   B  1  426  ? -21.263 21.640  105.308 1.00 27.63 ? 424  ASN   B CG    1 
ATOM   12094 O  OD1   . ASN   B  1  426  ? -22.456 21.462  105.564 1.00 26.52 ? 424  ASN   B OD1   1 
ATOM   12095 N  ND2   . ASN   B  1  426  ? -20.848 22.316  104.236 1.00 26.86 ? 424  ASN   B ND2   1 
ATOM   12096 N  N     . ALA   B  1  427  ? -22.625 21.103  108.770 1.00 29.18 ? 425  ALA   B N     1 
ATOM   12097 C  CA    . ALA   B  1  427  ? -23.760 20.380  109.333 1.00 33.16 ? 425  ALA   B CA    1 
ATOM   12098 C  C     . ALA   B  1  427  ? -24.557 19.651  108.262 1.00 26.07 ? 425  ALA   B C     1 
ATOM   12099 O  O     . ALA   B  1  427  ? -25.106 18.573  108.524 1.00 28.58 ? 425  ALA   B O     1 
ATOM   12100 C  CB    . ALA   B  1  427  ? -24.671 21.342  110.099 1.00 31.99 ? 425  ALA   B CB    1 
ATOM   12101 N  N     . GLN   B  1  428  ? -24.626 20.212  107.056 1.00 27.78 ? 426  GLN   B N     1 
ATOM   12102 C  CA    . GLN   B  1  428  ? -25.321 19.526  105.976 1.00 31.18 ? 426  GLN   B CA    1 
ATOM   12103 C  C     . GLN   B  1  428  ? -24.579 18.258  105.578 1.00 27.58 ? 426  GLN   B C     1 
ATOM   12104 O  O     . GLN   B  1  428  ? -25.188 17.192  105.424 1.00 29.69 ? 426  GLN   B O     1 
ATOM   12105 C  CB    . GLN   B  1  428  ? -25.497 20.467  104.784 1.00 29.96 ? 426  GLN   B CB    1 
ATOM   12106 C  CG    . GLN   B  1  428  ? -26.511 19.976  103.756 1.00 30.57 ? 426  GLN   B CG    1 
ATOM   12107 C  CD    . GLN   B  1  428  ? -25.990 18.823  102.920 1.00 29.05 ? 426  GLN   B CD    1 
ATOM   12108 O  OE1   . GLN   B  1  428  ? -24.810 18.784  102.557 1.00 31.33 ? 426  GLN   B OE1   1 
ATOM   12109 N  NE2   . GLN   B  1  428  ? -26.865 17.870  102.621 1.00 34.25 ? 426  GLN   B NE2   1 
ATOM   12110 N  N     . THR   B  1  429  ? -23.255 18.350  105.420 1.00 26.69 ? 427  THR   B N     1 
ATOM   12111 C  CA    . THR   B  1  429  ? -22.471 17.159  105.117 1.00 28.09 ? 427  THR   B CA    1 
ATOM   12112 C  C     . THR   B  1  429  ? -22.618 16.118  106.217 1.00 24.57 ? 427  THR   B C     1 
ATOM   12113 O  O     . THR   B  1  429  ? -22.847 14.933  105.945 1.00 26.39 ? 427  THR   B O     1 
ATOM   12114 C  CB    . THR   B  1  429  ? -20.997 17.531  104.968 1.00 26.03 ? 427  THR   B CB    1 
ATOM   12115 O  OG1   . THR   B  1  429  ? -20.858 18.612  104.043 1.00 24.40 ? 427  THR   B OG1   1 
ATOM   12116 C  CG2   . THR   B  1  429  ? -20.217 16.341  104.471 1.00 26.33 ? 427  THR   B CG2   1 
ATOM   12117 N  N     . LEU   B  1  430  ? -22.468 16.547  107.473 1.00 28.50 ? 428  LEU   B N     1 
ATOM   12118 C  CA    . LEU   B  1  430  ? -22.603 15.635  108.603 1.00 25.84 ? 428  LEU   B CA    1 
ATOM   12119 C  C     . LEU   B  1  430  ? -23.967 14.958  108.596 1.00 28.22 ? 428  LEU   B C     1 
ATOM   12120 O  O     . LEU   B  1  430  ? -24.064 13.736  108.736 1.00 26.10 ? 428  LEU   B O     1 
ATOM   12121 C  CB    . LEU   B  1  430  ? -22.407 16.410  109.906 1.00 26.93 ? 428  LEU   B CB    1 
ATOM   12122 C  CG    . LEU   B  1  430  ? -22.327 15.699  111.267 1.00 28.03 ? 428  LEU   B CG    1 
ATOM   12123 C  CD1   . LEU   B  1  430  ? -21.860 16.713  112.275 1.00 30.73 ? 428  LEU   B CD1   1 
ATOM   12124 C  CD2   . LEU   B  1  430  ? -23.639 15.094  111.746 1.00 33.40 ? 428  LEU   B CD2   1 
ATOM   12125 N  N     . ALA   B  1  431  ? -25.032 15.748  108.449 1.00 31.54 ? 429  ALA   B N     1 
ATOM   12126 C  CA    . ALA   B  1  431  ? -26.379 15.192  108.503 1.00 32.69 ? 429  ALA   B CA    1 
ATOM   12127 C  C     . ALA   B  1  431  ? -26.603 14.193  107.377 1.00 29.94 ? 429  ALA   B C     1 
ATOM   12128 O  O     . ALA   B  1  431  ? -27.259 13.165  107.573 1.00 33.83 ? 429  ALA   B O     1 
ATOM   12129 C  CB    . ALA   B  1  431  ? -27.407 16.321  108.443 1.00 31.16 ? 429  ALA   B CB    1 
ATOM   12130 N  N     . ALA   B  1  432  ? -26.046 14.470  106.193 1.00 29.10 ? 430  ALA   B N     1 
ATOM   12131 C  CA    . ALA   B  1  432  ? -26.177 13.529  105.085 1.00 28.50 ? 430  ALA   B CA    1 
ATOM   12132 C  C     . ALA   B  1  432  ? -25.520 12.200  105.419 1.00 28.99 ? 430  ALA   B C     1 
ATOM   12133 O  O     . ALA   B  1  432  ? -26.084 11.135  105.151 1.00 30.21 ? 430  ALA   B O     1 
ATOM   12134 C  CB    . ALA   B  1  432  ? -25.567 14.120  103.812 1.00 29.79 ? 430  ALA   B CB    1 
ATOM   12135 N  N     . ILE   B  1  433  ? -24.317 12.241  105.995 1.00 28.10 ? 431  ILE   B N     1 
ATOM   12136 C  CA    . ILE   B  1  433  ? -23.613 11.006  106.326 1.00 32.35 ? 431  ILE   B CA    1 
ATOM   12137 C  C     . ILE   B  1  433  ? -24.281 10.298  107.491 1.00 29.35 ? 431  ILE   B C     1 
ATOM   12138 O  O     . ILE   B  1  433  ? -24.364 9.064   107.524 1.00 28.20 ? 431  ILE   B O     1 
ATOM   12139 C  CB    . ILE   B  1  433  ? -22.138 11.307  106.623 1.00 32.13 ? 431  ILE   B CB    1 
ATOM   12140 C  CG1   . ILE   B  1  433  ? -21.421 11.701  105.339 1.00 33.92 ? 431  ILE   B CG1   1 
ATOM   12141 C  CG2   . ILE   B  1  433  ? -21.466 10.109  107.297 1.00 31.76 ? 431  ILE   B CG2   1 
ATOM   12142 C  CD1   . ILE   B  1  433  ? -20.009 11.992  105.570 1.00 34.10 ? 431  ILE   B CD1   1 
ATOM   12143 N  N     . TYR   B  1  434  ? -24.731 11.061  108.486 1.00 30.35 ? 432  TYR   B N     1 
ATOM   12144 C  CA    . TYR   B  1  434  ? -25.398 10.468  109.638 1.00 30.10 ? 432  TYR   B CA    1 
ATOM   12145 C  C     . TYR   B  1  434  ? -26.574 9.598   109.205 1.00 32.51 ? 432  TYR   B C     1 
ATOM   12146 O  O     . TYR   B  1  434  ? -26.726 8.459   109.661 1.00 32.04 ? 432  TYR   B O     1 
ATOM   12147 C  CB    . TYR   B  1  434  ? -25.837 11.586  110.582 1.00 30.06 ? 432  TYR   B CB    1 
ATOM   12148 C  CG    . TYR   B  1  434  ? -26.746 11.155  111.704 1.00 32.15 ? 432  TYR   B CG    1 
ATOM   12149 C  CD1   . TYR   B  1  434  ? -26.272 10.376  112.754 1.00 30.97 ? 432  TYR   B CD1   1 
ATOM   12150 C  CD2   . TYR   B  1  434  ? -28.077 11.543  111.723 1.00 34.91 ? 432  TYR   B CD2   1 
ATOM   12151 C  CE1   . TYR   B  1  434  ? -27.104 9.997   113.793 1.00 36.38 ? 432  TYR   B CE1   1 
ATOM   12152 C  CE2   . TYR   B  1  434  ? -28.913 11.168  112.754 1.00 33.91 ? 432  TYR   B CE2   1 
ATOM   12153 C  CZ    . TYR   B  1  434  ? -28.422 10.394  113.783 1.00 37.34 ? 432  TYR   B CZ    1 
ATOM   12154 O  OH    . TYR   B  1  434  ? -29.253 10.016  114.810 1.00 40.95 ? 432  TYR   B OH    1 
ATOM   12155 N  N     . HIS   B  1  435  ? -27.383 10.097  108.276 1.00 34.77 ? 433  HIS   B N     1 
ATOM   12156 C  CA    . HIS   B  1  435  ? -28.533 9.323   107.830 1.00 34.79 ? 433  HIS   B CA    1 
ATOM   12157 C  C     . HIS   B  1  435  ? -28.143 8.255   106.818 1.00 33.96 ? 433  HIS   B C     1 
ATOM   12158 O  O     . HIS   B  1  435  ? -28.707 7.153   106.827 1.00 33.27 ? 433  HIS   B O     1 
ATOM   12159 C  CB    . HIS   B  1  435  ? -29.608 10.260  107.297 1.00 36.19 ? 433  HIS   B CB    1 
ATOM   12160 C  CG    . HIS   B  1  435  ? -30.315 11.005  108.379 1.00 37.79 ? 433  HIS   B CG    1 
ATOM   12161 N  ND1   . HIS   B  1  435  ? -31.309 10.431  109.141 1.00 35.15 ? 433  HIS   B ND1   1 
ATOM   12162 C  CD2   . HIS   B  1  435  ? -30.150 12.261  108.858 1.00 36.87 ? 433  HIS   B CD2   1 
ATOM   12163 C  CE1   . HIS   B  1  435  ? -31.739 11.307  110.031 1.00 40.33 ? 433  HIS   B CE1   1 
ATOM   12164 N  NE2   . HIS   B  1  435  ? -31.054 12.426  109.880 1.00 33.59 ? 433  HIS   B NE2   1 
ATOM   12165 N  N     . MET   B  1  436  ? -27.166 8.555   105.958 1.00 34.55 ? 434  MET   B N     1 
ATOM   12166 C  CA    . MET   B  1  436  ? -26.671 7.555   105.023 1.00 29.24 ? 434  MET   B CA    1 
ATOM   12167 C  C     . MET   B  1  436  ? -26.167 6.316   105.745 1.00 29.74 ? 434  MET   B C     1 
ATOM   12168 O  O     . MET   B  1  436  ? -26.279 5.202   105.223 1.00 32.60 ? 434  MET   B O     1 
ATOM   12169 C  CB    . MET   B  1  436  ? -25.546 8.161   104.189 1.00 33.06 ? 434  MET   B CB    1 
ATOM   12170 C  CG    . MET   B  1  436  ? -24.849 7.171   103.287 1.00 36.24 ? 434  MET   B CG    1 
ATOM   12171 S  SD    . MET   B  1  436  ? -23.465 7.943   102.434 1.00 38.60 ? 434  MET   B SD    1 
ATOM   12172 C  CE    . MET   B  1  436  ? -24.338 8.978   101.276 1.00 33.86 ? 434  MET   B CE    1 
ATOM   12173 N  N     . ALA   B  1  437  ? -25.602 6.486   106.942 1.00 30.03 ? 435  ALA   B N     1 
ATOM   12174 C  CA    . ALA   B  1  437  ? -25.056 5.359   107.685 1.00 31.09 ? 435  ALA   B CA    1 
ATOM   12175 C  C     . ALA   B  1  437  ? -26.135 4.475   108.294 1.00 33.23 ? 435  ALA   B C     1 
ATOM   12176 O  O     . ALA   B  1  437  ? -25.826 3.363   108.737 1.00 35.68 ? 435  ALA   B O     1 
ATOM   12177 C  CB    . ALA   B  1  437  ? -24.113 5.864   108.779 1.00 35.57 ? 435  ALA   B CB    1 
ATOM   12178 N  N     . GLY   B  1  438  ? -27.378 4.929   108.325 1.00 37.63 ? 436  GLY   B N     1 
ATOM   12179 C  CA    . GLY   B  1  438  ? -28.451 4.107   108.837 1.00 39.47 ? 436  GLY   B CA    1 
ATOM   12180 C  C     . GLY   B  1  438  ? -28.528 4.129   110.351 1.00 42.89 ? 436  GLY   B C     1 
ATOM   12181 O  O     . GLY   B  1  438  ? -27.807 4.855   111.046 1.00 37.46 ? 436  GLY   B O     1 
ATOM   12182 N  N     . LYS   B  1  439  ? -29.431 3.290   110.867 1.00 41.69 ? 437  LYS   B N     1 
ATOM   12183 C  CA    . LYS   B  1  439  ? -29.762 3.293   112.288 1.00 39.13 ? 437  LYS   B CA    1 
ATOM   12184 C  C     . LYS   B  1  439  ? -28.796 2.483   113.143 1.00 40.52 ? 437  LYS   B C     1 
ATOM   12185 O  O     . LYS   B  1  439  ? -28.694 2.746   114.346 1.00 44.25 ? 437  LYS   B O     1 
ATOM   12186 C  CB    . LYS   B  1  439  ? -31.184 2.758   112.493 1.00 37.53 ? 437  LYS   B CB    1 
ATOM   12187 N  N     . ASP   B  1  440  ? -28.100 1.502   112.568 1.00 39.34 ? 438  ASP   B N     1 
ATOM   12188 C  CA    . ASP   B  1  440  ? -27.271 0.587   113.349 1.00 41.72 ? 438  ASP   B CA    1 
ATOM   12189 C  C     . ASP   B  1  440  ? -25.901 1.221   113.550 1.00 38.62 ? 438  ASP   B C     1 
ATOM   12190 O  O     . ASP   B  1  440  ? -25.155 1.420   112.586 1.00 39.73 ? 438  ASP   B O     1 
ATOM   12191 C  CB    . ASP   B  1  440  ? -27.144 -0.760  112.644 1.00 43.60 ? 438  ASP   B CB    1 
ATOM   12192 N  N     . PHE   B  1  441  ? -25.564 1.527   114.800 1.00 36.85 ? 439  PHE   B N     1 
ATOM   12193 C  CA    . PHE   B  1  441  ? -24.282 2.146   115.095 1.00 33.97 ? 439  PHE   B CA    1 
ATOM   12194 C  C     . PHE   B  1  441  ? -23.666 1.549   116.350 1.00 36.99 ? 439  PHE   B C     1 
ATOM   12195 O  O     . PHE   B  1  441  ? -24.359 1.218   117.316 1.00 37.38 ? 439  PHE   B O     1 
ATOM   12196 C  CB    . PHE   B  1  441  ? -24.372 3.665   115.272 1.00 33.66 ? 439  PHE   B CB    1 
ATOM   12197 C  CG    . PHE   B  1  441  ? -23.034 4.301   115.500 1.00 34.39 ? 439  PHE   B CG    1 
ATOM   12198 C  CD1   . PHE   B  1  441  ? -22.226 4.614   114.426 1.00 29.60 ? 439  PHE   B CD1   1 
ATOM   12199 C  CD2   . PHE   B  1  441  ? -22.563 4.534   116.786 1.00 31.44 ? 439  PHE   B CD2   1 
ATOM   12200 C  CE1   . PHE   B  1  441  ? -20.975 5.174   114.622 1.00 30.35 ? 439  PHE   B CE1   1 
ATOM   12201 C  CE2   . PHE   B  1  441  ? -21.316 5.087   116.989 1.00 32.29 ? 439  PHE   B CE2   1 
ATOM   12202 C  CZ    . PHE   B  1  441  ? -20.522 5.402   115.901 1.00 30.93 ? 439  PHE   B CZ    1 
ATOM   12203 N  N     . HIS   B  1  442  ? -22.340 1.439   116.330 1.00 33.78 ? 440  HIS   B N     1 
ATOM   12204 C  CA    . HIS   B  1  442  ? -21.572 1.098   117.513 1.00 33.92 ? 440  HIS   B CA    1 
ATOM   12205 C  C     . HIS   B  1  442  ? -20.231 1.801   117.401 1.00 33.51 ? 440  HIS   B C     1 
ATOM   12206 O  O     . HIS   B  1  442  ? -19.742 2.051   116.295 1.00 31.48 ? 440  HIS   B O     1 
ATOM   12207 C  CB    . HIS   B  1  442  ? -21.356 -0.412  117.604 1.00 34.23 ? 440  HIS   B CB    1 
ATOM   12208 C  CG    . HIS   B  1  442  ? -20.730 -0.999  116.380 1.00 39.89 ? 440  HIS   B CG    1 
ATOM   12209 N  ND1   . HIS   B  1  442  ? -19.364 -1.039  116.189 1.00 42.19 ? 440  HIS   B ND1   1 
ATOM   12210 C  CD2   . HIS   B  1  442  ? -21.282 -1.551  115.273 1.00 39.22 ? 440  HIS   B CD2   1 
ATOM   12211 C  CE1   . HIS   B  1  442  ? -19.102 -1.604  115.024 1.00 38.40 ? 440  HIS   B CE1   1 
ATOM   12212 N  NE2   . HIS   B  1  442  ? -20.248 -1.923  114.448 1.00 40.63 ? 440  HIS   B NE2   1 
ATOM   12213 N  N     . VAL   B  1  443  ? -19.643 2.135   118.553 1.00 33.46 ? 441  VAL   B N     1 
ATOM   12214 C  CA    . VAL   B  1  443  ? -18.310 2.724   118.540 1.00 31.87 ? 441  VAL   B CA    1 
ATOM   12215 C  C     . VAL   B  1  443  ? -17.355 1.759   117.856 1.00 31.37 ? 441  VAL   B C     1 
ATOM   12216 O  O     . VAL   B  1  443  ? -17.367 0.552   118.120 1.00 32.15 ? 441  VAL   B O     1 
ATOM   12217 C  CB    . VAL   B  1  443  ? -17.858 3.080   119.962 1.00 34.74 ? 441  VAL   B CB    1 
ATOM   12218 C  CG1   . VAL   B  1  443  ? -16.379 3.440   119.971 1.00 31.66 ? 441  VAL   B CG1   1 
ATOM   12219 C  CG2   . VAL   B  1  443  ? -18.683 4.242   120.495 1.00 35.48 ? 441  VAL   B CG2   1 
ATOM   12220 N  N     . GLY   B  1  444  ? -16.552 2.282   116.937 1.00 30.50 ? 442  GLY   B N     1 
ATOM   12221 C  CA    . GLY   B  1  444  ? -15.702 1.461   116.104 1.00 28.17 ? 442  GLY   B CA    1 
ATOM   12222 C  C     . GLY   B  1  444  ? -16.244 1.223   114.709 1.00 28.10 ? 442  GLY   B C     1 
ATOM   12223 O  O     . GLY   B  1  444  ? -15.505 0.719   113.854 1.00 27.51 ? 442  GLY   B O     1 
ATOM   12224 N  N     . LYS   B  1  445  ? -17.514 1.545   114.462 1.00 27.93 ? 443  LYS   B N     1 
ATOM   12225 C  CA    . LYS   B  1  445  ? -18.051 1.438   113.110 1.00 25.90 ? 443  LYS   B CA    1 
ATOM   12226 C  C     . LYS   B  1  445  ? -17.510 2.562   112.239 1.00 27.92 ? 443  LYS   B C     1 
ATOM   12227 O  O     . LYS   B  1  445  ? -16.916 2.323   111.181 1.00 27.37 ? 443  LYS   B O     1 
ATOM   12228 C  CB    . LYS   B  1  445  ? -19.584 1.458   113.140 1.00 29.07 ? 443  LYS   B CB    1 
ATOM   12229 C  CG    . LYS   B  1  445  ? -20.215 1.177   111.782 1.00 33.46 ? 443  LYS   B CG    1 
ATOM   12230 C  CD    . LYS   B  1  445  ? -21.732 1.123   111.842 1.00 37.68 ? 443  LYS   B CD    1 
ATOM   12231 C  CE    . LYS   B  1  445  ? -22.316 0.688   110.505 1.00 39.10 ? 443  LYS   B CE    1 
ATOM   12232 N  NZ    . LYS   B  1  445  ? -23.747 0.276   110.652 1.00 40.67 ? 443  LYS   B NZ    1 
ATOM   12233 N  N     . TYR   B  1  446  ? -17.721 3.798   112.672 1.00 25.15 ? 444  TYR   B N     1 
ATOM   12234 C  CA    . TYR   B  1  446  ? -17.145 4.984   112.057 1.00 24.33 ? 444  TYR   B CA    1 
ATOM   12235 C  C     . TYR   B  1  446  ? -17.192 6.072   113.115 1.00 24.84 ? 444  TYR   B C     1 
ATOM   12236 O  O     . TYR   B  1  446  ? -17.821 5.911   114.163 1.00 25.70 ? 444  TYR   B O     1 
ATOM   12237 C  CB    . TYR   B  1  446  ? -17.913 5.402   110.794 1.00 25.57 ? 444  TYR   B CB    1 
ATOM   12238 C  CG    . TYR   B  1  446  ? -19.333 5.870   111.046 1.00 29.20 ? 444  TYR   B CG    1 
ATOM   12239 C  CD1   . TYR   B  1  446  ? -19.613 7.205   111.318 1.00 26.57 ? 444  TYR   B CD1   1 
ATOM   12240 C  CD2   . TYR   B  1  446  ? -20.397 4.978   110.981 1.00 27.62 ? 444  TYR   B CD2   1 
ATOM   12241 C  CE1   . TYR   B  1  446  ? -20.916 7.631   111.552 1.00 33.37 ? 444  TYR   B CE1   1 
ATOM   12242 C  CE2   . TYR   B  1  446  ? -21.693 5.391   111.210 1.00 33.85 ? 444  TYR   B CE2   1 
ATOM   12243 C  CZ    . TYR   B  1  446  ? -21.949 6.718   111.492 1.00 32.59 ? 444  TYR   B CZ    1 
ATOM   12244 O  OH    . TYR   B  1  446  ? -23.251 7.115   111.712 1.00 40.62 ? 444  TYR   B OH    1 
ATOM   12245 N  N     . GLU   B  1  447  ? -16.538 7.188   112.829 1.00 24.26 ? 445  GLU   B N     1 
ATOM   12246 C  CA    . GLU   B  1  447  ? -16.649 8.341   113.699 1.00 23.45 ? 445  GLU   B CA    1 
ATOM   12247 C  C     . GLU   B  1  447  ? -16.666 9.586   112.843 1.00 21.46 ? 445  GLU   B C     1 
ATOM   12248 O  O     . GLU   B  1  447  ? -16.376 9.550   111.643 1.00 21.39 ? 445  GLU   B O     1 
ATOM   12249 C  CB    . GLU   B  1  447  ? -15.487 8.404   114.691 1.00 21.34 ? 445  GLU   B CB    1 
ATOM   12250 C  CG    . GLU   B  1  447  ? -14.171 8.692   113.990 1.00 21.80 ? 445  GLU   B CG    1 
ATOM   12251 C  CD    . GLU   B  1  447  ? -12.993 8.608   114.929 1.00 21.02 ? 445  GLU   B CD    1 
ATOM   12252 O  OE1   . GLU   B  1  447  ? -13.176 8.152   116.081 1.00 23.97 ? 445  GLU   B OE1   1 
ATOM   12253 O  OE2   . GLU   B  1  447  ? -11.890 9.004   114.504 1.00 21.68 ? 445  GLU   B OE2   1 
ATOM   12254 N  N     . PHE   B  1  448  ? -17.027 10.692  113.466 1.00 21.33 ? 446  PHE   B N     1 
ATOM   12255 C  CA    . PHE   B  1  448  ? -16.795 12.004  112.895 1.00 22.59 ? 446  PHE   B CA    1 
ATOM   12256 C  C     . PHE   B  1  448  ? -15.507 12.573  113.473 1.00 19.95 ? 446  PHE   B C     1 
ATOM   12257 O  O     . PHE   B  1  448  ? -14.951 12.054  114.443 1.00 21.51 ? 446  PHE   B O     1 
ATOM   12258 C  CB    . PHE   B  1  448  ? -17.971 12.925  113.197 1.00 25.11 ? 446  PHE   B CB    1 
ATOM   12259 C  CG    . PHE   B  1  448  ? -19.242 12.481  112.556 1.00 25.23 ? 446  PHE   B CG    1 
ATOM   12260 C  CD1   . PHE   B  1  448  ? -19.501 12.795  111.230 1.00 27.48 ? 446  PHE   B CD1   1 
ATOM   12261 C  CD2   . PHE   B  1  448  ? -20.166 11.725  113.262 1.00 27.73 ? 446  PHE   B CD2   1 
ATOM   12262 C  CE1   . PHE   B  1  448  ? -20.672 12.375  110.622 1.00 26.27 ? 446  PHE   B CE1   1 
ATOM   12263 C  CE2   . PHE   B  1  448  ? -21.332 11.301  112.660 1.00 30.12 ? 446  PHE   B CE2   1 
ATOM   12264 C  CZ    . PHE   B  1  448  ? -21.588 11.631  111.340 1.00 27.96 ? 446  PHE   B CZ    1 
ATOM   12265 N  N     . GLN   B  1  449  ? -15.023 13.638  112.846 1.00 21.75 ? 447  GLN   B N     1 
ATOM   12266 C  CA    . GLN   B  1  449  ? -13.841 14.338  113.320 1.00 20.78 ? 447  GLN   B CA    1 
ATOM   12267 C  C     . GLN   B  1  449  ? -14.051 15.827  113.117 1.00 21.64 ? 447  GLN   B C     1 
ATOM   12268 O  O     . GLN   B  1  449  ? -14.782 16.255  112.217 1.00 20.10 ? 447  GLN   B O     1 
ATOM   12269 C  CB    . GLN   B  1  449  ? -12.558 13.889  112.602 1.00 20.87 ? 447  GLN   B CB    1 
ATOM   12270 C  CG    . GLN   B  1  449  ? -12.274 12.411  112.732 1.00 21.44 ? 447  GLN   B CG    1 
ATOM   12271 C  CD    . GLN   B  1  449  ? -10.806 12.116  112.591 1.00 20.20 ? 447  GLN   B CD    1 
ATOM   12272 O  OE1   . GLN   B  1  449  ? -10.051 12.964  112.126 1.00 22.60 ? 447  GLN   B OE1   1 
ATOM   12273 N  NE2   . GLN   B  1  449  ? -10.391 10.922  112.994 1.00 20.88 ? 447  GLN   B NE2   1 
ATOM   12274 N  N     . CYS   B  1  450  ? -13.428 16.613  113.985 1.00 20.34 ? 448  CYS   B N     1 
ATOM   12275 C  CA    . CYS   B  1  450  ? -13.483 18.058  113.860 1.00 20.35 ? 448  CYS   B CA    1 
ATOM   12276 C  C     . CYS   B  1  450  ? -12.171 18.629  114.366 1.00 18.93 ? 448  CYS   B C     1 
ATOM   12277 O  O     . CYS   B  1  450  ? -11.339 17.921  114.935 1.00 21.62 ? 448  CYS   B O     1 
ATOM   12278 C  CB    . CYS   B  1  450  ? -14.655 18.647  114.649 1.00 22.51 ? 448  CYS   B CB    1 
ATOM   12279 S  SG    . CYS   B  1  450  ? -14.442 18.583  116.438 1.00 24.20 ? 448  CYS   B SG    1 
ATOM   12280 N  N     . LEU   B  1  451  ? -12.009 19.927  114.165 1.00 21.62 ? 449  LEU   B N     1 
ATOM   12281 C  CA    . LEU   B  1  451  ? -10.826 20.636  114.629 1.00 20.89 ? 449  LEU   B CA    1 
ATOM   12282 C  C     . LEU   B  1  451  ? -11.095 21.237  116.002 1.00 23.82 ? 449  LEU   B C     1 
ATOM   12283 O  O     . LEU   B  1  451  ? -12.179 21.763  116.268 1.00 24.87 ? 449  LEU   B O     1 
ATOM   12284 C  CB    . LEU   B  1  451  ? -10.494 21.751  113.640 1.00 23.26 ? 449  LEU   B CB    1 
ATOM   12285 C  CG    . LEU   B  1  451  ? -9.191  22.525  113.771 1.00 30.07 ? 449  LEU   B CG    1 
ATOM   12286 C  CD1   . LEU   B  1  451  ? -8.003  21.578  113.869 1.00 27.10 ? 449  LEU   B CD1   1 
ATOM   12287 C  CD2   . LEU   B  1  451  ? -9.043  23.460  112.578 1.00 33.20 ? 449  LEU   B CD2   1 
ATOM   12288 N  N     . HIS   B  1  452  ? -10.103 21.132  116.884 1.00 21.06 ? 450  HIS   B N     1 
ATOM   12289 C  CA    . HIS   B  1  452  ? -10.192 21.771  118.186 1.00 26.77 ? 450  HIS   B CA    1 
ATOM   12290 C  C     . HIS   B  1  452  ? -10.499 23.250  118.024 1.00 25.58 ? 450  HIS   B C     1 
ATOM   12291 O  O     . HIS   B  1  452  ? -9.948  23.918  117.147 1.00 27.46 ? 450  HIS   B O     1 
ATOM   12292 C  CB    . HIS   B  1  452  ? -8.854  21.631  118.916 1.00 22.32 ? 450  HIS   B CB    1 
ATOM   12293 C  CG    . HIS   B  1  452  ? -8.765  22.471  120.149 1.00 24.61 ? 450  HIS   B CG    1 
ATOM   12294 N  ND1   . HIS   B  1  452  ? -9.335  22.094  121.347 1.00 26.41 ? 450  HIS   B ND1   1 
ATOM   12295 C  CD2   . HIS   B  1  452  ? -8.194  23.678  120.368 1.00 27.75 ? 450  HIS   B CD2   1 
ATOM   12296 C  CE1   . HIS   B  1  452  ? -9.109  23.028  122.254 1.00 29.24 ? 450  HIS   B CE1   1 
ATOM   12297 N  NE2   . HIS   B  1  452  ? -8.423  24.002  121.685 1.00 28.76 ? 450  HIS   B NE2   1 
ATOM   12298 N  N     . GLY   B  1  453  ? -11.382 23.758  118.886 1.00 29.86 ? 451  GLY   B N     1 
ATOM   12299 C  CA    . GLY   B  1  453  ? -11.682 25.176  118.918 1.00 35.14 ? 451  GLY   B CA    1 
ATOM   12300 C  C     . GLY   B  1  453  ? -12.393 25.706  117.698 1.00 40.42 ? 451  GLY   B C     1 
ATOM   12301 O  O     . GLY   B  1  453  ? -12.435 26.924  117.498 1.00 45.18 ? 451  GLY   B O     1 
ATOM   12302 N  N     . MET   B  1  454  ? -12.923 24.823  116.858 1.00 29.45 ? 452  MET   B N     1 
ATOM   12303 C  CA    . MET   B  1  454  ? -13.732 25.216  115.716 1.00 29.03 ? 452  MET   B CA    1 
ATOM   12304 C  C     . MET   B  1  454  ? -14.938 24.291  115.659 1.00 32.26 ? 452  MET   B C     1 
ATOM   12305 O  O     . MET   B  1  454  ? -16.073 24.743  115.477 1.00 32.17 ? 452  MET   B O     1 
ATOM   12306 C  CB    . MET   B  1  454  ? -12.918 25.108  114.423 1.00 30.61 ? 452  MET   B CB    1 
ATOM   12307 C  CG    . MET   B  1  454  ? -13.750 25.303  113.166 1.00 31.93 ? 452  MET   B CG    1 
ATOM   12308 S  SD    . MET   B  1  454  ? -14.619 26.881  113.199 1.00 44.88 ? 452  MET   B SD    1 
ATOM   12309 C  CE    . MET   B  1  454  ? -13.228 28.012  113.178 1.00 39.67 ? 452  MET   B CE    1 
ATOM   12310 N  N     . GLY   B  1  455  ? -14.703 22.996  115.851 1.00 24.96 ? 453  GLY   B N     1 
ATOM   12311 C  CA    . GLY   B  1  455  ? -15.732 21.997  115.660 1.00 26.08 ? 453  GLY   B CA    1 
ATOM   12312 C  C     . GLY   B  1  455  ? -16.600 21.684  116.856 1.00 31.43 ? 453  GLY   B C     1 
ATOM   12313 O  O     . GLY   B  1  455  ? -17.634 21.038  116.688 1.00 29.68 ? 453  GLY   B O     1 
ATOM   12314 N  N     . GLU   B  1  456  ? -16.209 22.095  118.061 1.00 32.72 ? 454  GLU   B N     1 
ATOM   12315 C  CA    . GLU   B  1  456  ? -16.999 21.731  119.235 1.00 34.29 ? 454  GLU   B CA    1 
ATOM   12316 C  C     . GLU   B  1  456  ? -18.437 22.234  119.203 1.00 33.75 ? 454  GLU   B C     1 
ATOM   12317 O  O     . GLU   B  1  456  ? -19.330 21.465  119.595 1.00 35.79 ? 454  GLU   B O     1 
ATOM   12318 C  CB    . GLU   B  1  456  ? -16.290 22.124  120.535 1.00 36.63 ? 454  GLU   B CB    1 
ATOM   12319 C  CG    . GLU   B  1  456  ? -15.021 21.347  120.805 1.00 40.10 ? 454  GLU   B CG    1 
ATOM   12320 C  CD    . GLU   B  1  456  ? -13.812 22.007  120.187 1.00 38.79 ? 454  GLU   B CD    1 
ATOM   12321 O  OE1   . GLU   B  1  456  ? -13.950 22.593  119.088 1.00 37.75 ? 454  GLU   B OE1   1 
ATOM   12322 O  OE2   . GLU   B  1  456  ? -12.728 21.954  120.808 1.00 35.91 ? 454  GLU   B OE2   1 
ATOM   12323 N  N     . PRO   B  1  457  ? -18.735 23.472  118.784 1.00 33.37 ? 455  PRO   B N     1 
ATOM   12324 C  CA    . PRO   B  1  457  ? -20.144 23.898  118.753 1.00 34.60 ? 455  PRO   B CA    1 
ATOM   12325 C  C     . PRO   B  1  457  ? -21.033 22.983  117.935 1.00 34.34 ? 455  PRO   B C     1 
ATOM   12326 O  O     . PRO   B  1  457  ? -22.171 22.701  118.337 1.00 34.21 ? 455  PRO   B O     1 
ATOM   12327 C  CB    . PRO   B  1  457  ? -20.064 25.306  118.155 1.00 34.87 ? 455  PRO   B CB    1 
ATOM   12328 C  CG    . PRO   B  1  457  ? -18.724 25.791  118.562 1.00 39.05 ? 455  PRO   B CG    1 
ATOM   12329 C  CD    . PRO   B  1  457  ? -17.830 24.592  118.467 1.00 36.23 ? 455  PRO   B CD    1 
ATOM   12330 N  N     . LEU   B  1  458  ? -20.551 22.514  116.786 1.00 33.28 ? 456  LEU   B N     1 
ATOM   12331 C  CA    . LEU   B  1  458  ? -21.338 21.568  116.007 1.00 30.76 ? 456  LEU   B CA    1 
ATOM   12332 C  C     . LEU   B  1  458  ? -21.410 20.222  116.709 1.00 29.68 ? 456  LEU   B C     1 
ATOM   12333 O  O     . LEU   B  1  458  ? -22.493 19.653  116.885 1.00 30.12 ? 456  LEU   B O     1 
ATOM   12334 C  CB    . LEU   B  1  458  ? -20.738 21.414  114.612 1.00 29.62 ? 456  LEU   B CB    1 
ATOM   12335 C  CG    . LEU   B  1  458  ? -21.412 20.361  113.737 1.00 28.07 ? 456  LEU   B CG    1 
ATOM   12336 C  CD1   . LEU   B  1  458  ? -22.900 20.661  113.602 1.00 29.97 ? 456  LEU   B CD1   1 
ATOM   12337 C  CD2   . LEU   B  1  458  ? -20.757 20.316  112.363 1.00 29.75 ? 456  LEU   B CD2   1 
ATOM   12338 N  N     . TYR   B  1  459  ? -20.268 19.712  117.152 1.00 28.68 ? 457  TYR   B N     1 
ATOM   12339 C  CA    . TYR   B  1  459  ? -20.239 18.347  117.647 1.00 27.43 ? 457  TYR   B CA    1 
ATOM   12340 C  C     . TYR   B  1  459  ? -20.735 18.201  119.076 1.00 28.20 ? 457  TYR   B C     1 
ATOM   12341 O  O     . TYR   B  1  459  ? -21.011 17.077  119.495 1.00 26.14 ? 457  TYR   B O     1 
ATOM   12342 C  CB    . TYR   B  1  459  ? -18.866 17.721  117.420 1.00 27.91 ? 457  TYR   B CB    1 
ATOM   12343 C  CG    . TYR   B  1  459  ? -18.709 17.351  115.971 1.00 25.87 ? 457  TYR   B CG    1 
ATOM   12344 C  CD1   . TYR   B  1  459  ? -19.274 16.184  115.477 1.00 24.42 ? 457  TYR   B CD1   1 
ATOM   12345 C  CD2   . TYR   B  1  459  ? -18.040 18.187  115.083 1.00 25.65 ? 457  TYR   B CD2   1 
ATOM   12346 C  CE1   . TYR   B  1  459  ? -19.158 15.843  114.148 1.00 25.50 ? 457  TYR   B CE1   1 
ATOM   12347 C  CE2   . TYR   B  1  459  ? -17.919 17.847  113.735 1.00 29.65 ? 457  TYR   B CE2   1 
ATOM   12348 C  CZ    . TYR   B  1  459  ? -18.481 16.671  113.282 1.00 24.52 ? 457  TYR   B CZ    1 
ATOM   12349 O  OH    . TYR   B  1  459  ? -18.373 16.301  111.951 1.00 23.87 ? 457  TYR   B OH    1 
ATOM   12350 N  N     . GLU   B  1  460  ? -20.867 19.292  119.827 1.00 28.39 ? 458  GLU   B N     1 
ATOM   12351 C  CA    . GLU   B  1  460  ? -21.598 19.174  121.082 1.00 33.13 ? 458  GLU   B CA    1 
ATOM   12352 C  C     . GLU   B  1  460  ? -23.077 18.914  120.837 1.00 38.71 ? 458  GLU   B C     1 
ATOM   12353 O  O     . GLU   B  1  460  ? -23.784 18.488  121.759 1.00 33.85 ? 458  GLU   B O     1 
ATOM   12354 C  CB    . GLU   B  1  460  ? -21.361 20.386  121.989 1.00 33.97 ? 458  GLU   B CB    1 
ATOM   12355 C  CG    . GLU   B  1  460  ? -21.891 21.703  121.455 1.00 39.71 ? 458  GLU   B CG    1 
ATOM   12356 C  CD    . GLU   B  1  460  ? -21.498 22.885  122.332 1.00 50.30 ? 458  GLU   B CD    1 
ATOM   12357 O  OE1   . GLU   B  1  460  ? -20.754 22.672  123.315 1.00 48.76 ? 458  GLU   B OE1   1 
ATOM   12358 O  OE2   . GLU   B  1  460  ? -21.928 24.025  122.040 1.00 47.00 ? 458  GLU   B OE2   1 
ATOM   12359 N  N     . GLU   B  1  461  ? -23.549 19.138  119.611 1.00 33.70 ? 459  GLU   B N     1 
ATOM   12360 C  CA    . GLU   B  1  461  ? -24.894 18.759  119.189 1.00 35.19 ? 459  GLU   B CA    1 
ATOM   12361 C  C     . GLU   B  1  461  ? -24.950 17.363  118.584 1.00 36.44 ? 459  GLU   B C     1 
ATOM   12362 O  O     . GLU   B  1  461  ? -25.997 16.968  118.056 1.00 33.68 ? 459  GLU   B O     1 
ATOM   12363 C  CB    . GLU   B  1  461  ? -25.441 19.773  118.185 1.00 32.70 ? 459  GLU   B CB    1 
ATOM   12364 C  CG    . GLU   B  1  461  ? -25.295 21.231  118.590 1.00 32.84 ? 459  GLU   B CG    1 
ATOM   12365 C  CD    . GLU   B  1  461  ? -26.076 21.563  119.848 1.00 44.92 ? 459  GLU   B CD    1 
ATOM   12366 O  OE1   . GLU   B  1  461  ? -26.943 20.754  120.238 1.00 43.05 ? 459  GLU   B OE1   1 
ATOM   12367 O  OE2   . GLU   B  1  461  ? -25.820 22.633  120.443 1.00 45.51 ? 459  GLU   B OE2   1 
ATOM   12368 N  N     . VAL   B  1  462  ? -23.845 16.614  118.634 1.00 32.87 ? 460  VAL   B N     1 
ATOM   12369 C  CA    . VAL   B  1  462  ? -23.728 15.317  117.978 1.00 28.85 ? 460  VAL   B CA    1 
ATOM   12370 C  C     . VAL   B  1  462  ? -23.337 14.224  118.964 1.00 32.22 ? 460  VAL   B C     1 
ATOM   12371 O  O     . VAL   B  1  462  ? -23.985 13.174  119.037 1.00 31.90 ? 460  VAL   B O     1 
ATOM   12372 C  CB    . VAL   B  1  462  ? -22.734 15.373  116.787 1.00 31.56 ? 460  VAL   B CB    1 
ATOM   12373 C  CG1   . VAL   B  1  462  ? -22.493 13.986  116.209 1.00 28.60 ? 460  VAL   B CG1   1 
ATOM   12374 C  CG2   . VAL   B  1  462  ? -23.231 16.324  115.719 1.00 28.41 ? 460  VAL   B CG2   1 
ATOM   12375 N  N     . VAL   B  1  463  ? -22.271 14.452  119.733 1.00 26.88 ? 461  VAL   B N     1 
ATOM   12376 C  CA    . VAL   B  1  463  ? -21.781 13.448  120.666 1.00 27.44 ? 461  VAL   B CA    1 
ATOM   12377 C  C     . VAL   B  1  463  ? -22.723 13.342  121.855 1.00 29.37 ? 461  VAL   B C     1 
ATOM   12378 O  O     . VAL   B  1  463  ? -23.225 14.353  122.367 1.00 34.58 ? 461  VAL   B O     1 
ATOM   12379 C  CB    . VAL   B  1  463  ? -20.359 13.815  121.123 1.00 29.12 ? 461  VAL   B CB    1 
ATOM   12380 C  CG1   . VAL   B  1  463  ? -19.823 12.771  122.109 1.00 29.93 ? 461  VAL   B CG1   1 
ATOM   12381 C  CG2   . VAL   B  1  463  ? -19.444 13.956  119.909 1.00 26.73 ? 461  VAL   B CG2   1 
ATOM   12382 N  N     . GLY   B  1  464  ? -22.961 12.124  122.301 1.00 31.07 ? 462  GLY   B N     1 
ATOM   12383 C  CA    . GLY   B  1  464  ? -23.727 11.936  123.518 1.00 34.29 ? 462  GLY   B CA    1 
ATOM   12384 C  C     . GLY   B  1  464  ? -25.064 11.260  123.260 1.00 37.64 ? 462  GLY   B C     1 
ATOM   12385 O  O     . GLY   B  1  464  ? -25.693 11.437  122.209 1.00 36.38 ? 462  GLY   B O     1 
ATOM   12386 N  N     . ARG   B  1  465  ? -25.515 10.482  124.251 1.00 40.42 ? 463  ARG   B N     1 
ATOM   12387 C  CA    . ARG   B  1  465  ? -26.775 9.757   124.122 1.00 44.41 ? 463  ARG   B CA    1 
ATOM   12388 C  C     . ARG   B  1  465  ? -27.954 10.699  123.909 1.00 47.88 ? 463  ARG   B C     1 
ATOM   12389 O  O     . ARG   B  1  465  ? -28.932 10.331  123.245 1.00 47.39 ? 463  ARG   B O     1 
ATOM   12390 C  CB    . ARG   B  1  465  ? -27.005 8.882   125.356 1.00 48.43 ? 463  ARG   B CB    1 
ATOM   12391 N  N     . GLY   B  1  466  ? -27.878 11.912  124.445 1.00 43.12 ? 464  GLY   B N     1 
ATOM   12392 C  CA    . GLY   B  1  466  ? -28.923 12.898  124.269 1.00 44.70 ? 464  GLY   B CA    1 
ATOM   12393 C  C     . GLY   B  1  466  ? -28.857 13.707  122.999 1.00 46.17 ? 464  GLY   B C     1 
ATOM   12394 O  O     . GLY   B  1  466  ? -29.668 14.619  122.809 1.00 44.02 ? 464  GLY   B O     1 
ATOM   12395 N  N     . LYS   B  1  467  ? -27.898 13.405  122.116 1.00 42.02 ? 465  LYS   B N     1 
ATOM   12396 C  CA    . LYS   B  1  467  ? -27.744 14.121  120.855 1.00 38.84 ? 465  LYS   B CA    1 
ATOM   12397 C  C     . LYS   B  1  467  ? -27.914 13.106  119.730 1.00 39.69 ? 465  LYS   B C     1 
ATOM   12398 O  O     . LYS   B  1  467  ? -28.947 12.447  119.666 1.00 37.93 ? 465  LYS   B O     1 
ATOM   12399 C  CB    . LYS   B  1  467  ? -26.457 14.934  120.833 1.00 36.85 ? 465  LYS   B CB    1 
ATOM   12400 C  CG    . LYS   B  1  467  ? -26.383 16.010  121.908 1.00 39.28 ? 465  LYS   B CG    1 
ATOM   12401 C  CD    . LYS   B  1  467  ? -27.305 17.175  121.588 1.00 41.95 ? 465  LYS   B CD    1 
ATOM   12402 C  CE    . LYS   B  1  467  ? -27.277 18.227  122.689 1.00 41.62 ? 465  LYS   B CE    1 
ATOM   12403 N  NZ    . LYS   B  1  467  ? -27.935 19.492  122.249 1.00 44.77 ? 465  LYS   B NZ    1 
ATOM   12404 N  N     . LEU   B  1  468  ? -26.928 12.961  118.845 1.00 34.74 ? 466  LEU   B N     1 
ATOM   12405 C  CA    . LEU   B  1  468  ? -26.989 11.931  117.818 1.00 32.46 ? 466  LEU   B CA    1 
ATOM   12406 C  C     . LEU   B  1  468  ? -26.296 10.645  118.237 1.00 31.83 ? 466  LEU   B C     1 
ATOM   12407 O  O     . LEU   B  1  468  ? -26.353 9.657   117.497 1.00 30.28 ? 466  LEU   B O     1 
ATOM   12408 C  CB    . LEU   B  1  468  ? -26.406 12.446  116.495 1.00 34.73 ? 466  LEU   B CB    1 
ATOM   12409 C  CG    . LEU   B  1  468  ? -27.038 13.742  115.981 1.00 36.48 ? 466  LEU   B CG    1 
ATOM   12410 C  CD1   . LEU   B  1  468  ? -26.422 14.175  114.667 1.00 37.18 ? 466  LEU   B CD1   1 
ATOM   12411 C  CD2   . LEU   B  1  468  ? -28.554 13.575  115.848 1.00 38.31 ? 466  LEU   B CD2   1 
ATOM   12412 N  N     . ASP   B  1  469  ? -25.663 10.634  119.411 1.00 30.93 ? 467  ASP   B N     1 
ATOM   12413 C  CA    . ASP   B  1  469  ? -24.949 9.467   119.918 1.00 36.81 ? 467  ASP   B CA    1 
ATOM   12414 C  C     . ASP   B  1  469  ? -23.922 8.971   118.907 1.00 30.18 ? 467  ASP   B C     1 
ATOM   12415 O  O     . ASP   B  1  469  ? -23.811 7.778   118.622 1.00 33.34 ? 467  ASP   B O     1 
ATOM   12416 C  CB    . ASP   B  1  469  ? -25.904 8.353   120.351 1.00 37.26 ? 467  ASP   B CB    1 
ATOM   12417 C  CG    . ASP   B  1  469  ? -25.300 7.452   121.404 1.00 43.32 ? 467  ASP   B CG    1 
ATOM   12418 O  OD1   . ASP   B  1  469  ? -24.283 7.850   122.012 1.00 41.69 ? 467  ASP   B OD1   1 
ATOM   12419 O  OD2   . ASP   B  1  469  ? -25.840 6.346   121.629 1.00 49.57 ? 467  ASP   B OD2   1 
ATOM   12420 N  N     . ARG   B  1  470  ? -23.176 9.917   118.348 1.00 31.53 ? 468  ARG   B N     1 
ATOM   12421 C  CA    . ARG   B  1  470  ? -22.096 9.596   117.442 1.00 29.55 ? 468  ARG   B CA    1 
ATOM   12422 C  C     . ARG   B  1  470  ? -20.796 10.199  117.958 1.00 29.84 ? 468  ARG   B C     1 
ATOM   12423 O  O     . ARG   B  1  470  ? -20.771 11.362  118.377 1.00 30.11 ? 468  ARG   B O     1 
ATOM   12424 C  CB    . ARG   B  1  470  ? -22.371 10.141  116.036 1.00 28.51 ? 468  ARG   B CB    1 
ATOM   12425 C  CG    . ARG   B  1  470  ? -23.556 9.490   115.328 1.00 29.17 ? 468  ARG   B CG    1 
ATOM   12426 C  CD    . ARG   B  1  470  ? -23.389 7.979   115.208 1.00 27.41 ? 468  ARG   B CD    1 
ATOM   12427 N  NE    . ARG   B  1  470  ? -24.554 7.335   114.605 1.00 32.25 ? 468  ARG   B NE    1 
ATOM   12428 C  CZ    . ARG   B  1  470  ? -25.596 6.878   115.288 1.00 36.99 ? 468  ARG   B CZ    1 
ATOM   12429 N  NH1   . ARG   B  1  470  ? -25.662 6.990   116.606 1.00 33.73 ? 468  ARG   B NH1   1 
ATOM   12430 N  NH2   . ARG   B  1  470  ? -26.600 6.298   114.633 1.00 35.68 ? 468  ARG   B NH2   1 
ATOM   12431 N  N     . PRO   B  1  471  ? -19.705 9.448   117.921 1.00 27.23 ? 469  PRO   B N     1 
ATOM   12432 C  CA    . PRO   B  1  471  ? -18.442 9.952   118.455 1.00 27.06 ? 469  PRO   B CA    1 
ATOM   12433 C  C     . PRO   B  1  471  ? -17.794 10.929  117.490 1.00 26.08 ? 469  PRO   B C     1 
ATOM   12434 O  O     . PRO   B  1  471  ? -18.040 10.923  116.281 1.00 23.29 ? 469  PRO   B O     1 
ATOM   12435 C  CB    . PRO   B  1  471  ? -17.597 8.683   118.583 1.00 24.98 ? 469  PRO   B CB    1 
ATOM   12436 C  CG    . PRO   B  1  471  ? -18.086 7.819   117.493 1.00 30.49 ? 469  PRO   B CG    1 
ATOM   12437 C  CD    . PRO   B  1  471  ? -19.549 8.124   117.305 1.00 26.89 ? 469  PRO   B CD    1 
ATOM   12438 N  N     . CYS   B  1  472  ? -16.962 11.793  118.060 1.00 24.41 ? 470  CYS   B N     1 
ATOM   12439 C  CA    . CYS   B  1  472  ? -16.190 12.737  117.276 1.00 22.12 ? 470  CYS   B CA    1 
ATOM   12440 C  C     . CYS   B  1  472  ? -14.775 12.775  117.833 1.00 23.80 ? 470  CYS   B C     1 
ATOM   12441 O  O     . CYS   B  1  472  ? -14.583 12.904  119.049 1.00 24.64 ? 470  CYS   B O     1 
ATOM   12442 C  CB    . CYS   B  1  472  ? -16.813 14.130  117.319 1.00 24.32 ? 470  CYS   B CB    1 
ATOM   12443 S  SG    . CYS   B  1  472  ? -15.920 15.315  116.296 1.00 26.86 ? 470  CYS   B SG    1 
ATOM   12444 N  N     . ARG   B  1  473  ? -13.794 12.630  116.948 1.00 23.87 ? 471  ARG   B N     1 
ATOM   12445 C  CA    . ARG   B  1  473  ? -12.395 12.777  117.320 1.00 23.44 ? 471  ARG   B CA    1 
ATOM   12446 C  C     . ARG   B  1  473  ? -11.957 14.200  117.013 1.00 23.00 ? 471  ARG   B C     1 
ATOM   12447 O  O     . ARG   B  1  473  ? -12.124 14.684  115.890 1.00 22.47 ? 471  ARG   B O     1 
ATOM   12448 C  CB    . ARG   B  1  473  ? -11.516 11.795  116.548 1.00 20.59 ? 471  ARG   B CB    1 
ATOM   12449 C  CG    . ARG   B  1  473  ? -10.057 11.803  117.033 1.00 20.41 ? 471  ARG   B CG    1 
ATOM   12450 C  CD    . ARG   B  1  473  ? -9.268  10.680  116.392 1.00 20.29 ? 471  ARG   B CD    1 
ATOM   12451 N  NE    . ARG   B  1  473  ? -9.964  9.406   116.522 1.00 22.89 ? 471  ARG   B NE    1 
ATOM   12452 C  CZ    . ARG   B  1  473  ? -9.875  8.603   117.572 1.00 26.34 ? 471  ARG   B CZ    1 
ATOM   12453 N  NH1   . ARG   B  1  473  ? -9.057  8.871   118.580 1.00 23.68 ? 471  ARG   B NH1   1 
ATOM   12454 N  NH2   . ARG   B  1  473  ? -10.632 7.507   117.617 1.00 23.32 ? 471  ARG   B NH2   1 
ATOM   12455 N  N     . ILE   B  1  474  ? -11.395 14.863  118.013 1.00 22.70 ? 472  ILE   B N     1 
ATOM   12456 C  CA    . ILE   B  1  474  ? -10.946 16.240  117.880 1.00 20.54 ? 472  ILE   B CA    1 
ATOM   12457 C  C     . ILE   B  1  474  ? -9.486  16.237  117.453 1.00 20.11 ? 472  ILE   B C     1 
ATOM   12458 O  O     . ILE   B  1  474  ? -8.630  15.680  118.152 1.00 21.26 ? 472  ILE   B O     1 
ATOM   12459 C  CB    . ILE   B  1  474  ? -11.120 16.987  119.206 1.00 22.87 ? 472  ILE   B CB    1 
ATOM   12460 C  CG1   . ILE   B  1  474  ? -12.603 17.055  119.566 1.00 23.17 ? 472  ILE   B CG1   1 
ATOM   12461 C  CG2   . ILE   B  1  474  ? -10.533 18.370  119.108 1.00 24.37 ? 472  ILE   B CG2   1 
ATOM   12462 C  CD1   . ILE   B  1  474  ? -12.819 17.550  120.964 1.00 26.06 ? 472  ILE   B CD1   1 
ATOM   12463 N  N     . TYR   B  1  475  ? -9.211  16.851  116.305 1.00 18.48 ? 473  TYR   B N     1 
ATOM   12464 C  CA    . TYR   B  1  475  ? -7.848  17.099  115.848 1.00 18.91 ? 473  TYR   B CA    1 
ATOM   12465 C  C     . TYR   B  1  475  ? -7.294  18.253  116.667 1.00 21.29 ? 473  TYR   B C     1 
ATOM   12466 O  O     . TYR   B  1  475  ? -7.807  19.375  116.599 1.00 21.43 ? 473  TYR   B O     1 
ATOM   12467 C  CB    . TYR   B  1  475  ? -7.873  17.456  114.364 1.00 19.74 ? 473  TYR   B CB    1 
ATOM   12468 C  CG    . TYR   B  1  475  ? -6.520  17.505  113.698 1.00 19.40 ? 473  TYR   B CG    1 
ATOM   12469 C  CD1   . TYR   B  1  475  ? -5.749  18.656  113.728 1.00 20.59 ? 473  TYR   B CD1   1 
ATOM   12470 C  CD2   . TYR   B  1  475  ? -6.020  16.395  113.035 1.00 18.37 ? 473  TYR   B CD2   1 
ATOM   12471 C  CE1   . TYR   B  1  475  ? -4.505  18.702  113.098 1.00 19.96 ? 473  TYR   B CE1   1 
ATOM   12472 C  CE2   . TYR   B  1  475  ? -4.783  16.430  112.407 1.00 18.91 ? 473  TYR   B CE2   1 
ATOM   12473 C  CZ    . TYR   B  1  475  ? -4.034  17.580  112.449 1.00 22.18 ? 473  TYR   B CZ    1 
ATOM   12474 O  OH    . TYR   B  1  475  ? -2.804  17.612  111.829 1.00 23.64 ? 473  TYR   B OH    1 
ATOM   12475 N  N     . ALA   B  1  476  ? -6.266  17.971  117.459 1.00 19.91 ? 474  ALA   B N     1 
ATOM   12476 C  CA    . ALA   B  1  476  ? -5.828  18.867  118.526 1.00 22.52 ? 474  ALA   B CA    1 
ATOM   12477 C  C     . ALA   B  1  476  ? -4.413  19.354  118.260 1.00 21.98 ? 474  ALA   B C     1 
ATOM   12478 O  O     . ALA   B  1  476  ? -3.445  18.620  118.523 1.00 20.95 ? 474  ALA   B O     1 
ATOM   12479 C  CB    . ALA   B  1  476  ? -5.882  18.111  119.849 1.00 23.09 ? 474  ALA   B CB    1 
ATOM   12480 N  N     . PRO   B  1  477  ? -4.240  20.568  117.740 1.00 22.13 ? 475  PRO   B N     1 
ATOM   12481 C  CA    . PRO   B  1  477  ? -2.892  21.127  117.610 1.00 20.44 ? 475  PRO   B CA    1 
ATOM   12482 C  C     . PRO   B  1  477  ? -2.270  21.324  118.979 1.00 19.13 ? 475  PRO   B C     1 
ATOM   12483 O  O     . PRO   B  1  477  ? -2.940  21.704  119.940 1.00 22.14 ? 475  PRO   B O     1 
ATOM   12484 C  CB    . PRO   B  1  477  ? -3.136  22.477  116.933 1.00 22.75 ? 475  PRO   B CB    1 
ATOM   12485 C  CG    . PRO   B  1  477  ? -4.464  22.342  116.261 1.00 23.82 ? 475  PRO   B CG    1 
ATOM   12486 C  CD    . PRO   B  1  477  ? -5.266  21.460  117.175 1.00 22.36 ? 475  PRO   B CD    1 
ATOM   12487 N  N     . VAL   B  1  478  ? -0.968  21.083  119.059 1.00 18.87 ? 476  VAL   B N     1 
ATOM   12488 C  CA    . VAL   B  1  478  ? -0.239  21.206  120.312 1.00 20.15 ? 476  VAL   B CA    1 
ATOM   12489 C  C     . VAL   B  1  478  ? 1.065   21.909  119.998 1.00 25.36 ? 476  VAL   B C     1 
ATOM   12490 O  O     . VAL   B  1  478  ? 1.832   21.435  119.158 1.00 24.42 ? 476  VAL   B O     1 
ATOM   12491 C  CB    . VAL   B  1  478  ? 0.052   19.839  120.955 1.00 22.20 ? 476  VAL   B CB    1 
ATOM   12492 C  CG1   . VAL   B  1  478  ? 0.797   20.034  122.273 1.00 24.74 ? 476  VAL   B CG1   1 
ATOM   12493 C  CG2   . VAL   B  1  478  ? -1.235  19.054  121.165 1.00 20.63 ? 476  VAL   B CG2   1 
ATOM   12494 N  N     . GLY   B  1  479  ? 1.318   23.026  120.659 1.00 28.42 ? 477  GLY   B N     1 
ATOM   12495 C  CA    . GLY   B  1  479  ? 2.552   23.746  120.427 1.00 32.25 ? 477  GLY   B CA    1 
ATOM   12496 C  C     . GLY   B  1  479  ? 2.444   25.192  120.855 1.00 32.05 ? 477  GLY   B C     1 
ATOM   12497 O  O     . GLY   B  1  479  ? 1.395   25.667  121.294 1.00 29.97 ? 477  GLY   B O     1 
ATOM   12498 N  N     . THR   B  1  480  ? 3.559   25.894  120.666 1.00 37.75 ? 478  THR   B N     1 
ATOM   12499 C  CA    . THR   B  1  480  ? 3.762   27.239  121.181 1.00 42.75 ? 478  THR   B CA    1 
ATOM   12500 C  C     . THR   B  1  480  ? 3.050   28.264  120.301 1.00 47.56 ? 478  THR   B C     1 
ATOM   12501 O  O     . THR   B  1  480  ? 2.448   27.939  119.273 1.00 49.41 ? 478  THR   B O     1 
ATOM   12502 C  CB    . THR   B  1  480  ? 5.257   27.546  121.242 1.00 39.59 ? 478  THR   B CB    1 
ATOM   12503 O  OG1   . THR   B  1  480  ? 5.799   27.505  119.914 1.00 50.02 ? 478  THR   B OG1   1 
ATOM   12504 C  CG2   . THR   B  1  480  ? 5.976   26.527  122.097 1.00 40.63 ? 478  THR   B CG2   1 
ATOM   12505 N  N     . HIS   B  1  481  ? 3.137   29.532  120.710 1.00 52.52 ? 479  HIS   B N     1 
ATOM   12506 C  CA    . HIS   B  1  481  ? 2.518   30.612  119.947 1.00 50.59 ? 479  HIS   B CA    1 
ATOM   12507 C  C     . HIS   B  1  481  ? 3.193   30.792  118.592 1.00 55.47 ? 479  HIS   B C     1 
ATOM   12508 O  O     . HIS   B  1  481  ? 2.519   30.891  117.559 1.00 54.92 ? 479  HIS   B O     1 
ATOM   12509 C  CB    . HIS   B  1  481  ? 2.571   31.909  120.753 1.00 51.14 ? 479  HIS   B CB    1 
ATOM   12510 N  N     . GLU   B  1  482  ? 4.529   30.838  118.575 1.00 55.78 ? 480  GLU   B N     1 
ATOM   12511 C  CA    . GLU   B  1  482  ? 5.248   31.077  117.326 1.00 53.33 ? 480  GLU   B CA    1 
ATOM   12512 C  C     . GLU   B  1  482  ? 5.009   29.953  116.326 1.00 51.58 ? 480  GLU   B C     1 
ATOM   12513 O  O     . GLU   B  1  482  ? 4.899   30.198  115.118 1.00 52.36 ? 480  GLU   B O     1 
ATOM   12514 C  CB    . GLU   B  1  482  ? 6.742   31.247  117.606 1.00 53.63 ? 480  GLU   B CB    1 
ATOM   12515 N  N     . THR   B  1  483  ? 4.913   28.714  116.810 1.00 54.05 ? 481  THR   B N     1 
ATOM   12516 C  CA    . THR   B  1  483  ? 4.657   27.592  115.914 1.00 54.32 ? 481  THR   B CA    1 
ATOM   12517 C  C     . THR   B  1  483  ? 3.215   27.596  115.415 1.00 50.10 ? 481  THR   B C     1 
ATOM   12518 O  O     . THR   B  1  483  ? 2.956   27.263  114.252 1.00 56.63 ? 481  THR   B O     1 
ATOM   12519 C  CB    . THR   B  1  483  ? 4.995   26.274  116.615 1.00 52.01 ? 481  THR   B CB    1 
ATOM   12520 N  N     . LEU   B  1  484  ? 2.264   27.971  116.275 1.00 53.03 ? 482  LEU   B N     1 
ATOM   12521 C  CA    . LEU   B  1  484  ? 0.858   27.948  115.880 1.00 52.59 ? 482  LEU   B CA    1 
ATOM   12522 C  C     . LEU   B  1  484  ? 0.584   28.920  114.738 1.00 50.15 ? 482  LEU   B C     1 
ATOM   12523 O  O     . LEU   B  1  484  ? -0.149  28.594  113.795 1.00 52.69 ? 482  LEU   B O     1 
ATOM   12524 C  CB    . LEU   B  1  484  ? -0.033  28.267  117.084 1.00 48.49 ? 482  LEU   B CB    1 
ATOM   12525 N  N     . LEU   B  1  485  ? 1.179   30.112  114.797 1.00 48.54 ? 483  LEU   B N     1 
ATOM   12526 C  CA    . LEU   B  1  485  ? 0.876   31.162  113.830 1.00 55.82 ? 483  LEU   B CA    1 
ATOM   12527 C  C     . LEU   B  1  485  ? 1.240   30.781  112.400 1.00 51.17 ? 483  LEU   B C     1 
ATOM   12528 O  O     . LEU   B  1  485  ? 0.684   31.358  111.458 1.00 47.95 ? 483  LEU   B O     1 
ATOM   12529 C  CB    . LEU   B  1  485  ? 1.612   32.444  114.231 1.00 52.98 ? 483  LEU   B CB    1 
ATOM   12530 C  CG    . LEU   B  1  485  ? 1.126   33.097  115.526 1.00 45.09 ? 483  LEU   B CG    1 
ATOM   12531 C  CD1   . LEU   B  1  485  ? 2.228   33.921  116.163 1.00 45.14 ? 483  LEU   B CD1   1 
ATOM   12532 C  CD2   . LEU   B  1  485  ? -0.106  33.955  115.256 1.00 44.65 ? 483  LEU   B CD2   1 
ATOM   12533 N  N     . ALA   B  1  486  ? 2.142   29.813  112.215 1.00 52.84 ? 484  ALA   B N     1 
ATOM   12534 C  CA    . ALA   B  1  486  ? 2.762   29.545  110.921 1.00 48.73 ? 484  ALA   B CA    1 
ATOM   12535 C  C     . ALA   B  1  486  ? 1.825   28.915  109.889 1.00 51.60 ? 484  ALA   B C     1 
ATOM   12536 O  O     . ALA   B  1  486  ? 2.259   28.712  108.749 1.00 55.29 ? 484  ALA   B O     1 
ATOM   12537 C  CB    . ALA   B  1  486  ? 4.010   28.681  111.108 1.00 47.02 ? 484  ALA   B CB    1 
ATOM   12538 N  N     . TYR   B  1  487  ? 0.574   28.603  110.231 1.00 53.33 ? 485  TYR   B N     1 
ATOM   12539 C  CA    . TYR   B  1  487  ? -0.344  28.034  109.248 1.00 48.13 ? 485  TYR   B CA    1 
ATOM   12540 C  C     . TYR   B  1  487  ? -1.793  28.168  109.699 1.00 48.39 ? 485  TYR   B C     1 
ATOM   12541 O  O     . TYR   B  1  487  ? -2.652  27.381  109.291 1.00 41.25 ? 485  TYR   B O     1 
ATOM   12542 C  CB    . TYR   B  1  487  ? 0.001   26.568  108.970 1.00 45.57 ? 485  TYR   B CB    1 
ATOM   12543 N  N     . LEU   B  1  488  ? -2.076  29.192  110.508 1.00 53.92 ? 486  LEU   B N     1 
ATOM   12544 C  CA    . LEU   B  1  488  ? -3.385  29.385  111.128 1.00 54.09 ? 486  LEU   B CA    1 
ATOM   12545 C  C     . LEU   B  1  488  ? -4.498  29.684  110.127 1.00 50.82 ? 486  LEU   B C     1 
ATOM   12546 O  O     . LEU   B  1  488  ? -5.672  29.704  110.516 1.00 54.39 ? 486  LEU   B O     1 
ATOM   12547 C  CB    . LEU   B  1  488  ? -3.277  30.505  112.165 1.00 50.92 ? 486  LEU   B CB    1 
ATOM   12548 C  CG    . LEU   B  1  488  ? -4.408  30.765  113.152 1.00 47.84 ? 486  LEU   B CG    1 
ATOM   12549 C  CD1   . LEU   B  1  488  ? -3.793  31.172  114.458 1.00 44.46 ? 486  LEU   B CD1   1 
ATOM   12550 C  CD2   . LEU   B  1  488  ? -5.352  31.853  112.653 1.00 45.72 ? 486  LEU   B CD2   1 
ATOM   12551 N  N     . VAL   B  1  489  ? -4.172  29.913  108.855 1.00 57.55 ? 487  VAL   B N     1 
ATOM   12552 C  CA    . VAL   B  1  489  ? -5.210  30.135  107.857 1.00 49.87 ? 487  VAL   B CA    1 
ATOM   12553 C  C     . VAL   B  1  489  ? -6.167  28.952  107.755 1.00 56.18 ? 487  VAL   B C     1 
ATOM   12554 O  O     . VAL   B  1  489  ? -7.299  29.111  107.286 1.00 55.68 ? 487  VAL   B O     1 
ATOM   12555 C  CB    . VAL   B  1  489  ? -4.571  30.473  106.498 1.00 49.56 ? 487  VAL   B CB    1 
ATOM   12556 N  N     . ARG   B  1  490  ? -5.750  27.767  108.207 1.00 38.80 ? 488  ARG   B N     1 
ATOM   12557 C  CA    . ARG   B  1  490  ? -6.562  26.573  108.004 1.00 45.30 ? 488  ARG   B CA    1 
ATOM   12558 C  C     . ARG   B  1  490  ? -7.813  26.580  108.874 1.00 43.62 ? 488  ARG   B C     1 
ATOM   12559 O  O     . ARG   B  1  490  ? -8.902  26.239  108.399 1.00 44.79 ? 488  ARG   B O     1 
ATOM   12560 C  CB    . ARG   B  1  490  ? -5.722  25.326  108.245 1.00 42.52 ? 488  ARG   B CB    1 
ATOM   12561 C  CG    . ARG   B  1  490  ? -4.657  25.152  107.190 1.00 35.80 ? 488  ARG   B CG    1 
ATOM   12562 C  CD    . ARG   B  1  490  ? -3.779  23.957  107.460 1.00 36.84 ? 488  ARG   B CD    1 
ATOM   12563 N  NE    . ARG   B  1  490  ? -2.777  23.823  106.409 1.00 34.29 ? 488  ARG   B NE    1 
ATOM   12564 C  CZ    . ARG   B  1  490  ? -1.605  23.222  106.570 1.00 29.15 ? 488  ARG   B CZ    1 
ATOM   12565 N  NH1   . ARG   B  1  490  ? -1.266  22.676  107.724 1.00 29.73 ? 488  ARG   B NH1   1 
ATOM   12566 N  NH2   . ARG   B  1  490  ? -0.750  23.185  105.552 1.00 31.86 ? 488  ARG   B NH2   1 
ATOM   12567 N  N     . ARG   B  1  491  ? -7.682  26.960  110.147 1.00 42.84 ? 489  ARG   B N     1 
ATOM   12568 C  CA    . ARG   B  1  491  ? -8.856  27.010  111.013 1.00 47.15 ? 489  ARG   B CA    1 
ATOM   12569 C  C     . ARG   B  1  491  ? -9.929  27.935  110.448 1.00 50.85 ? 489  ARG   B C     1 
ATOM   12570 O  O     . ARG   B  1  491  ? -11.125 27.695  110.655 1.00 48.68 ? 489  ARG   B O     1 
ATOM   12571 C  CB    . ARG   B  1  491  ? -8.458  27.437  112.428 1.00 43.87 ? 489  ARG   B CB    1 
ATOM   12572 N  N     . LEU   B  1  492  ? -9.528  28.972  109.708 1.00 51.26 ? 490  LEU   B N     1 
ATOM   12573 C  CA    . LEU   B  1  492  ? -10.450 29.982  109.203 1.00 50.69 ? 490  LEU   B CA    1 
ATOM   12574 C  C     . LEU   B  1  492  ? -10.635 29.923  107.691 1.00 48.06 ? 490  LEU   B C     1 
ATOM   12575 O  O     . LEU   B  1  492  ? -11.756 29.706  107.221 1.00 57.42 ? 490  LEU   B O     1 
ATOM   12576 C  CB    . LEU   B  1  492  ? -10.004 31.383  109.652 1.00 50.17 ? 490  LEU   B CB    1 
ATOM   12577 N  N     . LEU   B  1  493  ? -9.574  30.124  106.908 1.00 59.42 ? 491  LEU   B N     1 
ATOM   12578 C  CA    . LEU   B  1  493  ? -9.708  30.181  105.448 1.00 47.50 ? 491  LEU   B CA    1 
ATOM   12579 C  C     . LEU   B  1  493  ? -10.223 28.863  104.884 1.00 47.54 ? 491  LEU   B C     1 
ATOM   12580 O  O     . LEU   B  1  493  ? -11.409 28.734  104.583 1.00 53.93 ? 491  LEU   B O     1 
ATOM   12581 C  CB    . LEU   B  1  493  ? -8.388  30.574  104.768 1.00 44.58 ? 491  LEU   B CB    1 
ATOM   12582 N  N     . ALA   B  1  497  ? -12.600 32.029  103.486 1.00 42.20 ? 495  ALA   B N     1 
ATOM   12583 C  CA    . ALA   B  1  497  ? -13.360 31.826  102.254 1.00 45.60 ? 495  ALA   B CA    1 
ATOM   12584 C  C     . ALA   B  1  497  ? -14.859 31.995  102.476 1.00 37.61 ? 495  ALA   B C     1 
ATOM   12585 O  O     . ALA   B  1  497  ? -15.430 31.398  103.385 1.00 40.74 ? 495  ALA   B O     1 
ATOM   12586 C  CB    . ALA   B  1  497  ? -13.064 30.453  101.664 1.00 38.56 ? 495  ALA   B CB    1 
ATOM   12587 N  N     . ASN   B  1  498  ? -15.492 32.804  101.620 1.00 40.30 ? 496  ASN   B N     1 
ATOM   12588 C  CA    . ASN   B  1  498  ? -16.924 33.059  101.743 1.00 42.76 ? 496  ASN   B CA    1 
ATOM   12589 C  C     . ASN   B  1  498  ? -17.753 31.804  101.498 1.00 40.29 ? 496  ASN   B C     1 
ATOM   12590 O  O     . ASN   B  1  498  ? -18.875 31.695  102.007 1.00 38.69 ? 496  ASN   B O     1 
ATOM   12591 C  CB    . ASN   B  1  498  ? -17.344 34.170  100.778 1.00 40.65 ? 496  ASN   B CB    1 
ATOM   12592 N  N     . SER   B  1  499  ? -17.230 30.853  100.729 1.00 36.77 ? 497  SER   B N     1 
ATOM   12593 C  CA    . SER   B  1  499  ? -17.970 29.641  100.407 1.00 34.22 ? 497  SER   B CA    1 
ATOM   12594 C  C     . SER   B  1  499  ? -17.928 28.608  101.519 1.00 32.30 ? 497  SER   B C     1 
ATOM   12595 O  O     . SER   B  1  499  ? -18.590 27.573  101.400 1.00 29.99 ? 497  SER   B O     1 
ATOM   12596 C  CB    . SER   B  1  499  ? -17.379 28.997  99.153  1.00 37.75 ? 497  SER   B CB    1 
ATOM   12597 O  OG    . SER   B  1  499  ? -16.035 28.623  99.394  1.00 38.18 ? 497  SER   B OG    1 
ATOM   12598 N  N     . SER   B  1  500  ? -17.151 28.847  102.571 1.00 33.21 ? 498  SER   B N     1 
ATOM   12599 C  CA    . SER   B  1  500  ? -16.987 27.860  103.621 1.00 29.79 ? 498  SER   B CA    1 
ATOM   12600 C  C     . SER   B  1  500  ? -18.148 27.917  104.607 1.00 34.67 ? 498  SER   B C     1 
ATOM   12601 O  O     . SER   B  1  500  ? -18.722 28.978  104.867 1.00 38.03 ? 498  SER   B O     1 
ATOM   12602 C  CB    . SER   B  1  500  ? -15.668 28.076  104.364 1.00 34.93 ? 498  SER   B CB    1 
ATOM   12603 O  OG    . SER   B  1  500  ? -15.660 29.325  105.038 1.00 40.49 ? 498  SER   B OG    1 
ATOM   12604 N  N     . PHE   B  1  501  ? -18.492 26.748  105.148 1.00 33.19 ? 499  PHE   B N     1 
ATOM   12605 C  CA    . PHE   B  1  501  ? -19.506 26.683  106.193 1.00 33.61 ? 499  PHE   B CA    1 
ATOM   12606 C  C     . PHE   B  1  501  ? -19.090 27.509  107.407 1.00 36.99 ? 499  PHE   B C     1 
ATOM   12607 O  O     . PHE   B  1  501  ? -19.936 28.127  108.064 1.00 43.74 ? 499  PHE   B O     1 
ATOM   12608 C  CB    . PHE   B  1  501  ? -19.749 25.222  106.576 1.00 31.39 ? 499  PHE   B CB    1 
ATOM   12609 C  CG    . PHE   B  1  501  ? -20.966 25.007  107.427 1.00 33.77 ? 499  PHE   B CG    1 
ATOM   12610 C  CD1   . PHE   B  1  501  ? -20.910 25.181  108.800 1.00 37.21 ? 499  PHE   B CD1   1 
ATOM   12611 C  CD2   . PHE   B  1  501  ? -22.158 24.612  106.855 1.00 33.58 ? 499  PHE   B CD2   1 
ATOM   12612 C  CE1   . PHE   B  1  501  ? -22.041 24.980  109.584 1.00 37.63 ? 499  PHE   B CE1   1 
ATOM   12613 C  CE2   . PHE   B  1  501  ? -23.285 24.406  107.629 1.00 37.61 ? 499  PHE   B CE2   1 
ATOM   12614 C  CZ    . PHE   B  1  501  ? -23.223 24.592  108.995 1.00 34.37 ? 499  PHE   B CZ    1 
ATOM   12615 N  N     . VAL   B  1  502  ? -17.786 27.545  107.704 1.00 40.43 ? 500  VAL   B N     1 
ATOM   12616 C  CA    . VAL   B  1  502  ? -17.284 28.305  108.850 1.00 45.06 ? 500  VAL   B CA    1 
ATOM   12617 C  C     . VAL   B  1  502  ? -17.678 29.775  108.739 1.00 44.26 ? 500  VAL   B C     1 
ATOM   12618 O  O     . VAL   B  1  502  ? -17.990 30.429  109.742 1.00 45.24 ? 500  VAL   B O     1 
ATOM   12619 C  CB    . VAL   B  1  502  ? -15.759 28.124  108.986 1.00 42.86 ? 500  VAL   B CB    1 
ATOM   12620 N  N     . HIS   B  1  503  ? -17.672 30.315  107.522 1.00 39.15 ? 501  HIS   B N     1 
ATOM   12621 C  CA    . HIS   B  1  503  ? -18.080 31.699  107.319 1.00 41.51 ? 501  HIS   B CA    1 
ATOM   12622 C  C     . HIS   B  1  503  ? -19.591 31.818  107.154 1.00 44.87 ? 501  HIS   B C     1 
ATOM   12623 O  O     . HIS   B  1  503  ? -20.203 32.762  107.669 1.00 42.88 ? 501  HIS   B O     1 
ATOM   12624 C  CB    . HIS   B  1  503  ? -17.350 32.274  106.103 1.00 42.97 ? 501  HIS   B CB    1 
ATOM   12625 C  CG    . HIS   B  1  503  ? -17.885 33.593  105.637 1.00 45.74 ? 501  HIS   B CG    1 
ATOM   12626 N  ND1   . HIS   B  1  503  ? -18.909 33.701  104.720 1.00 45.53 ? 501  HIS   B ND1   1 
ATOM   12627 C  CD2   . HIS   B  1  503  ? -17.526 34.861  105.950 1.00 47.01 ? 501  HIS   B CD2   1 
ATOM   12628 C  CE1   . HIS   B  1  503  ? -19.164 34.978  104.495 1.00 45.32 ? 501  HIS   B CE1   1 
ATOM   12629 N  NE2   . HIS   B  1  503  ? -18.338 35.702  105.228 1.00 46.47 ? 501  HIS   B NE2   1 
ATOM   12630 N  N     . ARG   B  1  504  ? -20.211 30.854  106.469 1.00 40.64 ? 502  ARG   B N     1 
ATOM   12631 C  CA    . ARG   B  1  504  ? -21.609 30.998  106.081 1.00 34.99 ? 502  ARG   B CA    1 
ATOM   12632 C  C     . ARG   B  1  504  ? -22.547 30.881  107.275 1.00 40.54 ? 502  ARG   B C     1 
ATOM   12633 O  O     . ARG   B  1  504  ? -23.587 31.549  107.316 1.00 41.36 ? 502  ARG   B O     1 
ATOM   12634 C  CB    . ARG   B  1  504  ? -21.959 29.982  104.995 1.00 37.23 ? 502  ARG   B CB    1 
ATOM   12635 C  CG    . ARG   B  1  504  ? -21.365 30.335  103.644 1.00 37.48 ? 502  ARG   B CG    1 
ATOM   12636 C  CD    . ARG   B  1  504  ? -21.392 29.155  102.679 1.00 33.96 ? 502  ARG   B CD    1 
ATOM   12637 N  NE    . ARG   B  1  504  ? -22.725 28.605  102.476 1.00 34.73 ? 502  ARG   B NE    1 
ATOM   12638 C  CZ    . ARG   B  1  504  ? -23.664 29.173  101.732 1.00 37.01 ? 502  ARG   B CZ    1 
ATOM   12639 N  NH1   . ARG   B  1  504  ? -23.471 30.350  101.155 1.00 37.49 ? 502  ARG   B NH1   1 
ATOM   12640 N  NH2   . ARG   B  1  504  ? -24.824 28.545  101.560 1.00 37.32 ? 502  ARG   B NH2   1 
ATOM   12641 N  N     . ILE   B  1  505  ? -22.211 30.031  108.249 1.00 37.49 ? 503  ILE   B N     1 
ATOM   12642 C  CA    . ILE   B  1  505  ? -23.051 29.883  109.432 1.00 40.22 ? 503  ILE   B CA    1 
ATOM   12643 C  C     . ILE   B  1  505  ? -23.190 31.197  110.192 1.00 45.15 ? 503  ILE   B C     1 
ATOM   12644 O  O     . ILE   B  1  505  ? -24.192 31.409  110.886 1.00 40.26 ? 503  ILE   B O     1 
ATOM   12645 C  CB    . ILE   B  1  505  ? -22.534 28.742  110.335 1.00 37.61 ? 503  ILE   B CB    1 
ATOM   12646 N  N     . ASN   B  1  506  ? -22.216 32.097  110.058 1.00 39.34 ? 504  ASN   B N     1 
ATOM   12647 C  CA    . ASN   B  1  506  ? -22.230 33.382  110.744 1.00 46.88 ? 504  ASN   B CA    1 
ATOM   12648 C  C     . ASN   B  1  506  ? -22.705 34.531  109.866 1.00 48.27 ? 504  ASN   B C     1 
ATOM   12649 O  O     . ASN   B  1  506  ? -22.691 35.680  110.314 1.00 50.87 ? 504  ASN   B O     1 
ATOM   12650 C  CB    . ASN   B  1  506  ? -20.841 33.704  111.304 1.00 47.54 ? 504  ASN   B CB    1 
ATOM   12651 C  CG    . ASN   B  1  506  ? -20.448 32.788  112.442 1.00 51.92 ? 504  ASN   B CG    1 
ATOM   12652 O  OD1   . ASN   B  1  506  ? -21.287 32.391  113.250 1.00 50.83 ? 504  ASN   B OD1   1 
ATOM   12653 N  ND2   . ASN   B  1  506  ? -19.168 32.441  112.508 1.00 56.89 ? 504  ASN   B ND2   1 
ATOM   12654 N  N     . ASP   B  1  507  ? -23.119 34.256  108.632 1.00 44.49 ? 505  ASP   B N     1 
ATOM   12655 C  CA    . ASP   B  1  507  ? -23.578 35.309  107.744 1.00 47.32 ? 505  ASP   B CA    1 
ATOM   12656 C  C     . ASP   B  1  507  ? -25.097 35.344  107.785 1.00 52.48 ? 505  ASP   B C     1 
ATOM   12657 O  O     . ASP   B  1  507  ? -25.740 34.411  107.281 1.00 49.28 ? 505  ASP   B O     1 
ATOM   12658 C  CB    . ASP   B  1  507  ? -23.092 35.044  106.321 1.00 46.10 ? 505  ASP   B CB    1 
ATOM   12659 C  CG    . ASP   B  1  507  ? -23.168 36.274  105.441 1.00 49.80 ? 505  ASP   B CG    1 
ATOM   12660 O  OD1   . ASP   B  1  507  ? -23.826 37.258  105.840 1.00 57.07 ? 505  ASP   B OD1   1 
ATOM   12661 O  OD2   . ASP   B  1  507  ? -22.556 36.262  104.353 1.00 59.17 ? 505  ASP   B OD2   1 
ATOM   12662 N  N     . PRO   B  1  508  ? -25.714 36.376  108.371 1.00 56.91 ? 506  PRO   B N     1 
ATOM   12663 C  CA    . PRO   B  1  508  ? -27.183 36.413  108.447 1.00 53.30 ? 506  PRO   B CA    1 
ATOM   12664 C  C     . PRO   B  1  508  ? -27.855 36.572  107.096 1.00 55.22 ? 506  PRO   B C     1 
ATOM   12665 O  O     . PRO   B  1  508  ? -29.069 36.350  106.999 1.00 57.68 ? 506  PRO   B O     1 
ATOM   12666 C  CB    . PRO   B  1  508  ? -27.468 37.625  109.348 1.00 61.30 ? 506  PRO   B CB    1 
ATOM   12667 C  CG    . PRO   B  1  508  ? -26.139 38.021  109.933 1.00 62.94 ? 506  PRO   B CG    1 
ATOM   12668 C  CD    . PRO   B  1  508  ? -25.105 37.581  108.953 1.00 56.45 ? 506  PRO   B CD    1 
ATOM   12669 N  N     . LYS   B  1  509  ? -27.110 36.964  106.061 1.00 54.87 ? 507  LYS   B N     1 
ATOM   12670 C  CA    . LYS   B  1  509  ? -27.651 37.016  104.710 1.00 54.02 ? 507  LYS   B CA    1 
ATOM   12671 C  C     . LYS   B  1  509  ? -27.793 35.634  104.089 1.00 55.96 ? 507  LYS   B C     1 
ATOM   12672 O  O     . LYS   B  1  509  ? -28.489 35.493  103.078 1.00 59.76 ? 507  LYS   B O     1 
ATOM   12673 C  CB    . LYS   B  1  509  ? -26.767 37.894  103.823 1.00 52.19 ? 507  LYS   B CB    1 
ATOM   12674 N  N     . VAL   B  1  510  ? -27.148 34.621  104.660 1.00 53.41 ? 508  VAL   B N     1 
ATOM   12675 C  CA    . VAL   B  1  510  ? -27.278 33.242  104.204 1.00 52.21 ? 508  VAL   B CA    1 
ATOM   12676 C  C     . VAL   B  1  510  ? -28.259 32.543  105.132 1.00 49.49 ? 508  VAL   B C     1 
ATOM   12677 O  O     . VAL   B  1  510  ? -28.020 32.445  106.341 1.00 49.56 ? 508  VAL   B O     1 
ATOM   12678 C  CB    . VAL   B  1  510  ? -25.918 32.525  104.184 1.00 44.58 ? 508  VAL   B CB    1 
ATOM   12679 N  N     . SER   B  1  511  ? -29.364 32.061  104.572 1.00 48.54 ? 509  SER   B N     1 
ATOM   12680 C  CA    . SER   B  1  511  ? -30.425 31.480  105.375 1.00 47.98 ? 509  SER   B CA    1 
ATOM   12681 C  C     . SER   B  1  511  ? -30.119 30.023  105.699 1.00 49.49 ? 509  SER   B C     1 
ATOM   12682 O  O     . SER   B  1  511  ? -29.192 29.412  105.161 1.00 49.06 ? 509  SER   B O     1 
ATOM   12683 C  CB    . SER   B  1  511  ? -31.756 31.546  104.631 1.00 51.67 ? 509  SER   B CB    1 
ATOM   12684 O  OG    . SER   B  1  511  ? -31.868 30.475  103.709 1.00 52.62 ? 509  SER   B OG    1 
ATOM   12685 N  N     . ILE   B  1  512  ? -30.937 29.463  106.590 1.00 45.55 ? 510  ILE   B N     1 
ATOM   12686 C  CA    . ILE   B  1  512  ? -30.798 28.056  106.941 1.00 46.86 ? 510  ILE   B CA    1 
ATOM   12687 C  C     . ILE   B  1  512  ? -31.213 27.162  105.778 1.00 51.21 ? 510  ILE   B C     1 
ATOM   12688 O  O     . ILE   B  1  512  ? -30.638 26.083  105.579 1.00 45.16 ? 510  ILE   B O     1 
ATOM   12689 C  CB    . ILE   B  1  512  ? -31.558 27.766  108.247 1.00 44.45 ? 510  ILE   B CB    1 
ATOM   12690 C  CG1   . ILE   B  1  512  ? -30.897 28.534  109.394 1.00 45.88 ? 510  ILE   B CG1   1 
ATOM   12691 C  CG2   . ILE   B  1  512  ? -31.612 26.274  108.535 1.00 43.93 ? 510  ILE   B CG2   1 
ATOM   12692 C  CD1   . ILE   B  1  512  ? -31.630 28.445  110.704 1.00 42.59 ? 510  ILE   B CD1   1 
ATOM   12693 N  N     . ASP   B  1  513  ? -32.192 27.599  104.978 1.00 49.37 ? 511  ASP   B N     1 
ATOM   12694 C  CA    . ASP   B  1  513  ? -32.565 26.840  103.786 1.00 48.31 ? 511  ASP   B CA    1 
ATOM   12695 C  C     . ASP   B  1  513  ? -31.388 26.690  102.828 1.00 44.00 ? 511  ASP   B C     1 
ATOM   12696 O  O     . ASP   B  1  513  ? -31.174 25.611  102.263 1.00 41.85 ? 511  ASP   B O     1 
ATOM   12697 C  CB    . ASP   B  1  513  ? -33.757 27.495  103.085 1.00 51.87 ? 511  ASP   B CB    1 
ATOM   12698 C  CG    . ASP   B  1  513  ? -35.087 27.131  103.727 1.00 55.55 ? 511  ASP   B CG    1 
ATOM   12699 O  OD1   . ASP   B  1  513  ? -35.201 26.022  104.294 1.00 55.66 ? 511  ASP   B OD1   1 
ATOM   12700 O  OD2   . ASP   B  1  513  ? -36.025 27.953  103.659 1.00 62.52 ? 511  ASP   B OD2   1 
ATOM   12701 N  N     . GLU   B  1  514  ? -30.613 27.758  102.629 1.00 41.25 ? 512  GLU   B N     1 
ATOM   12702 C  CA    . GLU   B  1  514  ? -29.435 27.652  101.772 1.00 45.76 ? 512  GLU   B CA    1 
ATOM   12703 C  C     . GLU   B  1  514  ? -28.424 26.663  102.341 1.00 42.73 ? 512  GLU   B C     1 
ATOM   12704 O  O     . GLU   B  1  514  ? -27.827 25.874  101.600 1.00 41.54 ? 512  GLU   B O     1 
ATOM   12705 C  CB    . GLU   B  1  514  ? -28.787 29.024  101.595 1.00 41.79 ? 512  GLU   B CB    1 
ATOM   12706 C  CG    . GLU   B  1  514  ? -29.726 30.113  101.127 1.00 51.93 ? 512  GLU   B CG    1 
ATOM   12707 C  CD    . GLU   B  1  514  ? -29.038 31.461  101.026 1.00 56.58 ? 512  GLU   B CD    1 
ATOM   12708 O  OE1   . GLU   B  1  514  ? -27.943 31.526  100.423 1.00 61.58 ? 512  GLU   B OE1   1 
ATOM   12709 O  OE2   . GLU   B  1  514  ? -29.586 32.451  101.559 1.00 57.16 ? 512  GLU   B OE2   1 
ATOM   12710 N  N     . LEU   B  1  515  ? -28.227 26.685  103.660 1.00 39.93 ? 513  LEU   B N     1 
ATOM   12711 C  CA    . LEU   B  1  515  ? -27.207 25.842  104.275 1.00 39.18 ? 513  LEU   B CA    1 
ATOM   12712 C  C     . LEU   B  1  515  ? -27.567 24.366  104.206 1.00 38.33 ? 513  LEU   B C     1 
ATOM   12713 O  O     . LEU   B  1  515  ? -26.673 23.513  104.217 1.00 35.54 ? 513  LEU   B O     1 
ATOM   12714 C  CB    . LEU   B  1  515  ? -26.998 26.262  105.727 1.00 36.20 ? 513  LEU   B CB    1 
ATOM   12715 C  CG    . LEU   B  1  515  ? -26.457 27.672  105.935 1.00 36.86 ? 513  LEU   B CG    1 
ATOM   12716 C  CD1   . LEU   B  1  515  ? -26.563 28.044  107.402 1.00 42.46 ? 513  LEU   B CD1   1 
ATOM   12717 C  CD2   . LEU   B  1  515  ? -25.012 27.777  105.458 1.00 36.66 ? 513  LEU   B CD2   1 
ATOM   12718 N  N     . ILE   B  1  516  ? -28.858 24.040  104.141 1.00 34.54 ? 514  ILE   B N     1 
ATOM   12719 C  CA    . ILE   B  1  516  ? -29.293 22.650  104.092 1.00 33.59 ? 514  ILE   B CA    1 
ATOM   12720 C  C     . ILE   B  1  516  ? -29.546 22.169  102.675 1.00 32.67 ? 514  ILE   B C     1 
ATOM   12721 O  O     . ILE   B  1  516  ? -29.979 21.022  102.490 1.00 34.30 ? 514  ILE   B O     1 
ATOM   12722 C  CB    . ILE   B  1  516  ? -30.518 22.389  104.989 1.00 38.98 ? 514  ILE   B CB    1 
ATOM   12723 C  CG1   . ILE   B  1  516  ? -31.766 23.043  104.387 1.00 39.64 ? 514  ILE   B CG1   1 
ATOM   12724 C  CG2   . ILE   B  1  516  ? -30.260 22.893  106.400 1.00 37.76 ? 514  ILE   B CG2   1 
ATOM   12725 C  CD1   . ILE   B  1  516  ? -33.025 22.813  105.195 1.00 43.96 ? 514  ILE   B CD1   1 
ATOM   12726 N  N     . ALA   B  1  517  ? -29.305 23.012  101.673 1.00 37.95 ? 515  ALA   B N     1 
ATOM   12727 C  CA    . ALA   B  1  517  ? -29.414 22.588  100.284 1.00 38.21 ? 515  ALA   B CA    1 
ATOM   12728 C  C     . ALA   B  1  517  ? -28.557 21.353  100.055 1.00 34.22 ? 515  ALA   B C     1 
ATOM   12729 O  O     . ALA   B  1  517  ? -27.412 21.282  100.512 1.00 32.07 ? 515  ALA   B O     1 
ATOM   12730 C  CB    . ALA   B  1  517  ? -28.961 23.718  99.359  1.00 35.96 ? 515  ALA   B CB    1 
ATOM   12731 N  N     . ASP   B  1  518  ? -29.137 20.365  99.380  1.00 35.03 ? 516  ASP   B N     1 
ATOM   12732 C  CA    . ASP   B  1  518  ? -28.480 19.095  99.127  1.00 34.15 ? 516  ASP   B CA    1 
ATOM   12733 C  C     . ASP   B  1  518  ? -27.577 19.282  97.918  1.00 29.91 ? 516  ASP   B C     1 
ATOM   12734 O  O     . ASP   B  1  518  ? -28.071 19.473  96.802  1.00 30.41 ? 516  ASP   B O     1 
ATOM   12735 C  CB    . ASP   B  1  518  ? -29.533 18.019  98.861  1.00 30.72 ? 516  ASP   B CB    1 
ATOM   12736 C  CG    . ASP   B  1  518  ? -28.934 16.637  98.644  1.00 35.55 ? 516  ASP   B CG    1 
ATOM   12737 O  OD1   . ASP   B  1  518  ? -27.692 16.503  98.577  1.00 29.86 ? 516  ASP   B OD1   1 
ATOM   12738 O  OD2   . ASP   B  1  518  ? -29.716 15.670  98.534  1.00 38.44 ? 516  ASP   B OD2   1 
ATOM   12739 N  N     . PRO   B  1  519  ? -26.255 19.250  98.093  1.00 26.11 ? 517  PRO   B N     1 
ATOM   12740 C  CA    . PRO   B  1  519  ? -25.369 19.443  96.938  1.00 28.44 ? 517  PRO   B CA    1 
ATOM   12741 C  C     . PRO   B  1  519  ? -25.593 18.419  95.846  1.00 26.70 ? 517  PRO   B C     1 
ATOM   12742 O  O     . PRO   B  1  519  ? -25.476 18.754  94.661  1.00 26.58 ? 517  PRO   B O     1 
ATOM   12743 C  CB    . PRO   B  1  519  ? -23.964 19.337  97.550  1.00 29.57 ? 517  PRO   B CB    1 
ATOM   12744 C  CG    . PRO   B  1  519  ? -24.151 18.552  98.800  1.00 30.29 ? 517  PRO   B CG    1 
ATOM   12745 C  CD    . PRO   B  1  519  ? -25.513 18.928  99.324  1.00 27.52 ? 517  PRO   B CD    1 
ATOM   12746 N  N     . VAL   B  1  520  ? -25.933 17.183  96.216  1.00 28.34 ? 518  VAL   B N     1 
ATOM   12747 C  CA    . VAL   B  1  520  ? -26.115 16.127  95.226  1.00 26.76 ? 518  VAL   B CA    1 
ATOM   12748 C  C     . VAL   B  1  520  ? -27.235 16.488  94.262  1.00 29.19 ? 518  VAL   B C     1 
ATOM   12749 O  O     . VAL   B  1  520  ? -27.074 16.415  93.039  1.00 28.78 ? 518  VAL   B O     1 
ATOM   12750 C  CB    . VAL   B  1  520  ? -26.374 14.779  95.918  1.00 29.00 ? 518  VAL   B CB    1 
ATOM   12751 C  CG1   . VAL   B  1  520  ? -26.498 13.667  94.878  1.00 30.89 ? 518  VAL   B CG1   1 
ATOM   12752 C  CG2   . VAL   B  1  520  ? -25.269 14.478  96.924  1.00 27.17 ? 518  VAL   B CG2   1 
ATOM   12753 N  N     . GLU   B  1  521  ? -28.383 16.903  94.798  1.00 28.73 ? 519  GLU   B N     1 
ATOM   12754 C  CA    . GLU   B  1  521  ? -29.499 17.233  93.921  1.00 28.98 ? 519  GLU   B CA    1 
ATOM   12755 C  C     . GLU   B  1  521  ? -29.267 18.534  93.168  1.00 30.01 ? 519  GLU   B C     1 
ATOM   12756 O  O     . GLU   B  1  521  ? -29.721 18.675  92.026  1.00 33.22 ? 519  GLU   B O     1 
ATOM   12757 C  CB    . GLU   B  1  521  ? -30.802 17.268  94.712  1.00 30.08 ? 519  GLU   B CB    1 
ATOM   12758 C  CG    . GLU   B  1  521  ? -31.146 15.925  95.316  1.00 33.46 ? 519  GLU   B CG    1 
ATOM   12759 C  CD    . GLU   B  1  521  ? -31.216 14.814  94.278  1.00 40.16 ? 519  GLU   B CD    1 
ATOM   12760 O  OE1   . GLU   B  1  521  ? -31.617 15.090  93.129  1.00 45.01 ? 519  GLU   B OE1   1 
ATOM   12761 O  OE2   . GLU   B  1  521  ? -30.870 13.660  94.612  1.00 44.07 ? 519  GLU   B OE2   1 
ATOM   12762 N  N     . VAL   B  1  522  ? -28.560 19.488  93.770  1.00 31.28 ? 520  VAL   B N     1 
ATOM   12763 C  CA    . VAL   B  1  522  ? -28.248 20.716  93.046  1.00 29.08 ? 520  VAL   B CA    1 
ATOM   12764 C  C     . VAL   B  1  522  ? -27.345 20.420  91.854  1.00 32.97 ? 520  VAL   B C     1 
ATOM   12765 O  O     . VAL   B  1  522  ? -27.572 20.924  90.747  1.00 32.75 ? 520  VAL   B O     1 
ATOM   12766 C  CB    . VAL   B  1  522  ? -27.665 21.783  93.989  1.00 31.40 ? 520  VAL   B CB    1 
ATOM   12767 C  CG1   . VAL   B  1  522  ? -27.300 23.037  93.209  1.00 34.16 ? 520  VAL   B CG1   1 
ATOM   12768 C  CG2   . VAL   B  1  522  ? -28.659 22.116  95.091  1.00 36.35 ? 520  VAL   B CG2   1 
ATOM   12769 N  N     . VAL   B  1  523  ? -26.322 19.579  92.048  1.00 27.37 ? 521  VAL   B N     1 
ATOM   12770 C  CA    . VAL   B  1  523  ? -25.452 19.210  90.933  1.00 27.24 ? 521  VAL   B CA    1 
ATOM   12771 C  C     . VAL   B  1  523  ? -26.227 18.443  89.871  1.00 29.14 ? 521  VAL   B C     1 
ATOM   12772 O  O     . VAL   B  1  523  ? -26.057 18.677  88.669  1.00 31.04 ? 521  VAL   B O     1 
ATOM   12773 C  CB    . VAL   B  1  523  ? -24.231 18.414  91.428  1.00 28.65 ? 521  VAL   B CB    1 
ATOM   12774 C  CG1   . VAL   B  1  523  ? -23.521 17.758  90.255  1.00 28.92 ? 521  VAL   B CG1   1 
ATOM   12775 C  CG2   . VAL   B  1  523  ? -23.287 19.322  92.182  1.00 31.61 ? 521  VAL   B CG2   1 
ATOM   12776 N  N     . ARG   B  1  524  ? -27.065 17.496  90.297  1.00 31.27 ? 522  ARG   B N     1 
ATOM   12777 C  CA    . ARG   B  1  524  ? -27.805 16.673  89.346  1.00 33.90 ? 522  ARG   B CA    1 
ATOM   12778 C  C     . ARG   B  1  524  ? -28.645 17.523  88.403  1.00 34.02 ? 522  ARG   B C     1 
ATOM   12779 O  O     . ARG   B  1  524  ? -28.842 17.150  87.242  1.00 36.39 ? 522  ARG   B O     1 
ATOM   12780 C  CB    . ARG   B  1  524  ? -28.703 15.690  90.097  1.00 34.58 ? 522  ARG   B CB    1 
ATOM   12781 C  CG    . ARG   B  1  524  ? -29.396 14.681  89.200  1.00 39.15 ? 522  ARG   B CG    1 
ATOM   12782 C  CD    . ARG   B  1  524  ? -30.568 14.012  89.904  1.00 36.49 ? 522  ARG   B CD    1 
ATOM   12783 N  NE    . ARG   B  1  524  ? -30.197 13.489  91.213  1.00 36.25 ? 522  ARG   B NE    1 
ATOM   12784 C  CZ    . ARG   B  1  524  ? -29.570 12.337  91.409  1.00 41.23 ? 522  ARG   B CZ    1 
ATOM   12785 N  NH1   . ARG   B  1  524  ? -29.205 11.565  90.397  1.00 35.70 ? 522  ARG   B NH1   1 
ATOM   12786 N  NH2   . ARG   B  1  524  ? -29.298 11.949  92.654  1.00 38.44 ? 522  ARG   B NH2   1 
ATOM   12787 N  N     . ALA   B  1  525  ? -29.122 18.673  88.871  1.00 32.57 ? 523  ALA   B N     1 
ATOM   12788 C  CA    . ALA   B  1  525  ? -30.045 19.498  88.105  1.00 37.45 ? 523  ALA   B CA    1 
ATOM   12789 C  C     . ALA   B  1  525  ? -29.353 20.554  87.258  1.00 38.59 ? 523  ALA   B C     1 
ATOM   12790 O  O     . ALA   B  1  525  ? -30.036 21.299  86.549  1.00 40.13 ? 523  ALA   B O     1 
ATOM   12791 C  CB    . ALA   B  1  525  ? -31.064 20.162  89.037  1.00 33.69 ? 523  ALA   B CB    1 
ATOM   12792 N  N     . MET   B  1  526  ? -28.029 20.639  87.310  1.00 36.57 ? 524  MET   B N     1 
ATOM   12793 C  CA    A MET   B  1  526  ? -27.301 21.600  86.496  0.50 36.45 ? 524  MET   B CA    1 
ATOM   12794 C  CA    B MET   B  1  526  ? -27.336 21.615  86.496  0.50 36.45 ? 524  MET   B CA    1 
ATOM   12795 C  C     . MET   B  1  526  ? -27.382 21.200  85.025  1.00 32.29 ? 524  MET   B C     1 
ATOM   12796 O  O     . MET   B  1  526  ? -27.446 20.010  84.706  1.00 34.19 ? 524  MET   B O     1 
ATOM   12797 C  CB    A MET   B  1  526  ? -25.836 21.630  86.917  0.50 36.41 ? 524  MET   B CB    1 
ATOM   12798 C  CB    B MET   B  1  526  ? -25.897 21.772  86.975  0.50 36.46 ? 524  MET   B CB    1 
ATOM   12799 C  CG    A MET   B  1  526  ? -25.620 22.175  88.309  0.50 38.50 ? 524  MET   B CG    1 
ATOM   12800 C  CG    B MET   B  1  526  ? -25.828 22.262  88.412  0.50 38.43 ? 524  MET   B CG    1 
ATOM   12801 S  SD    A MET   B  1  526  ? -26.281 23.842  88.457  0.50 44.08 ? 524  MET   B SD    1 
ATOM   12802 S  SD    B MET   B  1  526  ? -24.163 22.410  89.079  0.50 39.41 ? 524  MET   B SD    1 
ATOM   12803 C  CE    A MET   B  1  526  ? -25.262 24.722  87.274  0.50 37.13 ? 524  MET   B CE    1 
ATOM   12804 C  CE    B MET   B  1  526  ? -23.729 24.073  88.589  0.50 35.17 ? 524  MET   B CE    1 
ATOM   12805 N  N     . PRO   B  1  527  ? -27.379 22.173  84.107  1.00 39.09 ? 525  PRO   B N     1 
ATOM   12806 C  CA    . PRO   B  1  527  ? -27.487 21.818  82.680  1.00 41.02 ? 525  PRO   B CA    1 
ATOM   12807 C  C     . PRO   B  1  527  ? -26.362 20.922  82.196  1.00 37.81 ? 525  PRO   B C     1 
ATOM   12808 O  O     . PRO   B  1  527  ? -26.597 20.025  81.377  1.00 34.59 ? 525  PRO   B O     1 
ATOM   12809 C  CB    . PRO   B  1  527  ? -27.490 23.183  81.977  1.00 41.57 ? 525  PRO   B CB    1 
ATOM   12810 C  CG    . PRO   B  1  527  ? -26.796 24.093  82.927  1.00 42.13 ? 525  PRO   B CG    1 
ATOM   12811 C  CD    . PRO   B  1  527  ? -27.186 23.621  84.300  1.00 40.39 ? 525  PRO   B CD    1 
ATOM   12812 N  N     . VAL   B  1  528  ? -25.146 21.135  82.687  1.00 35.65 ? 526  VAL   B N     1 
ATOM   12813 C  CA    . VAL   B  1  528  ? -23.999 20.298  82.362  1.00 30.41 ? 526  VAL   B CA    1 
ATOM   12814 C  C     . VAL   B  1  528  ? -23.440 19.821  83.695  1.00 28.60 ? 526  VAL   B C     1 
ATOM   12815 O  O     . VAL   B  1  528  ? -22.774 20.585  84.405  1.00 32.10 ? 526  VAL   B O     1 
ATOM   12816 C  CB    . VAL   B  1  528  ? -22.937 21.054  81.554  1.00 29.44 ? 526  VAL   B CB    1 
ATOM   12817 C  CG1   . VAL   B  1  528  ? -21.691 20.190  81.370  1.00 30.69 ? 526  VAL   B CG1   1 
ATOM   12818 C  CG2   . VAL   B  1  528  ? -23.497 21.475  80.203  1.00 32.76 ? 526  VAL   B CG2   1 
ATOM   12819 N  N     . VAL   B  1  529  ? -23.696 18.562  84.037  1.00 25.83 ? 527  VAL   B N     1 
ATOM   12820 C  CA    . VAL   B  1  529  ? -23.230 18.036  85.316  1.00 23.85 ? 527  VAL   B CA    1 
ATOM   12821 C  C     . VAL   B  1  529  ? -21.709 18.089  85.359  1.00 26.61 ? 527  VAL   B C     1 
ATOM   12822 O  O     . VAL   B  1  529  ? -21.025 17.572  84.467  1.00 26.88 ? 527  VAL   B O     1 
ATOM   12823 C  CB    . VAL   B  1  529  ? -23.757 16.619  85.544  1.00 26.51 ? 527  VAL   B CB    1 
ATOM   12824 C  CG1   . VAL   B  1  529  ? -23.120 16.016  86.778  1.00 27.47 ? 527  VAL   B CG1   1 
ATOM   12825 C  CG2   . VAL   B  1  529  ? -25.287 16.639  85.679  1.00 28.66 ? 527  VAL   B CG2   1 
ATOM   12826 N  N     . GLY   B  1  530  ? -21.173 18.747  86.384  1.00 23.30 ? 528  GLY   B N     1 
ATOM   12827 C  CA    . GLY   B  1  530  ? -19.743 18.771  86.589  1.00 23.46 ? 528  GLY   B CA    1 
ATOM   12828 C  C     . GLY   B  1  530  ? -18.987 19.821  85.814  1.00 23.23 ? 528  GLY   B C     1 
ATOM   12829 O  O     . GLY   B  1  530  ? -17.762 19.735  85.726  1.00 22.67 ? 528  GLY   B O     1 
ATOM   12830 N  N     . ALA   B  1  531  ? -19.671 20.817  85.256  1.00 22.51 ? 529  ALA   B N     1 
ATOM   12831 C  CA    . ALA   B  1  531  ? -18.970 21.884  84.557  1.00 21.23 ? 529  ALA   B CA    1 
ATOM   12832 C  C     . ALA   B  1  531  ? -18.006 22.599  85.497  1.00 21.32 ? 529  ALA   B C     1 
ATOM   12833 O  O     . ALA   B  1  531  ? -18.319 22.844  86.665  1.00 24.22 ? 529  ALA   B O     1 
ATOM   12834 C  CB    . ALA   B  1  531  ? -19.971 22.883  83.980  1.00 27.46 ? 529  ALA   B CB    1 
ATOM   12835 N  N     . LYS   B  1  532  ? -16.819 22.910  84.980  1.00 19.31 ? 530  LYS   B N     1 
ATOM   12836 C  CA    . LYS   B  1  532  ? -15.834 23.691  85.713  1.00 20.75 ? 530  LYS   B CA    1 
ATOM   12837 C  C     . LYS   B  1  532  ? -16.442 25.019  86.145  1.00 21.77 ? 530  LYS   B C     1 
ATOM   12838 O  O     . LYS   B  1  532  ? -17.369 25.537  85.517  1.00 23.02 ? 530  LYS   B O     1 
ATOM   12839 C  CB    . LYS   B  1  532  ? -14.636 23.956  84.791  1.00 23.13 ? 530  LYS   B CB    1 
ATOM   12840 C  CG    . LYS   B  1  532  ? -13.583 24.940  85.299  1.00 25.43 ? 530  LYS   B CG    1 
ATOM   12841 C  CD    . LYS   B  1  532  ? -12.512 25.230  84.240  1.00 23.12 ? 530  LYS   B CD    1 
ATOM   12842 C  CE    . LYS   B  1  532  ? -13.032 26.010  83.037  1.00 21.18 ? 530  LYS   B CE    1 
ATOM   12843 N  NZ    . LYS   B  1  532  ? -13.456 27.423  83.348  1.00 22.92 ? 530  LYS   B NZ    1 
ATOM   12844 N  N     . HIS   B  1  533  ? -15.931 25.552  87.247  1.00 20.56 ? 531  HIS   B N     1 
ATOM   12845 C  CA    . HIS   B  1  533  ? -16.311 26.885  87.680  1.00 20.31 ? 531  HIS   B CA    1 
ATOM   12846 C  C     . HIS   B  1  533  ? -16.111 27.877  86.542  1.00 19.80 ? 531  HIS   B C     1 
ATOM   12847 O  O     . HIS   B  1  533  ? -15.064 27.886  85.890  1.00 21.52 ? 531  HIS   B O     1 
ATOM   12848 C  CB    . HIS   B  1  533  ? -15.436 27.280  88.862  1.00 21.48 ? 531  HIS   B CB    1 
ATOM   12849 C  CG    . HIS   B  1  533  ? -15.983 28.415  89.665  1.00 24.46 ? 531  HIS   B CG    1 
ATOM   12850 N  ND1   . HIS   B  1  533  ? -16.106 29.691  89.159  1.00 25.21 ? 531  HIS   B ND1   1 
ATOM   12851 C  CD2   . HIS   B  1  533  ? -16.445 28.469  90.937  1.00 29.70 ? 531  HIS   B CD2   1 
ATOM   12852 C  CE1   . HIS   B  1  533  ? -16.620 30.482  90.082  1.00 29.82 ? 531  HIS   B CE1   1 
ATOM   12853 N  NE2   . HIS   B  1  533  ? -16.837 29.766  91.171  1.00 35.40 ? 531  HIS   B NE2   1 
ATOM   12854 N  N     . ASP   B  1  534  ? -17.127 28.712  86.314  1.00 22.46 ? 532  ASP   B N     1 
ATOM   12855 C  CA    . ASP   B  1  534  ? -17.096 29.663  85.207  1.00 27.52 ? 532  ASP   B CA    1 
ATOM   12856 C  C     . ASP   B  1  534  ? -16.003 30.708  85.354  1.00 25.02 ? 532  ASP   B C     1 
ATOM   12857 O  O     . ASP   B  1  534  ? -15.592 31.300  84.350  1.00 26.76 ? 532  ASP   B O     1 
ATOM   12858 C  CB    . ASP   B  1  534  ? -18.442 30.380  85.100  1.00 29.09 ? 532  ASP   B CB    1 
ATOM   12859 C  CG    . ASP   B  1  534  ? -19.545 29.469  84.631  1.00 42.90 ? 532  ASP   B CG    1 
ATOM   12860 O  OD1   . ASP   B  1  534  ? -19.294 28.685  83.690  1.00 41.99 ? 532  ASP   B OD1   1 
ATOM   12861 O  OD2   . ASP   B  1  534  ? -20.655 29.534  85.204  1.00 49.73 ? 532  ASP   B OD2   1 
ATOM   12862 N  N     . ARG   B  1  535  ? -15.519 30.949  86.569  1.00 22.60 ? 533  ARG   B N     1 
ATOM   12863 C  CA    . ARG   B  1  535  ? -14.578 32.027  86.828  1.00 22.94 ? 533  ARG   B CA    1 
ATOM   12864 C  C     . ARG   B  1  535  ? -13.172 31.536  87.144  1.00 23.88 ? 533  ARG   B C     1 
ATOM   12865 O  O     . ARG   B  1  535  ? -12.347 32.328  87.607  1.00 26.16 ? 533  ARG   B O     1 
ATOM   12866 C  CB    . ARG   B  1  535  ? -15.090 32.920  87.961  1.00 27.49 ? 533  ARG   B CB    1 
ATOM   12867 N  N     . ILE   B  1  536  ? -12.880 30.257  86.925  1.00 20.56 ? 534  ILE   B N     1 
ATOM   12868 C  CA    . ILE   B  1  536  ? -11.545 29.706  87.130  1.00 18.90 ? 534  ILE   B CA    1 
ATOM   12869 C  C     . ILE   B  1  536  ? -11.085 29.168  85.788  1.00 18.04 ? 534  ILE   B C     1 
ATOM   12870 O  O     . ILE   B  1  536  ? -11.740 28.293  85.208  1.00 20.24 ? 534  ILE   B O     1 
ATOM   12871 C  CB    . ILE   B  1  536  ? -11.539 28.598  88.191  1.00 18.56 ? 534  ILE   B CB    1 
ATOM   12872 C  CG1   . ILE   B  1  536  ? -11.993 29.165  89.532  1.00 20.32 ? 534  ILE   B CG1   1 
ATOM   12873 C  CG2   . ILE   B  1  536  ? -10.133 28.012  88.340  1.00 20.90 ? 534  ILE   B CG2   1 
ATOM   12874 C  CD1   . ILE   B  1  536  ? -12.122 28.106  90.591  1.00 24.95 ? 534  ILE   B CD1   1 
ATOM   12875 N  N     . ALA   B  1  537  ? -9.985  29.705  85.282  1.00 17.16 ? 535  ALA   B N     1 
ATOM   12876 C  CA    . ALA   B  1  537  ? -9.512  29.299  83.966  1.00 17.68 ? 535  ALA   B CA    1 
ATOM   12877 C  C     . ALA   B  1  537  ? -8.766  27.976  84.059  1.00 17.83 ? 535  ALA   B C     1 
ATOM   12878 O  O     . ALA   B  1  537  ? -7.941  27.781  84.956  1.00 18.23 ? 535  ALA   B O     1 
ATOM   12879 C  CB    . ALA   B  1  537  ? -8.591  30.375  83.394  1.00 20.40 ? 535  ALA   B CB    1 
ATOM   12880 N  N     . LEU   B  1  538  ? -9.051  27.064  83.135  1.00 17.98 ? 536  LEU   B N     1 
ATOM   12881 C  CA    . LEU   B  1  538  ? -8.130  25.958  82.940  1.00 19.04 ? 536  LEU   B CA    1 
ATOM   12882 C  C     . LEU   B  1  538  ? -6.747  26.521  82.631  1.00 16.89 ? 536  LEU   B C     1 
ATOM   12883 O  O     . LEU   B  1  538  ? -6.628  27.608  82.053  1.00 18.75 ? 536  LEU   B O     1 
ATOM   12884 C  CB    . LEU   B  1  538  ? -8.568  25.100  81.760  1.00 19.78 ? 536  LEU   B CB    1 
ATOM   12885 C  CG    . LEU   B  1  538  ? -9.743  24.163  82.008  1.00 21.34 ? 536  LEU   B CG    1 
ATOM   12886 C  CD1   . LEU   B  1  538  ? -10.162 23.534  80.693  1.00 26.09 ? 536  LEU   B CD1   1 
ATOM   12887 C  CD2   . LEU   B  1  538  ? -9.389  23.091  83.039  1.00 21.04 ? 536  LEU   B CD2   1 
ATOM   12888 N  N     . PRO   B  1  539  ? -5.683  25.811  83.007  1.00 15.38 ? 537  PRO   B N     1 
ATOM   12889 C  CA    . PRO   B  1  539  ? -4.339  26.315  82.688  1.00 16.58 ? 537  PRO   B CA    1 
ATOM   12890 C  C     . PRO   B  1  539  ? -4.182  26.691  81.229  1.00 16.79 ? 537  PRO   B C     1 
ATOM   12891 O  O     . PRO   B  1  539  ? -3.604  27.742  80.938  1.00 16.85 ? 537  PRO   B O     1 
ATOM   12892 C  CB    . PRO   B  1  539  ? -3.421  25.173  83.139  1.00 17.11 ? 537  PRO   B CB    1 
ATOM   12893 C  CG    . PRO   B  1  539  ? -4.200  24.540  84.297  1.00 16.04 ? 537  PRO   B CG    1 
ATOM   12894 C  CD    . PRO   B  1  539  ? -5.639  24.581  83.818  1.00 16.63 ? 537  PRO   B CD    1 
ATOM   12895 N  N     . ALA   B  1  540  ? -4.733  25.898  80.311  1.00 17.06 ? 538  ALA   B N     1 
ATOM   12896 C  CA    . ALA   B  1  540  ? -4.599  26.210  78.895  1.00 19.57 ? 538  ALA   B CA    1 
ATOM   12897 C  C     . ALA   B  1  540  ? -5.301  27.504  78.527  1.00 21.27 ? 538  ALA   B C     1 
ATOM   12898 O  O     . ALA   B  1  540  ? -4.972  28.102  77.495  1.00 18.41 ? 538  ALA   B O     1 
ATOM   12899 C  CB    . ALA   B  1  540  ? -5.178  25.072  78.051  1.00 19.71 ? 538  ALA   B CB    1 
ATOM   12900 N  N     . GLU   B  1  541  ? -6.257  27.949  79.345  1.00 19.63 ? 539  GLU   B N     1 
ATOM   12901 C  CA    . GLU   B  1  541  ? -7.135  29.057  78.994  1.00 18.49 ? 539  GLU   B CA    1 
ATOM   12902 C  C     . GLU   B  1  541  ? -6.826  30.329  79.783  1.00 16.55 ? 539  GLU   B C     1 
ATOM   12903 O  O     . GLU   B  1  541  ? -7.636  31.258  79.799  1.00 18.81 ? 539  GLU   B O     1 
ATOM   12904 C  CB    . GLU   B  1  541  ? -8.600  28.617  79.102  1.00 21.51 ? 539  GLU   B CB    1 
ATOM   12905 C  CG    . GLU   B  1  541  ? -8.912  27.527  78.049  1.00 25.44 ? 539  GLU   B CG    1 
ATOM   12906 C  CD    . GLU   B  1  541  ? -10.275 26.842  78.173  1.00 34.55 ? 539  GLU   B CD    1 
ATOM   12907 O  OE1   . GLU   B  1  541  ? -11.086 27.200  79.049  1.00 35.80 ? 539  GLU   B OE1   1 
ATOM   12908 O  OE2   . GLU   B  1  541  ? -10.530 25.920  77.370  1.00 37.94 ? 539  GLU   B OE2   1 
ATOM   12909 N  N     . LEU   B  1  542  ? -5.632  30.419  80.377  1.00 17.09 ? 540  LEU   B N     1 
ATOM   12910 C  CA    . LEU   B  1  542  ? -5.300  31.589  81.190  1.00 18.18 ? 540  LEU   B CA    1 
ATOM   12911 C  C     . LEU   B  1  542  ? -5.424  32.896  80.420  1.00 17.65 ? 540  LEU   B C     1 
ATOM   12912 O  O     . LEU   B  1  542  ? -5.696  33.943  81.020  1.00 20.63 ? 540  LEU   B O     1 
ATOM   12913 C  CB    . LEU   B  1  542  ? -3.868  31.487  81.698  1.00 19.59 ? 540  LEU   B CB    1 
ATOM   12914 C  CG    . LEU   B  1  542  ? -3.550  30.589  82.877  1.00 22.22 ? 540  LEU   B CG    1 
ATOM   12915 C  CD1   . LEU   B  1  542  ? -2.109  30.859  83.329  1.00 19.92 ? 540  LEU   B CD1   1 
ATOM   12916 C  CD2   . LEU   B  1  542  ? -4.522  30.814  84.004  1.00 20.86 ? 540  LEU   B CD2   1 
ATOM   12917 N  N     . PHE   B  1  543  ? -5.200  32.870  79.110  1.00 17.00 ? 541  PHE   B N     1 
ATOM   12918 C  CA    . PHE   B  1  543  ? -5.200  34.086  78.306  1.00 19.31 ? 541  PHE   B CA    1 
ATOM   12919 C  C     . PHE   B  1  543  ? -6.466  34.235  77.485  1.00 19.63 ? 541  PHE   B C     1 
ATOM   12920 O  O     . PHE   B  1  543  ? -6.539  35.116  76.621  1.00 20.17 ? 541  PHE   B O     1 
ATOM   12921 C  CB    . PHE   B  1  543  ? -3.943  34.139  77.438  1.00 17.62 ? 541  PHE   B CB    1 
ATOM   12922 C  CG    . PHE   B  1  543  ? -2.707  33.893  78.224  1.00 19.89 ? 541  PHE   B CG    1 
ATOM   12923 C  CD1   . PHE   B  1  543  ? -2.430  34.677  79.337  1.00 20.81 ? 541  PHE   B CD1   1 
ATOM   12924 C  CD2   . PHE   B  1  543  ? -1.869  32.850  77.914  1.00 17.99 ? 541  PHE   B CD2   1 
ATOM   12925 C  CE1   . PHE   B  1  543  ? -1.307  34.440  80.101  1.00 20.71 ? 541  PHE   B CE1   1 
ATOM   12926 C  CE2   . PHE   B  1  543  ? -0.739  32.613  78.662  1.00 18.49 ? 541  PHE   B CE2   1 
ATOM   12927 C  CZ    . PHE   B  1  543  ? -0.453  33.404  79.758  1.00 21.62 ? 541  PHE   B CZ    1 
ATOM   12928 N  N     . GLY   B  1  544  ? -7.464  33.397  77.743  1.00 20.70 ? 542  GLY   B N     1 
ATOM   12929 C  CA    . GLY   B  1  544  ? -8.742  33.526  77.070  1.00 20.46 ? 542  GLY   B CA    1 
ATOM   12930 C  C     . GLY   B  1  544  ? -8.594  33.407  75.570  1.00 22.06 ? 542  GLY   B C     1 
ATOM   12931 O  O     . GLY   B  1  544  ? -7.834  32.579  75.052  1.00 23.78 ? 542  GLY   B O     1 
ATOM   12932 N  N     . ASP   B  1  545  ? -9.328  34.259  74.856  1.00 25.23 ? 543  ASP   B N     1 
ATOM   12933 C  CA    . ASP   B  1  545  ? -9.364  34.200  73.402  1.00 29.51 ? 543  ASP   B CA    1 
ATOM   12934 C  C     . ASP   B  1  545  ? -8.071  34.669  72.748  1.00 24.80 ? 543  ASP   B C     1 
ATOM   12935 O  O     . ASP   B  1  545  ? -7.906  34.452  71.544  1.00 24.89 ? 543  ASP   B O     1 
ATOM   12936 C  CB    . ASP   B  1  545  ? -10.526 35.051  72.882  1.00 27.58 ? 543  ASP   B CB    1 
ATOM   12937 C  CG    . ASP   B  1  545  ? -11.872 34.576  73.395  1.00 41.99 ? 543  ASP   B CG    1 
ATOM   12938 O  OD1   . ASP   B  1  545  ? -12.031 33.354  73.617  1.00 41.16 ? 543  ASP   B OD1   1 
ATOM   12939 O  OD2   . ASP   B  1  545  ? -12.773 35.425  73.569  1.00 48.44 ? 543  ASP   B OD2   1 
ATOM   12940 N  N     . ALA   B  1  546  ? -7.161  35.301  73.496  1.00 23.63 ? 544  ALA   B N     1 
ATOM   12941 C  CA    . ALA   B  1  546  ? -5.965  35.865  72.872  1.00 21.12 ? 544  ALA   B CA    1 
ATOM   12942 C  C     . ALA   B  1  546  ? -5.048  34.775  72.339  1.00 22.74 ? 544  ALA   B C     1 
ATOM   12943 O  O     . ALA   B  1  546  ? -4.511  34.892  71.230  1.00 21.55 ? 544  ALA   B O     1 
ATOM   12944 C  CB    . ALA   B  1  546  ? -5.203  36.749  73.861  1.00 21.81 ? 544  ALA   B CB    1 
ATOM   12945 N  N     . ARG   B  1  547  ? -4.850  33.714  73.114  1.00 20.53 ? 545  ARG   B N     1 
ATOM   12946 C  CA    . ARG   B  1  547  ? -3.957  32.645  72.706  1.00 19.58 ? 545  ARG   B CA    1 
ATOM   12947 C  C     . ARG   B  1  547  ? -4.082  31.514  73.707  1.00 19.37 ? 545  ARG   B C     1 
ATOM   12948 O  O     . ARG   B  1  547  ? -4.627  31.678  74.805  1.00 18.60 ? 545  ARG   B O     1 
ATOM   12949 C  CB    . ARG   B  1  547  ? -2.504  33.111  72.631  1.00 23.12 ? 545  ARG   B CB    1 
ATOM   12950 C  CG    . ARG   B  1  547  ? -1.976  33.610  73.938  1.00 16.92 ? 545  ARG   B CG    1 
ATOM   12951 C  CD    . ARG   B  1  547  ? -0.522  34.077  73.787  1.00 18.90 ? 545  ARG   B CD    1 
ATOM   12952 N  NE    . ARG   B  1  547  ? -0.195  34.931  74.910  1.00 18.19 ? 545  ARG   B NE    1 
ATOM   12953 C  CZ    . ARG   B  1  547  ? 0.582   34.581  75.926  1.00 19.81 ? 545  ARG   B CZ    1 
ATOM   12954 N  NH1   . ARG   B  1  547  ? 1.202   33.412  75.953  1.00 17.35 ? 545  ARG   B NH1   1 
ATOM   12955 N  NH2   . ARG   B  1  547  ? 0.735   35.425  76.941  1.00 20.52 ? 545  ARG   B NH2   1 
ATOM   12956 N  N     . THR   B  1  548  ? -3.579  30.364  73.301  1.00 16.86 ? 546  THR   B N     1 
ATOM   12957 C  CA    . THR   B  1  548  ? -3.581  29.184  74.143  1.00 16.80 ? 546  THR   B CA    1 
ATOM   12958 C  C     . THR   B  1  548  ? -2.279  29.141  74.926  1.00 15.72 ? 546  THR   B C     1 
ATOM   12959 O  O     . THR   B  1  548  ? -1.199  29.297  74.356  1.00 15.43 ? 546  THR   B O     1 
ATOM   12960 C  CB    . THR   B  1  548  ? -3.668  27.952  73.255  1.00 18.26 ? 546  THR   B CB    1 
ATOM   12961 O  OG1   . THR   B  1  548  ? -4.881  28.012  72.486  1.00 22.54 ? 546  THR   B OG1   1 
ATOM   12962 C  CG2   . THR   B  1  548  ? -3.634  26.697  74.108  1.00 18.90 ? 546  THR   B CG2   1 
ATOM   12963 N  N     . ASN   B  1  549  ? -2.389  28.944  76.233  1.00 14.50 ? 547  ASN   B N     1 
ATOM   12964 C  CA    . ASN   B  1  549  ? -1.217  28.859  77.077  1.00 14.39 ? 547  ASN   B CA    1 
ATOM   12965 C  C     . ASN   B  1  549  ? -0.441  27.592  76.747  1.00 14.28 ? 547  ASN   B C     1 
ATOM   12966 O  O     . ASN   B  1  549  ? -1.025  26.559  76.405  1.00 17.21 ? 547  ASN   B O     1 
ATOM   12967 C  CB    . ASN   B  1  549  ? -1.683  28.832  78.530  1.00 15.94 ? 547  ASN   B CB    1 
ATOM   12968 C  CG    . ASN   B  1  549  ? -0.543  28.972  79.511  1.00 14.44 ? 547  ASN   B CG    1 
ATOM   12969 O  OD1   . ASN   B  1  549  ? 0.546   29.423  79.175  1.00 15.73 ? 547  ASN   B OD1   1 
ATOM   12970 N  ND2   . ASN   B  1  549  ? -0.817  28.611  80.755  1.00 15.99 ? 547  ASN   B ND2   1 
ATOM   12971 N  N     . SER   B  1  550  ? 0.887   27.685  76.802  1.00 14.87 ? 548  SER   B N     1 
ATOM   12972 C  CA    . SER   B  1  550  ? 1.688   26.481  76.638  1.00 15.34 ? 548  SER   B CA    1 
ATOM   12973 C  C     . SER   B  1  550  ? 1.374   25.492  77.752  1.00 14.55 ? 548  SER   B C     1 
ATOM   12974 O  O     . SER   B  1  550  ? 0.988   25.865  78.863  1.00 16.48 ? 548  SER   B O     1 
ATOM   12975 C  CB    . SER   B  1  550  ? 3.175   26.807  76.679  1.00 14.44 ? 548  SER   B CB    1 
ATOM   12976 O  OG    . SER   B  1  550  ? 3.526   27.314  77.952  1.00 16.78 ? 548  SER   B OG    1 
ATOM   12977 N  N     . ALA   B  1  551  ? 1.516   24.215  77.433  1.00 17.86 ? 549  ALA   B N     1 
ATOM   12978 C  CA    . ALA   B  1  551  ? 1.265   23.158  78.400  1.00 17.28 ? 549  ALA   B CA    1 
ATOM   12979 C  C     . ALA   B  1  551  ? 2.578   22.549  78.862  1.00 17.39 ? 549  ALA   B C     1 
ATOM   12980 O  O     . ALA   B  1  551  ? 3.514   22.383  78.074  1.00 17.78 ? 549  ALA   B O     1 
ATOM   12981 C  CB    . ALA   B  1  551  ? 0.380   22.071  77.796  1.00 20.12 ? 549  ALA   B CB    1 
ATOM   12982 N  N     . GLY   B  1  552  ? 2.644   22.230  80.147  1.00 17.12 ? 550  GLY   B N     1 
ATOM   12983 C  CA    . GLY   B  1  552  ? 3.769   21.535  80.712  1.00 18.97 ? 550  GLY   B CA    1 
ATOM   12984 C  C     . GLY   B  1  552  ? 3.522   20.044  80.785  1.00 17.19 ? 550  GLY   B C     1 
ATOM   12985 O  O     . GLY   B  1  552  ? 2.657   19.487  80.100  1.00 18.68 ? 550  GLY   B O     1 
ATOM   12986 N  N     . LEU   B  1  553  ? 4.314   19.388  81.613  1.00 19.89 ? 551  LEU   B N     1 
ATOM   12987 C  CA    . LEU   B  1  553  ? 4.184   17.963  81.861  1.00 20.51 ? 551  LEU   B CA    1 
ATOM   12988 C  C     . LEU   B  1  553  ? 4.220   17.770  83.361  1.00 18.02 ? 551  LEU   B C     1 
ATOM   12989 O  O     . LEU   B  1  553  ? 4.977   18.450  84.057  1.00 20.25 ? 551  LEU   B O     1 
ATOM   12990 C  CB    . LEU   B  1  553  ? 5.342   17.187  81.223  1.00 20.85 ? 551  LEU   B CB    1 
ATOM   12991 C  CG    . LEU   B  1  553  ? 5.355   17.195  79.696  1.00 21.26 ? 551  LEU   B CG    1 
ATOM   12992 C  CD1   . LEU   B  1  553  ? 6.668   16.659  79.185  1.00 25.60 ? 551  LEU   B CD1   1 
ATOM   12993 C  CD2   . LEU   B  1  553  ? 4.214   16.360  79.153  1.00 24.96 ? 551  LEU   B CD2   1 
ATOM   12994 N  N     . ASP   B  1  554  ? 3.398   16.850  83.852  1.00 19.33 ? 552  ASP   B N     1 
ATOM   12995 C  CA    . ASP   B  1  554  ? 3.269   16.629  85.289  1.00 17.26 ? 552  ASP   B CA    1 
ATOM   12996 C  C     . ASP   B  1  554  ? 4.284   15.572  85.706  1.00 18.46 ? 552  ASP   B C     1 
ATOM   12997 O  O     . ASP   B  1  554  ? 4.074   14.376  85.491  1.00 19.22 ? 552  ASP   B O     1 
ATOM   12998 C  CB    . ASP   B  1  554  ? 1.848   16.198  85.619  1.00 20.39 ? 552  ASP   B CB    1 
ATOM   12999 C  CG    . ASP   B  1  554  ? 1.640   15.991  87.100  1.00 19.84 ? 552  ASP   B CG    1 
ATOM   13000 O  OD1   . ASP   B  1  554  ? 2.602   16.200  87.881  1.00 21.40 ? 552  ASP   B OD1   1 
ATOM   13001 O  OD2   . ASP   B  1  554  ? 0.516   15.614  87.478  1.00 22.93 ? 552  ASP   B OD2   1 
ATOM   13002 N  N     . LEU   B  1  555  ? 5.379   16.014  86.321  1.00 17.74 ? 553  LEU   B N     1 
ATOM   13003 C  CA    . LEU   B  1  555  ? 6.444   15.103  86.720  1.00 19.02 ? 553  LEU   B CA    1 
ATOM   13004 C  C     . LEU   B  1  555  ? 6.123   14.347  88.000  1.00 21.25 ? 553  LEU   B C     1 
ATOM   13005 O  O     . LEU   B  1  555  ? 6.981   13.629  88.516  1.00 19.31 ? 553  LEU   B O     1 
ATOM   13006 C  CB    . LEU   B  1  555  ? 7.781   15.839  86.817  1.00 18.24 ? 553  LEU   B CB    1 
ATOM   13007 C  CG    . LEU   B  1  555  ? 8.241   16.479  85.500  1.00 19.88 ? 553  LEU   B CG    1 
ATOM   13008 C  CD1   . LEU   B  1  555  ? 9.643   17.045  85.671  1.00 22.35 ? 553  LEU   B CD1   1 
ATOM   13009 C  CD2   . LEU   B  1  555  ? 8.205   15.486  84.342  1.00 23.98 ? 553  LEU   B CD2   1 
ATOM   13010 N  N     . SER   B  1  556  ? 4.907   14.488  88.523  1.00 19.93 ? 554  SER   B N     1 
ATOM   13011 C  CA    . SER   B  1  556  ? 4.433   13.618  89.584  1.00 20.14 ? 554  SER   B CA    1 
ATOM   13012 C  C     . SER   B  1  556  ? 3.478   12.554  89.078  1.00 19.78 ? 554  SER   B C     1 
ATOM   13013 O  O     . SER   B  1  556  ? 3.001   11.739  89.867  1.00 20.45 ? 554  SER   B O     1 
ATOM   13014 C  CB    . SER   B  1  556  ? 3.739   14.438  90.679  1.00 21.63 ? 554  SER   B CB    1 
ATOM   13015 O  OG    . SER   B  1  556  ? 2.463   14.869  90.219  1.00 21.33 ? 554  SER   B OG    1 
ATOM   13016 N  N     . ASN   B  1  557  ? 3.184   12.535  87.785  1.00 18.18 ? 555  ASN   B N     1 
ATOM   13017 C  CA    . ASN   B  1  557  ? 2.244   11.583  87.222  1.00 19.52 ? 555  ASN   B CA    1 
ATOM   13018 C  C     . ASN   B  1  557  ? 3.041   10.399  86.689  1.00 19.87 ? 555  ASN   B C     1 
ATOM   13019 O  O     . ASN   B  1  557  ? 3.918   10.576  85.839  1.00 18.96 ? 555  ASN   B O     1 
ATOM   13020 C  CB    . ASN   B  1  557  ? 1.456   12.279  86.114  1.00 19.39 ? 555  ASN   B CB    1 
ATOM   13021 C  CG    . ASN   B  1  557  ? 0.446   11.376  85.451  1.00 21.38 ? 555  ASN   B CG    1 
ATOM   13022 O  OD1   . ASN   B  1  557  ? 0.775   10.284  84.991  1.00 22.23 ? 555  ASN   B OD1   1 
ATOM   13023 N  ND2   . ASN   B  1  557  ? -0.805  11.833  85.385  1.00 21.32 ? 555  ASN   B ND2   1 
ATOM   13024 N  N     . GLU   B  1  558  ? 2.762   9.201   87.215  1.00 19.05 ? 556  GLU   B N     1 
ATOM   13025 C  CA    . GLU   B  1  558  ? 3.556   8.032   86.833  1.00 21.92 ? 556  GLU   B CA    1 
ATOM   13026 C  C     . GLU   B  1  558  ? 3.399   7.691   85.362  1.00 21.08 ? 556  GLU   B C     1 
ATOM   13027 O  O     . GLU   B  1  558  ? 4.343   7.192   84.743  1.00 20.88 ? 556  GLU   B O     1 
ATOM   13028 C  CB    . GLU   B  1  558  ? 3.208   6.806   87.674  1.00 22.69 ? 556  GLU   B CB    1 
ATOM   13029 C  CG    . GLU   B  1  558  ? 3.650   6.861   89.105  1.00 24.00 ? 556  GLU   B CG    1 
ATOM   13030 C  CD    . GLU   B  1  558  ? 5.161   6.945   89.327  1.00 26.10 ? 556  GLU   B CD    1 
ATOM   13031 O  OE1   . GLU   B  1  558  ? 5.991   6.720   88.407  1.00 24.30 ? 556  GLU   B OE1   1 
ATOM   13032 O  OE2   . GLU   B  1  558  ? 5.513   7.232   90.477  1.00 23.82 ? 556  GLU   B OE2   1 
ATOM   13033 N  N     . GLU   B  1  559  ? 2.203   7.886   84.795  1.00 20.32 ? 557  GLU   B N     1 
ATOM   13034 C  CA    . GLU   B  1  559  ? 2.042   7.659   83.361  1.00 17.52 ? 557  GLU   B CA    1 
ATOM   13035 C  C     . GLU   B  1  559  ? 2.951   8.600   82.595  1.00 20.41 ? 557  GLU   B C     1 
ATOM   13036 O  O     . GLU   B  1  559  ? 3.628   8.204   81.640  1.00 21.54 ? 557  GLU   B O     1 
ATOM   13037 C  CB    . GLU   B  1  559  ? 0.602   7.927   82.915  1.00 24.02 ? 557  GLU   B CB    1 
ATOM   13038 C  CG    . GLU   B  1  559  ? -0.483  7.058   83.478  1.00 29.12 ? 557  GLU   B CG    1 
ATOM   13039 C  CD    . GLU   B  1  559  ? -1.847  7.422   82.885  1.00 38.04 ? 557  GLU   B CD    1 
ATOM   13040 O  OE1   . GLU   B  1  559  ? -1.877  8.076   81.815  1.00 38.62 ? 557  GLU   B OE1   1 
ATOM   13041 O  OE2   . GLU   B  1  559  ? -2.884  7.066   83.488  1.00 31.76 ? 557  GLU   B OE2   1 
ATOM   13042 N  N     . THR   B  1  560  ? 2.970   9.864   83.007  1.00 18.95 ? 558  THR   B N     1 
ATOM   13043 C  CA    . THR   B  1  560  ? 3.801   10.848  82.333  1.00 18.71 ? 558  THR   B CA    1 
ATOM   13044 C  C     . THR   B  1  560  ? 5.269   10.485  82.463  1.00 20.43 ? 558  THR   B C     1 
ATOM   13045 O  O     . THR   B  1  560  ? 6.018   10.524  81.482  1.00 19.30 ? 558  THR   B O     1 
ATOM   13046 C  CB    . THR   B  1  560  ? 3.538   12.231  82.919  1.00 18.57 ? 558  THR   B CB    1 
ATOM   13047 O  OG1   . THR   B  1  560  ? 2.152   12.550  82.752  1.00 21.27 ? 558  THR   B OG1   1 
ATOM   13048 C  CG2   . THR   B  1  560  ? 4.379   13.270  82.208  1.00 20.77 ? 558  THR   B CG2   1 
ATOM   13049 N  N     . LEU   B  1  561  ? 5.695   10.110  83.671  1.00 17.31 ? 559  LEU   B N     1 
ATOM   13050 C  CA    . LEU   B  1  561  ? 7.096   9.764   83.868  1.00 17.37 ? 559  LEU   B CA    1 
ATOM   13051 C  C     . LEU   B  1  561  ? 7.483   8.559   83.028  1.00 19.87 ? 559  LEU   B C     1 
ATOM   13052 O  O     . LEU   B  1  561  ? 8.582   8.517   82.466  1.00 18.71 ? 559  LEU   B O     1 
ATOM   13053 C  CB    . LEU   B  1  561  ? 7.383   9.512   85.349  1.00 19.02 ? 559  LEU   B CB    1 
ATOM   13054 C  CG    . LEU   B  1  561  ? 7.335   10.750  86.254  1.00 16.42 ? 559  LEU   B CG    1 
ATOM   13055 C  CD1   . LEU   B  1  561  ? 7.568   10.342  87.711  1.00 19.31 ? 559  LEU   B CD1   1 
ATOM   13056 C  CD2   . LEU   B  1  561  ? 8.377   11.760  85.808  1.00 18.32 ? 559  LEU   B CD2   1 
ATOM   13057 N  N     . ALA   B  1  562  ? 6.592   7.574   82.929  1.00 18.08 ? 560  ALA   B N     1 
ATOM   13058 C  CA    . ALA   B  1  562  ? 6.888   6.383   82.145  1.00 20.41 ? 560  ALA   B CA    1 
ATOM   13059 C  C     . ALA   B  1  562  ? 7.008   6.724   80.664  1.00 22.25 ? 560  ALA   B C     1 
ATOM   13060 O  O     . ALA   B  1  562  ? 7.945   6.281   79.989  1.00 22.09 ? 560  ALA   B O     1 
ATOM   13061 C  CB    . ALA   B  1  562  ? 5.804   5.328   82.380  1.00 19.34 ? 560  ALA   B CB    1 
ATOM   13062 N  N     . SER   B  1  563  ? 6.067   7.502   80.136  1.00 19.36 ? 561  SER   B N     1 
ATOM   13063 C  CA    . SER   B  1  563  ? 6.135   7.836   78.719  1.00 19.27 ? 561  SER   B CA    1 
ATOM   13064 C  C     . SER   B  1  563  ? 7.280   8.793   78.441  1.00 21.92 ? 561  SER   B C     1 
ATOM   13065 O  O     . SER   B  1  563  ? 7.941   8.700   77.396  1.00 21.19 ? 561  SER   B O     1 
ATOM   13066 C  CB    . SER   B  1  563  ? 4.798   8.397   78.225  1.00 23.10 ? 561  SER   B CB    1 
ATOM   13067 O  OG    . SER   B  1  563  ? 4.522   9.660   78.794  1.00 27.75 ? 561  SER   B OG    1 
ATOM   13068 N  N     . LEU   B  1  564  ? 7.536   9.718   79.369  1.00 18.51 ? 562  LEU   B N     1 
ATOM   13069 C  CA    . LEU   B  1  564  ? 8.652   10.635  79.190  1.00 17.90 ? 562  LEU   B CA    1 
ATOM   13070 C  C     . LEU   B  1  564  ? 9.973   9.889   79.224  1.00 20.28 ? 562  LEU   B C     1 
ATOM   13071 O  O     . LEU   B  1  564  ? 10.862  10.156  78.407  1.00 20.17 ? 562  LEU   B O     1 
ATOM   13072 C  CB    . LEU   B  1  564  ? 8.596   11.734  80.253  1.00 19.57 ? 562  LEU   B CB    1 
ATOM   13073 C  CG    . LEU   B  1  564  ? 9.684   12.790  80.219  1.00 22.56 ? 562  LEU   B CG    1 
ATOM   13074 C  CD1   . LEU   B  1  564  ? 9.657   13.539  78.884  1.00 22.11 ? 562  LEU   B CD1   1 
ATOM   13075 C  CD2   . LEU   B  1  564  ? 9.508   13.748  81.392  1.00 21.71 ? 562  LEU   B CD2   1 
ATOM   13076 N  N     . THR   B  1  565  ? 10.115  8.937   80.148  1.00 19.00 ? 563  THR   B N     1 
ATOM   13077 C  CA    . THR   B  1  565  ? 11.316  8.111   80.181  1.00 18.51 ? 563  THR   B CA    1 
ATOM   13078 C  C     . THR   B  1  565  ? 11.615  7.526   78.808  1.00 21.17 ? 563  THR   B C     1 
ATOM   13079 O  O     . THR   B  1  565  ? 12.746  7.601   78.323  1.00 20.96 ? 563  THR   B O     1 
ATOM   13080 C  CB    . THR   B  1  565  ? 11.134  6.985   81.197  1.00 22.30 ? 563  THR   B CB    1 
ATOM   13081 O  OG1   . THR   B  1  565  ? 11.084  7.548   82.512  1.00 22.15 ? 563  THR   B OG1   1 
ATOM   13082 C  CG2   . THR   B  1  565  ? 12.304  6.017   81.122  1.00 22.74 ? 563  THR   B CG2   1 
ATOM   13083 N  N     . GLU   B  1  566  ? 10.601  6.960   78.154  1.00 20.32 ? 564  GLU   B N     1 
ATOM   13084 C  CA    . GLU   B  1  566  ? 10.836  6.331   76.858  1.00 20.05 ? 564  GLU   B CA    1 
ATOM   13085 C  C     . GLU   B  1  566  ? 11.156  7.370   75.796  1.00 20.22 ? 564  GLU   B C     1 
ATOM   13086 O  O     . GLU   B  1  566  ? 12.042  7.157   74.962  1.00 20.98 ? 564  GLU   B O     1 
ATOM   13087 C  CB    . GLU   B  1  566  ? 9.644   5.466   76.462  1.00 24.51 ? 564  GLU   B CB    1 
ATOM   13088 C  CG    . GLU   B  1  566  ? 9.452   4.274   77.411  1.00 30.01 ? 564  GLU   B CG    1 
ATOM   13089 C  CD    . GLU   B  1  566  ? 10.765  3.577   77.776  1.00 39.68 ? 564  GLU   B CD    1 
ATOM   13090 O  OE1   . GLU   B  1  566  ? 11.537  3.216   76.857  1.00 42.45 ? 564  GLU   B OE1   1 
ATOM   13091 O  OE2   . GLU   B  1  566  ? 11.026  3.385   78.988  1.00 37.99 ? 564  GLU   B OE2   1 
ATOM   13092 N  N     . ALA   B  1  567  ? 10.468  8.509   75.823  1.00 18.64 ? 565  ALA   B N     1 
ATOM   13093 C  CA    . ALA   B  1  567  ? 10.763  9.557   74.852  1.00 19.79 ? 565  ALA   B CA    1 
ATOM   13094 C  C     . ALA   B  1  567  ? 12.159  10.123  75.061  1.00 20.31 ? 565  ALA   B C     1 
ATOM   13095 O  O     . ALA   B  1  567  ? 12.867  10.425  74.090  1.00 19.38 ? 565  ALA   B O     1 
ATOM   13096 C  CB    . ALA   B  1  567  ? 9.720   10.665  74.949  1.00 20.61 ? 565  ALA   B CB    1 
ATOM   13097 N  N     . LEU   B  1  568  ? 12.577  10.267  76.317  1.00 17.48 ? 566  LEU   B N     1 
ATOM   13098 C  CA    . LEU   B  1  568  ? 13.907  10.791  76.597  1.00 18.35 ? 566  LEU   B CA    1 
ATOM   13099 C  C     . LEU   B  1  568  ? 14.974  9.815   76.139  1.00 19.07 ? 566  LEU   B C     1 
ATOM   13100 O  O     . LEU   B  1  568  ? 15.943  10.210  75.485  1.00 17.77 ? 566  LEU   B O     1 
ATOM   13101 C  CB    . LEU   B  1  568  ? 14.055  11.094  78.083  1.00 16.37 ? 566  LEU   B CB    1 
ATOM   13102 C  CG    . LEU   B  1  568  ? 13.137  12.194  78.628  1.00 17.44 ? 566  LEU   B CG    1 
ATOM   13103 C  CD1   . LEU   B  1  568  ? 13.238  12.288  80.137  1.00 19.14 ? 566  LEU   B CD1   1 
ATOM   13104 C  CD2   . LEU   B  1  568  ? 13.432  13.531  77.986  1.00 21.16 ? 566  LEU   B CD2   1 
ATOM   13105 N  N     . ARG   B  1  569  ? 14.811  8.533   76.471  1.00 19.79 ? 567  ARG   B N     1 
ATOM   13106 C  CA    . ARG   B  1  569  ? 15.732  7.518   75.973  1.00 19.10 ? 567  ARG   B CA    1 
ATOM   13107 C  C     . ARG   B  1  569  ? 15.817  7.549   74.455  1.00 22.37 ? 567  ARG   B C     1 
ATOM   13108 O  O     . ARG   B  1  569  ? 16.915  7.517   73.880  1.00 22.83 ? 567  ARG   B O     1 
ATOM   13109 C  CB    . ARG   B  1  569  ? 15.291  6.138   76.453  1.00 22.16 ? 567  ARG   B CB    1 
ATOM   13110 C  CG    . ARG   B  1  569  ? 15.576  5.915   77.913  1.00 28.62 ? 567  ARG   B CG    1 
ATOM   13111 C  CD    . ARG   B  1  569  ? 14.998  4.603   78.404  1.00 27.52 ? 567  ARG   B CD    1 
ATOM   13112 N  NE    . ARG   B  1  569  ? 15.204  4.451   79.838  1.00 35.72 ? 567  ARG   B NE    1 
ATOM   13113 C  CZ    . ARG   B  1  569  ? 14.595  3.545   80.588  1.00 36.99 ? 567  ARG   B CZ    1 
ATOM   13114 N  NH1   . ARG   B  1  569  ? 13.713  2.703   80.073  1.00 38.08 ? 567  ARG   B NH1   1 
ATOM   13115 N  NH2   . ARG   B  1  569  ? 14.870  3.489   81.890  1.00 39.17 ? 567  ARG   B NH2   1 
ATOM   13116 N  N     . GLU   B  1  570  ? 14.666  7.612   73.786  1.00 19.60 ? 568  GLU   B N     1 
ATOM   13117 C  CA    . GLU   B  1  570  ? 14.663  7.631   72.328  1.00 21.89 ? 568  GLU   B CA    1 
ATOM   13118 C  C     . GLU   B  1  570  ? 15.346  8.874   71.789  1.00 22.02 ? 568  GLU   B C     1 
ATOM   13119 O  O     . GLU   B  1  570  ? 15.986  8.818   70.732  1.00 21.60 ? 568  GLU   B O     1 
ATOM   13120 C  CB    . GLU   B  1  570  ? 13.232  7.557   71.809  1.00 23.00 ? 568  GLU   B CB    1 
ATOM   13121 C  CG    . GLU   B  1  570  ? 12.567  6.214   72.047  1.00 25.76 ? 568  GLU   B CG    1 
ATOM   13122 C  CD    . GLU   B  1  570  ? 11.046  6.302   72.053  1.00 36.23 ? 568  GLU   B CD    1 
ATOM   13123 O  OE1   . GLU   B  1  570  ? 10.498  7.377   71.715  1.00 35.36 ? 568  GLU   B OE1   1 
ATOM   13124 O  OE2   . GLU   B  1  570  ? 10.399  5.293   72.409  1.00 40.31 ? 568  GLU   B OE2   1 
ATOM   13125 N  N     . SER   B  1  571  ? 15.217  10.005  72.488  1.00 19.69 ? 569  SER   B N     1 
ATOM   13126 C  CA    . SER   B  1  571  ? 15.847  11.228  72.010  1.00 20.12 ? 569  SER   B CA    1 
ATOM   13127 C  C     . SER   B  1  571  ? 17.351  11.079  72.010  1.00 22.13 ? 569  SER   B C     1 
ATOM   13128 O  O     . SER   B  1  571  ? 18.039  11.680  71.181  1.00 23.84 ? 569  SER   B O     1 
ATOM   13129 C  CB    . SER   B  1  571  ? 15.447  12.418  72.884  1.00 21.88 ? 569  SER   B CB    1 
ATOM   13130 O  OG    . SER   B  1  571  ? 16.157  12.413  74.123  1.00 22.48 ? 569  SER   B OG    1 
ATOM   13131 N  N     . ALA   B  1  572  ? 17.879  10.281  72.934  1.00 21.34 ? 570  ALA   B N     1 
ATOM   13132 C  CA    . ALA   B  1  572  ? 19.315  10.103  73.007  1.00 22.34 ? 570  ALA   B CA    1 
ATOM   13133 C  C     . ALA   B  1  572  ? 19.831  9.189   71.903  1.00 23.85 ? 570  ALA   B C     1 
ATOM   13134 O  O     . ALA   B  1  572  ? 21.028  9.223   71.594  1.00 27.68 ? 570  ALA   B O     1 
ATOM   13135 C  CB    . ALA   B  1  572  ? 19.702  9.591   74.394  1.00 23.58 ? 570  ALA   B CB    1 
ATOM   13136 N  N     . ALA   B  1  573  ? 18.960  8.397   71.282  1.00 23.23 ? 571  ALA   B N     1 
ATOM   13137 C  CA    . ALA   B  1  573  ? 19.367  7.535   70.179  1.00 26.92 ? 571  ALA   B CA    1 
ATOM   13138 C  C     . ALA   B  1  573  ? 19.342  8.240   68.827  1.00 25.23 ? 571  ALA   B C     1 
ATOM   13139 O  O     . ALA   B  1  573  ? 19.824  7.673   67.839  1.00 25.03 ? 571  ALA   B O     1 
ATOM   13140 C  CB    . ALA   B  1  573  ? 18.475  6.293   70.125  1.00 26.35 ? 571  ALA   B CB    1 
ATOM   13141 N  N     . MET   B  1  574  ? 18.800  9.451   68.760  1.00 23.70 ? 572  MET   B N     1 
ATOM   13142 C  CA    . MET   B  1  574  ? 18.686  10.165  67.501  1.00 21.53 ? 572  MET   B CA    1 
ATOM   13143 C  C     . MET   B  1  574  ? 20.009  10.832  67.159  1.00 22.20 ? 572  MET   B C     1 
ATOM   13144 O  O     . MET   B  1  574  ? 20.787  11.196  68.040  1.00 22.46 ? 572  MET   B O     1 
ATOM   13145 C  CB    . MET   B  1  574  ? 17.617  11.244  67.628  1.00 22.97 ? 572  MET   B CB    1 
ATOM   13146 C  CG    . MET   B  1  574  ? 16.237  10.675  67.837  1.00 25.37 ? 572  MET   B CG    1 
ATOM   13147 S  SD    . MET   B  1  574  ? 15.075  11.969  68.268  1.00 27.52 ? 572  MET   B SD    1 
ATOM   13148 C  CE    . MET   B  1  574  ? 13.556  11.011  68.344  1.00 26.97 ? 572  MET   B CE    1 
ATOM   13149 N  N     . LYS   B  1  575  ? 20.254  10.995  65.860  1.00 19.41 ? 573  LYS   B N     1 
ATOM   13150 C  CA    . LYS   B  1  575  ? 21.449  11.685  65.379  1.00 20.29 ? 573  LYS   B CA    1 
ATOM   13151 C  C     . LYS   B  1  575  ? 21.124  13.169  65.313  1.00 20.41 ? 573  LYS   B C     1 
ATOM   13152 O  O     . LYS   B  1  575  ? 20.440  13.627  64.395  1.00 21.46 ? 573  LYS   B O     1 
ATOM   13153 C  CB    . LYS   B  1  575  ? 21.851  11.144  64.012  1.00 21.43 ? 573  LYS   B CB    1 
ATOM   13154 C  CG    . LYS   B  1  575  ? 23.106  11.779  63.424  1.00 26.71 ? 573  LYS   B CG    1 
ATOM   13155 C  CD    . LYS   B  1  575  ? 23.567  11.003  62.196  1.00 34.34 ? 573  LYS   B CD    1 
ATOM   13156 C  CE    . LYS   B  1  575  ? 24.826  11.598  61.579  1.00 41.29 ? 573  LYS   B CE    1 
ATOM   13157 N  NZ    . LYS   B  1  575  ? 24.520  12.769  60.708  1.00 39.66 ? 573  LYS   B NZ    1 
ATOM   13158 N  N     . TRP   B  1  576  ? 21.590  13.919  66.307  1.00 20.01 ? 574  TRP   B N     1 
ATOM   13159 C  CA    . TRP   B  1  576  ? 21.353  15.350  66.365  1.00 17.70 ? 574  TRP   B CA    1 
ATOM   13160 C  C     . TRP   B  1  576  ? 22.495  16.072  65.680  1.00 17.89 ? 574  TRP   B C     1 
ATOM   13161 O  O     . TRP   B  1  576  ? 23.666  15.847  65.997  1.00 18.58 ? 574  TRP   B O     1 
ATOM   13162 C  CB    . TRP   B  1  576  ? 21.259  15.821  67.812  1.00 18.96 ? 574  TRP   B CB    1 
ATOM   13163 C  CG    . TRP   B  1  576  ? 20.086  15.241  68.536  1.00 17.38 ? 574  TRP   B CG    1 
ATOM   13164 C  CD1   . TRP   B  1  576  ? 20.108  14.244  69.469  1.00 20.15 ? 574  TRP   B CD1   1 
ATOM   13165 C  CD2   . TRP   B  1  576  ? 18.714  15.616  68.381  1.00 16.76 ? 574  TRP   B CD2   1 
ATOM   13166 N  NE1   . TRP   B  1  576  ? 18.830  13.985  69.917  1.00 20.41 ? 574  TRP   B NE1   1 
ATOM   13167 C  CE2   . TRP   B  1  576  ? 17.959  14.812  69.260  1.00 20.21 ? 574  TRP   B CE2   1 
ATOM   13168 C  CE3   . TRP   B  1  576  ? 18.057  16.557  67.595  1.00 18.62 ? 574  TRP   B CE3   1 
ATOM   13169 C  CZ2   . TRP   B  1  576  ? 16.576  14.922  69.370  1.00 20.51 ? 574  TRP   B CZ2   1 
ATOM   13170 C  CZ3   . TRP   B  1  576  ? 16.678  16.672  67.711  1.00 22.12 ? 574  TRP   B CZ3   1 
ATOM   13171 C  CH2   . TRP   B  1  576  ? 15.956  15.860  68.592  1.00 22.27 ? 574  TRP   B CH2   1 
ATOM   13172 N  N     . THR   B  1  577  ? 22.145  16.944  64.748  1.00 18.51 ? 575  THR   B N     1 
ATOM   13173 C  CA    . THR   B  1  577  ? 23.135  17.703  64.009  1.00 16.77 ? 575  THR   B CA    1 
ATOM   13174 C  C     . THR   B  1  577  ? 22.667  19.142  63.955  1.00 17.01 ? 575  THR   B C     1 
ATOM   13175 O  O     . THR   B  1  577  ? 21.488  19.443  64.137  1.00 17.61 ? 575  THR   B O     1 
ATOM   13176 C  CB    . THR   B  1  577  ? 23.331  17.177  62.582  1.00 20.17 ? 575  THR   B CB    1 
ATOM   13177 O  OG1   . THR   B  1  577  ? 22.116  17.344  61.837  1.00 23.35 ? 575  THR   B OG1   1 
ATOM   13178 C  CG2   . THR   B  1  577  ? 23.717  15.713  62.603  1.00 20.58 ? 575  THR   B CG2   1 
ATOM   13179 N  N     . ALA   B  1  578  ? 23.620  20.034  63.708  1.00 17.01 ? 576  ALA   B N     1 
ATOM   13180 C  CA    . ALA   B  1  578  ? 23.317  21.426  63.433  1.00 16.17 ? 576  ALA   B CA    1 
ATOM   13181 C  C     . ALA   B  1  578  ? 24.265  21.827  62.328  1.00 15.95 ? 576  ALA   B C     1 
ATOM   13182 O  O     . ALA   B  1  578  ? 25.470  21.600  62.445  1.00 18.72 ? 576  ALA   B O     1 
ATOM   13183 C  CB    . ALA   B  1  578  ? 23.552  22.311  64.664  1.00 15.65 ? 576  ALA   B CB    1 
ATOM   13184 N  N     . LEU   B  1  579  ? 23.725  22.363  61.250  1.00 18.04 ? 577  LEU   B N     1 
ATOM   13185 C  CA    . LEU   B  1  579  ? 24.492  22.683  60.059  1.00 18.09 ? 577  LEU   B CA    1 
ATOM   13186 C  C     . LEU   B  1  579  ? 24.225  24.124  59.677  1.00 17.21 ? 577  LEU   B C     1 
ATOM   13187 O  O     . LEU   B  1  579  ? 23.192  24.689  60.042  1.00 16.17 ? 577  LEU   B O     1 
ATOM   13188 C  CB    . LEU   B  1  579  ? 24.052  21.800  58.879  1.00 19.22 ? 577  LEU   B CB    1 
ATOM   13189 C  CG    . LEU   B  1  579  ? 23.881  20.315  59.168  1.00 25.25 ? 577  LEU   B CG    1 
ATOM   13190 C  CD1   . LEU   B  1  579  ? 23.340  19.568  57.951  1.00 26.29 ? 577  LEU   B CD1   1 
ATOM   13191 C  CD2   . LEU   B  1  579  ? 25.209  19.770  59.591  1.00 25.90 ? 577  LEU   B CD2   1 
ATOM   13192 N  N     . PRO   B  1  580  ? 25.114  24.733  58.902  1.00 16.70 ? 578  PRO   B N     1 
ATOM   13193 C  CA    . PRO   B  1  580  ? 24.776  26.023  58.293  1.00 14.62 ? 578  PRO   B CA    1 
ATOM   13194 C  C     . PRO   B  1  580  ? 23.696  25.784  57.262  1.00 16.86 ? 578  PRO   B C     1 
ATOM   13195 O  O     . PRO   B  1  580  ? 23.965  25.258  56.183  1.00 19.62 ? 578  PRO   B O     1 
ATOM   13196 C  CB    . PRO   B  1  580  ? 26.096  26.471  57.652  1.00 20.11 ? 578  PRO   B CB    1 
ATOM   13197 C  CG    . PRO   B  1  580  ? 27.154  25.632  58.363  1.00 19.60 ? 578  PRO   B CG    1 
ATOM   13198 C  CD    . PRO   B  1  580  ? 26.482  24.317  58.570  1.00 17.87 ? 578  PRO   B CD    1 
ATOM   13199 N  N     . GLN   B  1  581  ? 22.468  26.120  57.611  1.00 15.72 ? 579  GLN   B N     1 
ATOM   13200 C  CA    . GLN   B  1  581  ? 21.309  25.875  56.757  1.00 16.89 ? 579  GLN   B CA    1 
ATOM   13201 C  C     . GLN   B  1  581  ? 21.021  27.170  56.025  1.00 19.29 ? 579  GLN   B C     1 
ATOM   13202 O  O     . GLN   B  1  581  ? 20.323  28.049  56.534  1.00 18.64 ? 579  GLN   B O     1 
ATOM   13203 C  CB    . GLN   B  1  581  ? 20.120  25.468  57.605  1.00 18.34 ? 579  GLN   B CB    1 
ATOM   13204 C  CG    . GLN   B  1  581  ? 20.323  24.173  58.317  1.00 18.50 ? 579  GLN   B CG    1 
ATOM   13205 C  CD    . GLN   B  1  581  ? 20.323  22.975  57.382  1.00 24.05 ? 579  GLN   B CD    1 
ATOM   13206 O  OE1   . GLN   B  1  581  ? 20.082  23.094  56.167  1.00 22.68 ? 579  GLN   B OE1   1 
ATOM   13207 N  NE2   . GLN   B  1  581  ? 20.569  21.803  57.950  1.00 28.31 ? 579  GLN   B NE2   1 
ATOM   13208 N  N     . LEU   B  1  582  ? 21.590  27.298  54.834  1.00 18.73 ? 580  LEU   B N     1 
ATOM   13209 C  CA    . LEU   B  1  582  ? 21.330  28.456  54.002  1.00 17.42 ? 580  LEU   B CA    1 
ATOM   13210 C  C     . LEU   B  1  582  ? 20.071  28.208  53.172  1.00 20.90 ? 580  LEU   B C     1 
ATOM   13211 O  O     . LEU   B  1  582  ? 19.514  27.106  53.156  1.00 22.98 ? 580  LEU   B O     1 
ATOM   13212 C  CB    . LEU   B  1  582  ? 22.543  28.778  53.124  1.00 20.93 ? 580  LEU   B CB    1 
ATOM   13213 C  CG    . LEU   B  1  582  ? 23.635  29.628  53.806  1.00 24.53 ? 580  LEU   B CG    1 
ATOM   13214 C  CD1   . LEU   B  1  582  ? 24.281  28.929  55.006  1.00 24.42 ? 580  LEU   B CD1   1 
ATOM   13215 C  CD2   . LEU   B  1  582  ? 24.698  30.067  52.813  1.00 25.67 ? 580  LEU   B CD2   1 
ATOM   13216 N  N     . ALA   B  1  583  ? 19.608  29.256  52.489  1.00 19.64 ? 581  ALA   B N     1 
ATOM   13217 C  CA    . ALA   B  1  583  ? 18.383  29.118  51.707  1.00 20.89 ? 581  ALA   B CA    1 
ATOM   13218 C  C     . ALA   B  1  583  ? 18.532  28.046  50.640  1.00 24.92 ? 581  ALA   B C     1 
ATOM   13219 O  O     . ALA   B  1  583  ? 17.564  27.350  50.315  1.00 27.01 ? 581  ALA   B O     1 
ATOM   13220 C  CB    . ALA   B  1  583  ? 18.028  30.452  51.067  1.00 22.55 ? 581  ALA   B CB    1 
ATOM   13221 N  N     . THR   B  1  584  ? 19.735  27.891  50.104  1.00 21.40 ? 582  THR   B N     1 
ATOM   13222 C  CA    . THR   B  1  584  ? 20.017  26.939  49.039  1.00 22.83 ? 582  THR   B CA    1 
ATOM   13223 C  C     . THR   B  1  584  ? 20.362  25.550  49.561  1.00 20.16 ? 582  THR   B C     1 
ATOM   13224 O  O     . THR   B  1  584  ? 20.635  24.651  48.758  1.00 21.40 ? 582  THR   B O     1 
ATOM   13225 C  CB    . THR   B  1  584  ? 21.168  27.470  48.179  1.00 25.35 ? 582  THR   B CB    1 
ATOM   13226 O  OG1   . THR   B  1  584  ? 22.256  27.832  49.037  1.00 27.26 ? 582  THR   B OG1   1 
ATOM   13227 C  CG2   . THR   B  1  584  ? 20.726  28.691  47.416  1.00 28.65 ? 582  THR   B CG2   1 
ATOM   13228 N  N     . GLY   B  1  585  ? 20.364  25.349  50.874  1.00 21.07 ? 583  GLY   B N     1 
ATOM   13229 C  CA    . GLY   B  1  585  ? 20.648  24.057  51.443  1.00 21.47 ? 583  GLY   B CA    1 
ATOM   13230 C  C     . GLY   B  1  585  ? 21.789  24.165  52.428  1.00 23.15 ? 583  GLY   B C     1 
ATOM   13231 O  O     . GLY   B  1  585  ? 22.356  25.243  52.627  1.00 20.90 ? 583  GLY   B O     1 
ATOM   13232 N  N     . PRO   B  1  586  ? 22.128  23.061  53.086  1.00 20.07 ? 584  PRO   B N     1 
ATOM   13233 C  CA    . PRO   B  1  586  ? 23.203  23.107  54.080  1.00 17.81 ? 584  PRO   B CA    1 
ATOM   13234 C  C     . PRO   B  1  586  ? 24.553  23.310  53.422  1.00 22.90 ? 584  PRO   B C     1 
ATOM   13235 O  O     . PRO   B  1  586  ? 24.837  22.757  52.359  1.00 22.69 ? 584  PRO   B O     1 
ATOM   13236 C  CB    . PRO   B  1  586  ? 23.128  21.730  54.746  1.00 23.69 ? 584  PRO   B CB    1 
ATOM   13237 C  CG    . PRO   B  1  586  ? 22.532  20.856  53.708  1.00 26.17 ? 584  PRO   B CG    1 
ATOM   13238 C  CD    . PRO   B  1  586  ? 21.505  21.730  53.033  1.00 23.45 ? 584  PRO   B CD    1 
ATOM   13239 N  N     . ALA   B  1  587  ? 25.392  24.097  54.080  1.00 21.34 ? 585  ALA   B N     1 
ATOM   13240 C  CA    . ALA   B  1  587  ? 26.727  24.397  53.593  1.00 19.95 ? 585  ALA   B CA    1 
ATOM   13241 C  C     . ALA   B  1  587  ? 27.748  23.556  54.341  1.00 21.37 ? 585  ALA   B C     1 
ATOM   13242 O  O     . ALA   B  1  587  ? 27.523  23.138  55.479  1.00 21.08 ? 585  ALA   B O     1 
ATOM   13243 C  CB    . ALA   B  1  587  ? 27.049  25.880  53.797  1.00 20.74 ? 585  ALA   B CB    1 
ATOM   13244 N  N     . ALA   B  1  588  ? 28.880  23.312  53.688  1.00 20.84 ? 586  ALA   B N     1 
ATOM   13245 C  CA    . ALA   B  1  588  ? 29.965  22.615  54.351  1.00 21.08 ? 586  ALA   B CA    1 
ATOM   13246 C  C     . ALA   B  1  588  ? 30.651  23.533  55.356  1.00 21.64 ? 586  ALA   B C     1 
ATOM   13247 O  O     . ALA   B  1  588  ? 30.581  24.762  55.273  1.00 23.49 ? 586  ALA   B O     1 
ATOM   13248 C  CB    . ALA   B  1  588  ? 30.991  22.147  53.326  1.00 20.11 ? 586  ALA   B CB    1 
ATOM   13249 N  N     . GLY   B  1  589  ? 31.322  22.922  56.319  1.00 22.69 ? 587  GLY   B N     1 
ATOM   13250 C  CA    . GLY   B  1  589  ? 32.050  23.709  57.295  1.00 21.62 ? 587  GLY   B CA    1 
ATOM   13251 C  C     . GLY   B  1  589  ? 32.839  22.821  58.227  1.00 24.32 ? 587  GLY   B C     1 
ATOM   13252 O  O     . GLY   B  1  589  ? 32.902  21.603  58.050  1.00 25.24 ? 587  GLY   B O     1 
ATOM   13253 N  N     . GLU   B  1  590  ? 33.439  23.449  59.236  1.00 24.66 ? 588  GLU   B N     1 
ATOM   13254 C  CA    . GLU   B  1  590  ? 34.208  22.716  60.232  1.00 24.93 ? 588  GLU   B CA    1 
ATOM   13255 C  C     . GLU   B  1  590  ? 33.256  22.063  61.223  1.00 22.90 ? 588  GLU   B C     1 
ATOM   13256 O  O     . GLU   B  1  590  ? 32.386  22.728  61.784  1.00 22.74 ? 588  GLU   B O     1 
ATOM   13257 C  CB    . GLU   B  1  590  ? 35.134  23.675  60.975  1.00 26.61 ? 588  GLU   B CB    1 
ATOM   13258 C  CG    . GLU   B  1  590  ? 36.272  24.210  60.122  1.00 38.15 ? 588  GLU   B CG    1 
ATOM   13259 C  CD    . GLU   B  1  590  ? 37.261  23.123  59.719  1.00 42.97 ? 588  GLU   B CD    1 
ATOM   13260 O  OE1   . GLU   B  1  590  ? 37.446  22.157  60.492  1.00 46.47 ? 588  GLU   B OE1   1 
ATOM   13261 O  OE2   . GLU   B  1  590  ? 37.850  23.233  58.625  1.00 52.60 ? 588  GLU   B OE2   1 
ATOM   13262 N  N     . THR   B  1  591  ? 33.432  20.767  61.456  1.00 24.86 ? 589  THR   B N     1 
ATOM   13263 C  CA    . THR   B  1  591  ? 32.504  20.005  62.278  1.00 24.46 ? 589  THR   B CA    1 
ATOM   13264 C  C     . THR   B  1  591  ? 33.169  19.568  63.576  1.00 23.50 ? 589  THR   B C     1 
ATOM   13265 O  O     . THR   B  1  591  ? 34.349  19.213  63.597  1.00 23.45 ? 589  THR   B O     1 
ATOM   13266 C  CB    . THR   B  1  591  ? 31.991  18.790  61.503  1.00 23.53 ? 589  THR   B CB    1 
ATOM   13267 O  OG1   . THR   B  1  591  ? 31.343  19.244  60.307  1.00 26.98 ? 589  THR   B OG1   1 
ATOM   13268 C  CG2   . THR   B  1  591  ? 30.990  18.006  62.331  1.00 25.05 ? 589  THR   B CG2   1 
ATOM   13269 N  N     . ARG   B  1  592  ? 32.415  19.613  64.667  1.00 22.07 ? 590  ARG   B N     1 
ATOM   13270 C  CA    . ARG   B  1  592  ? 32.902  19.080  65.926  1.00 24.48 ? 590  ARG   B CA    1 
ATOM   13271 C  C     . ARG   B  1  592  ? 31.741  18.454  66.680  1.00 23.57 ? 590  ARG   B C     1 
ATOM   13272 O  O     . ARG   B  1  592  ? 30.570  18.687  66.369  1.00 21.99 ? 590  ARG   B O     1 
ATOM   13273 C  CB    . ARG   B  1  592  ? 33.544  20.175  66.767  1.00 26.23 ? 590  ARG   B CB    1 
ATOM   13274 C  CG    . ARG   B  1  592  ? 32.564  21.226  67.186  1.00 24.60 ? 590  ARG   B CG    1 
ATOM   13275 C  CD    . ARG   B  1  592  ? 33.127  22.063  68.296  1.00 31.63 ? 590  ARG   B CD    1 
ATOM   13276 N  NE    . ARG   B  1  592  ? 32.268  23.207  68.565  1.00 31.74 ? 590  ARG   B NE    1 
ATOM   13277 C  CZ    . ARG   B  1  592  ? 31.277  23.213  69.445  1.00 33.18 ? 590  ARG   B CZ    1 
ATOM   13278 N  NH1   . ARG   B  1  592  ? 30.986  22.141  70.171  1.00 28.71 ? 590  ARG   B NH1   1 
ATOM   13279 N  NH2   . ARG   B  1  592  ? 30.562  24.323  69.603  1.00 30.46 ? 590  ARG   B NH2   1 
ATOM   13280 N  N     . THR   B  1  593  ? 32.078  17.667  67.696  1.00 22.16 ? 591  THR   B N     1 
ATOM   13281 C  CA    . THR   B  1  593  ? 31.060  17.051  68.528  1.00 22.25 ? 591  THR   B CA    1 
ATOM   13282 C  C     . THR   B  1  593  ? 30.535  18.035  69.559  1.00 22.18 ? 591  THR   B C     1 
ATOM   13283 O  O     . THR   B  1  593  ? 31.213  18.984  69.963  1.00 22.75 ? 591  THR   B O     1 
ATOM   13284 C  CB    . THR   B  1  593  ? 31.617  15.828  69.252  1.00 24.68 ? 591  THR   B CB    1 
ATOM   13285 O  OG1   . THR   B  1  593  ? 32.716  16.235  70.076  1.00 27.43 ? 591  THR   B OG1   1 
ATOM   13286 C  CG2   . THR   B  1  593  ? 32.091  14.786  68.246  1.00 30.94 ? 591  THR   B CG2   1 
ATOM   13287 N  N     . VAL   B  1  594  ? 29.295  17.806  69.964  1.00 18.70 ? 592  VAL   B N     1 
ATOM   13288 C  CA    . VAL   B  1  594  ? 28.663  18.521  71.058  1.00 16.47 ? 592  VAL   B CA    1 
ATOM   13289 C  C     . VAL   B  1  594  ? 28.567  17.521  72.197  1.00 21.06 ? 592  VAL   B C     1 
ATOM   13290 O  O     . VAL   B  1  594  ? 27.990  16.442  72.026  1.00 20.78 ? 592  VAL   B O     1 
ATOM   13291 C  CB    . VAL   B  1  594  ? 27.276  19.025  70.632  1.00 19.60 ? 592  VAL   B CB    1 
ATOM   13292 C  CG1   . VAL   B  1  594  ? 26.570  19.752  71.782  1.00 20.80 ? 592  VAL   B CG1   1 
ATOM   13293 C  CG2   . VAL   B  1  594  ? 27.400  19.932  69.409  1.00 22.96 ? 592  VAL   B CG2   1 
ATOM   13294 N  N     . LEU   B  1  595  ? 29.160  17.860  73.341  1.00 22.67 ? 593  LEU   B N     1 
ATOM   13295 C  CA    . LEU   B  1  595  ? 29.264  16.953  74.477  1.00 20.26 ? 593  LEU   B CA    1 
ATOM   13296 C  C     . LEU   B  1  595  ? 28.358  17.423  75.607  1.00 20.36 ? 593  LEU   B C     1 
ATOM   13297 O  O     . LEU   B  1  595  ? 28.135  18.621  75.792  1.00 21.23 ? 593  LEU   B O     1 
ATOM   13298 C  CB    . LEU   B  1  595  ? 30.707  16.894  74.985  1.00 22.22 ? 593  LEU   B CB    1 
ATOM   13299 C  CG    . LEU   B  1  595  ? 31.731  16.500  73.927  1.00 24.12 ? 593  LEU   B CG    1 
ATOM   13300 C  CD1   . LEU   B  1  595  ? 33.106  16.463  74.564  1.00 27.24 ? 593  LEU   B CD1   1 
ATOM   13301 C  CD2   . LEU   B  1  595  ? 31.385  15.154  73.304  1.00 22.12 ? 593  LEU   B CD2   1 
ATOM   13302 N  N     . ASN   B  1  596  ? 27.839  16.469  76.362  1.00 17.83 ? 594  ASN   B N     1 
ATOM   13303 C  CA    . ASN   B  1  596  ? 27.009  16.788  77.516  1.00 18.84 ? 594  ASN   B CA    1 
ATOM   13304 C  C     . ASN   B  1  596  ? 27.871  17.509  78.545  1.00 19.11 ? 594  ASN   B C     1 
ATOM   13305 O  O     . ASN   B  1  596  ? 28.887  16.954  78.972  1.00 18.06 ? 594  ASN   B O     1 
ATOM   13306 C  CB    . ASN   B  1  596  ? 26.522  15.457  78.086  1.00 16.63 ? 594  ASN   B CB    1 
ATOM   13307 C  CG    . ASN   B  1  596  ? 25.471  15.618  79.149  1.00 17.91 ? 594  ASN   B CG    1 
ATOM   13308 O  OD1   . ASN   B  1  596  ? 25.485  16.576  79.923  1.00 18.78 ? 594  ASN   B OD1   1 
ATOM   13309 N  ND2   . ASN   B  1  596  ? 24.542  14.668  79.198  1.00 20.57 ? 594  ASN   B ND2   1 
ATOM   13310 N  N     . PRO   B  1  597  ? 27.527  18.730  78.969  1.00 16.90 ? 595  PRO   B N     1 
ATOM   13311 C  CA    . PRO   B  1  597  ? 28.373  19.410  79.966  1.00 17.47 ? 595  PRO   B CA    1 
ATOM   13312 C  C     . PRO   B  1  597  ? 28.454  18.681  81.288  1.00 17.37 ? 595  PRO   B C     1 
ATOM   13313 O  O     . PRO   B  1  597  ? 29.416  18.887  82.034  1.00 17.47 ? 595  PRO   B O     1 
ATOM   13314 C  CB    . PRO   B  1  597  ? 27.708  20.784  80.128  1.00 14.74 ? 595  PRO   B CB    1 
ATOM   13315 C  CG    . PRO   B  1  597  ? 26.261  20.560  79.686  1.00 17.15 ? 595  PRO   B CG    1 
ATOM   13316 C  CD    . PRO   B  1  597  ? 26.386  19.567  78.552  1.00 17.35 ? 595  PRO   B CD    1 
ATOM   13317 N  N     . GLY   B  1  598  ? 27.470  17.842  81.606  1.00 17.76 ? 596  GLY   B N     1 
ATOM   13318 C  CA    . GLY   B  1  598  ? 27.517  17.071  82.833  1.00 17.84 ? 596  GLY   B CA    1 
ATOM   13319 C  C     . GLY   B  1  598  ? 28.289  15.779  82.732  1.00 20.45 ? 596  GLY   B C     1 
ATOM   13320 O  O     . GLY   B  1  598  ? 28.560  15.144  83.754  1.00 20.07 ? 596  GLY   B O     1 
ATOM   13321 N  N     . ASP   B  1  599  ? 28.674  15.385  81.524  1.00 18.24 ? 597  ASP   B N     1 
ATOM   13322 C  CA    . ASP   B  1  599  ? 29.433  14.163  81.320  1.00 20.09 ? 597  ASP   B CA    1 
ATOM   13323 C  C     . ASP   B  1  599  ? 29.966  14.190  79.902  1.00 20.67 ? 597  ASP   B C     1 
ATOM   13324 O  O     . ASP   B  1  599  ? 29.243  13.857  78.959  1.00 18.79 ? 597  ASP   B O     1 
ATOM   13325 C  CB    . ASP   B  1  599  ? 28.537  12.948  81.516  1.00 20.68 ? 597  ASP   B CB    1 
ATOM   13326 C  CG    . ASP   B  1  599  ? 29.310  11.659  81.560  1.00 24.05 ? 597  ASP   B CG    1 
ATOM   13327 O  OD1   . ASP   B  1  599  ? 30.467  11.630  81.076  1.00 23.12 ? 597  ASP   B OD1   1 
ATOM   13328 O  OD2   . ASP   B  1  599  ? 28.754  10.677  82.096  1.00 25.39 ? 597  ASP   B OD2   1 
ATOM   13329 N  N     . HIS   B  1  600  ? 31.226  14.594  79.742  1.00 19.91 ? 598  HIS   B N     1 
ATOM   13330 C  CA    . HIS   B  1  600  ? 31.790  14.726  78.408  1.00 19.96 ? 598  HIS   B CA    1 
ATOM   13331 C  C     . HIS   B  1  600  ? 31.880  13.403  77.662  1.00 21.49 ? 598  HIS   B C     1 
ATOM   13332 O  O     . HIS   B  1  600  ? 32.124  13.416  76.453  1.00 24.14 ? 598  HIS   B O     1 
ATOM   13333 C  CB    . HIS   B  1  600  ? 33.148  15.436  78.459  1.00 22.57 ? 598  HIS   B CB    1 
ATOM   13334 C  CG    . HIS   B  1  600  ? 33.037  16.896  78.761  1.00 22.42 ? 598  HIS   B CG    1 
ATOM   13335 N  ND1   . HIS   B  1  600  ? 34.126  17.742  78.791  1.00 27.29 ? 598  HIS   B ND1   1 
ATOM   13336 C  CD2   . HIS   B  1  600  ? 31.955  17.661  79.043  1.00 23.61 ? 598  HIS   B CD2   1 
ATOM   13337 C  CE1   . HIS   B  1  600  ? 33.718  18.966  79.087  1.00 29.71 ? 598  HIS   B CE1   1 
ATOM   13338 N  NE2   . HIS   B  1  600  ? 32.405  18.944  79.242  1.00 27.40 ? 598  HIS   B NE2   1 
ATOM   13339 N  N     . ARG   B  1  601  ? 31.672  12.271  78.337  1.00 20.78 ? 599  ARG   B N     1 
ATOM   13340 C  CA    . ARG   B  1  601  ? 31.622  10.997  77.636  1.00 19.00 ? 599  ARG   B CA    1 
ATOM   13341 C  C     . ARG   B  1  601  ? 30.331  10.833  76.847  1.00 21.54 ? 599  ARG   B C     1 
ATOM   13342 O  O     . ARG   B  1  601  ? 30.273  9.986   75.948  1.00 24.16 ? 599  ARG   B O     1 
ATOM   13343 C  CB    . ARG   B  1  601  ? 31.776  9.850   78.627  1.00 26.12 ? 599  ARG   B CB    1 
ATOM   13344 C  CG    . ARG   B  1  601  ? 33.040  9.941   79.465  1.00 27.52 ? 599  ARG   B CG    1 
ATOM   13345 C  CD    . ARG   B  1  601  ? 33.000  8.960   80.611  1.00 27.57 ? 599  ARG   B CD    1 
ATOM   13346 N  NE    . ARG   B  1  601  ? 31.898  9.227   81.523  1.00 26.86 ? 599  ARG   B NE    1 
ATOM   13347 C  CZ    . ARG   B  1  601  ? 31.592  8.463   82.561  1.00 32.78 ? 599  ARG   B CZ    1 
ATOM   13348 N  NH1   . ARG   B  1  601  ? 32.300  7.385   82.856  1.00 31.19 ? 599  ARG   B NH1   1 
ATOM   13349 N  NH2   . ARG   B  1  601  ? 30.547  8.787   83.321  1.00 27.51 ? 599  ARG   B NH2   1 
ATOM   13350 N  N     . ASP   B  1  602  ? 29.304  11.620  77.171  1.00 21.68 ? 600  ASP   B N     1 
ATOM   13351 C  CA    . ASP   B  1  602  ? 27.998  11.528  76.524  1.00 21.08 ? 600  ASP   B CA    1 
ATOM   13352 C  C     . ASP   B  1  602  ? 28.014  12.475  75.332  1.00 21.93 ? 600  ASP   B C     1 
ATOM   13353 O  O     . ASP   B  1  602  ? 27.907  13.693  75.492  1.00 20.43 ? 600  ASP   B O     1 
ATOM   13354 C  CB    . ASP   B  1  602  ? 26.908  11.891  77.526  1.00 22.81 ? 600  ASP   B CB    1 
ATOM   13355 C  CG    . ASP   B  1  602  ? 25.527  11.829  76.928  1.00 25.57 ? 600  ASP   B CG    1 
ATOM   13356 O  OD1   . ASP   B  1  602  ? 25.361  11.127  75.903  1.00 26.03 ? 600  ASP   B OD1   1 
ATOM   13357 O  OD2   . ASP   B  1  602  ? 24.617  12.494  77.473  1.00 24.89 ? 600  ASP   B OD2   1 
ATOM   13358 N  N     . VAL   B  1  603  ? 28.179  11.920  74.133  1.00 21.30 ? 601  VAL   B N     1 
ATOM   13359 C  CA    . VAL   B  1  603  ? 28.181  12.719  72.912  1.00 21.11 ? 601  VAL   B CA    1 
ATOM   13360 C  C     . VAL   B  1  603  ? 26.737  12.980  72.515  1.00 21.18 ? 601  VAL   B C     1 
ATOM   13361 O  O     . VAL   B  1  603  ? 25.965  12.045  72.280  1.00 23.51 ? 601  VAL   B O     1 
ATOM   13362 C  CB    . VAL   B  1  603  ? 28.929  12.007  71.782  1.00 22.53 ? 601  VAL   B CB    1 
ATOM   13363 C  CG1   . VAL   B  1  603  ? 28.898  12.869  70.520  1.00 21.10 ? 601  VAL   B CG1   1 
ATOM   13364 C  CG2   . VAL   B  1  603  ? 30.364  11.678  72.216  1.00 24.15 ? 601  VAL   B CG2   1 
ATOM   13365 N  N     . VAL   B  1  604  ? 26.361  14.251  72.464  1.00 19.24 ? 602  VAL   B N     1 
ATOM   13366 C  CA    . VAL   B  1  604  ? 24.976  14.587  72.161  1.00 19.16 ? 602  VAL   B CA    1 
ATOM   13367 C  C     . VAL   B  1  604  ? 24.748  14.671  70.664  1.00 18.34 ? 602  VAL   B C     1 
ATOM   13368 O  O     . VAL   B  1  604  ? 23.711  14.237  70.158  1.00 19.71 ? 602  VAL   B O     1 
ATOM   13369 C  CB    . VAL   B  1  604  ? 24.572  15.888  72.875  1.00 19.92 ? 602  VAL   B CB    1 
ATOM   13370 C  CG1   . VAL   B  1  604  ? 23.092  16.126  72.700  1.00 18.63 ? 602  VAL   B CG1   1 
ATOM   13371 C  CG2   . VAL   B  1  604  ? 24.935  15.787  74.353  1.00 18.68 ? 602  VAL   B CG2   1 
ATOM   13372 N  N     . GLY   B  1  605  ? 25.712  15.206  69.934  1.00 17.18 ? 603  GLY   B N     1 
ATOM   13373 C  CA    . GLY   B  1  605  ? 25.518  15.391  68.514  1.00 18.59 ? 603  GLY   B CA    1 
ATOM   13374 C  C     . GLY   B  1  605  ? 26.724  16.053  67.909  1.00 18.71 ? 603  GLY   B C     1 
ATOM   13375 O  O     . GLY   B  1  605  ? 27.811  16.038  68.486  1.00 19.03 ? 603  GLY   B O     1 
ATOM   13376 N  N     . SER   B  1  606  ? 26.528  16.629  66.733  1.00 16.91 ? 604  SER   B N     1 
ATOM   13377 C  CA    A SER   B  1  606  ? 27.623  17.247  66.007  0.45 19.08 ? 604  SER   B CA    1 
ATOM   13378 C  CA    B SER   B  1  606  ? 27.616  17.229  65.976  0.55 19.05 ? 604  SER   B CA    1 
ATOM   13379 C  C     . SER   B  1  606  ? 27.144  18.551  65.402  1.00 19.74 ? 604  SER   B C     1 
ATOM   13380 O  O     . SER   B  1  606  ? 25.990  18.672  64.990  1.00 20.51 ? 604  SER   B O     1 
ATOM   13381 C  CB    A SER   B  1  606  ? 28.162  16.333  64.902  0.45 23.88 ? 604  SER   B CB    1 
ATOM   13382 C  CB    B SER   B  1  606  ? 28.060  16.317  64.826  0.55 23.83 ? 604  SER   B CB    1 
ATOM   13383 O  OG    A SER   B  1  606  ? 27.182  16.096  63.915  0.45 25.18 ? 604  SER   B OG    1 
ATOM   13384 O  OG    B SER   B  1  606  ? 28.722  15.162  65.320  0.55 28.39 ? 604  SER   B OG    1 
ATOM   13385 N  N     . VAL   B  1  607  ? 28.035  19.530  65.366  1.00 17.82 ? 605  VAL   B N     1 
ATOM   13386 C  CA    . VAL   B  1  607  ? 27.725  20.826  64.792  1.00 16.55 ? 605  VAL   B CA    1 
ATOM   13387 C  C     . VAL   B  1  607  ? 28.733  21.134  63.701  1.00 18.05 ? 605  VAL   B C     1 
ATOM   13388 O  O     . VAL   B  1  607  ? 29.943  20.959  63.888  1.00 17.75 ? 605  VAL   B O     1 
ATOM   13389 C  CB    . VAL   B  1  607  ? 27.691  21.940  65.853  1.00 17.12 ? 605  VAL   B CB    1 
ATOM   13390 C  CG1   . VAL   B  1  607  ? 28.985  21.948  66.690  1.00 18.77 ? 605  VAL   B CG1   1 
ATOM   13391 C  CG2   . VAL   B  1  607  ? 27.448  23.289  65.186  1.00 18.36 ? 605  VAL   B CG2   1 
ATOM   13392 N  N     . THR   B  1  608  ? 28.233  21.573  62.562  1.00 16.62 ? 606  THR   B N     1 
ATOM   13393 C  CA    . THR   B  1  608  ? 29.065  22.080  61.490  1.00 18.53 ? 606  THR   B CA    1 
ATOM   13394 C  C     . THR   B  1  608  ? 28.942  23.596  61.509  1.00 16.95 ? 606  THR   B C     1 
ATOM   13395 O  O     . THR   B  1  608  ? 27.843  24.139  61.386  1.00 18.37 ? 606  THR   B O     1 
ATOM   13396 C  CB    . THR   B  1  608  ? 28.586  21.505  60.163  1.00 20.95 ? 606  THR   B CB    1 
ATOM   13397 O  OG1   . THR   B  1  608  ? 28.739  20.082  60.203  1.00 22.18 ? 606  THR   B OG1   1 
ATOM   13398 C  CG2   . THR   B  1  608  ? 29.397  22.072  59.007  1.00 21.41 ? 606  THR   B CG2   1 
ATOM   13399 N  N     . GLU   B  1  609  ? 30.062  24.270  61.680  1.00 18.03 ? 607  GLU   B N     1 
ATOM   13400 C  CA    . GLU   B  1  609  ? 30.004  25.697  61.909  1.00 20.74 ? 607  GLU   B CA    1 
ATOM   13401 C  C     . GLU   B  1  609  ? 30.181  26.450  60.598  1.00 16.39 ? 607  GLU   B C     1 
ATOM   13402 O  O     . GLU   B  1  609  ? 30.713  25.926  59.613  1.00 20.02 ? 607  GLU   B O     1 
ATOM   13403 C  CB    . GLU   B  1  609  ? 30.980  26.103  63.017  1.00 21.40 ? 607  GLU   B CB    1 
ATOM   13404 C  CG    . GLU   B  1  609  ? 30.473  25.589  64.375  1.00 25.84 ? 607  GLU   B CG    1 
ATOM   13405 C  CD    . GLU   B  1  609  ? 31.377  25.916  65.546  1.00 31.56 ? 607  GLU   B CD    1 
ATOM   13406 O  OE1   . GLU   B  1  609  ? 32.590  26.136  65.330  1.00 34.55 ? 607  GLU   B OE1   1 
ATOM   13407 O  OE2   . GLU   B  1  609  ? 30.872  25.942  66.687  1.00 28.77 ? 607  GLU   B OE2   1 
ATOM   13408 N  N     . THR   B  1  610  ? 29.690  27.682  60.591  1.00 18.10 ? 608  THR   B N     1 
ATOM   13409 C  CA    . THR   B  1  610  ? 29.513  28.452  59.366  1.00 17.56 ? 608  THR   B CA    1 
ATOM   13410 C  C     . THR   B  1  610  ? 30.773  29.248  59.088  1.00 18.14 ? 608  THR   B C     1 
ATOM   13411 O  O     . THR   B  1  610  ? 31.299  29.909  59.986  1.00 20.63 ? 608  THR   B O     1 
ATOM   13412 C  CB    . THR   B  1  610  ? 28.366  29.445  59.553  1.00 20.45 ? 608  THR   B CB    1 
ATOM   13413 O  OG1   . THR   B  1  610  ? 27.200  28.780  60.056  1.00 18.69 ? 608  THR   B OG1   1 
ATOM   13414 C  CG2   . THR   B  1  610  ? 28.033  30.123  58.236  1.00 19.10 ? 608  THR   B CG2   1 
ATOM   13415 N  N     . SER   B  1  611  ? 31.245  29.208  57.846  1.00 18.13 ? 609  SER   B N     1 
ATOM   13416 C  CA    . SER   B  1  611  ? 32.336  30.102  57.481  1.00 21.14 ? 609  SER   B CA    1 
ATOM   13417 C  C     . SER   B  1  611  ? 31.829  31.537  57.396  1.00 23.44 ? 609  SER   B C     1 
ATOM   13418 O  O     . SER   B  1  611  ? 30.647  31.789  57.155  1.00 19.44 ? 609  SER   B O     1 
ATOM   13419 C  CB    . SER   B  1  611  ? 32.918  29.699  56.130  1.00 24.13 ? 609  SER   B CB    1 
ATOM   13420 O  OG    . SER   B  1  611  ? 31.989  29.982  55.102  1.00 22.25 ? 609  SER   B OG    1 
ATOM   13421 N  N     . GLU   B  1  612  ? 32.739  32.495  57.595  1.00 22.18 ? 610  GLU   B N     1 
ATOM   13422 C  CA    . GLU   B  1  612  ? 32.335  33.891  57.475  1.00 23.23 ? 610  GLU   B CA    1 
ATOM   13423 C  C     . GLU   B  1  612  ? 31.825  34.201  56.072  1.00 24.47 ? 610  GLU   B C     1 
ATOM   13424 O  O     . GLU   B  1  612  ? 30.871  34.974  55.914  1.00 22.87 ? 610  GLU   B O     1 
ATOM   13425 C  CB    . GLU   B  1  612  ? 33.480  34.816  57.898  1.00 28.02 ? 610  GLU   B CB    1 
ATOM   13426 C  CG    . GLU   B  1  612  ? 33.840  34.648  59.379  1.00 31.46 ? 610  GLU   B CG    1 
ATOM   13427 C  CD    . GLU   B  1  612  ? 35.050  35.471  59.805  1.00 39.04 ? 610  GLU   B CD    1 
ATOM   13428 O  OE1   . GLU   B  1  612  ? 35.348  36.492  59.148  1.00 49.69 ? 610  GLU   B OE1   1 
ATOM   13429 O  OE2   . GLU   B  1  612  ? 35.699  35.092  60.804  1.00 39.64 ? 610  GLU   B OE2   1 
ATOM   13430 N  N     . GLU   B  1  613  ? 32.406  33.568  55.049  1.00 24.33 ? 611  GLU   B N     1 
ATOM   13431 C  CA    . GLU   B  1  613  ? 31.909  33.764  53.690  1.00 21.95 ? 611  GLU   B CA    1 
ATOM   13432 C  C     . GLU   B  1  613  ? 30.475  33.269  53.557  1.00 22.64 ? 611  GLU   B C     1 
ATOM   13433 O  O     . GLU   B  1  613  ? 29.644  33.922  52.919  1.00 26.15 ? 611  GLU   B O     1 
ATOM   13434 C  CB    . GLU   B  1  613  ? 32.824  33.074  52.674  1.00 29.57 ? 611  GLU   B CB    1 
ATOM   13435 N  N     . ASP   B  1  614  ? 30.163  32.113  54.150  1.00 20.34 ? 612  ASP   B N     1 
ATOM   13436 C  CA    . ASP   B  1  614  ? 28.791  31.627  54.064  1.00 18.38 ? 612  ASP   B CA    1 
ATOM   13437 C  C     . ASP   B  1  614  ? 27.844  32.458  54.912  1.00 20.66 ? 612  ASP   B C     1 
ATOM   13438 O  O     . ASP   B  1  614  ? 26.656  32.560  54.586  1.00 19.67 ? 612  ASP   B O     1 
ATOM   13439 C  CB    . ASP   B  1  614  ? 28.710  30.155  54.439  1.00 21.96 ? 612  ASP   B CB    1 
ATOM   13440 C  CG    . ASP   B  1  614  ? 29.195  29.252  53.314  1.00 28.56 ? 612  ASP   B CG    1 
ATOM   13441 O  OD1   . ASP   B  1  614  ? 29.079  29.653  52.131  1.00 29.35 ? 612  ASP   B OD1   1 
ATOM   13442 O  OD2   . ASP   B  1  614  ? 29.695  28.153  53.612  1.00 27.47 ? 612  ASP   B OD2   1 
ATOM   13443 N  N     . ALA   B  1  615  ? 28.343  33.057  55.992  1.00 20.00 ? 613  ALA   B N     1 
ATOM   13444 C  CA    . ALA   B  1  615  ? 27.508  33.976  56.756  1.00 19.18 ? 613  ALA   B CA    1 
ATOM   13445 C  C     . ALA   B  1  615  ? 27.111  35.167  55.901  1.00 18.05 ? 613  ALA   B C     1 
ATOM   13446 O  O     . ALA   B  1  615  ? 25.943  35.558  55.870  1.00 17.51 ? 613  ALA   B O     1 
ATOM   13447 C  CB    . ALA   B  1  615  ? 28.239  34.432  58.017  1.00 22.42 ? 613  ALA   B CB    1 
ATOM   13448 N  N     . ARG   B  1  616  ? 28.066  35.735  55.166  1.00 21.05 ? 614  ARG   B N     1 
ATOM   13449 C  CA    . ARG   B  1  616  ? 27.729  36.839  54.273  1.00 19.93 ? 614  ARG   B CA    1 
ATOM   13450 C  C     . ARG   B  1  616  ? 26.821  36.377  53.142  1.00 20.70 ? 614  ARG   B C     1 
ATOM   13451 O  O     . ARG   B  1  616  ? 25.882  37.090  52.765  1.00 19.46 ? 614  ARG   B O     1 
ATOM   13452 C  CB    . ARG   B  1  616  ? 29.004  37.485  53.739  1.00 23.14 ? 614  ARG   B CB    1 
ATOM   13453 C  CG    . ARG   B  1  616  ? 29.691  38.367  54.775  1.00 25.25 ? 614  ARG   B CG    1 
ATOM   13454 C  CD    . ARG   B  1  616  ? 30.867  39.116  54.170  1.00 30.49 ? 614  ARG   B CD    1 
ATOM   13455 N  NE    . ARG   B  1  616  ? 31.977  38.211  53.927  1.00 32.20 ? 614  ARG   B NE    1 
ATOM   13456 C  CZ    . ARG   B  1  616  ? 32.841  37.831  54.856  1.00 34.92 ? 614  ARG   B CZ    1 
ATOM   13457 N  NH1   . ARG   B  1  616  ? 32.748  38.264  56.105  1.00 31.72 ? 614  ARG   B NH1   1 
ATOM   13458 N  NH2   . ARG   B  1  616  ? 33.819  36.996  54.525  1.00 31.36 ? 614  ARG   B NH2   1 
ATOM   13459 N  N     . ARG   B  1  617  ? 27.070  35.183  52.598  1.00 19.25 ? 615  ARG   B N     1 
ATOM   13460 C  CA    . ARG   B  1  617  ? 26.183  34.655  51.567  1.00 21.25 ? 615  ARG   B CA    1 
ATOM   13461 C  C     . ARG   B  1  617  ? 24.764  34.514  52.095  1.00 18.55 ? 615  ARG   B C     1 
ATOM   13462 O  O     . ARG   B  1  617  ? 23.792  34.816  51.388  1.00 19.73 ? 615  ARG   B O     1 
ATOM   13463 C  CB    . ARG   B  1  617  ? 26.697  33.302  51.064  1.00 23.24 ? 615  ARG   B CB    1 
ATOM   13464 C  CG    . ARG   B  1  617  ? 25.865  32.719  49.913  1.00 24.06 ? 615  ARG   B CG    1 
ATOM   13465 C  CD    . ARG   B  1  617  ? 26.656  31.685  49.107  1.00 28.08 ? 615  ARG   B CD    1 
ATOM   13466 N  NE    . ARG   B  1  617  ? 26.811  30.417  49.809  1.00 32.12 ? 615  ARG   B NE    1 
ATOM   13467 C  CZ    . ARG   B  1  617  ? 25.959  29.403  49.717  1.00 41.34 ? 615  ARG   B CZ    1 
ATOM   13468 N  NH1   . ARG   B  1  617  ? 24.859  29.486  48.979  1.00 38.22 ? 615  ARG   B NH1   1 
ATOM   13469 N  NH2   . ARG   B  1  617  ? 26.211  28.281  50.386  1.00 39.89 ? 615  ARG   B NH2   1 
ATOM   13470 N  N     . ALA   B  1  618  ? 24.619  34.048  53.333  1.00 17.72 ? 616  ALA   B N     1 
ATOM   13471 C  CA    . ALA   B  1  618  ? 23.278  33.900  53.890  1.00 15.85 ? 616  ALA   B CA    1 
ATOM   13472 C  C     . ALA   B  1  618  ? 22.554  35.243  53.940  1.00 16.81 ? 616  ALA   B C     1 
ATOM   13473 O  O     . ALA   B  1  618  ? 21.356  35.330  53.637  1.00 17.79 ? 616  ALA   B O     1 
ATOM   13474 C  CB    . ALA   B  1  618  ? 23.364  33.284  55.283  1.00 16.87 ? 616  ALA   B CB    1 
ATOM   13475 N  N     . VAL   B  1  619  ? 23.260  36.304  54.319  1.00 19.23 ? 617  VAL   B N     1 
ATOM   13476 C  CA    . VAL   B  1  619  ? 22.608  37.606  54.401  1.00 16.59 ? 617  VAL   B CA    1 
ATOM   13477 C  C     . VAL   B  1  619  ? 22.167  38.065  53.019  1.00 18.50 ? 617  VAL   B C     1 
ATOM   13478 O  O     . VAL   B  1  619  ? 21.077  38.618  52.855  1.00 19.82 ? 617  VAL   B O     1 
ATOM   13479 C  CB    . VAL   B  1  619  ? 23.505  38.630  55.116  1.00 18.81 ? 617  VAL   B CB    1 
ATOM   13480 C  CG1   . VAL   B  1  619  ? 22.849  40.001  55.142  1.00 19.10 ? 617  VAL   B CG1   1 
ATOM   13481 C  CG2   . VAL   B  1  619  ? 23.785  38.162  56.528  1.00 19.62 ? 617  VAL   B CG2   1 
ATOM   13482 N  N     . ARG   B  1  620  ? 22.983  37.807  52.000  1.00 20.05 ? 618  ARG   B N     1 
ATOM   13483 C  CA    . ARG   B  1  620  ? 22.572  38.149  50.644  1.00 22.68 ? 618  ARG   B CA    1 
ATOM   13484 C  C     . ARG   B  1  620  ? 21.342  37.360  50.231  1.00 19.54 ? 618  ARG   B C     1 
ATOM   13485 O  O     . ARG   B  1  620  ? 20.430  37.905  49.600  1.00 19.96 ? 618  ARG   B O     1 
ATOM   13486 C  CB    . ARG   B  1  620  ? 23.721  37.901  49.666  1.00 22.96 ? 618  ARG   B CB    1 
ATOM   13487 C  CG    . ARG   B  1  620  ? 24.902  38.801  49.924  1.00 29.56 ? 618  ARG   B CG    1 
ATOM   13488 C  CD    . ARG   B  1  620  ? 25.966  38.684  48.845  1.00 34.81 ? 618  ARG   B CD    1 
ATOM   13489 N  NE    . ARG   B  1  620  ? 27.296  38.636  49.442  1.00 41.27 ? 618  ARG   B NE    1 
ATOM   13490 C  CZ    . ARG   B  1  620  ? 28.034  37.539  49.528  1.00 34.38 ? 618  ARG   B CZ    1 
ATOM   13491 N  NH1   . ARG   B  1  620  ? 27.621  36.387  49.025  1.00 38.69 ? 618  ARG   B NH1   1 
ATOM   13492 N  NH2   . ARG   B  1  620  ? 29.222  37.602  50.122  1.00 42.06 ? 618  ARG   B NH2   1 
ATOM   13493 N  N     . LEU   B  1  621  ? 21.310  36.067  50.557  1.00 18.13 ? 619  LEU   B N     1 
ATOM   13494 C  CA    . LEU   B  1  621  ? 20.139  35.257  50.253  1.00 18.53 ? 619  LEU   B CA    1 
ATOM   13495 C  C     . LEU   B  1  621  ? 18.913  35.772  50.988  1.00 19.55 ? 619  LEU   B C     1 
ATOM   13496 O  O     . LEU   B  1  621  ? 17.808  35.781  50.433  1.00 20.67 ? 619  LEU   B O     1 
ATOM   13497 C  CB    . LEU   B  1  621  ? 20.408  33.797  50.614  1.00 20.02 ? 619  LEU   B CB    1 
ATOM   13498 C  CG    . LEU   B  1  621  ? 21.444  33.087  49.737  1.00 22.46 ? 619  LEU   B CG    1 
ATOM   13499 C  CD1   . LEU   B  1  621  ? 21.792  31.719  50.306  1.00 22.59 ? 619  LEU   B CD1   1 
ATOM   13500 C  CD2   . LEU   B  1  621  ? 20.930  32.951  48.313  1.00 27.85 ? 619  LEU   B CD2   1 
ATOM   13501 N  N     . ALA   B  1  622  ? 19.086  36.202  52.239  1.00 18.09 ? 620  ALA   B N     1 
ATOM   13502 C  CA    . ALA   B  1  622  ? 17.965  36.766  52.979  1.00 18.92 ? 620  ALA   B CA    1 
ATOM   13503 C  C     . ALA   B  1  622  ? 17.481  38.066  52.344  1.00 17.89 ? 620  ALA   B C     1 
ATOM   13504 O  O     . ALA   B  1  622  ? 16.269  38.298  52.236  1.00 17.29 ? 620  ALA   B O     1 
ATOM   13505 C  CB    . ALA   B  1  622  ? 18.356  36.983  54.439  1.00 18.46 ? 620  ALA   B CB    1 
ATOM   13506 N  N     . ALA   B  1  623  ? 18.415  38.909  51.897  1.00 17.20 ? 621  ALA   B N     1 
ATOM   13507 C  CA    . ALA   B  1  623  ? 18.040  40.155  51.236  1.00 18.26 ? 621  ALA   B CA    1 
ATOM   13508 C  C     . ALA   B  1  623  ? 17.261  39.884  49.957  1.00 19.23 ? 621  ALA   B C     1 
ATOM   13509 O  O     . ALA   B  1  623  ? 16.248  40.543  49.685  1.00 21.65 ? 621  ALA   B O     1 
ATOM   13510 C  CB    . ALA   B  1  623  ? 19.291  40.972  50.927  1.00 19.66 ? 621  ALA   B CB    1 
ATOM   13511 N  N     . ASP   B  1  624  ? 17.704  38.897  49.173  1.00 21.14 ? 622  ASP   B N     1 
ATOM   13512 C  CA    . ASP   B  1  624  ? 17.004  38.575  47.935  1.00 22.07 ? 622  ASP   B CA    1 
ATOM   13513 C  C     . ASP   B  1  624  ? 15.582  38.127  48.217  1.00 24.15 ? 622  ASP   B C     1 
ATOM   13514 O  O     . ASP   B  1  624  ? 14.659  38.445  47.459  1.00 30.77 ? 622  ASP   B O     1 
ATOM   13515 C  CB    . ASP   B  1  624  ? 17.744  37.465  47.189  1.00 26.81 ? 622  ASP   B CB    1 
ATOM   13516 C  CG    . ASP   B  1  624  ? 19.119  37.889  46.703  1.00 30.34 ? 622  ASP   B CG    1 
ATOM   13517 O  OD1   . ASP   B  1  624  ? 19.375  39.102  46.552  1.00 36.98 ? 622  ASP   B OD1   1 
ATOM   13518 O  OD2   . ASP   B  1  624  ? 19.949  36.988  46.456  1.00 36.37 ? 622  ASP   B OD2   1 
ATOM   13519 N  N     . ALA   B  1  625  ? 15.387  37.392  49.304  1.00 22.42 ? 623  ALA   B N     1 
ATOM   13520 C  CA    . ALA   B  1  625  ? 14.089  36.836  49.637  1.00 27.21 ? 623  ALA   B CA    1 
ATOM   13521 C  C     . ALA   B  1  625  ? 13.244  37.776  50.476  1.00 24.51 ? 623  ALA   B C     1 
ATOM   13522 O  O     . ALA   B  1  625  ? 12.081  37.461  50.754  1.00 23.71 ? 623  ALA   B O     1 
ATOM   13523 C  CB    . ALA   B  1  625  ? 14.277  35.532  50.400  1.00 31.35 ? 623  ALA   B CB    1 
ATOM   13524 N  N     . ALA   B  1  626  ? 13.791  38.912  50.893  1.00 21.67 ? 624  ALA   B N     1 
ATOM   13525 C  CA    . ALA   B  1  626  ? 13.053  39.777  51.809  1.00 21.04 ? 624  ALA   B CA    1 
ATOM   13526 C  C     . ALA   B  1  626  ? 11.709  40.229  51.257  1.00 20.85 ? 624  ALA   B C     1 
ATOM   13527 O  O     . ALA   B  1  626  ? 10.707  40.136  51.986  1.00 20.82 ? 624  ALA   B O     1 
ATOM   13528 C  CB    . ALA   B  1  626  ? 13.937  40.925  52.314  1.00 19.19 ? 624  ALA   B CB    1 
ATOM   13529 N  N     . PRO   B  1  627  ? 11.593  40.687  50.009  1.00 21.91 ? 625  PRO   B N     1 
ATOM   13530 C  CA    . PRO   B  1  627  ? 10.265  41.099  49.525  1.00 21.84 ? 625  PRO   B CA    1 
ATOM   13531 C  C     . PRO   B  1  627  ? 9.235   39.983  49.540  1.00 22.64 ? 625  PRO   B C     1 
ATOM   13532 O  O     . PRO   B  1  627  ? 8.063   40.237  49.853  1.00 21.98 ? 625  PRO   B O     1 
ATOM   13533 C  CB    . PRO   B  1  627  ? 10.544  41.594  48.095  1.00 23.19 ? 625  PRO   B CB    1 
ATOM   13534 C  CG    . PRO   B  1  627  ? 11.999  41.921  48.078  1.00 29.66 ? 625  PRO   B CG    1 
ATOM   13535 C  CD    . PRO   B  1  627  ? 12.657  40.977  49.028  1.00 23.93 ? 625  PRO   B CD    1 
ATOM   13536 N  N     . ASP   B  1  628  ? 9.630   38.753  49.199  1.00 20.49 ? 626  ASP   B N     1 
ATOM   13537 C  CA    . ASP   B  1  628  ? 8.663   37.662  49.149  1.00 21.79 ? 626  ASP   B CA    1 
ATOM   13538 C  C     . ASP   B  1  628  ? 8.109   37.353  50.530  1.00 22.67 ? 626  ASP   B C     1 
ATOM   13539 O  O     . ASP   B  1  628  ? 6.919   37.054  50.675  1.00 23.53 ? 626  ASP   B O     1 
ATOM   13540 C  CB    . ASP   B  1  628  ? 9.293   36.399  48.568  1.00 24.34 ? 626  ASP   B CB    1 
ATOM   13541 C  CG    . ASP   B  1  628  ? 9.593   36.517  47.090  1.00 33.37 ? 626  ASP   B CG    1 
ATOM   13542 O  OD1   . ASP   B  1  628  ? 8.947   37.337  46.396  1.00 35.12 ? 626  ASP   B OD1   1 
ATOM   13543 O  OD2   . ASP   B  1  628  ? 10.484  35.779  46.632  1.00 36.29 ? 626  ASP   B OD2   1 
ATOM   13544 N  N     . TRP   B  1  629  ? 8.953   37.409  51.560  1.00 17.74 ? 627  TRP   B N     1 
ATOM   13545 C  CA    . TRP   B  1  629  ? 8.454   37.127  52.896  1.00 16.86 ? 627  TRP   B CA    1 
ATOM   13546 C  C     . TRP   B  1  629  ? 7.632   38.294  53.428  1.00 18.36 ? 627  TRP   B C     1 
ATOM   13547 O  O     . TRP   B  1  629  ? 6.604   38.091  54.086  1.00 19.02 ? 627  TRP   B O     1 
ATOM   13548 C  CB    . TRP   B  1  629  ? 9.623   36.797  53.819  1.00 17.21 ? 627  TRP   B CB    1 
ATOM   13549 C  CG    . TRP   B  1  629  ? 9.184   36.523  55.204  1.00 15.66 ? 627  TRP   B CG    1 
ATOM   13550 C  CD1   . TRP   B  1  629  ? 9.544   37.216  56.333  1.00 17.92 ? 627  TRP   B CD1   1 
ATOM   13551 C  CD2   . TRP   B  1  629  ? 8.291   35.495  55.631  1.00 16.95 ? 627  TRP   B CD2   1 
ATOM   13552 N  NE1   . TRP   B  1  629  ? 8.929   36.670  57.427  1.00 17.96 ? 627  TRP   B NE1   1 
ATOM   13553 C  CE2   . TRP   B  1  629  ? 8.155   35.615  57.028  1.00 17.26 ? 627  TRP   B CE2   1 
ATOM   13554 C  CE3   . TRP   B  1  629  ? 7.591   34.480  54.973  1.00 18.34 ? 627  TRP   B CE3   1 
ATOM   13555 C  CZ2   . TRP   B  1  629  ? 7.339   34.763  57.774  1.00 16.50 ? 627  TRP   B CZ2   1 
ATOM   13556 C  CZ3   . TRP   B  1  629  ? 6.785   33.639  55.721  1.00 18.54 ? 627  TRP   B CZ3   1 
ATOM   13557 C  CH2   . TRP   B  1  629  ? 6.667   33.784  57.100  1.00 19.27 ? 627  TRP   B CH2   1 
ATOM   13558 N  N     . ALA   B  1  630  ? 8.059   39.521  53.145  1.00 18.52 ? 628  ALA   B N     1 
ATOM   13559 C  CA    . ALA   B  1  630  ? 7.275   40.669  53.575  1.00 18.78 ? 628  ALA   B CA    1 
ATOM   13560 C  C     . ALA   B  1  630  ? 5.886   40.639  52.960  1.00 20.10 ? 628  ALA   B C     1 
ATOM   13561 O  O     . ALA   B  1  630  ? 4.936   41.155  53.554  1.00 20.99 ? 628  ALA   B O     1 
ATOM   13562 C  CB    . ALA   B  1  630  ? 7.988   41.968  53.216  1.00 21.13 ? 628  ALA   B CB    1 
ATOM   13563 N  N     . ALA   B  1  631  ? 5.747   40.022  51.786  1.00 19.21 ? 629  ALA   B N     1 
ATOM   13564 C  CA    . ALA   B  1  631  ? 4.466   39.977  51.100  1.00 20.49 ? 629  ALA   B CA    1 
ATOM   13565 C  C     . ALA   B  1  631  ? 3.531   38.912  51.651  1.00 21.83 ? 629  ALA   B C     1 
ATOM   13566 O  O     . ALA   B  1  631  ? 2.352   38.898  51.282  1.00 22.17 ? 629  ALA   B O     1 
ATOM   13567 C  CB    . ALA   B  1  631  ? 4.682   39.760  49.600  1.00 22.31 ? 629  ALA   B CB    1 
ATOM   13568 N  N     . VAL   B  1  632  ? 4.011   38.036  52.526  1.00 19.58 ? 630  VAL   B N     1 
ATOM   13569 C  CA    . VAL   B  1  632  ? 3.123   37.070  53.158  1.00 19.73 ? 630  VAL   B CA    1 
ATOM   13570 C  C     . VAL   B  1  632  ? 2.319   37.874  54.165  1.00 20.62 ? 630  VAL   B C     1 
ATOM   13571 O  O     . VAL   B  1  632  ? 2.915   38.570  55.003  1.00 20.47 ? 630  VAL   B O     1 
ATOM   13572 C  CB    . VAL   B  1  632  ? 3.902   35.934  53.836  1.00 19.73 ? 630  VAL   B CB    1 
ATOM   13573 C  CG1   . VAL   B  1  632  ? 2.931   35.018  54.576  1.00 19.48 ? 630  VAL   B CG1   1 
ATOM   13574 C  CG2   . VAL   B  1  632  ? 4.689   35.149  52.804  1.00 20.65 ? 630  VAL   B CG2   1 
ATOM   13575 N  N     . PRO   B  1  633  ? 0.991   37.826  54.110  1.00 17.81 ? 631  PRO   B N     1 
ATOM   13576 C  CA    . PRO   B  1  633  ? 0.174   38.644  55.011  1.00 19.05 ? 631  PRO   B CA    1 
ATOM   13577 C  C     . PRO   B  1  633  ? 0.518   38.361  56.460  1.00 18.96 ? 631  PRO   B C     1 
ATOM   13578 O  O     . PRO   B  1  633  ? 0.813   37.217  56.824  1.00 17.42 ? 631  PRO   B O     1 
ATOM   13579 C  CB    . PRO   B  1  633  ? -1.257  38.190  54.695  1.00 19.30 ? 631  PRO   B CB    1 
ATOM   13580 C  CG    . PRO   B  1  633  ? -1.184  37.732  53.262  1.00 23.39 ? 631  PRO   B CG    1 
ATOM   13581 C  CD    . PRO   B  1  633  ? 0.177   37.089  53.129  1.00 19.16 ? 631  PRO   B CD    1 
ATOM   13582 N  N     . PRO   B  1  634  ? 0.495   39.382  57.311  1.00 17.99 ? 632  PRO   B N     1 
ATOM   13583 C  CA    . PRO   B  1  634  ? 0.820   39.169  58.731  1.00 18.86 ? 632  PRO   B CA    1 
ATOM   13584 C  C     . PRO   B  1  634  ? 0.050   38.032  59.373  1.00 16.14 ? 632  PRO   B C     1 
ATOM   13585 O  O     . PRO   B  1  634  ? 0.636   37.274  60.154  1.00 17.56 ? 632  PRO   B O     1 
ATOM   13586 C  CB    . PRO   B  1  634  ? 0.473   40.516  59.380  1.00 20.60 ? 632  PRO   B CB    1 
ATOM   13587 C  CG    . PRO   B  1  634  ? 0.603   41.510  58.273  1.00 23.48 ? 632  PRO   B CG    1 
ATOM   13588 C  CD    . PRO   B  1  634  ? 0.323   40.801  56.967  1.00 19.55 ? 632  PRO   B CD    1 
ATOM   13589 N  N     . SER   B  1  635  ? -1.243  37.882  59.076  1.00 18.76 ? 633  SER   B N     1 
ATOM   13590 C  CA    . SER   B  1  635  ? -1.996  36.797  59.691  1.00 20.73 ? 633  SER   B CA    1 
ATOM   13591 C  C     . SER   B  1  635  ? -1.466  35.437  59.260  1.00 16.69 ? 633  SER   B C     1 
ATOM   13592 O  O     . SER   B  1  635  ? -1.494  34.485  60.045  1.00 19.00 ? 633  SER   B O     1 
ATOM   13593 C  CB    . SER   B  1  635  ? -3.486  36.918  59.358  1.00 23.84 ? 633  SER   B CB    1 
ATOM   13594 O  OG    . SER   B  1  635  ? -3.694  36.844  57.962  1.00 32.32 ? 633  SER   B OG    1 
ATOM   13595 N  N     . GLU   B  1  636  ? -0.962  35.322  58.027  1.00 17.37 ? 634  GLU   B N     1 
ATOM   13596 C  CA    . GLU   B  1  636  ? -0.383  34.049  57.614  1.00 18.09 ? 634  GLU   B CA    1 
ATOM   13597 C  C     . GLU   B  1  636  ? 1.009   33.849  58.196  1.00 17.57 ? 634  GLU   B C     1 
ATOM   13598 O  O     . GLU   B  1  636  ? 1.391   32.714  58.498  1.00 17.77 ? 634  GLU   B O     1 
ATOM   13599 C  CB    . GLU   B  1  636  ? -0.336  33.931  56.093  1.00 19.64 ? 634  GLU   B CB    1 
ATOM   13600 C  CG    . GLU   B  1  636  ? 0.255   32.594  55.606  1.00 31.59 ? 634  GLU   B CG    1 
ATOM   13601 C  CD    . GLU   B  1  636  ? -0.323  31.367  56.332  1.00 35.72 ? 634  GLU   B CD    1 
ATOM   13602 O  OE1   . GLU   B  1  636  ? -1.570  31.230  56.405  1.00 34.94 ? 634  GLU   B OE1   1 
ATOM   13603 O  OE2   . GLU   B  1  636  ? 0.476   30.536  56.837  1.00 29.07 ? 634  GLU   B OE2   1 
ATOM   13604 N  N     . ARG   B  1  637  ? 1.782   34.921  58.364  1.00 15.50 ? 635  ARG   B N     1 
ATOM   13605 C  CA    . ARG   B  1  637  ? 3.043   34.765  59.079  1.00 15.45 ? 635  ARG   B CA    1 
ATOM   13606 C  C     . ARG   B  1  637  ? 2.780   34.327  60.514  1.00 16.44 ? 635  ARG   B C     1 
ATOM   13607 O  O     . ARG   B  1  637  ? 3.470   33.443  61.043  1.00 15.50 ? 635  ARG   B O     1 
ATOM   13608 C  CB    . ARG   B  1  637  ? 3.831   36.068  59.034  1.00 16.62 ? 635  ARG   B CB    1 
ATOM   13609 C  CG    . ARG   B  1  637  ? 4.124   36.549  57.619  1.00 16.23 ? 635  ARG   B CG    1 
ATOM   13610 C  CD    . ARG   B  1  637  ? 5.153   37.661  57.623  1.00 16.67 ? 635  ARG   B CD    1 
ATOM   13611 N  NE    . ARG   B  1  637  ? 4.764   38.803  58.443  1.00 17.39 ? 635  ARG   B NE    1 
ATOM   13612 C  CZ    . ARG   B  1  637  ? 4.488   40.014  57.981  1.00 18.90 ? 635  ARG   B CZ    1 
ATOM   13613 N  NH1   . ARG   B  1  637  ? 4.365   40.253  56.682  1.00 21.99 ? 635  ARG   B NH1   1 
ATOM   13614 N  NH2   . ARG   B  1  637  ? 4.343   41.013  58.841  1.00 17.40 ? 635  ARG   B NH2   1 
ATOM   13615 N  N     . ALA   B  1  638  ? 1.762   34.920  61.148  1.00 14.83 ? 636  ALA   B N     1 
ATOM   13616 C  CA    . ALA   B  1  638  ? 1.392   34.519  62.503  1.00 14.98 ? 636  ALA   B CA    1 
ATOM   13617 C  C     . ALA   B  1  638  ? 0.937   33.067  62.544  1.00 15.43 ? 636  ALA   B C     1 
ATOM   13618 O  O     . ALA   B  1  638  ? 1.214   32.351  63.510  1.00 15.13 ? 636  ALA   B O     1 
ATOM   13619 C  CB    . ALA   B  1  638  ? 0.301   35.446  63.053  1.00 15.80 ? 636  ALA   B CB    1 
ATOM   13620 N  N     . ALA   B  1  639  ? 0.225   32.610  61.506  1.00 16.98 ? 637  ALA   B N     1 
ATOM   13621 C  CA    . ALA   B  1  639  ? -0.206  31.214  61.474  1.00 17.05 ? 637  ALA   B CA    1 
ATOM   13622 C  C     . ALA   B  1  639  ? 0.978   30.256  61.452  1.00 16.50 ? 637  ALA   B C     1 
ATOM   13623 O  O     . ALA   B  1  639  ? 0.900   29.159  62.015  1.00 16.85 ? 637  ALA   B O     1 
ATOM   13624 C  CB    . ALA   B  1  639  ? -1.112  30.971  60.269  1.00 16.75 ? 637  ALA   B CB    1 
ATOM   13625 N  N     . CYS   B  1  640  ? 2.080   30.644  60.807  1.00 15.49 ? 638  CYS   B N     1 
ATOM   13626 C  CA    . CYS   B  1  640  ? 3.283   29.821  60.849  1.00 15.31 ? 638  CYS   B CA    1 
ATOM   13627 C  C     . CYS   B  1  640  ? 3.806   29.708  62.265  1.00 12.96 ? 638  CYS   B C     1 
ATOM   13628 O  O     . CYS   B  1  640  ? 4.187   28.621  62.708  1.00 14.88 ? 638  CYS   B O     1 
ATOM   13629 C  CB    . CYS   B  1  640  ? 4.384   30.438  59.994  1.00 15.45 ? 638  CYS   B CB    1 
ATOM   13630 S  SG    . CYS   B  1  640  ? 4.079   30.410  58.245  1.00 19.12 ? 638  CYS   B SG    1 
ATOM   13631 N  N     . LEU   B  1  641  ? 3.839   30.829  62.990  1.00 14.21 ? 639  LEU   B N     1 
ATOM   13632 C  CA    . LEU   B  1  641  ? 4.272   30.789  64.379  1.00 13.88 ? 639  LEU   B CA    1 
ATOM   13633 C  C     . LEU   B  1  641  ? 3.366   29.877  65.193  1.00 14.83 ? 639  LEU   B C     1 
ATOM   13634 O  O     . LEU   B  1  641  ? 3.848   29.063  65.995  1.00 13.86 ? 639  LEU   B O     1 
ATOM   13635 C  CB    . LEU   B  1  641  ? 4.275   32.198  64.977  1.00 14.58 ? 639  LEU   B CB    1 
ATOM   13636 C  CG    . LEU   B  1  641  ? 5.541   33.039  64.828  1.00 15.21 ? 639  LEU   B CG    1 
ATOM   13637 C  CD1   . LEU   B  1  641  ? 5.962   33.242  63.373  1.00 17.43 ? 639  LEU   B CD1   1 
ATOM   13638 C  CD2   . LEU   B  1  641  ? 5.369   34.374  65.527  1.00 14.52 ? 639  LEU   B CD2   1 
ATOM   13639 N  N     . ASP   B  1  642  ? 2.050   29.995  64.997  1.00 13.94 ? 640  ASP   B N     1 
ATOM   13640 C  CA    . ASP   B  1  642  ? 1.135   29.144  65.748  1.00 13.99 ? 640  ASP   B CA    1 
ATOM   13641 C  C     . ASP   B  1  642  ? 1.326   27.683  65.380  1.00 14.76 ? 640  ASP   B C     1 
ATOM   13642 O  O     . ASP   B  1  642  ? 1.270   26.808  66.246  1.00 14.85 ? 640  ASP   B O     1 
ATOM   13643 C  CB    . ASP   B  1  642  ? -0.308  29.564  65.502  1.00 15.45 ? 640  ASP   B CB    1 
ATOM   13644 C  CG    . ASP   B  1  642  ? -0.713  30.768  66.313  1.00 19.96 ? 640  ASP   B CG    1 
ATOM   13645 O  OD1   . ASP   B  1  642  ? -0.064  31.050  67.331  1.00 19.95 ? 640  ASP   B OD1   1 
ATOM   13646 O  OD2   . ASP   B  1  642  ? -1.706  31.425  65.939  1.00 19.31 ? 640  ASP   B OD2   1 
ATOM   13647 N  N     . ARG   B  1  643  ? 1.573   27.395  64.099  1.00 15.15 ? 641  ARG   B N     1 
ATOM   13648 C  CA    . ARG   B  1  643  ? 1.847   26.008  63.730  1.00 17.21 ? 641  ARG   B CA    1 
ATOM   13649 C  C     . ARG   B  1  643  ? 3.125   25.513  64.385  1.00 16.58 ? 641  ARG   B C     1 
ATOM   13650 O  O     . ARG   B  1  643  ? 3.192   24.369  64.851  1.00 15.35 ? 641  ARG   B O     1 
ATOM   13651 C  CB    . ARG   B  1  643  ? 1.912   25.864  62.213  1.00 15.80 ? 641  ARG   B CB    1 
ATOM   13652 C  CG    . ARG   B  1  643  ? 0.515   25.753  61.601  1.00 19.27 ? 641  ARG   B CG    1 
ATOM   13653 C  CD    . ARG   B  1  643  ? 0.584   25.370  60.139  1.00 22.12 ? 641  ARG   B CD    1 
ATOM   13654 N  NE    . ARG   B  1  643  ? 1.276   26.380  59.348  1.00 20.29 ? 641  ARG   B NE    1 
ATOM   13655 C  CZ    . ARG   B  1  643  ? 0.687   27.393  58.732  1.00 21.15 ? 641  ARG   B CZ    1 
ATOM   13656 N  NH1   . ARG   B  1  643  ? -0.624  27.575  58.793  1.00 22.53 ? 641  ARG   B NH1   1 
ATOM   13657 N  NH2   . ARG   B  1  643  ? 1.432   28.244  58.030  1.00 24.94 ? 641  ARG   B NH2   1 
ATOM   13658 N  N     . ALA   B  1  644  ? 4.151   26.360  64.431  1.00 13.79 ? 642  ALA   B N     1 
ATOM   13659 C  CA    . ALA   B  1  644  ? 5.398   25.950  65.062  1.00 15.19 ? 642  ALA   B CA    1 
ATOM   13660 C  C     . ALA   B  1  644  ? 5.178   25.655  66.534  1.00 15.74 ? 642  ALA   B C     1 
ATOM   13661 O  O     . ALA   B  1  644  ? 5.739   24.698  67.077  1.00 15.02 ? 642  ALA   B O     1 
ATOM   13662 C  CB    . ALA   B  1  644  ? 6.457   27.028  64.860  1.00 15.22 ? 642  ALA   B CB    1 
ATOM   13663 N  N     . ALA   B  1  645  ? 4.326   26.451  67.188  1.00 15.02 ? 643  ALA   B N     1 
ATOM   13664 C  CA    . ALA   B  1  645  ? 4.063   26.213  68.598  1.00 15.54 ? 643  ALA   B CA    1 
ATOM   13665 C  C     . ALA   B  1  645  ? 3.376   24.873  68.809  1.00 15.76 ? 643  ALA   B C     1 
ATOM   13666 O  O     . ALA   B  1  645  ? 3.690   24.159  69.770  1.00 16.31 ? 643  ALA   B O     1 
ATOM   13667 C  CB    . ALA   B  1  645  ? 3.237   27.358  69.178  1.00 13.97 ? 643  ALA   B CB    1 
ATOM   13668 N  N     . GLU   B  1  646  ? 2.435   24.519  67.926  1.00 14.78 ? 644  GLU   B N     1 
ATOM   13669 C  CA    . GLU   B  1  646  ? 1.773   23.218  68.034  1.00 18.68 ? 644  GLU   B CA    1 
ATOM   13670 C  C     . GLU   B  1  646  ? 2.781   22.088  67.898  1.00 16.83 ? 644  GLU   B C     1 
ATOM   13671 O  O     . GLU   B  1  646  ? 2.709   21.088  68.622  1.00 17.25 ? 644  GLU   B O     1 
ATOM   13672 C  CB    . GLU   B  1  646  ? 0.703   23.072  66.946  1.00 20.72 ? 644  GLU   B CB    1 
ATOM   13673 C  CG    . GLU   B  1  646  ? -0.489  23.982  67.121  1.00 24.39 ? 644  GLU   B CG    1 
ATOM   13674 C  CD    . GLU   B  1  646  ? -1.237  23.711  68.411  1.00 31.37 ? 644  GLU   B CD    1 
ATOM   13675 O  OE1   . GLU   B  1  646  ? -1.430  22.524  68.757  1.00 41.23 ? 644  GLU   B OE1   1 
ATOM   13676 O  OE2   . GLU   B  1  646  ? -1.622  24.688  69.090  1.00 37.09 ? 644  GLU   B OE2   1 
ATOM   13677 N  N     . LEU   B  1  647  ? 3.732   22.232  66.969  1.00 16.90 ? 645  LEU   B N     1 
ATOM   13678 C  CA    . LEU   B  1  647  ? 4.754   21.201  66.795  1.00 18.75 ? 645  LEU   B CA    1 
ATOM   13679 C  C     . LEU   B  1  647  ? 5.664   21.107  68.010  1.00 17.23 ? 645  LEU   B C     1 
ATOM   13680 O  O     . LEU   B  1  647  ? 5.991   20.006  68.469  1.00 18.43 ? 645  LEU   B O     1 
ATOM   13681 C  CB    . LEU   B  1  647  ? 5.588   21.488  65.549  1.00 16.18 ? 645  LEU   B CB    1 
ATOM   13682 C  CG    . LEU   B  1  647  ? 4.822   21.467  64.236  1.00 17.43 ? 645  LEU   B CG    1 
ATOM   13683 C  CD1   . LEU   B  1  647  ? 5.769   21.802  63.098  1.00 18.26 ? 645  LEU   B CD1   1 
ATOM   13684 C  CD2   . LEU   B  1  647  ? 4.171   20.110  64.026  1.00 21.73 ? 645  LEU   B CD2   1 
ATOM   13685 N  N     . MET   B  1  648  ? 6.089   22.247  68.550  1.00 12.85 ? 646  MET   B N     1 
ATOM   13686 C  CA    . MET   B  1  648  ? 6.947   22.192  69.728  1.00 14.55 ? 646  MET   B CA    1 
ATOM   13687 C  C     . MET   B  1  648  ? 6.207   21.593  70.911  1.00 15.93 ? 646  MET   B C     1 
ATOM   13688 O  O     . MET   B  1  648  ? 6.800   20.887  71.728  1.00 17.72 ? 646  MET   B O     1 
ATOM   13689 C  CB    . MET   B  1  648  ? 7.448   23.578  70.099  1.00 17.82 ? 646  MET   B CB    1 
ATOM   13690 C  CG    . MET   B  1  648  ? 8.558   24.058  69.228  1.00 18.53 ? 646  MET   B CG    1 
ATOM   13691 S  SD    . MET   B  1  648  ? 9.270   25.507  70.009  1.00 19.41 ? 646  MET   B SD    1 
ATOM   13692 C  CE    . MET   B  1  648  ? 10.335  26.043  68.681  1.00 21.68 ? 646  MET   B CE    1 
ATOM   13693 N  N     . GLN   B  1  649  ? 4.912   21.893  71.039  1.00 14.86 ? 647  GLN   B N     1 
ATOM   13694 C  CA    . GLN   B  1  649  ? 4.142   21.314  72.132  1.00 16.20 ? 647  GLN   B CA    1 
ATOM   13695 C  C     . GLN   B  1  649  ? 4.068   19.803  71.985  1.00 15.27 ? 647  GLN   B C     1 
ATOM   13696 O  O     . GLN   B  1  649  ? 4.258   19.063  72.957  1.00 19.48 ? 647  GLN   B O     1 
ATOM   13697 C  CB    . GLN   B  1  649  ? 2.733   21.899  72.131  1.00 15.99 ? 647  GLN   B CB    1 
ATOM   13698 C  CG    . GLN   B  1  649  ? 1.892   21.442  73.308  1.00 18.00 ? 647  GLN   B CG    1 
ATOM   13699 C  CD    . GLN   B  1  649  ? 2.338   22.095  74.590  1.00 18.18 ? 647  GLN   B CD    1 
ATOM   13700 O  OE1   . GLN   B  1  649  ? 2.012   23.259  74.853  1.00 17.93 ? 647  GLN   B OE1   1 
ATOM   13701 N  NE2   . GLN   B  1  649  ? 3.105   21.363  75.397  1.00 18.94 ? 647  GLN   B NE2   1 
ATOM   13702 N  N     . ALA   B  1  650  ? 3.770   19.329  70.771  1.00 16.33 ? 648  ALA   B N     1 
ATOM   13703 C  CA    . ALA   B  1  650  ? 3.618   17.895  70.556  1.00 17.48 ? 648  ALA   B CA    1 
ATOM   13704 C  C     . ALA   B  1  650  ? 4.939   17.165  70.723  1.00 19.56 ? 648  ALA   B C     1 
ATOM   13705 O  O     . ALA   B  1  650  ? 4.962   16.020  71.182  1.00 21.96 ? 648  ALA   B O     1 
ATOM   13706 C  CB    . ALA   B  1  650  ? 3.044   17.631  69.164  1.00 19.84 ? 648  ALA   B CB    1 
ATOM   13707 N  N     . ARG   B  1  651  ? 6.044   17.819  70.383  1.00 17.22 ? 649  ARG   B N     1 
ATOM   13708 C  CA    . ARG   B  1  651  ? 7.359   17.211  70.438  1.00 17.33 ? 649  ARG   B CA    1 
ATOM   13709 C  C     . ARG   B  1  651  ? 8.116   17.570  71.699  1.00 17.87 ? 649  ARG   B C     1 
ATOM   13710 O  O     . ARG   B  1  651  ? 9.303   17.252  71.807  1.00 18.79 ? 649  ARG   B O     1 
ATOM   13711 C  CB    . ARG   B  1  651  ? 8.138   17.606  69.192  1.00 17.82 ? 649  ARG   B CB    1 
ATOM   13712 C  CG    . ARG   B  1  651  ? 7.425   17.074  67.975  1.00 19.15 ? 649  ARG   B CG    1 
ATOM   13713 C  CD    . ARG   B  1  651  ? 8.015   17.602  66.702  1.00 21.08 ? 649  ARG   B CD    1 
ATOM   13714 N  NE    . ARG   B  1  651  ? 7.131   17.292  65.592  1.00 21.93 ? 649  ARG   B NE    1 
ATOM   13715 C  CZ    . ARG   B  1  651  ? 7.339   17.719  64.359  1.00 23.11 ? 649  ARG   B CZ    1 
ATOM   13716 N  NH1   . ARG   B  1  651  ? 8.428   18.409  64.049  1.00 20.44 ? 649  ARG   B NH1   1 
ATOM   13717 N  NH2   . ARG   B  1  651  ? 6.437   17.446  63.418  1.00 22.94 ? 649  ARG   B NH2   1 
ATOM   13718 N  N     . MET   B  1  652  ? 7.453   18.211  72.657  1.00 17.58 ? 650  MET   B N     1 
ATOM   13719 C  CA    . MET   B  1  652  ? 8.118   18.591  73.901  1.00 17.09 ? 650  MET   B CA    1 
ATOM   13720 C  C     . MET   B  1  652  ? 8.947   17.474  74.528  1.00 18.82 ? 650  MET   B C     1 
ATOM   13721 O  O     . MET   B  1  652  ? 10.092  17.745  74.908  1.00 19.16 ? 650  MET   B O     1 
ATOM   13722 C  CB    . MET   B  1  652  ? 7.110   19.210  74.881  1.00 17.21 ? 650  MET   B CB    1 
ATOM   13723 C  CG    . MET   B  1  652  ? 7.765   19.583  76.202  1.00 17.02 ? 650  MET   B CG    1 
ATOM   13724 S  SD    . MET   B  1  652  ? 6.565   20.290  77.353  1.00 20.65 ? 650  MET   B SD    1 
ATOM   13725 C  CE    . MET   B  1  652  ? 6.294   21.881  76.592  1.00 19.29 ? 650  MET   B CE    1 
ATOM   13726 N  N     . PRO   B  1  653  ? 8.467   16.232  74.657  1.00 17.96 ? 651  PRO   B N     1 
ATOM   13727 C  CA    . PRO   B  1  653  ? 9.304   15.207  75.309  1.00 20.16 ? 651  PRO   B CA    1 
ATOM   13728 C  C     . PRO   B  1  653  ? 10.653  15.014  74.645  1.00 19.02 ? 651  PRO   B C     1 
ATOM   13729 O  O     . PRO   B  1  653  ? 11.672  14.925  75.343  1.00 19.93 ? 651  PRO   B O     1 
ATOM   13730 C  CB    . PRO   B  1  653  ? 8.432   13.949  75.235  1.00 20.31 ? 651  PRO   B CB    1 
ATOM   13731 C  CG    . PRO   B  1  653  ? 7.034   14.500  75.315  1.00 21.58 ? 651  PRO   B CG    1 
ATOM   13732 C  CD    . PRO   B  1  653  ? 7.096   15.733  74.426  1.00 19.57 ? 651  PRO   B CD    1 
ATOM   13733 N  N     . THR   B  1  654  ? 10.685  14.958  73.312  1.00 18.74 ? 652  THR   B N     1 
ATOM   13734 C  CA    . THR   B  1  654  ? 11.947  14.824  72.594  1.00 19.94 ? 652  THR   B CA    1 
ATOM   13735 C  C     . THR   B  1  654  ? 12.822  16.057  72.781  1.00 19.69 ? 652  THR   B C     1 
ATOM   13736 O  O     . THR   B  1  654  ? 14.029  15.945  73.021  1.00 19.42 ? 652  THR   B O     1 
ATOM   13737 C  CB    . THR   B  1  654  ? 11.663  14.599  71.109  1.00 21.24 ? 652  THR   B CB    1 
ATOM   13738 O  OG1   . THR   B  1  654  ? 10.868  13.421  70.959  1.00 21.61 ? 652  THR   B OG1   1 
ATOM   13739 C  CG2   . THR   B  1  654  ? 12.970  14.440  70.343  1.00 21.19 ? 652  THR   B CG2   1 
ATOM   13740 N  N     . LEU   B  1  655  ? 12.236  17.247  72.642  1.00 15.78 ? 653  LEU   B N     1 
ATOM   13741 C  CA    . LEU   B  1  655  ? 12.993  18.474  72.840  1.00 17.82 ? 653  LEU   B CA    1 
ATOM   13742 C  C     . LEU   B  1  655  ? 13.589  18.523  74.235  1.00 17.76 ? 653  LEU   B C     1 
ATOM   13743 O  O     . LEU   B  1  655  ? 14.734  18.956  74.409  1.00 18.40 ? 653  LEU   B O     1 
ATOM   13744 C  CB    . LEU   B  1  655  ? 12.087  19.679  72.620  1.00 17.28 ? 653  LEU   B CB    1 
ATOM   13745 C  CG    . LEU   B  1  655  ? 11.417  19.740  71.249  1.00 19.41 ? 653  LEU   B CG    1 
ATOM   13746 C  CD1   . LEU   B  1  655  ? 10.571  20.996  71.141  1.00 19.44 ? 653  LEU   B CD1   1 
ATOM   13747 C  CD2   . LEU   B  1  655  ? 12.467  19.695  70.165  1.00 22.31 ? 653  LEU   B CD2   1 
ATOM   13748 N  N     . LEU   B  1  656  ? 12.837  18.065  75.241  1.00 18.36 ? 654  LEU   B N     1 
ATOM   13749 C  CA    . LEU   B  1  656  ? 13.361  18.046  76.607  1.00 20.28 ? 654  LEU   B CA    1 
ATOM   13750 C  C     . LEU   B  1  656  ? 14.633  17.231  76.684  1.00 17.88 ? 654  LEU   B C     1 
ATOM   13751 O  O     . LEU   B  1  656  ? 15.609  17.637  77.325  1.00 20.48 ? 654  LEU   B O     1 
ATOM   13752 C  CB    . LEU   B  1  656  ? 12.356  17.401  77.556  1.00 21.83 ? 654  LEU   B CB    1 
ATOM   13753 C  CG    . LEU   B  1  656  ? 11.007  18.051  77.711  1.00 23.19 ? 654  LEU   B CG    1 
ATOM   13754 C  CD1   . LEU   B  1  656  ? 10.260  17.391  78.847  1.00 22.88 ? 654  LEU   B CD1   1 
ATOM   13755 C  CD2   . LEU   B  1  656  ? 11.172  19.534  77.929  1.00 21.86 ? 654  LEU   B CD2   1 
ATOM   13756 N  N     . GLY   B  1  657  ? 14.609  16.040  76.099  1.00 19.19 ? 655  GLY   B N     1 
ATOM   13757 C  CA    . GLY   B  1  657  ? 15.780  15.190  76.137  1.00 20.94 ? 655  GLY   B CA    1 
ATOM   13758 C  C     . GLY   B  1  657  ? 17.000  15.881  75.580  1.00 21.27 ? 655  GLY   B C     1 
ATOM   13759 O  O     . GLY   B  1  657  ? 18.084  15.808  76.159  1.00 20.77 ? 655  GLY   B O     1 
ATOM   13760 N  N     . LEU   B  1  658  ? 16.833  16.590  74.464  1.00 18.19 ? 656  LEU   B N     1 
ATOM   13761 C  CA    . LEU   B  1  658  ? 17.965  17.288  73.879  1.00 16.85 ? 656  LEU   B CA    1 
ATOM   13762 C  C     . LEU   B  1  658  ? 18.441  18.416  74.783  1.00 17.58 ? 656  LEU   B C     1 
ATOM   13763 O  O     . LEU   B  1  658  ? 19.646  18.574  75.011  1.00 17.42 ? 656  LEU   B O     1 
ATOM   13764 C  CB    . LEU   B  1  658  ? 17.588  17.794  72.487  1.00 17.01 ? 656  LEU   B CB    1 
ATOM   13765 C  CG    . LEU   B  1  658  ? 18.711  18.500  71.727  1.00 18.93 ? 656  LEU   B CG    1 
ATOM   13766 C  CD1   . LEU   B  1  658  ? 19.928  17.599  71.560  1.00 18.12 ? 656  LEU   B CD1   1 
ATOM   13767 C  CD2   . LEU   B  1  658  ? 18.183  18.946  70.375  1.00 18.93 ? 656  LEU   B CD2   1 
ATOM   13768 N  N     . ILE   B  1  659  ? 17.512  19.206  75.319  1.00 15.30 ? 657  ILE   B N     1 
ATOM   13769 C  CA    . ILE   B  1  659  ? 17.889  20.341  76.155  1.00 14.46 ? 657  ILE   B CA    1 
ATOM   13770 C  C     . ILE   B  1  659  ? 18.582  19.864  77.421  1.00 15.03 ? 657  ILE   B C     1 
ATOM   13771 O  O     . ILE   B  1  659  ? 19.565  20.461  77.879  1.00 17.31 ? 657  ILE   B O     1 
ATOM   13772 C  CB    . ILE   B  1  659  ? 16.643  21.181  76.473  1.00 15.97 ? 657  ILE   B CB    1 
ATOM   13773 C  CG1   . ILE   B  1  659  ? 16.145  21.853  75.197  1.00 17.49 ? 657  ILE   B CG1   1 
ATOM   13774 C  CG2   . ILE   B  1  659  ? 16.952  22.209  77.547  1.00 17.17 ? 657  ILE   B CG2   1 
ATOM   13775 C  CD1   . ILE   B  1  659  ? 14.708  22.328  75.320  1.00 17.44 ? 657  ILE   B CD1   1 
ATOM   13776 N  N     . ILE   B  1  660  ? 18.066  18.790  78.016  1.00 16.30 ? 658  ILE   B N     1 
ATOM   13777 C  CA    . ILE   B  1  660  ? 18.664  18.249  79.230  1.00 14.84 ? 658  ILE   B CA    1 
ATOM   13778 C  C     . ILE   B  1  660  ? 20.119  17.883  78.986  1.00 17.05 ? 658  ILE   B C     1 
ATOM   13779 O  O     . ILE   B  1  660  ? 21.005  18.192  79.798  1.00 18.99 ? 658  ILE   B O     1 
ATOM   13780 C  CB    . ILE   B  1  660  ? 17.846  17.033  79.700  1.00 17.25 ? 658  ILE   B CB    1 
ATOM   13781 C  CG1   . ILE   B  1  660  ? 16.513  17.492  80.300  1.00 17.50 ? 658  ILE   B CG1   1 
ATOM   13782 C  CG2   . ILE   B  1  660  ? 18.683  16.164  80.656  1.00 18.58 ? 658  ILE   B CG2   1 
ATOM   13783 C  CD1   . ILE   B  1  660  ? 15.559  16.346  80.579  1.00 20.79 ? 658  ILE   B CD1   1 
ATOM   13784 N  N     . ARG   B  1  661  ? 20.389  17.225  77.861  1.00 15.26 ? 659  ARG   B N     1 
ATOM   13785 C  CA    . ARG   B  1  661  ? 21.720  16.700  77.607  1.00 16.01 ? 659  ARG   B CA    1 
ATOM   13786 C  C     . ARG   B  1  661  ? 22.657  17.735  77.014  1.00 19.10 ? 659  ARG   B C     1 
ATOM   13787 O  O     . ARG   B  1  661  ? 23.860  17.685  77.284  1.00 18.15 ? 659  ARG   B O     1 
ATOM   13788 C  CB    . ARG   B  1  661  ? 21.647  15.455  76.728  1.00 16.71 ? 659  ARG   B CB    1 
ATOM   13789 C  CG    . ARG   B  1  661  ? 21.171  14.256  77.508  1.00 18.69 ? 659  ARG   B CG    1 
ATOM   13790 C  CD    . ARG   B  1  661  ? 21.025  13.028  76.633  1.00 22.59 ? 659  ARG   B CD    1 
ATOM   13791 N  NE    . ARG   B  1  661  ? 22.259  12.635  75.948  1.00 20.29 ? 659  ARG   B NE    1 
ATOM   13792 C  CZ    . ARG   B  1  661  ? 22.369  12.532  74.632  1.00 23.27 ? 659  ARG   B CZ    1 
ATOM   13793 N  NH1   . ARG   B  1  661  ? 21.366  12.850  73.828  1.00 25.34 ? 659  ARG   B NH1   1 
ATOM   13794 N  NH2   . ARG   B  1  661  ? 23.503  12.069  74.106  1.00 21.80 ? 659  ARG   B NH2   1 
ATOM   13795 N  N     . GLU   B  1  662  ? 22.148  18.666  76.214  1.00 17.89 ? 660  GLU   B N     1 
ATOM   13796 C  CA    . GLU   B  1  662  ? 23.023  19.641  75.569  1.00 17.73 ? 660  GLU   B CA    1 
ATOM   13797 C  C     . GLU   B  1  662  ? 23.325  20.828  76.476  1.00 19.25 ? 660  GLU   B C     1 
ATOM   13798 O  O     . GLU   B  1  662  ? 24.440  21.354  76.460  1.00 19.22 ? 660  GLU   B O     1 
ATOM   13799 C  CB    . GLU   B  1  662  ? 22.391  20.143  74.263  1.00 19.56 ? 660  GLU   B CB    1 
ATOM   13800 C  CG    . GLU   B  1  662  ? 23.300  21.132  73.498  1.00 20.39 ? 660  GLU   B CG    1 
ATOM   13801 C  CD    . GLU   B  1  662  ? 22.699  21.673  72.196  1.00 21.24 ? 660  GLU   B CD    1 
ATOM   13802 O  OE1   . GLU   B  1  662  ? 21.465  21.844  72.098  1.00 20.58 ? 660  GLU   B OE1   1 
ATOM   13803 O  OE2   . GLU   B  1  662  ? 23.489  21.946  71.272  1.00 20.42 ? 660  GLU   B OE2   1 
ATOM   13804 N  N     . ALA   B  1  663  ? 22.360  21.260  77.284  1.00 15.37 ? 661  ALA   B N     1 
ATOM   13805 C  CA    . ALA   B  1  663  ? 22.493  22.510  78.012  1.00 16.54 ? 661  ALA   B CA    1 
ATOM   13806 C  C     . ALA   B  1  663  ? 22.561  22.332  79.521  1.00 17.94 ? 661  ALA   B C     1 
ATOM   13807 O  O     . ALA   B  1  663  ? 22.533  23.329  80.244  1.00 25.54 ? 661  ALA   B O     1 
ATOM   13808 C  CB    . ALA   B  1  663  ? 21.385  23.490  77.627  1.00 18.85 ? 661  ALA   B CB    1 
ATOM   13809 N  N     . GLY   B  1  664  ? 22.637  21.097  80.014  1.00 19.62 ? 662  GLY   B N     1 
ATOM   13810 C  CA    . GLY   B  1  664  ? 22.752  20.905  81.451  1.00 22.24 ? 662  GLY   B CA    1 
ATOM   13811 C  C     . GLY   B  1  664  ? 21.508  21.224  82.240  1.00 21.06 ? 662  GLY   B C     1 
ATOM   13812 O  O     . GLY   B  1  664  ? 21.599  21.518  83.430  1.00 23.06 ? 662  GLY   B O     1 
ATOM   13813 N  N     . LYS   B  1  665  ? 20.344  21.184  81.613  1.00 17.86 ? 663  LYS   B N     1 
ATOM   13814 C  CA    . LYS   B  1  665  ? 19.115  21.553  82.293  1.00 17.60 ? 663  LYS   B CA    1 
ATOM   13815 C  C     . LYS   B  1  665  ? 18.481  20.331  82.933  1.00 15.97 ? 663  LYS   B C     1 
ATOM   13816 O  O     . LYS   B  1  665  ? 18.537  19.219  82.400  1.00 16.14 ? 663  LYS   B O     1 
ATOM   13817 C  CB    . LYS   B  1  665  ? 18.113  22.137  81.300  1.00 17.90 ? 663  LYS   B CB    1 
ATOM   13818 C  CG    . LYS   B  1  665  ? 18.605  23.339  80.530  1.00 23.07 ? 663  LYS   B CG    1 
ATOM   13819 C  CD    . LYS   B  1  665  ? 18.968  24.475  81.448  1.00 26.57 ? 663  LYS   B CD    1 
ATOM   13820 C  CE    . LYS   B  1  665  ? 19.406  25.698  80.650  1.00 27.43 ? 663  LYS   B CE    1 
ATOM   13821 N  NZ    . LYS   B  1  665  ? 19.908  26.789  81.543  1.00 29.83 ? 663  LYS   B NZ    1 
ATOM   13822 N  N     . SER   B  1  666  ? 17.832  20.560  84.068  1.00 18.19 ? 664  SER   B N     1 
ATOM   13823 C  CA    . SER   B  1  666  ? 16.963  19.554  84.642  1.00 18.05 ? 664  SER   B CA    1 
ATOM   13824 C  C     . SER   B  1  666  ? 15.676  19.458  83.831  1.00 20.19 ? 664  SER   B C     1 
ATOM   13825 O  O     . SER   B  1  666  ? 15.336  20.344  83.041  1.00 18.13 ? 664  SER   B O     1 
ATOM   13826 C  CB    . SER   B  1  666  ? 16.574  19.965  86.054  1.00 22.25 ? 664  SER   B CB    1 
ATOM   13827 O  OG    . SER   B  1  666  ? 15.713  21.096  85.998  1.00 23.79 ? 664  SER   B OG    1 
ATOM   13828 N  N     . ALA   B  1  667  ? 14.950  18.363  84.047  1.00 17.93 ? 665  ALA   B N     1 
ATOM   13829 C  CA    . ALA   B  1  667  ? 13.688  18.155  83.345  1.00 18.46 ? 665  ALA   B CA    1 
ATOM   13830 C  C     . ALA   B  1  667  ? 12.736  19.327  83.545  1.00 19.13 ? 665  ALA   B C     1 
ATOM   13831 O  O     . ALA   B  1  667  ? 12.132  19.805  82.581  1.00 16.87 ? 665  ALA   B O     1 
ATOM   13832 C  CB    . ALA   B  1  667  ? 13.043  16.854  83.818  1.00 20.14 ? 665  ALA   B CB    1 
ATOM   13833 N  N     . LEU   B  1  668  ? 12.581  19.805  84.787  1.00 18.77 ? 666  LEU   B N     1 
ATOM   13834 C  CA    . LEU   B  1  668  ? 11.648  20.904  85.023  1.00 21.76 ? 666  LEU   B CA    1 
ATOM   13835 C  C     . LEU   B  1  668  ? 12.066  22.153  84.268  1.00 17.87 ? 666  LEU   B C     1 
ATOM   13836 O  O     . LEU   B  1  668  ? 11.225  22.854  83.697  1.00 19.07 ? 666  LEU   B O     1 
ATOM   13837 C  CB    . LEU   B  1  668  ? 11.517  21.210  86.516  1.00 22.89 ? 666  LEU   B CB    1 
ATOM   13838 C  CG    . LEU   B  1  668  ? 10.482  20.380  87.264  1.00 29.10 ? 666  LEU   B CG    1 
ATOM   13839 C  CD1   . LEU   B  1  668  ? 10.449  20.764  88.737  1.00 32.74 ? 666  LEU   B CD1   1 
ATOM   13840 C  CD2   . LEU   B  1  668  ? 9.106   20.542  86.621  1.00 28.89 ? 666  LEU   B CD2   1 
ATOM   13841 N  N     . ASN   B  1  669  ? 13.361  22.452  84.249  1.00 17.11 ? 667  ASN   B N     1 
ATOM   13842 C  CA    . ASN   B  1  669  ? 13.768  23.661  83.546  1.00 18.75 ? 667  ASN   B CA    1 
ATOM   13843 C  C     . ASN   B  1  669  ? 13.749  23.484  82.039  1.00 20.45 ? 667  ASN   B C     1 
ATOM   13844 O  O     . ASN   B  1  669  ? 13.555  24.462  81.314  1.00 19.75 ? 667  ASN   B O     1 
ATOM   13845 C  CB    . ASN   B  1  669  ? 15.106  24.142  84.079  1.00 24.62 ? 667  ASN   B CB    1 
ATOM   13846 C  CG    . ASN   B  1  669  ? 14.975  24.653  85.486  1.00 27.64 ? 667  ASN   B CG    1 
ATOM   13847 O  OD1   . ASN   B  1  669  ? 13.972  25.297  85.827  1.00 31.62 ? 667  ASN   B OD1   1 
ATOM   13848 N  ND2   . ASN   B  1  669  ? 15.942  24.339  86.324  1.00 28.94 ? 667  ASN   B ND2   1 
ATOM   13849 N  N     . ALA   B  1  670  ? 13.932  22.256  81.553  1.00 15.31 ? 668  ALA   B N     1 
ATOM   13850 C  CA    . ALA   B  1  670  ? 13.762  22.011  80.126  1.00 16.48 ? 668  ALA   B CA    1 
ATOM   13851 C  C     . ALA   B  1  670  ? 12.308  22.178  79.711  1.00 16.13 ? 668  ALA   B C     1 
ATOM   13852 O  O     . ALA   B  1  670  ? 12.024  22.712  78.636  1.00 15.65 ? 668  ALA   B O     1 
ATOM   13853 C  CB    . ALA   B  1  670  ? 14.264  20.614  79.762  1.00 16.73 ? 668  ALA   B CB    1 
ATOM   13854 N  N     . ILE   B  1  671  ? 11.376  21.715  80.547  1.00 16.53 ? 669  ILE   B N     1 
ATOM   13855 C  CA    . ILE   B  1  671  ? 9.959   21.963  80.288  1.00 14.60 ? 669  ILE   B CA    1 
ATOM   13856 C  C     . ILE   B  1  671  ? 9.692   23.459  80.207  1.00 14.42 ? 669  ILE   B C     1 
ATOM   13857 O  O     . ILE   B  1  671  ? 9.004   23.939  79.298  1.00 16.87 ? 669  ILE   B O     1 
ATOM   13858 C  CB    . ILE   B  1  671  ? 9.098   21.291  81.371  1.00 14.92 ? 669  ILE   B CB    1 
ATOM   13859 C  CG1   . ILE   B  1  671  ? 9.122   19.778  81.196  1.00 17.22 ? 669  ILE   B CG1   1 
ATOM   13860 C  CG2   . ILE   B  1  671  ? 7.668   21.801  81.284  1.00 17.76 ? 669  ILE   B CG2   1 
ATOM   13861 C  CD1   . ILE   B  1  671  ? 8.554   19.030  82.379  1.00 19.88 ? 669  ILE   B CD1   1 
ATOM   13862 N  N     . ALA   B  1  672  ? 10.212  24.214  81.171  1.00 15.84 ? 670  ALA   B N     1 
ATOM   13863 C  CA    . ALA   B  1  672  ? 10.004  25.658  81.162  1.00 18.18 ? 670  ALA   B CA    1 
ATOM   13864 C  C     . ALA   B  1  672  ? 10.573  26.281  79.896  1.00 16.82 ? 670  ALA   B C     1 
ATOM   13865 O  O     . ALA   B  1  672  ? 9.983   27.205  79.325  1.00 17.14 ? 670  ALA   B O     1 
ATOM   13866 C  CB    . ALA   B  1  672  ? 10.661  26.279  82.396  1.00 18.77 ? 670  ALA   B CB    1 
ATOM   13867 N  N     . GLU   B  1  673  ? 11.730  25.793  79.456  1.00 15.68 ? 671  GLU   B N     1 
ATOM   13868 C  CA    . GLU   B  1  673  ? 12.363  26.283  78.238  1.00 17.27 ? 671  GLU   B CA    1 
ATOM   13869 C  C     . GLU   B  1  673  ? 11.454  26.090  77.031  1.00 17.24 ? 671  GLU   B C     1 
ATOM   13870 O  O     . GLU   B  1  673  ? 11.215  27.030  76.260  1.00 16.56 ? 671  GLU   B O     1 
ATOM   13871 C  CB    . GLU   B  1  673  ? 13.669  25.523  78.044  1.00 18.94 ? 671  GLU   B CB    1 
ATOM   13872 C  CG    . GLU   B  1  673  ? 14.522  26.009  76.894  1.00 19.67 ? 671  GLU   B CG    1 
ATOM   13873 C  CD    . GLU   B  1  673  ? 15.245  27.301  77.198  1.00 22.49 ? 671  GLU   B CD    1 
ATOM   13874 O  OE1   . GLU   B  1  673  ? 15.406  27.664  78.392  1.00 22.72 ? 671  GLU   B OE1   1 
ATOM   13875 O  OE2   . GLU   B  1  673  ? 15.670  27.952  76.228  1.00 19.04 ? 671  GLU   B OE2   1 
ATOM   13876 N  N     . VAL   B  1  674  ? 10.947  24.871  76.839  1.00 14.00 ? 672  VAL   B N     1 
ATOM   13877 C  CA    . VAL   B  1  674  ? 10.075  24.611  75.695  1.00 14.99 ? 672  VAL   B CA    1 
ATOM   13878 C  C     . VAL   B  1  674  ? 8.770   25.389  75.813  1.00 14.05 ? 672  VAL   B C     1 
ATOM   13879 O  O     . VAL   B  1  674  ? 8.285   25.962  74.830  1.00 14.40 ? 672  VAL   B O     1 
ATOM   13880 C  CB    . VAL   B  1  674  ? 9.830   23.104  75.510  1.00 14.53 ? 672  VAL   B CB    1 
ATOM   13881 C  CG1   . VAL   B  1  674  ? 9.002   22.874  74.267  1.00 14.64 ? 672  VAL   B CG1   1 
ATOM   13882 C  CG2   . VAL   B  1  674  ? 11.148  22.378  75.392  1.00 16.97 ? 672  VAL   B CG2   1 
ATOM   13883 N  N     . ARG   B  1  675  ? 8.196   25.449  77.017  1.00 13.73 ? 673  ARG   B N     1 
ATOM   13884 C  CA    . ARG   B  1  675  ? 6.968   26.220  77.192  1.00 13.66 ? 673  ARG   B CA    1 
ATOM   13885 C  C     . ARG   B  1  675  ? 7.186   27.673  76.816  1.00 13.83 ? 673  ARG   B C     1 
ATOM   13886 O  O     . ARG   B  1  675  ? 6.339   28.286  76.165  1.00 14.32 ? 673  ARG   B O     1 
ATOM   13887 C  CB    . ARG   B  1  675  ? 6.492   26.155  78.634  1.00 14.28 ? 673  ARG   B CB    1 
ATOM   13888 C  CG    . ARG   B  1  675  ? 5.949   24.801  79.043  1.00 15.70 ? 673  ARG   B CG    1 
ATOM   13889 C  CD    . ARG   B  1  675  ? 5.299   24.926  80.408  1.00 14.04 ? 673  ARG   B CD    1 
ATOM   13890 N  NE    . ARG   B  1  675  ? 4.121   25.777  80.307  1.00 15.47 ? 673  ARG   B NE    1 
ATOM   13891 C  CZ    . ARG   B  1  675  ? 3.538   26.358  81.343  1.00 15.77 ? 673  ARG   B CZ    1 
ATOM   13892 N  NH1   . ARG   B  1  675  ? 4.009   26.218  82.569  1.00 16.38 ? 673  ARG   B NH1   1 
ATOM   13893 N  NH2   . ARG   B  1  675  ? 2.452   27.093  81.139  1.00 15.70 ? 673  ARG   B NH2   1 
ATOM   13894 N  N     . GLU   B  1  676  ? 8.324   28.235  77.210  1.00 12.75 ? 674  GLU   B N     1 
ATOM   13895 C  CA    . GLU   B  1  676  ? 8.566   29.636  76.911  1.00 13.74 ? 674  GLU   B CA    1 
ATOM   13896 C  C     . GLU   B  1  676  ? 8.673   29.845  75.408  1.00 13.91 ? 674  GLU   B C     1 
ATOM   13897 O  O     . GLU   B  1  676  ? 8.170   30.839  74.876  1.00 14.53 ? 674  GLU   B O     1 
ATOM   13898 C  CB    . GLU   B  1  676  ? 9.838   30.100  77.618  1.00 16.78 ? 674  GLU   B CB    1 
ATOM   13899 C  CG    . GLU   B  1  676  ? 10.097  31.575  77.468  1.00 17.69 ? 674  GLU   B CG    1 
ATOM   13900 C  CD    . GLU   B  1  676  ? 9.511   32.388  78.594  1.00 24.42 ? 674  GLU   B CD    1 
ATOM   13901 O  OE1   . GLU   B  1  676  ? 8.691   31.850  79.377  1.00 29.79 ? 674  GLU   B OE1   1 
ATOM   13902 O  OE2   . GLU   B  1  676  ? 9.881   33.579  78.697  1.00 24.10 ? 674  GLU   B OE2   1 
ATOM   13903 N  N     . ALA   B  1  677  ? 9.325   28.916  74.702  1.00 13.12 ? 675  ALA   B N     1 
ATOM   13904 C  CA    . ALA   B  1  677  ? 9.401   29.040  73.251  1.00 14.19 ? 675  ALA   B CA    1 
ATOM   13905 C  C     . ALA   B  1  677  ? 8.011   28.998  72.635  1.00 12.97 ? 675  ALA   B C     1 
ATOM   13906 O  O     . ALA   B  1  677  ? 7.679   29.812  71.764  1.00 13.92 ? 675  ALA   B O     1 
ATOM   13907 C  CB    . ALA   B  1  677  ? 10.259  27.918  72.669  1.00 14.21 ? 675  ALA   B CB    1 
ATOM   13908 N  N     . ILE   B  1  678  ? 7.171   28.077  73.106  1.00 13.05 ? 676  ILE   B N     1 
ATOM   13909 C  CA    . ILE   B  1  678  ? 5.797   27.995  72.620  1.00 13.18 ? 676  ILE   B CA    1 
ATOM   13910 C  C     . ILE   B  1  678  ? 5.073   29.302  72.884  1.00 12.49 ? 676  ILE   B C     1 
ATOM   13911 O  O     . ILE   B  1  678  ? 4.353   29.818  72.021  1.00 13.84 ? 676  ILE   B O     1 
ATOM   13912 C  CB    . ILE   B  1  678  ? 5.083   26.810  73.291  1.00 13.31 ? 676  ILE   B CB    1 
ATOM   13913 C  CG1   . ILE   B  1  678  ? 5.639   25.486  72.769  1.00 14.66 ? 676  ILE   B CG1   1 
ATOM   13914 C  CG2   . ILE   B  1  678  ? 3.552   26.897  73.088  1.00 14.76 ? 676  ILE   B CG2   1 
ATOM   13915 C  CD1   . ILE   B  1  678  ? 5.412   24.327  73.726  1.00 14.44 ? 676  ILE   B CD1   1 
ATOM   13916 N  N     . ASP   B  1  679  ? 5.239   29.840  74.087  1.00 13.11 ? 677  ASP   B N     1 
ATOM   13917 C  CA    . ASP   B  1  679  ? 4.555   31.069  74.453  1.00 14.32 ? 677  ASP   B CA    1 
ATOM   13918 C  C     . ASP   B  1  679  ? 5.035   32.248  73.620  1.00 13.57 ? 677  ASP   B C     1 
ATOM   13919 O  O     . ASP   B  1  679  ? 4.223   33.087  73.226  1.00 13.89 ? 677  ASP   B O     1 
ATOM   13920 C  CB    . ASP   B  1  679  ? 4.719   31.343  75.944  1.00 14.37 ? 677  ASP   B CB    1 
ATOM   13921 C  CG    . ASP   B  1  679  ? 3.941   30.363  76.816  1.00 16.95 ? 677  ASP   B CG    1 
ATOM   13922 O  OD1   . ASP   B  1  679  ? 2.866   29.893  76.390  1.00 18.17 ? 677  ASP   B OD1   1 
ATOM   13923 O  OD2   . ASP   B  1  679  ? 4.399   30.087  77.940  1.00 17.64 ? 677  ASP   B OD2   1 
ATOM   13924 N  N     . PHE   B  1  680  ? 6.345   32.351  73.356  1.00 13.06 ? 678  PHE   B N     1 
ATOM   13925 C  CA    . PHE   B  1  680  ? 6.802   33.421  72.474  1.00 13.13 ? 678  PHE   B CA    1 
ATOM   13926 C  C     . PHE   B  1  680  ? 6.132   33.305  71.118  1.00 13.04 ? 678  PHE   B C     1 
ATOM   13927 O  O     . PHE   B  1  680  ? 5.672   34.304  70.550  1.00 13.42 ? 678  PHE   B O     1 
ATOM   13928 C  CB    . PHE   B  1  680  ? 8.312   33.345  72.268  1.00 11.93 ? 678  PHE   B CB    1 
ATOM   13929 C  CG    . PHE   B  1  680  ? 9.131   34.003  73.339  1.00 13.68 ? 678  PHE   B CG    1 
ATOM   13930 C  CD1   . PHE   B  1  680  ? 8.876   35.296  73.748  1.00 13.90 ? 678  PHE   B CD1   1 
ATOM   13931 C  CD2   . PHE   B  1  680  ? 10.186  33.315  73.917  1.00 15.56 ? 678  PHE   B CD2   1 
ATOM   13932 C  CE1   . PHE   B  1  680  ? 9.679   35.897  74.730  1.00 15.10 ? 678  PHE   B CE1   1 
ATOM   13933 C  CE2   . PHE   B  1  680  ? 10.981  33.901  74.889  1.00 17.02 ? 678  PHE   B CE2   1 
ATOM   13934 C  CZ    . PHE   B  1  680  ? 10.732  35.191  75.300  1.00 14.99 ? 678  PHE   B CZ    1 
ATOM   13935 N  N     . LEU   B  1  681  ? 6.128   32.094  70.553  1.00 12.70 ? 679  LEU   B N     1 
ATOM   13936 C  CA    . LEU   B  1  681  ? 5.504   31.899  69.247  1.00 10.94 ? 679  LEU   B CA    1 
ATOM   13937 C  C     . LEU   B  1  681  ? 4.072   32.384  69.265  1.00 13.49 ? 679  LEU   B C     1 
ATOM   13938 O  O     . LEU   B  1  681  ? 3.651   33.152  68.394  1.00 14.56 ? 679  LEU   B O     1 
ATOM   13939 C  CB    . LEU   B  1  681  ? 5.563   30.422  68.856  1.00 12.08 ? 679  LEU   B CB    1 
ATOM   13940 C  CG    . LEU   B  1  681  ? 6.991   29.966  68.539  1.00 12.59 ? 679  LEU   B CG    1 
ATOM   13941 C  CD1   . LEU   B  1  681  ? 7.070   28.439  68.573  1.00 13.54 ? 679  LEU   B CD1   1 
ATOM   13942 C  CD2   . LEU   B  1  681  ? 7.413   30.493  67.173  1.00 15.11 ? 679  LEU   B CD2   1 
ATOM   13943 N  N     . ARG   B  1  682  ? 3.307   31.944  70.261  1.00 12.39 ? 680  ARG   B N     1 
ATOM   13944 C  CA    . ARG   B  1  682  ? 1.888   32.264  70.260  1.00 10.97 ? 680  ARG   B CA    1 
ATOM   13945 C  C     . ARG   B  1  682  ? 1.640   33.713  70.620  1.00 13.17 ? 680  ARG   B C     1 
ATOM   13946 O  O     . ARG   B  1  682  ? 0.680   34.315  70.126  1.00 14.19 ? 680  ARG   B O     1 
ATOM   13947 C  CB    . ARG   B  1  682  ? 1.133   31.347  71.209  1.00 12.82 ? 680  ARG   B CB    1 
ATOM   13948 C  CG    . ARG   B  1  682  ? 1.144   29.926  70.720  1.00 13.62 ? 680  ARG   B CG    1 
ATOM   13949 C  CD    . ARG   B  1  682  ? 0.457   29.052  71.733  1.00 14.34 ? 680  ARG   B CD    1 
ATOM   13950 N  NE    . ARG   B  1  682  ? 0.215   27.716  71.209  1.00 16.60 ? 680  ARG   B NE    1 
ATOM   13951 C  CZ    . ARG   B  1  682  ? 0.016   26.655  71.969  1.00 16.67 ? 680  ARG   B CZ    1 
ATOM   13952 N  NH1   . ARG   B  1  682  ? 0.012   26.744  73.287  1.00 16.48 ? 680  ARG   B NH1   1 
ATOM   13953 N  NH2   . ARG   B  1  682  ? -0.163  25.471  71.391  1.00 19.38 ? 680  ARG   B NH2   1 
ATOM   13954 N  N     . TYR   B  1  683  ? 2.475   34.273  71.479  1.00 12.78 ? 681  TYR   B N     1 
ATOM   13955 C  CA    . TYR   B  1  683  ? 2.293   35.663  71.867  1.00 13.90 ? 681  TYR   B CA    1 
ATOM   13956 C  C     . TYR   B  1  683  ? 2.604   36.592  70.700  1.00 14.01 ? 681  TYR   B C     1 
ATOM   13957 O  O     . TYR   B  1  683  ? 1.809   37.480  70.372  1.00 14.55 ? 681  TYR   B O     1 
ATOM   13958 C  CB    . TYR   B  1  683  ? 3.181   35.966  73.073  1.00 12.42 ? 681  TYR   B CB    1 
ATOM   13959 C  CG    . TYR   B  1  683  ? 3.137   37.410  73.481  1.00 13.62 ? 681  TYR   B CG    1 
ATOM   13960 C  CD1   . TYR   B  1  683  ? 2.076   37.902  74.217  1.00 14.67 ? 681  TYR   B CD1   1 
ATOM   13961 C  CD2   . TYR   B  1  683  ? 4.169   38.270  73.148  1.00 14.32 ? 681  TYR   B CD2   1 
ATOM   13962 C  CE1   . TYR   B  1  683  ? 2.025   39.233  74.576  1.00 14.89 ? 681  TYR   B CE1   1 
ATOM   13963 C  CE2   . TYR   B  1  683  ? 4.134   39.602  73.513  1.00 14.44 ? 681  TYR   B CE2   1 
ATOM   13964 C  CZ    . TYR   B  1  683  ? 3.064   40.068  74.232  1.00 14.40 ? 681  TYR   B CZ    1 
ATOM   13965 O  OH    . TYR   B  1  683  ? 3.025   41.393  74.596  1.00 16.57 ? 681  TYR   B OH    1 
ATOM   13966 N  N     . TYR   B  1  684  ? 3.746   36.387  70.038  1.00 11.79 ? 682  TYR   B N     1 
ATOM   13967 C  CA    . TYR   B  1  684  ? 4.049   37.266  68.915  1.00 12.61 ? 682  TYR   B CA    1 
ATOM   13968 C  C     . TYR   B  1  684  ? 3.058   37.070  67.774  1.00 13.41 ? 682  TYR   B C     1 
ATOM   13969 O  O     . TYR   B  1  684  ? 2.771   38.019  67.039  1.00 14.55 ? 682  TYR   B O     1 
ATOM   13970 C  CB    . TYR   B  1  684  ? 5.493   37.099  68.454  1.00 12.84 ? 682  TYR   B CB    1 
ATOM   13971 C  CG    . TYR   B  1  684  ? 6.498   37.478  69.506  1.00 13.61 ? 682  TYR   B CG    1 
ATOM   13972 C  CD1   . TYR   B  1  684  ? 6.331   38.623  70.272  1.00 14.84 ? 682  TYR   B CD1   1 
ATOM   13973 C  CD2   . TYR   B  1  684  ? 7.622   36.699  69.729  1.00 12.85 ? 682  TYR   B CD2   1 
ATOM   13974 C  CE1   . TYR   B  1  684  ? 7.249   38.975  71.242  1.00 14.48 ? 682  TYR   B CE1   1 
ATOM   13975 C  CE2   . TYR   B  1  684  ? 8.550   37.041  70.691  1.00 12.38 ? 682  TYR   B CE2   1 
ATOM   13976 C  CZ    . TYR   B  1  684  ? 8.358   38.180  71.447  1.00 14.83 ? 682  TYR   B CZ    1 
ATOM   13977 O  OH    . TYR   B  1  684  ? 9.285   38.499  72.405  1.00 14.44 ? 682  TYR   B OH    1 
ATOM   13978 N  N     . ALA   B  1  685  ? 2.528   35.856  67.605  1.00 14.18 ? 683  ALA   B N     1 
ATOM   13979 C  CA    . ALA   B  1  685  ? 1.463   35.653  66.627  1.00 13.77 ? 683  ALA   B CA    1 
ATOM   13980 C  C     . ALA   B  1  685  ? 0.247   36.492  66.975  1.00 14.37 ? 683  ALA   B C     1 
ATOM   13981 O  O     . ALA   B  1  685  ? -0.306  37.194  66.118  1.00 15.43 ? 683  ALA   B O     1 
ATOM   13982 C  CB    . ALA   B  1  685  ? 1.091   34.173  66.552  1.00 12.80 ? 683  ALA   B CB    1 
ATOM   13983 N  N     . GLU   B  1  686  ? -0.183  36.436  68.235  1.00 14.66 ? 684  GLU   B N     1 
ATOM   13984 C  CA    . GLU   B  1  686  ? -1.344  37.226  68.625  1.00 15.30 ? 684  GLU   B CA    1 
ATOM   13985 C  C     . GLU   B  1  686  ? -1.059  38.719  68.534  1.00 16.37 ? 684  GLU   B C     1 
ATOM   13986 O  O     . GLU   B  1  686  ? -1.894  39.477  68.043  1.00 15.83 ? 684  GLU   B O     1 
ATOM   13987 C  CB    . GLU   B  1  686  ? -1.808  36.844  70.020  1.00 18.58 ? 684  GLU   B CB    1 
ATOM   13988 C  CG    . GLU   B  1  686  ? -2.964  37.744  70.530  1.00 21.08 ? 684  GLU   B CG    1 
ATOM   13989 C  CD    . GLU   B  1  686  ? -4.255  37.673  69.687  1.00 26.44 ? 684  GLU   B CD    1 
ATOM   13990 O  OE1   . GLU   B  1  686  ? -4.434  36.755  68.848  1.00 24.05 ? 684  GLU   B OE1   1 
ATOM   13991 O  OE2   . GLU   B  1  686  ? -5.119  38.551  69.894  1.00 27.20 ? 684  GLU   B OE2   1 
ATOM   13992 N  N     . GLN   B  1  687  ? 0.122   39.162  68.977  1.00 13.87 ? 685  GLN   B N     1 
ATOM   13993 C  CA    . GLN   B  1  687  ? 0.412   40.589  68.882  1.00 15.59 ? 685  GLN   B CA    1 
ATOM   13994 C  C     . GLN   B  1  687  ? 0.410   41.041  67.433  1.00 14.98 ? 685  GLN   B C     1 
ATOM   13995 O  O     . GLN   B  1  687  ? -0.049  42.145  67.115  1.00 15.81 ? 685  GLN   B O     1 
ATOM   13996 C  CB    . GLN   B  1  687  ? 1.755   40.898  69.531  1.00 15.25 ? 685  GLN   B CB    1 
ATOM   13997 C  CG    . GLN   B  1  687  ? 1.712   40.696  71.046  1.00 15.90 ? 685  GLN   B CG    1 
ATOM   13998 C  CD    . GLN   B  1  687  ? 0.667   41.571  71.695  1.00 19.52 ? 685  GLN   B CD    1 
ATOM   13999 O  OE1   . GLN   B  1  687  ? 0.695   42.793  71.551  1.00 19.62 ? 685  GLN   B OE1   1 
ATOM   14000 N  NE2   . GLN   B  1  687  ? -0.271  40.952  72.407  1.00 20.72 ? 685  GLN   B NE2   1 
ATOM   14001 N  N     . THR   B  1  688  ? 0.898   40.182  66.536  1.00 12.83 ? 686  THR   B N     1 
ATOM   14002 C  CA    . THR   B  1  688  ? 0.829   40.489  65.114  1.00 15.01 ? 686  THR   B CA    1 
ATOM   14003 C  C     . THR   B  1  688  ? -0.611  40.642  64.660  1.00 13.96 ? 686  THR   B C     1 
ATOM   14004 O  O     . THR   B  1  688  ? -0.951  41.599  63.958  1.00 16.44 ? 686  THR   B O     1 
ATOM   14005 C  CB    . THR   B  1  688  ? 1.507   39.377  64.331  1.00 13.46 ? 686  THR   B CB    1 
ATOM   14006 O  OG1   . THR   B  1  688  ? 2.907   39.414  64.624  1.00 15.33 ? 686  THR   B OG1   1 
ATOM   14007 C  CG2   . THR   B  1  688  ? 1.280   39.590  62.837  1.00 15.95 ? 686  THR   B CG2   1 
ATOM   14008 N  N     . ARG   B  1  689  ? -1.464  39.690  65.029  1.00 13.58 ? 687  ARG   B N     1 
ATOM   14009 C  CA    . ARG   B  1  689  ? -2.863  39.762  64.620  1.00 15.63 ? 687  ARG   B CA    1 
ATOM   14010 C  C     . ARG   B  1  689  ? -3.550  41.003  65.161  1.00 16.19 ? 687  ARG   B C     1 
ATOM   14011 O  O     . ARG   B  1  689  ? -4.501  41.497  64.552  1.00 18.21 ? 687  ARG   B O     1 
ATOM   14012 C  CB    . ARG   B  1  689  ? -3.601  38.506  65.068  1.00 16.38 ? 687  ARG   B CB    1 
ATOM   14013 C  CG    . ARG   B  1  689  ? -3.256  37.284  64.233  1.00 18.81 ? 687  ARG   B CG    1 
ATOM   14014 C  CD    . ARG   B  1  689  ? -4.174  36.143  64.592  1.00 19.29 ? 687  ARG   B CD    1 
ATOM   14015 N  NE    . ARG   B  1  689  ? -4.014  35.726  65.976  1.00 20.43 ? 687  ARG   B NE    1 
ATOM   14016 C  CZ    . ARG   B  1  689  ? -3.232  34.732  66.376  1.00 23.09 ? 687  ARG   B CZ    1 
ATOM   14017 N  NH1   . ARG   B  1  689  ? -2.532  34.014  65.513  1.00 19.01 ? 687  ARG   B NH1   1 
ATOM   14018 N  NH2   . ARG   B  1  689  ? -3.162  34.445  67.672  1.00 19.65 ? 687  ARG   B NH2   1 
ATOM   14019 N  N     . ARG   B  1  690  ? -3.093  41.520  66.296  1.00 14.55 ? 688  ARG   B N     1 
ATOM   14020 C  CA    . ARG   B  1  690  ? -3.656  42.733  66.870  1.00 14.95 ? 688  ARG   B CA    1 
ATOM   14021 C  C     . ARG   B  1  690  ? -3.145  44.017  66.230  1.00 16.56 ? 688  ARG   B C     1 
ATOM   14022 O  O     . ARG   B  1  690  ? -3.779  45.062  66.405  1.00 16.84 ? 688  ARG   B O     1 
ATOM   14023 C  CB    . ARG   B  1  690  ? -3.321  42.794  68.361  1.00 16.13 ? 688  ARG   B CB    1 
ATOM   14024 C  CG    . ARG   B  1  690  ? -3.983  41.712  69.188  1.00 18.07 ? 688  ARG   B CG    1 
ATOM   14025 C  CD    . ARG   B  1  690  ? -5.492  41.951  69.341  1.00 20.82 ? 688  ARG   B CD    1 
ATOM   14026 N  NE    . ARG   B  1  690  ? -5.766  43.195  70.058  1.00 24.18 ? 688  ARG   B NE    1 
ATOM   14027 C  CZ    . ARG   B  1  690  ? -6.346  44.257  69.520  1.00 26.08 ? 688  ARG   B CZ    1 
ATOM   14028 N  NH1   . ARG   B  1  690  ? -6.806  44.235  68.279  1.00 25.74 ? 688  ARG   B NH1   1 
ATOM   14029 N  NH2   . ARG   B  1  690  ? -6.493  45.361  70.254  1.00 21.57 ? 688  ARG   B NH2   1 
ATOM   14030 N  N     . THR   B  1  691  ? -2.010  43.987  65.531  1.00 15.82 ? 689  THR   B N     1 
ATOM   14031 C  CA    . THR   B  1  691  ? -1.357  45.254  65.204  1.00 17.49 ? 689  THR   B CA    1 
ATOM   14032 C  C     . THR   B  1  691  ? -0.942  45.436  63.748  1.00 18.85 ? 689  THR   B C     1 
ATOM   14033 O  O     . THR   B  1  691  ? -1.094  46.532  63.220  1.00 20.66 ? 689  THR   B O     1 
ATOM   14034 C  CB    . THR   B  1  691  ? -0.107  45.472  66.082  1.00 16.69 ? 689  THR   B CB    1 
ATOM   14035 O  OG1   . THR   B  1  691  ? 0.802   44.385  65.895  1.00 18.51 ? 689  THR   B OG1   1 
ATOM   14036 C  CG2   . THR   B  1  691  ? -0.478  45.567  67.542  1.00 18.16 ? 689  THR   B CG2   1 
ATOM   14037 N  N     . LEU   B  1  692  ? -0.365  44.427  63.104  1.00 16.90 ? 690  LEU   B N     1 
ATOM   14038 C  CA    . LEU   B  1  692  ? 0.403   44.706  61.897  1.00 16.93 ? 690  LEU   B CA    1 
ATOM   14039 C  C     . LEU   B  1  692  ? -0.477  44.848  60.665  1.00 17.65 ? 690  LEU   B C     1 
ATOM   14040 O  O     . LEU   B  1  692  ? -1.315  43.993  60.383  1.00 21.11 ? 690  LEU   B O     1 
ATOM   14041 C  CB    . LEU   B  1  692  ? 1.469   43.643  61.656  1.00 16.29 ? 690  LEU   B CB    1 
ATOM   14042 C  CG    . LEU   B  1  692  ? 2.552   43.645  62.738  1.00 19.33 ? 690  LEU   B CG    1 
ATOM   14043 C  CD1   . LEU   B  1  692  ? 3.662   42.725  62.305  1.00 20.35 ? 690  LEU   B CD1   1 
ATOM   14044 C  CD2   . LEU   B  1  692  ? 3.081   45.045  63.018  1.00 18.81 ? 690  LEU   B CD2   1 
ATOM   14045 N  N     . GLY   B  1  693  ? -0.247  45.926  59.926  1.00 19.30 ? 691  GLY   B N     1 
ATOM   14046 C  CA    . GLY   B  1  693  ? -0.962  46.218  58.713  1.00 19.41 ? 691  GLY   B CA    1 
ATOM   14047 C  C     . GLY   B  1  693  ? 0.005   46.603  57.618  1.00 21.04 ? 691  GLY   B C     1 
ATOM   14048 O  O     . GLY   B  1  693  ? 1.229   46.552  57.784  1.00 22.10 ? 691  GLY   B O     1 
ATOM   14049 N  N     . PRO   B  1  694  ? -0.537  47.024  56.478  1.00 25.77 ? 692  PRO   B N     1 
ATOM   14050 C  CA    . PRO   B  1  694  ? 0.315   47.272  55.305  1.00 24.94 ? 692  PRO   B CA    1 
ATOM   14051 C  C     . PRO   B  1  694  ? 1.367   48.339  55.525  1.00 26.38 ? 692  PRO   B C     1 
ATOM   14052 O  O     . PRO   B  1  694  ? 2.459   48.244  54.949  1.00 28.94 ? 692  PRO   B O     1 
ATOM   14053 C  CB    . PRO   B  1  694  ? -0.696  47.663  54.211  1.00 26.66 ? 692  PRO   B CB    1 
ATOM   14054 C  CG    . PRO   B  1  694  ? -1.969  47.993  54.943  1.00 30.61 ? 692  PRO   B CG    1 
ATOM   14055 C  CD    . PRO   B  1  694  ? -1.972  47.159  56.177  1.00 25.81 ? 692  PRO   B CD    1 
ATOM   14056 N  N     . GLY   B  1  695  ? 1.083   49.346  56.348  1.00 24.47 ? 693  GLY   B N     1 
ATOM   14057 C  CA    . GLY   B  1  695  ? 2.009   50.425  56.596  1.00 25.83 ? 693  GLY   B CA    1 
ATOM   14058 C  C     . GLY   B  1  695  ? 3.131   50.125  57.563  1.00 24.01 ? 693  GLY   B C     1 
ATOM   14059 O  O     . GLY   B  1  695  ? 3.981   50.987  57.790  1.00 28.66 ? 693  GLY   B O     1 
ATOM   14060 N  N     . HIS   B  1  696  ? 3.166   48.932  58.155  1.00 21.75 ? 694  HIS   B N     1 
ATOM   14061 C  CA    . HIS   B  1  696  ? 4.229   48.569  59.089  1.00 19.53 ? 694  HIS   B CA    1 
ATOM   14062 C  C     . HIS   B  1  696  ? 5.197   47.656  58.350  1.00 19.41 ? 694  HIS   B C     1 
ATOM   14063 O  O     . HIS   B  1  696  ? 5.226   46.439  58.534  1.00 23.47 ? 694  HIS   B O     1 
ATOM   14064 C  CB    . HIS   B  1  696  ? 3.642   47.892  60.317  1.00 18.96 ? 694  HIS   B CB    1 
ATOM   14065 C  CG    . HIS   B  1  696  ? 2.518   48.659  60.926  1.00 19.09 ? 694  HIS   B CG    1 
ATOM   14066 N  ND1   . HIS   B  1  696  ? 1.240   48.154  61.011  1.00 19.67 ? 694  HIS   B ND1   1 
ATOM   14067 C  CD2   . HIS   B  1  696  ? 2.466   49.912  61.436  1.00 20.86 ? 694  HIS   B CD2   1 
ATOM   14068 C  CE1   . HIS   B  1  696  ? 0.453   49.051  61.574  1.00 20.47 ? 694  HIS   B CE1   1 
ATOM   14069 N  NE2   . HIS   B  1  696  ? 1.168   50.132  61.827  1.00 22.19 ? 694  HIS   B NE2   1 
ATOM   14070 N  N     . GLY   B  1  697  ? 6.005   48.272  57.502  1.00 23.30 ? 695  GLY   B N     1 
ATOM   14071 C  CA    . GLY   B  1  697  ? 6.924   47.533  56.672  1.00 22.63 ? 695  GLY   B CA    1 
ATOM   14072 C  C     . GLY   B  1  697  ? 8.066   46.938  57.463  1.00 20.13 ? 695  GLY   B C     1 
ATOM   14073 O  O     . GLY   B  1  697  ? 8.496   47.479  58.479  1.00 20.76 ? 695  GLY   B O     1 
ATOM   14074 N  N     . PRO   B  1  698  ? 8.592   45.815  56.995  1.00 21.76 ? 696  PRO   B N     1 
ATOM   14075 C  CA    . PRO   B  1  698  ? 9.715   45.180  57.689  1.00 19.74 ? 696  PRO   B CA    1 
ATOM   14076 C  C     . PRO   B  1  698  ? 10.992  45.979  57.529  1.00 18.33 ? 696  PRO   B C     1 
ATOM   14077 O  O     . PRO   B  1  698  ? 11.146  46.800  56.624  1.00 19.99 ? 696  PRO   B O     1 
ATOM   14078 C  CB    . PRO   B  1  698  ? 9.854   43.836  56.968  1.00 21.69 ? 696  PRO   B CB    1 
ATOM   14079 C  CG    . PRO   B  1  698  ? 9.373   44.132  55.602  1.00 27.44 ? 696  PRO   B CG    1 
ATOM   14080 C  CD    . PRO   B  1  698  ? 8.184   45.046  55.810  1.00 25.05 ? 696  PRO   B CD    1 
ATOM   14081 N  N     . LEU   B  1  699  ? 11.924  45.722  58.444  1.00 17.76 ? 697  LEU   B N     1 
ATOM   14082 C  CA    . LEU   B  1  699  ? 13.258  46.300  58.299  1.00 15.95 ? 697  LEU   B CA    1 
ATOM   14083 C  C     . LEU   B  1  699  ? 14.023  45.661  57.146  1.00 17.73 ? 697  LEU   B C     1 
ATOM   14084 O  O     . LEU   B  1  699  ? 14.731  46.349  56.404  1.00 19.15 ? 697  LEU   B O     1 
ATOM   14085 C  CB    . LEU   B  1  699  ? 14.040  46.101  59.590  1.00 17.86 ? 697  LEU   B CB    1 
ATOM   14086 C  CG    . LEU   B  1  699  ? 13.437  46.723  60.841  1.00 19.74 ? 697  LEU   B CG    1 
ATOM   14087 C  CD1   . LEU   B  1  699  ? 14.304  46.342  62.025  1.00 20.41 ? 697  LEU   B CD1   1 
ATOM   14088 C  CD2   . LEU   B  1  699  ? 13.354  48.237  60.675  1.00 24.23 ? 697  LEU   B CD2   1 
ATOM   14089 N  N     . GLY   B  1  700  ? 13.923  44.347  56.998  1.00 16.66 ? 698  GLY   B N     1 
ATOM   14090 C  CA    . GLY   B  1  700  ? 14.793  43.613  56.113  1.00 18.27 ? 698  GLY   B CA    1 
ATOM   14091 C  C     . GLY   B  1  700  ? 15.451  42.491  56.886  1.00 16.54 ? 698  GLY   B C     1 
ATOM   14092 O  O     . GLY   B  1  700  ? 14.997  42.127  57.971  1.00 15.58 ? 698  GLY   B O     1 
ATOM   14093 N  N     . PRO   B  1  701  ? 16.536  41.929  56.355  1.00 16.34 ? 699  PRO   B N     1 
ATOM   14094 C  CA    . PRO   B  1  701  ? 17.210  40.820  57.047  1.00 15.50 ? 699  PRO   B CA    1 
ATOM   14095 C  C     . PRO   B  1  701  ? 17.589  41.201  58.468  1.00 16.67 ? 699  PRO   B C     1 
ATOM   14096 O  O     . PRO   B  1  701  ? 18.250  42.213  58.707  1.00 17.41 ? 699  PRO   B O     1 
ATOM   14097 C  CB    . PRO   B  1  701  ? 18.463  40.581  56.195  1.00 16.69 ? 699  PRO   B CB    1 
ATOM   14098 C  CG    . PRO   B  1  701  ? 18.075  41.079  54.845  1.00 19.05 ? 699  PRO   B CG    1 
ATOM   14099 C  CD    . PRO   B  1  701  ? 17.221  42.285  55.103  1.00 17.82 ? 699  PRO   B CD    1 
ATOM   14100 N  N     . ILE   B  1  702  ? 17.150  40.393  59.417  1.00 15.10 ? 700  ILE   B N     1 
ATOM   14101 C  CA    A ILE   B  1  702  ? 17.472  40.608  60.819  0.65 13.75 ? 700  ILE   B CA    1 
ATOM   14102 C  CA    B ILE   B  1  702  ? 17.453  40.597  60.828  0.35 13.80 ? 700  ILE   B CA    1 
ATOM   14103 C  C     . ILE   B  1  702  ? 18.392  39.492  61.275  1.00 15.70 ? 700  ILE   B C     1 
ATOM   14104 O  O     . ILE   B  1  702  ? 18.131  38.305  61.024  1.00 15.31 ? 700  ILE   B O     1 
ATOM   14105 C  CB    A ILE   B  1  702  ? 16.208  40.693  61.687  0.65 13.79 ? 700  ILE   B CB    1 
ATOM   14106 C  CB    B ILE   B  1  702  ? 16.176  40.589  61.683  0.35 13.81 ? 700  ILE   B CB    1 
ATOM   14107 C  CG1   A ILE   B  1  702  ? 15.513  42.032  61.431  0.65 15.67 ? 700  ILE   B CG1   1 
ATOM   14108 C  CG1   B ILE   B  1  702  ? 15.217  41.675  61.207  0.35 15.82 ? 700  ILE   B CG1   1 
ATOM   14109 C  CG2   A ILE   B  1  702  ? 16.572  40.529  63.165  0.65 15.06 ? 700  ILE   B CG2   1 
ATOM   14110 C  CG2   B ILE   B  1  702  ? 16.525  40.775  63.157  0.35 15.12 ? 700  ILE   B CG2   1 
ATOM   14111 C  CD1   A ILE   B  1  702  ? 14.241  42.240  62.237  0.65 17.11 ? 700  ILE   B CD1   1 
ATOM   14112 C  CD1   B ILE   B  1  702  ? 15.762  43.066  61.324  0.35 15.73 ? 700  ILE   B CD1   1 
ATOM   14113 N  N     . VAL   B  1  703  ? 19.476  39.876  61.927  1.00 13.76 ? 701  VAL   B N     1 
ATOM   14114 C  CA    . VAL   B  1  703  ? 20.411  38.927  62.502  1.00 13.34 ? 701  VAL   B CA    1 
ATOM   14115 C  C     . VAL   B  1  703  ? 20.014  38.710  63.952  1.00 14.26 ? 701  VAL   B C     1 
ATOM   14116 O  O     . VAL   B  1  703  ? 19.938  39.666  64.728  1.00 14.58 ? 701  VAL   B O     1 
ATOM   14117 C  CB    . VAL   B  1  703  ? 21.842  39.463  62.397  1.00 14.21 ? 701  VAL   B CB    1 
ATOM   14118 C  CG1   . VAL   B  1  703  ? 22.796  38.615  63.228  1.00 16.13 ? 701  VAL   B CG1   1 
ATOM   14119 C  CG2   . VAL   B  1  703  ? 22.264  39.489  60.941  1.00 15.08 ? 701  VAL   B CG2   1 
ATOM   14120 N  N     . CYS   B  1  704  ? 19.754  37.460  64.318  1.00 12.77 ? 702  CYS   B N     1 
ATOM   14121 C  CA    . CYS   B  1  704  ? 19.318  37.115  65.663  1.00 13.07 ? 702  CYS   B CA    1 
ATOM   14122 C  C     . CYS   B  1  704  ? 20.423  36.307  66.312  1.00 14.60 ? 702  CYS   B C     1 
ATOM   14123 O  O     . CYS   B  1  704  ? 20.739  35.197  65.857  1.00 13.15 ? 702  CYS   B O     1 
ATOM   14124 C  CB    . CYS   B  1  704  ? 18.034  36.298  65.636  1.00 13.60 ? 702  CYS   B CB    1 
ATOM   14125 S  SG    . CYS   B  1  704  ? 16.626  37.163  64.945  1.00 15.49 ? 702  CYS   B SG    1 
ATOM   14126 N  N     . ILE   B  1  705  ? 20.995  36.861  67.374  1.00 13.30 ? 703  ILE   B N     1 
ATOM   14127 C  CA    . ILE   B  1  705  ? 22.135  36.272  68.054  1.00 12.78 ? 703  ILE   B CA    1 
ATOM   14128 C  C     . ILE   B  1  705  ? 21.690  35.990  69.475  1.00 14.06 ? 703  ILE   B C     1 
ATOM   14129 O  O     . ILE   B  1  705  ? 21.206  36.893  70.163  1.00 14.02 ? 703  ILE   B O     1 
ATOM   14130 C  CB    . ILE   B  1  705  ? 23.346  37.213  68.022  1.00 14.51 ? 703  ILE   B CB    1 
ATOM   14131 C  CG1   . ILE   B  1  705  ? 23.898  37.308  66.598  1.00 16.62 ? 703  ILE   B CG1   1 
ATOM   14132 C  CG2   . ILE   B  1  705  ? 24.393  36.708  68.961  1.00 13.42 ? 703  ILE   B CG2   1 
ATOM   14133 C  CD1   . ILE   B  1  705  ? 24.874  38.443  66.432  1.00 17.18 ? 703  ILE   B CD1   1 
ATOM   14134 N  N     . SER   B  1  706  ? 21.837  34.751  69.904  1.00 13.67 ? 704  SER   B N     1 
ATOM   14135 C  CA    . SER   B  1  706  ? 21.186  34.297  71.117  1.00 16.11 ? 704  SER   B CA    1 
ATOM   14136 C  C     . SER   B  1  706  ? 22.197  33.663  72.060  1.00 14.66 ? 704  SER   B C     1 
ATOM   14137 O  O     . SER   B  1  706  ? 23.277  33.231  71.641  1.00 15.58 ? 704  SER   B O     1 
ATOM   14138 C  CB    . SER   B  1  706  ? 20.060  33.310  70.772  1.00 15.31 ? 704  SER   B CB    1 
ATOM   14139 O  OG    . SER   B  1  706  ? 20.544  32.265  69.950  1.00 14.46 ? 704  SER   B OG    1 
ATOM   14140 N  N     . PRO   B  1  707  ? 21.880  33.613  73.348  1.00 13.71 ? 705  PRO   B N     1 
ATOM   14141 C  CA    . PRO   B  1  707  ? 22.811  33.083  74.345  1.00 16.46 ? 705  PRO   B CA    1 
ATOM   14142 C  C     . PRO   B  1  707  ? 22.592  31.582  74.499  1.00 16.08 ? 705  PRO   B C     1 
ATOM   14143 O  O     . PRO   B  1  707  ? 21.589  31.021  74.049  1.00 17.32 ? 705  PRO   B O     1 
ATOM   14144 C  CB    . PRO   B  1  707  ? 22.360  33.812  75.619  1.00 15.80 ? 705  PRO   B CB    1 
ATOM   14145 C  CG    . PRO   B  1  707  ? 20.886  33.923  75.456  1.00 14.84 ? 705  PRO   B CG    1 
ATOM   14146 C  CD    . PRO   B  1  707  ? 20.655  34.156  73.972  1.00 15.55 ? 705  PRO   B CD    1 
ATOM   14147 N  N     . TRP   B  1  708  ? 23.545  30.935  75.166  1.00 14.60 ? 706  TRP   B N     1 
ATOM   14148 C  CA    . TRP   B  1  708  ? 23.432  29.490  75.328  1.00 15.00 ? 706  TRP   B CA    1 
ATOM   14149 C  C     . TRP   B  1  708  ? 22.424  29.098  76.398  1.00 16.59 ? 706  TRP   B C     1 
ATOM   14150 O  O     . TRP   B  1  708  ? 21.913  27.981  76.358  1.00 16.32 ? 706  TRP   B O     1 
ATOM   14151 C  CB    . TRP   B  1  708  ? 24.795  28.850  75.649  1.00 15.37 ? 706  TRP   B CB    1 
ATOM   14152 C  CG    . TRP   B  1  708  ? 25.184  29.108  77.065  1.00 16.71 ? 706  TRP   B CG    1 
ATOM   14153 C  CD1   . TRP   B  1  708  ? 25.959  30.134  77.531  1.00 17.93 ? 706  TRP   B CD1   1 
ATOM   14154 C  CD2   . TRP   B  1  708  ? 24.779  28.355  78.214  1.00 16.75 ? 706  TRP   B CD2   1 
ATOM   14155 N  NE1   . TRP   B  1  708  ? 26.055  30.065  78.897  1.00 18.03 ? 706  TRP   B NE1   1 
ATOM   14156 C  CE2   . TRP   B  1  708  ? 25.337  28.985  79.341  1.00 16.17 ? 706  TRP   B CE2   1 
ATOM   14157 C  CE3   . TRP   B  1  708  ? 24.011  27.200  78.396  1.00 16.87 ? 706  TRP   B CE3   1 
ATOM   14158 C  CZ2   . TRP   B  1  708  ? 25.137  28.510  80.632  1.00 16.26 ? 706  TRP   B CZ2   1 
ATOM   14159 C  CZ3   . TRP   B  1  708  ? 23.807  26.733  79.675  1.00 18.54 ? 706  TRP   B CZ3   1 
ATOM   14160 C  CH2   . TRP   B  1  708  ? 24.379  27.379  80.778  1.00 17.37 ? 706  TRP   B CH2   1 
ATOM   14161 N  N     . ASN   B  1  709  ? 22.153  29.970  77.369  1.00 16.13 ? 707  ASN   B N     1 
ATOM   14162 C  CA    . ASN   B  1  709  ? 21.587  29.479  78.622  1.00 16.77 ? 707  ASN   B CA    1 
ATOM   14163 C  C     . ASN   B  1  709  ? 20.082  29.289  78.569  1.00 17.97 ? 707  ASN   B C     1 
ATOM   14164 O  O     . ASN   B  1  709  ? 19.541  28.537  79.382  1.00 19.58 ? 707  ASN   B O     1 
ATOM   14165 C  CB    . ASN   B  1  709  ? 21.943  30.424  79.759  1.00 16.86 ? 707  ASN   B CB    1 
ATOM   14166 C  CG    . ASN   B  1  709  ? 21.197  31.721  79.661  1.00 16.57 ? 707  ASN   B CG    1 
ATOM   14167 O  OD1   . ASN   B  1  709  ? 21.451  32.515  78.770  1.00 20.55 ? 707  ASN   B OD1   1 
ATOM   14168 N  ND2   . ASN   B  1  709  ? 20.247  31.930  80.555  1.00 16.93 ? 707  ASN   B ND2   1 
ATOM   14169 N  N     . PHE   B  1  710  ? 19.401  29.964  77.650  1.00 16.39 ? 708  PHE   B N     1 
ATOM   14170 C  CA    . PHE   B  1  710  ? 18.013  29.684  77.301  1.00 18.30 ? 708  PHE   B CA    1 
ATOM   14171 C  C     . PHE   B  1  710  ? 18.049  29.307  75.826  1.00 17.05 ? 708  PHE   B C     1 
ATOM   14172 O  O     . PHE   B  1  710  ? 17.636  30.080  74.952  1.00 16.99 ? 708  PHE   B O     1 
ATOM   14173 C  CB    . PHE   B  1  710  ? 17.107  30.886  77.558  1.00 15.50 ? 708  PHE   B CB    1 
ATOM   14174 C  CG    . PHE   B  1  710  ? 17.023  31.292  79.017  1.00 17.37 ? 708  PHE   B CG    1 
ATOM   14175 C  CD1   . PHE   B  1  710  ? 16.952  30.336  80.022  1.00 18.36 ? 708  PHE   B CD1   1 
ATOM   14176 C  CD2   . PHE   B  1  710  ? 17.015  32.626  79.372  1.00 20.04 ? 708  PHE   B CD2   1 
ATOM   14177 C  CE1   . PHE   B  1  710  ? 16.865  30.714  81.357  1.00 21.52 ? 708  PHE   B CE1   1 
ATOM   14178 C  CE2   . PHE   B  1  710  ? 16.936  33.015  80.700  1.00 20.61 ? 708  PHE   B CE2   1 
ATOM   14179 C  CZ    . PHE   B  1  710  ? 16.861  32.052  81.699  1.00 21.22 ? 708  PHE   B CZ    1 
ATOM   14180 N  N     . PRO   B  1  711  ? 18.526  28.097  75.527  1.00 17.08 ? 709  PRO   B N     1 
ATOM   14181 C  CA    . PRO   B  1  711  ? 18.980  27.788  74.167  1.00 16.91 ? 709  PRO   B CA    1 
ATOM   14182 C  C     . PRO   B  1  711  ? 17.857  27.591  73.165  1.00 17.20 ? 709  PRO   B C     1 
ATOM   14183 O  O     . PRO   B  1  711  ? 18.114  27.608  71.954  1.00 15.75 ? 709  PRO   B O     1 
ATOM   14184 C  CB    . PRO   B  1  711  ? 19.783  26.497  74.360  1.00 17.83 ? 709  PRO   B CB    1 
ATOM   14185 C  CG    . PRO   B  1  711  ? 19.094  25.835  75.541  1.00 17.36 ? 709  PRO   B CG    1 
ATOM   14186 C  CD    . PRO   B  1  711  ? 18.741  26.975  76.458  1.00 16.99 ? 709  PRO   B CD    1 
ATOM   14187 N  N     . LEU   B  1  712  ? 16.632  27.365  73.620  1.00 15.77 ? 710  LEU   B N     1 
ATOM   14188 C  CA    . LEU   B  1  712  ? 15.492  27.330  72.719  1.00 15.32 ? 710  LEU   B CA    1 
ATOM   14189 C  C     . LEU   B  1  712  ? 14.580  28.525  72.883  1.00 14.97 ? 710  LEU   B C     1 
ATOM   14190 O  O     . LEU   B  1  712  ? 14.092  29.058  71.892  1.00 16.03 ? 710  LEU   B O     1 
ATOM   14191 C  CB    . LEU   B  1  712  ? 14.682  26.045  72.917  1.00 15.29 ? 710  LEU   B CB    1 
ATOM   14192 C  CG    . LEU   B  1  712  ? 13.507  25.860  71.955  1.00 13.92 ? 710  LEU   B CG    1 
ATOM   14193 C  CD1   . LEU   B  1  712  ? 13.968  25.752  70.502  1.00 15.70 ? 710  LEU   B CD1   1 
ATOM   14194 C  CD2   . LEU   B  1  712  ? 12.681  24.639  72.360  1.00 17.78 ? 710  LEU   B CD2   1 
ATOM   14195 N  N     . ALA   B  1  713  ? 14.350  28.972  74.112  1.00 14.35 ? 711  ALA   B N     1 
ATOM   14196 C  CA    . ALA   B  1  713  ? 13.323  29.979  74.346  1.00 15.94 ? 711  ALA   B CA    1 
ATOM   14197 C  C     . ALA   B  1  713  ? 13.731  31.333  73.782  1.00 14.32 ? 711  ALA   B C     1 
ATOM   14198 O  O     . ALA   B  1  713  ? 12.988  31.940  73.005  1.00 15.24 ? 711  ALA   B O     1 
ATOM   14199 C  CB    . ALA   B  1  713  ? 13.043  30.083  75.841  1.00 17.25 ? 711  ALA   B CB    1 
ATOM   14200 N  N     . ILE   B  1  714  ? 14.896  31.845  74.175  1.00 15.90 ? 712  ILE   B N     1 
ATOM   14201 C  CA    . ILE   B  1  714  ? 15.288  33.152  73.657  1.00 16.61 ? 712  ILE   B CA    1 
ATOM   14202 C  C     . ILE   B  1  714  ? 15.595  33.049  72.176  1.00 15.99 ? 712  ILE   B C     1 
ATOM   14203 O  O     . ILE   B  1  714  ? 15.249  33.939  71.385  1.00 14.67 ? 712  ILE   B O     1 
ATOM   14204 C  CB    . ILE   B  1  714  ? 16.466  33.711  74.467  1.00 17.27 ? 712  ILE   B CB    1 
ATOM   14205 C  CG1   . ILE   B  1  714  ? 15.923  34.070  75.842  1.00 19.02 ? 712  ILE   B CG1   1 
ATOM   14206 C  CG2   . ILE   B  1  714  ? 17.076  34.924  73.761  1.00 17.64 ? 712  ILE   B CG2   1 
ATOM   14207 C  CD1   . ILE   B  1  714  ? 16.855  34.873  76.663  1.00 22.65 ? 712  ILE   B CD1   1 
ATOM   14208 N  N     . PHE   B  1  715  ? 16.226  31.945  71.783  1.00 14.65 ? 713  PHE   B N     1 
ATOM   14209 C  CA    . PHE   B  1  715  ? 16.491  31.686  70.377  1.00 14.59 ? 713  PHE   B CA    1 
ATOM   14210 C  C     . PHE   B  1  715  ? 15.208  31.801  69.568  1.00 14.57 ? 713  PHE   B C     1 
ATOM   14211 O  O     . PHE   B  1  715  ? 15.136  32.564  68.596  1.00 14.33 ? 713  PHE   B O     1 
ATOM   14212 C  CB    . PHE   B  1  715  ? 17.078  30.289  70.247  1.00 14.22 ? 713  PHE   B CB    1 
ATOM   14213 C  CG    . PHE   B  1  715  ? 17.305  29.876  68.829  1.00 13.45 ? 713  PHE   B CG    1 
ATOM   14214 C  CD1   . PHE   B  1  715  ? 18.416  30.314  68.150  1.00 13.70 ? 713  PHE   B CD1   1 
ATOM   14215 C  CD2   . PHE   B  1  715  ? 16.386  29.070  68.162  1.00 15.15 ? 713  PHE   B CD2   1 
ATOM   14216 C  CE1   . PHE   B  1  715  ? 18.633  29.932  66.835  1.00 15.49 ? 713  PHE   B CE1   1 
ATOM   14217 C  CE2   . PHE   B  1  715  ? 16.590  28.698  66.842  1.00 15.57 ? 713  PHE   B CE2   1 
ATOM   14218 C  CZ    . PHE   B  1  715  ? 17.711  29.130  66.179  1.00 15.09 ? 713  PHE   B CZ    1 
ATOM   14219 N  N     . THR   B  1  716  ? 14.161  31.092  70.000  1.00 13.28 ? 714  THR   B N     1 
ATOM   14220 C  CA    . THR   B  1  716  ? 12.893  31.094  69.275  1.00 13.43 ? 714  THR   B CA    1 
ATOM   14221 C  C     . THR   B  1  716  ? 12.209  32.449  69.359  1.00 13.75 ? 714  THR   B C     1 
ATOM   14222 O  O     . THR   B  1  716  ? 11.651  32.923  68.365  1.00 15.85 ? 714  THR   B O     1 
ATOM   14223 C  CB    . THR   B  1  716  ? 11.968  30.017  69.845  1.00 15.33 ? 714  THR   B CB    1 
ATOM   14224 O  OG1   . THR   B  1  716  ? 12.562  28.727  69.657  1.00 16.34 ? 714  THR   B OG1   1 
ATOM   14225 C  CG2   . THR   B  1  716  ? 10.612  30.057  69.153  1.00 15.33 ? 714  THR   B CG2   1 
ATOM   14226 N  N     . GLY   B  1  717  ? 12.229  33.079  70.537  1.00 14.39 ? 715  GLY   B N     1 
ATOM   14227 C  CA    . GLY   B  1  717  ? 11.542  34.348  70.698  1.00 15.73 ? 715  GLY   B CA    1 
ATOM   14228 C  C     . GLY   B  1  717  ? 12.031  35.413  69.735  1.00 13.19 ? 715  GLY   B C     1 
ATOM   14229 O  O     . GLY   B  1  717  ? 11.233  36.077  69.066  1.00 14.55 ? 715  GLY   B O     1 
ATOM   14230 N  N     . GLN   B  1  718  ? 13.351  35.588  69.641  1.00 13.32 ? 716  GLN   B N     1 
ATOM   14231 C  CA    . GLN   B  1  718  ? 13.849  36.644  68.771  1.00 13.27 ? 716  GLN   B CA    1 
ATOM   14232 C  C     . GLN   B  1  718  ? 13.504  36.333  67.330  1.00 12.82 ? 716  GLN   B C     1 
ATOM   14233 O  O     . GLN   B  1  718  ? 13.043  37.201  66.589  1.00 13.55 ? 716  GLN   B O     1 
ATOM   14234 C  CB    . GLN   B  1  718  ? 15.363  36.779  68.908  1.00 11.90 ? 716  GLN   B CB    1 
ATOM   14235 C  CG    . GLN   B  1  718  ? 15.825  37.113  70.334  1.00 12.94 ? 716  GLN   B CG    1 
ATOM   14236 C  CD    . GLN   B  1  718  ? 17.296  37.431  70.431  1.00 14.49 ? 716  GLN   B CD    1 
ATOM   14237 O  OE1   . GLN   B  1  718  ? 17.668  38.419  71.068  1.00 16.40 ? 716  GLN   B OE1   1 
ATOM   14238 N  NE2   . GLN   B  1  718  ? 18.143  36.609  69.799  1.00 14.99 ? 716  GLN   B NE2   1 
ATOM   14239 N  N     . ILE   B  1  719  ? 13.707  35.086  66.929  1.00 12.81 ? 717  ILE   B N     1 
ATOM   14240 C  CA    . ILE   B  1  719  ? 13.468  34.711  65.546  1.00 14.86 ? 717  ILE   B CA    1 
ATOM   14241 C  C     . ILE   B  1  719  ? 12.002  34.858  65.205  1.00 13.41 ? 717  ILE   B C     1 
ATOM   14242 O  O     . ILE   B  1  719  ? 11.647  35.359  64.131  1.00 13.97 ? 717  ILE   B O     1 
ATOM   14243 C  CB    . ILE   B  1  719  ? 13.954  33.276  65.316  1.00 13.31 ? 717  ILE   B CB    1 
ATOM   14244 C  CG1   . ILE   B  1  719  ? 15.474  33.253  65.379  1.00 14.04 ? 717  ILE   B CG1   1 
ATOM   14245 C  CG2   . ILE   B  1  719  ? 13.460  32.746  63.993  1.00 21.47 ? 717  ILE   B CG2   1 
ATOM   14246 C  CD1   . ILE   B  1  719  ? 15.984  31.867  65.581  1.00 21.03 ? 717  ILE   B CD1   1 
ATOM   14247 N  N     . ALA   B  1  720  ? 11.130  34.399  66.102  1.00 13.45 ? 718  ALA   B N     1 
ATOM   14248 C  CA    . ALA   B  1  720  ? 9.705   34.435  65.833  1.00 12.60 ? 718  ALA   B CA    1 
ATOM   14249 C  C     . ALA   B  1  720  ? 9.244   35.863  65.642  1.00 13.61 ? 718  ALA   B C     1 
ATOM   14250 O  O     . ALA   B  1  720  ? 8.469   36.162  64.715  1.00 13.99 ? 718  ALA   B O     1 
ATOM   14251 C  CB    . ALA   B  1  720  ? 8.940   33.783  66.990  1.00 15.58 ? 718  ALA   B CB    1 
ATOM   14252 N  N     . ALA   B  1  721  ? 9.709   36.758  66.517  1.00 13.49 ? 719  ALA   B N     1 
ATOM   14253 C  CA    . ALA   B  1  721  ? 9.298   38.149  66.427  1.00 13.70 ? 719  ALA   B CA    1 
ATOM   14254 C  C     . ALA   B  1  721  ? 9.757   38.759  65.117  1.00 13.21 ? 719  ALA   B C     1 
ATOM   14255 O  O     . ALA   B  1  721  ? 8.981   39.421  64.415  1.00 13.85 ? 719  ALA   B O     1 
ATOM   14256 C  CB    . ALA   B  1  721  ? 9.864   38.921  67.619  1.00 14.62 ? 719  ALA   B CB    1 
ATOM   14257 N  N     . ALA   B  1  722  ? 11.029  38.551  64.779  1.00 12.61 ? 720  ALA   B N     1 
ATOM   14258 C  CA    . ALA   B  1  722  ? 11.555  39.115  63.548  1.00 13.05 ? 720  ALA   B CA    1 
ATOM   14259 C  C     . ALA   B  1  722  ? 10.793  38.577  62.345  1.00 13.72 ? 720  ALA   B C     1 
ATOM   14260 O  O     . ALA   B  1  722  ? 10.395  39.338  61.459  1.00 13.61 ? 720  ALA   B O     1 
ATOM   14261 C  CB    . ALA   B  1  722  ? 13.051  38.809  63.446  1.00 13.22 ? 720  ALA   B CB    1 
ATOM   14262 N  N     . LEU   B  1  723  ? 10.583  37.258  62.302  1.00 13.26 ? 721  LEU   B N     1 
ATOM   14263 C  CA    . LEU   B  1  723  ? 9.860   36.663  61.180  1.00 13.01 ? 721  LEU   B CA    1 
ATOM   14264 C  C     . LEU   B  1  723  ? 8.448   37.203  61.066  1.00 14.61 ? 721  LEU   B C     1 
ATOM   14265 O  O     . LEU   B  1  723  ? 7.984   37.535  59.969  1.00 15.70 ? 721  LEU   B O     1 
ATOM   14266 C  CB    . LEU   B  1  723  ? 9.783   35.152  61.358  1.00 13.15 ? 721  LEU   B CB    1 
ATOM   14267 C  CG    . LEU   B  1  723  ? 11.067  34.365  61.135  1.00 14.78 ? 721  LEU   B CG    1 
ATOM   14268 C  CD1   . LEU   B  1  723  ? 10.813  32.934  61.572  1.00 14.96 ? 721  LEU   B CD1   1 
ATOM   14269 C  CD2   . LEU   B  1  723  ? 11.477  34.426  59.678  1.00 16.34 ? 721  LEU   B CD2   1 
ATOM   14270 N  N     . VAL   B  1  724  ? 7.728   37.265  62.186  1.00 13.25 ? 722  VAL   B N     1 
ATOM   14271 C  CA    . VAL   B  1  724  ? 6.323   37.594  62.085  1.00 12.49 ? 722  VAL   B CA    1 
ATOM   14272 C  C     . VAL   B  1  724  ? 6.147   39.061  61.744  1.00 11.88 ? 722  VAL   B C     1 
ATOM   14273 O  O     . VAL   B  1  724  ? 5.131   39.446  61.145  1.00 15.77 ? 722  VAL   B O     1 
ATOM   14274 C  CB    . VAL   B  1  724  ? 5.567   37.139  63.350  1.00 12.96 ? 722  VAL   B CB    1 
ATOM   14275 C  CG1   . VAL   B  1  724  ? 5.733   38.138  64.505  1.00 16.07 ? 722  VAL   B CG1   1 
ATOM   14276 C  CG2   . VAL   B  1  724  ? 4.107   36.903  63.020  1.00 14.24 ? 722  VAL   B CG2   1 
ATOM   14277 N  N     . ALA   B  1  725  ? 7.136   39.887  62.080  1.00 15.27 ? 723  ALA   B N     1 
ATOM   14278 C  CA    . ALA   B  1  725  ? 7.144   41.274  61.641  1.00 15.52 ? 723  ALA   B CA    1 
ATOM   14279 C  C     . ALA   B  1  725  ? 7.480   41.403  60.161  1.00 16.55 ? 723  ALA   B C     1 
ATOM   14280 O  O     . ALA   B  1  725  ? 7.474   42.520  59.639  1.00 17.89 ? 723  ALA   B O     1 
ATOM   14281 C  CB    . ALA   B  1  725  ? 8.125   42.073  62.509  1.00 16.15 ? 723  ALA   B CB    1 
ATOM   14282 N  N     . GLY   B  1  726  ? 7.739   40.298  59.469  1.00 14.58 ? 724  GLY   B N     1 
ATOM   14283 C  CA    . GLY   B  1  726  ? 7.943   40.337  58.038  1.00 14.98 ? 724  GLY   B CA    1 
ATOM   14284 C  C     . GLY   B  1  726  ? 9.387   40.348  57.604  1.00 17.38 ? 724  GLY   B C     1 
ATOM   14285 O  O     . GLY   B  1  726  ? 9.658   40.654  56.437  1.00 19.18 ? 724  GLY   B O     1 
ATOM   14286 N  N     . ASN   B  1  727  ? 10.314  40.030  58.500  1.00 14.53 ? 725  ASN   B N     1 
ATOM   14287 C  CA    . ASN   B  1  727  ? 11.746  40.067  58.233  1.00 15.66 ? 725  ASN   B CA    1 
ATOM   14288 C  C     . ASN   B  1  727  ? 12.293  38.664  58.066  1.00 15.02 ? 725  ASN   B C     1 
ATOM   14289 O  O     . ASN   B  1  727  ? 12.023  37.796  58.901  1.00 17.57 ? 725  ASN   B O     1 
ATOM   14290 C  CB    . ASN   B  1  727  ? 12.493  40.720  59.393  1.00 15.16 ? 725  ASN   B CB    1 
ATOM   14291 C  CG    . ASN   B  1  727  ? 11.934  42.075  59.751  1.00 15.97 ? 725  ASN   B CG    1 
ATOM   14292 O  OD1   . ASN   B  1  727  ? 12.200  43.074  59.082  1.00 16.38 ? 725  ASN   B OD1   1 
ATOM   14293 N  ND2   . ASN   B  1  727  ? 11.157  42.119  60.817  1.00 14.90 ? 725  ASN   B ND2   1 
ATOM   14294 N  N     . PRO   B  1  728  ? 13.093  38.412  57.035  1.00 14.16 ? 726  PRO   B N     1 
ATOM   14295 C  CA    . PRO   B  1  728  ? 13.841  37.163  56.998  1.00 14.75 ? 726  PRO   B CA    1 
ATOM   14296 C  C     . PRO   B  1  728  ? 14.923  37.228  58.060  1.00 15.66 ? 726  PRO   B C     1 
ATOM   14297 O  O     . PRO   B  1  728  ? 15.399  38.306  58.432  1.00 15.91 ? 726  PRO   B O     1 
ATOM   14298 C  CB    . PRO   B  1  728  ? 14.439  37.154  55.591  1.00 16.60 ? 726  PRO   B CB    1 
ATOM   14299 C  CG    . PRO   B  1  728  ? 14.621  38.615  55.260  1.00 18.87 ? 726  PRO   B CG    1 
ATOM   14300 C  CD    . PRO   B  1  728  ? 13.525  39.361  55.991  1.00 15.16 ? 726  PRO   B CD    1 
ATOM   14301 N  N     . VAL   B  1  729  ? 15.282  36.063  58.575  1.00 13.33 ? 727  VAL   B N     1 
ATOM   14302 C  CA    . VAL   B  1  729  ? 16.130  35.974  59.751  1.00 13.60 ? 727  VAL   B CA    1 
ATOM   14303 C  C     . VAL   B  1  729  ? 17.379  35.160  59.462  1.00 16.27 ? 727  VAL   B C     1 
ATOM   14304 O  O     . VAL   B  1  729  ? 17.321  34.096  58.831  1.00 15.79 ? 727  VAL   B O     1 
ATOM   14305 C  CB    . VAL   B  1  729  ? 15.352  35.350  60.918  1.00 14.07 ? 727  VAL   B CB    1 
ATOM   14306 C  CG1   . VAL   B  1  729  ? 16.308  34.954  62.043  1.00 15.62 ? 727  VAL   B CG1   1 
ATOM   14307 C  CG2   . VAL   B  1  729  ? 14.318  36.330  61.426  1.00 14.75 ? 727  VAL   B CG2   1 
ATOM   14308 N  N     . LEU   B  1  730  ? 18.508  35.656  59.955  1.00 14.67 ? 728  LEU   B N     1 
ATOM   14309 C  CA    . LEU   B  1  730  ? 19.740  34.894  60.062  1.00 14.79 ? 728  LEU   B CA    1 
ATOM   14310 C  C     . LEU   B  1  730  ? 19.888  34.543  61.536  1.00 12.84 ? 728  LEU   B C     1 
ATOM   14311 O  O     . LEU   B  1  730  ? 20.093  35.423  62.368  1.00 15.74 ? 728  LEU   B O     1 
ATOM   14312 C  CB    . LEU   B  1  730  ? 20.939  35.717  59.598  1.00 16.24 ? 728  LEU   B CB    1 
ATOM   14313 C  CG    . LEU   B  1  730  ? 20.995  36.215  58.150  1.00 16.26 ? 728  LEU   B CG    1 
ATOM   14314 C  CD1   . LEU   B  1  730  ? 20.641  35.097  57.174  1.00 17.46 ? 728  LEU   B CD1   1 
ATOM   14315 C  CD2   . LEU   B  1  730  ? 20.107  37.433  57.940  1.00 16.83 ? 728  LEU   B CD2   1 
ATOM   14316 N  N     . ALA   B  1  731  ? 19.772  33.266  61.859  1.00 13.53 ? 729  ALA   B N     1 
ATOM   14317 C  CA    . ALA   B  1  731  ? 19.763  32.819  63.244  1.00 13.58 ? 729  ALA   B CA    1 
ATOM   14318 C  C     . ALA   B  1  731  ? 21.139  32.282  63.598  1.00 15.09 ? 729  ALA   B C     1 
ATOM   14319 O  O     . ALA   B  1  731  ? 21.583  31.287  63.024  1.00 15.32 ? 729  ALA   B O     1 
ATOM   14320 C  CB    . ALA   B  1  731  ? 18.690  31.749  63.431  1.00 16.61 ? 729  ALA   B CB    1 
ATOM   14321 N  N     . LYS   B  1  732  ? 21.804  32.939  64.539  1.00 13.16 ? 730  LYS   B N     1 
ATOM   14322 C  CA    . LYS   B  1  732  ? 23.147  32.558  64.968  1.00 15.70 ? 730  LYS   B CA    1 
ATOM   14323 C  C     . LYS   B  1  732  ? 23.052  32.135  66.427  1.00 13.74 ? 730  LYS   B C     1 
ATOM   14324 O  O     . LYS   B  1  732  ? 23.066  32.989  67.336  1.00 15.38 ? 730  LYS   B O     1 
ATOM   14325 C  CB    . LYS   B  1  732  ? 24.103  33.731  64.792  1.00 15.40 ? 730  LYS   B CB    1 
ATOM   14326 C  CG    . LYS   B  1  732  ? 25.542  33.334  64.478  1.00 15.42 ? 730  LYS   B CG    1 
ATOM   14327 C  CD    . LYS   B  1  732  ? 26.180  32.449  65.553  1.00 15.91 ? 730  LYS   B CD    1 
ATOM   14328 C  CE    . LYS   B  1  732  ? 26.526  33.231  66.808  1.00 15.21 ? 730  LYS   B CE    1 
ATOM   14329 N  NZ    . LYS   B  1  732  ? 27.084  32.302  67.842  1.00 15.15 ? 730  LYS   B NZ    1 
ATOM   14330 N  N     . PRO   B  1  733  ? 22.930  30.847  66.694  1.00 13.55 ? 731  PRO   B N     1 
ATOM   14331 C  CA    . PRO   B  1  733  ? 22.813  30.381  68.075  1.00 15.15 ? 731  PRO   B CA    1 
ATOM   14332 C  C     . PRO   B  1  733  ? 24.178  30.360  68.722  1.00 13.17 ? 731  PRO   B C     1 
ATOM   14333 O  O     . PRO   B  1  733  ? 25.213  30.356  68.059  1.00 14.73 ? 731  PRO   B O     1 
ATOM   14334 C  CB    . PRO   B  1  733  ? 22.302  28.946  67.911  1.00 15.12 ? 731  PRO   B CB    1 
ATOM   14335 C  CG    . PRO   B  1  733  ? 22.920  28.501  66.618  1.00 15.48 ? 731  PRO   B CG    1 
ATOM   14336 C  CD    . PRO   B  1  733  ? 22.865  29.741  65.723  1.00 15.07 ? 731  PRO   B CD    1 
ATOM   14337 N  N     . ALA   B  1  734  ? 24.158  30.359  70.047  1.00 15.22 ? 732  ALA   B N     1 
ATOM   14338 C  CA    . ALA   B  1  734  ? 25.400  30.305  70.801  1.00 15.52 ? 732  ALA   B CA    1 
ATOM   14339 C  C     . ALA   B  1  734  ? 26.176  29.036  70.460  1.00 16.67 ? 732  ALA   B C     1 
ATOM   14340 O  O     . ALA   B  1  734  ? 25.601  27.988  70.150  1.00 16.75 ? 732  ALA   B O     1 
ATOM   14341 C  CB    . ALA   B  1  734  ? 25.086  30.325  72.296  1.00 16.82 ? 732  ALA   B CB    1 
ATOM   14342 N  N     . GLU   B  1  735  ? 27.505  29.138  70.517  1.00 16.43 ? 733  GLU   B N     1 
ATOM   14343 C  CA    . GLU   B  1  735  ? 28.324  28.005  70.112  1.00 17.22 ? 733  GLU   B CA    1 
ATOM   14344 C  C     . GLU   B  1  735  ? 28.140  26.801  71.025  1.00 17.06 ? 733  GLU   B C     1 
ATOM   14345 O  O     . GLU   B  1  735  ? 28.332  25.668  70.576  1.00 16.58 ? 733  GLU   B O     1 
ATOM   14346 C  CB    . GLU   B  1  735  ? 29.791  28.407  69.989  1.00 20.18 ? 733  GLU   B CB    1 
ATOM   14347 C  CG    . GLU   B  1  735  ? 30.382  29.013  71.232  1.00 22.04 ? 733  GLU   B CG    1 
ATOM   14348 C  CD    . GLU   B  1  735  ? 30.244  30.535  71.290  1.00 25.13 ? 733  GLU   B CD    1 
ATOM   14349 O  OE1   . GLU   B  1  735  ? 29.274  31.097  70.736  1.00 22.40 ? 733  GLU   B OE1   1 
ATOM   14350 O  OE2   . GLU   B  1  735  ? 31.127  31.173  71.905  1.00 25.78 ? 733  GLU   B OE2   1 
ATOM   14351 N  N     . GLU   B  1  736  ? 27.724  27.020  72.274  1.00 16.09 ? 734  GLU   B N     1 
ATOM   14352 C  CA    . GLU   B  1  736  ? 27.593  25.910  73.206  1.00 17.86 ? 734  GLU   B CA    1 
ATOM   14353 C  C     . GLU   B  1  736  ? 26.369  25.051  72.914  1.00 16.55 ? 734  GLU   B C     1 
ATOM   14354 O  O     . GLU   B  1  736  ? 26.355  23.865  73.267  1.00 19.06 ? 734  GLU   B O     1 
ATOM   14355 C  CB    . GLU   B  1  736  ? 27.487  26.436  74.637  1.00 17.47 ? 734  GLU   B CB    1 
ATOM   14356 C  CG    . GLU   B  1  736  ? 28.725  27.163  75.139  1.00 19.60 ? 734  GLU   B CG    1 
ATOM   14357 C  CD    . GLU   B  1  736  ? 28.699  28.674  74.891  1.00 20.42 ? 734  GLU   B CD    1 
ATOM   14358 O  OE1   . GLU   B  1  736  ? 27.929  29.166  74.032  1.00 18.28 ? 734  GLU   B OE1   1 
ATOM   14359 O  OE2   . GLU   B  1  736  ? 29.459  29.380  75.585  1.00 24.76 ? 734  GLU   B OE2   1 
ATOM   14360 N  N     . THR   B  1  737  ? 25.323  25.618  72.301  1.00 16.59 ? 735  THR   B N     1 
ATOM   14361 C  CA    . THR   B  1  737  ? 24.017  24.950  72.230  1.00 17.07 ? 735  THR   B CA    1 
ATOM   14362 C  C     . THR   B  1  737  ? 23.399  25.014  70.839  1.00 16.22 ? 735  THR   B C     1 
ATOM   14363 O  O     . THR   B  1  737  ? 22.253  25.426  70.677  1.00 17.95 ? 735  THR   B O     1 
ATOM   14364 C  CB    . THR   B  1  737  ? 23.060  25.542  73.259  1.00 17.09 ? 735  THR   B CB    1 
ATOM   14365 O  OG1   . THR   B  1  737  ? 22.998  26.963  73.071  1.00 16.63 ? 735  THR   B OG1   1 
ATOM   14366 C  CG2   . THR   B  1  737  ? 23.535  25.230  74.664  1.00 17.68 ? 735  THR   B CG2   1 
ATOM   14367 N  N     . PRO   B  1  738  ? 24.122  24.584  69.809  1.00 15.29 ? 736  PRO   B N     1 
ATOM   14368 C  CA    . PRO   B  1  738  ? 23.566  24.675  68.456  1.00 16.22 ? 736  PRO   B CA    1 
ATOM   14369 C  C     . PRO   B  1  738  ? 22.514  23.626  68.157  1.00 16.03 ? 736  PRO   B C     1 
ATOM   14370 O  O     . PRO   B  1  738  ? 21.718  23.835  67.236  1.00 15.80 ? 736  PRO   B O     1 
ATOM   14371 C  CB    . PRO   B  1  738  ? 24.795  24.448  67.568  1.00 16.70 ? 736  PRO   B CB    1 
ATOM   14372 C  CG    . PRO   B  1  738  ? 25.651  23.520  68.379  1.00 17.53 ? 736  PRO   B CG    1 
ATOM   14373 C  CD    . PRO   B  1  738  ? 25.471  23.988  69.811  1.00 16.91 ? 736  PRO   B CD    1 
ATOM   14374 N  N     . LEU   B  1  739  ? 22.487  22.502  68.881  1.00 15.15 ? 737  LEU   B N     1 
ATOM   14375 C  CA    . LEU   B  1  739  ? 21.614  21.408  68.458  1.00 16.39 ? 737  LEU   B CA    1 
ATOM   14376 C  C     . LEU   B  1  739  ? 20.145  21.748  68.671  1.00 15.02 ? 737  LEU   B C     1 
ATOM   14377 O  O     . LEU   B  1  739  ? 19.310  21.504  67.792  1.00 15.52 ? 737  LEU   B O     1 
ATOM   14378 C  CB    . LEU   B  1  739  ? 21.979  20.113  69.174  1.00 14.63 ? 737  LEU   B CB    1 
ATOM   14379 C  CG    . LEU   B  1  739  ? 23.422  19.684  68.947  1.00 15.12 ? 737  LEU   B CG    1 
ATOM   14380 C  CD1   . LEU   B  1  739  ? 23.690  18.447  69.769  1.00 18.74 ? 737  LEU   B CD1   1 
ATOM   14381 C  CD2   . LEU   B  1  739  ? 23.687  19.415  67.461  1.00 16.88 ? 737  LEU   B CD2   1 
ATOM   14382 N  N     . ILE   B  1  740  ? 19.797  22.293  69.839  1.00 14.54 ? 738  ILE   B N     1 
ATOM   14383 C  CA    . ILE   B  1  740  ? 18.390  22.626  70.053  1.00 13.96 ? 738  ILE   B CA    1 
ATOM   14384 C  C     . ILE   B  1  740  ? 17.983  23.778  69.148  1.00 14.30 ? 738  ILE   B C     1 
ATOM   14385 O  O     . ILE   B  1  740  ? 16.831  23.853  68.702  1.00 15.41 ? 738  ILE   B O     1 
ATOM   14386 C  CB    . ILE   B  1  740  ? 18.083  22.890  71.540  1.00 17.93 ? 738  ILE   B CB    1 
ATOM   14387 C  CG1   . ILE   B  1  740  ? 16.570  22.994  71.761  1.00 17.01 ? 738  ILE   B CG1   1 
ATOM   14388 C  CG2   . ILE   B  1  740  ? 18.781  24.144  72.005  1.00 18.56 ? 738  ILE   B CG2   1 
ATOM   14389 C  CD1   . ILE   B  1  740  ? 15.829  21.709  71.519  1.00 20.32 ? 738  ILE   B CD1   1 
ATOM   14390 N  N     . ALA   B  1  741  ? 18.917  24.677  68.839  1.00 14.60 ? 739  ALA   B N     1 
ATOM   14391 C  CA    . ALA   B  1  741  ? 18.615  25.760  67.910  1.00 16.04 ? 739  ALA   B CA    1 
ATOM   14392 C  C     . ALA   B  1  741  ? 18.300  25.205  66.532  1.00 14.72 ? 739  ALA   B C     1 
ATOM   14393 O  O     . ALA   B  1  741  ? 17.315  25.613  65.900  1.00 16.15 ? 739  ALA   B O     1 
ATOM   14394 C  CB    . ALA   B  1  741  ? 19.794  26.728  67.838  1.00 16.36 ? 739  ALA   B CB    1 
ATOM   14395 N  N     . ALA   B  1  742  ? 19.109  24.250  66.062  1.00 15.07 ? 740  ALA   B N     1 
ATOM   14396 C  CA    . ALA   B  1  742  ? 18.833  23.619  64.777  1.00 15.19 ? 740  ALA   B CA    1 
ATOM   14397 C  C     . ALA   B  1  742  ? 17.455  22.984  64.784  1.00 16.61 ? 740  ALA   B C     1 
ATOM   14398 O  O     . ALA   B  1  742  ? 16.716  23.063  63.795  1.00 15.17 ? 740  ALA   B O     1 
ATOM   14399 C  CB    . ALA   B  1  742  ? 19.898  22.573  64.461  1.00 14.73 ? 740  ALA   B CB    1 
ATOM   14400 N  N     . GLU   B  1  743  ? 17.081  22.371  65.908  1.00 14.52 ? 741  GLU   B N     1 
ATOM   14401 C  CA    . GLU   B  1  743  ? 15.767  21.747  65.988  1.00 15.57 ? 741  GLU   B CA    1 
ATOM   14402 C  C     . GLU   B  1  743  ? 14.671  22.795  65.947  1.00 15.91 ? 741  GLU   B C     1 
ATOM   14403 O  O     . GLU   B  1  743  ? 13.655  22.608  65.267  1.00 17.12 ? 741  GLU   B O     1 
ATOM   14404 C  CB    . GLU   B  1  743  ? 15.686  20.869  67.234  1.00 18.98 ? 741  GLU   B CB    1 
ATOM   14405 C  CG    . GLU   B  1  743  ? 14.356  20.187  67.416  1.00 19.05 ? 741  GLU   B CG    1 
ATOM   14406 C  CD    . GLU   B  1  743  ? 14.034  19.137  66.358  1.00 23.61 ? 741  GLU   B CD    1 
ATOM   14407 O  OE1   . GLU   B  1  743  ? 14.905  18.752  65.551  1.00 20.27 ? 741  GLU   B OE1   1 
ATOM   14408 O  OE2   . GLU   B  1  743  ? 12.872  18.689  66.339  1.00 24.66 ? 741  GLU   B OE2   1 
ATOM   14409 N  N     . GLY   B  1  744  ? 14.881  23.928  66.620  1.00 16.24 ? 742  GLY   B N     1 
ATOM   14410 C  CA    . GLY   B  1  744  ? 13.946  25.032  66.502  1.00 16.96 ? 742  GLY   B CA    1 
ATOM   14411 C  C     . GLY   B  1  744  ? 13.760  25.489  65.064  1.00 14.62 ? 742  GLY   B C     1 
ATOM   14412 O  O     . GLY   B  1  744  ? 12.638  25.739  64.625  1.00 15.68 ? 742  GLY   B O     1 
ATOM   14413 N  N     . VAL   B  1  745  ? 14.852  25.603  64.313  1.00 14.27 ? 743  VAL   B N     1 
ATOM   14414 C  CA    . VAL   B  1  745  ? 14.742  26.038  62.927  1.00 14.24 ? 743  VAL   B CA    1 
ATOM   14415 C  C     . VAL   B  1  745  ? 14.020  24.994  62.089  1.00 15.96 ? 743  VAL   B C     1 
ATOM   14416 O  O     . VAL   B  1  745  ? 13.182  25.338  61.245  1.00 15.77 ? 743  VAL   B O     1 
ATOM   14417 C  CB    . VAL   B  1  745  ? 16.129  26.409  62.371  1.00 16.39 ? 743  VAL   B CB    1 
ATOM   14418 C  CG1   . VAL   B  1  745  ? 16.103  26.504  60.851  1.00 16.68 ? 743  VAL   B CG1   1 
ATOM   14419 C  CG2   . VAL   B  1  745  ? 16.548  27.744  62.949  1.00 16.83 ? 743  VAL   B CG2   1 
ATOM   14420 N  N     . ARG   B  1  746  ? 14.307  23.703  62.323  1.00 15.33 ? 744  ARG   B N     1 
ATOM   14421 C  CA    . ARG   B  1  746  ? 13.565  22.652  61.631  1.00 16.99 ? 744  ARG   B CA    1 
ATOM   14422 C  C     . ARG   B  1  746  ? 12.070  22.803  61.865  1.00 14.55 ? 744  ARG   B C     1 
ATOM   14423 O  O     . ARG   B  1  746  ? 11.266  22.648  60.937  1.00 16.50 ? 744  ARG   B O     1 
ATOM   14424 C  CB    . ARG   B  1  746  ? 13.973  21.270  62.139  1.00 16.77 ? 744  ARG   B CB    1 
ATOM   14425 C  CG    . ARG   B  1  746  ? 15.362  20.815  61.786  1.00 18.79 ? 744  ARG   B CG    1 
ATOM   14426 C  CD    . ARG   B  1  746  ? 15.585  19.401  62.317  1.00 17.76 ? 744  ARG   B CD    1 
ATOM   14427 N  NE    . ARG   B  1  746  ? 16.990  19.057  62.185  1.00 19.83 ? 744  ARG   B NE    1 
ATOM   14428 C  CZ    . ARG   B  1  746  ? 17.885  19.128  63.157  1.00 17.99 ? 744  ARG   B CZ    1 
ATOM   14429 N  NH1   . ARG   B  1  746  ? 17.522  19.273  64.424  1.00 18.10 ? 744  ARG   B NH1   1 
ATOM   14430 N  NH2   . ARG   B  1  746  ? 19.177  19.050  62.851  1.00 20.54 ? 744  ARG   B NH2   1 
ATOM   14431 N  N     . ILE   B  1  747  ? 11.678  23.081  63.107  1.00 14.39 ? 745  ILE   B N     1 
ATOM   14432 C  CA    . ILE   B  1  747  ? 10.261  23.156  63.422  1.00 15.96 ? 745  ILE   B CA    1 
ATOM   14433 C  C     . ILE   B  1  747  ? 9.627   24.375  62.769  1.00 16.54 ? 745  ILE   B C     1 
ATOM   14434 O  O     . ILE   B  1  747  ? 8.521   24.294  62.219  1.00 15.07 ? 745  ILE   B O     1 
ATOM   14435 C  CB    . ILE   B  1  747  ? 10.071  23.152  64.943  1.00 16.38 ? 745  ILE   B CB    1 
ATOM   14436 C  CG1   . ILE   B  1  747  ? 10.331  21.744  65.469  1.00 17.73 ? 745  ILE   B CG1   1 
ATOM   14437 C  CG2   . ILE   B  1  747  ? 8.674   23.622  65.293  1.00 16.01 ? 745  ILE   B CG2   1 
ATOM   14438 C  CD1   . ILE   B  1  747  ? 10.369  21.684  66.957  1.00 18.56 ? 745  ILE   B CD1   1 
ATOM   14439 N  N     . LEU   B  1  748  ? 10.308  25.520  62.813  1.00 14.78 ? 746  LEU   B N     1 
ATOM   14440 C  CA    . LEU   B  1  748  ? 9.767   26.711  62.161  1.00 14.24 ? 746  LEU   B CA    1 
ATOM   14441 C  C     . LEU   B  1  748  ? 9.650   26.508  60.659  1.00 14.10 ? 746  LEU   B C     1 
ATOM   14442 O  O     . LEU   B  1  748  ? 8.654   26.908  60.049  1.00 15.07 ? 746  LEU   B O     1 
ATOM   14443 C  CB    . LEU   B  1  748  ? 10.629  27.926  62.477  1.00 14.99 ? 746  LEU   B CB    1 
ATOM   14444 C  CG    . LEU   B  1  748  ? 10.304  28.569  63.827  1.00 18.73 ? 746  LEU   B CG    1 
ATOM   14445 C  CD1   . LEU   B  1  748  ? 11.484  29.413  64.318  1.00 20.02 ? 746  LEU   B CD1   1 
ATOM   14446 C  CD2   . LEU   B  1  748  ? 9.075   29.413  63.667  1.00 20.60 ? 746  LEU   B CD2   1 
ATOM   14447 N  N     . ARG   B  1  749  ? 10.650  25.881  60.043  1.00 15.11 ? 747  ARG   B N     1 
ATOM   14448 C  CA    . ARG   B  1  749  ? 10.537  25.603  58.615  1.00 16.67 ? 747  ARG   B CA    1 
ATOM   14449 C  C     . ARG   B  1  749  ? 9.403   24.630  58.337  1.00 16.09 ? 747  ARG   B C     1 
ATOM   14450 O  O     . ARG   B  1  749  ? 8.647   24.805  57.374  1.00 16.33 ? 747  ARG   B O     1 
ATOM   14451 C  CB    . ARG   B  1  749  ? 11.857  25.068  58.078  1.00 15.48 ? 747  ARG   B CB    1 
ATOM   14452 C  CG    . ARG   B  1  749  ? 12.914  26.134  57.936  1.00 18.18 ? 747  ARG   B CG    1 
ATOM   14453 C  CD    . ARG   B  1  749  ? 14.105  25.576  57.217  1.00 20.09 ? 747  ARG   B CD    1 
ATOM   14454 N  NE    . ARG   B  1  749  ? 15.097  26.594  56.915  1.00 16.94 ? 747  ARG   B NE    1 
ATOM   14455 C  CZ    . ARG   B  1  749  ? 16.149  26.354  56.145  1.00 21.80 ? 747  ARG   B CZ    1 
ATOM   14456 N  NH1   . ARG   B  1  749  ? 16.341  25.165  55.594  1.00 22.75 ? 747  ARG   B NH1   1 
ATOM   14457 N  NH2   . ARG   B  1  749  ? 17.024  27.328  55.919  1.00 21.98 ? 747  ARG   B NH2   1 
ATOM   14458 N  N     . GLU   B  1  750  ? 9.254   23.608  59.184  1.00 15.05 ? 748  GLU   B N     1 
ATOM   14459 C  CA    . GLU   B  1  750  ? 8.180   22.651  58.970  1.00 16.98 ? 748  GLU   B CA    1 
ATOM   14460 C  C     . GLU   B  1  750  ? 6.828   23.334  59.094  1.00 13.75 ? 748  GLU   B C     1 
ATOM   14461 O  O     . GLU   B  1  750  ? 5.882   22.994  58.372  1.00 16.03 ? 748  GLU   B O     1 
ATOM   14462 C  CB    . GLU   B  1  750  ? 8.287   21.530  60.003  1.00 15.86 ? 748  GLU   B CB    1 
ATOM   14463 C  CG    . GLU   B  1  750  ? 7.248   20.438  59.802  1.00 18.40 ? 748  GLU   B CG    1 
ATOM   14464 C  CD    . GLU   B  1  750  ? 7.442   19.274  60.754  1.00 20.79 ? 748  GLU   B CD    1 
ATOM   14465 O  OE1   . GLU   B  1  750  ? 8.502   19.220  61.417  1.00 21.09 ? 748  GLU   B OE1   1 
ATOM   14466 O  OE2   . GLU   B  1  750  ? 6.535   18.416  60.833  1.00 25.39 ? 748  GLU   B OE2   1 
ATOM   14467 N  N     . ALA   B  1  751  ? 6.746   24.338  59.961  1.00 15.85 ? 749  ALA   B N     1 
ATOM   14468 C  CA    . ALA   B  1  751  ? 5.514   25.070  60.191  1.00 15.50 ? 749  ALA   B CA    1 
ATOM   14469 C  C     . ALA   B  1  751  ? 5.196   26.057  59.082  1.00 16.43 ? 749  ALA   B C     1 
ATOM   14470 O  O     . ALA   B  1  751  ? 4.106   26.630  59.088  1.00 18.08 ? 749  ALA   B O     1 
ATOM   14471 C  CB    . ALA   B  1  751  ? 5.605   25.835  61.511  1.00 15.48 ? 749  ALA   B CB    1 
ATOM   14472 N  N     . GLY   B  1  752  ? 6.102   26.273  58.136  1.00 16.40 ? 750  GLY   B N     1 
ATOM   14473 C  CA    . GLY   B  1  752  ? 5.771   27.133  57.024  1.00 16.74 ? 750  GLY   B CA    1 
ATOM   14474 C  C     . GLY   B  1  752  ? 6.739   28.264  56.761  1.00 17.35 ? 750  GLY   B C     1 
ATOM   14475 O  O     . GLY   B  1  752  ? 6.575   28.987  55.776  1.00 19.15 ? 750  GLY   B O     1 
ATOM   14476 N  N     . ILE   B  1  753  ? 7.731   28.466  57.626  1.00 16.26 ? 751  ILE   B N     1 
ATOM   14477 C  CA    . ILE   B  1  753  ? 8.688   29.536  57.357  1.00 16.54 ? 751  ILE   B CA    1 
ATOM   14478 C  C     . ILE   B  1  753  ? 9.596   29.111  56.210  1.00 16.83 ? 751  ILE   B C     1 
ATOM   14479 O  O     . ILE   B  1  753  ? 10.263  28.074  56.307  1.00 17.92 ? 751  ILE   B O     1 
ATOM   14480 C  CB    . ILE   B  1  753  ? 9.534   29.857  58.594  1.00 15.04 ? 751  ILE   B CB    1 
ATOM   14481 C  CG1   . ILE   B  1  753  ? 8.636   30.177  59.794  1.00 16.47 ? 751  ILE   B CG1   1 
ATOM   14482 C  CG2   . ILE   B  1  753  ? 10.463  31.005  58.260  1.00 16.49 ? 751  ILE   B CG2   1 
ATOM   14483 C  CD1   . ILE   B  1  753  ? 7.802   31.440  59.596  1.00 16.65 ? 751  ILE   B CD1   1 
ATOM   14484 N  N     . PRO   B  1  754  ? 9.645   29.859  55.113  1.00 17.05 ? 752  PRO   B N     1 
ATOM   14485 C  CA    . PRO   B  1  754  ? 10.467  29.445  53.970  1.00 17.64 ? 752  PRO   B CA    1 
ATOM   14486 C  C     . PRO   B  1  754  ? 11.937  29.383  54.342  1.00 17.46 ? 752  PRO   B C     1 
ATOM   14487 O  O     . PRO   B  1  754  ? 12.419  30.121  55.200  1.00 17.60 ? 752  PRO   B O     1 
ATOM   14488 C  CB    . PRO   B  1  754  ? 10.220  30.543  52.930  1.00 18.96 ? 752  PRO   B CB    1 
ATOM   14489 C  CG    . PRO   B  1  754  ? 8.968   31.228  53.359  1.00 22.25 ? 752  PRO   B CG    1 
ATOM   14490 C  CD    . PRO   B  1  754  ? 8.842   31.061  54.841  1.00 18.03 ? 752  PRO   B CD    1 
ATOM   14491 N  N     . ALA   B  1  755  ? 12.656  28.484  53.670  1.00 18.52 ? 753  ALA   B N     1 
ATOM   14492 C  CA    . ALA   B  1  755  ? 14.079  28.352  53.951  1.00 21.42 ? 753  ALA   B CA    1 
ATOM   14493 C  C     . ALA   B  1  755  ? 14.811  29.668  53.730  1.00 18.41 ? 753  ALA   B C     1 
ATOM   14494 O  O     . ALA   B  1  755  ? 15.750  29.992  54.465  1.00 19.30 ? 753  ALA   B O     1 
ATOM   14495 C  CB    . ALA   B  1  755  ? 14.675  27.242  53.086  1.00 23.74 ? 753  ALA   B CB    1 
ATOM   14496 N  N     . SER   B  1  756  ? 14.368  30.467  52.764  1.00 17.21 ? 754  SER   B N     1 
ATOM   14497 C  CA    . SER   B  1  756  ? 15.039  31.734  52.522  1.00 17.99 ? 754  SER   B CA    1 
ATOM   14498 C  C     . SER   B  1  756  ? 14.744  32.758  53.600  1.00 18.10 ? 754  SER   B C     1 
ATOM   14499 O  O     . SER   B  1  756  ? 15.513  33.713  53.755  1.00 19.41 ? 754  SER   B O     1 
ATOM   14500 C  CB    . SER   B  1  756  ? 14.653  32.281  51.159  1.00 21.30 ? 754  SER   B CB    1 
ATOM   14501 O  OG    . SER   B  1  756  ? 13.252  32.412  51.075  1.00 24.56 ? 754  SER   B OG    1 
ATOM   14502 N  N     . ALA   B  1  757  ? 13.649  32.582  54.342  1.00 15.25 ? 755  ALA   B N     1 
ATOM   14503 C  CA    . ALA   B  1  757  ? 13.310  33.494  55.415  1.00 13.28 ? 755  ALA   B CA    1 
ATOM   14504 C  C     . ALA   B  1  757  ? 13.939  33.112  56.743  1.00 14.99 ? 755  ALA   B C     1 
ATOM   14505 O  O     . ALA   B  1  757  ? 13.935  33.931  57.659  1.00 15.96 ? 755  ALA   B O     1 
ATOM   14506 C  CB    . ALA   B  1  757  ? 11.779  33.599  55.570  1.00 15.30 ? 755  ALA   B CB    1 
ATOM   14507 N  N     . LEU   B  1  758  ? 14.476  31.898  56.877  1.00 15.94 ? 756  LEU   B N     1 
ATOM   14508 C  CA    . LEU   B  1  758  ? 15.045  31.477  58.156  1.00 15.39 ? 756  LEU   B CA    1 
ATOM   14509 C  C     . LEU   B  1  758  ? 16.229  30.562  57.882  1.00 15.66 ? 756  LEU   B C     1 
ATOM   14510 O  O     . LEU   B  1  758  ? 16.060  29.391  57.518  1.00 16.53 ? 756  LEU   B O     1 
ATOM   14511 C  CB    . LEU   B  1  758  ? 14.017  30.787  59.035  1.00 13.17 ? 756  LEU   B CB    1 
ATOM   14512 C  CG    . LEU   B  1  758  ? 14.585  30.239  60.345  1.00 14.84 ? 756  LEU   B CG    1 
ATOM   14513 C  CD1   . LEU   B  1  758  ? 15.155  31.329  61.251  1.00 15.83 ? 756  LEU   B CD1   1 
ATOM   14514 C  CD2   . LEU   B  1  758  ? 13.487  29.477  61.085  1.00 17.58 ? 756  LEU   B CD2   1 
ATOM   14515 N  N     . GLN   B  1  759  ? 17.421  31.107  58.048  1.00 15.01 ? 757  GLN   B N     1 
ATOM   14516 C  CA    . GLN   B  1  759  ? 18.658  30.383  57.842  1.00 15.37 ? 757  GLN   B CA    1 
ATOM   14517 C  C     . GLN   B  1  759  ? 19.378  30.279  59.175  1.00 17.00 ? 757  GLN   B C     1 
ATOM   14518 O  O     . GLN   B  1  759  ? 19.383  31.229  59.962  1.00 17.20 ? 757  GLN   B O     1 
ATOM   14519 C  CB    . GLN   B  1  759  ? 19.529  31.133  56.845  1.00 14.37 ? 757  GLN   B CB    1 
ATOM   14520 C  CG    . GLN   B  1  759  ? 18.906  31.166  55.458  1.00 16.31 ? 757  GLN   B CG    1 
ATOM   14521 C  CD    . GLN   B  1  759  ? 19.681  32.036  54.517  1.00 14.87 ? 757  GLN   B CD    1 
ATOM   14522 O  OE1   . GLN   B  1  759  ? 20.511  31.556  53.750  1.00 18.59 ? 757  GLN   B OE1   1 
ATOM   14523 N  NE2   . GLN   B  1  759  ? 19.420  33.333  54.565  1.00 16.93 ? 757  GLN   B NE2   1 
ATOM   14524 N  N     . LEU   B  1  760  ? 19.945  29.111  59.435  1.00 15.59 ? 758  LEU   B N     1 
ATOM   14525 C  CA    . LEU   B  1  760  ? 20.663  28.844  60.673  1.00 13.87 ? 758  LEU   B CA    1 
ATOM   14526 C  C     . LEU   B  1  760  ? 22.152  28.882  60.389  1.00 16.39 ? 758  LEU   B C     1 
ATOM   14527 O  O     . LEU   B  1  760  ? 22.627  28.178  59.501  1.00 16.91 ? 758  LEU   B O     1 
ATOM   14528 C  CB    . LEU   B  1  760  ? 20.311  27.456  61.196  1.00 17.27 ? 758  LEU   B CB    1 
ATOM   14529 C  CG    . LEU   B  1  760  ? 21.033  27.085  62.490  1.00 14.80 ? 758  LEU   B CG    1 
ATOM   14530 C  CD1   . LEU   B  1  760  ? 20.354  27.746  63.675  1.00 17.33 ? 758  LEU   B CD1   1 
ATOM   14531 C  CD2   . LEU   B  1  760  ? 21.084  25.572  62.638  1.00 17.45 ? 758  LEU   B CD2   1 
ATOM   14532 N  N     . LEU   B  1  761  ? 22.894  29.669  61.168  1.00 15.03 ? 759  LEU   B N     1 
ATOM   14533 C  CA    . LEU   B  1  761  ? 24.337  29.825  60.992  1.00 16.15 ? 759  LEU   B CA    1 
ATOM   14534 C  C     . LEU   B  1  761  ? 25.017  29.471  62.306  1.00 15.88 ? 759  LEU   B C     1 
ATOM   14535 O  O     . LEU   B  1  761  ? 25.304  30.356  63.131  1.00 16.46 ? 759  LEU   B O     1 
ATOM   14536 C  CB    . LEU   B  1  761  ? 24.711  31.239  60.554  1.00 16.16 ? 759  LEU   B CB    1 
ATOM   14537 C  CG    . LEU   B  1  761  ? 24.184  31.768  59.211  1.00 17.84 ? 759  LEU   B CG    1 
ATOM   14538 C  CD1   . LEU   B  1  761  ? 24.226  30.701  58.118  1.00 19.31 ? 759  LEU   B CD1   1 
ATOM   14539 C  CD2   . LEU   B  1  761  ? 22.798  32.326  59.341  1.00 21.18 ? 759  LEU   B CD2   1 
ATOM   14540 N  N     . PRO   B  1  762  ? 25.280  28.194  62.548  1.00 15.46 ? 760  PRO   B N     1 
ATOM   14541 C  CA    . PRO   B  1  762  ? 25.993  27.828  63.773  1.00 14.15 ? 760  PRO   B CA    1 
ATOM   14542 C  C     . PRO   B  1  762  ? 27.408  28.359  63.753  1.00 14.88 ? 760  PRO   B C     1 
ATOM   14543 O  O     . PRO   B  1  762  ? 28.032  28.531  62.699  1.00 17.21 ? 760  PRO   B O     1 
ATOM   14544 C  CB    . PRO   B  1  762  ? 25.985  26.293  63.756  1.00 14.86 ? 760  PRO   B CB    1 
ATOM   14545 C  CG    . PRO   B  1  762  ? 24.922  25.924  62.765  1.00 16.33 ? 760  PRO   B CG    1 
ATOM   14546 C  CD    . PRO   B  1  762  ? 24.956  27.013  61.739  1.00 14.87 ? 760  PRO   B CD    1 
ATOM   14547 N  N     . GLY   B  1  763  ? 27.921  28.600  64.943  1.00 14.61 ? 761  GLY   B N     1 
ATOM   14548 C  CA    . GLY   B  1  763  ? 29.318  28.947  65.094  1.00 16.64 ? 761  GLY   B CA    1 
ATOM   14549 C  C     . GLY   B  1  763  ? 29.496  29.869  66.279  1.00 16.35 ? 761  GLY   B C     1 
ATOM   14550 O  O     . GLY   B  1  763  ? 28.581  30.084  67.070  1.00 17.70 ? 761  GLY   B O     1 
ATOM   14551 N  N     . ASP   B  1  764  ? 30.702  30.399  66.396  1.00 18.83 ? 762  ASP   B N     1 
ATOM   14552 C  CA    . ASP   B  1  764  ? 31.029  31.195  67.568  1.00 20.04 ? 762  ASP   B CA    1 
ATOM   14553 C  C     . ASP   B  1  764  ? 30.807  32.674  67.260  1.00 21.77 ? 762  ASP   B C     1 
ATOM   14554 O  O     . ASP   B  1  764  ? 30.104  33.034  66.308  1.00 18.50 ? 762  ASP   B O     1 
ATOM   14555 C  CB    . ASP   B  1  764  ? 32.430  30.828  68.074  1.00 22.62 ? 762  ASP   B CB    1 
ATOM   14556 C  CG    . ASP   B  1  764  ? 33.542  31.246  67.118  1.00 27.45 ? 762  ASP   B CG    1 
ATOM   14557 O  OD1   . ASP   B  1  764  ? 33.328  32.047  66.182  1.00 22.47 ? 762  ASP   B OD1   1 
ATOM   14558 O  OD2   . ASP   B  1  764  ? 34.671  30.761  67.320  1.00 32.19 ? 762  ASP   B OD2   1 
ATOM   14559 N  N     . GLY   B  1  765  ? 31.395  33.548  68.079  1.00 19.46 ? 763  GLY   B N     1 
ATOM   14560 C  CA    . GLY   B  1  765  ? 31.148  34.967  67.925  1.00 17.38 ? 763  GLY   B CA    1 
ATOM   14561 C  C     . GLY   B  1  765  ? 31.637  35.541  66.615  1.00 18.86 ? 763  GLY   B C     1 
ATOM   14562 O  O     . GLY   B  1  765  ? 31.134  36.583  66.194  1.00 19.82 ? 763  GLY   B O     1 
ATOM   14563 N  N     . ARG   B  1  766  ? 32.605  34.889  65.963  1.00 19.53 ? 764  ARG   B N     1 
ATOM   14564 C  CA    . ARG   B  1  766  ? 33.049  35.370  64.658  1.00 20.93 ? 764  ARG   B CA    1 
ATOM   14565 C  C     . ARG   B  1  766  ? 31.935  35.258  63.632  1.00 18.31 ? 764  ARG   B C     1 
ATOM   14566 O  O     . ARG   B  1  766  ? 31.827  36.102  62.736  1.00 19.52 ? 764  ARG   B O     1 
ATOM   14567 C  CB    . ARG   B  1  766  ? 34.265  34.579  64.187  1.00 21.41 ? 764  ARG   B CB    1 
ATOM   14568 C  CG    . ARG   B  1  766  ? 35.472  34.719  65.084  1.00 25.82 ? 764  ARG   B CG    1 
ATOM   14569 C  CD    . ARG   B  1  766  ? 36.526  33.684  64.701  1.00 30.22 ? 764  ARG   B CD    1 
ATOM   14570 N  NE    . ARG   B  1  766  ? 36.027  32.331  64.919  1.00 33.64 ? 764  ARG   B NE    1 
ATOM   14571 C  CZ    . ARG   B  1  766  ? 36.654  31.229  64.533  1.00 37.32 ? 764  ARG   B CZ    1 
ATOM   14572 N  NH1   . ARG   B  1  766  ? 37.806  31.282  63.883  1.00 37.98 ? 764  ARG   B NH1   1 
ATOM   14573 N  NH2   . ARG   B  1  766  ? 36.108  30.045  64.797  1.00 40.34 ? 764  ARG   B NH2   1 
ATOM   14574 N  N     . VAL   B  1  767  ? 31.098  34.226  63.748  1.00 17.63 ? 765  VAL   B N     1 
ATOM   14575 C  CA    . VAL   B  1  767  ? 29.968  34.103  62.838  1.00 16.88 ? 765  VAL   B CA    1 
ATOM   14576 C  C     . VAL   B  1  767  ? 28.951  35.195  63.121  1.00 16.00 ? 765  VAL   B C     1 
ATOM   14577 O  O     . VAL   B  1  767  ? 28.418  35.825  62.196  1.00 17.94 ? 765  VAL   B O     1 
ATOM   14578 C  CB    . VAL   B  1  767  ? 29.353  32.695  62.933  1.00 16.32 ? 765  VAL   B CB    1 
ATOM   14579 C  CG1   . VAL   B  1  767  ? 28.166  32.575  61.988  1.00 18.13 ? 765  VAL   B CG1   1 
ATOM   14580 C  CG2   . VAL   B  1  767  ? 30.394  31.647  62.613  1.00 18.95 ? 765  VAL   B CG2   1 
ATOM   14581 N  N     . GLY   B  1  768  ? 28.666  35.439  64.402  1.00 15.85 ? 766  GLY   B N     1 
ATOM   14582 C  CA    . GLY   B  1  768  ? 27.779  36.540  64.737  1.00 17.36 ? 766  GLY   B CA    1 
ATOM   14583 C  C     . GLY   B  1  768  ? 28.318  37.864  64.227  1.00 16.92 ? 766  GLY   B C     1 
ATOM   14584 O  O     . GLY   B  1  768  ? 27.583  38.668  63.648  1.00 16.74 ? 766  GLY   B O     1 
ATOM   14585 N  N     . ALA   B  1  769  ? 29.621  38.091  64.407  1.00 16.83 ? 767  ALA   B N     1 
ATOM   14586 C  CA    . ALA   B  1  769  ? 30.205  39.355  63.971  1.00 18.20 ? 767  ALA   B CA    1 
ATOM   14587 C  C     . ALA   B  1  769  ? 30.103  39.514  62.459  1.00 19.59 ? 767  ALA   B C     1 
ATOM   14588 O  O     . ALA   B  1  769  ? 29.814  40.607  61.960  1.00 18.28 ? 767  ALA   B O     1 
ATOM   14589 C  CB    . ALA   B  1  769  ? 31.660  39.429  64.435  1.00 18.35 ? 767  ALA   B CB    1 
ATOM   14590 N  N     . ALA   B  1  770  ? 30.325  38.428  61.715  1.00 16.87 ? 768  ALA   B N     1 
ATOM   14591 C  CA    . ALA   B  1  770  ? 30.246  38.498  60.263  1.00 16.09 ? 768  ALA   B CA    1 
ATOM   14592 C  C     . ALA   B  1  770  ? 28.824  38.811  59.814  1.00 17.86 ? 768  ALA   B C     1 
ATOM   14593 O  O     . ALA   B  1  770  ? 28.615  39.535  58.832  1.00 19.71 ? 768  ALA   B O     1 
ATOM   14594 C  CB    . ALA   B  1  770  ? 30.715  37.175  59.658  1.00 17.38 ? 768  ALA   B CB    1 
ATOM   14595 N  N     . LEU   B  1  771  ? 27.831  38.273  60.524  1.00 16.45 ? 769  LEU   B N     1 
ATOM   14596 C  CA    . LEU   B  1  771  ? 26.450  38.555  60.163  1.00 16.37 ? 769  LEU   B CA    1 
ATOM   14597 C  C     . LEU   B  1  771  ? 26.113  40.010  60.440  1.00 17.79 ? 769  LEU   B C     1 
ATOM   14598 O  O     . LEU   B  1  771  ? 25.495  40.685  59.608  1.00 19.36 ? 769  LEU   B O     1 
ATOM   14599 C  CB    . LEU   B  1  771  ? 25.515  37.628  60.942  1.00 17.29 ? 769  LEU   B CB    1 
ATOM   14600 C  CG    . LEU   B  1  771  ? 25.585  36.161  60.518  1.00 15.57 ? 769  LEU   B CG    1 
ATOM   14601 C  CD1   . LEU   B  1  771  ? 24.793  35.316  61.500  1.00 16.85 ? 769  LEU   B CD1   1 
ATOM   14602 C  CD2   . LEU   B  1  771  ? 25.059  35.993  59.091  1.00 16.21 ? 769  LEU   B CD2   1 
ATOM   14603 N  N     . VAL   B  1  772  ? 26.520  40.505  61.607  1.00 16.39 ? 770  VAL   B N     1 
ATOM   14604 C  CA    . VAL   B  1  772  ? 26.240  41.885  61.988  1.00 15.81 ? 770  VAL   B CA    1 
ATOM   14605 C  C     . VAL   B  1  772  ? 26.836  42.853  60.979  1.00 21.59 ? 770  VAL   B C     1 
ATOM   14606 O  O     . VAL   B  1  772  ? 26.207  43.854  60.610  1.00 21.37 ? 770  VAL   B O     1 
ATOM   14607 C  CB    . VAL   B  1  772  ? 26.771  42.144  63.406  1.00 17.52 ? 770  VAL   B CB    1 
ATOM   14608 C  CG1   . VAL   B  1  772  ? 26.789  43.635  63.722  1.00 19.09 ? 770  VAL   B CG1   1 
ATOM   14609 C  CG2   . VAL   B  1  772  ? 25.943  41.381  64.422  1.00 17.92 ? 770  VAL   B CG2   1 
ATOM   14610 N  N     . ALA   B  1  773  ? 28.054  42.569  60.515  1.00 19.98 ? 771  ALA   B N     1 
ATOM   14611 C  CA    . ALA   B  1  773  ? 28.755  43.478  59.620  1.00 19.66 ? 771  ALA   B CA    1 
ATOM   14612 C  C     . ALA   B  1  773  ? 28.288  43.382  58.178  1.00 23.71 ? 771  ALA   B C     1 
ATOM   14613 O  O     . ALA   B  1  773  ? 28.667  44.239  57.370  1.00 24.60 ? 771  ALA   B O     1 
ATOM   14614 C  CB    . ALA   B  1  773  ? 30.255  43.197  59.678  1.00 21.99 ? 771  ALA   B CB    1 
ATOM   14615 N  N     . ALA   B  1  774  ? 27.505  42.363  57.831  1.00 20.88 ? 772  ALA   B N     1 
ATOM   14616 C  CA    . ALA   B  1  774  ? 27.119  42.156  56.442  1.00 20.74 ? 772  ALA   B CA    1 
ATOM   14617 C  C     . ALA   B  1  774  ? 26.301  43.334  55.928  1.00 23.08 ? 772  ALA   B C     1 
ATOM   14618 O  O     . ALA   B  1  774  ? 25.497  43.930  56.652  1.00 22.81 ? 772  ALA   B O     1 
ATOM   14619 C  CB    . ALA   B  1  774  ? 26.317  40.864  56.291  1.00 23.05 ? 772  ALA   B CB    1 
ATOM   14620 N  N     . ALA   B  1  775  ? 26.493  43.639  54.644  1.00 25.23 ? 773  ALA   B N     1 
ATOM   14621 C  CA    . ALA   B  1  775  ? 25.983  44.886  54.083  1.00 23.93 ? 773  ALA   B CA    1 
ATOM   14622 C  C     . ALA   B  1  775  ? 24.460  44.983  54.164  1.00 22.82 ? 773  ALA   B C     1 
ATOM   14623 O  O     . ALA   B  1  775  ? 23.915  46.068  54.396  1.00 24.42 ? 773  ALA   B O     1 
ATOM   14624 C  CB    . ALA   B  1  775  ? 26.447  45.021  52.634  1.00 28.20 ? 773  ALA   B CB    1 
ATOM   14625 N  N     . GLU   B  1  776  ? 23.756  43.870  53.972  1.00 20.85 ? 774  GLU   B N     1 
ATOM   14626 C  CA    . GLU   B  1  776  ? 22.300  43.901  53.896  1.00 20.14 ? 774  GLU   B CA    1 
ATOM   14627 C  C     . GLU   B  1  776  ? 21.618  43.692  55.243  1.00 17.50 ? 774  GLU   B C     1 
ATOM   14628 O  O     . GLU   B  1  776  ? 20.384  43.676  55.306  1.00 18.61 ? 774  GLU   B O     1 
ATOM   14629 C  CB    . GLU   B  1  776  ? 21.791  42.871  52.882  1.00 18.03 ? 774  GLU   B CB    1 
ATOM   14630 C  CG    . GLU   B  1  776  ? 22.399  43.021  51.480  1.00 26.26 ? 774  GLU   B CG    1 
ATOM   14631 C  CD    . GLU   B  1  776  ? 23.739  42.298  51.308  1.00 34.31 ? 774  GLU   B CD    1 
ATOM   14632 O  OE1   . GLU   B  1  776  ? 24.244  41.673  52.275  1.00 28.76 ? 774  GLU   B OE1   1 
ATOM   14633 O  OE2   . GLU   B  1  776  ? 24.295  42.358  50.189  1.00 35.88 ? 774  GLU   B OE2   1 
ATOM   14634 N  N     . THR   B  1  777  ? 22.376  43.523  56.317  1.00 18.60 ? 775  THR   B N     1 
ATOM   14635 C  CA    . THR   B  1  777  ? 21.753  43.372  57.624  1.00 17.29 ? 775  THR   B CA    1 
ATOM   14636 C  C     . THR   B  1  777  ? 21.018  44.648  57.994  1.00 17.29 ? 775  THR   B C     1 
ATOM   14637 O  O     . THR   B  1  777  ? 21.587  45.743  57.965  1.00 18.98 ? 775  THR   B O     1 
ATOM   14638 C  CB    . THR   B  1  777  ? 22.836  43.042  58.643  1.00 17.96 ? 775  THR   B CB    1 
ATOM   14639 O  OG1   . THR   B  1  777  ? 23.333  41.734  58.354  1.00 19.30 ? 775  THR   B OG1   1 
ATOM   14640 C  CG2   . THR   B  1  777  ? 22.278  43.060  60.053  1.00 17.42 ? 775  THR   B CG2   1 
ATOM   14641 N  N     . ALA   B  1  778  ? 19.727  44.501  58.308  1.00 15.16 ? 776  ALA   B N     1 
ATOM   14642 C  CA    . ALA   B  1  778  ? 18.844  45.633  58.537  1.00 15.22 ? 776  ALA   B CA    1 
ATOM   14643 C  C     . ALA   B  1  778  ? 18.449  45.789  59.997  1.00 15.81 ? 776  ALA   B C     1 
ATOM   14644 O  O     . ALA   B  1  778  ? 17.801  46.780  60.353  1.00 17.79 ? 776  ALA   B O     1 
ATOM   14645 C  CB    . ALA   B  1  778  ? 17.594  45.496  57.667  1.00 16.43 ? 776  ALA   B CB    1 
ATOM   14646 N  N     . GLY   B  1  779  ? 18.834  44.852  60.847  1.00 13.82 ? 777  GLY   B N     1 
ATOM   14647 C  CA    . GLY   B  1  779  ? 18.547  44.961  62.264  1.00 14.43 ? 777  GLY   B CA    1 
ATOM   14648 C  C     . GLY   B  1  779  ? 19.194  43.786  62.956  1.00 15.54 ? 777  GLY   B C     1 
ATOM   14649 O  O     . GLY   B  1  779  ? 19.482  42.757  62.339  1.00 15.75 ? 777  GLY   B O     1 
ATOM   14650 N  N     . VAL   B  1  780  ? 19.451  43.969  64.246  1.00 14.00 ? 778  VAL   B N     1 
ATOM   14651 C  CA    . VAL   B  1  780  ? 20.101  42.941  65.039  1.00 13.59 ? 778  VAL   B CA    1 
ATOM   14652 C  C     . VAL   B  1  780  ? 19.332  42.771  66.333  1.00 12.75 ? 778  VAL   B C     1 
ATOM   14653 O  O     . VAL   B  1  780  ? 19.013  43.754  67.011  1.00 13.68 ? 778  VAL   B O     1 
ATOM   14654 C  CB    . VAL   B  1  780  ? 21.588  43.241  65.318  1.00 13.31 ? 778  VAL   B CB    1 
ATOM   14655 C  CG1   . VAL   B  1  780  ? 22.178  42.154  66.201  1.00 15.87 ? 778  VAL   B CG1   1 
ATOM   14656 C  CG2   . VAL   B  1  780  ? 22.361  43.336  64.021  1.00 16.11 ? 778  VAL   B CG2   1 
ATOM   14657 N  N     . MET   B  1  781  ? 19.022  41.532  66.661  1.00 13.21 ? 779  MET   B N     1 
ATOM   14658 C  CA    . MET   B  1  781  ? 18.427  41.175  67.946  1.00 13.40 ? 779  MET   B CA    1 
ATOM   14659 C  C     . MET   B  1  781  ? 19.475  40.354  68.670  1.00 14.00 ? 779  MET   B C     1 
ATOM   14660 O  O     . MET   B  1  781  ? 19.897  39.302  68.184  1.00 14.57 ? 779  MET   B O     1 
ATOM   14661 C  CB    . MET   B  1  781  ? 17.142  40.381  67.744  1.00 13.78 ? 779  MET   B CB    1 
ATOM   14662 C  CG    . MET   B  1  781  ? 16.175  41.118  66.826  1.00 16.11 ? 779  MET   B CG    1 
ATOM   14663 S  SD    . MET   B  1  781  ? 14.692  40.191  66.506  1.00 15.60 ? 779  MET   B SD    1 
ATOM   14664 C  CE    . MET   B  1  781  ? 13.864  40.294  68.085  1.00 14.65 ? 779  MET   B CE    1 
ATOM   14665 N  N     . PHE   B  1  782  ? 19.960  40.877  69.779  1.00 13.90 ? 780  PHE   B N     1 
ATOM   14666 C  CA    . PHE   B  1  782  ? 21.039  40.253  70.514  1.00 13.67 ? 780  PHE   B CA    1 
ATOM   14667 C  C     . PHE   B  1  782  ? 20.588  40.032  71.942  1.00 12.49 ? 780  PHE   B C     1 
ATOM   14668 O  O     . PHE   B  1  782  ? 20.048  40.941  72.578  1.00 14.93 ? 780  PHE   B O     1 
ATOM   14669 C  CB    . PHE   B  1  782  ? 22.271  41.152  70.551  1.00 14.39 ? 780  PHE   B CB    1 
ATOM   14670 C  CG    . PHE   B  1  782  ? 23.342  40.633  71.441  1.00 13.58 ? 780  PHE   B CG    1 
ATOM   14671 C  CD1   . PHE   B  1  782  ? 24.162  39.594  71.016  1.00 13.85 ? 780  PHE   B CD1   1 
ATOM   14672 C  CD2   . PHE   B  1  782  ? 23.519  41.149  72.719  1.00 14.46 ? 780  PHE   B CD2   1 
ATOM   14673 C  CE1   . PHE   B  1  782  ? 25.149  39.093  71.825  1.00 16.49 ? 780  PHE   B CE1   1 
ATOM   14674 C  CE2   . PHE   B  1  782  ? 24.518  40.639  73.538  1.00 15.51 ? 780  PHE   B CE2   1 
ATOM   14675 C  CZ    . PHE   B  1  782  ? 25.332  39.620  73.085  1.00 16.62 ? 780  PHE   B CZ    1 
ATOM   14676 N  N     . THR   B  1  783  ? 20.800  38.825  72.431  1.00 13.76 ? 781  THR   B N     1 
ATOM   14677 C  CA    . THR   B  1  783  ? 20.696  38.557  73.853  1.00 14.84 ? 781  THR   B CA    1 
ATOM   14678 C  C     . THR   B  1  783  ? 21.979  37.869  74.272  1.00 14.76 ? 781  THR   B C     1 
ATOM   14679 O  O     . THR   B  1  783  ? 22.397  36.892  73.645  1.00 14.55 ? 781  THR   B O     1 
ATOM   14680 C  CB    . THR   B  1  783  ? 19.463  37.710  74.171  1.00 14.90 ? 781  THR   B CB    1 
ATOM   14681 O  OG1   . THR   B  1  783  ? 18.298  38.405  73.726  1.00 15.08 ? 781  THR   B OG1   1 
ATOM   14682 C  CG2   . THR   B  1  783  ? 19.344  37.536  75.672  1.00 16.15 ? 781  THR   B CG2   1 
ATOM   14683 N  N     . GLY   B  1  784  ? 22.618  38.390  75.310  1.00 14.34 ? 782  GLY   B N     1 
ATOM   14684 C  CA    . GLY   B  1  784  ? 23.914  37.872  75.690  1.00 14.11 ? 782  GLY   B CA    1 
ATOM   14685 C  C     . GLY   B  1  784  ? 24.585  38.831  76.641  1.00 15.57 ? 782  GLY   B C     1 
ATOM   14686 O  O     . GLY   B  1  784  ? 23.926  39.637  77.288  1.00 16.63 ? 782  GLY   B O     1 
ATOM   14687 N  N     . SER   B  1  785  ? 25.899  38.735  76.709  1.00 16.61 ? 783  SER   B N     1 
ATOM   14688 C  CA    . SER   B  1  785  ? 26.612  39.562  77.664  1.00 19.65 ? 783  SER   B CA    1 
ATOM   14689 C  C     . SER   B  1  785  ? 26.650  41.017  77.206  1.00 18.46 ? 783  SER   B C     1 
ATOM   14690 O  O     . SER   B  1  785  ? 26.653  41.328  76.009  1.00 18.42 ? 783  SER   B O     1 
ATOM   14691 C  CB    . SER   B  1  785  ? 28.029  39.028  77.855  1.00 18.32 ? 783  SER   B CB    1 
ATOM   14692 O  OG    . SER   B  1  785  ? 28.787  39.145  76.666  1.00 18.55 ? 783  SER   B OG    1 
ATOM   14693 N  N     . THR   B  1  786  ? 26.701  41.921  78.186  1.00 18.70 ? 784  THR   B N     1 
ATOM   14694 C  CA    . THR   B  1  786  ? 26.825  43.338  77.867  1.00 18.33 ? 784  THR   B CA    1 
ATOM   14695 C  C     . THR   B  1  786  ? 28.089  43.611  77.058  1.00 17.40 ? 784  THR   B C     1 
ATOM   14696 O  O     . THR   B  1  786  ? 28.072  44.422  76.123  1.00 20.24 ? 784  THR   B O     1 
ATOM   14697 C  CB    . THR   B  1  786  ? 26.816  44.152  79.165  1.00 20.36 ? 784  THR   B CB    1 
ATOM   14698 O  OG1   . THR   B  1  786  ? 25.663  43.792  79.940  1.00 22.15 ? 784  THR   B OG1   1 
ATOM   14699 C  CG2   . THR   B  1  786  ? 26.760  45.628  78.863  1.00 24.49 ? 784  THR   B CG2   1 
ATOM   14700 N  N     . GLU   B  1  787  ? 29.196  42.939  77.404  1.00 20.70 ? 785  GLU   B N     1 
ATOM   14701 C  CA    . GLU   B  1  787  ? 30.464  43.146  76.707  1.00 22.45 ? 785  GLU   B CA    1 
ATOM   14702 C  C     . GLU   B  1  787  ? 30.332  42.864  75.214  1.00 22.27 ? 785  GLU   B C     1 
ATOM   14703 O  O     . GLU   B  1  787  ? 30.817  43.636  74.375  1.00 20.07 ? 785  GLU   B O     1 
ATOM   14704 C  CB    . GLU   B  1  787  ? 31.544  42.249  77.326  1.00 23.33 ? 785  GLU   B CB    1 
ATOM   14705 N  N     . VAL   B  1  788  ? 29.683  41.752  74.866  1.00 17.17 ? 786  VAL   B N     1 
ATOM   14706 C  CA    . VAL   B  1  788  ? 29.501  41.415  73.459  1.00 16.87 ? 786  VAL   B CA    1 
ATOM   14707 C  C     . VAL   B  1  788  ? 28.545  42.399  72.796  1.00 17.35 ? 786  VAL   B C     1 
ATOM   14708 O  O     . VAL   B  1  788  ? 28.758  42.821  71.656  1.00 18.42 ? 786  VAL   B O     1 
ATOM   14709 C  CB    . VAL   B  1  788  ? 29.019  39.958  73.321  1.00 17.63 ? 786  VAL   B CB    1 
ATOM   14710 C  CG1   . VAL   B  1  788  ? 28.592  39.675  71.883  1.00 18.03 ? 786  VAL   B CG1   1 
ATOM   14711 C  CG2   . VAL   B  1  788  ? 30.113  38.992  73.759  1.00 18.66 ? 786  VAL   B CG2   1 
ATOM   14712 N  N     . ALA   B  1  789  ? 27.484  42.793  73.504  1.00 17.97 ? 787  ALA   B N     1 
ATOM   14713 C  CA    . ALA   B  1  789  ? 26.539  43.739  72.924  1.00 15.88 ? 787  ALA   B CA    1 
ATOM   14714 C  C     . ALA   B  1  789  ? 27.241  45.023  72.515  1.00 15.97 ? 787  ALA   B C     1 
ATOM   14715 O  O     . ALA   B  1  789  ? 26.909  45.624  71.493  1.00 16.49 ? 787  ALA   B O     1 
ATOM   14716 C  CB    . ALA   B  1  789  ? 25.410  44.044  73.910  1.00 15.46 ? 787  ALA   B CB    1 
ATOM   14717 N  N     . ARG   B  1  790  ? 28.214  45.467  73.313  1.00 16.98 ? 788  ARG   B N     1 
ATOM   14718 C  CA    . ARG   B  1  790  ? 28.904  46.711  72.988  1.00 19.36 ? 788  ARG   B CA    1 
ATOM   14719 C  C     . ARG   B  1  790  ? 29.720  46.572  71.708  1.00 18.80 ? 788  ARG   B C     1 
ATOM   14720 O  O     . ARG   B  1  790  ? 29.820  47.524  70.928  1.00 22.05 ? 788  ARG   B O     1 
ATOM   14721 C  CB    . ARG   B  1  790  ? 29.793  47.111  74.170  1.00 23.23 ? 788  ARG   B CB    1 
ATOM   14722 C  CG    . ARG   B  1  790  ? 30.243  48.557  74.180  1.00 33.78 ? 788  ARG   B CG    1 
ATOM   14723 C  CD    . ARG   B  1  790  ? 31.014  48.880  75.469  1.00 30.32 ? 788  ARG   B CD    1 
ATOM   14724 N  NE    . ARG   B  1  790  ? 30.218  48.641  76.668  1.00 31.79 ? 788  ARG   B NE    1 
ATOM   14725 C  CZ    . ARG   B  1  790  ? 29.299  49.479  77.132  1.00 34.76 ? 788  ARG   B CZ    1 
ATOM   14726 N  NH1   . ARG   B  1  790  ? 28.999  50.602  76.493  1.00 31.74 ? 788  ARG   B NH1   1 
ATOM   14727 N  NH2   . ARG   B  1  790  ? 28.659  49.180  78.262  1.00 35.24 ? 788  ARG   B NH2   1 
ATOM   14728 N  N     . LEU   B  1  791  ? 30.277  45.389  71.462  1.00 17.87 ? 789  LEU   B N     1 
ATOM   14729 C  CA    . LEU   B  1  791  ? 31.005  45.155  70.219  1.00 21.65 ? 789  LEU   B CA    1 
ATOM   14730 C  C     . LEU   B  1  791  ? 30.067  45.210  69.027  1.00 20.68 ? 789  LEU   B C     1 
ATOM   14731 O  O     . LEU   B  1  791  ? 30.401  45.786  67.986  1.00 20.51 ? 789  LEU   B O     1 
ATOM   14732 C  CB    . LEU   B  1  791  ? 31.684  43.789  70.279  1.00 20.82 ? 789  LEU   B CB    1 
ATOM   14733 C  CG    . LEU   B  1  791  ? 32.729  43.597  71.378  1.00 23.75 ? 789  LEU   B CG    1 
ATOM   14734 C  CD1   . LEU   B  1  791  ? 33.302  42.193  71.316  1.00 23.50 ? 789  LEU   B CD1   1 
ATOM   14735 C  CD2   . LEU   B  1  791  ? 33.836  44.649  71.270  1.00 23.06 ? 789  LEU   B CD2   1 
ATOM   14736 N  N     . ILE   B  1  792  ? 28.882  44.612  69.164  1.00 19.11 ? 790  ILE   B N     1 
ATOM   14737 C  CA    . ILE   B  1  792  ? 27.912  44.641  68.079  1.00 18.76 ? 790  ILE   B CA    1 
ATOM   14738 C  C     . ILE   B  1  792  ? 27.448  46.062  67.827  1.00 17.48 ? 790  ILE   B C     1 
ATOM   14739 O  O     . ILE   B  1  792  ? 27.299  46.495  66.676  1.00 20.25 ? 790  ILE   B O     1 
ATOM   14740 C  CB    . ILE   B  1  792  ? 26.740  43.721  68.439  1.00 16.76 ? 790  ILE   B CB    1 
ATOM   14741 C  CG1   . ILE   B  1  792  ? 27.205  42.271  68.413  1.00 16.80 ? 790  ILE   B CG1   1 
ATOM   14742 C  CG2   . ILE   B  1  792  ? 25.561  43.970  67.507  1.00 17.89 ? 790  ILE   B CG2   1 
ATOM   14743 C  CD1   . ILE   B  1  792  ? 26.219  41.297  68.986  1.00 18.27 ? 790  ILE   B CD1   1 
ATOM   14744 N  N     . GLN   B  1  793  ? 27.174  46.793  68.903  1.00 17.92 ? 791  GLN   B N     1 
ATOM   14745 C  CA    . GLN   B  1  793  ? 26.757  48.179  68.783  1.00 17.73 ? 791  GLN   B CA    1 
ATOM   14746 C  C     . GLN   B  1  793  ? 27.784  48.992  68.015  1.00 17.86 ? 791  GLN   B C     1 
ATOM   14747 O  O     . GLN   B  1  793  ? 27.427  49.806  67.155  1.00 20.17 ? 791  GLN   B O     1 
ATOM   14748 C  CB    . GLN   B  1  793  ? 26.578  48.753  70.184  1.00 19.79 ? 791  GLN   B CB    1 
ATOM   14749 C  CG    . GLN   B  1  793  ? 26.169  50.195  70.209  1.00 19.00 ? 791  GLN   B CG    1 
ATOM   14750 C  CD    . GLN   B  1  793  ? 26.434  50.830  71.549  1.00 23.97 ? 791  GLN   B CD    1 
ATOM   14751 O  OE1   . GLN   B  1  793  ? 27.451  50.557  72.193  1.00 24.36 ? 791  GLN   B OE1   1 
ATOM   14752 N  NE2   . GLN   B  1  793  ? 25.517  51.677  71.987  1.00 26.07 ? 791  GLN   B NE2   1 
ATOM   14753 N  N     . ALA   B  1  794  ? 29.065  48.776  68.305  1.00 21.45 ? 792  ALA   B N     1 
ATOM   14754 C  CA    . ALA   B  1  794  ? 30.106  49.506  67.589  1.00 22.09 ? 792  ALA   B CA    1 
ATOM   14755 C  C     . ALA   B  1  794  ? 30.115  49.153  66.105  1.00 23.70 ? 792  ALA   B C     1 
ATOM   14756 O  O     . ALA   B  1  794  ? 30.266  50.041  65.251  1.00 23.65 ? 792  ALA   B O     1 
ATOM   14757 C  CB    . ALA   B  1  794  ? 31.470  49.229  68.222  1.00 25.58 ? 792  ALA   B CB    1 
ATOM   14758 N  N     . GLN   B  1  795  ? 29.979  47.861  65.780  1.00 21.98 ? 793  GLN   B N     1 
ATOM   14759 C  CA    . GLN   B  1  795  ? 29.912  47.447  64.378  1.00 21.51 ? 793  GLN   B CA    1 
ATOM   14760 C  C     . GLN   B  1  795  ? 28.780  48.168  63.661  1.00 20.29 ? 793  GLN   B C     1 
ATOM   14761 O  O     . GLN   B  1  795  ? 28.954  48.679  62.548  1.00 22.11 ? 793  GLN   B O     1 
ATOM   14762 C  CB    . GLN   B  1  795  ? 29.662  45.934  64.270  1.00 23.14 ? 793  GLN   B CB    1 
ATOM   14763 C  CG    . GLN   B  1  795  ? 30.809  44.981  64.536  1.00 28.66 ? 793  GLN   B CG    1 
ATOM   14764 C  CD    . GLN   B  1  795  ? 30.406  43.512  64.297  1.00 29.47 ? 793  GLN   B CD    1 
ATOM   14765 O  OE1   . GLN   B  1  795  ? 29.782  42.878  65.151  1.00 31.35 ? 793  GLN   B OE1   1 
ATOM   14766 N  NE2   . GLN   B  1  795  ? 30.762  42.978  63.137  1.00 28.02 ? 793  GLN   B NE2   1 
ATOM   14767 N  N     . LEU   B  1  796  ? 27.597  48.208  64.287  1.00 17.23 ? 794  LEU   B N     1 
ATOM   14768 C  CA    . LEU   B  1  796  ? 26.419  48.743  63.612  1.00 18.08 ? 794  LEU   B CA    1 
ATOM   14769 C  C     . LEU   B  1  796  ? 26.509  50.245  63.424  1.00 21.29 ? 794  LEU   B C     1 
ATOM   14770 O  O     . LEU   B  1  796  ? 25.967  50.776  62.451  1.00 23.80 ? 794  LEU   B O     1 
ATOM   14771 C  CB    . LEU   B  1  796  ? 25.157  48.421  64.411  1.00 17.62 ? 794  LEU   B CB    1 
ATOM   14772 C  CG    . LEU   B  1  796  ? 24.755  46.952  64.363  1.00 19.77 ? 794  LEU   B CG    1 
ATOM   14773 C  CD1   . LEU   B  1  796  ? 23.528  46.745  65.220  1.00 18.85 ? 794  LEU   B CD1   1 
ATOM   14774 C  CD2   . LEU   B  1  796  ? 24.463  46.534  62.940  1.00 18.83 ? 794  LEU   B CD2   1 
ATOM   14775 N  N     . ALA   B  1  797  ? 27.172  50.939  64.349  1.00 20.85 ? 795  ALA   B N     1 
ATOM   14776 C  CA    . ALA   B  1  797  ? 27.242  52.393  64.290  1.00 25.71 ? 795  ALA   B CA    1 
ATOM   14777 C  C     . ALA   B  1  797  ? 28.067  52.879  63.113  1.00 24.72 ? 795  ALA   B C     1 
ATOM   14778 O  O     . ALA   B  1  797  ? 27.956  54.045  62.734  1.00 26.94 ? 795  ALA   B O     1 
ATOM   14779 C  CB    . ALA   B  1  797  ? 27.812  52.956  65.593  1.00 26.28 ? 795  ALA   B CB    1 
ATOM   14780 N  N     . ASP   B  1  798  ? 28.882  52.012  62.521  1.00 24.87 ? 796  ASP   B N     1 
ATOM   14781 C  CA    . ASP   B  1  798  ? 29.576  52.378  61.297  1.00 29.73 ? 796  ASP   B CA    1 
ATOM   14782 C  C     . ASP   B  1  798  ? 28.662  52.373  60.084  1.00 29.45 ? 796  ASP   B C     1 
ATOM   14783 O  O     . ASP   B  1  798  ? 29.062  52.868  59.025  1.00 30.76 ? 796  ASP   B O     1 
ATOM   14784 C  CB    . ASP   B  1  798  ? 30.714  51.393  61.049  1.00 29.12 ? 796  ASP   B CB    1 
ATOM   14785 N  N     . ARG   B  1  799  ? 27.451  51.855  60.211  1.00 26.03 ? 797  ARG   B N     1 
ATOM   14786 C  CA    A ARG   B  1  799  ? 26.575  51.576  59.086  0.41 28.24 ? 797  ARG   B CA    1 
ATOM   14787 C  CA    B ARG   B  1  799  ? 26.609  51.644  59.052  0.59 28.25 ? 797  ARG   B CA    1 
ATOM   14788 C  C     . ARG   B  1  799  ? 25.288  52.382  59.203  1.00 26.75 ? 797  ARG   B C     1 
ATOM   14789 O  O     . ARG   B  1  799  ? 24.907  52.826  60.289  1.00 25.59 ? 797  ARG   B O     1 
ATOM   14790 C  CB    A ARG   B  1  799  ? 26.200  50.088  59.063  0.41 29.16 ? 797  ARG   B CB    1 
ATOM   14791 C  CB    B ARG   B  1  799  ? 26.374  50.147  58.814  0.59 29.88 ? 797  ARG   B CB    1 
ATOM   14792 C  CG    A ARG   B  1  799  ? 27.341  49.118  59.381  0.41 29.13 ? 797  ARG   B CG    1 
ATOM   14793 C  CG    B ARG   B  1  799  ? 27.653  49.308  58.911  0.59 30.05 ? 797  ARG   B CG    1 
ATOM   14794 C  CD    A ARG   B  1  799  ? 26.796  47.697  59.427  0.41 27.81 ? 797  ARG   B CD    1 
ATOM   14795 C  CD    B ARG   B  1  799  ? 27.638  48.177  57.903  0.59 29.13 ? 797  ARG   B CD    1 
ATOM   14796 N  NE    A ARG   B  1  799  ? 25.776  47.545  58.398  0.41 30.58 ? 797  ARG   B NE    1 
ATOM   14797 N  NE    B ARG   B  1  799  ? 26.270  47.747  57.668  0.59 31.02 ? 797  ARG   B NE    1 
ATOM   14798 C  CZ    A ARG   B  1  799  ? 24.687  46.796  58.503  0.41 27.55 ? 797  ARG   B CZ    1 
ATOM   14799 C  CZ    B ARG   B  1  799  ? 25.679  46.742  58.298  0.59 28.32 ? 797  ARG   B CZ    1 
ATOM   14800 N  NH1   A ARG   B  1  799  ? 24.464  46.040  59.566  0.41 22.57 ? 797  ARG   B NH1   1 
ATOM   14801 N  NH1   B ARG   B  1  799  ? 26.350  45.953  59.118  0.59 25.70 ? 797  ARG   B NH1   1 
ATOM   14802 N  NH2   A ARG   B  1  799  ? 23.793  46.813  57.518  0.41 26.31 ? 797  ARG   B NH2   1 
ATOM   14803 N  NH2   B ARG   B  1  799  ? 24.378  46.534  58.109  0.59 28.80 ? 797  ARG   B NH2   1 
ATOM   14804 N  N     . LEU   B  1  800  ? 24.612  52.536  58.071  1.00 22.69 ? 798  LEU   B N     1 
ATOM   14805 C  CA    . LEU   B  1  800  ? 23.284  53.112  58.003  1.00 25.23 ? 798  LEU   B CA    1 
ATOM   14806 C  C     . LEU   B  1  800  ? 22.454  52.249  57.070  1.00 26.50 ? 798  LEU   B C     1 
ATOM   14807 O  O     . LEU   B  1  800  ? 22.990  51.571  56.191  1.00 26.46 ? 798  LEU   B O     1 
ATOM   14808 C  CB    . LEU   B  1  800  ? 23.300  54.527  57.416  1.00 27.66 ? 798  LEU   B CB    1 
ATOM   14809 C  CG    . LEU   B  1  800  ? 23.896  55.645  58.262  1.00 28.83 ? 798  LEU   B CG    1 
ATOM   14810 C  CD1   . LEU   B  1  800  ? 23.828  56.937  57.473  1.00 31.86 ? 798  LEU   B CD1   1 
ATOM   14811 C  CD2   . LEU   B  1  800  ? 23.132  55.759  59.561  1.00 23.76 ? 798  LEU   B CD2   1 
ATOM   14812 N  N     . SER   B  1  801  ? 21.140  52.283  57.266  1.00 25.65 ? 799  SER   B N     1 
ATOM   14813 C  CA    . SER   B  1  801  ? 20.232  51.643  56.337  1.00 29.44 ? 799  SER   B CA    1 
ATOM   14814 C  C     . SER   B  1  801  ? 20.325  52.357  54.995  1.00 31.38 ? 799  SER   B C     1 
ATOM   14815 O  O     . SER   B  1  801  ? 20.893  53.447  54.898  1.00 30.52 ? 799  SER   B O     1 
ATOM   14816 C  CB    . SER   B  1  801  ? 18.805  51.732  56.864  1.00 28.83 ? 799  SER   B CB    1 
ATOM   14817 O  OG    . SER   B  1  801  ? 18.330  53.065  56.772  1.00 31.89 ? 799  SER   B OG    1 
ATOM   14818 N  N     . PRO   B  1  802  ? 19.796  51.755  53.926  1.00 34.72 ? 800  PRO   B N     1 
ATOM   14819 C  CA    . PRO   B  1  802  ? 19.723  52.483  52.648  1.00 34.85 ? 800  PRO   B CA    1 
ATOM   14820 C  C     . PRO   B  1  802  ? 18.933  53.776  52.742  1.00 34.04 ? 800  PRO   B C     1 
ATOM   14821 O  O     . PRO   B  1  802  ? 19.158  54.686  51.935  1.00 36.91 ? 800  PRO   B O     1 
ATOM   14822 C  CB    . PRO   B  1  802  ? 19.064  51.470  51.705  1.00 32.50 ? 800  PRO   B CB    1 
ATOM   14823 C  CG    . PRO   B  1  802  ? 19.471  50.146  52.265  1.00 36.34 ? 800  PRO   B CG    1 
ATOM   14824 C  CD    . PRO   B  1  802  ? 19.460  50.327  53.766  1.00 30.14 ? 800  PRO   B CD    1 
ATOM   14825 N  N     . ALA   B  1  803  ? 18.030  53.893  53.712  1.00 31.99 ? 801  ALA   B N     1 
ATOM   14826 C  CA    . ALA   B  1  803  ? 17.314  55.136  53.974  1.00 34.78 ? 801  ALA   B CA    1 
ATOM   14827 C  C     . ALA   B  1  803  ? 18.129  56.121  54.804  1.00 35.85 ? 801  ALA   B C     1 
ATOM   14828 O  O     . ALA   B  1  803  ? 17.632  57.210  55.107  1.00 37.66 ? 801  ALA   B O     1 
ATOM   14829 C  CB    . ALA   B  1  803  ? 15.988  54.836  54.674  1.00 32.84 ? 801  ALA   B CB    1 
ATOM   14830 N  N     . GLY   B  1  804  ? 19.354  55.770  55.177  1.00 33.10 ? 802  GLY   B N     1 
ATOM   14831 C  CA    . GLY   B  1  804  ? 20.196  56.677  55.934  1.00 31.96 ? 802  GLY   B CA    1 
ATOM   14832 C  C     . GLY   B  1  804  ? 19.872  56.769  57.408  1.00 27.02 ? 802  GLY   B C     1 
ATOM   14833 O  O     . GLY   B  1  804  ? 19.996  57.845  58.002  1.00 29.63 ? 802  GLY   B O     1 
ATOM   14834 N  N     . ARG   B  1  805  ? 19.472  55.670  58.028  1.00 27.89 ? 803  ARG   B N     1 
ATOM   14835 C  CA    . ARG   B  1  805  ? 19.061  55.684  59.422  1.00 26.42 ? 803  ARG   B CA    1 
ATOM   14836 C  C     . ARG   B  1  805  ? 19.778  54.579  60.179  1.00 24.53 ? 803  ARG   B C     1 
ATOM   14837 O  O     . ARG   B  1  805  ? 20.244  53.606  59.576  1.00 24.51 ? 803  ARG   B O     1 
ATOM   14838 C  CB    . ARG   B  1  805  ? 17.542  55.499  59.541  1.00 28.15 ? 803  ARG   B CB    1 
ATOM   14839 C  CG    . ARG   B  1  805  ? 16.742  56.619  58.896  1.00 31.47 ? 803  ARG   B CG    1 
ATOM   14840 C  CD    . ARG   B  1  805  ? 17.069  57.964  59.529  1.00 34.15 ? 803  ARG   B CD    1 
ATOM   14841 N  NE    . ARG   B  1  805  ? 16.315  59.043  58.899  1.00 35.04 ? 803  ARG   B NE    1 
ATOM   14842 C  CZ    . ARG   B  1  805  ? 16.793  59.842  57.955  1.00 33.20 ? 803  ARG   B CZ    1 
ATOM   14843 N  NH1   . ARG   B  1  805  ? 18.047  59.750  57.538  1.00 33.11 ? 803  ARG   B NH1   1 
ATOM   14844 N  NH2   . ARG   B  1  805  ? 15.993  60.757  57.413  1.00 39.05 ? 803  ARG   B NH2   1 
ATOM   14845 N  N     . PRO   B  1  806  ? 19.910  54.710  61.502  1.00 21.70 ? 804  PRO   B N     1 
ATOM   14846 C  CA    . PRO   B  1  806  ? 20.649  53.694  62.253  1.00 22.39 ? 804  PRO   B CA    1 
ATOM   14847 C  C     . PRO   B  1  806  ? 19.977  52.339  62.137  1.00 20.18 ? 804  PRO   B C     1 
ATOM   14848 O  O     . PRO   B  1  806  ? 18.748  52.233  62.076  1.00 20.82 ? 804  PRO   B O     1 
ATOM   14849 C  CB    . PRO   B  1  806  ? 20.620  54.219  63.692  1.00 22.73 ? 804  PRO   B CB    1 
ATOM   14850 C  CG    . PRO   B  1  806  ? 20.427  55.699  63.532  1.00 23.64 ? 804  PRO   B CG    1 
ATOM   14851 C  CD    . PRO   B  1  806  ? 19.497  55.829  62.366  1.00 27.20 ? 804  PRO   B CD    1 
ATOM   14852 N  N     . ILE   B  1  807  ? 20.809  51.305  62.093  1.00 18.72 ? 805  ILE   B N     1 
ATOM   14853 C  CA    . ILE   B  1  807  ? 20.339  49.922  62.090  1.00 18.46 ? 805  ILE   B CA    1 
ATOM   14854 C  C     . ILE   B  1  807  ? 19.835  49.624  63.496  1.00 17.78 ? 805  ILE   B C     1 
ATOM   14855 O  O     . ILE   B  1  807  ? 20.606  49.766  64.456  1.00 18.64 ? 805  ILE   B O     1 
ATOM   14856 C  CB    . ILE   B  1  807  ? 21.484  48.966  61.737  1.00 18.55 ? 805  ILE   B CB    1 
ATOM   14857 C  CG1   . ILE   B  1  807  ? 22.098  49.323  60.378  1.00 23.05 ? 805  ILE   B CG1   1 
ATOM   14858 C  CG2   . ILE   B  1  807  ? 20.999  47.517  61.796  1.00 18.07 ? 805  ILE   B CG2   1 
ATOM   14859 C  CD1   . ILE   B  1  807  ? 21.152  49.131  59.238  1.00 25.93 ? 805  ILE   B CD1   1 
ATOM   14860 N  N     . PRO   B  1  808  ? 18.578  49.212  63.673  1.00 16.92 ? 806  PRO   B N     1 
ATOM   14861 C  CA    . PRO   B  1  808  ? 18.069  48.957  65.029  1.00 17.55 ? 806  PRO   B CA    1 
ATOM   14862 C  C     . PRO   B  1  808  ? 18.770  47.779  65.683  1.00 18.66 ? 806  PRO   B C     1 
ATOM   14863 O  O     . PRO   B  1  808  ? 19.044  46.756  65.049  1.00 15.89 ? 806  PRO   B O     1 
ATOM   14864 C  CB    . PRO   B  1  808  ? 16.585  48.650  64.800  1.00 18.97 ? 806  PRO   B CB    1 
ATOM   14865 C  CG    . PRO   B  1  808  ? 16.259  49.264  63.460  1.00 21.52 ? 806  PRO   B CG    1 
ATOM   14866 C  CD    . PRO   B  1  808  ? 17.519  49.123  62.657  1.00 15.59 ? 806  PRO   B CD    1 
ATOM   14867 N  N     . LEU   B  1  809  ? 19.073  47.939  66.967  1.00 16.57 ? 807  LEU   B N     1 
ATOM   14868 C  CA    . LEU   B  1  809  ? 19.661  46.876  67.764  1.00 15.33 ? 807  LEU   B CA    1 
ATOM   14869 C  C     . LEU   B  1  809  ? 18.810  46.730  69.007  1.00 15.39 ? 807  LEU   B C     1 
ATOM   14870 O  O     . LEU   B  1  809  ? 18.609  47.708  69.727  1.00 17.33 ? 807  LEU   B O     1 
ATOM   14871 C  CB    . LEU   B  1  809  ? 21.081  47.265  68.173  1.00 15.94 ? 807  LEU   B CB    1 
ATOM   14872 C  CG    . LEU   B  1  809  ? 21.736  46.392  69.237  1.00 17.27 ? 807  LEU   B CG    1 
ATOM   14873 C  CD1   . LEU   B  1  809  ? 21.869  44.960  68.729  1.00 15.98 ? 807  LEU   B CD1   1 
ATOM   14874 C  CD2   . LEU   B  1  809  ? 23.103  46.959  69.604  1.00 19.59 ? 807  LEU   B CD2   1 
ATOM   14875 N  N     . ILE   B  1  810  ? 18.304  45.526  69.252  1.00 14.11 ? 808  ILE   B N     1 
ATOM   14876 C  CA    . ILE   B  1  810  ? 17.751  45.173  70.553  1.00 14.69 ? 808  ILE   B CA    1 
ATOM   14877 C  C     . ILE   B  1  810  ? 18.849  44.384  71.230  1.00 16.38 ? 808  ILE   B C     1 
ATOM   14878 O  O     . ILE   B  1  810  ? 19.290  43.358  70.703  1.00 16.76 ? 808  ILE   B O     1 
ATOM   14879 C  CB    . ILE   B  1  810  ? 16.473  44.331  70.436  1.00 16.26 ? 808  ILE   B CB    1 
ATOM   14880 C  CG1   . ILE   B  1  810  ? 15.431  45.039  69.581  1.00 17.12 ? 808  ILE   B CG1   1 
ATOM   14881 C  CG2   . ILE   B  1  810  ? 15.921  44.033  71.845  1.00 19.57 ? 808  ILE   B CG2   1 
ATOM   14882 C  CD1   . ILE   B  1  810  ? 14.094  44.316  69.546  1.00 19.03 ? 808  ILE   B CD1   1 
ATOM   14883 N  N     . ALA   B  1  811  ? 19.334  44.874  72.364  1.00 15.38 ? 809  ALA   B N     1 
ATOM   14884 C  CA    . ALA   B  1  811  ? 20.431  44.209  73.058  1.00 14.62 ? 809  ALA   B CA    1 
ATOM   14885 C  C     . ALA   B  1  811  ? 19.997  43.987  74.496  1.00 17.67 ? 809  ALA   B C     1 
ATOM   14886 O  O     . ALA   B  1  811  ? 19.960  44.931  75.289  1.00 17.70 ? 809  ALA   B O     1 
ATOM   14887 C  CB    . ALA   B  1  811  ? 21.726  45.023  72.995  1.00 17.41 ? 809  ALA   B CB    1 
ATOM   14888 N  N     . GLU   B  1  812  ? 19.693  42.744  74.822  1.00 14.26 ? 810  GLU   B N     1 
ATOM   14889 C  CA    . GLU   B  1  812  ? 19.194  42.362  76.131  1.00 16.85 ? 810  GLU   B CA    1 
ATOM   14890 C  C     . GLU   B  1  812  ? 20.327  41.628  76.820  1.00 16.47 ? 810  GLU   B C     1 
ATOM   14891 O  O     . GLU   B  1  812  ? 20.788  40.584  76.340  1.00 16.57 ? 810  GLU   B O     1 
ATOM   14892 C  CB    . GLU   B  1  812  ? 17.940  41.507  75.970  1.00 17.67 ? 810  GLU   B CB    1 
ATOM   14893 C  CG    . GLU   B  1  812  ? 16.842  42.318  75.250  1.00 19.18 ? 810  GLU   B CG    1 
ATOM   14894 C  CD    . GLU   B  1  812  ? 16.478  43.602  76.015  1.00 22.40 ? 810  GLU   B CD    1 
ATOM   14895 O  OE1   . GLU   B  1  812  ? 15.772  43.495  77.032  1.00 20.58 ? 810  GLU   B OE1   1 
ATOM   14896 O  OE2   . GLU   B  1  812  ? 16.889  44.715  75.611  1.00 20.68 ? 810  GLU   B OE2   1 
ATOM   14897 N  N     . THR   B  1  813  ? 20.808  42.204  77.915  1.00 16.39 ? 811  THR   B N     1 
ATOM   14898 C  CA    . THR   B  1  813  ? 22.130  41.871  78.404  1.00 14.81 ? 811  THR   B CA    1 
ATOM   14899 C  C     . THR   B  1  813  ? 22.106  41.412  79.857  1.00 14.93 ? 811  THR   B C     1 
ATOM   14900 O  O     . THR   B  1  813  ? 21.088  40.921  80.331  1.00 16.88 ? 811  THR   B O     1 
ATOM   14901 C  CB    . THR   B  1  813  ? 23.106  43.012  78.089  1.00 16.90 ? 811  THR   B CB    1 
ATOM   14902 O  OG1   . THR   B  1  813  ? 22.561  44.267  78.522  1.00 17.50 ? 811  THR   B OG1   1 
ATOM   14903 C  CG2   . THR   B  1  813  ? 23.326  43.088  76.576  1.00 18.22 ? 811  THR   B CG2   1 
ATOM   14904 N  N     . GLY   B  1  814  ? 23.218  41.544  80.567  1.00 16.83 ? 812  GLY   B N     1 
ATOM   14905 C  CA    . GLY   B  1  814  ? 23.366  40.847  81.826  1.00 17.60 ? 812  GLY   B CA    1 
ATOM   14906 C  C     . GLY   B  1  814  ? 22.638  41.511  82.977  1.00 17.52 ? 812  GLY   B C     1 
ATOM   14907 O  O     . GLY   B  1  814  ? 21.966  42.529  82.841  1.00 19.42 ? 812  GLY   B O     1 
ATOM   14908 N  N     . GLY   B  1  815  ? 22.780  40.902  84.149  1.00 16.77 ? 813  GLY   B N     1 
ATOM   14909 C  CA    . GLY   B  1  815  ? 22.183  41.455  85.345  1.00 16.87 ? 813  GLY   B CA    1 
ATOM   14910 C  C     . GLY   B  1  815  ? 23.124  41.279  86.514  1.00 17.25 ? 813  GLY   B C     1 
ATOM   14911 O  O     . GLY   B  1  815  ? 24.092  40.521  86.454  1.00 19.48 ? 813  GLY   B O     1 
ATOM   14912 N  N     . GLN   B  1  816  ? 22.842  42.026  87.568  1.00 15.67 ? 814  GLN   B N     1 
ATOM   14913 C  CA    . GLN   B  1  816  ? 23.496  41.847  88.863  1.00 17.56 ? 814  GLN   B CA    1 
ATOM   14914 C  C     . GLN   B  1  816  ? 22.377  41.879  89.895  1.00 14.99 ? 814  GLN   B C     1 
ATOM   14915 O  O     . GLN   B  1  816  ? 22.193  42.863  90.614  1.00 17.94 ? 814  GLN   B O     1 
ATOM   14916 C  CB    . GLN   B  1  816  ? 24.540  42.924  89.120  1.00 18.43 ? 814  GLN   B CB    1 
ATOM   14917 C  CG    . GLN   B  1  816  ? 25.426  42.626  90.304  1.00 17.19 ? 814  GLN   B CG    1 
ATOM   14918 C  CD    . GLN   B  1  816  ? 26.322  41.436  90.042  1.00 19.14 ? 814  GLN   B CD    1 
ATOM   14919 O  OE1   . GLN   B  1  816  ? 25.885  40.290  90.151  1.00 18.49 ? 814  GLN   B OE1   1 
ATOM   14920 N  NE2   . GLN   B  1  816  ? 27.595  41.700  89.690  1.00 18.79 ? 814  GLN   B NE2   1 
ATOM   14921 N  N     . ASN   B  1  817  ? 21.615  40.801  89.949  1.00 14.19 ? 815  ASN   B N     1 
ATOM   14922 C  CA    . ASN   B  1  817  ? 20.257  40.869  90.473  1.00 13.06 ? 815  ASN   B CA    1 
ATOM   14923 C  C     . ASN   B  1  817  ? 20.259  40.649  91.974  1.00 15.19 ? 815  ASN   B C     1 
ATOM   14924 O  O     . ASN   B  1  817  ? 20.869  39.696  92.472  1.00 16.28 ? 815  ASN   B O     1 
ATOM   14925 C  CB    . ASN   B  1  817  ? 19.394  39.821  89.785  1.00 13.79 ? 815  ASN   B CB    1 
ATOM   14926 C  CG    . ASN   B  1  817  ? 19.529  39.894  88.286  1.00 14.18 ? 815  ASN   B CG    1 
ATOM   14927 O  OD1   . ASN   B  1  817  ? 19.342  40.958  87.690  1.00 14.12 ? 815  ASN   B OD1   1 
ATOM   14928 N  ND2   . ASN   B  1  817  ? 19.885  38.782  87.675  1.00 14.19 ? 815  ASN   B ND2   1 
ATOM   14929 N  N     . ALA   B  1  818  ? 19.554  41.517  92.680  1.00 15.13 ? 816  ALA   B N     1 
ATOM   14930 C  CA    . ALA   B  1  818  ? 19.481  41.460  94.129  1.00 14.55 ? 816  ALA   B CA    1 
ATOM   14931 C  C     . ALA   B  1  818  ? 18.094  41.034  94.579  1.00 13.09 ? 816  ALA   B C     1 
ATOM   14932 O  O     . ALA   B  1  818  ? 17.093  41.203  93.879  1.00 14.89 ? 816  ALA   B O     1 
ATOM   14933 C  CB    . ALA   B  1  818  ? 19.782  42.831  94.741  1.00 14.23 ? 816  ALA   B CB    1 
ATOM   14934 N  N     . MET   B  1  819  ? 18.049  40.476  95.779  1.00 12.72 ? 817  MET   B N     1 
ATOM   14935 C  CA    . MET   B  1  819  ? 16.812  40.269  96.499  1.00 14.65 ? 817  MET   B CA    1 
ATOM   14936 C  C     . MET   B  1  819  ? 17.009  40.865  97.876  1.00 14.65 ? 817  MET   B C     1 
ATOM   14937 O  O     . MET   B  1  819  ? 18.013  40.580  98.536  1.00 14.88 ? 817  MET   B O     1 
ATOM   14938 C  CB    . MET   B  1  819  ? 16.486  38.784  96.637  1.00 13.92 ? 817  MET   B CB    1 
ATOM   14939 C  CG    . MET   B  1  819  ? 15.219  38.545  97.484  1.00 16.21 ? 817  MET   B CG    1 
ATOM   14940 S  SD    . MET   B  1  819  ? 14.946  36.787  97.784  1.00 19.46 ? 817  MET   B SD    1 
ATOM   14941 C  CE    . MET   B  1  819  ? 14.374  36.287  96.167  1.00 19.70 ? 817  MET   B CE    1 
ATOM   14942 N  N     . ILE   B  1  820  ? 16.079  41.709  98.295  1.00 15.44 ? 818  ILE   B N     1 
ATOM   14943 C  CA    . ILE   B  1  820  ? 16.130  42.304  99.620  1.00 14.21 ? 818  ILE   B CA    1 
ATOM   14944 C  C     . ILE   B  1  820  ? 15.105  41.601  100.480 1.00 15.34 ? 818  ILE   B C     1 
ATOM   14945 O  O     . ILE   B  1  820  ? 13.947  41.466  100.078 1.00 15.51 ? 818  ILE   B O     1 
ATOM   14946 C  CB    . ILE   B  1  820  ? 15.844  43.807  99.554  1.00 15.12 ? 818  ILE   B CB    1 
ATOM   14947 C  CG1   . ILE   B  1  820  ? 16.942  44.497  98.758  1.00 15.72 ? 818  ILE   B CG1   1 
ATOM   14948 C  CG2   . ILE   B  1  820  ? 15.740  44.394  100.966 1.00 17.65 ? 818  ILE   B CG2   1 
ATOM   14949 C  CD1   . ILE   B  1  820  ? 16.747  45.978  98.686  1.00 18.86 ? 818  ILE   B CD1   1 
ATOM   14950 N  N     . VAL   B  1  821  ? 15.524  41.166  101.664 1.00 15.57 ? 819  VAL   B N     1 
ATOM   14951 C  CA    . VAL   B  1  821  ? 14.680  40.409  102.579 1.00 14.65 ? 819  VAL   B CA    1 
ATOM   14952 C  C     . VAL   B  1  821  ? 14.681  41.165  103.892 1.00 15.75 ? 819  VAL   B C     1 
ATOM   14953 O  O     . VAL   B  1  821  ? 15.748  41.421  104.456 1.00 17.34 ? 819  VAL   B O     1 
ATOM   14954 C  CB    . VAL   B  1  821  ? 15.249  39.001  102.796 1.00 14.90 ? 819  VAL   B CB    1 
ATOM   14955 C  CG1   . VAL   B  1  821  ? 14.389  38.201  103.765 1.00 16.89 ? 819  VAL   B CG1   1 
ATOM   14956 C  CG2   . VAL   B  1  821  ? 15.361  38.277  101.463 1.00 16.81 ? 819  VAL   B CG2   1 
ATOM   14957 N  N     . ASP   B  1  822  ? 13.502  41.518  104.384 1.00 17.28 ? 820  ASP   B N     1 
ATOM   14958 C  CA    . ASP   B  1  822  ? 13.451  42.171  105.682 1.00 18.63 ? 820  ASP   B CA    1 
ATOM   14959 C  C     . ASP   B  1  822  ? 13.036  41.178  106.765 1.00 18.52 ? 820  ASP   B C     1 
ATOM   14960 O  O     . ASP   B  1  822  ? 12.792  39.995  106.514 1.00 18.52 ? 820  ASP   B O     1 
ATOM   14961 C  CB    . ASP   B  1  822  ? 12.649  43.476  105.634 1.00 19.47 ? 820  ASP   B CB    1 
ATOM   14962 C  CG    . ASP   B  1  822  ? 11.143  43.267  105.594 1.00 20.69 ? 820  ASP   B CG    1 
ATOM   14963 O  OD1   . ASP   B  1  822  ? 10.648  42.139  105.780 1.00 19.54 ? 820  ASP   B OD1   1 
ATOM   14964 O  OD2   . ASP   B  1  822  ? 10.450  44.281  105.374 1.00 22.74 ? 820  ASP   B OD2   1 
ATOM   14965 N  N     . SER   B  1  823  ? 12.958  41.669  107.999 1.00 19.54 ? 821  SER   B N     1 
ATOM   14966 C  CA    . SER   B  1  823  ? 12.682  40.762  109.101 1.00 19.59 ? 821  SER   B CA    1 
ATOM   14967 C  C     . SER   B  1  823  ? 11.238  40.286  109.141 1.00 22.80 ? 821  SER   B C     1 
ATOM   14968 O  O     . SER   B  1  823  ? 10.910  39.430  109.972 1.00 24.75 ? 821  SER   B O     1 
ATOM   14969 C  CB    . SER   B  1  823  ? 13.067  41.416  110.426 1.00 20.58 ? 821  SER   B CB    1 
ATOM   14970 O  OG    . SER   B  1  823  ? 12.323  42.600  110.632 1.00 24.82 ? 821  SER   B OG    1 
ATOM   14971 N  N     . SER   B  1  824  ? 10.366  40.807  108.283 1.00 19.50 ? 822  SER   B N     1 
ATOM   14972 C  CA    . SER   B  1  824  ? 8.996   40.327  108.261 1.00 19.12 ? 822  SER   B CA    1 
ATOM   14973 C  C     . SER   B  1  824  ? 8.806   39.142  107.328 1.00 21.32 ? 822  SER   B C     1 
ATOM   14974 O  O     . SER   B  1  824  ? 7.748   38.504  107.358 1.00 23.08 ? 822  SER   B O     1 
ATOM   14975 C  CB    . SER   B  1  824  ? 8.030   41.449  107.868 1.00 21.29 ? 822  SER   B CB    1 
ATOM   14976 O  OG    . SER   B  1  824  ? 8.098   41.721  106.482 1.00 18.72 ? 822  SER   B OG    1 
ATOM   14977 N  N     . ALA   B  1  825  ? 9.793   38.846  106.495 1.00 18.75 ? 823  ALA   B N     1 
ATOM   14978 C  CA    . ALA   B  1  825  ? 9.649   37.789  105.514 1.00 17.84 ? 823  ALA   B CA    1 
ATOM   14979 C  C     . ALA   B  1  825  ? 9.632   36.435  106.205 1.00 20.11 ? 823  ALA   B C     1 
ATOM   14980 O  O     . ALA   B  1  825  ? 10.186  36.265  107.293 1.00 21.05 ? 823  ALA   B O     1 
ATOM   14981 C  CB    . ALA   B  1  825  ? 10.823  37.849  104.543 1.00 18.10 ? 823  ALA   B CB    1 
ATOM   14982 N  N     . LEU   B  1  826  ? 9.001   35.461  105.560 1.00 21.35 ? 824  LEU   B N     1 
ATOM   14983 C  CA    . LEU   B  1  826  ? 8.946   34.103  106.088 1.00 22.23 ? 824  LEU   B CA    1 
ATOM   14984 C  C     . LEU   B  1  826  ? 10.177  33.345  105.610 1.00 22.34 ? 824  LEU   B C     1 
ATOM   14985 O  O     . LEU   B  1  826  ? 10.362  33.159  104.403 1.00 19.77 ? 824  LEU   B O     1 
ATOM   14986 C  CB    . LEU   B  1  826  ? 7.679   33.399  105.611 1.00 27.49 ? 824  LEU   B CB    1 
ATOM   14987 C  CG    . LEU   B  1  826  ? 7.462   31.982  106.146 1.00 27.82 ? 824  LEU   B CG    1 
ATOM   14988 C  CD1   . LEU   B  1  826  ? 7.345   31.982  107.658 1.00 32.70 ? 824  LEU   B CD1   1 
ATOM   14989 C  CD2   . LEU   B  1  826  ? 6.214   31.383  105.524 1.00 35.46 ? 824  LEU   B CD2   1 
ATOM   14990 N  N     . ALA   B  1  827  ? 11.006  32.892  106.558 1.00 20.05 ? 825  ALA   B N     1 
ATOM   14991 C  CA    . ALA   B  1  827  ? 12.313  32.345  106.205 1.00 18.67 ? 825  ALA   B CA    1 
ATOM   14992 C  C     . ALA   B  1  827  ? 12.199  31.186  105.220 1.00 19.95 ? 825  ALA   B C     1 
ATOM   14993 O  O     . ALA   B  1  827  ? 12.969  31.113  104.252 1.00 18.73 ? 825  ALA   B O     1 
ATOM   14994 C  CB    . ALA   B  1  827  ? 13.050  31.909  107.469 1.00 21.38 ? 825  ALA   B CB    1 
ATOM   14995 N  N     . GLU   B  1  828  ? 11.250  30.269  105.453 1.00 21.03 ? 826  GLU   B N     1 
ATOM   14996 C  CA    . GLU   B  1  828  ? 11.107  29.113  104.569 1.00 20.72 ? 826  GLU   B CA    1 
ATOM   14997 C  C     . GLU   B  1  828  ? 10.793  29.546  103.145 1.00 23.15 ? 826  GLU   B C     1 
ATOM   14998 O  O     . GLU   B  1  828  ? 11.286  28.945  102.181 1.00 20.03 ? 826  GLU   B O     1 
ATOM   14999 C  CB    . GLU   B  1  828  ? 9.994   28.198  105.073 1.00 23.23 ? 826  GLU   B CB    1 
ATOM   15000 C  CG    . GLU   B  1  828  ? 10.349  27.366  106.294 1.00 29.95 ? 826  GLU   B CG    1 
ATOM   15001 C  CD    . GLU   B  1  828  ? 10.268  28.134  107.605 1.00 30.85 ? 826  GLU   B CD    1 
ATOM   15002 O  OE1   . GLU   B  1  828  ? 9.908   29.339  107.604 1.00 28.16 ? 826  GLU   B OE1   1 
ATOM   15003 O  OE2   . GLU   B  1  828  ? 10.572  27.513  108.650 1.00 31.52 ? 826  GLU   B OE2   1 
ATOM   15004 N  N     . GLN   B  1  829  ? 9.957   30.578  102.994 1.00 18.37 ? 827  GLN   B N     1 
ATOM   15005 C  CA    . GLN   B  1  829  ? 9.625   31.078  101.663 1.00 19.93 ? 827  GLN   B CA    1 
ATOM   15006 C  C     . GLN   B  1  829  ? 10.844  31.706  101.010 1.00 20.57 ? 827  GLN   B C     1 
ATOM   15007 O  O     . GLN   B  1  829  ? 11.135  31.462  99.833  1.00 18.92 ? 827  GLN   B O     1 
ATOM   15008 C  CB    . GLN   B  1  829  ? 8.526   32.132  101.774 1.00 24.15 ? 827  GLN   B CB    1 
ATOM   15009 C  CG    . GLN   B  1  829  ? 7.124   31.622  101.957 1.00 30.74 ? 827  GLN   B CG    1 
ATOM   15010 C  CD    . GLN   B  1  829  ? 6.109   32.725  101.701 1.00 35.56 ? 827  GLN   B CD    1 
ATOM   15011 O  OE1   . GLN   B  1  829  ? 6.419   33.913  101.847 1.00 32.33 ? 827  GLN   B OE1   1 
ATOM   15012 N  NE2   . GLN   B  1  829  ? 4.898   32.342  101.311 1.00 37.82 ? 827  GLN   B NE2   1 
ATOM   15013 N  N     . VAL   B  1  830  ? 11.558  32.539  101.764 1.00 19.04 ? 828  VAL   B N     1 
ATOM   15014 C  CA    . VAL   B  1  830  ? 12.787  33.141  101.265 1.00 17.01 ? 828  VAL   B CA    1 
ATOM   15015 C  C     . VAL   B  1  830  ? 13.746  32.056  100.802 1.00 18.68 ? 828  VAL   B C     1 
ATOM   15016 O  O     . VAL   B  1  830  ? 14.320  32.130  99.709  1.00 18.22 ? 828  VAL   B O     1 
ATOM   15017 C  CB    . VAL   B  1  830  ? 13.431  34.013  102.354 1.00 18.09 ? 828  VAL   B CB    1 
ATOM   15018 C  CG1   . VAL   B  1  830  ? 14.825  34.441  101.928 1.00 17.98 ? 828  VAL   B CG1   1 
ATOM   15019 C  CG2   . VAL   B  1  830  ? 12.555  35.217  102.695 1.00 18.39 ? 828  VAL   B CG2   1 
ATOM   15020 N  N     . VAL   B  1  831  ? 13.957  31.040  101.643 1.00 17.55 ? 829  VAL   B N     1 
ATOM   15021 C  CA    . VAL   B  1  831  ? 14.968  30.046  101.316 1.00 17.60 ? 829  VAL   B CA    1 
ATOM   15022 C  C     . VAL   B  1  831  ? 14.612  29.305  100.034 1.00 16.74 ? 829  VAL   B C     1 
ATOM   15023 O  O     . VAL   B  1  831  ? 15.471  29.097  99.167  1.00 18.61 ? 829  VAL   B O     1 
ATOM   15024 C  CB    . VAL   B  1  831  ? 15.217  29.112  102.510 1.00 17.65 ? 829  VAL   B CB    1 
ATOM   15025 C  CG1   . VAL   B  1  831  ? 15.954  27.857  102.068 1.00 19.08 ? 829  VAL   B CG1   1 
ATOM   15026 C  CG2   . VAL   B  1  831  ? 16.002  29.871  103.565 1.00 18.35 ? 829  VAL   B CG2   1 
ATOM   15027 N  N     . GLY   B  1  832  ? 13.344  28.927  99.872  1.00 16.95 ? 830  GLY   B N     1 
ATOM   15028 C  CA    . GLY   B  1  832  ? 12.951  28.252  98.646  1.00 18.55 ? 830  GLY   B CA    1 
ATOM   15029 C  C     . GLY   B  1  832  ? 13.140  29.135  97.432  1.00 17.87 ? 830  GLY   B C     1 
ATOM   15030 O  O     . GLY   B  1  832  ? 13.613  28.683  96.382  1.00 18.51 ? 830  GLY   B O     1 
ATOM   15031 N  N     . ASP   B  1  833  ? 12.808  30.415  97.569  1.00 15.26 ? 831  ASP   B N     1 
ATOM   15032 C  CA    . ASP   B  1  833  ? 12.928  31.325  96.437  1.00 16.96 ? 831  ASP   B CA    1 
ATOM   15033 C  C     . ASP   B  1  833  ? 14.381  31.657  96.139  1.00 17.00 ? 831  ASP   B C     1 
ATOM   15034 O  O     . ASP   B  1  833  ? 14.740  31.869  94.978  1.00 17.68 ? 831  ASP   B O     1 
ATOM   15035 C  CB    . ASP   B  1  833  ? 12.102  32.584  96.696  1.00 15.84 ? 831  ASP   B CB    1 
ATOM   15036 C  CG    . ASP   B  1  833  ? 10.609  32.302  96.684  1.00 18.03 ? 831  ASP   B CG    1 
ATOM   15037 O  OD1   . ASP   B  1  833  ? 10.207  31.235  96.167  1.00 21.39 ? 831  ASP   B OD1   1 
ATOM   15038 O  OD2   . ASP   B  1  833  ? 9.836   33.139  97.180  1.00 20.78 ? 831  ASP   B OD2   1 
ATOM   15039 N  N     . VAL   B  1  834  ? 15.227  31.689  97.166  1.00 15.41 ? 832  VAL   B N     1 
ATOM   15040 C  CA    . VAL   B  1  834  ? 16.651  31.899  96.952  1.00 15.00 ? 832  VAL   B CA    1 
ATOM   15041 C  C     . VAL   B  1  834  ? 17.251  30.707  96.230  1.00 15.67 ? 832  VAL   B C     1 
ATOM   15042 O  O     . VAL   B  1  834  ? 18.043  30.855  95.292  1.00 16.06 ? 832  VAL   B O     1 
ATOM   15043 C  CB    . VAL   B  1  834  ? 17.360  32.169  98.291  1.00 15.27 ? 832  VAL   B CB    1 
ATOM   15044 C  CG1   . VAL   B  1  834  ? 18.846  32.018  98.134  1.00 17.57 ? 832  VAL   B CG1   1 
ATOM   15045 C  CG2   . VAL   B  1  834  ? 17.030  33.563  98.791  1.00 18.03 ? 832  VAL   B CG2   1 
ATOM   15046 N  N     . ILE   B  1  835  ? 16.914  29.500  96.674  1.00 15.77 ? 833  ILE   B N     1 
ATOM   15047 C  CA    . ILE   B  1  835  ? 17.489  28.328  96.027  1.00 19.70 ? 833  ILE   B CA    1 
ATOM   15048 C  C     . ILE   B  1  835  ? 17.086  28.286  94.564  1.00 18.50 ? 833  ILE   B C     1 
ATOM   15049 O  O     . ILE   B  1  835  ? 17.925  28.101  93.673  1.00 21.71 ? 833  ILE   B O     1 
ATOM   15050 C  CB    . ILE   B  1  835  ? 17.105  27.051  96.783  1.00 20.82 ? 833  ILE   B CB    1 
ATOM   15051 C  CG1   . ILE   B  1  835  ? 17.824  27.044  98.122  1.00 25.77 ? 833  ILE   B CG1   1 
ATOM   15052 C  CG2   . ILE   B  1  835  ? 17.452  25.813  95.949  1.00 21.64 ? 833  ILE   B CG2   1 
ATOM   15053 C  CD1   . ILE   B  1  835  ? 17.526  25.844  98.923  1.00 24.54 ? 833  ILE   B CD1   1 
ATOM   15054 N  N     . THR   B  1  836  ? 15.803  28.509  94.291  1.00 16.39 ? 834  THR   B N     1 
ATOM   15055 C  CA    . THR   B  1  836  ? 15.335  28.548  92.914  1.00 18.28 ? 834  THR   B CA    1 
ATOM   15056 C  C     . THR   B  1  836  ? 16.048  29.645  92.134  1.00 19.14 ? 834  THR   B C     1 
ATOM   15057 O  O     . THR   B  1  836  ? 16.551  29.420  91.028  1.00 22.95 ? 834  THR   B O     1 
ATOM   15058 C  CB    . THR   B  1  836  ? 13.833  28.810  92.935  1.00 18.02 ? 834  THR   B CB    1 
ATOM   15059 O  OG1   . THR   B  1  836  ? 13.167  27.664  93.484  1.00 24.59 ? 834  THR   B OG1   1 
ATOM   15060 C  CG2   . THR   B  1  836  ? 13.324  29.066  91.530  1.00 22.81 ? 834  THR   B CG2   1 
ATOM   15061 N  N     . SER   B  1  837  ? 16.126  30.838  92.707  1.00 16.35 ? 835  SER   B N     1 
ATOM   15062 C  CA    . SER   B  1  837  ? 16.620  31.969  91.928  1.00 16.05 ? 835  SER   B CA    1 
ATOM   15063 C  C     . SER   B  1  837  ? 18.131  31.939  91.757  1.00 14.89 ? 835  SER   B C     1 
ATOM   15064 O  O     . SER   B  1  837  ? 18.645  32.370  90.721  1.00 16.51 ? 835  SER   B O     1 
ATOM   15065 C  CB    . SER   B  1  837  ? 16.216  33.273  92.605  1.00 16.31 ? 835  SER   B CB    1 
ATOM   15066 O  OG    . SER   B  1  837  ? 14.806  33.336  92.729  1.00 15.11 ? 835  SER   B OG    1 
ATOM   15067 N  N     . ALA   B  1  838  ? 18.862  31.468  92.766  1.00 14.97 ? 836  ALA   B N     1 
ATOM   15068 C  CA    . ALA   B  1  838  ? 20.313  31.564  92.750  1.00 14.75 ? 836  ALA   B CA    1 
ATOM   15069 C  C     . ALA   B  1  838  ? 20.976  30.329  92.171  1.00 16.66 ? 836  ALA   B C     1 
ATOM   15070 O  O     . ALA   B  1  838  ? 22.024  30.438  91.526  1.00 19.09 ? 836  ALA   B O     1 
ATOM   15071 C  CB    . ALA   B  1  838  ? 20.830  31.769  94.178  1.00 15.16 ? 836  ALA   B CB    1 
ATOM   15072 N  N     . PHE   B  1  839  ? 20.413  29.152  92.410  1.00 19.14 ? 837  PHE   B N     1 
ATOM   15073 C  CA    . PHE   B  1  839  ? 21.152  27.928  92.167  1.00 19.94 ? 837  PHE   B CA    1 
ATOM   15074 C  C     . PHE   B  1  839  ? 20.496  26.994  91.174  1.00 22.53 ? 837  PHE   B C     1 
ATOM   15075 O  O     . PHE   B  1  839  ? 21.183  26.121  90.635  1.00 21.86 ? 837  PHE   B O     1 
ATOM   15076 C  CB    . PHE   B  1  839  ? 21.401  27.184  93.484  1.00 18.22 ? 837  PHE   B CB    1 
ATOM   15077 C  CG    . PHE   B  1  839  ? 22.120  28.012  94.509  1.00 19.04 ? 837  PHE   B CG    1 
ATOM   15078 C  CD1   . PHE   B  1  839  ? 23.385  28.527  94.243  1.00 17.17 ? 837  PHE   B CD1   1 
ATOM   15079 C  CD2   . PHE   B  1  839  ? 21.543  28.281  95.732  1.00 20.49 ? 837  PHE   B CD2   1 
ATOM   15080 C  CE1   . PHE   B  1  839  ? 24.053  29.293  95.182  1.00 18.41 ? 837  PHE   B CE1   1 
ATOM   15081 C  CE2   . PHE   B  1  839  ? 22.216  29.051  96.683  1.00 20.12 ? 837  PHE   B CE2   1 
ATOM   15082 C  CZ    . PHE   B  1  839  ? 23.472  29.545  96.405  1.00 21.19 ? 837  PHE   B CZ    1 
ATOM   15083 N  N     . ASP   B  1  840  ? 19.202  27.133  90.930  1.00 22.60 ? 838  ASP   B N     1 
ATOM   15084 C  CA    . ASP   B  1  840  ? 18.582  26.414  89.832  1.00 23.49 ? 838  ASP   B CA    1 
ATOM   15085 C  C     . ASP   B  1  840  ? 19.318  26.762  88.544  1.00 23.93 ? 838  ASP   B C     1 
ATOM   15086 O  O     . ASP   B  1  840  ? 19.766  27.899  88.352  1.00 21.34 ? 838  ASP   B O     1 
ATOM   15087 C  CB    . ASP   B  1  840  ? 17.111  26.821  89.759  1.00 30.50 ? 838  ASP   B CB    1 
ATOM   15088 C  CG    . ASP   B  1  840  ? 16.330  26.076  88.706  1.00 37.47 ? 838  ASP   B CG    1 
ATOM   15089 O  OD1   . ASP   B  1  840  ? 16.636  26.227  87.503  1.00 43.96 ? 838  ASP   B OD1   1 
ATOM   15090 O  OD2   . ASP   B  1  840  ? 15.388  25.348  89.082  1.00 44.33 ? 838  ASP   B OD2   1 
ATOM   15091 N  N     . SER   B  1  841  ? 19.490  25.765  87.681  1.00 21.41 ? 839  SER   B N     1 
ATOM   15092 C  CA    . SER   B  1  841  ? 20.278  25.905  86.458  1.00 20.56 ? 839  SER   B CA    1 
ATOM   15093 C  C     . SER   B  1  841  ? 21.705  26.315  86.754  1.00 17.77 ? 839  SER   B C     1 
ATOM   15094 O  O     . SER   B  1  841  ? 22.379  26.915  85.900  1.00 17.16 ? 839  SER   B O     1 
ATOM   15095 C  CB    . SER   B  1  841  ? 19.641  26.859  85.439  1.00 26.41 ? 839  SER   B CB    1 
ATOM   15096 O  OG    . SER   B  1  841  ? 18.354  26.394  85.092  1.00 27.67 ? 839  SER   B OG    1 
ATOM   15097 N  N     . ALA   B  1  842  ? 22.164  25.994  87.963  1.00 18.31 ? 840  ALA   B N     1 
ATOM   15098 C  CA    . ALA   B  1  842  ? 23.486  26.375  88.436  1.00 15.82 ? 840  ALA   B CA    1 
ATOM   15099 C  C     . ALA   B  1  842  ? 23.711  27.875  88.278  1.00 14.59 ? 840  ALA   B C     1 
ATOM   15100 O  O     . ALA   B  1  842  ? 24.811  28.326  87.965  1.00 16.49 ? 840  ALA   B O     1 
ATOM   15101 C  CB    . ALA   B  1  842  ? 24.591  25.553  87.772  1.00 16.78 ? 840  ALA   B CB    1 
ATOM   15102 N  N     . GLY   B  1  843  ? 22.649  28.645  88.503  1.00 15.31 ? 841  GLY   B N     1 
ATOM   15103 C  CA    . GLY   B  1  843  ? 22.740  30.095  88.433  1.00 16.35 ? 841  GLY   B CA    1 
ATOM   15104 C  C     . GLY   B  1  843  ? 22.950  30.633  87.039  1.00 14.79 ? 841  GLY   B C     1 
ATOM   15105 O  O     . GLY   B  1  843  ? 23.281  31.812  86.882  1.00 15.33 ? 841  GLY   B O     1 
ATOM   15106 N  N     . GLN   B  1  844  ? 22.750  29.804  86.024  1.00 14.26 ? 842  GLN   B N     1 
ATOM   15107 C  CA    . GLN   B  1  844  ? 22.973  30.206  84.636  1.00 14.70 ? 842  GLN   B CA    1 
ATOM   15108 C  C     . GLN   B  1  844  ? 21.696  30.725  83.988  1.00 15.81 ? 842  GLN   B C     1 
ATOM   15109 O  O     . GLN   B  1  844  ? 21.236  30.253  82.957  1.00 16.49 ? 842  GLN   B O     1 
ATOM   15110 C  CB    . GLN   B  1  844  ? 23.591  29.050  83.865  1.00 14.17 ? 842  GLN   B CB    1 
ATOM   15111 C  CG    . GLN   B  1  844  ? 24.951  28.738  84.437  1.00 14.28 ? 842  GLN   B CG    1 
ATOM   15112 C  CD    . GLN   B  1  844  ? 25.506  27.431  83.940  1.00 15.66 ? 842  GLN   B CD    1 
ATOM   15113 O  OE1   . GLN   B  1  844  ? 26.576  27.398  83.339  1.00 16.03 ? 842  GLN   B OE1   1 
ATOM   15114 N  NE2   . GLN   B  1  844  ? 24.804  26.336  84.231  1.00 16.72 ? 842  GLN   B NE2   1 
ATOM   15115 N  N     . ARG   B  1  845  ? 21.098  31.706  84.650  1.00 16.42 ? 843  ARG   B N     1 
ATOM   15116 C  CA    . ARG   B  1  845  ? 19.998  32.486  84.111  1.00 13.80 ? 843  ARG   B CA    1 
ATOM   15117 C  C     . ARG   B  1  845  ? 20.391  33.948  84.237  1.00 14.29 ? 843  ARG   B C     1 
ATOM   15118 O  O     . ARG   B  1  845  ? 20.965  34.365  85.246  1.00 14.41 ? 843  ARG   B O     1 
ATOM   15119 C  CB    . ARG   B  1  845  ? 18.740  32.290  84.933  1.00 15.99 ? 843  ARG   B CB    1 
ATOM   15120 C  CG    . ARG   B  1  845  ? 18.201  30.893  84.928  1.00 18.45 ? 843  ARG   B CG    1 
ATOM   15121 C  CD    . ARG   B  1  845  ? 16.836  30.974  85.574  1.00 23.56 ? 843  ARG   B CD    1 
ATOM   15122 N  NE    . ARG   B  1  845  ? 16.078  29.740  85.463  1.00 28.52 ? 843  ARG   B NE    1 
ATOM   15123 C  CZ    . ARG   B  1  845  ? 15.946  28.875  86.451  1.00 31.39 ? 843  ARG   B CZ    1 
ATOM   15124 N  NH1   . ARG   B  1  845  ? 16.529  29.077  87.622  1.00 33.13 ? 843  ARG   B NH1   1 
ATOM   15125 N  NH2   . ARG   B  1  845  ? 15.208  27.784  86.264  1.00 37.44 ? 843  ARG   B NH2   1 
ATOM   15126 N  N     . CYS   B  1  846  ? 20.071  34.741  83.225  1.00 14.72 ? 844  CYS   B N     1 
ATOM   15127 C  CA    . CYS   B  1  846  ? 20.352  36.165  83.343  1.00 16.03 ? 844  CYS   B CA    1 
ATOM   15128 C  C     . CYS   B  1  846  ? 19.615  36.764  84.525  1.00 13.53 ? 844  CYS   B C     1 
ATOM   15129 O  O     . CYS   B  1  846  ? 20.083  37.738  85.121  1.00 15.73 ? 844  CYS   B O     1 
ATOM   15130 C  CB    . CYS   B  1  846  ? 19.930  36.868  82.064  1.00 16.20 ? 844  CYS   B CB    1 
ATOM   15131 S  SG    . CYS   B  1  846  ? 18.274  36.504  81.546  1.00 17.20 ? 844  CYS   B SG    1 
ATOM   15132 N  N     . SER   B  1  847  ? 18.451  36.204  84.849  1.00 13.40 ? 845  SER   B N     1 
ATOM   15133 C  CA    . SER   B  1  847  ? 17.596  36.636  85.945  1.00 13.28 ? 845  SER   B CA    1 
ATOM   15134 C  C     . SER   B  1  847  ? 18.043  36.111  87.303  1.00 14.98 ? 845  SER   B C     1 
ATOM   15135 O  O     . SER   B  1  847  ? 17.420  36.460  88.312  1.00 14.28 ? 845  SER   B O     1 
ATOM   15136 C  CB    . SER   B  1  847  ? 16.202  36.092  85.669  1.00 14.33 ? 845  SER   B CB    1 
ATOM   15137 O  OG    . SER   B  1  847  ? 16.309  34.690  85.427  1.00 15.78 ? 845  SER   B OG    1 
ATOM   15138 N  N     . ALA   B  1  848  ? 19.101  35.305  87.357  1.00 14.30 ? 846  ALA   B N     1 
ATOM   15139 C  CA    . ALA   B  1  848  ? 19.453  34.604  88.586  1.00 14.72 ? 846  ALA   B CA    1 
ATOM   15140 C  C     . ALA   B  1  848  ? 19.786  35.577  89.703  1.00 15.19 ? 846  ALA   B C     1 
ATOM   15141 O  O     . ALA   B  1  848  ? 20.345  36.655  89.482  1.00 14.63 ? 846  ALA   B O     1 
ATOM   15142 C  CB    . ALA   B  1  848  ? 20.674  33.711  88.348  1.00 14.05 ? 846  ALA   B CB    1 
ATOM   15143 N  N     . LEU   B  1  849  ? 19.455  35.162  90.927  1.00 14.57 ? 847  LEU   B N     1 
ATOM   15144 C  CA    . LEU   B  1  849  ? 19.773  35.943  92.113  1.00 15.01 ? 847  LEU   B CA    1 
ATOM   15145 C  C     . LEU   B  1  849  ? 21.274  35.916  92.363  1.00 14.46 ? 847  LEU   B C     1 
ATOM   15146 O  O     . LEU   B  1  849  ? 21.857  34.844  92.549  1.00 16.45 ? 847  LEU   B O     1 
ATOM   15147 C  CB    . LEU   B  1  849  ? 19.028  35.354  93.302  1.00 15.82 ? 847  LEU   B CB    1 
ATOM   15148 C  CG    . LEU   B  1  849  ? 19.393  35.975  94.644  1.00 15.98 ? 847  LEU   B CG    1 
ATOM   15149 C  CD1   . LEU   B  1  849  ? 19.114  37.471  94.662  1.00 17.05 ? 847  LEU   B CD1   1 
ATOM   15150 C  CD2   . LEU   B  1  849  ? 18.633  35.257  95.759  1.00 16.17 ? 847  LEU   B CD2   1 
ATOM   15151 N  N     . ARG   B  1  850  ? 21.894  37.095  92.351  1.00 14.34 ? 848  ARG   B N     1 
ATOM   15152 C  CA    . ARG   B  1  850  ? 23.326  37.239  92.575  1.00 14.11 ? 848  ARG   B CA    1 
ATOM   15153 C  C     . ARG   B  1  850  ? 23.663  37.807  93.938  1.00 14.77 ? 848  ARG   B C     1 
ATOM   15154 O  O     . ARG   B  1  850  ? 24.721  37.498  94.476  1.00 15.78 ? 848  ARG   B O     1 
ATOM   15155 C  CB    . ARG   B  1  850  ? 23.944  38.163  91.516  1.00 16.29 ? 848  ARG   B CB    1 
ATOM   15156 C  CG    . ARG   B  1  850  ? 23.605  37.785  90.095  1.00 17.61 ? 848  ARG   B CG    1 
ATOM   15157 C  CD    . ARG   B  1  850  ? 23.991  36.359  89.825  1.00 17.81 ? 848  ARG   B CD    1 
ATOM   15158 N  NE    . ARG   B  1  850  ? 23.804  36.033  88.420  1.00 17.03 ? 848  ARG   B NE    1 
ATOM   15159 C  CZ    . ARG   B  1  850  ? 23.924  34.810  87.928  1.00 15.25 ? 848  ARG   B CZ    1 
ATOM   15160 N  NH1   . ARG   B  1  850  ? 24.202  33.783  88.710  1.00 16.32 ? 848  ARG   B NH1   1 
ATOM   15161 N  NH2   . ARG   B  1  850  ? 23.723  34.614  86.625  1.00 16.39 ? 848  ARG   B NH2   1 
ATOM   15162 N  N     . VAL   B  1  851  ? 22.803  38.643  94.504  1.00 15.54 ? 849  VAL   B N     1 
ATOM   15163 C  CA    . VAL   B  1  851  ? 23.101  39.320  95.765  1.00 15.14 ? 849  VAL   B CA    1 
ATOM   15164 C  C     . VAL   B  1  851  ? 21.874  39.211  96.650  1.00 16.12 ? 849  VAL   B C     1 
ATOM   15165 O  O     . VAL   B  1  851  ? 20.837  39.814  96.355  1.00 16.10 ? 849  VAL   B O     1 
ATOM   15166 C  CB    . VAL   B  1  851  ? 23.479  40.793  95.571  1.00 18.06 ? 849  VAL   B CB    1 
ATOM   15167 C  CG1   . VAL   B  1  851  ? 23.873  41.391  96.916  1.00 19.83 ? 849  VAL   B CG1   1 
ATOM   15168 C  CG2   . VAL   B  1  851  ? 24.614  40.950  94.571  1.00 20.14 ? 849  VAL   B CG2   1 
ATOM   15169 N  N     . LEU   B  1  852  ? 21.990  38.459  97.737  1.00 15.55 ? 850  LEU   B N     1 
ATOM   15170 C  CA    . LEU   B  1  852  ? 20.913  38.312  98.701  1.00 13.79 ? 850  LEU   B CA    1 
ATOM   15171 C  C     . LEU   B  1  852  ? 21.195  39.278  99.836  1.00 15.32 ? 850  LEU   B C     1 
ATOM   15172 O  O     . LEU   B  1  852  ? 22.227  39.162  100.496 1.00 16.04 ? 850  LEU   B O     1 
ATOM   15173 C  CB    . LEU   B  1  852  ? 20.883  36.881  99.229  1.00 14.75 ? 850  LEU   B CB    1 
ATOM   15174 C  CG    . LEU   B  1  852  ? 19.867  36.605  100.328 1.00 14.62 ? 850  LEU   B CG    1 
ATOM   15175 C  CD1   . LEU   B  1  852  ? 18.453  36.868  99.827  1.00 15.71 ? 850  LEU   B CD1   1 
ATOM   15176 C  CD2   . LEU   B  1  852  ? 19.991  35.168  100.789 1.00 16.43 ? 850  LEU   B CD2   1 
ATOM   15177 N  N     . CYS   B  1  853  ? 20.290  40.225  100.056 1.00 15.53 ? 851  CYS   B N     1 
ATOM   15178 C  CA    . CYS   B  1  853  ? 20.445  41.242  101.089 1.00 15.01 ? 851  CYS   B CA    1 
ATOM   15179 C  C     . CYS   B  1  853  ? 19.488  40.929  102.229 1.00 14.31 ? 851  CYS   B C     1 
ATOM   15180 O  O     . CYS   B  1  853  ? 18.266  41.004  102.064 1.00 15.91 ? 851  CYS   B O     1 
ATOM   15181 C  CB    . CYS   B  1  853  ? 20.150  42.623  100.525 1.00 16.20 ? 851  CYS   B CB    1 
ATOM   15182 S  SG    . CYS   B  1  853  ? 21.103  42.995  99.040  1.00 19.76 ? 851  CYS   B SG    1 
ATOM   15183 N  N     . LEU   B  1  854  ? 20.045  40.606  103.387 1.00 16.24 ? 852  LEU   B N     1 
ATOM   15184 C  CA    . LEU   B  1  854  ? 19.262  40.137  104.516 1.00 15.67 ? 852  LEU   B CA    1 
ATOM   15185 C  C     . LEU   B  1  854  ? 19.338  41.166  105.627 1.00 16.52 ? 852  LEU   B C     1 
ATOM   15186 O  O     . LEU   B  1  854  ? 20.432  41.564  106.025 1.00 17.81 ? 852  LEU   B O     1 
ATOM   15187 C  CB    . LEU   B  1  854  ? 19.856  38.836  105.048 1.00 16.74 ? 852  LEU   B CB    1 
ATOM   15188 C  CG    . LEU   B  1  854  ? 19.885  37.694  104.039 1.00 15.75 ? 852  LEU   B CG    1 
ATOM   15189 C  CD1   . LEU   B  1  854  ? 20.618  36.484  104.650 1.00 17.77 ? 852  LEU   B CD1   1 
ATOM   15190 C  CD2   . LEU   B  1  854  ? 18.478  37.335  103.614 1.00 18.40 ? 852  LEU   B CD2   1 
ATOM   15191 N  N     . GLN   B  1  855  ? 18.185  41.553  106.150 1.00 16.35 ? 853  GLN   B N     1 
ATOM   15192 C  CA    . GLN   B  1  855  ? 18.186  42.425  107.315 1.00 16.88 ? 853  GLN   B CA    1 
ATOM   15193 C  C     . GLN   B  1  855  ? 18.970  41.743  108.429 1.00 19.47 ? 853  GLN   B C     1 
ATOM   15194 O  O     . GLN   B  1  855  ? 18.861  40.530  108.627 1.00 17.49 ? 853  GLN   B O     1 
ATOM   15195 C  CB    . GLN   B  1  855  ? 16.756  42.701  107.770 1.00 15.29 ? 853  GLN   B CB    1 
ATOM   15196 C  CG    . GLN   B  1  855  ? 16.692  43.831  108.785 1.00 19.49 ? 853  GLN   B CG    1 
ATOM   15197 C  CD    . GLN   B  1  855  ? 15.285  44.161  109.216 1.00 24.38 ? 853  GLN   B CD    1 
ATOM   15198 O  OE1   . GLN   B  1  855  ? 14.355  44.155  108.410 1.00 26.11 ? 853  GLN   B OE1   1 
ATOM   15199 N  NE2   . GLN   B  1  855  ? 15.120  44.461  110.501 1.00 25.58 ? 853  GLN   B NE2   1 
ATOM   15200 N  N     . GLU   B  1  856  ? 19.797  42.525  109.130 1.00 19.48 ? 854  GLU   B N     1 
ATOM   15201 C  CA    . GLU   B  1  856  ? 20.810  41.938  110.009 1.00 18.64 ? 854  GLU   B CA    1 
ATOM   15202 C  C     . GLU   B  1  856  ? 20.201  41.036  111.078 1.00 21.45 ? 854  GLU   B C     1 
ATOM   15203 O  O     . GLU   B  1  856  ? 20.809  40.026  111.451 1.00 24.19 ? 854  GLU   B O     1 
ATOM   15204 C  CB    . GLU   B  1  856  ? 21.648  43.043  110.652 1.00 26.08 ? 854  GLU   B CB    1 
ATOM   15205 N  N     . ASP   B  1  857  ? 19.003  41.366  111.562 1.00 20.43 ? 855  ASP   B N     1 
ATOM   15206 C  CA    . ASP   B  1  857  ? 18.415  40.641  112.685 1.00 21.82 ? 855  ASP   B CA    1 
ATOM   15207 C  C     . ASP   B  1  857  ? 17.928  39.248  112.307 1.00 23.48 ? 855  ASP   B C     1 
ATOM   15208 O  O     . ASP   B  1  857  ? 17.728  38.415  113.196 1.00 26.12 ? 855  ASP   B O     1 
ATOM   15209 C  CB    . ASP   B  1  857  ? 17.255  41.441  113.278 1.00 26.42 ? 855  ASP   B CB    1 
ATOM   15210 N  N     . VAL   B  1  858  ? 17.702  38.982  111.023 1.00 19.26 ? 856  VAL   B N     1 
ATOM   15211 C  CA    . VAL   B  1  858  ? 17.254  37.672  110.577 1.00 18.23 ? 856  VAL   B CA    1 
ATOM   15212 C  C     . VAL   B  1  858  ? 18.284  36.969  109.730 1.00 16.60 ? 856  VAL   B C     1 
ATOM   15213 O  O     . VAL   B  1  858  ? 18.054  35.819  109.319 1.00 19.52 ? 856  VAL   B O     1 
ATOM   15214 C  CB    . VAL   B  1  858  ? 15.908  37.742  109.839 1.00 18.74 ? 856  VAL   B CB    1 
ATOM   15215 C  CG1   . VAL   B  1  858  ? 14.844  38.284  110.780 1.00 22.40 ? 856  VAL   B CG1   1 
ATOM   15216 C  CG2   . VAL   B  1  858  ? 16.051  38.600  108.594 1.00 20.25 ? 856  VAL   B CG2   1 
ATOM   15217 N  N     . ALA   B  1  859  ? 19.420  37.611  109.461 1.00 17.85 ? 857  ALA   B N     1 
ATOM   15218 C  CA    . ALA   B  1  859  ? 20.375  37.061  108.506 1.00 19.00 ? 857  ALA   B CA    1 
ATOM   15219 C  C     . ALA   B  1  859  ? 20.886  35.691  108.944 1.00 17.18 ? 857  ALA   B C     1 
ATOM   15220 O  O     . ALA   B  1  859  ? 20.901  34.746  108.149 1.00 19.28 ? 857  ALA   B O     1 
ATOM   15221 C  CB    . ALA   B  1  859  ? 21.518  38.046  108.290 1.00 18.75 ? 857  ALA   B CB    1 
ATOM   15222 N  N     . ASP   B  1  860  ? 21.305  35.563  110.208 1.00 18.26 ? 858  ASP   B N     1 
ATOM   15223 C  CA    . ASP   B  1  860  ? 21.877  34.300  110.672 1.00 20.60 ? 858  ASP   B CA    1 
ATOM   15224 C  C     . ASP   B  1  860  ? 20.887  33.152  110.547 1.00 19.80 ? 858  ASP   B C     1 
ATOM   15225 O  O     . ASP   B  1  860  ? 21.241  32.065  110.076 1.00 19.68 ? 858  ASP   B O     1 
ATOM   15226 C  CB    . ASP   B  1  860  ? 22.357  34.423  112.120 1.00 19.07 ? 858  ASP   B CB    1 
ATOM   15227 C  CG    . ASP   B  1  860  ? 23.571  35.314  112.264 1.00 30.64 ? 858  ASP   B CG    1 
ATOM   15228 O  OD1   . ASP   B  1  860  ? 24.370  35.391  111.311 1.00 30.45 ? 858  ASP   B OD1   1 
ATOM   15229 O  OD2   . ASP   B  1  860  ? 23.731  35.937  113.334 1.00 35.12 ? 858  ASP   B OD2   1 
ATOM   15230 N  N     . ARG   B  1  861  ? 19.636  33.365  110.976 1.00 19.60 ? 859  ARG   B N     1 
ATOM   15231 C  CA    . ARG   B  1  861  ? 18.659  32.286  110.903 1.00 18.98 ? 859  ARG   B CA    1 
ATOM   15232 C  C     . ARG   B  1  861  ? 18.353  31.905  109.459 1.00 19.82 ? 859  ARG   B C     1 
ATOM   15233 O  O     . ARG   B  1  861  ? 18.252  30.718  109.131 1.00 19.84 ? 859  ARG   B O     1 
ATOM   15234 C  CB    . ARG   B  1  861  ? 17.376  32.656  111.651 1.00 25.82 ? 859  ARG   B CB    1 
ATOM   15235 C  CG    . ARG   B  1  861  ? 16.304  31.593  111.504 1.00 34.41 ? 859  ARG   B CG    1 
ATOM   15236 C  CD    . ARG   B  1  861  ? 15.217  31.672  112.552 1.00 40.66 ? 859  ARG   B CD    1 
ATOM   15237 N  NE    . ARG   B  1  861  ? 14.158  30.717  112.240 1.00 45.18 ? 859  ARG   B NE    1 
ATOM   15238 C  CZ    . ARG   B  1  861  ? 13.118  30.991  111.464 1.00 40.06 ? 859  ARG   B CZ    1 
ATOM   15239 N  NH1   . ARG   B  1  861  ? 12.940  32.199  110.950 1.00 42.05 ? 859  ARG   B NH1   1 
ATOM   15240 N  NH2   . ARG   B  1  861  ? 12.238  30.029  111.194 1.00 40.97 ? 859  ARG   B NH2   1 
ATOM   15241 N  N     . ILE   B  1  862  ? 18.227  32.895  108.576 1.00 18.41 ? 860  ILE   B N     1 
ATOM   15242 C  CA    . ILE   B  1  862  ? 17.964  32.582  107.175 1.00 16.56 ? 860  ILE   B CA    1 
ATOM   15243 C  C     . ILE   B  1  862  ? 19.149  31.862  106.550 1.00 15.70 ? 860  ILE   B C     1 
ATOM   15244 O  O     . ILE   B  1  862  ? 18.974  30.885  105.810 1.00 17.70 ? 860  ILE   B O     1 
ATOM   15245 C  CB    . ILE   B  1  862  ? 17.590  33.857  106.410 1.00 16.96 ? 860  ILE   B CB    1 
ATOM   15246 C  CG1   . ILE   B  1  862  ? 16.205  34.321  106.867 1.00 22.53 ? 860  ILE   B CG1   1 
ATOM   15247 C  CG2   . ILE   B  1  862  ? 17.618  33.593  104.913 1.00 17.97 ? 860  ILE   B CG2   1 
ATOM   15248 C  CD1   . ILE   B  1  862  ? 15.823  35.713  106.384 1.00 24.73 ? 860  ILE   B CD1   1 
ATOM   15249 N  N     . LEU   B  1  863  ? 20.370  32.309  106.847 1.00 17.52 ? 861  LEU   B N     1 
ATOM   15250 C  CA    . LEU   B  1  863  ? 21.540  31.649  106.280 1.00 18.25 ? 861  LEU   B CA    1 
ATOM   15251 C  C     . LEU   B  1  863  ? 21.658  30.214  106.774 1.00 19.36 ? 861  LEU   B C     1 
ATOM   15252 O  O     . LEU   B  1  863  ? 22.022  29.315  106.007 1.00 17.38 ? 861  LEU   B O     1 
ATOM   15253 C  CB    . LEU   B  1  863  ? 22.807  32.431  106.611 1.00 19.19 ? 861  LEU   B CB    1 
ATOM   15254 C  CG    . LEU   B  1  863  ? 22.886  33.748  105.849 1.00 22.22 ? 861  LEU   B CG    1 
ATOM   15255 C  CD1   . LEU   B  1  863  ? 24.035  34.570  106.396 1.00 23.56 ? 861  LEU   B CD1   1 
ATOM   15256 C  CD2   . LEU   B  1  863  ? 23.045  33.479  104.351 1.00 24.13 ? 861  LEU   B CD2   1 
ATOM   15257 N  N     . THR   B  1  864  ? 21.369  29.980  108.053 1.00 17.28 ? 862  THR   B N     1 
ATOM   15258 C  CA    . THR   B  1  864  ? 21.408  28.611  108.555 1.00 17.20 ? 862  THR   B CA    1 
ATOM   15259 C  C     . THR   B  1  864  ? 20.413  27.737  107.812 1.00 19.64 ? 862  THR   B C     1 
ATOM   15260 O  O     . THR   B  1  864  ? 20.727  26.610  107.417 1.00 19.41 ? 862  THR   B O     1 
ATOM   15261 C  CB    . THR   B  1  864  ? 21.113  28.594  110.051 1.00 23.66 ? 862  THR   B CB    1 
ATOM   15262 O  OG1   . THR   B  1  864  ? 22.179  29.248  110.738 1.00 25.10 ? 862  THR   B OG1   1 
ATOM   15263 C  CG2   . THR   B  1  864  ? 20.984  27.161  110.554 1.00 25.55 ? 862  THR   B CG2   1 
ATOM   15264 N  N     . MET   B  1  865  ? 19.207  28.252  107.595 1.00 17.91 ? 863  MET   B N     1 
ATOM   15265 C  CA    . MET   B  1  865  ? 18.192  27.479  106.901 1.00 18.81 ? 863  MET   B CA    1 
ATOM   15266 C  C     . MET   B  1  865  ? 18.575  27.273  105.442 1.00 17.29 ? 863  MET   B C     1 
ATOM   15267 O  O     . MET   B  1  865  ? 18.433  26.174  104.899 1.00 17.38 ? 863  MET   B O     1 
ATOM   15268 C  CB    . MET   B  1  865  ? 16.862  28.213  107.009 1.00 18.58 ? 863  MET   B CB    1 
ATOM   15269 C  CG    . MET   B  1  865  ? 15.718  27.463  106.405 1.00 20.94 ? 863  MET   B CG    1 
ATOM   15270 S  SD    . MET   B  1  865  ? 14.164  28.336  106.595 1.00 22.59 ? 863  MET   B SD    1 
ATOM   15271 C  CE    . MET   B  1  865  ? 14.064  28.534  108.373 1.00 25.40 ? 863  MET   B CE    1 
ATOM   15272 N  N     . LEU   B  1  866  ? 19.084  28.321  104.805 1.00 16.84 ? 864  LEU   B N     1 
ATOM   15273 C  CA    . LEU   B  1  866  ? 19.541  28.203  103.427 1.00 16.41 ? 864  LEU   B CA    1 
ATOM   15274 C  C     . LEU   B  1  866  ? 20.609  27.130  103.293 1.00 18.11 ? 864  LEU   B C     1 
ATOM   15275 O  O     . LEU   B  1  866  ? 20.534  26.270  102.406 1.00 17.50 ? 864  LEU   B O     1 
ATOM   15276 C  CB    . LEU   B  1  866  ? 20.068  29.553  102.956 1.00 16.10 ? 864  LEU   B CB    1 
ATOM   15277 C  CG    . LEU   B  1  866  ? 20.683  29.535  101.557 1.00 16.90 ? 864  LEU   B CG    1 
ATOM   15278 C  CD1   . LEU   B  1  866  ? 19.631  29.090  100.538 1.00 17.31 ? 864  LEU   B CD1   1 
ATOM   15279 C  CD2   . LEU   B  1  866  ? 21.203  30.933  101.258 1.00 19.67 ? 864  LEU   B CD2   1 
ATOM   15280 N  N     . LYS   B  1  867  ? 21.610  27.155  104.181 1.00 17.63 ? 865  LYS   B N     1 
ATOM   15281 C  CA    . LYS   B  1  867  ? 22.676  26.166  104.098 1.00 18.10 ? 865  LYS   B CA    1 
ATOM   15282 C  C     . LYS   B  1  867  ? 22.142  24.763  104.346 1.00 16.97 ? 865  LYS   B C     1 
ATOM   15283 O  O     . LYS   B  1  867  ? 22.549  23.813  103.669 1.00 17.70 ? 865  LYS   B O     1 
ATOM   15284 C  CB    . LYS   B  1  867  ? 23.820  26.526  105.050 1.00 17.77 ? 865  LYS   B CB    1 
ATOM   15285 C  CG    . LYS   B  1  867  ? 24.556  27.771  104.573 1.00 22.62 ? 865  LYS   B CG    1 
ATOM   15286 C  CD    . LYS   B  1  867  ? 25.476  28.354  105.617 1.00 23.52 ? 865  LYS   B CD    1 
ATOM   15287 C  CE    . LYS   B  1  867  ? 26.002  29.707  105.153 1.00 30.36 ? 865  LYS   B CE    1 
ATOM   15288 N  NZ    . LYS   B  1  867  ? 26.799  30.391  106.212 1.00 34.61 ? 865  LYS   B NZ    1 
ATOM   15289 N  N     . GLY   B  1  868  ? 21.206  24.615  105.289 1.00 17.01 ? 866  GLY   B N     1 
ATOM   15290 C  CA    . GLY   B  1  868  ? 20.617  23.303  105.511 1.00 16.74 ? 866  GLY   B CA    1 
ATOM   15291 C  C     . GLY   B  1  868  ? 19.848  22.816  104.302 1.00 18.01 ? 866  GLY   B C     1 
ATOM   15292 O  O     . GLY   B  1  868  ? 19.905  21.632  103.945 1.00 19.22 ? 866  GLY   B O     1 
ATOM   15293 N  N     . ALA   B  1  869  ? 19.127  23.725  103.646 1.00 17.23 ? 867  ALA   B N     1 
ATOM   15294 C  CA    . ALA   B  1  869  ? 18.400  23.363  102.438 1.00 18.33 ? 867  ALA   B CA    1 
ATOM   15295 C  C     . ALA   B  1  869  ? 19.358  23.025  101.307 1.00 18.01 ? 867  ALA   B C     1 
ATOM   15296 O  O     . ALA   B  1  869  ? 19.113  22.082  100.547 1.00 17.30 ? 867  ALA   B O     1 
ATOM   15297 C  CB    . ALA   B  1  869  ? 17.464  24.501  102.039 1.00 18.69 ? 867  ALA   B CB    1 
ATOM   15298 N  N     . LEU   B  1  870  ? 20.470  23.766  101.199 1.00 17.10 ? 868  LEU   B N     1 
ATOM   15299 C  CA    . LEU   B  1  870  ? 21.442  23.471  100.144 1.00 18.58 ? 868  LEU   B CA    1 
ATOM   15300 C  C     . LEU   B  1  870  ? 22.044  22.085  100.306 1.00 16.63 ? 868  LEU   B C     1 
ATOM   15301 O  O     . LEU   B  1  870  ? 22.362  21.426  99.311  1.00 19.00 ? 868  LEU   B O     1 
ATOM   15302 C  CB    . LEU   B  1  870  ? 22.556  24.520  100.119 1.00 16.82 ? 868  LEU   B CB    1 
ATOM   15303 C  CG    . LEU   B  1  870  ? 22.138  25.857  99.512  1.00 21.25 ? 868  LEU   B CG    1 
ATOM   15304 C  CD1   . LEU   B  1  870  ? 23.240  26.879  99.656  1.00 23.38 ? 868  LEU   B CD1   1 
ATOM   15305 C  CD2   . LEU   B  1  870  ? 21.782  25.670  98.043  1.00 19.15 ? 868  LEU   B CD2   1 
ATOM   15306 N  N     . HIS   B  1  871  ? 22.193  21.624  101.544 1.00 16.08 ? 869  HIS   B N     1 
ATOM   15307 C  CA    A HIS   B  1  871  ? 22.762  20.302  101.764 0.52 19.37 ? 869  HIS   B CA    1 
ATOM   15308 C  CA    B HIS   B  1  871  ? 22.747  20.301  101.800 0.48 19.38 ? 869  HIS   B CA    1 
ATOM   15309 C  C     . HIS   B  1  871  ? 21.869  19.188  101.246 1.00 19.44 ? 869  HIS   B C     1 
ATOM   15310 O  O     . HIS   B  1  871  ? 22.341  18.055  101.094 1.00 21.46 ? 869  HIS   B O     1 
ATOM   15311 C  CB    A HIS   B  1  871  ? 23.091  20.092  103.246 0.52 19.79 ? 869  HIS   B CB    1 
ATOM   15312 C  CB    B HIS   B  1  871  ? 22.942  20.119  103.309 0.48 19.73 ? 869  HIS   B CB    1 
ATOM   15313 C  CG    A HIS   B  1  871  ? 24.417  20.656  103.654 0.52 21.88 ? 869  HIS   B CG    1 
ATOM   15314 C  CG    B HIS   B  1  871  ? 23.515  18.791  103.691 0.48 22.07 ? 869  HIS   B CG    1 
ATOM   15315 N  ND1   A HIS   B  1  871  ? 24.544  21.848  104.334 0.52 22.70 ? 869  HIS   B ND1   1 
ATOM   15316 N  ND1   B HIS   B  1  871  ? 24.868  18.528  103.666 0.48 25.23 ? 869  HIS   B ND1   1 
ATOM   15317 C  CD2   A HIS   B  1  871  ? 25.677  20.197  103.463 0.52 25.80 ? 869  HIS   B CD2   1 
ATOM   15318 C  CD2   B HIS   B  1  871  ? 22.916  17.645  104.094 0.48 25.77 ? 869  HIS   B CD2   1 
ATOM   15319 C  CE1   A HIS   B  1  871  ? 25.822  22.092  104.557 0.52 22.88 ? 869  HIS   B CE1   1 
ATOM   15320 C  CE1   B HIS   B  1  871  ? 25.079  17.281  104.044 0.48 23.58 ? 869  HIS   B CE1   1 
ATOM   15321 N  NE2   A HIS   B  1  871  ? 26.531  21.109  104.033 0.52 21.22 ? 869  HIS   B NE2   1 
ATOM   15322 N  NE2   B HIS   B  1  871  ? 23.911  16.721  104.305 0.48 26.23 ? 869  HIS   B NE2   1 
ATOM   15323 N  N     . GLU   B  1  872  ? 20.609  19.479  100.943 1.00 16.79 ? 870  GLU   B N     1 
ATOM   15324 C  CA    . GLU   B  1  872  ? 19.687  18.466  100.459 1.00 16.95 ? 870  GLU   B CA    1 
ATOM   15325 C  C     . GLU   B  1  872  ? 19.617  18.407  98.944  1.00 16.45 ? 870  GLU   B C     1 
ATOM   15326 O  O     . GLU   B  1  872  ? 18.869  17.584  98.403  1.00 18.67 ? 870  GLU   B O     1 
ATOM   15327 C  CB    . GLU   B  1  872  ? 18.291  18.717  101.040 1.00 18.93 ? 870  GLU   B CB    1 
ATOM   15328 C  CG    . GLU   B  1  872  ? 18.281  18.719  102.553 1.00 18.95 ? 870  GLU   B CG    1 
ATOM   15329 C  CD    . GLU   B  1  872  ? 18.677  17.378  103.129 1.00 20.53 ? 870  GLU   B CD    1 
ATOM   15330 O  OE1   . GLU   B  1  872  ? 18.472  16.351  102.442 1.00 24.11 ? 870  GLU   B OE1   1 
ATOM   15331 O  OE2   . GLU   B  1  872  ? 19.196  17.339  104.262 1.00 22.21 ? 870  GLU   B OE2   1 
ATOM   15332 N  N     . LEU   B  1  873  ? 20.362  19.259  98.247  1.00 17.46 ? 871  LEU   B N     1 
ATOM   15333 C  CA    . LEU   B  1  873  ? 20.291  19.283  96.793  1.00 17.05 ? 871  LEU   B CA    1 
ATOM   15334 C  C     . LEU   B  1  873  ? 21.192  18.213  96.199  1.00 18.22 ? 871  LEU   B C     1 
ATOM   15335 O  O     . LEU   B  1  873  ? 22.257  17.893  96.730  1.00 19.75 ? 871  LEU   B O     1 
ATOM   15336 C  CB    . LEU   B  1  873  ? 20.737  20.639  96.255  1.00 18.52 ? 871  LEU   B CB    1 
ATOM   15337 C  CG    . LEU   B  1  873  ? 19.888  21.842  96.649  1.00 22.88 ? 871  LEU   B CG    1 
ATOM   15338 C  CD1   . LEU   B  1  873  ? 20.374  23.053  95.880  1.00 21.63 ? 871  LEU   B CD1   1 
ATOM   15339 C  CD2   . LEU   B  1  873  ? 18.401  21.603  96.394  1.00 20.92 ? 871  LEU   B CD2   1 
ATOM   15340 N  N     . HIS   B  1  874  ? 20.770  17.687  95.063  1.00 19.41 ? 872  HIS   B N     1 
ATOM   15341 C  CA    . HIS   B  1  874  ? 21.530  16.693  94.326  1.00 18.97 ? 872  HIS   B CA    1 
ATOM   15342 C  C     . HIS   B  1  874  ? 22.125  17.389  93.106  1.00 16.44 ? 872  HIS   B C     1 
ATOM   15343 O  O     . HIS   B  1  874  ? 21.383  17.911  92.271  1.00 18.67 ? 872  HIS   B O     1 
ATOM   15344 C  CB    . HIS   B  1  874  ? 20.588  15.564  93.913  1.00 19.30 ? 872  HIS   B CB    1 
ATOM   15345 C  CG    . HIS   B  1  874  ? 21.250  14.458  93.164  1.00 21.53 ? 872  HIS   B CG    1 
ATOM   15346 N  ND1   . HIS   B  1  874  ? 20.563  13.340  92.742  1.00 26.42 ? 872  HIS   B ND1   1 
ATOM   15347 C  CD2   . HIS   B  1  874  ? 22.528  14.298  92.745  1.00 23.76 ? 872  HIS   B CD2   1 
ATOM   15348 C  CE1   . HIS   B  1  874  ? 21.390  12.536  92.098  1.00 27.54 ? 872  HIS   B CE1   1 
ATOM   15349 N  NE2   . HIS   B  1  874  ? 22.589  13.094  92.086  1.00 27.92 ? 872  HIS   B NE2   1 
ATOM   15350 N  N     . ILE   B  1  875  ? 23.452  17.429  93.033  1.00 16.83 ? 873  ILE   B N     1 
ATOM   15351 C  CA    . ILE   B  1  875  ? 24.178  18.029  91.917  1.00 17.90 ? 873  ILE   B CA    1 
ATOM   15352 C  C     . ILE   B  1  875  ? 24.670  16.895  91.035  1.00 18.50 ? 873  ILE   B C     1 
ATOM   15353 O  O     . ILE   B  1  875  ? 25.333  15.974  91.523  1.00 19.52 ? 873  ILE   B O     1 
ATOM   15354 C  CB    . ILE   B  1  875  ? 25.382  18.835  92.420  1.00 20.84 ? 873  ILE   B CB    1 
ATOM   15355 C  CG1   . ILE   B  1  875  ? 24.955  19.887  93.442  1.00 23.31 ? 873  ILE   B CG1   1 
ATOM   15356 C  CG2   . ILE   B  1  875  ? 26.128  19.462  91.235  1.00 19.94 ? 873  ILE   B CG2   1 
ATOM   15357 C  CD1   . ILE   B  1  875  ? 26.123  20.397  94.263  1.00 27.97 ? 873  ILE   B CD1   1 
ATOM   15358 N  N     . GLY   B  1  876  ? 24.367  16.952  89.745  1.00 16.68 ? 874  GLY   B N     1 
ATOM   15359 C  CA    . GLY   B  1  876  ? 24.889  15.916  88.877  1.00 17.62 ? 874  GLY   B CA    1 
ATOM   15360 C  C     . GLY   B  1  876  ? 24.386  16.041  87.457  1.00 15.92 ? 874  GLY   B C     1 
ATOM   15361 O  O     . GLY   B  1  876  ? 23.802  17.049  87.065  1.00 17.87 ? 874  GLY   B O     1 
ATOM   15362 N  N     . ARG   B  1  877  ? 24.670  14.999  86.680  1.00 19.95 ? 875  ARG   B N     1 
ATOM   15363 C  CA    . ARG   B  1  877  ? 24.183  14.948  85.314  1.00 18.46 ? 875  ARG   B CA    1 
ATOM   15364 C  C     . ARG   B  1  877  ? 22.663  14.926  85.342  1.00 19.84 ? 875  ARG   B C     1 
ATOM   15365 O  O     . ARG   B  1  877  ? 22.053  14.208  86.136  1.00 20.62 ? 875  ARG   B O     1 
ATOM   15366 C  CB    . ARG   B  1  877  ? 24.725  13.696  84.633  1.00 20.96 ? 875  ARG   B CB    1 
ATOM   15367 C  CG    . ARG   B  1  877  ? 24.646  13.761  83.125  1.00 22.98 ? 875  ARG   B CG    1 
ATOM   15368 C  CD    . ARG   B  1  877  ? 25.313  12.550  82.512  1.00 28.11 ? 875  ARG   B CD    1 
ATOM   15369 N  NE    . ARG   B  1  877  ? 24.443  11.387  82.477  1.00 26.04 ? 875  ARG   B NE    1 
ATOM   15370 C  CZ    . ARG   B  1  877  ? 24.754  10.249  81.872  1.00 32.98 ? 875  ARG   B CZ    1 
ATOM   15371 N  NH1   . ARG   B  1  877  ? 25.950  10.062  81.328  1.00 31.69 ? 875  ARG   B NH1   1 
ATOM   15372 N  NH2   . ARG   B  1  877  ? 23.844  9.280   81.804  1.00 32.92 ? 875  ARG   B NH2   1 
ATOM   15373 N  N     . THR   B  1  878  ? 22.045  15.720  84.467  1.00 16.79 ? 876  THR   B N     1 
ATOM   15374 C  CA    . THR   B  1  878  ? 20.647  16.099  84.638  1.00 18.75 ? 876  THR   B CA    1 
ATOM   15375 C  C     . THR   B  1  878  ? 19.653  15.110  84.039  1.00 16.62 ? 876  THR   B C     1 
ATOM   15376 O  O     . THR   B  1  878  ? 18.450  15.385  84.040  1.00 18.45 ? 876  THR   B O     1 
ATOM   15377 C  CB    . THR   B  1  878  ? 20.418  17.496  84.069  1.00 17.54 ? 876  THR   B CB    1 
ATOM   15378 O  OG1   . THR   B  1  878  ? 20.982  17.571  82.754  1.00 21.42 ? 876  THR   B OG1   1 
ATOM   15379 C  CG2   . THR   B  1  878  ? 21.077  18.536  84.956  1.00 19.70 ? 876  THR   B CG2   1 
ATOM   15380 N  N     . ASP   B  1  879  ? 20.107  13.954  83.568  1.00 18.34 ? 877  ASP   B N     1 
ATOM   15381 C  CA    . ASP   B  1  879  ? 19.201  12.964  83.002  1.00 18.66 ? 877  ASP   B CA    1 
ATOM   15382 C  C     . ASP   B  1  879  ? 18.593  12.056  84.067  1.00 20.09 ? 877  ASP   B C     1 
ATOM   15383 O  O     . ASP   B  1  879  ? 18.215  10.914  83.779  1.00 20.19 ? 877  ASP   B O     1 
ATOM   15384 C  CB    . ASP   B  1  879  ? 19.886  12.170  81.889  1.00 20.17 ? 877  ASP   B CB    1 
ATOM   15385 C  CG    . ASP   B  1  879  ? 21.048  11.329  82.393  1.00 23.87 ? 877  ASP   B CG    1 
ATOM   15386 O  OD1   . ASP   B  1  879  ? 21.714  11.726  83.373  1.00 25.71 ? 877  ASP   B OD1   1 
ATOM   15387 O  OD2   . ASP   B  1  879  ? 21.287  10.261  81.811  1.00 24.20 ? 877  ASP   B OD2   1 
ATOM   15388 N  N     . ARG   B  1  880  ? 18.508  12.548  85.300  1.00 20.29 ? 878  ARG   B N     1 
ATOM   15389 C  CA    . ARG   B  1  880  ? 17.834  11.876  86.401  1.00 20.16 ? 878  ARG   B CA    1 
ATOM   15390 C  C     . ARG   B  1  880  ? 16.889  12.889  87.019  1.00 18.76 ? 878  ARG   B C     1 
ATOM   15391 O  O     . ARG   B  1  880  ? 17.291  14.024  87.291  1.00 17.98 ? 878  ARG   B O     1 
ATOM   15392 C  CB    . ARG   B  1  880  ? 18.837  11.434  87.477  1.00 21.86 ? 878  ARG   B CB    1 
ATOM   15393 C  CG    . ARG   B  1  880  ? 19.621  10.170  87.182  1.00 28.68 ? 878  ARG   B CG    1 
ATOM   15394 C  CD    . ARG   B  1  880  ? 20.499  9.801   88.381  1.00 30.93 ? 878  ARG   B CD    1 
ATOM   15395 N  NE    . ARG   B  1  880  ? 21.509  8.813   88.024  1.00 45.28 ? 878  ARG   B NE    1 
ATOM   15396 C  CZ    . ARG   B  1  880  ? 21.403  7.512   88.255  1.00 49.00 ? 878  ARG   B CZ    1 
ATOM   15397 N  NH1   . ARG   B  1  880  ? 20.351  7.003   88.879  1.00 48.26 ? 878  ARG   B NH1   1 
ATOM   15398 N  NH2   . ARG   B  1  880  ? 22.375  6.700   87.848  1.00 48.65 ? 878  ARG   B NH2   1 
ATOM   15399 N  N     . LEU   B  1  881  ? 15.640  12.474  87.245  1.00 17.75 ? 879  LEU   B N     1 
ATOM   15400 C  CA    . LEU   B  1  881  ? 14.657  13.359  87.865  1.00 18.65 ? 879  LEU   B CA    1 
ATOM   15401 C  C     . LEU   B  1  881  ? 15.117  13.858  89.231  1.00 18.59 ? 879  LEU   B C     1 
ATOM   15402 O  O     . LEU   B  1  881  ? 14.794  14.989  89.622  1.00 19.12 ? 879  LEU   B O     1 
ATOM   15403 C  CB    . LEU   B  1  881  ? 13.320  12.628  87.972  1.00 18.71 ? 879  LEU   B CB    1 
ATOM   15404 C  CG    . LEU   B  1  881  ? 12.160  13.458  88.514  1.00 21.48 ? 879  LEU   B CG    1 
ATOM   15405 C  CD1   . LEU   B  1  881  ? 11.802  14.557  87.529  1.00 21.92 ? 879  LEU   B CD1   1 
ATOM   15406 C  CD2   . LEU   B  1  881  ? 10.991  12.542  88.778  1.00 20.18 ? 879  LEU   B CD2   1 
ATOM   15407 N  N     . SER   B  1  882  ? 15.894  13.049  89.955  1.00 16.78 ? 880  SER   B N     1 
ATOM   15408 C  CA    . SER   B  1  882  ? 16.352  13.423  91.289  1.00 18.09 ? 880  SER   B CA    1 
ATOM   15409 C  C     . SER   B  1  882  ? 17.427  14.506  91.281  1.00 20.03 ? 880  SER   B C     1 
ATOM   15410 O  O     . SER   B  1  882  ? 17.825  14.954  92.357  1.00 19.51 ? 880  SER   B O     1 
ATOM   15411 C  CB    . SER   B  1  882  ? 16.898  12.188  92.005  1.00 19.84 ? 880  SER   B CB    1 
ATOM   15412 O  OG    . SER   B  1  882  ? 18.094  11.753  91.373  1.00 22.80 ? 880  SER   B OG    1 
ATOM   15413 N  N     . VAL   B  1  883  ? 17.914  14.948  90.129  1.00 17.95 ? 881  VAL   B N     1 
ATOM   15414 C  CA    . VAL   B  1  883  ? 18.974  15.949  90.099  1.00 17.60 ? 881  VAL   B CA    1 
ATOM   15415 C  C     . VAL   B  1  883  ? 18.373  17.343  90.154  1.00 18.84 ? 881  VAL   B C     1 
ATOM   15416 O  O     . VAL   B  1  883  ? 17.451  17.669  89.396  1.00 21.36 ? 881  VAL   B O     1 
ATOM   15417 C  CB    . VAL   B  1  883  ? 19.877  15.774  88.870  1.00 18.47 ? 881  VAL   B CB    1 
ATOM   15418 C  CG1   . VAL   B  1  883  ? 20.808  16.971  88.729  1.00 19.70 ? 881  VAL   B CG1   1 
ATOM   15419 C  CG2   . VAL   B  1  883  ? 20.676  14.505  89.013  1.00 20.11 ? 881  VAL   B CG2   1 
ATOM   15420 N  N     . ASP   B  1  884  ? 18.884  18.156  91.067  1.00 18.02 ? 882  ASP   B N     1 
ATOM   15421 C  CA    . ASP   B  1  884  ? 18.416  19.510  91.305  1.00 18.45 ? 882  ASP   B CA    1 
ATOM   15422 C  C     . ASP   B  1  884  ? 19.261  20.559  90.605  1.00 20.78 ? 882  ASP   B C     1 
ATOM   15423 O  O     . ASP   B  1  884  ? 18.710  21.511  90.049  1.00 24.12 ? 882  ASP   B O     1 
ATOM   15424 C  CB    . ASP   B  1  884  ? 18.448  19.787  92.804  1.00 19.18 ? 882  ASP   B CB    1 
ATOM   15425 C  CG    . ASP   B  1  884  ? 17.590  18.817  93.577  1.00 19.28 ? 882  ASP   B CG    1 
ATOM   15426 O  OD1   . ASP   B  1  884  ? 16.378  18.719  93.251  1.00 20.99 ? 882  ASP   B OD1   1 
ATOM   15427 O  OD2   . ASP   B  1  884  ? 18.118  18.132  94.472  1.00 19.45 ? 882  ASP   B OD2   1 
ATOM   15428 N  N     . VAL   B  1  885  ? 20.582  20.408  90.640  1.00 18.77 ? 883  VAL   B N     1 
ATOM   15429 C  CA    . VAL   B  1  885  ? 21.530  21.372  90.088  1.00 18.23 ? 883  VAL   B CA    1 
ATOM   15430 C  C     . VAL   B  1  885  ? 22.393  20.633  89.078  1.00 16.49 ? 883  VAL   B C     1 
ATOM   15431 O  O     . VAL   B  1  885  ? 23.034  19.627  89.417  1.00 17.82 ? 883  VAL   B O     1 
ATOM   15432 C  CB    . VAL   B  1  885  ? 22.410  21.989  91.183  1.00 20.58 ? 883  VAL   B CB    1 
ATOM   15433 C  CG1   . VAL   B  1  885  ? 23.388  22.999  90.578  1.00 21.73 ? 883  VAL   B CG1   1 
ATOM   15434 C  CG2   . VAL   B  1  885  ? 21.545  22.645  92.249  1.00 24.10 ? 883  VAL   B CG2   1 
ATOM   15435 N  N     . GLY   B  1  886  ? 22.406  21.133  87.845  1.00 18.60 ? 884  GLY   B N     1 
ATOM   15436 C  CA    . GLY   B  1  886  ? 23.203  20.561  86.794  1.00 18.02 ? 884  GLY   B CA    1 
ATOM   15437 C  C     . GLY   B  1  886  ? 24.554  21.224  86.674  1.00 16.38 ? 884  GLY   B C     1 
ATOM   15438 O  O     . GLY   B  1  886  ? 24.989  21.985  87.539  1.00 16.69 ? 884  GLY   B O     1 
ATOM   15439 N  N     . PRO   B  1  887  ? 25.239  20.943  85.576  1.00 17.29 ? 885  PRO   B N     1 
ATOM   15440 C  CA    . PRO   B  1  887  ? 26.594  21.456  85.380  1.00 15.98 ? 885  PRO   B CA    1 
ATOM   15441 C  C     . PRO   B  1  887  ? 26.604  22.901  84.897  1.00 14.73 ? 885  PRO   B C     1 
ATOM   15442 O  O     . PRO   B  1  887  ? 25.612  23.441  84.417  1.00 15.75 ? 885  PRO   B O     1 
ATOM   15443 C  CB    . PRO   B  1  887  ? 27.125  20.545  84.272  1.00 15.54 ? 885  PRO   B CB    1 
ATOM   15444 C  CG    . PRO   B  1  887  ? 25.893  20.230  83.468  1.00 14.86 ? 885  PRO   B CG    1 
ATOM   15445 C  CD    . PRO   B  1  887  ? 24.813  20.044  84.493  1.00 16.17 ? 885  PRO   B CD    1 
ATOM   15446 N  N     . VAL   B  1  888  ? 27.779  23.507  84.998  1.00 16.06 ? 886  VAL   B N     1 
ATOM   15447 C  CA    . VAL   B  1  888  ? 28.044  24.716  84.232  1.00 16.09 ? 886  VAL   B CA    1 
ATOM   15448 C  C     . VAL   B  1  888  ? 28.405  24.325  82.802  1.00 15.52 ? 886  VAL   B C     1 
ATOM   15449 O  O     . VAL   B  1  888  ? 28.823  23.196  82.521  1.00 16.22 ? 886  VAL   B O     1 
ATOM   15450 C  CB    . VAL   B  1  888  ? 29.115  25.607  84.891  1.00 19.63 ? 886  VAL   B CB    1 
ATOM   15451 C  CG1   . VAL   B  1  888  ? 28.652  26.024  86.292  1.00 17.02 ? 886  VAL   B CG1   1 
ATOM   15452 C  CG2   . VAL   B  1  888  ? 30.457  24.917  84.959  1.00 23.30 ? 886  VAL   B CG2   1 
ATOM   15453 N  N     . ILE   B  1  889  ? 28.203  25.263  81.875  1.00 16.82 ? 887  ILE   B N     1 
ATOM   15454 C  CA    . ILE   B  1  889  ? 28.098  24.868  80.474  1.00 16.63 ? 887  ILE   B CA    1 
ATOM   15455 C  C     . ILE   B  1  889  ? 29.430  24.422  79.891  1.00 16.18 ? 887  ILE   B C     1 
ATOM   15456 O  O     . ILE   B  1  889  ? 29.460  23.539  79.025  1.00 16.26 ? 887  ILE   B O     1 
ATOM   15457 C  CB    . ILE   B  1  889  ? 27.454  25.993  79.654  1.00 16.40 ? 887  ILE   B CB    1 
ATOM   15458 C  CG1   . ILE   B  1  889  ? 27.213  25.545  78.204  1.00 16.76 ? 887  ILE   B CG1   1 
ATOM   15459 C  CG2   . ILE   B  1  889  ? 28.317  27.249  79.699  1.00 18.32 ? 887  ILE   B CG2   1 
ATOM   15460 C  CD1   . ILE   B  1  889  ? 26.269  24.374  78.045  1.00 18.10 ? 887  ILE   B CD1   1 
ATOM   15461 N  N     . THR   B  1  890  ? 30.543  25.022  80.317  1.00 15.71 ? 888  THR   B N     1 
ATOM   15462 C  CA    . THR   B  1  890  ? 31.841  24.708  79.732  1.00 17.16 ? 888  THR   B CA    1 
ATOM   15463 C  C     . THR   B  1  890  ? 32.913  24.795  80.800  1.00 17.13 ? 888  THR   B C     1 
ATOM   15464 O  O     . THR   B  1  890  ? 32.715  25.394  81.861  1.00 16.77 ? 888  THR   B O     1 
ATOM   15465 C  CB    . THR   B  1  890  ? 32.248  25.711  78.643  1.00 19.67 ? 888  THR   B CB    1 
ATOM   15466 O  OG1   . THR   B  1  890  ? 32.261  27.036  79.190  1.00 18.80 ? 888  THR   B OG1   1 
ATOM   15467 C  CG2   . THR   B  1  890  ? 31.313  25.659  77.433  1.00 20.24 ? 888  THR   B CG2   1 
ATOM   15468 N  N     . SER   B  1  891  ? 34.077  24.217  80.484  1.00 19.36 ? 889  SER   B N     1 
ATOM   15469 C  CA    A SER   B  1  891  ? 35.240  24.365  81.355  0.47 19.04 ? 889  SER   B CA    1 
ATOM   15470 C  CA    B SER   B  1  891  ? 35.218  24.369  81.379  0.53 19.03 ? 889  SER   B CA    1 
ATOM   15471 C  C     . SER   B  1  891  ? 35.642  25.826  81.475  1.00 16.87 ? 889  SER   B C     1 
ATOM   15472 O  O     . SER   B  1  891  ? 36.074  26.272  82.542  1.00 18.86 ? 889  SER   B O     1 
ATOM   15473 C  CB    A SER   B  1  891  ? 36.415  23.545  80.818  0.47 22.34 ? 889  SER   B CB    1 
ATOM   15474 C  CB    B SER   B  1  891  ? 36.382  23.486  80.924  0.53 22.36 ? 889  SER   B CB    1 
ATOM   15475 O  OG    A SER   B  1  891  ? 36.130  22.161  80.835  0.47 24.13 ? 889  SER   B OG    1 
ATOM   15476 O  OG    B SER   B  1  891  ? 36.795  23.831  79.618  0.53 23.79 ? 889  SER   B OG    1 
ATOM   15477 N  N     . GLU   B  1  892  ? 35.512  26.582  80.380  1.00 16.64 ? 890  GLU   B N     1 
ATOM   15478 C  CA    . GLU   B  1  892  ? 35.843  28.001  80.409  1.00 19.37 ? 890  GLU   B CA    1 
ATOM   15479 C  C     . GLU   B  1  892  ? 34.946  28.737  81.387  1.00 18.09 ? 890  GLU   B C     1 
ATOM   15480 O  O     . GLU   B  1  892  ? 35.416  29.559  82.184  1.00 20.44 ? 890  GLU   B O     1 
ATOM   15481 C  CB    . GLU   B  1  892  ? 35.702  28.608  79.011  1.00 23.48 ? 890  GLU   B CB    1 
ATOM   15482 N  N     . ALA   B  1  893  ? 33.640  28.458  81.335  1.00 17.22 ? 891  ALA   B N     1 
ATOM   15483 C  CA    . ALA   B  1  893  ? 32.719  29.073  82.278  1.00 17.68 ? 891  ALA   B CA    1 
ATOM   15484 C  C     . ALA   B  1  893  ? 33.082  28.681  83.699  1.00 18.60 ? 891  ALA   B C     1 
ATOM   15485 O  O     . ALA   B  1  893  ? 33.122  29.524  84.599  1.00 18.95 ? 891  ALA   B O     1 
ATOM   15486 C  CB    . ALA   B  1  893  ? 31.285  28.646  81.954  1.00 18.46 ? 891  ALA   B CB    1 
ATOM   15487 N  N     . LYS   B  1  894  ? 33.359  27.400  83.911  1.00 17.45 ? 892  LYS   B N     1 
ATOM   15488 C  CA    . LYS   B  1  894  ? 33.744  26.942  85.237  1.00 17.70 ? 892  LYS   B CA    1 
ATOM   15489 C  C     . LYS   B  1  894  ? 34.977  27.686  85.739  1.00 19.12 ? 892  LYS   B C     1 
ATOM   15490 O  O     . LYS   B  1  894  ? 35.013  28.146  86.884  1.00 18.69 ? 892  LYS   B O     1 
ATOM   15491 C  CB    . LYS   B  1  894  ? 33.984  25.438  85.209  1.00 18.34 ? 892  LYS   B CB    1 
ATOM   15492 C  CG    . LYS   B  1  894  ? 34.428  24.867  86.530  1.00 18.84 ? 892  LYS   B CG    1 
ATOM   15493 C  CD    . LYS   B  1  894  ? 34.625  23.365  86.419  1.00 22.60 ? 892  LYS   B CD    1 
ATOM   15494 C  CE    . LYS   B  1  894  ? 35.495  22.877  87.560  1.00 28.65 ? 892  LYS   B CE    1 
ATOM   15495 N  NZ    . LYS   B  1  894  ? 34.812  21.904  88.439  1.00 33.98 ? 892  LYS   B NZ    1 
ATOM   15496 N  N     . ASP   B  1  895  ? 36.000  27.823  84.889  1.00 17.82 ? 893  ASP   B N     1 
ATOM   15497 C  CA    . ASP   B  1  895  ? 37.203  28.531  85.313  1.00 20.03 ? 893  ASP   B CA    1 
ATOM   15498 C  C     . ASP   B  1  895  ? 36.900  29.992  85.642  1.00 18.36 ? 893  ASP   B C     1 
ATOM   15499 O  O     . ASP   B  1  895  ? 37.480  30.558  86.574  1.00 20.13 ? 893  ASP   B O     1 
ATOM   15500 C  CB    . ASP   B  1  895  ? 38.274  28.449  84.224  1.00 22.30 ? 893  ASP   B CB    1 
ATOM   15501 C  CG    . ASP   B  1  895  ? 38.807  27.041  84.021  1.00 25.58 ? 893  ASP   B CG    1 
ATOM   15502 O  OD1   . ASP   B  1  895  ? 38.668  26.196  84.928  1.00 27.75 ? 893  ASP   B OD1   1 
ATOM   15503 O  OD2   . ASP   B  1  895  ? 39.387  26.787  82.944  1.00 30.92 ? 893  ASP   B OD2   1 
ATOM   15504 N  N     . ASN   B  1  896  ? 36.019  30.618  84.863  1.00 18.76 ? 894  ASN   B N     1 
ATOM   15505 C  CA    . ASN   B  1  896  ? 35.662  32.013  85.088  1.00 18.30 ? 894  ASN   B CA    1 
ATOM   15506 C  C     . ASN   B  1  896  ? 34.980  32.172  86.447  1.00 21.24 ? 894  ASN   B C     1 
ATOM   15507 O  O     . ASN   B  1  896  ? 35.334  33.053  87.247  1.00 19.84 ? 894  ASN   B O     1 
ATOM   15508 C  CB    . ASN   B  1  896  ? 34.743  32.433  83.939  1.00 20.52 ? 894  ASN   B CB    1 
ATOM   15509 C  CG    . ASN   B  1  896  ? 34.278  33.868  84.032  1.00 28.26 ? 894  ASN   B CG    1 
ATOM   15510 O  OD1   . ASN   B  1  896  ? 33.587  34.256  84.971  1.00 31.35 ? 894  ASN   B OD1   1 
ATOM   15511 N  ND2   . ASN   B  1  896  ? 34.603  34.653  83.011  1.00 34.45 ? 894  ASN   B ND2   1 
ATOM   15512 N  N     . ILE   B  1  897  ? 34.020  31.298  86.732  1.00 17.13 ? 895  ILE   B N     1 
ATOM   15513 C  CA    . ILE   B  1  897  ? 33.336  31.320  88.018  1.00 17.44 ? 895  ILE   B CA    1 
ATOM   15514 C  C     . ILE   B  1  897  ? 34.327  31.065  89.143  1.00 17.30 ? 895  ILE   B C     1 
ATOM   15515 O  O     . ILE   B  1  897  ? 34.326  31.757  90.167  1.00 18.09 ? 895  ILE   B O     1 
ATOM   15516 C  CB    . ILE   B  1  897  ? 32.209  30.277  88.025  1.00 17.80 ? 895  ILE   B CB    1 
ATOM   15517 C  CG1   . ILE   B  1  897  ? 31.149  30.625  86.981  1.00 17.78 ? 895  ILE   B CG1   1 
ATOM   15518 C  CG2   . ILE   B  1  897  ? 31.594  30.185  89.419  1.00 17.86 ? 895  ILE   B CG2   1 
ATOM   15519 C  CD1   . ILE   B  1  897  ? 30.388  29.414  86.503  1.00 16.14 ? 895  ILE   B CD1   1 
ATOM   15520 N  N     . GLU   B  1  898  ? 35.186  30.059  88.972  1.00 18.44 ? 896  GLU   B N     1 
ATOM   15521 C  CA    . GLU   B  1  898  ? 36.128  29.727  90.034  1.00 16.85 ? 896  GLU   B CA    1 
ATOM   15522 C  C     . GLU   B  1  898  ? 37.147  30.830  90.255  1.00 19.48 ? 896  GLU   B C     1 
ATOM   15523 O  O     . GLU   B  1  898  ? 37.589  31.036  91.390  1.00 20.13 ? 896  GLU   B O     1 
ATOM   15524 C  CB    . GLU   B  1  898  ? 36.771  28.366  89.781  1.00 22.94 ? 896  GLU   B CB    1 
ATOM   15525 C  CG    . GLU   B  1  898  ? 35.748  27.263  90.001  1.00 23.95 ? 896  GLU   B CG    1 
ATOM   15526 C  CD    . GLU   B  1  898  ? 36.269  25.875  89.700  1.00 33.06 ? 896  GLU   B CD    1 
ATOM   15527 O  OE1   . GLU   B  1  898  ? 37.340  25.753  89.071  1.00 32.58 ? 896  GLU   B OE1   1 
ATOM   15528 O  OE2   . GLU   B  1  898  ? 35.589  24.904  90.100  1.00 36.14 ? 896  GLU   B OE2   1 
ATOM   15529 N  N     . LYS   B  1  899  ? 37.516  31.560  89.199  1.00 17.48 ? 897  LYS   B N     1 
ATOM   15530 C  CA    . LYS   B  1  899  ? 38.432  32.678  89.381  1.00 19.57 ? 897  LYS   B CA    1 
ATOM   15531 C  C     . LYS   B  1  899  ? 37.820  33.731  90.292  1.00 18.26 ? 897  LYS   B C     1 
ATOM   15532 O  O     . LYS   B  1  899  ? 38.509  34.305  91.146  1.00 19.57 ? 897  LYS   B O     1 
ATOM   15533 C  CB    . LYS   B  1  899  ? 38.788  33.299  88.033  1.00 22.03 ? 897  LYS   B CB    1 
ATOM   15534 C  CG    . LYS   B  1  899  ? 39.658  34.531  88.195  1.00 24.48 ? 897  LYS   B CG    1 
ATOM   15535 C  CD    . LYS   B  1  899  ? 40.321  34.956  86.898  1.00 29.80 ? 897  LYS   B CD    1 
ATOM   15536 C  CE    . LYS   B  1  899  ? 39.364  35.714  86.011  1.00 30.91 ? 897  LYS   B CE    1 
ATOM   15537 N  NZ    . LYS   B  1  899  ? 40.093  36.561  85.012  1.00 34.04 ? 897  LYS   B NZ    1 
ATOM   15538 N  N     . HIS   B  1  900  ? 36.521  33.976  90.141  1.00 17.00 ? 898  HIS   B N     1 
ATOM   15539 C  CA    . HIS   B  1  900  ? 35.849  34.938  91.000  1.00 17.82 ? 898  HIS   B CA    1 
ATOM   15540 C  C     . HIS   B  1  900  ? 35.796  34.433  92.435  1.00 19.06 ? 898  HIS   B C     1 
ATOM   15541 O  O     . HIS   B  1  900  ? 36.049  35.188  93.383  1.00 18.95 ? 898  HIS   B O     1 
ATOM   15542 C  CB    . HIS   B  1  900  ? 34.435  35.173  90.493  1.00 16.89 ? 898  HIS   B CB    1 
ATOM   15543 C  CG    . HIS   B  1  900  ? 33.579  35.894  91.476  1.00 17.64 ? 898  HIS   B CG    1 
ATOM   15544 N  ND1   . HIS   B  1  900  ? 33.724  37.238  91.732  1.00 21.53 ? 898  HIS   B ND1   1 
ATOM   15545 C  CD2   . HIS   B  1  900  ? 32.582  35.457  92.282  1.00 17.77 ? 898  HIS   B CD2   1 
ATOM   15546 C  CE1   . HIS   B  1  900  ? 32.834  37.606  92.637  1.00 20.06 ? 898  HIS   B CE1   1 
ATOM   15547 N  NE2   . HIS   B  1  900  ? 32.136  36.544  92.992  1.00 19.56 ? 898  HIS   B NE2   1 
ATOM   15548 N  N     . ILE   B  1  901  ? 35.449  33.160  92.611  1.00 18.30 ? 899  ILE   B N     1 
ATOM   15549 C  CA    . ILE   B  1  901  ? 35.362  32.592  93.949  1.00 16.45 ? 899  ILE   B CA    1 
ATOM   15550 C  C     . ILE   B  1  901  ? 36.711  32.687  94.638  1.00 19.49 ? 899  ILE   B C     1 
ATOM   15551 O  O     . ILE   B  1  901  ? 36.813  33.120  95.793  1.00 21.50 ? 899  ILE   B O     1 
ATOM   15552 C  CB    . ILE   B  1  901  ? 34.859  31.143  93.866  1.00 15.84 ? 899  ILE   B CB    1 
ATOM   15553 C  CG1   . ILE   B  1  901  ? 33.422  31.124  93.336  1.00 16.42 ? 899  ILE   B CG1   1 
ATOM   15554 C  CG2   . ILE   B  1  901  ? 34.940  30.465  95.219  1.00 20.23 ? 899  ILE   B CG2   1 
ATOM   15555 C  CD1   . ILE   B  1  901  ? 32.940  29.709  93.017  1.00 19.72 ? 899  ILE   B CD1   1 
ATOM   15556 N  N     . GLU   B  1  902  ? 37.774  32.324  93.917  1.00 19.50 ? 900  GLU   B N     1 
ATOM   15557 C  CA    . GLU   B  1  902  ? 39.107  32.373  94.502  1.00 21.25 ? 900  GLU   B CA    1 
ATOM   15558 C  C     . GLU   B  1  902  ? 39.554  33.804  94.763  1.00 20.94 ? 900  GLU   B C     1 
ATOM   15559 O  O     . GLU   B  1  902  ? 40.309  34.049  95.711  1.00 23.45 ? 900  GLU   B O     1 
ATOM   15560 C  CB    . GLU   B  1  902  ? 40.108  31.631  93.612  1.00 22.25 ? 900  GLU   B CB    1 
ATOM   15561 C  CG    . GLU   B  1  902  ? 39.887  30.118  93.594  1.00 30.40 ? 900  GLU   B CG    1 
ATOM   15562 C  CD    . GLU   B  1  902  ? 39.661  29.526  94.991  1.00 36.98 ? 900  GLU   B CD    1 
ATOM   15563 O  OE1   . GLU   B  1  902  ? 40.499  29.761  95.888  1.00 35.67 ? 900  GLU   B OE1   1 
ATOM   15564 O  OE2   . GLU   B  1  902  ? 38.637  28.833  95.191  1.00 35.49 ? 900  GLU   B OE2   1 
ATOM   15565 N  N     . ARG   B  1  903  ? 39.106  34.757  93.946  1.00 20.82 ? 901  ARG   B N     1 
ATOM   15566 C  CA    . ARG   B  1  903  ? 39.433  36.152  94.213  1.00 22.98 ? 901  ARG   B CA    1 
ATOM   15567 C  C     . ARG   B  1  903  ? 38.775  36.616  95.502  1.00 26.47 ? 901  ARG   B C     1 
ATOM   15568 O  O     . ARG   B  1  903  ? 39.406  37.284  96.331  1.00 25.94 ? 901  ARG   B O     1 
ATOM   15569 C  CB    . ARG   B  1  903  ? 38.993  37.038  93.051  1.00 25.03 ? 901  ARG   B CB    1 
ATOM   15570 C  CG    . ARG   B  1  903  ? 39.520  38.459  93.161  1.00 34.32 ? 901  ARG   B CG    1 
ATOM   15571 C  CD    . ARG   B  1  903  ? 39.060  39.324  92.001  1.00 38.14 ? 901  ARG   B CD    1 
ATOM   15572 N  NE    . ARG   B  1  903  ? 37.857  40.078  92.332  1.00 43.05 ? 901  ARG   B NE    1 
ATOM   15573 C  CZ    . ARG   B  1  903  ? 37.863  41.296  92.857  1.00 39.46 ? 901  ARG   B CZ    1 
ATOM   15574 N  NH1   . ARG   B  1  903  ? 38.995  41.930  93.119  1.00 44.63 ? 901  ARG   B NH1   1 
ATOM   15575 N  NH2   . ARG   B  1  903  ? 36.705  41.895  93.118  1.00 48.46 ? 901  ARG   B NH2   1 
ATOM   15576 N  N     . MET   B  1  904  ? 37.500  36.277  95.682  1.00 22.44 ? 902  MET   B N     1 
ATOM   15577 C  CA    . MET   B  1  904  ? 36.816  36.623  96.923  1.00 21.98 ? 902  MET   B CA    1 
ATOM   15578 C  C     . MET   B  1  904  ? 37.477  35.950  98.115  1.00 23.09 ? 902  MET   B C     1 
ATOM   15579 O  O     . MET   B  1  904  ? 37.654  36.570  99.170  1.00 24.44 ? 902  MET   B O     1 
ATOM   15580 C  CB    . MET   B  1  904  ? 35.351  36.215  96.833  1.00 21.53 ? 902  MET   B CB    1 
ATOM   15581 C  CG    . MET   B  1  904  ? 34.610  36.890  95.700  1.00 21.06 ? 902  MET   B CG    1 
ATOM   15582 S  SD    . MET   B  1  904  ? 34.474  38.660  96.032  1.00 31.67 ? 902  MET   B SD    1 
ATOM   15583 C  CE    . MET   B  1  904  ? 35.636  39.319  94.850  1.00 33.13 ? 902  MET   B CE    1 
ATOM   15584 N  N     . ARG   B  1  905  ? 37.841  34.675  97.966  1.00 22.59 ? 903  ARG   B N     1 
ATOM   15585 C  CA    . ARG   B  1  905  ? 38.503  33.969  99.055  1.00 26.30 ? 903  ARG   B CA    1 
ATOM   15586 C  C     . ARG   B  1  905  ? 39.832  34.630  99.394  1.00 26.53 ? 903  ARG   B C     1 
ATOM   15587 O  O     . ARG   B  1  905  ? 40.156  34.829  100.572 1.00 25.64 ? 903  ARG   B O     1 
ATOM   15588 C  CB    . ARG   B  1  905  ? 38.711  32.504  98.662  1.00 26.29 ? 903  ARG   B CB    1 
ATOM   15589 C  CG    . ARG   B  1  905  ? 38.873  31.561  99.832  1.00 35.60 ? 903  ARG   B CG    1 
ATOM   15590 C  CD    . ARG   B  1  905  ? 39.342  30.193  99.362  1.00 34.68 ? 903  ARG   B CD    1 
ATOM   15591 N  NE    . ARG   B  1  905  ? 38.443  29.594  98.380  1.00 33.59 ? 903  ARG   B NE    1 
ATOM   15592 C  CZ    . ARG   B  1  905  ? 37.352  28.898  98.679  1.00 32.05 ? 903  ARG   B CZ    1 
ATOM   15593 N  NH1   . ARG   B  1  905  ? 36.937  28.764  99.927  1.00 33.31 ? 903  ARG   B NH1   1 
ATOM   15594 N  NH2   . ARG   B  1  905  ? 36.666  28.314  97.700  1.00 34.87 ? 903  ARG   B NH2   1 
ATOM   15595 N  N     . GLY   B  1  906  ? 40.597  35.016  98.371  1.00 25.18 ? 904  GLY   B N     1 
ATOM   15596 C  CA    . GLY   B  1  906  ? 41.888  35.636  98.621  1.00 27.91 ? 904  GLY   B CA    1 
ATOM   15597 C  C     . GLY   B  1  906  ? 41.775  37.007  99.252  1.00 29.09 ? 904  GLY   B C     1 
ATOM   15598 O  O     . GLY   B  1  906  ? 42.695  37.449  99.948  1.00 34.56 ? 904  GLY   B O     1 
ATOM   15599 N  N     . LEU   B  1  907  ? 40.662  37.698  99.020  1.00 29.96 ? 905  LEU   B N     1 
ATOM   15600 C  CA    . LEU   B  1  907  ? 40.389  38.974  99.667  1.00 30.46 ? 905  LEU   B CA    1 
ATOM   15601 C  C     . LEU   B  1  907  ? 39.905  38.822  101.103 1.00 28.29 ? 905  LEU   B C     1 
ATOM   15602 O  O     . LEU   B  1  907  ? 39.682  39.837  101.771 1.00 29.11 ? 905  LEU   B O     1 
ATOM   15603 C  CB    . LEU   B  1  907  ? 39.372  39.778  98.861  1.00 32.97 ? 905  LEU   B CB    1 
ATOM   15604 C  CG    . LEU   B  1  907  ? 39.877  40.289  97.511  1.00 38.33 ? 905  LEU   B CG    1 
ATOM   15605 C  CD1   . LEU   B  1  907  ? 38.804  41.110  96.824  1.00 42.12 ? 905  LEU   B CD1   1 
ATOM   15606 C  CD2   . LEU   B  1  907  ? 41.161  41.094  97.676  1.00 39.52 ? 905  LEU   B CD2   1 
ATOM   15607 N  N     . GLY   B  1  908  ? 39.754  37.595  101.594 1.00 26.85 ? 906  GLY   B N     1 
ATOM   15608 C  CA    . GLY   B  1  908  ? 39.332  37.364  102.956 1.00 28.72 ? 906  GLY   B CA    1 
ATOM   15609 C  C     . GLY   B  1  908  ? 37.840  37.238  103.159 1.00 30.92 ? 906  GLY   B C     1 
ATOM   15610 O  O     . GLY   B  1  908  ? 37.401  37.085  104.306 1.00 27.46 ? 906  GLY   B O     1 
ATOM   15611 N  N     . ARG   B  1  909  ? 37.046  37.297  102.093 1.00 23.83 ? 907  ARG   B N     1 
ATOM   15612 C  CA    . ARG   B  1  909  ? 35.611  37.130  102.231 1.00 22.58 ? 907  ARG   B CA    1 
ATOM   15613 C  C     . ARG   B  1  909  ? 35.290  35.696  102.632 1.00 24.54 ? 907  ARG   B C     1 
ATOM   15614 O  O     . ARG   B  1  909  ? 35.959  34.743  102.217 1.00 27.94 ? 907  ARG   B O     1 
ATOM   15615 C  CB    . ARG   B  1  909  ? 34.911  37.431  100.906 1.00 23.29 ? 907  ARG   B CB    1 
ATOM   15616 C  CG    . ARG   B  1  909  ? 35.168  38.824  100.337 1.00 27.15 ? 907  ARG   B CG    1 
ATOM   15617 C  CD    . ARG   B  1  909  ? 34.561  39.917  101.209 1.00 37.07 ? 907  ARG   B CD    1 
ATOM   15618 N  NE    . ARG   B  1  909  ? 34.787  41.243  100.643 1.00 43.29 ? 907  ARG   B NE    1 
ATOM   15619 C  CZ    . ARG   B  1  909  ? 35.735  42.080  101.044 1.00 45.37 ? 907  ARG   B CZ    1 
ATOM   15620 N  NH1   . ARG   B  1  909  ? 36.548  41.776  102.044 1.00 44.00 ? 907  ARG   B NH1   1 
ATOM   15621 N  NH2   . ARG   B  1  909  ? 35.867  43.253  100.429 1.00 48.38 ? 907  ARG   B NH2   1 
ATOM   15622 N  N     . LYS   B  1  910  ? 34.243  35.544  103.433 1.00 23.18 ? 908  LYS   B N     1 
ATOM   15623 C  CA    . LYS   B  1  910  ? 33.795  34.215  103.813 1.00 24.18 ? 908  LYS   B CA    1 
ATOM   15624 C  C     . LYS   B  1  910  ? 33.158  33.534  102.606 1.00 24.93 ? 908  LYS   B C     1 
ATOM   15625 O  O     . LYS   B  1  910  ? 32.210  34.059  102.012 1.00 22.25 ? 908  LYS   B O     1 
ATOM   15626 C  CB    . LYS   B  1  910  ? 32.784  34.302  104.952 1.00 26.64 ? 908  LYS   B CB    1 
ATOM   15627 C  CG    . LYS   B  1  910  ? 32.404  32.936  105.500 1.00 30.01 ? 908  LYS   B CG    1 
ATOM   15628 C  CD    . LYS   B  1  910  ? 31.293  33.021  106.527 1.00 39.11 ? 908  LYS   B CD    1 
ATOM   15629 C  CE    . LYS   B  1  910  ? 31.201  31.724  107.319 1.00 47.53 ? 908  LYS   B CE    1 
ATOM   15630 N  NZ    . LYS   B  1  910  ? 29.909  31.606  108.056 1.00 45.38 ? 908  LYS   B NZ    1 
ATOM   15631 N  N     . VAL   B  1  911  ? 33.667  32.362  102.254 1.00 22.53 ? 909  VAL   B N     1 
ATOM   15632 C  CA    . VAL   B  1  911  ? 33.196  31.602  101.104 1.00 20.15 ? 909  VAL   B CA    1 
ATOM   15633 C  C     . VAL   B  1  911  ? 32.837  30.209  101.587 1.00 20.95 ? 909  VAL   B C     1 
ATOM   15634 O  O     . VAL   B  1  911  ? 33.653  29.550  102.243 1.00 24.59 ? 909  VAL   B O     1 
ATOM   15635 C  CB    . VAL   B  1  911  ? 34.289  31.509  100.025 1.00 21.38 ? 909  VAL   B CB    1 
ATOM   15636 C  CG1   . VAL   B  1  911  ? 33.839  30.590  98.893  1.00 21.66 ? 909  VAL   B CG1   1 
ATOM   15637 C  CG2   . VAL   B  1  911  ? 34.652  32.903  99.523  1.00 22.11 ? 909  VAL   B CG2   1 
ATOM   15638 N  N     . GLU   B  1  912  ? 31.626  29.764  101.274 1.00 19.48 ? 910  GLU   B N     1 
ATOM   15639 C  CA    . GLU   B  1  912  ? 31.175  28.431  101.644 1.00 20.34 ? 910  GLU   B CA    1 
ATOM   15640 C  C     . GLU   B  1  912  ? 30.587  27.743  100.428 1.00 22.02 ? 910  GLU   B C     1 
ATOM   15641 O  O     . GLU   B  1  912  ? 29.824  28.351  99.670  1.00 21.07 ? 910  GLU   B O     1 
ATOM   15642 C  CB    . GLU   B  1  912  ? 30.115  28.492  102.742 1.00 24.27 ? 910  GLU   B CB    1 
ATOM   15643 C  CG    . GLU   B  1  912  ? 30.619  29.119  104.027 1.00 27.71 ? 910  GLU   B CG    1 
ATOM   15644 C  CD    . GLU   B  1  912  ? 29.529  29.233  105.071 1.00 40.42 ? 910  GLU   B CD    1 
ATOM   15645 O  OE1   . GLU   B  1  912  ? 29.005  28.184  105.508 1.00 43.46 ? 910  GLU   B OE1   1 
ATOM   15646 O  OE2   . GLU   B  1  912  ? 29.183  30.376  105.436 1.00 45.70 ? 910  GLU   B OE2   1 
ATOM   15647 N  N     . GLN   B  1  913  ? 30.930  26.468  100.251 1.00 20.40 ? 911  GLN   B N     1 
ATOM   15648 C  CA    . GLN   B  1  913  ? 30.414  25.692  99.135  1.00 20.40 ? 911  GLN   B CA    1 
ATOM   15649 C  C     . GLN   B  1  913  ? 29.835  24.378  99.622  1.00 26.37 ? 911  GLN   B C     1 
ATOM   15650 O  O     . GLN   B  1  913  ? 30.352  23.777  100.570 1.00 26.63 ? 911  GLN   B O     1 
ATOM   15651 C  CB    . GLN   B  1  913  ? 31.509  25.380  98.120  1.00 23.06 ? 911  GLN   B CB    1 
ATOM   15652 C  CG    . GLN   B  1  913  ? 32.083  26.618  97.477  1.00 23.60 ? 911  GLN   B CG    1 
ATOM   15653 C  CD    . GLN   B  1  913  ? 33.094  26.276  96.409  1.00 25.85 ? 911  GLN   B CD    1 
ATOM   15654 O  OE1   . GLN   B  1  913  ? 34.113  25.652  96.693  1.00 32.98 ? 911  GLN   B OE1   1 
ATOM   15655 N  NE2   . GLN   B  1  913  ? 32.814  26.671  95.170  1.00 22.81 ? 911  GLN   B NE2   1 
ATOM   15656 N  N     . ILE   B  1  914  ? 28.751  23.953  98.962  1.00 23.75 ? 912  ILE   B N     1 
ATOM   15657 C  CA    . ILE   B  1  914  ? 28.300  22.558  99.011  1.00 33.83 ? 912  ILE   B CA    1 
ATOM   15658 C  C     . ILE   B  1  914  ? 29.407  21.613  98.523  1.00 42.63 ? 912  ILE   B C     1 
ATOM   15659 O  O     . ILE   B  1  914  ? 30.374  22.016  97.864  1.00 41.63 ? 912  ILE   B O     1 
ATOM   15660 C  CB    . ILE   B  1  914  ? 27.044  22.396  98.138  1.00 24.32 ? 912  ILE   B CB    1 
ATOM   15661 N  N     . GLY   B  1  915  ? 29.244  20.327  98.840  1.00 51.48 ? 913  GLY   B N     1 
ATOM   15662 C  CA    . GLY   B  1  915  ? 30.108  19.309  98.282  1.00 47.03 ? 913  GLY   B CA    1 
ATOM   15663 C  C     . GLY   B  1  915  ? 29.585  18.786  96.952  1.00 47.20 ? 913  GLY   B C     1 
ATOM   15664 O  O     . GLY   B  1  915  ? 28.415  18.941  96.616  1.00 47.42 ? 913  GLY   B O     1 
ATOM   15665 N  N     . LEU   B  1  916  ? 30.470  18.159  96.181  1.00 47.07 ? 914  LEU   B N     1 
ATOM   15666 C  CA    . LEU   B  1  916  ? 30.098  17.604  94.886  1.00 39.14 ? 914  LEU   B CA    1 
ATOM   15667 C  C     . LEU   B  1  916  ? 30.477  16.132  94.838  1.00 43.96 ? 914  LEU   B C     1 
ATOM   15668 O  O     . LEU   B  1  916  ? 31.566  15.748  95.276  1.00 41.55 ? 914  LEU   B O     1 
ATOM   15669 C  CB    . LEU   B  1  916  ? 30.778  18.357  93.730  1.00 41.82 ? 914  LEU   B CB    1 
ATOM   15670 N  N     . ALA   B  1  917  ? 29.571  15.315  94.305  1.00 42.58 ? 915  ALA   B N     1 
ATOM   15671 C  CA    . ALA   B  1  917  ? 29.789  13.879  94.219  1.00 44.82 ? 915  ALA   B CA    1 
ATOM   15672 C  C     . ALA   B  1  917  ? 30.913  13.565  93.236  1.00 44.13 ? 915  ALA   B C     1 
ATOM   15673 O  O     . ALA   B  1  917  ? 31.221  14.345  92.330  1.00 40.69 ? 915  ALA   B O     1 
ATOM   15674 C  CB    . ALA   B  1  917  ? 28.508  13.176  93.769  1.00 42.39 ? 915  ALA   B CB    1 
ATOM   15675 N  N     . SER   B  1  918  ? 31.525  12.391  93.426  1.00 46.34 ? 916  SER   B N     1 
ATOM   15676 C  CA    . SER   B  1  918  ? 32.628  11.972  92.564  1.00 49.47 ? 916  SER   B CA    1 
ATOM   15677 C  C     . SER   B  1  918  ? 32.204  11.897  91.103  1.00 44.91 ? 916  SER   B C     1 
ATOM   15678 O  O     . SER   B  1  918  ? 33.013  12.167  90.205  1.00 43.76 ? 916  SER   B O     1 
ATOM   15679 C  CB    . SER   B  1  918  ? 33.179  10.624  93.038  1.00 42.63 ? 916  SER   B CB    1 
ATOM   15680 N  N     . GLU   B  1  919  ? 30.936  11.561  90.848  1.00 42.07 ? 917  GLU   B N     1 
ATOM   15681 C  CA    . GLU   B  1  919  ? 30.415  11.467  89.489  1.00 40.95 ? 917  GLU   B CA    1 
ATOM   15682 C  C     . GLU   B  1  919  ? 30.482  12.784  88.732  1.00 39.06 ? 917  GLU   B C     1 
ATOM   15683 O  O     . GLU   B  1  919  ? 30.333  12.778  87.506  1.00 38.61 ? 917  GLU   B O     1 
ATOM   15684 C  CB    . GLU   B  1  919  ? 28.969  10.971  89.515  1.00 38.56 ? 917  GLU   B CB    1 
ATOM   15685 N  N     . THR   B  1  920  ? 30.698  13.907  89.419  1.00 36.05 ? 918  THR   B N     1 
ATOM   15686 C  CA    . THR   B  1  920  ? 30.772  15.182  88.718  1.00 34.60 ? 918  THR   B CA    1 
ATOM   15687 C  C     . THR   B  1  920  ? 32.082  15.353  87.953  1.00 35.09 ? 918  THR   B C     1 
ATOM   15688 O  O     . THR   B  1  920  ? 32.143  16.192  87.048  1.00 31.50 ? 918  THR   B O     1 
ATOM   15689 C  CB    . THR   B  1  920  ? 30.528  16.350  89.688  1.00 34.86 ? 918  THR   B CB    1 
ATOM   15690 O  OG1   . THR   B  1  920  ? 31.486  16.314  90.753  1.00 32.78 ? 918  THR   B OG1   1 
ATOM   15691 C  CG2   . THR   B  1  920  ? 29.120  16.287  90.277  1.00 29.60 ? 918  THR   B CG2   1 
ATOM   15692 N  N     . GLY   B  1  921  ? 33.114  14.562  88.271  1.00 35.71 ? 919  GLY   B N     1 
ATOM   15693 C  CA    . GLY   B  1  921  ? 34.429  14.738  87.671  1.00 34.88 ? 919  GLY   B CA    1 
ATOM   15694 C  C     . GLY   B  1  921  ? 34.477  14.545  86.166  1.00 32.35 ? 919  GLY   B C     1 
ATOM   15695 O  O     . GLY   B  1  921  ? 35.425  15.004  85.521  1.00 36.55 ? 919  GLY   B O     1 
ATOM   15696 N  N     . VAL   B  1  922  ? 33.481  13.870  85.588  1.00 25.87 ? 920  VAL   B N     1 
ATOM   15697 C  CA    . VAL   B  1  922  ? 33.419  13.694  84.137  1.00 24.39 ? 920  VAL   B CA    1 
ATOM   15698 C  C     . VAL   B  1  922  ? 32.791  14.881  83.414  1.00 24.39 ? 920  VAL   B C     1 
ATOM   15699 O  O     . VAL   B  1  922  ? 32.855  14.946  82.174  1.00 21.54 ? 920  VAL   B O     1 
ATOM   15700 C  CB    . VAL   B  1  922  ? 32.670  12.399  83.772  1.00 25.11 ? 920  VAL   B CB    1 
ATOM   15701 C  CG1   . VAL   B  1  922  ? 33.452  11.187  84.260  1.00 28.09 ? 920  VAL   B CG1   1 
ATOM   15702 C  CG2   . VAL   B  1  922  ? 31.259  12.411  84.366  1.00 24.22 ? 920  VAL   B CG2   1 
ATOM   15703 N  N     . GLY   B  1  923  ? 32.195  15.817  84.142  1.00 20.36 ? 921  GLY   B N     1 
ATOM   15704 C  CA    . GLY   B  1  923  ? 31.590  16.997  83.550  1.00 18.14 ? 921  GLY   B CA    1 
ATOM   15705 C  C     . GLY   B  1  923  ? 32.133  18.245  84.209  1.00 22.31 ? 921  GLY   B C     1 
ATOM   15706 O  O     . GLY   B  1  923  ? 33.096  18.164  84.979  1.00 23.42 ? 921  GLY   B O     1 
ATOM   15707 N  N     . THR   B  1  924  ? 31.532  19.399  83.948  1.00 17.13 ? 922  THR   B N     1 
ATOM   15708 C  CA    . THR   B  1  924  ? 32.010  20.665  84.498  1.00 17.64 ? 922  THR   B CA    1 
ATOM   15709 C  C     . THR   B  1  924  ? 30.976  21.180  85.493  1.00 18.81 ? 922  THR   B C     1 
ATOM   15710 O  O     . THR   B  1  924  ? 29.935  21.700  85.096  1.00 19.24 ? 922  THR   B O     1 
ATOM   15711 C  CB    . THR   B  1  924  ? 32.256  21.675  83.381  1.00 16.95 ? 922  THR   B CB    1 
ATOM   15712 O  OG1   . THR   B  1  924  ? 31.128  21.697  82.504  1.00 19.24 ? 922  THR   B OG1   1 
ATOM   15713 C  CG2   . THR   B  1  924  ? 33.493  21.301  82.586  1.00 19.72 ? 922  THR   B CG2   1 
ATOM   15714 N  N     . PHE   B  1  925  ? 31.265  21.033  86.779  1.00 18.20 ? 923  PHE   B N     1 
ATOM   15715 C  CA    . PHE   B  1  925  ? 30.336  21.428  87.823  1.00 17.16 ? 923  PHE   B CA    1 
ATOM   15716 C  C     . PHE   B  1  925  ? 30.985  22.432  88.758  1.00 18.19 ? 923  PHE   B C     1 
ATOM   15717 O  O     . PHE   B  1  925  ? 32.191  22.378  89.022  1.00 18.95 ? 923  PHE   B O     1 
ATOM   15718 C  CB    . PHE   B  1  925  ? 29.897  20.224  88.660  1.00 17.53 ? 923  PHE   B CB    1 
ATOM   15719 C  CG    . PHE   B  1  925  ? 29.020  19.269  87.923  1.00 17.05 ? 923  PHE   B CG    1 
ATOM   15720 C  CD1   . PHE   B  1  925  ? 29.572  18.297  87.103  1.00 19.03 ? 923  PHE   B CD1   1 
ATOM   15721 C  CD2   . PHE   B  1  925  ? 27.637  19.342  88.046  1.00 16.58 ? 923  PHE   B CD2   1 
ATOM   15722 C  CE1   . PHE   B  1  925  ? 28.760  17.410  86.409  1.00 19.35 ? 923  PHE   B CE1   1 
ATOM   15723 C  CE2   . PHE   B  1  925  ? 26.819  18.467  87.360  1.00 17.89 ? 923  PHE   B CE2   1 
ATOM   15724 C  CZ    . PHE   B  1  925  ? 27.378  17.488  86.546  1.00 18.40 ? 923  PHE   B CZ    1 
ATOM   15725 N  N     . VAL   B  1  926  ? 30.156  23.340  89.261  1.00 17.16 ? 924  VAL   B N     1 
ATOM   15726 C  CA    . VAL   B  1  926  ? 30.523  24.233  90.350  1.00 15.85 ? 924  VAL   B CA    1 
ATOM   15727 C  C     . VAL   B  1  926  ? 29.421  24.059  91.381  1.00 15.98 ? 924  VAL   B C     1 
ATOM   15728 O  O     . VAL   B  1  926  ? 28.239  24.162  91.031  1.00 16.74 ? 924  VAL   B O     1 
ATOM   15729 C  CB    . VAL   B  1  926  ? 30.601  25.688  89.864  1.00 15.86 ? 924  VAL   B CB    1 
ATOM   15730 C  CG1   . VAL   B  1  926  ? 30.835  26.620  91.043  1.00 18.17 ? 924  VAL   B CG1   1 
ATOM   15731 C  CG2   . VAL   B  1  926  ? 31.722  25.847  88.825  1.00 18.91 ? 924  VAL   B CG2   1 
ATOM   15732 N  N     . PRO   B  1  927  ? 29.736  23.789  92.639  1.00 18.87 ? 925  PRO   B N     1 
ATOM   15733 C  CA    . PRO   B  1  927  ? 28.683  23.613  93.627  1.00 19.37 ? 925  PRO   B CA    1 
ATOM   15734 C  C     . PRO   B  1  927  ? 28.118  24.958  94.032  1.00 20.08 ? 925  PRO   B C     1 
ATOM   15735 O  O     . PRO   B  1  927  ? 28.800  25.987  93.903  1.00 19.76 ? 925  PRO   B O     1 
ATOM   15736 C  CB    . PRO   B  1  927  ? 29.424  22.970  94.804  1.00 23.38 ? 925  PRO   B CB    1 
ATOM   15737 C  CG    . PRO   B  1  927  ? 30.792  23.546  94.707  1.00 19.92 ? 925  PRO   B CG    1 
ATOM   15738 C  CD    . PRO   B  1  927  ? 31.079  23.716  93.235  1.00 20.35 ? 925  PRO   B CD    1 
ATOM   15739 N  N     . PRO   B  1  928  ? 26.874  24.991  94.506  1.00 17.53 ? 926  PRO   B N     1 
ATOM   15740 C  CA    . PRO   B  1  928  ? 26.336  26.213  95.103  1.00 17.24 ? 926  PRO   B CA    1 
ATOM   15741 C  C     . PRO   B  1  928  ? 27.315  26.824  96.090  1.00 18.47 ? 926  PRO   B C     1 
ATOM   15742 O  O     . PRO   B  1  928  ? 27.856  26.149  96.969  1.00 19.85 ? 926  PRO   B O     1 
ATOM   15743 C  CB    . PRO   B  1  928  ? 25.067  25.725  95.811  1.00 18.03 ? 926  PRO   B CB    1 
ATOM   15744 C  CG    . PRO   B  1  928  ? 24.619  24.588  94.981  1.00 23.57 ? 926  PRO   B CG    1 
ATOM   15745 C  CD    . PRO   B  1  928  ? 25.875  23.910  94.488  1.00 18.90 ? 926  PRO   B CD    1 
ATOM   15746 N  N     . THR   B  1  929  ? 27.537  28.116  95.931  1.00 17.27 ? 927  THR   B N     1 
ATOM   15747 C  CA    . THR   B  1  929  ? 28.565  28.838  96.649  1.00 15.33 ? 927  THR   B CA    1 
ATOM   15748 C  C     . THR   B  1  929  ? 27.929  30.088  97.224  1.00 17.78 ? 927  THR   B C     1 
ATOM   15749 O  O     . THR   B  1  929  ? 27.157  30.769  96.545  1.00 18.16 ? 927  THR   B O     1 
ATOM   15750 C  CB    . THR   B  1  929  ? 29.683  29.228  95.678  1.00 18.47 ? 927  THR   B CB    1 
ATOM   15751 O  OG1   . THR   B  1  929  ? 30.237  28.031  95.112  1.00 18.24 ? 927  THR   B OG1   1 
ATOM   15752 C  CG2   . THR   B  1  929  ? 30.775  30.013  96.380  1.00 18.44 ? 927  THR   B CG2   1 
ATOM   15753 N  N     . ILE   B  1  930  ? 28.235  30.362  98.487  1.00 17.96 ? 928  ILE   B N     1 
ATOM   15754 C  CA    . ILE   B  1  930  ? 27.755  31.543  99.188  1.00 18.22 ? 928  ILE   B CA    1 
ATOM   15755 C  C     . ILE   B  1  930  ? 28.971  32.333  99.628  1.00 18.94 ? 928  ILE   B C     1 
ATOM   15756 O  O     . ILE   B  1  930  ? 29.860  31.799  100.305 1.00 19.46 ? 928  ILE   B O     1 
ATOM   15757 C  CB    . ILE   B  1  930  ? 26.880  31.176  100.400 1.00 17.37 ? 928  ILE   B CB    1 
ATOM   15758 C  CG1   . ILE   B  1  930  ? 25.651  30.386  99.949  1.00 18.82 ? 928  ILE   B CG1   1 
ATOM   15759 C  CG2   . ILE   B  1  930  ? 26.485  32.447  101.159 1.00 18.64 ? 928  ILE   B CG2   1 
ATOM   15760 C  CD1   . ILE   B  1  930  ? 24.851  29.795  101.100 1.00 24.01 ? 928  ILE   B CD1   1 
ATOM   15761 N  N     . ILE   B  1  931  ? 29.000  33.607  99.259  1.00 19.13 ? 929  ILE   B N     1 
ATOM   15762 C  CA    . ILE   B  1  931  ? 30.106  34.498  99.569  1.00 19.16 ? 929  ILE   B CA    1 
ATOM   15763 C  C     . ILE   B  1  931  ? 29.543  35.688  100.324 1.00 18.66 ? 929  ILE   B C     1 
ATOM   15764 O  O     . ILE   B  1  931  ? 28.617  36.344  99.841  1.00 18.31 ? 929  ILE   B O     1 
ATOM   15765 C  CB    . ILE   B  1  931  ? 30.797  34.971  98.283  1.00 17.30 ? 929  ILE   B CB    1 
ATOM   15766 C  CG1   . ILE   B  1  931  ? 31.261  33.759  97.473  1.00 19.14 ? 929  ILE   B CG1   1 
ATOM   15767 C  CG2   . ILE   B  1  931  ? 31.982  35.878  98.616  1.00 18.04 ? 929  ILE   B CG2   1 
ATOM   15768 C  CD1   . ILE   B  1  931  ? 32.126  34.133  96.274  1.00 19.07 ? 929  ILE   B CD1   1 
ATOM   15769 N  N     . GLU   B  1  932  ? 30.094  35.970  101.497 1.00 19.00 ? 930  GLU   B N     1 
ATOM   15770 C  CA    . GLU   B  1  932  ? 29.635  37.104  102.281 1.00 19.00 ? 930  GLU   B CA    1 
ATOM   15771 C  C     . GLU   B  1  932  ? 30.413  38.337  101.857 1.00 19.22 ? 930  GLU   B C     1 
ATOM   15772 O  O     . GLU   B  1  932  ? 31.650  38.338  101.873 1.00 21.31 ? 930  GLU   B O     1 
ATOM   15773 C  CB    . GLU   B  1  932  ? 29.790  36.832  103.777 1.00 25.33 ? 930  GLU   B CB    1 
ATOM   15774 C  CG    . GLU   B  1  932  ? 28.984  35.634  104.244 1.00 27.17 ? 930  GLU   B CG    1 
ATOM   15775 C  CD    . GLU   B  1  932  ? 28.124  35.929  105.459 1.00 39.67 ? 930  GLU   B CD    1 
ATOM   15776 O  OE1   . GLU   B  1  932  ? 27.800  37.116  105.693 1.00 45.83 ? 930  GLU   B OE1   1 
ATOM   15777 O  OE2   . GLU   B  1  932  ? 27.774  34.970  106.180 1.00 37.52 ? 930  GLU   B OE2   1 
ATOM   15778 N  N     . LEU   B  1  933  ? 29.698  39.376  101.459 1.00 21.10 ? 931  LEU   B N     1 
ATOM   15779 C  CA    . LEU   B  1  933  ? 30.333  40.622  101.077 1.00 20.67 ? 931  LEU   B CA    1 
ATOM   15780 C  C     . LEU   B  1  933  ? 30.197  41.634  102.202 1.00 24.80 ? 931  LEU   B C     1 
ATOM   15781 O  O     . LEU   B  1  933  ? 29.255  41.586  102.994 1.00 28.31 ? 931  LEU   B O     1 
ATOM   15782 C  CB    . LEU   B  1  933  ? 29.667  41.199  99.833  1.00 21.75 ? 931  LEU   B CB    1 
ATOM   15783 C  CG    . LEU   B  1  933  ? 29.662  40.308  98.599  1.00 23.49 ? 931  LEU   B CG    1 
ATOM   15784 C  CD1   . LEU   B  1  933  ? 29.047  41.093  97.457  1.00 26.93 ? 931  LEU   B CD1   1 
ATOM   15785 C  CD2   . LEU   B  1  933  ? 31.073  39.854  98.265  1.00 29.08 ? 931  LEU   B CD2   1 
ATOM   15786 N  N     . GLU   B  1  934  ? 31.144  42.566  102.253 1.00 26.97 ? 932  GLU   B N     1 
ATOM   15787 C  CA    . GLU   B  1  934  ? 30.975  43.716  103.131 1.00 28.25 ? 932  GLU   B CA    1 
ATOM   15788 C  C     . GLU   B  1  934  ? 30.135  44.792  102.456 1.00 32.44 ? 932  GLU   B C     1 
ATOM   15789 O  O     . GLU   B  1  934  ? 29.359  45.489  103.117 1.00 33.80 ? 932  GLU   B O     1 
ATOM   15790 C  CB    . GLU   B  1  934  ? 32.343  44.275  103.534 1.00 31.80 ? 932  GLU   B CB    1 
ATOM   15791 N  N     . LYS   B  1  935  ? 30.266  44.928  101.141 1.00 28.44 ? 933  LYS   B N     1 
ATOM   15792 C  CA    . LYS   B  1  935  ? 29.558  45.956  100.400 1.00 30.00 ? 933  LYS   B CA    1 
ATOM   15793 C  C     . LYS   B  1  935  ? 29.269  45.416  99.011  1.00 26.06 ? 933  LYS   B C     1 
ATOM   15794 O  O     . LYS   B  1  935  ? 30.036  44.613  98.475  1.00 27.33 ? 933  LYS   B O     1 
ATOM   15795 C  CB    . LYS   B  1  935  ? 30.393  47.238  100.302 1.00 31.16 ? 933  LYS   B CB    1 
ATOM   15796 N  N     . LEU   B  1  936  ? 28.152  45.859  98.434  1.00 24.71 ? 934  LEU   B N     1 
ATOM   15797 C  CA    . LEU   B  1  936  ? 27.816  45.416  97.090  1.00 27.93 ? 934  LEU   B CA    1 
ATOM   15798 C  C     . LEU   B  1  936  ? 28.905  45.790  96.096  1.00 25.89 ? 934  LEU   B C     1 
ATOM   15799 O  O     . LEU   B  1  936  ? 29.127  45.066  95.123  1.00 25.80 ? 934  LEU   B O     1 
ATOM   15800 C  CB    . LEU   B  1  936  ? 26.463  45.986  96.672  1.00 29.02 ? 934  LEU   B CB    1 
ATOM   15801 C  CG    . LEU   B  1  936  ? 25.524  45.018  95.951  1.00 30.85 ? 934  LEU   B CG    1 
ATOM   15802 C  CD1   . LEU   B  1  936  ? 24.074  45.458  96.114  1.00 29.10 ? 934  LEU   B CD1   1 
ATOM   15803 C  CD2   . LEU   B  1  936  ? 25.895  44.917  94.496  1.00 32.10 ? 934  LEU   B CD2   1 
ATOM   15804 N  N     . SER   B  1  937  ? 29.614  46.893  96.339  1.00 25.63 ? 935  SER   B N     1 
ATOM   15805 C  CA    . SER   B  1  937  ? 30.671  47.311  95.427  1.00 26.86 ? 935  SER   B CA    1 
ATOM   15806 C  C     . SER   B  1  937  ? 31.851  46.347  95.397  1.00 26.02 ? 935  SER   B C     1 
ATOM   15807 O  O     . SER   B  1  937  ? 32.708  46.487  94.517  1.00 27.47 ? 935  SER   B O     1 
ATOM   15808 C  CB    . SER   B  1  937  ? 31.137  48.732  95.753  1.00 27.72 ? 935  SER   B CB    1 
ATOM   15809 O  OG    . SER   B  1  937  ? 31.585  48.820  97.092  1.00 32.85 ? 935  SER   B OG    1 
ATOM   15810 N  N     . ASP   B  1  938  ? 31.915  45.376  96.317  1.00 27.37 ? 936  ASP   B N     1 
ATOM   15811 C  CA    . ASP   B  1  938  ? 32.909  44.311  96.207  1.00 28.20 ? 936  ASP   B CA    1 
ATOM   15812 C  C     . ASP   B  1  938  ? 32.709  43.483  94.951  1.00 27.24 ? 936  ASP   B C     1 
ATOM   15813 O  O     . ASP   B  1  938  ? 33.635  42.794  94.518  1.00 28.04 ? 936  ASP   B O     1 
ATOM   15814 C  CB    . ASP   B  1  938  ? 32.810  43.331  97.379  1.00 29.48 ? 936  ASP   B CB    1 
ATOM   15815 C  CG    . ASP   B  1  938  ? 33.141  43.959  98.719  1.00 36.07 ? 936  ASP   B CG    1 
ATOM   15816 O  OD1   . ASP   B  1  938  ? 33.693  45.079  98.756  1.00 34.54 ? 936  ASP   B OD1   1 
ATOM   15817 O  OD2   . ASP   B  1  938  ? 32.830  43.313  99.747  1.00 40.49 ? 936  ASP   B OD2   1 
ATOM   15818 N  N     . LEU   B  1  939  ? 31.512  43.509  94.383  1.00 24.60 ? 937  LEU   B N     1 
ATOM   15819 C  CA    . LEU   B  1  939  ? 31.165  42.725  93.210  1.00 28.38 ? 937  LEU   B CA    1 
ATOM   15820 C  C     . LEU   B  1  939  ? 31.262  43.657  92.013  1.00 27.47 ? 937  LEU   B C     1 
ATOM   15821 O  O     . LEU   B  1  939  ? 30.551  44.665  91.960  1.00 33.76 ? 937  LEU   B O     1 
ATOM   15822 C  CB    . LEU   B  1  939  ? 29.722  42.251  93.352  1.00 26.57 ? 937  LEU   B CB    1 
ATOM   15823 C  CG    . LEU   B  1  939  ? 29.349  40.776  93.284  1.00 34.17 ? 937  LEU   B CG    1 
ATOM   15824 C  CD1   . LEU   B  1  939  ? 27.861  40.676  93.111  1.00 26.22 ? 937  LEU   B CD1   1 
ATOM   15825 C  CD2   . LEU   B  1  939  ? 30.049  40.050  92.149  1.00 30.08 ? 937  LEU   B CD2   1 
ATOM   15826 N  N     . GLN   B  1  940  ? 32.121  43.317  91.050  1.00 24.47 ? 938  GLN   B N     1 
ATOM   15827 C  CA    . GLN   B  1  940  ? 32.403  44.205  89.930  1.00 28.01 ? 938  GLN   B CA    1 
ATOM   15828 C  C     . GLN   B  1  940  ? 31.949  43.672  88.581  1.00 26.72 ? 938  GLN   B C     1 
ATOM   15829 O  O     . GLN   B  1  940  ? 32.026  44.405  87.589  1.00 27.45 ? 938  GLN   B O     1 
ATOM   15830 C  CB    . GLN   B  1  940  ? 33.905  44.526  89.860  1.00 36.33 ? 938  GLN   B CB    1 
ATOM   15831 N  N     . ARG   B  1  941  ? 31.477  42.432  88.505  1.00 22.01 ? 939  ARG   B N     1 
ATOM   15832 C  CA    . ARG   B  1  941  ? 31.088  41.867  87.224  1.00 23.65 ? 939  ARG   B CA    1 
ATOM   15833 C  C     . ARG   B  1  941  ? 30.021  40.810  87.456  1.00 19.87 ? 939  ARG   B C     1 
ATOM   15834 O  O     . ARG   B  1  941  ? 29.923  40.236  88.542  1.00 19.69 ? 939  ARG   B O     1 
ATOM   15835 C  CB    . ARG   B  1  941  ? 32.292  41.260  86.482  1.00 24.87 ? 939  ARG   B CB    1 
ATOM   15836 C  CG    . ARG   B  1  941  ? 32.932  40.062  87.176  1.00 26.48 ? 939  ARG   B CG    1 
ATOM   15837 C  CD    . ARG   B  1  941  ? 34.216  39.626  86.458  1.00 25.94 ? 939  ARG   B CD    1 
ATOM   15838 N  NE    . ARG   B  1  941  ? 34.811  38.419  87.026  1.00 24.13 ? 939  ARG   B NE    1 
ATOM   15839 C  CZ    . ARG   B  1  941  ? 34.555  37.187  86.605  1.00 25.50 ? 939  ARG   B CZ    1 
ATOM   15840 N  NH1   . ARG   B  1  941  ? 33.658  36.956  85.657  1.00 25.26 ? 939  ARG   B NH1   1 
ATOM   15841 N  NH2   . ARG   B  1  941  ? 35.224  36.164  87.136  1.00 24.95 ? 939  ARG   B NH2   1 
ATOM   15842 N  N     . GLU   B  1  942  ? 29.208  40.576  86.430  1.00 20.60 ? 940  GLU   B N     1 
ATOM   15843 C  CA    . GLU   B  1  942  ? 28.242  39.488  86.480  1.00 20.05 ? 940  GLU   B CA    1 
ATOM   15844 C  C     . GLU   B  1  942  ? 28.995  38.165  86.453  1.00 20.26 ? 940  GLU   B C     1 
ATOM   15845 O  O     . GLU   B  1  942  ? 29.761  37.899  85.522  1.00 22.43 ? 940  GLU   B O     1 
ATOM   15846 C  CB    . GLU   B  1  942  ? 27.307  39.585  85.279  1.00 20.69 ? 940  GLU   B CB    1 
ATOM   15847 C  CG    . GLU   B  1  942  ? 26.305  38.445  85.184  1.00 19.22 ? 940  GLU   B CG    1 
ATOM   15848 C  CD    . GLU   B  1  942  ? 25.576  38.436  83.847  1.00 20.51 ? 940  GLU   B CD    1 
ATOM   15849 O  OE1   . GLU   B  1  942  ? 26.247  38.660  82.812  1.00 23.58 ? 940  GLU   B OE1   1 
ATOM   15850 O  OE2   . GLU   B  1  942  ? 24.344  38.210  83.826  1.00 19.41 ? 940  GLU   B OE2   1 
ATOM   15851 N  N     . VAL   B  1  943  ? 28.792  37.341  87.477  1.00 16.09 ? 941  VAL   B N     1 
ATOM   15852 C  CA    . VAL   B  1  943  ? 29.404  36.020  87.564  1.00 18.44 ? 941  VAL   B CA    1 
ATOM   15853 C  C     . VAL   B  1  943  ? 28.314  35.001  87.275  1.00 18.00 ? 941  VAL   B C     1 
ATOM   15854 O  O     . VAL   B  1  943  ? 27.406  34.792  88.087  1.00 17.46 ? 941  VAL   B O     1 
ATOM   15855 C  CB    . VAL   B  1  943  ? 30.067  35.783  88.929  1.00 21.51 ? 941  VAL   B CB    1 
ATOM   15856 C  CG1   . VAL   B  1  943  ? 30.686  34.385  88.987  1.00 20.45 ? 941  VAL   B CG1   1 
ATOM   15857 C  CG2   . VAL   B  1  943  ? 31.115  36.856  89.187  1.00 24.06 ? 941  VAL   B CG2   1 
ATOM   15858 N  N     . PHE   B  1  944  ? 28.403  34.362  86.111  1.00 16.88 ? 942  PHE   B N     1 
ATOM   15859 C  CA    . PHE   B  1  944  ? 27.279  33.614  85.554  1.00 16.47 ? 942  PHE   B CA    1 
ATOM   15860 C  C     . PHE   B  1  944  ? 27.387  32.157  86.002  1.00 16.89 ? 942  PHE   B C     1 
ATOM   15861 O  O     . PHE   B  1  944  ? 27.725  31.244  85.250  1.00 17.08 ? 942  PHE   B O     1 
ATOM   15862 C  CB    . PHE   B  1  944  ? 27.275  33.738  84.035  1.00 17.60 ? 942  PHE   B CB    1 
ATOM   15863 C  CG    . PHE   B  1  944  ? 25.936  33.501  83.416  1.00 16.16 ? 942  PHE   B CG    1 
ATOM   15864 C  CD1   . PHE   B  1  944  ? 24.923  34.432  83.566  1.00 16.66 ? 942  PHE   B CD1   1 
ATOM   15865 C  CD2   . PHE   B  1  944  ? 25.690  32.353  82.666  1.00 17.28 ? 942  PHE   B CD2   1 
ATOM   15866 C  CE1   . PHE   B  1  944  ? 23.686  34.234  82.989  1.00 16.27 ? 942  PHE   B CE1   1 
ATOM   15867 C  CE2   . PHE   B  1  944  ? 24.440  32.146  82.076  1.00 17.28 ? 942  PHE   B CE2   1 
ATOM   15868 C  CZ    . PHE   B  1  944  ? 23.433  33.084  82.260  1.00 17.80 ? 942  PHE   B CZ    1 
ATOM   15869 N  N     . GLY   B  1  945  ? 27.096  31.956  87.273  1.00 15.08 ? 943  GLY   B N     1 
ATOM   15870 C  CA    . GLY   B  1  945  ? 27.289  30.669  87.885  1.00 16.95 ? 943  GLY   B CA    1 
ATOM   15871 C  C     . GLY   B  1  945  ? 26.562  30.614  89.205  1.00 16.78 ? 943  GLY   B C     1 
ATOM   15872 O  O     . GLY   B  1  945  ? 25.879  31.561  89.602  1.00 17.44 ? 943  GLY   B O     1 
ATOM   15873 N  N     . PRO   B  1  946  ? 26.713  29.509  89.925  1.00 16.63 ? 944  PRO   B N     1 
ATOM   15874 C  CA    . PRO   B  1  946  ? 25.913  29.300  91.144  1.00 18.21 ? 944  PRO   B CA    1 
ATOM   15875 C  C     . PRO   B  1  946  ? 26.584  29.944  92.352  1.00 16.06 ? 944  PRO   B C     1 
ATOM   15876 O  O     . PRO   B  1  946  ? 26.964  29.280  93.314  1.00 17.24 ? 944  PRO   B O     1 
ATOM   15877 C  CB    . PRO   B  1  946  ? 25.866  27.771  91.237  1.00 15.65 ? 944  PRO   B CB    1 
ATOM   15878 C  CG    . PRO   B  1  946  ? 27.238  27.348  90.695  1.00 19.91 ? 944  PRO   B CG    1 
ATOM   15879 C  CD    . PRO   B  1  946  ? 27.516  28.328  89.562  1.00 16.77 ? 944  PRO   B CD    1 
ATOM   15880 N  N     . VAL   B  1  947  ? 26.742  31.259  92.294  1.00 16.08 ? 945  VAL   B N     1 
ATOM   15881 C  CA    . VAL   B  1  947  ? 27.493  31.988  93.303  1.00 16.40 ? 945  VAL   B CA    1 
ATOM   15882 C  C     . VAL   B  1  947  ? 26.578  33.065  93.852  1.00 19.84 ? 945  VAL   B C     1 
ATOM   15883 O  O     . VAL   B  1  947  ? 26.273  34.046  93.163  1.00 19.52 ? 945  VAL   B O     1 
ATOM   15884 C  CB    . VAL   B  1  947  ? 28.793  32.579  92.747  1.00 18.33 ? 945  VAL   B CB    1 
ATOM   15885 C  CG1   . VAL   B  1  947  ? 29.571  33.262  93.860  1.00 19.92 ? 945  VAL   B CG1   1 
ATOM   15886 C  CG2   . VAL   B  1  947  ? 29.620  31.491  92.074  1.00 18.49 ? 945  VAL   B CG2   1 
ATOM   15887 N  N     . LEU   B  1  948  ? 26.123  32.872  95.083  1.00 15.84 ? 946  LEU   B N     1 
ATOM   15888 C  CA    . LEU   B  1  948  ? 25.251  33.822  95.745  1.00 15.36 ? 946  LEU   B CA    1 
ATOM   15889 C  C     . LEU   B  1  948  ? 26.092  34.664  96.681  1.00 16.51 ? 946  LEU   B C     1 
ATOM   15890 O  O     . LEU   B  1  948  ? 26.857  34.133  97.493  1.00 18.68 ? 946  LEU   B O     1 
ATOM   15891 C  CB    . LEU   B  1  948  ? 24.196  33.078  96.555  1.00 15.82 ? 946  LEU   B CB    1 
ATOM   15892 C  CG    . LEU   B  1  948  ? 23.235  33.977  97.313  1.00 15.98 ? 946  LEU   B CG    1 
ATOM   15893 C  CD1   . LEU   B  1  948  ? 22.378  34.759  96.320  1.00 16.33 ? 946  LEU   B CD1   1 
ATOM   15894 C  CD2   . LEU   B  1  948  ? 22.380  33.081  98.198  1.00 18.49 ? 946  LEU   B CD2   1 
ATOM   15895 N  N     . HIS   B  1  949  ? 25.960  35.968  96.561  1.00 15.01 ? 947  HIS   B N     1 
ATOM   15896 C  CA    . HIS   B  1  949  ? 26.642  36.885  97.452  1.00 15.50 ? 947  HIS   B CA    1 
ATOM   15897 C  C     . HIS   B  1  949  ? 25.645  37.359  98.485  1.00 18.08 ? 947  HIS   B C     1 
ATOM   15898 O  O     . HIS   B  1  949  ? 24.462  37.528  98.180  1.00 20.65 ? 947  HIS   B O     1 
ATOM   15899 C  CB    . HIS   B  1  949  ? 27.203  38.047  96.644  1.00 17.87 ? 947  HIS   B CB    1 
ATOM   15900 C  CG    . HIS   B  1  949  ? 28.089  37.591  95.532  1.00 16.27 ? 947  HIS   B CG    1 
ATOM   15901 N  ND1   . HIS   B  1  949  ? 27.598  37.228  94.297  1.00 17.92 ? 947  HIS   B ND1   1 
ATOM   15902 C  CD2   . HIS   B  1  949  ? 29.423  37.366  95.489  1.00 18.72 ? 947  HIS   B CD2   1 
ATOM   15903 C  CE1   . HIS   B  1  949  ? 28.594  36.827  93.530  1.00 17.29 ? 947  HIS   B CE1   1 
ATOM   15904 N  NE2   . HIS   B  1  949  ? 29.711  36.899  94.228  1.00 16.71 ? 947  HIS   B NE2   1 
ATOM   15905 N  N     . VAL   B  1  950  ? 26.105  37.502  99.721  1.00 16.63 ? 948  VAL   B N     1 
ATOM   15906 C  CA    . VAL   B  1  950  ? 25.229  37.848  100.830 1.00 18.25 ? 948  VAL   B CA    1 
ATOM   15907 C  C     . VAL   B  1  950  ? 25.691  39.155  101.446 1.00 18.06 ? 948  VAL   B C     1 
ATOM   15908 O  O     . VAL   B  1  950  ? 26.867  39.306  101.793 1.00 20.42 ? 948  VAL   B O     1 
ATOM   15909 C  CB    . VAL   B  1  950  ? 25.187  36.736  101.887 1.00 18.88 ? 948  VAL   B CB    1 
ATOM   15910 C  CG1   . VAL   B  1  950  ? 24.390  37.213  103.095 1.00 20.89 ? 948  VAL   B CG1   1 
ATOM   15911 C  CG2   . VAL   B  1  950  ? 24.580  35.479  101.298 1.00 20.67 ? 948  VAL   B CG2   1 
ATOM   15912 N  N     . ILE   B  1  951  ? 24.755  40.079  101.600 1.00 16.59 ? 949  ILE   B N     1 
ATOM   15913 C  CA    . ILE   B  1  951  ? 24.961  41.353  102.266 1.00 17.39 ? 949  ILE   B CA    1 
ATOM   15914 C  C     . ILE   B  1  951  ? 23.991  41.399  103.432 1.00 16.20 ? 949  ILE   B C     1 
ATOM   15915 O  O     . ILE   B  1  951  ? 22.828  41.013  103.283 1.00 18.80 ? 949  ILE   B O     1 
ATOM   15916 C  CB    . ILE   B  1  951  ? 24.641  42.495  101.282 1.00 21.02 ? 949  ILE   B CB    1 
ATOM   15917 C  CG1   . ILE   B  1  951  ? 25.723  42.583  100.218 1.00 26.69 ? 949  ILE   B CG1   1 
ATOM   15918 C  CG2   . ILE   B  1  951  ? 24.478  43.822  102.017 1.00 30.02 ? 949  ILE   B CG2   1 
ATOM   15919 C  CD1   . ILE   B  1  951  ? 25.447  43.646  99.208  1.00 32.15 ? 949  ILE   B CD1   1 
ATOM   15920 N  N     . ARG   B  1  952  ? 24.460  41.871  104.578 1.00 17.78 ? 950  ARG   B N     1 
ATOM   15921 C  CA    . ARG   B  1  952  ? 23.603  42.119  105.727 1.00 19.10 ? 950  ARG   B CA    1 
ATOM   15922 C  C     . ARG   B  1  952  ? 23.393  43.621  105.843 1.00 19.02 ? 950  ARG   B C     1 
ATOM   15923 O  O     . ARG   B  1  952  ? 24.320  44.403  105.622 1.00 23.60 ? 950  ARG   B O     1 
ATOM   15924 C  CB    . ARG   B  1  952  ? 24.269  41.588  107.001 1.00 20.10 ? 950  ARG   B CB    1 
ATOM   15925 C  CG    . ARG   B  1  952  ? 24.502  40.096  106.965 1.00 21.87 ? 950  ARG   B CG    1 
ATOM   15926 C  CD    . ARG   B  1  952  ? 25.578  39.691  107.947 1.00 30.20 ? 950  ARG   B CD    1 
ATOM   15927 N  NE    . ARG   B  1  952  ? 25.916  38.280  107.808 1.00 34.48 ? 950  ARG   B NE    1 
ATOM   15928 C  CZ    . ARG   B  1  952  ? 25.561  37.340  108.673 1.00 31.34 ? 950  ARG   B CZ    1 
ATOM   15929 N  NH1   . ARG   B  1  952  ? 24.829  37.622  109.736 1.00 28.47 ? 950  ARG   B NH1   1 
ATOM   15930 N  NH2   . ARG   B  1  952  ? 25.970  36.089  108.476 1.00 33.54 ? 950  ARG   B NH2   1 
ATOM   15931 N  N     . TYR   B  1  953  ? 22.165  44.036  106.158 1.00 17.51 ? 951  TYR   B N     1 
ATOM   15932 C  CA    . TYR   B  1  953  ? 21.912  45.467  106.250 1.00 19.86 ? 951  TYR   B CA    1 
ATOM   15933 C  C     . TYR   B  1  953  ? 21.059  45.775  107.470 1.00 18.88 ? 951  TYR   B C     1 
ATOM   15934 O  O     . TYR   B  1  953  ? 20.276  44.943  107.928 1.00 20.07 ? 951  TYR   B O     1 
ATOM   15935 C  CB    . TYR   B  1  953  ? 21.241  46.012  104.971 1.00 19.39 ? 951  TYR   B CB    1 
ATOM   15936 C  CG    . TYR   B  1  953  ? 19.812  45.577  104.818 1.00 18.31 ? 951  TYR   B CG    1 
ATOM   15937 C  CD1   . TYR   B  1  953  ? 19.495  44.343  104.265 1.00 16.98 ? 951  TYR   B CD1   1 
ATOM   15938 C  CD2   . TYR   B  1  953  ? 18.770  46.391  105.240 1.00 17.53 ? 951  TYR   B CD2   1 
ATOM   15939 C  CE1   . TYR   B  1  953  ? 18.184  43.947  104.136 1.00 17.63 ? 951  TYR   B CE1   1 
ATOM   15940 C  CE2   . TYR   B  1  953  ? 17.464  45.994  105.110 1.00 20.17 ? 951  TYR   B CE2   1 
ATOM   15941 C  CZ    . TYR   B  1  953  ? 17.178  44.770  104.561 1.00 18.27 ? 951  TYR   B CZ    1 
ATOM   15942 O  OH    . TYR   B  1  953  ? 15.869  44.374  104.441 1.00 18.56 ? 951  TYR   B OH    1 
ATOM   15943 N  N     . ARG   B  1  954  ? 21.232  46.985  107.995 1.00 22.47 ? 952  ARG   B N     1 
ATOM   15944 C  CA    . ARG   B  1  954  ? 20.362  47.508  109.033 1.00 23.28 ? 952  ARG   B CA    1 
ATOM   15945 C  C     . ARG   B  1  954  ? 19.163  48.152  108.356 1.00 22.27 ? 952  ARG   B C     1 
ATOM   15946 O  O     . ARG   B  1  954  ? 19.306  48.805  107.318 1.00 20.62 ? 952  ARG   B O     1 
ATOM   15947 C  CB    . ARG   B  1  954  ? 21.102  48.557  109.868 1.00 25.50 ? 952  ARG   B CB    1 
ATOM   15948 N  N     . ARG   B  1  955  ? 17.978  47.975  108.953 1.00 23.01 ? 953  ARG   B N     1 
ATOM   15949 C  CA    . ARG   B  1  955  ? 16.756  48.458  108.319 1.00 25.48 ? 953  ARG   B CA    1 
ATOM   15950 C  C     . ARG   B  1  955  ? 16.812  49.956  108.036 1.00 24.60 ? 953  ARG   B C     1 
ATOM   15951 O  O     . ARG   B  1  955  ? 16.286  50.419  107.020 1.00 24.95 ? 953  ARG   B O     1 
ATOM   15952 C  CB    . ARG   B  1  955  ? 15.536  48.105  109.172 1.00 27.50 ? 953  ARG   B CB    1 
ATOM   15953 C  CG    . ARG   B  1  955  ? 14.195  48.542  108.574 1.00 32.04 ? 953  ARG   B CG    1 
ATOM   15954 C  CD    . ARG   B  1  955  ? 14.028  48.114  107.111 1.00 32.29 ? 953  ARG   B CD    1 
ATOM   15955 N  NE    . ARG   B  1  955  ? 12.742  48.530  106.557 1.00 32.50 ? 953  ARG   B NE    1 
ATOM   15956 C  CZ    . ARG   B  1  955  ? 12.438  49.774  106.207 1.00 34.75 ? 953  ARG   B CZ    1 
ATOM   15957 N  NH1   . ARG   B  1  955  ? 13.303  50.767  106.353 1.00 32.98 ? 953  ARG   B NH1   1 
ATOM   15958 N  NH2   . ARG   B  1  955  ? 11.232  50.031  105.700 1.00 33.61 ? 953  ARG   B NH2   1 
ATOM   15959 N  N     . ASP   B  1  956  ? 17.441  50.733  108.916 1.00 23.06 ? 954  ASP   B N     1 
ATOM   15960 C  CA    . ASP   B  1  956  ? 17.499  52.166  108.637 1.00 26.34 ? 954  ASP   B CA    1 
ATOM   15961 C  C     . ASP   B  1  956  ? 18.438  52.516  107.485 1.00 25.98 ? 954  ASP   B C     1 
ATOM   15962 O  O     . ASP   B  1  956  ? 18.456  53.673  107.049 1.00 28.69 ? 954  ASP   B O     1 
ATOM   15963 C  CB    . ASP   B  1  956  ? 17.753  53.004  109.902 1.00 29.92 ? 954  ASP   B CB    1 
ATOM   15964 C  CG    . ASP   B  1  956  ? 19.062  52.673  110.594 1.00 36.74 ? 954  ASP   B CG    1 
ATOM   15965 O  OD1   . ASP   B  1  956  ? 20.005  52.186  109.932 1.00 37.80 ? 954  ASP   B OD1   1 
ATOM   15966 O  OD2   . ASP   B  1  956  ? 19.146  52.908  111.822 1.00 44.30 ? 954  ASP   B OD2   1 
ATOM   15967 N  N     . ASP   B  1  957  ? 19.187  51.549  106.962 1.00 23.14 ? 955  ASP   B N     1 
ATOM   15968 C  CA    . ASP   B  1  957  ? 20.007  51.769  105.780 1.00 24.06 ? 955  ASP   B CA    1 
ATOM   15969 C  C     . ASP   B  1  957  ? 19.355  51.247  104.506 1.00 21.10 ? 955  ASP   B C     1 
ATOM   15970 O  O     . ASP   B  1  957  ? 20.035  51.131  103.488 1.00 23.67 ? 955  ASP   B O     1 
ATOM   15971 C  CB    . ASP   B  1  957  ? 21.375  51.107  105.936 1.00 25.58 ? 955  ASP   B CB    1 
ATOM   15972 C  CG    . ASP   B  1  957  ? 22.240  51.794  106.956 1.00 35.80 ? 955  ASP   B CG    1 
ATOM   15973 O  OD1   . ASP   B  1  957  ? 22.139  53.033  107.090 1.00 34.89 ? 955  ASP   B OD1   1 
ATOM   15974 O  OD2   . ASP   B  1  957  ? 23.026  51.087  107.619 1.00 37.34 ? 955  ASP   B OD2   1 
ATOM   15975 N  N     . LEU   B  1  958  ? 18.063  50.921  104.544 1.00 18.42 ? 956  LEU   B N     1 
ATOM   15976 C  CA    . LEU   B  1  958  ? 17.421  50.312  103.383 1.00 18.18 ? 956  LEU   B CA    1 
ATOM   15977 C  C     . LEU   B  1  958  ? 17.530  51.204  102.150 1.00 18.97 ? 956  LEU   B C     1 
ATOM   15978 O  O     . LEU   B  1  958  ? 17.862  50.733  101.057 1.00 18.35 ? 956  LEU   B O     1 
ATOM   15979 C  CB    . LEU   B  1  958  ? 15.956  50.040  103.703 1.00 18.75 ? 956  LEU   B CB    1 
ATOM   15980 C  CG    . LEU   B  1  958  ? 15.146  49.461  102.553 1.00 20.70 ? 956  LEU   B CG    1 
ATOM   15981 C  CD1   . LEU   B  1  958  ? 15.754  48.147  102.072 1.00 19.97 ? 956  LEU   B CD1   1 
ATOM   15982 C  CD2   . LEU   B  1  958  ? 13.724  49.277  103.039 1.00 22.06 ? 956  LEU   B CD2   1 
ATOM   15983 N  N     . ASP   B  1  959  ? 17.257  52.499  102.300 1.00 18.65 ? 957  ASP   B N     1 
ATOM   15984 C  CA    . ASP   B  1  959  ? 17.319  53.373  101.132 1.00 18.97 ? 957  ASP   B CA    1 
ATOM   15985 C  C     . ASP   B  1  959  ? 18.714  53.381  100.517 1.00 17.87 ? 957  ASP   B C     1 
ATOM   15986 O  O     . ASP   B  1  959  ? 18.857  53.350  99.290  1.00 17.89 ? 957  ASP   B O     1 
ATOM   15987 C  CB    . ASP   B  1  959  ? 16.882  54.789  101.494 1.00 18.57 ? 957  ASP   B CB    1 
ATOM   15988 C  CG    . ASP   B  1  959  ? 16.423  55.568  100.285 1.00 20.57 ? 957  ASP   B CG    1 
ATOM   15989 O  OD1   . ASP   B  1  959  ? 15.706  54.984  99.446  1.00 19.27 ? 957  ASP   B OD1   1 
ATOM   15990 O  OD2   . ASP   B  1  959  ? 16.758  56.761  100.170 1.00 23.12 ? 957  ASP   B OD2   1 
ATOM   15991 N  N     . ARG   B  1  960  ? 19.750  53.444  101.353 1.00 17.24 ? 958  ARG   B N     1 
ATOM   15992 C  CA    . ARG   B  1  960  ? 21.119  53.383  100.858 1.00 16.88 ? 958  ARG   B CA    1 
ATOM   15993 C  C     . ARG   B  1  960  ? 21.403  52.041  100.203 1.00 19.34 ? 958  ARG   B C     1 
ATOM   15994 O  O     . ARG   B  1  960  ? 22.156  51.968  99.228  1.00 18.08 ? 958  ARG   B O     1 
ATOM   15995 C  CB    . ARG   B  1  960  ? 22.095  53.614  102.015 1.00 21.49 ? 958  ARG   B CB    1 
ATOM   15996 N  N     . LEU   B  1  961  ? 20.842  50.962  100.747 1.00 16.50 ? 959  LEU   B N     1 
ATOM   15997 C  CA    . LEU   B  1  961  ? 21.018  49.654  100.128 1.00 16.46 ? 959  LEU   B CA    1 
ATOM   15998 C  C     . LEU   B  1  961  ? 20.423  49.633  98.730  1.00 16.71 ? 959  LEU   B C     1 
ATOM   15999 O  O     . LEU   B  1  961  ? 21.029  49.093  97.798  1.00 16.88 ? 959  LEU   B O     1 
ATOM   16000 C  CB    . LEU   B  1  961  ? 20.371  48.574  100.991 1.00 18.74 ? 959  LEU   B CB    1 
ATOM   16001 C  CG    . LEU   B  1  961  ? 20.379  47.165  100.391 1.00 18.51 ? 959  LEU   B CG    1 
ATOM   16002 C  CD1   . LEU   B  1  961  ? 21.810  46.647  100.204 1.00 22.67 ? 959  LEU   B CD1   1 
ATOM   16003 C  CD2   . LEU   B  1  961  ? 19.556  46.200  101.234 1.00 20.32 ? 959  LEU   B CD2   1 
ATOM   16004 N  N     . VAL   B  1  962  ? 19.235  50.211  98.562  1.00 16.30 ? 960  VAL   B N     1 
ATOM   16005 C  CA    . VAL   B  1  962  ? 18.657  50.293  97.227  1.00 16.50 ? 960  VAL   B CA    1 
ATOM   16006 C  C     . VAL   B  1  962  ? 19.587  51.054  96.288  1.00 17.98 ? 960  VAL   B C     1 
ATOM   16007 O  O     . VAL   B  1  962  ? 19.783  50.652  95.135  1.00 17.51 ? 960  VAL   B O     1 
ATOM   16008 C  CB    . VAL   B  1  962  ? 17.259  50.922  97.282  1.00 16.93 ? 960  VAL   B CB    1 
ATOM   16009 C  CG1   . VAL   B  1  962  ? 16.762  51.183  95.883  1.00 20.37 ? 960  VAL   B CG1   1 
ATOM   16010 C  CG2   . VAL   B  1  962  ? 16.297  50.008  98.051  1.00 18.67 ? 960  VAL   B CG2   1 
ATOM   16011 N  N     . ASP   B  1  963  ? 20.175  52.159  96.766  1.00 17.66 ? 961  ASP   B N     1 
ATOM   16012 C  CA    . ASP   B  1  963  ? 21.179  52.862  95.965  1.00 19.25 ? 961  ASP   B CA    1 
ATOM   16013 C  C     . ASP   B  1  963  ? 22.314  51.937  95.571  1.00 20.20 ? 961  ASP   B C     1 
ATOM   16014 O  O     . ASP   B  1  963  ? 22.773  51.962  94.422  1.00 19.74 ? 961  ASP   B O     1 
ATOM   16015 C  CB    . ASP   B  1  963  ? 21.776  54.029  96.742  1.00 19.17 ? 961  ASP   B CB    1 
ATOM   16016 C  CG    . ASP   B  1  963  ? 20.835  55.164  96.890  1.00 23.40 ? 961  ASP   B CG    1 
ATOM   16017 O  OD1   . ASP   B  1  963  ? 19.871  55.226  96.108  1.00 27.13 ? 961  ASP   B OD1   1 
ATOM   16018 O  OD2   . ASP   B  1  963  ? 21.092  56.011  97.778  1.00 27.11 ? 961  ASP   B OD2   1 
ATOM   16019 N  N     . ASP   B  1  964  ? 22.806  51.143  96.527  1.00 19.40 ? 962  ASP   B N     1 
ATOM   16020 C  CA    . ASP   B  1  964  ? 23.900  50.220  96.249  1.00 19.67 ? 962  ASP   B CA    1 
ATOM   16021 C  C     . ASP   B  1  964  ? 23.513  49.229  95.167  1.00 21.10 ? 962  ASP   B C     1 
ATOM   16022 O  O     . ASP   B  1  964  ? 24.324  48.907  94.293  1.00 18.40 ? 962  ASP   B O     1 
ATOM   16023 C  CB    . ASP   B  1  964  ? 24.290  49.468  97.520  1.00 19.46 ? 962  ASP   B CB    1 
ATOM   16024 C  CG    . ASP   B  1  964  ? 24.953  50.358  98.548  1.00 25.46 ? 962  ASP   B CG    1 
ATOM   16025 O  OD1   . ASP   B  1  964  ? 25.268  51.524  98.220  1.00 25.41 ? 962  ASP   B OD1   1 
ATOM   16026 O  OD2   . ASP   B  1  964  ? 25.143  49.891  99.694  1.00 31.83 ? 962  ASP   B OD2   1 
ATOM   16027 N  N     . VAL   B  1  965  ? 22.272  48.742  95.203  1.00 16.25 ? 963  VAL   B N     1 
ATOM   16028 C  CA    . VAL   B  1  965  ? 21.821  47.823  94.164  1.00 14.21 ? 963  VAL   B CA    1 
ATOM   16029 C  C     . VAL   B  1  965  ? 21.793  48.534  92.820  1.00 17.10 ? 963  VAL   B C     1 
ATOM   16030 O  O     . VAL   B  1  965  ? 22.278  48.010  91.809  1.00 18.73 ? 963  VAL   B O     1 
ATOM   16031 C  CB    . VAL   B  1  965  ? 20.452  47.220  94.526  1.00 16.81 ? 963  VAL   B CB    1 
ATOM   16032 C  CG1   . VAL   B  1  965  ? 19.916  46.390  93.357  1.00 16.30 ? 963  VAL   B CG1   1 
ATOM   16033 C  CG2   . VAL   B  1  965  ? 20.581  46.360  95.774  1.00 17.93 ? 963  VAL   B CG2   1 
ATOM   16034 N  N     . ASN   B  1  966  ? 21.246  49.746  92.791  1.00 16.70 ? 964  ASN   B N     1 
ATOM   16035 C  CA    . ASN   B  1  966  ? 21.186  50.487  91.534  1.00 17.41 ? 964  ASN   B CA    1 
ATOM   16036 C  C     . ASN   B  1  966  ? 22.575  50.864  91.043  1.00 18.67 ? 964  ASN   B C     1 
ATOM   16037 O  O     . ASN   B  1  966  ? 22.784  51.023  89.834  1.00 21.05 ? 964  ASN   B O     1 
ATOM   16038 C  CB    . ASN   B  1  966  ? 20.361  51.758  91.704  1.00 16.89 ? 964  ASN   B CB    1 
ATOM   16039 C  CG    . ASN   B  1  966  ? 18.871  51.488  91.878  1.00 18.16 ? 964  ASN   B CG    1 
ATOM   16040 O  OD1   . ASN   B  1  966  ? 18.351  50.457  91.461  1.00 18.57 ? 964  ASN   B OD1   1 
ATOM   16041 N  ND2   . ASN   B  1  966  ? 18.186  52.430  92.505  1.00 18.48 ? 964  ASN   B ND2   1 
ATOM   16042 N  N     . ALA   B  1  967  ? 23.531  51.015  91.961  1.00 16.30 ? 965  ALA   B N     1 
ATOM   16043 C  CA    . ALA   B  1  967  ? 24.834  51.554  91.607  1.00 18.25 ? 965  ALA   B CA    1 
ATOM   16044 C  C     . ALA   B  1  967  ? 25.650  50.621  90.730  1.00 18.02 ? 965  ALA   B C     1 
ATOM   16045 O  O     . ALA   B  1  967  ? 26.659  51.066  90.171  1.00 21.23 ? 965  ALA   B O     1 
ATOM   16046 C  CB    . ALA   B  1  967  ? 25.630  51.846  92.879  1.00 21.74 ? 965  ALA   B CB    1 
ATOM   16047 N  N     . THR   B  1  968  ? 25.273  49.343  90.616  1.00 16.38 ? 966  THR   B N     1 
ATOM   16048 C  CA    . THR   B  1  968  ? 26.017  48.454  89.733  1.00 18.07 ? 966  THR   B CA    1 
ATOM   16049 C  C     . THR   B  1  968  ? 25.870  48.854  88.275  1.00 19.09 ? 966  THR   B C     1 
ATOM   16050 O  O     . THR   B  1  968  ? 26.701  48.458  87.449  1.00 20.15 ? 966  THR   B O     1 
ATOM   16051 C  CB    . THR   B  1  968  ? 25.531  47.010  89.862  1.00 17.27 ? 966  THR   B CB    1 
ATOM   16052 O  OG1   . THR   B  1  968  ? 24.234  46.890  89.258  1.00 18.71 ? 966  THR   B OG1   1 
ATOM   16053 C  CG2   . THR   B  1  968  ? 25.477  46.576  91.316  1.00 19.78 ? 966  THR   B CG2   1 
ATOM   16054 N  N     . GLY   B  1  969  ? 24.826  49.617  87.943  1.00 18.32 ? 967  GLY   B N     1 
ATOM   16055 C  CA    . GLY   B  1  969  ? 24.524  49.967  86.579  1.00 18.86 ? 967  GLY   B CA    1 
ATOM   16056 C  C     . GLY   B  1  969  ? 23.622  48.979  85.884  1.00 17.81 ? 967  GLY   B C     1 
ATOM   16057 O  O     . GLY   B  1  969  ? 23.084  49.294  84.816  1.00 18.07 ? 967  GLY   B O     1 
ATOM   16058 N  N     . TYR   B  1  970  ? 23.439  47.795  86.461  1.00 17.12 ? 968  TYR   B N     1 
ATOM   16059 C  CA    . TYR   B  1  970  ? 22.507  46.822  85.927  1.00 15.71 ? 968  TYR   B CA    1 
ATOM   16060 C  C     . TYR   B  1  970  ? 21.095  47.133  86.410  1.00 16.41 ? 968  TYR   B C     1 
ATOM   16061 O  O     . TYR   B  1  970  ? 20.874  47.949  87.308  1.00 17.71 ? 968  TYR   B O     1 
ATOM   16062 C  CB    . TYR   B  1  970  ? 22.926  45.429  86.386  1.00 15.69 ? 968  TYR   B CB    1 
ATOM   16063 C  CG    . TYR   B  1  970  ? 24.158  44.934  85.673  1.00 19.53 ? 968  TYR   B CG    1 
ATOM   16064 C  CD1   . TYR   B  1  970  ? 24.055  44.434  84.387  1.00 21.21 ? 968  TYR   B CD1   1 
ATOM   16065 C  CD2   . TYR   B  1  970  ? 25.412  44.972  86.276  1.00 20.60 ? 968  TYR   B CD2   1 
ATOM   16066 C  CE1   . TYR   B  1  970  ? 25.159  43.971  83.704  1.00 23.74 ? 968  TYR   B CE1   1 
ATOM   16067 C  CE2   . TYR   B  1  970  ? 26.537  44.497  85.593  1.00 23.40 ? 968  TYR   B CE2   1 
ATOM   16068 C  CZ    . TYR   B  1  970  ? 26.386  44.004  84.305  1.00 27.32 ? 968  TYR   B CZ    1 
ATOM   16069 O  OH    . TYR   B  1  970  ? 27.461  43.527  83.587  1.00 35.15 ? 968  TYR   B OH    1 
ATOM   16070 N  N     . GLY   B  1  971  ? 20.127  46.466  85.805  1.00 14.32 ? 969  GLY   B N     1 
ATOM   16071 C  CA    . GLY   B  1  971  ? 18.757  46.685  86.204  1.00 14.75 ? 969  GLY   B CA    1 
ATOM   16072 C  C     . GLY   B  1  971  ? 17.844  45.678  85.554  1.00 14.11 ? 969  GLY   B C     1 
ATOM   16073 O  O     . GLY   B  1  971  ? 16.914  46.041  84.830  1.00 15.29 ? 969  GLY   B O     1 
ATOM   16074 N  N     . LEU   B  1  972  ? 18.102  44.400  85.820  1.00 12.83 ? 970  LEU   B N     1 
ATOM   16075 C  CA    . LEU   B  1  972  ? 17.349  43.329  85.185  1.00 12.49 ? 970  LEU   B CA    1 
ATOM   16076 C  C     . LEU   B  1  972  ? 16.262  42.832  86.134  1.00 13.73 ? 970  LEU   B C     1 
ATOM   16077 O  O     . LEU   B  1  972  ? 15.139  43.327  86.079  1.00 15.34 ? 970  LEU   B O     1 
ATOM   16078 C  CB    . LEU   B  1  972  ? 18.285  42.234  84.671  1.00 14.50 ? 970  LEU   B CB    1 
ATOM   16079 C  CG    . LEU   B  1  972  ? 17.639  41.157  83.819  1.00 14.81 ? 970  LEU   B CG    1 
ATOM   16080 C  CD1   . LEU   B  1  972  ? 16.867  41.779  82.649  1.00 16.67 ? 970  LEU   B CD1   1 
ATOM   16081 C  CD2   . LEU   B  1  972  ? 18.707  40.189  83.321  1.00 16.93 ? 970  LEU   B CD2   1 
ATOM   16082 N  N     . THR   B  1  973  ? 16.563  41.865  86.995  1.00 13.00 ? 971  THR   B N     1 
ATOM   16083 C  CA    . THR   B  1  973  ? 15.556  41.395  87.931  1.00 11.94 ? 971  THR   B CA    1 
ATOM   16084 C  C     . THR   B  1  973  ? 15.879  41.892  89.328  1.00 11.51 ? 971  THR   B C     1 
ATOM   16085 O  O     . THR   B  1  973  ? 17.031  42.171  89.666  1.00 13.65 ? 971  THR   B O     1 
ATOM   16086 C  CB    . THR   B  1  973  ? 15.444  39.865  87.936  1.00 13.38 ? 971  THR   B CB    1 
ATOM   16087 O  OG1   . THR   B  1  973  ? 16.701  39.292  88.298  1.00 13.21 ? 971  THR   B OG1   1 
ATOM   16088 C  CG2   . THR   B  1  973  ? 15.017  39.378  86.571  1.00 14.95 ? 971  THR   B CG2   1 
ATOM   16089 N  N     . PHE   B  1  974  ? 14.833  41.962  90.147  1.00 13.13 ? 972  PHE   B N     1 
ATOM   16090 C  CA    . PHE   B  1  974  ? 14.982  42.370  91.531  1.00 12.96 ? 972  PHE   B CA    1 
ATOM   16091 C  C     . PHE   B  1  974  ? 13.851  41.763  92.344  1.00 11.92 ? 972  PHE   B C     1 
ATOM   16092 O  O     . PHE   B  1  974  ? 12.692  41.799  91.930  1.00 12.85 ? 972  PHE   B O     1 
ATOM   16093 C  CB    . PHE   B  1  974  ? 14.945  43.895  91.657  1.00 12.48 ? 972  PHE   B CB    1 
ATOM   16094 C  CG    . PHE   B  1  974  ? 14.860  44.352  93.074  1.00 13.10 ? 972  PHE   B CG    1 
ATOM   16095 C  CD1   . PHE   B  1  974  ? 16.013  44.441  93.838  1.00 15.35 ? 972  PHE   B CD1   1 
ATOM   16096 C  CD2   . PHE   B  1  974  ? 13.629  44.667  93.644  1.00 13.92 ? 972  PHE   B CD2   1 
ATOM   16097 C  CE1   . PHE   B  1  974  ? 15.947  44.838  95.157  1.00 15.28 ? 972  PHE   B CE1   1 
ATOM   16098 C  CE2   . PHE   B  1  974  ? 13.546  45.060  94.956  1.00 14.51 ? 972  PHE   B CE2   1 
ATOM   16099 C  CZ    . PHE   B  1  974  ? 14.708  45.146  95.716  1.00 15.62 ? 972  PHE   B CZ    1 
ATOM   16100 N  N     . GLY   B  1  975  ? 14.182  41.239  93.516  1.00 12.24 ? 973  GLY   B N     1 
ATOM   16101 C  CA    . GLY   B  1  975  ? 13.194  40.653  94.399  1.00 13.49 ? 973  GLY   B CA    1 
ATOM   16102 C  C     . GLY   B  1  975  ? 13.128  41.361  95.738  1.00 13.50 ? 973  GLY   B C     1 
ATOM   16103 O  O     . GLY   B  1  975  ? 14.122  41.869  96.242  1.00 14.66 ? 973  GLY   B O     1 
ATOM   16104 N  N     . LEU   B  1  976  ? 11.947  41.343  96.326  1.00 13.89 ? 974  LEU   B N     1 
ATOM   16105 C  CA    . LEU   B  1  976  ? 11.750  41.893  97.655  1.00 14.17 ? 974  LEU   B CA    1 
ATOM   16106 C  C     . LEU   B  1  976  ? 10.859  40.923  98.405  1.00 15.42 ? 974  LEU   B C     1 
ATOM   16107 O  O     . LEU   B  1  976  ? 9.772   40.585  97.928  1.00 15.44 ? 974  LEU   B O     1 
ATOM   16108 C  CB    . LEU   B  1  976  ? 11.096  43.269  97.544  1.00 15.53 ? 974  LEU   B CB    1 
ATOM   16109 C  CG    . LEU   B  1  976  ? 10.682  43.886  98.878  1.00 17.59 ? 974  LEU   B CG    1 
ATOM   16110 C  CD1   . LEU   B  1  976  ? 11.916  44.195  99.726  1.00 17.52 ? 974  LEU   B CD1   1 
ATOM   16111 C  CD2   . LEU   B  1  976  ? 9.848   45.135  98.621  1.00 17.25 ? 974  LEU   B CD2   1 
ATOM   16112 N  N     . HIS   B  1  977  ? 11.322  40.457  99.560  1.00 14.90 ? 975  HIS   B N     1 
ATOM   16113 C  CA    . HIS   B  1  977  ? 10.506  39.643  100.452 1.00 16.39 ? 975  HIS   B CA    1 
ATOM   16114 C  C     . HIS   B  1  977  ? 10.206  40.462  101.697 1.00 14.69 ? 975  HIS   B C     1 
ATOM   16115 O  O     . HIS   B  1  977  ? 11.110  40.778  102.480 1.00 15.93 ? 975  HIS   B O     1 
ATOM   16116 C  CB    . HIS   B  1  977  ? 11.190  38.334  100.818 1.00 15.56 ? 975  HIS   B CB    1 
ATOM   16117 C  CG    . HIS   B  1  977  ? 10.922  37.227  99.851  1.00 17.51 ? 975  HIS   B CG    1 
ATOM   16118 N  ND1   . HIS   B  1  977  ? 10.120  36.149  100.158 1.00 24.56 ? 975  HIS   B ND1   1 
ATOM   16119 C  CD2   . HIS   B  1  977  ? 11.353  37.030  98.586  1.00 22.96 ? 975  HIS   B CD2   1 
ATOM   16120 C  CE1   . HIS   B  1  977  ? 10.079  35.329  99.125  1.00 21.44 ? 975  HIS   B CE1   1 
ATOM   16121 N  NE2   . HIS   B  1  977  ? 10.816  35.843  98.157  1.00 23.39 ? 975  HIS   B NE2   1 
ATOM   16122 N  N     . THR   B  1  978  ? 8.940   40.807  101.855 1.00 14.66 ? 976  THR   B N     1 
ATOM   16123 C  CA    . THR   B  1  978  ? 8.462   41.568  102.996 1.00 15.97 ? 976  THR   B CA    1 
ATOM   16124 C  C     . THR   B  1  978  ? 6.956   41.421  103.041 1.00 16.56 ? 976  THR   B C     1 
ATOM   16125 O  O     . THR   B  1  978  ? 6.303   41.238  102.015 1.00 19.10 ? 976  THR   B O     1 
ATOM   16126 C  CB    . THR   B  1  978  ? 8.814   43.052  102.879 1.00 19.21 ? 976  THR   B CB    1 
ATOM   16127 O  OG1   . THR   B  1  978  ? 8.307   43.752  104.022 1.00 17.36 ? 976  THR   B OG1   1 
ATOM   16128 C  CG2   . THR   B  1  978  ? 8.182   43.646  101.648 1.00 20.29 ? 976  THR   B CG2   1 
ATOM   16129 N  N     . ARG   B  1  979  ? 6.415   41.509  104.239 1.00 17.91 ? 977  ARG   B N     1 
ATOM   16130 C  CA    . ARG   B  1  979  ? 4.975   41.568  104.380 1.00 17.78 ? 977  ARG   B CA    1 
ATOM   16131 C  C     . ARG   B  1  979  ? 4.458   42.991  104.507 1.00 18.78 ? 977  ARG   B C     1 
ATOM   16132 O  O     . ARG   B  1  979  ? 3.247   43.183  104.623 1.00 19.86 ? 977  ARG   B O     1 
ATOM   16133 C  CB    . ARG   B  1  979  ? 4.544   40.738  105.584 1.00 23.88 ? 977  ARG   B CB    1 
ATOM   16134 C  CG    . ARG   B  1  979  ? 4.738   39.267  105.342 1.00 28.42 ? 977  ARG   B CG    1 
ATOM   16135 C  CD    . ARG   B  1  979  ? 4.660   38.506  106.635 1.00 34.80 ? 977  ARG   B CD    1 
ATOM   16136 N  NE    . ARG   B  1  979  ? 4.576   37.072  106.402 1.00 41.90 ? 977  ARG   B NE    1 
ATOM   16137 C  CZ    . ARG   B  1  979  ? 4.392   36.178  107.362 1.00 44.69 ? 977  ARG   B CZ    1 
ATOM   16138 N  NH1   . ARG   B  1  979  ? 4.277   36.543  108.630 1.00 36.90 ? 977  ARG   B NH1   1 
ATOM   16139 N  NH2   . ARG   B  1  979  ? 4.316   34.888  107.042 1.00 42.57 ? 977  ARG   B NH2   1 
ATOM   16140 N  N     . LEU   B  1  980  ? 5.335   43.991  104.473 1.00 17.16 ? 978  LEU   B N     1 
ATOM   16141 C  CA    . LEU   B  1  980  ? 4.991   45.343  104.901 1.00 17.16 ? 978  LEU   B CA    1 
ATOM   16142 C  C     . LEU   B  1  980  ? 4.793   46.251  103.698 1.00 17.34 ? 978  LEU   B C     1 
ATOM   16143 O  O     . LEU   B  1  980  ? 5.737   46.500  102.941 1.00 17.36 ? 978  LEU   B O     1 
ATOM   16144 C  CB    . LEU   B  1  980  ? 6.095   45.900  105.794 1.00 17.00 ? 978  LEU   B CB    1 
ATOM   16145 C  CG    . LEU   B  1  980  ? 6.446   45.029  106.991 1.00 20.69 ? 978  LEU   B CG    1 
ATOM   16146 C  CD1   . LEU   B  1  980  ? 7.567   45.710  107.785 1.00 21.00 ? 978  LEU   B CD1   1 
ATOM   16147 C  CD2   . LEU   B  1  980  ? 5.222   44.797  107.851 1.00 20.38 ? 978  LEU   B CD2   1 
ATOM   16148 N  N     . ASP   B  1  981  ? 3.578   46.785  103.557 1.00 17.34 ? 979  ASP   B N     1 
ATOM   16149 C  CA    . ASP   B  1  981  ? 3.259   47.614  102.400 1.00 18.23 ? 979  ASP   B CA    1 
ATOM   16150 C  C     . ASP   B  1  981  ? 4.159   48.840  102.304 1.00 17.37 ? 979  ASP   B C     1 
ATOM   16151 O  O     . ASP   B  1  981  ? 4.481   49.284  101.197 1.00 17.19 ? 979  ASP   B O     1 
ATOM   16152 C  CB    . ASP   B  1  981  ? 1.804   48.065  102.460 1.00 18.74 ? 979  ASP   B CB    1 
ATOM   16153 C  CG    . ASP   B  1  981  ? 0.830   46.963  102.151 1.00 22.08 ? 979  ASP   B CG    1 
ATOM   16154 O  OD1   . ASP   B  1  981  ? 1.228   45.930  101.572 1.00 23.94 ? 979  ASP   B OD1   1 
ATOM   16155 O  OD2   . ASP   B  1  981  ? -0.363  47.162  102.485 1.00 25.73 ? 979  ASP   B OD2   1 
ATOM   16156 N  N     . GLU   B  1  982  ? 4.534   49.437  103.435 1.00 17.65 ? 980  GLU   B N     1 
ATOM   16157 C  CA    . GLU   B  1  982  ? 5.392   50.618  103.366 1.00 18.50 ? 980  GLU   B CA    1 
ATOM   16158 C  C     . GLU   B  1  982  ? 6.744   50.260  102.779 1.00 18.11 ? 980  GLU   B C     1 
ATOM   16159 O  O     . GLU   B  1  982  ? 7.314   51.023  101.993 1.00 18.90 ? 980  GLU   B O     1 
ATOM   16160 C  CB    . GLU   B  1  982  ? 5.577   51.256  104.742 1.00 20.65 ? 980  GLU   B CB    1 
ATOM   16161 C  CG    . GLU   B  1  982  ? 6.460   52.497  104.699 1.00 22.78 ? 980  GLU   B CG    1 
ATOM   16162 C  CD    . GLU   B  1  982  ? 6.986   52.905  106.062 1.00 29.60 ? 980  GLU   B CD    1 
ATOM   16163 O  OE1   . GLU   B  1  982  ? 7.304   52.008  106.876 1.00 36.55 ? 980  GLU   B OE1   1 
ATOM   16164 O  OE2   . GLU   B  1  982  ? 7.085   54.122  106.321 1.00 27.15 ? 980  GLU   B OE2   1 
ATOM   16165 N  N     . THR   B  1  983  ? 7.270   49.097  103.147 1.00 16.94 ? 981  THR   B N     1 
ATOM   16166 C  CA    . THR   B  1  983  ? 8.545   48.671  102.591 1.00 16.81 ? 981  THR   B CA    1 
ATOM   16167 C  C     . THR   B  1  983  ? 8.413   48.365  101.104 1.00 16.93 ? 981  THR   B C     1 
ATOM   16168 O  O     . THR   B  1  983  ? 9.302   48.709  100.308 1.00 17.24 ? 981  THR   B O     1 
ATOM   16169 C  CB    . THR   B  1  983  ? 9.045   47.461  103.376 1.00 18.16 ? 981  THR   B CB    1 
ATOM   16170 O  OG1   . THR   B  1  983  ? 9.270   47.853  104.737 1.00 19.69 ? 981  THR   B OG1   1 
ATOM   16171 C  CG2   . THR   B  1  983  ? 10.339  46.937  102.768 1.00 17.59 ? 981  THR   B CG2   1 
ATOM   16172 N  N     . ILE   B  1  984  ? 7.293   47.752  100.702 1.00 15.29 ? 982  ILE   B N     1 
ATOM   16173 C  CA    . ILE   B  1  984  ? 7.062   47.487  99.285  1.00 16.81 ? 982  ILE   B CA    1 
ATOM   16174 C  C     . ILE   B  1  984  ? 7.015   48.791  98.511  1.00 17.10 ? 982  ILE   B C     1 
ATOM   16175 O  O     . ILE   B  1  984  ? 7.646   48.932  97.454  1.00 18.13 ? 982  ILE   B O     1 
ATOM   16176 C  CB    . ILE   B  1  984  ? 5.768   46.681  99.095  1.00 16.65 ? 982  ILE   B CB    1 
ATOM   16177 C  CG1   . ILE   B  1  984  ? 5.938   45.282  99.685  1.00 20.15 ? 982  ILE   B CG1   1 
ATOM   16178 C  CG2   . ILE   B  1  984  ? 5.425   46.570  97.620  1.00 18.59 ? 982  ILE   B CG2   1 
ATOM   16179 C  CD1   . ILE   B  1  984  ? 4.641   44.533  99.808  1.00 18.53 ? 982  ILE   B CD1   1 
ATOM   16180 N  N     . ALA   B  1  985  ? 6.279   49.771  99.036  1.00 16.87 ? 983  ALA   B N     1 
ATOM   16181 C  CA    . ALA   B  1  985  ? 6.147   51.046  98.336  1.00 18.00 ? 983  ALA   B CA    1 
ATOM   16182 C  C     . ALA   B  1  985  ? 7.491   51.743  98.245  1.00 16.91 ? 983  ALA   B C     1 
ATOM   16183 O  O     . ALA   B  1  985  ? 7.872   52.225  97.174  1.00 17.79 ? 983  ALA   B O     1 
ATOM   16184 C  CB    . ALA   B  1  985  ? 5.118   51.940  99.030  1.00 19.24 ? 983  ALA   B CB    1 
ATOM   16185 N  N     . HIS   B  1  986  ? 8.232   51.769  99.349  1.00 17.43 ? 984  HIS   B N     1 
ATOM   16186 C  CA    . HIS   B  1  986  ? 9.539   52.415  99.361  1.00 18.05 ? 984  HIS   B CA    1 
ATOM   16187 C  C     . HIS   B  1  986  ? 10.461  51.753  98.353  1.00 17.24 ? 984  HIS   B C     1 
ATOM   16188 O  O     . HIS   B  1  986  ? 10.983  52.402  97.443  1.00 17.54 ? 984  HIS   B O     1 
ATOM   16189 C  CB    . HIS   B  1  986  ? 10.125  52.341  100.774 1.00 18.42 ? 984  HIS   B CB    1 
ATOM   16190 C  CG    . HIS   B  1  986  ? 11.517  52.885  100.899 1.00 22.61 ? 984  HIS   B CG    1 
ATOM   16191 N  ND1   . HIS   B  1  986  ? 12.144  53.015  102.119 1.00 28.42 ? 984  HIS   B ND1   1 
ATOM   16192 C  CD2   . HIS   B  1  986  ? 12.400  53.334  99.975  1.00 22.77 ? 984  HIS   B CD2   1 
ATOM   16193 C  CE1   . HIS   B  1  986  ? 13.354  53.517  101.940 1.00 25.98 ? 984  HIS   B CE1   1 
ATOM   16194 N  NE2   . HIS   B  1  986  ? 13.538  53.711  100.647 1.00 24.43 ? 984  HIS   B NE2   1 
ATOM   16195 N  N     . VAL   B  1  987  ? 10.641  50.445  98.478  1.00 14.29 ? 985  VAL   B N     1 
ATOM   16196 C  CA    . VAL   B  1  987  ? 11.646  49.777  97.662  1.00 17.52 ? 985  VAL   B CA    1 
ATOM   16197 C  C     . VAL   B  1  987  ? 11.270  49.804  96.187  1.00 17.92 ? 985  VAL   B C     1 
ATOM   16198 O  O     . VAL   B  1  987  ? 12.112  50.091  95.333  1.00 18.16 ? 985  VAL   B O     1 
ATOM   16199 C  CB    . VAL   B  1  987  ? 11.912  48.362  98.189  1.00 16.59 ? 985  VAL   B CB    1 
ATOM   16200 C  CG1   . VAL   B  1  987  ? 12.793  47.596  97.214  1.00 19.04 ? 985  VAL   B CG1   1 
ATOM   16201 C  CG2   . VAL   B  1  987  ? 12.575  48.450  99.569  1.00 16.43 ? 985  VAL   B CG2   1 
ATOM   16202 N  N     . THR   B  1  988  ? 10.008  49.528  95.856  1.00 16.72 ? 986  THR   B N     1 
ATOM   16203 C  CA    . THR   B  1  988  ? 9.648   49.507  94.440  1.00 17.93 ? 986  THR   B CA    1 
ATOM   16204 C  C     . THR   B  1  988  ? 9.677   50.901  93.824  1.00 19.17 ? 986  THR   B C     1 
ATOM   16205 O  O     . THR   B  1  988  ? 9.874   51.027  92.613  1.00 24.59 ? 986  THR   B O     1 
ATOM   16206 C  CB    . THR   B  1  988  ? 8.299   48.824  94.202  1.00 20.65 ? 986  THR   B CB    1 
ATOM   16207 O  OG1   . THR   B  1  988  ? 7.269   49.541  94.879  1.00 22.25 ? 986  THR   B OG1   1 
ATOM   16208 C  CG2   . THR   B  1  988  ? 8.339   47.395  94.692  1.00 19.77 ? 986  THR   B CG2   1 
ATOM   16209 N  N     . SER   B  1  989  ? 9.506   51.950  94.628  1.00 18.82 ? 987  SER   B N     1 
ATOM   16210 C  CA    . SER   B  1  989  ? 9.616   53.305  94.095  1.00 20.71 ? 987  SER   B CA    1 
ATOM   16211 C  C     . SER   B  1  989  ? 11.062  53.716  93.824  1.00 23.86 ? 987  SER   B C     1 
ATOM   16212 O  O     . SER   B  1  989  ? 11.288  54.637  93.032  1.00 26.22 ? 987  SER   B O     1 
ATOM   16213 C  CB    . SER   B  1  989  ? 8.926   54.317  95.017  1.00 23.81 ? 987  SER   B CB    1 
ATOM   16214 O  OG    . SER   B  1  989  ? 9.668   54.559  96.203  1.00 27.80 ? 987  SER   B OG    1 
ATOM   16215 N  N     . ARG   B  1  990  ? 12.040  53.059  94.444  1.00 17.56 ? 988  ARG   B N     1 
ATOM   16216 C  CA    . ARG   B  1  990  ? 13.433  53.488  94.372  1.00 16.54 ? 988  ARG   B CA    1 
ATOM   16217 C  C     . ARG   B  1  990  ? 14.322  52.563  93.557  1.00 17.62 ? 988  ARG   B C     1 
ATOM   16218 O  O     . ARG   B  1  990  ? 15.333  53.013  93.015  1.00 18.14 ? 988  ARG   B O     1 
ATOM   16219 C  CB    . ARG   B  1  990  ? 14.024  53.614  95.784  1.00 20.62 ? 988  ARG   B CB    1 
ATOM   16220 C  CG    . ARG   B  1  990  ? 13.201  54.480  96.718  1.00 26.29 ? 988  ARG   B CG    1 
ATOM   16221 C  CD    . ARG   B  1  990  ? 13.399  55.949  96.454  1.00 25.79 ? 988  ARG   B CD    1 
ATOM   16222 N  NE    . ARG   B  1  990  ? 14.514  56.487  97.223  1.00 21.78 ? 988  ARG   B NE    1 
ATOM   16223 C  CZ    . ARG   B  1  990  ? 14.911  57.749  97.154  1.00 21.90 ? 988  ARG   B CZ    1 
ATOM   16224 N  NH1   . ARG   B  1  990  ? 14.353  58.599  96.311  1.00 23.73 ? 988  ARG   B NH1   1 
ATOM   16225 N  NH2   . ARG   B  1  990  ? 15.887  58.170  97.952  1.00 23.16 ? 988  ARG   B NH2   1 
ATOM   16226 N  N     . ILE   B  1  991  ? 13.967  51.285  93.450  1.00 15.87 ? 989  ILE   B N     1 
ATOM   16227 C  CA    . ILE   B  1  991  ? 14.772  50.358  92.671  1.00 15.59 ? 989  ILE   B CA    1 
ATOM   16228 C  C     . ILE   B  1  991  ? 14.596  50.659  91.188  1.00 17.05 ? 989  ILE   B C     1 
ATOM   16229 O  O     . ILE   B  1  991  ? 13.528  51.095  90.734  1.00 18.04 ? 989  ILE   B O     1 
ATOM   16230 C  CB    . ILE   B  1  991  ? 14.345  48.920  93.012  1.00 16.72 ? 989  ILE   B CB    1 
ATOM   16231 C  CG1   . ILE   B  1  991  ? 15.378  47.914  92.522  1.00 20.94 ? 989  ILE   B CG1   1 
ATOM   16232 C  CG2   . ILE   B  1  991  ? 12.996  48.612  92.404  1.00 19.18 ? 989  ILE   B CG2   1 
ATOM   16233 C  CD1   . ILE   B  1  991  ? 16.693  48.026  93.269  1.00 22.51 ? 989  ILE   B CD1   1 
ATOM   16234 N  N     . LYS   B  1  992  ? 15.655  50.449  90.421  1.00 16.47 ? 990  LYS   B N     1 
ATOM   16235 C  CA    . LYS   B  1  992  ? 15.628  50.730  88.985  1.00 16.62 ? 990  LYS   B CA    1 
ATOM   16236 C  C     . LYS   B  1  992  ? 15.936  49.427  88.263  1.00 18.17 ? 990  LYS   B C     1 
ATOM   16237 O  O     . LYS   B  1  992  ? 17.055  49.208  87.809  1.00 21.51 ? 990  LYS   B O     1 
ATOM   16238 C  CB    . LYS   B  1  992  ? 16.631  51.797  88.647  1.00 17.12 ? 990  LYS   B CB    1 
ATOM   16239 C  CG    . LYS   B  1  992  ? 16.356  53.120  89.360  1.00 22.11 ? 990  LYS   B CG    1 
ATOM   16240 C  CD    . LYS   B  1  992  ? 17.491  54.103  89.102  1.00 31.60 ? 990  LYS   B CD    1 
ATOM   16241 C  CE    . LYS   B  1  992  ? 17.688  54.363  87.614  1.00 33.54 ? 990  LYS   B CE    1 
ATOM   16242 N  NZ    . LYS   B  1  992  ? 18.931  55.150  87.353  1.00 42.01 ? 990  LYS   B NZ    1 
ATOM   16243 N  N     . ALA   B  1  993  ? 14.943  48.555  88.178  1.00 17.21 ? 991  ALA   B N     1 
ATOM   16244 C  CA    . ALA   B  1  993  ? 15.091  47.289  87.479  1.00 14.35 ? 991  ALA   B CA    1 
ATOM   16245 C  C     . ALA   B  1  993  ? 13.848  47.050  86.637  1.00 15.58 ? 991  ALA   B C     1 
ATOM   16246 O  O     . ALA   B  1  993  ? 12.756  47.543  86.947  1.00 16.09 ? 991  ALA   B O     1 
ATOM   16247 C  CB    . ALA   B  1  993  ? 15.344  46.102  88.432  1.00 18.26 ? 991  ALA   B CB    1 
ATOM   16248 N  N     . GLY   B  1  994  ? 14.027  46.285  85.559  1.00 14.19 ? 992  GLY   B N     1 
ATOM   16249 C  CA    . GLY   B  1  994  ? 12.922  46.094  84.644  1.00 14.18 ? 992  GLY   B CA    1 
ATOM   16250 C  C     . GLY   B  1  994  ? 11.913  45.058  85.077  1.00 13.59 ? 992  GLY   B C     1 
ATOM   16251 O  O     . GLY   B  1  994  ? 10.772  45.104  84.620  1.00 13.69 ? 992  GLY   B O     1 
ATOM   16252 N  N     . ASN   B  1  995  ? 12.311  44.108  85.920  1.00 13.62 ? 993  ASN   B N     1 
ATOM   16253 C  CA    . ASN   B  1  995  ? 11.438  43.027  86.358  1.00 13.34 ? 993  ASN   B CA    1 
ATOM   16254 C  C     . ASN   B  1  995  ? 11.547  42.932  87.867  1.00 13.05 ? 993  ASN   B C     1 
ATOM   16255 O  O     . ASN   B  1  995  ? 12.615  42.609  88.393  1.00 13.87 ? 993  ASN   B O     1 
ATOM   16256 C  CB    . ASN   B  1  995  ? 11.838  41.714  85.694  1.00 13.81 ? 993  ASN   B CB    1 
ATOM   16257 C  CG    . ASN   B  1  995  ? 11.289  41.603  84.296  1.00 14.86 ? 993  ASN   B CG    1 
ATOM   16258 O  OD1   . ASN   B  1  995  ? 11.888  42.097  83.344  1.00 14.01 ? 993  ASN   B OD1   1 
ATOM   16259 N  ND2   . ASN   B  1  995  ? 10.124  40.994  84.171  1.00 14.62 ? 993  ASN   B ND2   1 
ATOM   16260 N  N     . LEU   B  1  996  ? 10.458  43.248  88.545  1.00 14.20 ? 994  LEU   B N     1 
ATOM   16261 C  CA    . LEU   B  1  996  ? 10.382  43.226  89.994  1.00 12.88 ? 994  LEU   B CA    1 
ATOM   16262 C  C     . LEU   B  1  996  ? 9.525   42.049  90.411  1.00 13.16 ? 994  LEU   B C     1 
ATOM   16263 O  O     . LEU   B  1  996  ? 8.560   41.695  89.730  1.00 13.06 ? 994  LEU   B O     1 
ATOM   16264 C  CB    . LEU   B  1  996  ? 9.746   44.507  90.518  1.00 13.07 ? 994  LEU   B CB    1 
ATOM   16265 C  CG    . LEU   B  1  996  ? 10.293  45.787  89.897  1.00 15.11 ? 994  LEU   B CG    1 
ATOM   16266 C  CD1   . LEU   B  1  996  ? 9.592   46.987  90.538  1.00 17.75 ? 994  LEU   B CD1   1 
ATOM   16267 C  CD2   . LEU   B  1  996  ? 11.800  45.880  90.080  1.00 14.94 ? 994  LEU   B CD2   1 
ATOM   16268 N  N     . TYR   B  1  997  ? 9.867   41.464  91.549  1.00 12.08 ? 995  TYR   B N     1 
ATOM   16269 C  CA    . TYR   B  1  997  ? 9.177   40.289  92.056  1.00 13.68 ? 995  TYR   B CA    1 
ATOM   16270 C  C     . TYR   B  1  997  ? 9.026   40.461  93.549  1.00 12.43 ? 995  TYR   B C     1 
ATOM   16271 O  O     . TYR   B  1  997  ? 10.008  40.727  94.242  1.00 15.13 ? 995  TYR   B O     1 
ATOM   16272 C  CB    . TYR   B  1  997  ? 9.963   39.011  91.779  1.00 14.70 ? 995  TYR   B CB    1 
ATOM   16273 C  CG    . TYR   B  1  997  ? 10.326  38.840  90.330  1.00 13.20 ? 995  TYR   B CG    1 
ATOM   16274 C  CD1   . TYR   B  1  997  ? 11.461  39.446  89.811  1.00 13.64 ? 995  TYR   B CD1   1 
ATOM   16275 C  CD2   . TYR   B  1  997  ? 9.518   38.096  89.475  1.00 15.54 ? 995  TYR   B CD2   1 
ATOM   16276 C  CE1   . TYR   B  1  997  ? 11.792  39.310  88.500  1.00 16.46 ? 995  TYR   B CE1   1 
ATOM   16277 C  CE2   . TYR   B  1  997  ? 9.852   37.939  88.149  1.00 14.96 ? 995  TYR   B CE2   1 
ATOM   16278 C  CZ    . TYR   B  1  997  ? 10.991  38.561  87.674  1.00 16.53 ? 995  TYR   B CZ    1 
ATOM   16279 O  OH    . TYR   B  1  997  ? 11.350  38.430  86.354  1.00 19.12 ? 995  TYR   B OH    1 
ATOM   16280 N  N     . ILE   B  1  998  ? 7.802   40.330  94.043  1.00 13.97 ? 996  ILE   B N     1 
ATOM   16281 C  CA    A ILE   B  1  998  ? 7.496   40.538  95.454  0.58 14.31 ? 996  ILE   B CA    1 
ATOM   16282 C  CA    B ILE   B  1  998  ? 7.509   40.530  95.455  0.42 14.33 ? 996  ILE   B CA    1 
ATOM   16283 C  C     . ILE   B  1  998  ? 7.048   39.207  96.046  1.00 13.89 ? 996  ILE   B C     1 
ATOM   16284 O  O     . ILE   B  1  998  ? 6.038   38.640  95.610  1.00 14.71 ? 996  ILE   B O     1 
ATOM   16285 C  CB    A ILE   B  1  998  ? 6.408   41.603  95.642  0.58 16.25 ? 996  ILE   B CB    1 
ATOM   16286 C  CB    B ILE   B  1  998  ? 6.473   41.641  95.665  0.42 16.24 ? 996  ILE   B CB    1 
ATOM   16287 C  CG1   A ILE   B  1  998  ? 6.733   42.870  94.839  0.58 17.22 ? 996  ILE   B CG1   1 
ATOM   16288 C  CG1   B ILE   B  1  998  ? 7.092   42.983  95.273  0.42 16.93 ? 996  ILE   B CG1   1 
ATOM   16289 C  CG2   A ILE   B  1  998  ? 6.221   41.910  97.130  0.58 16.35 ? 996  ILE   B CG2   1 
ATOM   16290 C  CG2   B ILE   B  1  998  ? 5.978   41.647  97.113  0.42 16.24 ? 996  ILE   B CG2   1 
ATOM   16291 C  CD1   A ILE   B  1  998  ? 7.962   43.605  95.300  0.58 17.47 ? 996  ILE   B CD1   1 
ATOM   16292 C  CD1   B ILE   B  1  998  ? 6.104   44.081  95.080  0.42 18.64 ? 996  ILE   B CD1   1 
ATOM   16293 N  N     . ASN   B  1  999  ? 7.801   38.718  97.032  1.00 13.25 ? 997  ASN   B N     1 
ATOM   16294 C  CA    . ASN   B  1  999  ? 7.441   37.523  97.790  1.00 14.67 ? 997  ASN   B CA    1 
ATOM   16295 C  C     . ASN   B  1  999  ? 7.402   36.268  96.926  1.00 14.94 ? 997  ASN   B C     1 
ATOM   16296 O  O     . ASN   B  1  999  ? 6.577   35.373  97.126  1.00 15.56 ? 997  ASN   B O     1 
ATOM   16297 C  CB    . ASN   B  1  999  ? 6.148   37.734  98.566  1.00 15.13 ? 997  ASN   B CB    1 
ATOM   16298 C  CG    . ASN   B  1  999  ? 6.322   38.749  99.658  1.00 15.37 ? 997  ASN   B CG    1 
ATOM   16299 O  OD1   . ASN   B  1  999  ? 7.405   38.859  100.230 1.00 17.33 ? 997  ASN   B OD1   1 
ATOM   16300 N  ND2   . ASN   B  1  999  ? 5.275   39.510  99.950  1.00 16.82 ? 997  ASN   B ND2   1 
ATOM   16301 N  N     . ARG   B  1  1000 ? 8.327   36.189  95.978  1.00 14.30 ? 998  ARG   B N     1 
ATOM   16302 C  CA    . ARG   B  1  1000 ? 8.443   35.037  95.092  1.00 12.98 ? 998  ARG   B CA    1 
ATOM   16303 C  C     . ARG   B  1  1000 ? 9.869   35.000  94.566  1.00 15.64 ? 998  ARG   B C     1 
ATOM   16304 O  O     . ARG   B  1  1000 ? 10.688  35.858  94.891  1.00 16.57 ? 998  ARG   B O     1 
ATOM   16305 C  CB    . ARG   B  1  1000 ? 7.439   35.132  93.941  1.00 14.92 ? 998  ARG   B CB    1 
ATOM   16306 C  CG    . ARG   B  1  1000 ? 7.478   36.477  93.233  1.00 14.82 ? 998  ARG   B CG    1 
ATOM   16307 C  CD    . ARG   B  1  1000 ? 6.959   36.338  91.819  1.00 13.95 ? 998  ARG   B CD    1 
ATOM   16308 N  NE    . ARG   B  1  1000 ? 7.831   35.472  91.039  1.00 13.66 ? 998  ARG   B NE    1 
ATOM   16309 C  CZ    . ARG   B  1  1000 ? 7.519   35.012  89.838  1.00 15.70 ? 998  ARG   B CZ    1 
ATOM   16310 N  NH1   . ARG   B  1  1000 ? 6.384   35.348  89.245  1.00 15.90 ? 998  ARG   B NH1   1 
ATOM   16311 N  NH2   . ARG   B  1  1000 ? 8.362   34.199  89.215  1.00 17.83 ? 998  ARG   B NH2   1 
ATOM   16312 N  N     . ASN   B  1  1001 ? 10.160  33.990  93.750  1.00 13.58 ? 999  ASN   B N     1 
ATOM   16313 C  CA    . ASN   B  1  1001 ? 11.465  33.943  93.116  1.00 13.42 ? 999  ASN   B CA    1 
ATOM   16314 C  C     . ASN   B  1  1001 ? 11.577  35.072  92.094  1.00 13.99 ? 999  ASN   B C     1 
ATOM   16315 O  O     . ASN   B  1  1001 ? 10.588  35.707  91.729  1.00 15.46 ? 999  ASN   B O     1 
ATOM   16316 C  CB    . ASN   B  1  1001 ? 11.717  32.562  92.494  1.00 13.71 ? 999  ASN   B CB    1 
ATOM   16317 C  CG    . ASN   B  1  1001 ? 10.851  32.283  91.278  1.00 16.85 ? 999  ASN   B CG    1 
ATOM   16318 O  OD1   . ASN   B  1  1001 ? 10.751  33.089  90.360  1.00 17.52 ? 999  ASN   B OD1   1 
ATOM   16319 N  ND2   . ASN   B  1  1001 ? 10.223  31.118  91.270  1.00 24.87 ? 999  ASN   B ND2   1 
ATOM   16320 N  N     . ILE   B  1  1002 ? 12.790  35.296  91.597  1.00 13.96 ? 1000 ILE   B N     1 
ATOM   16321 C  CA    . ILE   B  1  1002 ? 13.034  36.412  90.687  1.00 13.82 ? 1000 ILE   B CA    1 
ATOM   16322 C  C     . ILE   B  1  1002 ? 13.342  35.951  89.270  1.00 15.71 ? 1000 ILE   B C     1 
ATOM   16323 O  O     . ILE   B  1  1002 ? 13.948  36.691  88.503  1.00 16.35 ? 1000 ILE   B O     1 
ATOM   16324 C  CB    . ILE   B  1  1002 ? 14.101  37.389  91.208  1.00 15.03 ? 1000 ILE   B CB    1 
ATOM   16325 C  CG1   . ILE   B  1  1002 ? 15.504  36.758  91.257  1.00 13.44 ? 1000 ILE   B CG1   1 
ATOM   16326 C  CG2   . ILE   B  1  1002 ? 13.702  37.943  92.563  1.00 16.60 ? 1000 ILE   B CG2   1 
ATOM   16327 C  CD1   . ILE   B  1  1002 ? 16.608  37.777  91.477  1.00 15.47 ? 1000 ILE   B CD1   1 
ATOM   16328 N  N     . ILE   B  1  1003 ? 12.937  34.745  88.901  1.00 15.94 ? 1001 ILE   B N     1 
ATOM   16329 C  CA    . ILE   B  1  1003 ? 13.290  34.235  87.585  1.00 16.57 ? 1001 ILE   B CA    1 
ATOM   16330 C  C     . ILE   B  1  1003 ? 12.089  34.173  86.649  1.00 19.34 ? 1001 ILE   B C     1 
ATOM   16331 O  O     . ILE   B  1  1003 ? 12.181  33.595  85.559  1.00 20.24 ? 1001 ILE   B O     1 
ATOM   16332 C  CB    . ILE   B  1  1003 ? 14.042  32.908  87.686  1.00 17.13 ? 1001 ILE   B CB    1 
ATOM   16333 C  CG1   . ILE   B  1  1003 ? 13.206  31.879  88.433  1.00 24.83 ? 1001 ILE   B CG1   1 
ATOM   16334 C  CG2   . ILE   B  1  1003 ? 15.359  33.137  88.429  1.00 17.89 ? 1001 ILE   B CG2   1 
ATOM   16335 C  CD1   . ILE   B  1  1003 ? 13.826  30.534  88.416  1.00 30.79 ? 1001 ILE   B CD1   1 
ATOM   16336 N  N     . GLY   B  1  1004 ? 10.971  34.786  87.032  1.00 18.51 ? 1002 GLY   B N     1 
ATOM   16337 C  CA    . GLY   B  1  1004 ? 9.776   34.727  86.209  1.00 18.75 ? 1002 GLY   B CA    1 
ATOM   16338 C  C     . GLY   B  1  1004 ? 9.907   35.550  84.939  1.00 19.15 ? 1002 GLY   B C     1 
ATOM   16339 O  O     . GLY   B  1  1004 ? 10.207  36.750  84.974  1.00 19.71 ? 1002 GLY   B O     1 
ATOM   16340 N  N     . ALA   B  1  1005 ? 9.657   34.907  83.809  1.00 17.05 ? 1003 ALA   B N     1 
ATOM   16341 C  CA    . ALA   B  1  1005 ? 9.662   35.585  82.528  1.00 18.15 ? 1003 ALA   B CA    1 
ATOM   16342 C  C     . ALA   B  1  1005 ? 8.513   35.068  81.690  1.00 19.03 ? 1003 ALA   B C     1 
ATOM   16343 O  O     . ALA   B  1  1005 ? 8.640   34.895  80.473  1.00 20.00 ? 1003 ALA   B O     1 
ATOM   16344 C  CB    . ALA   B  1  1005 ? 10.998  35.398  81.803  1.00 20.14 ? 1003 ALA   B CB    1 
ATOM   16345 N  N     . VAL   B  1  1006 ? 7.368   34.818  82.330  1.00 15.89 ? 1004 VAL   B N     1 
ATOM   16346 C  CA    . VAL   B  1  1006 ? 6.224   34.283  81.604  1.00 15.66 ? 1004 VAL   B CA    1 
ATOM   16347 C  C     . VAL   B  1  1006 ? 5.819   35.273  80.523  1.00 14.40 ? 1004 VAL   B C     1 
ATOM   16348 O  O     . VAL   B  1  1006 ? 5.543   36.444  80.803  1.00 15.04 ? 1004 VAL   B O     1 
ATOM   16349 C  CB    . VAL   B  1  1006 ? 5.072   33.953  82.558  1.00 16.07 ? 1004 VAL   B CB    1 
ATOM   16350 C  CG1   . VAL   B  1  1006 ? 3.851   33.487  81.752  1.00 17.55 ? 1004 VAL   B CG1   1 
ATOM   16351 C  CG2   . VAL   B  1  1006 ? 5.489   32.860  83.523  1.00 17.82 ? 1004 VAL   B CG2   1 
ATOM   16352 N  N     . VAL   B  1  1007 ? 5.825   34.805  79.273  1.00 16.44 ? 1005 VAL   B N     1 
ATOM   16353 C  CA    . VAL   B  1  1007 ? 5.572   35.683  78.138  1.00 16.04 ? 1005 VAL   B CA    1 
ATOM   16354 C  C     . VAL   B  1  1007 ? 4.210   36.350  78.279  1.00 16.89 ? 1005 VAL   B C     1 
ATOM   16355 O  O     . VAL   B  1  1007 ? 3.200   35.699  78.568  1.00 15.84 ? 1005 VAL   B O     1 
ATOM   16356 C  CB    . VAL   B  1  1007 ? 5.654   34.864  76.849  1.00 14.75 ? 1005 VAL   B CB    1 
ATOM   16357 C  CG1   . VAL   B  1  1007 ? 5.276   35.725  75.681  1.00 17.24 ? 1005 VAL   B CG1   1 
ATOM   16358 C  CG2   . VAL   B  1  1007 ? 7.058   34.318  76.670  1.00 16.89 ? 1005 VAL   B CG2   1 
ATOM   16359 N  N     . GLY   B  1  1008 ? 4.171   37.658  78.052  1.00 14.54 ? 1006 GLY   B N     1 
ATOM   16360 C  CA    . GLY   B  1  1008 ? 2.922   38.376  78.150  1.00 17.64 ? 1006 GLY   B CA    1 
ATOM   16361 C  C     . GLY   B  1  1008 ? 2.381   38.513  79.553  1.00 17.04 ? 1006 GLY   B C     1 
ATOM   16362 O  O     . GLY   B  1  1008 ? 1.289   39.072  79.721  1.00 18.69 ? 1006 GLY   B O     1 
ATOM   16363 N  N     . VAL   B  1  1009 ? 3.093   38.006  80.559  1.00 14.84 ? 1007 VAL   B N     1 
ATOM   16364 C  CA    . VAL   B  1  1009 ? 2.671   38.085  81.953  1.00 15.60 ? 1007 VAL   B CA    1 
ATOM   16365 C  C     . VAL   B  1  1009 ? 3.711   38.807  82.796  1.00 16.63 ? 1007 VAL   B C     1 
ATOM   16366 O  O     . VAL   B  1  1009 ? 3.397   39.760  83.513  1.00 16.40 ? 1007 VAL   B O     1 
ATOM   16367 C  CB    . VAL   B  1  1009 ? 2.363   36.682  82.528  1.00 15.35 ? 1007 VAL   B CB    1 
ATOM   16368 C  CG1   . VAL   B  1  1009 ? 1.890   36.775  83.983  1.00 16.77 ? 1007 VAL   B CG1   1 
ATOM   16369 C  CG2   . VAL   B  1  1009 ? 1.304   35.988  81.658  1.00 16.49 ? 1007 VAL   B CG2   1 
ATOM   16370 N  N     . GLN   B  1  1010 ? 4.969   38.384  82.691  1.00 15.46 ? 1008 GLN   B N     1 
ATOM   16371 C  CA    . GLN   B  1  1010 ? 6.130   39.182  83.083  1.00 16.66 ? 1008 GLN   B CA    1 
ATOM   16372 C  C     . GLN   B  1  1010 ? 6.943   39.461  81.824  1.00 16.19 ? 1008 GLN   B C     1 
ATOM   16373 O  O     . GLN   B  1  1010 ? 7.975   38.816  81.603  1.00 18.36 ? 1008 GLN   B O     1 
ATOM   16374 C  CB    . GLN   B  1  1010 ? 7.020   38.473  84.105  1.00 16.82 ? 1008 GLN   B CB    1 
ATOM   16375 C  CG    . GLN   B  1  1010 ? 6.334   38.118  85.398  1.00 19.65 ? 1008 GLN   B CG    1 
ATOM   16376 C  CD    . GLN   B  1  1010 ? 5.923   36.662  85.452  1.00 17.04 ? 1008 GLN   B CD    1 
ATOM   16377 O  OE1   . GLN   B  1  1010 ? 6.621   35.782  84.954  1.00 17.28 ? 1008 GLN   B OE1   1 
ATOM   16378 N  NE2   . GLN   B  1  1010 ? 4.777   36.403  86.069  1.00 17.54 ? 1008 GLN   B NE2   1 
ATOM   16379 N  N     . PRO   B  1  1011 ? 6.512   40.406  80.983  1.00 14.53 ? 1009 PRO   B N     1 
ATOM   16380 C  CA    . PRO   B  1  1011 ? 7.376   40.881  79.895  1.00 16.73 ? 1009 PRO   B CA    1 
ATOM   16381 C  C     . PRO   B  1  1011 ? 8.748   41.174  80.467  1.00 14.22 ? 1009 PRO   B C     1 
ATOM   16382 O  O     . PRO   B  1  1011 ? 8.888   41.834  81.501  1.00 14.05 ? 1009 PRO   B O     1 
ATOM   16383 C  CB    . PRO   B  1  1011 ? 6.684   42.167  79.434  1.00 16.06 ? 1009 PRO   B CB    1 
ATOM   16384 C  CG    . PRO   B  1  1011 ? 5.268   41.967  79.784  1.00 16.24 ? 1009 PRO   B CG    1 
ATOM   16385 C  CD    . PRO   B  1  1011 ? 5.281   41.204  81.085  1.00 16.09 ? 1009 PRO   B CD    1 
ATOM   16386 N  N     . PHE   B  1  1012 ? 9.760   40.644  79.819  1.00 13.43 ? 1010 PHE   B N     1 
ATOM   16387 C  CA    . PHE   B  1  1012 ? 11.039  40.501  80.476  1.00 13.78 ? 1010 PHE   B CA    1 
ATOM   16388 C  C     . PHE   B  1  1012 ? 12.078  41.381  79.808  1.00 15.91 ? 1010 PHE   B C     1 
ATOM   16389 O  O     . PHE   B  1  1012 ? 12.239  41.353  78.585  1.00 15.72 ? 1010 PHE   B O     1 
ATOM   16390 C  CB    . PHE   B  1  1012 ? 11.502  39.047  80.469  1.00 14.73 ? 1010 PHE   B CB    1 
ATOM   16391 C  CG    . PHE   B  1  1012 ? 12.729  38.837  81.283  1.00 12.96 ? 1010 PHE   B CG    1 
ATOM   16392 C  CD1   . PHE   B  1  1012 ? 12.631  38.665  82.648  1.00 15.74 ? 1010 PHE   B CD1   1 
ATOM   16393 C  CD2   . PHE   B  1  1012 ? 13.978  38.874  80.700  1.00 16.81 ? 1010 PHE   B CD2   1 
ATOM   16394 C  CE1   . PHE   B  1  1012 ? 13.757  38.494  83.411  1.00 14.48 ? 1010 PHE   B CE1   1 
ATOM   16395 C  CE2   . PHE   B  1  1012 ? 15.121  38.710  81.465  1.00 16.61 ? 1010 PHE   B CE2   1 
ATOM   16396 C  CZ    . PHE   B  1  1012 ? 15.005  38.517  82.822  1.00 15.69 ? 1010 PHE   B CZ    1 
ATOM   16397 N  N     . GLY   B  1  1013 ? 12.786  42.143  80.616  1.00 13.38 ? 1011 GLY   B N     1 
ATOM   16398 C  CA    . GLY   B  1  1013 ? 13.920  42.878  80.100  1.00 13.84 ? 1011 GLY   B CA    1 
ATOM   16399 C  C     . GLY   B  1  1013 ? 14.217  44.045  80.995  1.00 14.45 ? 1011 GLY   B C     1 
ATOM   16400 O  O     . GLY   B  1  1013 ? 13.316  44.567  81.661  1.00 15.21 ? 1011 GLY   B O     1 
ATOM   16401 N  N     . GLY   B  1  1014 ? 15.481  44.431  81.036  1.00 16.18 ? 1012 GLY   B N     1 
ATOM   16402 C  CA    . GLY   B  1  1014 ? 15.870  45.472  81.943  1.00 16.31 ? 1012 GLY   B CA    1 
ATOM   16403 C  C     . GLY   B  1  1014 ? 16.423  46.711  81.292  1.00 17.82 ? 1012 GLY   B C     1 
ATOM   16404 O  O     . GLY   B  1  1014 ? 16.328  46.901  80.077  1.00 19.19 ? 1012 GLY   B O     1 
ATOM   16405 N  N     . ARG   B  1  1015 ? 17.018  47.556  82.122  1.00 17.22 ? 1013 ARG   B N     1 
ATOM   16406 C  CA    . ARG   B  1  1015 ? 17.516  48.857  81.737  1.00 17.85 ? 1013 ARG   B CA    1 
ATOM   16407 C  C     . ARG   B  1  1015 ? 18.979  48.956  82.139  1.00 17.29 ? 1013 ARG   B C     1 
ATOM   16408 O  O     . ARG   B  1  1015 ? 19.562  48.032  82.721  1.00 16.18 ? 1013 ARG   B O     1 
ATOM   16409 C  CB    . ARG   B  1  1015 ? 16.725  49.966  82.449  1.00 17.65 ? 1013 ARG   B CB    1 
ATOM   16410 C  CG    . ARG   B  1  1015 ? 16.733  49.831  83.974  1.00 20.77 ? 1013 ARG   B CG    1 
ATOM   16411 C  CD    . ARG   B  1  1015 ? 16.664  51.189  84.687  1.00 23.21 ? 1013 ARG   B CD    1 
ATOM   16412 N  NE    . ARG   B  1  1015 ? 17.952  51.877  84.659  1.00 27.07 ? 1013 ARG   B NE    1 
ATOM   16413 C  CZ    . ARG   B  1  1015 ? 18.986  51.556  85.425  1.00 27.98 ? 1013 ARG   B CZ    1 
ATOM   16414 N  NH1   . ARG   B  1  1015 ? 18.925  50.553  86.291  1.00 24.09 ? 1013 ARG   B NH1   1 
ATOM   16415 N  NH2   . ARG   B  1  1015 ? 20.114  52.253  85.315  1.00 32.25 ? 1013 ARG   B NH2   1 
ATOM   16416 N  N     . GLY   B  1  1016 ? 19.568  50.109  81.855  1.00 17.01 ? 1014 GLY   B N     1 
ATOM   16417 C  CA    . GLY   B  1  1016 ? 20.967  50.287  82.191  1.00 16.23 ? 1014 GLY   B CA    1 
ATOM   16418 C  C     . GLY   B  1  1016 ? 21.817  49.310  81.403  1.00 17.49 ? 1014 GLY   B C     1 
ATOM   16419 O  O     . GLY   B  1  1016 ? 21.610  49.105  80.202  1.00 18.45 ? 1014 GLY   B O     1 
ATOM   16420 N  N     . LEU   B  1  1017 ? 22.776  48.686  82.086  1.00 16.46 ? 1015 LEU   B N     1 
ATOM   16421 C  CA    . LEU   B  1  1017 ? 23.626  47.681  81.473  1.00 18.12 ? 1015 LEU   B CA    1 
ATOM   16422 C  C     . LEU   B  1  1017 ? 22.872  46.410  81.138  1.00 16.83 ? 1015 LEU   B C     1 
ATOM   16423 O  O     . LEU   B  1  1017 ? 23.467  45.495  80.562  1.00 16.31 ? 1015 LEU   B O     1 
ATOM   16424 C  CB    . LEU   B  1  1017 ? 24.787  47.332  82.413  1.00 17.11 ? 1015 LEU   B CB    1 
ATOM   16425 C  CG    . LEU   B  1  1017 ? 25.693  48.508  82.761  1.00 19.55 ? 1015 LEU   B CG    1 
ATOM   16426 C  CD1   . LEU   B  1  1017 ? 26.725  48.070  83.788  1.00 20.44 ? 1015 LEU   B CD1   1 
ATOM   16427 C  CD2   . LEU   B  1  1017 ? 26.376  49.004  81.487  1.00 21.81 ? 1015 LEU   B CD2   1 
ATOM   16428 N  N     . SER   B  1  1018 ? 21.598  46.318  81.502  1.00 14.68 ? 1016 SER   B N     1 
ATOM   16429 C  CA    . SER   B  1  1018 ? 20.848  45.099  81.299  1.00 15.00 ? 1016 SER   B CA    1 
ATOM   16430 C  C     . SER   B  1  1018 ? 20.020  45.100  80.028  1.00 13.80 ? 1016 SER   B C     1 
ATOM   16431 O  O     . SER   B  1  1018 ? 19.519  44.041  79.653  1.00 17.07 ? 1016 SER   B O     1 
ATOM   16432 C  CB    . SER   B  1  1018 ? 19.905  44.857  82.487  1.00 14.75 ? 1016 SER   B CB    1 
ATOM   16433 O  OG    . SER   B  1  1018 ? 20.694  44.660  83.651  1.00 14.94 ? 1016 SER   B OG    1 
ATOM   16434 N  N     . GLY   B  1  1019 ? 19.843  46.226  79.358  1.00 14.19 ? 1017 GLY   B N     1 
ATOM   16435 C  CA    . GLY   B  1  1019 ? 19.035  46.159  78.163  1.00 15.07 ? 1017 GLY   B CA    1 
ATOM   16436 C  C     . GLY   B  1  1019 ? 18.845  47.501  77.512  1.00 14.94 ? 1017 GLY   B C     1 
ATOM   16437 O  O     . GLY   B  1  1019 ? 18.879  48.548  78.166  1.00 17.82 ? 1017 GLY   B O     1 
ATOM   16438 N  N     . THR   B  1  1020 ? 18.587  47.442  76.208  1.00 15.79 ? 1018 THR   B N     1 
ATOM   16439 C  CA    . THR   B  1  1020 ? 18.062  48.579  75.477  1.00 16.04 ? 1018 THR   B CA    1 
ATOM   16440 C  C     . THR   B  1  1020 ? 16.549  48.621  75.507  1.00 17.95 ? 1018 THR   B C     1 
ATOM   16441 O  O     . THR   B  1  1020 ? 15.968  49.696  75.327  1.00 17.76 ? 1018 THR   B O     1 
ATOM   16442 C  CB    . THR   B  1  1020 ? 18.469  48.475  74.004  1.00 17.72 ? 1018 THR   B CB    1 
ATOM   16443 O  OG1   . THR   B  1  1020 ? 17.983  47.234  73.463  1.00 15.44 ? 1018 THR   B OG1   1 
ATOM   16444 C  CG2   . THR   B  1  1020 ? 19.997  48.498  73.858  1.00 16.28 ? 1018 THR   B CG2   1 
ATOM   16445 N  N     . GLY   B  1  1021 ? 15.908  47.485  75.734  1.00 15.62 ? 1019 GLY   B N     1 
ATOM   16446 C  CA    . GLY   B  1  1021 ? 14.505  47.359  75.446  1.00 16.70 ? 1019 GLY   B CA    1 
ATOM   16447 C  C     . GLY   B  1  1021 ? 14.270  47.376  73.950  1.00 15.94 ? 1019 GLY   B C     1 
ATOM   16448 O  O     . GLY   B  1  1021 ? 15.195  47.527  73.150  1.00 16.20 ? 1019 GLY   B O     1 
ATOM   16449 N  N     . PRO   B  1  1022 ? 13.030  47.206  73.541  1.00 15.36 ? 1020 PRO   B N     1 
ATOM   16450 C  CA    . PRO   B  1  1022 ? 11.841  46.949  74.355  1.00 14.38 ? 1020 PRO   B CA    1 
ATOM   16451 C  C     . PRO   B  1  1022 ? 11.894  45.527  74.905  1.00 16.28 ? 1020 PRO   B C     1 
ATOM   16452 O  O     . PRO   B  1  1022 ? 12.678  44.683  74.453  1.00 17.09 ? 1020 PRO   B O     1 
ATOM   16453 C  CB    . PRO   B  1  1022 ? 10.699  47.124  73.345  1.00 17.39 ? 1020 PRO   B CB    1 
ATOM   16454 C  CG    . PRO   B  1  1022 ? 11.292  46.672  72.055  1.00 16.41 ? 1020 PRO   B CG    1 
ATOM   16455 C  CD    . PRO   B  1  1022 ? 12.712  47.198  72.102  1.00 16.12 ? 1020 PRO   B CD    1 
ATOM   16456 N  N     . LYS   B  1  1023 ? 11.053  45.249  75.895  1.00 14.23 ? 1021 LYS   B N     1 
ATOM   16457 C  CA    . LYS   B  1  1023 ? 11.057  43.937  76.522  1.00 14.97 ? 1021 LYS   B CA    1 
ATOM   16458 C  C     . LYS   B  1  1023 ? 10.586  42.859  75.563  1.00 14.97 ? 1021 LYS   B C     1 
ATOM   16459 O  O     . LYS   B  1  1023 ? 9.537   42.988  74.921  1.00 14.77 ? 1021 LYS   B O     1 
ATOM   16460 C  CB    . LYS   B  1  1023 ? 10.096  43.933  77.694  1.00 13.87 ? 1021 LYS   B CB    1 
ATOM   16461 C  CG    . LYS   B  1  1023 ? 10.545  44.726  78.899  1.00 14.24 ? 1021 LYS   B CG    1 
ATOM   16462 C  CD    . LYS   B  1  1023 ? 9.416   44.687  79.891  1.00 13.18 ? 1021 LYS   B CD    1 
ATOM   16463 C  CE    . LYS   B  1  1023 ? 9.813   45.192  81.259  1.00 16.12 ? 1021 LYS   B CE    1 
ATOM   16464 N  NZ    . LYS   B  1  1023 ? 10.582  44.174  82.011  1.00 15.55 ? 1021 LYS   B NZ    1 
ATOM   16465 N  N     . ALA   B  1  1024 ? 11.323  41.756  75.539  1.00 15.85 ? 1022 ALA   B N     1 
ATOM   16466 C  CA    . ALA   B  1  1024 ? 10.819  40.527  74.955  1.00 15.25 ? 1022 ALA   B CA    1 
ATOM   16467 C  C     . ALA   B  1  1024 ? 9.568   40.065  75.694  1.00 14.24 ? 1022 ALA   B C     1 
ATOM   16468 O  O     . ALA   B  1  1024 ? 9.411   40.272  76.903  1.00 14.96 ? 1022 ALA   B O     1 
ATOM   16469 C  CB    . ALA   B  1  1024 ? 11.906  39.450  75.032  1.00 16.81 ? 1022 ALA   B CB    1 
ATOM   16470 N  N     . GLY   B  1  1025 ? 8.654   39.447  74.953  1.00 12.48 ? 1023 GLY   B N     1 
ATOM   16471 C  CA    . GLY   B  1  1025 ? 7.444   38.960  75.579  1.00 15.17 ? 1023 GLY   B CA    1 
ATOM   16472 C  C     . GLY   B  1  1025 ? 6.532   40.067  76.031  1.00 13.83 ? 1023 GLY   B C     1 
ATOM   16473 O  O     . GLY   B  1  1025 ? 5.662   39.836  76.869  1.00 15.23 ? 1023 GLY   B O     1 
ATOM   16474 N  N     . GLY   B  1  1026 ? 6.716   41.265  75.490  1.00 15.99 ? 1024 GLY   B N     1 
ATOM   16475 C  CA    . GLY   B  1  1026 ? 5.908   42.410  75.838  1.00 13.80 ? 1024 GLY   B CA    1 
ATOM   16476 C  C     . GLY   B  1  1026 ? 5.397   43.071  74.575  1.00 14.24 ? 1024 GLY   B C     1 
ATOM   16477 O  O     . GLY   B  1  1026 ? 5.809   42.744  73.461  1.00 14.25 ? 1024 GLY   B O     1 
ATOM   16478 N  N     . PRO   B  1  1027 ? 4.479   44.021  74.736  1.00 15.15 ? 1025 PRO   B N     1 
ATOM   16479 C  CA    . PRO   B  1  1027 ? 3.721   44.536  73.588  1.00 14.03 ? 1025 PRO   B CA    1 
ATOM   16480 C  C     . PRO   B  1  1027 ? 4.467   45.560  72.756  1.00 13.92 ? 1025 PRO   B C     1 
ATOM   16481 O  O     . PRO   B  1  1027 ? 3.971   45.931  71.689  1.00 14.35 ? 1025 PRO   B O     1 
ATOM   16482 C  CB    . PRO   B  1  1027 ? 2.486   45.160  74.251  1.00 16.44 ? 1025 PRO   B CB    1 
ATOM   16483 C  CG    . PRO   B  1  1027 ? 2.978   45.550  75.612  1.00 17.71 ? 1025 PRO   B CG    1 
ATOM   16484 C  CD    . PRO   B  1  1027 ? 3.923   44.467  76.026  1.00 16.81 ? 1025 PRO   B CD    1 
ATOM   16485 N  N     . LEU   B  1  1028 ? 5.627   46.035  73.202  1.00 14.53 ? 1026 LEU   B N     1 
ATOM   16486 C  CA    . LEU   B  1  1028 ? 6.381   46.994  72.399  1.00 15.55 ? 1026 LEU   B CA    1 
ATOM   16487 C  C     . LEU   B  1  1028 ? 7.379   46.330  71.474  1.00 15.46 ? 1026 LEU   B C     1 
ATOM   16488 O  O     . LEU   B  1  1028 ? 7.971   47.012  70.633  1.00 16.69 ? 1026 LEU   B O     1 
ATOM   16489 C  CB    . LEU   B  1  1028 ? 7.152   47.967  73.296  1.00 15.25 ? 1026 LEU   B CB    1 
ATOM   16490 C  CG    . LEU   B  1  1028 ? 6.268   48.819  74.195  1.00 19.55 ? 1026 LEU   B CG    1 
ATOM   16491 C  CD1   . LEU   B  1  1028 ? 7.140   49.764  74.996  1.00 19.63 ? 1026 LEU   B CD1   1 
ATOM   16492 C  CD2   . LEU   B  1  1028 ? 5.281   49.577  73.360  1.00 23.55 ? 1026 LEU   B CD2   1 
ATOM   16493 N  N     . TYR   B  1  1029 ? 7.561   45.021  71.599  1.00 14.29 ? 1027 TYR   B N     1 
ATOM   16494 C  CA    . TYR   B  1  1029 ? 8.696   44.352  70.979  1.00 13.11 ? 1027 TYR   B CA    1 
ATOM   16495 C  C     . TYR   B  1  1029 ? 8.589   44.351  69.463  1.00 13.34 ? 1027 TYR   B C     1 
ATOM   16496 O  O     . TYR   B  1  1029 ? 9.554   44.684  68.769  1.00 13.85 ? 1027 TYR   B O     1 
ATOM   16497 C  CB    . TYR   B  1  1029 ? 8.702   42.922  71.480  1.00 15.00 ? 1027 TYR   B CB    1 
ATOM   16498 C  CG    . TYR   B  1  1029 ? 9.967   42.140  71.340  1.00 14.96 ? 1027 TYR   B CG    1 
ATOM   16499 C  CD1   . TYR   B  1  1029 ? 11.108  42.465  72.078  1.00 14.03 ? 1027 TYR   B CD1   1 
ATOM   16500 C  CD2   . TYR   B  1  1029 ? 9.997   41.000  70.555  1.00 15.40 ? 1027 TYR   B CD2   1 
ATOM   16501 C  CE1   . TYR   B  1  1029 ? 12.249  41.693  71.993  1.00 14.86 ? 1027 TYR   B CE1   1 
ATOM   16502 C  CE2   . TYR   B  1  1029 ? 11.124  40.216  70.484  1.00 14.43 ? 1027 TYR   B CE2   1 
ATOM   16503 C  CZ    . TYR   B  1  1029 ? 12.247  40.561  71.198  1.00 15.96 ? 1027 TYR   B CZ    1 
ATOM   16504 O  OH    . TYR   B  1  1029 ? 13.356  39.758  71.116  1.00 17.44 ? 1027 TYR   B OH    1 
ATOM   16505 N  N     . LEU   B  1  1030 ? 7.434   43.934  68.926  1.00 13.86 ? 1028 LEU   B N     1 
ATOM   16506 C  CA    . LEU   B  1  1030 ? 7.324   43.798  67.477  1.00 13.27 ? 1028 LEU   B CA    1 
ATOM   16507 C  C     . LEU   B  1  1030 ? 7.521   45.128  66.786  1.00 13.70 ? 1028 LEU   B C     1 
ATOM   16508 O  O     . LEU   B  1  1030 ? 8.044   45.172  65.668  1.00 14.67 ? 1028 LEU   B O     1 
ATOM   16509 C  CB    . LEU   B  1  1030 ? 5.975   43.197  67.083  1.00 14.99 ? 1028 LEU   B CB    1 
ATOM   16510 C  CG    . LEU   B  1  1030 ? 5.744   41.744  67.499  1.00 17.33 ? 1028 LEU   B CG    1 
ATOM   16511 C  CD1   . LEU   B  1  1030 ? 4.406   41.277  66.942  1.00 20.00 ? 1028 LEU   B CD1   1 
ATOM   16512 C  CD2   . LEU   B  1  1030 ? 6.880   40.838  67.007  1.00 18.85 ? 1028 LEU   B CD2   1 
ATOM   16513 N  N     . GLY   B  1  1031 ? 7.142   46.223  67.445  1.00 14.63 ? 1029 GLY   B N     1 
ATOM   16514 C  CA    . GLY   B  1  1031 ? 7.205   47.528  66.810  1.00 15.78 ? 1029 GLY   B CA    1 
ATOM   16515 C  C     . GLY   B  1  1031 ? 8.613   47.987  66.526  1.00 13.96 ? 1029 GLY   B C     1 
ATOM   16516 O  O     . GLY   B  1  1031 ? 8.815   48.888  65.706  1.00 17.29 ? 1029 GLY   B O     1 
ATOM   16517 N  N     . ARG   B  1  1032 ? 9.589   47.385  67.184  1.00 13.34 ? 1030 ARG   B N     1 
ATOM   16518 C  CA    . ARG   B  1  1032 ? 10.976  47.692  66.921  1.00 14.02 ? 1030 ARG   B CA    1 
ATOM   16519 C  C     . ARG   B  1  1032 ? 11.473  47.027  65.653  1.00 15.19 ? 1030 ARG   B C     1 
ATOM   16520 O  O     . ARG   B  1  1032 ? 12.538  47.400  65.147  1.00 17.70 ? 1030 ARG   B O     1 
ATOM   16521 C  CB    . ARG   B  1  1032 ? 11.798  47.233  68.128  1.00 15.08 ? 1030 ARG   B CB    1 
ATOM   16522 C  CG    . ARG   B  1  1032 ? 13.220  47.736  68.149  1.00 15.46 ? 1030 ARG   B CG    1 
ATOM   16523 C  CD    . ARG   B  1  1032 ? 13.260  49.253  68.298  1.00 16.76 ? 1030 ARG   B CD    1 
ATOM   16524 N  NE    . ARG   B  1  1032 ? 14.622  49.703  68.564  1.00 18.83 ? 1030 ARG   B NE    1 
ATOM   16525 C  CZ    . ARG   B  1  1032 ? 15.270  50.612  67.848  1.00 20.98 ? 1030 ARG   B CZ    1 
ATOM   16526 N  NH1   . ARG   B  1  1032 ? 14.691  51.235  66.832  1.00 22.35 ? 1030 ARG   B NH1   1 
ATOM   16527 N  NH2   . ARG   B  1  1032 ? 16.529  50.903  68.160  1.00 22.83 ? 1030 ARG   B NH2   1 
ATOM   16528 N  N     . LEU   B  1  1033 ? 10.724  46.059  65.130  1.00 15.18 ? 1031 LEU   B N     1 
ATOM   16529 C  CA    . LEU   B  1  1033 ? 11.174  45.241  64.015  1.00 14.81 ? 1031 LEU   B CA    1 
ATOM   16530 C  C     . LEU   B  1  1033 ? 10.486  45.624  62.716  1.00 14.62 ? 1031 LEU   B C     1 
ATOM   16531 O  O     . LEU   B  1  1033 ? 10.544  44.863  61.741  1.00 16.16 ? 1031 LEU   B O     1 
ATOM   16532 C  CB    . LEU   B  1  1033 ? 10.937  43.767  64.335  1.00 15.71 ? 1031 LEU   B CB    1 
ATOM   16533 C  CG    . LEU   B  1  1033 ? 11.481  43.387  65.714  1.00 15.37 ? 1031 LEU   B CG    1 
ATOM   16534 C  CD1   . LEU   B  1  1033 ? 11.105  41.957  66.063  1.00 15.62 ? 1031 LEU   B CD1   1 
ATOM   16535 C  CD2   . LEU   B  1  1033 ? 12.989  43.606  65.843  1.00 17.72 ? 1031 LEU   B CD2   1 
ATOM   16536 N  N     . VAL   B  1  1034 ? 9.824   46.777  62.695  1.00 15.59 ? 1032 VAL   B N     1 
ATOM   16537 C  CA    . VAL   B  1  1034 ? 9.196   47.334  61.506  1.00 17.32 ? 1032 VAL   B CA    1 
ATOM   16538 C  C     . VAL   B  1  1034 ? 9.639   48.786  61.410  1.00 18.02 ? 1032 VAL   B C     1 
ATOM   16539 O  O     . VAL   B  1  1034 ? 10.136  49.367  62.375  1.00 19.10 ? 1032 VAL   B O     1 
ATOM   16540 C  CB    . VAL   B  1  1034 ? 7.660   47.218  61.537  1.00 16.97 ? 1032 VAL   B CB    1 
ATOM   16541 C  CG1   . VAL   B  1  1034 ? 7.224   45.754  61.411  1.00 16.53 ? 1032 VAL   B CG1   1 
ATOM   16542 C  CG2   . VAL   B  1  1034 ? 7.118   47.803  62.835  1.00 15.73 ? 1032 VAL   B CG2   1 
ATOM   16543 N  N     . THR   B  1  1035 ? 9.498   49.364  60.216  1.00 19.35 ? 1033 THR   B N     1 
ATOM   16544 C  CA    . THR   B  1  1035 ? 9.997   50.718  60.022  1.00 22.25 ? 1033 THR   B CA    1 
ATOM   16545 C  C     . THR   B  1  1035 ? 9.068   51.778  60.587  1.00 22.13 ? 1033 THR   B C     1 
ATOM   16546 O  O     . THR   B  1  1035 ? 9.516   52.899  60.847  1.00 25.65 ? 1033 THR   B O     1 
ATOM   16547 C  CB    . THR   B  1  1035 ? 10.330  50.994  58.552  1.00 26.01 ? 1033 THR   B CB    1 
ATOM   16548 O  OG1   . THR   B  1  1035 ? 9.254   50.554  57.719  1.00 31.72 ? 1033 THR   B OG1   1 
ATOM   16549 C  CG2   . THR   B  1  1035 ? 11.605  50.265  58.156  1.00 29.82 ? 1033 THR   B CG2   1 
ATOM   16550 N  N     . THR   B  1  1036 ? 7.793   51.453  60.777  1.00 19.34 ? 1034 THR   B N     1 
ATOM   16551 C  CA    . THR   B  1  1036 ? 6.843   52.329  61.442  1.00 22.56 ? 1034 THR   B CA    1 
ATOM   16552 C  C     . THR   B  1  1036 ? 6.175   51.499  62.524  1.00 22.72 ? 1034 THR   B C     1 
ATOM   16553 O  O     . THR   B  1  1036 ? 5.556   50.477  62.223  1.00 20.44 ? 1034 THR   B O     1 
ATOM   16554 C  CB    . THR   B  1  1036 ? 5.784   52.818  60.458  1.00 26.71 ? 1034 THR   B CB    1 
ATOM   16555 O  OG1   . THR   B  1  1036 ? 6.423   53.417  59.325  1.00 32.13 ? 1034 THR   B OG1   1 
ATOM   16556 C  CG2   . THR   B  1  1036 ? 4.865   53.833  61.132  1.00 27.91 ? 1034 THR   B CG2   1 
ATOM   16557 N  N     . ALA   B  1  1037 ? 6.308   51.920  63.771  1.00 21.35 ? 1035 ALA   B N     1 
ATOM   16558 C  CA    . ALA   B  1  1037 ? 5.775   51.110  64.858  1.00 19.96 ? 1035 ALA   B CA    1 
ATOM   16559 C  C     . ALA   B  1  1037 ? 4.252   51.211  64.890  1.00 19.56 ? 1035 ALA   B C     1 
ATOM   16560 O  O     . ALA   B  1  1037 ? 3.691   52.298  64.724  1.00 21.02 ? 1035 ALA   B O     1 
ATOM   16561 C  CB    . ALA   B  1  1037 ? 6.346   51.569  66.199  1.00 21.96 ? 1035 ALA   B CB    1 
ATOM   16562 N  N     . PRO   B  1  1038 ? 3.561   50.106  65.100  1.00 16.14 ? 1036 PRO   B N     1 
ATOM   16563 C  CA    . PRO   B  1  1038 ? 2.115   50.163  65.323  1.00 16.83 ? 1036 PRO   B CA    1 
ATOM   16564 C  C     . PRO   B  1  1038 ? 1.827   50.612  66.746  1.00 17.57 ? 1036 PRO   B C     1 
ATOM   16565 O  O     . PRO   B  1  1038 ? 2.708   50.684  67.600  1.00 17.65 ? 1036 PRO   B O     1 
ATOM   16566 C  CB    . PRO   B  1  1038 ? 1.686   48.702  65.148  1.00 19.04 ? 1036 PRO   B CB    1 
ATOM   16567 C  CG    . PRO   B  1  1038 ? 2.854   47.939  65.651  1.00 21.21 ? 1036 PRO   B CG    1 
ATOM   16568 C  CD    . PRO   B  1  1038 ? 4.075   48.726  65.170  1.00 18.78 ? 1036 PRO   B CD    1 
ATOM   16569 N  N     . VAL   B  1  1039 ? 0.554   50.892  67.001  1.00 17.46 ? 1037 VAL   B N     1 
ATOM   16570 C  CA    . VAL   B  1  1039 ? 0.076   51.175  68.350  1.00 16.86 ? 1037 VAL   B CA    1 
ATOM   16571 C  C     . VAL   B  1  1039 ? -0.210  49.832  69.017  1.00 16.72 ? 1037 VAL   B C     1 
ATOM   16572 O  O     . VAL   B  1  1039 ? -1.127  49.123  68.578  1.00 17.33 ? 1037 VAL   B O     1 
ATOM   16573 C  CB    . VAL   B  1  1039 ? -1.184  52.040  68.312  1.00 19.15 ? 1037 VAL   B CB    1 
ATOM   16574 C  CG1   . VAL   B  1  1039 ? -1.667  52.263  69.741  1.00 20.25 ? 1037 VAL   B CG1   1 
ATOM   16575 C  CG2   . VAL   B  1  1039 ? -0.869  53.366  67.612  1.00 21.32 ? 1037 VAL   B CG2   1 
ATOM   16576 N  N     . PRO   B  1  1040 ? 0.531   49.444  70.047  1.00 17.08 ? 1038 PRO   B N     1 
ATOM   16577 C  CA    . PRO   B  1  1040 ? 0.315   48.133  70.648  1.00 17.10 ? 1038 PRO   B CA    1 
ATOM   16578 C  C     . PRO   B  1  1040 ? -1.031  48.069  71.343  1.00 17.66 ? 1038 PRO   B C     1 
ATOM   16579 O  O     . PRO   B  1  1040 ? -1.590  49.104  71.726  1.00 16.55 ? 1038 PRO   B O     1 
ATOM   16580 C  CB    . PRO   B  1  1040 ? 1.466   48.024  71.667  1.00 19.30 ? 1038 PRO   B CB    1 
ATOM   16581 C  CG    . PRO   B  1  1040 ? 2.482   49.016  71.191  1.00 21.19 ? 1038 PRO   B CG    1 
ATOM   16582 C  CD    . PRO   B  1  1040 ? 1.689   50.139  70.629  1.00 18.55 ? 1038 PRO   B CD    1 
ATOM   16583 N  N     . PRO   B  1  1041 ? -1.561  46.867  71.547  1.00 16.60 ? 1039 PRO   B N     1 
ATOM   16584 C  CA    . PRO   B  1  1041 ? -2.769  46.710  72.359  1.00 16.92 ? 1039 PRO   B CA    1 
ATOM   16585 C  C     . PRO   B  1  1041 ? -2.607  47.358  73.725  1.00 17.88 ? 1039 PRO   B C     1 
ATOM   16586 O  O     . PRO   B  1  1041 ? -1.547  47.275  74.356  1.00 19.17 ? 1039 PRO   B O     1 
ATOM   16587 C  CB    . PRO   B  1  1041 ? -2.921  45.190  72.483  1.00 19.16 ? 1039 PRO   B CB    1 
ATOM   16588 C  CG    . PRO   B  1  1041 ? -2.169  44.643  71.299  1.00 21.34 ? 1039 PRO   B CG    1 
ATOM   16589 C  CD    . PRO   B  1  1041 ? -1.021  45.575  71.086  1.00 21.09 ? 1039 PRO   B CD    1 
ATOM   16590 N  N     . GLN   B  1  1042 ? -3.659  48.044  74.155  1.00 18.34 ? 1040 GLN   B N     1 
ATOM   16591 C  CA    . GLN   B  1  1042 ? -3.742  48.650  75.478  1.00 19.25 ? 1040 GLN   B CA    1 
ATOM   16592 C  C     . GLN   B  1  1042 ? -2.721  49.758  75.697  1.00 17.87 ? 1040 GLN   B C     1 
ATOM   16593 O  O     . GLN   B  1  1042 ? -2.537  50.206  76.835  1.00 18.46 ? 1040 GLN   B O     1 
ATOM   16594 C  CB    . GLN   B  1  1042 ? -3.609  47.600  76.594  1.00 21.35 ? 1040 GLN   B CB    1 
ATOM   16595 C  CG    . GLN   B  1  1042 ? -4.650  46.499  76.532  1.00 25.05 ? 1040 GLN   B CG    1 
ATOM   16596 C  CD    . GLN   B  1  1042 ? -4.393  45.449  77.596  1.00 33.00 ? 1040 GLN   B CD    1 
ATOM   16597 O  OE1   . GLN   B  1  1042 ? -3.360  44.777  77.583  1.00 40.32 ? 1040 GLN   B OE1   1 
ATOM   16598 N  NE2   . GLN   B  1  1042 ? -5.310  45.334  78.542  1.00 41.24 ? 1040 GLN   B NE2   1 
ATOM   16599 N  N     . HIS   B  1  1043 ? -2.053  50.228  74.649  1.00 16.67 ? 1041 HIS   B N     1 
ATOM   16600 C  CA    . HIS   B  1  1043 ? -0.936  51.150  74.821  1.00 16.42 ? 1041 HIS   B CA    1 
ATOM   16601 C  C     . HIS   B  1  1043 ? -1.456  52.576  74.715  1.00 17.23 ? 1041 HIS   B C     1 
ATOM   16602 O  O     . HIS   B  1  1043 ? -1.565  53.150  73.629  1.00 19.56 ? 1041 HIS   B O     1 
ATOM   16603 C  CB    . HIS   B  1  1043 ? 0.132   50.867  73.772  1.00 17.59 ? 1041 HIS   B CB    1 
ATOM   16604 C  CG    . HIS   B  1  1043 ? 1.330   51.763  73.854  1.00 16.34 ? 1041 HIS   B CG    1 
ATOM   16605 N  ND1   . HIS   B  1  1043 ? 2.425   51.482  74.645  1.00 16.64 ? 1041 HIS   B ND1   1 
ATOM   16606 C  CD2   . HIS   B  1  1043 ? 1.618   52.924  73.216  1.00 18.92 ? 1041 HIS   B CD2   1 
ATOM   16607 C  CE1   . HIS   B  1  1043 ? 3.329   52.434  74.498  1.00 18.97 ? 1041 HIS   B CE1   1 
ATOM   16608 N  NE2   . HIS   B  1  1043 ? 2.870   53.317  73.631  1.00 17.69 ? 1041 HIS   B NE2   1 
ATOM   16609 N  N     . SER   B  1  1044 ? -1.778  53.156  75.865  1.00 15.52 ? 1042 SER   B N     1 
ATOM   16610 C  CA    . SER   B  1  1044 ? -2.225  54.538  75.950  1.00 17.73 ? 1042 SER   B CA    1 
ATOM   16611 C  C     . SER   B  1  1044 ? -2.166  54.929  77.413  1.00 16.52 ? 1042 SER   B C     1 
ATOM   16612 O  O     . SER   B  1  1044 ? -2.010  54.082  78.292  1.00 17.43 ? 1042 SER   B O     1 
ATOM   16613 C  CB    . SER   B  1  1044 ? -3.652  54.711  75.418  1.00 16.65 ? 1042 SER   B CB    1 
ATOM   16614 O  OG    . SER   B  1  1044 ? -4.577  54.109  76.306  1.00 19.43 ? 1042 SER   B OG    1 
ATOM   16615 N  N     . SER   B  1  1045 ? -2.309  56.219  77.660  1.00 15.97 ? 1043 SER   B N     1 
ATOM   16616 C  CA    . SER   B  1  1045 ? -2.358  56.736  79.017  1.00 15.25 ? 1043 SER   B CA    1 
ATOM   16617 C  C     . SER   B  1  1045 ? -3.216  57.985  79.026  1.00 16.43 ? 1043 SER   B C     1 
ATOM   16618 O  O     . SER   B  1  1045 ? -3.160  58.786  78.096  1.00 17.93 ? 1043 SER   B O     1 
ATOM   16619 C  CB    . SER   B  1  1045 ? -0.929  57.088  79.462  1.00 15.93 ? 1043 SER   B CB    1 
ATOM   16620 O  OG    . SER   B  1  1045 ? -0.945  57.709  80.737  1.00 18.37 ? 1043 SER   B OG    1 
ATOM   16621 N  N     . VAL   B  1  1046 ? -4.002  58.165  80.092  1.00 16.52 ? 1044 VAL   B N     1 
ATOM   16622 C  CA    . VAL   B  1  1046 ? -4.780  59.396  80.213  1.00 17.48 ? 1044 VAL   B CA    1 
ATOM   16623 C  C     . VAL   B  1  1046 ? -3.975  60.518  80.837  1.00 18.33 ? 1044 VAL   B C     1 
ATOM   16624 O  O     . VAL   B  1  1046 ? -4.456  61.658  80.911  1.00 19.57 ? 1044 VAL   B O     1 
ATOM   16625 C  CB    . VAL   B  1  1046 ? -6.079  59.171  81.011  1.00 22.26 ? 1044 VAL   B CB    1 
ATOM   16626 C  CG1   . VAL   B  1  1046 ? -6.943  58.144  80.293  1.00 24.41 ? 1044 VAL   B CG1   1 
ATOM   16627 C  CG2   . VAL   B  1  1046 ? -5.752  58.727  82.424  1.00 19.61 ? 1044 VAL   B CG2   1 
ATOM   16628 N  N     . HIS   B  1  1047 ? -2.748  60.227  81.254  1.00 18.59 ? 1045 HIS   B N     1 
ATOM   16629 C  CA    A HIS   B  1  1047 ? -1.936  61.216  81.923  0.50 19.69 ? 1045 HIS   B CA    1 
ATOM   16630 C  CA    B HIS   B  1  1047 ? -1.878  61.179  81.933  0.50 19.70 ? 1045 HIS   B CA    1 
ATOM   16631 C  C     . HIS   B  1  1047 ? -1.130  62.019  80.914  1.00 17.05 ? 1045 HIS   B C     1 
ATOM   16632 O  O     . HIS   B  1  1047 ? -0.674  61.503  79.894  1.00 19.34 ? 1045 HIS   B O     1 
ATOM   16633 C  CB    A HIS   B  1  1047 ? -1.045  60.521  82.941  0.50 19.98 ? 1045 HIS   B CB    1 
ATOM   16634 C  CB    B HIS   B  1  1047 ? -0.837  60.406  82.744  0.50 19.37 ? 1045 HIS   B CB    1 
ATOM   16635 C  CG    A HIS   B  1  1047 ? -1.821  59.690  83.915  0.50 21.37 ? 1045 HIS   B CG    1 
ATOM   16636 C  CG    B HIS   B  1  1047 ? 0.340   61.229  83.180  0.50 19.62 ? 1045 HIS   B CG    1 
ATOM   16637 N  ND1   A HIS   B  1  1047 ? -2.627  60.245  84.885  0.50 24.39 ? 1045 HIS   B ND1   1 
ATOM   16638 N  ND1   B HIS   B  1  1047 ? 0.244   62.219  84.135  0.50 21.22 ? 1045 HIS   B ND1   1 
ATOM   16639 C  CD2   A HIS   B  1  1047 ? -1.941  58.347  84.048  0.50 22.30 ? 1045 HIS   B CD2   1 
ATOM   16640 C  CD2   B HIS   B  1  1047 ? 1.644   61.190  82.808  0.50 19.89 ? 1045 HIS   B CD2   1 
ATOM   16641 C  CE1   A HIS   B  1  1047 ? -3.199  59.280  85.583  0.50 23.69 ? 1045 HIS   B CE1   1 
ATOM   16642 C  CE1   B HIS   B  1  1047 ? 1.434   62.763  84.325  0.50 22.92 ? 1045 HIS   B CE1   1 
ATOM   16643 N  NE2   A HIS   B  1  1047 ? -2.796  58.119  85.099  0.50 27.08 ? 1045 HIS   B NE2   1 
ATOM   16644 N  NE2   B HIS   B  1  1047 ? 2.301   62.157  83.532  0.50 22.05 ? 1045 HIS   B NE2   1 
ATOM   16645 N  N     . THR   B  1  1048 ? -1.003  63.308  81.193  1.00 16.85 ? 1046 THR   B N     1 
ATOM   16646 C  CA    . THR   B  1  1048 ? -0.209  64.189  80.359  1.00 17.36 ? 1046 THR   B CA    1 
ATOM   16647 C  C     . THR   B  1  1048 ? 0.911   64.753  81.217  1.00 19.69 ? 1046 THR   B C     1 
ATOM   16648 O  O     . THR   B  1  1048 ? 0.667   65.292  82.304  1.00 19.18 ? 1046 THR   B O     1 
ATOM   16649 C  CB    . THR   B  1  1048 ? -1.056  65.323  79.801  1.00 23.32 ? 1046 THR   B CB    1 
ATOM   16650 O  OG1   . THR   B  1  1048 ? -2.232  64.781  79.186  1.00 19.57 ? 1046 THR   B OG1   1 
ATOM   16651 C  CG2   . THR   B  1  1048 ? -0.257  66.103  78.762  1.00 24.26 ? 1046 THR   B CG2   1 
ATOM   16652 N  N     . ASP   B  1  1049 ? 2.126   64.617  80.733  1.00 17.87 ? 1047 ASP   B N     1 
ATOM   16653 C  CA    . ASP   B  1  1049 ? 3.248   65.113  81.496  1.00 17.53 ? 1047 ASP   B CA    1 
ATOM   16654 C  C     . ASP   B  1  1049 ? 3.080   66.613  81.717  1.00 16.78 ? 1047 ASP   B C     1 
ATOM   16655 O  O     . ASP   B  1  1049 ? 2.781   67.349  80.766  1.00 18.22 ? 1047 ASP   B O     1 
ATOM   16656 C  CB    . ASP   B  1  1049 ? 4.541   64.813  80.756  1.00 16.50 ? 1047 ASP   B CB    1 
ATOM   16657 C  CG    . ASP   B  1  1049 ? 5.746   65.253  81.546  1.00 17.25 ? 1047 ASP   B CG    1 
ATOM   16658 O  OD1   . ASP   B  1  1049 ? 6.061   66.457  81.474  1.00 19.55 ? 1047 ASP   B OD1   1 
ATOM   16659 O  OD2   . ASP   B  1  1049 ? 6.308   64.418  82.279  1.00 19.49 ? 1047 ASP   B OD2   1 
ATOM   16660 N  N     . PRO   B  1  1050 ? 3.216   67.101  82.952  1.00 18.23 ? 1048 PRO   B N     1 
ATOM   16661 C  CA    . PRO   B  1  1050 ? 2.953   68.523  83.194  1.00 20.37 ? 1048 PRO   B CA    1 
ATOM   16662 C  C     . PRO   B  1  1050 ? 4.031   69.424  82.636  1.00 20.21 ? 1048 PRO   B C     1 
ATOM   16663 O  O     . PRO   B  1  1050 ? 3.732   70.572  82.283  1.00 21.61 ? 1048 PRO   B O     1 
ATOM   16664 C  CB    . PRO   B  1  1050 ? 2.865   68.615  84.725  1.00 24.96 ? 1048 PRO   B CB    1 
ATOM   16665 C  CG    . PRO   B  1  1050 ? 3.675   67.475  85.202  1.00 24.05 ? 1048 PRO   B CG    1 
ATOM   16666 C  CD    . PRO   B  1  1050 ? 3.497   66.367  84.191  1.00 20.36 ? 1048 PRO   B CD    1 
ATOM   16667 N  N     . VAL   B  1  1051 ? 5.274   68.939  82.555  1.00 21.30 ? 1049 VAL   B N     1 
ATOM   16668 C  CA    . VAL   B  1  1051 ? 6.333   69.758  81.979  1.00 20.62 ? 1049 VAL   B CA    1 
ATOM   16669 C  C     . VAL   B  1  1051 ? 6.140   69.882  80.478  1.00 18.57 ? 1049 VAL   B C     1 
ATOM   16670 O  O     . VAL   B  1  1051 ? 6.342   70.955  79.903  1.00 19.30 ? 1049 VAL   B O     1 
ATOM   16671 C  CB    . VAL   B  1  1051 ? 7.717   69.215  82.366  1.00 20.49 ? 1049 VAL   B CB    1 
ATOM   16672 C  CG1   . VAL   B  1  1051 ? 8.814   70.033  81.675  1.00 22.57 ? 1049 VAL   B CG1   1 
ATOM   16673 C  CG2   . VAL   B  1  1051 ? 7.883   69.251  83.878  1.00 23.16 ? 1049 VAL   B CG2   1 
ATOM   16674 N  N     . LEU   B  1  1052 ? 5.702   68.801  79.828  1.00 17.49 ? 1050 LEU   B N     1 
ATOM   16675 C  CA    . LEU   B  1  1052 ? 5.274   68.896  78.438  1.00 17.57 ? 1050 LEU   B CA    1 
ATOM   16676 C  C     . LEU   B  1  1052 ? 4.243   70.003  78.266  1.00 21.16 ? 1050 LEU   B C     1 
ATOM   16677 O  O     . LEU   B  1  1052 ? 4.339   70.819  77.342  1.00 20.44 ? 1050 LEU   B O     1 
ATOM   16678 C  CB    . LEU   B  1  1052 ? 4.717   67.550  77.973  1.00 17.57 ? 1050 LEU   B CB    1 
ATOM   16679 C  CG    . LEU   B  1  1052 ? 4.232   67.415  76.521  1.00 16.20 ? 1050 LEU   B CG    1 
ATOM   16680 C  CD1   . LEU   B  1  1052 ? 2.825   67.977  76.293  1.00 17.81 ? 1050 LEU   B CD1   1 
ATOM   16681 C  CD2   . LEU   B  1  1052 ? 5.236   68.037  75.545  1.00 17.22 ? 1050 LEU   B CD2   1 
ATOM   16682 N  N     . LEU   B  1  1053 ? 3.239   70.046  79.153  1.00 19.42 ? 1051 LEU   B N     1 
ATOM   16683 C  CA    . LEU   B  1  1053 ? 2.202   71.062  79.030  1.00 22.44 ? 1051 LEU   B CA    1 
ATOM   16684 C  C     . LEU   B  1  1053 ? 2.784   72.463  79.163  1.00 20.24 ? 1051 LEU   B C     1 
ATOM   16685 O  O     . LEU   B  1  1053 ? 2.422   73.367  78.407  1.00 21.73 ? 1051 LEU   B O     1 
ATOM   16686 C  CB    . LEU   B  1  1053 ? 1.110   70.836  80.079  1.00 25.12 ? 1051 LEU   B CB    1 
ATOM   16687 C  CG    . LEU   B  1  1053 ? 0.198   69.639  79.788  1.00 26.84 ? 1051 LEU   B CG    1 
ATOM   16688 C  CD1   . LEU   B  1  1053 ? -0.689  69.353  80.989  1.00 25.93 ? 1051 LEU   B CD1   1 
ATOM   16689 C  CD2   . LEU   B  1  1053 ? -0.632  69.877  78.544  1.00 27.48 ? 1051 LEU   B CD2   1 
ATOM   16690 N  N     . ASP   B  1  1054 ? 3.695   72.655  80.117  1.00 22.58 ? 1052 ASP   B N     1 
ATOM   16691 C  CA    . ASP   B  1  1054 ? 4.333   73.957  80.273  1.00 23.17 ? 1052 ASP   B CA    1 
ATOM   16692 C  C     . ASP   B  1  1054 ? 5.166   74.302  79.047  1.00 20.15 ? 1052 ASP   B C     1 
ATOM   16693 O  O     . ASP   B  1  1054 ? 5.226   75.468  78.636  1.00 21.96 ? 1052 ASP   B O     1 
ATOM   16694 C  CB    . ASP   B  1  1054 ? 5.201   73.951  81.529  1.00 22.84 ? 1052 ASP   B CB    1 
ATOM   16695 C  CG    . ASP   B  1  1054 ? 4.380   73.894  82.801  1.00 31.55 ? 1052 ASP   B CG    1 
ATOM   16696 O  OD1   . ASP   B  1  1054 ? 3.165   74.173  82.732  1.00 29.02 ? 1052 ASP   B OD1   1 
ATOM   16697 O  OD2   . ASP   B  1  1054 ? 4.951   73.583  83.868  1.00 35.49 ? 1052 ASP   B OD2   1 
ATOM   16698 N  N     . PHE   B  1  1055 ? 5.797   73.297  78.441  1.00 20.64 ? 1053 PHE   B N     1 
ATOM   16699 C  CA    . PHE   B  1  1055 ? 6.570   73.531  77.230  1.00 20.76 ? 1053 PHE   B CA    1 
ATOM   16700 C  C     . PHE   B  1  1055 ? 5.667   73.958  76.083  1.00 20.89 ? 1053 PHE   B C     1 
ATOM   16701 O  O     . PHE   B  1  1055 ? 5.990   74.900  75.348  1.00 21.31 ? 1053 PHE   B O     1 
ATOM   16702 C  CB    . PHE   B  1  1055 ? 7.349   72.265  76.874  1.00 19.90 ? 1053 PHE   B CB    1 
ATOM   16703 C  CG    . PHE   B  1  1055 ? 8.276   72.423  75.698  1.00 18.98 ? 1053 PHE   B CG    1 
ATOM   16704 C  CD1   . PHE   B  1  1055 ? 9.245   73.409  75.692  1.00 21.23 ? 1053 PHE   B CD1   1 
ATOM   16705 C  CD2   . PHE   B  1  1055 ? 8.187   71.562  74.610  1.00 21.87 ? 1053 PHE   B CD2   1 
ATOM   16706 C  CE1   . PHE   B  1  1055 ? 10.104  73.555  74.608  1.00 21.92 ? 1053 PHE   B CE1   1 
ATOM   16707 C  CE2   . PHE   B  1  1055 ? 9.042   71.703  73.522  1.00 22.13 ? 1053 PHE   B CE2   1 
ATOM   16708 C  CZ    . PHE   B  1  1055 ? 9.999   72.702  73.529  1.00 22.14 ? 1053 PHE   B CZ    1 
ATOM   16709 N  N     . ALA   B  1  1056 ? 4.517   73.288  75.925  1.00 19.76 ? 1054 ALA   B N     1 
ATOM   16710 C  CA    . ALA   B  1  1056 ? 3.594   73.654  74.855  1.00 21.06 ? 1054 ALA   B CA    1 
ATOM   16711 C  C     . ALA   B  1  1056 ? 3.120   75.095  75.006  1.00 20.63 ? 1054 ALA   B C     1 
ATOM   16712 O  O     . ALA   B  1  1056 ? 3.026   75.827  74.016  1.00 23.98 ? 1054 ALA   B O     1 
ATOM   16713 C  CB    . ALA   B  1  1056 ? 2.397   72.701  74.831  1.00 24.08 ? 1054 ALA   B CB    1 
ATOM   16714 N  N     . LYS   B  1  1057 ? 2.823   75.519  76.238  1.00 22.99 ? 1055 LYS   B N     1 
ATOM   16715 C  CA    . LYS   B  1  1057 ? 2.389   76.896  76.459  1.00 24.90 ? 1055 LYS   B CA    1 
ATOM   16716 C  C     . LYS   B  1  1057 ? 3.500   77.881  76.130  1.00 27.58 ? 1055 LYS   B C     1 
ATOM   16717 O  O     . LYS   B  1  1057 ? 3.244   78.956  75.570  1.00 26.57 ? 1055 LYS   B O     1 
ATOM   16718 C  CB    . LYS   B  1  1057 ? 1.941   77.084  77.906  1.00 25.40 ? 1055 LYS   B CB    1 
ATOM   16719 C  CG    . LYS   B  1  1057 ? 0.550   76.567  78.191  1.00 30.67 ? 1055 LYS   B CG    1 
ATOM   16720 C  CD    . LYS   B  1  1057 ? 0.175   76.847  79.629  1.00 27.54 ? 1055 LYS   B CD    1 
ATOM   16721 C  CE    . LYS   B  1  1057 ? 1.224   76.299  80.581  1.00 30.27 ? 1055 LYS   B CE    1 
ATOM   16722 N  NZ    . LYS   B  1  1057 ? 0.692   76.266  81.969  1.00 31.32 ? 1055 LYS   B NZ    1 
ATOM   16723 N  N     . TRP   B  1  1058 ? 4.740   77.535  76.486  1.00 26.58 ? 1056 TRP   B N     1 
ATOM   16724 C  CA    . TRP   B  1  1058 ? 5.874   78.382  76.137  1.00 27.10 ? 1056 TRP   B CA    1 
ATOM   16725 C  C     . TRP   B  1  1058 ? 6.017   78.498  74.627  1.00 25.72 ? 1056 TRP   B C     1 
ATOM   16726 O  O     . TRP   B  1  1058 ? 6.192   79.600  74.096  1.00 27.70 ? 1056 TRP   B O     1 
ATOM   16727 C  CB    . TRP   B  1  1058 ? 7.148   77.832  76.782  1.00 27.43 ? 1056 TRP   B CB    1 
ATOM   16728 C  CG    . TRP   B  1  1058 ? 8.398   78.588  76.426  1.00 27.92 ? 1056 TRP   B CG    1 
ATOM   16729 C  CD1   . TRP   B  1  1058 ? 8.810   79.786  76.941  1.00 33.99 ? 1056 TRP   B CD1   1 
ATOM   16730 C  CD2   . TRP   B  1  1058 ? 9.403   78.186  75.492  1.00 27.94 ? 1056 TRP   B CD2   1 
ATOM   16731 N  NE1   . TRP   B  1  1058 ? 10.006  80.156  76.376  1.00 31.29 ? 1056 TRP   B NE1   1 
ATOM   16732 C  CE2   . TRP   B  1  1058 ? 10.394  79.191  75.486  1.00 31.20 ? 1056 TRP   B CE2   1 
ATOM   16733 C  CE3   . TRP   B  1  1058 ? 9.565   77.072  74.662  1.00 25.87 ? 1056 TRP   B CE3   1 
ATOM   16734 C  CZ2   . TRP   B  1  1058 ? 11.527  79.115  74.677  1.00 29.52 ? 1056 TRP   B CZ2   1 
ATOM   16735 C  CZ3   . TRP   B  1  1058 ? 10.691  77.001  73.853  1.00 32.36 ? 1056 TRP   B CZ3   1 
ATOM   16736 C  CH2   . TRP   B  1  1058 ? 11.659  78.017  73.873  1.00 29.42 ? 1056 TRP   B CH2   1 
ATOM   16737 N  N     . LEU   B  1  1059 ? 5.915   77.369  73.914  1.00 22.26 ? 1057 LEU   B N     1 
ATOM   16738 C  CA    . LEU   B  1  1059 ? 5.985   77.393  72.457  1.00 26.48 ? 1057 LEU   B CA    1 
ATOM   16739 C  C     . LEU   B  1  1059 ? 4.895   78.272  71.867  1.00 30.74 ? 1057 LEU   B C     1 
ATOM   16740 O  O     . LEU   B  1  1059 ? 5.140   79.045  70.932  1.00 29.66 ? 1057 LEU   B O     1 
ATOM   16741 C  CB    . LEU   B  1  1059 ? 5.859   75.977  71.905  1.00 24.52 ? 1057 LEU   B CB    1 
ATOM   16742 C  CG    . LEU   B  1  1059 ? 7.073   75.084  72.129  1.00 24.57 ? 1057 LEU   B CG    1 
ATOM   16743 C  CD1   . LEU   B  1  1059 ? 6.792   73.681  71.623  1.00 25.95 ? 1057 LEU   B CD1   1 
ATOM   16744 C  CD2   . LEU   B  1  1059 ? 8.289   75.686  71.424  1.00 25.55 ? 1057 LEU   B CD2   1 
ATOM   16745 N  N     . ASP   B  1  1060 ? 3.672   78.150  72.382  1.00 29.09 ? 1058 ASP   B N     1 
ATOM   16746 C  CA    . ASP   B  1  1060 ? 2.596   78.989  71.874  1.00 28.51 ? 1058 ASP   B CA    1 
ATOM   16747 C  C     . ASP   B  1  1060 ? 2.862   80.456  72.172  1.00 31.64 ? 1058 ASP   B C     1 
ATOM   16748 O  O     . ASP   B  1  1060 ? 2.518   81.331  71.368  1.00 35.07 ? 1058 ASP   B O     1 
ATOM   16749 C  CB    . ASP   B  1  1060 ? 1.255   78.544  72.451  1.00 30.97 ? 1058 ASP   B CB    1 
ATOM   16750 C  CG    . ASP   B  1  1060 ? 0.543   77.569  71.547  1.00 35.77 ? 1058 ASP   B CG    1 
ATOM   16751 O  OD1   . ASP   B  1  1060 ? 0.524   77.803  70.315  1.00 43.16 ? 1058 ASP   B OD1   1 
ATOM   16752 O  OD2   . ASP   B  1  1060 ? 0.021   76.566  72.057  1.00 37.94 ? 1058 ASP   B OD2   1 
ATOM   16753 N  N     . GLY   B  1  1061 ? 3.483   80.740  73.319  1.00 31.45 ? 1059 GLY   B N     1 
ATOM   16754 C  CA    . GLY   B  1  1061 ? 3.814   82.115  73.652  1.00 32.50 ? 1059 GLY   B CA    1 
ATOM   16755 C  C     . GLY   B  1  1061 ? 4.736   82.762  72.636  1.00 34.85 ? 1059 GLY   B C     1 
ATOM   16756 O  O     . GLY   B  1  1061 ? 4.568   83.933  72.291  1.00 34.19 ? 1059 GLY   B O     1 
ATOM   16757 N  N     . LYS   B  1  1062 ? 5.719   82.011  72.137  1.00 32.75 ? 1060 LYS   B N     1 
ATOM   16758 C  CA    . LYS   B  1  1062 ? 6.644   82.545  71.145  1.00 35.45 ? 1060 LYS   B CA    1 
ATOM   16759 C  C     . LYS   B  1  1062 ? 6.180   82.320  69.710  1.00 37.57 ? 1060 LYS   B C     1 
ATOM   16760 O  O     . LYS   B  1  1062 ? 6.948   82.571  68.776  1.00 40.33 ? 1060 LYS   B O     1 
ATOM   16761 C  CB    . LYS   B  1  1062 ? 8.065   82.019  71.372  1.00 36.20 ? 1060 LYS   B CB    1 
ATOM   16762 C  CG    . LYS   B  1  1062 ? 8.221   80.527  71.261  1.00 36.67 ? 1060 LYS   B CG    1 
ATOM   16763 C  CD    . LYS   B  1  1062 ? 9.621   80.098  71.706  1.00 35.85 ? 1060 LYS   B CD    1 
ATOM   16764 C  CE    . LYS   B  1  1062 ? 10.699  80.733  70.841  1.00 33.14 ? 1060 LYS   B CE    1 
ATOM   16765 N  NZ    . LYS   B  1  1062 ? 12.047  80.588  71.451  1.00 37.74 ? 1060 LYS   B NZ    1 
ATOM   16766 N  N     . GLY   B  1  1063 ? 4.944   81.873  69.513  1.00 34.56 ? 1061 GLY   B N     1 
ATOM   16767 C  CA    . GLY   B  1  1063 ? 4.399   81.734  68.181  1.00 34.50 ? 1061 GLY   B CA    1 
ATOM   16768 C  C     . GLY   B  1  1063 ? 4.889   80.541  67.397  1.00 38.56 ? 1061 GLY   B C     1 
ATOM   16769 O  O     . GLY   B  1  1063 ? 4.687   80.500  66.177  1.00 37.06 ? 1061 GLY   B O     1 
ATOM   16770 N  N     . ALA   B  1  1064 ? 5.525   79.566  68.051  1.00 31.97 ? 1062 ALA   B N     1 
ATOM   16771 C  CA    . ALA   B  1  1064 ? 5.958   78.341  67.383  1.00 29.87 ? 1062 ALA   B CA    1 
ATOM   16772 C  C     . ALA   B  1  1064 ? 4.758   77.399  67.280  1.00 31.70 ? 1062 ALA   B C     1 
ATOM   16773 O  O     . ALA   B  1  1064 ? 4.659   76.374  67.961  1.00 27.86 ? 1062 ALA   B O     1 
ATOM   16774 C  CB    . ALA   B  1  1064 ? 7.126   77.706  68.126  1.00 31.43 ? 1062 ALA   B CB    1 
ATOM   16775 N  N     . ARG   B  1  1065 ? 3.834   77.773  66.388  1.00 32.58 ? 1063 ARG   B N     1 
ATOM   16776 C  CA    . ARG   B  1  1065 ? 2.521   77.131  66.348  1.00 30.02 ? 1063 ARG   B CA    1 
ATOM   16777 C  C     . ARG   B  1  1065 ? 2.620   75.667  65.944  1.00 29.40 ? 1063 ARG   B C     1 
ATOM   16778 O  O     . ARG   B  1  1065 ? 1.964   74.806  66.544  1.00 29.89 ? 1063 ARG   B O     1 
ATOM   16779 C  CB    . ARG   B  1  1065 ? 1.588   77.896  65.405  1.00 35.73 ? 1063 ARG   B CB    1 
ATOM   16780 N  N     . ALA   B  1  1066 ? 3.424   75.359  64.926  1.00 28.03 ? 1064 ALA   B N     1 
ATOM   16781 C  CA    . ALA   B  1  1066 ? 3.577   73.966  64.523  1.00 28.67 ? 1064 ALA   B CA    1 
ATOM   16782 C  C     . ALA   B  1  1066 ? 4.188   73.137  65.647  1.00 27.77 ? 1064 ALA   B C     1 
ATOM   16783 O  O     . ALA   B  1  1066 ? 3.746   72.014  65.917  1.00 25.84 ? 1064 ALA   B O     1 
ATOM   16784 C  CB    . ALA   B  1  1066 ? 4.433   73.871  63.262  1.00 30.18 ? 1064 ALA   B CB    1 
ATOM   16785 N  N     . GLU   B  1  1067 ? 5.197   73.685  66.324  1.00 24.63 ? 1065 GLU   B N     1 
ATOM   16786 C  CA    . GLU   B  1  1067 ? 5.872   72.937  67.377  1.00 26.31 ? 1065 GLU   B CA    1 
ATOM   16787 C  C     . GLU   B  1  1067 ? 4.967   72.739  68.584  1.00 23.08 ? 1065 GLU   B C     1 
ATOM   16788 O  O     . GLU   B  1  1067 ? 4.968   71.664  69.193  1.00 22.94 ? 1065 GLU   B O     1 
ATOM   16789 C  CB    . GLU   B  1  1067 ? 7.163   73.653  67.770  1.00 24.67 ? 1065 GLU   B CB    1 
ATOM   16790 C  CG    . GLU   B  1  1067 ? 8.238   73.602  66.686  1.00 25.31 ? 1065 GLU   B CG    1 
ATOM   16791 C  CD    . GLU   B  1  1067 ? 8.013   74.599  65.562  1.00 31.57 ? 1065 GLU   B CD    1 
ATOM   16792 O  OE1   . GLU   B  1  1067 ? 7.102   75.447  65.673  1.00 29.48 ? 1065 GLU   B OE1   1 
ATOM   16793 O  OE2   . GLU   B  1  1067 ? 8.760   74.534  64.560  1.00 33.64 ? 1065 GLU   B OE2   1 
ATOM   16794 N  N     . ALA   B  1  1068 ? 4.215   73.773  68.958  1.00 23.94 ? 1066 ALA   B N     1 
ATOM   16795 C  CA    . ALA   B  1  1068 ? 3.284   73.641  70.074  1.00 28.11 ? 1066 ALA   B CA    1 
ATOM   16796 C  C     . ALA   B  1  1068 ? 2.251   72.558  69.793  1.00 25.44 ? 1066 ALA   B C     1 
ATOM   16797 O  O     . ALA   B  1  1068 ? 1.899   71.774  70.684  1.00 22.34 ? 1066 ALA   B O     1 
ATOM   16798 C  CB    . ALA   B  1  1068 ? 2.606   74.983  70.337  1.00 25.33 ? 1066 ALA   B CB    1 
ATOM   16799 N  N     . GLU   B  1  1069 ? 1.772   72.485  68.552  1.00 22.48 ? 1067 GLU   B N     1 
ATOM   16800 C  CA    . GLU   B  1  1069 ? 0.839   71.430  68.176  1.00 28.53 ? 1067 GLU   B CA    1 
ATOM   16801 C  C     . GLU   B  1  1069 ? 1.493   70.054  68.258  1.00 27.83 ? 1067 GLU   B C     1 
ATOM   16802 O  O     . GLU   B  1  1069 ? 0.900   69.107  68.791  1.00 24.91 ? 1067 GLU   B O     1 
ATOM   16803 C  CB    . GLU   B  1  1069 ? 0.281   71.704  66.779  1.00 28.99 ? 1067 GLU   B CB    1 
ATOM   16804 C  CG    . GLU   B  1  1069 ? -0.633  70.623  66.233  1.00 30.33 ? 1067 GLU   B CG    1 
ATOM   16805 C  CD    . GLU   B  1  1069 ? -2.004  70.614  66.898  1.00 39.18 ? 1067 GLU   B CD    1 
ATOM   16806 O  OE1   . GLU   B  1  1069 ? -2.295  71.527  67.701  1.00 41.12 ? 1067 GLU   B OE1   1 
ATOM   16807 O  OE2   . GLU   B  1  1069 ? -2.794  69.690  66.612  1.00 43.76 ? 1067 GLU   B OE2   1 
ATOM   16808 N  N     . ALA   B  1  1070 ? 2.719   69.921  67.746  1.00 23.28 ? 1068 ALA   B N     1 
ATOM   16809 C  CA    . ALA   B  1  1070 ? 3.432   68.658  67.905  1.00 25.19 ? 1068 ALA   B CA    1 
ATOM   16810 C  C     . ALA   B  1  1070 ? 3.628   68.325  69.380  1.00 19.84 ? 1068 ALA   B C     1 
ATOM   16811 O  O     . ALA   B  1  1070 ? 3.549   67.157  69.774  1.00 23.73 ? 1068 ALA   B O     1 
ATOM   16812 C  CB    . ALA   B  1  1070 ? 4.778   68.713  67.178  1.00 27.51 ? 1068 ALA   B CB    1 
ATOM   16813 N  N     . ALA   B  1  1071 ? 3.877   69.339  70.211  1.00 21.07 ? 1069 ALA   B N     1 
ATOM   16814 C  CA    . ALA   B  1  1071 ? 4.065   69.081  71.632  1.00 20.92 ? 1069 ALA   B CA    1 
ATOM   16815 C  C     . ALA   B  1  1071 ? 2.784   68.548  72.261  1.00 20.06 ? 1069 ALA   B C     1 
ATOM   16816 O  O     . ALA   B  1  1071 ? 2.812   67.551  72.991  1.00 20.55 ? 1069 ALA   B O     1 
ATOM   16817 C  CB    . ALA   B  1  1071 ? 4.548   70.334  72.355  1.00 20.57 ? 1069 ALA   B CB    1 
ATOM   16818 N  N     . ARG   B  1  1072 ? 1.652   69.205  71.993  1.00 20.15 ? 1070 ARG   B N     1 
ATOM   16819 C  CA    . ARG   B  1  1072 ? 0.378   68.720  72.518  1.00 20.44 ? 1070 ARG   B CA    1 
ATOM   16820 C  C     . ARG   B  1  1072 ? 0.074   67.316  72.019  1.00 21.63 ? 1070 ARG   B C     1 
ATOM   16821 O  O     . ARG   B  1  1072 ? -0.377  66.459  72.790  1.00 21.19 ? 1070 ARG   B O     1 
ATOM   16822 C  CB    . ARG   B  1  1072 ? -0.752  69.688  72.150  1.00 21.61 ? 1070 ARG   B CB    1 
ATOM   16823 C  CG    . ARG   B  1  1072 ? -0.691  71.006  72.900  1.00 27.78 ? 1070 ARG   B CG    1 
ATOM   16824 C  CD    . ARG   B  1  1072 ? -1.926  71.858  72.628  1.00 27.10 ? 1070 ARG   B CD    1 
ATOM   16825 N  NE    . ARG   B  1  1072 ? -1.966  72.300  71.237  1.00 33.46 ? 1070 ARG   B NE    1 
ATOM   16826 C  CZ    . ARG   B  1  1072 ? -1.448  73.443  70.807  1.00 33.32 ? 1070 ARG   B CZ    1 
ATOM   16827 N  NH1   . ARG   B  1  1072 ? -0.902  74.311  71.646  1.00 31.47 ? 1070 ARG   B NH1   1 
ATOM   16828 N  NH2   . ARG   B  1  1072 ? -1.472  73.720  69.504  1.00 27.80 ? 1070 ARG   B NH2   1 
ATOM   16829 N  N     . ASN   B  1  1073 ? 0.333   67.051  70.735  1.00 20.50 ? 1071 ASN   B N     1 
ATOM   16830 C  CA    . ASN   B  1  1073 ? 0.072   65.719  70.198  1.00 21.01 ? 1071 ASN   B CA    1 
ATOM   16831 C  C     . ASN   B  1  1073 ? 0.951   64.670  70.859  1.00 23.34 ? 1071 ASN   B C     1 
ATOM   16832 O  O     . ASN   B  1  1073 ? 0.500   63.551  71.127  1.00 23.78 ? 1071 ASN   B O     1 
ATOM   16833 C  CB    . ASN   B  1  1073 ? 0.255   65.714  68.685  1.00 23.46 ? 1071 ASN   B CB    1 
ATOM   16834 C  CG    . ASN   B  1  1073 ? -0.836  66.483  67.979  1.00 28.13 ? 1071 ASN   B CG    1 
ATOM   16835 O  OD1   . ASN   B  1  1073 ? -1.959  66.595  68.485  1.00 29.87 ? 1071 ASN   B OD1   1 
ATOM   16836 N  ND2   . ASN   B  1  1073 ? -0.515  67.036  66.814  1.00 32.77 ? 1071 ASN   B ND2   1 
ATOM   16837 N  N     . ALA   B  1  1074 ? 2.213   65.009  71.122  1.00 21.23 ? 1072 ALA   B N     1 
ATOM   16838 C  CA    . ALA   B  1  1074 ? 3.082   64.083  71.834  1.00 19.51 ? 1072 ALA   B CA    1 
ATOM   16839 C  C     . ALA   B  1  1074 ? 2.574   63.856  73.247  1.00 15.70 ? 1072 ALA   B C     1 
ATOM   16840 O  O     . ALA   B  1  1074 ? 2.580   62.725  73.745  1.00 18.02 ? 1072 ALA   B O     1 
ATOM   16841 C  CB    . ALA   B  1  1074 ? 4.500   64.641  71.875  1.00 22.50 ? 1072 ALA   B CB    1 
ATOM   16842 N  N     . GLY   B  1  1075 ? 2.150   64.926  73.915  1.00 16.68 ? 1073 GLY   B N     1 
ATOM   16843 C  CA    . GLY   B  1  1075 ? 1.618   64.775  75.258  1.00 19.37 ? 1073 GLY   B CA    1 
ATOM   16844 C  C     . GLY   B  1  1075 ? 0.461   63.796  75.302  1.00 22.01 ? 1073 GLY   B C     1 
ATOM   16845 O  O     . GLY   B  1  1075 ? 0.359   62.979  76.224  1.00 21.18 ? 1073 GLY   B O     1 
ATOM   16846 N  N     . SER   B  1  1076 ? -0.399  63.837  74.283  1.00 22.42 ? 1074 SER   B N     1 
ATOM   16847 C  CA    . SER   B  1  1076 ? -1.556  62.951  74.267  1.00 19.88 ? 1074 SER   B CA    1 
ATOM   16848 C  C     . SER   B  1  1076 ? -1.178  61.535  73.862  1.00 21.71 ? 1074 SER   B C     1 
ATOM   16849 O  O     . SER   B  1  1076 ? -1.642  60.571  74.476  1.00 22.81 ? 1074 SER   B O     1 
ATOM   16850 C  CB    . SER   B  1  1076 ? -2.642  63.511  73.341  1.00 25.10 ? 1074 SER   B CB    1 
ATOM   16851 O  OG    . SER   B  1  1076 ? -3.233  64.675  73.898  1.00 27.14 ? 1074 SER   B OG    1 
ATOM   16852 N  N     . SER   B  1  1077 ? -0.327  61.380  72.852  1.00 19.11 ? 1075 SER   B N     1 
ATOM   16853 C  CA    . SER   B  1  1077 ? -0.046  60.033  72.372  1.00 22.55 ? 1075 SER   B CA    1 
ATOM   16854 C  C     . SER   B  1  1077 ? 0.977   59.298  73.226  1.00 20.08 ? 1075 SER   B C     1 
ATOM   16855 O  O     . SER   B  1  1077 ? 1.099   58.075  73.100  1.00 24.14 ? 1075 SER   B O     1 
ATOM   16856 C  CB    . SER   B  1  1077 ? 0.387   60.061  70.910  1.00 28.87 ? 1075 SER   B CB    1 
ATOM   16857 O  OG    . SER   B  1  1077 ? 1.707   60.529  70.803  1.00 29.56 ? 1075 SER   B OG    1 
ATOM   16858 N  N     . SER   B  1  1078 ? 1.701   60.007  74.088  1.00 17.27 ? 1076 SER   B N     1 
ATOM   16859 C  CA    . SER   B  1  1078 ? 2.588   59.343  75.027  1.00 18.18 ? 1076 SER   B CA    1 
ATOM   16860 C  C     . SER   B  1  1078 ? 1.787   58.378  75.879  1.00 16.80 ? 1076 SER   B C     1 
ATOM   16861 O  O     . SER   B  1  1078 ? 0.660   58.675  76.293  1.00 18.57 ? 1076 SER   B O     1 
ATOM   16862 C  CB    . SER   B  1  1078 ? 3.221   60.379  75.947  1.00 17.93 ? 1076 SER   B CB    1 
ATOM   16863 O  OG    . SER   B  1  1078 ? 3.932   59.754  77.005  1.00 15.82 ? 1076 SER   B OG    1 
ATOM   16864 N  N     . ALA   B  1  1079 ? 2.372   57.210  76.130  1.00 14.91 ? 1077 ALA   B N     1 
ATOM   16865 C  CA    . ALA   B  1  1079 ? 1.762   56.238  77.021  1.00 15.11 ? 1077 ALA   B CA    1 
ATOM   16866 C  C     . ALA   B  1  1079 ? 2.403   56.250  78.394  1.00 16.44 ? 1077 ALA   B C     1 
ATOM   16867 O  O     . ALA   B  1  1079 ? 2.176   55.331  79.183  1.00 16.39 ? 1077 ALA   B O     1 
ATOM   16868 C  CB    . ALA   B  1  1079 ? 1.819   54.841  76.415  1.00 18.13 ? 1077 ALA   B CB    1 
ATOM   16869 N  N     . LEU   B  1  1080 ? 3.218   57.257  78.682  1.00 15.94 ? 1078 LEU   B N     1 
ATOM   16870 C  CA    . LEU   B  1  1080 ? 3.748   57.420  80.029  1.00 14.55 ? 1078 LEU   B CA    1 
ATOM   16871 C  C     . LEU   B  1  1080 ? 2.615   57.384  81.051  1.00 14.58 ? 1078 LEU   B C     1 
ATOM   16872 O  O     . LEU   B  1  1080 ? 1.615   58.096  80.920  1.00 17.54 ? 1078 LEU   B O     1 
ATOM   16873 C  CB    . LEU   B  1  1080 ? 4.441   58.773  80.119  1.00 14.89 ? 1078 LEU   B CB    1 
ATOM   16874 C  CG    . LEU   B  1  1080 ? 4.872   59.163  81.525  1.00 16.58 ? 1078 LEU   B CG    1 
ATOM   16875 C  CD1   . LEU   B  1  1080 ? 6.059   58.314  81.944  1.00 17.03 ? 1078 LEU   B CD1   1 
ATOM   16876 C  CD2   . LEU   B  1  1080 ? 5.190   60.648  81.548  1.00 16.50 ? 1078 LEU   B CD2   1 
ATOM   16877 N  N     . GLY   B  1  1081 ? 2.781   56.563  82.081  1.00 15.19 ? 1079 GLY   B N     1 
ATOM   16878 C  CA    . GLY   B  1  1081 ? 1.764   56.425  83.107  1.00 16.17 ? 1079 GLY   B CA    1 
ATOM   16879 C  C     . GLY   B  1  1081 ? 0.838   55.243  82.909  1.00 18.39 ? 1079 GLY   B C     1 
ATOM   16880 O  O     . GLY   B  1  1081 ? -0.018  54.987  83.770  1.00 18.38 ? 1079 GLY   B O     1 
ATOM   16881 N  N     . LEU   B  1  1082 ? 0.958   54.542  81.791  1.00 16.65 ? 1080 LEU   B N     1 
ATOM   16882 C  CA    A LEU   B  1  1082 ? 0.220   53.302  81.612  0.56 17.99 ? 1080 LEU   B CA    1 
ATOM   16883 C  CA    B LEU   B  1  1082 ? 0.221   53.300  81.611  0.44 17.99 ? 1080 LEU   B CA    1 
ATOM   16884 C  C     . LEU   B  1  1082 ? 0.482   52.389  82.799  1.00 17.74 ? 1080 LEU   B C     1 
ATOM   16885 O  O     . LEU   B  1  1082 ? 1.606   52.278  83.277  1.00 17.47 ? 1080 LEU   B O     1 
ATOM   16886 C  CB    A LEU   B  1  1082 ? 0.684   52.622  80.326  0.56 16.04 ? 1080 LEU   B CB    1 
ATOM   16887 C  CB    B LEU   B  1  1082 ? 0.677   52.619  80.318  0.44 16.06 ? 1080 LEU   B CB    1 
ATOM   16888 C  CG    A LEU   B  1  1082 ? 0.068   51.265  79.988  0.56 17.20 ? 1080 LEU   B CG    1 
ATOM   16889 C  CG    B LEU   B  1  1082 ? 0.085   51.267  79.904  0.44 17.22 ? 1080 LEU   B CG    1 
ATOM   16890 C  CD1   A LEU   B  1  1082 ? -1.432  51.358  80.065  0.56 20.16 ? 1080 LEU   B CD1   1 
ATOM   16891 C  CD1   B LEU   B  1  1082 ? 0.167   51.117  78.392  0.44 17.73 ? 1080 LEU   B CD1   1 
ATOM   16892 C  CD2   A LEU   B  1  1082 ? 0.499   50.825  78.596  0.56 18.10 ? 1080 LEU   B CD2   1 
ATOM   16893 C  CD2   B LEU   B  1  1082 ? 0.804   50.107  80.578  0.44 17.39 ? 1080 LEU   B CD2   1 
ATOM   16894 N  N     . ASP   B  1  1083 ? -0.572  51.744  83.289  1.00 16.40 ? 1081 ASP   B N     1 
ATOM   16895 C  CA    . ASP   B  1  1083 ? -0.442  50.939  84.499  1.00 19.87 ? 1081 ASP   B CA    1 
ATOM   16896 C  C     . ASP   B  1  1083 ? -1.519  49.867  84.396  1.00 20.46 ? 1081 ASP   B C     1 
ATOM   16897 O  O     . ASP   B  1  1083 ? -2.698  50.142  84.644  1.00 24.10 ? 1081 ASP   B O     1 
ATOM   16898 C  CB    . ASP   B  1  1083 ? -0.642  51.831  85.717  1.00 22.59 ? 1081 ASP   B CB    1 
ATOM   16899 C  CG    . ASP   B  1  1083 ? -0.541  51.081  87.034  1.00 30.35 ? 1081 ASP   B CG    1 
ATOM   16900 O  OD1   . ASP   B  1  1083 ? 0.068   49.994  87.082  1.00 34.77 ? 1081 ASP   B OD1   1 
ATOM   16901 O  OD2   . ASP   B  1  1083 ? -1.087  51.593  88.036  1.00 37.82 ? 1081 ASP   B OD2   1 
ATOM   16902 N  N     . LEU   B  1  1084 ? -1.113  48.671  83.993  1.00 19.80 ? 1082 LEU   B N     1 
ATOM   16903 C  CA    . LEU   B  1  1084 ? -2.028  47.603  83.637  1.00 18.54 ? 1082 LEU   B CA    1 
ATOM   16904 C  C     . LEU   B  1  1084 ? -1.745  46.403  84.517  1.00 18.93 ? 1082 LEU   B C     1 
ATOM   16905 O  O     . LEU   B  1  1084 ? -0.608  46.176  84.935  1.00 18.23 ? 1082 LEU   B O     1 
ATOM   16906 C  CB    . LEU   B  1  1084 ? -1.792  47.142  82.202  1.00 22.07 ? 1082 LEU   B CB    1 
ATOM   16907 C  CG    . LEU   B  1  1084 ? -2.118  48.094  81.060  1.00 25.42 ? 1082 LEU   B CG    1 
ATOM   16908 C  CD1   . LEU   B  1  1084 ? -1.692  47.508  79.729  1.00 25.94 ? 1082 LEU   B CD1   1 
ATOM   16909 C  CD2   . LEU   B  1  1084 ? -3.608  48.432  81.074  1.00 28.57 ? 1082 LEU   B CD2   1 
ATOM   16910 N  N     . GLU   B  1  1085 ? -2.785  45.636  84.788  1.00 18.30 ? 1083 GLU   B N     1 
ATOM   16911 C  CA    . GLU   B  1  1085 ? -2.621  44.297  85.313  1.00 16.68 ? 1083 GLU   B CA    1 
ATOM   16912 C  C     . GLU   B  1  1085 ? -2.812  43.320  84.167  1.00 17.98 ? 1083 GLU   B C     1 
ATOM   16913 O  O     . GLU   B  1  1085 ? -3.819  43.383  83.448  1.00 21.07 ? 1083 GLU   B O     1 
ATOM   16914 C  CB    . GLU   B  1  1085 ? -3.602  43.999  86.451  1.00 18.92 ? 1083 GLU   B CB    1 
ATOM   16915 C  CG    . GLU   B  1  1085 ? -3.416  42.567  86.923  1.00 21.63 ? 1083 GLU   B CG    1 
ATOM   16916 C  CD    . GLU   B  1  1085 ? -4.141  42.220  88.205  1.00 27.22 ? 1083 GLU   B CD    1 
ATOM   16917 O  OE1   . GLU   B  1  1085 ? -4.761  43.116  88.823  1.00 29.65 ? 1083 GLU   B OE1   1 
ATOM   16918 O  OE2   . GLU   B  1  1085 ? -4.075  41.027  88.590  1.00 27.87 ? 1083 GLU   B OE2   1 
ATOM   16919 N  N     . LEU   B  1  1086 ? -1.850  42.448  83.983  1.00 17.57 ? 1084 LEU   B N     1 
ATOM   16920 C  CA    . LEU   B  1  1086 ? -1.857  41.491  82.888  1.00 17.59 ? 1084 LEU   B CA    1 
ATOM   16921 C  C     . LEU   B  1  1086 ? -2.520  40.191  83.336  1.00 23.26 ? 1084 LEU   B C     1 
ATOM   16922 O  O     . LEU   B  1  1086 ? -2.355  39.777  84.486  1.00 21.88 ? 1084 LEU   B O     1 
ATOM   16923 C  CB    . LEU   B  1  1086 ? -0.428  41.199  82.452  1.00 18.07 ? 1084 LEU   B CB    1 
ATOM   16924 C  CG    . LEU   B  1  1086 ? 0.337   42.416  81.926  1.00 20.33 ? 1084 LEU   B CG    1 
ATOM   16925 C  CD1   . LEU   B  1  1086 ? 1.722   42.051  81.419  1.00 18.53 ? 1084 LEU   B CD1   1 
ATOM   16926 C  CD2   . LEU   B  1  1086 ? -0.487  43.102  80.834  1.00 22.95 ? 1084 LEU   B CD2   1 
ATOM   16927 N  N     . PRO   B  1  1087 ? -3.287  39.551  82.456  1.00 21.33 ? 1085 PRO   B N     1 
ATOM   16928 C  CA    . PRO   B  1  1087 ? -3.896  38.261  82.808  1.00 24.83 ? 1085 PRO   B CA    1 
ATOM   16929 C  C     . PRO   B  1  1087 ? -2.828  37.229  83.124  1.00 21.21 ? 1085 PRO   B C     1 
ATOM   16930 O  O     . PRO   B  1  1087 ? -1.801  37.147  82.455  1.00 22.45 ? 1085 PRO   B O     1 
ATOM   16931 C  CB    . PRO   B  1  1087 ? -4.663  37.876  81.536  1.00 23.26 ? 1085 PRO   B CB    1 
ATOM   16932 C  CG    . PRO   B  1  1087 ? -4.905  39.155  80.827  1.00 26.22 ? 1085 PRO   B CG    1 
ATOM   16933 C  CD    . PRO   B  1  1087 ? -3.744  40.051  81.145  1.00 22.90 ? 1085 PRO   B CD    1 
ATOM   16934 N  N     . GLY   B  1  1088 ? -3.074  36.436  84.156  1.00 20.44 ? 1086 GLY   B N     1 
ATOM   16935 C  CA    . GLY   B  1  1088 ? -2.129  35.432  84.568  1.00 20.40 ? 1086 GLY   B CA    1 
ATOM   16936 C  C     . GLY   B  1  1088 ? -2.765  34.462  85.536  1.00 17.94 ? 1086 GLY   B C     1 
ATOM   16937 O  O     . GLY   B  1  1088 ? -3.988  34.384  85.659  1.00 20.08 ? 1086 GLY   B O     1 
ATOM   16938 N  N     . PRO   B  1  1089 ? -1.936  33.715  86.255  1.00 18.76 ? 1087 PRO   B N     1 
ATOM   16939 C  CA    . PRO   B  1  1089 ? -2.460  32.747  87.220  1.00 19.64 ? 1087 PRO   B CA    1 
ATOM   16940 C  C     . PRO   B  1  1089 ? -3.092  33.435  88.420  1.00 18.11 ? 1087 PRO   B C     1 
ATOM   16941 O  O     . PRO   B  1  1089 ? -2.791  34.583  88.759  1.00 19.76 ? 1087 PRO   B O     1 
ATOM   16942 C  CB    . PRO   B  1  1089 ? -1.210  31.971  87.647  1.00 21.13 ? 1087 PRO   B CB    1 
ATOM   16943 C  CG    . PRO   B  1  1089 ? -0.079  32.962  87.448  1.00 23.97 ? 1087 PRO   B CG    1 
ATOM   16944 C  CD    . PRO   B  1  1089 ? -0.461  33.758  86.231  1.00 21.47 ? 1087 PRO   B CD    1 
ATOM   16945 N  N     . VAL   B  1  1090 ? -3.987  32.693  89.077  1.00 17.48 ? 1088 VAL   B N     1 
ATOM   16946 C  CA    . VAL   B  1  1090 ? -4.510  33.147  90.350  1.00 16.69 ? 1088 VAL   B CA    1 
ATOM   16947 C  C     . VAL   B  1  1090 ? -3.379  33.221  91.366  1.00 17.13 ? 1088 VAL   B C     1 
ATOM   16948 O  O     . VAL   B  1  1090 ? -2.324  32.594  91.215  1.00 17.78 ? 1088 VAL   B O     1 
ATOM   16949 C  CB    . VAL   B  1  1090 ? -5.627  32.230  90.862  1.00 18.11 ? 1088 VAL   B CB    1 
ATOM   16950 C  CG1   . VAL   B  1  1090 ? -6.779  32.184  89.868  1.00 18.53 ? 1088 VAL   B CG1   1 
ATOM   16951 C  CG2   . VAL   B  1  1090 ? -5.090  30.829  91.169  1.00 18.66 ? 1088 VAL   B CG2   1 
ATOM   16952 N  N     . GLY   B  1  1091 ? -3.617  33.993  92.425  1.00 17.48 ? 1089 GLY   B N     1 
ATOM   16953 C  CA    . GLY   B  1  1091 ? -2.616  34.090  93.475  1.00 18.13 ? 1089 GLY   B CA    1 
ATOM   16954 C  C     . GLY   B  1  1091 ? -1.394  34.889  93.103  1.00 18.16 ? 1089 GLY   B C     1 
ATOM   16955 O  O     . GLY   B  1  1091 ? -0.384  34.826  93.805  1.00 17.10 ? 1089 GLY   B O     1 
ATOM   16956 N  N     . GLU   B  1  1092 ? -1.460  35.636  92.012  1.00 17.36 ? 1090 GLU   B N     1 
ATOM   16957 C  CA    . GLU   B  1  1092 ? -0.376  36.488  91.578  1.00 17.84 ? 1090 GLU   B CA    1 
ATOM   16958 C  C     . GLU   B  1  1092 ? -1.006  37.722  90.961  1.00 18.81 ? 1090 GLU   B C     1 
ATOM   16959 O  O     . GLU   B  1  1092 ? -2.085  37.643  90.362  1.00 20.95 ? 1090 GLU   B O     1 
ATOM   16960 C  CB    . GLU   B  1  1092 ? 0.439   35.757  90.509  1.00 19.63 ? 1090 GLU   B CB    1 
ATOM   16961 C  CG    . GLU   B  1  1092 ? 1.911   35.804  90.708  1.00 27.31 ? 1090 GLU   B CG    1 
ATOM   16962 C  CD    . GLU   B  1  1092 ? 2.640   34.954  89.678  1.00 28.48 ? 1090 GLU   B CD    1 
ATOM   16963 O  OE1   . GLU   B  1  1092 ? 2.444   35.189  88.464  1.00 25.02 ? 1090 GLU   B OE1   1 
ATOM   16964 O  OE2   . GLU   B  1  1092 ? 3.386   34.039  90.088  1.00 28.19 ? 1090 GLU   B OE2   1 
ATOM   16965 N  N     . ARG   B  1  1093 ? -0.367  38.867  91.147  1.00 17.35 ? 1091 ARG   B N     1 
ATOM   16966 C  CA    . ARG   B  1  1093 ? -0.747  40.077  90.429  1.00 16.88 ? 1091 ARG   B CA    1 
ATOM   16967 C  C     . ARG   B  1  1093 ? 0.438   40.465  89.578  1.00 16.90 ? 1091 ARG   B C     1 
ATOM   16968 O  O     . ARG   B  1  1093 ? 1.538   40.663  90.097  1.00 17.24 ? 1091 ARG   B O     1 
ATOM   16969 C  CB    . ARG   B  1  1093 ? -1.116  41.225  91.372  1.00 18.64 ? 1091 ARG   B CB    1 
ATOM   16970 C  CG    . ARG   B  1  1093 ? -2.525  41.131  91.936  1.00 29.49 ? 1091 ARG   B CG    1 
ATOM   16971 C  CD    . ARG   B  1  1093 ? -3.011  42.495  92.436  1.00 37.51 ? 1091 ARG   B CD    1 
ATOM   16972 N  NE    . ARG   B  1  1093 ? -2.138  43.036  93.471  1.00 44.22 ? 1091 ARG   B NE    1 
ATOM   16973 C  CZ    . ARG   B  1  1093 ? -2.295  42.831  94.773  1.00 48.41 ? 1091 ARG   B CZ    1 
ATOM   16974 N  NH1   . ARG   B  1  1093 ? -3.309  42.121  95.245  1.00 43.61 ? 1091 ARG   B NH1   1 
ATOM   16975 N  NH2   . ARG   B  1  1093 ? -1.411  43.347  95.623  1.00 45.47 ? 1091 ARG   B NH2   1 
ATOM   16976 N  N     . ASN   B  1  1094 ? 0.218   40.545  88.279  1.00 15.11 ? 1092 ASN   B N     1 
ATOM   16977 C  CA    . ASN   B  1  1094 ? 1.293   40.817  87.340  1.00 14.83 ? 1092 ASN   B CA    1 
ATOM   16978 C  C     . ASN   B  1  1094 ? 1.000   42.160  86.700  1.00 16.75 ? 1092 ASN   B C     1 
ATOM   16979 O  O     . ASN   B  1  1094 ? 0.002   42.312  85.987  1.00 18.08 ? 1092 ASN   B O     1 
ATOM   16980 C  CB    . ASN   B  1  1094 ? 1.404   39.672  86.345  1.00 16.69 ? 1092 ASN   B CB    1 
ATOM   16981 C  CG    . ASN   B  1  1094 ? 2.000   38.450  86.989  1.00 17.21 ? 1092 ASN   B CG    1 
ATOM   16982 O  OD1   . ASN   B  1  1094 ? 3.190   38.432  87.287  1.00 16.57 ? 1092 ASN   B OD1   1 
ATOM   16983 N  ND2   . ASN   B  1  1094 ? 1.178   37.453  87.271  1.00 17.65 ? 1092 ASN   B ND2   1 
ATOM   16984 N  N     . LEU   B  1  1095 ? 1.832   43.134  87.017  1.00 14.51 ? 1093 LEU   B N     1 
ATOM   16985 C  CA    . LEU   B  1  1095 ? 1.626   44.521  86.653  1.00 14.23 ? 1093 LEU   B CA    1 
ATOM   16986 C  C     . LEU   B  1  1095 ? 2.626   44.937  85.590  1.00 14.36 ? 1093 LEU   B C     1 
ATOM   16987 O  O     . LEU   B  1  1095 ? 3.762   44.451  85.542  1.00 16.16 ? 1093 LEU   B O     1 
ATOM   16988 C  CB    . LEU   B  1  1095 ? 1.804   45.419  87.867  1.00 17.67 ? 1093 LEU   B CB    1 
ATOM   16989 C  CG    . LEU   B  1  1095 ? 0.942   44.960  89.050  1.00 19.38 ? 1093 LEU   B CG    1 
ATOM   16990 C  CD1   . LEU   B  1  1095 ? 1.206   45.871  90.253  1.00 21.05 ? 1093 LEU   B CD1   1 
ATOM   16991 C  CD2   . LEU   B  1  1095 ? -0.539  44.916  88.676  1.00 21.32 ? 1093 LEU   B CD2   1 
ATOM   16992 N  N     . TYR   B  1  1096 ? 2.195   45.868  84.751  1.00 13.45 ? 1094 TYR   B N     1 
ATOM   16993 C  CA    . TYR   B  1  1096 ? 3.021   46.352  83.658  1.00 13.68 ? 1094 TYR   B CA    1 
ATOM   16994 C  C     . TYR   B  1  1096 ? 2.804   47.852  83.588  1.00 15.49 ? 1094 TYR   B C     1 
ATOM   16995 O  O     . TYR   B  1  1096 ? 1.665   48.313  83.505  1.00 15.41 ? 1094 TYR   B O     1 
ATOM   16996 C  CB    . TYR   B  1  1096 ? 2.620   45.656  82.357  1.00 14.15 ? 1094 TYR   B CB    1 
ATOM   16997 C  CG    . TYR   B  1  1096 ? 3.256   46.201  81.119  1.00 15.59 ? 1094 TYR   B CG    1 
ATOM   16998 C  CD1   . TYR   B  1  1096 ? 4.505   45.758  80.701  1.00 15.52 ? 1094 TYR   B CD1   1 
ATOM   16999 C  CD2   . TYR   B  1  1096 ? 2.590   47.123  80.338  1.00 17.91 ? 1094 TYR   B CD2   1 
ATOM   17000 C  CE1   . TYR   B  1  1096 ? 5.085   46.246  79.547  1.00 16.45 ? 1094 TYR   B CE1   1 
ATOM   17001 C  CE2   . TYR   B  1  1096 ? 3.154   47.604  79.163  1.00 17.48 ? 1094 TYR   B CE2   1 
ATOM   17002 C  CZ    . TYR   B  1  1096 ? 4.402   47.160  78.784  1.00 17.78 ? 1094 TYR   B CZ    1 
ATOM   17003 O  OH    . TYR   B  1  1096 ? 4.968   47.641  77.631  1.00 17.50 ? 1094 TYR   B OH    1 
ATOM   17004 N  N     . THR   B  1  1097 ? 3.888   48.612  83.685  1.00 14.47 ? 1095 THR   B N     1 
ATOM   17005 C  CA    . THR   B  1  1097 ? 3.792   50.055  83.813  1.00 15.08 ? 1095 THR   B CA    1 
ATOM   17006 C  C     . THR   B  1  1097 ? 4.822   50.707  82.909  1.00 13.38 ? 1095 THR   B C     1 
ATOM   17007 O  O     . THR   B  1  1097 ? 5.907   50.168  82.683  1.00 15.79 ? 1095 THR   B O     1 
ATOM   17008 C  CB    . THR   B  1  1097 ? 4.030   50.488  85.260  1.00 19.30 ? 1095 THR   B CB    1 
ATOM   17009 O  OG1   . THR   B  1  1097 ? 5.324   50.054  85.689  1.00 22.26 ? 1095 THR   B OG1   1 
ATOM   17010 C  CG2   . THR   B  1  1097 ? 3.021   49.849  86.170  1.00 19.41 ? 1095 THR   B CG2   1 
ATOM   17011 N  N     . LEU   B  1  1098 ? 4.491   51.890  82.410  1.00 14.83 ? 1096 LEU   B N     1 
ATOM   17012 C  CA    . LEU   B  1  1098 ? 5.415   52.640  81.572  1.00 13.79 ? 1096 LEU   B CA    1 
ATOM   17013 C  C     . LEU   B  1  1098 ? 5.844   53.882  82.326  1.00 14.80 ? 1096 LEU   B C     1 
ATOM   17014 O  O     . LEU   B  1  1098 ? 5.007   54.699  82.723  1.00 15.67 ? 1096 LEU   B O     1 
ATOM   17015 C  CB    . LEU   B  1  1098 ? 4.797   53.023  80.233  1.00 13.83 ? 1096 LEU   B CB    1 
ATOM   17016 C  CG    . LEU   B  1  1098 ? 4.426   51.822  79.370  1.00 15.20 ? 1096 LEU   B CG    1 
ATOM   17017 C  CD1   . LEU   B  1  1098 ? 3.824   52.329  78.069  1.00 16.09 ? 1096 LEU   B CD1   1 
ATOM   17018 C  CD2   . LEU   B  1  1098 ? 5.634   50.964  79.091  1.00 15.84 ? 1096 LEU   B CD2   1 
ATOM   17019 N  N     . HIS   B  1  1099 ? 7.148   54.009  82.511  1.00 14.23 ? 1097 HIS   B N     1 
ATOM   17020 C  CA    . HIS   B  1  1099 ? 7.754   55.121  83.209  1.00 15.59 ? 1097 HIS   B CA    1 
ATOM   17021 C  C     . HIS   B  1  1099 ? 8.614   55.890  82.223  1.00 14.19 ? 1097 HIS   B C     1 
ATOM   17022 O  O     . HIS   B  1  1099 ? 8.851   55.448  81.097  1.00 15.67 ? 1097 HIS   B O     1 
ATOM   17023 C  CB    . HIS   B  1  1099 ? 8.649   54.596  84.326  1.00 16.51 ? 1097 HIS   B CB    1 
ATOM   17024 C  CG    . HIS   B  1  1099 ? 7.917   53.763  85.327  1.00 19.50 ? 1097 HIS   B CG    1 
ATOM   17025 N  ND1   . HIS   B  1  1099 ? 7.503   54.257  86.546  1.00 21.60 ? 1097 HIS   B ND1   1 
ATOM   17026 C  CD2   . HIS   B  1  1099 ? 7.513   52.472  85.283  1.00 22.11 ? 1097 HIS   B CD2   1 
ATOM   17027 C  CE1   . HIS   B  1  1099 ? 6.883   53.298  87.215  1.00 22.15 ? 1097 HIS   B CE1   1 
ATOM   17028 N  NE2   . HIS   B  1  1099 ? 6.877   52.206  86.471  1.00 21.77 ? 1097 HIS   B NE2   1 
ATOM   17029 N  N     . ALA   B  1  1100 ? 9.100   57.043  82.665  1.00 15.97 ? 1098 ALA   B N     1 
ATOM   17030 C  CA    . ALA   B  1  1100 ? 10.105  57.738  81.876  1.00 17.07 ? 1098 ALA   B CA    1 
ATOM   17031 C  C     . ALA   B  1  1100 ? 11.361  56.883  81.785  1.00 17.44 ? 1098 ALA   B C     1 
ATOM   17032 O  O     . ALA   B  1  1100 ? 11.661  56.086  82.683  1.00 19.51 ? 1098 ALA   B O     1 
ATOM   17033 C  CB    . ALA   B  1  1100 ? 10.450  59.073  82.532  1.00 18.66 ? 1098 ALA   B CB    1 
ATOM   17034 N  N     . ARG   B  1  1101 ? 12.087  57.038  80.676  1.00 16.85 ? 1099 ARG   B N     1 
ATOM   17035 C  CA    . ARG   B  1  1101 ? 13.375  56.363  80.529  1.00 17.80 ? 1099 ARG   B CA    1 
ATOM   17036 C  C     . ARG   B  1  1101 ? 14.426  56.950  81.458  1.00 18.87 ? 1099 ARG   B C     1 
ATOM   17037 O  O     . ARG   B  1  1101 ? 15.243  56.215  82.023  1.00 19.88 ? 1099 ARG   B O     1 
ATOM   17038 C  CB    . ARG   B  1  1101 ? 13.855  56.447  79.078  1.00 20.76 ? 1099 ARG   B CB    1 
ATOM   17039 C  CG    . ARG   B  1  1101 ? 13.231  55.436  78.121  1.00 21.29 ? 1099 ARG   B CG    1 
ATOM   17040 C  CD    . ARG   B  1  1101 ? 14.111  54.216  77.941  1.00 25.93 ? 1099 ARG   B CD    1 
ATOM   17041 N  NE    . ARG   B  1  1101 ? 13.502  53.206  77.078  1.00 21.99 ? 1099 ARG   B NE    1 
ATOM   17042 C  CZ    . ARG   B  1  1101 ? 14.189  52.287  76.417  1.00 22.29 ? 1099 ARG   B CZ    1 
ATOM   17043 N  NH1   . ARG   B  1  1101 ? 15.507  52.213  76.508  1.00 22.30 ? 1099 ARG   B NH1   1 
ATOM   17044 N  NH2   . ARG   B  1  1101 ? 13.542  51.433  75.634  1.00 26.74 ? 1099 ARG   B NH2   1 
ATOM   17045 N  N     . GLY   B  1  1102 ? 14.423  58.268  81.633  1.00 17.74 ? 1100 GLY   B N     1 
ATOM   17046 C  CA    . GLY   B  1  1102 ? 15.476  58.906  82.392  1.00 19.04 ? 1100 GLY   B CA    1 
ATOM   17047 C  C     . GLY   B  1  1102 ? 15.900  60.196  81.727  1.00 19.77 ? 1100 GLY   B C     1 
ATOM   17048 O  O     . GLY   B  1  1102 ? 15.070  61.063  81.442  1.00 20.70 ? 1100 GLY   B O     1 
ATOM   17049 N  N     . ARG   B  1  1103 ? 17.191  60.345  81.467  1.00 17.77 ? 1101 ARG   B N     1 
ATOM   17050 C  CA    . ARG   B  1  1103 ? 17.677  61.524  80.773  1.00 19.56 ? 1101 ARG   B CA    1 
ATOM   17051 C  C     . ARG   B  1  1103 ? 18.010  61.141  79.340  1.00 18.30 ? 1101 ARG   B C     1 
ATOM   17052 O  O     . ARG   B  1  1103 ? 18.738  60.170  79.102  1.00 19.30 ? 1101 ARG   B O     1 
ATOM   17053 C  CB    . ARG   B  1  1103 ? 18.906  62.119  81.458  1.00 18.66 ? 1101 ARG   B CB    1 
ATOM   17054 C  CG    . ARG   B  1  1103 ? 19.330  63.423  80.802  1.00 21.26 ? 1101 ARG   B CG    1 
ATOM   17055 C  CD    . ARG   B  1  1103 ? 20.344  64.184  81.642  1.00 26.76 ? 1101 ARG   B CD    1 
ATOM   17056 N  NE    . ARG   B  1  1103 ? 19.697  64.961  82.690  1.00 32.41 ? 1101 ARG   B NE    1 
ATOM   17057 C  CZ    . ARG   B  1  1103 ? 19.819  64.728  83.986  1.00 34.10 ? 1101 ARG   B CZ    1 
ATOM   17058 N  NH1   . ARG   B  1  1103 ? 20.584  63.748  84.442  1.00 41.87 ? 1101 ARG   B NH1   1 
ATOM   17059 N  NH2   . ARG   B  1  1103 ? 19.170  65.511  84.847  1.00 32.87 ? 1101 ARG   B NH2   1 
ATOM   17060 N  N     . ILE   B  1  1104 ? 17.446  61.878  78.397  1.00 15.32 ? 1102 ILE   B N     1 
ATOM   17061 C  CA    . ILE   B  1  1104 ? 17.610  61.582  76.982  1.00 16.80 ? 1102 ILE   B CA    1 
ATOM   17062 C  C     . ILE   B  1  1104 ? 18.630  62.551  76.414  1.00 17.67 ? 1102 ILE   B C     1 
ATOM   17063 O  O     . ILE   B  1  1104 ? 18.537  63.764  76.636  1.00 17.29 ? 1102 ILE   B O     1 
ATOM   17064 C  CB    . ILE   B  1  1104 ? 16.276  61.698  76.234  1.00 17.15 ? 1102 ILE   B CB    1 
ATOM   17065 C  CG1   . ILE   B  1  1104 ? 15.212  60.859  76.951  1.00 17.09 ? 1102 ILE   B CG1   1 
ATOM   17066 C  CG2   . ILE   B  1  1104 ? 16.458  61.265  74.771  1.00 17.66 ? 1102 ILE   B CG2   1 
ATOM   17067 C  CD1   . ILE   B  1  1104 ? 15.486  59.367  76.942  1.00 17.10 ? 1102 ILE   B CD1   1 
ATOM   17068 N  N     . LEU   B  1  1105 ? 19.602  62.018  75.684  1.00 16.08 ? 1103 LEU   B N     1 
ATOM   17069 C  CA    . LEU   B  1  1105 ? 20.554  62.861  74.978  1.00 17.77 ? 1103 LEU   B CA    1 
ATOM   17070 C  C     . LEU   B  1  1105 ? 19.888  63.393  73.713  1.00 16.21 ? 1103 LEU   B C     1 
ATOM   17071 O  O     . LEU   B  1  1105 ? 19.378  62.620  72.901  1.00 17.49 ? 1103 LEU   B O     1 
ATOM   17072 C  CB    . LEU   B  1  1105 ? 21.790  62.036  74.638  1.00 17.48 ? 1103 LEU   B CB    1 
ATOM   17073 C  CG    . LEU   B  1  1105 ? 22.846  62.698  73.760  1.00 19.65 ? 1103 LEU   B CG    1 
ATOM   17074 C  CD1   . LEU   B  1  1105 ? 23.465  63.883  74.481  1.00 18.58 ? 1103 LEU   B CD1   1 
ATOM   17075 C  CD2   . LEU   B  1  1105 ? 23.907  61.668  73.375  1.00 17.96 ? 1103 LEU   B CD2   1 
ATOM   17076 N  N     . LEU   B  1  1106 ? 19.863  64.708  73.563  1.00 15.68 ? 1104 LEU   B N     1 
ATOM   17077 C  CA    . LEU   B  1  1106 ? 19.278  65.355  72.400  1.00 17.15 ? 1104 LEU   B CA    1 
ATOM   17078 C  C     . LEU   B  1  1106 ? 20.416  65.911  71.563  1.00 18.04 ? 1104 LEU   B C     1 
ATOM   17079 O  O     . LEU   B  1  1106 ? 21.247  66.674  72.067  1.00 19.25 ? 1104 LEU   B O     1 
ATOM   17080 C  CB    . LEU   B  1  1106 ? 18.342  66.493  72.804  1.00 16.72 ? 1104 LEU   B CB    1 
ATOM   17081 C  CG    . LEU   B  1  1106 ? 16.865  66.135  72.939  1.00 23.22 ? 1104 LEU   B CG    1 
ATOM   17082 C  CD1   . LEU   B  1  1106 ? 16.667  64.840  73.689  1.00 22.54 ? 1104 LEU   B CD1   1 
ATOM   17083 C  CD2   . LEU   B  1  1106 ? 16.102  67.279  73.594  1.00 18.87 ? 1104 LEU   B CD2   1 
ATOM   17084 N  N     . VAL   B  1  1107 ? 20.450  65.515  70.298  1.00 17.03 ? 1105 VAL   B N     1 
ATOM   17085 C  CA    . VAL   B  1  1107 ? 21.460  66.005  69.371  1.00 17.80 ? 1105 VAL   B CA    1 
ATOM   17086 C  C     . VAL   B  1  1107 ? 20.702  66.689  68.244  1.00 16.58 ? 1105 VAL   B C     1 
ATOM   17087 O  O     . VAL   B  1  1107 ? 20.470  66.086  67.188  1.00 18.87 ? 1105 VAL   B O     1 
ATOM   17088 C  CB    . VAL   B  1  1107 ? 22.354  64.862  68.874  1.00 17.04 ? 1105 VAL   B CB    1 
ATOM   17089 C  CG1   . VAL   B  1  1107 ? 23.524  65.422  68.076  1.00 18.91 ? 1105 VAL   B CG1   1 
ATOM   17090 C  CG2   . VAL   B  1  1107 ? 22.845  64.028  70.045  1.00 18.11 ? 1105 VAL   B CG2   1 
ATOM   17091 N  N     . PRO   B  1  1108 ? 20.272  67.928  68.439  1.00 17.77 ? 1106 PRO   B N     1 
ATOM   17092 C  CA    . PRO   B  1  1108 ? 19.527  68.632  67.401  1.00 19.91 ? 1106 PRO   B CA    1 
ATOM   17093 C  C     . PRO   B  1  1108 ? 20.465  69.276  66.395  1.00 21.65 ? 1106 PRO   B C     1 
ATOM   17094 O  O     . PRO   B  1  1108 ? 21.654  69.484  66.647  1.00 24.34 ? 1106 PRO   B O     1 
ATOM   17095 C  CB    . PRO   B  1  1108 ? 18.805  69.724  68.196  1.00 19.23 ? 1106 PRO   B CB    1 
ATOM   17096 C  CG    . PRO   B  1  1108 ? 19.770  70.032  69.295  1.00 20.19 ? 1106 PRO   B CG    1 
ATOM   17097 C  CD    . PRO   B  1  1108 ? 20.339  68.700  69.692  1.00 20.04 ? 1106 PRO   B CD    1 
ATOM   17098 N  N     . ALA   B  1  1109 ? 19.893  69.599  65.245  1.00 22.44 ? 1107 ALA   B N     1 
ATOM   17099 C  CA    . ALA   B  1  1109 ? 20.549  70.433  64.248  1.00 22.28 ? 1107 ALA   B CA    1 
ATOM   17100 C  C     . ALA   B  1  1109 ? 19.906  71.801  64.126  1.00 22.92 ? 1107 ALA   B C     1 
ATOM   17101 O  O     . ALA   B  1  1109 ? 20.603  72.801  63.934  1.00 25.15 ? 1107 ALA   B O     1 
ATOM   17102 C  CB    . ALA   B  1  1109 ? 20.495  69.742  62.879  1.00 22.94 ? 1107 ALA   B CB    1 
ATOM   17103 N  N     . THR   B  1  1110 ? 18.585  71.867  64.225  1.00 20.86 ? 1108 THR   B N     1 
ATOM   17104 C  CA    . THR   B  1  1110 ? 17.861  73.106  64.023  1.00 21.80 ? 1108 THR   B CA    1 
ATOM   17105 C  C     . THR   B  1  1110 ? 17.001  73.399  65.239  1.00 22.70 ? 1108 THR   B C     1 
ATOM   17106 O  O     . THR   B  1  1110 ? 16.700  72.515  66.046  1.00 20.62 ? 1108 THR   B O     1 
ATOM   17107 C  CB    . THR   B  1  1110 ? 16.935  73.016  62.806  1.00 24.19 ? 1108 THR   B CB    1 
ATOM   17108 O  OG1   . THR   B  1  1110 ? 15.932  72.015  63.034  1.00 23.69 ? 1108 THR   B OG1   1 
ATOM   17109 C  CG2   . THR   B  1  1110 ? 17.726  72.678  61.537  1.00 25.26 ? 1108 THR   B CG2   1 
ATOM   17110 N  N     . GLU   B  1  1111 ? 16.586  74.658  65.338  1.00 20.85 ? 1109 GLU   B N     1 
ATOM   17111 C  CA    . GLU   B  1  1111 ? 15.730  75.060  66.448  1.00 22.98 ? 1109 GLU   B CA    1 
ATOM   17112 C  C     . GLU   B  1  1111 ? 14.420  74.282  66.445  1.00 21.43 ? 1109 GLU   B C     1 
ATOM   17113 O  O     . GLU   B  1  1111 ? 13.996  73.767  67.484  1.00 21.97 ? 1109 GLU   B O     1 
ATOM   17114 C  CB    . GLU   B  1  1111 ? 15.474  76.560  66.386  1.00 22.32 ? 1109 GLU   B CB    1 
ATOM   17115 C  CG    . GLU   B  1  1111 ? 14.376  77.021  67.325  1.00 24.96 ? 1109 GLU   B CG    1 
ATOM   17116 C  CD    . GLU   B  1  1111 ? 14.189  78.520  67.288  1.00 27.15 ? 1109 GLU   B CD    1 
ATOM   17117 O  OE1   . GLU   B  1  1111 ? 14.997  79.223  67.924  1.00 29.37 ? 1109 GLU   B OE1   1 
ATOM   17118 O  OE2   . GLU   B  1  1111 ? 13.240  78.991  66.623  1.00 31.68 ? 1109 GLU   B OE2   1 
ATOM   17119 N  N     . SER   B  1  1112 ? 13.764  74.184  65.286  1.00 20.16 ? 1110 SER   B N     1 
ATOM   17120 C  CA    . SER   B  1  1112 ? 12.526  73.412  65.223  1.00 22.79 ? 1110 SER   B CA    1 
ATOM   17121 C  C     . SER   B  1  1112 ? 12.774  71.952  65.576  1.00 22.77 ? 1110 SER   B C     1 
ATOM   17122 O  O     . SER   B  1  1112 ? 11.977  71.331  66.289  1.00 22.05 ? 1110 SER   B O     1 
ATOM   17123 C  CB    . SER   B  1  1112 ? 11.888  73.527  63.840  1.00 26.79 ? 1110 SER   B CB    1 
ATOM   17124 O  OG    . SER   B  1  1112 ? 10.711  72.730  63.761  1.00 27.63 ? 1110 SER   B OG    1 
ATOM   17125 N  N     . GLY   B  1  1113 ? 13.883  71.388  65.098  1.00 20.95 ? 1111 GLY   B N     1 
ATOM   17126 C  CA    . GLY   B  1  1113 ? 14.207  70.021  65.463  1.00 20.54 ? 1111 GLY   B CA    1 
ATOM   17127 C  C     . GLY   B  1  1113 ? 14.360  69.856  66.961  1.00 19.28 ? 1111 GLY   B C     1 
ATOM   17128 O  O     . GLY   B  1  1113 ? 13.870  68.885  67.541  1.00 19.64 ? 1111 GLY   B O     1 
ATOM   17129 N  N     . LEU   B  1  1114 ? 15.049  70.802  67.605  1.00 18.91 ? 1112 LEU   B N     1 
ATOM   17130 C  CA    . LEU   B  1  1114 ? 15.202  70.754  69.056  1.00 18.28 ? 1112 LEU   B CA    1 
ATOM   17131 C  C     . LEU   B  1  1114 ? 13.848  70.806  69.752  1.00 19.16 ? 1112 LEU   B C     1 
ATOM   17132 O  O     . LEU   B  1  1114 ? 13.607  70.055  70.704  1.00 17.68 ? 1112 LEU   B O     1 
ATOM   17133 C  CB    . LEU   B  1  1114 ? 16.081  71.910  69.531  1.00 18.92 ? 1112 LEU   B CB    1 
ATOM   17134 C  CG    . LEU   B  1  1114 ? 16.185  72.095  71.042  1.00 20.31 ? 1112 LEU   B CG    1 
ATOM   17135 C  CD1   . LEU   B  1  1114 ? 16.692  70.826  71.701  1.00 19.51 ? 1112 LEU   B CD1   1 
ATOM   17136 C  CD2   . LEU   B  1  1114 ? 17.077  73.290  71.378  1.00 24.43 ? 1112 LEU   B CD2   1 
ATOM   17137 N  N     . TYR   B  1  1115 ? 12.955  71.678  69.284  1.00 19.75 ? 1113 TYR   B N     1 
ATOM   17138 C  CA    . TYR   B  1  1115 ? 11.631  71.765  69.900  1.00 20.20 ? 1113 TYR   B CA    1 
ATOM   17139 C  C     . TYR   B  1  1115 ? 10.872  70.454  69.757  1.00 19.27 ? 1113 TYR   B C     1 
ATOM   17140 O  O     . TYR   B  1  1115 ? 10.217  70.007  70.704  1.00 19.95 ? 1113 TYR   B O     1 
ATOM   17141 C  CB    . TYR   B  1  1115 ? 10.827  72.907  69.286  1.00 21.06 ? 1113 TYR   B CB    1 
ATOM   17142 C  CG    . TYR   B  1  1115 ? 11.342  74.291  69.585  1.00 21.29 ? 1113 TYR   B CG    1 
ATOM   17143 C  CD1   . TYR   B  1  1115 ? 12.280  74.518  70.580  1.00 20.09 ? 1113 TYR   B CD1   1 
ATOM   17144 C  CD2   . TYR   B  1  1115 ? 10.882  75.373  68.860  1.00 22.88 ? 1113 TYR   B CD2   1 
ATOM   17145 C  CE1   . TYR   B  1  1115 ? 12.743  75.808  70.842  1.00 23.32 ? 1113 TYR   B CE1   1 
ATOM   17146 C  CE2   . TYR   B  1  1115 ? 11.325  76.652  69.115  1.00 25.26 ? 1113 TYR   B CE2   1 
ATOM   17147 C  CZ    . TYR   B  1  1115 ? 12.261  76.866  70.099  1.00 26.17 ? 1113 TYR   B CZ    1 
ATOM   17148 O  OH    . TYR   B  1  1115 ? 12.699  78.153  70.322  1.00 29.94 ? 1113 TYR   B OH    1 
ATOM   17149 N  N     . HIS   B  1  1116 ? 10.948  69.824  68.582  1.00 18.42 ? 1114 HIS   B N     1 
ATOM   17150 C  CA    . HIS   B  1  1116 ? 10.300  68.529  68.404  1.00 19.48 ? 1114 HIS   B CA    1 
ATOM   17151 C  C     . HIS   B  1  1116 ? 10.941  67.466  69.283  1.00 20.47 ? 1114 HIS   B C     1 
ATOM   17152 O  O     . HIS   B  1  1116 ? 10.245  66.616  69.844  1.00 20.15 ? 1114 HIS   B O     1 
ATOM   17153 C  CB    . HIS   B  1  1116 ? 10.352  68.097  66.942  1.00 18.08 ? 1114 HIS   B CB    1 
ATOM   17154 C  CG    . HIS   B  1  1116 ? 9.315   68.748  66.085  1.00 22.22 ? 1114 HIS   B CG    1 
ATOM   17155 N  ND1   . HIS   B  1  1116 ? 9.500   69.980  65.496  1.00 24.60 ? 1114 HIS   B ND1   1 
ATOM   17156 C  CD2   . HIS   B  1  1116 ? 8.080   68.336  65.717  1.00 23.66 ? 1114 HIS   B CD2   1 
ATOM   17157 C  CE1   . HIS   B  1  1116 ? 8.422   70.301  64.804  1.00 25.28 ? 1114 HIS   B CE1   1 
ATOM   17158 N  NE2   . HIS   B  1  1116 ? 7.549   69.318  64.915  1.00 26.89 ? 1114 HIS   B NE2   1 
ATOM   17159 N  N     . GLN   B  1  1117 ? 12.272  67.477  69.400  1.00 16.60 ? 1115 GLN   B N     1 
ATOM   17160 C  CA    . GLN   B  1  1117 ? 12.920  66.488  70.254  1.00 15.73 ? 1115 GLN   B CA    1 
ATOM   17161 C  C     . GLN   B  1  1117 ? 12.526  66.690  71.705  1.00 16.60 ? 1115 GLN   B C     1 
ATOM   17162 O  O     . GLN   B  1  1117 ? 12.242  65.721  72.420  1.00 16.24 ? 1115 GLN   B O     1 
ATOM   17163 C  CB    . GLN   B  1  1117 ? 14.437  66.604  70.121  1.00 16.43 ? 1115 GLN   B CB    1 
ATOM   17164 C  CG    . GLN   B  1  1117 ? 14.985  66.128  68.804  1.00 17.00 ? 1115 GLN   B CG    1 
ATOM   17165 C  CD    . GLN   B  1  1117 ? 16.495  66.293  68.720  1.00 17.96 ? 1115 GLN   B CD    1 
ATOM   17166 O  OE1   . GLN   B  1  1117 ? 17.103  66.973  69.538  1.00 18.38 ? 1115 GLN   B OE1   1 
ATOM   17167 N  NE2   . GLN   B  1  1117 ? 17.101  65.666  67.722  1.00 18.46 ? 1115 GLN   B NE2   1 
ATOM   17168 N  N     . LEU   B  1  1118 ? 12.541  67.944  72.160  1.00 16.18 ? 1116 LEU   B N     1 
ATOM   17169 C  CA    . LEU   B  1  1118 ? 12.124  68.248  73.522  1.00 15.76 ? 1116 LEU   B CA    1 
ATOM   17170 C  C     . LEU   B  1  1118 ? 10.694  67.809  73.759  1.00 17.28 ? 1116 LEU   B C     1 
ATOM   17171 O  O     . LEU   B  1  1118 ? 10.390  67.228  74.800  1.00 17.92 ? 1116 LEU   B O     1 
ATOM   17172 C  CB    . LEU   B  1  1118 ? 12.237  69.745  73.783  1.00 18.80 ? 1116 LEU   B CB    1 
ATOM   17173 C  CG    . LEU   B  1  1118 ? 13.630  70.267  74.083  1.00 23.14 ? 1116 LEU   B CG    1 
ATOM   17174 C  CD1   . LEU   B  1  1118 ? 13.623  71.778  73.979  1.00 23.86 ? 1116 LEU   B CD1   1 
ATOM   17175 C  CD2   . LEU   B  1  1118 ? 14.037  69.835  75.472  1.00 22.86 ? 1116 LEU   B CD2   1 
ATOM   17176 N  N     . ALA   B  1  1119 ? 9.810   68.063  72.796  1.00 18.92 ? 1117 ALA   B N     1 
ATOM   17177 C  CA    . ALA   B  1  1119 ? 8.416   67.663  72.956  1.00 18.69 ? 1117 ALA   B CA    1 
ATOM   17178 C  C     . ALA   B  1  1119 ? 8.317   66.159  73.171  1.00 18.67 ? 1117 ALA   B C     1 
ATOM   17179 O  O     . ALA   B  1  1119 ? 7.643   65.699  74.103  1.00 17.79 ? 1117 ALA   B O     1 
ATOM   17180 C  CB    . ALA   B  1  1119 ? 7.594   68.100  71.741  1.00 18.56 ? 1117 ALA   B CB    1 
ATOM   17181 N  N     . ALA   B  1  1120 ? 9.004   65.379  72.333  1.00 15.69 ? 1118 ALA   B N     1 
ATOM   17182 C  CA    . ALA   B  1  1120 ? 8.952   63.927  72.461  1.00 15.08 ? 1118 ALA   B CA    1 
ATOM   17183 C  C     . ALA   B  1  1120 ? 9.492   63.475  73.810  1.00 17.23 ? 1118 ALA   B C     1 
ATOM   17184 O  O     . ALA   B  1  1120 ? 8.874   62.650  74.494  1.00 17.36 ? 1118 ALA   B O     1 
ATOM   17185 C  CB    . ALA   B  1  1120 ? 9.736   63.264  71.325  1.00 17.33 ? 1118 ALA   B CB    1 
ATOM   17186 N  N     . ALA   B  1  1121 ? 10.657  63.996  74.209  1.00 14.88 ? 1119 ALA   B N     1 
ATOM   17187 C  CA    . ALA   B  1  1121 ? 11.254  63.570  75.468  1.00 16.99 ? 1119 ALA   B CA    1 
ATOM   17188 C  C     . ALA   B  1  1121 ? 10.435  64.022  76.676  1.00 14.23 ? 1119 ALA   B C     1 
ATOM   17189 O  O     . ALA   B  1  1121 ? 10.286  63.262  77.644  1.00 14.99 ? 1119 ALA   B O     1 
ATOM   17190 C  CB    . ALA   B  1  1121 ? 12.677  64.096  75.566  1.00 17.68 ? 1119 ALA   B CB    1 
ATOM   17191 N  N     . LEU   B  1  1122 ? 9.946   65.267  76.669  1.00 15.57 ? 1120 LEU   B N     1 
ATOM   17192 C  CA    . LEU   B  1  1122 ? 9.178   65.744  77.816  1.00 16.03 ? 1120 LEU   B CA    1 
ATOM   17193 C  C     . LEU   B  1  1122 ? 7.852   65.018  77.925  1.00 14.95 ? 1120 LEU   B C     1 
ATOM   17194 O  O     . LEU   B  1  1122 ? 7.409   64.702  79.037  1.00 16.44 ? 1120 LEU   B O     1 
ATOM   17195 C  CB    . LEU   B  1  1122 ? 8.939   67.250  77.743  1.00 15.89 ? 1120 LEU   B CB    1 
ATOM   17196 C  CG    . LEU   B  1  1122 ? 10.186  68.121  77.852  1.00 19.43 ? 1120 LEU   B CG    1 
ATOM   17197 C  CD1   . LEU   B  1  1122 ? 9.826   69.567  77.566  1.00 19.00 ? 1120 LEU   B CD1   1 
ATOM   17198 C  CD2   . LEU   B  1  1122 ? 10.859  67.971  79.223  1.00 20.67 ? 1120 LEU   B CD2   1 
ATOM   17199 N  N     . ALA   B  1  1123 ? 7.221   64.732  76.782  1.00 15.85 ? 1121 ALA   B N     1 
ATOM   17200 C  CA    . ALA   B  1  1123 ? 5.910   64.085  76.802  1.00 15.95 ? 1121 ALA   B CA    1 
ATOM   17201 C  C     . ALA   B  1  1123 ? 5.990   62.703  77.424  1.00 17.10 ? 1121 ALA   B C     1 
ATOM   17202 O  O     . ALA   B  1  1123 ? 4.984   62.190  77.923  1.00 16.37 ? 1121 ALA   B O     1 
ATOM   17203 C  CB    . ALA   B  1  1123 ? 5.376   63.947  75.384  1.00 16.63 ? 1121 ALA   B CB    1 
ATOM   17204 N  N     . THR   B  1  1124 ? 7.160   62.082  77.370  1.00 15.23 ? 1122 THR   B N     1 
ATOM   17205 C  CA    . THR   B  1  1124 ? 7.397   60.770  77.941  1.00 13.65 ? 1122 THR   B CA    1 
ATOM   17206 C  C     . THR   B  1  1124 ? 8.086   60.850  79.298  1.00 12.69 ? 1122 THR   B C     1 
ATOM   17207 O  O     . THR   B  1  1124 ? 8.603   59.843  79.778  1.00 15.94 ? 1122 THR   B O     1 
ATOM   17208 C  CB    . THR   B  1  1124 ? 8.185   59.911  76.947  1.00 16.08 ? 1122 THR   B CB    1 
ATOM   17209 O  OG1   . THR   B  1  1124 ? 9.276   60.675  76.405  1.00 15.55 ? 1122 THR   B OG1   1 
ATOM   17210 C  CG2   . THR   B  1  1124 ? 7.254   59.474  75.794  1.00 15.47 ? 1122 THR   B CG2   1 
ATOM   17211 N  N     . GLY   B  1  1125 ? 8.102   62.028  79.914  1.00 14.69 ? 1123 GLY   B N     1 
ATOM   17212 C  CA    . GLY   B  1  1125 ? 8.494   62.196  81.300  1.00 16.08 ? 1123 GLY   B CA    1 
ATOM   17213 C  C     . GLY   B  1  1125 ? 9.977   62.341  81.526  1.00 15.66 ? 1123 GLY   B C     1 
ATOM   17214 O  O     . GLY   B  1  1125 ? 10.420  62.345  82.677  1.00 16.10 ? 1123 GLY   B O     1 
ATOM   17215 N  N     . ASN   B  1  1126 ? 10.754  62.457  80.469  1.00 15.07 ? 1124 ASN   B N     1 
ATOM   17216 C  CA    . ASN   B  1  1126 ? 12.198  62.433  80.592  1.00 13.70 ? 1124 ASN   B CA    1 
ATOM   17217 C  C     . ASN   B  1  1126 ? 12.757  63.824  80.840  1.00 15.17 ? 1124 ASN   B C     1 
ATOM   17218 O  O     . ASN   B  1  1126 ? 12.133  64.842  80.546  1.00 16.94 ? 1124 ASN   B O     1 
ATOM   17219 C  CB    . ASN   B  1  1126 ? 12.800  61.875  79.312  1.00 14.84 ? 1124 ASN   B CB    1 
ATOM   17220 C  CG    . ASN   B  1  1126 ? 12.330  60.467  79.023  1.00 14.77 ? 1124 ASN   B CG    1 
ATOM   17221 O  OD1   . ASN   B  1  1126 ? 12.693  59.536  79.723  1.00 17.69 ? 1124 ASN   B OD1   1 
ATOM   17222 N  ND2   . ASN   B  1  1126 ? 11.530  60.306  77.977  1.00 14.47 ? 1124 ASN   B ND2   1 
ATOM   17223 N  N     . SER   B  1  1127 ? 13.963  63.840  81.402  1.00 16.19 ? 1125 SER   B N     1 
ATOM   17224 C  CA    . SER   B  1  1127 ? 14.810  65.013  81.332  1.00 16.00 ? 1125 SER   B CA    1 
ATOM   17225 C  C     . SER   B  1  1127 ? 15.692  64.881  80.095  1.00 16.38 ? 1125 SER   B C     1 
ATOM   17226 O  O     . SER   B  1  1127 ? 15.732  63.838  79.446  1.00 16.96 ? 1125 SER   B O     1 
ATOM   17227 C  CB    . SER   B  1  1127 ? 15.666  65.134  82.592  1.00 19.90 ? 1125 SER   B CB    1 
ATOM   17228 O  OG    . SER   B  1  1127 ? 16.490  63.992  82.760  1.00 23.07 ? 1125 SER   B OG    1 
ATOM   17229 N  N     . VAL   B  1  1128 ? 16.386  65.955  79.757  1.00 18.05 ? 1126 VAL   B N     1 
ATOM   17230 C  CA    . VAL   B  1  1128 ? 17.225  65.926  78.567  1.00 16.87 ? 1126 VAL   B CA    1 
ATOM   17231 C  C     . VAL   B  1  1128 ? 18.579  66.537  78.858  1.00 19.31 ? 1126 VAL   B C     1 
ATOM   17232 O  O     . VAL   B  1  1128 ? 18.729  67.402  79.729  1.00 20.70 ? 1126 VAL   B O     1 
ATOM   17233 C  CB    . VAL   B  1  1128 ? 16.584  66.627  77.353  1.00 17.73 ? 1126 VAL   B CB    1 
ATOM   17234 C  CG1   . VAL   B  1  1128 ? 15.245  65.983  77.004  1.00 16.93 ? 1126 VAL   B CG1   1 
ATOM   17235 C  CG2   . VAL   B  1  1128 ? 16.414  68.121  77.624  1.00 18.84 ? 1126 VAL   B CG2   1 
ATOM   17236 N  N     . ALA   B  1  1129 ? 19.569  66.084  78.098  1.00 17.58 ? 1127 ALA   B N     1 
ATOM   17237 C  CA    . ALA   B  1  1129 ? 20.837  66.780  77.964  1.00 19.96 ? 1127 ALA   B CA    1 
ATOM   17238 C  C     . ALA   B  1  1129 ? 20.973  67.107  76.491  1.00 17.17 ? 1127 ALA   B C     1 
ATOM   17239 O  O     . ALA   B  1  1129 ? 20.929  66.201  75.649  1.00 17.85 ? 1127 ALA   B O     1 
ATOM   17240 C  CB    . ALA   B  1  1129 ? 21.996  65.905  78.427  1.00 20.42 ? 1127 ALA   B CB    1 
ATOM   17241 N  N     . ILE   B  1  1130 ? 21.080  68.390  76.176  1.00 16.42 ? 1128 ILE   B N     1 
ATOM   17242 C  CA    . ILE   B  1  1130 ? 21.115  68.843  74.795  1.00 17.16 ? 1128 ILE   B CA    1 
ATOM   17243 C  C     . ILE   B  1  1130 ? 22.560  69.087  74.411  1.00 18.33 ? 1128 ILE   B C     1 
ATOM   17244 O  O     . ILE   B  1  1130 ? 23.322  69.700  75.171  1.00 17.96 ? 1128 ILE   B O     1 
ATOM   17245 C  CB    . ILE   B  1  1130 ? 20.299  70.123  74.584  1.00 18.52 ? 1128 ILE   B CB    1 
ATOM   17246 C  CG1   . ILE   B  1  1130 ? 18.870  69.959  75.125  1.00 19.86 ? 1128 ILE   B CG1   1 
ATOM   17247 C  CG2   . ILE   B  1  1130 ? 20.266  70.457  73.095  1.00 17.41 ? 1128 ILE   B CG2   1 
ATOM   17248 C  CD1   . ILE   B  1  1130 ? 18.167  71.273  75.295  1.00 20.76 ? 1128 ILE   B CD1   1 
ATOM   17249 N  N     . ASP   B  1  1131 ? 22.932  68.609  73.234  1.00 17.06 ? 1129 ASP   B N     1 
ATOM   17250 C  CA    . ASP   B  1  1131 ? 24.289  68.795  72.744  1.00 16.77 ? 1129 ASP   B CA    1 
ATOM   17251 C  C     . ASP   B  1  1131 ? 24.615  70.278  72.611  1.00 17.15 ? 1129 ASP   B C     1 
ATOM   17252 O  O     . ASP   B  1  1131 ? 24.040  70.976  71.773  1.00 20.17 ? 1129 ASP   B O     1 
ATOM   17253 C  CB    . ASP   B  1  1131 ? 24.392  68.111  71.391  1.00 18.27 ? 1129 ASP   B CB    1 
ATOM   17254 C  CG    . ASP   B  1  1131 ? 25.740  68.284  70.757  1.00 20.28 ? 1129 ASP   B CG    1 
ATOM   17255 O  OD1   . ASP   B  1  1131 ? 26.732  68.421  71.496  1.00 20.35 ? 1129 ASP   B OD1   1 
ATOM   17256 O  OD2   . ASP   B  1  1131 ? 25.779  68.284  69.518  1.00 21.65 ? 1129 ASP   B OD2   1 
ATOM   17257 N  N     . ALA   B  1  1132 ? 25.567  70.758  73.418  1.00 19.21 ? 1130 ALA   B N     1 
ATOM   17258 C  CA    . ALA   B  1  1132 ? 25.945  72.169  73.348  1.00 21.07 ? 1130 ALA   B CA    1 
ATOM   17259 C  C     . ALA   B  1  1132 ? 26.554  72.525  72.000  1.00 22.34 ? 1130 ALA   B C     1 
ATOM   17260 O  O     . ALA   B  1  1132 ? 26.461  73.680  71.561  1.00 23.95 ? 1130 ALA   B O     1 
ATOM   17261 C  CB    . ALA   B  1  1132 ? 26.923  72.505  74.476  1.00 22.28 ? 1130 ALA   B CB    1 
ATOM   17262 N  N     . ALA   B  1  1133 ? 27.176  71.557  71.325  1.00 22.23 ? 1131 ALA   B N     1 
ATOM   17263 C  CA    . ALA   B  1  1133 ? 27.757  71.844  70.021  1.00 24.41 ? 1131 ALA   B CA    1 
ATOM   17264 C  C     . ALA   B  1  1133 ? 26.711  72.197  68.973  1.00 25.22 ? 1131 ALA   B C     1 
ATOM   17265 O  O     . ALA   B  1  1133 ? 27.077  72.669  67.895  1.00 25.78 ? 1131 ALA   B O     1 
ATOM   17266 C  CB    . ALA   B  1  1133 ? 28.615  70.672  69.535  1.00 24.93 ? 1131 ALA   B CB    1 
ATOM   17267 N  N     . SER   B  1  1134 ? 25.422  71.984  69.261  1.00 21.32 ? 1132 SER   B N     1 
ATOM   17268 C  CA    . SER   B  1  1134 ? 24.392  72.413  68.328  1.00 22.01 ? 1132 SER   B CA    1 
ATOM   17269 C  C     . SER   B  1  1134 ? 24.336  73.930  68.203  1.00 20.55 ? 1132 SER   B C     1 
ATOM   17270 O  O     . SER   B  1  1134 ? 23.824  74.436  67.203  1.00 22.70 ? 1132 SER   B O     1 
ATOM   17271 C  CB    . SER   B  1  1134 ? 23.021  71.900  68.776  1.00 21.77 ? 1132 SER   B CB    1 
ATOM   17272 O  OG    . SER   B  1  1134 ? 22.635  72.539  69.982  1.00 21.81 ? 1132 SER   B OG    1 
ATOM   17273 N  N     . GLY   B  1  1135 ? 24.836  74.663  69.192  1.00 22.43 ? 1133 GLY   B N     1 
ATOM   17274 C  CA    . GLY   B  1  1135 ? 24.787  76.109  69.122  1.00 21.73 ? 1133 GLY   B CA    1 
ATOM   17275 C  C     . GLY   B  1  1135 ? 23.400  76.698  69.262  1.00 22.97 ? 1133 GLY   B C     1 
ATOM   17276 O  O     . GLY   B  1  1135 ? 23.191  77.867  68.914  1.00 25.82 ? 1133 GLY   B O     1 
ATOM   17277 N  N     . LEU   B  1  1136 ? 22.447  75.925  69.785  1.00 24.01 ? 1134 LEU   B N     1 
ATOM   17278 C  CA    . LEU   B  1  1136 ? 21.045  76.324  69.822  1.00 23.65 ? 1134 LEU   B CA    1 
ATOM   17279 C  C     . LEU   B  1  1136 ? 20.622  76.876  71.179  1.00 26.15 ? 1134 LEU   B C     1 
ATOM   17280 O  O     . LEU   B  1  1136 ? 19.422  76.953  71.460  1.00 24.59 ? 1134 LEU   B O     1 
ATOM   17281 C  CB    . LEU   B  1  1136 ? 20.159  75.144  69.415  1.00 21.79 ? 1134 LEU   B CB    1 
ATOM   17282 C  CG    . LEU   B  1  1136 ? 20.331  74.624  67.986  1.00 23.40 ? 1134 LEU   B CG    1 
ATOM   17283 C  CD1   . LEU   B  1  1136 ? 19.540  73.339  67.765  1.00 24.87 ? 1134 LEU   B CD1   1 
ATOM   17284 C  CD2   . LEU   B  1  1136 ? 19.905  75.694  66.985  1.00 24.89 ? 1134 LEU   B CD2   1 
ATOM   17285 N  N     . GLN   B  1  1137 ? 21.578  77.277  72.017  1.00 23.37 ? 1135 GLN   B N     1 
ATOM   17286 C  CA    . GLN   B  1  1137 ? 21.251  77.716  73.371  1.00 24.83 ? 1135 GLN   B CA    1 
ATOM   17287 C  C     . GLN   B  1  1137 ? 20.262  78.881  73.379  1.00 28.57 ? 1135 GLN   B C     1 
ATOM   17288 O  O     . GLN   B  1  1137 ? 19.371  78.938  74.235  1.00 28.64 ? 1135 GLN   B O     1 
ATOM   17289 C  CB    . GLN   B  1  1137 ? 22.523  78.070  74.137  1.00 28.71 ? 1135 GLN   B CB    1 
ATOM   17290 C  CG    . GLN   B  1  1137 ? 23.389  76.868  74.485  1.00 26.65 ? 1135 GLN   B CG    1 
ATOM   17291 C  CD    . GLN   B  1  1137 ? 24.350  76.473  73.369  1.00 26.38 ? 1135 GLN   B CD    1 
ATOM   17292 O  OE1   . GLN   B  1  1137 ? 24.227  76.916  72.228  1.00 25.82 ? 1135 GLN   B OE1   1 
ATOM   17293 N  NE2   . GLN   B  1  1137 ? 25.314  75.625  73.705  1.00 28.42 ? 1135 GLN   B NE2   1 
ATOM   17294 N  N     . ALA   B  1  1138 ? 20.379  79.805  72.423  1.00 25.86 ? 1136 ALA   B N     1 
ATOM   17295 C  CA    . ALA   B  1  1138 ? 19.477  80.954  72.411  1.00 27.43 ? 1136 ALA   B CA    1 
ATOM   17296 C  C     . ALA   B  1  1138 ? 18.037  80.562  72.110  1.00 30.06 ? 1136 ALA   B C     1 
ATOM   17297 O  O     . ALA   B  1  1138 ? 17.128  81.356  72.367  1.00 30.85 ? 1136 ALA   B O     1 
ATOM   17298 C  CB    . ALA   B  1  1138 ? 19.951  81.996  71.402  1.00 28.93 ? 1136 ALA   B CB    1 
ATOM   17299 N  N     . SER   B  1  1139 ? 17.813  79.361  71.573  1.00 26.29 ? 1137 SER   B N     1 
ATOM   17300 C  CA    . SER   B  1  1139 ? 16.467  78.914  71.239  1.00 26.14 ? 1137 SER   B CA    1 
ATOM   17301 C  C     . SER   B  1  1139 ? 15.624  78.627  72.474  1.00 28.53 ? 1137 SER   B C     1 
ATOM   17302 O  O     . SER   B  1  1139 ? 14.394  78.557  72.365  1.00 26.32 ? 1137 SER   B O     1 
ATOM   17303 C  CB    . SER   B  1  1139 ? 16.537  77.649  70.381  1.00 25.27 ? 1137 SER   B CB    1 
ATOM   17304 O  OG    . SER   B  1  1139 ? 17.033  77.943  69.088  1.00 29.84 ? 1137 SER   B OG    1 
ATOM   17305 N  N     . LEU   B  1  1140 ? 16.254  78.431  73.630  1.00 27.13 ? 1138 LEU   B N     1 
ATOM   17306 C  CA    . LEU   B  1  1140 ? 15.555  78.170  74.881  1.00 30.64 ? 1138 LEU   B CA    1 
ATOM   17307 C  C     . LEU   B  1  1140 ? 15.603  79.370  75.818  1.00 31.07 ? 1138 LEU   B C     1 
ATOM   17308 O  O     . LEU   B  1  1140 ? 15.567  79.212  77.039  1.00 34.78 ? 1138 LEU   B O     1 
ATOM   17309 C  CB    . LEU   B  1  1140 ? 16.100  76.917  75.565  1.00 29.10 ? 1138 LEU   B CB    1 
ATOM   17310 C  CG    . LEU   B  1  1140 ? 15.952  75.642  74.735  1.00 30.38 ? 1138 LEU   B CG    1 
ATOM   17311 C  CD1   . LEU   B  1  1140 ? 16.389  74.411  75.524  1.00 27.70 ? 1138 LEU   B CD1   1 
ATOM   17312 C  CD2   . LEU   B  1  1140 ? 14.521  75.500  74.214  1.00 30.04 ? 1138 LEU   B CD2   1 
ATOM   17313 N  N     . LYS   B  1  1141 ? 15.690  80.575  75.262  1.00 35.48 ? 1139 LYS   B N     1 
ATOM   17314 C  CA    . LYS   B  1  1141 ? 15.672  81.773  76.089  1.00 33.36 ? 1139 LYS   B CA    1 
ATOM   17315 C  C     . LYS   B  1  1141 ? 14.297  81.938  76.724  1.00 36.60 ? 1139 LYS   B C     1 
ATOM   17316 O  O     . LYS   B  1  1141 ? 13.268  81.738  76.073  1.00 37.56 ? 1139 LYS   B O     1 
ATOM   17317 C  CB    . LYS   B  1  1141 ? 15.997  83.000  75.236  1.00 34.77 ? 1139 LYS   B CB    1 
ATOM   17318 N  N     . ASN   B  1  1142 ? 14.286  82.279  78.016  1.00 37.56 ? 1140 ASN   B N     1 
ATOM   17319 C  CA    . ASN   B  1  1142 ? 13.056  82.535  78.768  1.00 37.63 ? 1140 ASN   B CA    1 
ATOM   17320 C  C     . ASN   B  1  1142 ? 12.208  81.278  78.954  1.00 37.82 ? 1140 ASN   B C     1 
ATOM   17321 O  O     . ASN   B  1  1142 ? 10.990  81.358  79.134  1.00 34.54 ? 1140 ASN   B O     1 
ATOM   17322 C  CB    . ASN   B  1  1142 ? 12.240  83.687  78.172  1.00 40.97 ? 1140 ASN   B CB    1 
ATOM   17323 C  CG    . ASN   B  1  1142 ? 13.029  84.987  78.111  1.00 47.86 ? 1140 ASN   B CG    1 
ATOM   17324 O  OD1   . ASN   B  1  1142 ? 13.615  85.418  79.105  1.00 53.19 ? 1140 ASN   B OD1   1 
ATOM   17325 N  ND2   . ASN   B  1  1142 ? 13.059  85.609  76.937  1.00 50.78 ? 1140 ASN   B ND2   1 
ATOM   17326 N  N     . LEU   B  1  1143 ? 12.844  80.116  78.915  1.00 38.83 ? 1141 LEU   B N     1 
ATOM   17327 C  CA    . LEU   B  1  1143 ? 12.136  78.875  79.166  1.00 33.95 ? 1141 LEU   B CA    1 
ATOM   17328 C  C     . LEU   B  1  1143 ? 11.591  78.885  80.592  1.00 32.99 ? 1141 LEU   B C     1 
ATOM   17329 O  O     . LEU   B  1  1143 ? 12.285  79.319  81.517  1.00 37.71 ? 1141 LEU   B O     1 
ATOM   17330 C  CB    . LEU   B  1  1143 ? 13.113  77.711  79.003  1.00 29.90 ? 1141 LEU   B CB    1 
ATOM   17331 C  CG    . LEU   B  1  1143 ? 12.562  76.306  78.835  1.00 30.35 ? 1141 LEU   B CG    1 
ATOM   17332 C  CD1   . LEU   B  1  1143 ? 11.880  76.169  77.485  1.00 27.55 ? 1141 LEU   B CD1   1 
ATOM   17333 C  CD2   . LEU   B  1  1143 ? 13.692  75.305  78.980  1.00 26.20 ? 1141 LEU   B CD2   1 
ATOM   17334 N  N     . PRO   B  1  1144 ? 10.358  78.428  80.806  1.00 31.92 ? 1142 PRO   B N     1 
ATOM   17335 C  CA    . PRO   B  1  1144 ? 9.831   78.344  82.176  1.00 34.21 ? 1142 PRO   B CA    1 
ATOM   17336 C  C     . PRO   B  1  1144 ? 10.697  77.437  83.038  1.00 32.82 ? 1142 PRO   B C     1 
ATOM   17337 O  O     . PRO   B  1  1144 ? 11.227  76.427  82.568  1.00 29.39 ? 1142 PRO   B O     1 
ATOM   17338 C  CB    . PRO   B  1  1144 ? 8.434   77.739  81.980  1.00 38.95 ? 1142 PRO   B CB    1 
ATOM   17339 C  CG    . PRO   B  1  1144 ? 8.084   78.004  80.549  1.00 37.13 ? 1142 PRO   B CG    1 
ATOM   17340 C  CD    . PRO   B  1  1144 ? 9.384   77.980  79.797  1.00 31.34 ? 1142 PRO   B CD    1 
ATOM   17341 N  N     . GLN   B  1  1145 ? 10.823  77.803  84.317  1.00 33.76 ? 1143 GLN   B N     1 
ATOM   17342 C  CA    . GLN   B  1  1145 ? 11.640  77.028  85.247  1.00 31.26 ? 1143 GLN   B CA    1 
ATOM   17343 C  C     . GLN   B  1  1145 ? 11.190  75.578  85.326  1.00 29.58 ? 1143 GLN   B C     1 
ATOM   17344 O  O     . GLN   B  1  1145 ? 12.019  74.686  85.520  1.00 27.07 ? 1143 GLN   B O     1 
ATOM   17345 C  CB    . GLN   B  1  1145 ? 11.620  77.668  86.638  1.00 32.71 ? 1143 GLN   B CB    1 
ATOM   17346 N  N     . THR   B  1  1146 ? 9.888   75.319  85.185  1.00 29.71 ? 1144 THR   B N     1 
ATOM   17347 C  CA    . THR   B  1  1146 ? 9.422   73.938  85.211  1.00 31.03 ? 1144 THR   B CA    1 
ATOM   17348 C  C     . THR   B  1  1146 ? 10.062  73.132  84.094  1.00 27.33 ? 1144 THR   B C     1 
ATOM   17349 O  O     . THR   B  1  1146 ? 10.459  71.976  84.293  1.00 31.76 ? 1144 THR   B O     1 
ATOM   17350 C  CB    . THR   B  1  1146 ? 7.904   73.896  85.069  1.00 32.65 ? 1144 THR   B CB    1 
ATOM   17351 O  OG1   . THR   B  1  1146 ? 7.507   74.790  84.023  1.00 36.63 ? 1144 THR   B OG1   1 
ATOM   17352 C  CG2   . THR   B  1  1146 ? 7.240   74.311  86.372  1.00 37.40 ? 1144 THR   B CG2   1 
ATOM   17353 N  N     . VAL   B  1  1147 ? 10.174  73.728  82.912  1.00 26.65 ? 1145 VAL   B N     1 
ATOM   17354 C  CA    . VAL   B  1  1147 ? 10.828  73.029  81.815  1.00 25.29 ? 1145 VAL   B CA    1 
ATOM   17355 C  C     . VAL   B  1  1147 ? 12.334  73.053  81.998  1.00 26.31 ? 1145 VAL   B C     1 
ATOM   17356 O  O     . VAL   B  1  1147 ? 13.017  72.052  81.757  1.00 24.50 ? 1145 VAL   B O     1 
ATOM   17357 C  CB    . VAL   B  1  1147 ? 10.407  73.625  80.462  1.00 23.13 ? 1145 VAL   B CB    1 
ATOM   17358 C  CG1   . VAL   B  1  1147 ? 10.982  72.780  79.320  1.00 24.50 ? 1145 VAL   B CG1   1 
ATOM   17359 C  CG2   . VAL   B  1  1147 ? 8.888   73.727  80.364  1.00 24.09 ? 1145 VAL   B CG2   1 
ATOM   17360 N  N     . GLY   B  1  1148 ? 12.867  74.192  82.442  1.00 25.76 ? 1146 GLY   B N     1 
ATOM   17361 C  CA    . GLY   B  1  1148 ? 14.305  74.322  82.587  1.00 26.73 ? 1146 GLY   B CA    1 
ATOM   17362 C  C     . GLY   B  1  1148 ? 14.902  73.325  83.555  1.00 26.09 ? 1146 GLY   B C     1 
ATOM   17363 O  O     . GLY   B  1  1148 ? 16.028  72.862  83.353  1.00 27.28 ? 1146 GLY   B O     1 
ATOM   17364 N  N     . LEU   B  1  1149 ? 14.164  72.976  84.614  1.00 25.17 ? 1147 LEU   B N     1 
ATOM   17365 C  CA    . LEU   B  1  1149 ? 14.638  71.980  85.566  1.00 26.57 ? 1147 LEU   B CA    1 
ATOM   17366 C  C     . LEU   B  1  1149 ? 14.886  70.630  84.910  1.00 26.45 ? 1147 LEU   B C     1 
ATOM   17367 O  O     . LEU   B  1  1149 ? 15.658  69.826  85.446  1.00 28.15 ? 1147 LEU   B O     1 
ATOM   17368 C  CB    . LEU   B  1  1149 ? 13.624  71.819  86.707  1.00 30.92 ? 1147 LEU   B CB    1 
ATOM   17369 N  N     . ARG   B  1  1150 ? 14.252  70.364  83.767  1.00 22.49 ? 1148 ARG   B N     1 
ATOM   17370 C  CA    . ARG   B  1  1150 ? 14.443  69.117  83.036  1.00 23.62 ? 1148 ARG   B CA    1 
ATOM   17371 C  C     . ARG   B  1  1150 ? 15.514  69.219  81.964  1.00 20.91 ? 1148 ARG   B C     1 
ATOM   17372 O  O     . ARG   B  1  1150 ? 15.813  68.213  81.318  1.00 19.06 ? 1148 ARG   B O     1 
ATOM   17373 C  CB    . ARG   B  1  1150 ? 13.146  68.715  82.330  1.00 21.96 ? 1148 ARG   B CB    1 
ATOM   17374 C  CG    . ARG   B  1  1150 ? 12.041  68.237  83.244  1.00 24.29 ? 1148 ARG   B CG    1 
ATOM   17375 C  CD    . ARG   B  1  1150 ? 11.769  66.751  83.073  1.00 27.47 ? 1148 ARG   B CD    1 
ATOM   17376 N  NE    . ARG   B  1  1150 ? 10.493  66.395  83.679  1.00 23.79 ? 1148 ARG   B NE    1 
ATOM   17377 C  CZ    . ARG   B  1  1150 ? 9.435   65.951  83.014  1.00 23.52 ? 1148 ARG   B CZ    1 
ATOM   17378 N  NH1   . ARG   B  1  1150 ? 9.489   65.686  81.712  1.00 19.58 ? 1148 ARG   B NH1   1 
ATOM   17379 N  NH2   . ARG   B  1  1150 ? 8.300   65.746  83.676  1.00 20.79 ? 1148 ARG   B NH2   1 
ATOM   17380 N  N     . VAL   B  1  1151 ? 16.064  70.403  81.731  1.00 24.42 ? 1149 VAL   B N     1 
ATOM   17381 C  CA    . VAL   B  1  1151 ? 16.942  70.645  80.593  1.00 20.23 ? 1149 VAL   B CA    1 
ATOM   17382 C  C     . VAL   B  1  1151 ? 18.348  70.907  81.100  1.00 24.29 ? 1149 VAL   B C     1 
ATOM   17383 O  O     . VAL   B  1  1151 ? 18.554  71.747  81.978  1.00 24.97 ? 1149 VAL   B O     1 
ATOM   17384 C  CB    . VAL   B  1  1151 ? 16.451  71.823  79.740  1.00 23.70 ? 1149 VAL   B CB    1 
ATOM   17385 C  CG1   . VAL   B  1  1151 ? 17.499  72.187  78.679  1.00 26.07 ? 1149 VAL   B CG1   1 
ATOM   17386 C  CG2   . VAL   B  1  1151 ? 15.129  71.479  79.092  1.00 23.70 ? 1149 VAL   B CG2   1 
ATOM   17387 N  N     . SER   B  1  1152 ? 19.314  70.197  80.546  1.00 21.99 ? 1150 SER   B N     1 
ATOM   17388 C  CA    . SER   B  1  1152 ? 20.703  70.567  80.723  1.00 23.61 ? 1150 SER   B CA    1 
ATOM   17389 C  C     . SER   B  1  1152 ? 21.351  70.612  79.351  1.00 20.85 ? 1150 SER   B C     1 
ATOM   17390 O  O     . SER   B  1  1152 ? 20.819  70.077  78.375  1.00 21.46 ? 1150 SER   B O     1 
ATOM   17391 C  CB    . SER   B  1  1152 ? 21.441  69.598  81.649  1.00 23.06 ? 1150 SER   B CB    1 
ATOM   17392 O  OG    . SER   B  1  1152 ? 21.446  68.295  81.099  1.00 28.47 ? 1150 SER   B OG    1 
ATOM   17393 N  N     . TRP   B  1  1153 ? 22.487  71.287  79.277  1.00 21.83 ? 1151 TRP   B N     1 
ATOM   17394 C  CA    . TRP   B  1  1153 ? 23.276  71.354  78.062  1.00 18.47 ? 1151 TRP   B CA    1 
ATOM   17395 C  C     . TRP   B  1  1153 ? 24.566  70.600  78.320  1.00 21.19 ? 1151 TRP   B C     1 
ATOM   17396 O  O     . TRP   B  1  1153 ? 25.172  70.755  79.384  1.00 24.73 ? 1151 TRP   B O     1 
ATOM   17397 C  CB    . TRP   B  1  1153 ? 23.582  72.809  77.712  1.00 22.67 ? 1151 TRP   B CB    1 
ATOM   17398 C  CG    . TRP   B  1  1153 ? 22.357  73.523  77.234  1.00 23.68 ? 1151 TRP   B CG    1 
ATOM   17399 C  CD1   . TRP   B  1  1153 ? 21.427  74.171  78.004  1.00 24.88 ? 1151 TRP   B CD1   1 
ATOM   17400 C  CD2   . TRP   B  1  1153 ? 21.916  73.642  75.882  1.00 25.13 ? 1151 TRP   B CD2   1 
ATOM   17401 N  NE1   . TRP   B  1  1153 ? 20.439  74.695  77.202  1.00 24.31 ? 1151 TRP   B NE1   1 
ATOM   17402 C  CE2   . TRP   B  1  1153 ? 20.714  74.380  75.897  1.00 23.80 ? 1151 TRP   B CE2   1 
ATOM   17403 C  CE3   . TRP   B  1  1153 ? 22.422  73.199  74.654  1.00 20.57 ? 1151 TRP   B CE3   1 
ATOM   17404 C  CZ2   . TRP   B  1  1153 ? 20.017  74.685  74.733  1.00 24.49 ? 1151 TRP   B CZ2   1 
ATOM   17405 C  CZ3   . TRP   B  1  1153 ? 21.728  73.501  73.507  1.00 20.78 ? 1151 TRP   B CZ3   1 
ATOM   17406 C  CH2   . TRP   B  1  1153 ? 20.539  74.240  73.552  1.00 23.69 ? 1151 TRP   B CH2   1 
ATOM   17407 N  N     . SER   B  1  1154 ? 24.963  69.760  77.369  1.00 19.79 ? 1152 SER   B N     1 
ATOM   17408 C  CA    . SER   B  1  1154 ? 26.148  68.927  77.545  1.00 21.30 ? 1152 SER   B CA    1 
ATOM   17409 C  C     . SER   B  1  1154 ? 27.185  69.277  76.493  1.00 19.76 ? 1152 SER   B C     1 
ATOM   17410 O  O     . SER   B  1  1154 ? 26.902  69.225  75.290  1.00 20.82 ? 1152 SER   B O     1 
ATOM   17411 C  CB    . SER   B  1  1154 ? 25.810  67.442  77.458  1.00 23.81 ? 1152 SER   B CB    1 
ATOM   17412 O  OG    . SER   B  1  1154 ? 27.010  66.691  77.578  1.00 21.54 ? 1152 SER   B OG    1 
ATOM   17413 N  N     . LYS   B  1  1155 ? 28.381  69.645  76.958  1.00 19.73 ? 1153 LYS   B N     1 
ATOM   17414 C  CA    . LYS   B  1  1155 ? 29.568  69.749  76.127  1.00 23.89 ? 1153 LYS   B CA    1 
ATOM   17415 C  C     . LYS   B  1  1155 ? 30.455  68.524  76.270  1.00 25.22 ? 1153 LYS   B C     1 
ATOM   17416 O  O     . LYS   B  1  1155 ? 31.596  68.531  75.797  1.00 25.63 ? 1153 LYS   B O     1 
ATOM   17417 C  CB    . LYS   B  1  1155 ? 30.355  71.008  76.487  1.00 26.42 ? 1153 LYS   B CB    1 
ATOM   17418 N  N     . ASP   B  1  1156 ? 29.966  67.484  76.939  1.00 19.41 ? 1154 ASP   B N     1 
ATOM   17419 C  CA    . ASP   B  1  1156 ? 30.772  66.287  77.187  1.00 18.32 ? 1154 ASP   B CA    1 
ATOM   17420 C  C     . ASP   B  1  1156 ? 29.780  65.148  77.434  1.00 19.52 ? 1154 ASP   B C     1 
ATOM   17421 O  O     . ASP   B  1  1156 ? 29.403  64.889  78.576  1.00 19.56 ? 1154 ASP   B O     1 
ATOM   17422 C  CB    . ASP   B  1  1156 ? 31.671  66.486  78.388  1.00 17.94 ? 1154 ASP   B CB    1 
ATOM   17423 C  CG    . ASP   B  1  1156 ? 32.685  65.377  78.550  1.00 21.75 ? 1154 ASP   B CG    1 
ATOM   17424 O  OD1   . ASP   B  1  1156 ? 32.421  64.238  78.109  1.00 19.99 ? 1154 ASP   B OD1   1 
ATOM   17425 O  OD2   . ASP   B  1  1156 ? 33.750  65.669  79.122  1.00 22.24 ? 1154 ASP   B OD2   1 
ATOM   17426 N  N     . TRP   B  1  1157 ? 29.383  64.470  76.356  1.00 16.53 ? 1155 TRP   B N     1 
ATOM   17427 C  CA    . TRP   B  1  1157 ? 28.307  63.487  76.483  1.00 16.25 ? 1155 TRP   B CA    1 
ATOM   17428 C  C     . TRP   B  1  1157 ? 28.714  62.348  77.394  1.00 19.66 ? 1155 TRP   B C     1 
ATOM   17429 O  O     . TRP   B  1  1157 ? 27.910  61.864  78.199  1.00 19.39 ? 1155 TRP   B O     1 
ATOM   17430 C  CB    . TRP   B  1  1157 ? 27.919  62.915  75.127  1.00 18.94 ? 1155 TRP   B CB    1 
ATOM   17431 C  CG    . TRP   B  1  1157 ? 27.483  63.907  74.124  1.00 16.91 ? 1155 TRP   B CG    1 
ATOM   17432 C  CD1   . TRP   B  1  1157 ? 27.243  65.235  74.311  1.00 17.36 ? 1155 TRP   B CD1   1 
ATOM   17433 C  CD2   . TRP   B  1  1157 ? 27.231  63.637  72.751  1.00 15.66 ? 1155 TRP   B CD2   1 
ATOM   17434 N  NE1   . TRP   B  1  1157 ? 26.863  65.813  73.122  1.00 18.72 ? 1155 TRP   B NE1   1 
ATOM   17435 C  CE2   . TRP   B  1  1157 ? 26.857  64.849  72.146  1.00 17.95 ? 1155 TRP   B CE2   1 
ATOM   17436 C  CE3   . TRP   B  1  1157 ? 27.308  62.479  71.963  1.00 17.91 ? 1155 TRP   B CE3   1 
ATOM   17437 C  CZ2   . TRP   B  1  1157 ? 26.541  64.939  70.794  1.00 19.16 ? 1155 TRP   B CZ2   1 
ATOM   17438 C  CZ3   . TRP   B  1  1157 ? 26.997  62.567  70.627  1.00 20.18 ? 1155 TRP   B CZ3   1 
ATOM   17439 C  CH2   . TRP   B  1  1157 ? 26.624  63.792  70.049  1.00 19.82 ? 1155 TRP   B CH2   1 
ATOM   17440 N  N     . ALA   B  1  1158 ? 29.964  61.903  77.289  1.00 18.12 ? 1156 ALA   B N     1 
ATOM   17441 C  CA    . ALA   B  1  1158 ? 30.378  60.753  78.079  1.00 19.15 ? 1156 ALA   B CA    1 
ATOM   17442 C  C     . ALA   B  1  1158 ? 30.443  61.078  79.561  1.00 21.97 ? 1156 ALA   B C     1 
ATOM   17443 O  O     . ALA   B  1  1158 ? 30.171  60.207  80.391  1.00 23.83 ? 1156 ALA   B O     1 
ATOM   17444 C  CB    . ALA   B  1  1158 ? 31.722  60.226  77.588  1.00 18.37 ? 1156 ALA   B CB    1 
ATOM   17445 N  N     . ALA   B  1  1159 ? 30.808  62.309  79.913  1.00 18.54 ? 1157 ALA   B N     1 
ATOM   17446 C  CA    . ALA   B  1  1159 ? 30.885  62.682  81.318  1.00 20.31 ? 1157 ALA   B CA    1 
ATOM   17447 C  C     . ALA   B  1  1159 ? 29.508  62.948  81.909  1.00 21.69 ? 1157 ALA   B C     1 
ATOM   17448 O  O     . ALA   B  1  1159 ? 29.316  62.772  83.113  1.00 23.47 ? 1157 ALA   B O     1 
ATOM   17449 C  CB    . ALA   B  1  1159 ? 31.789  63.900  81.488  1.00 23.00 ? 1157 ALA   B CB    1 
ATOM   17450 N  N     . ASP   B  1  1160 ? 28.541  63.328  81.079  1.00 22.26 ? 1158 ASP   B N     1 
ATOM   17451 C  CA    . ASP   B  1  1160 ? 27.248  63.802  81.551  1.00 23.02 ? 1158 ASP   B CA    1 
ATOM   17452 C  C     . ASP   B  1  1160 ? 26.176  62.722  81.573  1.00 22.98 ? 1158 ASP   B C     1 
ATOM   17453 O  O     . ASP   B  1  1160 ? 25.052  62.995  82.009  1.00 25.14 ? 1158 ASP   B O     1 
ATOM   17454 C  CB    . ASP   B  1  1160 ? 26.803  65.001  80.706  1.00 22.51 ? 1158 ASP   B CB    1 
ATOM   17455 C  CG    . ASP   B  1  1160 ? 27.704  66.209  80.902  1.00 23.90 ? 1158 ASP   B CG    1 
ATOM   17456 O  OD1   . ASP   B  1  1160 ? 28.510  66.204  81.863  1.00 27.14 ? 1158 ASP   B OD1   1 
ATOM   17457 O  OD2   . ASP   B  1  1160 ? 27.631  67.168  80.103  1.00 25.22 ? 1158 ASP   B OD2   1 
ATOM   17458 N  N     . GLY   B  1  1161 ? 26.486  61.514  81.115  1.00 20.01 ? 1159 GLY   B N     1 
ATOM   17459 C  CA    . GLY   B  1  1161 ? 25.575  60.400  81.216  1.00 23.00 ? 1159 GLY   B CA    1 
ATOM   17460 C  C     . GLY   B  1  1161 ? 25.613  59.774  82.597  1.00 24.47 ? 1159 GLY   B C     1 
ATOM   17461 O  O     . GLY   B  1  1161 ? 26.180  60.334  83.543  1.00 29.09 ? 1159 GLY   B O     1 
ATOM   17462 N  N     . PRO   B  1  1162 ? 25.031  58.578  82.738  1.00 27.42 ? 1160 PRO   B N     1 
ATOM   17463 C  CA    . PRO   B  1  1162 ? 24.427  57.759  81.685  1.00 23.15 ? 1160 PRO   B CA    1 
ATOM   17464 C  C     . PRO   B  1  1162 ? 23.093  58.316  81.229  1.00 23.64 ? 1160 PRO   B C     1 
ATOM   17465 O  O     . PRO   B  1  1162 ? 22.283  58.838  81.988  1.00 24.74 ? 1160 PRO   B O     1 
ATOM   17466 C  CB    . PRO   B  1  1162 ? 24.250  56.398  82.374  1.00 26.87 ? 1160 PRO   B CB    1 
ATOM   17467 C  CG    . PRO   B  1  1162 ? 23.977  56.758  83.801  1.00 29.83 ? 1160 PRO   B CG    1 
ATOM   17468 C  CD    . PRO   B  1  1162 ? 24.883  57.947  84.065  1.00 29.94 ? 1160 PRO   B CD    1 
ATOM   17469 N  N     . PHE   B  1  1163 ? 22.865  58.213  79.936  1.00 17.49 ? 1161 PHE   B N     1 
ATOM   17470 C  CA    . PHE   B  1  1163 ? 21.579  58.539  79.355  1.00 19.11 ? 1161 PHE   B CA    1 
ATOM   17471 C  C     . PHE   B  1  1163 ? 20.768  57.265  79.193  1.00 16.98 ? 1161 PHE   B C     1 
ATOM   17472 O  O     . PHE   B  1  1163 ? 21.250  56.154  79.429  1.00 18.76 ? 1161 PHE   B O     1 
ATOM   17473 C  CB    . PHE   B  1  1163 ? 21.789  59.273  78.029  1.00 16.97 ? 1161 PHE   B CB    1 
ATOM   17474 C  CG    . PHE   B  1  1163 ? 22.645  60.501  78.167  1.00 18.04 ? 1161 PHE   B CG    1 
ATOM   17475 C  CD1   . PHE   B  1  1163 ? 22.222  61.571  78.934  1.00 22.59 ? 1161 PHE   B CD1   1 
ATOM   17476 C  CD2   . PHE   B  1  1163 ? 23.885  60.574  77.553  1.00 20.89 ? 1161 PHE   B CD2   1 
ATOM   17477 C  CE1   . PHE   B  1  1163 ? 23.005  62.696  79.086  1.00 23.73 ? 1161 PHE   B CE1   1 
ATOM   17478 C  CE2   . PHE   B  1  1163 ? 24.674  61.714  77.699  1.00 20.61 ? 1161 PHE   B CE2   1 
ATOM   17479 C  CZ    . PHE   B  1  1163 ? 24.233  62.772  78.459  1.00 21.80 ? 1161 PHE   B CZ    1 
ATOM   17480 N  N     . ALA   B  1  1164 ? 19.493  57.436  78.842  1.00 17.01 ? 1162 ALA   B N     1 
ATOM   17481 C  CA    . ALA   B  1  1164 ? 18.606  56.302  78.636  1.00 18.84 ? 1162 ALA   B CA    1 
ATOM   17482 C  C     . ALA   B  1  1164 ? 18.051  56.258  77.223  1.00 20.32 ? 1162 ALA   B C     1 
ATOM   17483 O  O     . ALA   B  1  1164 ? 17.129  55.485  76.948  1.00 22.03 ? 1162 ALA   B O     1 
ATOM   17484 C  CB    . ALA   B  1  1164 ? 17.467  56.326  79.659  1.00 20.77 ? 1162 ALA   B CB    1 
ATOM   17485 N  N     . GLY   B  1  1165 ? 18.581  57.083  76.331  1.00 16.16 ? 1163 GLY   B N     1 
ATOM   17486 C  CA    . GLY   B  1  1165 ? 18.175  57.100  74.945  1.00 17.63 ? 1163 GLY   B CA    1 
ATOM   17487 C  C     . GLY   B  1  1165 ? 18.734  58.351  74.310  1.00 17.93 ? 1163 GLY   B C     1 
ATOM   17488 O  O     . GLY   B  1  1165 ? 19.338  59.195  74.979  1.00 16.79 ? 1163 GLY   B O     1 
ATOM   17489 N  N     . ALA   B  1  1166 ? 18.529  58.458  73.002  1.00 17.44 ? 1164 ALA   B N     1 
ATOM   17490 C  CA    . ALA   B  1  1166 ? 19.033  59.628  72.297  1.00 15.56 ? 1164 ALA   B CA    1 
ATOM   17491 C  C     . ALA   B  1  1166 ? 18.147  59.927  71.107  1.00 16.47 ? 1164 ALA   B C     1 
ATOM   17492 O  O     . ALA   B  1  1166 ? 17.662  59.015  70.438  1.00 18.27 ? 1164 ALA   B O     1 
ATOM   17493 C  CB    . ALA   B  1  1166 ? 20.477  59.422  71.834  1.00 17.38 ? 1164 ALA   B CB    1 
ATOM   17494 N  N     . LEU   B  1  1167 ? 17.946  61.213  70.854  1.00 14.78 ? 1165 LEU   B N     1 
ATOM   17495 C  CA    . LEU   B  1  1167 ? 17.242  61.682  69.677  1.00 16.88 ? 1165 LEU   B CA    1 
ATOM   17496 C  C     . LEU   B  1  1167 ? 18.236  62.501  68.877  1.00 19.10 ? 1165 LEU   B C     1 
ATOM   17497 O  O     . LEU   B  1  1167 ? 18.905  63.372  69.433  1.00 17.99 ? 1165 LEU   B O     1 
ATOM   17498 C  CB    . LEU   B  1  1167 ? 16.065  62.566  70.075  1.00 16.28 ? 1165 LEU   B CB    1 
ATOM   17499 C  CG    . LEU   B  1  1167 ? 15.047  61.862  70.974  1.00 16.67 ? 1165 LEU   B CG    1 
ATOM   17500 C  CD1   . LEU   B  1  1167 ? 13.920  62.833  71.293  1.00 18.42 ? 1165 LEU   B CD1   1 
ATOM   17501 C  CD2   . LEU   B  1  1167 ? 14.501  60.597  70.282  1.00 18.66 ? 1165 LEU   B CD2   1 
ATOM   17502 N  N     . VAL   B  1  1168 ? 18.352  62.197  67.592  1.00 17.06 ? 1166 VAL   B N     1 
ATOM   17503 C  CA    . VAL   B  1  1168 ? 19.354  62.820  66.744  1.00 17.53 ? 1166 VAL   B CA    1 
ATOM   17504 C  C     . VAL   B  1  1168 ? 18.647  63.410  65.539  1.00 17.37 ? 1166 VAL   B C     1 
ATOM   17505 O  O     . VAL   B  1  1168 ? 17.746  62.788  64.962  1.00 18.14 ? 1166 VAL   B O     1 
ATOM   17506 C  CB    . VAL   B  1  1168 ? 20.413  61.792  66.303  1.00 19.21 ? 1166 VAL   B CB    1 
ATOM   17507 C  CG1   . VAL   B  1  1168 ? 21.479  62.463  65.449  1.00 18.41 ? 1166 VAL   B CG1   1 
ATOM   17508 C  CG2   . VAL   B  1  1168 ? 21.028  61.087  67.525  1.00 18.46 ? 1166 VAL   B CG2   1 
ATOM   17509 N  N     . GLU   B  1  1169 ? 19.038  64.621  65.177  1.00 18.40 ? 1167 GLU   B N     1 
ATOM   17510 C  CA    . GLU   B  1  1169 ? 18.567  65.274  63.969  1.00 17.53 ? 1167 GLU   B CA    1 
ATOM   17511 C  C     . GLU   B  1  1169 ? 19.772  65.551  63.085  1.00 19.11 ? 1167 GLU   B C     1 
ATOM   17512 O  O     . GLU   B  1  1169 ? 20.800  66.020  63.576  1.00 22.42 ? 1167 GLU   B O     1 
ATOM   17513 C  CB    . GLU   B  1  1169 ? 17.904  66.604  64.309  1.00 18.75 ? 1167 GLU   B CB    1 
ATOM   17514 C  CG    . GLU   B  1  1169 ? 17.411  67.363  63.093  1.00 20.26 ? 1167 GLU   B CG    1 
ATOM   17515 C  CD    . GLU   B  1  1169 ? 17.037  68.799  63.408  1.00 22.46 ? 1167 GLU   B CD    1 
ATOM   17516 O  OE1   . GLU   B  1  1169 ? 17.308  69.267  64.533  1.00 20.36 ? 1167 GLU   B OE1   1 
ATOM   17517 O  OE2   . GLU   B  1  1169 ? 16.457  69.463  62.530  1.00 23.90 ? 1167 GLU   B OE2   1 
ATOM   17518 N  N     . GLY   B  1  1170 ? 19.648  65.262  61.801  1.00 20.68 ? 1168 GLY   B N     1 
ATOM   17519 C  CA    . GLY   B  1  1170 ? 20.702  65.625  60.874  1.00 22.40 ? 1168 GLY   B CA    1 
ATOM   17520 C  C     . GLY   B  1  1170 ? 20.596  64.838  59.588  1.00 24.78 ? 1168 GLY   B C     1 
ATOM   17521 O  O     . GLY   B  1  1170 ? 19.729  63.983  59.423  1.00 21.82 ? 1168 GLY   B O     1 
ATOM   17522 N  N     . ASP   B  1  1171 ? 21.502  65.155  58.667  1.00 25.20 ? 1169 ASP   B N     1 
ATOM   17523 C  CA    . ASP   B  1  1171 ? 21.552  64.373  57.446  1.00 25.48 ? 1169 ASP   B CA    1 
ATOM   17524 C  C     . ASP   B  1  1171 ? 22.234  63.036  57.715  1.00 23.25 ? 1169 ASP   B C     1 
ATOM   17525 O  O     . ASP   B  1  1171 ? 22.695  62.751  58.824  1.00 23.99 ? 1169 ASP   B O     1 
ATOM   17526 C  CB    . ASP   B  1  1171 ? 22.170  65.163  56.290  1.00 27.05 ? 1169 ASP   B CB    1 
ATOM   17527 C  CG    . ASP   B  1  1171 ? 23.637  65.506  56.504  1.00 29.79 ? 1169 ASP   B CG    1 
ATOM   17528 O  OD1   . ASP   B  1  1171 ? 24.273  65.044  57.477  1.00 27.34 ? 1169 ASP   B OD1   1 
ATOM   17529 O  OD2   . ASP   B  1  1171 ? 24.172  66.266  55.664  1.00 35.57 ? 1169 ASP   B OD2   1 
ATOM   17530 N  N     . ALA   B  1  1172 ? 22.313  62.208  56.675  1.00 25.04 ? 1170 ALA   B N     1 
ATOM   17531 C  CA    . ALA   B  1  1172 ? 22.784  60.841  56.858  1.00 27.23 ? 1170 ALA   B CA    1 
ATOM   17532 C  C     . ALA   B  1  1172 ? 24.188  60.816  57.447  1.00 24.38 ? 1170 ALA   B C     1 
ATOM   17533 O  O     . ALA   B  1  1172 ? 24.471  60.055  58.379  1.00 23.61 ? 1170 ALA   B O     1 
ATOM   17534 C  CB    . ALA   B  1  1172 ? 22.730  60.083  55.531  1.00 27.28 ? 1170 ALA   B CB    1 
ATOM   17535 N  N     . GLU   B  1  1173 ? 25.089  61.650  56.929  1.00 24.79 ? 1171 GLU   B N     1 
ATOM   17536 C  CA    . GLU   B  1  1173 ? 26.446  61.595  57.455  1.00 25.02 ? 1171 GLU   B CA    1 
ATOM   17537 C  C     . GLU   B  1  1173 ? 26.530  62.138  58.877  1.00 22.36 ? 1171 GLU   B C     1 
ATOM   17538 O  O     . GLU   B  1  1173 ? 27.325  61.637  59.681  1.00 24.18 ? 1171 GLU   B O     1 
ATOM   17539 C  CB    . GLU   B  1  1173 ? 27.438  62.248  56.494  1.00 33.41 ? 1171 GLU   B CB    1 
ATOM   17540 C  CG    . GLU   B  1  1173 ? 27.634  61.429  55.213  1.00 38.16 ? 1171 GLU   B CG    1 
ATOM   17541 C  CD    . GLU   B  1  1173 ? 27.916  59.942  55.470  1.00 40.18 ? 1171 GLU   B CD    1 
ATOM   17542 O  OE1   . GLU   B  1  1173 ? 28.743  59.612  56.351  1.00 37.27 ? 1171 GLU   B OE1   1 
ATOM   17543 O  OE2   . GLU   B  1  1173 ? 27.304  59.091  54.785  1.00 44.13 ? 1171 GLU   B OE2   1 
ATOM   17544 N  N     . ARG   B  1  1174 ? 25.710  63.142  59.210  1.00 21.66 ? 1172 ARG   B N     1 
ATOM   17545 C  CA    . ARG   B  1  1174 ? 25.633  63.600  60.593  1.00 22.90 ? 1172 ARG   B CA    1 
ATOM   17546 C  C     . ARG   B  1  1174 ? 25.118  62.488  61.496  1.00 20.02 ? 1172 ARG   B C     1 
ATOM   17547 O  O     . ARG   B  1  1174 ? 25.679  62.239  62.568  1.00 20.55 ? 1172 ARG   B O     1 
ATOM   17548 C  CB    . ARG   B  1  1174 ? 24.727  64.830  60.678  1.00 25.19 ? 1172 ARG   B CB    1 
ATOM   17549 C  CG    . ARG   B  1  1174 ? 24.450  65.323  62.085  1.00 21.68 ? 1172 ARG   B CG    1 
ATOM   17550 C  CD    . ARG   B  1  1174 ? 25.730  65.759  62.770  1.00 23.23 ? 1172 ARG   B CD    1 
ATOM   17551 N  NE    . ARG   B  1  1174 ? 25.477  66.261  64.115  1.00 24.04 ? 1172 ARG   B NE    1 
ATOM   17552 C  CZ    . ARG   B  1  1174 ? 26.405  66.370  65.056  1.00 25.41 ? 1172 ARG   B CZ    1 
ATOM   17553 N  NH1   . ARG   B  1  1174 ? 27.665  66.027  64.829  1.00 25.02 ? 1172 ARG   B NH1   1 
ATOM   17554 N  NH2   . ARG   B  1  1174 ? 26.060  66.825  66.258  1.00 24.79 ? 1172 ARG   B NH2   1 
ATOM   17555 N  N     . ILE   B  1  1175 ? 24.069  61.797  61.056  1.00 19.35 ? 1173 ILE   B N     1 
ATOM   17556 C  CA    . ILE   B  1  1175 ? 23.507  60.698  61.838  1.00 19.78 ? 1173 ILE   B CA    1 
ATOM   17557 C  C     . ILE   B  1  1175 ? 24.555  59.623  62.087  1.00 21.31 ? 1173 ILE   B C     1 
ATOM   17558 O  O     . ILE   B  1  1175 ? 24.697  59.122  63.208  1.00 20.38 ? 1173 ILE   B O     1 
ATOM   17559 C  CB    . ILE   B  1  1175 ? 22.261  60.135  61.137  1.00 20.20 ? 1173 ILE   B CB    1 
ATOM   17560 C  CG1   . ILE   B  1  1175 ? 21.103  61.128  61.250  1.00 21.38 ? 1173 ILE   B CG1   1 
ATOM   17561 C  CG2   . ILE   B  1  1175 ? 21.890  58.780  61.719  1.00 20.68 ? 1173 ILE   B CG2   1 
ATOM   17562 C  CD1   . ILE   B  1  1175 ? 19.964  60.826  60.328  1.00 21.24 ? 1173 ILE   B CD1   1 
ATOM   17563 N  N     . ARG   B  1  1176 ? 25.305  59.246  61.043  1.00 21.31 ? 1174 ARG   B N     1 
ATOM   17564 C  CA    . ARG   B  1  1176 ? 26.329  58.217  61.214  1.00 21.06 ? 1174 ARG   B CA    1 
ATOM   17565 C  C     . ARG   B  1  1176 ? 27.386  58.651  62.222  1.00 19.98 ? 1174 ARG   B C     1 
ATOM   17566 O  O     . ARG   B  1  1176 ? 27.786  57.868  63.088  1.00 20.01 ? 1174 ARG   B O     1 
ATOM   17567 C  CB    . ARG   B  1  1176 ? 26.979  57.873  59.870  1.00 21.68 ? 1174 ARG   B CB    1 
ATOM   17568 C  CG    . ARG   B  1  1176 ? 27.925  56.678  59.939  1.00 25.82 ? 1174 ARG   B CG    1 
ATOM   17569 C  CD    . ARG   B  1  1176 ? 28.865  56.588  58.725  1.00 29.90 ? 1174 ARG   B CD    1 
ATOM   17570 N  NE    . ARG   B  1  1176 ? 28.171  56.788  57.458  1.00 32.27 ? 1174 ARG   B NE    1 
ATOM   17571 C  CZ    . ARG   B  1  1176 ? 27.654  55.818  56.715  1.00 33.46 ? 1174 ARG   B CZ    1 
ATOM   17572 N  NH1   . ARG   B  1  1176 ? 27.711  54.552  57.091  1.00 31.74 ? 1174 ARG   B NH1   1 
ATOM   17573 N  NH2   . ARG   B  1  1176 ? 27.083  56.125  55.552  1.00 35.37 ? 1174 ARG   B NH2   1 
ATOM   17574 N  N     . ALA   B  1  1177 ? 27.842  59.904  62.130  1.00 19.85 ? 1175 ALA   B N     1 
ATOM   17575 C  CA    . ALA   B  1  1177 ? 28.872  60.389  63.040  1.00 21.17 ? 1175 ALA   B CA    1 
ATOM   17576 C  C     . ALA   B  1  1177 ? 28.363  60.424  64.473  1.00 17.46 ? 1175 ALA   B C     1 
ATOM   17577 O  O     . ALA   B  1  1177 ? 29.086  60.063  65.411  1.00 19.83 ? 1175 ALA   B O     1 
ATOM   17578 C  CB    . ALA   B  1  1177 ? 29.332  61.782  62.615  1.00 21.54 ? 1175 ALA   B CB    1 
ATOM   17579 N  N     . VAL   B  1  1178 ? 27.113  60.842  64.656  1.00 20.17 ? 1176 VAL   B N     1 
ATOM   17580 C  CA    . VAL   B  1  1178 ? 26.557  60.900  66.000  1.00 17.23 ? 1176 VAL   B CA    1 
ATOM   17581 C  C     . VAL   B  1  1178 ? 26.357  59.495  66.535  1.00 18.01 ? 1176 VAL   B C     1 
ATOM   17582 O  O     . VAL   B  1  1178 ? 26.639  59.211  67.701  1.00 19.22 ? 1176 VAL   B O     1 
ATOM   17583 C  CB    . VAL   B  1  1178 ? 25.249  61.704  65.991  1.00 19.83 ? 1176 VAL   B CB    1 
ATOM   17584 C  CG1   . VAL   B  1  1178 ? 24.547  61.562  67.328  1.00 20.71 ? 1176 VAL   B CG1   1 
ATOM   17585 C  CG2   . VAL   B  1  1178 ? 25.537  63.166  65.701  1.00 20.79 ? 1176 VAL   B CG2   1 
ATOM   17586 N  N     . ASN   B  1  1179 ? 25.878  58.593  65.684  1.00 18.58 ? 1177 ASN   B N     1 
ATOM   17587 C  CA    . ASN   B  1  1179 ? 25.652  57.221  66.118  1.00 19.12 ? 1177 ASN   B CA    1 
ATOM   17588 C  C     . ASN   B  1  1179 ? 26.956  56.558  66.539  1.00 20.24 ? 1177 ASN   B C     1 
ATOM   17589 O  O     . ASN   B  1  1179 ? 27.006  55.836  67.542  1.00 20.45 ? 1177 ASN   B O     1 
ATOM   17590 C  CB    . ASN   B  1  1179 ? 24.976  56.457  64.982  1.00 19.37 ? 1177 ASN   B CB    1 
ATOM   17591 C  CG    . ASN   B  1  1179 ? 24.259  55.223  65.457  1.00 24.31 ? 1177 ASN   B CG    1 
ATOM   17592 O  OD1   . ASN   B  1  1179 ? 23.833  55.137  66.609  1.00 24.42 ? 1177 ASN   B OD1   1 
ATOM   17593 N  ND2   . ASN   B  1  1179 ? 24.109  54.257  64.562  1.00 23.43 ? 1177 ASN   B ND2   1 
ATOM   17594 N  N     . LYS   B  1  1180 ? 28.034  56.803  65.791  1.00 19.61 ? 1178 LYS   B N     1 
ATOM   17595 C  CA    . LYS   B  1  1180 ? 29.341  56.296  66.190  1.00 20.01 ? 1178 LYS   B CA    1 
ATOM   17596 C  C     . LYS   B  1  1180 ? 29.758  56.849  67.542  1.00 18.14 ? 1178 LYS   B C     1 
ATOM   17597 O  O     . LYS   B  1  1180 ? 30.267  56.112  68.393  1.00 21.24 ? 1178 LYS   B O     1 
ATOM   17598 C  CB    . LYS   B  1  1180 ? 30.390  56.661  65.142  1.00 22.85 ? 1178 LYS   B CB    1 
ATOM   17599 C  CG    . LYS   B  1  1180 ? 30.420  55.754  63.941  1.00 27.19 ? 1178 LYS   B CG    1 
ATOM   17600 C  CD    . LYS   B  1  1180 ? 31.597  56.123  63.036  1.00 29.81 ? 1178 LYS   B CD    1 
ATOM   17601 C  CE    . LYS   B  1  1180 ? 31.939  54.976  62.112  1.00 40.42 ? 1178 LYS   B CE    1 
ATOM   17602 N  NZ    . LYS   B  1  1180 ? 32.230  53.729  62.886  1.00 40.16 ? 1178 LYS   B NZ    1 
ATOM   17603 N  N     . ALA   B  1  1181 ? 29.569  58.155  67.752  1.00 18.82 ? 1179 ALA   B N     1 
ATOM   17604 C  CA    . ALA   B  1  1181 ? 29.953  58.747  69.027  1.00 18.05 ? 1179 ALA   B CA    1 
ATOM   17605 C  C     . ALA   B  1  1181 ? 29.126  58.161  70.161  1.00 18.15 ? 1179 ALA   B C     1 
ATOM   17606 O  O     . ALA   B  1  1181 ? 29.653  57.878  71.245  1.00 19.98 ? 1179 ALA   B O     1 
ATOM   17607 C  CB    . ALA   B  1  1181 ? 29.773  60.262  68.974  1.00 19.24 ? 1179 ALA   B CB    1 
ATOM   17608 N  N     . ILE   B  1  1182 ? 27.830  57.963  69.922  1.00 18.45 ? 1180 ILE   B N     1 
ATOM   17609 C  CA    . ILE   B  1  1182 ? 26.975  57.399  70.955  1.00 18.88 ? 1180 ILE   B CA    1 
ATOM   17610 C  C     . ILE   B  1  1182 ? 27.387  55.970  71.268  1.00 20.51 ? 1180 ILE   B C     1 
ATOM   17611 O  O     . ILE   B  1  1182 ? 27.402  55.555  72.429  1.00 19.27 ? 1180 ILE   B O     1 
ATOM   17612 C  CB    . ILE   B  1  1182 ? 25.498  57.499  70.543  1.00 18.98 ? 1180 ILE   B CB    1 
ATOM   17613 C  CG1   . ILE   B  1  1182 ? 25.068  58.959  70.578  1.00 16.50 ? 1180 ILE   B CG1   1 
ATOM   17614 C  CG2   . ILE   B  1  1182 ? 24.631  56.641  71.464  1.00 21.98 ? 1180 ILE   B CG2   1 
ATOM   17615 C  CD1   . ILE   B  1  1182 ? 23.678  59.191  70.013  1.00 19.54 ? 1180 ILE   B CD1   1 
ATOM   17616 N  N     . ALA   B  1  1183 ? 27.742  55.195  70.239  1.00 21.14 ? 1181 ALA   B N     1 
ATOM   17617 C  CA    . ALA   B  1  1183 ? 28.165  53.822  70.488  1.00 21.22 ? 1181 ALA   B CA    1 
ATOM   17618 C  C     . ALA   B  1  1183 ? 29.413  53.755  71.346  1.00 23.76 ? 1181 ALA   B C     1 
ATOM   17619 O  O     . ALA   B  1  1183 ? 29.622  52.752  72.039  1.00 25.80 ? 1181 ALA   B O     1 
ATOM   17620 C  CB    . ALA   B  1  1183 ? 28.387  53.066  69.176  1.00 22.00 ? 1181 ALA   B CB    1 
ATOM   17621 N  N     . ALA   B  1  1184 ? 30.227  54.808  71.343  1.00 21.87 ? 1182 ALA   B N     1 
ATOM   17622 C  CA    . ALA   B  1  1184 ? 31.445  54.859  72.137  1.00 21.98 ? 1182 ALA   B CA    1 
ATOM   17623 C  C     . ALA   B  1  1184 ? 31.224  55.385  73.549  1.00 21.47 ? 1182 ALA   B C     1 
ATOM   17624 O  O     . ALA   B  1  1184 ? 32.176  55.438  74.326  1.00 23.16 ? 1182 ALA   B O     1 
ATOM   17625 C  CB    . ALA   B  1  1184 ? 32.517  55.700  71.426  1.00 21.97 ? 1182 ALA   B CB    1 
ATOM   17626 N  N     . LEU   B  1  1185 ? 30.010  55.789  73.902  1.00 19.00 ? 1183 LEU   B N     1 
ATOM   17627 C  CA    . LEU   B  1  1185 ? 29.788  56.283  75.254  1.00 19.83 ? 1183 LEU   B CA    1 
ATOM   17628 C  C     . LEU   B  1  1185 ? 29.885  55.123  76.239  1.00 22.69 ? 1183 LEU   B C     1 
ATOM   17629 O  O     . LEU   B  1  1185 ? 29.445  54.008  75.936  1.00 22.00 ? 1183 LEU   B O     1 
ATOM   17630 C  CB    . LEU   B  1  1185 ? 28.409  56.926  75.379  1.00 18.93 ? 1183 LEU   B CB    1 
ATOM   17631 C  CG    . LEU   B  1  1185 ? 28.199  58.140  74.484  1.00 18.64 ? 1183 LEU   B CG    1 
ATOM   17632 C  CD1   . LEU   B  1  1185 ? 26.751  58.564  74.570  1.00 18.88 ? 1183 LEU   B CD1   1 
ATOM   17633 C  CD2   . LEU   B  1  1185 ? 29.148  59.268  74.869  1.00 18.22 ? 1183 LEU   B CD2   1 
ATOM   17634 N  N     . PRO   B  1  1186 ? 30.471  55.342  77.410  1.00 22.44 ? 1184 PRO   B N     1 
ATOM   17635 C  CA    . PRO   B  1  1186 ? 30.494  54.287  78.422  1.00 22.30 ? 1184 PRO   B CA    1 
ATOM   17636 C  C     . PRO   B  1  1186 ? 29.099  54.056  78.971  1.00 21.31 ? 1184 PRO   B C     1 
ATOM   17637 O  O     . PRO   B  1  1186 ? 28.198  54.886  78.834  1.00 24.43 ? 1184 PRO   B O     1 
ATOM   17638 C  CB    . PRO   B  1  1186 ? 31.409  54.861  79.507  1.00 25.01 ? 1184 PRO   B CB    1 
ATOM   17639 C  CG    . PRO   B  1  1186 ? 31.240  56.344  79.381  1.00 29.16 ? 1184 PRO   B CG    1 
ATOM   17640 C  CD    . PRO   B  1  1186 ? 31.015  56.616  77.914  1.00 24.34 ? 1184 PRO   B CD    1 
ATOM   17641 N  N     . GLY   B  1  1187 ? 28.938  52.906  79.614  1.00 21.31 ? 1185 GLY   B N     1 
ATOM   17642 C  CA    . GLY   B  1  1187 ? 27.707  52.598  80.302  1.00 21.39 ? 1185 GLY   B CA    1 
ATOM   17643 C  C     . GLY   B  1  1187 ? 26.694  51.929  79.401  1.00 21.02 ? 1185 GLY   B C     1 
ATOM   17644 O  O     . GLY   B  1  1187 ? 27.032  51.087  78.565  1.00 24.78 ? 1185 GLY   B O     1 
ATOM   17645 N  N     . PRO   B  1  1188 ? 25.425  52.272  79.575  1.00 20.25 ? 1186 PRO   B N     1 
ATOM   17646 C  CA    . PRO   B  1  1188 ? 24.369  51.548  78.860  1.00 19.71 ? 1186 PRO   B CA    1 
ATOM   17647 C  C     . PRO   B  1  1188 ? 24.432  51.779  77.363  1.00 18.75 ? 1186 PRO   B C     1 
ATOM   17648 O  O     . PRO   B  1  1188 ? 24.884  52.818  76.882  1.00 20.94 ? 1186 PRO   B O     1 
ATOM   17649 C  CB    . PRO   B  1  1188 ? 23.077  52.128  79.443  1.00 21.05 ? 1186 PRO   B CB    1 
ATOM   17650 C  CG    . PRO   B  1  1188 ? 23.464  53.471  79.954  1.00 25.56 ? 1186 PRO   B CG    1 
ATOM   17651 C  CD    . PRO   B  1  1188 ? 24.882  53.322  80.452  1.00 20.01 ? 1186 PRO   B CD    1 
ATOM   17652 N  N     . LEU   B  1  1189 ? 23.958  50.784  76.626  1.00 19.36 ? 1187 LEU   B N     1 
ATOM   17653 C  CA    . LEU   B  1  1189 ? 23.776  50.929  75.191  1.00 18.69 ? 1187 LEU   B CA    1 
ATOM   17654 C  C     . LEU   B  1  1189 ? 22.525  51.758  74.961  1.00 19.94 ? 1187 LEU   B C     1 
ATOM   17655 O  O     . LEU   B  1  1189 ? 21.441  51.384  75.421  1.00 22.68 ? 1187 LEU   B O     1 
ATOM   17656 C  CB    . LEU   B  1  1189 ? 23.601  49.557  74.549  1.00 16.43 ? 1187 LEU   B CB    1 
ATOM   17657 C  CG    . LEU   B  1  1189 ? 24.860  48.734  74.293  1.00 21.92 ? 1187 LEU   B CG    1 
ATOM   17658 C  CD1   . LEU   B  1  1189 ? 25.363  48.131  75.596  1.00 26.28 ? 1187 LEU   B CD1   1 
ATOM   17659 C  CD2   . LEU   B  1  1189 ? 24.564  47.652  73.267  1.00 22.66 ? 1187 LEU   B CD2   1 
ATOM   17660 N  N     . LEU   B  1  1190 ? 22.662  52.878  74.259  1.00 18.30 ? 1188 LEU   B N     1 
ATOM   17661 C  CA    . LEU   B  1  1190 ? 21.550  53.801  74.099  1.00 19.52 ? 1188 LEU   B CA    1 
ATOM   17662 C  C     . LEU   B  1  1190 ? 20.696  53.421  72.900  1.00 19.03 ? 1188 LEU   B C     1 
ATOM   17663 O  O     . LEU   B  1  1190 ? 21.217  53.149  71.810  1.00 19.32 ? 1188 LEU   B O     1 
ATOM   17664 C  CB    . LEU   B  1  1190 ? 22.041  55.237  73.925  1.00 17.72 ? 1188 LEU   B CB    1 
ATOM   17665 C  CG    . LEU   B  1  1190 ? 22.861  55.848  75.050  1.00 17.26 ? 1188 LEU   B CG    1 
ATOM   17666 C  CD1   . LEU   B  1  1190 ? 22.943  57.342  74.796  1.00 19.31 ? 1188 LEU   B CD1   1 
ATOM   17667 C  CD2   . LEU   B  1  1190 ? 22.219  55.537  76.399  1.00 19.78 ? 1188 LEU   B CD2   1 
ATOM   17668 N  N     . LEU   B  1  1191 ? 19.383  53.430  73.103  1.00 17.98 ? 1189 LEU   B N     1 
ATOM   17669 C  CA    . LEU   B  1  1191 ? 18.430  53.296  72.009  1.00 17.13 ? 1189 LEU   B CA    1 
ATOM   17670 C  C     . LEU   B  1  1191 ? 18.365  54.640  71.292  1.00 19.72 ? 1189 LEU   B C     1 
ATOM   17671 O  O     . LEU   B  1  1191 ? 17.838  55.618  71.836  1.00 19.90 ? 1189 LEU   B O     1 
ATOM   17672 C  CB    . LEU   B  1  1191 ? 17.066  52.888  72.558  1.00 20.10 ? 1189 LEU   B CB    1 
ATOM   17673 C  CG    . LEU   B  1  1191 ? 16.091  52.267  71.559  1.00 17.97 ? 1189 LEU   B CG    1 
ATOM   17674 C  CD1   . LEU   B  1  1191 ? 14.933  51.652  72.318  1.00 18.35 ? 1189 LEU   B CD1   1 
ATOM   17675 C  CD2   . LEU   B  1  1191 ? 15.580  53.291  70.542  1.00 17.82 ? 1189 LEU   B CD2   1 
ATOM   17676 N  N     . VAL   B  1  1192 ? 18.915  54.687  70.080  1.00 17.78 ? 1190 VAL   B N     1 
ATOM   17677 C  CA    . VAL   B  1  1192 ? 19.064  55.921  69.316  1.00 18.34 ? 1190 VAL   B CA    1 
ATOM   17678 C  C     . VAL   B  1  1192 ? 17.946  56.019  68.288  1.00 18.08 ? 1190 VAL   B C     1 
ATOM   17679 O  O     . VAL   B  1  1192 ? 17.667  55.054  67.564  1.00 20.02 ? 1190 VAL   B O     1 
ATOM   17680 C  CB    . VAL   B  1  1192 ? 20.433  55.968  68.619  1.00 21.42 ? 1190 VAL   B CB    1 
ATOM   17681 C  CG1   . VAL   B  1  1192 ? 20.562  57.217  67.759  1.00 19.81 ? 1190 VAL   B CG1   1 
ATOM   17682 C  CG2   . VAL   B  1  1192 ? 21.576  55.906  69.648  1.00 20.07 ? 1190 VAL   B CG2   1 
ATOM   17683 N  N     . GLN   B  1  1193 ? 17.337  57.194  68.190  1.00 17.07 ? 1191 GLN   B N     1 
ATOM   17684 C  CA    . GLN   B  1  1193 ? 16.383  57.496  67.136  1.00 17.01 ? 1191 GLN   B CA    1 
ATOM   17685 C  C     . GLN   B  1  1193 ? 16.893  58.699  66.371  1.00 18.37 ? 1191 GLN   B C     1 
ATOM   17686 O  O     . GLN   B  1  1193 ? 17.234  59.721  66.975  1.00 18.27 ? 1191 GLN   B O     1 
ATOM   17687 C  CB    . GLN   B  1  1193 ? 15.025  57.846  67.715  1.00 17.61 ? 1191 GLN   B CB    1 
ATOM   17688 C  CG    . GLN   B  1  1193 ? 14.468  56.778  68.604  1.00 19.83 ? 1191 GLN   B CG    1 
ATOM   17689 C  CD    . GLN   B  1  1193 ? 13.002  56.977  68.815  1.00 20.33 ? 1191 GLN   B CD    1 
ATOM   17690 O  OE1   . GLN   B  1  1193 ? 12.215  56.900  67.875  1.00 19.75 ? 1191 GLN   B OE1   1 
ATOM   17691 N  NE2   . GLN   B  1  1193 ? 12.622  57.260  70.049  1.00 18.72 ? 1191 GLN   B NE2   1 
ATOM   17692 N  N     . ALA   B  1  1194 ? 16.915  58.591  65.052  1.00 16.88 ? 1192 ALA   B N     1 
ATOM   17693 C  CA    . ALA   B  1  1194 ? 17.426  59.670  64.225  1.00 19.29 ? 1192 ALA   B CA    1 
ATOM   17694 C  C     . ALA   B  1  1194 ? 16.415  60.033  63.155  1.00 19.15 ? 1192 ALA   B C     1 
ATOM   17695 O  O     . ALA   B  1  1194 ? 15.610  59.202  62.718  1.00 24.07 ? 1192 ALA   B O     1 
ATOM   17696 C  CB    . ALA   B  1  1194 ? 18.746  59.296  63.566  1.00 20.31 ? 1192 ALA   B CB    1 
ATOM   17697 N  N     . ALA   B  1  1195 ? 16.467  61.293  62.740  1.00 18.74 ? 1193 ALA   B N     1 
ATOM   17698 C  CA    . ALA   B  1  1195 ? 15.602  61.779  61.685  1.00 21.14 ? 1193 ALA   B CA    1 
ATOM   17699 C  C     . ALA   B  1  1195 ? 16.290  62.978  61.070  1.00 23.24 ? 1193 ALA   B C     1 
ATOM   17700 O  O     . ALA   B  1  1195 ? 17.079  63.656  61.728  1.00 21.75 ? 1193 ALA   B O     1 
ATOM   17701 C  CB    . ALA   B  1  1195 ? 14.235  62.216  62.230  1.00 20.75 ? 1193 ALA   B CB    1 
ATOM   17702 N  N     . SER   B  1  1196 ? 16.001  63.219  59.801  1.00 20.82 ? 1194 SER   B N     1 
ATOM   17703 C  CA    . SER   B  1  1196 ? 16.446  64.453  59.189  1.00 22.70 ? 1194 SER   B CA    1 
ATOM   17704 C  C     . SER   B  1  1196 ? 15.496  65.583  59.556  1.00 24.83 ? 1194 SER   B C     1 
ATOM   17705 O  O     . SER   B  1  1196 ? 14.373  65.365  60.026  1.00 23.76 ? 1194 SER   B O     1 
ATOM   17706 C  CB    . SER   B  1  1196 ? 16.434  64.308  57.677  1.00 25.29 ? 1194 SER   B CB    1 
ATOM   17707 O  OG    . SER   B  1  1196 ? 15.113  64.048  57.257  1.00 26.48 ? 1194 SER   B OG    1 
ATOM   17708 N  N     . SER   B  1  1197 ? 15.960  66.813  59.327  1.00 23.89 ? 1195 SER   B N     1 
ATOM   17709 C  CA    . SER   B  1  1197 ? 15.114  67.973  59.566  1.00 23.55 ? 1195 SER   B CA    1 
ATOM   17710 C  C     . SER   B  1  1197 ? 13.846  67.906  58.730  1.00 23.55 ? 1195 SER   B C     1 
ATOM   17711 O  O     . SER   B  1  1197 ? 12.763  68.266  59.203  1.00 24.54 ? 1195 SER   B O     1 
ATOM   17712 C  CB    . SER   B  1  1197 ? 15.890  69.246  59.248  1.00 25.40 ? 1195 SER   B CB    1 
ATOM   17713 O  OG    . SER   B  1  1197 ? 17.070  69.308  60.020  1.00 26.55 ? 1195 SER   B OG    1 
ATOM   17714 N  N     . GLY   B  1  1198 ? 13.959  67.456  57.480  1.00 25.20 ? 1196 GLY   B N     1 
ATOM   17715 C  CA    . GLY   B  1  1198 ? 12.773  67.350  56.649  1.00 28.72 ? 1196 GLY   B CA    1 
ATOM   17716 C  C     . GLY   B  1  1198 ? 11.827  66.274  57.141  1.00 31.77 ? 1196 GLY   B C     1 
ATOM   17717 O  O     . GLY   B  1  1198 ? 10.604  66.430  57.079  1.00 29.03 ? 1196 GLY   B O     1 
ATOM   17718 N  N     . GLU   B  1  1199 ? 12.382  65.172  57.647  1.00 26.75 ? 1197 GLU   B N     1 
ATOM   17719 C  CA    . GLU   B  1  1199 ? 11.558  64.114  58.215  1.00 29.29 ? 1197 GLU   B CA    1 
ATOM   17720 C  C     . GLU   B  1  1199 ? 10.803  64.614  59.444  1.00 29.05 ? 1197 GLU   B C     1 
ATOM   17721 O  O     . GLU   B  1  1199 ? 9.615   64.324  59.618  1.00 29.03 ? 1197 GLU   B O     1 
ATOM   17722 C  CB    . GLU   B  1  1199 ? 12.464  62.928  58.549  1.00 28.32 ? 1197 GLU   B CB    1 
ATOM   17723 C  CG    . GLU   B  1  1199 ? 11.784  61.651  58.963  1.00 37.17 ? 1197 GLU   B CG    1 
ATOM   17724 C  CD    . GLU   B  1  1199 ? 12.796  60.542  59.219  1.00 38.17 ? 1197 GLU   B CD    1 
ATOM   17725 O  OE1   . GLU   B  1  1199 ? 14.001  60.750  58.927  1.00 38.60 ? 1197 GLU   B OE1   1 
ATOM   17726 O  OE2   . GLU   B  1  1199 ? 12.396  59.471  59.715  1.00 46.11 ? 1197 GLU   B OE2   1 
ATOM   17727 N  N     . ILE   B  1  1200 ? 11.474  65.385  60.302  1.00 24.33 ? 1198 ILE   B N     1 
ATOM   17728 C  CA    . ILE   B  1  1200 ? 10.796  65.986  61.446  1.00 26.25 ? 1198 ILE   B CA    1 
ATOM   17729 C  C     . ILE   B  1  1200 ? 9.646   66.874  60.989  1.00 28.71 ? 1198 ILE   B C     1 
ATOM   17730 O  O     . ILE   B  1  1200 ? 8.548   66.843  61.563  1.00 28.05 ? 1198 ILE   B O     1 
ATOM   17731 C  CB    . ILE   B  1  1200 ? 11.808  66.755  62.311  1.00 23.72 ? 1198 ILE   B CB    1 
ATOM   17732 C  CG1   . ILE   B  1  1200 ? 12.809  65.784  62.935  1.00 23.94 ? 1198 ILE   B CG1   1 
ATOM   17733 C  CG2   . ILE   B  1  1200 ? 11.095  67.600  63.358  1.00 23.44 ? 1198 ILE   B CG2   1 
ATOM   17734 C  CD1   . ILE   B  1  1200 ? 13.921  66.473  63.677  1.00 23.57 ? 1198 ILE   B CD1   1 
ATOM   17735 N  N     . ALA   B  1  1201 ? 9.873   67.681  59.950  1.00 28.13 ? 1199 ALA   B N     1 
ATOM   17736 C  CA    . ALA   B  1  1201 ? 8.833   68.599  59.500  1.00 30.76 ? 1199 ALA   B CA    1 
ATOM   17737 C  C     . ALA   B  1  1201 ? 7.651   67.863  58.881  1.00 33.19 ? 1199 ALA   B C     1 
ATOM   17738 O  O     . ALA   B  1  1201 ? 6.507   68.304  59.027  1.00 33.90 ? 1199 ALA   B O     1 
ATOM   17739 C  CB    . ALA   B  1  1201 ? 9.407   69.604  58.502  1.00 29.15 ? 1199 ALA   B CB    1 
ATOM   17740 N  N     . ARG   B  1  1202 ? 7.898   66.744  58.198  1.00 34.10 ? 1200 ARG   B N     1 
ATOM   17741 C  CA    . ARG   B  1  1202 ? 6.846   66.094  57.426  1.00 31.66 ? 1200 ARG   B CA    1 
ATOM   17742 C  C     . ARG   B  1  1202 ? 6.169   64.942  58.157  1.00 34.47 ? 1200 ARG   B C     1 
ATOM   17743 O  O     . ARG   B  1  1202 ? 5.002   64.651  57.871  1.00 36.14 ? 1200 ARG   B O     1 
ATOM   17744 C  CB    . ARG   B  1  1202 ? 7.396   65.601  56.080  1.00 37.40 ? 1200 ARG   B CB    1 
ATOM   17745 C  CG    . ARG   B  1  1202 ? 7.914   64.183  56.083  1.00 39.02 ? 1200 ARG   B CG    1 
ATOM   17746 C  CD    . ARG   B  1  1202 ? 8.392   63.768  54.696  1.00 44.97 ? 1200 ARG   B CD    1 
ATOM   17747 N  NE    . ARG   B  1  1202 ? 9.656   64.405  54.346  1.00 44.32 ? 1200 ARG   B NE    1 
ATOM   17748 C  CZ    . ARG   B  1  1202 ? 10.846  63.845  54.519  1.00 42.81 ? 1200 ARG   B CZ    1 
ATOM   17749 N  NH1   . ARG   B  1  1202 ? 10.970  62.623  55.010  1.00 41.27 ? 1200 ARG   B NH1   1 
ATOM   17750 N  NH2   . ARG   B  1  1202 ? 11.938  64.529  54.189  1.00 44.22 ? 1200 ARG   B NH2   1 
ATOM   17751 N  N     . ASN   B  1  1203 ? 6.846   64.308  59.104  1.00 30.08 ? 1201 ASN   B N     1 
ATOM   17752 C  CA    . ASN   B  1  1203 ? 6.343   63.089  59.739  1.00 30.65 ? 1201 ASN   B CA    1 
ATOM   17753 C  C     . ASN   B  1  1203 ? 6.119   63.332  61.222  1.00 29.83 ? 1201 ASN   B C     1 
ATOM   17754 O  O     . ASN   B  1  1203 ? 7.102   63.462  61.979  1.00 27.54 ? 1201 ASN   B O     1 
ATOM   17755 C  CB    . ASN   B  1  1203 ? 7.343   61.953  59.524  1.00 31.66 ? 1201 ASN   B CB    1 
ATOM   17756 C  CG    . ASN   B  1  1203 ? 6.891   60.641  60.142  1.00 33.33 ? 1201 ASN   B CG    1 
ATOM   17757 O  OD1   . ASN   B  1  1203 ? 5.767   60.520  60.638  1.00 34.34 ? 1201 ASN   B OD1   1 
ATOM   17758 N  ND2   . ASN   B  1  1203 ? 7.765   59.643  60.100  1.00 34.48 ? 1201 ASN   B ND2   1 
ATOM   17759 N  N     . PRO   B  1  1204 ? 4.867   63.377  61.687  1.00 30.56 ? 1202 PRO   B N     1 
ATOM   17760 C  CA    . PRO   B  1  1204 ? 4.617   63.555  63.129  1.00 33.33 ? 1202 PRO   B CA    1 
ATOM   17761 C  C     . PRO   B  1  1204 ? 5.229   62.465  63.983  1.00 29.25 ? 1202 PRO   B C     1 
ATOM   17762 O  O     . PRO   B  1  1204 ? 5.490   62.695  65.171  1.00 30.11 ? 1202 PRO   B O     1 
ATOM   17763 C  CB    . PRO   B  1  1204 ? 3.082   63.539  63.230  1.00 35.37 ? 1202 PRO   B CB    1 
ATOM   17764 C  CG    . PRO   B  1  1204 ? 2.592   63.813  61.850  1.00 38.79 ? 1202 PRO   B CG    1 
ATOM   17765 C  CD    . PRO   B  1  1204 ? 3.617   63.244  60.918  1.00 35.09 ? 1202 PRO   B CD    1 
ATOM   17766 N  N     . ASP   B  1  1205 ? 5.463   61.283  63.419  1.00 30.40 ? 1203 ASP   B N     1 
ATOM   17767 C  CA    . ASP   B  1  1205 ? 6.066   60.168  64.134  1.00 32.75 ? 1203 ASP   B CA    1 
ATOM   17768 C  C     . ASP   B  1  1205 ? 7.538   59.977  63.782  1.00 31.60 ? 1203 ASP   B C     1 
ATOM   17769 O  O     . ASP   B  1  1205 ? 8.055   58.858  63.874  1.00 27.89 ? 1203 ASP   B O     1 
ATOM   17770 C  CB    . ASP   B  1  1205 ? 5.275   58.883  63.886  1.00 31.96 ? 1203 ASP   B CB    1 
ATOM   17771 C  CG    . ASP   B  1  1205 ? 3.864   58.945  64.459  1.00 37.19 ? 1203 ASP   B CG    1 
ATOM   17772 O  OD1   . ASP   B  1  1205 ? 3.609   59.801  65.331  1.00 33.89 ? 1203 ASP   B OD1   1 
ATOM   17773 O  OD2   . ASP   B  1  1205 ? 3.012   58.134  64.040  1.00 43.86 ? 1203 ASP   B OD2   1 
ATOM   17774 N  N     . ALA   B  1  1206 ? 8.220   61.049  63.368  1.00 27.70 ? 1204 ALA   B N     1 
ATOM   17775 C  CA    . ALA   B  1  1206 ? 9.654   60.957  63.104  1.00 29.31 ? 1204 ALA   B CA    1 
ATOM   17776 C  C     . ALA   B  1  1206 ? 10.393  60.336  64.283  1.00 24.07 ? 1204 ALA   B C     1 
ATOM   17777 O  O     . ALA   B  1  1206 ? 11.283  59.497  64.099  1.00 27.34 ? 1204 ALA   B O     1 
ATOM   17778 C  CB    . ALA   B  1  1206 ? 10.212  62.346  62.782  1.00 27.98 ? 1204 ALA   B CB    1 
ATOM   17779 N  N     . TYR   B  1  1207 ? 10.040  60.741  65.504  1.00 21.42 ? 1205 TYR   B N     1 
ATOM   17780 C  CA    . TYR   B  1  1207 ? 10.533  60.112  66.719  1.00 22.38 ? 1205 TYR   B CA    1 
ATOM   17781 C  C     . TYR   B  1  1207 ? 9.384   59.337  67.346  1.00 21.78 ? 1205 TYR   B C     1 
ATOM   17782 O  O     . TYR   B  1  1207 ? 8.279   59.869  67.494  1.00 27.11 ? 1205 TYR   B O     1 
ATOM   17783 C  CB    . TYR   B  1  1207 ? 11.080  61.150  67.704  1.00 20.06 ? 1205 TYR   B CB    1 
ATOM   17784 C  CG    . TYR   B  1  1207 ? 12.259  61.928  67.155  1.00 19.16 ? 1205 TYR   B CG    1 
ATOM   17785 C  CD1   . TYR   B  1  1207 ? 13.431  61.276  66.789  1.00 20.69 ? 1205 TYR   B CD1   1 
ATOM   17786 C  CD2   . TYR   B  1  1207 ? 12.204  63.311  67.009  1.00 20.18 ? 1205 TYR   B CD2   1 
ATOM   17787 C  CE1   . TYR   B  1  1207 ? 14.516  61.977  66.283  1.00 18.26 ? 1205 TYR   B CE1   1 
ATOM   17788 C  CE2   . TYR   B  1  1207 ? 13.288  64.023  66.495  1.00 20.07 ? 1205 TYR   B CE2   1 
ATOM   17789 C  CZ    . TYR   B  1  1207 ? 14.433  63.347  66.138  1.00 20.46 ? 1205 TYR   B CZ    1 
ATOM   17790 O  OH    . TYR   B  1  1207 ? 15.513  64.045  65.624  1.00 19.97 ? 1205 TYR   B OH    1 
ATOM   17791 N  N     . CYS   B  1  1208 ? 9.648   58.086  67.688  1.00 18.47 ? 1206 CYS   B N     1 
ATOM   17792 C  CA    . CYS   B  1  1208 ? 8.637   57.196  68.235  1.00 18.79 ? 1206 CYS   B CA    1 
ATOM   17793 C  C     . CYS   B  1  1208 ? 8.663   57.279  69.757  1.00 18.97 ? 1206 CYS   B C     1 
ATOM   17794 O  O     . CYS   B  1  1208 ? 9.700   57.034  70.381  1.00 19.00 ? 1206 CYS   B O     1 
ATOM   17795 C  CB    . CYS   B  1  1208 ? 8.934   55.773  67.771  1.00 22.88 ? 1206 CYS   B CB    1 
ATOM   17796 S  SG    . CYS   B  1  1208 ? 7.727   54.572  68.332  1.00 23.71 ? 1206 CYS   B SG    1 
ATOM   17797 N  N     . LEU   B  1  1209 ? 7.513   57.600  70.354  1.00 17.16 ? 1207 LEU   B N     1 
ATOM   17798 C  CA    . LEU   B  1  1209 ? 7.427   57.672  71.809  1.00 18.06 ? 1207 LEU   B CA    1 
ATOM   17799 C  C     . LEU   B  1  1209 ? 7.485   56.301  72.468  1.00 17.30 ? 1207 LEU   B C     1 
ATOM   17800 O  O     . LEU   B  1  1209 ? 7.706   56.236  73.677  1.00 16.90 ? 1207 LEU   B O     1 
ATOM   17801 C  CB    . LEU   B  1  1209 ? 6.161   58.419  72.238  1.00 16.15 ? 1207 LEU   B CB    1 
ATOM   17802 C  CG    . LEU   B  1  1209 ? 5.972   59.790  71.584  1.00 18.79 ? 1207 LEU   B CG    1 
ATOM   17803 C  CD1   . LEU   B  1  1209 ? 4.723   60.472  72.118  1.00 21.95 ? 1207 LEU   B CD1   1 
ATOM   17804 C  CD2   . LEU   B  1  1209 ? 7.191   60.674  71.771  1.00 19.90 ? 1207 LEU   B CD2   1 
ATOM   17805 N  N     . ASN   B  1  1210 ? 7.293   55.212  71.715  1.00 17.65 ? 1208 ASN   B N     1 
ATOM   17806 C  CA    . ASN   B  1  1210 ? 7.381   53.887  72.324  1.00 19.62 ? 1208 ASN   B CA    1 
ATOM   17807 C  C     . ASN   B  1  1210 ? 8.745   53.661  72.952  1.00 18.44 ? 1208 ASN   B C     1 
ATOM   17808 O  O     . ASN   B  1  1210 ? 8.854   52.952  73.957  1.00 19.81 ? 1208 ASN   B O     1 
ATOM   17809 C  CB    . ASN   B  1  1210 ? 7.158   52.783  71.283  1.00 23.10 ? 1208 ASN   B CB    1 
ATOM   17810 C  CG    . ASN   B  1  1210 ? 5.746   52.787  70.690  1.00 23.79 ? 1208 ASN   B CG    1 
ATOM   17811 O  OD1   . ASN   B  1  1210 ? 4.980   53.730  70.862  1.00 27.82 ? 1208 ASN   B OD1   1 
ATOM   17812 N  ND2   . ASN   B  1  1210 ? 5.419   51.728  69.960  1.00 29.62 ? 1208 ASN   B ND2   1 
ATOM   17813 N  N     . TRP   B  1  1211 ? 9.793   54.244  72.375  1.00 15.66 ? 1209 TRP   B N     1 
ATOM   17814 C  CA    . TRP   B  1  1211 ? 11.152  53.972  72.814  1.00 17.06 ? 1209 TRP   B CA    1 
ATOM   17815 C  C     . TRP   B  1  1211 ? 11.633  54.964  73.849  1.00 19.15 ? 1209 TRP   B C     1 
ATOM   17816 O  O     . TRP   B  1  1211 ? 12.776  54.858  74.298  1.00 20.02 ? 1209 TRP   B O     1 
ATOM   17817 C  CB    . TRP   B  1  1211 ? 12.122  53.958  71.622  1.00 19.54 ? 1209 TRP   B CB    1 
ATOM   17818 C  CG    . TRP   B  1  1211 ? 11.534  53.294  70.421  1.00 20.17 ? 1209 TRP   B CG    1 
ATOM   17819 C  CD1   . TRP   B  1  1211 ? 11.467  53.799  69.151  1.00 22.32 ? 1209 TRP   B CD1   1 
ATOM   17820 C  CD2   . TRP   B  1  1211 ? 10.885  52.020  70.381  1.00 17.96 ? 1209 TRP   B CD2   1 
ATOM   17821 N  NE1   . TRP   B  1  1211 ? 10.823  52.915  68.327  1.00 20.53 ? 1209 TRP   B NE1   1 
ATOM   17822 C  CE2   . TRP   B  1  1211 ? 10.465  51.809  69.053  1.00 20.03 ? 1209 TRP   B CE2   1 
ATOM   17823 C  CE3   . TRP   B  1  1211 ? 10.622  51.028  71.340  1.00 19.72 ? 1209 TRP   B CE3   1 
ATOM   17824 C  CZ2   . TRP   B  1  1211 ? 9.789   50.654  68.656  1.00 20.30 ? 1209 TRP   B CZ2   1 
ATOM   17825 C  CZ3   . TRP   B  1  1211 ? 9.945   49.885  70.945  1.00 19.69 ? 1209 TRP   B CZ3   1 
ATOM   17826 C  CH2   . TRP   B  1  1211 ? 9.534   49.710  69.615  1.00 19.54 ? 1209 TRP   B CH2   1 
ATOM   17827 N  N     . LEU   B  1  1212 ? 10.791  55.921  74.228  1.00 16.82 ? 1210 LEU   B N     1 
ATOM   17828 C  CA    . LEU   B  1  1212 ? 11.165  56.961  75.167  1.00 14.51 ? 1210 LEU   B CA    1 
ATOM   17829 C  C     . LEU   B  1  1212 ? 10.551  56.736  76.535  1.00 16.17 ? 1210 LEU   B C     1 
ATOM   17830 O  O     . LEU   B  1  1212 ? 10.702  57.576  77.424  1.00 15.00 ? 1210 LEU   B O     1 
ATOM   17831 C  CB    . LEU   B  1  1212 ? 10.788  58.330  74.610  1.00 14.32 ? 1210 LEU   B CB    1 
ATOM   17832 C  CG    . LEU   B  1  1212 ? 11.725  58.783  73.482  1.00 14.51 ? 1210 LEU   B CG    1 
ATOM   17833 C  CD1   . LEU   B  1  1212 ? 11.108  59.942  72.777  1.00 16.97 ? 1210 LEU   B CD1   1 
ATOM   17834 C  CD2   . LEU   B  1  1212 ? 13.080  59.164  74.043  1.00 16.39 ? 1210 LEU   B CD2   1 
ATOM   17835 N  N     . VAL   B  1  1213 ? 9.863   55.618  76.715  1.00 15.49 ? 1211 VAL   B N     1 
ATOM   17836 C  CA    . VAL   B  1  1213 ? 9.395   55.189  78.022  1.00 15.67 ? 1211 VAL   B CA    1 
ATOM   17837 C  C     . VAL   B  1  1213 ? 10.125  53.907  78.375  1.00 17.98 ? 1211 VAL   B C     1 
ATOM   17838 O  O     . VAL   B  1  1213 ? 10.664  53.215  77.508  1.00 17.86 ? 1211 VAL   B O     1 
ATOM   17839 C  CB    . VAL   B  1  1213 ? 7.871   54.986  78.029  1.00 15.31 ? 1211 VAL   B CB    1 
ATOM   17840 C  CG1   . VAL   B  1  1213 ? 7.183   56.333  77.866  1.00 16.85 ? 1211 VAL   B CG1   1 
ATOM   17841 C  CG2   . VAL   B  1  1213 ? 7.467   54.027  76.913  1.00 16.47 ? 1211 VAL   B CG2   1 
ATOM   17842 N  N     . GLU   B  1  1214 ? 10.191  53.621  79.674  1.00 16.48 ? 1212 GLU   B N     1 
ATOM   17843 C  CA    . GLU   B  1  1214 ? 10.764  52.382  80.177  1.00 17.10 ? 1212 GLU   B CA    1 
ATOM   17844 C  C     . GLU   B  1  1214 ? 9.638   51.505  80.699  1.00 14.51 ? 1212 GLU   B C     1 
ATOM   17845 O  O     . GLU   B  1  1214 ? 8.800   51.963  81.475  1.00 15.78 ? 1212 GLU   B O     1 
ATOM   17846 C  CB    . GLU   B  1  1214 ? 11.755  52.642  81.313  1.00 20.06 ? 1212 GLU   B CB    1 
ATOM   17847 C  CG    . GLU   B  1  1214 ? 12.420  51.354  81.790  1.00 22.73 ? 1212 GLU   B CG    1 
ATOM   17848 C  CD    . GLU   B  1  1214 ? 13.262  51.514  83.047  1.00 28.13 ? 1212 GLU   B CD    1 
ATOM   17849 O  OE1   . GLU   B  1  1214 ? 13.741  52.635  83.321  1.00 29.19 ? 1212 GLU   B OE1   1 
ATOM   17850 O  OE2   . GLU   B  1  1214 ? 13.430  50.500  83.764  1.00 32.55 ? 1212 GLU   B OE2   1 
ATOM   17851 N  N     . GLU   B  1  1215 ? 9.629   50.255  80.267  1.00 15.28 ? 1213 GLU   B N     1 
ATOM   17852 C  CA    . GLU   B  1  1215 ? 8.677   49.279  80.759  1.00 15.46 ? 1213 GLU   B CA    1 
ATOM   17853 C  C     . GLU   B  1  1215 ? 9.172   48.689  82.066  1.00 13.02 ? 1213 GLU   B C     1 
ATOM   17854 O  O     . GLU   B  1  1215 ? 10.354  48.356  82.213  1.00 14.62 ? 1213 GLU   B O     1 
ATOM   17855 C  CB    . GLU   B  1  1215 ? 8.578   48.134  79.760  1.00 15.69 ? 1213 GLU   B CB    1 
ATOM   17856 C  CG    . GLU   B  1  1215 ? 8.040   48.515  78.392  1.00 15.83 ? 1213 GLU   B CG    1 
ATOM   17857 C  CD    . GLU   B  1  1215 ? 8.270   47.410  77.387  1.00 13.88 ? 1213 GLU   B CD    1 
ATOM   17858 O  OE1   . GLU   B  1  1215 ? 9.416   47.298  76.904  1.00 15.75 ? 1213 GLU   B OE1   1 
ATOM   17859 O  OE2   . GLU   B  1  1215 ? 7.326   46.654  77.104  1.00 17.11 ? 1213 GLU   B OE2   1 
ATOM   17860 N  N     . VAL   B  1  1216 ? 8.260   48.541  83.018  1.00 15.05 ? 1214 VAL   B N     1 
ATOM   17861 C  CA    . VAL   B  1  1216 ? 8.571   47.862  84.263  1.00 15.91 ? 1214 VAL   B CA    1 
ATOM   17862 C  C     . VAL   B  1  1216 ? 7.501   46.817  84.498  1.00 14.54 ? 1214 VAL   B C     1 
ATOM   17863 O  O     . VAL   B  1  1216 ? 6.303   47.120  84.441  1.00 15.80 ? 1214 VAL   B O     1 
ATOM   17864 C  CB    . VAL   B  1  1216 ? 8.676   48.827  85.455  1.00 16.02 ? 1214 VAL   B CB    1 
ATOM   17865 C  CG1   . VAL   B  1  1216 ? 8.834   48.037  86.763  1.00 17.88 ? 1214 VAL   B CG1   1 
ATOM   17866 C  CG2   . VAL   B  1  1216 ? 9.842   49.799  85.245  1.00 17.45 ? 1214 VAL   B CG2   1 
ATOM   17867 N  N     . SER   B  1  1217 ? 7.933   45.585  84.729  1.00 13.46 ? 1215 SER   B N     1 
ATOM   17868 C  CA    . SER   B  1  1217 ? 7.052   44.488  85.085  1.00 13.22 ? 1215 SER   B CA    1 
ATOM   17869 C  C     . SER   B  1  1217 ? 7.230   44.195  86.563  1.00 13.32 ? 1215 SER   B C     1 
ATOM   17870 O  O     . SER   B  1  1217 ? 8.358   44.169  87.062  1.00 14.98 ? 1215 SER   B O     1 
ATOM   17871 C  CB    . SER   B  1  1217 ? 7.451   43.252  84.287  1.00 16.28 ? 1215 SER   B CB    1 
ATOM   17872 O  OG    . SER   B  1  1217 ? 6.964   42.067  84.891  1.00 18.95 ? 1215 SER   B OG    1 
ATOM   17873 N  N     . ALA   B  1  1218 ? 6.122   43.998  87.264  1.00 13.97 ? 1216 ALA   B N     1 
ATOM   17874 C  CA    . ALA   B  1  1218 ? 6.169   43.638  88.671  1.00 15.96 ? 1216 ALA   B CA    1 
ATOM   17875 C  C     . ALA   B  1  1218 ? 5.247   42.456  88.886  1.00 16.91 ? 1216 ALA   B C     1 
ATOM   17876 O  O     . ALA   B  1  1218 ? 4.062   42.514  88.534  1.00 17.37 ? 1216 ALA   B O     1 
ATOM   17877 C  CB    . ALA   B  1  1218 ? 5.747   44.807  89.561  1.00 16.27 ? 1216 ALA   B CB    1 
ATOM   17878 N  N     . SER   B  1  1219 ? 5.779   41.390  89.469  1.00 14.98 ? 1217 SER   B N     1 
ATOM   17879 C  CA    . SER   B  1  1219 ? 4.996   40.202  89.759  1.00 14.67 ? 1217 SER   B CA    1 
ATOM   17880 C  C     . SER   B  1  1219 ? 4.928   40.037  91.265  1.00 13.58 ? 1217 SER   B C     1 
ATOM   17881 O  O     . SER   B  1  1219 ? 5.960   39.851  91.913  1.00 13.42 ? 1217 SER   B O     1 
ATOM   17882 C  CB    . SER   B  1  1219 ? 5.638   38.974  89.134  1.00 15.53 ? 1217 SER   B CB    1 
ATOM   17883 O  OG    . SER   B  1  1219 ? 4.853   37.820  89.383  1.00 17.44 ? 1217 SER   B OG    1 
ATOM   17884 N  N     . ILE   B  1  1220 ? 3.723   40.108  91.811  1.00 15.32 ? 1218 ILE   B N     1 
ATOM   17885 C  CA    . ILE   B  1  1220 ? 3.502   40.028  93.250  1.00 16.42 ? 1218 ILE   B CA    1 
ATOM   17886 C  C     . ILE   B  1  1220 ? 2.796   38.713  93.543  1.00 17.12 ? 1218 ILE   B C     1 
ATOM   17887 O  O     . ILE   B  1  1220 ? 1.696   38.470  93.035  1.00 17.47 ? 1218 ILE   B O     1 
ATOM   17888 C  CB    . ILE   B  1  1220 ? 2.645   41.207  93.720  1.00 19.64 ? 1218 ILE   B CB    1 
ATOM   17889 C  CG1   . ILE   B  1  1220 ? 3.275   42.516  93.237  1.00 22.87 ? 1218 ILE   B CG1   1 
ATOM   17890 C  CG2   . ILE   B  1  1220 ? 2.462   41.168  95.237  1.00 20.69 ? 1218 ILE   B CG2   1 
ATOM   17891 C  CD1   . ILE   B  1  1220 ? 2.302   43.640  93.066  1.00 30.96 ? 1218 ILE   B CD1   1 
ATOM   17892 N  N     . ASN   B  1  1221 ? 3.403   37.889  94.388  1.00 15.41 ? 1219 ASN   B N     1 
ATOM   17893 C  CA    . ASN   B  1  1221 ? 2.758   36.677  94.878  1.00 16.95 ? 1219 ASN   B CA    1 
ATOM   17894 C  C     . ASN   B  1  1221 ? 1.747   37.080  95.944  1.00 19.84 ? 1219 ASN   B C     1 
ATOM   17895 O  O     . ASN   B  1  1221 ? 2.128   37.465  97.054  1.00 19.27 ? 1219 ASN   B O     1 
ATOM   17896 C  CB    . ASN   B  1  1221 ? 3.826   35.748  95.453  1.00 16.56 ? 1219 ASN   B CB    1 
ATOM   17897 C  CG    . ASN   B  1  1221 ? 3.241   34.511  96.108  1.00 19.09 ? 1219 ASN   B CG    1 
ATOM   17898 O  OD1   . ASN   B  1  1221 ? 2.053   34.234  95.983  1.00 18.26 ? 1219 ASN   B OD1   1 
ATOM   17899 N  ND2   . ASN   B  1  1221 ? 4.082   33.763  96.819  1.00 20.39 ? 1219 ASN   B ND2   1 
ATOM   17900 N  N     . THR   B  1  1222 ? 0.463   37.004  95.614  1.00 16.23 ? 1220 THR   B N     1 
ATOM   17901 C  CA    . THR   B  1  1222 ? -0.591  37.379  96.549  1.00 17.63 ? 1220 THR   B CA    1 
ATOM   17902 C  C     . THR   B  1  1222 ? -1.089  36.194  97.356  1.00 23.13 ? 1220 THR   B C     1 
ATOM   17903 O  O     . THR   B  1  1222 ? -2.019  36.346  98.158  1.00 26.64 ? 1220 THR   B O     1 
ATOM   17904 C  CB    . THR   B  1  1222 ? -1.743  38.053  95.805  1.00 19.22 ? 1220 THR   B CB    1 
ATOM   17905 O  OG1   . THR   B  1  1222 ? -2.265  37.154  94.823  1.00 21.17 ? 1220 THR   B OG1   1 
ATOM   17906 C  CG2   . THR   B  1  1222 ? -1.263  39.326  95.107  1.00 22.32 ? 1220 THR   B CG2   1 
ATOM   17907 N  N     . ALA   B  1  1223 ? -0.496  35.023  97.162  1.00 20.20 ? 1221 ALA   B N     1 
ATOM   17908 C  CA    . ALA   B  1  1223 ? -0.745  33.871  98.013  1.00 26.20 ? 1221 ALA   B CA    1 
ATOM   17909 C  C     . ALA   B  1  1223 ? 0.301   33.725  99.110  1.00 35.05 ? 1221 ALA   B C     1 
ATOM   17910 O  O     . ALA   B  1  1223 ? 0.294   32.717  99.824  1.00 40.65 ? 1221 ALA   B O     1 
ATOM   17911 C  CB    . ALA   B  1  1223 ? -0.794  32.596  97.169  1.00 25.84 ? 1221 ALA   B CB    1 
ATOM   17912 N  N     . ALA   B  1  1224 ? 1.194   34.712  99.266  1.00 33.91 ? 1222 ALA   B N     1 
ATOM   17913 C  CA    . ALA   B  1  1224 ? 2.367   34.527  100.119 1.00 35.06 ? 1222 ALA   B CA    1 
ATOM   17914 C  C     . ALA   B  1  1224 ? 2.004   34.434  101.597 1.00 43.82 ? 1222 ALA   B C     1 
ATOM   17915 O  O     . ALA   B  1  1224 ? 2.746   33.823  102.375 1.00 40.57 ? 1222 ALA   B O     1 
ATOM   17916 C  CB    . ALA   B  1  1224 ? 3.392   35.639  99.882  1.00 30.34 ? 1222 ALA   B CB    1 
ATOM   17917 N  N     . ALA   B  1  1225 ? 0.880   35.029  102.006 1.00 48.13 ? 1223 ALA   B N     1 
ATOM   17918 C  CA    . ALA   B  1  1225 ? 0.463   34.979  103.404 1.00 43.47 ? 1223 ALA   B CA    1 
ATOM   17919 C  C     . ALA   B  1  1225 ? -0.141  33.639  103.804 1.00 48.67 ? 1223 ALA   B C     1 
ATOM   17920 O  O     . ALA   B  1  1225 ? -0.463  33.452  104.983 1.00 50.36 ? 1223 ALA   B O     1 
ATOM   17921 C  CB    . ALA   B  1  1225 ? -0.515  36.117  103.722 1.00 43.38 ? 1223 ALA   B CB    1 
ATOM   17922 N  N     . GLY   B  1  1226 ? -0.308  32.711  102.865 1.00 45.81 ? 1224 GLY   B N     1 
ATOM   17923 C  CA    . GLY   B  1  1226 ? -0.843  31.395  103.169 1.00 46.07 ? 1224 GLY   B CA    1 
ATOM   17924 C  C     . GLY   B  1  1226 ? -2.124  31.040  102.444 1.00 48.47 ? 1224 GLY   B C     1 
ATOM   17925 O  O     . GLY   B  1  1226 ? -2.611  29.912  102.610 1.00 42.11 ? 1224 GLY   B O     1 
ATOM   17926 N  N     . GLY   B  1  1227 ? -2.697  31.938  101.651 1.00 41.84 ? 1225 GLY   B N     1 
ATOM   17927 C  CA    . GLY   B  1  1227 ? -3.908  31.623  100.916 1.00 44.44 ? 1225 GLY   B CA    1 
ATOM   17928 C  C     . GLY   B  1  1227 ? -4.189  32.693  99.884  1.00 47.78 ? 1225 GLY   B C     1 
ATOM   17929 O  O     . GLY   B  1  1227 ? -3.441  33.665  99.742  1.00 43.79 ? 1225 GLY   B O     1 
ATOM   17930 N  N     . ASN   B  1  1228 ? -5.295  32.504  99.167  1.00 42.85 ? 1226 ASN   B N     1 
ATOM   17931 C  CA    . ASN   B  1  1228 ? -5.710  33.402  98.094  1.00 48.35 ? 1226 ASN   B CA    1 
ATOM   17932 C  C     . ASN   B  1  1228 ? -6.931  34.194  98.544  1.00 50.27 ? 1226 ASN   B C     1 
ATOM   17933 O  O     . ASN   B  1  1228 ? -7.949  33.609  98.931  1.00 55.37 ? 1226 ASN   B O     1 
ATOM   17934 C  CB    . ASN   B  1  1228 ? -6.033  32.609  96.822  1.00 46.28 ? 1226 ASN   B CB    1 
ATOM   17935 C  CG    . ASN   B  1  1228 ? -6.148  33.493  95.583  1.00 47.39 ? 1226 ASN   B CG    1 
ATOM   17936 O  OD1   . ASN   B  1  1228 ? -6.633  34.626  95.646  1.00 46.25 ? 1226 ASN   B OD1   1 
ATOM   17937 N  ND2   . ASN   B  1  1228 ? -5.692  32.977  94.451  1.00 38.41 ? 1226 ASN   B ND2   1 
ATOM   17938 N  N     . ALA   B  1  1229 ? -6.827  35.523  98.480  1.00 51.15 ? 1227 ALA   B N     1 
ATOM   17939 C  CA    . ALA   B  1  1229 ? -7.928  36.381  98.908  1.00 54.26 ? 1227 ALA   B CA    1 
ATOM   17940 C  C     . ALA   B  1  1229 ? -9.079  36.348  97.907  1.00 57.39 ? 1227 ALA   B C     1 
ATOM   17941 O  O     . ALA   B  1  1229 ? -10.246 36.205  98.292  1.00 54.57 ? 1227 ALA   B O     1 
ATOM   17942 C  CB    . ALA   B  1  1229 ? -7.427  37.812  99.103  1.00 49.22 ? 1227 ALA   B CB    1 
ATOM   17943 N  N     . SER   B  1  1230 ? -8.768  36.479  96.614  1.00 57.58 ? 1228 SER   B N     1 
ATOM   17944 C  CA    . SER   B  1  1230 ? -9.821  36.564  95.605  1.00 58.60 ? 1228 SER   B CA    1 
ATOM   17945 C  C     . SER   B  1  1230 ? -10.549 35.234  95.442  1.00 61.21 ? 1228 SER   B C     1 
ATOM   17946 O  O     . SER   B  1  1230 ? -11.772 35.210  95.254  1.00 62.55 ? 1228 SER   B O     1 
ATOM   17947 C  CB    . SER   B  1  1230 ? -9.239  37.042  94.274  1.00 57.55 ? 1228 SER   B CB    1 
ATOM   17948 N  N     . LEU   B  1  1231 ? -9.820  34.117  95.510  1.00 57.38 ? 1229 LEU   B N     1 
ATOM   17949 C  CA    . LEU   B  1  1231 ? -10.462 32.811  95.404  1.00 57.05 ? 1229 LEU   B CA    1 
ATOM   17950 C  C     . LEU   B  1  1231 ? -11.275 32.447  96.641  1.00 59.60 ? 1229 LEU   B C     1 
ATOM   17951 O  O     . LEU   B  1  1231 ? -11.989 31.438  96.616  1.00 59.84 ? 1229 LEU   B O     1 
ATOM   17952 C  CB    . LEU   B  1  1231 ? -9.433  31.716  95.110  1.00 52.48 ? 1229 LEU   B CB    1 
ATOM   17953 C  CG    . LEU   B  1  1231 ? -8.774  31.609  93.732  1.00 43.84 ? 1229 LEU   B CG    1 
ATOM   17954 C  CD1   . LEU   B  1  1231 ? -7.885  30.382  93.703  1.00 37.10 ? 1229 LEU   B CD1   1 
ATOM   17955 C  CD2   . LEU   B  1  1231 ? -9.798  31.536  92.624  1.00 44.46 ? 1229 LEU   B CD2   1 
ATOM   17956 N  N     . MET   B  1  1232 ? -11.182 33.235  97.717  1.00 58.16 ? 1230 MET   B N     1 
ATOM   17957 C  CA    . MET   B  1  1232 ? -12.039 33.003  98.876  1.00 57.76 ? 1230 MET   B CA    1 
ATOM   17958 C  C     . MET   B  1  1232 ? -13.511 33.194  98.518  1.00 58.84 ? 1230 MET   B C     1 
ATOM   17959 O  O     . MET   B  1  1232 ? -14.380 32.462  99.010  1.00 51.75 ? 1230 MET   B O     1 
ATOM   17960 C  CB    . MET   B  1  1232 ? -11.627 33.928  100.022 1.00 53.62 ? 1230 MET   B CB    1 
ATOM   17961 N  N     . ALA   B  1  1233 ? -13.808 34.162  97.648  1.00 65.21 ? 1231 ALA   B N     1 
ATOM   17962 C  CA    . ALA   B  1  1233 ? -15.174 34.384  97.188  1.00 69.71 ? 1231 ALA   B CA    1 
ATOM   17963 C  C     . ALA   B  1  1233 ? -15.588 33.439  96.067  1.00 70.23 ? 1231 ALA   B C     1 
ATOM   17964 O  O     . ALA   B  1  1233 ? -16.786 33.326  95.786  1.00 73.04 ? 1231 ALA   B O     1 
ATOM   17965 C  CB    . ALA   B  1  1233 ? -15.351 35.837  96.734  1.00 66.92 ? 1231 ALA   B CB    1 
ATOM   17966 N  N     . ILE   B  1  1234 ? -14.639 32.757  95.431  1.00 64.83 ? 1232 ILE   B N     1 
ATOM   17967 C  CA    . ILE   B  1  1234 ? -14.922 31.878  94.301  1.00 62.11 ? 1232 ILE   B CA    1 
ATOM   17968 C  C     . ILE   B  1  1234 ? -15.280 30.492  94.834  1.00 59.37 ? 1232 ILE   B C     1 
ATOM   17969 O  O     . ILE   B  1  1234 ? -14.418 29.760  95.329  1.00 56.90 ? 1232 ILE   B O     1 
ATOM   17970 C  CB    . ILE   B  1  1234 ? -13.742 31.830  93.321  1.00 56.51 ? 1232 ILE   B CB    1 
ATOM   17971 C  CG1   . ILE   B  1  1234 ? -13.643 33.155  92.559  1.00 58.98 ? 1232 ILE   B CG1   1 
ATOM   17972 C  CG2   . ILE   B  1  1234 ? -13.880 30.660  92.362  1.00 47.04 ? 1232 ILE   B CG2   1 
ATOM   17973 C  CD1   . ILE   B  1  1234 ? -12.708 33.129  91.380  1.00 46.39 ? 1232 ILE   B CD1   1 
ATOM   17974 N  N     . GLY   B  1  1235 ? -16.558 30.136  94.736  1.00 54.75 ? 1233 GLY   B N     1 
ATOM   17975 C  CA    . GLY   B  1  1235 ? -17.037 28.831  95.159  1.00 40.96 ? 1233 GLY   B CA    1 
ATOM   17976 C  C     . GLY   B  1  1235 ? -17.938 28.204  94.109  1.00 40.66 ? 1233 GLY   B C     1 
ATOM   17977 O  O     . GLY   B  1  1235 ? -18.707 28.893  93.434  1.00 51.13 ? 1233 GLY   B O     1 
ATOM   17978 O  OXT   . GLY   B  1  1235 ? -17.931 26.994  93.892  1.00 25.33 ? 1233 GLY   B OXT   1 
HETATM 17979 P  PA    . FAD   C  2  .    ? -37.764 43.547  82.446  1.00 21.00 ? 1301 FAD   A PA    1 
HETATM 17980 O  O1A   . FAD   C  2  .    ? -36.295 43.128  82.242  1.00 23.31 ? 1301 FAD   A O1A   1 
HETATM 17981 O  O2A   . FAD   C  2  .    ? -38.751 42.558  82.808  1.00 22.87 ? 1301 FAD   A O2A   1 
HETATM 17982 O  O5B   . FAD   C  2  .    ? -37.931 44.584  83.488  1.00 20.93 ? 1301 FAD   A O5B   1 
HETATM 17983 C  C5B   . FAD   C  2  .    ? -36.879 45.521  83.708  1.00 20.68 ? 1301 FAD   A C5B   1 
HETATM 17984 C  C4B   . FAD   C  2  .    ? -37.356 46.601  84.669  1.00 21.34 ? 1301 FAD   A C4B   1 
HETATM 17985 O  O4B   . FAD   C  2  .    ? -37.345 46.150  85.988  1.00 19.52 ? 1301 FAD   A O4B   1 
HETATM 17986 C  C3B   . FAD   C  2  .    ? -36.551 47.861  84.706  1.00 20.45 ? 1301 FAD   A C3B   1 
HETATM 17987 O  O3B   . FAD   C  2  .    ? -36.750 48.687  83.612  1.00 19.36 ? 1301 FAD   A O3B   1 
HETATM 17988 C  C2B   . FAD   C  2  .    ? -37.052 48.468  85.962  1.00 19.04 ? 1301 FAD   A C2B   1 
HETATM 17989 O  O2B   . FAD   C  2  .    ? -38.281 49.085  85.810  1.00 18.66 ? 1301 FAD   A O2B   1 
HETATM 17990 C  C1B   . FAD   C  2  .    ? -37.225 47.261  86.822  1.00 19.79 ? 1301 FAD   A C1B   1 
HETATM 17991 N  N9A   . FAD   C  2  .    ? -36.131 46.995  87.722  1.00 21.22 ? 1301 FAD   A N9A   1 
HETATM 17992 C  C8A   . FAD   C  2  .    ? -34.831 46.645  87.384  1.00 21.92 ? 1301 FAD   A C8A   1 
HETATM 17993 N  N7A   . FAD   C  2  .    ? -34.119 46.476  88.505  1.00 21.41 ? 1301 FAD   A N7A   1 
HETATM 17994 C  C5A   . FAD   C  2  .    ? -34.926 46.696  89.610  1.00 20.80 ? 1301 FAD   A C5A   1 
HETATM 17995 C  C6A   . FAD   C  2  .    ? -34.738 46.650  90.978  1.00 20.32 ? 1301 FAD   A C6A   1 
HETATM 17996 N  N6A   . FAD   C  2  .    ? -33.468 46.310  91.560  1.00 21.65 ? 1301 FAD   A N6A   1 
HETATM 17997 N  N1A   . FAD   C  2  .    ? -35.766 46.925  91.794  1.00 20.37 ? 1301 FAD   A N1A   1 
HETATM 17998 C  C2A   . FAD   C  2  .    ? -36.988 47.239  91.307  1.00 19.14 ? 1301 FAD   A C2A   1 
HETATM 17999 N  N3A   . FAD   C  2  .    ? -37.208 47.285  89.975  1.00 19.19 ? 1301 FAD   A N3A   1 
HETATM 18000 C  C4A   . FAD   C  2  .    ? -36.212 47.024  89.121  1.00 20.86 ? 1301 FAD   A C4A   1 
HETATM 18001 N  N1    . FAD   C  2  .    ? -40.924 53.623  81.361  1.00 17.71 ? 1301 FAD   A N1    1 
HETATM 18002 C  C2    . FAD   C  2  .    ? -41.231 54.854  81.994  1.00 17.25 ? 1301 FAD   A C2    1 
HETATM 18003 O  O2    . FAD   C  2  .    ? -40.690 55.144  83.168  1.00 16.42 ? 1301 FAD   A O2    1 
HETATM 18004 N  N3    . FAD   C  2  .    ? -42.097 55.757  81.424  1.00 16.70 ? 1301 FAD   A N3    1 
HETATM 18005 C  C4    . FAD   C  2  .    ? -42.670 55.503  80.211  1.00 17.65 ? 1301 FAD   A C4    1 
HETATM 18006 O  O4    . FAD   C  2  .    ? -43.532 56.412  79.704  1.00 18.03 ? 1301 FAD   A O4    1 
HETATM 18007 C  C4X   . FAD   C  2  .    ? -42.411 54.228  79.504  1.00 17.30 ? 1301 FAD   A C4X   1 
HETATM 18008 N  N5    . FAD   C  2  .    ? -43.016 53.911  78.294  1.00 18.19 ? 1301 FAD   A N5    1 
HETATM 18009 C  C5X   . FAD   C  2  .    ? -42.741 52.675  77.723  1.00 17.92 ? 1301 FAD   A C5X   1 
HETATM 18010 C  C6    . FAD   C  2  .    ? -43.321 52.307  76.504  1.00 17.53 ? 1301 FAD   A C6    1 
HETATM 18011 C  C7    . FAD   C  2  .    ? -43.041 51.061  75.960  1.00 18.51 ? 1301 FAD   A C7    1 
HETATM 18012 C  C7M   . FAD   C  2  .    ? -43.675 50.670  74.658  1.00 19.11 ? 1301 FAD   A C7M   1 
HETATM 18013 C  C8    . FAD   C  2  .    ? -42.176 50.175  76.583  1.00 19.77 ? 1301 FAD   A C8    1 
HETATM 18014 C  C8M   . FAD   C  2  .    ? -41.879 48.837  75.981  1.00 18.83 ? 1301 FAD   A C8M   1 
HETATM 18015 C  C9    . FAD   C  2  .    ? -41.585 50.525  77.791  1.00 19.53 ? 1301 FAD   A C9    1 
HETATM 18016 C  C9A   . FAD   C  2  .    ? -41.872 51.770  78.342  1.00 22.14 ? 1301 FAD   A C9A   1 
HETATM 18017 N  N10   . FAD   C  2  .    ? -41.241 52.091  79.557  1.00 21.96 ? 1301 FAD   A N10   1 
HETATM 18018 C  C10   . FAD   C  2  .    ? -41.512 53.313  80.165  1.00 17.95 ? 1301 FAD   A C10   1 
HETATM 18019 C  "C1'" . FAD   C  2  .    ? -40.423 51.075  80.251  1.00 27.10 ? 1301 FAD   A "C1'" 1 
HETATM 18020 C  "C2'" . FAD   C  2  .    ? -38.959 51.233  80.449  1.00 27.75 ? 1301 FAD   A "C2'" 1 
HETATM 18021 O  "O2'" . FAD   C  2  .    ? -38.481 52.073  79.482  1.00 28.73 ? 1301 FAD   A "O2'" 1 
HETATM 18022 C  "C3'" . FAD   C  2  .    ? -38.452 49.787  80.315  1.00 24.68 ? 1301 FAD   A "C3'" 1 
HETATM 18023 O  "O3'" . FAD   C  2  .    ? -38.620 49.409  79.008  1.00 27.63 ? 1301 FAD   A "O3'" 1 
HETATM 18024 C  "C4'" . FAD   C  2  .    ? -39.203 48.742  81.117  1.00 23.04 ? 1301 FAD   A "C4'" 1 
HETATM 18025 O  "O4'" . FAD   C  2  .    ? -39.271 49.090  82.446  1.00 23.60 ? 1301 FAD   A "O4'" 1 
HETATM 18026 C  "C5'" . FAD   C  2  .    ? -38.519 47.389  80.924  1.00 23.07 ? 1301 FAD   A "C5'" 1 
HETATM 18027 O  "O5'" . FAD   C  2  .    ? -39.316 46.385  81.500  1.00 24.53 ? 1301 FAD   A "O5'" 1 
HETATM 18028 P  P     . FAD   C  2  .    ? -39.556 45.036  80.678  1.00 21.65 ? 1301 FAD   A P     1 
HETATM 18029 O  O1P   . FAD   C  2  .    ? -39.631 45.168  79.117  1.00 22.37 ? 1301 FAD   A O1P   1 
HETATM 18030 O  O2P   . FAD   C  2  .    ? -40.778 44.449  81.450  1.00 25.09 ? 1301 FAD   A O2P   1 
HETATM 18031 O  O3P   . FAD   C  2  .    ? -38.343 44.072  81.184  1.00 21.86 ? 1301 FAD   A O3P   1 
HETATM 18032 C  C1    . PEG   D  3  .    ? -0.218  62.946  96.677  1.00 28.44 ? 1302 PEG   A C1    1 
HETATM 18033 O  O1    . PEG   D  3  .    ? -1.188  61.959  96.393  1.00 34.40 ? 1302 PEG   A O1    1 
HETATM 18034 C  C2    . PEG   D  3  .    ? 1.091   62.618  95.999  1.00 36.12 ? 1302 PEG   A C2    1 
HETATM 18035 O  O2    . PEG   D  3  .    ? 1.648   61.460  96.561  1.00 42.15 ? 1302 PEG   A O2    1 
HETATM 18036 C  C3    . PEG   D  3  .    ? 2.486   60.752  95.677  1.00 41.87 ? 1302 PEG   A C3    1 
HETATM 18037 C  C4    . PEG   D  3  .    ? 2.456   59.282  96.019  1.00 39.94 ? 1302 PEG   A C4    1 
HETATM 18038 O  O4    . PEG   D  3  .    ? 2.355   58.502  94.847  1.00 44.01 ? 1302 PEG   A O4    1 
HETATM 18039 C  C     . FMT   E  4  .    ? -40.270 61.449  102.594 0.68 21.32 ? 1303 FMT   A C     1 
HETATM 18040 O  O1    . FMT   E  4  .    ? -39.448 61.060  103.437 0.68 27.84 ? 1303 FMT   A O1    1 
HETATM 18041 O  O2    . FMT   E  4  .    ? -41.511 61.588  102.705 0.68 28.89 ? 1303 FMT   A O2    1 
HETATM 18042 C  C4    . A1AQC F  5  .    ? -40.570 56.900  78.122  0.79 21.93 ? 1304 A1AQC A C4    1 
HETATM 18043 C  C5    . A1AQC F  5  .    ? -40.071 58.218  79.998  0.79 20.44 ? 1304 A1AQC A C5    1 
HETATM 18044 C  C6    . A1AQC F  5  .    ? -39.061 57.127  79.879  0.79 22.63 ? 1304 A1AQC A C6    1 
HETATM 18045 C  C7    . A1AQC F  5  .    ? -39.485 56.297  78.721  0.79 23.03 ? 1304 A1AQC A C7    1 
HETATM 18046 C  C8    . A1AQC F  5  .    ? -38.980 55.086  78.192  0.79 25.41 ? 1304 A1AQC A C8    1 
HETATM 18047 C  C     . A1AQC F  5  .    ? -39.058 53.211  76.487  0.79 27.67 ? 1304 A1AQC A C     1 
HETATM 18048 O  O     . A1AQC F  5  .    ? -37.670 53.344  76.389  0.79 30.13 ? 1304 A1AQC A O     1 
HETATM 18049 C  C1    . A1AQC F  5  .    ? -39.586 54.514  77.075  0.79 25.09 ? 1304 A1AQC A C1    1 
HETATM 18050 C  C2    . A1AQC F  5  .    ? -40.682 55.134  76.475  0.79 23.36 ? 1304 A1AQC A C2    1 
HETATM 18051 C  C3    . A1AQC F  5  .    ? -41.176 56.320  76.992  0.79 22.77 ? 1304 A1AQC A C3    1 
HETATM 18052 O  O1    . A1AQC F  5  .    ? -40.908 58.134  78.844  0.79 21.32 ? 1304 A1AQC A O1    1 
HETATM 18053 C  C     . FMT   G  4  .    ? 9.168   68.592  114.609 0.62 22.97 ? 1305 FMT   A C     1 
HETATM 18054 O  O1    . FMT   G  4  .    ? 10.368  68.374  114.357 0.62 27.55 ? 1305 FMT   A O1    1 
HETATM 18055 O  O2    . FMT   G  4  .    ? 8.180   67.854  114.449 0.62 27.89 ? 1305 FMT   A O2    1 
HETATM 18056 C  C     . FMT   H  4  .    ? 5.529   71.213  95.736  0.67 28.67 ? 1306 FMT   A C     1 
HETATM 18057 O  O1    . FMT   H  4  .    ? 6.555   70.552  95.979  0.67 31.01 ? 1306 FMT   A O1    1 
HETATM 18058 O  O2    . FMT   H  4  .    ? 4.657   71.607  96.531  0.67 31.90 ? 1306 FMT   A O2    1 
HETATM 18059 P  PA    . NAD   I  6  .    ? -18.002 88.416  107.108 1.00 23.05 ? 1307 NAD   A PA    1 
HETATM 18060 O  O1A   . NAD   I  6  .    ? -16.474 88.395  106.852 1.00 22.29 ? 1307 NAD   A O1A   1 
HETATM 18061 O  O2A   . NAD   I  6  .    ? -18.757 89.591  106.722 1.00 23.46 ? 1307 NAD   A O2A   1 
HETATM 18062 O  O5B   . NAD   I  6  .    ? -18.460 88.183  108.500 1.00 22.81 ? 1307 NAD   A O5B   1 
HETATM 18063 C  C5B   . NAD   I  6  .    ? -18.175 86.961  109.144 1.00 22.17 ? 1307 NAD   A C5B   1 
HETATM 18064 C  C4B   . NAD   I  6  .    ? -18.164 87.040  110.672 1.00 21.06 ? 1307 NAD   A C4B   1 
HETATM 18065 O  O4B   . NAD   I  6  .    ? -17.043 87.754  111.154 1.00 22.19 ? 1307 NAD   A O4B   1 
HETATM 18066 C  C3B   . NAD   I  6  .    ? -19.390 87.652  111.280 1.00 20.75 ? 1307 NAD   A C3B   1 
HETATM 18067 O  O3B   . NAD   I  6  .    ? -19.786 86.959  112.409 1.00 22.27 ? 1307 NAD   A O3B   1 
HETATM 18068 C  C2B   . NAD   I  6  .    ? -18.949 89.022  111.582 1.00 23.15 ? 1307 NAD   A C2B   1 
HETATM 18069 O  O2B   . NAD   I  6  .    ? -19.697 89.590  112.600 1.00 24.24 ? 1307 NAD   A O2B   1 
HETATM 18070 C  C1B   . NAD   I  6  .    ? -17.549 88.768  111.990 1.00 24.35 ? 1307 NAD   A C1B   1 
HETATM 18071 N  N9A   . NAD   I  6  .    ? -16.667 89.905  111.903 1.00 21.37 ? 1307 NAD   A N9A   1 
HETATM 18072 C  C8A   . NAD   I  6  .    ? -16.722 90.998  111.059 1.00 25.17 ? 1307 NAD   A C8A   1 
HETATM 18073 N  N7A   . NAD   I  6  .    ? -15.673 91.788  111.303 1.00 24.27 ? 1307 NAD   A N7A   1 
HETATM 18074 C  C5A   . NAD   I  6  .    ? -14.896 91.240  112.307 1.00 23.31 ? 1307 NAD   A C5A   1 
HETATM 18075 C  C6A   . NAD   I  6  .    ? -13.731 91.600  112.949 1.00 24.81 ? 1307 NAD   A C6A   1 
HETATM 18076 N  N6A   . NAD   I  6  .    ? -13.055 92.812  112.599 1.00 26.48 ? 1307 NAD   A N6A   1 
HETATM 18077 N  N1A   . NAD   I  6  .    ? -13.235 90.815  113.904 1.00 23.90 ? 1307 NAD   A N1A   1 
HETATM 18078 C  C2A   . NAD   I  6  .    ? -13.822 89.656  114.277 1.00 24.58 ? 1307 NAD   A C2A   1 
HETATM 18079 N  N3A   . NAD   I  6  .    ? -14.974 89.273  113.674 1.00 24.20 ? 1307 NAD   A N3A   1 
HETATM 18080 C  C4A   . NAD   I  6  .    ? -15.509 90.029  112.696 1.00 23.77 ? 1307 NAD   A C4A   1 
HETATM 18081 O  O3    . NAD   I  6  .    ? -18.738 87.331  106.356 1.00 20.82 ? 1307 NAD   A O3    1 
HETATM 18082 P  PN    . NAD   I  6  .    ? -20.274 87.045  105.992 1.00 23.33 ? 1307 NAD   A PN    1 
HETATM 18083 O  O1N   . NAD   I  6  .    ? -20.783 88.108  105.067 1.00 24.35 ? 1307 NAD   A O1N   1 
HETATM 18084 O  O2N   . NAD   I  6  .    ? -21.120 86.828  107.199 1.00 23.47 ? 1307 NAD   A O2N   1 
HETATM 18085 O  O5D   . NAD   I  6  .    ? -20.229 85.676  105.186 1.00 22.67 ? 1307 NAD   A O5D   1 
HETATM 18086 C  C5D   . NAD   I  6  .    ? -19.875 85.688  103.830 1.00 22.61 ? 1307 NAD   A C5D   1 
HETATM 18087 C  C4D   . NAD   I  6  .    ? -18.433 85.260  103.608 1.00 20.67 ? 1307 NAD   A C4D   1 
HETATM 18088 O  O4D   . NAD   I  6  .    ? -18.169 84.038  104.249 1.00 20.62 ? 1307 NAD   A O4D   1 
HETATM 18089 C  C3D   . NAD   I  6  .    ? -18.146 85.107  102.147 1.00 22.40 ? 1307 NAD   A C3D   1 
HETATM 18090 O  O3D   . NAD   I  6  .    ? -16.977 85.728  101.795 1.00 23.11 ? 1307 NAD   A O3D   1 
HETATM 18091 C  C2D   . NAD   I  6  .    ? -18.066 83.642  101.993 1.00 19.37 ? 1307 NAD   A C2D   1 
HETATM 18092 O  O2D   . NAD   I  6  .    ? -17.350 83.174  100.886 1.00 20.44 ? 1307 NAD   A O2D   1 
HETATM 18093 C  C1D   . NAD   I  6  .    ? -17.491 83.249  103.303 1.00 20.88 ? 1307 NAD   A C1D   1 
HETATM 18094 N  N1N   . NAD   I  6  .    ? -17.766 81.874  103.587 1.00 19.34 ? 1307 NAD   A N1N   1 
HETATM 18095 C  C2N   . NAD   I  6  .    ? -16.746 80.887  103.524 1.00 20.87 ? 1307 NAD   A C2N   1 
HETATM 18096 C  C3N   . NAD   I  6  .    ? -17.100 79.571  103.801 1.00 20.64 ? 1307 NAD   A C3N   1 
HETATM 18097 C  C7N   . NAD   I  6  .    ? -16.110 78.462  103.748 1.00 18.83 ? 1307 NAD   A C7N   1 
HETATM 18098 O  O7N   . NAD   I  6  .    ? -16.428 77.349  104.150 1.00 22.39 ? 1307 NAD   A O7N   1 
HETATM 18099 N  N7N   . NAD   I  6  .    ? -14.831 78.722  103.191 1.00 18.52 ? 1307 NAD   A N7N   1 
HETATM 18100 C  C4N   . NAD   I  6  .    ? -18.430 79.259  104.150 1.00 29.73 ? 1307 NAD   A C4N   1 
HETATM 18101 C  C5N   . NAD   I  6  .    ? -19.437 80.241  104.178 1.00 23.36 ? 1307 NAD   A C5N   1 
HETATM 18102 C  C6N   . NAD   I  6  .    ? -19.095 81.549  103.901 1.00 19.64 ? 1307 NAD   A C6N   1 
HETATM 18103 S  S     . SO4   J  7  .    ? -9.061  52.962  110.951 1.00 20.12 ? 1308 SO4   A S     1 
HETATM 18104 O  O1    . SO4   J  7  .    ? -7.988  53.201  109.949 1.00 21.93 ? 1308 SO4   A O1    1 
HETATM 18105 O  O2    . SO4   J  7  .    ? -10.130 52.117  110.350 1.00 25.21 ? 1308 SO4   A O2    1 
HETATM 18106 O  O3    . SO4   J  7  .    ? -8.488  52.243  112.132 1.00 20.39 ? 1308 SO4   A O3    1 
HETATM 18107 O  O4    . SO4   J  7  .    ? -9.543  54.325  111.345 1.00 23.45 ? 1308 SO4   A O4    1 
HETATM 18108 S  S     . SO4   K  7  .    ? 12.920  75.477  125.706 0.76 37.90 ? 1309 SO4   A S     1 
HETATM 18109 O  O1    . SO4   K  7  .    ? 13.691  75.931  124.501 0.76 40.14 ? 1309 SO4   A O1    1 
HETATM 18110 O  O2    . SO4   K  7  .    ? 11.634  74.827  125.301 0.76 35.00 ? 1309 SO4   A O2    1 
HETATM 18111 O  O3    . SO4   K  7  .    ? 13.765  74.490  126.457 0.76 41.53 ? 1309 SO4   A O3    1 
HETATM 18112 O  O4    . SO4   K  7  .    ? 12.604  76.658  126.576 0.76 47.10 ? 1309 SO4   A O4    1 
HETATM 18113 S  S     . SO4   L  7  .    ? 29.511  71.134  105.635 0.87 41.18 ? 1310 SO4   A S     1 
HETATM 18114 O  O1    . SO4   L  7  .    ? 29.584  70.769  104.184 0.87 46.77 ? 1310 SO4   A O1    1 
HETATM 18115 O  O2    . SO4   L  7  .    ? 28.099  71.463  106.012 0.87 48.08 ? 1310 SO4   A O2    1 
HETATM 18116 O  O3    . SO4   L  7  .    ? 30.013  69.986  106.454 0.87 45.60 ? 1310 SO4   A O3    1 
HETATM 18117 O  O4    . SO4   L  7  .    ? 30.374  72.336  105.888 0.87 41.35 ? 1310 SO4   A O4    1 
HETATM 18118 S  S     . SO4   M  7  .    ? -34.031 24.899  79.544  0.75 42.95 ? 1311 SO4   A S     1 
HETATM 18119 O  O1    . SO4   M  7  .    ? -33.206 26.013  78.972  0.75 40.95 ? 1311 SO4   A O1    1 
HETATM 18120 O  O2    . SO4   M  7  .    ? -34.999 24.419  78.509  0.75 40.98 ? 1311 SO4   A O2    1 
HETATM 18121 O  O3    . SO4   M  7  .    ? -33.118 23.772  79.920  0.75 52.44 ? 1311 SO4   A O3    1 
HETATM 18122 O  O4    . SO4   M  7  .    ? -34.756 25.358  80.775  0.75 40.11 ? 1311 SO4   A O4    1 
HETATM 18123 S  S     . SO4   N  7  .    ? -12.188 75.329  70.129  0.61 33.58 ? 1312 SO4   A S     1 
HETATM 18124 O  O1    . SO4   N  7  .    ? -11.043 75.143  71.067  0.61 31.43 ? 1312 SO4   A O1    1 
HETATM 18125 O  O2    . SO4   N  7  .    ? -12.145 76.727  69.588  0.61 39.06 ? 1312 SO4   A O2    1 
HETATM 18126 O  O3    . SO4   N  7  .    ? -12.044 74.352  69.001  0.61 40.35 ? 1312 SO4   A O3    1 
HETATM 18127 O  O4    . SO4   N  7  .    ? -13.495 75.093  70.827  0.61 26.44 ? 1312 SO4   A O4    1 
HETATM 18128 MG MG    . MG    O  8  .    ? -19.789 91.397  106.972 1.00 27.68 ? 1313 MG    A MG    1 
HETATM 18129 P  PA    . FAD   P  2  .    ? -16.908 23.329  104.044 1.00 21.24 ? 1301 FAD   B PA    1 
HETATM 18130 O  O1A   . FAD   P  2  .    ? -17.120 24.849  104.110 1.00 25.78 ? 1301 FAD   B O1A   1 
HETATM 18131 O  O2A   . FAD   P  2  .    ? -18.038 22.451  103.834 1.00 23.27 ? 1301 FAD   B O2A   1 
HETATM 18132 O  O5B   . FAD   P  2  .    ? -16.031 22.879  102.900 1.00 21.67 ? 1301 FAD   B O5B   1 
HETATM 18133 C  C5B   . FAD   P  2  .    ? -14.948 23.724  102.541 1.00 20.90 ? 1301 FAD   B C5B   1 
HETATM 18134 C  C4B   . FAD   P  2  .    ? -13.991 22.990  101.604 1.00 19.41 ? 1301 FAD   B C4B   1 
HETATM 18135 O  O4B   . FAD   P  2  .    ? -14.500 22.938  100.305 1.00 19.92 ? 1301 FAD   B O4B   1 
HETATM 18136 C  C3B   . FAD   P  2  .    ? -12.640 23.617  101.460 1.00 17.65 ? 1301 FAD   B C3B   1 
HETATM 18137 O  O3B   . FAD   P  2  .    ? -11.781 23.385  102.533 1.00 17.77 ? 1301 FAD   B O3B   1 
HETATM 18138 C  C2B   . FAD   P  2  .    ? -12.159 22.986  100.201 1.00 18.26 ? 1301 FAD   B C2B   1 
HETATM 18139 O  O2B   . FAD   P  2  .    ? -11.724 21.695  100.391 1.00 18.33 ? 1301 FAD   B O2B   1 
HETATM 18140 C  C1B   . FAD   P  2  .    ? -13.414 22.922  99.411  1.00 18.58 ? 1301 FAD   B C1B   1 
HETATM 18141 N  N9A   . FAD   P  2  .    ? -13.615 24.004  98.484  1.00 18.92 ? 1301 FAD   B N9A   1 
HETATM 18142 C  C8A   . FAD   P  2  .    ? -13.725 25.358  98.723  1.00 21.93 ? 1301 FAD   B C8A   1 
HETATM 18143 N  N7A   . FAD   P  2  .    ? -13.916 26.021  97.576  1.00 20.39 ? 1301 FAD   B N7A   1 
HETATM 18144 C  C5A   . FAD   P  2  .    ? -13.938 25.104  96.536  1.00 17.52 ? 1301 FAD   B C5A   1 
HETATM 18145 C  C6A   . FAD   P  2  .    ? -14.102 25.183  95.165  1.00 18.42 ? 1301 FAD   B C6A   1 
HETATM 18146 N  N6A   . FAD   P  2  .    ? -14.319 26.444  94.515  1.00 20.39 ? 1301 FAD   B N6A   1 
HETATM 18147 N  N1A   . FAD   P  2  .    ? -14.061 24.058  94.446  1.00 17.19 ? 1301 FAD   B N1A   1 
HETATM 18148 C  C2A   . FAD   P  2  .    ? -13.892 22.845  95.001  1.00 15.88 ? 1301 FAD   B C2A   1 
HETATM 18149 N  N3A   . FAD   P  2  .    ? -13.720 22.730  96.345  1.00 16.77 ? 1301 FAD   B N3A   1 
HETATM 18150 C  C4A   . FAD   P  2  .    ? -13.736 23.821  97.103  1.00 17.16 ? 1301 FAD   B C4A   1 
HETATM 18151 N  N1    . FAD   P  2  .    ? -7.369  18.618  104.834 1.00 18.23 ? 1301 FAD   B N1    1 
HETATM 18152 C  C2    . FAD   P  2  .    ? -6.208  18.113  104.198 1.00 17.54 ? 1301 FAD   B C2    1 
HETATM 18153 O  O2    . FAD   P  2  .    ? -5.943  18.578  102.982 1.00 17.06 ? 1301 FAD   B O2    1 
HETATM 18154 N  N3    . FAD   P  2  .    ? -5.397  17.177  104.779 1.00 17.78 ? 1301 FAD   B N3    1 
HETATM 18155 C  C4    . FAD   P  2  .    ? -5.654  16.705  106.034 1.00 16.41 ? 1301 FAD   B C4    1 
HETATM 18156 O  O4    . FAD   P  2  .    ? -4.857  15.761  106.571 1.00 17.38 ? 1301 FAD   B O4    1 
HETATM 18157 C  C4X   . FAD   P  2  .    ? -6.843  17.212  106.763 1.00 19.04 ? 1301 FAD   B C4X   1 
HETATM 18158 N  N5    . FAD   P  2  .    ? -7.173  16.765  108.033 1.00 18.91 ? 1301 FAD   B N5    1 
HETATM 18159 C  C5X   . FAD   P  2  .    ? -8.314  17.262  108.643 1.00 17.94 ? 1301 FAD   B C5X   1 
HETATM 18160 C  C6    . FAD   P  2  .    ? -8.646  16.803  109.928 1.00 18.43 ? 1301 FAD   B C6    1 
HETATM 18161 C  C7    . FAD   P  2  .    ? -9.794  17.294  110.533 1.00 20.62 ? 1301 FAD   B C7    1 
HETATM 18162 C  C7M   . FAD   P  2  .    ? -10.173 16.810  111.907 1.00 21.87 ? 1301 FAD   B C7M   1 
HETATM 18163 C  C8    . FAD   P  2  .    ? -10.602 18.207  109.893 1.00 19.40 ? 1301 FAD   B C8    1 
HETATM 18164 C  C8M   . FAD   P  2  .    ? -11.843 18.742  110.533 1.00 19.22 ? 1301 FAD   B C8M   1 
HETATM 18165 C  C9    . FAD   P  2  .    ? -10.277 18.663  108.625 1.00 20.20 ? 1301 FAD   B C9    1 
HETATM 18166 C  C9A   . FAD   P  2  .    ? -9.140  18.188  108.008 1.00 19.63 ? 1301 FAD   B C9A   1 
HETATM 18167 N  N10   . FAD   P  2  .    ? -8.808  18.671  106.710 1.00 20.62 ? 1301 FAD   B N10   1 
HETATM 18168 C  C10   . FAD   P  2  .    ? -7.675  18.168  106.086 1.00 19.91 ? 1301 FAD   B C10   1 
HETATM 18169 C  "C1'" . FAD   P  2  .    ? -9.729  19.582  105.980 1.00 24.05 ? 1301 FAD   B "C1'" 1 
HETATM 18170 C  "C2'" . FAD   P  2  .    ? -9.422  21.034  105.779 1.00 25.19 ? 1301 FAD   B "C2'" 1 
HETATM 18171 O  "O2'" . FAD   P  2  .    ? -8.513  21.420  106.725 1.00 25.21 ? 1301 FAD   B "O2'" 1 
HETATM 18172 C  "C3'" . FAD   P  2  .    ? -10.748 21.791  105.932 1.00 26.48 ? 1301 FAD   B "C3'" 1 
HETATM 18173 O  "O3'" . FAD   P  2  .    ? -11.123 21.793  107.254 1.00 26.75 ? 1301 FAD   B "O3'" 1 
HETATM 18174 C  "C4'" . FAD   P  2  .    ? -11.910 21.186  105.179 1.00 25.11 ? 1301 FAD   B "C4'" 1 
HETATM 18175 O  "O4'" . FAD   P  2  .    ? -11.596 21.096  103.834 1.00 24.64 ? 1301 FAD   B "O4'" 1 
HETATM 18176 C  "C5'" . FAD   P  2  .    ? -13.160 22.028  105.441 1.00 21.91 ? 1301 FAD   B "C5'" 1 
HETATM 18177 O  "O5'" . FAD   P  2  .    ? -14.268 21.274  105.019 1.00 20.59 ? 1301 FAD   B "O5'" 1 
HETATM 18178 P  P     . FAD   P  2  .    ? -15.720 21.303  105.705 1.00 21.93 ? 1301 FAD   B P     1 
HETATM 18179 O  O1P   . FAD   P  2  .    ? -16.571 20.028  105.399 1.00 25.63 ? 1301 FAD   B O1P   1 
HETATM 18180 O  O2P   . FAD   P  2  .    ? -15.387 21.613  107.213 1.00 23.51 ? 1301 FAD   B O2P   1 
HETATM 18181 O  O3P   . FAD   P  2  .    ? -16.255 22.772  105.276 1.00 24.41 ? 1301 FAD   B O3P   1 
HETATM 18182 O  OH2   . 1PE   Q  9  .    ? 42.453  35.059  84.301  1.00 29.00 ? 1302 1PE   B OH2   1 
HETATM 18183 C  C12   . 1PE   Q  9  .    ? 42.352  33.889  83.522  1.00 30.22 ? 1302 1PE   B C12   1 
HETATM 18184 C  C22   . 1PE   Q  9  .    ? 41.425  34.097  82.352  1.00 37.69 ? 1302 1PE   B C22   1 
HETATM 18185 O  OH3   . 1PE   Q  9  .    ? 40.191  34.652  82.743  1.00 39.55 ? 1302 1PE   B OH3   1 
HETATM 18186 C  C13   . 1PE   Q  9  .    ? 38.063  35.463  81.985  1.00 37.77 ? 1302 1PE   B C13   1 
HETATM 18187 C  C23   . 1PE   Q  9  .    ? 39.494  35.154  81.628  1.00 38.06 ? 1302 1PE   B C23   1 
HETATM 18188 O  OH4   . 1PE   Q  9  .    ? 38.019  36.418  83.013  1.00 42.74 ? 1302 1PE   B OH4   1 
HETATM 18189 C  C14   . 1PE   Q  9  .    ? 36.639  38.044  84.093  1.00 37.18 ? 1302 1PE   B C14   1 
HETATM 18190 C  C24   . 1PE   Q  9  .    ? 37.033  37.397  82.792  1.00 39.49 ? 1302 1PE   B C24   1 
HETATM 18191 O  OH5   . 1PE   Q  9  .    ? 37.774  38.407  84.840  1.00 37.61 ? 1302 1PE   B OH5   1 
HETATM 18192 C  C15   . 1PE   Q  9  .    ? 39.042  40.178  85.849  1.00 36.37 ? 1302 1PE   B C15   1 
HETATM 18193 C  C25   . 1PE   Q  9  .    ? 37.954  39.805  84.880  1.00 36.22 ? 1302 1PE   B C25   1 
HETATM 18194 O  OH6   . 1PE   Q  9  .    ? 40.262  39.583  85.480  1.00 37.02 ? 1302 1PE   B OH6   1 
HETATM 18195 C  C16   . 1PE   Q  9  .    ? 42.413  39.479  86.509  1.00 32.73 ? 1302 1PE   B C16   1 
HETATM 18196 C  C26   . 1PE   Q  9  .    ? 41.371  40.355  85.870  1.00 33.68 ? 1302 1PE   B C26   1 
HETATM 18197 O  OH7   . 1PE   Q  9  .    ? 42.427  38.230  85.851  1.00 33.38 ? 1302 1PE   B OH7   1 
HETATM 18198 C  C1    . PGE   R  10 .    ? 1.164   59.765  86.083  1.00 34.08 ? 1303 PGE   B C1    1 
HETATM 18199 O  O1    . PGE   R  10 .    ? 0.347   59.757  87.236  1.00 39.25 ? 1303 PGE   B O1    1 
HETATM 18200 C  C2    . PGE   R  10 .    ? 2.569   60.176  86.448  1.00 35.82 ? 1303 PGE   B C2    1 
HETATM 18201 O  O2    . PGE   R  10 .    ? 3.396   59.040  86.569  1.00 39.85 ? 1303 PGE   B O2    1 
HETATM 18202 C  C3    . PGE   R  10 .    ? 3.959   58.545  85.375  1.00 30.11 ? 1303 PGE   B C3    1 
HETATM 18203 C  C4    . PGE   R  10 .    ? 4.538   57.153  85.512  1.00 30.04 ? 1303 PGE   B C4    1 
HETATM 18204 O  O4    . PGE   R  10 .    ? 2.013   54.606  87.325  1.00 41.43 ? 1303 PGE   B O4    1 
HETATM 18205 C  C6    . PGE   R  10 .    ? 3.349   54.189  87.149  1.00 37.71 ? 1303 PGE   B C6    1 
HETATM 18206 C  C5    . PGE   R  10 .    ? 3.929   54.934  85.959  1.00 34.23 ? 1303 PGE   B C5    1 
HETATM 18207 O  O3    . PGE   R  10 .    ? 3.587   56.290  86.076  1.00 35.10 ? 1303 PGE   B O3    1 
HETATM 18208 C  C     . FMT   S  4  .    ? -0.826  16.785  83.192  0.80 16.70 ? 1304 FMT   B C     1 
HETATM 18209 O  O1    . FMT   S  4  .    ? -1.079  15.564  83.300  0.80 31.20 ? 1304 FMT   B O1    1 
HETATM 18210 O  O2    . FMT   S  4  .    ? -1.118  17.557  82.288  0.80 24.41 ? 1304 FMT   B O2    1 
HETATM 18211 C  C1    . PEG   T  3  .    ? 15.647  66.945  54.520  1.00 40.33 ? 1305 PEG   B C1    1 
HETATM 18212 O  O1    . PEG   T  3  .    ? 16.324  67.276  55.713  1.00 31.34 ? 1305 PEG   B O1    1 
HETATM 18213 C  C2    . PEG   T  3  .    ? 15.066  65.563  54.636  1.00 41.37 ? 1305 PEG   B C2    1 
HETATM 18214 O  O2    . PEG   T  3  .    ? 14.800  65.000  53.381  1.00 44.73 ? 1305 PEG   B O2    1 
HETATM 18215 C  C3    . PEG   T  3  .    ? 15.454  63.763  53.220  1.00 44.63 ? 1305 PEG   B C3    1 
HETATM 18216 C  C4    . PEG   T  3  .    ? 14.987  62.792  54.272  1.00 38.70 ? 1305 PEG   B C4    1 
HETATM 18217 O  O4    . PEG   T  3  .    ? 15.879  61.708  54.341  1.00 43.02 ? 1305 PEG   B O4    1 
HETATM 18218 C  C1    . PEG   U  3  .    ? 13.423  33.515  78.401  0.69 26.47 ? 1306 PEG   B C1    1 
HETATM 18219 O  O1    . PEG   U  3  .    ? 13.531  34.839  78.868  0.69 27.18 ? 1306 PEG   B O1    1 
HETATM 18220 C  C2    . PEG   U  3  .    ? 13.349  32.551  79.556  0.69 25.01 ? 1306 PEG   B C2    1 
HETATM 18221 O  O2    . PEG   U  3  .    ? 13.079  31.269  79.038  0.69 28.51 ? 1306 PEG   B O2    1 
HETATM 18222 C  C3    . PEG   U  3  .    ? 13.411  30.196  79.884  0.69 24.19 ? 1306 PEG   B C3    1 
HETATM 18223 C  C4    . PEG   U  3  .    ? 12.215  29.747  80.688  0.69 27.86 ? 1306 PEG   B C4    1 
HETATM 18224 O  O4    . PEG   U  3  .    ? 11.699  30.822  81.446  0.69 33.63 ? 1306 PEG   B O4    1 
HETATM 18225 C  C1    . PEG   V  3  .    ? -5.557  31.574  67.815  1.00 38.59 ? 1307 PEG   B C1    1 
HETATM 18226 O  O1    . PEG   V  3  .    ? -6.211  32.693  67.253  1.00 43.38 ? 1307 PEG   B O1    1 
HETATM 18227 C  C2    . PEG   V  3  .    ? -5.458  31.737  69.311  1.00 34.18 ? 1307 PEG   B C2    1 
HETATM 18228 O  O2    . PEG   V  3  .    ? -6.715  31.546  69.919  1.00 40.31 ? 1307 PEG   B O2    1 
HETATM 18229 C  C3    . PEG   V  3  .    ? -6.712  30.541  70.902  1.00 35.96 ? 1307 PEG   B C3    1 
HETATM 18230 C  C4    . PEG   V  3  .    ? -7.604  30.939  72.054  1.00 32.47 ? 1307 PEG   B C4    1 
HETATM 18231 O  O4    . PEG   V  3  .    ? -8.946  30.633  71.741  1.00 40.01 ? 1307 PEG   B O4    1 
HETATM 18232 C  C     . FMT   W  4  .    ? 11.181  49.384  77.837  0.52 15.05 ? 1308 FMT   B C     1 
HETATM 18233 O  O1    . FMT   W  4  .    ? 11.310  49.269  76.598  0.52 22.20 ? 1308 FMT   B O1    1 
HETATM 18234 O  O2    . FMT   W  4  .    ? 12.031  49.588  78.735  0.52 22.60 ? 1308 FMT   B O2    1 
HETATM 18235 C  C     . FMT   X  4  .    ? -30.278 7.502   111.651 1.00 44.99 ? 1309 FMT   B C     1 
HETATM 18236 O  O1    . FMT   X  4  .    ? -30.895 7.602   112.729 1.00 47.67 ? 1309 FMT   B O1    1 
HETATM 18237 O  O2    . FMT   X  4  .    ? -30.677 7.020   110.574 1.00 47.10 ? 1309 FMT   B O2    1 
HETATM 18238 C  C4    . A1AQC Y  5  .    ? -3.839  18.719  107.945 0.88 21.63 ? 1310 A1AQC B C4    1 
HETATM 18239 C  C5    . A1AQC Y  5  .    ? -2.524  18.954  106.014 0.88 20.90 ? 1310 A1AQC B C5    1 
HETATM 18240 C  C6    . A1AQC Y  5  .    ? -3.553  20.031  106.045 0.88 22.47 ? 1310 A1AQC B C6    1 
HETATM 18241 C  C7    . A1AQC Y  5  .    ? -4.350  19.823  107.288 0.88 22.97 ? 1310 A1AQC B C7    1 
HETATM 18242 C  C8    . A1AQC Y  5  .    ? -5.441  20.529  107.849 0.88 24.07 ? 1310 A1AQC B C8    1 
HETATM 18243 C  C     . A1AQC Y  5  .    ? -7.182  20.831  109.685 0.88 27.70 ? 1310 A1AQC B C     1 
HETATM 18244 O  O     . A1AQC Y  5  .    ? -6.818  22.171  109.849 0.88 30.14 ? 1310 A1AQC B O     1 
HETATM 18245 C  C1    . A1AQC Y  5  .    ? -6.002  20.099  109.052 0.88 24.96 ? 1310 A1AQC B C1    1 
HETATM 18246 C  C2    . A1AQC Y  5  .    ? -5.482  18.980  109.702 0.88 23.39 ? 1310 A1AQC B C2    1 
HETATM 18247 C  C3    . A1AQC Y  5  .    ? -4.410  18.290  109.156 0.88 22.86 ? 1310 A1AQC B C3    1 
HETATM 18248 O  O1    . A1AQC Y  5  .    ? -2.722  18.154  107.184 0.88 23.04 ? 1310 A1AQC B O1    1 
HETATM 18249 C  C1    . PEG   Z  3  .    ? 18.675  65.087  54.634  0.84 40.82 ? 1311 PEG   B C1    1 
HETATM 18250 O  O1    . PEG   Z  3  .    ? 18.748  65.987  55.721  0.84 33.01 ? 1311 PEG   B O1    1 
HETATM 18251 C  C2    . PEG   Z  3  .    ? 18.755  63.654  55.101  0.84 30.19 ? 1311 PEG   B C2    1 
HETATM 18252 O  O2    . PEG   Z  3  .    ? 19.251  62.826  54.077  0.84 41.88 ? 1311 PEG   B O2    1 
HETATM 18253 C  C3    . PEG   Z  3  .    ? 20.658  62.775  54.045  0.84 28.90 ? 1311 PEG   B C3    1 
HETATM 18254 C  C4    . PEG   Z  3  .    ? 21.180  63.291  52.727  0.84 34.40 ? 1311 PEG   B C4    1 
HETATM 18255 O  O4    . PEG   Z  3  .    ? 22.587  63.357  52.774  0.84 40.67 ? 1311 PEG   B O4    1 
HETATM 18256 P  PA    . NAD   AA 6  .    ? 27.604  35.742  75.200  1.00 16.82 ? 1312 NAD   B PA    1 
HETATM 18257 O  O1A   . NAD   AA 6  .    ? 27.686  37.287  75.145  1.00 15.76 ? 1312 NAD   B O1A   1 
HETATM 18258 O  O2A   . NAD   AA 6  .    ? 28.812  34.996  75.510  1.00 18.97 ? 1312 NAD   B O2A   1 
HETATM 18259 O  O5B   . NAD   AA 6  .    ? 27.250  35.137  73.864  1.00 17.01 ? 1312 NAD   B O5B   1 
HETATM 18260 C  C5B   . NAD   AA 6  .    ? 25.992  35.432  73.299  1.00 18.33 ? 1312 NAD   B C5B   1 
HETATM 18261 C  C4B   . NAD   AA 6  .    ? 25.968  35.289  71.782  1.00 16.17 ? 1312 NAD   B C4B   1 
HETATM 18262 O  O4B   . NAD   AA 6  .    ? 26.741  36.301  71.159  1.00 15.07 ? 1312 NAD   B O4B   1 
HETATM 18263 C  C3B   . NAD   AA 6  .    ? 26.427  33.949  71.283  1.00 15.06 ? 1312 NAD   B C3B   1 
HETATM 18264 O  O3B   . NAD   AA 6  .    ? 25.662  33.530  70.188  1.00 15.21 ? 1312 NAD   B O3B   1 
HETATM 18265 C  C2B   . NAD   AA 6  .    ? 27.809  34.271  70.870  1.00 16.87 ? 1312 NAD   B C2B   1 
HETATM 18266 O  O2B   . NAD   AA 6  .    ? 28.353  33.433  69.915  1.00 15.91 ? 1312 NAD   B O2B   1 
HETATM 18267 C  C1B   . NAD   AA 6  .    ? 27.627  35.624  70.304  1.00 15.93 ? 1312 NAD   B C1B   1 
HETATM 18268 N  N9A   . NAD   AA 6  .    ? 28.845  36.390  70.185  1.00 16.79 ? 1312 NAD   B N9A   1 
HETATM 18269 C  C8A   . NAD   AA 6  .    ? 29.981  36.318  70.976  1.00 17.86 ? 1312 NAD   B C8A   1 
HETATM 18270 N  N7A   . NAD   AA 6  .    ? 30.857  37.247  70.562  1.00 20.08 ? 1312 NAD   B N7A   1 
HETATM 18271 C  C5A   . NAD   AA 6  .    ? 30.315  37.956  69.499  1.00 18.18 ? 1312 NAD   B C5A   1 
HETATM 18272 C  C6A   . NAD   AA 6  .    ? 30.718  38.999  68.689  1.00 17.89 ? 1312 NAD   B C6A   1 
HETATM 18273 N  N6A   . NAD   AA 6  .    ? 32.022  39.598  68.860  1.00 22.77 ? 1312 NAD   B N6A   1 
HETATM 18274 N  N1A   . NAD   AA 6  .    ? 29.916  39.467  67.733  1.00 19.55 ? 1312 NAD   B N1A   1 
HETATM 18275 C  C2A   . NAD   AA 6  .    ? 28.679  38.949  67.507  1.00 18.45 ? 1312 NAD   B C2A   1 
HETATM 18276 N  N3A   . NAD   AA 6  .    ? 28.255  37.927  68.273  1.00 16.52 ? 1312 NAD   B N3A   1 
HETATM 18277 C  C4A   . NAD   AA 6  .    ? 29.020  37.428  69.257  1.00 14.71 ? 1312 NAD   B C4A   1 
HETATM 18278 O  O3    . NAD   AA 6  .    ? 26.528  35.209  76.109  1.00 15.13 ? 1312 NAD   B O3    1 
HETATM 18279 P  PN    . NAD   AA 6  .    ? 26.186  33.771  76.670  1.00 16.87 ? 1312 NAD   B PN    1 
HETATM 18280 O  O1N   . NAD   AA 6  .    ? 27.312  33.270  77.522  1.00 19.85 ? 1312 NAD   B O1N   1 
HETATM 18281 O  O2N   . NAD   AA 6  .    ? 25.850  32.833  75.542  1.00 16.34 ? 1312 NAD   B O2N   1 
HETATM 18282 O  O5D   . NAD   AA 6  .    ? 24.896  34.004  77.542  1.00 18.44 ? 1312 NAD   B O5D   1 
HETATM 18283 C  C5D   . NAD   AA 6  .    ? 24.998  34.501  78.851  1.00 19.40 ? 1312 NAD   B C5D   1 
HETATM 18284 C  C4D   . NAD   AA 6  .    ? 24.774  36.002  78.881  1.00 16.20 ? 1312 NAD   B C4D   1 
HETATM 18285 O  O4D   . NAD   AA 6  .    ? 23.529  36.326  78.316  1.00 15.68 ? 1312 NAD   B O4D   1 
HETATM 18286 C  C3D   . NAD   AA 6  .    ? 24.798  36.530  80.286  1.00 15.87 ? 1312 NAD   B C3D   1 
HETATM 18287 O  O3D   . NAD   AA 6  .    ? 25.507  37.710  80.364  1.00 18.72 ? 1312 NAD   B O3D   1 
HETATM 18288 C  C2D   . NAD   AA 6  .    ? 23.357  36.735  80.548  1.00 17.35 ? 1312 NAD   B C2D   1 
HETATM 18289 O  O2D   . NAD   AA 6  .    ? 23.036  37.616  81.572  1.00 16.53 ? 1312 NAD   B O2D   1 
HETATM 18290 C  C1D   . NAD   AA 6  .    ? 22.867  37.176  79.215  1.00 16.09 ? 1312 NAD   B C1D   1 
HETATM 18291 N  N1N   . NAD   AA 6  .    ? 21.450  36.963  79.067  1.00 15.93 ? 1312 NAD   B N1N   1 
HETATM 18292 C  C2N   . NAD   AA 6  .    ? 20.553  38.049  79.072  1.00 14.69 ? 1312 NAD   B C2N   1 
HETATM 18293 C  C3N   . NAD   AA 6  .    ? 19.199  37.775  78.974  1.00 16.40 ? 1312 NAD   B C3N   1 
HETATM 18294 C  C7N   . NAD   AA 6  .    ? 18.191  38.860  78.972  1.00 14.58 ? 1312 NAD   B C7N   1 
HETATM 18295 O  O7N   . NAD   AA 6  .    ? 17.032  38.571  78.701  1.00 16.92 ? 1312 NAD   B O7N   1 
HETATM 18296 N  N7N   . NAD   AA 6  .    ? 18.550  40.190  79.312  1.00 16.68 ? 1312 NAD   B N7N   1 
HETATM 18297 C  C4N   . NAD   AA 6  .    ? 18.755  36.447  78.797  1.00 26.37 ? 1312 NAD   B C4N   1 
HETATM 18298 C  C5N   . NAD   AA 6  .    ? 19.650  35.360  78.831  1.00 20.49 ? 1312 NAD   B C5N   1 
HETATM 18299 C  C6N   . NAD   AA 6  .    ? 21.001  35.640  78.943  1.00 15.51 ? 1312 NAD   B C6N   1 
HETATM 18300 S  S     . SO4   BA 7  .    ? -7.154  47.535  73.132  1.00 18.23 ? 1313 SO4   B S     1 
HETATM 18301 O  O1    . SO4   BA 7  .    ? -5.926  46.809  72.696  1.00 23.08 ? 1313 SO4   B O1    1 
HETATM 18302 O  O2    . SO4   BA 7  .    ? -7.895  48.033  71.935  1.00 16.90 ? 1313 SO4   B O2    1 
HETATM 18303 O  O3    . SO4   BA 7  .    ? -8.027  46.633  73.904  1.00 21.46 ? 1313 SO4   B O3    1 
HETATM 18304 O  O4    . SO4   BA 7  .    ? -6.720  48.682  73.964  1.00 22.87 ? 1313 SO4   B O4    1 
HETATM 18305 MG MG    . MG    CA 8  .    ? 30.312  33.554  75.274  1.00 26.51 ? 1314 MG    B MG    1 
HETATM 18306 C  C1    . PEG   DA 3  .    ? 11.932  25.408  48.606  1.00 30.45 ? 1315 PEG   B C1    1 
HETATM 18307 O  O1    . PEG   DA 3  .    ? 11.253  26.415  47.887  1.00 42.62 ? 1315 PEG   B O1    1 
HETATM 18308 C  C2    . PEG   DA 3  .    ? 13.274  25.899  49.080  1.00 30.40 ? 1315 PEG   B C2    1 
HETATM 18309 O  O2    . PEG   DA 3  .    ? 14.192  25.811  48.020  1.00 38.94 ? 1315 PEG   B O2    1 
HETATM 18310 C  C3    . PEG   DA 3  .    ? 15.535  25.722  48.436  1.00 32.55 ? 1315 PEG   B C3    1 
HETATM 18311 C  C4    . PEG   DA 3  .    ? 16.461  25.900  47.252  1.00 32.79 ? 1315 PEG   B C4    1 
HETATM 18312 O  O4    . PEG   DA 3  .    ? 16.216  27.140  46.624  1.00 43.24 ? 1315 PEG   B O4    1 
HETATM 18313 O  O     . HOH   EA 11 .    ? -10.536 91.358  114.354 1.00 32.14 ? 1401 HOH   A O     1 
HETATM 18314 O  O     . HOH   EA 11 .    ? -32.135 56.037  85.966  1.00 27.37 ? 1402 HOH   A O     1 
HETATM 18315 O  O     . HOH   EA 11 .    ? 1.555   94.035  116.888 1.00 38.93 ? 1403 HOH   A O     1 
HETATM 18316 O  O     . HOH   EA 11 .    ? -1.113  88.797  105.468 1.00 22.54 ? 1404 HOH   A O     1 
HETATM 18317 O  O     . HOH   EA 11 .    ? -39.445 72.123  66.126  1.00 31.81 ? 1405 HOH   A O     1 
HETATM 18318 O  O     . HOH   EA 11 .    ? -57.768 67.156  61.694  1.00 30.96 ? 1406 HOH   A O     1 
HETATM 18319 O  O     . HOH   EA 11 .    ? -19.350 72.603  97.606  1.00 29.75 ? 1407 HOH   A O     1 
HETATM 18320 O  O     . HOH   EA 11 .    ? -52.283 61.173  101.904 1.00 27.49 ? 1408 HOH   A O     1 
HETATM 18321 O  O     . HOH   EA 11 .    ? -51.286 74.027  68.206  1.00 34.06 ? 1409 HOH   A O     1 
HETATM 18322 O  O     . HOH   EA 11 .    ? -32.031 79.574  99.181  1.00 27.78 ? 1410 HOH   A O     1 
HETATM 18323 O  O     . HOH   EA 11 .    ? -25.210 60.650  127.933 1.00 36.90 ? 1411 HOH   A O     1 
HETATM 18324 O  O     . HOH   EA 11 .    ? 30.192  60.367  110.153 1.00 39.30 ? 1412 HOH   A O     1 
HETATM 18325 O  O     . HOH   EA 11 .    ? -35.930 85.519  104.194 1.00 31.43 ? 1413 HOH   A O     1 
HETATM 18326 O  O     . HOH   EA 11 .    ? -21.597 95.447  120.915 1.00 39.32 ? 1414 HOH   A O     1 
HETATM 18327 O  O     . HOH   EA 11 .    ? -0.570  91.815  115.323 1.00 38.79 ? 1415 HOH   A O     1 
HETATM 18328 O  O     . HOH   EA 11 .    ? -35.656 56.135  78.071  1.00 40.08 ? 1416 HOH   A O     1 
HETATM 18329 O  O     . HOH   EA 11 .    ? -0.422  79.718  81.828  1.00 37.85 ? 1417 HOH   A O     1 
HETATM 18330 O  O     . HOH   EA 11 .    ? -39.176 37.683  64.499  1.00 39.67 ? 1418 HOH   A O     1 
HETATM 18331 O  O     . HOH   EA 11 .    ? -2.370  67.618  124.872 1.00 39.87 ? 1419 HOH   A O     1 
HETATM 18332 O  O     . HOH   EA 11 .    ? -0.291  71.856  119.725 1.00 36.50 ? 1420 HOH   A O     1 
HETATM 18333 O  O     . HOH   EA 11 .    ? -10.454 63.303  48.589  1.00 46.41 ? 1421 HOH   A O     1 
HETATM 18334 O  O     . HOH   EA 11 .    ? -2.718  81.768  114.608 1.00 37.46 ? 1422 HOH   A O     1 
HETATM 18335 O  O     . HOH   EA 11 .    ? -38.903 67.176  69.268  1.00 33.02 ? 1423 HOH   A O     1 
HETATM 18336 O  O     . HOH   EA 11 .    ? -31.179 58.432  115.500 1.00 43.34 ? 1424 HOH   A O     1 
HETATM 18337 O  O     . HOH   EA 11 .    ? -55.039 75.364  92.142  1.00 38.50 ? 1425 HOH   A O     1 
HETATM 18338 O  O     . HOH   EA 11 .    ? -54.840 33.674  71.330  1.00 34.57 ? 1426 HOH   A O     1 
HETATM 18339 O  O     . HOH   EA 11 .    ? -43.097 80.553  89.751  1.00 33.46 ? 1427 HOH   A O     1 
HETATM 18340 O  O     . HOH   EA 11 .    ? 21.649  68.026  116.498 1.00 35.03 ? 1428 HOH   A O     1 
HETATM 18341 O  O     . HOH   EA 11 .    ? -40.433 96.520  109.378 1.00 38.98 ? 1429 HOH   A O     1 
HETATM 18342 O  O     . HOH   EA 11 .    ? -31.241 46.449  88.351  1.00 35.10 ? 1430 HOH   A O     1 
HETATM 18343 O  O     . HOH   EA 11 .    ? -30.933 90.199  127.927 1.00 42.69 ? 1431 HOH   A O     1 
HETATM 18344 O  O     . HOH   EA 11 .    ? -33.256 71.670  76.824  1.00 34.60 ? 1432 HOH   A O     1 
HETATM 18345 O  O     . HOH   EA 11 .    ? -0.327  63.731  109.755 1.00 25.66 ? 1433 HOH   A O     1 
HETATM 18346 O  O     . HOH   EA 11 .    ? -12.386 87.789  98.955  1.00 35.43 ? 1434 HOH   A O     1 
HETATM 18347 O  O     . HOH   EA 11 .    ? 15.043  55.207  110.790 1.00 35.04 ? 1435 HOH   A O     1 
HETATM 18348 O  O     . HOH   EA 11 .    ? 8.323   89.639  120.265 1.00 29.88 ? 1436 HOH   A O     1 
HETATM 18349 O  O     . HOH   EA 11 .    ? -24.133 92.772  126.753 1.00 34.12 ? 1437 HOH   A O     1 
HETATM 18350 O  O     . HOH   EA 11 .    ? -49.146 66.695  94.128  1.00 24.37 ? 1438 HOH   A O     1 
HETATM 18351 O  O     . HOH   EA 11 .    ? -48.473 54.588  61.215  1.00 24.33 ? 1439 HOH   A O     1 
HETATM 18352 O  O     . HOH   EA 11 .    ? -66.872 72.413  75.270  1.00 31.85 ? 1440 HOH   A O     1 
HETATM 18353 O  O     . HOH   EA 11 .    ? 4.904   74.435  120.008 1.00 38.02 ? 1441 HOH   A O     1 
HETATM 18354 O  O     . HOH   EA 11 .    ? -52.399 24.563  82.501  1.00 40.99 ? 1442 HOH   A O     1 
HETATM 18355 O  O     . HOH   EA 11 .    ? -34.955 75.023  70.832  1.00 39.92 ? 1443 HOH   A O     1 
HETATM 18356 O  O     . HOH   EA 11 .    ? -38.339 38.319  87.824  1.00 40.14 ? 1444 HOH   A O     1 
HETATM 18357 O  O     . HOH   EA 11 .    ? -11.708 68.610  76.569  1.00 28.71 ? 1445 HOH   A O     1 
HETATM 18358 O  O     . HOH   EA 11 .    ? -52.176 49.314  62.738  1.00 37.74 ? 1446 HOH   A O     1 
HETATM 18359 O  O     . HOH   EA 11 .    ? -55.050 76.198  83.720  1.00 35.48 ? 1447 HOH   A O     1 
HETATM 18360 O  O     . HOH   EA 11 .    ? -28.936 57.700  115.395 1.00 35.81 ? 1448 HOH   A O     1 
HETATM 18361 O  O     . HOH   EA 11 .    ? -5.707  70.581  72.814  1.00 41.13 ? 1449 HOH   A O     1 
HETATM 18362 O  O     . HOH   EA 11 .    ? -14.118 61.424  107.643 1.00 25.32 ? 1450 HOH   A O     1 
HETATM 18363 O  O     . HOH   EA 11 .    ? -63.544 73.323  78.360  1.00 33.54 ? 1451 HOH   A O     1 
HETATM 18364 O  O     . HOH   EA 11 .    ? -24.900 66.910  86.561  1.00 31.53 ? 1452 HOH   A O     1 
HETATM 18365 O  O     . HOH   EA 11 .    ? -6.544  58.495  119.990 1.00 23.27 ? 1453 HOH   A O     1 
HETATM 18366 O  O     . HOH   EA 11 .    ? -29.105 37.959  85.163  1.00 44.00 ? 1454 HOH   A O     1 
HETATM 18367 O  O     . HOH   EA 11 .    ? -22.890 80.454  110.229 1.00 30.57 ? 1455 HOH   A O     1 
HETATM 18368 O  O     . HOH   EA 11 .    ? -35.916 51.903  69.230  1.00 35.05 ? 1456 HOH   A O     1 
HETATM 18369 O  O     . HOH   EA 11 .    ? 26.015  72.024  104.715 1.00 35.21 ? 1457 HOH   A O     1 
HETATM 18370 O  O     . HOH   EA 11 .    ? -10.121 81.124  91.175  1.00 25.30 ? 1458 HOH   A O     1 
HETATM 18371 O  O     . HOH   EA 11 .    ? -44.861 89.291  109.675 1.00 38.10 ? 1459 HOH   A O     1 
HETATM 18372 O  O     . HOH   EA 11 .    ? -21.464 47.204  57.980  1.00 34.57 ? 1460 HOH   A O     1 
HETATM 18373 O  O     . HOH   EA 11 .    ? -44.720 30.299  96.383  1.00 43.78 ? 1461 HOH   A O     1 
HETATM 18374 O  O     . HOH   EA 11 .    ? -46.893 35.130  86.999  1.00 33.42 ? 1462 HOH   A O     1 
HETATM 18375 O  O     . HOH   EA 11 .    ? -14.752 63.994  99.235  1.00 27.26 ? 1463 HOH   A O     1 
HETATM 18376 O  O     . HOH   EA 11 .    ? -0.445  60.125  94.810  1.00 38.64 ? 1464 HOH   A O     1 
HETATM 18377 O  O     . HOH   EA 11 .    ? -41.001 71.711  114.321 1.00 33.62 ? 1465 HOH   A O     1 
HETATM 18378 O  O     . HOH   EA 11 .    ? -10.432 49.621  109.990 1.00 23.76 ? 1466 HOH   A O     1 
HETATM 18379 O  O     . HOH   EA 11 .    ? -14.247 75.778  109.941 1.00 23.37 ? 1467 HOH   A O     1 
HETATM 18380 O  O     . HOH   EA 11 .    ? -41.152 63.173  73.568  1.00 30.39 ? 1468 HOH   A O     1 
HETATM 18381 O  O     . HOH   EA 11 .    ? -37.734 62.567  81.685  1.00 27.50 ? 1469 HOH   A O     1 
HETATM 18382 O  O     . HOH   EA 11 .    ? -3.909  79.198  103.863 1.00 24.03 ? 1470 HOH   A O     1 
HETATM 18383 O  O     . HOH   EA 11 .    ? 0.354   76.722  123.287 1.00 35.08 ? 1471 HOH   A O     1 
HETATM 18384 O  O     . HOH   EA 11 .    ? -43.197 33.241  102.476 1.00 37.01 ? 1472 HOH   A O     1 
HETATM 18385 O  O     . HOH   EA 11 .    ? -62.674 43.795  82.276  1.00 32.55 ? 1473 HOH   A O     1 
HETATM 18386 O  O     . HOH   EA 11 .    ? -54.968 56.535  64.727  1.00 19.57 ? 1474 HOH   A O     1 
HETATM 18387 O  O     . HOH   EA 11 .    ? -6.150  68.520  92.439  1.00 31.49 ? 1475 HOH   A O     1 
HETATM 18388 O  O     . HOH   EA 11 .    ? -42.468 38.761  84.908  1.00 28.22 ? 1476 HOH   A O     1 
HETATM 18389 O  O     . HOH   EA 11 .    ? 13.821  87.136  98.450  1.00 37.39 ? 1477 HOH   A O     1 
HETATM 18390 O  O     . HOH   EA 11 .    ? -27.534 58.810  76.057  1.00 44.58 ? 1478 HOH   A O     1 
HETATM 18391 O  O     . HOH   EA 11 .    ? 11.142  67.437  116.614 1.00 28.32 ? 1479 HOH   A O     1 
HETATM 18392 O  O     . HOH   EA 11 .    ? -37.348 64.098  67.018  1.00 29.87 ? 1480 HOH   A O     1 
HETATM 18393 O  O     . HOH   EA 11 .    ? -44.248 41.398  104.146 1.00 35.64 ? 1481 HOH   A O     1 
HETATM 18394 O  O     . HOH   EA 11 .    ? -13.115 59.271  122.487 1.00 28.77 ? 1482 HOH   A O     1 
HETATM 18395 O  O     . HOH   EA 11 .    ? -39.275 35.323  85.766  1.00 36.30 ? 1483 HOH   A O     1 
HETATM 18396 O  O     . HOH   EA 11 .    ? 9.647   76.455  125.432 1.00 47.11 ? 1484 HOH   A O     1 
HETATM 18397 O  O     . HOH   EA 11 .    ? -38.599 49.551  102.397 1.00 31.75 ? 1485 HOH   A O     1 
HETATM 18398 O  O     . HOH   EA 11 .    ? -32.280 82.407  97.693  1.00 31.39 ? 1486 HOH   A O     1 
HETATM 18399 O  O     . HOH   EA 11 .    ? -48.150 82.599  111.409 1.00 34.08 ? 1487 HOH   A O     1 
HETATM 18400 O  O     . HOH   EA 11 .    ? 14.638  61.084  94.542  1.00 29.98 ? 1488 HOH   A O     1 
HETATM 18401 O  O     . HOH   EA 11 .    ? 7.024   54.114  101.420 1.00 20.13 ? 1489 HOH   A O     1 
HETATM 18402 O  O     . HOH   EA 11 .    ? 7.798   66.826  112.117 1.00 36.01 ? 1490 HOH   A O     1 
HETATM 18403 O  O     . HOH   EA 11 .    ? -33.230 60.924  114.378 1.00 43.81 ? 1491 HOH   A O     1 
HETATM 18404 O  O     . HOH   EA 11 .    ? -33.650 97.567  98.018  1.00 41.03 ? 1492 HOH   A O     1 
HETATM 18405 O  O     . HOH   EA 11 .    ? -11.479 63.158  113.217 1.00 20.32 ? 1493 HOH   A O     1 
HETATM 18406 O  O     . HOH   EA 11 .    ? -0.863  58.347  110.665 1.00 32.83 ? 1494 HOH   A O     1 
HETATM 18407 O  O     . HOH   EA 11 .    ? -46.642 59.717  102.022 1.00 23.57 ? 1495 HOH   A O     1 
HETATM 18408 O  O     . HOH   EA 11 .    ? -23.180 63.726  97.936  1.00 23.22 ? 1496 HOH   A O     1 
HETATM 18409 O  O     . HOH   EA 11 .    ? -3.518  70.286  117.493 1.00 26.51 ? 1497 HOH   A O     1 
HETATM 18410 O  O     . HOH   EA 11 .    ? -35.183 76.346  92.135  1.00 35.76 ? 1498 HOH   A O     1 
HETATM 18411 O  O     . HOH   EA 11 .    ? -23.083 56.761  83.944  1.00 35.52 ? 1499 HOH   A O     1 
HETATM 18412 O  O     . HOH   EA 11 .    ? -14.215 64.445  51.148  1.00 38.97 ? 1500 HOH   A O     1 
HETATM 18413 O  O     . HOH   EA 11 .    ? -13.371 77.849  111.102 1.00 22.04 ? 1501 HOH   A O     1 
HETATM 18414 O  O     . HOH   EA 11 .    ? -13.721 74.304  105.993 1.00 22.97 ? 1502 HOH   A O     1 
HETATM 18415 O  O     . HOH   EA 11 .    ? -50.066 32.711  91.609  1.00 38.40 ? 1503 HOH   A O     1 
HETATM 18416 O  O     . HOH   EA 11 .    ? -7.095  50.490  76.711  1.00 27.59 ? 1504 HOH   A O     1 
HETATM 18417 O  O     . HOH   EA 11 .    ? -59.468 54.260  74.800  1.00 20.98 ? 1505 HOH   A O     1 
HETATM 18418 O  O     . HOH   EA 11 .    ? -41.182 85.780  113.786 1.00 28.61 ? 1506 HOH   A O     1 
HETATM 18419 O  O     . HOH   EA 11 .    ? -19.948 59.205  76.214  1.00 24.14 ? 1507 HOH   A O     1 
HETATM 18420 O  O     . HOH   EA 11 .    ? -44.074 62.335  70.078  1.00 24.99 ? 1508 HOH   A O     1 
HETATM 18421 O  O     . HOH   EA 11 .    ? -61.852 57.367  63.748  1.00 29.02 ? 1509 HOH   A O     1 
HETATM 18422 O  O     . HOH   EA 11 .    ? -14.648 48.794  75.790  1.00 29.80 ? 1510 HOH   A O     1 
HETATM 18423 O  O     . HOH   EA 11 .    ? -27.707 55.914  90.430  1.00 31.67 ? 1511 HOH   A O     1 
HETATM 18424 O  O     . HOH   EA 11 .    ? -56.255 34.593  86.438  1.00 26.98 ? 1512 HOH   A O     1 
HETATM 18425 O  O     . HOH   EA 11 .    ? -43.007 48.439  60.030  1.00 27.25 ? 1513 HOH   A O     1 
HETATM 18426 O  O     . HOH   EA 11 .    ? -37.468 30.693  66.385  1.00 41.89 ? 1514 HOH   A O     1 
HETATM 18427 O  O     . HOH   EA 11 .    ? -22.988 60.443  115.810 1.00 24.01 ? 1515 HOH   A O     1 
HETATM 18428 O  O     . HOH   EA 11 .    ? 18.127  58.988  95.678  1.00 32.95 ? 1516 HOH   A O     1 
HETATM 18429 O  O     . HOH   EA 11 .    ? -38.008 85.985  83.899  1.00 41.91 ? 1517 HOH   A O     1 
HETATM 18430 O  O     . HOH   EA 11 .    ? 20.852  58.502  111.023 1.00 32.09 ? 1518 HOH   A O     1 
HETATM 18431 O  O     . HOH   EA 11 .    ? -43.318 75.441  114.014 1.00 30.47 ? 1519 HOH   A O     1 
HETATM 18432 O  O     . HOH   EA 11 .    ? -2.354  53.820  104.574 1.00 29.41 ? 1520 HOH   A O     1 
HETATM 18433 O  O     . HOH   EA 11 .    ? -46.490 37.830  64.102  1.00 38.94 ? 1521 HOH   A O     1 
HETATM 18434 O  O     . HOH   EA 11 .    ? -42.589 61.237  100.101 1.00 27.91 ? 1522 HOH   A O     1 
HETATM 18435 O  O     . HOH   EA 11 .    ? -60.621 68.075  94.471  1.00 38.97 ? 1523 HOH   A O     1 
HETATM 18436 O  O     . HOH   EA 11 .    ? -27.729 78.664  101.205 1.00 33.86 ? 1524 HOH   A O     1 
HETATM 18437 O  O     . HOH   EA 11 .    ? -51.916 47.505  68.847  1.00 29.92 ? 1525 HOH   A O     1 
HETATM 18438 O  O     . HOH   EA 11 .    ? -38.869 77.603  97.176  1.00 23.36 ? 1526 HOH   A O     1 
HETATM 18439 O  O     . HOH   EA 11 .    ? 25.605  79.726  107.453 1.00 33.43 ? 1527 HOH   A O     1 
HETATM 18440 O  O     . HOH   EA 11 .    ? -39.824 57.232  87.978  1.00 17.35 ? 1528 HOH   A O     1 
HETATM 18441 O  O     . HOH   EA 11 .    ? -51.022 69.808  93.962  1.00 25.14 ? 1529 HOH   A O     1 
HETATM 18442 O  O     . HOH   EA 11 .    ? -4.009  70.003  106.738 1.00 28.36 ? 1530 HOH   A O     1 
HETATM 18443 O  O     . HOH   EA 11 .    ? -30.912 67.055  98.723  1.00 39.02 ? 1531 HOH   A O     1 
HETATM 18444 O  O     . HOH   EA 11 .    ? -13.328 55.541  81.472  1.00 35.07 ? 1532 HOH   A O     1 
HETATM 18445 O  O     . HOH   EA 11 .    ? -51.434 55.273  75.844  1.00 18.92 ? 1533 HOH   A O     1 
HETATM 18446 O  O     . HOH   EA 11 .    ? 0.446   85.472  103.009 1.00 23.90 ? 1534 HOH   A O     1 
HETATM 18447 O  O     . HOH   EA 11 .    ? -27.382 73.442  129.427 1.00 33.03 ? 1535 HOH   A O     1 
HETATM 18448 O  O     . HOH   EA 11 .    ? -45.664 76.005  94.381  1.00 27.55 ? 1536 HOH   A O     1 
HETATM 18449 O  O     . HOH   EA 11 .    ? -5.193  91.074  122.922 1.00 41.90 ? 1537 HOH   A O     1 
HETATM 18450 O  O     . HOH   EA 11 .    ? 4.497   73.710  116.366 1.00 30.89 ? 1538 HOH   A O     1 
HETATM 18451 O  O     . HOH   EA 11 .    ? -33.500 93.221  86.184  1.00 36.54 ? 1539 HOH   A O     1 
HETATM 18452 O  O     . HOH   EA 11 .    ? -6.997  80.463  128.009 1.00 31.99 ? 1540 HOH   A O     1 
HETATM 18453 O  O     . HOH   EA 11 .    ? -26.453 85.813  137.258 1.00 39.83 ? 1541 HOH   A O     1 
HETATM 18454 O  O     . HOH   EA 11 .    ? -25.686 70.305  131.126 1.00 35.75 ? 1542 HOH   A O     1 
HETATM 18455 O  O     . HOH   EA 11 .    ? -20.368 54.944  91.122  1.00 36.29 ? 1543 HOH   A O     1 
HETATM 18456 O  O     . HOH   EA 11 .    ? 8.427   92.994  98.801  1.00 45.24 ? 1544 HOH   A O     1 
HETATM 18457 O  O     . HOH   EA 11 .    ? -15.961 91.395  104.440 1.00 31.66 ? 1545 HOH   A O     1 
HETATM 18458 O  O     . HOH   EA 11 .    ? 14.424  86.852  110.186 1.00 33.07 ? 1546 HOH   A O     1 
HETATM 18459 O  O     . HOH   EA 11 .    ? -1.091  77.920  114.531 1.00 27.37 ? 1547 HOH   A O     1 
HETATM 18460 O  O     . HOH   EA 11 .    ? -36.829 61.627  74.922  1.00 35.13 ? 1548 HOH   A O     1 
HETATM 18461 O  O     . HOH   EA 11 .    ? -10.634 63.086  72.632  1.00 31.21 ? 1549 HOH   A O     1 
HETATM 18462 O  O     . HOH   EA 11 .    ? -1.064  50.252  57.863  1.00 28.36 ? 1550 HOH   A O     1 
HETATM 18463 O  O     . HOH   EA 11 .    ? -48.141 66.243  57.742  1.00 30.88 ? 1551 HOH   A O     1 
HETATM 18464 O  O     . HOH   EA 11 .    ? 1.718   73.178  115.788 1.00 32.37 ? 1552 HOH   A O     1 
HETATM 18465 O  O     . HOH   EA 11 .    ? -24.797 65.201  94.800  1.00 34.20 ? 1553 HOH   A O     1 
HETATM 18466 O  O     . HOH   EA 11 .    ? -31.990 61.823  111.477 1.00 25.47 ? 1554 HOH   A O     1 
HETATM 18467 O  O     . HOH   EA 11 .    ? -42.870 85.241  97.391  1.00 27.79 ? 1555 HOH   A O     1 
HETATM 18468 O  O     . HOH   EA 11 .    ? -28.590 42.058  92.704  1.00 49.90 ? 1556 HOH   A O     1 
HETATM 18469 O  O     . HOH   EA 11 .    ? -18.675 59.020  104.252 1.00 25.98 ? 1557 HOH   A O     1 
HETATM 18470 O  O     . HOH   EA 11 .    ? 7.873   91.390  113.313 1.00 37.16 ? 1558 HOH   A O     1 
HETATM 18471 O  O     . HOH   EA 11 .    ? -20.721 47.528  54.832  1.00 36.11 ? 1559 HOH   A O     1 
HETATM 18472 O  O     . HOH   EA 11 .    ? -28.146 62.001  102.062 1.00 20.10 ? 1560 HOH   A O     1 
HETATM 18473 O  O     . HOH   EA 11 .    ? -31.262 60.149  105.500 1.00 27.14 ? 1561 HOH   A O     1 
HETATM 18474 O  O     . HOH   EA 11 .    ? -36.369 64.820  83.121  1.00 33.84 ? 1562 HOH   A O     1 
HETATM 18475 O  O     . HOH   EA 11 .    ? -50.726 50.505  57.323  1.00 36.06 ? 1563 HOH   A O     1 
HETATM 18476 O  O     . HOH   EA 11 .    ? 5.882   74.377  95.457  1.00 40.85 ? 1564 HOH   A O     1 
HETATM 18477 O  O     . HOH   EA 11 .    ? -5.509  53.545  110.762 1.00 16.95 ? 1565 HOH   A O     1 
HETATM 18478 O  O     . HOH   EA 11 .    ? -16.464 76.437  108.557 1.00 21.66 ? 1566 HOH   A O     1 
HETATM 18479 O  O     . HOH   EA 11 .    ? -57.721 28.078  85.683  1.00 39.24 ? 1567 HOH   A O     1 
HETATM 18480 O  O     . HOH   EA 11 .    ? 17.639  78.673  119.661 1.00 36.17 ? 1568 HOH   A O     1 
HETATM 18481 O  O     . HOH   EA 11 .    ? -21.475 90.368  106.230 1.00 29.28 ? 1569 HOH   A O     1 
HETATM 18482 O  O     . HOH   EA 11 .    ? -27.748 61.168  84.334  1.00 39.68 ? 1570 HOH   A O     1 
HETATM 18483 O  O     . HOH   EA 11 .    ? -23.641 83.104  111.955 1.00 22.52 ? 1571 HOH   A O     1 
HETATM 18484 O  O     . HOH   EA 11 .    ? 16.346  61.631  116.027 1.00 33.99 ? 1572 HOH   A O     1 
HETATM 18485 O  O     . HOH   EA 11 .    ? -24.043 67.128  105.263 1.00 22.89 ? 1573 HOH   A O     1 
HETATM 18486 O  O     . HOH   EA 11 .    ? -4.757  70.152  76.499  1.00 35.25 ? 1574 HOH   A O     1 
HETATM 18487 O  O     . HOH   EA 11 .    ? -45.064 63.731  105.349 1.00 38.13 ? 1575 HOH   A O     1 
HETATM 18488 O  O     . HOH   EA 11 .    ? -38.969 27.657  86.494  1.00 43.65 ? 1576 HOH   A O     1 
HETATM 18489 O  O     . HOH   EA 11 .    ? -61.822 58.169  70.161  1.00 23.81 ? 1577 HOH   A O     1 
HETATM 18490 O  O     . HOH   EA 11 .    ? -23.996 59.516  121.541 1.00 34.55 ? 1578 HOH   A O     1 
HETATM 18491 O  O     . HOH   EA 11 .    ? -38.571 65.169  96.404  1.00 31.76 ? 1579 HOH   A O     1 
HETATM 18492 O  O     . HOH   EA 11 .    ? -32.306 79.287  96.277  1.00 31.09 ? 1580 HOH   A O     1 
HETATM 18493 O  O     . HOH   EA 11 .    ? -12.209 77.035  103.175 1.00 21.36 ? 1581 HOH   A O     1 
HETATM 18494 O  O     . HOH   EA 11 .    ? -60.379 59.733  90.479  1.00 21.01 ? 1582 HOH   A O     1 
HETATM 18495 O  O     . HOH   EA 11 .    ? -48.397 81.017  84.989  1.00 36.30 ? 1583 HOH   A O     1 
HETATM 18496 O  O     . HOH   EA 11 .    ? -3.861  78.393  122.529 1.00 25.50 ? 1584 HOH   A O     1 
HETATM 18497 O  O     . HOH   EA 11 .    ? -4.473  60.002  125.433 1.00 32.54 ? 1585 HOH   A O     1 
HETATM 18498 O  O     . HOH   EA 11 .    ? 12.616  74.155  91.504  1.00 37.14 ? 1586 HOH   A O     1 
HETATM 18499 O  O     . HOH   EA 11 .    ? -20.165 90.970  109.118 1.00 28.19 ? 1587 HOH   A O     1 
HETATM 18500 O  O     . HOH   EA 11 .    ? -49.556 33.353  100.294 1.00 46.90 ? 1588 HOH   A O     1 
HETATM 18501 O  O     . HOH   EA 11 .    ? -9.156  45.017  55.808  1.00 35.06 ? 1589 HOH   A O     1 
HETATM 18502 O  O     . HOH   EA 11 .    ? -4.922  54.500  108.212 1.00 22.09 ? 1590 HOH   A O     1 
HETATM 18503 O  O     . HOH   EA 11 .    ? -11.619 88.558  128.891 1.00 35.40 ? 1591 HOH   A O     1 
HETATM 18504 O  O     . HOH   EA 11 .    ? -40.939 49.005  63.986  1.00 26.56 ? 1592 HOH   A O     1 
HETATM 18505 O  O     . HOH   EA 11 .    ? 0.610   85.187  111.737 1.00 28.39 ? 1593 HOH   A O     1 
HETATM 18506 O  O     . HOH   EA 11 .    ? -31.190 71.750  82.480  1.00 33.58 ? 1594 HOH   A O     1 
HETATM 18507 O  O     . HOH   EA 11 .    ? -22.874 67.061  97.432  1.00 23.11 ? 1595 HOH   A O     1 
HETATM 18508 O  O     . HOH   EA 11 .    ? -32.434 70.368  100.322 1.00 35.65 ? 1596 HOH   A O     1 
HETATM 18509 O  O     . HOH   EA 11 .    ? -34.521 76.633  96.085  1.00 34.84 ? 1597 HOH   A O     1 
HETATM 18510 O  O     . HOH   EA 11 .    ? -19.719 55.057  106.995 1.00 32.05 ? 1598 HOH   A O     1 
HETATM 18511 O  O     . HOH   EA 11 .    ? -0.116  92.977  104.684 1.00 27.31 ? 1599 HOH   A O     1 
HETATM 18512 O  O     . HOH   EA 11 .    ? -17.875 82.634  96.627  1.00 21.83 ? 1600 HOH   A O     1 
HETATM 18513 O  O     . HOH   EA 11 .    ? -2.240  74.521  84.255  1.00 33.54 ? 1601 HOH   A O     1 
HETATM 18514 O  O     . HOH   EA 11 .    ? -55.619 36.768  76.223  1.00 30.21 ? 1602 HOH   A O     1 
HETATM 18515 O  O     . HOH   EA 11 .    ? -0.940  73.302  88.959  1.00 34.53 ? 1603 HOH   A O     1 
HETATM 18516 O  O     . HOH   EA 11 .    ? -0.021  82.323  113.411 1.00 37.13 ? 1604 HOH   A O     1 
HETATM 18517 O  O     . HOH   EA 11 .    ? -45.658 65.254  91.803  1.00 21.13 ? 1605 HOH   A O     1 
HETATM 18518 O  O     . HOH   EA 11 .    ? -46.342 30.606  85.419  1.00 31.12 ? 1606 HOH   A O     1 
HETATM 18519 O  O     . HOH   EA 11 .    ? -31.261 84.232  99.170  1.00 25.08 ? 1607 HOH   A O     1 
HETATM 18520 O  O     . HOH   EA 11 .    ? -12.187 79.283  94.549  1.00 18.51 ? 1608 HOH   A O     1 
HETATM 18521 O  O     . HOH   EA 11 .    ? -19.903 78.645  70.212  1.00 26.37 ? 1609 HOH   A O     1 
HETATM 18522 O  O     . HOH   EA 11 .    ? -5.316  77.620  94.954  1.00 26.98 ? 1610 HOH   A O     1 
HETATM 18523 O  O     . HOH   EA 11 .    ? -27.222 82.545  129.636 1.00 32.41 ? 1611 HOH   A O     1 
HETATM 18524 O  O     . HOH   EA 11 .    ? -9.370  64.898  76.423  1.00 23.48 ? 1612 HOH   A O     1 
HETATM 18525 O  O     . HOH   EA 11 .    ? -68.575 56.594  82.752  1.00 31.91 ? 1613 HOH   A O     1 
HETATM 18526 O  O     . HOH   EA 11 .    ? -19.757 59.552  79.087  1.00 33.37 ? 1614 HOH   A O     1 
HETATM 18527 O  O     . HOH   EA 11 .    ? -10.478 69.126  133.471 1.00 35.36 ? 1615 HOH   A O     1 
HETATM 18528 O  O     . HOH   EA 11 .    ? -8.438  80.559  74.747  1.00 32.72 ? 1616 HOH   A O     1 
HETATM 18529 O  O     . HOH   EA 11 .    ? -16.198 75.463  106.021 1.00 22.23 ? 1617 HOH   A O     1 
HETATM 18530 O  O     . HOH   EA 11 .    ? -17.502 72.712  111.197 1.00 19.42 ? 1618 HOH   A O     1 
HETATM 18531 O  O     . HOH   EA 11 .    ? -33.991 82.595  118.455 1.00 24.22 ? 1619 HOH   A O     1 
HETATM 18532 O  O     . HOH   EA 11 .    ? -36.918 80.530  78.968  1.00 22.49 ? 1620 HOH   A O     1 
HETATM 18533 O  O     . HOH   EA 11 .    ? -58.170 65.317  94.411  1.00 26.73 ? 1621 HOH   A O     1 
HETATM 18534 O  O     . HOH   EA 11 .    ? -45.282 89.477  106.193 1.00 37.12 ? 1622 HOH   A O     1 
HETATM 18535 O  O     . HOH   EA 11 .    ? 13.910  86.624  120.948 1.00 35.90 ? 1623 HOH   A O     1 
HETATM 18536 O  O     . HOH   EA 11 .    ? -44.830 63.535  84.248  1.00 20.02 ? 1624 HOH   A O     1 
HETATM 18537 O  O     . HOH   EA 11 .    ? -44.685 63.348  81.410  1.00 17.87 ? 1625 HOH   A O     1 
HETATM 18538 O  O     . HOH   EA 11 .    ? 23.276  69.415  113.088 1.00 36.22 ? 1626 HOH   A O     1 
HETATM 18539 O  O     . HOH   EA 11 .    ? -6.045  54.742  105.123 1.00 32.83 ? 1627 HOH   A O     1 
HETATM 18540 O  O     . HOH   EA 11 .    ? -41.619 79.818  79.935  1.00 30.51 ? 1628 HOH   A O     1 
HETATM 18541 O  O     . HOH   EA 11 .    ? -36.599 63.331  95.945  1.00 28.64 ? 1629 HOH   A O     1 
HETATM 18542 O  O     . HOH   EA 11 .    ? -3.812  79.238  111.143 1.00 32.81 ? 1630 HOH   A O     1 
HETATM 18543 O  O     . HOH   EA 11 .    ? -26.166 82.624  112.565 1.00 25.07 ? 1631 HOH   A O     1 
HETATM 18544 O  O     . HOH   EA 11 .    ? -65.371 47.778  85.570  1.00 37.72 ? 1632 HOH   A O     1 
HETATM 18545 O  O     . HOH   EA 11 .    ? -11.271 58.686  125.561 1.00 35.45 ? 1633 HOH   A O     1 
HETATM 18546 O  O     . HOH   EA 11 .    ? -2.533  55.976  99.696  1.00 31.25 ? 1634 HOH   A O     1 
HETATM 18547 O  O     . HOH   EA 11 .    ? -23.271 63.827  106.113 1.00 19.43 ? 1635 HOH   A O     1 
HETATM 18548 O  O     . HOH   EA 11 .    ? -47.615 84.937  101.955 1.00 39.18 ? 1636 HOH   A O     1 
HETATM 18549 O  O     . HOH   EA 11 .    ? -11.619 73.023  128.539 1.00 29.21 ? 1637 HOH   A O     1 
HETATM 18550 O  O     . HOH   EA 11 .    ? -38.067 62.371  105.358 1.00 34.07 ? 1638 HOH   A O     1 
HETATM 18551 O  O     . HOH   EA 11 .    ? -58.509 38.218  76.171  1.00 32.34 ? 1639 HOH   A O     1 
HETATM 18552 O  O     . HOH   EA 11 .    ? -33.284 48.739  75.313  1.00 30.09 ? 1640 HOH   A O     1 
HETATM 18553 O  O     . HOH   EA 11 .    ? -47.482 49.173  95.881  1.00 20.27 ? 1641 HOH   A O     1 
HETATM 18554 O  O     . HOH   EA 11 .    ? -49.796 68.653  92.025  1.00 24.00 ? 1642 HOH   A O     1 
HETATM 18555 O  O     . HOH   EA 11 .    ? -12.324 64.254  129.730 1.00 35.37 ? 1643 HOH   A O     1 
HETATM 18556 O  O     . HOH   EA 11 .    ? -67.257 59.906  69.964  1.00 29.06 ? 1644 HOH   A O     1 
HETATM 18557 O  O     . HOH   EA 11 .    ? -50.629 52.143  63.857  1.00 23.54 ? 1645 HOH   A O     1 
HETATM 18558 O  O     . HOH   EA 11 .    ? -39.102 61.427  74.349  1.00 37.16 ? 1646 HOH   A O     1 
HETATM 18559 O  O     . HOH   EA 11 .    ? 16.714  57.851  102.691 1.00 22.49 ? 1647 HOH   A O     1 
HETATM 18560 O  O     . HOH   EA 11 .    ? -56.042 55.790  94.995  1.00 21.31 ? 1648 HOH   A O     1 
HETATM 18561 O  O     . HOH   EA 11 .    ? 12.064  75.634  94.929  1.00 33.87 ? 1649 HOH   A O     1 
HETATM 18562 O  O     . HOH   EA 11 .    ? 21.166  57.499  105.016 1.00 32.47 ? 1650 HOH   A O     1 
HETATM 18563 O  O     . HOH   EA 11 .    ? -11.009 92.218  124.125 1.00 37.61 ? 1651 HOH   A O     1 
HETATM 18564 O  O     . HOH   EA 11 .    ? -21.742 88.878  108.941 1.00 27.40 ? 1652 HOH   A O     1 
HETATM 18565 O  O     . HOH   EA 11 .    ? -43.212 85.577  94.722  1.00 36.93 ? 1653 HOH   A O     1 
HETATM 18566 O  O     . HOH   EA 11 .    ? -51.042 64.937  94.875  1.00 23.82 ? 1654 HOH   A O     1 
HETATM 18567 O  O     . HOH   EA 11 .    ? -36.479 58.943  94.126  1.00 19.70 ? 1655 HOH   A O     1 
HETATM 18568 O  O     . HOH   EA 11 .    ? -3.174  60.362  95.545  1.00 42.75 ? 1656 HOH   A O     1 
HETATM 18569 O  O     . HOH   EA 11 .    ? -17.142 86.775  92.121  1.00 25.05 ? 1657 HOH   A O     1 
HETATM 18570 O  O     . HOH   EA 11 .    ? -23.838 63.525  91.692  1.00 23.66 ? 1658 HOH   A O     1 
HETATM 18571 O  O     . HOH   EA 11 .    ? -36.787 85.378  85.833  1.00 34.61 ? 1659 HOH   A O     1 
HETATM 18572 O  O     . HOH   EA 11 .    ? 23.326  65.828  114.808 1.00 26.29 ? 1660 HOH   A O     1 
HETATM 18573 O  O     . HOH   EA 11 .    ? -26.191 56.505  107.952 1.00 23.35 ? 1661 HOH   A O     1 
HETATM 18574 O  O     . HOH   EA 11 .    ? -67.457 50.863  77.805  1.00 40.52 ? 1662 HOH   A O     1 
HETATM 18575 O  O     . HOH   EA 11 .    ? -16.331 60.250  106.399 1.00 24.07 ? 1663 HOH   A O     1 
HETATM 18576 O  O     . HOH   EA 11 .    ? -19.811 88.665  75.008  1.00 34.57 ? 1664 HOH   A O     1 
HETATM 18577 O  O     . HOH   EA 11 .    ? -22.153 67.598  81.324  1.00 29.44 ? 1665 HOH   A O     1 
HETATM 18578 O  O     . HOH   EA 11 .    ? 9.178   55.446  104.895 1.00 29.38 ? 1666 HOH   A O     1 
HETATM 18579 O  O     . HOH   EA 11 .    ? -50.536 69.768  100.318 1.00 23.58 ? 1667 HOH   A O     1 
HETATM 18580 O  O     . HOH   EA 11 .    ? 18.530  62.229  94.361  1.00 33.30 ? 1668 HOH   A O     1 
HETATM 18581 O  O     . HOH   EA 11 .    ? -66.618 68.115  72.116  1.00 33.52 ? 1669 HOH   A O     1 
HETATM 18582 O  O     . HOH   EA 11 .    ? -60.179 51.139  61.983  1.00 33.46 ? 1670 HOH   A O     1 
HETATM 18583 O  O     . HOH   EA 11 .    ? -21.224 56.731  53.421  1.00 38.50 ? 1671 HOH   A O     1 
HETATM 18584 O  O     . HOH   EA 11 .    ? -13.843 95.348  129.655 1.00 50.03 ? 1672 HOH   A O     1 
HETATM 18585 O  O     . HOH   EA 11 .    ? -61.209 55.475  67.595  1.00 21.75 ? 1673 HOH   A O     1 
HETATM 18586 O  O     . HOH   EA 11 .    ? -38.374 36.411  82.329  1.00 34.95 ? 1674 HOH   A O     1 
HETATM 18587 O  O     . HOH   EA 11 .    ? -47.736 64.175  96.670  1.00 25.09 ? 1675 HOH   A O     1 
HETATM 18588 O  O     . HOH   EA 11 .    ? -59.678 60.817  75.949  1.00 18.51 ? 1676 HOH   A O     1 
HETATM 18589 O  O     . HOH   EA 11 .    ? -15.231 55.396  121.670 1.00 35.71 ? 1677 HOH   A O     1 
HETATM 18590 O  O     . HOH   EA 11 .    ? 17.000  71.475  119.146 1.00 29.07 ? 1678 HOH   A O     1 
HETATM 18591 O  O     . HOH   EA 11 .    ? -60.305 61.440  92.713  1.00 22.67 ? 1679 HOH   A O     1 
HETATM 18592 O  O     . HOH   EA 11 .    ? -32.471 60.583  73.320  1.00 40.49 ? 1680 HOH   A O     1 
HETATM 18593 O  O     . HOH   EA 11 .    ? -8.563  65.082  113.901 1.00 20.18 ? 1681 HOH   A O     1 
HETATM 18594 O  O     . HOH   EA 11 .    ? -7.080  84.959  86.649  1.00 34.83 ? 1682 HOH   A O     1 
HETATM 18595 O  O     . HOH   EA 11 .    ? -41.326 64.137  103.580 1.00 23.84 ? 1683 HOH   A O     1 
HETATM 18596 O  O     . HOH   EA 11 .    ? -39.340 78.318  99.882  1.00 23.85 ? 1684 HOH   A O     1 
HETATM 18597 O  O     . HOH   EA 11 .    ? -42.742 66.309  63.597  1.00 34.38 ? 1685 HOH   A O     1 
HETATM 18598 O  O     . HOH   EA 11 .    ? -6.250  82.675  103.266 1.00 22.67 ? 1686 HOH   A O     1 
HETATM 18599 O  O     . HOH   EA 11 .    ? -25.222 62.550  110.001 1.00 22.52 ? 1687 HOH   A O     1 
HETATM 18600 O  O     . HOH   EA 11 .    ? -52.241 78.289  87.556  1.00 30.52 ? 1688 HOH   A O     1 
HETATM 18601 O  O     . HOH   EA 11 .    ? -49.595 78.110  77.580  1.00 30.43 ? 1689 HOH   A O     1 
HETATM 18602 O  O     . HOH   EA 11 .    ? -21.848 42.993  60.803  1.00 36.19 ? 1690 HOH   A O     1 
HETATM 18603 O  O     . HOH   EA 11 .    ? 5.050   67.189  95.956  1.00 27.94 ? 1691 HOH   A O     1 
HETATM 18604 O  O     . HOH   EA 11 .    ? -1.043  83.785  117.874 1.00 27.18 ? 1692 HOH   A O     1 
HETATM 18605 O  O     . HOH   EA 11 .    ? -34.626 80.476  120.279 1.00 27.46 ? 1693 HOH   A O     1 
HETATM 18606 O  O     . HOH   EA 11 .    ? -35.493 51.753  85.305  1.00 18.76 ? 1694 HOH   A O     1 
HETATM 18607 O  O     . HOH   EA 11 .    ? -18.195 79.386  127.253 1.00 25.78 ? 1695 HOH   A O     1 
HETATM 18608 O  O     . HOH   EA 11 .    ? 9.399   57.004  97.452  1.00 30.17 ? 1696 HOH   A O     1 
HETATM 18609 O  O     . HOH   EA 11 .    ? -56.715 46.037  71.079  1.00 22.82 ? 1697 HOH   A O     1 
HETATM 18610 O  O     . HOH   EA 11 .    ? 15.261  83.046  111.184 1.00 26.24 ? 1698 HOH   A O     1 
HETATM 18611 O  O     . HOH   EA 11 .    ? -43.919 25.227  76.259  1.00 38.81 ? 1699 HOH   A O     1 
HETATM 18612 O  O     . HOH   EA 11 .    ? -46.609 67.496  59.658  1.00 27.76 ? 1700 HOH   A O     1 
HETATM 18613 O  O     . HOH   EA 11 .    ? 17.183  80.467  96.710  1.00 34.68 ? 1701 HOH   A O     1 
HETATM 18614 O  O     . HOH   EA 11 .    ? -18.757 69.991  87.735  1.00 27.22 ? 1702 HOH   A O     1 
HETATM 18615 O  O     . HOH   EA 11 .    ? -48.726 83.193  108.979 1.00 34.62 ? 1703 HOH   A O     1 
HETATM 18616 O  O     . HOH   EA 11 .    ? -5.772  76.038  111.181 1.00 19.62 ? 1704 HOH   A O     1 
HETATM 18617 O  O     . HOH   EA 11 .    ? 10.829  57.328  105.766 1.00 28.50 ? 1705 HOH   A O     1 
HETATM 18618 O  O     . HOH   EA 11 .    ? -46.562 81.117  93.340  1.00 41.14 ? 1706 HOH   A O     1 
HETATM 18619 O  O     . HOH   EA 11 .    ? -32.337 59.705  109.465 1.00 29.36 ? 1707 HOH   A O     1 
HETATM 18620 O  O     . HOH   EA 11 .    ? -2.772  85.839  124.531 1.00 38.74 ? 1708 HOH   A O     1 
HETATM 18621 O  O     . HOH   EA 11 .    ? -23.870 60.998  63.344  1.00 36.40 ? 1709 HOH   A O     1 
HETATM 18622 O  O     . HOH   EA 11 .    ? -23.155 86.295  73.767  1.00 39.75 ? 1710 HOH   A O     1 
HETATM 18623 O  O     . HOH   EA 11 .    ? -3.992  72.976  116.962 1.00 27.66 ? 1711 HOH   A O     1 
HETATM 18624 O  O     . HOH   EA 11 .    ? -26.953 53.864  109.593 1.00 30.54 ? 1712 HOH   A O     1 
HETATM 18625 O  O     . HOH   EA 11 .    ? 5.778   62.986  97.181  1.00 20.88 ? 1713 HOH   A O     1 
HETATM 18626 O  O     . HOH   EA 11 .    ? -52.854 63.695  98.383  1.00 21.97 ? 1714 HOH   A O     1 
HETATM 18627 O  O     . HOH   EA 11 .    ? 9.637   68.034  93.990  1.00 37.13 ? 1715 HOH   A O     1 
HETATM 18628 O  O     . HOH   EA 11 .    ? -6.966  41.873  66.294  1.00 26.95 ? 1716 HOH   A O     1 
HETATM 18629 O  O     . HOH   EA 11 .    ? -32.203 93.078  103.835 1.00 31.20 ? 1717 HOH   A O     1 
HETATM 18630 O  O     . HOH   EA 11 .    ? -47.831 57.716  86.240  1.00 17.61 ? 1718 HOH   A O     1 
HETATM 18631 O  O     . HOH   EA 11 .    ? -31.758 88.949  108.601 1.00 31.05 ? 1719 HOH   A O     1 
HETATM 18632 O  O     . HOH   EA 11 .    ? -52.350 54.033  100.226 1.00 27.64 ? 1720 HOH   A O     1 
HETATM 18633 O  O     . HOH   EA 11 .    ? 4.152   57.887  104.886 1.00 21.83 ? 1721 HOH   A O     1 
HETATM 18634 O  O     . HOH   EA 11 .    ? -7.555  42.440  62.093  1.00 28.55 ? 1722 HOH   A O     1 
HETATM 18635 O  O     . HOH   EA 11 .    ? 2.341   85.730  118.050 1.00 28.66 ? 1723 HOH   A O     1 
HETATM 18636 O  O     . HOH   EA 11 .    ? -18.747 61.439  85.315  1.00 25.29 ? 1724 HOH   A O     1 
HETATM 18637 O  O     . HOH   EA 11 .    ? -10.573 86.979  91.599  1.00 36.37 ? 1725 HOH   A O     1 
HETATM 18638 O  O     . HOH   EA 11 .    ? -65.780 58.896  75.896  1.00 22.96 ? 1726 HOH   A O     1 
HETATM 18639 O  O     . HOH   EA 11 .    ? -3.374  57.524  68.105  1.00 34.62 ? 1727 HOH   A O     1 
HETATM 18640 O  O     . HOH   EA 11 .    ? 10.438  63.102  112.984 1.00 31.15 ? 1728 HOH   A O     1 
HETATM 18641 O  O     . HOH   EA 11 .    ? -9.667  74.303  104.145 1.00 22.67 ? 1729 HOH   A O     1 
HETATM 18642 O  O     . HOH   EA 11 .    ? -19.928 52.366  78.151  1.00 31.38 ? 1730 HOH   A O     1 
HETATM 18643 O  O     . HOH   EA 11 .    ? 20.611  83.486  101.003 1.00 40.01 ? 1731 HOH   A O     1 
HETATM 18644 O  O     . HOH   EA 11 .    ? -1.866  85.437  113.025 1.00 27.22 ? 1732 HOH   A O     1 
HETATM 18645 O  O     . HOH   EA 11 .    ? -60.121 47.033  88.643  1.00 26.24 ? 1733 HOH   A O     1 
HETATM 18646 O  O     . HOH   EA 11 .    ? -47.183 60.276  85.132  1.00 17.17 ? 1734 HOH   A O     1 
HETATM 18647 O  O     . HOH   EA 11 .    ? -17.310 80.610  134.708 1.00 41.95 ? 1735 HOH   A O     1 
HETATM 18648 O  O     . HOH   EA 11 .    ? -10.632 67.751  108.075 1.00 19.68 ? 1736 HOH   A O     1 
HETATM 18649 O  O     . HOH   EA 11 .    ? -46.311 32.127  70.297  1.00 34.65 ? 1737 HOH   A O     1 
HETATM 18650 O  O     . HOH   EA 11 .    ? -1.160  83.710  115.195 1.00 31.74 ? 1738 HOH   A O     1 
HETATM 18651 O  O     . HOH   EA 11 .    ? -70.062 61.148  85.396  1.00 35.09 ? 1739 HOH   A O     1 
HETATM 18652 O  O     . HOH   EA 11 .    ? -3.093  89.952  108.739 1.00 25.10 ? 1740 HOH   A O     1 
HETATM 18653 O  O     . HOH   EA 11 .    ? 28.594  64.004  112.549 1.00 30.54 ? 1741 HOH   A O     1 
HETATM 18654 O  O     . HOH   EA 11 .    ? -18.349 97.559  126.804 1.00 45.78 ? 1742 HOH   A O     1 
HETATM 18655 O  O     . HOH   EA 11 .    ? -45.324 65.473  53.026  1.00 38.19 ? 1743 HOH   A O     1 
HETATM 18656 O  O     . HOH   EA 11 .    ? -1.416  76.964  87.799  1.00 29.92 ? 1744 HOH   A O     1 
HETATM 18657 O  O     . HOH   EA 11 .    ? -34.129 69.403  76.219  1.00 31.52 ? 1745 HOH   A O     1 
HETATM 18658 O  O     . HOH   EA 11 .    ? -20.445 81.467  115.789 1.00 21.86 ? 1746 HOH   A O     1 
HETATM 18659 O  O     . HOH   EA 11 .    ? -69.601 64.969  73.969  1.00 28.87 ? 1747 HOH   A O     1 
HETATM 18660 O  O     . HOH   EA 11 .    ? -37.957 65.430  88.306  1.00 33.34 ? 1748 HOH   A O     1 
HETATM 18661 O  O     . HOH   EA 11 .    ? -52.339 72.672  64.329  1.00 28.97 ? 1749 HOH   A O     1 
HETATM 18662 O  O     . HOH   EA 11 .    ? -38.943 52.847  105.372 1.00 36.68 ? 1750 HOH   A O     1 
HETATM 18663 O  O     . HOH   EA 11 .    ? -64.493 59.676  92.803  1.00 33.99 ? 1751 HOH   A O     1 
HETATM 18664 O  O     . HOH   EA 11 .    ? -3.208  90.623  100.659 1.00 24.76 ? 1752 HOH   A O     1 
HETATM 18665 O  O     . HOH   EA 11 .    ? -38.492 73.284  90.028  1.00 35.66 ? 1753 HOH   A O     1 
HETATM 18666 O  O     . HOH   EA 11 .    ? -6.750  70.562  94.099  1.00 25.60 ? 1754 HOH   A O     1 
HETATM 18667 O  O     . HOH   EA 11 .    ? -32.517 92.455  110.223 1.00 34.65 ? 1755 HOH   A O     1 
HETATM 18668 O  O     . HOH   EA 11 .    ? -25.702 63.721  104.665 1.00 22.86 ? 1756 HOH   A O     1 
HETATM 18669 O  O     . HOH   EA 11 .    ? -34.558 66.535  101.551 1.00 24.88 ? 1757 HOH   A O     1 
HETATM 18670 O  O     . HOH   EA 11 .    ? -65.444 71.434  80.450  1.00 29.44 ? 1758 HOH   A O     1 
HETATM 18671 O  O     . HOH   EA 11 .    ? 25.190  77.364  109.127 1.00 34.50 ? 1759 HOH   A O     1 
HETATM 18672 O  O     . HOH   EA 11 .    ? -16.534 55.956  112.181 1.00 35.18 ? 1760 HOH   A O     1 
HETATM 18673 O  O     . HOH   EA 11 .    ? -44.413 73.859  74.941  1.00 26.37 ? 1761 HOH   A O     1 
HETATM 18674 O  O     . HOH   EA 11 .    ? -46.959 48.913  93.074  1.00 18.86 ? 1762 HOH   A O     1 
HETATM 18675 O  O     . HOH   EA 11 .    ? -33.167 98.152  93.222  1.00 47.94 ? 1763 HOH   A O     1 
HETATM 18676 O  O     . HOH   EA 11 .    ? -32.084 52.339  86.007  1.00 28.06 ? 1764 HOH   A O     1 
HETATM 18677 O  O     . HOH   EA 11 .    ? -41.552 71.323  64.139  1.00 27.61 ? 1765 HOH   A O     1 
HETATM 18678 O  O     . HOH   EA 11 .    ? 6.350   90.840  106.465 1.00 31.92 ? 1766 HOH   A O     1 
HETATM 18679 O  O     . HOH   EA 11 .    ? -20.707 70.850  75.654  1.00 26.84 ? 1767 HOH   A O     1 
HETATM 18680 O  O     . HOH   EA 11 .    ? -36.390 95.117  93.813  1.00 33.65 ? 1768 HOH   A O     1 
HETATM 18681 O  O     . HOH   EA 11 .    ? -41.334 27.965  70.103  1.00 37.46 ? 1769 HOH   A O     1 
HETATM 18682 O  O     . HOH   EA 11 .    ? -40.953 90.726  98.578  1.00 28.46 ? 1770 HOH   A O     1 
HETATM 18683 O  O     . HOH   EA 11 .    ? -6.510  53.859  100.141 1.00 41.54 ? 1771 HOH   A O     1 
HETATM 18684 O  O     . HOH   EA 11 .    ? -38.604 32.136  96.874  1.00 38.97 ? 1772 HOH   A O     1 
HETATM 18685 O  O     . HOH   EA 11 .    ? -55.120 29.619  79.919  1.00 33.47 ? 1773 HOH   A O     1 
HETATM 18686 O  O     . HOH   EA 11 .    ? -61.146 52.988  91.232  1.00 27.03 ? 1774 HOH   A O     1 
HETATM 18687 O  O     . HOH   EA 11 .    ? -56.824 31.808  80.368  1.00 34.63 ? 1775 HOH   A O     1 
HETATM 18688 O  O     . HOH   EA 11 .    ? -24.795 88.270  79.157  1.00 28.60 ? 1776 HOH   A O     1 
HETATM 18689 O  O     . HOH   EA 11 .    ? -24.491 92.693  105.198 1.00 36.95 ? 1777 HOH   A O     1 
HETATM 18690 O  O     . HOH   EA 11 .    ? -63.048 54.103  72.250  1.00 29.74 ? 1778 HOH   A O     1 
HETATM 18691 O  O     . HOH   EA 11 .    ? -18.044 57.404  97.226  1.00 21.64 ? 1779 HOH   A O     1 
HETATM 18692 O  O     . HOH   EA 11 .    ? -64.388 44.945  78.080  1.00 35.30 ? 1780 HOH   A O     1 
HETATM 18693 O  O     . HOH   EA 11 .    ? -34.868 95.000  96.197  1.00 29.87 ? 1781 HOH   A O     1 
HETATM 18694 O  O     . HOH   EA 11 .    ? -24.563 88.944  99.806  1.00 23.44 ? 1782 HOH   A O     1 
HETATM 18695 O  O     . HOH   EA 11 .    ? -20.209 66.014  81.078  1.00 27.27 ? 1783 HOH   A O     1 
HETATM 18696 O  O     . HOH   EA 11 .    ? -41.613 70.777  95.241  1.00 26.41 ? 1784 HOH   A O     1 
HETATM 18697 O  O     . HOH   EA 11 .    ? -26.306 50.265  96.553  1.00 28.10 ? 1785 HOH   A O     1 
HETATM 18698 O  O     . HOH   EA 11 .    ? -12.344 77.269  91.010  1.00 17.61 ? 1786 HOH   A O     1 
HETATM 18699 O  O     . HOH   EA 11 .    ? -46.632 82.334  101.428 1.00 25.84 ? 1787 HOH   A O     1 
HETATM 18700 O  O     . HOH   EA 11 .    ? -42.312 47.544  81.134  1.00 20.97 ? 1788 HOH   A O     1 
HETATM 18701 O  O     . HOH   EA 11 .    ? 14.978  75.903  94.098  1.00 36.36 ? 1789 HOH   A O     1 
HETATM 18702 O  O     . HOH   EA 11 .    ? -1.401  79.380  99.903  1.00 27.09 ? 1790 HOH   A O     1 
HETATM 18703 O  O     . HOH   EA 11 .    ? -51.633 72.976  105.515 1.00 30.15 ? 1791 HOH   A O     1 
HETATM 18704 O  O     . HOH   EA 11 .    ? -38.995 88.766  90.659  1.00 35.58 ? 1792 HOH   A O     1 
HETATM 18705 O  O     . HOH   EA 11 .    ? -37.959 40.974  71.524  1.00 26.94 ? 1793 HOH   A O     1 
HETATM 18706 O  O     . HOH   EA 11 .    ? -55.041 47.721  69.778  1.00 24.08 ? 1794 HOH   A O     1 
HETATM 18707 O  O     . HOH   EA 11 .    ? -41.653 29.601  89.195  1.00 38.23 ? 1795 HOH   A O     1 
HETATM 18708 O  O     . HOH   EA 11 .    ? -4.000  76.139  124.535 1.00 29.66 ? 1796 HOH   A O     1 
HETATM 18709 O  O     . HOH   EA 11 .    ? -12.514 89.861  101.585 1.00 32.46 ? 1797 HOH   A O     1 
HETATM 18710 O  O     . HOH   EA 11 .    ? -46.085 65.076  107.065 1.00 36.03 ? 1798 HOH   A O     1 
HETATM 18711 O  O     . HOH   EA 11 .    ? -31.782 82.400  75.332  1.00 23.22 ? 1799 HOH   A O     1 
HETATM 18712 O  O     . HOH   EA 11 .    ? -22.408 98.520  100.396 1.00 36.68 ? 1800 HOH   A O     1 
HETATM 18713 O  O     . HOH   EA 11 .    ? -3.690  57.611  72.760  1.00 24.76 ? 1801 HOH   A O     1 
HETATM 18714 O  O     . HOH   EA 11 .    ? -43.079 49.971  55.639  1.00 33.15 ? 1802 HOH   A O     1 
HETATM 18715 O  O     . HOH   EA 11 .    ? -28.874 76.549  72.826  1.00 29.50 ? 1803 HOH   A O     1 
HETATM 18716 O  O     . HOH   EA 11 .    ? -44.073 55.780  94.999  1.00 17.40 ? 1804 HOH   A O     1 
HETATM 18717 O  O     . HOH   EA 11 .    ? -65.117 54.567  90.871  1.00 33.22 ? 1805 HOH   A O     1 
HETATM 18718 O  O     . HOH   EA 11 .    ? -0.454  83.737  109.581 1.00 27.82 ? 1806 HOH   A O     1 
HETATM 18719 O  O     . HOH   EA 11 .    ? -8.207  59.996  94.112  1.00 36.30 ? 1807 HOH   A O     1 
HETATM 18720 O  O     . HOH   EA 11 .    ? -27.989 60.363  124.970 1.00 39.07 ? 1808 HOH   A O     1 
HETATM 18721 O  O     . HOH   EA 11 .    ? -30.966 60.899  90.496  1.00 23.61 ? 1809 HOH   A O     1 
HETATM 18722 O  O     . HOH   EA 11 .    ? -30.546 91.140  107.086 1.00 28.37 ? 1810 HOH   A O     1 
HETATM 18723 O  O     . HOH   EA 11 .    ? -34.125 75.488  83.115  1.00 27.65 ? 1811 HOH   A O     1 
HETATM 18724 O  O     . HOH   EA 11 .    ? -0.135  86.545  105.807 1.00 26.06 ? 1812 HOH   A O     1 
HETATM 18725 O  O     . HOH   EA 11 .    ? -31.637 59.079  63.161  1.00 32.28 ? 1813 HOH   A O     1 
HETATM 18726 O  O     . HOH   EA 11 .    ? -2.877  62.474  77.552  1.00 23.47 ? 1814 HOH   A O     1 
HETATM 18727 O  O     . HOH   EA 11 .    ? -46.424 54.334  89.653  1.00 19.46 ? 1815 HOH   A O     1 
HETATM 18728 O  O     . HOH   EA 11 .    ? -57.394 57.955  101.272 1.00 25.53 ? 1816 HOH   A O     1 
HETATM 18729 O  O     . HOH   EA 11 .    ? -8.614  60.051  107.049 1.00 21.54 ? 1817 HOH   A O     1 
HETATM 18730 O  O     . HOH   EA 11 .    ? -30.024 62.927  91.854  1.00 35.17 ? 1818 HOH   A O     1 
HETATM 18731 O  O     . HOH   EA 11 .    ? -59.282 51.972  66.117  1.00 21.06 ? 1819 HOH   A O     1 
HETATM 18732 O  O     . HOH   EA 11 .    ? 7.407   57.453  112.294 1.00 33.17 ? 1820 HOH   A O     1 
HETATM 18733 O  O     . HOH   EA 11 .    ? -57.467 64.765  91.097  1.00 31.70 ? 1821 HOH   A O     1 
HETATM 18734 O  O     . HOH   EA 11 .    ? -14.028 84.960  77.017  1.00 33.33 ? 1822 HOH   A O     1 
HETATM 18735 O  O     . HOH   EA 11 .    ? -29.578 83.404  101.260 1.00 28.73 ? 1823 HOH   A O     1 
HETATM 18736 O  O     . HOH   EA 11 .    ? -47.447 70.655  111.141 1.00 33.93 ? 1824 HOH   A O     1 
HETATM 18737 O  O     . HOH   EA 11 .    ? -30.929 91.471  80.619  1.00 33.48 ? 1825 HOH   A O     1 
HETATM 18738 O  O     . HOH   EA 11 .    ? -9.060  87.317  88.923  1.00 43.37 ? 1826 HOH   A O     1 
HETATM 18739 O  O     . HOH   EA 11 .    ? -14.759 67.241  73.090  1.00 24.65 ? 1827 HOH   A O     1 
HETATM 18740 O  O     . HOH   EA 11 .    ? 10.617  67.225  111.847 1.00 34.90 ? 1828 HOH   A O     1 
HETATM 18741 O  O     . HOH   EA 11 .    ? -53.801 55.583  68.406  1.00 18.74 ? 1829 HOH   A O     1 
HETATM 18742 O  O     . HOH   EA 11 .    ? -35.389 73.190  83.578  1.00 25.29 ? 1830 HOH   A O     1 
HETATM 18743 O  O     . HOH   EA 11 .    ? -61.609 70.383  82.940  1.00 23.44 ? 1831 HOH   A O     1 
HETATM 18744 O  O     . HOH   EA 11 .    ? 17.161  69.163  117.799 1.00 29.20 ? 1832 HOH   A O     1 
HETATM 18745 O  O     . HOH   EA 11 .    ? -45.284 62.587  92.581  1.00 17.97 ? 1833 HOH   A O     1 
HETATM 18746 O  O     . HOH   EA 11 .    ? -48.197 75.146  95.493  1.00 23.33 ? 1834 HOH   A O     1 
HETATM 18747 O  O     . HOH   EA 11 .    ? -42.672 28.696  86.052  1.00 40.87 ? 1835 HOH   A O     1 
HETATM 18748 O  O     . HOH   EA 11 .    ? -21.995 67.231  73.960  1.00 38.26 ? 1836 HOH   A O     1 
HETATM 18749 O  O     . HOH   EA 11 .    ? -13.132 55.229  103.434 1.00 34.31 ? 1837 HOH   A O     1 
HETATM 18750 O  O     . HOH   EA 11 .    ? -49.498 75.947  101.522 1.00 26.37 ? 1838 HOH   A O     1 
HETATM 18751 O  O     . HOH   EA 11 .    ? -45.955 72.613  64.272  1.00 19.70 ? 1839 HOH   A O     1 
HETATM 18752 O  O     . HOH   EA 11 .    ? -33.454 45.739  84.612  1.00 26.40 ? 1840 HOH   A O     1 
HETATM 18753 O  O     . HOH   EA 11 .    ? -54.437 47.435  67.307  1.00 33.53 ? 1841 HOH   A O     1 
HETATM 18754 O  O     . HOH   EA 11 .    ? -37.069 45.410  104.123 1.00 34.23 ? 1842 HOH   A O     1 
HETATM 18755 O  O     . HOH   EA 11 .    ? 20.619  62.062  98.838  1.00 23.96 ? 1843 HOH   A O     1 
HETATM 18756 O  O     . HOH   EA 11 .    ? -28.407 61.943  116.725 1.00 24.28 ? 1844 HOH   A O     1 
HETATM 18757 O  O     . HOH   EA 11 .    ? -46.039 29.435  89.378  1.00 37.79 ? 1845 HOH   A O     1 
HETATM 18758 O  O     . HOH   EA 11 .    ? -47.787 59.162  82.764  1.00 16.12 ? 1846 HOH   A O     1 
HETATM 18759 O  O     . HOH   EA 11 .    ? -22.566 74.970  99.620  1.00 27.50 ? 1847 HOH   A O     1 
HETATM 18760 O  O     . HOH   EA 11 .    ? -49.088 47.673  97.421  1.00 25.23 ? 1848 HOH   A O     1 
HETATM 18761 O  O     . HOH   EA 11 .    ? -23.342 54.303  101.261 1.00 29.31 ? 1849 HOH   A O     1 
HETATM 18762 O  O     . HOH   EA 11 .    ? -36.821 51.839  60.934  1.00 31.70 ? 1850 HOH   A O     1 
HETATM 18763 O  O     . HOH   EA 11 .    ? 12.736  67.343  93.246  1.00 30.44 ? 1851 HOH   A O     1 
HETATM 18764 O  O     . HOH   EA 11 .    ? 6.803   61.111  103.186 1.00 19.34 ? 1852 HOH   A O     1 
HETATM 18765 O  O     . HOH   EA 11 .    ? -57.193 60.234  61.001  1.00 20.51 ? 1853 HOH   A O     1 
HETATM 18766 O  O     . HOH   EA 11 .    ? 14.030  82.132  114.037 1.00 24.64 ? 1854 HOH   A O     1 
HETATM 18767 O  O     . HOH   EA 11 .    ? -0.249  77.280  117.090 1.00 26.78 ? 1855 HOH   A O     1 
HETATM 18768 O  O     . HOH   EA 11 .    ? -54.336 37.477  89.199  1.00 32.35 ? 1856 HOH   A O     1 
HETATM 18769 O  O     . HOH   EA 11 .    ? -17.575 85.546  77.536  1.00 31.67 ? 1857 HOH   A O     1 
HETATM 18770 O  O     . HOH   EA 11 .    ? -8.029  77.163  92.043  1.00 23.99 ? 1858 HOH   A O     1 
HETATM 18771 O  O     . HOH   EA 11 .    ? -25.802 50.669  105.161 1.00 37.12 ? 1859 HOH   A O     1 
HETATM 18772 O  O     . HOH   EA 11 .    ? -26.715 89.253  77.572  1.00 33.54 ? 1860 HOH   A O     1 
HETATM 18773 O  O     . HOH   EA 11 .    ? -19.549 84.987  75.449  1.00 34.51 ? 1861 HOH   A O     1 
HETATM 18774 O  O     . HOH   EA 11 .    ? -21.027 54.947  94.902  1.00 36.99 ? 1862 HOH   A O     1 
HETATM 18775 O  O     . HOH   EA 11 .    ? -66.222 61.579  75.806  1.00 19.86 ? 1863 HOH   A O     1 
HETATM 18776 O  O     . HOH   EA 11 .    ? -43.139 77.348  67.902  1.00 29.62 ? 1864 HOH   A O     1 
HETATM 18777 O  O     . HOH   EA 11 .    ? -5.774  65.137  114.234 1.00 24.60 ? 1865 HOH   A O     1 
HETATM 18778 O  O     . HOH   EA 11 .    ? -46.496 66.507  93.822  1.00 22.04 ? 1866 HOH   A O     1 
HETATM 18779 O  O     . HOH   EA 11 .    ? -1.493  77.800  121.273 1.00 29.00 ? 1867 HOH   A O     1 
HETATM 18780 O  O     . HOH   EA 11 .    ? -6.460  70.627  104.352 1.00 29.77 ? 1868 HOH   A O     1 
HETATM 18781 O  O     . HOH   EA 11 .    ? -18.869 59.621  69.998  1.00 22.91 ? 1869 HOH   A O     1 
HETATM 18782 O  O     . HOH   EA 11 .    ? -52.252 61.995  94.748  1.00 22.00 ? 1870 HOH   A O     1 
HETATM 18783 O  O     . HOH   EA 11 .    ? -4.289  54.802  61.395  1.00 34.83 ? 1871 HOH   A O     1 
HETATM 18784 O  O     . HOH   EA 11 .    ? -42.418 77.842  75.813  1.00 27.41 ? 1872 HOH   A O     1 
HETATM 18785 O  O     . HOH   EA 11 .    ? -24.979 82.659  72.569  1.00 33.16 ? 1873 HOH   A O     1 
HETATM 18786 O  O     . HOH   EA 11 .    ? 22.875  76.170  114.679 1.00 28.22 ? 1874 HOH   A O     1 
HETATM 18787 O  O     . HOH   EA 11 .    ? -31.931 75.176  126.315 1.00 29.38 ? 1875 HOH   A O     1 
HETATM 18788 O  O     . HOH   EA 11 .    ? -8.872  78.252  131.481 1.00 38.83 ? 1876 HOH   A O     1 
HETATM 18789 O  O     . HOH   EA 11 .    ? -38.312 61.506  91.793  1.00 20.42 ? 1877 HOH   A O     1 
HETATM 18790 O  O     . HOH   EA 11 .    ? 22.956  72.952  98.299  1.00 32.54 ? 1878 HOH   A O     1 
HETATM 18791 O  O     . HOH   EA 11 .    ? -31.687 88.531  95.109  1.00 23.31 ? 1879 HOH   A O     1 
HETATM 18792 O  O     . HOH   EA 11 .    ? -7.079  62.371  107.055 1.00 22.11 ? 1880 HOH   A O     1 
HETATM 18793 O  O     . HOH   EA 11 .    ? -62.001 61.763  68.218  1.00 25.68 ? 1881 HOH   A O     1 
HETATM 18794 O  O     . HOH   EA 11 .    ? -1.749  77.950  105.315 1.00 22.50 ? 1882 HOH   A O     1 
HETATM 18795 O  O     . HOH   EA 11 .    ? -59.552 40.207  78.690  1.00 39.53 ? 1883 HOH   A O     1 
HETATM 18796 O  O     . HOH   EA 11 .    ? -9.443  56.024  82.532  1.00 34.71 ? 1884 HOH   A O     1 
HETATM 18797 O  O     . HOH   EA 11 .    ? 5.221   55.169  96.865  1.00 27.47 ? 1885 HOH   A O     1 
HETATM 18798 O  O     . HOH   EA 11 .    ? -50.057 56.755  71.729  1.00 26.66 ? 1886 HOH   A O     1 
HETATM 18799 O  O     . HOH   EA 11 .    ? -36.824 68.336  83.267  1.00 30.24 ? 1887 HOH   A O     1 
HETATM 18800 O  O     . HOH   EA 11 .    ? -49.974 27.336  77.221  1.00 34.83 ? 1888 HOH   A O     1 
HETATM 18801 O  O     . HOH   EA 11 .    ? -63.644 70.954  70.824  1.00 29.08 ? 1889 HOH   A O     1 
HETATM 18802 O  O     . HOH   EA 11 .    ? -34.573 77.511  84.903  1.00 25.59 ? 1890 HOH   A O     1 
HETATM 18803 O  O     . HOH   EA 11 .    ? -25.072 79.264  94.999  1.00 22.78 ? 1891 HOH   A O     1 
HETATM 18804 O  O     . HOH   EA 11 .    ? -35.881 37.648  83.324  1.00 35.78 ? 1892 HOH   A O     1 
HETATM 18805 O  O     . HOH   EA 11 .    ? -59.558 38.394  82.616  1.00 33.10 ? 1893 HOH   A O     1 
HETATM 18806 O  O     . HOH   EA 11 .    ? -22.688 58.999  75.703  1.00 30.29 ? 1894 HOH   A O     1 
HETATM 18807 O  O     . HOH   EA 11 .    ? -50.213 37.852  99.658  1.00 35.17 ? 1895 HOH   A O     1 
HETATM 18808 O  O     . HOH   EA 11 .    ? -46.120 24.386  82.496  1.00 40.34 ? 1896 HOH   A O     1 
HETATM 18809 O  O     . HOH   EA 11 .    ? -0.642  70.093  96.017  1.00 32.68 ? 1897 HOH   A O     1 
HETATM 18810 O  O     . HOH   EA 11 .    ? -18.362 60.814  66.829  1.00 28.88 ? 1898 HOH   A O     1 
HETATM 18811 O  O     . HOH   EA 11 .    ? -27.054 64.856  100.132 1.00 25.32 ? 1899 HOH   A O     1 
HETATM 18812 O  O     . HOH   EA 11 .    ? -41.876 67.863  91.149  1.00 20.56 ? 1900 HOH   A O     1 
HETATM 18813 O  O     . HOH   EA 11 .    ? -33.912 90.576  122.096 1.00 33.02 ? 1901 HOH   A O     1 
HETATM 18814 O  O     . HOH   EA 11 .    ? -22.675 83.432  91.423  1.00 20.79 ? 1902 HOH   A O     1 
HETATM 18815 O  O     . HOH   EA 11 .    ? 2.536   84.071  101.653 1.00 23.63 ? 1903 HOH   A O     1 
HETATM 18816 O  O     . HOH   EA 11 .    ? -45.675 78.295  96.045  1.00 20.70 ? 1904 HOH   A O     1 
HETATM 18817 O  O     . HOH   EA 11 .    ? -35.163 40.413  91.994  1.00 25.53 ? 1905 HOH   A O     1 
HETATM 18818 O  O     . HOH   EA 11 .    ? -53.533 39.883  66.266  1.00 38.36 ? 1906 HOH   A O     1 
HETATM 18819 O  O     . HOH   EA 11 .    ? 3.022   64.956  113.047 1.00 30.69 ? 1907 HOH   A O     1 
HETATM 18820 O  O     . HOH   EA 11 .    ? -16.007 47.067  53.635  1.00 33.93 ? 1908 HOH   A O     1 
HETATM 18821 O  O     . HOH   EA 11 .    ? -34.058 56.424  105.365 1.00 25.35 ? 1909 HOH   A O     1 
HETATM 18822 O  O     . HOH   EA 11 .    ? -33.078 77.961  74.041  1.00 27.76 ? 1910 HOH   A O     1 
HETATM 18823 O  O     . HOH   EA 11 .    ? -59.948 50.260  90.831  1.00 35.32 ? 1911 HOH   A O     1 
HETATM 18824 O  O     . HOH   EA 11 .    ? -30.944 74.116  87.927  1.00 34.44 ? 1912 HOH   A O     1 
HETATM 18825 O  O     . HOH   EA 11 .    ? -27.559 70.875  90.048  1.00 28.97 ? 1913 HOH   A O     1 
HETATM 18826 O  O     . HOH   EA 11 .    ? -25.554 94.155  78.274  1.00 35.23 ? 1914 HOH   A O     1 
HETATM 18827 O  O     . HOH   EA 11 .    ? -58.110 57.870  62.992  1.00 20.20 ? 1915 HOH   A O     1 
HETATM 18828 O  O     . HOH   EA 11 .    ? -54.111 79.340  81.567  1.00 37.30 ? 1916 HOH   A O     1 
HETATM 18829 O  O     . HOH   EA 11 .    ? -30.224 81.219  122.899 1.00 31.57 ? 1917 HOH   A O     1 
HETATM 18830 O  O     . HOH   EA 11 .    ? -65.708 69.057  68.896  1.00 38.70 ? 1918 HOH   A O     1 
HETATM 18831 O  O     . HOH   EA 11 .    ? -4.016  72.989  77.066  1.00 30.40 ? 1919 HOH   A O     1 
HETATM 18832 O  O     . HOH   EA 11 .    ? -46.186 56.026  87.386  1.00 16.13 ? 1920 HOH   A O     1 
HETATM 18833 O  O     . HOH   EA 11 .    ? 16.321  65.084  119.794 1.00 31.80 ? 1921 HOH   A O     1 
HETATM 18834 O  O     . HOH   EA 11 .    ? -13.920 41.930  71.198  1.00 31.11 ? 1922 HOH   A O     1 
HETATM 18835 O  O     . HOH   EA 11 .    ? -19.870 86.680  91.564  1.00 23.00 ? 1923 HOH   A O     1 
HETATM 18836 O  O     . HOH   EA 11 .    ? -41.614 64.637  58.473  1.00 29.67 ? 1924 HOH   A O     1 
HETATM 18837 O  O     . HOH   EA 11 .    ? -7.501  50.787  53.089  1.00 29.75 ? 1925 HOH   A O     1 
HETATM 18838 O  O     . HOH   EA 11 .    ? -17.130 53.222  76.220  1.00 32.22 ? 1926 HOH   A O     1 
HETATM 18839 O  O     . HOH   EA 11 .    ? -47.998 55.081  58.154  1.00 33.50 ? 1927 HOH   A O     1 
HETATM 18840 O  O     . HOH   EA 11 .    ? -43.824 59.453  87.540  1.00 17.37 ? 1928 HOH   A O     1 
HETATM 18841 O  O     . HOH   EA 11 .    ? 19.324  82.049  113.131 1.00 29.73 ? 1929 HOH   A O     1 
HETATM 18842 O  O     . HOH   EA 11 .    ? -50.181 66.327  106.320 1.00 30.47 ? 1930 HOH   A O     1 
HETATM 18843 O  O     . HOH   EA 11 .    ? 4.165   60.449  101.027 1.00 26.06 ? 1931 HOH   A O     1 
HETATM 18844 O  O     . HOH   EA 11 .    ? -44.667 85.697  99.736  1.00 37.55 ? 1932 HOH   A O     1 
HETATM 18845 O  O     . HOH   EA 11 .    ? -1.477  79.998  88.089  1.00 38.25 ? 1933 HOH   A O     1 
HETATM 18846 O  O     . HOH   EA 11 .    ? -3.011  77.811  101.343 1.00 27.43 ? 1934 HOH   A O     1 
HETATM 18847 O  O     . HOH   EA 11 .    ? -59.475 62.957  77.596  1.00 23.94 ? 1935 HOH   A O     1 
HETATM 18848 O  O     . HOH   EA 11 .    ? -5.412  67.911  77.904  1.00 34.71 ? 1936 HOH   A O     1 
HETATM 18849 O  O     . HOH   EA 11 .    ? -22.824 55.184  88.591  1.00 37.50 ? 1937 HOH   A O     1 
HETATM 18850 O  O     . HOH   EA 11 .    ? -35.129 63.165  115.851 1.00 34.72 ? 1938 HOH   A O     1 
HETATM 18851 O  O     . HOH   EA 11 .    ? -14.785 89.890  98.501  1.00 37.72 ? 1939 HOH   A O     1 
HETATM 18852 O  O     . HOH   EA 11 .    ? -64.487 43.013  86.189  1.00 29.62 ? 1940 HOH   A O     1 
HETATM 18853 O  O     . HOH   EA 11 .    ? -49.742 48.993  99.784  1.00 26.03 ? 1941 HOH   A O     1 
HETATM 18854 O  O     . HOH   EA 11 .    ? -22.269 95.803  129.641 1.00 44.53 ? 1942 HOH   A O     1 
HETATM 18855 O  O     . HOH   EA 11 .    ? -19.223 90.864  76.952  1.00 33.16 ? 1943 HOH   A O     1 
HETATM 18856 O  O     . HOH   EA 11 .    ? -33.754 52.566  82.035  1.00 37.35 ? 1944 HOH   A O     1 
HETATM 18857 O  O     . HOH   EA 11 .    ? -58.755 42.527  89.429  1.00 33.86 ? 1945 HOH   A O     1 
HETATM 18858 O  O     . HOH   EA 11 .    ? -19.353 90.769  97.598  1.00 34.31 ? 1946 HOH   A O     1 
HETATM 18859 O  O     . HOH   EA 11 .    ? -1.384  58.193  96.470  1.00 34.39 ? 1947 HOH   A O     1 
HETATM 18860 O  O     . HOH   EA 11 .    ? 18.327  57.328  105.040 1.00 27.73 ? 1948 HOH   A O     1 
HETATM 18861 O  O     . HOH   EA 11 .    ? -37.947 67.608  98.059  1.00 27.89 ? 1949 HOH   A O     1 
HETATM 18862 O  O     . HOH   EA 11 .    ? -26.877 51.892  98.612  1.00 22.92 ? 1950 HOH   A O     1 
HETATM 18863 O  O     . HOH   EA 11 .    ? -36.505 73.194  125.525 1.00 42.47 ? 1951 HOH   A O     1 
HETATM 18864 O  O     . HOH   EA 11 .    ? -62.279 54.911  63.362  1.00 35.69 ? 1952 HOH   A O     1 
HETATM 18865 O  O     . HOH   EA 11 .    ? -53.544 68.784  93.500  1.00 26.09 ? 1953 HOH   A O     1 
HETATM 18866 O  O     . HOH   EA 11 .    ? -40.718 80.099  87.597  1.00 21.78 ? 1954 HOH   A O     1 
HETATM 18867 O  O     . HOH   EA 11 .    ? -41.838 55.502  104.805 1.00 38.36 ? 1955 HOH   A O     1 
HETATM 18868 O  O     . HOH   EA 11 .    ? -20.357 89.082  102.431 1.00 40.50 ? 1956 HOH   A O     1 
HETATM 18869 O  O     . HOH   EA 11 .    ? -54.269 62.482  103.389 1.00 41.93 ? 1957 HOH   A O     1 
HETATM 18870 O  O     . HOH   EA 11 .    ? -45.131 57.486  102.063 1.00 29.12 ? 1958 HOH   A O     1 
HETATM 18871 O  O     . HOH   EA 11 .    ? 1.291   66.521  96.546  1.00 23.95 ? 1959 HOH   A O     1 
HETATM 18872 O  O     . HOH   EA 11 .    ? -38.001 72.897  87.546  1.00 33.31 ? 1960 HOH   A O     1 
HETATM 18873 O  O     . HOH   EA 11 .    ? 10.457  81.308  125.207 1.00 30.92 ? 1961 HOH   A O     1 
HETATM 18874 O  O     . HOH   EA 11 .    ? -48.360 56.438  56.152  1.00 36.18 ? 1962 HOH   A O     1 
HETATM 18875 O  O     . HOH   EA 11 .    ? -49.733 72.340  101.144 1.00 24.39 ? 1963 HOH   A O     1 
HETATM 18876 O  O     . HOH   EA 11 .    ? -44.904 59.437  55.113  1.00 35.90 ? 1964 HOH   A O     1 
HETATM 18877 O  O     . HOH   EA 11 .    ? -38.268 50.448  98.238  1.00 26.97 ? 1965 HOH   A O     1 
HETATM 18878 O  O     . HOH   EA 11 .    ? -39.965 47.126  106.516 1.00 38.51 ? 1966 HOH   A O     1 
HETATM 18879 O  O     . HOH   EA 11 .    ? -22.794 53.783  92.559  1.00 30.24 ? 1967 HOH   A O     1 
HETATM 18880 O  O     . HOH   EA 11 .    ? -40.513 81.733  110.674 1.00 29.26 ? 1968 HOH   A O     1 
HETATM 18881 O  O     . HOH   EA 11 .    ? -39.208 76.635  93.221  1.00 26.44 ? 1969 HOH   A O     1 
HETATM 18882 O  O     . HOH   EA 11 .    ? 28.711  74.273  107.358 1.00 42.82 ? 1970 HOH   A O     1 
HETATM 18883 O  O     . HOH   EA 11 .    ? -53.483 49.429  60.262  1.00 31.16 ? 1971 HOH   A O     1 
HETATM 18884 O  O     . HOH   EA 11 .    ? 11.052  61.087  115.200 1.00 34.64 ? 1972 HOH   A O     1 
HETATM 18885 O  O     . HOH   EA 11 .    ? -33.507 83.758  123.273 1.00 30.12 ? 1973 HOH   A O     1 
HETATM 18886 O  O     . HOH   EA 11 .    ? -4.483  59.114  118.384 1.00 21.66 ? 1974 HOH   A O     1 
HETATM 18887 O  O     . HOH   EA 11 .    ? -19.585 93.981  111.533 1.00 34.97 ? 1975 HOH   A O     1 
HETATM 18888 O  O     . HOH   EA 11 .    ? 25.633  64.383  102.428 1.00 28.07 ? 1976 HOH   A O     1 
HETATM 18889 O  O     . HOH   EA 11 .    ? -10.198 63.661  115.627 1.00 22.43 ? 1977 HOH   A O     1 
HETATM 18890 O  O     . HOH   EA 11 .    ? 2.509   76.509  116.900 1.00 26.92 ? 1978 HOH   A O     1 
HETATM 18891 O  O     . HOH   EA 11 .    ? -32.242 64.548  121.952 1.00 27.71 ? 1979 HOH   A O     1 
HETATM 18892 O  O     . HOH   EA 11 .    ? -48.827 61.620  56.715  1.00 23.18 ? 1980 HOH   A O     1 
HETATM 18893 O  O     . HOH   EA 11 .    ? 32.533  72.107  107.739 1.00 45.09 ? 1981 HOH   A O     1 
HETATM 18894 O  O     . HOH   EA 11 .    ? -30.437 50.271  104.706 1.00 30.63 ? 1982 HOH   A O     1 
HETATM 18895 O  O     . HOH   EA 11 .    ? -45.893 33.465  82.542  1.00 34.08 ? 1983 HOH   A O     1 
HETATM 18896 O  O     . HOH   EA 11 .    ? -8.249  81.922  104.963 1.00 24.62 ? 1984 HOH   A O     1 
HETATM 18897 O  O     . HOH   EA 11 .    ? -15.914 68.035  96.669  1.00 17.47 ? 1985 HOH   A O     1 
HETATM 18898 O  O     . HOH   EA 11 .    ? -8.129  87.550  93.191  1.00 42.24 ? 1986 HOH   A O     1 
HETATM 18899 O  O     . HOH   EA 11 .    ? 23.566  58.459  103.506 1.00 32.65 ? 1987 HOH   A O     1 
HETATM 18900 O  O     . HOH   EA 11 .    ? -1.119  70.153  116.317 1.00 27.40 ? 1988 HOH   A O     1 
HETATM 18901 O  O     . HOH   EA 11 .    ? -38.373 70.397  81.751  1.00 22.95 ? 1989 HOH   A O     1 
HETATM 18902 O  O     . HOH   EA 11 .    ? -25.281 59.305  114.357 1.00 26.25 ? 1990 HOH   A O     1 
HETATM 18903 O  O     . HOH   EA 11 .    ? -67.774 37.446  75.515  1.00 39.81 ? 1991 HOH   A O     1 
HETATM 18904 O  O     . HOH   EA 11 .    ? -30.468 91.385  111.475 1.00 35.06 ? 1992 HOH   A O     1 
HETATM 18905 O  O     . HOH   EA 11 .    ? -27.243 61.952  88.997  1.00 23.15 ? 1993 HOH   A O     1 
HETATM 18906 O  O     . HOH   EA 11 .    ? -59.020 58.430  76.874  1.00 19.14 ? 1994 HOH   A O     1 
HETATM 18907 O  O     . HOH   EA 11 .    ? -21.740 52.779  104.346 1.00 37.78 ? 1995 HOH   A O     1 
HETATM 18908 O  O     . HOH   EA 11 .    ? -18.344 68.853  104.539 1.00 21.59 ? 1996 HOH   A O     1 
HETATM 18909 O  O     . HOH   EA 11 .    ? -32.973 92.297  106.779 1.00 34.54 ? 1997 HOH   A O     1 
HETATM 18910 O  O     . HOH   EA 11 .    ? -11.534 59.604  84.777  1.00 33.77 ? 1998 HOH   A O     1 
HETATM 18911 O  O     . HOH   EA 11 .    ? -41.575 88.761  96.727  1.00 28.73 ? 1999 HOH   A O     1 
HETATM 18912 O  O     . HOH   EA 11 .    ? -56.266 68.842  100.051 1.00 37.79 ? 2000 HOH   A O     1 
HETATM 18913 O  O     . HOH   EA 11 .    ? -60.947 68.766  68.664  1.00 25.53 ? 2001 HOH   A O     1 
HETATM 18914 O  O     . HOH   EA 11 .    ? -14.091 58.273  109.995 1.00 36.97 ? 2002 HOH   A O     1 
HETATM 18915 O  O     . HOH   EA 11 .    ? -44.710 61.087  85.479  1.00 18.45 ? 2003 HOH   A O     1 
HETATM 18916 O  O     . HOH   EA 11 .    ? 18.937  73.237  118.069 1.00 26.92 ? 2004 HOH   A O     1 
HETATM 18917 O  O     . HOH   EA 11 .    ? -7.218  37.921  63.730  1.00 35.18 ? 2005 HOH   A O     1 
HETATM 18918 O  O     . HOH   EA 11 .    ? -0.158  52.753  63.073  1.00 28.30 ? 2006 HOH   A O     1 
HETATM 18919 O  O     . HOH   EA 11 .    ? -9.740  82.240  78.007  1.00 43.43 ? 2007 HOH   A O     1 
HETATM 18920 O  O     . HOH   EA 11 .    ? -19.222 91.865  105.039 1.00 34.21 ? 2008 HOH   A O     1 
HETATM 18921 O  O     . HOH   EA 11 .    ? -19.791 79.008  114.902 1.00 21.63 ? 2009 HOH   A O     1 
HETATM 18922 O  O     . HOH   EA 11 .    ? -20.782 58.182  97.263  1.00 25.41 ? 2010 HOH   A O     1 
HETATM 18923 O  O     . HOH   EA 11 .    ? -28.010 69.398  85.874  1.00 32.46 ? 2011 HOH   A O     1 
HETATM 18924 O  O     . HOH   EA 11 .    ? -14.937 59.023  126.648 1.00 29.16 ? 2012 HOH   A O     1 
HETATM 18925 O  O     . HOH   EA 11 .    ? -28.702 57.107  59.590  1.00 40.58 ? 2013 HOH   A O     1 
HETATM 18926 O  O     . HOH   EA 11 .    ? -13.862 95.291  119.602 1.00 34.59 ? 2014 HOH   A O     1 
HETATM 18927 O  O     . HOH   EA 11 .    ? 2.873   74.338  109.399 1.00 25.86 ? 2015 HOH   A O     1 
HETATM 18928 O  O     . HOH   EA 11 .    ? -26.431 84.401  74.144  1.00 35.78 ? 2016 HOH   A O     1 
HETATM 18929 O  O     . HOH   EA 11 .    ? -7.860  75.024  70.349  1.00 32.78 ? 2017 HOH   A O     1 
HETATM 18930 O  O     . HOH   EA 11 .    ? -51.741 87.112  103.505 1.00 39.84 ? 2018 HOH   A O     1 
HETATM 18931 O  O     . HOH   EA 11 .    ? 14.356  78.500  120.719 1.00 30.65 ? 2019 HOH   A O     1 
HETATM 18932 O  O     . HOH   EA 11 .    ? -3.133  87.639  104.893 1.00 28.48 ? 2020 HOH   A O     1 
HETATM 18933 O  O     . HOH   EA 11 .    ? 2.756   77.899  98.064  1.00 24.40 ? 2021 HOH   A O     1 
HETATM 18934 O  O     . HOH   EA 11 .    ? -56.109 25.397  88.377  1.00 38.22 ? 2022 HOH   A O     1 
HETATM 18935 O  O     . HOH   EA 11 .    ? -34.153 96.554  112.280 1.00 42.59 ? 2023 HOH   A O     1 
HETATM 18936 O  O     . HOH   EA 11 .    ? -25.265 88.353  116.085 1.00 23.99 ? 2024 HOH   A O     1 
HETATM 18937 O  O     . HOH   EA 11 .    ? -11.446 43.586  74.133  1.00 27.36 ? 2025 HOH   A O     1 
HETATM 18938 O  O     . HOH   EA 11 .    ? -28.401 76.633  103.047 1.00 36.65 ? 2026 HOH   A O     1 
HETATM 18939 O  O     . HOH   EA 11 .    ? -42.196 56.718  89.416  1.00 18.09 ? 2027 HOH   A O     1 
HETATM 18940 O  O     . HOH   EA 11 .    ? -1.954  77.979  75.766  1.00 29.67 ? 2028 HOH   A O     1 
HETATM 18941 O  O     . HOH   EA 11 .    ? -63.798 47.655  73.917  1.00 37.67 ? 2029 HOH   A O     1 
HETATM 18942 O  O     . HOH   EA 11 .    ? -24.755 69.224  74.517  1.00 29.94 ? 2030 HOH   A O     1 
HETATM 18943 O  O     . HOH   EA 11 .    ? -39.623 39.417  98.653  1.00 38.66 ? 2031 HOH   A O     1 
HETATM 18944 O  O     . HOH   EA 11 .    ? -36.764 49.893  100.654 1.00 31.55 ? 2032 HOH   A O     1 
HETATM 18945 O  O     . HOH   EA 11 .    ? -30.906 81.465  129.085 1.00 39.97 ? 2033 HOH   A O     1 
HETATM 18946 O  O     . HOH   EA 11 .    ? -39.289 88.666  119.126 1.00 34.29 ? 2034 HOH   A O     1 
HETATM 18947 O  O     . HOH   EA 11 .    ? -3.388  82.233  109.940 1.00 32.33 ? 2035 HOH   A O     1 
HETATM 18948 O  O     . HOH   EA 11 .    ? 11.338  89.459  104.499 1.00 38.61 ? 2036 HOH   A O     1 
HETATM 18949 O  O     . HOH   EA 11 .    ? -36.769 60.588  96.280  1.00 20.00 ? 2037 HOH   A O     1 
HETATM 18950 O  O     . HOH   EA 11 .    ? -40.496 64.874  62.083  1.00 32.49 ? 2038 HOH   A O     1 
HETATM 18951 O  O     . HOH   EA 11 .    ? -12.534 65.852  112.776 1.00 18.75 ? 2039 HOH   A O     1 
HETATM 18952 O  O     . HOH   EA 11 .    ? -1.875  90.988  105.638 1.00 30.18 ? 2040 HOH   A O     1 
HETATM 18953 O  O     . HOH   EA 11 .    ? -39.601 61.491  94.414  1.00 23.01 ? 2041 HOH   A O     1 
HETATM 18954 O  O     . HOH   EA 11 .    ? -12.830 69.121  73.942  1.00 36.57 ? 2042 HOH   A O     1 
HETATM 18955 O  O     . HOH   EA 11 .    ? -16.043 53.792  100.782 1.00 37.18 ? 2043 HOH   A O     1 
HETATM 18956 O  O     . HOH   EA 11 .    ? -39.104 86.393  89.231  1.00 30.33 ? 2044 HOH   A O     1 
HETATM 18957 O  O     . HOH   EA 11 .    ? -56.843 39.301  91.442  1.00 40.22 ? 2045 HOH   A O     1 
HETATM 18958 O  O     . HOH   EA 11 .    ? -56.099 37.150  92.858  1.00 39.88 ? 2046 HOH   A O     1 
HETATM 18959 O  O     . HOH   EA 11 .    ? -38.942 66.748  94.357  1.00 28.02 ? 2047 HOH   A O     1 
HETATM 18960 O  O     . HOH   EA 11 .    ? -9.201  60.550  84.281  1.00 24.21 ? 2048 HOH   A O     1 
HETATM 18961 O  O     . HOH   EA 11 .    ? -13.786 86.599  100.825 1.00 27.53 ? 2049 HOH   A O     1 
HETATM 18962 O  O     . HOH   EA 11 .    ? 21.794  72.940  115.769 1.00 27.66 ? 2050 HOH   A O     1 
HETATM 18963 O  O     . HOH   EA 11 .    ? -13.451 54.184  77.297  1.00 27.10 ? 2051 HOH   A O     1 
HETATM 18964 O  O     . HOH   EA 11 .    ? -1.377  80.311  111.979 1.00 31.54 ? 2052 HOH   A O     1 
HETATM 18965 O  O     . HOH   EA 11 .    ? -3.279  82.373  97.515  1.00 24.52 ? 2053 HOH   A O     1 
HETATM 18966 O  O     . HOH   EA 11 .    ? -2.749  75.951  77.412  1.00 23.98 ? 2054 HOH   A O     1 
HETATM 18967 O  O     . HOH   EA 11 .    ? -36.605 69.186  119.247 1.00 35.24 ? 2055 HOH   A O     1 
HETATM 18968 O  O     . HOH   EA 11 .    ? -63.691 52.960  89.898  1.00 32.65 ? 2056 HOH   A O     1 
HETATM 18969 O  O     . HOH   EA 11 .    ? -3.697  78.946  93.475  1.00 34.84 ? 2057 HOH   A O     1 
HETATM 18970 O  O     . HOH   EA 11 .    ? -53.771 43.119  65.512  1.00 40.97 ? 2058 HOH   A O     1 
HETATM 18971 O  O     . HOH   EA 11 .    ? 8.880   64.899  94.278  1.00 31.47 ? 2059 HOH   A O     1 
HETATM 18972 O  O     . HOH   EA 11 .    ? 21.463  71.259  94.934  1.00 37.98 ? 2060 HOH   A O     1 
HETATM 18973 O  O     . HOH   EA 11 .    ? -48.843 65.569  54.261  1.00 35.76 ? 2061 HOH   A O     1 
HETATM 18974 O  O     . HOH   EA 11 .    ? -5.357  90.531  119.905 1.00 36.06 ? 2062 HOH   A O     1 
HETATM 18975 O  O     . HOH   EA 11 .    ? -53.559 72.371  68.213  1.00 28.78 ? 2063 HOH   A O     1 
HETATM 18976 O  O     . HOH   EA 11 .    ? -0.233  74.004  96.097  1.00 38.49 ? 2064 HOH   A O     1 
HETATM 18977 O  O     . HOH   EA 11 .    ? -25.132 96.320  123.337 1.00 41.93 ? 2065 HOH   A O     1 
HETATM 18978 O  O     . HOH   EA 11 .    ? -30.347 54.151  57.858  1.00 40.23 ? 2066 HOH   A O     1 
HETATM 18979 O  O     . HOH   EA 11 .    ? -18.382 51.099  84.916  1.00 44.09 ? 2067 HOH   A O     1 
HETATM 18980 O  O     . HOH   EA 11 .    ? -30.633 95.865  104.906 1.00 33.41 ? 2068 HOH   A O     1 
HETATM 18981 O  O     . HOH   EA 11 .    ? -45.679 29.345  66.444  1.00 48.12 ? 2069 HOH   A O     1 
HETATM 18982 O  O     . HOH   EA 11 .    ? -44.359 31.619  83.912  1.00 30.18 ? 2070 HOH   A O     1 
HETATM 18983 O  O     . HOH   EA 11 .    ? 1.369   62.279  111.153 1.00 31.24 ? 2071 HOH   A O     1 
HETATM 18984 O  O     . HOH   EA 11 .    ? -26.718 39.384  77.087  1.00 42.45 ? 2072 HOH   A O     1 
HETATM 18985 O  O     . HOH   EA 11 .    ? -30.526 86.779  102.091 1.00 30.12 ? 2073 HOH   A O     1 
HETATM 18986 O  O     . HOH   EA 11 .    ? 18.504  75.258  96.514  1.00 36.97 ? 2074 HOH   A O     1 
HETATM 18987 O  O     . HOH   EA 11 .    ? -48.948 29.507  73.794  1.00 37.24 ? 2075 HOH   A O     1 
HETATM 18988 O  O     . HOH   EA 11 .    ? -51.146 79.603  78.856  1.00 35.25 ? 2076 HOH   A O     1 
HETATM 18989 O  O     . HOH   EA 11 .    ? 11.307  85.124  124.524 1.00 29.47 ? 2077 HOH   A O     1 
HETATM 18990 O  O     . HOH   EA 11 .    ? -62.614 67.614  66.487  1.00 31.55 ? 2078 HOH   A O     1 
HETATM 18991 O  O     . HOH   EA 11 .    ? -64.560 55.191  80.875  1.00 26.49 ? 2079 HOH   A O     1 
HETATM 18992 O  O     . HOH   EA 11 .    ? -40.724 46.907  59.572  1.00 39.02 ? 2080 HOH   A O     1 
HETATM 18993 O  O     . HOH   EA 11 .    ? -42.617 77.654  78.393  1.00 25.58 ? 2081 HOH   A O     1 
HETATM 18994 O  O     . HOH   EA 11 .    ? -54.961 42.105  96.700  1.00 38.52 ? 2082 HOH   A O     1 
HETATM 18995 O  O     . HOH   EA 11 .    ? -43.516 90.553  99.970  1.00 31.69 ? 2083 HOH   A O     1 
HETATM 18996 O  O     . HOH   EA 11 .    ? -61.075 41.896  67.011  1.00 39.86 ? 2084 HOH   A O     1 
HETATM 18997 O  O     . HOH   EA 11 .    ? -25.457 68.136  90.474  1.00 29.44 ? 2085 HOH   A O     1 
HETATM 18998 O  O     . HOH   EA 11 .    ? -4.929  55.705  101.182 1.00 31.71 ? 2086 HOH   A O     1 
HETATM 18999 O  O     . HOH   EA 11 .    ? -65.831 72.402  72.089  1.00 41.59 ? 2087 HOH   A O     1 
HETATM 19000 O  O     . HOH   EA 11 .    ? -64.482 59.153  99.485  1.00 41.39 ? 2088 HOH   A O     1 
HETATM 19001 O  O     . HOH   EA 11 .    ? -17.573 59.090  86.302  1.00 36.42 ? 2089 HOH   A O     1 
HETATM 19002 O  O     . HOH   EA 11 .    ? -6.945  93.758  113.310 1.00 33.41 ? 2090 HOH   A O     1 
HETATM 19003 O  O     . HOH   EA 11 .    ? -0.109  67.695  117.637 1.00 32.30 ? 2091 HOH   A O     1 
HETATM 19004 O  O     . HOH   EA 11 .    ? 1.302   74.842  107.201 1.00 29.05 ? 2092 HOH   A O     1 
HETATM 19005 O  O     . HOH   EA 11 .    ? -25.277 87.970  132.775 1.00 43.33 ? 2093 HOH   A O     1 
HETATM 19006 O  O     . HOH   EA 11 .    ? -26.648 62.836  86.435  1.00 25.47 ? 2094 HOH   A O     1 
HETATM 19007 O  O     . HOH   EA 11 .    ? -21.359 59.188  122.437 1.00 30.10 ? 2095 HOH   A O     1 
HETATM 19008 O  O     . HOH   EA 11 .    ? -28.151 65.059  64.146  1.00 43.83 ? 2096 HOH   A O     1 
HETATM 19009 O  O     . HOH   EA 11 .    ? -34.951 97.936  116.029 1.00 38.67 ? 2097 HOH   A O     1 
HETATM 19010 O  O     . HOH   EA 11 .    ? -68.732 52.855  85.071  1.00 40.92 ? 2098 HOH   A O     1 
HETATM 19011 O  O     . HOH   EA 11 .    ? -30.804 83.906  123.238 1.00 27.72 ? 2099 HOH   A O     1 
HETATM 19012 O  O     . HOH   EA 11 .    ? -9.529  63.826  96.100  1.00 23.04 ? 2100 HOH   A O     1 
HETATM 19013 O  O     . HOH   EA 11 .    ? -38.694 71.120  84.294  1.00 28.01 ? 2101 HOH   A O     1 
HETATM 19014 O  O     . HOH   EA 11 .    ? -54.975 26.701  91.850  1.00 36.76 ? 2102 HOH   A O     1 
HETATM 19015 O  O     . HOH   EA 11 .    ? -20.892 50.416  108.607 1.00 37.50 ? 2103 HOH   A O     1 
HETATM 19016 O  O     . HOH   EA 11 .    ? -57.013 53.527  96.288  1.00 24.26 ? 2104 HOH   A O     1 
HETATM 19017 O  O     . HOH   EA 11 .    ? -46.791 77.225  92.061  1.00 25.90 ? 2105 HOH   A O     1 
HETATM 19018 O  O     . HOH   EA 11 .    ? -49.587 35.401  87.842  1.00 29.88 ? 2106 HOH   A O     1 
HETATM 19019 O  O     . HOH   EA 11 .    ? -49.861 73.004  62.855  1.00 22.98 ? 2107 HOH   A O     1 
HETATM 19020 O  O     . HOH   EA 11 .    ? -32.072 98.092  124.084 1.00 43.33 ? 2108 HOH   A O     1 
HETATM 19021 O  O     . HOH   EA 11 .    ? -12.254 39.981  68.304  1.00 40.62 ? 2109 HOH   A O     1 
HETATM 19022 O  O     . HOH   EA 11 .    ? -22.186 76.826  70.226  1.00 24.86 ? 2110 HOH   A O     1 
HETATM 19023 O  O     . HOH   EA 11 .    ? -66.263 68.713  83.991  1.00 29.86 ? 2111 HOH   A O     1 
HETATM 19024 O  O     . HOH   EA 11 .    ? 0.562   64.221  107.258 1.00 19.41 ? 2112 HOH   A O     1 
HETATM 19025 O  O     . HOH   EA 11 .    ? -26.484 97.191  89.028  1.00 40.64 ? 2113 HOH   A O     1 
HETATM 19026 O  O     . HOH   EA 11 .    ? 2.509   86.478  126.180 1.00 40.39 ? 2114 HOH   A O     1 
HETATM 19027 O  O     . HOH   EA 11 .    ? 12.965  88.724  116.182 1.00 34.84 ? 2115 HOH   A O     1 
HETATM 19028 O  O     . HOH   EA 11 .    ? -22.621 94.542  118.233 1.00 35.00 ? 2116 HOH   A O     1 
HETATM 19029 O  O     . HOH   EA 11 .    ? -0.668  77.511  126.524 1.00 39.55 ? 2117 HOH   A O     1 
HETATM 19030 O  O     . HOH   EA 11 .    ? -1.529  54.345  101.792 1.00 26.06 ? 2118 HOH   A O     1 
HETATM 19031 O  O     . HOH   EA 11 .    ? -13.881 55.905  111.491 1.00 33.49 ? 2119 HOH   A O     1 
HETATM 19032 O  O     . HOH   EA 11 .    ? -39.481 84.668  103.735 1.00 30.34 ? 2120 HOH   A O     1 
HETATM 19033 O  O     . HOH   EA 11 .    ? -23.104 89.195  102.146 1.00 27.34 ? 2121 HOH   A O     1 
HETATM 19034 O  O     . HOH   EA 11 .    ? -22.190 54.512  97.175  1.00 33.28 ? 2122 HOH   A O     1 
HETATM 19035 O  O     . HOH   EA 11 .    ? -28.530 94.991  89.245  1.00 37.08 ? 2123 HOH   A O     1 
HETATM 19036 O  O     . HOH   EA 11 .    ? -32.949 57.455  72.649  1.00 41.15 ? 2124 HOH   A O     1 
HETATM 19037 O  O     . HOH   EA 11 .    ? 20.756  75.612  99.965  1.00 39.08 ? 2125 HOH   A O     1 
HETATM 19038 O  O     . HOH   EA 11 .    ? 4.640   86.085  100.960 1.00 28.03 ? 2126 HOH   A O     1 
HETATM 19039 O  O     . HOH   EA 11 .    ? 1.409   57.240  107.626 1.00 20.03 ? 2127 HOH   A O     1 
HETATM 19040 O  O     . HOH   EA 11 .    ? -54.322 44.997  91.941  1.00 34.80 ? 2128 HOH   A O     1 
HETATM 19041 O  O     . HOH   EA 11 .    ? -0.625  74.863  116.625 1.00 33.63 ? 2129 HOH   A O     1 
HETATM 19042 O  O     . HOH   EA 11 .    ? -40.665 70.503  92.773  1.00 28.95 ? 2130 HOH   A O     1 
HETATM 19043 O  O     . HOH   EA 11 .    ? -67.690 64.288  85.313  1.00 33.96 ? 2131 HOH   A O     1 
HETATM 19044 O  O     . HOH   EA 11 .    ? -36.781 37.843  102.419 1.00 41.99 ? 2132 HOH   A O     1 
HETATM 19045 O  O     . HOH   EA 11 .    ? -36.080 80.681  75.677  1.00 25.49 ? 2133 HOH   A O     1 
HETATM 19046 O  O     . HOH   EA 11 .    ? -12.563 53.788  110.690 1.00 34.55 ? 2134 HOH   A O     1 
HETATM 19047 O  O     . HOH   EA 11 .    ? -62.914 62.151  97.875  1.00 32.15 ? 2135 HOH   A O     1 
HETATM 19048 O  O     . HOH   EA 11 .    ? 0.148   87.290  124.292 1.00 33.51 ? 2136 HOH   A O     1 
HETATM 19049 O  O     . HOH   EA 11 .    ? -36.085 71.485  121.201 1.00 36.33 ? 2137 HOH   A O     1 
HETATM 19050 O  O     . HOH   EA 11 .    ? -49.455 54.358  73.963  1.00 21.68 ? 2138 HOH   A O     1 
HETATM 19051 O  O     . HOH   EA 11 .    ? -31.452 41.352  98.165  1.00 37.12 ? 2139 HOH   A O     1 
HETATM 19052 O  O     . HOH   EA 11 .    ? -45.485 55.021  92.108  1.00 17.15 ? 2140 HOH   A O     1 
HETATM 19053 O  O     . HOH   EA 11 .    ? -35.615 43.656  79.378  1.00 26.14 ? 2141 HOH   A O     1 
HETATM 19054 O  O     . HOH   EA 11 .    ? -31.362 94.328  127.092 1.00 36.63 ? 2142 HOH   A O     1 
HETATM 19055 O  O     . HOH   EA 11 .    ? -20.261 54.782  98.794  1.00 29.99 ? 2143 HOH   A O     1 
HETATM 19056 O  O     . HOH   EA 11 .    ? -7.879  72.548  100.621 1.00 27.24 ? 2144 HOH   A O     1 
HETATM 19057 O  O     . HOH   EA 11 .    ? 11.093  64.662  114.709 1.00 37.75 ? 2145 HOH   A O     1 
HETATM 19058 O  O     . HOH   EA 11 .    ? -47.607 80.051  95.811  1.00 36.30 ? 2146 HOH   A O     1 
HETATM 19059 O  O     . HOH   EA 11 .    ? 7.262   55.191  98.826  1.00 21.42 ? 2147 HOH   A O     1 
HETATM 19060 O  O     . HOH   EA 11 .    ? -0.460  52.576  59.130  1.00 37.15 ? 2148 HOH   A O     1 
HETATM 19061 O  O     . HOH   EA 11 .    ? -28.980 54.849  111.228 1.00 35.98 ? 2149 HOH   A O     1 
HETATM 19062 O  O     . HOH   EA 11 .    ? -39.934 37.902  85.063  1.00 31.55 ? 2150 HOH   A O     1 
HETATM 19063 O  O     . HOH   EA 11 .    ? -42.943 56.296  91.962  1.00 18.37 ? 2151 HOH   A O     1 
HETATM 19064 O  O     . HOH   EA 11 .    ? -8.809  51.814  107.419 1.00 31.52 ? 2152 HOH   A O     1 
HETATM 19065 O  O     . HOH   EA 11 .    ? -56.648 73.508  96.351  1.00 37.48 ? 2153 HOH   A O     1 
HETATM 19066 O  O     . HOH   EA 11 .    ? -11.018 53.912  100.388 1.00 27.74 ? 2154 HOH   A O     1 
HETATM 19067 O  O     . HOH   EA 11 .    ? -57.077 63.573  104.930 1.00 48.07 ? 2155 HOH   A O     1 
HETATM 19068 O  O     . HOH   EA 11 .    ? 5.758   58.670  97.286  1.00 31.96 ? 2156 HOH   A O     1 
HETATM 19069 O  O     . HOH   EA 11 .    ? -44.105 91.580  111.168 1.00 36.93 ? 2157 HOH   A O     1 
HETATM 19070 O  O     . HOH   EA 11 .    ? -51.997 29.991  73.012  1.00 41.44 ? 2158 HOH   A O     1 
HETATM 19071 O  O     . HOH   EA 11 .    ? -37.299 86.139  101.890 1.00 27.44 ? 2159 HOH   A O     1 
HETATM 19072 O  O     . HOH   EA 11 .    ? -55.161 36.422  96.766  1.00 46.69 ? 2160 HOH   A O     1 
HETATM 19073 O  O     . HOH   EA 11 .    ? -0.000  66.995  86.271  1.00 38.17 ? 2161 HOH   A O     1 
HETATM 19074 O  O     . HOH   EA 11 .    ? -41.451 88.708  93.854  1.00 32.56 ? 2162 HOH   A O     1 
HETATM 19075 O  O     . HOH   EA 11 .    ? 13.298  57.337  116.590 1.00 45.18 ? 2163 HOH   A O     1 
HETATM 19076 O  O     . HOH   EA 11 .    ? -18.346 53.918  86.482  1.00 45.66 ? 2164 HOH   A O     1 
HETATM 19077 O  O     . HOH   EA 11 .    ? -61.984 67.156  60.547  1.00 38.59 ? 2165 HOH   A O     1 
HETATM 19078 O  O     . HOH   EA 11 .    ? -16.975 54.831  78.211  1.00 35.52 ? 2166 HOH   A O     1 
HETATM 19079 O  O     . HOH   EA 11 .    ? -56.805 32.329  87.890  1.00 29.51 ? 2167 HOH   A O     1 
HETATM 19080 O  O     . HOH   EA 11 .    ? -21.310 53.036  88.882  1.00 41.62 ? 2168 HOH   A O     1 
HETATM 19081 O  O     . HOH   EA 11 .    ? -61.190 61.640  62.686  1.00 33.97 ? 2169 HOH   A O     1 
HETATM 19082 O  O     . HOH   EA 11 .    ? -27.100 90.377  115.661 1.00 27.65 ? 2170 HOH   A O     1 
HETATM 19083 O  O     . HOH   EA 11 .    ? -37.194 75.480  97.576  1.00 29.02 ? 2171 HOH   A O     1 
HETATM 19084 O  O     . HOH   EA 11 .    ? -32.362 44.705  103.283 1.00 40.34 ? 2172 HOH   A O     1 
HETATM 19085 O  O     . HOH   EA 11 .    ? -46.495 78.477  117.246 1.00 36.58 ? 2173 HOH   A O     1 
HETATM 19086 O  O     . HOH   EA 11 .    ? -37.790 40.434  74.201  1.00 30.17 ? 2174 HOH   A O     1 
HETATM 19087 O  O     . HOH   EA 11 .    ? -31.890 98.633  99.318  1.00 43.57 ? 2175 HOH   A O     1 
HETATM 19088 O  O     . HOH   EA 11 .    ? -18.232 39.494  68.578  1.00 42.35 ? 2176 HOH   A O     1 
HETATM 19089 O  O     . HOH   EA 11 .    ? -14.918 53.299  75.549  1.00 32.92 ? 2177 HOH   A O     1 
HETATM 19090 O  O     . HOH   EA 11 .    ? -3.137  75.239  101.985 1.00 32.99 ? 2178 HOH   A O     1 
HETATM 19091 O  O     . HOH   EA 11 .    ? 13.002  63.522  120.751 1.00 37.55 ? 2179 HOH   A O     1 
HETATM 19092 O  O     . HOH   EA 11 .    ? -12.252 81.789  72.731  1.00 40.26 ? 2180 HOH   A O     1 
HETATM 19093 O  O     . HOH   EA 11 .    ? 22.413  65.483  92.753  1.00 40.50 ? 2181 HOH   A O     1 
HETATM 19094 O  O     . HOH   EA 11 .    ? -56.369 40.353  67.493  1.00 38.52 ? 2182 HOH   A O     1 
HETATM 19095 O  O     . HOH   EA 11 .    ? -26.806 79.782  70.046  1.00 37.03 ? 2183 HOH   A O     1 
HETATM 19096 O  O     . HOH   EA 11 .    ? -61.891 59.901  95.915  1.00 27.53 ? 2184 HOH   A O     1 
HETATM 19097 O  O     . HOH   EA 11 .    ? -16.795 54.541  117.188 1.00 36.97 ? 2185 HOH   A O     1 
HETATM 19098 O  O     . HOH   EA 11 .    ? 15.093  82.492  119.315 1.00 33.19 ? 2186 HOH   A O     1 
HETATM 19099 O  O     . HOH   EA 11 .    ? -10.696 66.823  127.500 1.00 38.23 ? 2187 HOH   A O     1 
HETATM 19100 O  O     . HOH   EA 11 .    ? -50.230 54.810  104.738 1.00 38.33 ? 2188 HOH   A O     1 
HETATM 19101 O  O     . HOH   EA 11 .    ? -9.124  73.221  131.797 1.00 40.16 ? 2189 HOH   A O     1 
HETATM 19102 O  O     . HOH   EA 11 .    ? -32.321 48.390  84.071  1.00 34.68 ? 2190 HOH   A O     1 
HETATM 19103 O  O     . HOH   EA 11 .    ? -34.278 55.106  71.347  1.00 40.08 ? 2191 HOH   A O     1 
HETATM 19104 O  O     . HOH   EA 11 .    ? -36.375 82.544  120.803 1.00 30.01 ? 2192 HOH   A O     1 
HETATM 19105 O  O     . HOH   EA 11 .    ? 2.809   66.765  120.287 1.00 38.83 ? 2193 HOH   A O     1 
HETATM 19106 O  O     . HOH   EA 11 .    ? -34.106 50.264  83.546  1.00 35.39 ? 2194 HOH   A O     1 
HETATM 19107 O  O     . HOH   EA 11 .    ? -34.050 59.119  106.125 1.00 29.55 ? 2195 HOH   A O     1 
HETATM 19108 O  O     . HOH   EA 11 .    ? 12.600  65.071  118.510 1.00 35.63 ? 2196 HOH   A O     1 
HETATM 19109 O  O     . HOH   EA 11 .    ? -19.565 87.547  135.796 1.00 48.18 ? 2197 HOH   A O     1 
HETATM 19110 O  O     . HOH   EA 11 .    ? -49.677 49.501  104.444 1.00 40.09 ? 2198 HOH   A O     1 
HETATM 19111 O  O     . HOH   EA 11 .    ? -45.736 78.364  89.958  1.00 24.83 ? 2199 HOH   A O     1 
HETATM 19112 O  O     . HOH   EA 11 .    ? -65.975 64.337  88.184  1.00 34.05 ? 2200 HOH   A O     1 
HETATM 19113 O  O     . HOH   EA 11 .    ? -5.662  74.878  103.086 1.00 30.50 ? 2201 HOH   A O     1 
HETATM 19114 O  O     . HOH   EA 11 .    ? -35.017 70.663  82.548  1.00 35.35 ? 2202 HOH   A O     1 
HETATM 19115 O  O     . HOH   EA 11 .    ? -23.296 75.955  133.377 1.00 35.27 ? 2203 HOH   A O     1 
HETATM 19116 O  O     . HOH   EA 11 .    ? -23.769 100.537 100.865 1.00 40.83 ? 2204 HOH   A O     1 
HETATM 19117 O  O     . HOH   EA 11 .    ? -38.480 57.910  75.380  1.00 37.48 ? 2205 HOH   A O     1 
HETATM 19118 O  O     . HOH   EA 11 .    ? -52.760 66.350  101.957 1.00 39.53 ? 2206 HOH   A O     1 
HETATM 19119 O  O     . HOH   EA 11 .    ? -34.829 64.950  66.243  1.00 32.72 ? 2207 HOH   A O     1 
HETATM 19120 O  O     . HOH   EA 11 .    ? -18.681 59.571  108.273 1.00 35.12 ? 2208 HOH   A O     1 
HETATM 19121 O  O     . HOH   EA 11 .    ? -5.410  46.636  55.520  1.00 38.83 ? 2209 HOH   A O     1 
HETATM 19122 O  O     . HOH   EA 11 .    ? -64.415 63.146  68.602  1.00 39.18 ? 2210 HOH   A O     1 
HETATM 19123 O  O     . HOH   EA 11 .    ? -16.282 43.153  71.773  1.00 41.29 ? 2211 HOH   A O     1 
HETATM 19124 O  O     . HOH   EA 11 .    ? -42.220 85.506  105.228 1.00 36.30 ? 2212 HOH   A O     1 
HETATM 19125 O  O     . HOH   EA 11 .    ? 17.137  87.344  111.636 1.00 40.95 ? 2213 HOH   A O     1 
HETATM 19126 O  O     . HOH   EA 11 .    ? 1.083   69.766  87.573  1.00 36.13 ? 2214 HOH   A O     1 
HETATM 19127 O  O     . HOH   EA 11 .    ? 8.328   69.733  125.211 1.00 39.30 ? 2215 HOH   A O     1 
HETATM 19128 O  O     . HOH   EA 11 .    ? 19.495  64.395  93.098  1.00 33.63 ? 2216 HOH   A O     1 
HETATM 19129 O  O     . HOH   EA 11 .    ? -8.818  41.286  69.443  1.00 33.98 ? 2217 HOH   A O     1 
HETATM 19130 O  O     . HOH   EA 11 .    ? -8.695  53.102  104.622 1.00 38.64 ? 2218 HOH   A O     1 
HETATM 19131 O  O     . HOH   EA 11 .    ? -25.896 74.382  132.574 1.00 37.34 ? 2219 HOH   A O     1 
HETATM 19132 O  O     . HOH   EA 11 .    ? -12.653 93.497  130.599 1.00 44.62 ? 2220 HOH   A O     1 
HETATM 19133 O  O     . HOH   EA 11 .    ? -10.707 63.036  68.818  1.00 30.35 ? 2221 HOH   A O     1 
HETATM 19134 O  O     . HOH   EA 11 .    ? -26.817 60.575  122.614 1.00 33.27 ? 2222 HOH   A O     1 
HETATM 19135 O  O     . HOH   EA 11 .    ? -31.657 67.925  101.327 1.00 32.94 ? 2223 HOH   A O     1 
HETATM 19136 O  O     . HOH   EA 11 .    ? -39.387 47.117  103.967 1.00 34.43 ? 2224 HOH   A O     1 
HETATM 19137 O  O     . HOH   EA 11 .    ? -52.688 57.033  73.791  1.00 27.42 ? 2225 HOH   A O     1 
HETATM 19138 O  O     . HOH   EA 11 .    ? -1.750  80.096  97.276  1.00 29.21 ? 2226 HOH   A O     1 
HETATM 19139 O  O     . HOH   EA 11 .    ? -50.381 24.045  80.968  1.00 42.74 ? 2227 HOH   A O     1 
HETATM 19140 O  O     . HOH   EA 11 .    ? 7.310   91.610  118.485 1.00 34.93 ? 2228 HOH   A O     1 
HETATM 19141 O  O     . HOH   EA 11 .    ? -22.781 67.216  129.714 1.00 41.15 ? 2229 HOH   A O     1 
HETATM 19142 O  O     . HOH   EA 11 .    ? -60.754 68.949  92.052  1.00 41.50 ? 2230 HOH   A O     1 
HETATM 19143 O  O     . HOH   EA 11 .    ? 19.233  71.479  92.258  1.00 41.04 ? 2231 HOH   A O     1 
HETATM 19144 O  O     . HOH   EA 11 .    ? 11.546  74.598  128.827 1.00 39.42 ? 2232 HOH   A O     1 
HETATM 19145 O  O     . HOH   EA 11 .    ? -18.172 92.543  107.908 1.00 36.60 ? 2233 HOH   A O     1 
HETATM 19146 O  O     . HOH   EA 11 .    ? 26.208  74.322  97.849  1.00 40.17 ? 2234 HOH   A O     1 
HETATM 19147 O  O     . HOH   EA 11 .    ? -44.399 69.516  111.088 1.00 40.96 ? 2235 HOH   A O     1 
HETATM 19148 O  O     . HOH   EA 11 .    ? -41.828 75.545  120.454 1.00 44.12 ? 2236 HOH   A O     1 
HETATM 19149 O  O     . HOH   EA 11 .    ? -47.407 33.186  85.625  1.00 38.35 ? 2237 HOH   A O     1 
HETATM 19150 O  O     . HOH   EA 11 .    ? -25.852 69.508  95.815  1.00 34.55 ? 2238 HOH   A O     1 
HETATM 19151 O  O     . HOH   EA 11 .    ? -18.868 54.612  118.433 1.00 39.49 ? 2239 HOH   A O     1 
HETATM 19152 O  O     . HOH   EA 11 .    ? -52.442 41.477  101.484 1.00 44.61 ? 2240 HOH   A O     1 
HETATM 19153 O  O     . HOH   EA 11 .    ? -15.179 57.751  106.211 1.00 36.33 ? 2241 HOH   A O     1 
HETATM 19154 O  O     . HOH   EA 11 .    ? -51.820 55.223  70.493  1.00 28.55 ? 2242 HOH   A O     1 
HETATM 19155 O  O     . HOH   EA 11 .    ? -60.604 59.598  62.121  1.00 33.82 ? 2243 HOH   A O     1 
HETATM 19156 O  O     . HOH   EA 11 .    ? -39.887 67.709  89.117  1.00 31.55 ? 2244 HOH   A O     1 
HETATM 19157 O  O     . HOH   EA 11 .    ? -26.811 65.414  102.718 1.00 28.97 ? 2245 HOH   A O     1 
HETATM 19158 O  O     . HOH   EA 11 .    ? -55.136 27.863  82.023  1.00 38.75 ? 2246 HOH   A O     1 
HETATM 19159 O  O     . HOH   EA 11 .    ? -28.822 61.092  121.049 1.00 37.49 ? 2247 HOH   A O     1 
HETATM 19160 O  O     . HOH   EA 11 .    ? -17.959 53.790  98.670  1.00 34.30 ? 2248 HOH   A O     1 
HETATM 19161 O  O     . HOH   EA 11 .    ? -64.327 58.668  67.739  1.00 42.19 ? 2249 HOH   A O     1 
HETATM 19162 O  O     . HOH   EA 11 .    ? -18.543 59.610  111.003 1.00 31.01 ? 2250 HOH   A O     1 
HETATM 19163 O  O     . HOH   EA 11 .    ? -55.087 57.733  102.279 1.00 32.08 ? 2251 HOH   A O     1 
HETATM 19164 O  O     . HOH   EA 11 .    ? -34.730 39.111  94.910  1.00 37.49 ? 2252 HOH   A O     1 
HETATM 19165 O  O     . HOH   EA 11 .    ? -47.570 63.870  55.985  1.00 38.07 ? 2253 HOH   A O     1 
HETATM 19166 O  O     . HOH   EA 11 .    ? -46.160 63.285  53.627  1.00 41.04 ? 2254 HOH   A O     1 
HETATM 19167 O  O     . HOH   EA 11 .    ? -8.168  89.013  95.243  1.00 48.43 ? 2255 HOH   A O     1 
HETATM 19168 O  O     . HOH   EA 11 .    ? -25.901 67.462  94.134  1.00 38.69 ? 2256 HOH   A O     1 
HETATM 19169 O  O     . HOH   EA 11 .    ? -48.431 27.279  74.988  1.00 43.18 ? 2257 HOH   A O     1 
HETATM 19170 O  O     . HOH   EA 11 .    ? -64.120 51.137  73.372  1.00 35.61 ? 2258 HOH   A O     1 
HETATM 19171 O  O     . HOH   EA 11 .    ? -22.637 74.177  69.812  1.00 34.40 ? 2259 HOH   A O     1 
HETATM 19172 O  O     . HOH   EA 11 .    ? -40.874 66.675  70.762  1.00 33.43 ? 2260 HOH   A O     1 
HETATM 19173 O  O     . HOH   EA 11 .    ? -7.477  72.899  103.689 1.00 31.90 ? 2261 HOH   A O     1 
HETATM 19174 O  O     . HOH   EA 11 .    ? 12.542  88.559  118.737 1.00 39.05 ? 2262 HOH   A O     1 
HETATM 19175 O  O     . HOH   EA 11 .    ? -3.181  68.295  93.212  1.00 43.53 ? 2263 HOH   A O     1 
HETATM 19176 O  O     . HOH   EA 11 .    ? -61.208 72.552  81.909  1.00 39.80 ? 2264 HOH   A O     1 
HETATM 19177 O  O     . HOH   EA 11 .    ? -27.551 63.783  90.597  1.00 35.92 ? 2265 HOH   A O     1 
HETATM 19178 O  O     . HOH   EA 11 .    ? 7.771   62.524  112.463 1.00 34.40 ? 2266 HOH   A O     1 
HETATM 19179 O  O     . HOH   EA 11 .    ? -27.282 51.286  109.662 1.00 35.92 ? 2267 HOH   A O     1 
HETATM 19180 O  O     . HOH   EA 11 .    ? -11.400 59.772  106.643 1.00 36.18 ? 2268 HOH   A O     1 
HETATM 19181 O  O     . HOH   EA 11 .    ? -67.375 62.166  68.671  1.00 39.23 ? 2269 HOH   A O     1 
HETATM 19182 O  O     . HOH   EA 11 .    ? -44.647 88.154  99.482  1.00 37.76 ? 2270 HOH   A O     1 
HETATM 19183 O  O     . HOH   EA 11 .    ? -9.879  66.744  74.320  1.00 36.34 ? 2271 HOH   A O     1 
HETATM 19184 O  O     . HOH   EA 11 .    ? -28.514 57.426  88.531  1.00 31.67 ? 2272 HOH   A O     1 
HETATM 19185 O  O     . HOH   EA 11 .    ? -22.784 71.038  73.953  1.00 36.61 ? 2273 HOH   A O     1 
HETATM 19186 O  O     . HOH   EA 11 .    ? -70.425 49.520  81.912  1.00 41.45 ? 2274 HOH   A O     1 
HETATM 19187 O  O     . HOH   EA 11 .    ? -59.770 64.262  92.349  1.00 32.65 ? 2275 HOH   A O     1 
HETATM 19188 O  O     . HOH   EA 11 .    ? -58.706 30.718  86.640  1.00 34.80 ? 2276 HOH   A O     1 
HETATM 19189 O  O     . HOH   EA 11 .    ? -23.286 54.754  52.117  1.00 43.01 ? 2277 HOH   A O     1 
HETATM 19190 O  O     . HOH   EA 11 .    ? -21.034 92.985  107.127 1.00 32.59 ? 2278 HOH   A O     1 
HETATM 19191 O  O     . HOH   EA 11 .    ? -33.018 84.260  76.970  1.00 28.18 ? 2279 HOH   A O     1 
HETATM 19192 O  O     . HOH   EA 11 .    ? -62.858 61.104  93.534  1.00 35.33 ? 2280 HOH   A O     1 
HETATM 19193 O  O     . HOH   EA 11 .    ? -51.272 68.481  107.769 1.00 37.20 ? 2281 HOH   A O     1 
HETATM 19194 O  O     . HOH   EA 11 .    ? -9.937  93.718  114.092 1.00 33.06 ? 2282 HOH   A O     1 
HETATM 19195 O  O     . HOH   EA 11 .    ? -21.238 63.160  81.330  1.00 36.67 ? 2283 HOH   A O     1 
HETATM 19196 O  O     . HOH   EA 11 .    ? -66.788 54.697  82.273  1.00 33.35 ? 2284 HOH   A O     1 
HETATM 19197 O  O     . HOH   EA 11 .    ? -37.108 31.969  99.190  1.00 46.69 ? 2285 HOH   A O     1 
HETATM 19198 O  O     . HOH   EA 11 .    ? -63.927 65.276  66.395  1.00 35.04 ? 2286 HOH   A O     1 
HETATM 19199 O  O     . HOH   EA 11 .    ? -65.725 54.568  78.239  1.00 35.07 ? 2287 HOH   A O     1 
HETATM 19200 O  O     . HOH   EA 11 .    ? -39.027 35.809  88.806  1.00 33.32 ? 2288 HOH   A O     1 
HETATM 19201 O  O     . HOH   EA 11 .    ? -8.929  67.155  129.465 1.00 36.56 ? 2289 HOH   A O     1 
HETATM 19202 O  O     . HOH   EA 11 .    ? -34.918 54.931  107.323 1.00 33.19 ? 2290 HOH   A O     1 
HETATM 19203 O  O     . HOH   EA 11 .    ? -31.327 76.387  74.500  1.00 33.47 ? 2291 HOH   A O     1 
HETATM 19204 O  O     . HOH   EA 11 .    ? 4.966   60.493  98.268  1.00 25.53 ? 2292 HOH   A O     1 
HETATM 19205 O  O     . HOH   EA 11 .    ? 23.089  62.650  99.516  1.00 37.16 ? 2293 HOH   A O     1 
HETATM 19206 O  O     . HOH   EA 11 .    ? -16.838 57.591  110.358 1.00 41.25 ? 2294 HOH   A O     1 
HETATM 19207 O  O     . HOH   EA 11 .    ? -9.709  67.038  132.297 1.00 36.22 ? 2295 HOH   A O     1 
HETATM 19208 O  O     . HOH   EA 11 .    ? -8.751  62.233  70.065  1.00 41.21 ? 2296 HOH   A O     1 
HETATM 19209 O  O     . HOH   EA 11 .    ? -10.911 60.472  127.926 1.00 37.25 ? 2297 HOH   A O     1 
HETATM 19210 O  O     . HOH   EA 11 .    ? -6.172  86.822  88.612  1.00 43.85 ? 2298 HOH   A O     1 
HETATM 19211 O  O     . HOH   EA 11 .    ? -45.219 28.840  87.022  1.00 36.44 ? 2299 HOH   A O     1 
HETATM 19212 O  O     . HOH   EA 11 .    ? -35.313 73.517  86.622  1.00 32.52 ? 2300 HOH   A O     1 
HETATM 19213 O  O     . HOH   EA 11 .    ? -36.038 63.395  90.393  1.00 38.58 ? 2301 HOH   A O     1 
HETATM 19214 O  O     . HOH   EA 11 .    ? 16.055  83.196  116.400 1.00 38.09 ? 2302 HOH   A O     1 
HETATM 19215 O  O     . HOH   EA 11 .    ? -31.749 74.284  83.727  1.00 29.97 ? 2303 HOH   A O     1 
HETATM 19216 O  O     . HOH   EA 11 .    ? -52.578 48.455  57.817  1.00 38.67 ? 2304 HOH   A O     1 
HETATM 19217 O  O     . HOH   EA 11 .    ? -10.448 78.673  92.376  1.00 21.09 ? 2305 HOH   A O     1 
HETATM 19218 O  O     . HOH   EA 11 .    ? 7.034   94.084  120.269 1.00 47.15 ? 2306 HOH   A O     1 
HETATM 19219 O  O     . HOH   EA 11 .    ? -6.780  55.167  82.746  1.00 31.40 ? 2307 HOH   A O     1 
HETATM 19220 O  O     . HOH   EA 11 .    ? -6.846  65.571  93.022  1.00 41.18 ? 2308 HOH   A O     1 
HETATM 19221 O  O     . HOH   EA 11 .    ? -63.356 48.675  72.013  1.00 40.33 ? 2309 HOH   A O     1 
HETATM 19222 O  O     . HOH   EA 11 .    ? -52.263 74.136  61.948  1.00 24.18 ? 2310 HOH   A O     1 
HETATM 19223 O  O     . HOH   EA 11 .    ? -53.873 42.322  60.787  1.00 49.56 ? 2311 HOH   A O     1 
HETATM 19224 O  O     . HOH   EA 11 .    ? -55.893 32.257  92.309  1.00 40.13 ? 2312 HOH   A O     1 
HETATM 19225 O  O     . HOH   EA 11 .    ? -59.990 52.458  95.923  1.00 44.06 ? 2313 HOH   A O     1 
HETATM 19226 O  O     . HOH   EA 11 .    ? 6.606   66.864  93.871  1.00 38.59 ? 2314 HOH   A O     1 
HETATM 19227 O  O     . HOH   EA 11 .    ? -34.425 76.123  87.324  1.00 29.92 ? 2315 HOH   A O     1 
HETATM 19228 O  O     . HOH   EA 11 .    ? -25.685 64.921  91.592  1.00 40.86 ? 2316 HOH   A O     1 
HETATM 19229 O  O     . HOH   EA 11 .    ? -14.867 57.828  123.939 1.00 39.32 ? 2317 HOH   A O     1 
HETATM 19230 O  O     . HOH   EA 11 .    ? -66.892 66.084  83.320  1.00 27.19 ? 2318 HOH   A O     1 
HETATM 19231 O  O     . HOH   EA 11 .    ? -15.075 54.018  105.174 1.00 45.60 ? 2319 HOH   A O     1 
HETATM 19232 O  O     . HOH   EA 11 .    ? 3.158   74.042  87.748  1.00 47.61 ? 2320 HOH   A O     1 
HETATM 19233 O  O     . HOH   EA 11 .    ? -35.842 90.473  123.620 1.00 35.84 ? 2321 HOH   A O     1 
HETATM 19234 O  O     . HOH   EA 11 .    ? -52.967 45.593  94.626  1.00 37.35 ? 2322 HOH   A O     1 
HETATM 19235 O  O     . HOH   EA 11 .    ? -41.626 63.998  106.159 1.00 39.16 ? 2323 HOH   A O     1 
HETATM 19236 O  O     . HOH   EA 11 .    ? -57.902 32.309  90.178  1.00 30.95 ? 2324 HOH   A O     1 
HETATM 19237 O  O     . HOH   EA 11 .    ? -22.516 46.616  55.735  1.00 41.34 ? 2325 HOH   A O     1 
HETATM 19238 O  O     . HOH   EA 11 .    ? -52.332 64.220  100.786 1.00 32.70 ? 2326 HOH   A O     1 
HETATM 19239 O  O     . HOH   EA 11 .    ? -30.045 79.575  125.604 1.00 37.23 ? 2327 HOH   A O     1 
HETATM 19240 O  O     . HOH   EA 11 .    ? -37.560 82.235  74.123  1.00 41.76 ? 2328 HOH   A O     1 
HETATM 19241 O  O     . HOH   EA 11 .    ? -56.370 74.792  79.383  1.00 32.22 ? 2329 HOH   A O     1 
HETATM 19242 O  O     . HOH   EA 11 .    ? -24.459 46.994  57.690  1.00 46.66 ? 2330 HOH   A O     1 
HETATM 19243 O  O     . HOH   EA 11 .    ? -12.956 53.178  79.461  1.00 41.37 ? 2331 HOH   A O     1 
HETATM 19244 O  O     . HOH   EA 11 .    ? 10.975  79.499  128.626 1.00 36.49 ? 2332 HOH   A O     1 
HETATM 19245 O  O     . HOH   EA 11 .    ? -44.710 82.524  88.937  1.00 36.86 ? 2333 HOH   A O     1 
HETATM 19246 O  O     . HOH   EA 11 .    ? 18.599  89.293  111.282 1.00 42.35 ? 2334 HOH   A O     1 
HETATM 19247 O  O     . HOH   EA 11 .    ? -37.224 63.145  114.130 1.00 34.28 ? 2335 HOH   A O     1 
HETATM 19248 O  O     . HOH   EA 11 .    ? -35.259 38.957  89.862  1.00 38.10 ? 2336 HOH   A O     1 
HETATM 19249 O  O     . HOH   EA 11 .    ? 16.259  66.545  90.088  1.00 34.92 ? 2337 HOH   A O     1 
HETATM 19250 O  O     . HOH   EA 11 .    ? 3.385   68.551  94.464  1.00 39.47 ? 2338 HOH   A O     1 
HETATM 19251 O  O     . HOH   EA 11 .    ? -11.200 96.210  112.095 1.00 38.01 ? 2339 HOH   A O     1 
HETATM 19252 O  O     . HOH   EA 11 .    ? -30.328 70.413  87.792  1.00 44.35 ? 2340 HOH   A O     1 
HETATM 19253 O  O     . HOH   EA 11 .    ? -25.788 83.287  69.835  1.00 40.70 ? 2341 HOH   A O     1 
HETATM 19254 O  O     . HOH   EA 11 .    ? -33.592 80.735  74.501  1.00 29.49 ? 2342 HOH   A O     1 
HETATM 19255 O  O     . HOH   EA 11 .    ? -28.207 76.016  129.947 1.00 39.14 ? 2343 HOH   A O     1 
HETATM 19256 O  O     . HOH   EA 11 .    ? -24.783 97.354  125.937 1.00 43.72 ? 2344 HOH   A O     1 
HETATM 19257 O  O     . HOH   EA 11 .    ? -33.486 81.027  122.652 1.00 30.57 ? 2345 HOH   A O     1 
HETATM 19258 O  O     . HOH   EA 11 .    ? 20.503  61.701  96.314  1.00 31.28 ? 2346 HOH   A O     1 
HETATM 19259 O  O     . HOH   EA 11 .    ? -18.387 74.544  109.213 1.00 24.81 ? 2347 HOH   A O     1 
HETATM 19260 O  O     . HOH   EA 11 .    ? -22.681 91.409  103.648 1.00 36.45 ? 2348 HOH   A O     1 
HETATM 19261 O  O     . HOH   EA 11 .    ? -36.819 62.417  118.115 1.00 44.76 ? 2349 HOH   A O     1 
HETATM 19262 O  O     . HOH   EA 11 .    ? -56.766 44.108  92.276  1.00 39.25 ? 2350 HOH   A O     1 
HETATM 19263 O  O     . HOH   EA 11 .    ? -54.442 78.441  85.913  1.00 40.74 ? 2351 HOH   A O     1 
HETATM 19264 O  O     . HOH   EA 11 .    ? -24.250 97.066  121.083 1.00 43.85 ? 2352 HOH   A O     1 
HETATM 19265 O  O     . HOH   EA 11 .    ? -62.407 53.928  65.764  1.00 35.83 ? 2353 HOH   A O     1 
HETATM 19266 O  O     . HOH   EA 11 .    ? -9.269  73.620  129.226 1.00 37.85 ? 2354 HOH   A O     1 
HETATM 19267 O  O     . HOH   EA 11 .    ? -40.896 68.428  93.536  1.00 34.71 ? 2355 HOH   A O     1 
HETATM 19268 O  O     . HOH   EA 11 .    ? -40.961 82.663  68.785  1.00 36.07 ? 2356 HOH   A O     1 
HETATM 19269 O  O     . HOH   EA 11 .    ? -14.663 48.847  51.461  1.00 40.45 ? 2357 HOH   A O     1 
HETATM 19270 O  O     . HOH   EA 11 .    ? -25.455 62.172  102.062 1.00 32.39 ? 2358 HOH   A O     1 
HETATM 19271 O  O     . HOH   EA 11 .    ? 2.235   74.935  119.652 1.00 41.43 ? 2359 HOH   A O     1 
HETATM 19272 O  O     . HOH   EA 11 .    ? 27.744  76.153  109.259 1.00 40.27 ? 2360 HOH   A O     1 
HETATM 19273 O  O     . HOH   EA 11 .    ? -8.794  57.601  84.289  1.00 37.20 ? 2361 HOH   A O     1 
HETATM 19274 O  O     . HOH   EA 11 .    ? -52.996 69.077  100.845 1.00 31.13 ? 2362 HOH   A O     1 
HETATM 19275 O  O     . HOH   EA 11 .    ? -3.949  80.095  124.870 1.00 35.84 ? 2363 HOH   A O     1 
HETATM 19276 O  O     . HOH   EA 11 .    ? 3.806   64.948  96.337  1.00 27.39 ? 2364 HOH   A O     1 
HETATM 19277 O  O     . HOH   EA 11 .    ? -33.684 76.449  89.939  1.00 40.39 ? 2365 HOH   A O     1 
HETATM 19278 O  O     . HOH   EA 11 .    ? 25.072  62.630  100.513 1.00 36.94 ? 2366 HOH   A O     1 
HETATM 19279 O  O     . HOH   EA 11 .    ? -66.679 47.537  73.705  1.00 34.03 ? 2367 HOH   A O     1 
HETATM 19280 O  O     . HOH   EA 11 .    ? 8.609   73.592  128.755 1.00 43.32 ? 2368 HOH   A O     1 
HETATM 19281 O  O     . HOH   EA 11 .    ? 23.071  70.253  115.788 1.00 32.04 ? 2369 HOH   A O     1 
HETATM 19282 O  O     . HOH   EA 11 .    ? -69.634 61.611  72.654  1.00 27.82 ? 2370 HOH   A O     1 
HETATM 19283 O  O     . HOH   EA 11 .    ? -46.679 80.893  89.779  1.00 33.34 ? 2371 HOH   A O     1 
HETATM 19284 O  O     . HOH   EA 11 .    ? -2.070  73.756  118.826 1.00 38.13 ? 2372 HOH   A O     1 
HETATM 19285 O  O     . HOH   EA 11 .    ? -52.221 38.628  101.945 1.00 43.08 ? 2373 HOH   A O     1 
HETATM 19286 O  O     . HOH   EA 11 .    ? -36.648 82.482  77.267  1.00 38.94 ? 2374 HOH   A O     1 
HETATM 19287 O  O     . HOH   EA 11 .    ? 0.930   71.312  117.422 1.00 35.36 ? 2375 HOH   A O     1 
HETATM 19288 O  O     . HOH   EA 11 .    ? -43.936 28.718  90.294  1.00 38.80 ? 2376 HOH   A O     1 
HETATM 19289 O  O     . HOH   EA 11 .    ? 18.461  64.557  90.266  1.00 40.67 ? 2377 HOH   A O     1 
HETATM 19290 O  O     . HOH   EA 11 .    ? -33.167 58.413  113.521 1.00 41.37 ? 2378 HOH   A O     1 
HETATM 19291 O  O     . HOH   EA 11 .    ? 7.877   76.633  127.816 1.00 44.27 ? 2379 HOH   A O     1 
HETATM 19292 O  O     . HOH   EA 11 .    ? -51.960 73.208  102.648 1.00 30.73 ? 2380 HOH   A O     1 
HETATM 19293 O  O     . HOH   EA 11 .    ? -0.600  60.861  112.475 1.00 33.53 ? 2381 HOH   A O     1 
HETATM 19294 O  O     . HOH   EA 11 .    ? -52.376 76.401  91.208  1.00 41.88 ? 2382 HOH   A O     1 
HETATM 19295 O  O     . HOH   EA 11 .    ? -44.970 60.996  53.140  1.00 37.34 ? 2383 HOH   A O     1 
HETATM 19296 O  O     . HOH   EA 11 .    ? -47.877 37.355  100.557 1.00 39.44 ? 2384 HOH   A O     1 
HETATM 19297 O  O     . HOH   EA 11 .    ? -20.737 52.875  101.171 1.00 37.86 ? 2385 HOH   A O     1 
HETATM 19298 O  O     . HOH   EA 11 .    ? -60.173 45.105  90.422  1.00 39.10 ? 2386 HOH   A O     1 
HETATM 19299 O  O     . HOH   EA 11 .    ? -18.728 46.765  53.027  1.00 38.12 ? 2387 HOH   A O     1 
HETATM 19300 O  O     . HOH   EA 11 .    ? -8.384  77.071  129.409 1.00 37.13 ? 2388 HOH   A O     1 
HETATM 19301 O  O     . HOH   EA 11 .    ? -64.854 56.681  69.794  1.00 41.59 ? 2389 HOH   A O     1 
HETATM 19302 O  O     . HOH   EA 11 .    ? 6.757   62.596  94.789  1.00 29.09 ? 2390 HOH   A O     1 
HETATM 19303 O  O     . HOH   EA 11 .    ? -32.076 74.873  85.906  1.00 38.36 ? 2391 HOH   A O     1 
HETATM 19304 O  O     . HOH   EA 11 .    ? -35.503 39.102  104.406 1.00 48.96 ? 2392 HOH   A O     1 
HETATM 19305 O  O     . HOH   EA 11 .    ? -56.690 73.130  99.081  1.00 37.85 ? 2393 HOH   A O     1 
HETATM 19306 O  O     . HOH   EA 11 .    ? -54.491 54.759  102.165 1.00 39.94 ? 2394 HOH   A O     1 
HETATM 19307 O  O     . HOH   EA 11 .    ? -58.541 55.407  101.287 1.00 42.73 ? 2395 HOH   A O     1 
HETATM 19308 O  O     . HOH   EA 11 .    ? -61.769 51.012  66.264  1.00 39.90 ? 2396 HOH   A O     1 
HETATM 19309 O  O     . HOH   EA 11 .    ? -0.347  86.250  96.793  1.00 39.58 ? 2397 HOH   A O     1 
HETATM 19310 O  O     . HOH   EA 11 .    ? -29.908 60.306  86.030  1.00 35.54 ? 2398 HOH   A O     1 
HETATM 19311 O  O     . HOH   EA 11 .    ? -20.172 74.813  101.763 1.00 28.80 ? 2399 HOH   A O     1 
HETATM 19312 O  O     . HOH   EA 11 .    ? -28.599 77.635  70.229  1.00 34.34 ? 2400 HOH   A O     1 
HETATM 19313 O  O     . HOH   EA 11 .    ? -51.544 43.281  103.522 1.00 44.54 ? 2401 HOH   A O     1 
HETATM 19314 O  O     . HOH   EA 11 .    ? -9.239  62.264  94.016  1.00 35.51 ? 2402 HOH   A O     1 
HETATM 19315 O  O     . HOH   EA 11 .    ? -2.216  91.929  98.243  1.00 31.02 ? 2403 HOH   A O     1 
HETATM 19316 O  O     . HOH   EA 11 .    ? -62.576 55.551  69.951  1.00 30.10 ? 2404 HOH   A O     1 
HETATM 19317 O  O     . HOH   EA 11 .    ? -31.575 54.664  110.959 1.00 40.21 ? 2405 HOH   A O     1 
HETATM 19318 O  O     . HOH   EA 11 .    ? -19.124 57.669  106.637 1.00 30.70 ? 2406 HOH   A O     1 
HETATM 19319 O  O     . HOH   EA 11 .    ? -30.983 84.027  73.568  1.00 35.43 ? 2407 HOH   A O     1 
HETATM 19320 O  O     . HOH   EA 11 .    ? -55.400 46.287  65.108  1.00 39.93 ? 2408 HOH   A O     1 
HETATM 19321 O  O     . HOH   EA 11 .    ? -24.480 52.136  100.203 1.00 34.95 ? 2409 HOH   A O     1 
HETATM 19322 O  O     . HOH   EA 11 .    ? -29.272 92.527  108.701 1.00 33.37 ? 2410 HOH   A O     1 
HETATM 19323 O  O     . HOH   EA 11 .    ? -9.907  49.075  107.130 1.00 37.08 ? 2411 HOH   A O     1 
HETATM 19324 O  O     . HOH   EA 11 .    ? -66.817 39.308  74.037  1.00 39.06 ? 2412 HOH   A O     1 
HETATM 19325 O  O     . HOH   EA 11 .    ? 10.706  89.582  106.894 1.00 40.88 ? 2413 HOH   A O     1 
HETATM 19326 O  O     . HOH   EA 11 .    ? -56.527 76.278  76.945  1.00 29.74 ? 2414 HOH   A O     1 
HETATM 19327 O  O     . HOH   EA 11 .    ? -32.322 65.596  124.559 1.00 34.80 ? 2415 HOH   A O     1 
HETATM 19328 O  O     . HOH   EA 11 .    ? -61.259 52.746  93.981  1.00 40.20 ? 2416 HOH   A O     1 
HETATM 19329 O  O     . HOH   EA 11 .    ? -21.741 68.710  132.029 1.00 41.40 ? 2417 HOH   A O     1 
HETATM 19330 O  O     . HOH   EA 11 .    ? -18.443 73.942  106.231 1.00 25.98 ? 2418 HOH   A O     1 
HETATM 19331 O  O     . HOH   EA 11 .    ? -29.240 60.035  88.581  1.00 24.12 ? 2419 HOH   A O     1 
HETATM 19332 O  O     . HOH   EA 11 .    ? -58.238 59.498  103.070 1.00 39.44 ? 2420 HOH   A O     1 
HETATM 19333 O  O     . HOH   EA 11 .    ? -1.668  75.263  120.938 1.00 38.53 ? 2421 HOH   A O     1 
HETATM 19334 O  O     . HOH   EA 11 .    ? -24.025 50.302  95.283  1.00 34.82 ? 2422 HOH   A O     1 
HETATM 19335 O  O     . HOH   EA 11 .    ? -14.893 39.255  70.248  1.00 44.84 ? 2423 HOH   A O     1 
HETATM 19336 O  O     . HOH   EA 11 .    ? -2.521  85.118  96.682  1.00 34.03 ? 2424 HOH   A O     1 
HETATM 19337 O  O     . HOH   EA 11 .    ? -63.237 57.556  96.406  1.00 36.48 ? 2425 HOH   A O     1 
HETATM 19338 O  O     . HOH   EA 11 .    ? -8.733  52.657  101.416 1.00 40.39 ? 2426 HOH   A O     1 
HETATM 19339 O  O     . HOH   EA 11 .    ? -3.243  83.391  112.332 1.00 32.68 ? 2427 HOH   A O     1 
HETATM 19340 O  O     . HOH   EA 11 .    ? -51.764 47.160  96.578  1.00 28.69 ? 2428 HOH   A O     1 
HETATM 19341 O  O     . HOH   EA 11 .    ? -61.414 70.616  85.733  1.00 32.58 ? 2429 HOH   A O     1 
HETATM 19342 O  O     . HOH   EA 11 .    ? -3.736  87.785  96.723  1.00 41.56 ? 2430 HOH   A O     1 
HETATM 19343 O  O     . HOH   EA 11 .    ? 12.680  62.673  93.244  1.00 36.25 ? 2431 HOH   A O     1 
HETATM 19344 O  O     . HOH   EA 11 .    ? 20.878  73.463  96.292  1.00 41.44 ? 2432 HOH   A O     1 
HETATM 19345 O  O     . HOH   EA 11 .    ? 3.728   69.250  88.296  1.00 37.01 ? 2433 HOH   A O     1 
HETATM 19346 O  O     . HOH   EA 11 .    ? -56.737 74.066  85.281  1.00 46.12 ? 2434 HOH   A O     1 
HETATM 19347 O  O     . HOH   EA 11 .    ? -56.920 28.188  92.310  1.00 37.11 ? 2435 HOH   A O     1 
HETATM 19348 O  O     . HOH   EA 11 .    ? 6.748   59.891  94.356  1.00 41.56 ? 2436 HOH   A O     1 
HETATM 19349 O  O     . HOH   EA 11 .    ? -8.994  43.096  57.735  1.00 39.34 ? 2437 HOH   A O     1 
HETATM 19350 O  O     . HOH   EA 11 .    ? -54.828 80.064  84.221  1.00 45.90 ? 2438 HOH   A O     1 
HETATM 19351 O  O     . HOH   EA 11 .    ? 22.930  63.310  95.360  1.00 43.84 ? 2439 HOH   A O     1 
HETATM 19352 O  O     . HOH   EA 11 .    ? -39.657 83.296  76.429  1.00 42.96 ? 2440 HOH   A O     1 
HETATM 19353 O  O     . HOH   EA 11 .    ? -37.909 69.217  95.720  1.00 35.80 ? 2441 HOH   A O     1 
HETATM 19354 O  O     . HOH   EA 11 .    ? -8.272  70.963  132.223 1.00 41.71 ? 2442 HOH   A O     1 
HETATM 19355 O  O     . HOH   EA 11 .    ? -56.600 52.636  98.803  1.00 33.38 ? 2443 HOH   A O     1 
HETATM 19356 O  O     . HOH   EA 11 .    ? -54.829 52.895  100.579 1.00 32.82 ? 2444 HOH   A O     1 
HETATM 19357 O  O     . HOH   EA 11 .    ? -26.138 66.506  98.084  1.00 39.58 ? 2445 HOH   A O     1 
HETATM 19358 O  O     . HOH   EA 11 .    ? -46.143 38.976  104.419 1.00 35.54 ? 2446 HOH   A O     1 
HETATM 19359 O  O     . HOH   EA 11 .    ? -56.370 76.527  80.790  1.00 38.94 ? 2447 HOH   A O     1 
HETATM 19360 O  O     . HOH   EA 11 .    ? -54.958 42.370  62.770  1.00 47.28 ? 2448 HOH   A O     1 
HETATM 19361 O  O     . HOH   EA 11 .    ? -35.526 39.483  73.252  1.00 41.69 ? 2449 HOH   A O     1 
HETATM 19362 O  O     . HOH   EA 11 .    ? -32.955 57.532  110.994 1.00 35.40 ? 2450 HOH   A O     1 
HETATM 19363 O  O     . HOH   EA 11 .    ? -24.980 62.910  99.760  1.00 32.36 ? 2451 HOH   A O     1 
HETATM 19364 O  O     . HOH   EA 11 .    ? 11.370  64.704  93.109  1.00 38.10 ? 2452 HOH   A O     1 
HETATM 19365 O  O     . HOH   EA 11 .    ? -63.734 63.879  95.244  1.00 42.09 ? 2453 HOH   A O     1 
HETATM 19366 O  O     . HOH   EA 11 .    ? -31.565 61.531  121.811 1.00 34.48 ? 2454 HOH   A O     1 
HETATM 19367 O  O     . HOH   EA 11 .    ? -0.069  56.952  67.823  1.00 40.47 ? 2455 HOH   A O     1 
HETATM 19368 O  O     . HOH   EA 11 .    ? -33.206 78.242  71.076  1.00 40.47 ? 2456 HOH   A O     1 
HETATM 19369 O  O     . HOH   EA 11 .    ? 13.796  65.970  90.587  1.00 36.27 ? 2457 HOH   A O     1 
HETATM 19370 O  O     . HOH   EA 11 .    ? -37.108 34.379  89.908  1.00 35.11 ? 2458 HOH   A O     1 
HETATM 19371 O  O     . HOH   EA 11 .    ? -68.054 70.183  69.265  1.00 37.73 ? 2459 HOH   A O     1 
HETATM 19372 O  O     . HOH   EA 11 .    ? -38.912 72.138  95.656  1.00 35.85 ? 2460 HOH   A O     1 
HETATM 19373 O  O     . HOH   EA 11 .    ? -56.538 71.624  100.757 1.00 41.43 ? 2461 HOH   A O     1 
HETATM 19374 O  O     . HOH   EA 11 .    ? -35.914 81.250  70.441  1.00 43.37 ? 2462 HOH   A O     1 
HETATM 19375 O  O     . HOH   EA 11 .    ? -53.771 71.378  102.337 1.00 37.04 ? 2463 HOH   A O     1 
HETATM 19376 O  O     . HOH   EA 11 .    ? -36.461 32.169  90.844  1.00 37.37 ? 2464 HOH   A O     1 
HETATM 19377 O  O     . HOH   EA 11 .    ? -52.792 79.342  91.546  1.00 41.19 ? 2465 HOH   A O     1 
HETATM 19378 O  O     . HOH   EA 11 .    ? -33.856 81.345  71.647  1.00 39.78 ? 2466 HOH   A O     1 
HETATM 19379 O  O     . HOH   EA 11 .    ? -53.659 47.571  98.490  1.00 34.36 ? 2467 HOH   A O     1 
HETATM 19380 O  O     . HOH   FA 11 .    ? 30.555  42.018  66.809  1.00 29.36 ? 1401 HOH   B O     1 
HETATM 19381 O  O     . HOH   FA 11 .    ? -11.055 27.762  81.092  1.00 27.38 ? 1402 HOH   B O     1 
HETATM 19382 O  O     . HOH   FA 11 .    ? 15.337  36.080  79.271  1.00 33.49 ? 1403 HOH   B O     1 
HETATM 19383 O  O     . HOH   FA 11 .    ? -2.349  29.421  57.475  1.00 35.82 ? 1404 HOH   B O     1 
HETATM 19384 O  O     . HOH   FA 11 .    ? -36.098 25.004  115.822 1.00 36.07 ? 1405 HOH   B O     1 
HETATM 19385 O  O     . HOH   FA 11 .    ? 4.233   72.176  85.486  1.00 38.92 ? 1406 HOH   B O     1 
HETATM 19386 O  O     . HOH   FA 11 .    ? 3.566   56.312  62.746  1.00 39.74 ? 1407 HOH   B O     1 
HETATM 19387 O  O     . HOH   FA 11 .    ? 5.330   22.617  122.686 1.00 34.70 ? 1408 HOH   B O     1 
HETATM 19388 O  O     . HOH   FA 11 .    ? 21.279  39.842  47.698  1.00 40.85 ? 1409 HOH   B O     1 
HETATM 19389 O  O     . HOH   FA 11 .    ? -7.482  34.455  66.367  1.00 41.83 ? 1410 HOH   B O     1 
HETATM 19390 O  O     . HOH   FA 11 .    ? -5.344  -1.578  123.307 1.00 35.92 ? 1411 HOH   B O     1 
HETATM 19391 O  O     . HOH   FA 11 .    ? 22.934  35.055  115.407 1.00 32.41 ? 1412 HOH   B O     1 
HETATM 19392 O  O     . HOH   FA 11 .    ? 14.078  58.036  60.662  1.00 37.04 ? 1413 HOH   B O     1 
HETATM 19393 O  O     . HOH   FA 11 .    ? 4.150   55.289  72.505  1.00 27.04 ? 1414 HOH   B O     1 
HETATM 19394 O  O     . HOH   FA 11 .    ? 18.912  67.236  82.492  1.00 27.91 ? 1415 HOH   B O     1 
HETATM 19395 O  O     . HOH   FA 11 .    ? -18.677 50.020  120.388 1.00 39.11 ? 1416 HOH   B O     1 
HETATM 19396 O  O     . HOH   FA 11 .    ? 3.348   18.287  88.862  1.00 30.60 ? 1417 HOH   B O     1 
HETATM 19397 O  O     . HOH   FA 11 .    ? -17.118 15.564  79.654  1.00 36.41 ? 1418 HOH   B O     1 
HETATM 19398 O  O     . HOH   FA 11 .    ? -31.946 17.936  91.360  1.00 37.29 ? 1419 HOH   B O     1 
HETATM 19399 O  O     . HOH   FA 11 .    ? 6.936   51.274  57.473  1.00 31.53 ? 1420 HOH   B O     1 
HETATM 19400 O  O     . HOH   FA 11 .    ? -4.283  45.399  89.540  1.00 41.61 ? 1421 HOH   B O     1 
HETATM 19401 O  O     . HOH   FA 11 .    ? 3.800   21.533  102.315 1.00 29.18 ? 1422 HOH   B O     1 
HETATM 19402 O  O     . HOH   FA 11 .    ? 29.489  42.251  84.119  1.00 26.59 ? 1423 HOH   B O     1 
HETATM 19403 O  O     . HOH   FA 11 .    ? 8.443   -0.955  107.155 1.00 37.40 ? 1424 HOH   B O     1 
HETATM 19404 O  O     . HOH   FA 11 .    ? 17.838  12.851  117.180 1.00 28.10 ? 1425 HOH   B O     1 
HETATM 19405 O  O     . HOH   FA 11 .    ? 0.058   18.627  80.409  1.00 26.37 ? 1426 HOH   B O     1 
HETATM 19406 O  O     . HOH   FA 11 .    ? 9.874   49.272  55.711  1.00 37.70 ? 1427 HOH   B O     1 
HETATM 19407 O  O     . HOH   FA 11 .    ? 2.315   17.191  112.484 1.00 31.57 ? 1428 HOH   B O     1 
HETATM 19408 O  O     . HOH   FA 11 .    ? -19.697 27.983  91.366  1.00 41.01 ? 1429 HOH   B O     1 
HETATM 19409 O  O     . HOH   FA 11 .    ? 12.552  12.895  110.450 1.00 26.20 ? 1430 HOH   B O     1 
HETATM 19410 O  O     . HOH   FA 11 .    ? -4.492  35.740  96.197  1.00 37.95 ? 1431 HOH   B O     1 
HETATM 19411 O  O     . HOH   FA 11 .    ? -0.980  22.450  71.191  1.00 33.56 ? 1432 HOH   B O     1 
HETATM 19412 O  O     . HOH   FA 11 .    ? 10.643  51.292  75.335  1.00 23.86 ? 1433 HOH   B O     1 
HETATM 19413 O  O     . HOH   FA 11 .    ? -2.592  5.009   84.837  1.00 28.84 ? 1434 HOH   B O     1 
HETATM 19414 O  O     . HOH   FA 11 .    ? 1.833   57.200  87.575  1.00 35.35 ? 1435 HOH   B O     1 
HETATM 19415 O  O     . HOH   FA 11 .    ? -14.061 54.037  118.072 1.00 31.24 ? 1436 HOH   B O     1 
HETATM 19416 O  O     . HOH   FA 11 .    ? -11.730 -4.620  109.331 1.00 31.47 ? 1437 HOH   B O     1 
HETATM 19417 O  O     . HOH   FA 11 .    ? -7.560  24.340  116.574 1.00 39.19 ? 1438 HOH   B O     1 
HETATM 19418 O  O     . HOH   FA 11 .    ? 15.572  21.775  88.392  1.00 37.23 ? 1439 HOH   B O     1 
HETATM 19419 O  O     . HOH   FA 11 .    ? -14.200 9.537   118.462 1.00 33.23 ? 1440 HOH   B O     1 
HETATM 19420 O  O     . HOH   FA 11 .    ? 7.205   19.416  116.359 1.00 31.53 ? 1441 HOH   B O     1 
HETATM 19421 O  O     . HOH   FA 11 .    ? -1.174  14.690  85.885  1.00 23.54 ? 1442 HOH   B O     1 
HETATM 19422 O  O     . HOH   FA 11 .    ? 1.866   20.482  103.858 1.00 25.65 ? 1443 HOH   B O     1 
HETATM 19423 O  O     . HOH   FA 11 .    ? -25.662 6.440   111.695 1.00 40.21 ? 1444 HOH   B O     1 
HETATM 19424 O  O     . HOH   FA 11 .    ? 25.823  8.797   75.109  1.00 40.51 ? 1445 HOH   B O     1 
HETATM 19425 O  O     . HOH   FA 11 .    ? -10.005 10.994  129.678 1.00 34.54 ? 1446 HOH   B O     1 
HETATM 19426 O  O     . HOH   FA 11 .    ? 32.630  19.116  57.922  1.00 31.66 ? 1447 HOH   B O     1 
HETATM 19427 O  O     . HOH   FA 11 .    ? 30.201  35.365  50.689  1.00 31.74 ? 1448 HOH   B O     1 
HETATM 19428 O  O     . HOH   FA 11 .    ? 7.526   32.635  98.014  1.00 29.27 ? 1449 HOH   B O     1 
HETATM 19429 O  O     . HOH   FA 11 .    ? 6.708   15.854  124.364 1.00 33.33 ? 1450 HOH   B O     1 
HETATM 19430 O  O     . HOH   FA 11 .    ? 14.074  41.478  76.873  1.00 19.11 ? 1451 HOH   B O     1 
HETATM 19431 O  O     . HOH   FA 11 .    ? 0.965   -10.180 110.698 1.00 33.76 ? 1452 HOH   B O     1 
HETATM 19432 O  O     . HOH   FA 11 .    ? -10.042 39.954  127.115 1.00 41.15 ? 1453 HOH   B O     1 
HETATM 19433 O  O     . HOH   FA 11 .    ? 11.235  5.926   121.554 1.00 29.11 ? 1454 HOH   B O     1 
HETATM 19434 O  O     . HOH   FA 11 .    ? 11.126  46.459  106.465 1.00 30.60 ? 1455 HOH   B O     1 
HETATM 19435 O  O     . HOH   FA 11 .    ? -14.431 15.265  78.584  1.00 37.25 ? 1456 HOH   B O     1 
HETATM 19436 O  O     . HOH   FA 11 .    ? -22.382 19.334  102.102 1.00 30.36 ? 1457 HOH   B O     1 
HETATM 19437 O  O     . HOH   FA 11 .    ? -17.413 0.383   99.523  1.00 33.77 ? 1458 HOH   B O     1 
HETATM 19438 O  O     . HOH   FA 11 .    ? 5.468   43.916  58.666  1.00 31.73 ? 1459 HOH   B O     1 
HETATM 19439 O  O     . HOH   FA 11 .    ? 4.363   21.394  118.964 1.00 31.49 ? 1460 HOH   B O     1 
HETATM 19440 O  O     . HOH   FA 11 .    ? -28.471 26.675  120.389 1.00 43.46 ? 1461 HOH   B O     1 
HETATM 19441 O  O     . HOH   FA 11 .    ? 29.928  27.424  56.034  1.00 25.69 ? 1462 HOH   B O     1 
HETATM 19442 O  O     . HOH   FA 11 .    ? 27.273  32.799  104.960 1.00 39.94 ? 1463 HOH   B O     1 
HETATM 19443 O  O     . HOH   FA 11 .    ? 33.123  29.773  61.749  1.00 26.25 ? 1464 HOH   B O     1 
HETATM 19444 O  O     . HOH   FA 11 .    ? 28.953  69.327  79.891  1.00 26.15 ? 1465 HOH   B O     1 
HETATM 19445 O  O     . HOH   FA 11 .    ? 22.915  54.328  53.636  1.00 35.55 ? 1466 HOH   B O     1 
HETATM 19446 O  O     . HOH   FA 11 .    ? -9.975  -2.563  115.619 1.00 32.43 ? 1467 HOH   B O     1 
HETATM 19447 O  O     . HOH   FA 11 .    ? 36.540  20.746  89.900  1.00 43.39 ? 1468 HOH   B O     1 
HETATM 19448 O  O     . HOH   FA 11 .    ? -4.668  27.061  70.138  1.00 34.67 ? 1469 HOH   B O     1 
HETATM 19449 O  O     . HOH   FA 11 .    ? 9.708   30.632  109.784 1.00 40.67 ? 1470 HOH   B O     1 
HETATM 19450 O  O     . HOH   FA 11 .    ? 9.602   25.926  55.117  1.00 21.93 ? 1471 HOH   B O     1 
HETATM 19451 O  O     . HOH   FA 11 .    ? 37.590  23.952  84.409  1.00 34.96 ? 1472 HOH   B O     1 
HETATM 19452 O  O     . HOH   FA 11 .    ? 32.500  26.627  68.517  1.00 35.71 ? 1473 HOH   B O     1 
HETATM 19453 O  O     . HOH   FA 11 .    ? 12.362  70.035  60.986  1.00 35.33 ? 1474 HOH   B O     1 
HETATM 19454 O  O     . HOH   FA 11 .    ? 6.100   -5.611  116.666 1.00 37.72 ? 1475 HOH   B O     1 
HETATM 19455 O  O     . HOH   FA 11 .    ? 4.022   14.216  72.714  1.00 36.85 ? 1476 HOH   B O     1 
HETATM 19456 O  O     . HOH   FA 11 .    ? -2.987  24.400  103.937 1.00 34.40 ? 1477 HOH   B O     1 
HETATM 19457 O  O     . HOH   FA 11 .    ? 17.491  27.430  82.931  1.00 29.16 ? 1478 HOH   B O     1 
HETATM 19458 O  O     . HOH   FA 11 .    ? 1.253   19.700  111.701 1.00 33.35 ? 1479 HOH   B O     1 
HETATM 19459 O  O     . HOH   FA 11 .    ? 5.058   32.340  89.173  1.00 32.91 ? 1480 HOH   B O     1 
HETATM 19460 O  O     . HOH   FA 11 .    ? 8.209   8.155   72.540  1.00 38.66 ? 1481 HOH   B O     1 
HETATM 19461 O  O     . HOH   FA 11 .    ? 11.043  19.428  61.582  1.00 28.11 ? 1482 HOH   B O     1 
HETATM 19462 O  O     . HOH   FA 11 .    ? 34.319  62.538  78.297  1.00 19.04 ? 1483 HOH   B O     1 
HETATM 19463 O  O     . HOH   FA 11 .    ? -11.510 -4.652  97.708  1.00 34.59 ? 1484 HOH   B O     1 
HETATM 19464 O  O     . HOH   FA 11 .    ? 18.941  24.910  54.335  1.00 26.95 ? 1485 HOH   B O     1 
HETATM 19465 O  O     . HOH   FA 11 .    ? 3.784   7.867   92.252  1.00 25.01 ? 1486 HOH   B O     1 
HETATM 19466 O  O     . HOH   FA 11 .    ? -4.588  -1.991  96.935  1.00 23.20 ? 1487 HOH   B O     1 
HETATM 19467 O  O     . HOH   FA 11 .    ? -28.586 17.719  84.708  1.00 39.55 ? 1488 HOH   B O     1 
HETATM 19468 O  O     . HOH   FA 11 .    ? 22.393  45.616  90.503  1.00 18.34 ? 1489 HOH   B O     1 
HETATM 19469 O  O     . HOH   FA 11 .    ? 28.441  13.427  85.905  1.00 26.77 ? 1490 HOH   B O     1 
HETATM 19470 O  O     . HOH   FA 11 .    ? -6.337  12.349  125.326 1.00 27.87 ? 1491 HOH   B O     1 
HETATM 19471 O  O     . HOH   FA 11 .    ? 6.000   48.117  110.657 1.00 34.42 ? 1492 HOH   B O     1 
HETATM 19472 O  O     . HOH   FA 11 .    ? 15.959  52.915  57.741  1.00 31.65 ? 1493 HOH   B O     1 
HETATM 19473 O  O     . HOH   FA 11 .    ? -5.700  37.303  77.670  1.00 30.20 ? 1494 HOH   B O     1 
HETATM 19474 O  O     . HOH   FA 11 .    ? 19.850  16.533  111.588 1.00 37.57 ? 1495 HOH   B O     1 
HETATM 19475 O  O     . HOH   FA 11 .    ? 15.095  20.816  92.510  1.00 27.79 ? 1496 HOH   B O     1 
HETATM 19476 O  O     . HOH   FA 11 .    ? -5.462  55.173  78.470  1.00 25.86 ? 1497 HOH   B O     1 
HETATM 19477 O  O     . HOH   FA 11 .    ? -8.695  45.391  108.764 1.00 32.53 ? 1498 HOH   B O     1 
HETATM 19478 O  O     . HOH   FA 11 .    ? 15.132  40.380  72.865  1.00 20.80 ? 1499 HOH   B O     1 
HETATM 19479 O  O     . HOH   FA 11 .    ? 18.967  31.356  73.162  1.00 21.33 ? 1500 HOH   B O     1 
HETATM 19480 O  O     . HOH   FA 11 .    ? 6.736   5.807   92.233  1.00 24.73 ? 1501 HOH   B O     1 
HETATM 19481 O  O     . HOH   FA 11 .    ? -8.644  24.199  77.064  1.00 35.41 ? 1502 HOH   B O     1 
HETATM 19482 O  O     . HOH   FA 11 .    ? 27.621  13.207  66.577  1.00 35.29 ? 1503 HOH   B O     1 
HETATM 19483 O  O     . HOH   FA 11 .    ? 6.359   5.802   86.032  1.00 21.29 ? 1504 HOH   B O     1 
HETATM 19484 O  O     . HOH   FA 11 .    ? -6.323  51.014  72.952  1.00 16.67 ? 1505 HOH   B O     1 
HETATM 19485 O  O     . HOH   FA 11 .    ? 11.107  18.357  64.493  1.00 27.66 ? 1506 HOH   B O     1 
HETATM 19486 O  O     . HOH   FA 11 .    ? 18.830  12.983  95.388  1.00 28.42 ? 1507 HOH   B O     1 
HETATM 19487 O  O     . HOH   FA 11 .    ? 15.106  38.914  77.023  1.00 17.76 ? 1508 HOH   B O     1 
HETATM 19488 O  O     . HOH   FA 11 .    ? 4.256   19.380  97.174  1.00 33.57 ? 1509 HOH   B O     1 
HETATM 19489 O  O     . HOH   FA 11 .    ? 10.579  24.699  103.456 1.00 31.45 ? 1510 HOH   B O     1 
HETATM 19490 O  O     . HOH   FA 11 .    ? 33.652  12.273  74.718  1.00 30.77 ? 1511 HOH   B O     1 
HETATM 19491 O  O     . HOH   FA 11 .    ? 3.501   33.828  86.544  1.00 21.74 ? 1512 HOH   B O     1 
HETATM 19492 O  O     . HOH   FA 11 .    ? 10.946  9.114   69.858  1.00 34.40 ? 1513 HOH   B O     1 
HETATM 19493 O  O     . HOH   FA 11 .    ? 15.488  53.588  81.674  1.00 25.40 ? 1514 HOH   B O     1 
HETATM 19494 O  O     . HOH   FA 11 .    ? 38.379  33.943  102.640 1.00 31.08 ? 1515 HOH   B O     1 
HETATM 19495 O  O     . HOH   FA 11 .    ? -4.293  46.224  133.171 1.00 45.59 ? 1516 HOH   B O     1 
HETATM 19496 O  O     . HOH   FA 11 .    ? -4.206  38.059  93.375  1.00 38.14 ? 1517 HOH   B O     1 
HETATM 19497 O  O     . HOH   FA 11 .    ? 18.381  38.305  115.696 1.00 34.62 ? 1518 HOH   B O     1 
HETATM 19498 O  O     . HOH   FA 11 .    ? -21.028 15.769  82.610  1.00 28.68 ? 1519 HOH   B O     1 
HETATM 19499 O  O     . HOH   FA 11 .    ? 15.138  55.910  74.435  1.00 28.34 ? 1520 HOH   B O     1 
HETATM 19500 O  O     . HOH   FA 11 .    ? 26.749  41.825  49.557  1.00 40.61 ? 1521 HOH   B O     1 
HETATM 19501 O  O     . HOH   FA 11 .    ? -2.241  48.843  63.478  1.00 20.00 ? 1522 HOH   B O     1 
HETATM 19502 O  O     . HOH   FA 11 .    ? 19.822  51.084  77.425  1.00 22.07 ? 1523 HOH   B O     1 
HETATM 19503 O  O     . HOH   FA 11 .    ? -3.778  24.750  70.531  1.00 40.63 ? 1524 HOH   B O     1 
HETATM 19504 O  O     . HOH   FA 11 .    ? -4.226  64.242  80.903  1.00 18.89 ? 1525 HOH   B O     1 
HETATM 19505 O  O     . HOH   FA 11 .    ? 10.117  50.831  64.583  1.00 23.69 ? 1526 HOH   B O     1 
HETATM 19506 O  O     . HOH   FA 11 .    ? 39.007  25.885  80.540  1.00 36.78 ? 1527 HOH   B O     1 
HETATM 19507 O  O     . HOH   FA 11 .    ? 15.483  16.911  87.882  1.00 21.53 ? 1528 HOH   B O     1 
HETATM 19508 O  O     . HOH   FA 11 .    ? 12.760  6.351   117.755 1.00 36.86 ? 1529 HOH   B O     1 
HETATM 19509 O  O     . HOH   FA 11 .    ? 2.659   39.469  98.620  1.00 21.78 ? 1530 HOH   B O     1 
HETATM 19510 O  O     . HOH   FA 11 .    ? 15.924  55.535  92.812  1.00 29.06 ? 1531 HOH   B O     1 
HETATM 19511 O  O     . HOH   FA 11 .    ? -6.316  52.574  106.998 1.00 29.59 ? 1532 HOH   B O     1 
HETATM 19512 O  O     . HOH   FA 11 .    ? 18.855  50.294  69.858  1.00 30.63 ? 1533 HOH   B O     1 
HETATM 19513 O  O     . HOH   FA 11 .    ? -1.210  38.447  80.085  1.00 24.05 ? 1534 HOH   B O     1 
HETATM 19514 O  O     . HOH   FA 11 .    ? -12.693 8.911   124.361 1.00 35.19 ? 1535 HOH   B O     1 
HETATM 19515 O  O     . HOH   FA 11 .    ? 1.181   38.823  108.150 1.00 24.47 ? 1536 HOH   B O     1 
HETATM 19516 O  O     . HOH   FA 11 .    ? 26.063  35.448  47.155  1.00 41.83 ? 1537 HOH   B O     1 
HETATM 19517 O  O     . HOH   FA 11 .    ? -6.944  8.515   110.988 1.00 23.43 ? 1538 HOH   B O     1 
HETATM 19518 O  O     . HOH   FA 11 .    ? -2.203  39.609  87.086  1.00 19.65 ? 1539 HOH   B O     1 
HETATM 19519 O  O     . HOH   FA 11 .    ? -27.147 26.890  99.294  1.00 44.44 ? 1540 HOH   B O     1 
HETATM 19520 O  O     . HOH   FA 11 .    ? 23.585  52.736  70.587  1.00 29.78 ? 1541 HOH   B O     1 
HETATM 19521 O  O     . HOH   FA 11 .    ? 33.999  11.649  87.844  1.00 42.38 ? 1542 HOH   B O     1 
HETATM 19522 O  O     . HOH   FA 11 .    ? 1.059   28.805  82.965  1.00 16.08 ? 1543 HOH   B O     1 
HETATM 19523 O  O     . HOH   FA 11 .    ? 6.044   25.682  86.233  1.00 32.34 ? 1544 HOH   B O     1 
HETATM 19524 O  O     . HOH   FA 11 .    ? 4.402   42.186  84.379  1.00 25.04 ? 1545 HOH   B O     1 
HETATM 19525 O  O     . HOH   FA 11 .    ? -25.448 7.247   98.427  1.00 33.53 ? 1546 HOH   B O     1 
HETATM 19526 O  O     . HOH   FA 11 .    ? 36.505  20.876  78.588  1.00 41.07 ? 1547 HOH   B O     1 
HETATM 19527 O  O     . HOH   FA 11 .    ? 29.452  32.245  76.421  1.00 24.88 ? 1548 HOH   B O     1 
HETATM 19528 O  O     . HOH   FA 11 .    ? 31.165  21.384  79.907  1.00 20.53 ? 1549 HOH   B O     1 
HETATM 19529 O  O     . HOH   FA 11 .    ? 16.028  43.083  50.279  1.00 32.98 ? 1550 HOH   B O     1 
HETATM 19530 O  O     . HOH   FA 11 .    ? 33.297  17.970  89.841  1.00 38.98 ? 1551 HOH   B O     1 
HETATM 19531 O  O     . HOH   FA 11 .    ? 18.009  23.768  110.383 1.00 23.17 ? 1552 HOH   B O     1 
HETATM 19532 O  O     . HOH   FA 11 .    ? -2.253  24.243  76.398  1.00 25.05 ? 1553 HOH   B O     1 
HETATM 19533 O  O     . HOH   FA 11 .    ? 3.601   -3.509  92.783  1.00 37.19 ? 1554 HOH   B O     1 
HETATM 19534 O  O     . HOH   FA 11 .    ? -5.144  51.698  75.443  1.00 22.49 ? 1555 HOH   B O     1 
HETATM 19535 O  O     . HOH   FA 11 .    ? 31.695  53.965  67.910  1.00 27.29 ? 1556 HOH   B O     1 
HETATM 19536 O  O     . HOH   FA 11 .    ? 29.211  68.387  72.356  1.00 34.49 ? 1557 HOH   B O     1 
HETATM 19537 O  O     . HOH   FA 11 .    ? 28.387  18.861  57.907  1.00 32.82 ? 1558 HOH   B O     1 
HETATM 19538 O  O     . HOH   FA 11 .    ? -3.993  18.793  98.040  1.00 15.61 ? 1559 HOH   B O     1 
HETATM 19539 O  O     . HOH   FA 11 .    ? -13.519 29.112  97.709  1.00 42.92 ? 1560 HOH   B O     1 
HETATM 19540 O  O     . HOH   FA 11 .    ? -2.282  45.376  102.629 1.00 32.39 ? 1561 HOH   B O     1 
HETATM 19541 O  O     . HOH   FA 11 .    ? 23.584  18.370  80.266  1.00 27.76 ? 1562 HOH   B O     1 
HETATM 19542 O  O     . HOH   FA 11 .    ? -12.489 20.007  83.895  1.00 24.74 ? 1563 HOH   B O     1 
HETATM 19543 O  O     . HOH   FA 11 .    ? 2.696   21.913  130.190 1.00 28.80 ? 1564 HOH   B O     1 
HETATM 19544 O  O     . HOH   FA 11 .    ? 9.982   50.536  90.032  1.00 27.90 ? 1565 HOH   B O     1 
HETATM 19545 O  O     . HOH   FA 11 .    ? -24.890 10.528  87.521  1.00 32.85 ? 1566 HOH   B O     1 
HETATM 19546 O  O     . HOH   FA 11 .    ? -13.922 -0.149  96.783  1.00 34.22 ? 1567 HOH   B O     1 
HETATM 19547 O  O     . HOH   FA 11 .    ? -4.637  50.624  78.365  1.00 29.58 ? 1568 HOH   B O     1 
HETATM 19548 O  O     . HOH   FA 11 .    ? 7.687   49.207  106.553 1.00 24.15 ? 1569 HOH   B O     1 
HETATM 19549 O  O     . HOH   FA 11 .    ? 2.658   44.052  70.327  1.00 17.84 ? 1570 HOH   B O     1 
HETATM 19550 O  O     . HOH   FA 11 .    ? 31.864  38.370  84.008  1.00 32.37 ? 1571 HOH   B O     1 
HETATM 19551 O  O     . HOH   FA 11 .    ? -2.537  62.824  85.413  1.00 26.96 ? 1572 HOH   B O     1 
HETATM 19552 O  O     . HOH   FA 11 .    ? 34.397  54.643  75.498  1.00 39.94 ? 1573 HOH   B O     1 
HETATM 19553 O  O     . HOH   FA 11 .    ? -10.607 46.531  74.428  1.00 20.21 ? 1574 HOH   B O     1 
HETATM 19554 O  O     . HOH   FA 11 .    ? -0.027  4.432   88.367  1.00 22.82 ? 1575 HOH   B O     1 
HETATM 19555 O  O     . HOH   FA 11 .    ? -0.078  -7.206  106.770 1.00 28.52 ? 1576 HOH   B O     1 
HETATM 19556 O  O     . HOH   FA 11 .    ? 6.066   31.927  79.114  1.00 21.54 ? 1577 HOH   B O     1 
HETATM 19557 O  O     . HOH   FA 11 .    ? 18.333  11.650  106.135 1.00 39.58 ? 1578 HOH   B O     1 
HETATM 19558 O  O     . HOH   FA 11 .    ? -4.515  2.159   123.940 1.00 26.35 ? 1579 HOH   B O     1 
HETATM 19559 O  O     . HOH   FA 11 .    ? 21.791  79.762  70.107  1.00 35.46 ? 1580 HOH   B O     1 
HETATM 19560 O  O     . HOH   FA 11 .    ? 13.619  10.335  91.248  1.00 25.63 ? 1581 HOH   B O     1 
HETATM 19561 O  O     . HOH   FA 11 .    ? 1.692   13.236  101.803 1.00 19.64 ? 1582 HOH   B O     1 
HETATM 19562 O  O     . HOH   FA 11 .    ? -9.682  -4.648  107.105 1.00 28.28 ? 1583 HOH   B O     1 
HETATM 19563 O  O     . HOH   FA 11 .    ? 2.682   30.727  80.026  1.00 20.34 ? 1584 HOH   B O     1 
HETATM 19564 O  O     . HOH   FA 11 .    ? 19.812  19.615  105.652 1.00 19.32 ? 1585 HOH   B O     1 
HETATM 19565 O  O     . HOH   FA 11 .    ? 13.597  58.265  64.445  1.00 28.88 ? 1586 HOH   B O     1 
HETATM 19566 O  O     . HOH   FA 11 .    ? 17.219  41.002  71.413  1.00 18.72 ? 1587 HOH   B O     1 
HETATM 19567 O  O     . HOH   FA 11 .    ? 31.729  60.148  65.471  1.00 27.21 ? 1588 HOH   B O     1 
HETATM 19568 O  O     . HOH   FA 11 .    ? -16.915 16.082  131.095 1.00 38.42 ? 1589 HOH   B O     1 
HETATM 19569 O  O     . HOH   FA 11 .    ? -5.071  42.749  72.571  1.00 33.76 ? 1590 HOH   B O     1 
HETATM 19570 O  O     . HOH   FA 11 .    ? -31.093 16.252  102.227 1.00 35.12 ? 1591 HOH   B O     1 
HETATM 19571 O  O     . HOH   FA 11 .    ? 21.510  50.541  87.566  1.00 23.37 ? 1592 HOH   B O     1 
HETATM 19572 O  O     . HOH   FA 11 .    ? 25.529  54.821  62.020  1.00 23.31 ? 1593 HOH   B O     1 
HETATM 19573 O  O     . HOH   FA 11 .    ? 12.028  0.574   93.957  1.00 41.93 ? 1594 HOH   B O     1 
HETATM 19574 O  O     . HOH   FA 11 .    ? 10.691  66.753  53.465  1.00 46.20 ? 1595 HOH   B O     1 
HETATM 19575 O  O     . HOH   FA 11 .    ? 11.300  24.736  108.090 1.00 30.70 ? 1596 HOH   B O     1 
HETATM 19576 O  O     . HOH   FA 11 .    ? 7.023   42.664  49.603  1.00 26.22 ? 1597 HOH   B O     1 
HETATM 19577 O  O     . HOH   FA 11 .    ? 25.676  69.281  81.531  1.00 38.84 ? 1598 HOH   B O     1 
HETATM 19578 O  O     . HOH   FA 11 .    ? 1.454   22.188  110.874 1.00 36.49 ? 1599 HOH   B O     1 
HETATM 19579 O  O     . HOH   FA 11 .    ? 13.129  55.997  65.553  1.00 32.40 ? 1600 HOH   B O     1 
HETATM 19580 O  O     . HOH   FA 11 .    ? 9.348   23.209  108.883 1.00 33.61 ? 1601 HOH   B O     1 
HETATM 19581 O  O     . HOH   FA 11 .    ? 7.908   56.726  87.435  1.00 32.93 ? 1602 HOH   B O     1 
HETATM 19582 O  O     . HOH   FA 11 .    ? -6.987  15.588  81.750  1.00 35.28 ? 1603 HOH   B O     1 
HETATM 19583 O  O     . HOH   FA 11 .    ? 33.761  67.899  80.566  1.00 23.64 ? 1604 HOH   B O     1 
HETATM 19584 O  O     . HOH   FA 11 .    ? -6.030  40.341  62.712  1.00 32.82 ? 1605 HOH   B O     1 
HETATM 19585 O  O     . HOH   FA 11 .    ? 1.711   13.592  104.701 1.00 18.50 ? 1606 HOH   B O     1 
HETATM 19586 O  O     . HOH   FA 11 .    ? 4.824   49.357  68.511  1.00 22.91 ? 1607 HOH   B O     1 
HETATM 19587 O  O     . HOH   FA 11 .    ? 12.936  50.014  64.868  1.00 25.86 ? 1608 HOH   B O     1 
HETATM 19588 O  O     . HOH   FA 11 .    ? 25.687  53.402  96.385  1.00 37.86 ? 1609 HOH   B O     1 
HETATM 19589 O  O     . HOH   FA 11 .    ? 13.240  36.882  77.191  1.00 21.14 ? 1610 HOH   B O     1 
HETATM 19590 O  O     . HOH   FA 11 .    ? 25.985  55.216  77.397  1.00 24.16 ? 1611 HOH   B O     1 
HETATM 19591 O  O     . HOH   FA 11 .    ? -10.861 1.837   121.539 1.00 23.57 ? 1612 HOH   B O     1 
HETATM 19592 O  O     . HOH   FA 11 .    ? 12.363  21.401  101.339 1.00 27.75 ? 1613 HOH   B O     1 
HETATM 19593 O  O     . HOH   FA 11 .    ? 21.578  30.255  71.353  1.00 16.10 ? 1614 HOH   B O     1 
HETATM 19594 O  O     . HOH   FA 11 .    ? 17.153  42.869  79.219  1.00 16.61 ? 1615 HOH   B O     1 
HETATM 19595 O  O     . HOH   FA 11 .    ? 10.475  66.480  86.339  1.00 39.15 ? 1616 HOH   B O     1 
HETATM 19596 O  O     . HOH   FA 11 .    ? -5.649  39.420  106.644 1.00 29.29 ? 1617 HOH   B O     1 
HETATM 19597 O  O     . HOH   FA 11 .    ? -29.734 11.996  96.352  1.00 39.66 ? 1618 HOH   B O     1 
HETATM 19598 O  O     . HOH   FA 11 .    ? 14.340  33.728  83.915  1.00 21.79 ? 1619 HOH   B O     1 
HETATM 19599 O  O     . HOH   FA 11 .    ? 37.190  28.128  93.070  1.00 30.88 ? 1620 HOH   B O     1 
HETATM 19600 O  O     . HOH   FA 11 .    ? -5.503  5.278   122.079 1.00 24.53 ? 1621 HOH   B O     1 
HETATM 19601 O  O     . HOH   FA 11 .    ? 11.874  -2.046  109.516 1.00 39.65 ? 1622 HOH   B O     1 
HETATM 19602 O  O     . HOH   FA 11 .    ? 19.652  5.366   76.895  1.00 30.71 ? 1623 HOH   B O     1 
HETATM 19603 O  O     . HOH   FA 11 .    ? -26.662 15.091  100.589 1.00 35.56 ? 1624 HOH   B O     1 
HETATM 19604 O  O     . HOH   FA 11 .    ? -2.870  -2.287  94.550  1.00 26.25 ? 1625 HOH   B O     1 
HETATM 19605 O  O     . HOH   FA 11 .    ? 9.145   3.960   80.787  1.00 27.28 ? 1626 HOH   B O     1 
HETATM 19606 O  O     . HOH   FA 11 .    ? 2.788   11.710  94.351  1.00 20.23 ? 1627 HOH   B O     1 
HETATM 19607 O  O     . HOH   FA 11 .    ? 19.292  79.230  68.496  1.00 31.80 ? 1628 HOH   B O     1 
HETATM 19608 O  O     . HOH   FA 11 .    ? 15.447  3.974   98.436  1.00 31.50 ? 1629 HOH   B O     1 
HETATM 19609 O  O     . HOH   FA 11 .    ? 16.646  14.459  109.324 1.00 27.60 ? 1630 HOH   B O     1 
HETATM 19610 O  O     . HOH   FA 11 .    ? -5.150  9.877   114.946 1.00 25.81 ? 1631 HOH   B O     1 
HETATM 19611 O  O     . HOH   FA 11 .    ? 18.246  52.646  66.570  1.00 26.79 ? 1632 HOH   B O     1 
HETATM 19612 O  O     . HOH   FA 11 .    ? 33.070  28.711  53.019  1.00 36.70 ? 1633 HOH   B O     1 
HETATM 19613 O  O     . HOH   FA 11 .    ? 5.263   3.500   92.887  1.00 24.17 ? 1634 HOH   B O     1 
HETATM 19614 O  O     . HOH   FA 11 .    ? 2.836   53.369  69.311  1.00 32.51 ? 1635 HOH   B O     1 
HETATM 19615 O  O     . HOH   FA 11 .    ? -2.422  41.901  61.621  1.00 25.56 ? 1636 HOH   B O     1 
HETATM 19616 O  O     . HOH   FA 11 .    ? 22.867  67.382  64.582  1.00 25.12 ? 1637 HOH   B O     1 
HETATM 19617 O  O     . HOH   FA 11 .    ? 27.959  67.589  68.134  1.00 29.65 ? 1638 HOH   B O     1 
HETATM 19618 O  O     . HOH   FA 11 .    ? 2.786   45.915  53.676  1.00 39.36 ? 1639 HOH   B O     1 
HETATM 19619 O  O     . HOH   FA 11 .    ? -7.822  27.119  99.765  1.00 29.58 ? 1640 HOH   B O     1 
HETATM 19620 O  O     . HOH   FA 11 .    ? -11.921 3.889   129.560 1.00 45.11 ? 1641 HOH   B O     1 
HETATM 19621 O  O     . HOH   FA 11 .    ? 22.913  48.534  77.936  1.00 21.33 ? 1642 HOH   B O     1 
HETATM 19622 O  O     . HOH   FA 11 .    ? 19.076  70.738  58.975  1.00 35.29 ? 1643 HOH   B O     1 
HETATM 19623 O  O     . HOH   FA 11 .    ? -20.302 -1.361  105.911 1.00 38.76 ? 1644 HOH   B O     1 
HETATM 19624 O  O     . HOH   FA 11 .    ? 31.214  28.935  77.618  1.00 32.13 ? 1645 HOH   B O     1 
HETATM 19625 O  O     . HOH   FA 11 .    ? 14.250  25.734  110.801 1.00 35.40 ? 1646 HOH   B O     1 
HETATM 19626 O  O     . HOH   FA 11 .    ? 5.596   7.185   94.143  1.00 24.74 ? 1647 HOH   B O     1 
HETATM 19627 O  O     . HOH   FA 11 .    ? 5.018   62.942  84.106  1.00 22.16 ? 1648 HOH   B O     1 
HETATM 19628 O  O     . HOH   FA 11 .    ? -15.080 47.236  113.881 1.00 31.67 ? 1649 HOH   B O     1 
HETATM 19629 O  O     . HOH   FA 11 .    ? -7.343  25.552  103.902 1.00 38.24 ? 1650 HOH   B O     1 
HETATM 19630 O  O     . HOH   FA 11 .    ? 18.883  45.226  53.716  1.00 26.13 ? 1651 HOH   B O     1 
HETATM 19631 O  O     . HOH   FA 11 .    ? 27.137  52.641  75.439  1.00 30.83 ? 1652 HOH   B O     1 
HETATM 19632 O  O     . HOH   FA 11 .    ? -1.328  32.702  69.023  1.00 16.02 ? 1653 HOH   B O     1 
HETATM 19633 O  O     . HOH   FA 11 .    ? 7.658   45.031  74.995  1.00 15.33 ? 1654 HOH   B O     1 
HETATM 19634 O  O     . HOH   FA 11 .    ? 18.771  7.417   100.536 1.00 34.77 ? 1655 HOH   B O     1 
HETATM 19635 O  O     . HOH   FA 11 .    ? -4.820  30.777  77.337  1.00 19.87 ? 1656 HOH   B O     1 
HETATM 19636 O  O     . HOH   FA 11 .    ? 23.373  48.543  106.835 1.00 30.57 ? 1657 HOH   B O     1 
HETATM 19637 O  O     . HOH   FA 11 .    ? 10.979  38.392  95.729  1.00 26.26 ? 1658 HOH   B O     1 
HETATM 19638 O  O     . HOH   FA 11 .    ? 4.292   -8.721  104.072 1.00 34.77 ? 1659 HOH   B O     1 
HETATM 19639 O  O     . HOH   FA 11 .    ? 38.633  32.727  83.783  1.00 30.38 ? 1660 HOH   B O     1 
HETATM 19640 O  O     . HOH   FA 11 .    ? 17.423  54.989  97.189  1.00 26.40 ? 1661 HOH   B O     1 
HETATM 19641 O  O     . HOH   FA 11 .    ? -4.809  34.528  57.180  1.00 43.59 ? 1662 HOH   B O     1 
HETATM 19642 O  O     . HOH   FA 11 .    ? -7.542  -0.856  119.794 1.00 28.39 ? 1663 HOH   B O     1 
HETATM 19643 O  O     . HOH   FA 11 .    ? 21.595  6.982   83.381  1.00 34.84 ? 1664 HOH   B O     1 
HETATM 19644 O  O     . HOH   FA 11 .    ? -1.048  55.456  72.345  1.00 29.03 ? 1665 HOH   B O     1 
HETATM 19645 O  O     . HOH   FA 11 .    ? 31.785  59.269  72.115  1.00 24.35 ? 1666 HOH   B O     1 
HETATM 19646 O  O     . HOH   FA 11 .    ? -8.227  -8.774  105.711 1.00 24.73 ? 1667 HOH   B O     1 
HETATM 19647 O  O     . HOH   FA 11 .    ? 1.100   55.595  110.444 1.00 27.20 ? 1668 HOH   B O     1 
HETATM 19648 O  O     . HOH   FA 11 .    ? 30.218  50.146  71.388  1.00 32.12 ? 1669 HOH   B O     1 
HETATM 19649 O  O     . HOH   FA 11 .    ? 19.027  5.896   74.279  1.00 26.56 ? 1670 HOH   B O     1 
HETATM 19650 O  O     . HOH   FA 11 .    ? 9.932   43.730  110.119 1.00 29.72 ? 1671 HOH   B O     1 
HETATM 19651 O  O     . HOH   FA 11 .    ? -0.458  24.071  74.148  1.00 19.93 ? 1672 HOH   B O     1 
HETATM 19652 O  O     . HOH   FA 11 .    ? 27.720  31.862  73.863  1.00 19.99 ? 1673 HOH   B O     1 
HETATM 19653 O  O     . HOH   FA 11 .    ? -9.627  6.126   87.010  1.00 24.59 ? 1674 HOH   B O     1 
HETATM 19654 O  O     . HOH   FA 11 .    ? -10.020 32.524  88.954  1.00 21.25 ? 1675 HOH   B O     1 
HETATM 19655 O  O     . HOH   FA 11 .    ? -13.452 18.220  105.550 1.00 23.94 ? 1676 HOH   B O     1 
HETATM 19656 O  O     . HOH   FA 11 .    ? 17.047  53.087  63.986  1.00 27.85 ? 1677 HOH   B O     1 
HETATM 19657 O  O     . HOH   FA 11 .    ? 10.105  71.273  61.574  1.00 30.28 ? 1678 HOH   B O     1 
HETATM 19658 O  O     . HOH   FA 11 .    ? 20.169  43.525  87.702  1.00 14.98 ? 1679 HOH   B O     1 
HETATM 19659 O  O     . HOH   FA 11 .    ? 7.815   65.416  63.731  1.00 28.81 ? 1680 HOH   B O     1 
HETATM 19660 O  O     . HOH   FA 11 .    ? 11.047  52.765  104.571 1.00 36.69 ? 1681 HOH   B O     1 
HETATM 19661 O  O     . HOH   FA 11 .    ? 23.489  55.993  99.016  1.00 28.23 ? 1682 HOH   B O     1 
HETATM 19662 O  O     . HOH   FA 11 .    ? 12.063  11.068  71.522  1.00 24.15 ? 1683 HOH   B O     1 
HETATM 19663 O  O     . HOH   FA 11 .    ? 1.290   9.444   89.599  1.00 24.33 ? 1684 HOH   B O     1 
HETATM 19664 O  O     . HOH   FA 11 .    ? 11.969  11.999  121.320 1.00 28.54 ? 1685 HOH   B O     1 
HETATM 19665 O  O     . HOH   FA 11 .    ? 0.916   -7.808  109.417 1.00 31.39 ? 1686 HOH   B O     1 
HETATM 19666 O  O     . HOH   FA 11 .    ? 5.392   25.740  89.771  1.00 37.02 ? 1687 HOH   B O     1 
HETATM 19667 O  O     . HOH   FA 11 .    ? 26.723  20.568  55.693  1.00 33.88 ? 1688 HOH   B O     1 
HETATM 19668 O  O     . HOH   FA 11 .    ? 11.738  37.385  72.223  1.00 15.48 ? 1689 HOH   B O     1 
HETATM 19669 O  O     . HOH   FA 11 .    ? 27.440  38.104  89.838  1.00 21.75 ? 1690 HOH   B O     1 
HETATM 19670 O  O     . HOH   FA 11 .    ? -9.218  10.088  122.920 1.00 25.50 ? 1691 HOH   B O     1 
HETATM 19671 O  O     . HOH   FA 11 .    ? -3.339  10.759  84.321  1.00 26.38 ? 1692 HOH   B O     1 
HETATM 19672 O  O     . HOH   FA 11 .    ? 11.776  16.639  67.715  1.00 32.73 ? 1693 HOH   B O     1 
HETATM 19673 O  O     . HOH   FA 11 .    ? 18.490  66.927  58.386  1.00 29.64 ? 1694 HOH   B O     1 
HETATM 19674 O  O     . HOH   FA 11 .    ? 32.978  46.120  67.246  1.00 30.81 ? 1695 HOH   B O     1 
HETATM 19675 O  O     . HOH   FA 11 .    ? -4.202  -0.239  110.505 1.00 24.24 ? 1696 HOH   B O     1 
HETATM 19676 O  O     . HOH   FA 11 .    ? 25.273  13.838  65.169  1.00 29.50 ? 1697 HOH   B O     1 
HETATM 19677 O  O     . HOH   FA 11 .    ? -10.837 20.259  122.657 1.00 29.71 ? 1698 HOH   B O     1 
HETATM 19678 O  O     . HOH   FA 11 .    ? 18.771  9.324   92.348  1.00 39.82 ? 1699 HOH   B O     1 
HETATM 19679 O  O     . HOH   FA 11 .    ? 0.453   20.250  69.855  1.00 26.23 ? 1700 HOH   B O     1 
HETATM 19680 O  O     . HOH   FA 11 .    ? 26.752  22.034  75.233  1.00 22.84 ? 1701 HOH   B O     1 
HETATM 19681 O  O     . HOH   FA 11 .    ? -5.234  39.876  72.249  1.00 26.20 ? 1702 HOH   B O     1 
HETATM 19682 O  O     . HOH   FA 11 .    ? 6.649   33.730  86.717  1.00 20.35 ? 1703 HOH   B O     1 
HETATM 19683 O  O     . HOH   FA 11 .    ? 0.975   30.870  74.702  1.00 17.23 ? 1704 HOH   B O     1 
HETATM 19684 O  O     . HOH   FA 11 .    ? 24.341  19.036  98.023  1.00 31.53 ? 1705 HOH   B O     1 
HETATM 19685 O  O     . HOH   FA 11 .    ? 15.382  54.037  66.531  1.00 28.89 ? 1706 HOH   B O     1 
HETATM 19686 O  O     . HOH   FA 11 .    ? 18.370  15.103  97.444  1.00 26.21 ? 1707 HOH   B O     1 
HETATM 19687 O  O     . HOH   FA 11 .    ? 32.595  69.775  73.611  1.00 35.49 ? 1708 HOH   B O     1 
HETATM 19688 O  O     . HOH   FA 11 .    ? -1.924  35.781  100.803 1.00 38.60 ? 1709 HOH   B O     1 
HETATM 19689 O  O     . HOH   FA 11 .    ? 24.206  68.775  67.371  1.00 24.29 ? 1710 HOH   B O     1 
HETATM 19690 O  O     . HOH   FA 11 .    ? -16.651 5.048   116.446 1.00 27.80 ? 1711 HOH   B O     1 
HETATM 19691 O  O     . HOH   FA 11 .    ? -24.763 17.047  82.064  1.00 32.62 ? 1712 HOH   B O     1 
HETATM 19692 O  O     . HOH   FA 11 .    ? 23.408  52.044  62.403  1.00 22.79 ? 1713 HOH   B O     1 
HETATM 19693 O  O     . HOH   FA 11 .    ? 6.463   -4.082  104.421 1.00 29.32 ? 1714 HOH   B O     1 
HETATM 19694 O  O     . HOH   FA 11 .    ? 19.939  24.435  46.150  1.00 23.42 ? 1715 HOH   B O     1 
HETATM 19695 O  O     . HOH   FA 11 .    ? -5.495  -6.372  112.031 1.00 33.30 ? 1716 HOH   B O     1 
HETATM 19696 O  O     . HOH   FA 11 .    ? 29.063  22.827  76.441  1.00 22.24 ? 1717 HOH   B O     1 
HETATM 19697 O  O     . HOH   FA 11 .    ? 22.862  37.355  85.928  1.00 17.39 ? 1718 HOH   B O     1 
HETATM 19698 O  O     . HOH   FA 11 .    ? 21.252  5.388   68.133  1.00 40.01 ? 1719 HOH   B O     1 
HETATM 19699 O  O     . HOH   FA 11 .    ? 32.914  45.223  75.033  1.00 26.99 ? 1720 HOH   B O     1 
HETATM 19700 O  O     . HOH   FA 11 .    ? 8.562   24.883  105.330 1.00 33.56 ? 1721 HOH   B O     1 
HETATM 19701 O  O     . HOH   FA 11 .    ? 27.025  48.945  94.524  1.00 29.17 ? 1722 HOH   B O     1 
HETATM 19702 O  O     . HOH   FA 11 .    ? -11.652 18.342  126.631 1.00 26.42 ? 1723 HOH   B O     1 
HETATM 19703 O  O     . HOH   FA 11 .    ? -18.079 8.200   122.097 1.00 34.62 ? 1724 HOH   B O     1 
HETATM 19704 O  O     . HOH   FA 11 .    ? 1.862   20.691  89.567  1.00 23.96 ? 1725 HOH   B O     1 
HETATM 19705 O  O     . HOH   FA 11 .    ? 6.908   8.036   74.976  1.00 27.71 ? 1726 HOH   B O     1 
HETATM 19706 O  O     . HOH   FA 11 .    ? 7.413   37.800  102.729 1.00 31.16 ? 1727 HOH   B O     1 
HETATM 19707 O  O     . HOH   FA 11 .    ? 37.459  31.227  81.543  1.00 29.54 ? 1728 HOH   B O     1 
HETATM 19708 O  O     . HOH   FA 11 .    ? 1.636   6.197   91.677  1.00 21.04 ? 1729 HOH   B O     1 
HETATM 19709 O  O     . HOH   FA 11 .    ? 0.919   42.213  76.100  1.00 24.34 ? 1730 HOH   B O     1 
HETATM 19710 O  O     . HOH   FA 11 .    ? 3.095   35.562  121.276 1.00 33.72 ? 1731 HOH   B O     1 
HETATM 19711 O  O     . HOH   FA 11 .    ? 20.711  27.700  71.163  1.00 16.19 ? 1732 HOH   B O     1 
HETATM 19712 O  O     . HOH   FA 11 .    ? 23.456  2.667   81.956  1.00 44.19 ? 1733 HOH   B O     1 
HETATM 19713 O  O     . HOH   FA 11 .    ? 21.417  53.847  83.542  1.00 30.02 ? 1734 HOH   B O     1 
HETATM 19714 O  O     . HOH   FA 11 .    ? 15.689  10.077  89.415  1.00 21.24 ? 1735 HOH   B O     1 
HETATM 19715 O  O     . HOH   FA 11 .    ? 2.285   41.642  53.904  1.00 27.01 ? 1736 HOH   B O     1 
HETATM 19716 O  O     . HOH   FA 11 .    ? 11.962  38.116  47.381  1.00 32.52 ? 1737 HOH   B O     1 
HETATM 19717 O  O     . HOH   FA 11 .    ? 1.596   49.347  89.235  1.00 36.81 ? 1738 HOH   B O     1 
HETATM 19718 O  O     . HOH   FA 11 .    ? -7.907  12.533  97.059  1.00 20.37 ? 1739 HOH   B O     1 
HETATM 19719 O  O     . HOH   FA 11 .    ? -1.795  2.593   125.747 1.00 25.46 ? 1740 HOH   B O     1 
HETATM 19720 O  O     . HOH   FA 11 .    ? 12.236  7.938   90.399  1.00 23.80 ? 1741 HOH   B O     1 
HETATM 19721 O  O     . HOH   FA 11 .    ? 12.534  2.009   111.193 1.00 26.65 ? 1742 HOH   B O     1 
HETATM 19722 O  O     . HOH   FA 11 .    ? 4.003   29.660  84.580  1.00 24.31 ? 1743 HOH   B O     1 
HETATM 19723 O  O     . HOH   FA 11 .    ? -13.522 11.892  91.149  1.00 19.97 ? 1744 HOH   B O     1 
HETATM 19724 O  O     . HOH   FA 11 .    ? 13.205  51.405  86.320  1.00 30.21 ? 1745 HOH   B O     1 
HETATM 19725 O  O     . HOH   FA 11 .    ? -0.808  -8.821  101.925 1.00 27.50 ? 1746 HOH   B O     1 
HETATM 19726 O  O     . HOH   FA 11 .    ? 12.033  49.739  88.383  1.00 21.01 ? 1747 HOH   B O     1 
HETATM 19727 O  O     . HOH   FA 11 .    ? 11.277  41.451  54.399  1.00 19.50 ? 1748 HOH   B O     1 
HETATM 19728 O  O     . HOH   FA 11 .    ? 32.810  47.464  91.978  1.00 37.79 ? 1749 HOH   B O     1 
HETATM 19729 O  O     . HOH   FA 11 .    ? -1.035  60.557  77.293  1.00 23.17 ? 1750 HOH   B O     1 
HETATM 19730 O  O     . HOH   FA 11 .    ? -20.087 25.557  102.568 1.00 37.83 ? 1751 HOH   B O     1 
HETATM 19731 O  O     . HOH   FA 11 .    ? 13.158  67.013  52.560  1.00 45.97 ? 1752 HOH   B O     1 
HETATM 19732 O  O     . HOH   FA 11 .    ? -23.090 3.369   101.464 1.00 36.87 ? 1753 HOH   B O     1 
HETATM 19733 O  O     . HOH   FA 11 .    ? 4.698   30.536  54.548  1.00 38.15 ? 1754 HOH   B O     1 
HETATM 19734 O  O     . HOH   FA 11 .    ? -0.090  39.588  131.355 1.00 39.49 ? 1755 HOH   B O     1 
HETATM 19735 O  O     . HOH   FA 11 .    ? 1.465   15.011  116.071 1.00 21.85 ? 1756 HOH   B O     1 
HETATM 19736 O  O     . HOH   FA 11 .    ? 5.763   55.804  104.630 1.00 24.71 ? 1757 HOH   B O     1 
HETATM 19737 O  O     . HOH   FA 11 .    ? -1.063  66.762  83.815  1.00 29.93 ? 1758 HOH   B O     1 
HETATM 19738 O  O     . HOH   FA 11 .    ? -1.832  11.262  101.312 1.00 18.86 ? 1759 HOH   B O     1 
HETATM 19739 O  O     . HOH   FA 11 .    ? 21.911  53.292  67.195  1.00 26.63 ? 1760 HOH   B O     1 
HETATM 19740 O  O     . HOH   FA 11 .    ? -0.358  27.031  68.490  1.00 17.71 ? 1761 HOH   B O     1 
HETATM 19741 O  O     . HOH   FA 11 .    ? -14.618 6.340   117.526 1.00 25.90 ? 1762 HOH   B O     1 
HETATM 19742 O  O     . HOH   FA 11 .    ? -6.093  12.801  99.172  1.00 17.68 ? 1763 HOH   B O     1 
HETATM 19743 O  O     . HOH   FA 11 .    ? -4.477  10.911  100.340 1.00 18.02 ? 1764 HOH   B O     1 
HETATM 19744 O  O     . HOH   FA 11 .    ? 14.211  72.338  60.938  1.00 29.40 ? 1765 HOH   B O     1 
HETATM 19745 O  O     . HOH   FA 11 .    ? 30.669  40.409  57.258  1.00 25.52 ? 1766 HOH   B O     1 
HETATM 19746 O  O     . HOH   FA 11 .    ? 15.670  38.303  74.465  1.00 15.86 ? 1767 HOH   B O     1 
HETATM 19747 O  O     . HOH   FA 11 .    ? 6.251   50.058  88.259  1.00 36.25 ? 1768 HOH   B O     1 
HETATM 19748 O  O     . HOH   FA 11 .    ? 26.154  47.379  100.066 1.00 32.93 ? 1769 HOH   B O     1 
HETATM 19749 O  O     . HOH   FA 11 .    ? 33.181  57.980  74.318  1.00 28.95 ? 1770 HOH   B O     1 
HETATM 19750 O  O     . HOH   FA 11 .    ? 23.162  72.816  64.895  1.00 34.20 ? 1771 HOH   B O     1 
HETATM 19751 O  O     . HOH   FA 11 .    ? -0.083  40.224  77.655  1.00 25.30 ? 1772 HOH   B O     1 
HETATM 19752 O  O     . HOH   FA 11 .    ? 28.115  29.639  83.041  1.00 17.56 ? 1773 HOH   B O     1 
HETATM 19753 O  O     . HOH   FA 11 .    ? 18.408  43.788  91.391  1.00 14.95 ? 1774 HOH   B O     1 
HETATM 19754 O  O     . HOH   FA 11 .    ? 6.718   81.924  75.441  1.00 35.40 ? 1775 HOH   B O     1 
HETATM 19755 O  O     . HOH   FA 11 .    ? 22.256  24.611  108.491 1.00 26.40 ? 1776 HOH   B O     1 
HETATM 19756 O  O     . HOH   FA 11 .    ? -0.953  74.382  74.381  1.00 34.03 ? 1777 HOH   B O     1 
HETATM 19757 O  O     . HOH   FA 11 .    ? 2.356   20.342  92.384  1.00 33.71 ? 1778 HOH   B O     1 
HETATM 19758 O  O     . HOH   FA 11 .    ? 4.099   64.985  68.201  1.00 38.80 ? 1779 HOH   B O     1 
HETATM 19759 O  O     . HOH   FA 11 .    ? -4.070  30.800  94.805  1.00 30.06 ? 1780 HOH   B O     1 
HETATM 19760 O  O     . HOH   FA 11 .    ? 0.217   12.385  93.663  1.00 18.16 ? 1781 HOH   B O     1 
HETATM 19761 O  O     . HOH   FA 11 .    ? -8.723  24.080  100.721 1.00 18.87 ? 1782 HOH   B O     1 
HETATM 19762 O  O     . HOH   FA 11 .    ? -1.119  50.983  64.834  1.00 19.06 ? 1783 HOH   B O     1 
HETATM 19763 O  O     . HOH   FA 11 .    ? 31.800  30.222  74.437  1.00 39.45 ? 1784 HOH   B O     1 
HETATM 19764 O  O     . HOH   FA 11 .    ? 7.966   74.487  61.938  1.00 38.46 ? 1785 HOH   B O     1 
HETATM 19765 O  O     . HOH   FA 11 .    ? -6.314  0.487   86.115  1.00 30.37 ? 1786 HOH   B O     1 
HETATM 19766 O  O     . HOH   FA 11 .    ? 35.062  64.690  81.320  1.00 22.87 ? 1787 HOH   B O     1 
HETATM 19767 O  O     . HOH   FA 11 .    ? 17.423  49.073  58.899  1.00 21.98 ? 1788 HOH   B O     1 
HETATM 19768 O  O     . HOH   FA 11 .    ? 20.228  50.732  66.995  1.00 28.33 ? 1789 HOH   B O     1 
HETATM 19769 O  O     . HOH   FA 11 .    ? -31.726 22.372  117.531 1.00 43.00 ? 1790 HOH   B O     1 
HETATM 19770 O  O     . HOH   FA 11 .    ? -24.041 -1.751  112.478 1.00 44.20 ? 1791 HOH   B O     1 
HETATM 19771 O  O     . HOH   FA 11 .    ? -2.740  54.866  83.443  1.00 32.33 ? 1792 HOH   B O     1 
HETATM 19772 O  O     . HOH   FA 11 .    ? 23.430  65.199  82.217  1.00 36.45 ? 1793 HOH   B O     1 
HETATM 19773 O  O     . HOH   FA 11 .    ? -2.708  26.964  60.472  1.00 38.11 ? 1794 HOH   B O     1 
HETATM 19774 O  O     . HOH   FA 11 .    ? -0.125  75.755  68.052  1.00 35.95 ? 1795 HOH   B O     1 
HETATM 19775 O  O     . HOH   FA 11 .    ? 18.005  68.776  84.480  1.00 34.82 ? 1796 HOH   B O     1 
HETATM 19776 O  O     . HOH   FA 11 .    ? 16.071  69.965  55.213  1.00 42.46 ? 1797 HOH   B O     1 
HETATM 19777 O  O     . HOH   FA 11 .    ? 41.240  34.598  91.214  1.00 26.31 ? 1798 HOH   B O     1 
HETATM 19778 O  O     . HOH   FA 11 .    ? -16.380 -8.331  106.247 1.00 32.44 ? 1799 HOH   B O     1 
HETATM 19779 O  O     . HOH   FA 11 .    ? 6.349   16.202  121.706 1.00 29.83 ? 1800 HOH   B O     1 
HETATM 19780 O  O     . HOH   FA 11 .    ? 8.497   40.752  86.755  1.00 16.42 ? 1801 HOH   B O     1 
HETATM 19781 O  O     . HOH   FA 11 .    ? 2.483   63.288  78.229  1.00 18.82 ? 1802 HOH   B O     1 
HETATM 19782 O  O     . HOH   FA 11 .    ? 23.623  33.021  91.492  1.00 19.07 ? 1803 HOH   B O     1 
HETATM 19783 O  O     . HOH   FA 11 .    ? 16.033  16.138  85.249  1.00 21.96 ? 1804 HOH   B O     1 
HETATM 19784 O  O     . HOH   FA 11 .    ? -7.664  29.963  75.887  1.00 27.13 ? 1805 HOH   B O     1 
HETATM 19785 O  O     . HOH   FA 11 .    ? 28.648  25.531  104.872 1.00 42.39 ? 1806 HOH   B O     1 
HETATM 19786 O  O     . HOH   FA 11 .    ? 5.090   36.020  48.898  1.00 33.93 ? 1807 HOH   B O     1 
HETATM 19787 O  O     . HOH   FA 11 .    ? -4.276  55.892  81.619  1.00 30.32 ? 1808 HOH   B O     1 
HETATM 19788 O  O     . HOH   FA 11 .    ? 22.380  12.142  71.369  1.00 26.50 ? 1809 HOH   B O     1 
HETATM 19789 O  O     . HOH   FA 11 .    ? 20.986  37.470  112.457 1.00 23.70 ? 1810 HOH   B O     1 
HETATM 19790 O  O     . HOH   FA 11 .    ? 28.608  37.246  82.727  1.00 32.45 ? 1811 HOH   B O     1 
HETATM 19791 O  O     . HOH   FA 11 .    ? 19.771  19.242  66.291  1.00 15.63 ? 1812 HOH   B O     1 
HETATM 19792 O  O     . HOH   FA 11 .    ? 20.065  22.552  74.361  1.00 28.55 ? 1813 HOH   B O     1 
HETATM 19793 O  O     . HOH   FA 11 .    ? -0.176  56.071  86.297  1.00 33.69 ? 1814 HOH   B O     1 
HETATM 19794 O  O     . HOH   FA 11 .    ? 2.772   70.294  63.996  1.00 33.71 ? 1815 HOH   B O     1 
HETATM 19795 O  O     . HOH   FA 11 .    ? -5.558  12.629  84.390  1.00 27.75 ? 1816 HOH   B O     1 
HETATM 19796 O  O     . HOH   FA 11 .    ? 33.809  37.818  61.882  1.00 27.48 ? 1817 HOH   B O     1 
HETATM 19797 O  O     . HOH   FA 11 .    ? -2.372  21.471  91.553  1.00 18.13 ? 1818 HOH   B O     1 
HETATM 19798 O  O     . HOH   FA 11 .    ? -22.248 20.608  88.230  1.00 32.76 ? 1819 HOH   B O     1 
HETATM 19799 O  O     . HOH   FA 11 .    ? -9.103  45.713  130.892 1.00 34.23 ? 1820 HOH   B O     1 
HETATM 19800 O  O     . HOH   FA 11 .    ? 2.793   32.977  78.382  1.00 16.54 ? 1821 HOH   B O     1 
HETATM 19801 O  O     . HOH   FA 11 .    ? 19.862  33.061  67.367  1.00 15.34 ? 1822 HOH   B O     1 
HETATM 19802 O  O     . HOH   FA 11 .    ? -5.900  -7.360  115.492 1.00 36.22 ? 1823 HOH   B O     1 
HETATM 19803 O  O     . HOH   FA 11 .    ? 23.907  26.155  50.535  1.00 27.27 ? 1824 HOH   B O     1 
HETATM 19804 O  O     . HOH   FA 11 .    ? 3.430   40.965  117.227 1.00 30.26 ? 1825 HOH   B O     1 
HETATM 19805 O  O     . HOH   FA 11 .    ? -16.227 25.488  106.724 1.00 32.53 ? 1826 HOH   B O     1 
HETATM 19806 O  O     . HOH   FA 11 .    ? 33.375  26.428  59.079  1.00 25.70 ? 1827 HOH   B O     1 
HETATM 19807 O  O     . HOH   FA 11 .    ? -9.562  10.337  82.449  1.00 38.55 ? 1828 HOH   B O     1 
HETATM 19808 O  O     . HOH   FA 11 .    ? 17.043  33.889  48.572  1.00 29.96 ? 1829 HOH   B O     1 
HETATM 19809 O  O     . HOH   FA 11 .    ? 8.005   65.825  68.433  1.00 31.69 ? 1830 HOH   B O     1 
HETATM 19810 O  O     . HOH   FA 11 .    ? -6.887  35.325  69.128  1.00 35.13 ? 1831 HOH   B O     1 
HETATM 19811 O  O     . HOH   FA 11 .    ? 14.727  22.434  101.686 1.00 23.28 ? 1832 HOH   B O     1 
HETATM 19812 O  O     . HOH   FA 11 .    ? 8.695   23.377  84.681  1.00 32.84 ? 1833 HOH   B O     1 
HETATM 19813 O  O     . HOH   FA 11 .    ? 25.623  53.799  73.757  1.00 23.51 ? 1834 HOH   B O     1 
HETATM 19814 O  O     . HOH   FA 11 .    ? 1.139   80.745  75.697  1.00 42.17 ? 1835 HOH   B O     1 
HETATM 19815 O  O     . HOH   FA 11 .    ? -18.723 24.075  115.051 1.00 31.50 ? 1836 HOH   B O     1 
HETATM 19816 O  O     . HOH   FA 11 .    ? 31.479  52.504  65.590  1.00 29.60 ? 1837 HOH   B O     1 
HETATM 19817 O  O     . HOH   FA 11 .    ? -8.063  2.569   92.277  1.00 21.60 ? 1838 HOH   B O     1 
HETATM 19818 O  O     . HOH   FA 11 .    ? 0.287   47.748  76.373  1.00 20.36 ? 1839 HOH   B O     1 
HETATM 19819 O  O     . HOH   FA 11 .    ? 5.893   15.228  94.576  1.00 19.74 ? 1840 HOH   B O     1 
HETATM 19820 O  O     . HOH   FA 11 .    ? 4.097   17.650  75.332  1.00 30.51 ? 1841 HOH   B O     1 
HETATM 19821 O  O     . HOH   FA 11 .    ? 18.673  13.526  74.430  1.00 25.60 ? 1842 HOH   B O     1 
HETATM 19822 O  O     . HOH   FA 11 .    ? 1.146   -0.796  92.717  1.00 26.03 ? 1843 HOH   B O     1 
HETATM 19823 O  O     . HOH   FA 11 .    ? -2.925  33.894  62.341  1.00 22.34 ? 1844 HOH   B O     1 
HETATM 19824 O  O     . HOH   FA 11 .    ? 22.867  23.679  84.702  1.00 20.35 ? 1845 HOH   B O     1 
HETATM 19825 O  O     . HOH   FA 11 .    ? -1.303  67.222  75.288  1.00 30.40 ? 1846 HOH   B O     1 
HETATM 19826 O  O     . HOH   FA 11 .    ? 1.571   15.205  82.210  1.00 22.06 ? 1847 HOH   B O     1 
HETATM 19827 O  O     . HOH   FA 11 .    ? 6.360   51.921  93.788  1.00 40.51 ? 1848 HOH   B O     1 
HETATM 19828 O  O     . HOH   FA 11 .    ? 16.042  48.566  70.655  1.00 16.60 ? 1849 HOH   B O     1 
HETATM 19829 O  O     . HOH   FA 11 .    ? 39.781  29.544  87.740  1.00 25.25 ? 1850 HOH   B O     1 
HETATM 19830 O  O     . HOH   FA 11 .    ? -4.582  8.241   131.472 1.00 40.05 ? 1851 HOH   B O     1 
HETATM 19831 O  O     . HOH   FA 11 .    ? 12.083  21.063  58.814  1.00 19.10 ? 1852 HOH   B O     1 
HETATM 19832 O  O     . HOH   FA 11 .    ? 24.949  57.517  78.245  1.00 23.40 ? 1853 HOH   B O     1 
HETATM 19833 O  O     . HOH   FA 11 .    ? 2.834   5.962   80.215  1.00 28.50 ? 1854 HOH   B O     1 
HETATM 19834 O  O     . HOH   FA 11 .    ? 10.829  29.440  94.147  1.00 25.51 ? 1855 HOH   B O     1 
HETATM 19835 O  O     . HOH   FA 11 .    ? 1.778   9.980   79.039  1.00 31.63 ? 1856 HOH   B O     1 
HETATM 19836 O  O     . HOH   FA 11 .    ? 8.615   14.929  90.342  1.00 26.88 ? 1857 HOH   B O     1 
HETATM 19837 O  O     . HOH   FA 11 .    ? 30.958  37.650  77.530  1.00 35.28 ? 1858 HOH   B O     1 
HETATM 19838 O  O     . HOH   FA 11 .    ? -2.981  30.950  63.521  1.00 28.78 ? 1859 HOH   B O     1 
HETATM 19839 O  O     . HOH   FA 11 .    ? 20.404  52.512  69.213  1.00 23.67 ? 1860 HOH   B O     1 
HETATM 19840 O  O     . HOH   FA 11 .    ? 19.614  54.860  93.369  1.00 25.96 ? 1861 HOH   B O     1 
HETATM 19841 O  O     . HOH   FA 11 .    ? 27.327  23.007  88.631  1.00 18.18 ? 1862 HOH   B O     1 
HETATM 19842 O  O     . HOH   FA 11 .    ? 33.117  37.846  104.499 1.00 31.03 ? 1863 HOH   B O     1 
HETATM 19843 O  O     . HOH   FA 11 .    ? 7.605   20.570  102.136 1.00 27.47 ? 1864 HOH   B O     1 
HETATM 19844 O  O     . HOH   FA 11 .    ? 27.164  59.202  78.460  1.00 21.76 ? 1865 HOH   B O     1 
HETATM 19845 O  O     . HOH   FA 11 .    ? -1.354  5.486   92.025  1.00 21.15 ? 1866 HOH   B O     1 
HETATM 19846 O  O     . HOH   FA 11 .    ? 28.323  33.799  80.055  1.00 36.14 ? 1867 HOH   B O     1 
HETATM 19847 O  O     . HOH   FA 11 .    ? 27.331  42.438  104.808 1.00 29.93 ? 1868 HOH   B O     1 
HETATM 19848 O  O     . HOH   FA 11 .    ? 17.373  28.653  110.769 1.00 26.98 ? 1869 HOH   B O     1 
HETATM 19849 O  O     . HOH   FA 11 .    ? 18.016  53.912  82.768  1.00 30.36 ? 1870 HOH   B O     1 
HETATM 19850 O  O     . HOH   FA 11 .    ? 11.993  45.508  108.971 1.00 36.72 ? 1871 HOH   B O     1 
HETATM 19851 O  O     . HOH   FA 11 .    ? 13.356  25.945  95.974  1.00 29.59 ? 1872 HOH   B O     1 
HETATM 19852 O  O     . HOH   FA 11 .    ? 15.460  26.932  81.075  1.00 30.68 ? 1873 HOH   B O     1 
HETATM 19853 O  O     . HOH   FA 11 .    ? -6.599  14.316  91.478  1.00 19.14 ? 1874 HOH   B O     1 
HETATM 19854 O  O     . HOH   FA 11 .    ? 25.229  23.795  81.684  1.00 25.33 ? 1875 HOH   B O     1 
HETATM 19855 O  O     . HOH   FA 11 .    ? 0.120   19.485  93.938  1.00 20.88 ? 1876 HOH   B O     1 
HETATM 19856 O  O     . HOH   FA 11 .    ? -10.328 31.800  80.254  1.00 31.24 ? 1877 HOH   B O     1 
HETATM 19857 O  O     . HOH   FA 11 .    ? 19.029  30.581  88.481  1.00 19.42 ? 1878 HOH   B O     1 
HETATM 19858 O  O     . HOH   FA 11 .    ? 29.822  58.274  82.365  1.00 37.33 ? 1879 HOH   B O     1 
HETATM 19859 O  O     . HOH   FA 11 .    ? 8.763   35.744  102.556 1.00 29.24 ? 1880 HOH   B O     1 
HETATM 19860 O  O     . HOH   FA 11 .    ? 10.100  2.508   117.310 1.00 27.53 ? 1881 HOH   B O     1 
HETATM 19861 O  O     . HOH   FA 11 .    ? 17.119  34.321  55.948  1.00 16.78 ? 1882 HOH   B O     1 
HETATM 19862 O  O     . HOH   FA 11 .    ? 28.122  9.158   73.773  1.00 32.59 ? 1883 HOH   B O     1 
HETATM 19863 O  O     . HOH   FA 11 .    ? 30.035  33.254  73.402  1.00 23.66 ? 1884 HOH   B O     1 
HETATM 19864 O  O     . HOH   FA 11 .    ? -6.509  6.490   118.547 1.00 22.38 ? 1885 HOH   B O     1 
HETATM 19865 O  O     . HOH   FA 11 .    ? 23.340  12.519  67.995  1.00 28.15 ? 1886 HOH   B O     1 
HETATM 19866 O  O     . HOH   FA 11 .    ? 1.183   10.545  129.529 1.00 25.79 ? 1887 HOH   B O     1 
HETATM 19867 O  O     . HOH   FA 11 .    ? 9.384   32.133  83.743  1.00 34.28 ? 1888 HOH   B O     1 
HETATM 19868 O  O     . HOH   FA 11 .    ? 6.495   12.241  126.476 1.00 22.28 ? 1889 HOH   B O     1 
HETATM 19869 O  O     . HOH   FA 11 .    ? 2.258   40.417  114.359 1.00 27.61 ? 1890 HOH   B O     1 
HETATM 19870 O  O     . HOH   FA 11 .    ? 9.674   -5.830  109.053 1.00 39.67 ? 1891 HOH   B O     1 
HETATM 19871 O  O     . HOH   FA 11 .    ? 15.980  7.059   108.150 1.00 34.52 ? 1892 HOH   B O     1 
HETATM 19872 O  O     . HOH   FA 11 .    ? 3.913   19.189  60.274  1.00 37.60 ? 1893 HOH   B O     1 
HETATM 19873 O  O     . HOH   FA 11 .    ? 9.432   18.977  103.692 1.00 23.20 ? 1894 HOH   B O     1 
HETATM 19874 O  O     . HOH   FA 11 .    ? 12.532  6.137   84.455  1.00 23.06 ? 1895 HOH   B O     1 
HETATM 19875 O  O     . HOH   FA 11 .    ? -14.433 7.260   120.150 1.00 29.65 ? 1896 HOH   B O     1 
HETATM 19876 O  O     . HOH   FA 11 .    ? 29.149  24.150  51.038  1.00 33.25 ? 1897 HOH   B O     1 
HETATM 19877 O  O     . HOH   FA 11 .    ? -4.096  42.500  108.225 1.00 33.26 ? 1898 HOH   B O     1 
HETATM 19878 O  O     . HOH   FA 11 .    ? 19.600  16.130  63.483  1.00 20.77 ? 1899 HOH   B O     1 
HETATM 19879 O  O     . HOH   FA 11 .    ? -10.776 12.085  79.675  1.00 41.51 ? 1900 HOH   B O     1 
HETATM 19880 O  O     . HOH   FA 11 .    ? -0.639  55.941  121.688 1.00 35.88 ? 1901 HOH   B O     1 
HETATM 19881 O  O     . HOH   FA 11 .    ? 4.916   21.979  83.728  1.00 23.81 ? 1902 HOH   B O     1 
HETATM 19882 O  O     . HOH   FA 11 .    ? -0.283  73.361  77.705  1.00 30.17 ? 1903 HOH   B O     1 
HETATM 19883 O  O     . HOH   FA 11 .    ? 0.462   27.008  94.683  1.00 21.64 ? 1904 HOH   B O     1 
HETATM 19884 O  O     . HOH   FA 11 .    ? -5.044  16.398  96.836  1.00 17.14 ? 1905 HOH   B O     1 
HETATM 19885 O  O     . HOH   FA 11 .    ? 25.098  53.458  68.452  1.00 25.07 ? 1906 HOH   B O     1 
HETATM 19886 O  O     . HOH   FA 11 .    ? 35.246  19.401  59.825  1.00 36.95 ? 1907 HOH   B O     1 
HETATM 19887 O  O     . HOH   FA 11 .    ? -11.208 20.495  88.039  1.00 22.69 ? 1908 HOH   B O     1 
HETATM 19888 O  O     . HOH   FA 11 .    ? -14.462 24.074  108.319 1.00 25.81 ? 1909 HOH   B O     1 
HETATM 19889 O  O     . HOH   FA 11 .    ? -4.738  36.966  89.793  1.00 33.05 ? 1910 HOH   B O     1 
HETATM 19890 O  O     . HOH   FA 11 .    ? 30.105  20.358  76.759  1.00 29.18 ? 1911 HOH   B O     1 
HETATM 19891 O  O     . HOH   FA 11 .    ? 8.182   13.857  71.615  1.00 24.61 ? 1912 HOH   B O     1 
HETATM 19892 O  O     . HOH   FA 11 .    ? 2.700   49.063  76.028  1.00 20.12 ? 1913 HOH   B O     1 
HETATM 19893 O  O     . HOH   FA 11 .    ? 25.999  17.545  96.857  1.00 43.25 ? 1914 HOH   B O     1 
HETATM 19894 O  O     . HOH   FA 11 .    ? 26.350  39.853  52.766  1.00 28.07 ? 1915 HOH   B O     1 
HETATM 19895 O  O     . HOH   FA 11 .    ? 9.167   61.901  85.144  1.00 27.07 ? 1916 HOH   B O     1 
HETATM 19896 O  O     . HOH   FA 11 .    ? -23.919 23.992  104.424 1.00 36.46 ? 1917 HOH   B O     1 
HETATM 19897 O  O     . HOH   FA 11 .    ? 4.740   46.695  69.103  1.00 17.54 ? 1918 HOH   B O     1 
HETATM 19898 O  O     . HOH   FA 11 .    ? -13.465 12.607  93.803  1.00 18.70 ? 1919 HOH   B O     1 
HETATM 19899 O  O     . HOH   FA 11 .    ? 27.928  10.704  84.776  1.00 28.28 ? 1920 HOH   B O     1 
HETATM 19900 O  O     . HOH   FA 11 .    ? 27.118  35.385  90.848  1.00 18.74 ? 1921 HOH   B O     1 
HETATM 19901 O  O     . HOH   FA 11 .    ? 27.569  39.649  104.511 1.00 32.28 ? 1922 HOH   B O     1 
HETATM 19902 O  O     . HOH   FA 11 .    ? -6.121  34.600  83.714  1.00 27.60 ? 1923 HOH   B O     1 
HETATM 19903 O  O     . HOH   FA 11 .    ? -0.970  14.852  130.968 1.00 34.27 ? 1924 HOH   B O     1 
HETATM 19904 O  O     . HOH   FA 11 .    ? 23.994  31.569  110.317 1.00 29.84 ? 1925 HOH   B O     1 
HETATM 19905 O  O     . HOH   FA 11 .    ? 17.947  49.954  111.566 1.00 32.69 ? 1926 HOH   B O     1 
HETATM 19906 O  O     . HOH   FA 11 .    ? -0.984  20.765  89.433  1.00 18.86 ? 1927 HOH   B O     1 
HETATM 19907 O  O     . HOH   FA 11 .    ? 36.034  31.524  103.513 1.00 33.13 ? 1928 HOH   B O     1 
HETATM 19908 O  O     . HOH   FA 11 .    ? 25.993  8.803   78.792  1.00 36.37 ? 1929 HOH   B O     1 
HETATM 19909 O  O     . HOH   FA 11 .    ? 11.562  34.501  51.899  1.00 30.63 ? 1930 HOH   B O     1 
HETATM 19910 O  O     . HOH   FA 11 .    ? 5.670   11.935  77.606  1.00 33.00 ? 1931 HOH   B O     1 
HETATM 19911 O  O     . HOH   FA 11 .    ? 8.280   62.832  66.175  1.00 34.62 ? 1932 HOH   B O     1 
HETATM 19912 O  O     . HOH   FA 11 .    ? 29.682  60.284  58.948  1.00 29.14 ? 1933 HOH   B O     1 
HETATM 19913 O  O     . HOH   FA 11 .    ? -14.418 39.989  124.663 1.00 41.16 ? 1934 HOH   B O     1 
HETATM 19914 O  O     . HOH   FA 11 .    ? 35.624  38.845  90.416  1.00 32.81 ? 1935 HOH   B O     1 
HETATM 19915 O  O     . HOH   FA 11 .    ? 26.294  27.671  67.045  1.00 17.35 ? 1936 HOH   B O     1 
HETATM 19916 O  O     . HOH   FA 11 .    ? -1.600  25.472  79.901  1.00 23.12 ? 1937 HOH   B O     1 
HETATM 19917 O  O     . HOH   FA 11 .    ? 19.072  52.103  79.929  1.00 24.02 ? 1938 HOH   B O     1 
HETATM 19918 O  O     . HOH   FA 11 .    ? 22.886  11.926  87.563  1.00 29.98 ? 1939 HOH   B O     1 
HETATM 19919 O  O     . HOH   FA 11 .    ? 22.614  54.371  92.969  1.00 25.26 ? 1940 HOH   B O     1 
HETATM 19920 O  O     . HOH   FA 11 .    ? 20.269  54.185  81.190  1.00 24.80 ? 1941 HOH   B O     1 
HETATM 19921 O  O     . HOH   FA 11 .    ? -7.814  48.296  76.533  1.00 31.41 ? 1942 HOH   B O     1 
HETATM 19922 O  O     . HOH   FA 11 .    ? 6.970   -8.360  107.289 1.00 35.48 ? 1943 HOH   B O     1 
HETATM 19923 O  O     . HOH   FA 11 .    ? 3.754   33.683  92.861  1.00 22.07 ? 1944 HOH   B O     1 
HETATM 19924 O  O     . HOH   FA 11 .    ? 19.202  8.281   83.991  1.00 26.28 ? 1945 HOH   B O     1 
HETATM 19925 O  O     . HOH   FA 11 .    ? 10.664  33.420  109.308 1.00 27.46 ? 1946 HOH   B O     1 
HETATM 19926 O  O     . HOH   FA 11 .    ? 12.707  37.406  107.842 1.00 24.18 ? 1947 HOH   B O     1 
HETATM 19927 O  O     . HOH   FA 11 .    ? -2.398  60.206  120.016 1.00 28.65 ? 1948 HOH   B O     1 
HETATM 19928 O  O     . HOH   FA 11 .    ? -4.475  44.686  108.582 1.00 33.42 ? 1949 HOH   B O     1 
HETATM 19929 O  O     . HOH   FA 11 .    ? 9.525   29.385  98.187  1.00 29.86 ? 1950 HOH   B O     1 
HETATM 19930 O  O     . HOH   FA 11 .    ? 32.634  33.236  70.597  1.00 27.80 ? 1951 HOH   B O     1 
HETATM 19931 O  O     . HOH   FA 11 .    ? 35.623  25.519  77.681  1.00 26.23 ? 1952 HOH   B O     1 
HETATM 19932 O  O     . HOH   FA 11 .    ? 23.639  51.821  83.681  1.00 27.29 ? 1953 HOH   B O     1 
HETATM 19933 O  O     . HOH   FA 11 .    ? -28.718 17.573  117.587 1.00 36.68 ? 1954 HOH   B O     1 
HETATM 19934 O  O     . HOH   FA 11 .    ? -3.327  66.303  77.069  1.00 33.01 ? 1955 HOH   B O     1 
HETATM 19935 O  O     . HOH   FA 11 .    ? 11.797  26.199  101.737 1.00 27.94 ? 1956 HOH   B O     1 
HETATM 19936 O  O     . HOH   FA 11 .    ? 5.741   18.636  87.318  1.00 26.23 ? 1957 HOH   B O     1 
HETATM 19937 O  O     . HOH   FA 11 .    ? -36.640 8.171   96.721  1.00 41.93 ? 1958 HOH   B O     1 
HETATM 19938 O  O     . HOH   FA 11 .    ? 31.070  67.302  82.365  1.00 34.06 ? 1959 HOH   B O     1 
HETATM 19939 O  O     . HOH   FA 11 .    ? 14.846  16.725  91.951  1.00 23.71 ? 1960 HOH   B O     1 
HETATM 19940 O  O     . HOH   FA 11 .    ? 14.520  45.748  78.203  1.00 19.87 ? 1961 HOH   B O     1 
HETATM 19941 O  O     . HOH   FA 11 .    ? -3.350  46.074  106.769 1.00 24.20 ? 1962 HOH   B O     1 
HETATM 19942 O  O     . HOH   FA 11 .    ? 9.054   6.097   85.023  1.00 22.21 ? 1963 HOH   B O     1 
HETATM 19943 O  O     . HOH   FA 11 .    ? -23.617 23.288  84.429  1.00 35.35 ? 1964 HOH   B O     1 
HETATM 19944 O  O     . HOH   FA 11 .    ? 24.933  63.201  54.353  1.00 32.74 ? 1965 HOH   B O     1 
HETATM 19945 O  O     . HOH   FA 11 .    ? -30.044 17.083  124.155 1.00 39.99 ? 1966 HOH   B O     1 
HETATM 19946 O  O     . HOH   FA 11 .    ? -11.297 -2.023  96.479  1.00 29.08 ? 1967 HOH   B O     1 
HETATM 19947 O  O     . HOH   FA 11 .    ? 30.465  20.349  73.705  1.00 34.95 ? 1968 HOH   B O     1 
HETATM 19948 O  O     . HOH   FA 11 .    ? 15.308  49.037  57.093  1.00 28.36 ? 1969 HOH   B O     1 
HETATM 19949 O  O     . HOH   FA 11 .    ? -16.190 4.660   92.801  1.00 40.92 ? 1970 HOH   B O     1 
HETATM 19950 O  O     . HOH   FA 11 .    ? -6.200  48.016  78.775  1.00 37.09 ? 1971 HOH   B O     1 
HETATM 19951 O  O     . HOH   FA 11 .    ? -14.836 18.791  80.082  1.00 37.00 ? 1972 HOH   B O     1 
HETATM 19952 O  O     . HOH   FA 11 .    ? -5.343  23.142  80.596  1.00 21.21 ? 1973 HOH   B O     1 
HETATM 19953 O  O     . HOH   FA 11 .    ? 4.993   47.589  87.057  1.00 20.09 ? 1974 HOH   B O     1 
HETATM 19954 O  O     . HOH   FA 11 .    ? -1.467  -2.714  118.787 1.00 37.90 ? 1975 HOH   B O     1 
HETATM 19955 O  O     . HOH   FA 11 .    ? -5.644  35.582  87.630  1.00 32.30 ? 1976 HOH   B O     1 
HETATM 19956 O  O     . HOH   FA 11 .    ? -32.435 16.485  98.445  1.00 39.06 ? 1977 HOH   B O     1 
HETATM 19957 O  O     . HOH   FA 11 .    ? 17.490  34.135  68.352  1.00 15.35 ? 1978 HOH   B O     1 
HETATM 19958 O  O     . HOH   FA 11 .    ? 28.391  44.427  89.718  1.00 26.55 ? 1979 HOH   B O     1 
HETATM 19959 O  O     . HOH   FA 11 .    ? 28.138  75.864  70.859  1.00 42.84 ? 1980 HOH   B O     1 
HETATM 19960 O  O     . HOH   FA 11 .    ? 12.640  2.316   92.131  1.00 37.03 ? 1981 HOH   B O     1 
HETATM 19961 O  O     . HOH   FA 11 .    ? 3.943   10.585  92.288  1.00 19.88 ? 1982 HOH   B O     1 
HETATM 19962 O  O     . HOH   FA 11 .    ? 43.850  36.954  87.956  1.00 30.41 ? 1983 HOH   B O     1 
HETATM 19963 O  O     . HOH   FA 11 .    ? 28.223  25.646  67.677  1.00 20.80 ? 1984 HOH   B O     1 
HETATM 19964 O  O     . HOH   FA 11 .    ? 14.200  34.569  111.898 1.00 40.17 ? 1985 HOH   B O     1 
HETATM 19965 O  O     . HOH   FA 11 .    ? 39.543  26.851  87.637  1.00 35.64 ? 1986 HOH   B O     1 
HETATM 19966 O  O     . HOH   FA 11 .    ? 18.182  23.315  61.363  1.00 21.87 ? 1987 HOH   B O     1 
HETATM 19967 O  O     . HOH   FA 11 .    ? 15.373  62.031  84.503  1.00 35.99 ? 1988 HOH   B O     1 
HETATM 19968 O  O     . HOH   FA 11 .    ? 11.707  18.038  94.865  1.00 31.59 ? 1989 HOH   B O     1 
HETATM 19969 O  O     . HOH   FA 11 .    ? -6.472  11.303  127.526 1.00 31.94 ? 1990 HOH   B O     1 
HETATM 19970 O  O     . HOH   FA 11 .    ? 22.059  46.377  76.669  1.00 21.11 ? 1991 HOH   B O     1 
HETATM 19971 O  O     . HOH   FA 11 .    ? -6.051  41.728  84.096  1.00 36.28 ? 1992 HOH   B O     1 
HETATM 19972 O  O     . HOH   FA 11 .    ? 8.431   37.476  79.125  1.00 18.71 ? 1993 HOH   B O     1 
HETATM 19973 O  O     . HOH   FA 11 .    ? -5.216  -2.183  116.953 1.00 28.74 ? 1994 HOH   B O     1 
HETATM 19974 O  O     . HOH   FA 11 .    ? -0.299  17.977  91.409  1.00 26.29 ? 1995 HOH   B O     1 
HETATM 19975 O  O     . HOH   FA 11 .    ? 33.497  19.374  87.533  1.00 24.39 ? 1996 HOH   B O     1 
HETATM 19976 O  O     . HOH   FA 11 .    ? 24.812  50.940  67.001  1.00 22.98 ? 1997 HOH   B O     1 
HETATM 19977 O  O     . HOH   FA 11 .    ? 27.265  18.352  61.931  1.00 23.91 ? 1998 HOH   B O     1 
HETATM 19978 O  O     . HOH   FA 11 .    ? 24.928  16.120  95.097  1.00 26.88 ? 1999 HOH   B O     1 
HETATM 19979 O  O     . HOH   FA 11 .    ? 5.006   18.664  124.139 1.00 29.35 ? 2000 HOH   B O     1 
HETATM 19980 O  O     . HOH   FA 11 .    ? -1.661  36.803  87.363  1.00 24.01 ? 2001 HOH   B O     1 
HETATM 19981 O  O     . HOH   FA 11 .    ? 18.696  48.067  89.936  1.00 22.32 ? 2002 HOH   B O     1 
HETATM 19982 O  O     . HOH   FA 11 .    ? 33.097  25.577  101.885 1.00 29.88 ? 2003 HOH   B O     1 
HETATM 19983 O  O     . HOH   FA 11 .    ? 0.441   36.605  108.754 1.00 35.00 ? 2004 HOH   B O     1 
HETATM 19984 O  O     . HOH   FA 11 .    ? -2.865  10.984  103.767 1.00 16.86 ? 2005 HOH   B O     1 
HETATM 19985 O  O     . HOH   FA 11 .    ? 28.730  46.482  87.830  1.00 28.73 ? 2006 HOH   B O     1 
HETATM 19986 O  O     . HOH   FA 11 .    ? 29.553  41.646  79.928  1.00 26.81 ? 2007 HOH   B O     1 
HETATM 19987 O  O     . HOH   FA 11 .    ? 4.440   77.273  63.062  1.00 36.42 ? 2008 HOH   B O     1 
HETATM 19988 O  O     . HOH   FA 11 .    ? 32.560  40.539  90.535  1.00 33.88 ? 2009 HOH   B O     1 
HETATM 19989 O  O     . HOH   FA 11 .    ? -15.908 52.068  123.415 1.00 38.42 ? 2010 HOH   B O     1 
HETATM 19990 O  O     . HOH   FA 11 .    ? 10.224  22.063  102.630 1.00 32.00 ? 2011 HOH   B O     1 
HETATM 19991 O  O     . HOH   FA 11 .    ? 1.732   46.498  98.814  1.00 28.25 ? 2012 HOH   B O     1 
HETATM 19992 O  O     A HOH   FA 11 .    ? 0.541   63.563  84.580  0.50 23.12 ? 2013 HOH   B O     1 
HETATM 19993 O  O     . HOH   FA 11 .    ? 32.556  29.320  64.502  1.00 24.66 ? 2014 HOH   B O     1 
HETATM 19994 O  O     . HOH   FA 11 .    ? 4.692   77.763  80.260  1.00 29.15 ? 2015 HOH   B O     1 
HETATM 19995 O  O     . HOH   FA 11 .    ? 18.576  34.505  46.080  1.00 36.54 ? 2016 HOH   B O     1 
HETATM 19996 O  O     . HOH   FA 11 .    ? -6.934  43.996  73.681  1.00 31.31 ? 2017 HOH   B O     1 
HETATM 19997 O  O     . HOH   FA 11 .    ? -8.490  31.627  86.790  1.00 19.46 ? 2018 HOH   B O     1 
HETATM 19998 O  O     . HOH   FA 11 .    ? 25.694  45.719  107.764 1.00 42.43 ? 2019 HOH   B O     1 
HETATM 19999 O  O     . HOH   FA 11 .    ? -10.462 1.836   91.241  1.00 24.14 ? 2020 HOH   B O     1 
HETATM 20000 O  O     . HOH   FA 11 .    ? 1.782   65.803  65.622  1.00 39.45 ? 2021 HOH   B O     1 
HETATM 20001 O  O     . HOH   FA 11 .    ? -0.822  13.589  100.687 1.00 19.97 ? 2022 HOH   B O     1 
HETATM 20002 O  O     . HOH   FA 11 .    ? -16.243 22.201  82.262  1.00 26.69 ? 2023 HOH   B O     1 
HETATM 20003 O  O     . HOH   FA 11 .    ? -22.857 25.859  103.292 1.00 35.72 ? 2024 HOH   B O     1 
HETATM 20004 O  O     . HOH   FA 11 .    ? 4.814   60.611  67.805  1.00 39.49 ? 2025 HOH   B O     1 
HETATM 20005 O  O     . HOH   FA 11 .    ? 1.488   22.489  63.512  1.00 26.41 ? 2026 HOH   B O     1 
HETATM 20006 O  O     . HOH   FA 11 .    ? -4.611  56.506  126.990 1.00 37.37 ? 2027 HOH   B O     1 
HETATM 20007 O  O     . HOH   FA 11 .    ? 5.258   42.795  70.645  1.00 14.07 ? 2028 HOH   B O     1 
HETATM 20008 O  O     . HOH   FA 11 .    ? 34.584  13.106  80.809  1.00 33.44 ? 2029 HOH   B O     1 
HETATM 20009 O  O     . HOH   FA 11 .    ? 34.858  16.968  67.534  1.00 30.12 ? 2030 HOH   B O     1 
HETATM 20010 O  O     . HOH   FA 11 .    ? -9.210  14.138  114.608 1.00 28.61 ? 2031 HOH   B O     1 
HETATM 20011 O  O     . HOH   FA 11 .    ? 0.808   0.145   96.033  1.00 27.77 ? 2032 HOH   B O     1 
HETATM 20012 O  O     . HOH   FA 11 .    ? 30.752  34.279  84.458  1.00 27.60 ? 2033 HOH   B O     1 
HETATM 20013 O  O     . HOH   FA 11 .    ? 14.917  7.041   68.741  1.00 30.52 ? 2034 HOH   B O     1 
HETATM 20014 O  O     . HOH   FA 11 .    ? -20.965 1.365   120.988 1.00 36.71 ? 2035 HOH   B O     1 
HETATM 20015 O  O     . HOH   FA 11 .    ? -13.445 48.950  110.565 1.00 31.31 ? 2036 HOH   B O     1 
HETATM 20016 O  O     . HOH   FA 11 .    ? 18.070  76.544  63.746  1.00 30.83 ? 2037 HOH   B O     1 
HETATM 20017 O  O     . HOH   FA 11 .    ? -2.425  14.567  98.701  1.00 17.13 ? 2038 HOH   B O     1 
HETATM 20018 O  O     . HOH   FA 11 .    ? -10.621 52.438  128.389 1.00 36.33 ? 2039 HOH   B O     1 
HETATM 20019 O  O     . HOH   FA 11 .    ? -4.109  53.984  130.730 1.00 37.23 ? 2040 HOH   B O     1 
HETATM 20020 O  O     . HOH   FA 11 .    ? 35.069  32.472  54.935  1.00 29.85 ? 2041 HOH   B O     1 
HETATM 20021 O  O     . HOH   FA 11 .    ? 35.724  33.132  80.834  1.00 38.35 ? 2042 HOH   B O     1 
HETATM 20022 O  O     . HOH   FA 11 .    ? 16.406  21.534  99.721  1.00 22.85 ? 2043 HOH   B O     1 
HETATM 20023 O  O     . HOH   FA 11 .    ? -20.315 25.456  94.419  1.00 27.51 ? 2044 HOH   B O     1 
HETATM 20024 O  O     . HOH   FA 11 .    ? 18.621  53.251  75.882  1.00 21.36 ? 2045 HOH   B O     1 
HETATM 20025 O  O     . HOH   FA 11 .    ? -26.767 34.155  100.630 1.00 50.35 ? 2046 HOH   B O     1 
HETATM 20026 O  O     . HOH   FA 11 .    ? 11.446  26.548  51.902  1.00 29.17 ? 2047 HOH   B O     1 
HETATM 20027 O  O     . HOH   FA 11 .    ? 20.367  19.014  60.220  1.00 27.16 ? 2048 HOH   B O     1 
HETATM 20028 O  O     . HOH   FA 11 .    ? -1.549  49.409  101.112 1.00 33.34 ? 2049 HOH   B O     1 
HETATM 20029 O  O     . HOH   FA 11 .    ? 18.395  23.428  85.100  1.00 20.14 ? 2050 HOH   B O     1 
HETATM 20030 O  O     . HOH   FA 11 .    ? 23.024  9.773   85.051  1.00 38.05 ? 2051 HOH   B O     1 
HETATM 20031 O  O     . HOH   FA 11 .    ? -14.110 9.528   87.336  1.00 23.77 ? 2052 HOH   B O     1 
HETATM 20032 O  O     . HOH   FA 11 .    ? 2.086   30.716  95.921  1.00 21.77 ? 2053 HOH   B O     1 
HETATM 20033 O  O     . HOH   FA 11 .    ? 8.086   58.130  85.146  1.00 24.00 ? 2054 HOH   B O     1 
HETATM 20034 O  O     . HOH   FA 11 .    ? -29.651 18.356  103.566 1.00 32.03 ? 2055 HOH   B O     1 
HETATM 20035 O  O     . HOH   FA 11 .    ? 33.392  23.216  64.453  1.00 33.52 ? 2056 HOH   B O     1 
HETATM 20036 O  O     . HOH   FA 11 .    ? -1.743  28.203  62.705  1.00 29.99 ? 2057 HOH   B O     1 
HETATM 20037 O  O     . HOH   FA 11 .    ? -14.121 44.681  113.152 1.00 39.31 ? 2058 HOH   B O     1 
HETATM 20038 O  O     . HOH   FA 11 .    ? 27.042  65.811  57.828  1.00 39.05 ? 2059 HOH   B O     1 
HETATM 20039 O  O     . HOH   FA 11 .    ? -2.161  -7.452  110.418 1.00 25.15 ? 2060 HOH   B O     1 
HETATM 20040 O  O     . HOH   FA 11 .    ? 10.061  53.220  65.551  1.00 25.09 ? 2061 HOH   B O     1 
HETATM 20041 O  O     . HOH   FA 11 .    ? 16.240  56.057  63.824  1.00 28.30 ? 2062 HOH   B O     1 
HETATM 20042 O  O     . HOH   FA 11 .    ? -7.063  27.863  74.384  1.00 30.59 ? 2063 HOH   B O     1 
HETATM 20043 O  O     . HOH   FA 11 .    ? 13.187  27.491  45.886  1.00 32.08 ? 2064 HOH   B O     1 
HETATM 20044 O  O     . HOH   FA 11 .    ? 33.070  47.106  87.504  1.00 45.18 ? 2065 HOH   B O     1 
HETATM 20045 O  O     . HOH   FA 11 .    ? 5.775   53.419  113.264 1.00 37.31 ? 2066 HOH   B O     1 
HETATM 20046 O  O     . HOH   FA 11 .    ? -2.887  39.869  57.751  1.00 25.69 ? 2067 HOH   B O     1 
HETATM 20047 O  O     . HOH   FA 11 .    ? 3.240   31.370  98.226  1.00 29.08 ? 2068 HOH   B O     1 
HETATM 20048 O  O     . HOH   FA 11 .    ? 2.699   48.981  98.927  1.00 24.71 ? 2069 HOH   B O     1 
HETATM 20049 O  O     . HOH   FA 11 .    ? 9.962   18.398  100.964 1.00 26.00 ? 2070 HOH   B O     1 
HETATM 20050 O  O     . HOH   FA 11 .    ? 16.053  10.341  95.549  1.00 24.77 ? 2071 HOH   B O     1 
HETATM 20051 O  O     . HOH   FA 11 .    ? -12.016 34.860  86.221  1.00 43.43 ? 2072 HOH   B O     1 
HETATM 20052 O  O     . HOH   FA 11 .    ? 34.175  22.476  78.159  1.00 24.90 ? 2073 HOH   B O     1 
HETATM 20053 O  O     . HOH   FA 11 .    ? -31.640 14.682  114.097 1.00 37.44 ? 2074 HOH   B O     1 
HETATM 20054 O  O     . HOH   FA 11 .    ? 31.021  20.038  56.122  1.00 29.82 ? 2075 HOH   B O     1 
HETATM 20055 O  O     . HOH   FA 11 .    ? -4.052  52.722  79.852  1.00 31.82 ? 2076 HOH   B O     1 
HETATM 20056 O  O     . HOH   FA 11 .    ? 16.434  53.680  104.827 1.00 28.05 ? 2077 HOH   B O     1 
HETATM 20057 O  O     . HOH   FA 11 .    ? -7.310  13.249  94.472  1.00 18.20 ? 2078 HOH   B O     1 
HETATM 20058 O  O     . HOH   FA 11 .    ? 5.044   57.752  68.824  1.00 25.90 ? 2079 HOH   B O     1 
HETATM 20059 O  O     . HOH   FA 11 .    ? -10.035 18.339  130.941 1.00 35.67 ? 2080 HOH   B O     1 
HETATM 20060 O  O     . HOH   FA 11 .    ? 28.938  22.626  72.180  1.00 31.92 ? 2081 HOH   B O     1 
HETATM 20061 O  O     . HOH   FA 11 .    ? 3.019   23.251  58.823  1.00 32.85 ? 2082 HOH   B O     1 
HETATM 20062 O  O     . HOH   FA 11 .    ? 22.134  25.164  82.477  1.00 23.80 ? 2083 HOH   B O     1 
HETATM 20063 O  O     . HOH   FA 11 .    ? -13.334 53.966  122.533 1.00 32.80 ? 2084 HOH   B O     1 
HETATM 20064 O  O     . HOH   FA 11 .    ? -15.245 10.332  89.731  1.00 19.58 ? 2085 HOH   B O     1 
HETATM 20065 O  O     . HOH   FA 11 .    ? -11.769 22.068  85.573  1.00 24.90 ? 2086 HOH   B O     1 
HETATM 20066 O  O     . HOH   FA 11 .    ? -13.905 -7.926  103.189 1.00 36.96 ? 2087 HOH   B O     1 
HETATM 20067 O  O     . HOH   FA 11 .    ? 7.324   66.370  86.347  1.00 36.46 ? 2088 HOH   B O     1 
HETATM 20068 O  O     . HOH   FA 11 .    ? 0.375   11.157  80.914  1.00 35.13 ? 2089 HOH   B O     1 
HETATM 20069 O  O     . HOH   FA 11 .    ? 22.648  61.553  82.978  1.00 36.72 ? 2090 HOH   B O     1 
HETATM 20070 O  O     . HOH   FA 11 .    ? 16.932  46.974  54.601  1.00 33.96 ? 2091 HOH   B O     1 
HETATM 20071 O  O     . HOH   FA 11 .    ? 31.671  62.395  74.980  1.00 22.15 ? 2092 HOH   B O     1 
HETATM 20072 O  O     . HOH   FA 11 .    ? -10.652 36.450  76.247  1.00 38.90 ? 2093 HOH   B O     1 
HETATM 20073 O  O     . HOH   FA 11 .    ? -5.926  35.770  92.451  1.00 31.36 ? 2094 HOH   B O     1 
HETATM 20074 O  O     . HOH   FA 11 .    ? -9.334  0.659   112.434 1.00 25.72 ? 2095 HOH   B O     1 
HETATM 20075 O  O     . HOH   FA 11 .    ? -0.526  -7.834  99.401  1.00 26.39 ? 2096 HOH   B O     1 
HETATM 20076 O  O     . HOH   FA 11 .    ? -19.471 24.086  112.471 1.00 33.77 ? 2097 HOH   B O     1 
HETATM 20077 O  O     . HOH   FA 11 .    ? 24.151  31.510  46.993  1.00 39.43 ? 2098 HOH   B O     1 
HETATM 20078 O  O     . HOH   FA 11 .    ? 1.456   38.508  105.477 1.00 34.75 ? 2099 HOH   B O     1 
HETATM 20079 O  O     . HOH   FA 11 .    ? -2.488  30.494  70.590  1.00 19.94 ? 2100 HOH   B O     1 
HETATM 20080 O  O     . HOH   FA 11 .    ? 2.938   44.263  58.414  1.00 31.81 ? 2101 HOH   B O     1 
HETATM 20081 O  O     . HOH   FA 11 .    ? 8.237   31.788  93.860  1.00 23.29 ? 2102 HOH   B O     1 
HETATM 20082 O  O     . HOH   FA 11 .    ? 14.206  75.756  62.856  1.00 27.98 ? 2103 HOH   B O     1 
HETATM 20083 O  O     . HOH   FA 11 .    ? 2.224   62.285  68.514  1.00 39.51 ? 2104 HOH   B O     1 
HETATM 20084 O  O     . HOH   FA 11 .    ? 8.558   15.927  92.648  1.00 32.55 ? 2105 HOH   B O     1 
HETATM 20085 O  O     . HOH   FA 11 .    ? 23.120  72.857  81.676  1.00 32.14 ? 2106 HOH   B O     1 
HETATM 20086 O  O     . HOH   FA 11 .    ? 31.304  51.171  79.734  1.00 31.12 ? 2107 HOH   B O     1 
HETATM 20087 O  O     . HOH   FA 11 .    ? 25.123  18.095  100.155 1.00 35.38 ? 2108 HOH   B O     1 
HETATM 20088 O  O     . HOH   FA 11 .    ? -5.470  46.627  84.129  1.00 24.79 ? 2109 HOH   B O     1 
HETATM 20089 O  O     . HOH   FA 11 .    ? -2.639  64.576  83.277  1.00 18.61 ? 2110 HOH   B O     1 
HETATM 20090 O  O     . HOH   FA 11 .    ? -7.947  35.813  80.766  1.00 36.93 ? 2111 HOH   B O     1 
HETATM 20091 O  O     . HOH   FA 11 .    ? 21.099  47.681  55.812  1.00 30.89 ? 2112 HOH   B O     1 
HETATM 20092 O  O     . HOH   FA 11 .    ? 29.665  8.878   86.122  1.00 38.12 ? 2113 HOH   B O     1 
HETATM 20093 O  O     . HOH   FA 11 .    ? 28.437  49.177  97.765  1.00 36.89 ? 2114 HOH   B O     1 
HETATM 20094 O  O     . HOH   FA 11 .    ? 10.367  28.715  49.489  1.00 38.41 ? 2115 HOH   B O     1 
HETATM 20095 O  O     . HOH   FA 11 .    ? 2.929   45.074  67.804  1.00 19.03 ? 2116 HOH   B O     1 
HETATM 20096 O  O     . HOH   FA 11 .    ? 7.759   54.384  64.454  1.00 30.33 ? 2117 HOH   B O     1 
HETATM 20097 O  O     . HOH   FA 11 .    ? 5.844   70.427  60.950  1.00 38.41 ? 2118 HOH   B O     1 
HETATM 20098 O  O     . HOH   FA 11 .    ? -3.296  52.492  82.473  1.00 26.97 ? 2119 HOH   B O     1 
HETATM 20099 O  O     . HOH   FA 11 .    ? 20.233  20.482  109.165 1.00 22.04 ? 2120 HOH   B O     1 
HETATM 20100 O  O     . HOH   FA 11 .    ? 11.516  18.613  97.758  1.00 28.48 ? 2121 HOH   B O     1 
HETATM 20101 O  O     . HOH   FA 11 .    ? 16.981  51.381  59.884  1.00 28.57 ? 2122 HOH   B O     1 
HETATM 20102 O  O     . HOH   FA 11 .    ? 26.320  20.267  52.870  1.00 30.27 ? 2123 HOH   B O     1 
HETATM 20103 O  O     . HOH   FA 11 .    ? 7.415   2.296   126.509 1.00 41.94 ? 2124 HOH   B O     1 
HETATM 20104 O  O     . HOH   FA 11 .    ? -1.672  -0.913  108.966 1.00 29.35 ? 2125 HOH   B O     1 
HETATM 20105 O  O     . HOH   FA 11 .    ? 5.013   17.920  91.031  1.00 23.45 ? 2126 HOH   B O     1 
HETATM 20106 O  O     . HOH   FA 11 .    ? -19.299 28.948  88.293  1.00 30.47 ? 2127 HOH   B O     1 
HETATM 20107 O  O     . HOH   FA 11 .    ? 26.479  13.063  87.975  1.00 29.11 ? 2128 HOH   B O     1 
HETATM 20108 O  O     . HOH   FA 11 .    ? -1.782  62.517  69.571  1.00 36.22 ? 2129 HOH   B O     1 
HETATM 20109 O  O     . HOH   FA 11 .    ? -6.524  9.019   81.975  1.00 36.20 ? 2130 HOH   B O     1 
HETATM 20110 O  O     . HOH   FA 11 .    ? 4.872   56.284  74.861  1.00 18.85 ? 2131 HOH   B O     1 
HETATM 20111 O  O     . HOH   FA 11 .    ? 19.350  58.496  82.273  1.00 26.38 ? 2132 HOH   B O     1 
HETATM 20112 O  O     . HOH   FA 11 .    ? -17.494 54.707  121.191 1.00 38.38 ? 2133 HOH   B O     1 
HETATM 20113 O  O     . HOH   FA 11 .    ? 31.173  34.568  77.237  1.00 29.79 ? 2134 HOH   B O     1 
HETATM 20114 O  O     . HOH   FA 11 .    ? 13.272  48.010  81.885  1.00 27.28 ? 2135 HOH   B O     1 
HETATM 20115 O  O     . HOH   FA 11 .    ? 18.935  35.512  112.886 1.00 22.51 ? 2136 HOH   B O     1 
HETATM 20116 O  O     . HOH   FA 11 .    ? 29.183  65.424  62.361  1.00 31.20 ? 2137 HOH   B O     1 
HETATM 20117 O  O     . HOH   FA 11 .    ? 14.628  9.207   93.530  1.00 21.89 ? 2138 HOH   B O     1 
HETATM 20118 O  O     . HOH   FA 11 .    ? 13.477  18.735  87.399  1.00 24.93 ? 2139 HOH   B O     1 
HETATM 20119 O  O     . HOH   FA 11 .    ? -7.368  10.600  112.791 1.00 21.01 ? 2140 HOH   B O     1 
HETATM 20120 O  O     . HOH   FA 11 .    ? 16.128  8.213   110.810 1.00 34.25 ? 2141 HOH   B O     1 
HETATM 20121 O  O     . HOH   FA 11 .    ? 4.556   17.096  127.705 1.00 32.04 ? 2142 HOH   B O     1 
HETATM 20122 O  O     . HOH   FA 11 .    ? 8.070   77.619  85.628  1.00 39.20 ? 2143 HOH   B O     1 
HETATM 20123 O  O     . HOH   FA 11 .    ? 25.776  33.367  109.662 1.00 40.37 ? 2144 HOH   B O     1 
HETATM 20124 O  O     . HOH   FA 11 .    ? 19.861  78.186  77.065  1.00 40.40 ? 2145 HOH   B O     1 
HETATM 20125 O  O     . HOH   FA 11 .    ? -5.645  15.547  94.405  1.00 17.82 ? 2146 HOH   B O     1 
HETATM 20126 O  O     . HOH   FA 11 .    ? 19.372  54.596  104.069 1.00 27.95 ? 2147 HOH   B O     1 
HETATM 20127 O  O     . HOH   FA 11 .    ? -1.953  57.670  75.086  1.00 19.40 ? 2148 HOH   B O     1 
HETATM 20128 O  O     . HOH   FA 11 .    ? 4.695   0.291   86.631  1.00 32.45 ? 2149 HOH   B O     1 
HETATM 20129 O  O     . HOH   FA 11 .    ? 8.904   30.681  88.635  1.00 33.46 ? 2150 HOH   B O     1 
HETATM 20130 O  O     . HOH   FA 11 .    ? 0.657   26.251  112.141 1.00 48.43 ? 2151 HOH   B O     1 
HETATM 20131 O  O     . HOH   FA 11 .    ? 26.234  52.239  55.589  1.00 38.77 ? 2152 HOH   B O     1 
HETATM 20132 O  O     . HOH   FA 11 .    ? 23.034  51.375  65.095  1.00 22.83 ? 2153 HOH   B O     1 
HETATM 20133 O  O     . HOH   FA 11 .    ? -4.886  -3.813  91.653  1.00 29.67 ? 2154 HOH   B O     1 
HETATM 20134 O  O     . HOH   FA 11 .    ? 2.611   18.951  77.164  1.00 29.26 ? 2155 HOH   B O     1 
HETATM 20135 O  O     . HOH   FA 11 .    ? 29.519  32.423  103.209 1.00 28.09 ? 2156 HOH   B O     1 
HETATM 20136 O  O     . HOH   FA 11 .    ? 31.651  35.137  74.579  1.00 34.70 ? 2157 HOH   B O     1 
HETATM 20137 O  O     . HOH   FA 11 .    ? 18.094  14.710  105.168 1.00 37.44 ? 2158 HOH   B O     1 
HETATM 20138 O  O     . HOH   FA 11 .    ? -23.942 10.497  126.798 1.00 42.19 ? 2159 HOH   B O     1 
HETATM 20139 O  O     . HOH   FA 11 .    ? 5.082   43.050  55.869  1.00 30.54 ? 2160 HOH   B O     1 
HETATM 20140 O  O     . HOH   FA 11 .    ? 29.156  35.389  78.562  1.00 36.16 ? 2161 HOH   B O     1 
HETATM 20141 O  O     . HOH   FA 11 .    ? 20.692  21.964  60.939  1.00 18.78 ? 2162 HOH   B O     1 
HETATM 20142 O  O     . HOH   FA 11 .    ? -7.514  23.991  125.208 1.00 37.47 ? 2163 HOH   B O     1 
HETATM 20143 O  O     . HOH   FA 11 .    ? 22.184  14.985  81.023  1.00 25.48 ? 2164 HOH   B O     1 
HETATM 20144 O  O     . HOH   FA 11 .    ? -12.063 7.956   126.997 1.00 30.76 ? 2165 HOH   B O     1 
HETATM 20145 O  O     . HOH   FA 11 .    ? 8.793   25.542  46.407  1.00 30.88 ? 2166 HOH   B O     1 
HETATM 20146 O  O     . HOH   FA 11 .    ? -32.890 4.557   101.298 1.00 49.09 ? 2167 HOH   B O     1 
HETATM 20147 O  O     . HOH   FA 11 .    ? 42.565  32.218  96.472  1.00 40.10 ? 2168 HOH   B O     1 
HETATM 20148 O  O     . HOH   FA 11 .    ? 11.012  16.265  121.754 1.00 34.71 ? 2169 HOH   B O     1 
HETATM 20149 O  O     . HOH   FA 11 .    ? 15.591  49.542  78.844  1.00 25.43 ? 2170 HOH   B O     1 
HETATM 20150 O  O     . HOH   FA 11 .    ? -12.694 31.541  83.582  1.00 37.37 ? 2171 HOH   B O     1 
HETATM 20151 O  O     . HOH   FA 11 .    ? -32.720 7.932   108.240 1.00 44.05 ? 2172 HOH   B O     1 
HETATM 20152 O  O     . HOH   FA 11 .    ? 12.338  77.666  64.075  1.00 36.49 ? 2173 HOH   B O     1 
HETATM 20153 O  O     . HOH   FA 11 .    ? 12.766  29.525  50.374  1.00 28.55 ? 2174 HOH   B O     1 
HETATM 20154 O  O     . HOH   FA 11 .    ? 37.274  37.510  88.884  1.00 22.13 ? 2175 HOH   B O     1 
HETATM 20155 O  O     . HOH   FA 11 .    ? 2.422   30.155  54.568  1.00 36.81 ? 2176 HOH   B O     1 
HETATM 20156 O  O     . HOH   FA 11 .    ? 3.066   54.279  66.907  1.00 37.14 ? 2177 HOH   B O     1 
HETATM 20157 O  O     . HOH   FA 11 .    ? -14.387 27.019  101.345 1.00 30.72 ? 2178 HOH   B O     1 
HETATM 20158 O  O     . HOH   FA 11 .    ? -18.028 6.151   95.585  1.00 34.67 ? 2179 HOH   B O     1 
HETATM 20159 O  O     . HOH   FA 11 .    ? 23.982  17.206  82.585  1.00 23.89 ? 2180 HOH   B O     1 
HETATM 20160 O  O     . HOH   FA 11 .    ? -22.770 21.946  101.927 1.00 29.19 ? 2181 HOH   B O     1 
HETATM 20161 O  O     . HOH   FA 11 .    ? -14.862 19.417  82.534  1.00 27.74 ? 2182 HOH   B O     1 
HETATM 20162 O  O     . HOH   FA 11 .    ? 5.655   24.039  119.501 1.00 40.16 ? 2183 HOH   B O     1 
HETATM 20163 O  O     . HOH   FA 11 .    ? 16.399  14.070  106.792 1.00 27.87 ? 2184 HOH   B O     1 
HETATM 20164 O  O     . HOH   FA 11 .    ? -6.643  39.103  67.331  1.00 31.95 ? 2185 HOH   B O     1 
HETATM 20165 O  O     . HOH   FA 11 .    ? 25.090  46.929  104.128 1.00 41.98 ? 2186 HOH   B O     1 
HETATM 20166 O  O     . HOH   FA 11 .    ? -2.597  -5.400  89.608  1.00 32.29 ? 2187 HOH   B O     1 
HETATM 20167 O  O     . HOH   FA 11 .    ? 12.598  58.050  93.894  1.00 31.46 ? 2188 HOH   B O     1 
HETATM 20168 O  O     . HOH   FA 11 .    ? 34.245  25.302  92.796  1.00 34.70 ? 2189 HOH   B O     1 
HETATM 20169 O  O     . HOH   FA 11 .    ? 28.410  30.896  80.629  1.00 23.77 ? 2190 HOH   B O     1 
HETATM 20170 O  O     . HOH   FA 11 .    ? 18.133  75.982  78.713  1.00 36.39 ? 2191 HOH   B O     1 
HETATM 20171 O  O     . HOH   FA 11 .    ? 10.689  37.600  77.602  1.00 26.66 ? 2192 HOH   B O     1 
HETATM 20172 O  O     . HOH   FA 11 .    ? 14.506  35.379  81.701  1.00 25.59 ? 2193 HOH   B O     1 
HETATM 20173 O  O     . HOH   FA 11 .    ? 26.781  41.161  81.160  1.00 25.36 ? 2194 HOH   B O     1 
HETATM 20174 O  O     . HOH   FA 11 .    ? -16.705 49.394  116.453 1.00 38.56 ? 2195 HOH   B O     1 
HETATM 20175 O  O     . HOH   FA 11 .    ? 32.067  36.906  51.176  1.00 39.34 ? 2196 HOH   B O     1 
HETATM 20176 O  O     . HOH   FA 11 .    ? 32.288  45.123  61.598  1.00 35.36 ? 2197 HOH   B O     1 
HETATM 20177 O  O     . HOH   FA 11 .    ? -37.139 11.340  94.540  1.00 51.23 ? 2198 HOH   B O     1 
HETATM 20178 O  O     . HOH   FA 11 .    ? -1.022  37.811  76.190  1.00 28.87 ? 2199 HOH   B O     1 
HETATM 20179 O  O     . HOH   FA 11 .    ? 2.627   3.928   84.537  1.00 32.99 ? 2200 HOH   B O     1 
HETATM 20180 O  O     . HOH   FA 11 .    ? 23.414  24.564  47.470  1.00 34.13 ? 2201 HOH   B O     1 
HETATM 20181 O  O     . HOH   FA 11 .    ? 4.673   -3.755  94.976  1.00 39.13 ? 2202 HOH   B O     1 
HETATM 20182 O  O     . HOH   FA 11 .    ? 35.712  32.055  61.238  1.00 41.65 ? 2203 HOH   B O     1 
HETATM 20183 O  O     . HOH   FA 11 .    ? 38.006  22.950  90.127  1.00 44.72 ? 2204 HOH   B O     1 
HETATM 20184 O  O     . HOH   FA 11 .    ? 25.736  75.332  76.732  1.00 32.66 ? 2205 HOH   B O     1 
HETATM 20185 O  O     . HOH   FA 11 .    ? 8.700   -0.853  98.595  1.00 40.30 ? 2206 HOH   B O     1 
HETATM 20186 O  O     . HOH   FA 11 .    ? 42.389  37.738  95.697  1.00 33.66 ? 2207 HOH   B O     1 
HETATM 20187 O  O     . HOH   FA 11 .    ? 25.326  24.340  49.758  1.00 39.50 ? 2208 HOH   B O     1 
HETATM 20188 O  O     . HOH   FA 11 .    ? 35.601  31.562  58.268  1.00 31.95 ? 2209 HOH   B O     1 
HETATM 20189 O  O     . HOH   FA 11 .    ? 9.161   0.647   119.493 1.00 36.42 ? 2210 HOH   B O     1 
HETATM 20190 O  O     . HOH   FA 11 .    ? 10.198  77.162  65.312  1.00 42.12 ? 2211 HOH   B O     1 
HETATM 20191 O  O     . HOH   FA 11 .    ? 2.928   57.191  70.772  1.00 29.55 ? 2212 HOH   B O     1 
HETATM 20192 O  O     . HOH   FA 11 .    ? -4.176  26.706  99.696  1.00 26.09 ? 2213 HOH   B O     1 
HETATM 20193 O  O     . HOH   FA 11 .    ? -30.591 5.799   99.894  1.00 40.76 ? 2214 HOH   B O     1 
HETATM 20194 O  O     . HOH   FA 11 .    ? 33.517  38.201  71.835  1.00 39.01 ? 2215 HOH   B O     1 
HETATM 20195 O  O     . HOH   FA 11 .    ? 18.497  8.647   107.105 1.00 44.92 ? 2216 HOH   B O     1 
HETATM 20196 O  O     . HOH   FA 11 .    ? -2.341  60.132  124.079 1.00 38.73 ? 2217 HOH   B O     1 
HETATM 20197 O  O     . HOH   FA 11 .    ? -0.951  44.370  75.279  1.00 31.93 ? 2218 HOH   B O     1 
HETATM 20198 O  O     . HOH   FA 11 .    ? 32.835  20.365  72.229  1.00 37.89 ? 2219 HOH   B O     1 
HETATM 20199 O  O     . HOH   FA 11 .    ? 12.081  22.825  113.298 1.00 38.21 ? 2220 HOH   B O     1 
HETATM 20200 O  O     . HOH   FA 11 .    ? -0.270  44.889  77.228  1.00 36.51 ? 2221 HOH   B O     1 
HETATM 20201 O  O     . HOH   FA 11 .    ? 24.217  50.183  102.655 1.00 40.38 ? 2222 HOH   B O     1 
HETATM 20202 O  O     . HOH   FA 11 .    ? 23.098  67.694  59.514  1.00 28.10 ? 2223 HOH   B O     1 
HETATM 20203 O  O     . HOH   FA 11 .    ? -34.234 13.372  111.084 1.00 34.82 ? 2224 HOH   B O     1 
HETATM 20204 O  O     . HOH   FA 11 .    ? 15.064  57.058  71.976  1.00 27.04 ? 2225 HOH   B O     1 
HETATM 20205 O  O     . HOH   FA 11 .    ? 6.533   24.704  83.608  1.00 25.89 ? 2226 HOH   B O     1 
HETATM 20206 O  O     . HOH   FA 11 .    ? -29.577 12.092  87.337  1.00 46.47 ? 2227 HOH   B O     1 
HETATM 20207 O  O     . HOH   FA 11 .    ? -37.308 13.764  94.732  1.00 51.54 ? 2228 HOH   B O     1 
HETATM 20208 O  O     . HOH   FA 11 .    ? -3.196  -2.459  85.024  1.00 40.97 ? 2229 HOH   B O     1 
HETATM 20209 O  O     . HOH   FA 11 .    ? 8.734   79.899  85.399  1.00 47.40 ? 2230 HOH   B O     1 
HETATM 20210 O  O     . HOH   FA 11 .    ? 4.566   25.534  128.844 1.00 34.66 ? 2231 HOH   B O     1 
HETATM 20211 O  O     . HOH   FA 11 .    ? -5.286  37.601  86.081  1.00 28.14 ? 2232 HOH   B O     1 
HETATM 20212 O  O     . HOH   FA 11 .    ? -2.414  42.319  74.282  1.00 34.00 ? 2233 HOH   B O     1 
HETATM 20213 O  O     . HOH   FA 11 .    ? 16.377  52.117  79.544  1.00 25.93 ? 2234 HOH   B O     1 
HETATM 20214 O  O     . HOH   FA 11 .    ? 20.806  67.489  53.851  1.00 42.88 ? 2235 HOH   B O     1 
HETATM 20215 O  O     . HOH   FA 11 .    ? 37.092  21.725  83.816  1.00 34.66 ? 2236 HOH   B O     1 
HETATM 20216 O  O     . HOH   FA 11 .    ? -9.031  8.141   81.895  1.00 42.78 ? 2237 HOH   B O     1 
HETATM 20217 O  O     . HOH   FA 11 .    ? 17.178  24.931  52.334  1.00 29.25 ? 2238 HOH   B O     1 
HETATM 20218 O  O     . HOH   FA 11 .    ? 28.444  41.666  53.078  1.00 32.33 ? 2239 HOH   B O     1 
HETATM 20219 O  O     . HOH   FA 11 .    ? 35.729  19.873  85.533  1.00 36.69 ? 2240 HOH   B O     1 
HETATM 20220 O  O     . HOH   FA 11 .    ? 34.690  16.397  62.133  1.00 38.58 ? 2241 HOH   B O     1 
HETATM 20221 O  O     . HOH   FA 11 .    ? -0.905  22.933  96.707  1.00 32.78 ? 2242 HOH   B O     1 
HETATM 20222 O  O     . HOH   FA 11 .    ? -0.613  43.897  55.804  1.00 32.84 ? 2243 HOH   B O     1 
HETATM 20223 O  O     . HOH   FA 11 .    ? 11.492  43.753  50.927  1.00 35.64 ? 2244 HOH   B O     1 
HETATM 20224 O  O     . HOH   FA 11 .    ? 15.131  29.077  49.149  1.00 32.16 ? 2245 HOH   B O     1 
HETATM 20225 O  O     . HOH   FA 11 .    ? 7.886   -8.992  110.951 1.00 39.05 ? 2246 HOH   B O     1 
HETATM 20226 O  O     . HOH   FA 11 .    ? 35.108  6.340   81.681  1.00 40.65 ? 2247 HOH   B O     1 
HETATM 20227 O  O     . HOH   FA 11 .    ? -1.588  -9.579  108.964 1.00 36.34 ? 2248 HOH   B O     1 
HETATM 20228 O  O     . HOH   FA 11 .    ? -2.713  22.951  79.324  1.00 25.31 ? 2249 HOH   B O     1 
HETATM 20229 O  O     . HOH   FA 11 .    ? 6.256   17.487  96.265  1.00 31.27 ? 2250 HOH   B O     1 
HETATM 20230 O  O     . HOH   FA 11 .    ? 13.052  61.714  84.435  1.00 37.48 ? 2251 HOH   B O     1 
HETATM 20231 O  O     . HOH   FA 11 .    ? -3.783  -4.610  94.142  1.00 35.46 ? 2252 HOH   B O     1 
HETATM 20232 O  O     . HOH   FA 11 .    ? 10.926  10.198  123.251 1.00 33.62 ? 2253 HOH   B O     1 
HETATM 20233 O  O     . HOH   FA 11 .    ? -21.935 7.862   85.931  1.00 35.93 ? 2254 HOH   B O     1 
HETATM 20234 O  O     . HOH   FA 11 .    ? -27.733 14.277  86.193  1.00 36.20 ? 2255 HOH   B O     1 
HETATM 20235 O  O     . HOH   FA 11 .    ? -23.917 25.335  124.265 1.00 41.38 ? 2256 HOH   B O     1 
HETATM 20236 O  O     . HOH   FA 11 .    ? 6.085   20.982  85.788  1.00 41.74 ? 2257 HOH   B O     1 
HETATM 20237 O  O     . HOH   FA 11 .    ? 0.730   21.160  132.050 1.00 33.45 ? 2258 HOH   B O     1 
HETATM 20238 O  O     . HOH   FA 11 .    ? 32.216  46.325  77.863  1.00 36.69 ? 2259 HOH   B O     1 
HETATM 20239 O  O     . HOH   FA 11 .    ? 6.317   17.343  114.937 1.00 28.52 ? 2260 HOH   B O     1 
HETATM 20240 O  O     . HOH   FA 11 .    ? 7.374   33.822  51.251  1.00 33.69 ? 2261 HOH   B O     1 
HETATM 20241 O  O     . HOH   FA 11 .    ? 16.782  56.372  94.808  1.00 33.69 ? 2262 HOH   B O     1 
HETATM 20242 O  O     . HOH   FA 11 .    ? 10.916  29.309  46.303  1.00 45.43 ? 2263 HOH   B O     1 
HETATM 20243 O  O     . HOH   FA 11 .    ? -1.357  37.708  73.478  1.00 23.98 ? 2264 HOH   B O     1 
HETATM 20244 O  O     . HOH   FA 11 .    ? -5.928  48.593  132.979 1.00 42.35 ? 2265 HOH   B O     1 
HETATM 20245 O  O     . HOH   FA 11 .    ? 12.750  46.660  111.362 1.00 37.51 ? 2266 HOH   B O     1 
HETATM 20246 O  O     . HOH   FA 11 .    ? 17.351  8.149   90.131  1.00 38.71 ? 2267 HOH   B O     1 
HETATM 20247 O  O     . HOH   FA 11 .    ? -22.127 25.846  91.470  1.00 43.47 ? 2268 HOH   B O     1 
HETATM 20248 O  O     . HOH   FA 11 .    ? 1.138   55.846  65.639  1.00 40.96 ? 2269 HOH   B O     1 
HETATM 20249 O  O     . HOH   FA 11 .    ? 16.146  35.446  113.379 1.00 34.92 ? 2270 HOH   B O     1 
HETATM 20250 O  O     . HOH   FA 11 .    ? -6.097  39.846  86.149  1.00 34.80 ? 2271 HOH   B O     1 
HETATM 20251 O  O     . HOH   FA 11 .    ? 5.138   4.579   78.689  1.00 34.18 ? 2272 HOH   B O     1 
HETATM 20252 O  O     . HOH   FA 11 .    ? 21.313  6.256   73.222  1.00 40.27 ? 2273 HOH   B O     1 
HETATM 20253 O  O     A HOH   FA 11 .    ? 2.408   62.409  83.306  0.50 21.93 ? 2274 HOH   B O     1 
HETATM 20254 O  O     . HOH   FA 11 .    ? 36.270  21.853  64.561  1.00 41.99 ? 2275 HOH   B O     1 
HETATM 20255 O  O     . HOH   FA 11 .    ? 9.721   49.000  108.573 1.00 36.80 ? 2276 HOH   B O     1 
HETATM 20256 O  O     . HOH   FA 11 .    ? 12.495  39.836  132.098 1.00 44.06 ? 2277 HOH   B O     1 
HETATM 20257 O  O     . HOH   FA 11 .    ? 9.774   19.190  98.779  1.00 34.14 ? 2278 HOH   B O     1 
HETATM 20258 O  O     . HOH   FA 11 .    ? 32.953  35.182  72.291  1.00 32.48 ? 2279 HOH   B O     1 
HETATM 20259 O  O     . HOH   FA 11 .    ? 34.407  38.183  66.870  1.00 41.38 ? 2280 HOH   B O     1 
HETATM 20260 O  O     . HOH   FA 11 .    ? 28.696  64.787  59.436  1.00 37.32 ? 2281 HOH   B O     1 
HETATM 20261 O  O     . HOH   FA 11 .    ? 0.027   -1.989  94.742  1.00 31.41 ? 2282 HOH   B O     1 
HETATM 20262 O  O     . HOH   FA 11 .    ? 39.662  29.519  80.879  1.00 37.65 ? 2283 HOH   B O     1 
HETATM 20263 O  O     . HOH   FA 11 .    ? 30.802  31.861  83.610  1.00 34.29 ? 2284 HOH   B O     1 
HETATM 20264 O  O     . HOH   FA 11 .    ? -6.618  8.153   116.265 1.00 26.31 ? 2285 HOH   B O     1 
HETATM 20265 O  O     . HOH   FA 11 .    ? 30.778  42.312  55.443  1.00 31.45 ? 2286 HOH   B O     1 
HETATM 20266 O  O     . HOH   FA 11 .    ? 4.571   29.704  81.910  1.00 25.18 ? 2287 HOH   B O     1 
HETATM 20267 O  O     . HOH   FA 11 .    ? 6.490   23.932  125.060 1.00 36.47 ? 2288 HOH   B O     1 
HETATM 20268 O  O     . HOH   FA 11 .    ? -2.457  29.840  96.778  1.00 33.60 ? 2289 HOH   B O     1 
HETATM 20269 O  O     . HOH   FA 11 .    ? 7.674   19.264  97.319  1.00 40.00 ? 2290 HOH   B O     1 
HETATM 20270 O  O     . HOH   FA 11 .    ? -6.557  2.826   84.866  1.00 32.89 ? 2291 HOH   B O     1 
HETATM 20271 O  O     . HOH   FA 11 .    ? 4.737   26.461  92.031  1.00 36.18 ? 2292 HOH   B O     1 
HETATM 20272 O  O     . HOH   FA 11 .    ? -7.144  37.215  66.217  1.00 38.44 ? 2293 HOH   B O     1 
HETATM 20273 O  O     . HOH   FA 11 .    ? 32.968  58.794  67.338  1.00 30.68 ? 2294 HOH   B O     1 
HETATM 20274 O  O     . HOH   FA 11 .    ? 6.293   60.568  87.761  1.00 36.77 ? 2295 HOH   B O     1 
HETATM 20275 O  O     . HOH   FA 11 .    ? 32.992  42.308  66.885  1.00 32.37 ? 2296 HOH   B O     1 
HETATM 20276 O  O     . HOH   FA 11 .    ? 34.437  36.417  68.517  1.00 38.72 ? 2297 HOH   B O     1 
HETATM 20277 O  O     . HOH   FA 11 .    ? 40.796  30.246  90.241  1.00 28.26 ? 2298 HOH   B O     1 
HETATM 20278 O  O     . HOH   FA 11 .    ? 33.262  40.342  61.420  1.00 35.25 ? 2299 HOH   B O     1 
HETATM 20279 O  O     . HOH   FA 11 .    ? 5.812   50.570  54.822  1.00 42.93 ? 2300 HOH   B O     1 
HETATM 20280 O  O     . HOH   FA 11 .    ? 12.101  -1.795  113.041 1.00 44.63 ? 2301 HOH   B O     1 
HETATM 20281 O  O     . HOH   FA 11 .    ? 39.864  38.346  88.760  1.00 32.28 ? 2302 HOH   B O     1 
HETATM 20282 O  O     . HOH   FA 11 .    ? -1.776  26.302  64.535  1.00 31.97 ? 2303 HOH   B O     1 
HETATM 20283 O  O     . HOH   FA 11 .    ? 4.896   43.574  50.965  1.00 28.52 ? 2304 HOH   B O     1 
HETATM 20284 O  O     . HOH   FA 11 .    ? 32.754  20.536  76.093  1.00 35.77 ? 2305 HOH   B O     1 
HETATM 20285 O  O     . HOH   FA 11 .    ? -7.420  12.544  82.607  1.00 38.69 ? 2306 HOH   B O     1 
HETATM 20286 O  O     . HOH   FA 11 .    ? 23.801  68.802  62.273  1.00 32.60 ? 2307 HOH   B O     1 
HETATM 20287 O  O     . HOH   FA 11 .    ? 2.248   24.324  129.716 1.00 38.83 ? 2308 HOH   B O     1 
HETATM 20288 O  O     . HOH   FA 11 .    ? -4.084  64.018  69.743  1.00 38.10 ? 2309 HOH   B O     1 
HETATM 20289 O  O     . HOH   FA 11 .    ? 2.641   3.766   81.965  1.00 36.30 ? 2310 HOH   B O     1 
HETATM 20290 O  O     . HOH   FA 11 .    ? 14.306  53.360  86.789  1.00 39.18 ? 2311 HOH   B O     1 
HETATM 20291 O  O     . HOH   FA 11 .    ? -36.314 27.898  115.274 1.00 42.49 ? 2312 HOH   B O     1 
HETATM 20292 O  O     . HOH   FA 11 .    ? 5.375   44.734  53.520  1.00 31.84 ? 2313 HOH   B O     1 
HETATM 20293 O  O     . HOH   FA 11 .    ? -2.292  51.884  100.896 1.00 31.57 ? 2314 HOH   B O     1 
HETATM 20294 O  O     . HOH   FA 11 .    ? 39.356  26.351  92.016  1.00 39.74 ? 2315 HOH   B O     1 
HETATM 20295 O  O     . HOH   FA 11 .    ? 19.792  45.453  89.703  1.00 18.37 ? 2316 HOH   B O     1 
HETATM 20296 O  O     . HOH   FA 11 .    ? -10.317 30.179  76.180  1.00 35.73 ? 2317 HOH   B O     1 
HETATM 20297 O  O     . HOH   FA 11 .    ? 4.968   77.315  83.158  1.00 39.54 ? 2318 HOH   B O     1 
HETATM 20298 O  O     . HOH   FA 11 .    ? 8.849   -3.307  105.519 1.00 39.37 ? 2319 HOH   B O     1 
HETATM 20299 O  O     . HOH   FA 11 .    ? -2.518  41.232  77.955  1.00 34.28 ? 2320 HOH   B O     1 
HETATM 20300 O  O     . HOH   FA 11 .    ? 30.453  30.749  78.859  1.00 31.45 ? 2321 HOH   B O     1 
HETATM 20301 O  O     . HOH   FA 11 .    ? 39.371  40.886  89.059  1.00 37.08 ? 2322 HOH   B O     1 
HETATM 20302 O  O     . HOH   FA 11 .    ? 42.667  32.133  99.424  1.00 41.00 ? 2323 HOH   B O     1 
HETATM 20303 O  O     . HOH   FA 11 .    ? 31.130  58.916  60.734  1.00 32.21 ? 2324 HOH   B O     1 
HETATM 20304 O  O     . HOH   FA 11 .    ? 21.449  18.567  110.888 1.00 35.96 ? 2325 HOH   B O     1 
HETATM 20305 O  O     . HOH   FA 11 .    ? 1.543   14.589  79.715  1.00 31.95 ? 2326 HOH   B O     1 
HETATM 20306 O  O     . HOH   FA 11 .    ? -7.255  22.403  78.571  1.00 31.56 ? 2327 HOH   B O     1 
HETATM 20307 O  O     . HOH   FA 11 .    ? -3.063  39.603  74.443  1.00 45.64 ? 2328 HOH   B O     1 
HETATM 20308 O  O     . HOH   FA 11 .    ? 28.773  69.383  65.959  1.00 43.11 ? 2329 HOH   B O     1 
HETATM 20309 O  O     . HOH   FA 11 .    ? 18.403  7.096   98.000  1.00 33.11 ? 2330 HOH   B O     1 
HETATM 20310 O  O     . HOH   FA 11 .    ? 14.058  51.934  63.236  1.00 31.39 ? 2331 HOH   B O     1 
HETATM 20311 O  O     . HOH   FA 11 .    ? 16.812  26.286  109.660 1.00 28.04 ? 2332 HOH   B O     1 
HETATM 20312 O  O     . HOH   FA 11 .    ? 27.826  50.912  95.584  1.00 33.73 ? 2333 HOH   B O     1 
HETATM 20313 O  O     . HOH   FA 11 .    ? 5.892   10.914  75.208  1.00 33.59 ? 2334 HOH   B O     1 
HETATM 20314 O  O     . HOH   FA 11 .    ? 0.514   4.741   85.892  1.00 32.68 ? 2335 HOH   B O     1 
HETATM 20315 O  O     . HOH   FA 11 .    ? 20.747  58.434  52.962  1.00 39.78 ? 2336 HOH   B O     1 
HETATM 20316 O  O     . HOH   FA 11 .    ? 4.361   34.514  119.225 1.00 47.94 ? 2337 HOH   B O     1 
HETATM 20317 O  O     . HOH   FA 11 .    ? -18.586 17.365  78.205  1.00 44.01 ? 2338 HOH   B O     1 
HETATM 20318 O  O     . HOH   FA 11 .    ? 0.304   18.425  71.854  1.00 32.96 ? 2339 HOH   B O     1 
HETATM 20319 O  O     . HOH   FA 11 .    ? 1.966   43.587  55.621  1.00 33.92 ? 2340 HOH   B O     1 
HETATM 20320 O  O     . HOH   FA 11 .    ? -15.149 8.036   124.715 1.00 37.10 ? 2341 HOH   B O     1 
HETATM 20321 O  O     . HOH   FA 11 .    ? 15.570  4.226   72.442  1.00 38.19 ? 2342 HOH   B O     1 
HETATM 20322 O  O     . HOH   FA 11 .    ? 32.102  32.534  75.266  1.00 29.75 ? 2343 HOH   B O     1 
HETATM 20323 O  O     . HOH   FA 11 .    ? 4.099   29.999  94.159  1.00 34.85 ? 2344 HOH   B O     1 
HETATM 20324 O  O     . HOH   FA 11 .    ? -12.825 -7.986  106.116 1.00 35.94 ? 2345 HOH   B O     1 
HETATM 20325 O  O     . HOH   FA 11 .    ? -1.922  19.645  78.711  1.00 39.05 ? 2346 HOH   B O     1 
HETATM 20326 O  O     . HOH   FA 11 .    ? 12.334  21.203  98.588  1.00 32.18 ? 2347 HOH   B O     1 
HETATM 20327 O  O     . HOH   FA 11 .    ? 37.370  44.430  90.413  1.00 39.04 ? 2348 HOH   B O     1 
HETATM 20328 O  O     B HOH   FA 11 .    ? -3.465  60.219  84.952  0.50 25.36 ? 2349 HOH   B O     1 
HETATM 20329 O  O     . HOH   FA 11 .    ? 0.004   19.233  75.652  1.00 39.66 ? 2350 HOH   B O     1 
HETATM 20330 O  O     . HOH   FA 11 .    ? 5.448   80.109  79.152  1.00 39.17 ? 2351 HOH   B O     1 
HETATM 20331 O  O     . HOH   FA 11 .    ? 33.183  15.670  64.683  1.00 40.94 ? 2352 HOH   B O     1 
HETATM 20332 O  O     . HOH   FA 11 .    ? -12.790 9.295   129.489 1.00 35.21 ? 2353 HOH   B O     1 
HETATM 20333 O  O     . HOH   FA 11 .    ? -4.944  51.985  101.709 1.00 42.30 ? 2354 HOH   B O     1 
HETATM 20334 O  O     . HOH   FA 11 .    ? 11.939  17.506  89.538  1.00 35.40 ? 2355 HOH   B O     1 
HETATM 20335 O  O     . HOH   FA 11 .    ? -32.725 18.008  101.052 1.00 40.91 ? 2356 HOH   B O     1 
HETATM 20336 O  O     . HOH   FA 11 .    ? 24.397  44.281  109.432 1.00 41.31 ? 2357 HOH   B O     1 
HETATM 20337 O  O     . HOH   FA 11 .    ? 8.746   58.017  94.863  1.00 38.93 ? 2358 HOH   B O     1 
HETATM 20338 O  O     . HOH   FA 11 .    ? 14.730  55.675  61.506  1.00 39.43 ? 2359 HOH   B O     1 
HETATM 20339 O  O     . HOH   FA 11 .    ? 11.455  4.137   118.792 1.00 41.45 ? 2360 HOH   B O     1 
HETATM 20340 O  O     . HOH   FA 11 .    ? 25.274  70.473  65.311  1.00 33.88 ? 2361 HOH   B O     1 
HETATM 20341 O  O     . HOH   FA 11 .    ? -2.703  28.423  68.811  1.00 26.76 ? 2362 HOH   B O     1 
HETATM 20342 O  O     . HOH   FA 11 .    ? 30.647  63.192  58.517  1.00 40.42 ? 2363 HOH   B O     1 
HETATM 20343 O  O     . HOH   FA 11 .    ? 24.327  32.731  115.379 1.00 35.61 ? 2364 HOH   B O     1 
HETATM 20344 O  O     . HOH   FA 11 .    ? 7.003   18.854  89.758  1.00 32.73 ? 2365 HOH   B O     1 
HETATM 20345 O  O     . HOH   FA 11 .    ? 1.076   64.905  86.769  1.00 39.43 ? 2366 HOH   B O     1 
HETATM 20346 O  O     . HOH   FA 11 .    ? 22.190  78.013  78.091  1.00 43.60 ? 2367 HOH   B O     1 
HETATM 20347 O  O     . HOH   FA 11 .    ? 33.726  47.449  64.908  1.00 41.34 ? 2368 HOH   B O     1 
HETATM 20348 O  O     . HOH   FA 11 .    ? 14.986  51.267  56.016  1.00 35.61 ? 2369 HOH   B O     1 
HETATM 20349 O  O     . HOH   FA 11 .    ? 15.008  1.931   100.083 1.00 40.68 ? 2370 HOH   B O     1 
HETATM 20350 O  O     . HOH   FA 11 .    ? -10.369 -6.768  105.695 1.00 29.89 ? 2371 HOH   B O     1 
HETATM 20351 O  O     . HOH   FA 11 .    ? -11.818 -1.002  91.492  1.00 43.61 ? 2372 HOH   B O     1 
HETATM 20352 O  O     . HOH   FA 11 .    ? -17.747 7.052   92.933  1.00 36.76 ? 2373 HOH   B O     1 
HETATM 20353 O  O     . HOH   FA 11 .    ? 26.718  69.118  61.771  1.00 40.31 ? 2374 HOH   B O     1 
HETATM 20354 O  O     . HOH   FA 11 .    ? 21.533  11.194  98.924  1.00 42.06 ? 2375 HOH   B O     1 
HETATM 20355 O  O     . HOH   FA 11 .    ? -4.050  40.168  60.548  1.00 29.29 ? 2376 HOH   B O     1 
HETATM 20356 O  O     . HOH   FA 11 .    ? 7.148   2.456   79.812  1.00 38.98 ? 2377 HOH   B O     1 
HETATM 20357 O  O     . HOH   FA 11 .    ? 20.515  22.963  109.863 1.00 31.23 ? 2378 HOH   B O     1 
HETATM 20358 O  O     . HOH   FA 11 .    ? -7.877  37.581  79.358  1.00 39.98 ? 2379 HOH   B O     1 
HETATM 20359 O  O     . HOH   FA 11 .    ? 25.665  68.302  59.157  1.00 41.00 ? 2380 HOH   B O     1 
HETATM 20360 O  O     . HOH   FA 11 .    ? -4.060  68.506  73.679  1.00 41.35 ? 2381 HOH   B O     1 
HETATM 20361 O  O     . HOH   FA 11 .    ? 10.185  18.274  93.026  1.00 41.22 ? 2382 HOH   B O     1 
HETATM 20362 O  O     . HOH   FA 11 .    ? 5.186   31.636  92.648  1.00 39.67 ? 2383 HOH   B O     1 
HETATM 20363 O  O     . HOH   FA 11 .    ? 14.081  25.106  100.573 1.00 25.40 ? 2384 HOH   B O     1 
HETATM 20364 O  O     . HOH   FA 11 .    ? -4.311  40.002  55.657  1.00 42.00 ? 2385 HOH   B O     1 
HETATM 20365 O  O     . HOH   FA 11 .    ? 6.226   27.915  87.758  1.00 38.69 ? 2386 HOH   B O     1 
HETATM 20366 O  O     . HOH   FA 11 .    ? 32.846  27.706  74.383  1.00 37.74 ? 2387 HOH   B O     1 
HETATM 20367 O  O     . HOH   FA 11 .    ? -7.924  -2.526  117.547 1.00 35.56 ? 2388 HOH   B O     1 
HETATM 20368 O  O     . HOH   FA 11 .    ? 12.747  18.250  91.702  1.00 34.69 ? 2389 HOH   B O     1 
HETATM 20369 O  O     . HOH   FA 11 .    ? 6.488   15.808  91.925  1.00 30.13 ? 2390 HOH   B O     1 
HETATM 20370 O  O     . HOH   FA 11 .    ? 1.644   11.342  76.604  1.00 42.06 ? 2391 HOH   B O     1 
HETATM 20371 O  O     . HOH   FA 11 .    ? 11.673  0.656   113.553 1.00 37.50 ? 2392 HOH   B O     1 
HETATM 20372 O  O     . HOH   FA 11 .    ? 1.223   31.558  82.566  1.00 29.32 ? 2393 HOH   B O     1 
HETATM 20373 O  O     . HOH   FA 11 .    ? 18.353  56.333  91.560  1.00 40.21 ? 2394 HOH   B O     1 
HETATM 20374 O  O     . HOH   FA 11 .    ? 15.023  22.180  97.590  1.00 27.12 ? 2395 HOH   B O     1 
HETATM 20375 O  O     . HOH   FA 11 .    ? -15.917 6.600   122.391 1.00 38.52 ? 2396 HOH   B O     1 
HETATM 20376 O  O     . HOH   FA 11 .    ? 3.386   13.296  77.498  1.00 37.94 ? 2397 HOH   B O     1 
HETATM 20377 O  O     . HOH   FA 11 .    ? -15.932 3.502   123.387 1.00 44.57 ? 2398 HOH   B O     1 
HETATM 20378 O  O     . HOH   FA 11 .    ? 10.616  0.731   107.116 1.00 34.01 ? 2399 HOH   B O     1 
HETATM 20379 O  O     . HOH   FA 11 .    ? 3.993   51.538  89.204  1.00 45.47 ? 2400 HOH   B O     1 
HETATM 20380 O  O     . HOH   FA 11 .    ? 20.082  34.182  114.907 1.00 26.11 ? 2401 HOH   B O     1 
HETATM 20381 O  O     . HOH   FA 11 .    ? 23.411  71.505  61.324  1.00 41.11 ? 2402 HOH   B O     1 
HETATM 20382 O  O     . HOH   FA 11 .    ? 18.119  3.704   73.244  1.00 38.53 ? 2403 HOH   B O     1 
HETATM 20383 O  O     . HOH   FA 11 .    ? -31.142 12.385  126.813 1.00 49.16 ? 2404 HOH   B O     1 
HETATM 20384 O  O     . HOH   FA 11 .    ? 15.119  5.300   111.565 1.00 43.43 ? 2405 HOH   B O     1 
HETATM 20385 O  O     . HOH   FA 11 .    ? 34.672  26.459  56.800  1.00 28.29 ? 2406 HOH   B O     1 
HETATM 20386 O  O     . HOH   FA 11 .    ? 22.853  56.777  53.365  1.00 43.48 ? 2407 HOH   B O     1 
HETATM 20387 O  O     . HOH   FA 11 .    ? 1.049   55.344  70.079  1.00 39.11 ? 2408 HOH   B O     1 
HETATM 20388 O  O     B HOH   FA 11 .    ? -3.152  58.078  84.701  0.50 27.23 ? 2409 HOH   B O     1 
HETATM 20389 O  O     . HOH   FA 11 .    ? 36.592  41.945  88.925  1.00 39.52 ? 2410 HOH   B O     1 
HETATM 20390 O  O     . HOH   FA 11 .    ? 2.248   44.619  96.922  1.00 32.23 ? 2411 HOH   B O     1 
HETATM 20391 O  O     . HOH   FA 11 .    ? 16.356  77.050  62.025  1.00 38.88 ? 2412 HOH   B O     1 
HETATM 20392 O  O     . HOH   FA 11 .    ? -5.039  3.314   83.101  1.00 44.26 ? 2413 HOH   B O     1 
HETATM 20393 O  O     . HOH   FA 11 .    ? 12.105  43.882  53.356  1.00 27.35 ? 2414 HOH   B O     1 
HETATM 20394 O  O     . HOH   FA 11 .    ? 25.753  11.358  68.077  1.00 41.61 ? 2415 HOH   B O     1 
HETATM 20395 O  O     . HOH   FA 11 .    ? 18.904  48.425  56.412  1.00 29.71 ? 2416 HOH   B O     1 
HETATM 20396 O  O     . HOH   FA 11 .    ? 15.313  8.437   113.615 1.00 40.50 ? 2417 HOH   B O     1 
HETATM 20397 O  O     . HOH   FA 11 .    ? 13.618  36.537  74.128  1.00 19.84 ? 2418 HOH   B O     1 
HETATM 20398 O  O     . HOH   FA 11 .    ? 9.476   3.912   83.681  1.00 28.08 ? 2419 HOH   B O     1 
HETATM 20399 O  O     . HOH   FA 11 .    ? 5.197   56.042  66.877  1.00 38.78 ? 2420 HOH   B O     1 
HETATM 20400 O  O     . HOH   FA 11 .    ? 6.797   60.959  85.141  1.00 26.06 ? 2421 HOH   B O     1 
HETATM 20401 O  O     . HOH   FA 11 .    ? 14.621  44.379  52.743  1.00 35.03 ? 2422 HOH   B O     1 
HETATM 20402 O  O     . HOH   FA 11 .    ? 16.960  43.802  52.169  1.00 36.80 ? 2423 HOH   B O     1 
HETATM 20403 O  O     . HOH   FA 11 .    ? 15.846  59.734  92.598  1.00 38.31 ? 2424 HOH   B O     1 
HETATM 20404 O  O     . HOH   FA 11 .    ? 2.259   -7.569  98.594  1.00 39.48 ? 2425 HOH   B O     1 
HETATM 20405 O  O     . HOH   FA 11 .    ? -10.753 33.529  83.794  1.00 44.53 ? 2426 HOH   B O     1 
HETATM 20406 O  O     . HOH   FA 11 .    ? -0.536  18.545  67.828  1.00 38.81 ? 2427 HOH   B O     1 
HETATM 20407 O  O     . HOH   FA 11 .    ? 34.535  27.583  61.258  1.00 29.92 ? 2428 HOH   B O     1 
HETATM 20408 O  O     . HOH   FA 11 .    ? -8.948  3.914   84.917  1.00 37.61 ? 2429 HOH   B O     1 
HETATM 20409 O  O     . HOH   FA 11 .    ? 18.424  9.106   95.665  1.00 35.16 ? 2430 HOH   B O     1 
HETATM 20410 O  O     . HOH   FA 11 .    ? 5.362   3.238   85.713  1.00 32.20 ? 2431 HOH   B O     1 
HETATM 20411 O  O     . HOH   FA 11 .    ? 15.589  72.906  58.437  1.00 40.13 ? 2432 HOH   B O     1 
HETATM 20412 O  O     . HOH   FA 11 .    ? 21.876  19.721  107.129 1.00 26.44 ? 2433 HOH   B O     1 
HETATM 20413 O  O     . HOH   FA 11 .    ? -13.549 17.322  78.565  1.00 39.46 ? 2434 HOH   B O     1 
HETATM 20414 O  O     . HOH   FA 11 .    ? 42.017  37.131  89.929  1.00 34.87 ? 2435 HOH   B O     1 
HETATM 20415 O  O     . HOH   FA 11 .    ? 30.465  23.980  74.325  1.00 26.98 ? 2436 HOH   B O     1 
HETATM 20416 O  O     . HOH   FA 11 .    ? 30.408  64.293  71.340  1.00 37.38 ? 2437 HOH   B O     1 
HETATM 20417 O  O     . HOH   FA 11 .    ? 31.699  32.449  80.816  1.00 35.88 ? 2438 HOH   B O     1 
HETATM 20418 O  O     . HOH   FA 11 .    ? 4.655   64.065  86.535  1.00 37.08 ? 2439 HOH   B O     1 
HETATM 20419 O  O     . HOH   FA 11 .    ? 13.916  24.761  98.084  1.00 30.08 ? 2440 HOH   B O     1 
HETATM 20420 O  O     . HOH   FA 11 .    ? -0.540  80.229  77.143  1.00 43.36 ? 2441 HOH   B O     1 
HETATM 20421 O  O     . HOH   FA 11 .    ? 8.976   24.674  86.882  1.00 40.28 ? 2442 HOH   B O     1 
HETATM 20422 O  O     . HOH   FA 11 .    ? 18.780  3.107   77.658  1.00 38.17 ? 2443 HOH   B O     1 
HETATM 20423 O  O     . HOH   FA 11 .    ? 12.415  0.456   108.993 1.00 35.16 ? 2444 HOH   B O     1 
HETATM 20424 O  O     . HOH   FA 11 .    ? -8.289  33.683  85.198  1.00 33.83 ? 2445 HOH   B O     1 
HETATM 20425 O  O     . HOH   FA 11 .    ? 12.896  55.727  105.406 1.00 33.24 ? 2446 HOH   B O     1 
HETATM 20426 O  O     . HOH   FA 11 .    ? -7.018  25.095  74.863  1.00 32.02 ? 2447 HOH   B O     1 
HETATM 20427 O  O     . HOH   FA 11 .    ? 18.871  78.836  65.271  1.00 40.54 ? 2448 HOH   B O     1 
HETATM 20428 O  O     . HOH   FA 11 .    ? 31.743  69.664  80.237  1.00 35.27 ? 2449 HOH   B O     1 
HETATM 20429 O  O     . HOH   FA 11 .    ? -22.616 24.650  82.311  1.00 40.13 ? 2450 HOH   B O     1 
HETATM 20430 O  O     . HOH   FA 11 .    ? 7.745   28.152  83.692  1.00 42.40 ? 2451 HOH   B O     1 
HETATM 20431 O  O     . HOH   FA 11 .    ? 8.956   44.487  50.266  1.00 38.89 ? 2452 HOH   B O     1 
HETATM 20432 O  O     . HOH   FA 11 .    ? 13.074  74.946  60.831  1.00 37.54 ? 2453 HOH   B O     1 
HETATM 20433 O  O     . HOH   FA 11 .    ? 2.754   10.000  74.814  1.00 45.61 ? 2454 HOH   B O     1 
HETATM 20434 O  O     . HOH   FA 11 .    ? 6.718   25.940  106.642 1.00 42.28 ? 2455 HOH   B O     1 
HETATM 20435 O  O     . HOH   FA 11 .    ? 11.835  1.428   115.862 1.00 39.55 ? 2456 HOH   B O     1 
HETATM 20436 O  O     . HOH   FA 11 .    ? -16.227 7.945   90.816  1.00 30.91 ? 2457 HOH   B O     1 
HETATM 20437 O  O     . HOH   FA 11 .    ? -25.186 13.070  86.624  1.00 36.86 ? 2458 HOH   B O     1 
HETATM 20438 O  O     . HOH   FA 11 .    ? 32.473  60.202  62.609  1.00 32.50 ? 2459 HOH   B O     1 
HETATM 20439 O  O     . HOH   FA 11 .    ? -5.080  -0.739  84.324  1.00 38.07 ? 2460 HOH   B O     1 
HETATM 20440 O  O     . HOH   FA 11 .    ? 10.671  28.710  85.181  1.00 44.43 ? 2461 HOH   B O     1 
HETATM 20441 O  O     . HOH   FA 11 .    ? -9.306  -0.175  86.632  1.00 43.19 ? 2462 HOH   B O     1 
HETATM 20442 O  O     . HOH   FA 11 .    ? 20.055  10.813  96.362  1.00 37.61 ? 2463 HOH   B O     1 
HETATM 20443 O  O     . HOH   FA 11 .    ? 22.655  50.408  68.617  1.00 26.85 ? 2464 HOH   B O     1 
HETATM 20444 O  O     . HOH   FA 11 .    ? 9.432   17.111  89.799  1.00 32.15 ? 2465 HOH   B O     1 
HETATM 20445 O  O     . HOH   FA 11 .    ? 26.296  52.518  83.930  1.00 34.71 ? 2466 HOH   B O     1 
HETATM 20446 O  O     . HOH   FA 11 .    ? 23.914  58.137  100.483 1.00 33.73 ? 2467 HOH   B O     1 
HETATM 20447 O  O     . HOH   FA 11 .    ? -20.952 16.591  80.125  1.00 37.02 ? 2468 HOH   B O     1 
HETATM 20448 O  O     . HOH   FA 11 .    ? 5.596   30.486  86.596  1.00 35.06 ? 2469 HOH   B O     1 
HETATM 20449 O  O     . HOH   FA 11 .    ? -11.074 47.191  77.121  1.00 35.49 ? 2470 HOH   B O     1 
HETATM 20450 O  O     . HOH   FA 11 .    ? 5.472   70.491  87.058  1.00 41.67 ? 2471 HOH   B O     1 
HETATM 20451 O  O     . HOH   FA 11 .    ? 6.353   -4.861  101.887 1.00 35.29 ? 2472 HOH   B O     1 
HETATM 20452 O  O     . HOH   FA 11 .    ? -11.521 1.852   88.876  1.00 37.92 ? 2473 HOH   B O     1 
HETATM 20453 O  O     . HOH   FA 11 .    ? -23.299 14.389  82.255  1.00 32.28 ? 2474 HOH   B O     1 
HETATM 20454 O  O     . HOH   FA 11 .    ? 15.219  55.958  104.330 1.00 30.84 ? 2475 HOH   B O     1 
HETATM 20455 O  O     . HOH   FA 11 .    ? 24.321  76.563  78.501  1.00 46.30 ? 2476 HOH   B O     1 
HETATM 20456 O  O     . HOH   FA 11 .    ? -7.114  -4.993  91.450  1.00 41.16 ? 2477 HOH   B O     1 
HETATM 20457 O  O     . HOH   FA 11 .    ? -4.299  23.194  72.419  1.00 40.45 ? 2478 HOH   B O     1 
HETATM 20458 O  O     . HOH   FA 11 .    ? 6.404   12.074  72.870  1.00 37.16 ? 2479 HOH   B O     1 
HETATM 20459 O  O     . HOH   FA 11 .    ? 35.033  38.676  64.637  1.00 39.79 ? 2480 HOH   B O     1 
HETATM 20460 O  O     . HOH   FA 11 .    ? 33.648  19.533  54.088  1.00 36.44 ? 2481 HOH   B O     1 
HETATM 20461 O  O     . HOH   FA 11 .    ? -12.252 53.126  126.439 1.00 42.63 ? 2482 HOH   B O     1 
HETATM 20462 O  O     . HOH   FA 11 .    ? -7.572  36.972  83.917  1.00 38.53 ? 2483 HOH   B O     1 
HETATM 20463 O  O     . HOH   FA 11 .    ? 10.588  25.346  99.455  1.00 40.74 ? 2484 HOH   B O     1 
HETATM 20464 O  O     . HOH   FA 11 .    ? 8.238   31.052  85.757  1.00 40.87 ? 2485 HOH   B O     1 
HETATM 20465 O  O     . HOH   FA 11 .    ? 0.140   28.888  96.514  1.00 25.62 ? 2486 HOH   B O     1 
HETATM 20466 O  O     . HOH   FA 11 .    ? -8.108  35.221  87.431  1.00 40.52 ? 2487 HOH   B O     1 
HETATM 20467 O  O     . HOH   FA 11 .    ? -10.934 3.809   86.747  1.00 32.50 ? 2488 HOH   B O     1 
HETATM 20468 O  O     . HOH   FA 11 .    ? -1.176  23.398  63.906  1.00 34.22 ? 2489 HOH   B O     1 
HETATM 20469 O  O     . HOH   FA 11 .    ? -2.524  69.433  75.572  1.00 34.97 ? 2490 HOH   B O     1 
HETATM 20470 O  O     . HOH   FA 11 .    ? 2.134   21.878  61.090  1.00 33.21 ? 2491 HOH   B O     1 
HETATM 20471 O  O     . HOH   FA 11 .    ? 36.307  28.762  56.275  1.00 45.09 ? 2492 HOH   B O     1 
HETATM 20472 O  O     . HOH   FA 11 .    ? -12.810 -0.254  121.340 1.00 39.49 ? 2493 HOH   B O     1 
HETATM 20473 O  O     . HOH   FA 11 .    ? 3.585   15.199  75.552  1.00 34.39 ? 2494 HOH   B O     1 
HETATM 20474 O  O     . HOH   FA 11 .    ? 28.648  51.155  83.918  1.00 39.72 ? 2495 HOH   B O     1 
HETATM 20475 O  O     . HOH   FA 11 .    ? -18.241 22.076  80.623  1.00 39.10 ? 2496 HOH   B O     1 
HETATM 20476 O  O     . HOH   FA 11 .    ? 13.991  44.665  49.371  1.00 39.80 ? 2497 HOH   B O     1 
HETATM 20477 O  O     . HOH   FA 11 .    ? 2.295   31.843  84.944  1.00 26.24 ? 2498 HOH   B O     1 
HETATM 20478 O  O     . HOH   FA 11 .    ? 33.591  43.665  59.388  1.00 42.49 ? 2499 HOH   B O     1 
HETATM 20479 O  O     . HOH   FA 11 .    ? 34.649  47.614  69.190  1.00 37.83 ? 2500 HOH   B O     1 
HETATM 20480 O  O     . HOH   FA 11 .    ? 22.388  31.335  45.313  1.00 39.55 ? 2501 HOH   B O     1 
HETATM 20481 O  O     . HOH   FA 11 .    ? 41.389  27.896  91.364  1.00 42.75 ? 2502 HOH   B O     1 
HETATM 20482 O  O     . HOH   FA 11 .    ? 0.819   28.022  98.888  1.00 37.31 ? 2503 HOH   B O     1 
HETATM 20483 O  O     . HOH   FA 11 .    ? 14.818  1.566   90.866  1.00 47.40 ? 2504 HOH   B O     1 
HETATM 20484 O  O     . HOH   FA 11 .    ? -4.664  23.573  74.988  1.00 34.94 ? 2505 HOH   B O     1 
HETATM 20485 O  O     . HOH   FA 11 .    ? -2.408  23.562  61.424  1.00 40.23 ? 2506 HOH   B O     1 
HETATM 20486 O  O     . HOH   FA 11 .    ? 11.265  60.266  92.389  1.00 39.33 ? 2507 HOH   B O     1 
HETATM 20487 O  O     . HOH   FA 11 .    ? -24.835 13.019  84.105  1.00 34.96 ? 2508 HOH   B O     1 
HETATM 20488 O  O     . HOH   FA 11 .    ? 20.617  27.851  43.461  1.00 35.01 ? 2509 HOH   B O     1 
HETATM 20489 O  O     . HOH   FA 11 .    ? 22.960  29.281  43.762  1.00 46.45 ? 2510 HOH   B O     1 
HETATM 20490 O  O     . HOH   FA 11 .    ? 19.601  2.830   71.027  1.00 38.95 ? 2511 HOH   B O     1 
HETATM 20491 O  O     . HOH   FA 11 .    ? 7.347   2.022   84.190  1.00 37.10 ? 2512 HOH   B O     1 
HETATM 20492 O  O     . HOH   FA 11 .    ? -15.854 5.704   88.885  1.00 40.39 ? 2513 HOH   B O     1 
HETATM 20493 O  O     . HOH   FA 11 .    ? 12.475  -1.230  116.768 1.00 46.75 ? 2514 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   ? 0.5326 0.5871 0.6447 0.0923  -0.0267 -0.1325 14   ALA A N   
2     C CA  . ALA A 16   ? 0.5596 0.6143 0.6612 0.0895  -0.0238 -0.1276 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5479 0.6102 0.6391 0.0879  -0.0181 -0.1218 14   ALA A C   
4     O O   . ALA A 16   ? 0.5805 0.6553 0.6695 0.0906  -0.0156 -0.1259 14   ALA A O   
5     C CB  . ALA A 16   ? 0.6034 0.6647 0.7049 0.0925  -0.0248 -0.1355 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5240 0.5791 0.6090 0.0833  -0.0161 -0.1121 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4822 0.5433 0.5584 0.0815  -0.0111 -0.1060 15   PRO A CA  
8     C C   . PRO A 17   ? 0.4695 0.5411 0.5375 0.0822  -0.0078 -0.1071 15   PRO A C   
9     O O   . PRO A 17   ? 0.4528 0.5227 0.5186 0.0820  -0.0088 -0.1085 15   PRO A O   
10    C CB  . PRO A 17   ? 0.4915 0.5412 0.5644 0.0766  -0.0106 -0.0963 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.5144 0.5548 0.5905 0.0757  -0.0143 -0.0971 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.5066 0.5482 0.5927 0.0797  -0.0184 -0.1064 15   PRO A CD  
13    N N   . ALA A 18   ? 0.4117 0.4943 0.4752 0.0831  -0.0040 -0.1064 16   ALA A N   
14    C CA  . ALA A 18   ? 0.3984 0.4924 0.4543 0.0838  -0.0009 -0.1070 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3496 0.4378 0.3976 0.0796  0.0009  -0.0988 16   ALA A C   
16    O O   . ALA A 18   ? 0.3356 0.4152 0.3820 0.0761  0.0016  -0.0913 16   ALA A O   
17    C CB  . ALA A 18   ? 0.4144 0.5213 0.4675 0.0849  0.0028  -0.1065 16   ALA A CB  
18    N N   . PRO A 19   ? 0.3467 0.4395 0.3898 0.0800  0.0016  -0.1003 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3133 0.4005 0.3494 0.0762  0.0031  -0.0929 17   PRO A CA  
20    C C   . PRO A 19   ? 0.2749 0.3652 0.3048 0.0734  0.0071  -0.0847 17   PRO A C   
21    O O   . PRO A 19   ? 0.3326 0.4349 0.3601 0.0748  0.0098  -0.0851 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3467 0.4417 0.3793 0.0780  0.0032  -0.0973 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.3541 0.4533 0.3939 0.0823  0.0002  -0.1076 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3384 0.4413 0.3829 0.0840  0.0006  -0.1093 17   PRO A CD  
25    N N   . PHE A 20   ? 0.2798 0.3594 0.3076 0.0695  0.0073  -0.0772 18   PHE A N   
26    C CA  . PHE A 20   ? 0.3082 0.3883 0.3306 0.0664  0.0106  -0.0689 18   PHE A CA  
27    C C   . PHE A 20   ? 0.3055 0.3893 0.3303 0.0667  0.0120  -0.0676 18   PHE A C   
28    O O   . PHE A 20   ? 0.3076 0.3942 0.3284 0.0646  0.0148  -0.0613 18   PHE A O   
29    C CB  . PHE A 20   ? 0.2807 0.3699 0.2959 0.0659  0.0135  -0.0663 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2844 0.3703 0.2969 0.0654  0.0123  -0.0672 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2682 0.3431 0.2786 0.0621  0.0118  -0.0617 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.2867 0.3810 0.2989 0.0684  0.0117  -0.0737 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.2698 0.3419 0.2779 0.0616  0.0107  -0.0624 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.3080 0.3993 0.3179 0.0680  0.0105  -0.0745 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.2985 0.3786 0.3064 0.0646  0.0101  -0.0688 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3121 0.3961 0.3437 0.0694  0.0099  -0.0733 19   ALA A N   
37    C CA  . ALA A 21   ? 0.3350 0.4224 0.3693 0.0698  0.0111  -0.0723 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3476 0.4250 0.3815 0.0660  0.0114  -0.0646 19   ALA A C   
39    O O   . ALA A 21   ? 0.3601 0.4410 0.3940 0.0654  0.0133  -0.0615 19   ALA A O   
40    C CB  . ALA A 21   ? 0.3756 0.4641 0.4183 0.0735  0.0082  -0.0803 19   ALA A CB  
41    N N   . ASP A 22   ? 0.3216 0.3873 0.3552 0.0636  0.0096  -0.0617 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3748 0.4310 0.4081 0.0600  0.0096  -0.0548 20   ASP A CA  
43    C C   . ASP A 22   ? 0.2824 0.3335 0.3097 0.0568  0.0106  -0.0493 20   ASP A C   
44    O O   . ASP A 22   ? 0.2893 0.3303 0.3170 0.0542  0.0092  -0.0457 20   ASP A O   
45    C CB  . ASP A 22   ? 0.4115 0.4581 0.4516 0.0600  0.0059  -0.0566 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.5165 0.5675 0.5635 0.0633  0.0046  -0.0621 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.5802 0.6389 0.6265 0.0641  0.0069  -0.0616 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.6372 0.6839 0.6905 0.0650  0.0011  -0.0670 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2428 0.3013 0.2647 0.0569  0.0129  -0.0485 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2438 0.2977 0.2608 0.0544  0.0133  -0.0446 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2512 0.2981 0.2660 0.0507  0.0143  -0.0371 21   PHE A C   
52    O O   . PHE A 23   ? 0.2595 0.2970 0.2741 0.0486  0.0129  -0.0349 21   PHE A O   
53    C CB  . PHE A 23   ? 0.2430 0.3069 0.2548 0.0553  0.0156  -0.0447 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2213 0.2809 0.2281 0.0526  0.0162  -0.0401 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2630 0.3153 0.2702 0.0522  0.0140  -0.0418 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.2586 0.3214 0.2611 0.0505  0.0188  -0.0339 21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2479 0.2961 0.2508 0.0499  0.0145  -0.0376 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.2949 0.3534 0.2934 0.0481  0.0192  -0.0298 21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.2375 0.2890 0.2361 0.0479  0.0171  -0.0318 21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2604 0.3121 0.2736 0.0498  0.0168  -0.0333 22   ALA A N   
61    C CA  . ALA A 24   ? 0.2662 0.3120 0.2777 0.0463  0.0177  -0.0265 22   ALA A CA  
62    C C   . ALA A 24   ? 0.2466 0.2971 0.2593 0.0461  0.0194  -0.0239 22   ALA A C   
63    O O   . ALA A 24   ? 0.2405 0.2942 0.2503 0.0443  0.0216  -0.0190 22   ALA A O   
64    C CB  . ALA A 24   ? 0.2885 0.3346 0.2946 0.0444  0.0192  -0.0224 22   ALA A CB  
65    N N   . PRO A 25   ? 0.2738 0.3246 0.2913 0.0476  0.0183  -0.0269 23   PRO A N   
66    C CA  . PRO A 25   ? 0.2866 0.3422 0.3055 0.0474  0.0200  -0.0246 23   PRO A CA  
67    C C   . PRO A 25   ? 0.2686 0.3175 0.2863 0.0439  0.0204  -0.0181 23   PRO A C   
68    O O   . PRO A 25   ? 0.2763 0.3156 0.2946 0.0422  0.0187  -0.0169 23   PRO A O   
69    C CB  . PRO A 25   ? 0.2935 0.3482 0.3184 0.0497  0.0179  -0.0295 23   PRO A CB  
70    C CG  . PRO A 25   ? 0.3066 0.3516 0.3334 0.0495  0.0150  -0.0315 23   PRO A CG  
71    C CD  . PRO A 25   ? 0.2821 0.3277 0.3045 0.0493  0.0153  -0.0319 23   PRO A CD  
72    N N   . PRO A 26   ? 0.2645 0.3185 0.2807 0.0426  0.0227  -0.0138 24   PRO A N   
73    C CA  . PRO A 26   ? 0.2867 0.3346 0.3024 0.0393  0.0230  -0.0080 24   PRO A CA  
74    C C   . PRO A 26   ? 0.2619 0.3044 0.2817 0.0390  0.0215  -0.0083 24   PRO A C   
75    O O   . PRO A 26   ? 0.2611 0.3065 0.2846 0.0412  0.0208  -0.0120 24   PRO A O   
76    C CB  . PRO A 26   ? 0.2831 0.3394 0.2974 0.0386  0.0256  -0.0040 24   PRO A CB  
77    C CG  . PRO A 26   ? 0.3221 0.3892 0.3378 0.0417  0.0266  -0.0081 24   PRO A CG  
78    C CD  . PRO A 26   ? 0.3029 0.3692 0.3184 0.0441  0.0250  -0.0140 24   PRO A CD  
79    N N   . VAL A 27   ? 0.2394 0.2740 0.2587 0.0362  0.0209  -0.0043 25   VAL A N   
80    C CA  . VAL A 27   ? 0.2634 0.2930 0.2863 0.0354  0.0195  -0.0037 25   VAL A CA  
81    C C   . VAL A 27   ? 0.3008 0.3371 0.3266 0.0364  0.0207  -0.0035 25   VAL A C   
82    O O   . VAL A 27   ? 0.3232 0.3587 0.3531 0.0376  0.0193  -0.0058 25   VAL A O   
83    C CB  . VAL A 27   ? 0.2659 0.2883 0.2872 0.0321  0.0192  0.0009  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2916 0.3103 0.3163 0.0311  0.0180  0.0021  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2876 0.3032 0.3067 0.0312  0.0177  0.0003  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.3035 0.3466 0.3276 0.0358  0.0230  -0.0006 26   ARG A N   
87    C CA  . ARG A 28   ? 0.3094 0.3597 0.3361 0.0365  0.0244  0.0002  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3294 0.3900 0.3539 0.0370  0.0268  0.0015  26   ARG A C   
89    O O   . ARG A 28   ? 0.2899 0.3503 0.3107 0.0360  0.0274  0.0034  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3428 0.3891 0.3709 0.0337  0.0244  0.0050  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.3421 0.3880 0.3673 0.0310  0.0256  0.0102  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.3904 0.4312 0.4173 0.0283  0.0251  0.0141  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.4186 0.4496 0.4450 0.0271  0.0230  0.0135  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.4338 0.4607 0.4629 0.0273  0.0214  0.0121  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.4301 0.4610 0.4627 0.0287  0.0215  0.0109  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.3891 0.4080 0.4174 0.0261  0.0196  0.0119  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.3076 0.3776 0.3342 0.0386  0.0282  0.0007  27   PRO A N   
98    C CA  . PRO A 29   ? 0.3246 0.4053 0.3490 0.0387  0.0307  0.0030  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2904 0.3689 0.3134 0.0353  0.0315  0.0099  27   PRO A C   
100   O O   . PRO A 29   ? 0.2909 0.3637 0.3158 0.0332  0.0309  0.0130  27   PRO A O   
101   C CB  . PRO A 29   ? 0.3335 0.4238 0.3614 0.0405  0.0318  0.0015  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3604 0.4458 0.3918 0.0426  0.0297  -0.0040 27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3465 0.4186 0.3776 0.0404  0.0276  -0.0023 27   PRO A CD  
104   N N   . GLN A 30   ? 0.2924 0.3754 0.3121 0.0347  0.0327  0.0122  28   GLN A N   
105   C CA  . GLN A 30   ? 0.2979 0.3780 0.3165 0.0315  0.0331  0.0185  28   GLN A CA  
106   C C   . GLN A 30   ? 0.2982 0.3861 0.3193 0.0303  0.0347  0.0233  28   GLN A C   
107   O O   . GLN A 30   ? 0.3123 0.4118 0.3331 0.0314  0.0365  0.0238  28   GLN A O   
108   C CB  . GLN A 30   ? 0.2816 0.3637 0.2964 0.0314  0.0336  0.0193  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2723 0.3470 0.2848 0.0326  0.0319  0.0146  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2930 0.3551 0.3059 0.0306  0.0302  0.0156  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2822 0.3401 0.2939 0.0283  0.0300  0.0193  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.2596 0.3163 0.2747 0.0313  0.0287  0.0123  28   GLN A NE2 
113   N N   . SER A 31   ? 0.2911 0.3732 0.3149 0.0279  0.0341  0.0270  29   SER A N   
114   C CA  . SER A 31   ? 0.2511 0.3396 0.2779 0.0263  0.0353  0.0321  29   SER A CA  
115   C C   . SER A 31   ? 0.2673 0.3606 0.2929 0.0245  0.0363  0.0376  29   SER A C   
116   O O   . SER A 31   ? 0.2595 0.3495 0.2820 0.0242  0.0359  0.0376  29   SER A O   
117   C CB  . SER A 31   ? 0.2487 0.3289 0.2787 0.0240  0.0340  0.0344  29   SER A CB  
118   O OG  . SER A 31   ? 0.2345 0.3060 0.2635 0.0218  0.0328  0.0368  29   SER A OG  
119   N N   . THR A 32   ? 0.2560 0.3574 0.2844 0.0232  0.0376  0.0425  30   THR A N   
120   C CA  . THR A 32   ? 0.2395 0.3453 0.2679 0.0210  0.0382  0.0488  30   THR A CA  
121   C C   . THR A 32   ? 0.2442 0.3385 0.2727 0.0186  0.0364  0.0513  30   THR A C   
122   O O   . THR A 32   ? 0.2572 0.3513 0.2838 0.0178  0.0363  0.0534  30   THR A O   
123   C CB  . THR A 32   ? 0.2580 0.3723 0.2907 0.0195  0.0393  0.0543  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3443 0.4703 0.3767 0.0219  0.0411  0.0517  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.3046 0.4235 0.3382 0.0170  0.0397  0.0614  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2360 0.3210 0.2671 0.0175  0.0350  0.0507  31   LEU A N   
127   C CA  . LEU A 33   ? 0.2531 0.3278 0.2847 0.0153  0.0332  0.0525  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2433 0.3115 0.2705 0.0164  0.0324  0.0484  31   LEU A C   
129   O O   . LEU A 33   ? 0.2326 0.2965 0.2590 0.0151  0.0316  0.0504  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2591 0.3266 0.2943 0.0141  0.0319  0.0523  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2654 0.3372 0.3058 0.0120  0.0321  0.0577  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.2521 0.3183 0.2956 0.0114  0.0310  0.0564  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.3145 0.3848 0.3572 0.0094  0.0313  0.0632  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.2130 0.2802 0.2378 0.0189  0.0324  0.0426  32   ARG A N   
135   C CA  . ARG A 34   ? 0.2122 0.2738 0.2330 0.0199  0.0316  0.0388  32   ARG A CA  
136   C C   . ARG A 34   ? 0.1992 0.2674 0.2170 0.0207  0.0326  0.0397  32   ARG A C   
137   O O   . ARG A 34   ? 0.2203 0.2837 0.2357 0.0202  0.0319  0.0395  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2299 0.2895 0.2496 0.0224  0.0311  0.0327  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2585 0.3099 0.2805 0.0216  0.0297  0.0315  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2581 0.2993 0.2787 0.0201  0.0280  0.0313  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2598 0.2979 0.2770 0.0216  0.0274  0.0273  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.3198 0.3535 0.3367 0.0228  0.0262  0.0232  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.2824 0.3141 0.3021 0.0228  0.0255  0.0223  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.2775 0.3087 0.2918 0.0240  0.0256  0.0200  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2192 0.2988 0.2371 0.0218  0.0343  0.0407  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2393 0.3262 0.2542 0.0225  0.0353  0.0416  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2403 0.3264 0.2561 0.0198  0.0350  0.0480  33   ARG A C   
148   O O   . ARG A 35   ? 0.2347 0.3216 0.2478 0.0198  0.0350  0.0485  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2672 0.3678 0.2820 0.0242  0.0373  0.0414  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.2869 0.3891 0.3007 0.0274  0.0374  0.0341  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.3563 0.4727 0.3707 0.0292  0.0393  0.0335  33   ARG A CD  
152   N NE  . ARG A 35   ? 0.4732 0.5903 0.4875 0.0324  0.0390  0.0262  33   ARG A NE  
153   C CZ  . ARG A 35   ? 0.5534 0.6723 0.5648 0.0349  0.0388  0.0206  33   ARG A CZ  
154   N NH1 . ARG A 35   ? 0.5662 0.6870 0.5741 0.0348  0.0389  0.0216  33   ARG A NH1 
155   N NH2 . ARG A 35   ? 0.5757 0.6944 0.5883 0.0378  0.0381  0.0139  33   ARG A NH2 
156   N N   . ALA A 36   ? 0.2238 0.3081 0.2440 0.0174  0.0347  0.0528  34   ALA A N   
157   C CA  . ALA A 36   ? 0.2519 0.3345 0.2741 0.0147  0.0339  0.0588  34   ALA A CA  
158   C C   . ALA A 36   ? 0.2438 0.3151 0.2647 0.0141  0.0322  0.0570  34   ALA A C   
159   O O   . ALA A 36   ? 0.2542 0.3247 0.2748 0.0131  0.0316  0.0599  34   ALA A O   
160   C CB  . ALA A 36   ? 0.2437 0.3267 0.2717 0.0124  0.0336  0.0639  34   ALA A CB  
161   N N   . ILE A 37   ? 0.2035 0.2662 0.2236 0.0149  0.0312  0.0521  35   ILE A N   
162   C CA  . ILE A 37   ? 0.2000 0.2529 0.2183 0.0145  0.0297  0.0498  35   ILE A CA  
163   C C   . ILE A 37   ? 0.2120 0.2670 0.2258 0.0161  0.0301  0.0474  35   ILE A C   
164   O O   . ILE A 37   ? 0.2175 0.2697 0.2304 0.0152  0.0294  0.0491  35   ILE A O   
165   C CB  . ILE A 37   ? 0.1811 0.2260 0.1994 0.0150  0.0287  0.0453  35   ILE A CB  
166   C CG1 . ILE A 37   ? 0.2161 0.2584 0.2390 0.0132  0.0281  0.0479  35   ILE A CG1 
167   C CG2 . ILE A 37   ? 0.2107 0.2470 0.2266 0.0149  0.0274  0.0426  35   ILE A CG2 
168   C CD1 . ILE A 37   ? 0.2263 0.2632 0.2494 0.0137  0.0273  0.0439  35   ILE A CD1 
169   N N   . THR A 38   ? 0.2220 0.2818 0.2330 0.0185  0.0311  0.0433  36   THR A N   
170   C CA  . THR A 38   ? 0.2190 0.2804 0.2258 0.0202  0.0312  0.0402  36   THR A CA  
171   C C   . THR A 38   ? 0.2321 0.3009 0.2381 0.0196  0.0320  0.0446  36   THR A C   
172   O O   . THR A 38   ? 0.2336 0.3006 0.2370 0.0198  0.0315  0.0441  36   THR A O   
173   C CB  . THR A 38   ? 0.2483 0.3144 0.2533 0.0231  0.0320  0.0348  36   THR A CB  
174   O OG1 . THR A 38   ? 0.2466 0.3058 0.2532 0.0234  0.0310  0.0315  36   THR A OG1 
175   C CG2 . THR A 38   ? 0.2599 0.3265 0.2610 0.0249  0.0317  0.0309  36   THR A CG2 
176   N N   . ALA A 39   ? 0.2275 0.3048 0.2359 0.0188  0.0331  0.0493  37   ALA A N   
177   C CA  . ALA A 39   ? 0.2417 0.3273 0.2497 0.0180  0.0338  0.0543  37   ALA A CA  
178   C C   . ALA A 39   ? 0.2571 0.3361 0.2667 0.0157  0.0323  0.0584  37   ALA A C   
179   O O   . ALA A 39   ? 0.2755 0.3589 0.2838 0.0154  0.0324  0.0613  37   ALA A O   
180   C CB  . ALA A 39   ? 0.2421 0.3378 0.2532 0.0171  0.0351  0.0592  37   ALA A CB  
181   N N   . ALA A 40   ? 0.2281 0.2970 0.2407 0.0142  0.0309  0.0586  38   ALA A N   
182   C CA  . ALA A 40   ? 0.2529 0.3154 0.2679 0.0121  0.0293  0.0621  38   ALA A CA  
183   C C   . ALA A 40   ? 0.2508 0.3049 0.2628 0.0128  0.0282  0.0578  38   ALA A C   
184   O O   . ALA A 40   ? 0.2444 0.2932 0.2583 0.0113  0.0269  0.0600  38   ALA A O   
185   C CB  . ALA A 40   ? 0.2328 0.2897 0.2534 0.0101  0.0282  0.0645  38   ALA A CB  
186   N N   . TYR A 41   ? 0.2309 0.2838 0.2387 0.0149  0.0287  0.0519  39   TYR A N   
187   C CA  . TYR A 41   ? 0.2277 0.2721 0.2330 0.0155  0.0276  0.0476  39   TYR A CA  
188   C C   . TYR A 41   ? 0.2368 0.2796 0.2414 0.0147  0.0268  0.0498  39   TYR A C   
189   O O   . TYR A 41   ? 0.2276 0.2623 0.2336 0.0137  0.0254  0.0495  39   TYR A O   
190   C CB  . TYR A 41   ? 0.2306 0.2769 0.2317 0.0181  0.0283  0.0418  39   TYR A CB  
191   C CG  . TYR A 41   ? 0.2352 0.2726 0.2345 0.0187  0.0271  0.0367  39   TYR A CG  
192   C CD1 . TYR A 41   ? 0.2306 0.2602 0.2300 0.0175  0.0259  0.0369  39   TYR A CD1 
193   C CD2 . TYR A 41   ? 0.2473 0.2846 0.2451 0.0206  0.0273  0.0318  39   TYR A CD2 
194   C CE1 . TYR A 41   ? 0.2299 0.2525 0.2277 0.0180  0.0249  0.0326  39   TYR A CE1 
195   C CE2 . TYR A 41   ? 0.2554 0.2852 0.2520 0.0210  0.0261  0.0277  39   TYR A CE2 
196   C CZ  . TYR A 41   ? 0.2452 0.2679 0.2415 0.0197  0.0250  0.0283  39   TYR A CZ  
197   O OH  . TYR A 41   ? 0.2458 0.2619 0.2410 0.0199  0.0239  0.0246  39   TYR A OH  
198   N N   . ARG A 42   ? 0.2526 0.3035 0.2555 0.0153  0.0276  0.0520  40   ARG A N   
199   C CA  . ARG A 42   ? 0.2594 0.3097 0.2617 0.0147  0.0268  0.0542  40   ARG A CA  
200   C C   . ARG A 42   ? 0.2384 0.2966 0.2434 0.0133  0.0271  0.0611  40   ARG A C   
201   O O   . ARG A 42   ? 0.2824 0.3449 0.2859 0.0134  0.0270  0.0632  40   ARG A O   
202   C CB  . ARG A 42   ? 0.3007 0.3523 0.2978 0.0167  0.0271  0.0497  40   ARG A CB  
203   C CG  . ARG A 42   ? 0.2724 0.3152 0.2677 0.0176  0.0264  0.0437  40   ARG A CG  
204   C CD  . ARG A 42   ? 0.3130 0.3568 0.3038 0.0197  0.0265  0.0389  40   ARG A CD  
205   N NE  . ARG A 42   ? 0.2983 0.3355 0.2884 0.0205  0.0260  0.0337  40   ARG A NE  
206   C CZ  . ARG A 42   ? 0.2726 0.3008 0.2629 0.0197  0.0248  0.0320  40   ARG A CZ  
207   N NH1 . ARG A 42   ? 0.2679 0.2925 0.2589 0.0185  0.0239  0.0342  40   ARG A NH1 
208   N NH2 . ARG A 42   ? 0.2546 0.2777 0.2447 0.0203  0.0243  0.0281  40   ARG A NH2 
209   N N   . ARG A 43   ? 0.2447 0.3049 0.2541 0.0119  0.0272  0.0650  41   ARG A N   
210   C CA  . ARG A 43   ? 0.2528 0.3208 0.2656 0.0102  0.0273  0.0723  41   ARG A CA  
211   C C   . ARG A 43   ? 0.2920 0.3561 0.3077 0.0086  0.0255  0.0762  41   ARG A C   
212   O O   . ARG A 43   ? 0.2562 0.3103 0.2740 0.0079  0.0239  0.0746  41   ARG A O   
213   C CB  . ARG A 43   ? 0.2545 0.3226 0.2725 0.0087  0.0273  0.0754  41   ARG A CB  
214   C CG  . ARG A 43   ? 0.2766 0.3519 0.2997 0.0065  0.0270  0.0837  41   ARG A CG  
215   C CD  . ARG A 43   ? 0.2684 0.3455 0.2958 0.0055  0.0274  0.0858  41   ARG A CD  
216   N NE  . ARG A 43   ? 0.2796 0.3639 0.3030 0.0074  0.0296  0.0824  41   ARG A NE  
217   C CZ  . ARG A 43   ? 0.2376 0.3214 0.2626 0.0076  0.0301  0.0808  41   ARG A CZ  
218   N NH1 . ARG A 43   ? 0.2704 0.3468 0.3005 0.0059  0.0287  0.0820  41   ARG A NH1 
219   N NH2 . ARG A 43   ? 0.2914 0.3825 0.3131 0.0096  0.0320  0.0776  41   ARG A NH2 
220   N N   . PRO A 44   ? 0.2929 0.3650 0.3087 0.0081  0.0256  0.0813  42   PRO A N   
221   C CA  . PRO A 44   ? 0.3015 0.3700 0.3207 0.0065  0.0237  0.0853  42   PRO A CA  
222   C C   . PRO A 44   ? 0.2412 0.3023 0.2678 0.0043  0.0217  0.0885  42   PRO A C   
223   O O   . PRO A 44   ? 0.2802 0.3434 0.3107 0.0032  0.0220  0.0912  42   PRO A O   
224   C CB  . PRO A 44   ? 0.3171 0.3976 0.3362 0.0059  0.0242  0.0917  42   PRO A CB  
225   C CG  . PRO A 44   ? 0.3483 0.4377 0.3611 0.0082  0.0266  0.0879  42   PRO A CG  
226   C CD  . PRO A 44   ? 0.3217 0.4069 0.3343 0.0090  0.0274  0.0832  42   PRO A CD  
227   N N   . GLU A 45   ? 0.2858 0.3383 0.3148 0.0038  0.0198  0.0876  43   GLU A N   
228   C CA  . GLU A 45   ? 0.2830 0.3278 0.3192 0.0020  0.0177  0.0892  43   GLU A CA  
229   C C   . GLU A 45   ? 0.2906 0.3405 0.3342 -0.0003 0.0166  0.0975  43   GLU A C   
230   O O   . GLU A 45   ? 0.2959 0.3425 0.3455 -0.0017 0.0155  0.0991  43   GLU A O   
231   C CB  . GLU A 45   ? 0.3177 0.3537 0.3549 0.0022  0.0158  0.0865  43   GLU A CB  
232   C CG  . GLU A 45   ? 0.3627 0.3888 0.4017 0.0022  0.0148  0.0814  43   GLU A CG  
233   C CD  . GLU A 45   ? 0.3033 0.3219 0.3418 0.0027  0.0135  0.0776  43   GLU A CD  
234   O OE1 . GLU A 45   ? 0.2907 0.3108 0.3241 0.0039  0.0141  0.0760  43   GLU A OE1 
235   O OE2 . GLU A 45   ? 0.2767 0.2882 0.3201 0.0020  0.0117  0.0760  43   GLU A OE2 
236   N N   . THR A 46   ? 0.2956 0.3537 0.3392 -0.0008 0.0167  0.1032  44   THR A N   
237   C CA  . THR A 46   ? 0.3475 0.4117 0.3983 -0.0032 0.0156  0.1119  44   THR A CA  
238   C C   . THR A 46   ? 0.3588 0.4299 0.4101 -0.0037 0.0173  0.1139  44   THR A C   
239   O O   . THR A 46   ? 0.3819 0.4557 0.4405 -0.0060 0.0161  0.1205  44   THR A O   
240   C CB  . THR A 46   ? 0.3184 0.3914 0.3681 -0.0036 0.0156  0.1176  44   THR A CB  
241   O OG1 . THR A 46   ? 0.3329 0.4144 0.3739 -0.0016 0.0183  0.1147  44   THR A OG1 
242   C CG2 . THR A 46   ? 0.3247 0.3908 0.3755 -0.0035 0.0135  0.1168  44   THR A CG2 
243   N N   . GLU A 47   ? 0.3041 0.3783 0.3484 -0.0017 0.0198  0.1085  45   GLU A N   
244   C CA  . GLU A 47   ? 0.2897 0.3698 0.3346 -0.0019 0.0214  0.1095  45   GLU A CA  
245   C C   . GLU A 47   ? 0.2903 0.3612 0.3382 -0.0021 0.0207  0.1056  45   GLU A C   
246   O O   . GLU A 47   ? 0.3131 0.3869 0.3650 -0.0033 0.0209  0.1086  45   GLU A O   
247   C CB  . GLU A 47   ? 0.3427 0.4310 0.3792 0.0006  0.0243  0.1053  45   GLU A CB  
248   C CG  . GLU A 47   ? 0.4528 0.5505 0.4854 0.0012  0.0250  0.1078  45   GLU A CG  
249   C CD  . GLU A 47   ? 0.4577 0.5657 0.4834 0.0035  0.0278  0.1043  45   GLU A CD  
250   O OE1 . GLU A 47   ? 0.5305 0.6379 0.5548 0.0046  0.0291  0.0999  45   GLU A OE1 
251   O OE2 . GLU A 47   ? 0.6009 0.7179 0.6229 0.0042  0.0286  0.1059  45   GLU A OE2 
252   N N   . CYS A 48   ? 0.2574 0.3175 0.3034 -0.0011 0.0198  0.0993  46   CYS A N   
253   C CA  . CYS A 48   ? 0.2567 0.3087 0.3050 -0.0012 0.0192  0.0953  46   CYS A CA  
254   C C   . CYS A 48   ? 0.2367 0.2837 0.2943 -0.0036 0.0166  0.0995  46   CYS A C   
255   O O   . CYS A 48   ? 0.2577 0.3025 0.3191 -0.0044 0.0162  0.0992  46   CYS A O   
256   C CB  . CYS A 48   ? 0.2825 0.3254 0.3261 0.0005  0.0190  0.0876  46   CYS A CB  
257   S SG  . CYS A 48   ? 0.2951 0.3417 0.3288 0.0034  0.0216  0.0815  46   CYS A SG  
258   N N   . LEU A 49   ? 0.2726 0.3175 0.3345 -0.0047 0.0145  0.1031  47   LEU A N   
259   C CA  . LEU A 49   ? 0.3054 0.3433 0.3765 -0.0066 0.0114  0.1052  47   LEU A CA  
260   C C   . LEU A 49   ? 0.2912 0.3336 0.3704 -0.0090 0.0105  0.1123  47   LEU A C   
261   O O   . LEU A 49   ? 0.2877 0.3245 0.3729 -0.0100 0.0088  0.1114  47   LEU A O   
262   C CB  . LEU A 49   ? 0.3076 0.3411 0.3816 -0.0069 0.0092  0.1062  47   LEU A CB  
263   C CG  . LEU A 49   ? 0.3117 0.3350 0.3835 -0.0056 0.0083  0.0986  47   LEU A CG  
264   C CD1 . LEU A 49   ? 0.2856 0.3017 0.3633 -0.0063 0.0066  0.0959  47   LEU A CD1 
265   C CD2 . LEU A 49   ? 0.2705 0.2943 0.3320 -0.0032 0.0110  0.0922  47   LEU A CD2 
266   N N   . PRO A 50   ? 0.3080 0.3607 0.3880 -0.0100 0.0113  0.1194  48   PRO A N   
267   C CA  . PRO A 50   ? 0.3175 0.3746 0.4064 -0.0126 0.0100  0.1270  48   PRO A CA  
268   C C   . PRO A 50   ? 0.3098 0.3656 0.4003 -0.0128 0.0106  0.1248  48   PRO A C   
269   O O   . PRO A 50   ? 0.3421 0.3936 0.4415 -0.0147 0.0082  0.1273  48   PRO A O   
270   C CB  . PRO A 50   ? 0.3252 0.3957 0.4115 -0.0130 0.0118  0.1336  48   PRO A CB  
271   C CG  . PRO A 50   ? 0.3278 0.3981 0.4080 -0.0115 0.0122  0.1315  48   PRO A CG  
272   C CD  . PRO A 50   ? 0.3052 0.3659 0.3793 -0.0091 0.0129  0.1214  48   PRO A CD  
273   N N   . PRO A 51   ? 0.3011 0.3603 0.3839 -0.0110 0.0136  0.1202  49   PRO A N   
274   C CA  . PRO A 51   ? 0.3421 0.3994 0.4270 -0.0112 0.0139  0.1180  49   PRO A CA  
275   C C   . PRO A 51   ? 0.2746 0.3197 0.3620 -0.0110 0.0119  0.1121  49   PRO A C   
276   O O   . PRO A 51   ? 0.3128 0.3553 0.4057 -0.0121 0.0108  0.1124  49   PRO A O   
277   C CB  . PRO A 51   ? 0.3060 0.3695 0.3820 -0.0090 0.0173  0.1139  49   PRO A CB  
278   C CG  . PRO A 51   ? 0.3171 0.3811 0.3855 -0.0070 0.0184  0.1108  49   PRO A CG  
279   C CD  . PRO A 51   ? 0.2950 0.3604 0.3678 -0.0086 0.0166  0.1169  49   PRO A CD  
280   N N   . LEU A 52   ? 0.3083 0.3465 0.3917 -0.0095 0.0114  0.1068  50   LEU A N   
281   C CA  . LEU A 52   ? 0.2900 0.3176 0.3760 -0.0094 0.0094  0.1013  50   LEU A CA  
282   C C   . LEU A 52   ? 0.2686 0.2920 0.3655 -0.0116 0.0058  0.1054  50   LEU A C   
283   O O   . LEU A 52   ? 0.2632 0.2814 0.3657 -0.0124 0.0040  0.1036  50   LEU A O   
284   C CB  . LEU A 52   ? 0.2659 0.2881 0.3450 -0.0074 0.0098  0.0949  50   LEU A CB  
285   C CG  . LEU A 52   ? 0.3018 0.3268 0.3708 -0.0051 0.0128  0.0900  50   LEU A CG  
286   C CD1 . LEU A 52   ? 0.2582 0.2784 0.3213 -0.0035 0.0129  0.0850  50   LEU A CD1 
287   C CD2 . LEU A 52   ? 0.2958 0.3183 0.3636 -0.0046 0.0135  0.0857  50   LEU A CD2 
288   N N   . VAL A 53   ? 0.2920 0.3179 0.3925 -0.0126 0.0046  0.1110  51   VAL A N   
289   C CA  . VAL A 53   ? 0.3266 0.3493 0.4387 -0.0148 0.0009  0.1157  51   VAL A CA  
290   C C   . VAL A 53   ? 0.3095 0.3353 0.4289 -0.0168 0.0002  0.1204  51   VAL A C   
291   O O   . VAL A 53   ? 0.3036 0.3235 0.4315 -0.0180 -0.0027 0.1198  51   VAL A O   
292   C CB  . VAL A 53   ? 0.2768 0.3036 0.3913 -0.0157 0.0000  0.1222  51   VAL A CB  
293   C CG1 . VAL A 53   ? 0.3139 0.3385 0.4416 -0.0182 -0.0040 0.1284  51   VAL A CG1 
294   C CG2 . VAL A 53   ? 0.2781 0.3004 0.3867 -0.0138 0.0001  0.1171  51   VAL A CG2 
295   N N   . GLU A 54   ? 0.2990 0.3346 0.4153 -0.0172 0.0027  0.1248  52   GLU A N   
296   C CA  . GLU A 54   ? 0.3379 0.3774 0.4609 -0.0191 0.0022  0.1295  52   GLU A CA  
297   C C   . GLU A 54   ? 0.2852 0.3184 0.4084 -0.0185 0.0020  0.1231  52   GLU A C   
298   O O   . GLU A 54   ? 0.3347 0.3644 0.4671 -0.0202 -0.0006 0.1246  52   GLU A O   
299   C CB  . GLU A 54   ? 0.3700 0.4219 0.4883 -0.0193 0.0054  0.1344  52   GLU A CB  
300   N N   . ALA A 55   ? 0.2862 0.3176 0.3995 -0.0161 0.0045  0.1157  53   ALA A N   
301   C CA  . ALA A 55   ? 0.3269 0.3535 0.4396 -0.0155 0.0046  0.1099  53   ALA A CA  
302   C C   . ALA A 55   ? 0.2817 0.2980 0.3998 -0.0157 0.0013  0.1055  53   ALA A C   
303   O O   . ALA A 55   ? 0.3248 0.3375 0.4468 -0.0162 0.0001  0.1029  53   ALA A O   
304   C CB  . ALA A 55   ? 0.3059 0.3332 0.4073 -0.0129 0.0077  0.1034  53   ALA A CB  
305   N N   . ALA A 56   ? 0.2733 0.2853 0.3919 -0.0153 -0.0001 0.1043  54   ALA A N   
306   C CA  . ALA A 56   ? 0.2917 0.2945 0.4149 -0.0152 -0.0031 0.0993  54   ALA A CA  
307   C C   . ALA A 56   ? 0.3585 0.3590 0.4948 -0.0174 -0.0070 0.1041  54   ALA A C   
308   O O   . ALA A 56   ? 0.3010 0.2943 0.4427 -0.0173 -0.0099 0.0999  54   ALA A O   
309   C CB  . ALA A 56   ? 0.2742 0.2734 0.3913 -0.0133 -0.0026 0.0948  54   ALA A CB  
310   N N   . THR A 57   ? 0.3267 0.3335 0.4685 -0.0193 -0.0074 0.1127  55   THR A N   
311   C CA  . THR A 57   ? 0.2933 0.2982 0.4484 -0.0217 -0.0114 0.1181  55   THR A CA  
312   C C   . THR A 57   ? 0.3151 0.3158 0.4777 -0.0226 -0.0136 0.1158  55   THR A C   
313   O O   . THR A 57   ? 0.3305 0.3342 0.4902 -0.0226 -0.0118 0.1151  55   THR A O   
314   C CB  . THR A 57   ? 0.3581 0.3721 0.5167 -0.0237 -0.0109 0.1284  55   THR A CB  
315   O OG1 . THR A 57   ? 0.3528 0.3706 0.5053 -0.0229 -0.0093 0.1305  55   THR A OG1 
316   C CG2 . THR A 57   ? 0.3756 0.3881 0.5491 -0.0265 -0.0153 0.1350  55   THR A CG2 
317   N N   . GLN A 58   ? 0.3049 0.2986 0.4775 -0.0233 -0.0178 0.1141  56   GLN A N   
318   C CA  . GLN A 58   ? 0.3042 0.2940 0.4858 -0.0243 -0.0206 0.1123  56   GLN A CA  
319   C C   . GLN A 58   ? 0.3163 0.3046 0.5130 -0.0267 -0.0251 0.1186  56   GLN A C   
320   O O   . GLN A 58   ? 0.3294 0.3180 0.5292 -0.0272 -0.0264 0.1229  56   GLN A O   
321   C CB  . GLN A 58   ? 0.3023 0.2846 0.4814 -0.0224 -0.0214 0.1019  56   GLN A CB  
322   C CG  . GLN A 58   ? 0.2986 0.2820 0.4635 -0.0202 -0.0173 0.0958  56   GLN A CG  
323   C CD  . GLN A 58   ? 0.3086 0.2860 0.4724 -0.0188 -0.0183 0.0866  56   GLN A CD  
324   O OE1 . GLN A 58   ? 0.3280 0.3048 0.4948 -0.0194 -0.0191 0.0849  56   GLN A OE1 
325   N NE2 . GLN A 58   ? 0.3423 0.3155 0.5018 -0.0171 -0.0185 0.0806  56   GLN A NE2 
326   N N   . SER A 59   ? 0.3058 0.2921 0.5121 -0.0282 -0.0278 0.1190  57   SER A N   
327   C CA  . SER A 59   ? 0.3079 0.2949 0.5272 -0.0297 -0.0323 0.1226  57   SER A CA  
328   C C   . SER A 59   ? 0.3793 0.3595 0.6045 -0.0287 -0.0360 0.1178  57   SER A C   
329   O O   . SER A 59   ? 0.3127 0.2862 0.5338 -0.0270 -0.0357 0.1105  57   SER A O   
330   C CB  . SER A 59   ? 0.3611 0.3476 0.5883 -0.0309 -0.0345 0.1217  57   SER A CB  
331   O OG  . SER A 59   ? 0.3632 0.3414 0.5919 -0.0297 -0.0361 0.1130  57   SER A OG  
332   N N   . LYS A 60   ? 0.3262 0.3086 0.5615 -0.0298 -0.0397 0.1218  58   LYS A N   
333   C CA  . LYS A 60   ? 0.3537 0.3304 0.5963 -0.0288 -0.0436 0.1175  58   LYS A CA  
334   C C   . LYS A 60   ? 0.3364 0.3057 0.5840 -0.0278 -0.0462 0.1086  58   LYS A C   
335   O O   . LYS A 60   ? 0.3819 0.3451 0.6289 -0.0261 -0.0473 0.1016  58   LYS A O   
336   C CB  . LYS A 60   ? 0.3620 0.3429 0.6161 -0.0304 -0.0475 0.1238  58   LYS A CB  
337   C CG  . LYS A 60   ? 0.3736 0.3496 0.6361 -0.0295 -0.0517 0.1200  58   LYS A CG  
338   C CD  . LYS A 60   ? 0.4589 0.4328 0.7128 -0.0280 -0.0495 0.1180  58   LYS A CD  
339   C CE  . LYS A 60   ? 0.4944 0.4660 0.7570 -0.0276 -0.0535 0.1172  58   LYS A CE  
340   N NZ  . LYS A 60   ? 0.5227 0.4868 0.7919 -0.0260 -0.0569 0.1079  58   LYS A NZ  
341   N N   . GLU A 61   ? 0.3428 0.3127 0.5952 -0.0289 -0.0473 0.1086  59   GLU A N   
342   C CA  . GLU A 61   ? 0.3496 0.3132 0.6065 -0.0279 -0.0497 0.1000  59   GLU A CA  
343   C C   . GLU A 61   ? 0.3833 0.3421 0.6293 -0.0261 -0.0466 0.0927  59   GLU A C   
344   O O   . GLU A 61   ? 0.3731 0.3261 0.6210 -0.0245 -0.0485 0.0845  59   GLU A O   
345   C CB  . GLU A 61   ? 0.3539 0.3200 0.6165 -0.0294 -0.0508 0.1018  59   GLU A CB  
346   N N   . ILE A 62   ? 0.3564 0.3181 0.5913 -0.0263 -0.0418 0.0956  60   ILE A N   
347   C CA  . ILE A 62   ? 0.3316 0.2913 0.5538 -0.0241 -0.0385 0.0880  60   ILE A CA  
348   C C   . ILE A 62   ? 0.3329 0.2900 0.5506 -0.0222 -0.0382 0.0844  60   ILE A C   
349   O O   . ILE A 62   ? 0.3254 0.2790 0.5386 -0.0201 -0.0381 0.0755  60   ILE A O   
350   C CB  . ILE A 62   ? 0.3350 0.3009 0.5448 -0.0240 -0.0334 0.0907  60   ILE A CB  
351   C CG1 . ILE A 62   ? 0.3887 0.3560 0.6014 -0.0250 -0.0336 0.0905  60   ILE A CG1 
352   C CG2 . ILE A 62   ? 0.3354 0.3011 0.5306 -0.0213 -0.0297 0.0839  60   ILE A CG2 
353   C CD1 . ILE A 62   ? 0.3885 0.3624 0.5919 -0.0253 -0.0292 0.0944  60   ILE A CD1 
354   N N   . ARG A 63   ? 0.3148 0.2742 0.5333 -0.0229 -0.0379 0.0914  61   ARG A N   
355   C CA  . ARG A 63   ? 0.3519 0.3091 0.5662 -0.0212 -0.0376 0.0884  61   ARG A CA  
356   C C   . ARG A 63   ? 0.3419 0.2924 0.5665 -0.0204 -0.0423 0.0824  61   ARG A C   
357   O O   . ARG A 63   ? 0.3351 0.2828 0.5545 -0.0182 -0.0418 0.0750  61   ARG A O   
358   C CB  . ARG A 63   ? 0.3110 0.2725 0.5250 -0.0223 -0.0367 0.0976  61   ARG A CB  
359   C CG  . ARG A 63   ? 0.4162 0.3845 0.6170 -0.0221 -0.0315 0.1008  61   ARG A CG  
360   C CD  . ARG A 63   ? 0.4650 0.4385 0.6641 -0.0229 -0.0303 0.1091  61   ARG A CD  
361   N NE  . ARG A 63   ? 0.4733 0.4514 0.6826 -0.0254 -0.0327 0.1173  61   ARG A NE  
362   C CZ  . ARG A 63   ? 0.5015 0.4803 0.7193 -0.0259 -0.0362 0.1199  61   ARG A CZ  
363   N NH1 . ARG A 63   ? 0.4777 0.4516 0.6965 -0.0246 -0.0378 0.1159  61   ARG A NH1 
364   N NH2 . ARG A 63   ? 0.4836 0.4684 0.7093 -0.0279 -0.0381 0.1267  61   ARG A NH2 
365   N N   . ASP A 64   ? 0.3550 0.3053 0.5927 -0.0217 -0.0465 0.0840  62   ASP A N   
366   C CA  . ASP A 64   ? 0.3774 0.3232 0.6245 -0.0205 -0.0510 0.0768  62   ASP A CA  
367   C C   . ASP A 64   ? 0.3460 0.2871 0.5912 -0.0191 -0.0511 0.0672  62   ASP A C   
368   O O   . ASP A 64   ? 0.3567 0.2937 0.6024 -0.0172 -0.0525 0.0593  62   ASP A O   
369   C CB  . ASP A 64   ? 0.3710 0.3191 0.6319 -0.0220 -0.0555 0.0805  62   ASP A CB  
370   C CG  . ASP A 64   ? 0.4035 0.3562 0.6676 -0.0232 -0.0561 0.0892  62   ASP A CG  
371   O OD1 . ASP A 64   ? 0.4118 0.3654 0.6678 -0.0227 -0.0534 0.0914  62   ASP A OD1 
372   O OD2 . ASP A 64   ? 0.4677 0.4234 0.7428 -0.0247 -0.0595 0.0939  62   ASP A OD2 
373   N N   . ALA A 65   ? 0.2974 0.2395 0.5403 -0.0201 -0.0496 0.0676  63   ALA A N   
374   C CA  . ALA A 65   ? 0.3046 0.2452 0.5433 -0.0185 -0.0493 0.0579  63   ALA A CA  
375   C C   . ALA A 65   ? 0.3529 0.2945 0.5763 -0.0162 -0.0452 0.0521  63   ALA A C   
376   O O   . ALA A 65   ? 0.3314 0.2709 0.5530 -0.0143 -0.0459 0.0429  63   ALA A O   
377   C CB  . ALA A 65   ? 0.3355 0.2788 0.5730 -0.0199 -0.0481 0.0600  63   ALA A CB  
378   N N   . ALA A 66   ? 0.3185 0.2639 0.5310 -0.0162 -0.0409 0.0571  64   ALA A N   
379   C CA  . ALA A 66   ? 0.3457 0.2921 0.5442 -0.0142 -0.0371 0.0522  64   ALA A CA  
380   C C   . ALA A 66   ? 0.3424 0.2857 0.5428 -0.0126 -0.0388 0.0480  64   ALA A C   
381   O O   . ALA A 66   ? 0.3293 0.2717 0.5231 -0.0107 -0.0378 0.0402  64   ALA A O   
382   C CB  . ALA A 66   ? 0.3084 0.2595 0.4964 -0.0146 -0.0327 0.0588  64   ALA A CB  
383   N N   . ALA A 67   ? 0.3040 0.2459 0.5136 -0.0135 -0.0414 0.0534  65   ALA A N   
384   C CA  . ALA A 67   ? 0.3325 0.2713 0.5452 -0.0121 -0.0433 0.0497  65   ALA A CA  
385   C C   . ALA A 67   ? 0.3379 0.2729 0.5578 -0.0108 -0.0468 0.0402  65   ALA A C   
386   O O   . ALA A 67   ? 0.3704 0.3042 0.5868 -0.0087 -0.0467 0.0332  65   ALA A O   
387   C CB  . ALA A 67   ? 0.3553 0.2932 0.5784 -0.0136 -0.0461 0.0578  65   ALA A CB  
388   N N   . SER A 68   ? 0.3478 0.2815 0.5780 -0.0119 -0.0500 0.0397  66   SER A N   
389   C CA  . SER A 68   ? 0.3818 0.3125 0.6194 -0.0106 -0.0536 0.0302  66   SER A CA  
390   C C   . SER A 68   ? 0.4017 0.3345 0.6272 -0.0089 -0.0505 0.0219  66   SER A C   
391   O O   . SER A 68   ? 0.3488 0.2808 0.5743 -0.0069 -0.0516 0.0132  66   SER A O   
392   C CB  . SER A 68   ? 0.3920 0.3210 0.6436 -0.0123 -0.0577 0.0321  66   SER A CB  
393   O OG  . SER A 68   ? 0.4856 0.4125 0.7436 -0.0109 -0.0610 0.0223  66   SER A OG  
394   N N   . THR A 69   ? 0.3445 0.2807 0.5602 -0.0096 -0.0468 0.0245  67   THR A N   
395   C CA  . THR A 69   ? 0.3283 0.2668 0.5320 -0.0082 -0.0438 0.0176  67   THR A CA  
396   C C   . THR A 69   ? 0.3141 0.2535 0.5076 -0.0064 -0.0411 0.0146  67   THR A C   
397   O O   . THR A 69   ? 0.3097 0.2497 0.4988 -0.0048 -0.0408 0.0064  67   THR A O   
398   C CB  . THR A 69   ? 0.3314 0.2731 0.5270 -0.0094 -0.0404 0.0221  67   THR A CB  
399   O OG1 . THR A 69   ? 0.3465 0.2876 0.5515 -0.0109 -0.0430 0.0237  67   THR A OG1 
400   C CG2 . THR A 69   ? 0.3337 0.2779 0.5165 -0.0080 -0.0372 0.0159  67   THR A CG2 
401   N N   . ALA A 70   ? 0.3035 0.2433 0.4929 -0.0068 -0.0390 0.0212  68   ALA A N   
402   C CA  . ALA A 70   ? 0.3323 0.2729 0.5122 -0.0052 -0.0364 0.0188  68   ALA A CA  
403   C C   . ALA A 70   ? 0.3616 0.2997 0.5484 -0.0037 -0.0396 0.0125  68   ALA A C   
404   O O   . ALA A 70   ? 0.3585 0.2976 0.5384 -0.0020 -0.0382 0.0061  68   ALA A O   
405   C CB  . ALA A 70   ? 0.3597 0.3016 0.5349 -0.0060 -0.0340 0.0272  68   ALA A CB  
406   N N   . ARG A 71   ? 0.3543 0.2892 0.5552 -0.0043 -0.0439 0.0142  69   ARG A N   
407   C CA  . ARG A 71   ? 0.3638 0.2963 0.5728 -0.0027 -0.0474 0.0077  69   ARG A CA  
408   C C   . ARG A 71   ? 0.3731 0.3065 0.5824 -0.0013 -0.0485 -0.0027 69   ARG A C   
409   O O   . ARG A 71   ? 0.3896 0.3238 0.5960 0.0007  -0.0484 -0.0099 69   ARG A O   
410   C CB  . ARG A 71   ? 0.3638 0.2926 0.5892 -0.0038 -0.0523 0.0118  69   ARG A CB  
411   C CG  . ARG A 71   ? 0.3799 0.3059 0.6166 -0.0021 -0.0568 0.0039  69   ARG A CG  
412   C CD  . ARG A 71   ? 0.3769 0.2995 0.6296 -0.0032 -0.0616 0.0089  69   ARG A CD  
413   N NE  . ARG A 71   ? 0.4335 0.3561 0.6840 -0.0035 -0.0605 0.0156  69   ARG A NE  
414   C CZ  . ARG A 71   ? 0.4398 0.3618 0.6891 -0.0016 -0.0606 0.0117  69   ARG A CZ  
415   N NH1 . ARG A 71   ? 0.4492 0.3707 0.6989 0.0007  -0.0617 0.0012  69   ARG A NH1 
416   N NH2 . ARG A 71   ? 0.4579 0.3802 0.7052 -0.0021 -0.0596 0.0185  69   ARG A NH2 
417   N N   . LYS A 72   ? 0.3121 0.2459 0.5246 -0.0022 -0.0496 -0.0035 70   LYS A N   
418   C CA  . LYS A 72   ? 0.3865 0.3220 0.5987 -0.0010 -0.0506 -0.0131 70   LYS A CA  
419   C C   . LYS A 72   ? 0.4027 0.3423 0.5995 0.0003  -0.0462 -0.0173 70   LYS A C   
420   O O   . LYS A 72   ? 0.3844 0.3260 0.5800 0.0020  -0.0468 -0.0260 70   LYS A O   
421   C CB  . LYS A 72   ? 0.3463 0.2819 0.5632 -0.0025 -0.0519 -0.0117 70   LYS A CB  
422   C CG  . LYS A 72   ? 0.4252 0.3631 0.6418 -0.0014 -0.0530 -0.0211 70   LYS A CG  
423   C CD  . LYS A 72   ? 0.4384 0.3760 0.6612 -0.0030 -0.0548 -0.0191 70   LYS A CD  
424   C CE  . LYS A 72   ? 0.5265 0.4661 0.7526 -0.0019 -0.0572 -0.0290 70   LYS A CE  
425   N NZ  . LYS A 72   ? 0.6927 0.6372 0.9047 -0.0007 -0.0535 -0.0344 70   LYS A NZ  
426   N N   . LEU A 73   ? 0.3384 0.2797 0.5236 -0.0007 -0.0419 -0.0114 71   LEU A N   
427   C CA  . LEU A 73   ? 0.3243 0.2693 0.4954 0.0003  -0.0379 -0.0146 71   LEU A CA  
428   C C   . LEU A 73   ? 0.3620 0.3072 0.5299 0.0019  -0.0372 -0.0176 71   LEU A C   
429   O O   . LEU A 73   ? 0.3516 0.2997 0.5133 0.0032  -0.0361 -0.0243 71   LEU A O   
430   C CB  . LEU A 73   ? 0.2916 0.2380 0.4524 -0.0009 -0.0338 -0.0073 71   LEU A CB  
431   C CG  . LEU A 73   ? 0.3336 0.2806 0.4952 -0.0024 -0.0336 -0.0042 71   LEU A CG  
432   C CD1 . LEU A 73   ? 0.3183 0.2667 0.4710 -0.0034 -0.0298 0.0034  71   LEU A CD1 
433   C CD2 . LEU A 73   ? 0.3363 0.2861 0.4943 -0.0018 -0.0336 -0.0112 71   LEU A CD2 
434   N N   . ILE A 74   ? 0.3089 0.2513 0.4809 0.0016  -0.0378 -0.0125 72   ILE A N   
435   C CA  . ILE A 74   ? 0.3397 0.2822 0.5088 0.0031  -0.0372 -0.0147 72   ILE A CA  
436   C C   . ILE A 74   ? 0.3767 0.3188 0.5545 0.0048  -0.0408 -0.0233 72   ILE A C   
437   O O   . ILE A 74   ? 0.3616 0.3060 0.5346 0.0064  -0.0398 -0.0290 72   ILE A O   
438   C CB  . ILE A 74   ? 0.3663 0.3064 0.5375 0.0023  -0.0370 -0.0064 72   ILE A CB  
439   C CG1 . ILE A 74   ? 0.3423 0.2842 0.5021 0.0011  -0.0327 0.0006  72   ILE A CG1 
440   C CG2 . ILE A 74   ? 0.3418 0.2811 0.5137 0.0038  -0.0375 -0.0090 72   ILE A CG2 
441   C CD1 . ILE A 74   ? 0.3819 0.3224 0.5447 -0.0001 -0.0327 0.0097  72   ILE A CD1 
442   N N   . GLU A 75   ? 0.3849 0.3244 0.5762 0.0045  -0.0451 -0.0246 73   GLU A N   
443   C CA  . GLU A 75   ? 0.3932 0.3327 0.5936 0.0063  -0.0488 -0.0338 73   GLU A CA  
444   C C   . GLU A 75   ? 0.4161 0.3607 0.6095 0.0075  -0.0475 -0.0424 73   GLU A C   
445   O O   . GLU A 75   ? 0.3909 0.3379 0.5843 0.0094  -0.0482 -0.0502 73   GLU A O   
446   C CB  . GLU A 75   ? 0.4196 0.3553 0.6363 0.0056  -0.0540 -0.0333 73   GLU A CB  
447   C CG  . GLU A 75   ? 0.4435 0.3748 0.6702 0.0051  -0.0565 -0.0273 73   GLU A CG  
448   C CD  . GLU A 75   ? 0.5100 0.4374 0.7519 0.0037  -0.0611 -0.0237 73   GLU A CD  
449   O OE1 . GLU A 75   ? 0.5017 0.4297 0.7463 0.0030  -0.0622 -0.0257 73   GLU A OE1 
450   O OE2 . GLU A 75   ? 0.5392 0.4631 0.7908 0.0032  -0.0637 -0.0186 73   GLU A OE2 
451   N N   . ALA A 76   ? 0.4059 0.3525 0.5930 0.0063  -0.0456 -0.0410 74   ALA A N   
452   C CA  . ALA A 76   ? 0.3897 0.3417 0.5688 0.0072  -0.0440 -0.0480 74   ALA A CA  
453   C C   . ALA A 76   ? 0.4210 0.3765 0.5873 0.0080  -0.0401 -0.0489 74   ALA A C   
454   O O   . ALA A 76   ? 0.4724 0.4323 0.6359 0.0095  -0.0400 -0.0566 74   ALA A O   
455   C CB  . ALA A 76   ? 0.4467 0.3998 0.6216 0.0056  -0.0427 -0.0450 74   ALA A CB  
456   N N   . LEU A 77   ? 0.4000 0.3540 0.5584 0.0070  -0.0368 -0.0412 75   LEU A N   
457   C CA  . LEU A 77   ? 0.3800 0.3369 0.5267 0.0076  -0.0332 -0.0414 75   LEU A CA  
458   C C   . LEU A 77   ? 0.4524 0.4098 0.6027 0.0094  -0.0345 -0.0466 75   LEU A C   
459   O O   . LEU A 77   ? 0.4621 0.4241 0.6065 0.0106  -0.0333 -0.0525 75   LEU A O   
460   C CB  . LEU A 77   ? 0.3918 0.3465 0.5317 0.0064  -0.0302 -0.0322 75   LEU A CB  
461   C CG  . LEU A 77   ? 0.3801 0.3361 0.5109 0.0050  -0.0271 -0.0277 75   LEU A CG  
462   C CD1 . LEU A 77   ? 0.3927 0.3468 0.5183 0.0042  -0.0246 -0.0195 75   LEU A CD1 
463   C CD2 . LEU A 77   ? 0.4152 0.3761 0.5359 0.0055  -0.0248 -0.0324 75   LEU A CD2 
464   N N   . ARG A 78   ? 0.3920 0.3449 0.5521 0.0096  -0.0372 -0.0442 76   ARG A N   
465   C CA  . ARG A 78   ? 0.4241 0.3771 0.5885 0.0113  -0.0386 -0.0487 76   ARG A CA  
466   C C   . ARG A 78   ? 0.4394 0.3953 0.6112 0.0131  -0.0418 -0.0590 76   ARG A C   
467   O O   . ARG A 78   ? 0.4912 0.4493 0.6638 0.0148  -0.0422 -0.0646 76   ARG A O   
468   C CB  . ARG A 78   ? 0.3786 0.3260 0.5521 0.0109  -0.0409 -0.0429 76   ARG A CB  
469   C CG  . ARG A 78   ? 0.4094 0.3555 0.5745 0.0098  -0.0375 -0.0341 76   ARG A CG  
470   C CD  . ARG A 78   ? 0.3731 0.3149 0.5468 0.0095  -0.0397 -0.0287 76   ARG A CD  
471   N NE  . ARG A 78   ? 0.3704 0.3123 0.5348 0.0091  -0.0364 -0.0227 76   ARG A NE  
472   C CZ  . ARG A 78   ? 0.3640 0.3031 0.5327 0.0087  -0.0374 -0.0168 76   ARG A CZ  
473   N NH1 . ARG A 78   ? 0.4042 0.3398 0.5866 0.0086  -0.0416 -0.0155 76   ARG A NH1 
474   N NH2 . ARG A 78   ? 0.3931 0.3331 0.5526 0.0084  -0.0342 -0.0121 76   ARG A NH2 
475   N N   . GLY A 79   ? 0.4622 0.4185 0.6395 0.0127  -0.0439 -0.0619 77   GLY A N   
476   C CA  . GLY A 79   ? 0.4925 0.4522 0.6769 0.0145  -0.0470 -0.0721 77   GLY A CA  
477   C C   . GLY A 79   ? 0.5445 0.5119 0.7188 0.0152  -0.0446 -0.0787 77   GLY A C   
478   O O   . GLY A 79   ? 0.5576 0.5291 0.7368 0.0167  -0.0469 -0.0878 77   GLY A O   
479   N N   . LYS A 80   ? 0.5569 0.5267 0.7175 0.0141  -0.0401 -0.0743 78   LYS A N   
480   C CA  . LYS A 80   ? 0.5708 0.5482 0.7215 0.0146  -0.0378 -0.0793 78   LYS A CA  
481   C C   . LYS A 80   ? 0.5631 0.5429 0.7018 0.0145  -0.0337 -0.0766 78   LYS A C   
482   O O   . LYS A 80   ? 0.6522 0.6381 0.7813 0.0143  -0.0313 -0.0786 78   LYS A O   
483   C CB  . LYS A 80   ? 0.5850 0.5639 0.7312 0.0130  -0.0368 -0.0774 78   LYS A CB  
484   C CG  . LYS A 80   ? 0.5535 0.5284 0.6928 0.0110  -0.0340 -0.0673 78   LYS A CG  
485   C CD  . LYS A 80   ? 0.5219 0.4974 0.6599 0.0097  -0.0339 -0.0656 78   LYS A CD  
486   C CE  . LYS A 80   ? 0.4631 0.4354 0.5939 0.0079  -0.0309 -0.0561 78   LYS A CE  
487   N NZ  . LYS A 80   ? 0.3737 0.3469 0.5028 0.0065  -0.0307 -0.0543 78   LYS A NZ  
488   N N   . HIS A 81   ? 0.5551 0.5305 0.6945 0.0145  -0.0332 -0.0719 79   HIS A N   
489   C CA  . HIS A 81   ? 0.6300 0.6070 0.7588 0.0144  -0.0295 -0.0687 79   HIS A CA  
490   C C   . HIS A 81   ? 0.7074 0.6921 0.8311 0.0157  -0.0285 -0.0760 79   HIS A C   
491   O O   . HIS A 81   ? 0.7644 0.7517 0.8953 0.0174  -0.0309 -0.0835 79   HIS A O   
492   C CB  . HIS A 81   ? 0.6223 0.5938 0.7550 0.0146  -0.0300 -0.0641 79   HIS A CB  
493   N N   . SER A 84   ? 0.6050 0.6047 0.6762 0.0133  -0.0117 -0.0636 82   SER A N   
494   C CA  . SER A 84   ? 0.6010 0.6057 0.6784 0.0149  -0.0138 -0.0720 82   SER A CA  
495   C C   . SER A 84   ? 0.5665 0.5807 0.6373 0.0150  -0.0121 -0.0760 82   SER A C   
496   O O   . SER A 84   ? 0.4994 0.5180 0.5730 0.0165  -0.0128 -0.0815 82   SER A O   
497   C CB  . SER A 84   ? 0.6534 0.6583 0.7379 0.0153  -0.0165 -0.0759 82   SER A CB  
498   N N   . GLY A 85   ? 0.5621 0.5796 0.6245 0.0134  -0.0101 -0.0730 83   GLY A N   
499   C CA  . GLY A 85   ? 0.4866 0.5133 0.5423 0.0131  -0.0084 -0.0754 83   GLY A CA  
500   C C   . GLY A 85   ? 0.3990 0.4263 0.4515 0.0133  -0.0068 -0.0740 83   GLY A C   
501   O O   . GLY A 85   ? 0.3942 0.4283 0.4475 0.0144  -0.0069 -0.0794 83   GLY A O   
502   N N   . VAL A 86   ? 0.4336 0.4542 0.4826 0.0124  -0.0054 -0.0670 84   VAL A N   
503   C CA  . VAL A 86   ? 0.4251 0.4454 0.4716 0.0126  -0.0041 -0.0654 84   VAL A CA  
504   C C   . VAL A 86   ? 0.4135 0.4323 0.4680 0.0147  -0.0060 -0.0699 84   VAL A C   
505   O O   . VAL A 86   ? 0.3666 0.3900 0.4208 0.0155  -0.0056 -0.0731 84   VAL A O   
506   C CB  . VAL A 86   ? 0.4884 0.5015 0.5303 0.0114  -0.0025 -0.0573 84   VAL A CB  
507   C CG1 . VAL A 86   ? 0.4634 0.4745 0.5047 0.0120  -0.0018 -0.0558 84   VAL A CG1 
508   C CG2 . VAL A 86   ? 0.4840 0.4999 0.5176 0.0096  -0.0006 -0.0535 84   VAL A CG2 
509   N N   . GLU A 87   ? 0.4207 0.4332 0.4831 0.0154  -0.0082 -0.0701 85   GLU A N   
510   C CA  . GLU A 87   ? 0.4305 0.4411 0.5018 0.0173  -0.0105 -0.0743 85   GLU A CA  
511   C C   . GLU A 87   ? 0.4252 0.4444 0.4998 0.0189  -0.0116 -0.0832 85   GLU A C   
512   O O   . GLU A 87   ? 0.4392 0.4606 0.5167 0.0203  -0.0120 -0.0867 85   GLU A O   
513   C CB  . GLU A 87   ? 0.5149 0.5180 0.5947 0.0177  -0.0130 -0.0729 85   GLU A CB  
514   N N   . GLY A 88   ? 0.3883 0.4131 0.4625 0.0187  -0.0121 -0.0871 86   GLY A N   
515   C CA  . GLY A 88   ? 0.3726 0.4067 0.4499 0.0202  -0.0131 -0.0961 86   GLY A CA  
516   C C   . GLY A 88   ? 0.3530 0.3957 0.4232 0.0201  -0.0108 -0.0973 86   GLY A C   
517   O O   . GLY A 88   ? 0.3754 0.4246 0.4492 0.0218  -0.0115 -0.1041 86   GLY A O   
518   N N   . LEU A 89   ? 0.3632 0.4061 0.4239 0.0180  -0.0080 -0.0907 87   LEU A N   
519   C CA  . LEU A 89   ? 0.3727 0.4234 0.4267 0.0175  -0.0057 -0.0908 87   LEU A CA  
520   C C   . LEU A 89   ? 0.3060 0.3536 0.3623 0.0185  -0.0056 -0.0903 87   LEU A C   
521   O O   . LEU A 89   ? 0.3292 0.3841 0.3861 0.0196  -0.0053 -0.0951 87   LEU A O   
522   C CB  . LEU A 89   ? 0.3684 0.4189 0.4128 0.0149  -0.0033 -0.0833 87   LEU A CB  
523   C CG  . LEU A 89   ? 0.3955 0.4560 0.4321 0.0136  -0.0011 -0.0827 87   LEU A CG  
524   C CD1 . LEU A 89   ? 0.4019 0.4594 0.4310 0.0111  0.0006  -0.0748 87   LEU A CD1 
525   C CD2 . LEU A 89   ? 0.4293 0.4926 0.4653 0.0142  -0.0001 -0.0836 87   LEU A CD2 
526   N N   . VAL A 90   ? 0.3352 0.3724 0.3928 0.0182  -0.0058 -0.0846 88   VAL A N   
527   C CA  . VAL A 90   ? 0.3328 0.3663 0.3932 0.0193  -0.0060 -0.0838 88   VAL A CA  
528   C C   . VAL A 90   ? 0.3290 0.3650 0.3989 0.0218  -0.0084 -0.0918 88   VAL A C   
529   O O   . VAL A 90   ? 0.3176 0.3570 0.3886 0.0229  -0.0082 -0.0945 88   VAL A O   
530   C CB  . VAL A 90   ? 0.3383 0.3605 0.3996 0.0186  -0.0062 -0.0767 88   VAL A CB  
531   C CG1 . VAL A 90   ? 0.3918 0.4098 0.4581 0.0200  -0.0072 -0.0767 88   VAL A CG1 
532   C CG2 . VAL A 90   ? 0.3369 0.3574 0.3887 0.0165  -0.0036 -0.0694 88   VAL A CG2 
533   N N   . GLN A 91   ? 0.3559 0.3903 0.4331 0.0228  -0.0110 -0.0958 89   GLN A N   
534   C CA  . GLN A 91   ? 0.3318 0.3684 0.4192 0.0253  -0.0138 -0.1040 89   GLN A CA  
535   C C   . GLN A 91   ? 0.3639 0.4131 0.4498 0.0263  -0.0132 -0.1117 89   GLN A C   
536   O O   . GLN A 91   ? 0.3809 0.4338 0.4710 0.0281  -0.0138 -0.1166 89   GLN A O   
537   C CB  . GLN A 91   ? 0.3761 0.4083 0.4720 0.0260  -0.0168 -0.1064 89   GLN A CB  
538   N N   . GLU A 92   ? 0.3410 0.3976 0.4209 0.0252  -0.0119 -0.1127 90   GLU A N   
539   C CA  . GLU A 92   ? 0.3585 0.4282 0.4374 0.0262  -0.0115 -0.1205 90   GLU A CA  
540   C C   . GLU A 92   ? 0.3172 0.3930 0.3911 0.0260  -0.0093 -0.1200 90   GLU A C   
541   O O   . GLU A 92   ? 0.3277 0.4122 0.4049 0.0278  -0.0098 -0.1273 90   GLU A O   
542   C CB  . GLU A 92   ? 0.3683 0.4447 0.4409 0.0246  -0.0105 -0.1203 90   GLU A CB  
543   C CG  . GLU A 92   ? 0.3888 0.4804 0.4590 0.0252  -0.0097 -0.1274 90   GLU A CG  
544   C CD  . GLU A 92   ? 0.4414 0.5397 0.5056 0.0235  -0.0089 -0.1268 90   GLU A CD  
545   O OE1 . GLU A 92   ? 0.4637 0.5545 0.5270 0.0222  -0.0093 -0.1220 90   GLU A OE1 
546   O OE2 . GLU A 92   ? 0.4578 0.5694 0.5183 0.0235  -0.0079 -0.1310 90   GLU A OE2 
547   N N   . TYR A 93   ? 0.2897 0.3613 0.3560 0.0240  -0.0069 -0.1115 91   TYR A N   
548   C CA  . TYR A 93   ? 0.3138 0.3908 0.3750 0.0235  -0.0047 -0.1102 91   TYR A CA  
549   C C   . TYR A 93   ? 0.3279 0.3967 0.3923 0.0242  -0.0050 -0.1072 91   TYR A C   
550   O O   . TYR A 93   ? 0.3073 0.3787 0.3672 0.0236  -0.0032 -0.1047 91   TYR A O   
551   C CB  . TYR A 93   ? 0.3116 0.3917 0.3622 0.0206  -0.0019 -0.1034 91   TYR A CB  
552   C CG  . TYR A 93   ? 0.3103 0.4015 0.3576 0.0200  -0.0015 -0.1070 91   TYR A CG  
553   C CD1 . TYR A 93   ? 0.3163 0.4211 0.3621 0.0204  -0.0006 -0.1122 91   TYR A CD1 
554   C CD2 . TYR A 93   ? 0.3211 0.4099 0.3671 0.0189  -0.0020 -0.1052 91   TYR A CD2 
555   C CE1 . TYR A 93   ? 0.3280 0.4440 0.3707 0.0198  -0.0003 -0.1154 91   TYR A CE1 
556   C CE2 . TYR A 93   ? 0.3612 0.4606 0.4043 0.0183  -0.0017 -0.1084 91   TYR A CE2 
557   C CZ  . TYR A 93   ? 0.3230 0.4361 0.3643 0.0187  -0.0009 -0.1135 91   TYR A CZ  
558   O OH  . TYR A 93   ? 0.3978 0.5222 0.4361 0.0181  -0.0006 -0.1166 91   TYR A OH  
559   N N   . SER A 94   ? 0.2823 0.3414 0.3545 0.0255  -0.0074 -0.1072 92   SER A N   
560   C CA  . SER A 94   ? 0.2784 0.3299 0.3546 0.0263  -0.0082 -0.1047 92   SER A CA  
561   C C   . SER A 94   ? 0.2399 0.2872 0.3076 0.0242  -0.0056 -0.0960 92   SER A C   
562   O O   . SER A 94   ? 0.2795 0.3271 0.3463 0.0245  -0.0048 -0.0949 92   SER A O   
563   C CB  . SER A 94   ? 0.3201 0.3777 0.4020 0.0287  -0.0091 -0.1119 92   SER A CB  
564   O OG  . SER A 94   ? 0.3296 0.3919 0.4194 0.0307  -0.0116 -0.1207 92   SER A OG  
565   N N   . LEU A 95   ? 0.2284 0.2720 0.2902 0.0222  -0.0044 -0.0900 93   LEU A N   
566   C CA  . LEU A 95   ? 0.2569 0.2969 0.3107 0.0202  -0.0022 -0.0821 93   LEU A CA  
567   C C   . LEU A 95   ? 0.2500 0.2792 0.3067 0.0205  -0.0030 -0.0772 93   LEU A C   
568   O O   . LEU A 95   ? 0.2727 0.2955 0.3353 0.0211  -0.0050 -0.0769 93   LEU A O   
569   C CB  . LEU A 95   ? 0.2462 0.2860 0.2935 0.0181  -0.0009 -0.0779 93   LEU A CB  
570   C CG  . LEU A 95   ? 0.2458 0.2964 0.2891 0.0174  0.0001  -0.0814 93   LEU A CG  
571   C CD1 . LEU A 95   ? 0.2869 0.3360 0.3235 0.0151  0.0014  -0.0756 93   LEU A CD1 
572   C CD2 . LEU A 95   ? 0.2562 0.3160 0.2962 0.0172  0.0016  -0.0834 93   LEU A CD2 
573   N N   . SER A 96   ? 0.2296 0.2574 0.2824 0.0199  -0.0016 -0.0733 94   SER A N   
574   C CA  . SER A 96   ? 0.2426 0.2609 0.2955 0.0196  -0.0018 -0.0671 94   SER A CA  
575   C C   . SER A 96   ? 0.2325 0.2466 0.2797 0.0177  -0.0007 -0.0611 94   SER A C   
576   O O   . SER A 96   ? 0.2253 0.2438 0.2679 0.0165  0.0004  -0.0613 94   SER A O   
577   C CB  . SER A 96   ? 0.2519 0.2706 0.3014 0.0193  -0.0005 -0.0646 94   SER A CB  
578   O OG  . SER A 96   ? 0.2280 0.2505 0.2689 0.0174  0.0018  -0.0615 94   SER A OG  
579   N N   . SER A 97   ? 0.2341 0.2401 0.2818 0.0174  -0.0010 -0.0557 95   SER A N   
580   C CA  . SER A 97   ? 0.2468 0.2490 0.2892 0.0158  0.0001  -0.0501 95   SER A CA  
581   C C   . SER A 97   ? 0.2362 0.2418 0.2700 0.0142  0.0025  -0.0473 95   SER A C   
582   O O   . SER A 97   ? 0.2246 0.2318 0.2541 0.0129  0.0034  -0.0458 95   SER A O   
583   C CB  . SER A 97   ? 0.2918 0.2859 0.3362 0.0158  -0.0005 -0.0449 95   SER A CB  
584   O OG  . SER A 97   ? 0.4086 0.3995 0.4613 0.0169  -0.0029 -0.0467 95   SER A OG  
585   N N   . GLN A 98   ? 0.2177 0.2246 0.2494 0.0142  0.0033  -0.0466 96   GLN A N   
586   C CA  . GLN A 98   ? 0.2103 0.2202 0.2346 0.0127  0.0052  -0.0437 96   GLN A CA  
587   C C   . GLN A 98   ? 0.1889 0.2074 0.2109 0.0119  0.0059  -0.0471 96   GLN A C   
588   O O   . GLN A 98   ? 0.1944 0.2148 0.2109 0.0102  0.0071  -0.0442 96   GLN A O   
589   C CB  . GLN A 98   ? 0.2103 0.2199 0.2334 0.0129  0.0057  -0.0425 96   GLN A CB  
590   C CG  . GLN A 98   ? 0.2332 0.2350 0.2562 0.0130  0.0055  -0.0377 96   GLN A CG  
591   C CD  . GLN A 98   ? 0.2235 0.2221 0.2410 0.0116  0.0066  -0.0325 96   GLN A CD  
592   O OE1 . GLN A 98   ? 0.2508 0.2466 0.2687 0.0113  0.0063  -0.0312 96   GLN A OE1 
593   N NE2 . GLN A 98   ? 0.2657 0.2647 0.2784 0.0106  0.0077  -0.0297 96   GLN A NE2 
594   N N   . GLU A 99   ? 0.1806 0.2046 0.2071 0.0132  0.0050  -0.0532 97   GLU A N   
595   C CA  . GLU A 99   ? 0.1827 0.2160 0.2072 0.0126  0.0056  -0.0567 97   GLU A CA  
596   C C   . GLU A 99   ? 0.1925 0.2250 0.2158 0.0117  0.0054  -0.0559 97   GLU A C   
597   O O   . GLU A 99   ? 0.1937 0.2315 0.2121 0.0102  0.0064  -0.0546 97   GLU A O   
598   C CB  . GLU A 99   ? 0.1720 0.2116 0.2021 0.0144  0.0045  -0.0641 97   GLU A CB  
599   C CG  . GLU A 99   ? 0.1710 0.2137 0.2011 0.0149  0.0051  -0.0650 97   GLU A CG  
600   C CD  . GLU A 99   ? 0.1982 0.2456 0.2351 0.0172  0.0038  -0.0724 97   GLU A CD  
601   O OE1 . GLU A 99   ? 0.2106 0.2581 0.2529 0.0185  0.0021  -0.0769 97   GLU A OE1 
602   O OE2 . GLU A 99   ? 0.2128 0.2640 0.2501 0.0177  0.0042  -0.0739 97   GLU A OE2 
603   N N   . GLY A 100  ? 0.1933 0.2196 0.2213 0.0127  0.0039  -0.0563 98   GLY A N   
604   C CA  . GLY A 100  ? 0.2025 0.2277 0.2298 0.0119  0.0036  -0.0554 98   GLY A CA  
605   C C   . GLY A 100  ? 0.2072 0.2295 0.2278 0.0100  0.0051  -0.0488 98   GLY A C   
606   O O   . GLY A 100  ? 0.2079 0.2340 0.2250 0.0087  0.0056  -0.0481 98   GLY A O   
607   N N   . VAL A 101  ? 0.1882 0.2042 0.2073 0.0098  0.0056  -0.0441 99   VAL A N   
608   C CA  . VAL A 101  ? 0.2085 0.2216 0.2218 0.0082  0.0068  -0.0383 99   VAL A CA  
609   C C   . VAL A 101  ? 0.1953 0.2153 0.2033 0.0067  0.0081  -0.0376 99   VAL A C   
610   O O   . VAL A 101  ? 0.2044 0.2259 0.2087 0.0052  0.0086  -0.0350 99   VAL A O   
611   C CB  . VAL A 101  ? 0.2023 0.2083 0.2152 0.0085  0.0070  -0.0342 99   VAL A CB  
612   C CG1 . VAL A 101  ? 0.2133 0.2173 0.2205 0.0070  0.0082  -0.0290 99   VAL A CG1 
613   C CG2 . VAL A 101  ? 0.2218 0.2215 0.2398 0.0096  0.0058  -0.0338 99   VAL A CG2 
614   N N   . ALA A 102  ? 0.1787 0.2033 0.1869 0.0070  0.0084  -0.0397 100  ALA A N   
615   C CA  . ALA A 102  ? 0.1900 0.2214 0.1935 0.0054  0.0096  -0.0384 100  ALA A CA  
616   C C   . ALA A 102  ? 0.1635 0.2030 0.1660 0.0045  0.0096  -0.0408 100  ALA A C   
617   O O   . ALA A 102  ? 0.2034 0.2466 0.2016 0.0026  0.0103  -0.0376 100  ALA A O   
618   C CB  . ALA A 102  ? 0.1927 0.2280 0.1971 0.0060  0.0099  -0.0406 100  ALA A CB  
619   N N   . LEU A 103  ? 0.1801 0.2226 0.1867 0.0059  0.0087  -0.0464 101  LEU A N   
620   C CA  . LEU A 103  ? 0.1887 0.2394 0.1946 0.0054  0.0085  -0.0493 101  LEU A CA  
621   C C   . LEU A 103  ? 0.2005 0.2480 0.2037 0.0040  0.0085  -0.0453 101  LEU A C   
622   O O   . LEU A 103  ? 0.2232 0.2771 0.2227 0.0023  0.0090  -0.0438 101  LEU A O   
623   C CB  . LEU A 103  ? 0.1713 0.2244 0.1831 0.0074  0.0071  -0.0563 101  LEU A CB  
624   C CG  . LEU A 103  ? 0.1977 0.2594 0.2091 0.0070  0.0068  -0.0599 101  LEU A CG  
625   C CD1 . LEU A 103  ? 0.2304 0.3037 0.2375 0.0057  0.0080  -0.0604 101  LEU A CD1 
626   C CD2 . LEU A 103  ? 0.2321 0.2950 0.2503 0.0093  0.0051  -0.0672 101  LEU A CD2 
627   N N   . MET A 104  ? 0.2119 0.2501 0.2171 0.0046  0.0079  -0.0433 102  MET A N   
628   C CA  . MET A 104  ? 0.1894 0.2246 0.1924 0.0034  0.0079  -0.0397 102  MET A CA  
629   C C   . MET A 104  ? 0.2209 0.2553 0.2185 0.0015  0.0089  -0.0337 102  MET A C   
630   O O   . MET A 104  ? 0.2343 0.2711 0.2292 0.0001  0.0090  -0.0313 102  MET A O   
631   C CB  . MET A 104  ? 0.1993 0.2253 0.2059 0.0045  0.0070  -0.0387 102  MET A CB  
632   C CG  . MET A 104  ? 0.2210 0.2474 0.2338 0.0062  0.0055  -0.0444 102  MET A CG  
633   S SD  . MET A 104  ? 0.3511 0.3875 0.3643 0.0060  0.0049  -0.0497 102  MET A SD  
634   C CE  . MET A 104  ? 0.3366 0.3693 0.3474 0.0046  0.0048  -0.0452 102  MET A CE  
635   N N   . CYS A 105  ? 0.1897 0.2212 0.1862 0.0015  0.0096  -0.0313 103  CYS A N   
636   C CA  . CYS A 105  ? 0.2007 0.2318 0.1929 -0.0002 0.0103  -0.0260 103  CYS A CA  
637   C C   . CYS A 105  ? 0.2561 0.2972 0.2457 -0.0019 0.0107  -0.0260 103  CYS A C   
638   O O   . CYS A 105  ? 0.2622 0.3046 0.2489 -0.0037 0.0108  -0.0220 103  CYS A O   
639   C CB  . CYS A 105  ? 0.2256 0.2525 0.2177 0.0002  0.0107  -0.0243 103  CYS A CB  
640   S SG  . CYS A 105  ? 0.2432 0.2590 0.2373 0.0017  0.0104  -0.0226 103  CYS A SG  
641   N N   . LEU A 106  ? 0.2111 0.2597 0.2018 -0.0014 0.0108  -0.0303 104  LEU A N   
642   C CA  . LEU A 106  ? 0.2175 0.2770 0.2057 -0.0030 0.0113  -0.0305 104  LEU A CA  
643   C C   . LEU A 106  ? 0.2611 0.3248 0.2485 -0.0038 0.0108  -0.0309 104  LEU A C   
644   O O   . LEU A 106  ? 0.2610 0.3301 0.2453 -0.0059 0.0110  -0.0274 104  LEU A O   
645   C CB  . LEU A 106  ? 0.2176 0.2851 0.2078 -0.0019 0.0115  -0.0360 104  LEU A CB  
646   C CG  . LEU A 106  ? 0.2222 0.3029 0.2102 -0.0034 0.0119  -0.0371 104  LEU A CG  
647   C CD1 . LEU A 106  ? 0.2502 0.3338 0.2344 -0.0060 0.0126  -0.0310 104  LEU A CD1 
648   C CD2 . LEU A 106  ? 0.2906 0.3795 0.2812 -0.0019 0.0120  -0.0438 104  LEU A CD2 
649   N N   . ALA A 107  ? 0.2234 0.2847 0.2139 -0.0022 0.0100  -0.0350 105  ALA A N   
650   C CA  . ALA A 107  ? 0.2436 0.3087 0.2335 -0.0028 0.0095  -0.0357 105  ALA A CA  
651   C C   . ALA A 107  ? 0.2988 0.3587 0.2860 -0.0045 0.0094  -0.0293 105  ALA A C   
652   O O   . ALA A 107  ? 0.2744 0.3402 0.2591 -0.0062 0.0093  -0.0272 105  ALA A O   
653   C CB  . ALA A 107  ? 0.2272 0.2896 0.2217 -0.0008 0.0084  -0.0411 105  ALA A CB  
654   N N   . GLU A 108  ? 0.2717 0.3211 0.2595 -0.0039 0.0095  -0.0263 106  GLU A N   
655   C CA  . GLU A 108  ? 0.2993 0.3435 0.2850 -0.0052 0.0094  -0.0206 106  GLU A CA  
656   C C   . GLU A 108  ? 0.3463 0.3958 0.3287 -0.0075 0.0097  -0.0162 106  GLU A C   
657   O O   . GLU A 108  ? 0.3593 0.4106 0.3400 -0.0091 0.0093  -0.0129 106  GLU A O   
658   C CB  . GLU A 108  ? 0.3149 0.3485 0.3018 -0.0041 0.0095  -0.0185 106  GLU A CB  
659   C CG  . GLU A 108  ? 0.3271 0.3549 0.3123 -0.0051 0.0094  -0.0131 106  GLU A CG  
660   C CD  . GLU A 108  ? 0.3640 0.3836 0.3495 -0.0042 0.0097  -0.0110 106  GLU A CD  
661   O OE1 . GLU A 108  ? 0.3468 0.3632 0.3344 -0.0026 0.0099  -0.0136 106  GLU A OE1 
662   O OE2 . GLU A 108  ? 0.4036 0.4201 0.3874 -0.0051 0.0097  -0.0068 106  GLU A OE2 
663   N N   . ALA A 109  ? 0.2899 0.3422 0.2717 -0.0078 0.0102  -0.0161 107  ALA A N   
664   C CA  . ALA A 109  ? 0.3391 0.3964 0.3184 -0.0101 0.0104  -0.0116 107  ALA A CA  
665   C C   . ALA A 109  ? 0.3634 0.4323 0.3411 -0.0117 0.0102  -0.0120 107  ALA A C   
666   O O   . ALA A 109  ? 0.3933 0.4653 0.3692 -0.0139 0.0098  -0.0071 107  ALA A O   
667   C CB  . ALA A 109  ? 0.3317 0.3895 0.3111 -0.0099 0.0110  -0.0118 107  ALA A CB  
668   N N   . LEU A 110  ? 0.2928 0.3687 0.2714 -0.0106 0.0105  -0.0177 108  LEU A N   
669   C CA  . LEU A 110  ? 0.3159 0.4041 0.2930 -0.0119 0.0104  -0.0188 108  LEU A CA  
670   C C   . LEU A 110  ? 0.3489 0.4364 0.3252 -0.0127 0.0095  -0.0169 108  LEU A C   
671   O O   . LEU A 110  ? 0.3533 0.4494 0.3275 -0.0147 0.0093  -0.0143 108  LEU A O   
672   C CB  . LEU A 110  ? 0.2760 0.3712 0.2548 -0.0101 0.0106  -0.0263 108  LEU A CB  
673   C CG  . LEU A 110  ? 0.3230 0.4225 0.3023 -0.0097 0.0115  -0.0283 108  LEU A CG  
674   C CD1 . LEU A 110  ? 0.2886 0.3925 0.2710 -0.0072 0.0115  -0.0365 108  LEU A CD1 
675   C CD2 . LEU A 110  ? 0.3350 0.4458 0.3113 -0.0123 0.0120  -0.0246 108  LEU A CD2 
676   N N   . LEU A 111  ? 0.3343 0.4121 0.3125 -0.0112 0.0091  -0.0178 109  LEU A N   
677   C CA  . LEU A 111  ? 0.3574 0.4339 0.3352 -0.0119 0.0083  -0.0160 109  LEU A CA  
678   C C   . LEU A 111  ? 0.4456 0.5184 0.4217 -0.0138 0.0079  -0.0088 109  LEU A C   
679   O O   . LEU A 111  ? 0.4631 0.5367 0.4386 -0.0148 0.0071  -0.0065 109  LEU A O   
680   C CB  . LEU A 111  ? 0.3584 0.4262 0.3391 -0.0097 0.0079  -0.0193 109  LEU A CB  
681   C CG  . LEU A 111  ? 0.3494 0.4219 0.3327 -0.0079 0.0077  -0.0267 109  LEU A CG  
682   C CD1 . LEU A 111  ? 0.3724 0.4357 0.3595 -0.0059 0.0071  -0.0294 109  LEU A CD1 
683   C CD2 . LEU A 111  ? 0.3670 0.4508 0.3491 -0.0088 0.0072  -0.0289 109  LEU A CD2 
684   N N   . ARG A 112  ? 0.4119 0.4806 0.3877 -0.0144 0.0082  -0.0053 110  ARG A N   
685   C CA  . ARG A 112  ? 0.4606 0.5270 0.4355 -0.0164 0.0076  0.0014  110  ARG A CA  
686   C C   . ARG A 112  ? 0.4733 0.5509 0.4463 -0.0190 0.0072  0.0048  110  ARG A C   
687   O O   . ARG A 112  ? 0.5272 0.6042 0.5001 -0.0210 0.0062  0.0106  110  ARG A O   
688   C CB  . ARG A 112  ? 0.4531 0.5115 0.4287 -0.0160 0.0078  0.0037  110  ARG A CB  
689   C CG  . ARG A 112  ? 0.4578 0.5051 0.4351 -0.0137 0.0080  0.0019  110  ARG A CG  
690   C CD  . ARG A 112  ? 0.5083 0.5500 0.4861 -0.0127 0.0085  0.0019  110  ARG A CD  
691   N NE  . ARG A 112  ? 0.6148 0.6542 0.5924 -0.0142 0.0079  0.0071  110  ARG A NE  
692   C CZ  . ARG A 112  ? 0.7192 0.7502 0.6977 -0.0138 0.0074  0.0097  110  ARG A CZ  
693   N NH1 . ARG A 112  ? 0.7074 0.7318 0.6867 -0.0120 0.0075  0.0080  110  ARG A NH1 
694   N NH2 . ARG A 112  ? 0.7499 0.7794 0.7288 -0.0151 0.0066  0.0139  110  ARG A NH2 
695   N N   . ILE A 113  ? 0.4858 0.5739 0.4579 -0.0192 0.0078  0.0014  111  ILE A N   
696   C CA  . ILE A 113  ? 0.4914 0.5922 0.4616 -0.0217 0.0075  0.0041  111  ILE A CA  
697   C C   . ILE A 113  ? 0.5174 0.6220 0.4870 -0.0220 0.0067  0.0034  111  ILE A C   
698   O O   . ILE A 113  ? 0.5215 0.6281 0.4915 -0.0202 0.0070  -0.0028 111  ILE A O   
699   C CB  . ILE A 113  ? 0.4301 0.5417 0.3995 -0.0215 0.0085  -0.0001 111  ILE A CB  
700   C CG1 . ILE A 113  ? 0.4162 0.5246 0.3863 -0.0214 0.0092  0.0011  111  ILE A CG1 
701   C CG2 . ILE A 113  ? 0.5023 0.6286 0.4696 -0.0240 0.0083  0.0024  111  ILE A CG2 
702   C CD1 . ILE A 113  ? 0.4265 0.5447 0.3963 -0.0209 0.0103  -0.0034 111  ILE A CD1 
703   N N   . PRO A 114  ? 0.5672 0.6728 0.5361 -0.0242 0.0056  0.0094  112  PRO A N   
704   C CA  . PRO A 114  ? 0.5673 0.6749 0.5359 -0.0244 0.0047  0.0090  112  PRO A CA  
705   C C   . PRO A 114  ? 0.5546 0.6761 0.5214 -0.0247 0.0049  0.0052  112  PRO A C   
706   O O   . PRO A 114  ? 0.6337 0.7555 0.6010 -0.0232 0.0048  0.0001  112  PRO A O   
707   C CB  . PRO A 114  ? 0.5938 0.7001 0.5626 -0.0269 0.0033  0.0171  112  PRO A CB  
708   C CG  . PRO A 114  ? 0.6307 0.7293 0.6008 -0.0271 0.0034  0.0206  112  PRO A CG  
709   C CD  . PRO A 114  ? 0.5804 0.6837 0.5498 -0.0265 0.0048  0.0169  112  PRO A CD  
710   N N   . ASP A 115  ? 0.6026 0.7362 0.5676 -0.0268 0.0051  0.0074  113  ASP A N   
711   C CA  . ASP A 115  ? 0.6125 0.7610 0.5756 -0.0274 0.0052  0.0042  113  ASP A CA  
712   C C   . ASP A 115  ? 0.5756 0.7277 0.5393 -0.0248 0.0064  -0.0046 113  ASP A C   
713   O O   . ASP A 115  ? 0.5669 0.7181 0.5312 -0.0241 0.0074  -0.0060 113  ASP A O   
714   C CB  . ASP A 115  ? 0.5901 0.7514 0.5513 -0.0306 0.0050  0.0101  113  ASP A CB  
715   C CG  . ASP A 115  ? 0.6490 0.8274 0.6079 -0.0311 0.0053  0.0064  113  ASP A CG  
716   O OD1 . ASP A 115  ? 0.6546 0.8365 0.6128 -0.0312 0.0045  0.0053  113  ASP A OD1 
717   O OD2 . ASP A 115  ? 0.6013 0.7899 0.5592 -0.0314 0.0064  0.0044  113  ASP A OD2 
718   N N   . THR A 116  ? 0.5599 0.7166 0.5238 -0.0234 0.0061  -0.0107 114  THR A N   
719   C CA  . THR A 116  ? 0.5503 0.7098 0.5157 -0.0206 0.0068  -0.0197 114  THR A CA  
720   C C   . THR A 116  ? 0.5760 0.7500 0.5398 -0.0213 0.0078  -0.0217 114  THR A C   
721   O O   . THR A 116  ? 0.5297 0.7031 0.4950 -0.0195 0.0087  -0.0264 114  THR A O   
722   C CB  . THR A 116  ? 0.5394 0.7010 0.5058 -0.0191 0.0060  -0.0256 114  THR A CB  
723   O OG1 . THR A 116  ? 0.6124 0.7604 0.5806 -0.0185 0.0052  -0.0236 114  THR A OG1 
724   C CG2 . THR A 116  ? 0.5706 0.7346 0.5397 -0.0162 0.0063  -0.0352 114  THR A CG2 
725   N N   . ALA A 117  ? 0.5158 0.7035 0.4767 -0.0239 0.0076  -0.0179 115  ALA A N   
726   C CA  . ALA A 117  ? 0.5493 0.7523 0.5085 -0.0247 0.0086  -0.0195 115  ALA A CA  
727   C C   . ALA A 117  ? 0.5165 0.7155 0.4761 -0.0255 0.0095  -0.0155 115  ALA A C   
728   O O   . ALA A 117  ? 0.4855 0.6907 0.4456 -0.0245 0.0106  -0.0199 115  ALA A O   
729   C CB  . ALA A 117  ? 0.5361 0.7547 0.4921 -0.0277 0.0081  -0.0150 115  ALA A CB  
730   N N   . THR A 118  ? 0.5062 0.6950 0.4661 -0.0272 0.0090  -0.0075 116  THR A N   
731   C CA  . THR A 118  ? 0.4987 0.6827 0.4593 -0.0279 0.0096  -0.0038 116  THR A CA  
732   C C   . THR A 118  ? 0.4454 0.6189 0.4085 -0.0247 0.0104  -0.0099 116  THR A C   
733   O O   . THR A 118  ? 0.4399 0.6158 0.4035 -0.0243 0.0114  -0.0115 116  THR A O   
734   C CB  . THR A 118  ? 0.5134 0.6878 0.4744 -0.0301 0.0085  0.0053  116  THR A CB  
735   O OG1 . THR A 118  ? 0.6459 0.8302 0.6051 -0.0332 0.0075  0.0114  116  THR A OG1 
736   C CG2 . THR A 118  ? 0.4520 0.6224 0.4141 -0.0310 0.0090  0.0092  116  THR A CG2 
737   N N   . ARG A 119  ? 0.4399 0.6018 0.4047 -0.0224 0.0099  -0.0133 117  ARG A N   
738   C CA  . ARG A 119  ? 0.4443 0.5962 0.4119 -0.0194 0.0104  -0.0189 117  ARG A CA  
739   C C   . ARG A 119  ? 0.4508 0.6125 0.4194 -0.0175 0.0111  -0.0272 117  ARG A C   
740   O O   . ARG A 119  ? 0.4270 0.5868 0.3971 -0.0162 0.0119  -0.0299 117  ARG A O   
741   C CB  . ARG A 119  ? 0.4088 0.5483 0.3782 -0.0177 0.0096  -0.0206 117  ARG A CB  
742   C CG  . ARG A 119  ? 0.3971 0.5252 0.3697 -0.0148 0.0099  -0.0250 117  ARG A CG  
743   C CD  . ARG A 119  ? 0.4227 0.5419 0.3975 -0.0131 0.0090  -0.0278 117  ARG A CD  
744   N NE  . ARG A 119  ? 0.4446 0.5578 0.4182 -0.0146 0.0083  -0.0216 117  ARG A NE  
745   C CZ  . ARG A 119  ? 0.4337 0.5481 0.4071 -0.0148 0.0074  -0.0219 117  ARG A CZ  
746   N NH1 . ARG A 119  ? 0.4442 0.5655 0.4187 -0.0136 0.0071  -0.0283 117  ARG A NH1 
747   N NH2 . ARG A 119  ? 0.5516 0.6603 0.5242 -0.0162 0.0068  -0.0160 117  ARG A NH2 
748   N N   . ASP A 120  ? 0.4585 0.6310 0.4263 -0.0173 0.0108  -0.0315 118  ASP A N   
749   C CA  . ASP A 120  ? 0.4708 0.6532 0.4401 -0.0151 0.0112  -0.0403 118  ASP A CA  
750   C C   . ASP A 120  ? 0.4572 0.6517 0.4249 -0.0164 0.0124  -0.0394 118  ASP A C   
751   O O   . ASP A 120  ? 0.4118 0.6094 0.3816 -0.0143 0.0131  -0.0456 118  ASP A O   
752   C CB  . ASP A 120  ? 0.4399 0.6320 0.4087 -0.0147 0.0105  -0.0451 118  ASP A CB  
753   C CG  . ASP A 120  ? 0.5373 0.7177 0.5085 -0.0132 0.0092  -0.0470 118  ASP A CG  
754   O OD1 . ASP A 120  ? 0.5340 0.6992 0.5070 -0.0125 0.0091  -0.0446 118  ASP A OD1 
755   O OD2 . ASP A 120  ? 0.5412 0.7281 0.5125 -0.0127 0.0083  -0.0510 118  ASP A OD2 
756   N N   . ALA A 121  ? 0.4383 0.6399 0.4028 -0.0197 0.0126  -0.0316 119  ALA A N   
757   C CA  . ALA A 121  ? 0.4591 0.6720 0.4223 -0.0213 0.0137  -0.0296 119  ALA A CA  
758   C C   . ALA A 121  ? 0.4505 0.6527 0.4155 -0.0206 0.0143  -0.0280 119  ALA A C   
759   O O   . ALA A 121  ? 0.4696 0.6779 0.4355 -0.0197 0.0153  -0.0316 119  ALA A O   
760   C CB  . ALA A 121  ? 0.4812 0.7033 0.4412 -0.0253 0.0135  -0.0207 119  ALA A CB  
761   N N   . LEU A 122  ? 0.4713 0.6581 0.4370 -0.0210 0.0137  -0.0228 120  LEU A N   
762   C CA  . LEU A 122  ? 0.4543 0.6306 0.4219 -0.0203 0.0141  -0.0215 120  LEU A CA  
763   C C   . LEU A 122  ? 0.4402 0.6125 0.4108 -0.0167 0.0146  -0.0302 120  LEU A C   
764   O O   . LEU A 122  ? 0.4431 0.6162 0.4149 -0.0159 0.0153  -0.0318 120  LEU A O   
765   C CB  . LEU A 122  ? 0.4494 0.6100 0.4174 -0.0209 0.0133  -0.0155 120  LEU A CB  
766   C CG  . LEU A 122  ? 0.4290 0.5805 0.3983 -0.0208 0.0136  -0.0127 120  LEU A CG  
767   C CD1 . LEU A 122  ? 0.5264 0.6875 0.4944 -0.0237 0.0139  -0.0073 120  LEU A CD1 
768   C CD2 . LEU A 122  ? 0.4119 0.5477 0.3819 -0.0208 0.0127  -0.0083 120  LEU A CD2 
769   N N   . ILE A 123  ? 0.4390 0.6071 0.4113 -0.0144 0.0139  -0.0358 121  ILE A N   
770   C CA  . ILE A 123  ? 0.4278 0.5926 0.4038 -0.0110 0.0139  -0.0441 121  ILE A CA  
771   C C   . ILE A 123  ? 0.4443 0.6242 0.4207 -0.0103 0.0147  -0.0499 121  ILE A C   
772   O O   . ILE A 123  ? 0.4318 0.6108 0.4104 -0.0088 0.0153  -0.0529 121  ILE A O   
773   C CB  . ILE A 123  ? 0.3904 0.5497 0.3686 -0.0091 0.0128  -0.0488 121  ILE A CB  
774   C CG1 . ILE A 123  ? 0.3885 0.5317 0.3669 -0.0093 0.0121  -0.0438 121  ILE A CG1 
775   C CG2 . ILE A 123  ? 0.3738 0.5333 0.3565 -0.0057 0.0124  -0.0582 121  ILE A CG2 
776   C CD1 . ILE A 123  ? 0.3732 0.5121 0.3533 -0.0081 0.0109  -0.0467 121  ILE A CD1 
777   N N   . ARG A 124  ? 0.4120 0.6064 0.3863 -0.0113 0.0148  -0.0515 122  ARG A N   
778   C CA  . ARG A 124  ? 0.4845 0.6947 0.4595 -0.0102 0.0154  -0.0583 122  ARG A CA  
779   C C   . ARG A 124  ? 0.5280 0.7453 0.5016 -0.0118 0.0168  -0.0548 122  ARG A C   
780   O O   . ARG A 124  ? 0.5300 0.7520 0.5060 -0.0099 0.0174  -0.0606 122  ARG A O   
781   C CB  . ARG A 124  ? 0.4531 0.6781 0.4255 -0.0113 0.0152  -0.0600 122  ARG A CB  
782   N N   . ASP A 125  ? 0.5107 0.7288 0.4810 -0.0153 0.0171  -0.0454 123  ASP A N   
783   C CA  . ASP A 125  ? 0.5642 0.7921 0.5331 -0.0174 0.0182  -0.0415 123  ASP A CA  
784   C C   . ASP A 125  ? 0.5683 0.7841 0.5387 -0.0176 0.0184  -0.0374 123  ASP A C   
785   O O   . ASP A 125  ? 0.5883 0.8110 0.5588 -0.0182 0.0194  -0.0367 123  ASP A O   
786   C CB  . ASP A 125  ? 0.6340 0.8725 0.5991 -0.0214 0.0182  -0.0335 123  ASP A CB  
787   C CG  . ASP A 125  ? 0.6454 0.8971 0.6087 -0.0214 0.0179  -0.0370 123  ASP A CG  
788   O OD1 . ASP A 125  ? 0.6699 0.9301 0.6345 -0.0188 0.0182  -0.0462 123  ASP A OD1 
789   O OD2 . ASP A 125  ? 0.6464 0.9000 0.6071 -0.0240 0.0172  -0.0308 123  ASP A OD2 
790   N N   . LYS A 126  ? 0.5130 0.7114 0.4844 -0.0169 0.0176  -0.0347 124  LYS A N   
791   C CA  . LYS A 126  ? 0.4886 0.6759 0.4609 -0.0175 0.0176  -0.0299 124  LYS A CA  
792   C C   . LYS A 126  ? 0.5267 0.6990 0.5022 -0.0143 0.0173  -0.0343 124  LYS A C   
793   O O   . LYS A 126  ? 0.5691 0.7385 0.5464 -0.0133 0.0177  -0.0356 124  LYS A O   
794   C CB  . LYS A 126  ? 0.5729 0.7543 0.5433 -0.0206 0.0169  -0.0203 124  LYS A CB  
795   N N   . ILE A 127  ? 0.4712 0.6342 0.4475 -0.0129 0.0164  -0.0361 125  ILE A N   
796   C CA  . ILE A 127  ? 0.4633 0.6123 0.4428 -0.0101 0.0159  -0.0393 125  ILE A CA  
797   C C   . ILE A 127  ? 0.5055 0.6589 0.4885 -0.0072 0.0161  -0.0481 125  ILE A C   
798   O O   . ILE A 127  ? 0.5485 0.6964 0.5339 -0.0057 0.0163  -0.0496 125  ILE A O   
799   C CB  . ILE A 127  ? 0.4501 0.5891 0.4300 -0.0094 0.0149  -0.0390 125  ILE A CB  
800   C CG1 . ILE A 127  ? 0.5106 0.6465 0.4874 -0.0123 0.0145  -0.0307 125  ILE A CG1 
801   C CG2 . ILE A 127  ? 0.4475 0.5719 0.4306 -0.0070 0.0144  -0.0409 125  ILE A CG2 
802   C CD1 . ILE A 127  ? 0.4631 0.5913 0.4394 -0.0136 0.0146  -0.0244 125  ILE A CD1 
803   N N   . ALA A 128  ? 0.4856 0.6492 0.4692 -0.0062 0.0160  -0.0541 126  ALA A N   
804   C CA  . ALA A 128  ? 0.4186 0.5859 0.4064 -0.0031 0.0158  -0.0632 126  ALA A CA  
805   C C   . ALA A 128  ? 0.5560 0.7325 0.5442 -0.0031 0.0169  -0.0647 126  ALA A C   
806   O O   . ALA A 128  ? 0.4904 0.6641 0.4827 -0.0006 0.0167  -0.0698 126  ALA A O   
807   C CB  . ALA A 128  ? 0.4309 0.6084 0.4193 -0.0021 0.0152  -0.0696 126  ALA A CB  
808   N N   . ASP A 129  ? 0.7416 0.9291 0.7260 -0.0059 0.0179  -0.0599 127  ASP A N   
809   C CA  . ASP A 129  ? 0.7221 0.9211 0.7067 -0.0062 0.0191  -0.0612 127  ASP A CA  
810   C C   . ASP A 129  ? 0.7286 0.9187 0.7141 -0.0065 0.0194  -0.0572 127  ASP A C   
811   O O   . ASP A 129  ? 0.7977 0.9962 0.7837 -0.0067 0.0203  -0.0582 127  ASP A O   
812   C CB  . ASP A 129  ? 0.7054 0.9203 0.6857 -0.0094 0.0200  -0.0569 127  ASP A CB  
813   N N   . GLY A 130  ? 0.6811 0.8550 0.6669 -0.0065 0.0187  -0.0530 128  GLY A N   
814   C CA  . GLY A 130  ? 0.7224 0.8878 0.7093 -0.0064 0.0189  -0.0502 128  GLY A CA  
815   C C   . GLY A 130  ? 0.7035 0.8538 0.6892 -0.0075 0.0182  -0.0434 128  GLY A C   
816   O O   . GLY A 130  ? 0.6545 0.7933 0.6418 -0.0058 0.0173  -0.0447 128  GLY A O   
817   N N   . ASN A 131  ? 0.7510 0.9016 0.7345 -0.0103 0.0185  -0.0362 129  ASN A N   
818   C CA  . ASN A 131  ? 0.7195 0.8564 0.7025 -0.0111 0.0179  -0.0302 129  ASN A CA  
819   C C   . ASN A 131  ? 0.6183 0.7490 0.5995 -0.0120 0.0171  -0.0268 129  ASN A C   
820   O O   . ASN A 131  ? 0.6707 0.8062 0.6495 -0.0147 0.0170  -0.0215 129  ASN A O   
821   C CB  . ASN A 131  ? 0.7104 0.8506 0.6923 -0.0138 0.0182  -0.0239 129  ASN A CB  
822   N N   . TRP A 132  ? 0.5997 0.7200 0.5825 -0.0097 0.0165  -0.0297 130  TRP A N   
823   C CA  . TRP A 132  ? 0.5133 0.6260 0.4946 -0.0104 0.0157  -0.0263 130  TRP A CA  
824   C C   . TRP A 132  ? 0.4983 0.6023 0.4786 -0.0121 0.0153  -0.0192 130  TRP A C   
825   O O   . TRP A 132  ? 0.5409 0.6417 0.5196 -0.0136 0.0146  -0.0147 130  TRP A O   
826   C CB  . TRP A 132  ? 0.4667 0.5702 0.4504 -0.0076 0.0151  -0.0309 130  TRP A CB  
827   C CG  . TRP A 132  ? 0.4282 0.5221 0.4144 -0.0056 0.0150  -0.0322 130  TRP A CG  
828   C CD1 . TRP A 132  ? 0.3722 0.4678 0.3615 -0.0035 0.0151  -0.0377 130  TRP A CD1 
829   C CD2 . TRP A 132  ? 0.3441 0.4257 0.3302 -0.0056 0.0146  -0.0280 130  TRP A CD2 
830   N NE1 . TRP A 132  ? 0.3711 0.4561 0.3621 -0.0022 0.0148  -0.0368 130  TRP A NE1 
831   C CE2 . TRP A 132  ? 0.2850 0.3617 0.2738 -0.0035 0.0145  -0.0309 130  TRP A CE2 
832   C CE3 . TRP A 132  ? 0.3648 0.4396 0.3489 -0.0071 0.0142  -0.0222 130  TRP A CE3 
833   C CZ2 . TRP A 132  ? 0.2963 0.3619 0.2855 -0.0029 0.0142  -0.0282 130  TRP A CZ2 
834   C CZ3 . TRP A 132  ? 0.3567 0.4206 0.3413 -0.0064 0.0138  -0.0199 130  TRP A CZ3 
835   C CH2 . TRP A 132  ? 0.3359 0.3955 0.3228 -0.0043 0.0139  -0.0228 130  TRP A CH2 
836   N N   . LYS A 133  ? 0.5288 0.6287 0.5101 -0.0118 0.0154  -0.0183 131  LYS A N   
837   C CA  . LYS A 133  ? 0.5658 0.6575 0.5466 -0.0132 0.0148  -0.0122 131  LYS A CA  
838   C C   . LYS A 133  ? 0.6625 0.7608 0.6416 -0.0165 0.0145  -0.0060 131  LYS A C   
839   O O   . LYS A 133  ? 0.7239 0.8159 0.7026 -0.0179 0.0136  -0.0009 131  LYS A O   
840   C CB  . LYS A 133  ? 0.4648 0.5526 0.4471 -0.0122 0.0150  -0.0129 131  LYS A CB  
841   N N   . SER A 134  ? 0.6887 0.8003 0.6672 -0.0179 0.0152  -0.0064 132  SER A N   
842   C CA  . SER A 134  ? 0.7362 0.8556 0.7135 -0.0214 0.0148  -0.0001 132  SER A CA  
843   C C   . SER A 134  ? 0.7847 0.9024 0.7608 -0.0227 0.0139  0.0033  132  SER A C   
844   O O   . SER A 134  ? 0.8161 0.9354 0.7919 -0.0255 0.0130  0.0099  132  SER A O   
845   C CB  . SER A 134  ? 0.7448 0.8803 0.7216 -0.0224 0.0158  -0.0019 132  SER A CB  
846   N N   . HIS A 135  ? 0.7848 0.8992 0.7603 -0.0207 0.0140  -0.0009 133  HIS A N   
847   C CA  . HIS A 135  ? 0.8062 0.9186 0.7807 -0.0217 0.0131  0.0019  133  HIS A CA  
848   C C   . HIS A 135  ? 0.7790 0.8779 0.7543 -0.0193 0.0127  -0.0002 133  HIS A C   
849   O O   . HIS A 135  ? 0.8181 0.9117 0.7930 -0.0198 0.0119  0.0028  133  HIS A O   
850   C CB  . HIS A 135  ? 0.7515 0.8762 0.7245 -0.0220 0.0136  -0.0009 133  HIS A CB  
851   C CG  . HIS A 135  ? 0.7917 0.9306 0.7642 -0.0228 0.0145  -0.0027 133  HIS A CG  
852   N ND1 . HIS A 135  ? 0.8028 0.9441 0.7765 -0.0205 0.0155  -0.0092 133  HIS A ND1 
853   C CD2 . HIS A 135  ? 0.8059 0.9579 0.7772 -0.0257 0.0146  0.0013  133  HIS A CD2 
854   C CE1 . HIS A 135  ? 0.7870 0.9424 0.7602 -0.0218 0.0163  -0.0095 133  HIS A CE1 
855   N NE2 . HIS A 135  ? 0.7610 0.9234 0.7325 -0.0250 0.0159  -0.0031 133  HIS A NE2 
856   N N   . SER A 139  ? 0.5744 0.6156 0.5566 -0.0201 0.0065  0.0207  137  SER A N   
857   C CA  . SER A 139  ? 0.6350 0.6669 0.6188 -0.0196 0.0052  0.0228  137  SER A CA  
858   C C   . SER A 139  ? 0.6597 0.6844 0.6425 -0.0168 0.0059  0.0190  137  SER A C   
859   O O   . SER A 139  ? 0.6287 0.6458 0.6125 -0.0159 0.0051  0.0198  137  SER A O   
860   C CB  . SER A 139  ? 0.6179 0.6514 0.6029 -0.0219 0.0035  0.0277  137  SER A CB  
861   N N   . ARG A 140  ? 0.4710 0.4986 0.4523 -0.0155 0.0073  0.0149  138  ARG A N   
862   C CA  . ARG A 140  ? 0.4452 0.4669 0.4260 -0.0130 0.0080  0.0116  138  ARG A CA  
863   C C   . ARG A 140  ? 0.4193 0.4442 0.3996 -0.0116 0.0093  0.0069  138  ARG A C   
864   O O   . ARG A 140  ? 0.3945 0.4273 0.3741 -0.0124 0.0098  0.0055  138  ARG A O   
865   C CB  . ARG A 140  ? 0.4599 0.4817 0.4403 -0.0133 0.0077  0.0124  138  ARG A CB  
866   C CG  . ARG A 140  ? 0.4793 0.4977 0.4594 -0.0112 0.0085  0.0087  138  ARG A CG  
867   C CD  . ARG A 140  ? 0.5583 0.5796 0.5379 -0.0119 0.0082  0.0093  138  ARG A CD  
868   N NE  . ARG A 140  ? 0.5917 0.6098 0.5716 -0.0101 0.0088  0.0060  138  ARG A NE  
869   C CZ  . ARG A 140  ? 0.6337 0.6556 0.6137 -0.0092 0.0094  0.0020  138  ARG A CZ  
870   N NH1 . ARG A 140  ? 0.5697 0.5987 0.5494 -0.0097 0.0099  0.0002  138  ARG A NH1 
871   N NH2 . ARG A 140  ? 0.5510 0.5696 0.5319 -0.0078 0.0096  -0.0003 138  ARG A NH2 
872   N N   . SER A 141  ? 0.3770 0.3962 0.3579 -0.0095 0.0097  0.0045  139  SER A N   
873   C CA  . SER A 141  ? 0.3332 0.3543 0.3144 -0.0079 0.0107  0.0000  139  SER A CA  
874   C C   . SER A 141  ? 0.3174 0.3414 0.2986 -0.0075 0.0110  -0.0025 139  SER A C   
875   O O   . SER A 141  ? 0.3151 0.3358 0.2962 -0.0074 0.0106  -0.0015 139  SER A O   
876   C CB  . SER A 141  ? 0.3416 0.3551 0.3237 -0.0058 0.0108  -0.0015 139  SER A CB  
877   O OG  . SER A 141  ? 0.3070 0.3217 0.2902 -0.0041 0.0114  -0.0056 139  SER A OG  
878   N N   . LEU A 142  ? 0.2984 0.3290 0.2801 -0.0071 0.0115  -0.0061 140  LEU A N   
879   C CA  . LEU A 142  ? 0.2736 0.3068 0.2559 -0.0063 0.0116  -0.0094 140  LEU A CA  
880   C C   . LEU A 142  ? 0.2468 0.2720 0.2308 -0.0042 0.0115  -0.0112 140  LEU A C   
881   O O   . LEU A 142  ? 0.2560 0.2811 0.2409 -0.0037 0.0113  -0.0129 140  LEU A O   
882   C CB  . LEU A 142  ? 0.2700 0.3112 0.2533 -0.0058 0.0121  -0.0138 140  LEU A CB  
883   C CG  . LEU A 142  ? 0.3742 0.4246 0.3570 -0.0066 0.0122  -0.0160 140  LEU A CG  
884   C CD1 . LEU A 142  ? 0.3781 0.4353 0.3585 -0.0093 0.0122  -0.0117 140  LEU A CD1 
885   C CD2 . LEU A 142  ? 0.3567 0.4133 0.3414 -0.0053 0.0126  -0.0215 140  LEU A CD2 
886   N N   . PHE A 143  ? 0.2337 0.2525 0.2184 -0.0031 0.0115  -0.0106 141  PHE A N   
887   C CA  . PHE A 143  ? 0.2200 0.2326 0.2067 -0.0011 0.0114  -0.0124 141  PHE A CA  
888   C C   . PHE A 143  ? 0.2532 0.2584 0.2393 -0.0009 0.0112  -0.0093 141  PHE A C   
889   O O   . PHE A 143  ? 0.2556 0.2556 0.2431 0.0006  0.0112  -0.0098 141  PHE A O   
890   C CB  . PHE A 143  ? 0.2187 0.2305 0.2070 0.0001  0.0116  -0.0145 141  PHE A CB  
891   C CG  . PHE A 143  ? 0.2221 0.2417 0.2112 0.0000  0.0118  -0.0179 141  PHE A CG  
892   C CD1 . PHE A 143  ? 0.2165 0.2402 0.2075 0.0006  0.0116  -0.0218 141  PHE A CD1 
893   C CD2 . PHE A 143  ? 0.2177 0.2411 0.2060 -0.0007 0.0121  -0.0174 141  PHE A CD2 
894   C CE1 . PHE A 143  ? 0.2242 0.2559 0.2161 0.0007  0.0118  -0.0254 141  PHE A CE1 
895   C CE2 . PHE A 143  ? 0.2448 0.2764 0.2340 -0.0008 0.0124  -0.0207 141  PHE A CE2 
896   C CZ  . PHE A 143  ? 0.2112 0.2472 0.2021 0.0000  0.0123  -0.0249 141  PHE A CZ  
897   N N   . VAL A 144  ? 0.2474 0.2526 0.2316 -0.0023 0.0110  -0.0060 142  VAL A N   
898   C CA  A VAL A 144  ? 0.2822 0.2810 0.2660 -0.0020 0.0108  -0.0033 142  VAL A CA  
899   C CA  B VAL A 144  ? 0.2822 0.2811 0.2660 -0.0020 0.0107  -0.0033 142  VAL A CA  
900   C C   . VAL A 144  ? 0.2900 0.2851 0.2753 -0.0006 0.0108  -0.0045 142  VAL A C   
901   O O   . VAL A 144  ? 0.2872 0.2769 0.2728 0.0004  0.0108  -0.0034 142  VAL A O   
902   C CB  A VAL A 144  ? 0.2939 0.2937 0.2763 -0.0037 0.0102  0.0001  142  VAL A CB  
903   C CB  B VAL A 144  ? 0.2930 0.2932 0.2755 -0.0038 0.0102  0.0000  142  VAL A CB  
904   C CG1 A VAL A 144  ? 0.3125 0.3149 0.2941 -0.0050 0.0100  0.0019  142  VAL A CG1 
905   C CG1 B VAL A 144  ? 0.2720 0.2661 0.2544 -0.0032 0.0099  0.0021  142  VAL A CG1 
906   C CG2 A VAL A 144  ? 0.3035 0.3079 0.2857 -0.0047 0.0101  -0.0003 142  VAL A CG2 
907   C CG2 B VAL A 144  ? 0.3126 0.3152 0.2943 -0.0051 0.0099  0.0020  142  VAL A CG2 
908   N N   . ASN A 145  ? 0.2555 0.2538 0.2419 -0.0007 0.0107  -0.0067 143  ASN A N   
909   C CA  . ASN A 145  ? 0.2882 0.2833 0.2766 0.0004  0.0106  -0.0078 143  ASN A CA  
910   C C   . ASN A 145  ? 0.2804 0.2755 0.2719 0.0018  0.0104  -0.0112 143  ASN A C   
911   O O   . ASN A 145  ? 0.2575 0.2516 0.2516 0.0025  0.0100  -0.0128 143  ASN A O   
912   C CB  . ASN A 145  ? 0.3228 0.3207 0.3110 -0.0005 0.0102  -0.0078 143  ASN A CB  
913   C CG  . ASN A 145  ? 0.3173 0.3137 0.3034 -0.0016 0.0101  -0.0040 143  ASN A CG  
914   O OD1 . ASN A 145  ? 0.3903 0.3816 0.3763 -0.0010 0.0102  -0.0019 143  ASN A OD1 
915   N ND2 . ASN A 145  ? 0.3589 0.3604 0.3437 -0.0032 0.0098  -0.0031 143  ASN A ND2 
916   N N   . ALA A 146  ? 0.2250 0.2210 0.2168 0.0023  0.0106  -0.0125 144  ALA A N   
917   C CA  . ALA A 146  ? 0.2368 0.2331 0.2322 0.0037  0.0102  -0.0159 144  ALA A CA  
918   C C   . ALA A 146  ? 0.2357 0.2260 0.2339 0.0049  0.0098  -0.0151 144  ALA A C   
919   O O   . ALA A 146  ? 0.2846 0.2746 0.2868 0.0059  0.0090  -0.0177 144  ALA A O   
920   C CB  . ALA A 146  ? 0.2215 0.2200 0.2168 0.0039  0.0104  -0.0171 144  ALA A CB  
921   N N   . ALA A 147  ? 0.2754 0.2612 0.2718 0.0050  0.0101  -0.0115 145  ALA A N   
922   C CA  . ALA A 147  ? 0.3167 0.2979 0.3156 0.0060  0.0098  -0.0103 145  ALA A CA  
923   C C   . ALA A 147  ? 0.3054 0.2865 0.3069 0.0059  0.0092  -0.0112 145  ALA A C   
924   O O   . ALA A 147  ? 0.3071 0.2864 0.3129 0.0068  0.0084  -0.0121 145  ALA A O   
925   C CB  . ALA A 147  ? 0.3493 0.3270 0.3456 0.0060  0.0103  -0.0067 145  ALA A CB  
926   N N   . THR A 148  ? 0.2719 0.2551 0.2714 0.0049  0.0094  -0.0109 146  THR A N   
927   C CA  . THR A 148  ? 0.2688 0.2523 0.2705 0.0048  0.0089  -0.0119 146  THR A CA  
928   C C   . THR A 148  ? 0.2637 0.2505 0.2691 0.0052  0.0080  -0.0163 146  THR A C   
929   O O   . THR A 148  ? 0.2615 0.2467 0.2714 0.0059  0.0070  -0.0177 146  THR A O   
930   C CB  . THR A 148  ? 0.3224 0.3080 0.3209 0.0035  0.0092  -0.0105 146  THR A CB  
931   O OG1 . THR A 148  ? 0.3549 0.3371 0.3508 0.0033  0.0098  -0.0068 146  THR A OG1 
932   C CG2 . THR A 148  ? 0.3975 0.3838 0.3982 0.0033  0.0086  -0.0115 146  THR A CG2 
933   N N   . TRP A 149  ? 0.2382 0.2301 0.2421 0.0048  0.0082  -0.0187 147  TRP A N   
934   C CA  . TRP A 149  ? 0.2583 0.2541 0.2659 0.0055  0.0074  -0.0237 147  TRP A CA  
935   C C   . TRP A 149  ? 0.2400 0.2327 0.2524 0.0070  0.0065  -0.0251 147  TRP A C   
936   O O   . TRP A 149  ? 0.2439 0.2374 0.2613 0.0079  0.0053  -0.0288 147  TRP A O   
937   C CB  . TRP A 149  ? 0.2722 0.2750 0.2771 0.0048  0.0079  -0.0258 147  TRP A CB  
938   C CG  . TRP A 149  ? 0.2499 0.2568 0.2513 0.0033  0.0083  -0.0247 147  TRP A CG  
939   C CD1 . TRP A 149  ? 0.3093 0.3181 0.3061 0.0019  0.0091  -0.0215 147  TRP A CD1 
940   C CD2 . TRP A 149  ? 0.2798 0.2893 0.2824 0.0031  0.0076  -0.0266 147  TRP A CD2 
941   N NE1 . TRP A 149  ? 0.2919 0.3045 0.2870 0.0007  0.0090  -0.0211 147  TRP A NE1 
942   C CE2 . TRP A 149  ? 0.2878 0.3011 0.2861 0.0014  0.0082  -0.0242 147  TRP A CE2 
943   C CE3 . TRP A 149  ? 0.2864 0.2955 0.2936 0.0040  0.0064  -0.0301 147  TRP A CE3 
944   C CZ2 . TRP A 149  ? 0.3026 0.3196 0.3008 0.0007  0.0077  -0.0251 147  TRP A CZ2 
945   C CZ3 . TRP A 149  ? 0.3255 0.3381 0.3326 0.0034  0.0060  -0.0313 147  TRP A CZ3 
946   C CH2 . TRP A 149  ? 0.3421 0.3587 0.3445 0.0017  0.0066  -0.0288 147  TRP A CH2 
947   N N   . GLY A 150  ? 0.2310 0.2203 0.2423 0.0073  0.0070  -0.0225 148  GLY A N   
948   C CA  . GLY A 150  ? 0.2558 0.2418 0.2718 0.0086  0.0061  -0.0231 148  GLY A CA  
949   C C   . GLY A 150  ? 0.2741 0.2561 0.2946 0.0090  0.0050  -0.0220 148  GLY A C   
950   O O   . GLY A 150  ? 0.2899 0.2708 0.3165 0.0100  0.0035  -0.0242 148  GLY A O   
951   N N   . LEU A 151  ? 0.2783 0.2581 0.2963 0.0083  0.0056  -0.0185 149  LEU A N   
952   C CA  . LEU A 151  ? 0.2990 0.2756 0.3212 0.0084  0.0047  -0.0172 149  LEU A CA  
953   C C   . LEU A 151  ? 0.2915 0.2704 0.3181 0.0086  0.0033  -0.0214 149  LEU A C   
954   O O   . LEU A 151  ? 0.3418 0.3187 0.3748 0.0092  0.0017  -0.0225 149  LEU A O   
955   C CB  . LEU A 151  ? 0.3291 0.3039 0.3475 0.0076  0.0057  -0.0130 149  LEU A CB  
956   C CG  . LEU A 151  ? 0.3992 0.3704 0.4208 0.0077  0.0052  -0.0099 149  LEU A CG  
957   C CD1 . LEU A 151  ? 0.3941 0.3626 0.4190 0.0085  0.0046  -0.0081 149  LEU A CD1 
958   C CD2 . LEU A 151  ? 0.4464 0.4167 0.4631 0.0070  0.0066  -0.0063 149  LEU A CD2 
959   N N   . VAL A 152  ? 0.2639 0.2475 0.2874 0.0079  0.0038  -0.0239 150  VAL A N   
960   C CA  . VAL A 152  ? 0.2951 0.2820 0.3223 0.0081  0.0026  -0.0285 150  VAL A CA  
961   C C   . VAL A 152  ? 0.3263 0.3146 0.3594 0.0095  0.0011  -0.0332 150  VAL A C   
962   O O   . VAL A 152  ? 0.3240 0.3115 0.3636 0.0102  -0.0007 -0.0361 150  VAL A O   
963   C CB  . VAL A 152  ? 0.2987 0.2915 0.3209 0.0071  0.0035  -0.0300 150  VAL A CB  
964   C CG1 . VAL A 152  ? 0.3443 0.3421 0.3702 0.0075  0.0022  -0.0356 150  VAL A CG1 
965   C CG2 . VAL A 152  ? 0.3264 0.3175 0.3444 0.0059  0.0044  -0.0256 150  VAL A CG2 
966   N N   . VAL A 153  ? 0.2814 0.2717 0.3125 0.0099  0.0017  -0.0343 151  VAL A N   
967   C CA  . VAL A 153  ? 0.2997 0.2925 0.3361 0.0112  0.0005  -0.0394 151  VAL A CA  
968   C C   . VAL A 153  ? 0.3069 0.2941 0.3497 0.0123  -0.0011 -0.0382 151  VAL A C   
969   O O   . VAL A 153  ? 0.3389 0.3259 0.3892 0.0134  -0.0031 -0.0421 151  VAL A O   
970   C CB  . VAL A 153  ? 0.2730 0.2706 0.3050 0.0112  0.0017  -0.0408 151  VAL A CB  
971   C CG1 . VAL A 153  ? 0.2958 0.2957 0.3335 0.0128  0.0004  -0.0460 151  VAL A CG1 
972   C CG2 . VAL A 153  ? 0.2724 0.2767 0.2993 0.0100  0.0028  -0.0422 151  VAL A CG2 
973   N N   . THR A 154  ? 0.3034 0.2863 0.3438 0.0120  -0.0002 -0.0330 152  THR A N   
974   C CA  . THR A 154  ? 0.3211 0.2996 0.3668 0.0129  -0.0015 -0.0313 152  THR A CA  
975   C C   . THR A 154  ? 0.3685 0.3419 0.4166 0.0124  -0.0021 -0.0265 152  THR A C   
976   O O   . THR A 154  ? 0.3600 0.3300 0.4137 0.0130  -0.0036 -0.0248 152  THR A O   
977   C CB  . THR A 154  ? 0.3306 0.3088 0.3723 0.0130  -0.0003 -0.0291 152  THR A CB  
978   O OG1 . THR A 154  ? 0.3601 0.3362 0.3954 0.0120  0.0014  -0.0238 152  THR A OG1 
979   C CG2 . THR A 154  ? 0.3640 0.3477 0.4025 0.0132  0.0006  -0.0331 152  THR A CG2 
980   N N   . GLY A 155  ? 0.3447 0.3176 0.3889 0.0114  -0.0010 -0.0238 153  GLY A N   
981   C CA  . GLY A 155  ? 0.3383 0.3072 0.3841 0.0109  -0.0013 -0.0188 153  GLY A CA  
982   C C   . GLY A 155  ? 0.3826 0.3493 0.4245 0.0107  0.0000  -0.0137 153  GLY A C   
983   O O   . GLY A 155  ? 0.3928 0.3569 0.4355 0.0103  0.0000  -0.0093 153  GLY A O   
984   N N   . LYS A 156  ? 0.3433 0.3114 0.3809 0.0110  0.0011  -0.0141 154  LYS A N   
985   C CA  . LYS A 156  ? 0.4032 0.3697 0.4371 0.0109  0.0021  -0.0099 154  LYS A CA  
986   C C   . LYS A 156  ? 0.4145 0.3827 0.4403 0.0103  0.0042  -0.0091 154  LYS A C   
987   O O   . LYS A 156  ? 0.3405 0.3117 0.3637 0.0100  0.0047  -0.0123 154  LYS A O   
988   C CB  . LYS A 156  ? 0.4230 0.3893 0.4592 0.0119  0.0014  -0.0108 154  LYS A CB  
989   N N   . LEU A 157  ? 0.3948 0.3615 0.4170 0.0100  0.0052  -0.0049 155  LEU A N   
990   C CA  . LEU A 157  ? 0.4124 0.3801 0.4278 0.0095  0.0069  -0.0040 155  LEU A CA  
991   C C   . LEU A 157  ? 0.4810 0.4488 0.4938 0.0099  0.0073  -0.0033 155  LEU A C   
992   O O   . LEU A 157  ? 0.4950 0.4614 0.5094 0.0105  0.0070  -0.0010 155  LEU A O   
993   C CB  . LEU A 157  ? 0.4232 0.3897 0.4366 0.0091  0.0076  -0.0003 155  LEU A CB  
994   C CG  . LEU A 157  ? 0.4879 0.4551 0.4952 0.0086  0.0090  0.0005  155  LEU A CG  
995   C CD1 . LEU A 157  ? 0.4594 0.4287 0.4652 0.0079  0.0091  -0.0022 155  LEU A CD1 
996   C CD2 . LEU A 157  ? 0.5528 0.5190 0.5590 0.0086  0.0096  0.0038  155  LEU A CD2 
997   N N   . THR A 158  ? 0.5564 0.5263 0.5654 0.0096  0.0081  -0.0051 156  THR A N   
998   C CA  . THR A 158  ? 0.5579 0.5280 0.5636 0.0098  0.0086  -0.0043 156  THR A CA  
999   C C   . THR A 158  ? 0.5738 0.5442 0.5743 0.0091  0.0097  -0.0028 156  THR A C   
1000  O O   . THR A 158  ? 0.6652 0.6369 0.6644 0.0083  0.0100  -0.0036 156  THR A O   
1001  C CB  . THR A 158  ? 0.5387 0.5112 0.5449 0.0099  0.0084  -0.0075 156  THR A CB  
1002  N N   . SER A 159  ? 0.4259 0.3951 0.4239 0.0095  0.0101  -0.0005 157  SER A N   
1003  C CA  . SER A 159  ? 0.3877 0.3567 0.3817 0.0090  0.0109  0.0008  157  SER A CA  
1004  C C   . SER A 159  ? 0.4204 0.3912 0.4119 0.0082  0.0110  -0.0007 157  SER A C   
1005  O O   . SER A 159  ? 0.4608 0.4322 0.4503 0.0074  0.0113  -0.0003 157  SER A O   
1006  C CB  . SER A 159  ? 0.4780 0.4460 0.4705 0.0098  0.0111  0.0031  157  SER A CB  
1007  O OG  . SER A 159  ? 0.5306 0.4983 0.5247 0.0105  0.0107  0.0033  157  SER A OG  
1008  N N   . THR A 160  ? 0.3723 0.3444 0.3643 0.0084  0.0108  -0.0021 158  THR A N   
1009  C CA  . THR A 160  ? 0.3339 0.3083 0.3241 0.0075  0.0109  -0.0033 158  THR A CA  
1010  C C   . THR A 160  ? 0.2872 0.2645 0.2797 0.0074  0.0106  -0.0061 158  THR A C   
1011  O O   . THR A 160  ? 0.3463 0.3232 0.3421 0.0082  0.0102  -0.0073 158  THR A O   
1012  C CB  . THR A 160  ? 0.3425 0.3164 0.3310 0.0078  0.0109  -0.0026 158  THR A CB  
1013  O OG1 . THR A 160  ? 0.3787 0.3521 0.3692 0.0088  0.0105  -0.0032 158  THR A OG1 
1014  C CG2 . THR A 160  ? 0.4150 0.3866 0.4015 0.0081  0.0110  -0.0005 158  THR A CG2 
1015  N N   . VAL A 161  ? 0.2386 0.2193 0.2297 0.0063  0.0108  -0.0071 159  VAL A N   
1016  C CA  . VAL A 161  ? 0.2435 0.2284 0.2361 0.0060  0.0107  -0.0100 159  VAL A CA  
1017  C C   . VAL A 161  ? 0.2306 0.2177 0.2233 0.0061  0.0107  -0.0112 159  VAL A C   
1018  O O   . VAL A 161  ? 0.2315 0.2190 0.2220 0.0054  0.0109  -0.0097 159  VAL A O   
1019  C CB  . VAL A 161  ? 0.2796 0.2680 0.2702 0.0044  0.0110  -0.0097 159  VAL A CB  
1020  C CG1 . VAL A 161  ? 0.2871 0.2815 0.2786 0.0040  0.0111  -0.0127 159  VAL A CG1 
1021  C CG2 . VAL A 161  ? 0.3169 0.3034 0.3077 0.0044  0.0110  -0.0088 159  VAL A CG2 
1022  N N   . ASN A 162  ? 0.2007 0.1893 0.1967 0.0071  0.0104  -0.0140 160  ASN A N   
1023  C CA  . ASN A 162  ? 0.2236 0.2152 0.2201 0.0072  0.0104  -0.0156 160  ASN A CA  
1024  C C   . ASN A 162  ? 0.1815 0.1795 0.1770 0.0060  0.0108  -0.0175 160  ASN A C   
1025  O O   . ASN A 162  ? 0.2039 0.2057 0.2019 0.0065  0.0106  -0.0209 160  ASN A O   
1026  C CB  . ASN A 162  ? 0.2356 0.2263 0.2363 0.0088  0.0096  -0.0178 160  ASN A CB  
1027  C CG  . ASN A 162  ? 0.2342 0.2276 0.2353 0.0090  0.0096  -0.0192 160  ASN A CG  
1028  O OD1 . ASN A 162  ? 0.2419 0.2396 0.2409 0.0079  0.0102  -0.0195 160  ASN A OD1 
1029  N ND2 . ASN A 162  ? 0.2729 0.2642 0.2771 0.0104  0.0089  -0.0198 160  ASN A ND2 
1030  N N   . ASP A 163  ? 0.1867 0.1862 0.1789 0.0045  0.0112  -0.0151 161  ASP A N   
1031  C CA  . ASP A 163  ? 0.2004 0.2065 0.1915 0.0030  0.0116  -0.0158 161  ASP A CA  
1032  C C   . ASP A 163  ? 0.1880 0.2000 0.1803 0.0030  0.0118  -0.0185 161  ASP A C   
1033  O O   . ASP A 163  ? 0.1998 0.2186 0.1923 0.0024  0.0121  -0.0205 161  ASP A O   
1034  C CB  . ASP A 163  ? 0.2255 0.2317 0.2136 0.0012  0.0117  -0.0120 161  ASP A CB  
1035  C CG  . ASP A 163  ? 0.2791 0.2818 0.2661 0.0010  0.0114  -0.0096 161  ASP A CG  
1036  O OD1 . ASP A 163  ? 0.2509 0.2488 0.2386 0.0024  0.0112  -0.0097 161  ASP A OD1 
1037  O OD2 . ASP A 163  ? 0.3032 0.3082 0.2888 -0.0006 0.0113  -0.0074 161  ASP A OD2 
1038  N N   . ARG A 164  ? 0.1961 0.2062 0.1894 0.0039  0.0116  -0.0186 162  ARG A N   
1039  C CA  . ARG A 164  ? 0.1837 0.1996 0.1786 0.0041  0.0118  -0.0214 162  ARG A CA  
1040  C C   . ARG A 164  ? 0.1939 0.2117 0.1926 0.0058  0.0114  -0.0261 162  ARG A C   
1041  O O   . ARG A 164  ? 0.1883 0.2133 0.1883 0.0058  0.0117  -0.0294 162  ARG A O   
1042  C CB  . ARG A 164  ? 0.2147 0.2280 0.2096 0.0045  0.0116  -0.0202 162  ARG A CB  
1043  C CG  . ARG A 164  ? 0.2509 0.2632 0.2427 0.0028  0.0117  -0.0162 162  ARG A CG  
1044  C CD  . ARG A 164  ? 0.3393 0.3577 0.3294 0.0006  0.0121  -0.0150 162  ARG A CD  
1045  N NE  . ARG A 164  ? 0.3560 0.3829 0.3472 0.0002  0.0126  -0.0176 162  ARG A NE  
1046  C CZ  . ARG A 164  ? 0.4097 0.4438 0.4000 -0.0012 0.0130  -0.0178 162  ARG A CZ  
1047  N NH1 . ARG A 164  ? 0.4214 0.4550 0.4099 -0.0025 0.0129  -0.0154 162  ARG A NH1 
1048  N NH2 . ARG A 164  ? 0.3910 0.4335 0.3824 -0.0014 0.0135  -0.0204 162  ARG A NH2 
1049  N N   . SER A 165  ? 0.1887 0.2006 0.1898 0.0072  0.0107  -0.0264 163  SER A N   
1050  C CA  . SER A 165  ? 0.1773 0.1903 0.1831 0.0088  0.0100  -0.0307 163  SER A CA  
1051  C C   . SER A 165  ? 0.1833 0.2011 0.1888 0.0082  0.0102  -0.0329 163  SER A C   
1052  O O   . SER A 165  ? 0.1770 0.2005 0.1854 0.0089  0.0099  -0.0375 163  SER A O   
1053  C CB  . SER A 165  ? 0.2009 0.2064 0.2093 0.0101  0.0091  -0.0296 163  SER A CB  
1054  O OG  . SER A 165  ? 0.2167 0.2227 0.2301 0.0114  0.0081  -0.0333 163  SER A OG  
1055  N N   . LEU A 166  ? 0.1810 0.1971 0.1833 0.0069  0.0106  -0.0298 164  LEU A N   
1056  C CA  . LEU A 166  ? 0.1985 0.2195 0.2002 0.0062  0.0107  -0.0315 164  LEU A CA  
1057  C C   . LEU A 166  ? 0.1738 0.2042 0.1736 0.0049  0.0115  -0.0328 164  LEU A C   
1058  O O   . LEU A 166  ? 0.1803 0.2173 0.1814 0.0051  0.0114  -0.0366 164  LEU A O   
1059  C CB  . LEU A 166  ? 0.1950 0.2120 0.1936 0.0050  0.0109  -0.0274 164  LEU A CB  
1060  C CG  . LEU A 166  ? 0.1931 0.2025 0.1941 0.0062  0.0102  -0.0267 164  LEU A CG  
1061  C CD1 . LEU A 166  ? 0.2097 0.2154 0.2076 0.0051  0.0105  -0.0226 164  LEU A CD1 
1062  C CD2 . LEU A 166  ? 0.2109 0.2218 0.2164 0.0074  0.0093  -0.0310 164  LEU A CD2 
1063  N N   . ALA A 167  ? 0.1844 0.2159 0.1813 0.0036  0.0121  -0.0296 165  ALA A N   
1064  C CA  . ALA A 167  ? 0.1810 0.2221 0.1764 0.0022  0.0128  -0.0303 165  ALA A CA  
1065  C C   . ALA A 167  ? 0.1906 0.2376 0.1894 0.0037  0.0127  -0.0358 165  ALA A C   
1066  O O   . ALA A 167  ? 0.2016 0.2577 0.2005 0.0034  0.0131  -0.0389 165  ALA A O   
1067  C CB  . ALA A 167  ? 0.2246 0.2652 0.2172 0.0006  0.0131  -0.0257 165  ALA A CB  
1068  N N   . ALA A 168  ? 0.1883 0.2307 0.1899 0.0054  0.0122  -0.0371 166  ALA A N   
1069  C CA  . ALA A 168  ? 0.1987 0.2461 0.2045 0.0071  0.0120  -0.0426 166  ALA A CA  
1070  C C   . ALA A 168  ? 0.1722 0.2221 0.1814 0.0085  0.0112  -0.0477 166  ALA A C   
1071  O O   . ALA A 168  ? 0.1791 0.2378 0.1901 0.0090  0.0113  -0.0525 166  ALA A O   
1072  C CB  . ALA A 168  ? 0.1936 0.2343 0.2022 0.0087  0.0113  -0.0425 166  ALA A CB  
1073  N N   . ALA A 169  ? 0.1657 0.2084 0.1760 0.0090  0.0104  -0.0467 167  ALA A N   
1074  C CA  . ALA A 169  ? 0.1605 0.2045 0.1748 0.0103  0.0094  -0.0515 167  ALA A CA  
1075  C C   . ALA A 169  ? 0.1616 0.2146 0.1734 0.0091  0.0101  -0.0531 167  ALA A C   
1076  O O   . ALA A 169  ? 0.1743 0.2336 0.1892 0.0102  0.0095  -0.0589 167  ALA A O   
1077  C CB  . ALA A 169  ? 0.1725 0.2069 0.1882 0.0108  0.0085  -0.0490 167  ALA A CB  
1078  N N   . LEU A 170  ? 0.1703 0.2241 0.1766 0.0069  0.0111  -0.0482 168  LEU A N   
1079  C CA  . LEU A 170  ? 0.1671 0.2297 0.1707 0.0055  0.0116  -0.0489 168  LEU A CA  
1080  C C   . LEU A 170  ? 0.1854 0.2598 0.1889 0.0053  0.0123  -0.0522 168  LEU A C   
1081  O O   . LEU A 170  ? 0.1935 0.2766 0.1980 0.0057  0.0122  -0.0569 168  LEU A O   
1082  C CB  . LEU A 170  ? 0.1942 0.2545 0.1927 0.0030  0.0122  -0.0423 168  LEU A CB  
1083  C CG  . LEU A 170  ? 0.1921 0.2607 0.1879 0.0014  0.0125  -0.0421 168  LEU A CG  
1084  C CD1 . LEU A 170  ? 0.2407 0.3098 0.2393 0.0028  0.0117  -0.0467 168  LEU A CD1 
1085  C CD2 . LEU A 170  ? 0.2220 0.2869 0.2137 -0.0008 0.0128  -0.0353 168  LEU A CD2 
1086  N N   . THR A 171  ? 0.1799 0.2550 0.1822 0.0047  0.0130  -0.0501 169  THR A N   
1087  C CA  . THR A 171  ? 0.1876 0.2742 0.1902 0.0046  0.0137  -0.0532 169  THR A CA  
1088  C C   . THR A 171  ? 0.1696 0.2597 0.1777 0.0073  0.0129  -0.0611 169  THR A C   
1089  O O   . THR A 171  ? 0.1870 0.2883 0.1957 0.0076  0.0132  -0.0658 169  THR A O   
1090  C CB  . THR A 171  ? 0.2165 0.3014 0.2180 0.0038  0.0143  -0.0498 169  THR A CB  
1091  O OG1 . THR A 171  ? 0.2531 0.3354 0.2501 0.0013  0.0148  -0.0428 169  THR A OG1 
1092  C CG2 . THR A 171  ? 0.2260 0.3228 0.2283 0.0038  0.0151  -0.0531 169  THR A CG2 
1093  N N   . ARG A 172  ? 0.1676 0.2485 0.1801 0.0094  0.0118  -0.0627 170  ARG A N   
1094  C CA  . ARG A 172  ? 0.1808 0.2639 0.1997 0.0121  0.0106  -0.0701 170  ARG A CA  
1095  C C   . ARG A 172  ? 0.1855 0.2730 0.2064 0.0129  0.0098  -0.0749 170  ARG A C   
1096  O O   . ARG A 172  ? 0.1895 0.2863 0.2135 0.0142  0.0095  -0.0817 170  ARG A O   
1097  C CB  . ARG A 172  ? 0.1853 0.2568 0.2087 0.0138  0.0092  -0.0696 170  ARG A CB  
1098  C CG  . ARG A 172  ? 0.1792 0.2525 0.2101 0.0167  0.0078  -0.0768 170  ARG A CG  
1099  C CD  . ARG A 172  ? 0.2035 0.2651 0.2394 0.0182  0.0061  -0.0756 170  ARG A CD  
1100  N NE  . ARG A 172  ? 0.1884 0.2428 0.2208 0.0171  0.0068  -0.0690 170  ARG A NE  
1101  C CZ  . ARG A 172  ? 0.1755 0.2214 0.2052 0.0160  0.0068  -0.0633 170  ARG A CZ  
1102  N NH1 . ARG A 172  ? 0.1834 0.2261 0.2133 0.0158  0.0063  -0.0629 170  ARG A NH1 
1103  N NH2 . ARG A 172  ? 0.1938 0.2344 0.2205 0.0152  0.0074  -0.0581 170  ARG A NH2 
1104  N N   . LEU A 173  ? 0.1731 0.2546 0.1924 0.0120  0.0094  -0.0719 171  LEU A N   
1105  C CA  . LEU A 173  ? 0.1683 0.2532 0.1901 0.0129  0.0084  -0.0766 171  LEU A CA  
1106  C C   . LEU A 173  ? 0.1766 0.2748 0.1945 0.0116  0.0095  -0.0784 171  LEU A C   
1107  O O   . LEU A 173  ? 0.1957 0.3018 0.2166 0.0129  0.0088  -0.0851 171  LEU A O   
1108  C CB  . LEU A 173  ? 0.2033 0.2781 0.2248 0.0124  0.0077  -0.0730 171  LEU A CB  
1109  C CG  . LEU A 173  ? 0.2171 0.2902 0.2319 0.0098  0.0088  -0.0663 171  LEU A CG  
1110  C CD1 . LEU A 173  ? 0.2399 0.3214 0.2531 0.0090  0.0088  -0.0686 171  LEU A CD1 
1111  C CD2 . LEU A 173  ? 0.2155 0.2760 0.2307 0.0097  0.0082  -0.0615 171  LEU A CD2 
1112  N N   . ILE A 174  ? 0.1921 0.2934 0.2036 0.0089  0.0111  -0.0723 172  ILE A N   
1113  C CA  . ILE A 174  ? 0.1800 0.2947 0.1878 0.0074  0.0121  -0.0731 172  ILE A CA  
1114  C C   . ILE A 174  ? 0.1701 0.2965 0.1800 0.0085  0.0125  -0.0789 172  ILE A C   
1115  O O   . ILE A 174  ? 0.2022 0.3404 0.2126 0.0090  0.0126  -0.0843 172  ILE A O   
1116  C CB  . ILE A 174  ? 0.2063 0.3212 0.2077 0.0041  0.0133  -0.0647 172  ILE A CB  
1117  C CG1 . ILE A 174  ? 0.2401 0.3458 0.2395 0.0031  0.0128  -0.0600 172  ILE A CG1 
1118  C CG2 . ILE A 174  ? 0.2507 0.3809 0.2485 0.0023  0.0144  -0.0649 172  ILE A CG2 
1119  C CD1 . ILE A 174  ? 0.2478 0.3509 0.2422 0.0003  0.0136  -0.0517 172  ILE A CD1 
1120  N N   . SER A 175  ? 0.1879 0.3116 0.1992 0.0091  0.0129  -0.0783 173  SER A N   
1121  C CA  . SER A 175  ? 0.1850 0.3200 0.1985 0.0102  0.0134  -0.0837 173  SER A CA  
1122  C C   . SER A 175  ? 0.1910 0.3280 0.2115 0.0135  0.0118  -0.0930 173  SER A C   
1123  O O   . SER A 175  ? 0.2222 0.3716 0.2446 0.0147  0.0121  -0.0993 173  SER A O   
1124  C CB  . SER A 175  ? 0.2115 0.3425 0.2252 0.0101  0.0139  -0.0807 173  SER A CB  
1125  O OG  . SER A 175  ? 0.2698 0.4015 0.2777 0.0070  0.0153  -0.0729 173  SER A OG  
1126  N N   . ARG A 176  ? 0.1980 0.3234 0.2227 0.0151  0.0101  -0.0941 174  ARG A N   
1127  C CA  . ARG A 176  ? 0.1818 0.3082 0.2142 0.0183  0.0082  -0.1028 174  ARG A CA  
1128  C C   . ARG A 176  ? 0.2426 0.3758 0.2752 0.0185  0.0076  -0.1073 174  ARG A C   
1129  O O   . ARG A 176  ? 0.2693 0.4119 0.3063 0.0205  0.0068  -0.1157 174  ARG A O   
1130  C CB  . ARG A 176  ? 0.2437 0.3549 0.2813 0.0197  0.0064  -0.1015 174  ARG A CB  
1131  C CG  . ARG A 176  ? 0.2718 0.3822 0.3188 0.0230  0.0041  -0.1098 174  ARG A CG  
1132  C CD  . ARG A 176  ? 0.2405 0.3362 0.2923 0.0240  0.0024  -0.1070 174  ARG A CD  
1133  N NE  . ARG A 176  ? 0.2304 0.3173 0.2816 0.0231  0.0016  -0.1032 174  ARG A NE  
1134  C CZ  . ARG A 176  ? 0.2579 0.3348 0.3051 0.0214  0.0022  -0.0952 174  ARG A CZ  
1135  N NH1 . ARG A 176  ? 0.2164 0.2897 0.2601 0.0204  0.0035  -0.0898 174  ARG A NH1 
1136  N NH2 . ARG A 176  ? 0.3067 0.3774 0.3536 0.0207  0.0015  -0.0927 174  ARG A NH2 
1137  N N   . CYS A 177  ? 0.2263 0.3552 0.2545 0.0165  0.0078  -0.1021 175  CYS A N   
1138  C CA  . CYS A 177  ? 0.2461 0.3790 0.2754 0.0169  0.0068  -0.1061 175  CYS A CA  
1139  C C   . CYS A 177  ? 0.2686 0.4117 0.2906 0.0143  0.0083  -0.1031 175  CYS A C   
1140  O O   . CYS A 177  ? 0.3061 0.4558 0.3288 0.0147  0.0076  -0.1075 175  CYS A O   
1141  C CB  . CYS A 177  ? 0.2790 0.3980 0.3110 0.0172  0.0052  -0.1036 175  CYS A CB  
1142  S SG  . CYS A 177  ? 0.3336 0.4397 0.3744 0.0199  0.0032  -0.1058 175  CYS A SG  
1143  N N   . GLY A 178  ? 0.2659 0.4102 0.2816 0.0116  0.0101  -0.0956 176  GLY A N   
1144  C CA  . GLY A 178  ? 0.2755 0.4314 0.2850 0.0091  0.0114  -0.0928 176  GLY A CA  
1145  C C   . GLY A 178  ? 0.2652 0.4182 0.2719 0.0077  0.0109  -0.0895 176  GLY A C   
1146  O O   . GLY A 178  ? 0.2539 0.3939 0.2619 0.0079  0.0100  -0.0869 176  GLY A O   
1147  N N   . GLU A 179  ? 0.2735 0.4397 0.2762 0.0061  0.0116  -0.0896 177  GLU A N   
1148  C CA  . GLU A 179  ? 0.2442 0.4098 0.2437 0.0044  0.0112  -0.0864 177  GLU A CA  
1149  C C   . GLU A 179  ? 0.2169 0.3747 0.2211 0.0065  0.0094  -0.0909 177  GLU A C   
1150  O O   . GLU A 179  ? 0.2647 0.4137 0.2674 0.0053  0.0089  -0.0859 177  GLU A O   
1151  C CB  . GLU A 179  ? 0.2633 0.4466 0.2587 0.0028  0.0121  -0.0872 177  GLU A CB  
1152  N N   . PRO A 180  ? 0.2309 0.3916 0.2412 0.0094  0.0080  -0.1002 178  PRO A N   
1153  C CA  . PRO A 180  ? 0.2310 0.3841 0.2463 0.0111  0.0060  -0.1040 178  PRO A CA  
1154  C C   . PRO A 180  ? 0.2582 0.3938 0.2751 0.0110  0.0054  -0.0985 178  PRO A C   
1155  O O   . PRO A 180  ? 0.2578 0.3875 0.2747 0.0105  0.0045  -0.0966 178  PRO A O   
1156  C CB  . PRO A 180  ? 0.2975 0.4555 0.3203 0.0145  0.0046  -0.1145 178  PRO A CB  
1157  C CG  . PRO A 180  ? 0.2728 0.4469 0.2926 0.0141  0.0060  -0.1173 178  PRO A CG  
1158  C CD  . PRO A 180  ? 0.2423 0.4152 0.2554 0.0113  0.0082  -0.1080 178  PRO A CD  
1159  N N   . VAL A 181  ? 0.2252 0.3528 0.2433 0.0114  0.0058  -0.0957 179  VAL A N   
1160  C CA  . VAL A 181  ? 0.2100 0.3218 0.2294 0.0113  0.0053  -0.0905 179  VAL A CA  
1161  C C   . VAL A 181  ? 0.2281 0.3359 0.2408 0.0085  0.0065  -0.0815 179  VAL A C   
1162  O O   . VAL A 181  ? 0.2266 0.3243 0.2398 0.0081  0.0059  -0.0780 179  VAL A O   
1163  C CB  . VAL A 181  ? 0.2209 0.3256 0.2437 0.0127  0.0052  -0.0903 179  VAL A CB  
1164  C CG1 . VAL A 181  ? 0.2134 0.3212 0.2308 0.0109  0.0073  -0.0851 179  VAL A CG1 
1165  C CG2 . VAL A 181  ? 0.2845 0.3740 0.3102 0.0130  0.0042  -0.0864 179  VAL A CG2 
1166  N N   . ILE A 182  ? 0.2325 0.3484 0.2393 0.0063  0.0081  -0.0777 180  ILE A N   
1167  C CA  . ILE A 182  ? 0.2312 0.3439 0.2323 0.0036  0.0090  -0.0694 180  ILE A CA  
1168  C C   . ILE A 182  ? 0.2645 0.3791 0.2647 0.0029  0.0082  -0.0696 180  ILE A C   
1169  O O   . ILE A 182  ? 0.2485 0.3543 0.2473 0.0019  0.0080  -0.0646 180  ILE A O   
1170  C CB  . ILE A 182  ? 0.2343 0.3563 0.2303 0.0013  0.0106  -0.0654 180  ILE A CB  
1171  C CG1 . ILE A 182  ? 0.2341 0.3534 0.2311 0.0019  0.0113  -0.0648 180  ILE A CG1 
1172  C CG2 . ILE A 182  ? 0.2519 0.3704 0.2429 -0.0015 0.0111  -0.0569 180  ILE A CG2 
1173  C CD1 . ILE A 182  ? 0.2687 0.3995 0.2621 0.0002  0.0127  -0.0630 180  ILE A CD1 
1174  N N   . ARG A 183  ? 0.2415 0.3680 0.2424 0.0035  0.0078  -0.0757 181  ARG A N   
1175  C CA  A ARG A 183  ? 0.2998 0.4291 0.3002 0.0030  0.0069  -0.0768 181  ARG A CA  
1176  C CA  B ARG A 183  ? 0.2999 0.4293 0.3003 0.0031  0.0069  -0.0769 181  ARG A CA  
1177  C C   . ARG A 183  ? 0.2954 0.4124 0.3006 0.0046  0.0053  -0.0781 181  ARG A C   
1178  O O   . ARG A 183  ? 0.3007 0.4128 0.3043 0.0034  0.0049  -0.0742 181  ARG A O   
1179  C CB  A ARG A 183  ? 0.2986 0.4431 0.2999 0.0039  0.0065  -0.0845 181  ARG A CB  
1180  C CB  B ARG A 183  ? 0.2979 0.4422 0.2995 0.0041  0.0064  -0.0849 181  ARG A CB  
1181  C CG  A ARG A 183  ? 0.3601 0.5082 0.3616 0.0039  0.0052  -0.0870 181  ARG A CG  
1182  C CG  B ARG A 183  ? 0.3605 0.5101 0.3618 0.0038  0.0054  -0.0872 181  ARG A CG  
1183  C CD  A ARG A 183  ? 0.3743 0.5209 0.3701 0.0009  0.0058  -0.0786 181  ARG A CD  
1184  C CD  B ARG A 183  ? 0.3928 0.5491 0.3871 0.0006  0.0064  -0.0803 181  ARG A CD  
1185  N NE  A ARG A 183  ? 0.3677 0.5240 0.3578 -0.0015 0.0074  -0.0737 181  ARG A NE  
1186  N NE  B ARG A 183  ? 0.3513 0.4954 0.3437 -0.0009 0.0063  -0.0725 181  ARG A NE  
1187  C CZ  A ARG A 183  ? 0.3955 0.5492 0.3811 -0.0042 0.0081  -0.0650 181  ARG A CZ  
1188  C CZ  B ARG A 183  ? 0.4009 0.5461 0.3881 -0.0037 0.0072  -0.0645 181  ARG A CZ  
1189  N NH1 A ARG A 183  ? 0.3928 0.5346 0.3783 -0.0048 0.0075  -0.0604 181  ARG A NH1 
1190  N NH1 B ARG A 183  ? 0.4212 0.5787 0.4044 -0.0055 0.0083  -0.0624 181  ARG A NH1 
1191  N NH2 A ARG A 183  ? 0.4121 0.5754 0.3933 -0.0065 0.0092  -0.0607 181  ARG A NH2 
1192  N NH2 B ARG A 183  ? 0.3764 0.5104 0.3628 -0.0047 0.0070  -0.0585 181  ARG A NH2 
1193  N N   . ARG A 184  ? 0.2514 0.3636 0.2629 0.0071  0.0042  -0.0834 182  ARG A N   
1194  C CA  . ARG A 184  ? 0.2775 0.3783 0.2943 0.0084  0.0026  -0.0843 182  ARG A CA  
1195  C C   . ARG A 184  ? 0.2823 0.3704 0.2968 0.0072  0.0032  -0.0760 182  ARG A C   
1196  O O   . ARG A 184  ? 0.2818 0.3627 0.2975 0.0069  0.0024  -0.0738 182  ARG A O   
1197  C CB  . ARG A 184  ? 0.3095 0.4080 0.3340 0.0112  0.0011  -0.0912 182  ARG A CB  
1198  C CG  . ARG A 184  ? 0.3814 0.4906 0.4100 0.0130  -0.0002 -0.1007 182  ARG A CG  
1199  C CD  . ARG A 184  ? 0.3674 0.4719 0.4017 0.0141  -0.0026 -0.1042 182  ARG A CD  
1200  N NE  . ARG A 184  ? 0.3981 0.4931 0.4409 0.0163  -0.0045 -0.1071 182  ARG A NE  
1201  C CZ  . ARG A 184  ? 0.3731 0.4556 0.4191 0.0162  -0.0055 -0.1031 182  ARG A CZ  
1202  N NH1 . ARG A 184  ? 0.4236 0.5010 0.4651 0.0142  -0.0047 -0.0964 182  ARG A NH1 
1203  N NH2 . ARG A 184  ? 0.3707 0.4460 0.4249 0.0181  -0.0073 -0.1058 182  ARG A NH2 
1204  N N   . GLY A 185  ? 0.2571 0.3429 0.2688 0.0064  0.0046  -0.0716 183  GLY A N   
1205  C CA  . GLY A 185  ? 0.2515 0.3262 0.2609 0.0053  0.0053  -0.0641 183  GLY A CA  
1206  C C   . GLY A 185  ? 0.2974 0.3725 0.3017 0.0031  0.0058  -0.0586 183  GLY A C   
1207  O O   . GLY A 185  ? 0.2479 0.3141 0.2524 0.0027  0.0055  -0.0548 183  GLY A O   
1208  N N   . VAL A 186  ? 0.2760 0.3616 0.2759 0.0015  0.0066  -0.0578 184  VAL A N   
1209  C CA  . VAL A 186  ? 0.2911 0.3779 0.2865 -0.0008 0.0069  -0.0524 184  VAL A CA  
1210  C C   . VAL A 186  ? 0.2896 0.3746 0.2872 -0.0003 0.0056  -0.0545 184  VAL A C   
1211  O O   . VAL A 186  ? 0.2825 0.3608 0.2789 -0.0012 0.0054  -0.0498 184  VAL A O   
1212  C CB  . VAL A 186  ? 0.2980 0.3980 0.2890 -0.0026 0.0077  -0.0515 184  VAL A CB  
1213  C CG1 . VAL A 186  ? 0.2980 0.4007 0.2855 -0.0047 0.0075  -0.0472 184  VAL A CG1 
1214  C CG2 . VAL A 186  ? 0.3005 0.4003 0.2890 -0.0037 0.0089  -0.0472 184  VAL A CG2 
1215  N N   . ASP A 187  ? 0.2680 0.3592 0.2691 0.0012  0.0045  -0.0618 185  ASP A N   
1216  C CA  . ASP A 187  ? 0.3021 0.3923 0.3058 0.0016  0.0031  -0.0643 185  ASP A CA  
1217  C C   . ASP A 187  ? 0.3353 0.4119 0.3431 0.0027  0.0023  -0.0628 185  ASP A C   
1218  O O   . ASP A 187  ? 0.3166 0.3890 0.3246 0.0021  0.0017  -0.0604 185  ASP A O   
1219  C CB  . ASP A 187  ? 0.3352 0.4349 0.3425 0.0033  0.0019  -0.0731 185  ASP A CB  
1220  C CG  . ASP A 187  ? 0.3914 0.5061 0.3942 0.0020  0.0027  -0.0744 185  ASP A CG  
1221  O OD1 . ASP A 187  ? 0.4426 0.5598 0.4396 -0.0004 0.0038  -0.0679 185  ASP A OD1 
1222  O OD2 . ASP A 187  ? 0.4214 0.5457 0.4266 0.0034  0.0021  -0.0819 185  ASP A OD2 
1223  N N   . MET A 188  ? 0.3137 0.3840 0.3251 0.0041  0.0022  -0.0639 186  MET A N   
1224  C CA  . MET A 188  ? 0.3176 0.3758 0.3330 0.0049  0.0015  -0.0617 186  MET A CA  
1225  C C   . MET A 188  ? 0.3295 0.3807 0.3404 0.0033  0.0026  -0.0536 186  MET A C   
1226  O O   . MET A 188  ? 0.3233 0.3681 0.3355 0.0031  0.0021  -0.0511 186  MET A O   
1227  C CB  . MET A 188  ? 0.3482 0.4020 0.3679 0.0067  0.0012  -0.0639 186  MET A CB  
1228  C CG  . MET A 188  ? 0.4137 0.4558 0.4378 0.0075  0.0004  -0.0614 186  MET A CG  
1229  S SD  . MET A 188  ? 0.5538 0.5943 0.5855 0.0087  -0.0022 -0.0665 186  MET A SD  
1230  C CE  . MET A 188  ? 0.4590 0.5092 0.4951 0.0106  -0.0034 -0.0760 186  MET A CE  
1231  N N   . ALA A 189  ? 0.3021 0.3545 0.3082 0.0022  0.0041  -0.0496 187  ALA A N   
1232  C CA  . ALA A 189  ? 0.3236 0.3695 0.3260 0.0008  0.0050  -0.0424 187  ALA A CA  
1233  C C   . ALA A 189  ? 0.3296 0.3778 0.3294 -0.0007 0.0049  -0.0397 187  ALA A C   
1234  O O   . ALA A 189  ? 0.3177 0.3589 0.3169 -0.0012 0.0049  -0.0355 187  ALA A O   
1235  C CB  . ALA A 189  ? 0.3195 0.3672 0.3179 -0.0002 0.0064  -0.0391 187  ALA A CB  
1236  N N   . MET A 190  ? 0.3040 0.3624 0.3020 -0.0015 0.0047  -0.0422 188  MET A N   
1237  C CA  . MET A 190  ? 0.3224 0.3837 0.3180 -0.0030 0.0043  -0.0398 188  MET A CA  
1238  C C   . MET A 190  ? 0.3216 0.3776 0.3210 -0.0021 0.0031  -0.0415 188  MET A C   
1239  O O   . MET A 190  ? 0.3534 0.4054 0.3516 -0.0031 0.0030  -0.0373 188  MET A O   
1240  C CB  . MET A 190  ? 0.3372 0.4117 0.3306 -0.0038 0.0042  -0.0428 188  MET A CB  
1241  C CG  . MET A 190  ? 0.4612 0.5403 0.4513 -0.0058 0.0039  -0.0392 188  MET A CG  
1242  S SD  . MET A 190  ? 0.5098 0.6057 0.4977 -0.0066 0.0037  -0.0434 188  MET A SD  
1243  C CE  . MET A 190  ? 0.4251 0.5266 0.4113 -0.0067 0.0050  -0.0438 188  MET A CE  
1244  N N   . ARG A 191  ? 0.3013 0.3573 0.3059 -0.0003 0.0020  -0.0476 189  ARG A N   
1245  C CA  . ARG A 191  ? 0.3591 0.4097 0.3684 0.0006  0.0006  -0.0492 189  ARG A CA  
1246  C C   . ARG A 191  ? 0.3823 0.4214 0.3927 0.0007  0.0010  -0.0442 189  ARG A C   
1247  O O   . ARG A 191  ? 0.3616 0.3965 0.3727 0.0002  0.0006  -0.0415 189  ARG A O   
1248  C CB  . ARG A 191  ? 0.3628 0.4153 0.3784 0.0026  -0.0009 -0.0568 189  ARG A CB  
1249  C CG  . ARG A 191  ? 0.4698 0.5176 0.4914 0.0034  -0.0027 -0.0591 189  ARG A CG  
1250  C CD  . ARG A 191  ? 0.5502 0.5966 0.5793 0.0056  -0.0043 -0.0654 189  ARG A CD  
1251  N NE  . ARG A 191  ? 0.7152 0.7560 0.7508 0.0062  -0.0063 -0.0668 189  ARG A NE  
1252  C CZ  . ARG A 191  ? 0.7601 0.8048 0.8012 0.0073  -0.0084 -0.0735 189  ARG A CZ  
1253  N NH1 . ARG A 191  ? 0.7150 0.7696 0.7560 0.0081  -0.0088 -0.0799 189  ARG A NH1 
1254  N NH2 . ARG A 191  ? 0.7578 0.7967 0.8051 0.0077  -0.0102 -0.0739 189  ARG A NH2 
1255  N N   . MET A 192  ? 0.3041 0.3386 0.3150 0.0014  0.0017  -0.0429 190  MET A N   
1256  C CA  . MET A 192  ? 0.3028 0.3273 0.3151 0.0017  0.0020  -0.0387 190  MET A CA  
1257  C C   . MET A 192  ? 0.3524 0.3743 0.3598 0.0002  0.0031  -0.0323 190  MET A C   
1258  O O   . MET A 192  ? 0.3426 0.3586 0.3510 0.0001  0.0029  -0.0293 190  MET A O   
1259  C CB  . MET A 192  ? 0.3586 0.3795 0.3723 0.0027  0.0024  -0.0389 190  MET A CB  
1260  C CG  . MET A 192  ? 0.3330 0.3552 0.3527 0.0044  0.0011  -0.0449 190  MET A CG  
1261  S SD  . MET A 192  ? 0.4891 0.5065 0.5102 0.0055  0.0016  -0.0442 190  MET A SD  
1262  C CE  . MET A 192  ? 0.4083 0.4153 0.4323 0.0057  0.0013  -0.0392 190  MET A CE  
1263  N N   . MET A 193  ? 0.3135 0.3397 0.3159 -0.0010 0.0041  -0.0301 191  MET A N   
1264  C CA  A MET A 193  ? 0.3748 0.3981 0.3733 -0.0023 0.0049  -0.0241 191  MET A CA  
1265  C CA  B MET A 193  ? 0.3748 0.3981 0.3734 -0.0023 0.0049  -0.0241 191  MET A CA  
1266  C C   . MET A 193  ? 0.3609 0.3870 0.3581 -0.0035 0.0043  -0.0226 191  MET A C   
1267  O O   . MET A 193  ? 0.3940 0.4159 0.3896 -0.0042 0.0046  -0.0181 191  MET A O   
1268  C CB  A MET A 193  ? 0.3575 0.3841 0.3520 -0.0032 0.0058  -0.0219 191  MET A CB  
1269  C CB  B MET A 193  ? 0.3575 0.3838 0.3521 -0.0032 0.0058  -0.0218 191  MET A CB  
1270  C CG  A MET A 193  ? 0.3521 0.3766 0.3476 -0.0021 0.0064  -0.0234 191  MET A CG  
1271  C CG  B MET A 193  ? 0.3500 0.3716 0.3453 -0.0022 0.0065  -0.0216 191  MET A CG  
1272  S SD  A MET A 193  ? 0.3759 0.4053 0.3671 -0.0034 0.0074  -0.0210 191  MET A SD  
1273  S SD  B MET A 193  ? 0.4191 0.4422 0.4099 -0.0035 0.0075  -0.0174 191  MET A SD  
1274  C CE  A MET A 193  ? 0.4344 0.4558 0.4235 -0.0041 0.0078  -0.0145 191  MET A CE  
1275  C CE  B MET A 193  ? 0.3776 0.4127 0.3666 -0.0046 0.0075  -0.0202 191  MET A CE  
1276  N N   . GLY A 194  ? 0.3536 0.3867 0.3515 -0.0036 0.0035  -0.0265 192  GLY A N   
1277  C CA  . GLY A 194  ? 0.3523 0.3889 0.3488 -0.0049 0.0028  -0.0252 192  GLY A CA  
1278  C C   . GLY A 194  ? 0.4126 0.4467 0.4132 -0.0041 0.0017  -0.0275 192  GLY A C   
1279  O O   . GLY A 194  ? 0.3706 0.4053 0.3705 -0.0050 0.0012  -0.0254 192  GLY A O   
1280  N N   . GLU A 195  ? 0.3519 0.3832 0.3573 -0.0025 0.0011  -0.0317 193  GLU A N   
1281  C CA  . GLU A 195  ? 0.3469 0.3764 0.3572 -0.0018 -0.0004 -0.0345 193  GLU A CA  
1282  C C   . GLU A 195  ? 0.2981 0.3188 0.3133 -0.0006 -0.0007 -0.0340 193  GLU A C   
1283  O O   . GLU A 195  ? 0.2917 0.3095 0.3107 -0.0004 -0.0018 -0.0345 193  GLU A O   
1284  C CB  . GLU A 195  ? 0.3788 0.4159 0.3917 -0.0011 -0.0017 -0.0415 193  GLU A CB  
1285  C CG  . GLU A 195  ? 0.4738 0.5215 0.4821 -0.0022 -0.0014 -0.0426 193  GLU A CG  
1286  C CD  . GLU A 195  ? 0.5591 0.6148 0.5701 -0.0012 -0.0026 -0.0502 193  GLU A CD  
1287  O OE1 . GLU A 195  ? 0.5970 0.6497 0.6141 0.0003  -0.0040 -0.0546 193  GLU A OE1 
1288  O OE2 . GLU A 195  ? 0.6477 0.7131 0.6553 -0.0018 -0.0021 -0.0518 193  GLU A OE2 
1289  N N   . GLN A 196  ? 0.3627 0.3794 0.3781 0.0001  0.0001  -0.0331 194  GLN A N   
1290  C CA  . GLN A 196  ? 0.3373 0.3463 0.3575 0.0012  -0.0003 -0.0324 194  GLN A CA  
1291  C C   . GLN A 196  ? 0.3642 0.3670 0.3819 0.0008  0.0010  -0.0263 194  GLN A C   
1292  O O   . GLN A 196  ? 0.3890 0.3869 0.4092 0.0009  0.0008  -0.0238 194  GLN A O   
1293  C CB  . GLN A 196  ? 0.3718 0.3811 0.3954 0.0025  -0.0007 -0.0362 194  GLN A CB  
1294  C CG  . GLN A 196  ? 0.4858 0.4876 0.5149 0.0035  -0.0014 -0.0351 194  GLN A CG  
1295  C CD  . GLN A 196  ? 0.4872 0.4883 0.5189 0.0047  -0.0016 -0.0375 194  GLN A CD  
1296  O OE1 . GLN A 196  ? 0.5365 0.5432 0.5686 0.0052  -0.0020 -0.0424 194  GLN A OE1 
1297  N NE2 . GLN A 196  ? 0.5656 0.5604 0.5991 0.0051  -0.0014 -0.0341 194  GLN A NE2 
1298  N N   . PHE A 197  ? 0.3410 0.3441 0.3542 0.0005  0.0024  -0.0239 195  PHE A N   
1299  C CA  . PHE A 197  ? 0.3537 0.3514 0.3644 0.0003  0.0036  -0.0187 195  PHE A CA  
1300  C C   . PHE A 197  ? 0.3776 0.3753 0.3858 -0.0008 0.0038  -0.0153 195  PHE A C   
1301  O O   . PHE A 197  ? 0.3562 0.3492 0.3639 -0.0007 0.0044  -0.0115 195  PHE A O   
1302  C CB  . PHE A 197  ? 0.3810 0.3796 0.3878 0.0002  0.0047  -0.0174 195  PHE A CB  
1303  C CG  . PHE A 197  ? 0.3866 0.3849 0.3958 0.0013  0.0046  -0.0203 195  PHE A CG  
1304  C CD1 . PHE A 197  ? 0.4463 0.4403 0.4606 0.0024  0.0038  -0.0214 195  PHE A CD1 
1305  C CD2 . PHE A 197  ? 0.4073 0.4096 0.4138 0.0011  0.0051  -0.0216 195  PHE A CD2 
1306  C CE1 . PHE A 197  ? 0.4632 0.4568 0.4802 0.0034  0.0034  -0.0239 195  PHE A CE1 
1307  C CE2 . PHE A 197  ? 0.4261 0.4281 0.4350 0.0022  0.0049  -0.0243 195  PHE A CE2 
1308  C CZ  . PHE A 197  ? 0.3897 0.3872 0.4040 0.0034  0.0041  -0.0255 195  PHE A CZ  
1309  N N   . VAL A 198  ? 0.3215 0.3247 0.3283 -0.0017 0.0032  -0.0167 196  VAL A N   
1310  C CA  . VAL A 198  ? 0.3261 0.3298 0.3313 -0.0027 0.0031  -0.0139 196  VAL A CA  
1311  C C   . VAL A 198  ? 0.2926 0.3006 0.3001 -0.0029 0.0018  -0.0173 196  VAL A C   
1312  O O   . VAL A 198  ? 0.3406 0.3531 0.3496 -0.0026 0.0011  -0.0219 196  VAL A O   
1313  C CB  . VAL A 198  ? 0.3293 0.3361 0.3295 -0.0039 0.0037  -0.0109 196  VAL A CB  
1314  C CG1 . VAL A 198  ? 0.3374 0.3400 0.3356 -0.0036 0.0048  -0.0080 196  VAL A CG1 
1315  C CG2 . VAL A 198  ? 0.3344 0.3492 0.3327 -0.0046 0.0034  -0.0138 196  VAL A CG2 
1316  N N   . THR A 199  ? 0.2856 0.2923 0.2937 -0.0034 0.0013  -0.0153 197  THR A N   
1317  C CA  A THR A 199  ? 0.2819 0.2933 0.2917 -0.0039 0.0000  -0.0182 197  THR A CA  
1318  C CA  B THR A 199  ? 0.2824 0.2938 0.2922 -0.0039 0.0000  -0.0182 197  THR A CA  
1319  C C   . THR A 199  ? 0.3373 0.3564 0.3428 -0.0051 -0.0001 -0.0183 197  THR A C   
1320  O O   . THR A 199  ? 0.3433 0.3688 0.3495 -0.0053 -0.0011 -0.0223 197  THR A O   
1321  C CB  A THR A 199  ? 0.2805 0.2882 0.2925 -0.0040 -0.0004 -0.0157 197  THR A CB  
1322  C CB  B THR A 199  ? 0.2801 0.2883 0.2917 -0.0042 -0.0005 -0.0156 197  THR A CB  
1323  O OG1 A THR A 199  ? 0.2824 0.2834 0.2980 -0.0030 -0.0002 -0.0148 197  THR A OG1 
1324  O OG1 B THR A 199  ? 0.2534 0.2587 0.2618 -0.0047 0.0006  -0.0105 197  THR A OG1 
1325  C CG2 A THR A 199  ? 0.2957 0.3075 0.3105 -0.0043 -0.0021 -0.0192 197  THR A CG2 
1326  C CG2 B THR A 199  ? 0.2798 0.2826 0.2969 -0.0031 -0.0009 -0.0165 197  THR A CG2 
1327  N N   . GLY A 200  ? 0.2907 0.3097 0.2921 -0.0060 0.0008  -0.0140 198  GLY A N   
1328  C CA  . GLY A 200  ? 0.3133 0.3397 0.3108 -0.0074 0.0007  -0.0131 198  GLY A CA  
1329  C C   . GLY A 200  ? 0.3119 0.3363 0.3062 -0.0081 0.0016  -0.0084 198  GLY A C   
1330  O O   . GLY A 200  ? 0.2750 0.2923 0.2699 -0.0075 0.0023  -0.0058 198  GLY A O   
1331  N N   . GLU A 201  ? 0.3171 0.3483 0.3082 -0.0094 0.0016  -0.0075 199  GLU A N   
1332  C CA  . GLU A 201  ? 0.3024 0.3320 0.2910 -0.0103 0.0021  -0.0029 199  GLU A CA  
1333  C C   . GLU A 201  ? 0.3126 0.3396 0.3009 -0.0112 0.0015  0.0019  199  GLU A C   
1334  O O   . GLU A 201  ? 0.3492 0.3718 0.3370 -0.0114 0.0018  0.0055  199  GLU A O   
1335  C CB  . GLU A 201  ? 0.3366 0.3747 0.3223 -0.0117 0.0022  -0.0029 199  GLU A CB  
1336  N N   . THR A 202  ? 0.2881 0.3178 0.2772 -0.0117 0.0006  0.0016  200  THR A N   
1337  C CA  . THR A 202  ? 0.2822 0.3099 0.2716 -0.0125 -0.0002 0.0059  200  THR A CA  
1338  C C   . THR A 202  ? 0.2819 0.3069 0.2740 -0.0117 -0.0006 0.0042  200  THR A C   
1339  O O   . THR A 202  ? 0.2564 0.2830 0.2500 -0.0109 -0.0007 -0.0002 200  THR A O   
1340  C CB  . THR A 202  ? 0.2783 0.3141 0.2656 -0.0145 -0.0013 0.0083  200  THR A CB  
1341  O OG1 . THR A 202  ? 0.3229 0.3656 0.3102 -0.0147 -0.0018 0.0044  200  THR A OG1 
1342  C CG2 . THR A 202  ? 0.2991 0.3390 0.2840 -0.0157 -0.0010 0.0103  200  THR A CG2 
1343  N N   . ILE A 203  ? 0.2681 0.2892 0.2612 -0.0118 -0.0011 0.0076  201  ILE A N   
1344  C CA  . ILE A 203  ? 0.2641 0.2826 0.2600 -0.0111 -0.0015 0.0064  201  ILE A CA  
1345  C C   . ILE A 203  ? 0.2841 0.3096 0.2802 -0.0119 -0.0026 0.0039  201  ILE A C   
1346  O O   . ILE A 203  ? 0.2652 0.2900 0.2638 -0.0111 -0.0029 0.0005  201  ILE A O   
1347  C CB  . ILE A 203  ? 0.2685 0.2820 0.2657 -0.0110 -0.0016 0.0105  201  ILE A CB  
1348  C CG1 . ILE A 203  ? 0.2423 0.2527 0.2427 -0.0101 -0.0018 0.0091  201  ILE A CG1 
1349  C CG2 . ILE A 203  ? 0.2767 0.2942 0.2726 -0.0126 -0.0029 0.0142  201  ILE A CG2 
1350  C CD1 . ILE A 203  ? 0.2302 0.2366 0.2327 -0.0086 -0.0008 0.0061  201  ILE A CD1 
1351  N N   . ARG A 204  ? 0.2643 0.2969 0.2578 -0.0135 -0.0034 0.0055  202  ARG A N   
1352  C CA  . ARG A 204  ? 0.2705 0.3111 0.2638 -0.0143 -0.0045 0.0029  202  ARG A CA  
1353  C C   . ARG A 204  ? 0.2720 0.3160 0.2659 -0.0134 -0.0043 -0.0031 202  ARG A C   
1354  O O   . ARG A 204  ? 0.2817 0.3281 0.2777 -0.0129 -0.0051 -0.0070 202  ARG A O   
1355  C CB  . ARG A 204  ? 0.3460 0.3944 0.3362 -0.0163 -0.0054 0.0063  202  ARG A CB  
1356  C CG  . ARG A 204  ? 0.4488 0.4967 0.4396 -0.0173 -0.0066 0.0108  202  ARG A CG  
1357  C CD  . ARG A 204  ? 0.4846 0.5370 0.4732 -0.0193 -0.0073 0.0161  202  ARG A CD  
1358  N NE  . ARG A 204  ? 0.4962 0.5459 0.4863 -0.0200 -0.0085 0.0207  202  ARG A NE  
1359  C CZ  . ARG A 204  ? 0.4900 0.5311 0.4823 -0.0191 -0.0083 0.0232  202  ARG A CZ  
1360  N NH1 . ARG A 204  ? 0.3521 0.3865 0.3449 -0.0176 -0.0068 0.0219  202  ARG A NH1 
1361  N NH2 . ARG A 204  ? 0.4257 0.4653 0.4199 -0.0196 -0.0096 0.0269  202  ARG A NH2 
1362  N N   . GLU A 205  ? 0.2775 0.3220 0.2699 -0.0130 -0.0033 -0.0043 203  GLU A N   
1363  C CA  . GLU A 205  ? 0.2987 0.3461 0.2922 -0.0120 -0.0031 -0.0102 203  GLU A CA  
1364  C C   . GLU A 205  ? 0.2497 0.2896 0.2476 -0.0102 -0.0031 -0.0131 203  GLU A C   
1365  O O   . GLU A 205  ? 0.2884 0.3306 0.2891 -0.0095 -0.0039 -0.0181 203  GLU A O   
1366  C CB  . GLU A 205  ? 0.3046 0.3536 0.2958 -0.0120 -0.0020 -0.0103 203  GLU A CB  
1367  C CG  . GLU A 205  ? 0.3425 0.3949 0.3352 -0.0108 -0.0019 -0.0166 203  GLU A CG  
1368  C CD  . GLU A 205  ? 0.4277 0.4830 0.4179 -0.0110 -0.0008 -0.0166 203  GLU A CD  
1369  O OE1 . GLU A 205  ? 0.4029 0.4512 0.3933 -0.0103 0.0001  -0.0146 203  GLU A OE1 
1370  O OE2 . GLU A 205  ? 0.4648 0.5300 0.4529 -0.0117 -0.0010 -0.0185 203  GLU A OE2 
1371  N N   . ALA A 206  ? 0.2553 0.2866 0.2542 -0.0096 -0.0022 -0.0098 204  ALA A N   
1372  C CA  . ALA A 206  ? 0.2545 0.2790 0.2577 -0.0082 -0.0022 -0.0116 204  ALA A CA  
1373  C C   . ALA A 206  ? 0.2570 0.2819 0.2633 -0.0083 -0.0034 -0.0127 204  ALA A C   
1374  O O   . ALA A 206  ? 0.2689 0.2923 0.2793 -0.0073 -0.0041 -0.0165 204  ALA A O   
1375  C CB  . ALA A 206  ? 0.2673 0.2839 0.2704 -0.0077 -0.0010 -0.0074 204  ALA A CB  
1376  N N   . LEU A 207  ? 0.2423 0.2691 0.2470 -0.0094 -0.0040 -0.0095 205  LEU A N   
1377  C CA  . LEU A 207  ? 0.2463 0.2736 0.2539 -0.0095 -0.0052 -0.0104 205  LEU A CA  
1378  C C   . LEU A 207  ? 0.2867 0.3213 0.2953 -0.0096 -0.0066 -0.0159 205  LEU A C   
1379  O O   . LEU A 207  ? 0.3057 0.3394 0.3186 -0.0090 -0.0077 -0.0190 205  LEU A O   
1380  C CB  . LEU A 207  ? 0.2785 0.3066 0.2842 -0.0107 -0.0056 -0.0057 205  LEU A CB  
1381  C CG  . LEU A 207  ? 0.2590 0.2796 0.2653 -0.0103 -0.0046 -0.0012 205  LEU A CG  
1382  C CD1 . LEU A 207  ? 0.2689 0.2911 0.2731 -0.0115 -0.0051 0.0034  205  LEU A CD1 
1383  C CD2 . LEU A 207  ? 0.2670 0.2823 0.2779 -0.0093 -0.0048 -0.0019 205  LEU A CD2 
1384  N N   . LYS A 208  ? 0.2683 0.3106 0.2733 -0.0103 -0.0066 -0.0172 206  LYS A N   
1385  C CA  . LYS A 208  ? 0.3061 0.3566 0.3121 -0.0102 -0.0078 -0.0230 206  LYS A CA  
1386  C C   . LYS A 208  ? 0.3250 0.3727 0.3354 -0.0085 -0.0081 -0.0286 206  LYS A C   
1387  O O   . LYS A 208  ? 0.3453 0.3952 0.3596 -0.0079 -0.0096 -0.0334 206  LYS A O   
1388  C CB  . LYS A 208  ? 0.3549 0.4149 0.3560 -0.0113 -0.0076 -0.0231 206  LYS A CB  
1389  C CG  . LYS A 208  ? 0.4227 0.4880 0.4203 -0.0131 -0.0081 -0.0186 206  LYS A CG  
1390  C CD  . LYS A 208  ? 0.4325 0.5086 0.4257 -0.0144 -0.0080 -0.0186 206  LYS A CD  
1391  C CE  . LYS A 208  ? 0.4627 0.5437 0.4529 -0.0164 -0.0087 -0.0130 206  LYS A CE  
1392  N NZ  . LYS A 208  ? 0.6404 0.7328 0.6264 -0.0179 -0.0087 -0.0122 206  LYS A NZ  
1393  N N   . ARG A 209  ? 0.2949 0.3376 0.3054 -0.0077 -0.0068 -0.0278 207  ARG A N   
1394  C CA  . ARG A 209  ? 0.3037 0.3435 0.3188 -0.0062 -0.0071 -0.0326 207  ARG A CA  
1395  C C   . ARG A 209  ? 0.3116 0.3433 0.3324 -0.0054 -0.0078 -0.0322 207  ARG A C   
1396  O O   . ARG A 209  ? 0.3453 0.3746 0.3711 -0.0042 -0.0086 -0.0362 207  ARG A O   
1397  C CB  . ARG A 209  ? 0.3183 0.3557 0.3313 -0.0057 -0.0056 -0.0316 207  ARG A CB  
1398  C CG  . ARG A 209  ? 0.3358 0.3819 0.3441 -0.0064 -0.0051 -0.0326 207  ARG A CG  
1399  C CD  . ARG A 209  ? 0.3439 0.3875 0.3506 -0.0059 -0.0036 -0.0316 207  ARG A CD  
1400  N NE  . ARG A 209  ? 0.3934 0.4458 0.3958 -0.0067 -0.0031 -0.0323 207  ARG A NE  
1401  C CZ  . ARG A 209  ? 0.4306 0.4825 0.4304 -0.0068 -0.0018 -0.0305 207  ARG A CZ  
1402  N NH1 . ARG A 209  ? 0.3839 0.4272 0.3848 -0.0061 -0.0009 -0.0281 207  ARG A NH1 
1403  N NH2 . ARG A 209  ? 0.4855 0.5464 0.4818 -0.0077 -0.0015 -0.0312 207  ARG A NH2 
1404  N N   . SER A 210  ? 0.2947 0.3223 0.3152 -0.0061 -0.0076 -0.0275 208  SER A N   
1405  C CA  . SER A 210  ? 0.2709 0.2914 0.2968 -0.0055 -0.0080 -0.0266 208  SER A CA  
1406  C C   . SER A 210  ? 0.2989 0.3217 0.3296 -0.0055 -0.0101 -0.0301 208  SER A C   
1407  O O   . SER A 210  ? 0.2927 0.3104 0.3291 -0.0050 -0.0109 -0.0304 208  SER A O   
1408  C CB  . SER A 210  ? 0.2761 0.2916 0.3000 -0.0060 -0.0068 -0.0201 208  SER A CB  
1409  O OG  . SER A 210  ? 0.3016 0.3143 0.3221 -0.0058 -0.0051 -0.0172 208  SER A OG  
1410  N N   . LYS A 211  ? 0.3399 0.3706 0.3685 -0.0062 -0.0111 -0.0327 209  LYS A N   
1411  C CA  . LYS A 211  ? 0.3464 0.3795 0.3790 -0.0063 -0.0132 -0.0359 209  LYS A CA  
1412  C C   . LYS A 211  ? 0.3215 0.3533 0.3613 -0.0050 -0.0149 -0.0418 209  LYS A C   
1413  O O   . LYS A 211  ? 0.3449 0.3740 0.3906 -0.0049 -0.0165 -0.0429 209  LYS A O   
1414  C CB  . LYS A 211  ? 0.4122 0.4551 0.4407 -0.0072 -0.0139 -0.0378 209  LYS A CB  
1415  C CG  . LYS A 211  ? 0.4512 0.4955 0.4735 -0.0085 -0.0126 -0.0316 209  LYS A CG  
1416  C CD  . LYS A 211  ? 0.5502 0.6052 0.5683 -0.0096 -0.0133 -0.0331 209  LYS A CD  
1417  C CE  . LYS A 211  ? 0.5949 0.6507 0.6084 -0.0111 -0.0127 -0.0265 209  LYS A CE  
1418  N NZ  . LYS A 211  ? 0.6342 0.6831 0.6505 -0.0112 -0.0129 -0.0229 209  LYS A NZ  
1419  N N   . GLU A 212  ? 0.3242 0.3579 0.3642 -0.0041 -0.0147 -0.0456 210  GLU A N   
1420  C CA  . GLU A 212  ? 0.3726 0.4056 0.4199 -0.0027 -0.0167 -0.0519 210  GLU A CA  
1421  C C   . GLU A 212  ? 0.3454 0.3691 0.3994 -0.0024 -0.0172 -0.0494 210  GLU A C   
1422  O O   . GLU A 212  ? 0.3599 0.3822 0.4210 -0.0020 -0.0194 -0.0523 210  GLU A O   
1423  C CB  . GLU A 212  ? 0.4025 0.4387 0.4485 -0.0018 -0.0161 -0.0556 210  GLU A CB  
1424  C CG  . GLU A 212  ? 0.5232 0.5580 0.5774 -0.0002 -0.0182 -0.0619 210  GLU A CG  
1425  C CD  . GLU A 212  ? 0.5906 0.6275 0.6436 0.0009  -0.0174 -0.0648 210  GLU A CD  
1426  O OE1 . GLU A 212  ? 0.6391 0.6794 0.6847 0.0002  -0.0153 -0.0622 210  GLU A OE1 
1427  O OE2 . GLU A 212  ? 0.6796 0.7147 0.7395 0.0023  -0.0190 -0.0697 210  GLU A OE2 
1428  N N   . LEU A 213  ? 0.3221 0.3396 0.3741 -0.0024 -0.0152 -0.0440 211  LEU A N   
1429  C CA  . LEU A 213  ? 0.3194 0.3289 0.3775 -0.0022 -0.0156 -0.0411 211  LEU A CA  
1430  C C   . LEU A 213  ? 0.3288 0.3357 0.3878 -0.0032 -0.0156 -0.0367 211  LEU A C   
1431  O O   . LEU A 213  ? 0.3082 0.3106 0.3740 -0.0032 -0.0169 -0.0359 211  LEU A O   
1432  C CB  . LEU A 213  ? 0.2748 0.2794 0.3307 -0.0018 -0.0136 -0.0372 211  LEU A CB  
1433  C CG  . LEU A 213  ? 0.3329 0.3388 0.3906 -0.0007 -0.0141 -0.0419 211  LEU A CG  
1434  C CD1 . LEU A 213  ? 0.3953 0.3963 0.4512 -0.0003 -0.0123 -0.0381 211  LEU A CD1 
1435  C CD2 . LEU A 213  ? 0.4080 0.4130 0.4753 0.0002  -0.0170 -0.0471 211  LEU A CD2 
1436  N N   . GLU A 214  ? 0.2822 0.2921 0.3349 -0.0041 -0.0145 -0.0338 212  GLU A N   
1437  C CA  . GLU A 214  ? 0.3172 0.3252 0.3713 -0.0049 -0.0147 -0.0303 212  GLU A CA  
1438  C C   . GLU A 214  ? 0.3561 0.3662 0.4167 -0.0050 -0.0175 -0.0347 212  GLU A C   
1439  O O   . GLU A 214  ? 0.3320 0.3385 0.3977 -0.0053 -0.0183 -0.0327 212  GLU A O   
1440  C CB  . GLU A 214  ? 0.2785 0.2896 0.3253 -0.0059 -0.0134 -0.0268 212  GLU A CB  
1441  C CG  . GLU A 214  ? 0.2891 0.2965 0.3311 -0.0059 -0.0109 -0.0214 212  GLU A CG  
1442  C CD  . GLU A 214  ? 0.3367 0.3468 0.3726 -0.0068 -0.0100 -0.0178 212  GLU A CD  
1443  O OE1 . GLU A 214  ? 0.3883 0.4044 0.4226 -0.0075 -0.0110 -0.0198 212  GLU A OE1 
1444  O OE2 . GLU A 214  ? 0.3643 0.3708 0.3975 -0.0068 -0.0083 -0.0131 212  GLU A OE2 
1445  N N   . GLU A 215  ? 0.3137 0.3300 0.3744 -0.0046 -0.0189 -0.0410 213  GLU A N   
1446  C CA  . GLU A 215  ? 0.3870 0.4059 0.4540 -0.0044 -0.0218 -0.0462 213  GLU A CA  
1447  C C   . GLU A 215  ? 0.4180 0.4314 0.4948 -0.0037 -0.0237 -0.0480 213  GLU A C   
1448  O O   . GLU A 215  ? 0.4728 0.4859 0.5563 -0.0039 -0.0260 -0.0502 213  GLU A O   
1449  C CB  . GLU A 215  ? 0.3956 0.4234 0.4604 -0.0040 -0.0229 -0.0529 213  GLU A CB  
1450  N N   . LYS A 216  ? 0.3686 0.3775 0.4465 -0.0031 -0.0228 -0.0468 214  LYS A N   
1451  C CA  . LYS A 216  ? 0.3764 0.3796 0.4637 -0.0025 -0.0245 -0.0476 214  LYS A CA  
1452  C C   . LYS A 216  ? 0.3888 0.3854 0.4786 -0.0033 -0.0236 -0.0403 214  LYS A C   
1453  O O   . LYS A 216  ? 0.4288 0.4208 0.5270 -0.0032 -0.0253 -0.0399 214  LYS A O   
1454  C CB  . LYS A 216  ? 0.3601 0.3626 0.4482 -0.0013 -0.0244 -0.0503 214  LYS A CB  
1455  C CG  . LYS A 216  ? 0.4109 0.4207 0.4979 -0.0004 -0.0255 -0.0581 214  LYS A CG  
1456  C CD  . LYS A 216  ? 0.5668 0.5760 0.6542 0.0009  -0.0251 -0.0606 214  LYS A CD  
1457  C CE  . LYS A 216  ? 0.5835 0.6014 0.6681 0.0018  -0.0256 -0.0679 214  LYS A CE  
1458  N NZ  . LYS A 216  ? 0.5963 0.6184 0.6873 0.0023  -0.0288 -0.0749 214  LYS A NZ  
1459  N N   . GLY A 217  ? 0.3134 0.3096 0.3964 -0.0041 -0.0212 -0.0346 215  GLY A N   
1460  C CA  . GLY A 217  ? 0.3203 0.3113 0.4051 -0.0048 -0.0201 -0.0280 215  GLY A CA  
1461  C C   . GLY A 217  ? 0.3224 0.3106 0.4015 -0.0047 -0.0172 -0.0229 215  GLY A C   
1462  O O   . GLY A 217  ? 0.3315 0.3161 0.4119 -0.0051 -0.0162 -0.0174 215  GLY A O   
1463  N N   . PHE A 218  ? 0.2915 0.2816 0.3646 -0.0040 -0.0159 -0.0245 216  PHE A N   
1464  C CA  . PHE A 218  ? 0.2468 0.2347 0.3141 -0.0039 -0.0132 -0.0198 216  PHE A CA  
1465  C C   . PHE A 218  ? 0.2881 0.2778 0.3484 -0.0045 -0.0114 -0.0164 216  PHE A C   
1466  O O   . PHE A 218  ? 0.2845 0.2782 0.3432 -0.0051 -0.0122 -0.0181 216  PHE A O   
1467  C CB  . PHE A 218  ? 0.2399 0.2293 0.3035 -0.0031 -0.0125 -0.0227 216  PHE A CB  
1468  C CG  . PHE A 218  ? 0.2813 0.2681 0.3514 -0.0023 -0.0139 -0.0252 216  PHE A CG  
1469  C CD1 . PHE A 218  ? 0.3237 0.3125 0.4000 -0.0018 -0.0166 -0.0313 216  PHE A CD1 
1470  C CD2 . PHE A 218  ? 0.2847 0.2674 0.3550 -0.0019 -0.0127 -0.0217 216  PHE A CD2 
1471  C CE1 . PHE A 218  ? 0.3394 0.3256 0.4224 -0.0010 -0.0182 -0.0337 216  PHE A CE1 
1472  C CE2 . PHE A 218  ? 0.3048 0.2850 0.3814 -0.0012 -0.0142 -0.0237 216  PHE A CE2 
1473  C CZ  . PHE A 218  ? 0.3038 0.2857 0.3871 -0.0008 -0.0170 -0.0297 216  PHE A CZ  
1474  N N   . SER A 219  ? 0.2589 0.2459 0.3154 -0.0045 -0.0092 -0.0116 217  SER A N   
1475  C CA  . SER A 219  ? 0.2352 0.2237 0.2850 -0.0048 -0.0075 -0.0085 217  SER A CA  
1476  C C   . SER A 219  ? 0.2378 0.2256 0.2821 -0.0043 -0.0057 -0.0074 217  SER A C   
1477  O O   . SER A 219  ? 0.2123 0.1986 0.2580 -0.0037 -0.0057 -0.0089 217  SER A O   
1478  C CB  . SER A 219  ? 0.2684 0.2545 0.3194 -0.0052 -0.0068 -0.0037 217  SER A CB  
1479  O OG  . SER A 219  ? 0.2868 0.2691 0.3399 -0.0047 -0.0057 -0.0006 217  SER A OG  
1480  N N   . TYR A 220  ? 0.2235 0.2122 0.2619 -0.0045 -0.0043 -0.0047 218  TYR A N   
1481  C CA  . TYR A 220  ? 0.2261 0.2147 0.2593 -0.0042 -0.0028 -0.0038 218  TYR A CA  
1482  C C   . TYR A 220  ? 0.2149 0.2012 0.2451 -0.0040 -0.0011 0.0008  218  TYR A C   
1483  O O   . TYR A 220  ? 0.2289 0.2155 0.2593 -0.0044 -0.0012 0.0029  218  TYR A O   
1484  C CB  . TYR A 220  ? 0.2251 0.2187 0.2539 -0.0047 -0.0031 -0.0062 218  TYR A CB  
1485  C CG  . TYR A 220  ? 0.2170 0.2131 0.2475 -0.0044 -0.0042 -0.0112 218  TYR A CG  
1486  C CD1 . TYR A 220  ? 0.2685 0.2672 0.3032 -0.0045 -0.0061 -0.0151 218  TYR A CD1 
1487  C CD2 . TYR A 220  ? 0.2252 0.2213 0.2536 -0.0038 -0.0034 -0.0124 218  TYR A CD2 
1488  C CE1 . TYR A 220  ? 0.2779 0.2793 0.3148 -0.0040 -0.0073 -0.0203 218  TYR A CE1 
1489  C CE2 . TYR A 220  ? 0.2496 0.2483 0.2801 -0.0034 -0.0045 -0.0173 218  TYR A CE2 
1490  C CZ  . TYR A 220  ? 0.2664 0.2678 0.3011 -0.0034 -0.0064 -0.0214 218  TYR A CZ  
1491  O OH  . TYR A 220  ? 0.2778 0.2822 0.3150 -0.0028 -0.0076 -0.0268 218  TYR A OH  
1492  N N   . SER A 221  ? 0.2020 0.1863 0.2297 -0.0034 0.0002  0.0021  219  SER A N   
1493  C CA  . SER A 221  ? 0.2091 0.1920 0.2331 -0.0031 0.0017  0.0056  219  SER A CA  
1494  C C   . SER A 221  ? 0.2180 0.2019 0.2374 -0.0031 0.0023  0.0048  219  SER A C   
1495  O O   . SER A 221  ? 0.2629 0.2459 0.2823 -0.0026 0.0026  0.0034  219  SER A O   
1496  C CB  . SER A 221  ? 0.2210 0.2006 0.2470 -0.0024 0.0028  0.0082  219  SER A CB  
1497  O OG  . SER A 221  ? 0.2498 0.2286 0.2723 -0.0019 0.0041  0.0109  219  SER A OG  
1498  N N   . TYR A 222  ? 0.1886 0.1745 0.2045 -0.0036 0.0023  0.0059  220  TYR A N   
1499  C CA  . TYR A 222  ? 0.2121 0.1996 0.2239 -0.0039 0.0025  0.0054  220  TYR A CA  
1500  C C   . TYR A 222  ? 0.2354 0.2200 0.2450 -0.0032 0.0038  0.0079  220  TYR A C   
1501  O O   . TYR A 222  ? 0.2371 0.2201 0.2468 -0.0029 0.0042  0.0104  220  TYR A O   
1502  C CB  . TYR A 222  ? 0.2168 0.2087 0.2264 -0.0050 0.0016  0.0054  220  TYR A CB  
1503  C CG  . TYR A 222  ? 0.2053 0.2010 0.2168 -0.0056 0.0003  0.0023  220  TYR A CG  
1504  C CD1 . TYR A 222  ? 0.2107 0.2094 0.2219 -0.0057 -0.0001 -0.0014 220  TYR A CD1 
1505  C CD2 . TYR A 222  ? 0.2065 0.2028 0.2204 -0.0060 -0.0006 0.0026  220  TYR A CD2 
1506  C CE1 . TYR A 222  ? 0.2362 0.2388 0.2496 -0.0060 -0.0014 -0.0049 220  TYR A CE1 
1507  C CE2 . TYR A 222  ? 0.2318 0.2316 0.2477 -0.0064 -0.0019 -0.0006 220  TYR A CE2 
1508  C CZ  . TYR A 222  ? 0.2392 0.2422 0.2549 -0.0064 -0.0024 -0.0045 220  TYR A CZ  
1509  O OH  . TYR A 222  ? 0.2597 0.2666 0.2778 -0.0067 -0.0038 -0.0082 220  TYR A OH  
1510  N N   . ASP A 223  ? 0.2559 0.2403 0.2636 -0.0029 0.0043  0.0068  221  ASP A N   
1511  C CA  . ASP A 223  ? 0.2795 0.2615 0.2851 -0.0023 0.0054  0.0086  221  ASP A CA  
1512  C C   . ASP A 223  ? 0.3058 0.2902 0.3080 -0.0031 0.0051  0.0087  221  ASP A C   
1513  O O   . ASP A 223  ? 0.2917 0.2783 0.2929 -0.0034 0.0050  0.0065  221  ASP A O   
1514  C CB  . ASP A 223  ? 0.2872 0.2670 0.2940 -0.0013 0.0061  0.0076  221  ASP A CB  
1515  C CG  . ASP A 223  ? 0.3654 0.3433 0.3696 -0.0007 0.0070  0.0087  221  ASP A CG  
1516  O OD1 . ASP A 223  ? 0.3917 0.3691 0.3942 -0.0006 0.0072  0.0106  221  ASP A OD1 
1517  O OD2 . ASP A 223  ? 0.4579 0.4350 0.4623 -0.0002 0.0074  0.0075  221  ASP A OD2 
1518  N N   . MET A 224  ? 0.3062 0.2903 0.3070 -0.0034 0.0049  0.0111  222  MET A N   
1519  C CA  . MET A 224  ? 0.2968 0.2832 0.2950 -0.0043 0.0044  0.0121  222  MET A CA  
1520  C C   . MET A 224  ? 0.3479 0.3324 0.3445 -0.0037 0.0052  0.0121  222  MET A C   
1521  O O   . MET A 224  ? 0.4062 0.3921 0.4010 -0.0046 0.0048  0.0132  222  MET A O   
1522  C CB  . MET A 224  ? 0.3169 0.3035 0.3152 -0.0049 0.0035  0.0149  222  MET A CB  
1523  C CG  . MET A 224  ? 0.3154 0.3045 0.3151 -0.0057 0.0026  0.0150  222  MET A CG  
1524  S SD  . MET A 224  ? 0.3872 0.3823 0.3859 -0.0069 0.0020  0.0123  222  MET A SD  
1525  C CE  . MET A 224  ? 0.4310 0.4302 0.4267 -0.0085 0.0013  0.0143  222  MET A CE  
1526  N N   . LEU A 225  ? 0.3812 0.3627 0.3787 -0.0025 0.0062  0.0111  223  LEU A N   
1527  C CA  . LEU A 225  ? 0.4084 0.3883 0.4046 -0.0018 0.0070  0.0106  223  LEU A CA  
1528  C C   . LEU A 225  ? 0.4208 0.3985 0.4159 -0.0013 0.0071  0.0126  223  LEU A C   
1529  O O   . LEU A 225  ? 0.4444 0.4211 0.4383 -0.0009 0.0075  0.0123  223  LEU A O   
1530  C CB  . LEU A 225  ? 0.4063 0.3894 0.4011 -0.0026 0.0068  0.0087  223  LEU A CB  
1531  C CG  . LEU A 225  ? 0.3771 0.3618 0.3735 -0.0024 0.0067  0.0057  223  LEU A CG  
1532  C CD1 . LEU A 225  ? 0.4204 0.4096 0.4154 -0.0032 0.0065  0.0036  223  LEU A CD1 
1533  C CD2 . LEU A 225  ? 0.3888 0.3700 0.3872 -0.0011 0.0074  0.0049  223  LEU A CD2 
1534  N N   . GLY A 226  ? 0.3582 0.3351 0.3542 -0.0013 0.0065  0.0144  224  GLY A N   
1535  C CA  . GLY A 226  ? 0.4108 0.3855 0.4067 -0.0006 0.0065  0.0157  224  GLY A CA  
1536  C C   . GLY A 226  ? 0.3955 0.3676 0.3918 0.0012  0.0077  0.0151  224  GLY A C   
1537  O O   . GLY A 226  ? 0.3338 0.3058 0.3315 0.0018  0.0084  0.0147  224  GLY A O   
1538  N N   . GLU A 227  ? 0.3466 0.3173 0.3420 0.0019  0.0078  0.0151  225  GLU A N   
1539  C CA  . GLU A 227  ? 0.3033 0.2725 0.2987 0.0035  0.0089  0.0145  225  GLU A CA  
1540  C C   . GLU A 227  ? 0.2991 0.2671 0.2938 0.0042  0.0087  0.0143  225  GLU A C   
1541  O O   . GLU A 227  ? 0.2864 0.2545 0.2800 0.0033  0.0079  0.0144  225  GLU A O   
1542  C CB  . GLU A 227  ? 0.3776 0.3471 0.3725 0.0035  0.0098  0.0134  225  GLU A CB  
1543  C CG  . GLU A 227  ? 0.4004 0.3690 0.3955 0.0050  0.0108  0.0133  225  GLU A CG  
1544  C CD  . GLU A 227  ? 0.4647 0.4335 0.4603 0.0048  0.0113  0.0127  225  GLU A CD  
1545  O OE1 . GLU A 227  ? 0.4022 0.3719 0.3984 0.0038  0.0108  0.0118  225  GLU A OE1 
1546  O OE2 . GLU A 227  ? 0.5018 0.4703 0.4976 0.0058  0.0121  0.0129  225  GLU A OE2 
1547  N N   . ALA A 228  ? 0.2925 0.2596 0.2877 0.0058  0.0092  0.0141  226  ALA A N   
1548  C CA  . ALA A 228  ? 0.2807 0.2468 0.2752 0.0068  0.0090  0.0133  226  ALA A CA  
1549  C C   . ALA A 228  ? 0.2476 0.2129 0.2429 0.0060  0.0073  0.0138  226  ALA A C   
1550  O O   . ALA A 228  ? 0.2933 0.2584 0.2877 0.0054  0.0068  0.0137  226  ALA A O   
1551  C CB  . ALA A 228  ? 0.3323 0.2985 0.3250 0.0070  0.0098  0.0125  226  ALA A CB  
1552  N N   . ALA A 229  ? 0.2413 0.2065 0.2388 0.0060  0.0063  0.0146  227  ALA A N   
1553  C CA  . ALA A 229  ? 0.2552 0.2195 0.2544 0.0053  0.0044  0.0155  227  ALA A CA  
1554  C C   . ALA A 229  ? 0.2570 0.2198 0.2566 0.0066  0.0039  0.0141  227  ALA A C   
1555  O O   . ALA A 229  ? 0.2464 0.2091 0.2463 0.0085  0.0046  0.0124  227  ALA A O   
1556  C CB  . ALA A 229  ? 0.2509 0.2151 0.2530 0.0054  0.0032  0.0164  227  ALA A CB  
1557  N N   . THR A 230  ? 0.2471 0.2093 0.2471 0.0054  0.0025  0.0148  228  THR A N   
1558  C CA  . THR A 230  ? 0.2601 0.2208 0.2611 0.0064  0.0017  0.0136  228  THR A CA  
1559  C C   . THR A 230  ? 0.2417 0.2008 0.2470 0.0066  -0.0007 0.0140  228  THR A C   
1560  O O   . THR A 230  ? 0.2445 0.2023 0.2517 0.0082  -0.0015 0.0121  228  THR A O   
1561  C CB  . THR A 230  ? 0.2754 0.2363 0.2745 0.0050  0.0016  0.0141  228  THR A CB  
1562  O OG1 . THR A 230  ? 0.3827 0.3450 0.3785 0.0049  0.0036  0.0135  228  THR A OG1 
1563  C CG2 . THR A 230  ? 0.3415 0.3010 0.3417 0.0060  0.0007  0.0126  228  THR A CG2 
1564  N N   . THR A 231  ? 0.2448 0.2042 0.2520 0.0050  -0.0020 0.0164  229  THR A N   
1565  C CA  . THR A 231  ? 0.2191 0.1770 0.2312 0.0048  -0.0047 0.0175  229  THR A CA  
1566  C C   . THR A 231  ? 0.2216 0.1800 0.2354 0.0047  -0.0051 0.0187  229  THR A C   
1567  O O   . THR A 231  ? 0.2368 0.1970 0.2480 0.0042  -0.0035 0.0193  229  THR A O   
1568  C CB  . THR A 231  ? 0.2593 0.2173 0.2725 0.0023  -0.0066 0.0204  229  THR A CB  
1569  O OG1 . THR A 231  ? 0.2557 0.2163 0.2671 0.0002  -0.0062 0.0231  229  THR A OG1 
1570  C CG2 . THR A 231  ? 0.2627 0.2207 0.2737 0.0021  -0.0060 0.0195  229  THR A CG2 
1571  N N   . ALA A 232  ? 0.2176 0.1744 0.2365 0.0053  -0.0075 0.0190  230  ALA A N   
1572  C CA  . ALA A 232  ? 0.2350 0.1923 0.2563 0.0049  -0.0084 0.0207  230  ALA A CA  
1573  C C   . ALA A 232  ? 0.2618 0.2212 0.2815 0.0020  -0.0086 0.0243  230  ALA A C   
1574  O O   . ALA A 232  ? 0.2672 0.2283 0.2858 0.0015  -0.0079 0.0252  230  ALA A O   
1575  C CB  . ALA A 232  ? 0.2786 0.2336 0.3064 0.0056  -0.0114 0.0207  230  ALA A CB  
1576  N N   . ALA A 233  ? 0.2539 0.2138 0.2733 0.0000  -0.0097 0.0265  231  ALA A N   
1577  C CA  . ALA A 233  ? 0.3063 0.2694 0.3241 -0.0027 -0.0100 0.0299  231  ALA A CA  
1578  C C   . ALA A 233  ? 0.2846 0.2502 0.2969 -0.0029 -0.0072 0.0287  231  ALA A C   
1579  O O   . ALA A 233  ? 0.2875 0.2559 0.2987 -0.0043 -0.0070 0.0303  231  ALA A O   
1580  C CB  . ALA A 233  ? 0.3009 0.2648 0.3194 -0.0048 -0.0115 0.0324  231  ALA A CB  
1581  N N   . ASP A 234  ? 0.2546 0.2196 0.2640 -0.0016 -0.0051 0.0258  232  ASP A N   
1582  C CA  . ASP A 234  ? 0.2843 0.2513 0.2895 -0.0016 -0.0027 0.0245  232  ASP A CA  
1583  C C   . ASP A 234  ? 0.2683 0.2354 0.2740 -0.0007 -0.0019 0.0238  232  ASP A C   
1584  O O   . ASP A 234  ? 0.2639 0.2333 0.2679 -0.0016 -0.0012 0.0242  232  ASP A O   
1585  C CB  . ASP A 234  ? 0.3148 0.2805 0.3176 -0.0001 -0.0009 0.0217  232  ASP A CB  
1586  C CG  . ASP A 234  ? 0.4036 0.3697 0.4051 -0.0010 -0.0011 0.0219  232  ASP A CG  
1587  O OD1 . ASP A 234  ? 0.3855 0.3539 0.3869 -0.0032 -0.0021 0.0241  232  ASP A OD1 
1588  O OD2 . ASP A 234  ? 0.4075 0.3721 0.4082 0.0004  -0.0002 0.0198  232  ASP A OD2 
1589  N N   . ALA A 235  ? 0.2540 0.2188 0.2621 0.0013  -0.0021 0.0225  233  ALA A N   
1590  C CA  . ALA A 235  ? 0.2324 0.1976 0.2413 0.0024  -0.0013 0.0219  233  ALA A CA  
1591  C C   . ALA A 235  ? 0.2638 0.2304 0.2744 0.0008  -0.0028 0.0244  233  ALA A C   
1592  O O   . ALA A 235  ? 0.2434 0.2115 0.2532 0.0006  -0.0020 0.0245  233  ALA A O   
1593  C CB  . ALA A 235  ? 0.2451 0.2084 0.2565 0.0048  -0.0014 0.0200  233  ALA A CB  
1594  N N   . GLU A 236  ? 0.2491 0.2153 0.2626 -0.0003 -0.0052 0.0267  234  GLU A N   
1595  C CA  . GLU A 236  ? 0.2585 0.2264 0.2737 -0.0020 -0.0068 0.0296  234  GLU A CA  
1596  C C   . GLU A 236  ? 0.2318 0.2036 0.2434 -0.0041 -0.0061 0.0308  234  GLU A C   
1597  O O   . GLU A 236  ? 0.2551 0.2291 0.2665 -0.0049 -0.0062 0.0317  234  GLU A O   
1598  C CB  . GLU A 236  ? 0.2952 0.2621 0.3147 -0.0029 -0.0098 0.0323  234  GLU A CB  
1599  C CG  . GLU A 236  ? 0.3828 0.3464 0.4072 -0.0008 -0.0112 0.0310  234  GLU A CG  
1600  C CD  . GLU A 236  ? 0.5289 0.4904 0.5576 -0.0012 -0.0139 0.0324  234  GLU A CD  
1601  O OE1 . GLU A 236  ? 0.5561 0.5192 0.5847 -0.0037 -0.0152 0.0357  234  GLU A OE1 
1602  O OE2 . GLU A 236  ? 0.5725 0.5312 0.6051 0.0009  -0.0149 0.0303  234  GLU A OE2 
1603  N N   . ARG A 237  ? 0.2322 0.2050 0.2409 -0.0049 -0.0054 0.0305  235  ARG A N   
1604  C CA  . ARG A 237  ? 0.2712 0.2482 0.2766 -0.0067 -0.0046 0.0309  235  ARG A CA  
1605  C C   . ARG A 237  ? 0.2741 0.2518 0.2774 -0.0058 -0.0026 0.0284  235  ARG A C   
1606  O O   . ARG A 237  ? 0.2457 0.2266 0.2481 -0.0069 -0.0026 0.0287  235  ARG A O   
1607  C CB  . ARG A 237  ? 0.2846 0.2628 0.2878 -0.0075 -0.0042 0.0307  235  ARG A CB  
1608  C CG  . ARG A 237  ? 0.3673 0.3505 0.3672 -0.0092 -0.0034 0.0306  235  ARG A CG  
1609  C CD  . ARG A 237  ? 0.4409 0.4261 0.4395 -0.0103 -0.0035 0.0312  235  ARG A CD  
1610  N NE  . ARG A 237  ? 0.5326 0.5138 0.5308 -0.0086 -0.0025 0.0290  235  ARG A NE  
1611  C CZ  . ARG A 237  ? 0.5315 0.5124 0.5271 -0.0076 -0.0005 0.0260  235  ARG A CZ  
1612  N NH1 . ARG A 237  ? 0.5741 0.5583 0.5677 -0.0080 0.0006  0.0245  235  ARG A NH1 
1613  N NH2 . ARG A 237  ? 0.4925 0.4700 0.4881 -0.0061 0.0002  0.0243  235  ARG A NH2 
1614  N N   . TYR A 238  ? 0.2259 0.2008 0.2288 -0.0038 -0.0011 0.0258  236  TYR A N   
1615  C CA  . TYR A 238  ? 0.2365 0.2118 0.2382 -0.0030 0.0006  0.0238  236  TYR A CA  
1616  C C   . TYR A 238  ? 0.2206 0.1961 0.2245 -0.0028 0.0001  0.0246  236  TYR A C   
1617  O O   . TYR A 238  ? 0.2521 0.2295 0.2553 -0.0033 0.0006  0.0240  236  TYR A O   
1618  C CB  . TYR A 238  ? 0.2194 0.1921 0.2205 -0.0011 0.0022  0.0216  236  TYR A CB  
1619  C CG  . TYR A 238  ? 0.2178 0.1905 0.2166 -0.0012 0.0029  0.0206  236  TYR A CG  
1620  C CD1 . TYR A 238  ? 0.2913 0.2668 0.2881 -0.0027 0.0030  0.0205  236  TYR A CD1 
1621  C CD2 . TYR A 238  ? 0.2377 0.2079 0.2364 0.0003  0.0035  0.0195  236  TYR A CD2 
1622  C CE1 . TYR A 238  ? 0.3289 0.3047 0.3239 -0.0028 0.0036  0.0194  236  TYR A CE1 
1623  C CE2 . TYR A 238  ? 0.2838 0.2540 0.2805 0.0001  0.0041  0.0186  236  TYR A CE2 
1624  C CZ  . TYR A 238  ? 0.3215 0.2943 0.3164 -0.0014 0.0042  0.0186  236  TYR A CZ  
1625  O OH  . TYR A 238  ? 0.3618 0.3348 0.3551 -0.0015 0.0047  0.0176  236  TYR A OH  
1626  N N   . TYR A 239  ? 0.2190 0.1926 0.2258 -0.0021 -0.0011 0.0257  237  TYR A N   
1627  C CA  . TYR A 239  ? 0.2294 0.2034 0.2386 -0.0019 -0.0018 0.0265  237  TYR A CA  
1628  C C   . TYR A 239  ? 0.2416 0.2190 0.2504 -0.0040 -0.0030 0.0285  237  TYR A C   
1629  O O   . TYR A 239  ? 0.2223 0.2014 0.2311 -0.0043 -0.0026 0.0282  237  TYR A O   
1630  C CB  . TYR A 239  ? 0.2247 0.1964 0.2377 -0.0008 -0.0032 0.0273  237  TYR A CB  
1631  C CG  . TYR A 239  ? 0.2270 0.1994 0.2427 -0.0006 -0.0040 0.0282  237  TYR A CG  
1632  C CD1 . TYR A 239  ? 0.2670 0.2412 0.2843 -0.0023 -0.0060 0.0310  237  TYR A CD1 
1633  C CD2 . TYR A 239  ? 0.2421 0.2137 0.2589 0.0012  -0.0027 0.0266  237  TYR A CD2 
1634  C CE1 . TYR A 239  ? 0.2999 0.2748 0.3197 -0.0022 -0.0068 0.0318  237  TYR A CE1 
1635  C CE2 . TYR A 239  ? 0.2536 0.2261 0.2730 0.0013  -0.0034 0.0274  237  TYR A CE2 
1636  C CZ  . TYR A 239  ? 0.2850 0.2588 0.3059 -0.0003 -0.0054 0.0299  237  TYR A CZ  
1637  O OH  . TYR A 239  ? 0.3286 0.3033 0.3523 -0.0001 -0.0062 0.0307  237  TYR A OH  
1638  N N   . ARG A 240  ? 0.2435 0.2225 0.2523 -0.0057 -0.0045 0.0308  238  ARG A N   
1639  C CA  . ARG A 240  ? 0.2460 0.2293 0.2545 -0.0078 -0.0058 0.0330  238  ARG A CA  
1640  C C   . ARG A 240  ? 0.2178 0.2046 0.2228 -0.0086 -0.0045 0.0311  238  ARG A C   
1641  O O   . ARG A 240  ? 0.2366 0.2271 0.2414 -0.0097 -0.0051 0.0316  238  ARG A O   
1642  C CB  . ARG A 240  ? 0.2663 0.2510 0.2761 -0.0095 -0.0080 0.0365  238  ARG A CB  
1643  C CG  . ARG A 240  ? 0.2830 0.2689 0.2903 -0.0104 -0.0075 0.0364  238  ARG A CG  
1644  C CD  . ARG A 240  ? 0.2839 0.2720 0.2931 -0.0125 -0.0099 0.0406  238  ARG A CD  
1645  N NE  . ARG A 240  ? 0.3061 0.2946 0.3137 -0.0131 -0.0096 0.0406  238  ARG A NE  
1646  C CZ  . ARG A 240  ? 0.3354 0.3198 0.3453 -0.0123 -0.0103 0.0408  238  ARG A CZ  
1647  N NH1 . ARG A 240  ? 0.3095 0.2894 0.3235 -0.0108 -0.0115 0.0409  238  ARG A NH1 
1648  N NH2 . ARG A 240  ? 0.3883 0.3734 0.3966 -0.0129 -0.0099 0.0407  238  ARG A NH2 
1649  N N   . ASP A 241  ? 0.2324 0.2185 0.2351 -0.0080 -0.0029 0.0288  239  ASP A N   
1650  C CA  . ASP A 241  ? 0.2402 0.2293 0.2405 -0.0083 -0.0017 0.0263  239  ASP A CA  
1651  C C   . ASP A 241  ? 0.2443 0.2324 0.2457 -0.0073 -0.0010 0.0246  239  ASP A C   
1652  O O   . ASP A 241  ? 0.2389 0.2304 0.2399 -0.0081 -0.0011 0.0236  239  ASP A O   
1653  C CB  . ASP A 241  ? 0.2998 0.2876 0.2981 -0.0077 -0.0003 0.0242  239  ASP A CB  
1654  C CG  . ASP A 241  ? 0.3832 0.3734 0.3801 -0.0090 -0.0009 0.0256  239  ASP A CG  
1655  O OD1 . ASP A 241  ? 0.4134 0.4065 0.4108 -0.0107 -0.0025 0.0286  239  ASP A OD1 
1656  O OD2 . ASP A 241  ? 0.4771 0.4663 0.4725 -0.0085 0.0001  0.0240  239  ASP A OD2 
1657  N N   . TYR A 242  ? 0.2243 0.2082 0.2274 -0.0056 -0.0002 0.0241  240  TYR A N   
1658  C CA  . TYR A 242  ? 0.2107 0.1940 0.2155 -0.0047 0.0005  0.0230  240  TYR A CA  
1659  C C   . TYR A 242  ? 0.1881 0.1733 0.1945 -0.0056 -0.0010 0.0246  240  TYR A C   
1660  O O   . TYR A 242  ? 0.2000 0.1871 0.2070 -0.0059 -0.0010 0.0236  240  TYR A O   
1661  C CB  . TYR A 242  ? 0.1951 0.1745 0.2014 -0.0028 0.0015  0.0227  240  TYR A CB  
1662  C CG  . TYR A 242  ? 0.1918 0.1694 0.1968 -0.0017 0.0030  0.0209  240  TYR A CG  
1663  C CD1 . TYR A 242  ? 0.2136 0.1923 0.2173 -0.0021 0.0038  0.0192  240  TYR A CD1 
1664  C CD2 . TYR A 242  ? 0.2172 0.1922 0.2226 -0.0002 0.0036  0.0209  240  TYR A CD2 
1665  C CE1 . TYR A 242  ? 0.2352 0.2122 0.2380 -0.0011 0.0051  0.0179  240  TYR A CE1 
1666  C CE2 . TYR A 242  ? 0.2012 0.1749 0.2053 0.0008  0.0050  0.0196  240  TYR A CE2 
1667  C CZ  . TYR A 242  ? 0.2049 0.1795 0.2078 0.0003  0.0057  0.0183  240  TYR A CZ  
1668  O OH  . TYR A 242  ? 0.2265 0.1998 0.2285 0.0012  0.0069  0.0172  240  TYR A OH  
1669  N N   . GLU A 243  ? 0.1778 0.1625 0.1856 -0.0059 -0.0024 0.0271  241  GLU A N   
1670  C CA  . GLU A 243  ? 0.1990 0.1856 0.2090 -0.0066 -0.0039 0.0290  241  GLU A CA  
1671  C C   . GLU A 243  ? 0.2136 0.2053 0.2218 -0.0086 -0.0048 0.0293  241  GLU A C   
1672  O O   . GLU A 243  ? 0.2069 0.2007 0.2159 -0.0090 -0.0052 0.0290  241  GLU A O   
1673  C CB  . GLU A 243  ? 0.2295 0.2145 0.2418 -0.0066 -0.0056 0.0317  241  GLU A CB  
1674  C CG  . GLU A 243  ? 0.2735 0.2604 0.2883 -0.0076 -0.0075 0.0342  241  GLU A CG  
1675  C CD  . GLU A 243  ? 0.2919 0.2777 0.3095 -0.0080 -0.0097 0.0373  241  GLU A CD  
1676  O OE1 . GLU A 243  ? 0.4161 0.4015 0.4327 -0.0086 -0.0100 0.0381  241  GLU A OE1 
1677  O OE2 . GLU A 243  ? 0.3087 0.2940 0.3297 -0.0078 -0.0112 0.0389  241  GLU A OE2 
1678  N N   . SER A 244  ? 0.2238 0.2181 0.2294 -0.0098 -0.0050 0.0297  242  SER A N   
1679  C CA  . SER A 244  ? 0.2268 0.2272 0.2305 -0.0117 -0.0057 0.0298  242  SER A CA  
1680  C C   . SER A 244  ? 0.2201 0.2220 0.2229 -0.0112 -0.0045 0.0259  242  SER A C   
1681  O O   . SER A 244  ? 0.2364 0.2425 0.2390 -0.0121 -0.0053 0.0253  242  SER A O   
1682  C CB  . SER A 244  ? 0.2337 0.2373 0.2352 -0.0131 -0.0061 0.0311  242  SER A CB  
1683  O OG  . SER A 244  ? 0.3067 0.3082 0.3066 -0.0121 -0.0045 0.0287  242  SER A OG  
1684  N N   . ALA A 245  ? 0.2139 0.2122 0.2164 -0.0098 -0.0029 0.0234  243  ALA A N   
1685  C CA  . ALA A 245  ? 0.2069 0.2059 0.2095 -0.0093 -0.0021 0.0199  243  ALA A CA  
1686  C C   . ALA A 245  ? 0.2191 0.2171 0.2246 -0.0088 -0.0023 0.0197  243  ALA A C   
1687  O O   . ALA A 245  ? 0.2172 0.2179 0.2233 -0.0092 -0.0027 0.0177  243  ALA A O   
1688  C CB  . ALA A 245  ? 0.2305 0.2258 0.2328 -0.0079 -0.0004 0.0179  243  ALA A CB  
1689  N N   . ILE A 246  ? 0.1984 0.1925 0.2060 -0.0078 -0.0022 0.0216  244  ILE A N   
1690  C CA  . ILE A 246  ? 0.2030 0.1965 0.2134 -0.0074 -0.0025 0.0217  244  ILE A CA  
1691  C C   . ILE A 246  ? 0.2275 0.2255 0.2381 -0.0089 -0.0042 0.0225  244  ILE A C   
1692  O O   . ILE A 246  ? 0.2366 0.2362 0.2487 -0.0091 -0.0045 0.0210  244  ILE A O   
1693  C CB  . ILE A 246  ? 0.1954 0.1851 0.2080 -0.0061 -0.0021 0.0235  244  ILE A CB  
1694  C CG1 . ILE A 246  ? 0.1945 0.1806 0.2069 -0.0046 -0.0003 0.0223  244  ILE A CG1 
1695  C CG2 . ILE A 246  ? 0.2084 0.1983 0.2239 -0.0060 -0.0026 0.0241  244  ILE A CG2 
1696  C CD1 . ILE A 246  ? 0.2319 0.2150 0.2458 -0.0032 0.0001  0.0236  244  ILE A CD1 
1697  N N   . HIS A 247  ? 0.2093 0.2097 0.2186 -0.0101 -0.0054 0.0250  245  HIS A N   
1698  C CA  . HIS A 247  ? 0.2127 0.2183 0.2219 -0.0116 -0.0071 0.0261  245  HIS A CA  
1699  C C   . HIS A 247  ? 0.2075 0.2179 0.2150 -0.0124 -0.0071 0.0229  245  HIS A C   
1700  O O   . HIS A 247  ? 0.2294 0.2428 0.2381 -0.0128 -0.0080 0.0218  245  HIS A O   
1701  C CB  . HIS A 247  ? 0.2191 0.2270 0.2274 -0.0130 -0.0086 0.0298  245  HIS A CB  
1702  C CG  . HIS A 247  ? 0.2423 0.2464 0.2536 -0.0124 -0.0094 0.0329  245  HIS A CG  
1703  N ND1 . HIS A 247  ? 0.2387 0.2425 0.2527 -0.0122 -0.0104 0.0341  245  HIS A ND1 
1704  C CD2 . HIS A 247  ? 0.2678 0.2684 0.2799 -0.0118 -0.0095 0.0348  245  HIS A CD2 
1705  C CE1 . HIS A 247  ? 0.2819 0.2823 0.2987 -0.0114 -0.0111 0.0365  245  HIS A CE1 
1706  N NE2 . HIS A 247  ? 0.2450 0.2432 0.2606 -0.0112 -0.0106 0.0368  245  HIS A NE2 
1707  N N   . ALA A 248  ? 0.1981 0.2098 0.2032 -0.0125 -0.0063 0.0212  246  ALA A N   
1708  C CA  . ALA A 248  ? 0.2202 0.2370 0.2239 -0.0130 -0.0064 0.0176  246  ALA A CA  
1709  C C   . ALA A 248  ? 0.2465 0.2611 0.2528 -0.0119 -0.0059 0.0140  246  ALA A C   
1710  O O   . ALA A 248  ? 0.2200 0.2387 0.2271 -0.0124 -0.0069 0.0116  246  ALA A O   
1711  C CB  . ALA A 248  ? 0.2303 0.2488 0.2312 -0.0132 -0.0056 0.0165  246  ALA A CB  
1712  N N   . ILE A 249  ? 0.2206 0.2290 0.2286 -0.0105 -0.0046 0.0138  247  ILE A N   
1713  C CA  . ILE A 249  ? 0.2048 0.2108 0.2160 -0.0096 -0.0043 0.0112  247  ILE A CA  
1714  C C   . ILE A 249  ? 0.2208 0.2271 0.2347 -0.0098 -0.0053 0.0121  247  ILE A C   
1715  O O   . ILE A 249  ? 0.2284 0.2362 0.2448 -0.0098 -0.0060 0.0095  247  ILE A O   
1716  C CB  . ILE A 249  ? 0.1862 0.1862 0.1984 -0.0082 -0.0027 0.0116  247  ILE A CB  
1717  C CG1 . ILE A 249  ? 0.2066 0.2066 0.2163 -0.0079 -0.0018 0.0102  247  ILE A CG1 
1718  C CG2 . ILE A 249  ? 0.2267 0.2243 0.2429 -0.0074 -0.0025 0.0099  247  ILE A CG2 
1719  C CD1 . ILE A 249  ? 0.2170 0.2118 0.2267 -0.0067 -0.0003 0.0116  247  ILE A CD1 
1720  N N   . GLY A 250  ? 0.2002 0.2050 0.2144 -0.0098 -0.0055 0.0157  248  GLY A N   
1721  C CA  . GLY A 250  ? 0.2045 0.2096 0.2215 -0.0100 -0.0064 0.0167  248  GLY A CA  
1722  C C   . GLY A 250  ? 0.2336 0.2447 0.2500 -0.0113 -0.0081 0.0159  248  GLY A C   
1723  O O   . GLY A 250  ? 0.2322 0.2445 0.2513 -0.0115 -0.0090 0.0146  248  GLY A O   
1724  N N   . LYS A 251  ? 0.2109 0.2264 0.2240 -0.0125 -0.0088 0.0167  249  LYS A N   
1725  C CA  . LYS A 251  ? 0.2332 0.2558 0.2453 -0.0139 -0.0104 0.0158  249  LYS A CA  
1726  C C   . LYS A 251  ? 0.2542 0.2794 0.2671 -0.0136 -0.0106 0.0107  249  LYS A C   
1727  O O   . LYS A 251  ? 0.2528 0.2821 0.2671 -0.0142 -0.0119 0.0090  249  LYS A O   
1728  C CB  . LYS A 251  ? 0.2357 0.2634 0.2440 -0.0152 -0.0109 0.0177  249  LYS A CB  
1729  C CG  . LYS A 251  ? 0.2629 0.2899 0.2710 -0.0159 -0.0117 0.0229  249  LYS A CG  
1730  C CD  . LYS A 251  ? 0.2819 0.3136 0.2865 -0.0173 -0.0120 0.0246  249  LYS A CD  
1731  C CE  . LYS A 251  ? 0.2914 0.3215 0.2965 -0.0179 -0.0129 0.0300  249  LYS A CE  
1732  N NZ  . LYS A 251  ? 0.2948 0.3294 0.2968 -0.0193 -0.0131 0.0316  249  LYS A NZ  
1733  N N   . ALA A 252  ? 0.2199 0.2428 0.2325 -0.0128 -0.0093 0.0081  250  ALA A N   
1734  C CA  . ALA A 252  ? 0.2353 0.2604 0.2495 -0.0124 -0.0097 0.0030  250  ALA A CA  
1735  C C   . ALA A 252  ? 0.2596 0.2803 0.2787 -0.0115 -0.0098 0.0016  250  ALA A C   
1736  O O   . ALA A 252  ? 0.2568 0.2800 0.2785 -0.0116 -0.0110 -0.0021 250  ALA A O   
1737  C CB  . ALA A 252  ? 0.2777 0.3017 0.2904 -0.0117 -0.0084 0.0009  250  ALA A CB  
1738  N N   . SER A 253  ? 0.2474 0.2617 0.2681 -0.0108 -0.0087 0.0045  251  SER A N   
1739  C CA  . SER A 253  ? 0.2328 0.2435 0.2584 -0.0101 -0.0088 0.0040  251  SER A CA  
1740  C C   . SER A 253  ? 0.2640 0.2779 0.2917 -0.0109 -0.0105 0.0037  251  SER A C   
1741  O O   . SER A 253  ? 0.2451 0.2592 0.2770 -0.0108 -0.0114 0.0010  251  SER A O   
1742  C CB  . SER A 253  ? 0.2448 0.2499 0.2713 -0.0093 -0.0073 0.0077  251  SER A CB  
1743  O OG  . SER A 253  ? 0.2766 0.2789 0.3078 -0.0089 -0.0074 0.0077  251  SER A OG  
1744  N N   . ALA A 254  ? 0.2432 0.2600 0.2686 -0.0117 -0.0111 0.0065  252  ALA A N   
1745  C CA  . ALA A 254  ? 0.2738 0.2947 0.3005 -0.0126 -0.0129 0.0064  252  ALA A CA  
1746  C C   . ALA A 254  ? 0.3005 0.3181 0.3324 -0.0121 -0.0132 0.0063  252  ALA A C   
1747  O O   . ALA A 254  ? 0.2840 0.3043 0.3188 -0.0125 -0.0147 0.0036  252  ALA A O   
1748  C CB  . ALA A 254  ? 0.3315 0.3594 0.3567 -0.0134 -0.0143 0.0024  252  ALA A CB  
1749  N N   . GLY A 255  ? 0.2778 0.2900 0.3112 -0.0113 -0.0118 0.0093  253  GLY A N   
1750  C CA  . GLY A 255  ? 0.2833 0.2930 0.3217 -0.0110 -0.0119 0.0100  253  GLY A CA  
1751  C C   . GLY A 255  ? 0.2602 0.2673 0.3027 -0.0105 -0.0117 0.0075  253  GLY A C   
1752  O O   . GLY A 255  ? 0.3009 0.3066 0.3481 -0.0105 -0.0121 0.0080  253  GLY A O   
1753  N N   . ARG A 256  ? 0.2623 0.2686 0.3038 -0.0101 -0.0112 0.0050  254  ARG A N   
1754  C CA  . ARG A 256  ? 0.2551 0.2587 0.3014 -0.0097 -0.0113 0.0030  254  ARG A CA  
1755  C C   . ARG A 256  ? 0.2625 0.2613 0.3111 -0.0090 -0.0096 0.0064  254  ARG A C   
1756  O O   . ARG A 256  ? 0.2655 0.2621 0.3191 -0.0089 -0.0099 0.0059  254  ARG A O   
1757  C CB  . ARG A 256  ? 0.2608 0.2649 0.3056 -0.0094 -0.0113 -0.0006 254  ARG A CB  
1758  C CG  . ARG A 256  ? 0.3276 0.3368 0.3732 -0.0099 -0.0133 -0.0054 254  ARG A CG  
1759  C CD  . ARG A 256  ? 0.3315 0.3416 0.3756 -0.0094 -0.0131 -0.0090 254  ARG A CD  
1760  N NE  . ARG A 256  ? 0.2979 0.3104 0.3354 -0.0096 -0.0120 -0.0078 254  ARG A NE  
1761  C CZ  . ARG A 256  ? 0.3185 0.3320 0.3536 -0.0092 -0.0114 -0.0100 254  ARG A CZ  
1762  N NH1 . ARG A 256  ? 0.3256 0.3375 0.3643 -0.0085 -0.0118 -0.0135 254  ARG A NH1 
1763  N NH2 . ARG A 256  ? 0.2836 0.2998 0.3130 -0.0096 -0.0106 -0.0085 254  ARG A NH2 
1764  N N   . GLY A 257  ? 0.2449 0.2423 0.2901 -0.0085 -0.0081 0.0098  255  GLY A N   
1765  C CA  . GLY A 257  ? 0.2342 0.2282 0.2813 -0.0078 -0.0064 0.0128  255  GLY A CA  
1766  C C   . GLY A 257  ? 0.2149 0.2062 0.2609 -0.0071 -0.0050 0.0127  255  GLY A C   
1767  O O   . GLY A 257  ? 0.2408 0.2325 0.2847 -0.0071 -0.0052 0.0103  255  GLY A O   
1768  N N   . ILE A 258  ? 0.2038 0.1929 0.2513 -0.0064 -0.0035 0.0155  256  ILE A N   
1769  C CA  . ILE A 258  ? 0.2119 0.1987 0.2574 -0.0056 -0.0020 0.0162  256  ILE A CA  
1770  C C   . ILE A 258  ? 0.2369 0.2223 0.2859 -0.0057 -0.0024 0.0146  256  ILE A C   
1771  O O   . ILE A 258  ? 0.2177 0.2016 0.2647 -0.0052 -0.0015 0.0144  256  ILE A O   
1772  C CB  . ILE A 258  ? 0.1987 0.1846 0.2441 -0.0047 -0.0002 0.0196  256  ILE A CB  
1773  C CG1 . ILE A 258  ? 0.2228 0.2089 0.2739 -0.0049 -0.0002 0.0215  256  ILE A CG1 
1774  C CG2 . ILE A 258  ? 0.2028 0.1897 0.2450 -0.0043 0.0000  0.0207  256  ILE A CG2 
1775  C CD1 . ILE A 258  ? 0.2561 0.2425 0.3071 -0.0040 0.0017  0.0246  256  ILE A CD1 
1776  N N   . TYR A 259  ? 0.2280 0.2138 0.2825 -0.0064 -0.0039 0.0136  257  TYR A N   
1777  C CA  . TYR A 259  ? 0.2318 0.2159 0.2908 -0.0065 -0.0048 0.0122  257  TYR A CA  
1778  C C   . TYR A 259  ? 0.2772 0.2624 0.3365 -0.0068 -0.0066 0.0074  257  TYR A C   
1779  O O   . TYR A 259  ? 0.3004 0.2845 0.3595 -0.0064 -0.0066 0.0057  257  TYR A O   
1780  C CB  . TYR A 259  ? 0.2614 0.2450 0.3275 -0.0071 -0.0056 0.0142  257  TYR A CB  
1781  C CG  . TYR A 259  ? 0.2387 0.2224 0.3046 -0.0068 -0.0037 0.0188  257  TYR A CG  
1782  C CD1 . TYR A 259  ? 0.2578 0.2405 0.3216 -0.0061 -0.0018 0.0212  257  TYR A CD1 
1783  C CD2 . TYR A 259  ? 0.2535 0.2389 0.3213 -0.0072 -0.0039 0.0205  257  TYR A CD2 
1784  C CE1 . TYR A 259  ? 0.2478 0.2315 0.3114 -0.0056 -0.0001 0.0250  257  TYR A CE1 
1785  C CE2 . TYR A 259  ? 0.2957 0.2820 0.3636 -0.0068 -0.0022 0.0243  257  TYR A CE2 
1786  C CZ  . TYR A 259  ? 0.2504 0.2360 0.3161 -0.0060 -0.0003 0.0264  257  TYR A CZ  
1787  O OH  . TYR A 259  ? 0.2564 0.2437 0.3220 -0.0054 0.0015  0.0297  257  TYR A OH  
1788  N N   . GLU A 260  ? 0.2469 0.2349 0.3066 -0.0074 -0.0081 0.0051  258  GLU A N   
1789  C CA  . GLU A 260  ? 0.3159 0.3061 0.3755 -0.0075 -0.0098 0.0001  258  GLU A CA  
1790  C C   . GLU A 260  ? 0.3070 0.2994 0.3594 -0.0073 -0.0089 -0.0010 258  GLU A C   
1791  O O   . GLU A 260  ? 0.3627 0.3565 0.4142 -0.0071 -0.0095 -0.0047 258  GLU A O   
1792  C CB  . GLU A 260  ? 0.3269 0.3201 0.3895 -0.0083 -0.0119 -0.0023 258  GLU A CB  
1793  C CG  . GLU A 260  ? 0.4314 0.4277 0.4950 -0.0083 -0.0139 -0.0081 258  GLU A CG  
1794  C CD  . GLU A 260  ? 0.4976 0.4984 0.5618 -0.0090 -0.0158 -0.0107 258  GLU A CD  
1795  O OE1 . GLU A 260  ? 0.5345 0.5348 0.6018 -0.0095 -0.0163 -0.0086 258  GLU A OE1 
1796  O OE2 . GLU A 260  ? 0.5028 0.5080 0.5644 -0.0090 -0.0167 -0.0148 258  GLU A OE2 
1797  N N   . GLY A 261  ? 0.2412 0.2341 0.2889 -0.0073 -0.0076 0.0021  259  GLY A N   
1798  C CA  . GLY A 261  ? 0.2382 0.2335 0.2797 -0.0074 -0.0070 0.0017  259  GLY A CA  
1799  C C   . GLY A 261  ? 0.2492 0.2419 0.2872 -0.0066 -0.0052 0.0032  259  GLY A C   
1800  O O   . GLY A 261  ? 0.2315 0.2208 0.2714 -0.0060 -0.0041 0.0051  259  GLY A O   
1801  N N   . PRO A 262  ? 0.2008 0.1958 0.2339 -0.0068 -0.0049 0.0023  260  PRO A N   
1802  C CA  . PRO A 262  ? 0.2119 0.2049 0.2418 -0.0061 -0.0034 0.0033  260  PRO A CA  
1803  C C   . PRO A 262  ? 0.2189 0.2095 0.2467 -0.0057 -0.0020 0.0074  260  PRO A C   
1804  O O   . PRO A 262  ? 0.2588 0.2499 0.2866 -0.0060 -0.0022 0.0095  260  PRO A O   
1805  C CB  . PRO A 262  ? 0.2278 0.2249 0.2533 -0.0067 -0.0038 0.0012  260  PRO A CB  
1806  C CG  . PRO A 262  ? 0.2606 0.2618 0.2857 -0.0076 -0.0051 0.0014  260  PRO A CG  
1807  C CD  . PRO A 262  ? 0.2240 0.2243 0.2545 -0.0076 -0.0061 0.0004  260  PRO A CD  
1808  N N   . GLY A 263  ? 0.2107 0.1987 0.2368 -0.0050 -0.0006 0.0084  261  GLY A N   
1809  C CA  . GLY A 263  ? 0.2283 0.2142 0.2525 -0.0043 0.0007  0.0116  261  GLY A CA  
1810  C C   . GLY A 263  ? 0.1999 0.1852 0.2200 -0.0040 0.0016  0.0116  261  GLY A C   
1811  O O   . GLY A 263  ? 0.2097 0.1967 0.2281 -0.0044 0.0012  0.0093  261  GLY A O   
1812  N N   . ILE A 264  ? 0.2062 0.1895 0.2248 -0.0033 0.0027  0.0139  262  ILE A N   
1813  C CA  . ILE A 264  ? 0.2123 0.1948 0.2275 -0.0029 0.0034  0.0141  262  ILE A CA  
1814  C C   . ILE A 264  ? 0.2153 0.1949 0.2310 -0.0016 0.0048  0.0152  262  ILE A C   
1815  O O   . ILE A 264  ? 0.1999 0.1787 0.2181 -0.0011 0.0053  0.0166  262  ILE A O   
1816  C CB  . ILE A 264  ? 0.2089 0.1922 0.2216 -0.0032 0.0029  0.0158  262  ILE A CB  
1817  C CG1 . ILE A 264  ? 0.2269 0.2100 0.2364 -0.0033 0.0033  0.0157  262  ILE A CG1 
1818  C CG2 . ILE A 264  ? 0.2230 0.2046 0.2372 -0.0023 0.0034  0.0181  262  ILE A CG2 
1819  C CD1 . ILE A 264  ? 0.2592 0.2436 0.2671 -0.0039 0.0024  0.0176  262  ILE A CD1 
1820  N N   . SER A 265  ? 0.1950 0.1736 0.2085 -0.0013 0.0055  0.0145  263  SER A N   
1821  C CA  . SER A 265  ? 0.2143 0.1908 0.2276 -0.0001 0.0068  0.0156  263  SER A CA  
1822  C C   . SER A 265  ? 0.2416 0.2176 0.2517 0.0003  0.0071  0.0161  263  SER A C   
1823  O O   . SER A 265  ? 0.2555 0.2324 0.2633 -0.0004 0.0065  0.0153  263  SER A O   
1824  C CB  . SER A 265  ? 0.2421 0.2177 0.2564 0.0001  0.0072  0.0144  263  SER A CB  
1825  O OG  . SER A 265  ? 0.2699 0.2456 0.2882 -0.0001 0.0067  0.0143  263  SER A OG  
1826  N N   . ILE A 266  ? 0.2155 0.1904 0.2255 0.0015  0.0080  0.0175  264  ILE A N   
1827  C CA  . ILE A 266  ? 0.2222 0.1963 0.2299 0.0021  0.0080  0.0178  264  ILE A CA  
1828  C C   . ILE A 266  ? 0.2037 0.1767 0.2109 0.0034  0.0093  0.0178  264  ILE A C   
1829  O O   . ILE A 266  ? 0.2045 0.1778 0.2132 0.0040  0.0102  0.0183  264  ILE A O   
1830  C CB  . ILE A 266  ? 0.2308 0.2051 0.2395 0.0024  0.0074  0.0190  264  ILE A CB  
1831  C CG1 . ILE A 266  ? 0.2341 0.2086 0.2450 0.0037  0.0083  0.0197  264  ILE A CG1 
1832  C CG2 . ILE A 266  ? 0.2172 0.1930 0.2266 0.0010  0.0060  0.0193  264  ILE A CG2 
1833  C CD1 . ILE A 266  ? 0.2613 0.2358 0.2733 0.0044  0.0077  0.0204  264  ILE A CD1 
1834  N N   . LYS A 267  ? 0.2076 0.1798 0.2126 0.0038  0.0093  0.0174  265  LYS A N   
1835  C CA  . LYS A 267  ? 0.1954 0.1670 0.1995 0.0052  0.0104  0.0173  265  LYS A CA  
1836  C C   . LYS A 267  ? 0.2194 0.1908 0.2236 0.0062  0.0101  0.0174  265  LYS A C   
1837  O O   . LYS A 267  ? 0.2122 0.1828 0.2159 0.0057  0.0089  0.0174  265  LYS A O   
1838  C CB  . LYS A 267  ? 0.2350 0.2057 0.2369 0.0049  0.0105  0.0164  265  LYS A CB  
1839  C CG  . LYS A 267  ? 0.2640 0.2349 0.2666 0.0044  0.0108  0.0159  265  LYS A CG  
1840  C CD  . LYS A 267  ? 0.3334 0.3038 0.3341 0.0041  0.0108  0.0147  265  LYS A CD  
1841  C CE  . LYS A 267  ? 0.3892 0.3598 0.3915 0.0037  0.0108  0.0140  265  LYS A CE  
1842  N NZ  . LYS A 267  ? 0.4116 0.3832 0.4157 0.0027  0.0100  0.0135  265  LYS A NZ  
1843  N N   . LEU A 268  ? 0.1844 0.1566 0.1895 0.0077  0.0110  0.0176  266  LEU A N   
1844  C CA  . LEU A 268  ? 0.2058 0.1781 0.2115 0.0090  0.0105  0.0170  266  LEU A CA  
1845  C C   . LEU A 268  ? 0.2058 0.1766 0.2098 0.0093  0.0100  0.0160  266  LEU A C   
1846  O O   . LEU A 268  ? 0.2112 0.1811 0.2162 0.0097  0.0088  0.0155  266  LEU A O   
1847  C CB  . LEU A 268  ? 0.2076 0.1823 0.2145 0.0107  0.0118  0.0170  266  LEU A CB  
1848  C CG  . LEU A 268  ? 0.2268 0.2032 0.2360 0.0104  0.0123  0.0183  266  LEU A CG  
1849  C CD1 . LEU A 268  ? 0.2570 0.2367 0.2672 0.0120  0.0136  0.0184  266  LEU A CD1 
1850  C CD2 . LEU A 268  ? 0.2638 0.2396 0.2748 0.0098  0.0109  0.0185  266  LEU A CD2 
1851  N N   . SER A 269  ? 0.2081 0.1785 0.2100 0.0092  0.0107  0.0156  267  SER A N   
1852  C CA  . SER A 269  ? 0.2230 0.1921 0.2234 0.0094  0.0102  0.0146  267  SER A CA  
1853  C C   . SER A 269  ? 0.2284 0.1962 0.2287 0.0079  0.0086  0.0150  267  SER A C   
1854  O O   . SER A 269  ? 0.2299 0.1966 0.2300 0.0080  0.0077  0.0146  267  SER A O   
1855  C CB  . SER A 269  ? 0.2364 0.2056 0.2347 0.0095  0.0112  0.0142  267  SER A CB  
1856  O OG  . SER A 269  ? 0.2508 0.2196 0.2484 0.0079  0.0110  0.0146  267  SER A OG  
1857  N N   . ALA A 270  ? 0.1954 0.1637 0.1960 0.0064  0.0082  0.0160  268  ALA A N   
1858  C CA  . ALA A 270  ? 0.2352 0.2033 0.2358 0.0048  0.0067  0.0169  268  ALA A CA  
1859  C C   . ALA A 270  ? 0.2147 0.1823 0.2178 0.0050  0.0052  0.0177  268  ALA A C   
1860  O O   . ALA A 270  ? 0.2189 0.1862 0.2224 0.0038  0.0037  0.0188  268  ALA A O   
1861  C CB  . ALA A 270  ? 0.2431 0.2128 0.2434 0.0032  0.0067  0.0174  268  ALA A CB  
1862  N N   . LEU A 271  ? 0.2089 0.1766 0.2139 0.0064  0.0055  0.0174  269  LEU A N   
1863  C CA  . LEU A 271  ? 0.2120 0.1794 0.2200 0.0066  0.0039  0.0182  269  LEU A CA  
1864  C C   . LEU A 271  ? 0.2067 0.1729 0.2168 0.0083  0.0032  0.0169  269  LEU A C   
1865  O O   . LEU A 271  ? 0.2360 0.2017 0.2494 0.0087  0.0016  0.0173  269  LEU A O   
1866  C CB  . LEU A 271  ? 0.2245 0.1932 0.2341 0.0069  0.0045  0.0186  269  LEU A CB  
1867  C CG  . LEU A 271  ? 0.2433 0.2132 0.2518 0.0050  0.0046  0.0197  269  LEU A CG  
1868  C CD1 . LEU A 271  ? 0.2581 0.2292 0.2684 0.0055  0.0052  0.0199  269  LEU A CD1 
1869  C CD2 . LEU A 271  ? 0.2437 0.2137 0.2528 0.0034  0.0026  0.0213  269  LEU A CD2 
1870  N N   . HIS A 272  ? 0.2196 0.1855 0.2282 0.0094  0.0041  0.0152  270  HIS A N   
1871  C CA  . HIS A 272  ? 0.2137 0.1786 0.2243 0.0111  0.0031  0.0136  270  HIS A CA  
1872  C C   . HIS A 272  ? 0.2165 0.1809 0.2247 0.0114  0.0037  0.0124  270  HIS A C   
1873  O O   . HIS A 272  ? 0.2261 0.1917 0.2314 0.0115  0.0055  0.0121  270  HIS A O   
1874  C CB  . HIS A 272  ? 0.2305 0.1972 0.2430 0.0134  0.0039  0.0118  270  HIS A CB  
1875  C CG  . HIS A 272  ? 0.2630 0.2290 0.2790 0.0152  0.0022  0.0098  270  HIS A CG  
1876  N ND1 . HIS A 272  ? 0.2752 0.2408 0.2907 0.0164  0.0021  0.0076  270  HIS A ND1 
1877  C CD2 . HIS A 272  ? 0.3017 0.2672 0.3221 0.0160  0.0004  0.0094  270  HIS A CD2 
1878  C CE1 . HIS A 272  ? 0.2721 0.2371 0.2918 0.0179  0.0002  0.0057  270  HIS A CE1 
1879  N NE2 . HIS A 272  ? 0.3050 0.2698 0.3278 0.0177  -0.0008 0.0067  270  HIS A NE2 
1880  N N   . PRO A 273  ? 0.2399 0.2026 0.2495 0.0115  0.0020  0.0118  271  PRO A N   
1881  C CA  . PRO A 273  ? 0.2285 0.1908 0.2359 0.0118  0.0025  0.0106  271  PRO A CA  
1882  C C   . PRO A 273  ? 0.2453 0.2090 0.2521 0.0142  0.0036  0.0078  271  PRO A C   
1883  O O   . PRO A 273  ? 0.2458 0.2095 0.2504 0.0145  0.0043  0.0069  271  PRO A O   
1884  C CB  . PRO A 273  ? 0.2420 0.2021 0.2520 0.0110  0.0000  0.0110  271  PRO A CB  
1885  C CG  . PRO A 273  ? 0.2643 0.2237 0.2788 0.0118  -0.0018 0.0110  271  PRO A CG  
1886  C CD  . PRO A 273  ? 0.2538 0.2148 0.2677 0.0113  -0.0006 0.0124  271  PRO A CD  
1887  N N   . ARG A 274  ? 0.2094 0.1747 0.2181 0.0160  0.0039  0.0065  272  ARG A N   
1888  C CA  . ARG A 274  ? 0.2355 0.2035 0.2436 0.0184  0.0051  0.0039  272  ARG A CA  
1889  C C   . ARG A 274  ? 0.2517 0.2230 0.2590 0.0190  0.0071  0.0045  272  ARG A C   
1890  O O   . ARG A 274  ? 0.2484 0.2224 0.2575 0.0209  0.0074  0.0028  272  ARG A O   
1891  C CB  . ARG A 274  ? 0.2343 0.2022 0.2463 0.0204  0.0033  0.0009  272  ARG A CB  
1892  C CG  . ARG A 274  ? 0.2331 0.1978 0.2466 0.0199  0.0011  0.0003  272  ARG A CG  
1893  C CD  . ARG A 274  ? 0.2502 0.2151 0.2600 0.0196  0.0021  -0.0001 272  ARG A CD  
1894  N NE  . ARG A 274  ? 0.2622 0.2308 0.2700 0.0218  0.0038  -0.0026 272  ARG A NE  
1895  C CZ  . ARG A 274  ? 0.2363 0.2065 0.2460 0.0241  0.0030  -0.0062 272  ARG A CZ  
1896  N NH1 . ARG A 274  ? 0.2679 0.2357 0.2821 0.0247  0.0003  -0.0080 272  ARG A NH1 
1897  N NH2 . ARG A 274  ? 0.2819 0.2564 0.2892 0.0258  0.0047  -0.0080 272  ARG A NH2 
1898  N N   . TYR A 275  ? 0.2297 0.2011 0.2346 0.0174  0.0084  0.0068  273  TYR A N   
1899  C CA  . TYR A 275  ? 0.2052 0.1794 0.2097 0.0176  0.0102  0.0079  273  TYR A CA  
1900  C C   . TYR A 275  ? 0.2208 0.1982 0.2230 0.0188  0.0119  0.0072  273  TYR A C   
1901  O O   . TYR A 275  ? 0.2400 0.2171 0.2398 0.0178  0.0127  0.0084  273  TYR A O   
1902  C CB  . TYR A 275  ? 0.2176 0.1904 0.2212 0.0153  0.0104  0.0105  273  TYR A CB  
1903  C CG  . TYR A 275  ? 0.2154 0.1908 0.2190 0.0153  0.0120  0.0118  273  TYR A CG  
1904  C CD1 . TYR A 275  ? 0.2167 0.1949 0.2226 0.0165  0.0124  0.0116  273  TYR A CD1 
1905  C CD2 . TYR A 275  ? 0.2106 0.1859 0.2126 0.0140  0.0130  0.0134  273  TYR A CD2 
1906  C CE1 . TYR A 275  ? 0.2457 0.2266 0.2520 0.0163  0.0139  0.0132  273  TYR A CE1 
1907  C CE2 . TYR A 275  ? 0.2242 0.2019 0.2271 0.0139  0.0142  0.0149  273  TYR A CE2 
1908  C CZ  . TYR A 275  ? 0.2317 0.2122 0.2366 0.0149  0.0146  0.0150  273  TYR A CZ  
1909  O OH  . TYR A 275  ? 0.2573 0.2404 0.2633 0.0146  0.0158  0.0168  273  TYR A OH  
1910  N N   . SER A 276  ? 0.2151 0.1961 0.2184 0.0209  0.0123  0.0052  274  SER A N   
1911  C CA  . SER A 276  ? 0.1815 0.1667 0.1827 0.0222  0.0138  0.0046  274  SER A CA  
1912  C C   . SER A 276  ? 0.2071 0.1975 0.2100 0.0244  0.0145  0.0028  274  SER A C   
1913  O O   . SER A 276  ? 0.2316 0.2215 0.2375 0.0254  0.0133  0.0011  274  SER A O   
1914  C CB  . SER A 276  ? 0.2618 0.2459 0.2614 0.0228  0.0132  0.0027  274  SER A CB  
1915  O OG  . SER A 276  ? 0.3113 0.2954 0.3132 0.0246  0.0117  -0.0006 274  SER A OG  
1916  N N   . ARG A 277  ? 0.2145 0.2102 0.2157 0.0252  0.0162  0.0034  275  ARG A N   
1917  C CA  . ARG A 277  ? 0.2047 0.2068 0.2072 0.0274  0.0171  0.0017  275  ARG A CA  
1918  C C   . ARG A 277  ? 0.2214 0.2243 0.2252 0.0297  0.0158  -0.0030 275  ARG A C   
1919  O O   . ARG A 277  ? 0.2228 0.2288 0.2294 0.0315  0.0155  -0.0054 275  ARG A O   
1920  C CB  . ARG A 277  ? 0.2218 0.2302 0.2219 0.0276  0.0192  0.0035  275  ARG A CB  
1921  C CG  . ARG A 277  ? 0.2183 0.2350 0.2192 0.0300  0.0203  0.0015  275  ARG A CG  
1922  C CD  . ARG A 277  ? 0.2209 0.2393 0.2250 0.0303  0.0204  0.0017  275  ARG A CD  
1923  N NE  . ARG A 277  ? 0.2075 0.2346 0.2124 0.0327  0.0216  -0.0005 275  ARG A NE  
1924  C CZ  . ARG A 277  ? 0.2037 0.2332 0.2103 0.0352  0.0206  -0.0054 275  ARG A CZ  
1925  N NH1 . ARG A 277  ? 0.2226 0.2460 0.2305 0.0357  0.0185  -0.0085 275  ARG A NH1 
1926  N NH2 . ARG A 277  ? 0.2257 0.2642 0.2331 0.0374  0.0218  -0.0074 275  ARG A NH2 
1927  N N   . ALA A 278  ? 0.2314 0.2317 0.2339 0.0298  0.0148  -0.0046 276  ALA A N   
1928  C CA  . ALA A 278  ? 0.2366 0.2375 0.2410 0.0320  0.0132  -0.0093 276  ALA A CA  
1929  C C   . ALA A 278  ? 0.2343 0.2310 0.2431 0.0322  0.0111  -0.0107 276  ALA A C   
1930  O O   . ALA A 278  ? 0.2579 0.2563 0.2700 0.0345  0.0098  -0.0147 276  ALA A O   
1931  C CB  . ALA A 278  ? 0.2427 0.2408 0.2452 0.0318  0.0123  -0.0103 276  ALA A CB  
1932  N N   . GLN A 279  ? 0.2085 0.2002 0.2180 0.0299  0.0105  -0.0074 277  GLN A N   
1933  C CA  . GLN A 279  ? 0.1958 0.1834 0.2095 0.0296  0.0084  -0.0079 277  GLN A CA  
1934  C C   . GLN A 279  ? 0.2427 0.2318 0.2578 0.0292  0.0092  -0.0060 277  GLN A C   
1935  O O   . GLN A 279  ? 0.2152 0.2004 0.2326 0.0279  0.0078  -0.0043 277  GLN A O   
1936  C CB  . GLN A 279  ? 0.2526 0.2338 0.2660 0.0272  0.0068  -0.0057 277  GLN A CB  
1937  C CG  . GLN A 279  ? 0.2453 0.2246 0.2578 0.0275  0.0057  -0.0075 277  GLN A CG  
1938  C CD  . GLN A 279  ? 0.2810 0.2608 0.2976 0.0299  0.0037  -0.0119 277  GLN A CD  
1939  O OE1 . GLN A 279  ? 0.3697 0.3485 0.3909 0.0306  0.0021  -0.0129 277  GLN A OE1 
1940  N NE2 . GLN A 279  ? 0.2565 0.2381 0.2720 0.0313  0.0036  -0.0147 277  GLN A NE2 
1941  N N   . ALA A 280  ? 0.2144 0.2096 0.2285 0.0304  0.0113  -0.0060 278  ALA A N   
1942  C CA  . ALA A 280  ? 0.2453 0.2424 0.2608 0.0298  0.0122  -0.0038 278  ALA A CA  
1943  C C   . ALA A 280  ? 0.2340 0.2293 0.2544 0.0306  0.0103  -0.0053 278  ALA A C   
1944  O O   . ALA A 280  ? 0.2318 0.2252 0.2534 0.0291  0.0101  -0.0027 278  ALA A O   
1945  C CB  . ALA A 280  ? 0.2456 0.2506 0.2600 0.0313  0.0146  -0.0041 278  ALA A CB  
1946  N N   . ALA A 281  ? 0.2105 0.2066 0.2340 0.0329  0.0088  -0.0095 279  ALA A N   
1947  C CA  . ALA A 281  ? 0.2382 0.2327 0.2672 0.0338  0.0066  -0.0110 279  ALA A CA  
1948  C C   . ALA A 281  ? 0.2490 0.2362 0.2793 0.0313  0.0045  -0.0082 279  ALA A C   
1949  O O   . ALA A 281  ? 0.2508 0.2365 0.2839 0.0306  0.0036  -0.0065 279  ALA A O   
1950  C CB  . ALA A 281  ? 0.2885 0.2849 0.3214 0.0369  0.0050  -0.0165 279  ALA A CB  
1951  N N   . ARG A 282  ? 0.2182 0.2014 0.2466 0.0300  0.0036  -0.0075 280  ARG A N   
1952  C CA  . ARG A 282  ? 0.2237 0.2012 0.2530 0.0275  0.0017  -0.0045 280  ARG A CA  
1953  C C   . ARG A 282  ? 0.2256 0.2027 0.2517 0.0250  0.0033  -0.0003 280  ARG A C   
1954  O O   . ARG A 282  ? 0.2269 0.2011 0.2547 0.0234  0.0020  0.0021  280  ARG A O   
1955  C CB  . ARG A 282  ? 0.2421 0.2161 0.2698 0.0266  0.0007  -0.0045 280  ARG A CB  
1956  C CG  . ARG A 282  ? 0.2736 0.2469 0.3054 0.0286  -0.0016 -0.0085 280  ARG A CG  
1957  C CD  . ARG A 282  ? 0.2905 0.2596 0.3215 0.0271  -0.0031 -0.0075 280  ARG A CD  
1958  N NE  . ARG A 282  ? 0.2778 0.2428 0.3099 0.0243  -0.0046 -0.0035 280  ARG A NE  
1959  C CZ  . ARG A 282  ? 0.2981 0.2601 0.3287 0.0221  -0.0054 -0.0011 280  ARG A CZ  
1960  N NH1 . ARG A 282  ? 0.2675 0.2294 0.2953 0.0222  -0.0049 -0.0023 280  ARG A NH1 
1961  N NH2 . ARG A 282  ? 0.2819 0.2415 0.3137 0.0197  -0.0068 0.0025  280  ARG A NH2 
1962  N N   . VAL A 283  ? 0.2171 0.1971 0.2390 0.0248  0.0059  0.0006  281  VAL A N   
1963  C CA  . VAL A 283  ? 0.2109 0.1907 0.2305 0.0226  0.0073  0.0041  281  VAL A CA  
1964  C C   . VAL A 283  ? 0.2269 0.2082 0.2495 0.0228  0.0072  0.0050  281  VAL A C   
1965  O O   . VAL A 283  ? 0.2239 0.2029 0.2470 0.0209  0.0065  0.0075  281  VAL A O   
1966  C CB  . VAL A 283  ? 0.2074 0.1902 0.2230 0.0225  0.0098  0.0049  281  VAL A CB  
1967  C CG1 . VAL A 283  ? 0.2559 0.2391 0.2705 0.0207  0.0110  0.0081  281  VAL A CG1 
1968  C CG2 . VAL A 283  ? 0.2274 0.2079 0.2400 0.0218  0.0097  0.0047  281  VAL A CG2 
1969  N N   . MET A 284  ? 0.2148 0.2005 0.2394 0.0251  0.0079  0.0028  282  MET A N   
1970  C CA  . MET A 284  ? 0.2171 0.2046 0.2449 0.0253  0.0079  0.0035  282  MET A CA  
1971  C C   . MET A 284  ? 0.2364 0.2203 0.2686 0.0253  0.0051  0.0031  282  MET A C   
1972  O O   . MET A 284  ? 0.2735 0.2569 0.3076 0.0243  0.0045  0.0050  282  MET A O   
1973  C CB  . MET A 284  ? 0.2305 0.2244 0.2594 0.0279  0.0094  0.0010  282  MET A CB  
1974  C CG  . MET A 284  ? 0.2502 0.2482 0.2750 0.0278  0.0121  0.0021  282  MET A CG  
1975  S SD  . MET A 284  ? 0.2920 0.2893 0.3144 0.0248  0.0136  0.0069  282  MET A SD  
1976  C CE  . MET A 284  ? 0.2708 0.2706 0.2974 0.0251  0.0135  0.0077  282  MET A CE  
1977  N N   . GLY A 285  ? 0.2126 0.1941 0.2467 0.0263  0.0031  0.0008  283  GLY A N   
1978  C CA  . GLY A 285  ? 0.2290 0.2073 0.2683 0.0263  0.0001  0.0007  283  GLY A CA  
1979  C C   . GLY A 285  ? 0.2453 0.2190 0.2838 0.0233  -0.0015 0.0043  283  GLY A C   
1980  O O   . GLY A 285  ? 0.2617 0.2336 0.3038 0.0225  -0.0035 0.0060  283  GLY A O   
1981  N N   . GLU A 286  ? 0.2359 0.2081 0.2699 0.0217  -0.0006 0.0057  284  GLU A N   
1982  C CA  . GLU A 286  ? 0.2258 0.1943 0.2591 0.0190  -0.0022 0.0087  284  GLU A CA  
1983  C C   . GLU A 286  ? 0.2379 0.2068 0.2666 0.0167  -0.0005 0.0115  284  GLU A C   
1984  O O   . GLU A 286  ? 0.2634 0.2309 0.2922 0.0145  -0.0016 0.0142  284  GLU A O   
1985  C CB  . GLU A 286  ? 0.2357 0.2019 0.2685 0.0190  -0.0033 0.0076  284  GLU A CB  
1986  C CG  . GLU A 286  ? 0.3106 0.2759 0.3487 0.0212  -0.0056 0.0046  284  GLU A CG  
1987  C CD  . GLU A 286  ? 0.3013 0.2651 0.3387 0.0216  -0.0062 0.0029  284  GLU A CD  
1988  O OE1 . GLU A 286  ? 0.3080 0.2700 0.3422 0.0194  -0.0061 0.0052  284  GLU A OE1 
1989  O OE2 . GLU A 286  ? 0.3379 0.3026 0.3779 0.0241  -0.0068 -0.0011 284  GLU A OE2 
1990  N N   . LEU A 287  ? 0.2197 0.1907 0.2446 0.0171  0.0021  0.0109  285  LEU A N   
1991  C CA  A LEU A 287  ? 0.2272 0.1984 0.2484 0.0150  0.0035  0.0131  285  LEU A CA  
1992  C CA  B LEU A 287  ? 0.2273 0.1985 0.2485 0.0150  0.0035  0.0131  285  LEU A CA  
1993  C C   . LEU A 287  ? 0.2299 0.2030 0.2523 0.0147  0.0041  0.0144  285  LEU A C   
1994  O O   . LEU A 287  ? 0.2305 0.2029 0.2523 0.0127  0.0038  0.0166  285  LEU A O   
1995  C CB  A LEU A 287  ? 0.2429 0.2155 0.2604 0.0155  0.0057  0.0123  285  LEU A CB  
1996  C CB  B LEU A 287  ? 0.2429 0.2154 0.2604 0.0155  0.0057  0.0122  285  LEU A CB  
1997  C CG  A LEU A 287  ? 0.2377 0.2094 0.2515 0.0135  0.0066  0.0139  285  LEU A CG  
1998  C CG  B LEU A 287  ? 0.2386 0.2120 0.2533 0.0140  0.0073  0.0141  285  LEU A CG  
1999  C CD1 A LEU A 287  ? 0.2374 0.2103 0.2484 0.0143  0.0083  0.0129  285  LEU A CD1 
2000  C CD1 B LEU A 287  ? 0.2674 0.2386 0.2812 0.0116  0.0062  0.0158  285  LEU A CD1 
2001  C CD2 A LEU A 287  ? 0.2712 0.2439 0.2850 0.0122  0.0072  0.0157  285  LEU A CD2 
2002  C CD2 B LEU A 287  ? 0.2268 0.2013 0.2386 0.0145  0.0090  0.0134  285  LEU A CD2 
2003  N N   . LEU A 288  ? 0.2243 0.2003 0.2486 0.0166  0.0051  0.0130  286  LEU A N   
2004  C CA  . LEU A 288  ? 0.2232 0.2013 0.2489 0.0164  0.0058  0.0143  286  LEU A CA  
2005  C C   . LEU A 288  ? 0.2307 0.2072 0.2590 0.0151  0.0038  0.0160  286  LEU A C   
2006  O O   . LEU A 288  ? 0.2264 0.2032 0.2539 0.0134  0.0041  0.0179  286  LEU A O   
2007  C CB  . LEU A 288  ? 0.2632 0.2453 0.2911 0.0188  0.0070  0.0123  286  LEU A CB  
2008  C CG  . LEU A 288  ? 0.3193 0.3039 0.3498 0.0188  0.0073  0.0134  286  LEU A CG  
2009  C CD1 . LEU A 288  ? 0.2670 0.2528 0.2951 0.0172  0.0091  0.0157  286  LEU A CD1 
2010  C CD2 . LEU A 288  ? 0.3958 0.3846 0.4290 0.0215  0.0080  0.0110  286  LEU A CD2 
2011  N N   . PRO A 289  ? 0.2140 0.1887 0.2456 0.0156  0.0015  0.0155  287  PRO A N   
2012  C CA  . PRO A 289  ? 0.2171 0.1906 0.2511 0.0141  -0.0005 0.0177  287  PRO A CA  
2013  C C   . PRO A 289  ? 0.2245 0.1967 0.2555 0.0113  -0.0009 0.0201  287  PRO A C   
2014  O O   . PRO A 289  ? 0.2203 0.1930 0.2521 0.0098  -0.0018 0.0221  287  PRO A O   
2015  C CB  . PRO A 289  ? 0.2468 0.2184 0.2852 0.0152  -0.0031 0.0167  287  PRO A CB  
2016  C CG  . PRO A 289  ? 0.3018 0.2748 0.3412 0.0180  -0.0021 0.0132  287  PRO A CG  
2017  C CD  . PRO A 289  ? 0.2428 0.2171 0.2770 0.0178  0.0005  0.0128  287  PRO A CD  
2018  N N   . ARG A 290  ? 0.2030 0.1740 0.2307 0.0107  -0.0004 0.0199  288  ARG A N   
2019  C CA  . ARG A 290  ? 0.2015 0.1720 0.2262 0.0082  -0.0007 0.0218  288  ARG A CA  
2020  C C   . ARG A 290  ? 0.2052 0.1775 0.2275 0.0074  0.0011  0.0221  288  ARG A C   
2021  O O   . ARG A 290  ? 0.2151 0.1881 0.2369 0.0056  0.0004  0.0237  288  ARG A O   
2022  C CB  . ARG A 290  ? 0.2163 0.1853 0.2383 0.0079  -0.0006 0.0212  288  ARG A CB  
2023  C CG  . ARG A 290  ? 0.2538 0.2210 0.2787 0.0083  -0.0028 0.0212  288  ARG A CG  
2024  C CD  . ARG A 290  ? 0.2779 0.2437 0.3005 0.0082  -0.0025 0.0204  288  ARG A CD  
2025  N NE  . ARG A 290  ? 0.3109 0.2747 0.3372 0.0088  -0.0049 0.0202  288  ARG A NE  
2026  C CZ  . ARG A 290  ? 0.3342 0.2967 0.3604 0.0098  -0.0050 0.0184  288  ARG A CZ  
2027  N NH1 . ARG A 290  ? 0.2834 0.2465 0.3056 0.0103  -0.0028 0.0169  288  ARG A NH1 
2028  N NH2 . ARG A 290  ? 0.3689 0.3294 0.3994 0.0104  -0.0075 0.0181  288  ARG A NH2 
2029  N N   . VAL A 291  ? 0.1999 0.1732 0.2212 0.0086  0.0032  0.0208  289  VAL A N   
2030  C CA  . VAL A 291  ? 0.1937 0.1685 0.2140 0.0079  0.0046  0.0213  289  VAL A CA  
2031  C C   . VAL A 291  ? 0.1966 0.1728 0.2197 0.0076  0.0039  0.0223  289  VAL A C   
2032  O O   . VAL A 291  ? 0.2096 0.1866 0.2325 0.0061  0.0038  0.0232  289  VAL A O   
2033  C CB  . VAL A 291  ? 0.2069 0.1830 0.2263 0.0092  0.0067  0.0202  289  VAL A CB  
2034  C CG1 . VAL A 291  ? 0.2303 0.2076 0.2493 0.0082  0.0078  0.0211  289  VAL A CG1 
2035  C CG2 . VAL A 291  ? 0.2437 0.2186 0.2604 0.0096  0.0072  0.0192  289  VAL A CG2 
2036  N N   . LYS A 292  ? 0.2025 0.1793 0.2288 0.0092  0.0034  0.0218  290  LYS A N   
2037  C CA  . LYS A 292  ? 0.1717 0.1499 0.2011 0.0090  0.0027  0.0228  290  LYS A CA  
2038  C C   . LYS A 292  ? 0.2278 0.2052 0.2575 0.0071  0.0007  0.0245  290  LYS A C   
2039  O O   . LYS A 292  ? 0.1880 0.1667 0.2183 0.0059  0.0005  0.0256  290  LYS A O   
2040  C CB  . LYS A 292  ? 0.2085 0.1874 0.2417 0.0112  0.0023  0.0217  290  LYS A CB  
2041  C CG  . LYS A 292  ? 0.2196 0.1999 0.2562 0.0111  0.0014  0.0227  290  LYS A CG  
2042  C CD  . LYS A 292  ? 0.2370 0.2185 0.2779 0.0134  0.0008  0.0213  290  LYS A CD  
2043  C CE  . LYS A 292  ? 0.2845 0.2674 0.3289 0.0131  -0.0001 0.0225  290  LYS A CE  
2044  N NZ  . LYS A 292  ? 0.2562 0.2410 0.3049 0.0155  -0.0003 0.0208  290  LYS A NZ  
2045  N N   . ALA A 293  ? 0.1813 0.1570 0.2106 0.0065  -0.0009 0.0250  291  ALA A N   
2046  C CA  . ALA A 293  ? 0.1945 0.1703 0.2239 0.0045  -0.0029 0.0272  291  ALA A CA  
2047  C C   . ALA A 293  ? 0.1934 0.1706 0.2194 0.0026  -0.0022 0.0275  291  ALA A C   
2048  O O   . ALA A 293  ? 0.2168 0.1956 0.2432 0.0012  -0.0031 0.0287  291  ALA A O   
2049  C CB  . ALA A 293  ? 0.2138 0.1879 0.2439 0.0041  -0.0048 0.0281  291  ALA A CB  
2050  N N   . LEU A 294  ? 0.1695 0.1462 0.1924 0.0026  -0.0006 0.0262  292  LEU A N   
2051  C CA  . LEU A 294  ? 0.1967 0.1747 0.2170 0.0011  0.0000  0.0260  292  LEU A CA  
2052  C C   . LEU A 294  ? 0.1943 0.1736 0.2160 0.0012  0.0008  0.0256  292  LEU A C   
2053  O O   . LEU A 294  ? 0.1840 0.1649 0.2055 -0.0002 0.0002  0.0258  292  LEU A O   
2054  C CB  . LEU A 294  ? 0.2146 0.1916 0.2319 0.0013  0.0014  0.0246  292  LEU A CB  
2055  C CG  . LEU A 294  ? 0.1932 0.1691 0.2089 0.0009  0.0005  0.0249  292  LEU A CG  
2056  C CD1 . LEU A 294  ? 0.2065 0.1813 0.2196 0.0015  0.0021  0.0234  292  LEU A CD1 
2057  C CD2 . LEU A 294  ? 0.2198 0.1977 0.2343 -0.0012 -0.0010 0.0263  292  LEU A CD2 
2058  N N   . ALA A 295  ? 0.1692 0.1482 0.1927 0.0028  0.0020  0.0251  293  ALA A N   
2059  C CA  . ALA A 295  ? 0.1916 0.1721 0.2171 0.0028  0.0028  0.0252  293  ALA A CA  
2060  C C   . ALA A 295  ? 0.1981 0.1799 0.2261 0.0022  0.0013  0.0263  293  ALA A C   
2061  O O   . ALA A 295  ? 0.1950 0.1782 0.2240 0.0012  0.0011  0.0264  293  ALA A O   
2062  C CB  . ALA A 295  ? 0.1921 0.1729 0.2190 0.0047  0.0045  0.0247  293  ALA A CB  
2063  N N   . LEU A 296  ? 0.1766 0.1580 0.2062 0.0027  0.0000  0.0271  294  LEU A N   
2064  C CA  . LEU A 296  ? 0.1736 0.1563 0.2058 0.0020  -0.0017 0.0284  294  LEU A CA  
2065  C C   . LEU A 296  ? 0.1930 0.1771 0.2234 -0.0002 -0.0030 0.0291  294  LEU A C   
2066  O O   . LEU A 296  ? 0.1912 0.1771 0.2231 -0.0011 -0.0037 0.0297  294  LEU A O   
2067  C CB  . LEU A 296  ? 0.1815 0.1633 0.2162 0.0028  -0.0033 0.0293  294  LEU A CB  
2068  C CG  . LEU A 296  ? 0.2175 0.1990 0.2551 0.0052  -0.0025 0.0283  294  LEU A CG  
2069  C CD1 . LEU A 296  ? 0.2237 0.2037 0.2639 0.0062  -0.0043 0.0285  294  LEU A CD1 
2070  C CD2 . LEU A 296  ? 0.2428 0.2265 0.2836 0.0056  -0.0022 0.0286  294  LEU A CD2 
2071  N N   . LEU A 297  ? 0.1882 0.1719 0.2155 -0.0011 -0.0032 0.0290  295  LEU A N   
2072  C CA  . LEU A 297  ? 0.2062 0.1922 0.2314 -0.0031 -0.0043 0.0294  295  LEU A CA  
2073  C C   . LEU A 297  ? 0.1921 0.1793 0.2167 -0.0036 -0.0032 0.0275  295  LEU A C   
2074  O O   . LEU A 297  ? 0.2020 0.1918 0.2269 -0.0048 -0.0042 0.0273  295  LEU A O   
2075  C CB  . LEU A 297  ? 0.2333 0.2193 0.2556 -0.0039 -0.0048 0.0298  295  LEU A CB  
2076  C CG  . LEU A 297  ? 0.2800 0.2697 0.3004 -0.0061 -0.0062 0.0306  295  LEU A CG  
2077  C CD1 . LEU A 297  ? 0.3158 0.3074 0.3385 -0.0070 -0.0084 0.0332  295  LEU A CD1 
2078  C CD2 . LEU A 297  ? 0.3252 0.3148 0.3428 -0.0067 -0.0063 0.0310  295  LEU A CD2 
2079  N N   . ALA A 298  ? 0.1759 0.1613 0.1997 -0.0026 -0.0014 0.0260  296  ALA A N   
2080  C CA  . ALA A 298  ? 0.1916 0.1777 0.2159 -0.0029 -0.0007 0.0244  296  ALA A CA  
2081  C C   . ALA A 298  ? 0.1933 0.1804 0.2212 -0.0029 -0.0010 0.0249  296  ALA A C   
2082  O O   . ALA A 298  ? 0.2060 0.1947 0.2349 -0.0039 -0.0016 0.0239  296  ALA A O   
2083  C CB  . ALA A 298  ? 0.1960 0.1800 0.2197 -0.0019 0.0012  0.0235  296  ALA A CB  
2084  N N   . LYS A 299  ? 0.1841 0.1705 0.2142 -0.0017 -0.0006 0.0262  297  LYS A N   
2085  C CA  A LYS A 299  ? 0.1839 0.1716 0.2176 -0.0017 -0.0010 0.0269  297  LYS A CA  
2086  C CA  B LYS A 299  ? 0.1843 0.1720 0.2180 -0.0017 -0.0010 0.0269  297  LYS A CA  
2087  C C   . LYS A 299  ? 0.2200 0.2099 0.2542 -0.0031 -0.0030 0.0274  297  LYS A C   
2088  O O   . LYS A 299  ? 0.2117 0.2031 0.2479 -0.0038 -0.0035 0.0270  297  LYS A O   
2089  C CB  A LYS A 299  ? 0.1875 0.1747 0.2234 0.0000  -0.0004 0.0279  297  LYS A CB  
2090  C CB  B LYS A 299  ? 0.1878 0.1750 0.2237 0.0000  -0.0004 0.0279  297  LYS A CB  
2091  C CG  A LYS A 299  ? 0.2074 0.1964 0.2471 0.0000  -0.0013 0.0289  297  LYS A CG  
2092  C CG  B LYS A 299  ? 0.2081 0.1970 0.2478 0.0001  -0.0011 0.0289  297  LYS A CG  
2093  C CD  A LYS A 299  ? 0.2350 0.2240 0.2771 0.0019  -0.0007 0.0294  297  LYS A CD  
2094  C CD  B LYS A 299  ? 0.2271 0.2162 0.2692 0.0020  -0.0001 0.0292  297  LYS A CD  
2095  C CE  A LYS A 299  ? 0.2446 0.2354 0.2904 0.0018  -0.0018 0.0305  297  LYS A CE  
2096  C CE  B LYS A 299  ? 0.2538 0.2446 0.2997 0.0022  -0.0011 0.0302  297  LYS A CE  
2097  N NZ  A LYS A 299  ? 0.2472 0.2387 0.2961 0.0038  -0.0011 0.0305  297  LYS A NZ  
2098  N NZ  B LYS A 299  ? 0.2666 0.2573 0.3126 0.0014  -0.0034 0.0311  297  LYS A NZ  
2099  N N   . ASN A 300  ? 0.2127 0.2030 0.2452 -0.0036 -0.0043 0.0284  298  ASN A N   
2100  C CA  . ASN A 300  ? 0.2024 0.1954 0.2355 -0.0050 -0.0064 0.0293  298  ASN A CA  
2101  C C   . ASN A 300  ? 0.2231 0.2186 0.2546 -0.0065 -0.0068 0.0276  298  ASN A C   
2102  O O   . ASN A 300  ? 0.2653 0.2634 0.2982 -0.0074 -0.0081 0.0274  298  ASN A O   
2103  C CB  . ASN A 300  ? 0.2513 0.2447 0.2836 -0.0054 -0.0079 0.0314  298  ASN A CB  
2104  C CG  . ASN A 300  ? 0.3839 0.3804 0.4176 -0.0067 -0.0101 0.0330  298  ASN A CG  
2105  O OD1 . ASN A 300  ? 0.4192 0.4157 0.4564 -0.0061 -0.0108 0.0342  298  ASN A OD1 
2106  N ND2 . ASN A 300  ? 0.3153 0.3152 0.3464 -0.0084 -0.0111 0.0329  298  ASN A ND2 
2107  N N   . TYR A 301  ? 0.2078 0.2029 0.2365 -0.0066 -0.0060 0.0259  299  TYR A N   
2108  C CA  . TYR A 301  ? 0.2021 0.1996 0.2297 -0.0077 -0.0064 0.0236  299  TYR A CA  
2109  C C   . TYR A 301  ? 0.2066 0.2028 0.2369 -0.0072 -0.0055 0.0217  299  TYR A C   
2110  O O   . TYR A 301  ? 0.2226 0.2207 0.2532 -0.0079 -0.0062 0.0193  299  TYR A O   
2111  C CB  . TYR A 301  ? 0.2046 0.2026 0.2284 -0.0081 -0.0060 0.0225  299  TYR A CB  
2112  C CG  . TYR A 301  ? 0.2096 0.2102 0.2307 -0.0091 -0.0072 0.0242  299  TYR A CG  
2113  C CD1 . TYR A 301  ? 0.2335 0.2393 0.2539 -0.0106 -0.0089 0.0241  299  TYR A CD1 
2114  C CD2 . TYR A 301  ? 0.2089 0.2075 0.2285 -0.0088 -0.0068 0.0260  299  TYR A CD2 
2115  C CE1 . TYR A 301  ? 0.2431 0.2520 0.2611 -0.0119 -0.0101 0.0263  299  TYR A CE1 
2116  C CE2 . TYR A 301  ? 0.2474 0.2486 0.2651 -0.0100 -0.0082 0.0280  299  TYR A CE2 
2117  C CZ  . TYR A 301  ? 0.2634 0.2699 0.2803 -0.0116 -0.0098 0.0285  299  TYR A CZ  
2118  O OH  . TYR A 301  ? 0.2607 0.2706 0.2759 -0.0130 -0.0111 0.0311  299  TYR A OH  
2119  N N   . ASP A 302  ? 0.1899 0.1833 0.2224 -0.0060 -0.0042 0.0227  300  ASP A N   
2120  C CA  . ASP A 302  ? 0.1967 0.1890 0.2323 -0.0056 -0.0033 0.0217  300  ASP A CA  
2121  C C   . ASP A 302  ? 0.2023 0.1938 0.2366 -0.0058 -0.0028 0.0194  300  ASP A C   
2122  O O   . ASP A 302  ? 0.2192 0.2114 0.2556 -0.0063 -0.0035 0.0174  300  ASP A O   
2123  C CB  . ASP A 302  ? 0.2328 0.2268 0.2722 -0.0063 -0.0045 0.0214  300  ASP A CB  
2124  C CG  . ASP A 302  ? 0.2818 0.2745 0.3254 -0.0058 -0.0036 0.0218  300  ASP A CG  
2125  O OD1 . ASP A 302  ? 0.2733 0.2642 0.3169 -0.0047 -0.0019 0.0233  300  ASP A OD1 
2126  O OD2 . ASP A 302  ? 0.2772 0.2709 0.3243 -0.0066 -0.0046 0.0207  300  ASP A OD2 
2127  N N   . ILE A 303  ? 0.1882 0.1781 0.2193 -0.0052 -0.0018 0.0196  301  ILE A N   
2128  C CA  . ILE A 303  ? 0.1826 0.1714 0.2125 -0.0051 -0.0011 0.0178  301  ILE A CA  
2129  C C   . ILE A 303  ? 0.2286 0.2147 0.2589 -0.0038 0.0007  0.0190  301  ILE A C   
2130  O O   . ILE A 303  ? 0.1941 0.1794 0.2243 -0.0030 0.0015  0.0210  301  ILE A O   
2131  C CB  . ILE A 303  ? 0.1978 0.1880 0.2234 -0.0056 -0.0015 0.0166  301  ILE A CB  
2132  C CG1 . ILE A 303  ? 0.1944 0.1831 0.2172 -0.0050 -0.0007 0.0186  301  ILE A CG1 
2133  C CG2 . ILE A 303  ? 0.2388 0.2330 0.2638 -0.0069 -0.0033 0.0158  301  ILE A CG2 
2134  C CD1 . ILE A 303  ? 0.2141 0.2039 0.2331 -0.0055 -0.0009 0.0178  301  ILE A CD1 
2135  N N   . GLY A 304  ? 0.2093 0.1941 0.2400 -0.0037 0.0012  0.0177  302  GLY A N   
2136  C CA  . GLY A 304  ? 0.2021 0.1848 0.2326 -0.0026 0.0029  0.0190  302  GLY A CA  
2137  C C   . GLY A 304  ? 0.2044 0.1863 0.2306 -0.0020 0.0036  0.0191  302  GLY A C   
2138  O O   . GLY A 304  ? 0.2190 0.2016 0.2425 -0.0026 0.0029  0.0178  302  GLY A O   
2139  N N   . LEU A 305  ? 0.2040 0.1848 0.2298 -0.0008 0.0049  0.0207  303  LEU A N   
2140  C CA  . LEU A 305  ? 0.1968 0.1766 0.2192 -0.0001 0.0056  0.0208  303  LEU A CA  
2141  C C   . LEU A 305  ? 0.2172 0.1961 0.2400 0.0010  0.0072  0.0214  303  LEU A C   
2142  O O   . LEU A 305  ? 0.2042 0.1838 0.2288 0.0018  0.0080  0.0228  303  LEU A O   
2143  C CB  . LEU A 305  ? 0.2090 0.1890 0.2307 0.0005  0.0054  0.0219  303  LEU A CB  
2144  C CG  . LEU A 305  ? 0.2476 0.2264 0.2663 0.0012  0.0056  0.0217  303  LEU A CG  
2145  C CD1 . LEU A 305  ? 0.2805 0.2595 0.2988 0.0009  0.0043  0.0225  303  LEU A CD1 
2146  C CD2 . LEU A 305  ? 0.2950 0.2730 0.3137 0.0028  0.0071  0.0220  303  LEU A CD2 
2147  N N   . ASN A 306  ? 0.2018 0.1797 0.2231 0.0009  0.0075  0.0203  304  ASN A N   
2148  C CA  . ASN A 306  ? 0.2083 0.1856 0.2302 0.0017  0.0087  0.0211  304  ASN A CA  
2149  C C   . ASN A 306  ? 0.2152 0.1917 0.2336 0.0027  0.0096  0.0209  304  ASN A C   
2150  O O   . ASN A 306  ? 0.2145 0.1902 0.2302 0.0024  0.0091  0.0197  304  ASN A O   
2151  C CB  . ASN A 306  ? 0.1868 0.1634 0.2102 0.0010  0.0082  0.0200  304  ASN A CB  
2152  C CG  . ASN A 306  ? 0.2367 0.2126 0.2604 0.0016  0.0092  0.0209  304  ASN A CG  
2153  O OD1 . ASN A 306  ? 0.2783 0.2533 0.2993 0.0020  0.0096  0.0200  304  ASN A OD1 
2154  N ND2 . ASN A 306  ? 0.2124 0.1893 0.2394 0.0017  0.0097  0.0231  304  ASN A ND2 
2155  N N   . ILE A 307  ? 0.1892 0.1664 0.2078 0.0039  0.0108  0.0222  305  ILE A N   
2156  C CA  . ILE A 307  ? 0.2050 0.1818 0.2208 0.0050  0.0116  0.0218  305  ILE A CA  
2157  C C   . ILE A 307  ? 0.1766 0.1529 0.1921 0.0050  0.0122  0.0219  305  ILE A C   
2158  O O   . ILE A 307  ? 0.1986 0.1761 0.2162 0.0052  0.0129  0.0235  305  ILE A O   
2159  C CB  . ILE A 307  ? 0.2412 0.2198 0.2573 0.0065  0.0126  0.0226  305  ILE A CB  
2160  C CG1 . ILE A 307  ? 0.2527 0.2315 0.2696 0.0066  0.0117  0.0223  305  ILE A CG1 
2161  C CG2 . ILE A 307  ? 0.2389 0.2174 0.2522 0.0077  0.0133  0.0218  305  ILE A CG2 
2162  C CD1 . ILE A 307  ? 0.3121 0.2934 0.3305 0.0080  0.0125  0.0228  305  ILE A CD1 
2163  N N   . ASP A 308  ? 0.1919 0.1665 0.2050 0.0046  0.0118  0.0204  306  ASP A N   
2164  C CA  . ASP A 308  ? 0.1968 0.1708 0.2097 0.0047  0.0122  0.0203  306  ASP A CA  
2165  C C   . ASP A 308  ? 0.2208 0.1959 0.2325 0.0060  0.0134  0.0214  306  ASP A C   
2166  O O   . ASP A 308  ? 0.2145 0.1903 0.2245 0.0070  0.0138  0.0212  306  ASP A O   
2167  C CB  . ASP A 308  ? 0.2100 0.1826 0.2205 0.0042  0.0115  0.0183  306  ASP A CB  
2168  C CG  . ASP A 308  ? 0.2926 0.2651 0.3043 0.0029  0.0103  0.0169  306  ASP A CG  
2169  O OD1 . ASP A 308  ? 0.2470 0.2200 0.2620 0.0024  0.0098  0.0173  306  ASP A OD1 
2170  O OD2 . ASP A 308  ? 0.2841 0.2565 0.2937 0.0024  0.0097  0.0153  306  ASP A OD2 
2171  N N   . ALA A 309  ? 0.1840 0.1595 0.1970 0.0060  0.0139  0.0225  307  ALA A N   
2172  C CA  . ALA A 309  ? 0.1817 0.1590 0.1934 0.0072  0.0150  0.0237  307  ALA A CA  
2173  C C   . ALA A 309  ? 0.2078 0.1836 0.2165 0.0076  0.0150  0.0223  307  ALA A C   
2174  O O   . ALA A 309  ? 0.2102 0.1841 0.2192 0.0068  0.0143  0.0214  307  ALA A O   
2175  C CB  . ALA A 309  ? 0.2109 0.1902 0.2258 0.0069  0.0155  0.0265  307  ALA A CB  
2176  N N   . GLU A 310  ? 0.1876 0.1646 0.1938 0.0088  0.0158  0.0219  308  GLU A N   
2177  C CA  . GLU A 310  ? 0.1897 0.1654 0.1930 0.0092  0.0157  0.0205  308  GLU A CA  
2178  C C   . GLU A 310  ? 0.2029 0.1809 0.2055 0.0102  0.0166  0.0216  308  GLU A C   
2179  O O   . GLU A 310  ? 0.2029 0.1824 0.2076 0.0099  0.0169  0.0238  308  GLU A O   
2180  C CB  . GLU A 310  ? 0.2015 0.1761 0.2027 0.0096  0.0152  0.0185  308  GLU A CB  
2181  C CG  . GLU A 310  ? 0.2251 0.1980 0.2271 0.0084  0.0142  0.0179  308  GLU A CG  
2182  C CD  . GLU A 310  ? 0.2570 0.2288 0.2574 0.0085  0.0134  0.0166  308  GLU A CD  
2183  O OE1 . GLU A 310  ? 0.2700 0.2405 0.2686 0.0083  0.0130  0.0157  308  GLU A OE1 
2184  O OE2 . GLU A 310  ? 0.2391 0.2113 0.2405 0.0088  0.0130  0.0168  308  GLU A OE2 
2185  N N   . GLU A 311  ? 0.2122 0.1907 0.2120 0.0113  0.0168  0.0202  309  GLU A N   
2186  C CA  . GLU A 311  ? 0.2181 0.1991 0.2167 0.0123  0.0176  0.0211  309  GLU A CA  
2187  C C   . GLU A 311  ? 0.1739 0.1597 0.1737 0.0131  0.0187  0.0229  309  GLU A C   
2188  O O   . GLU A 311  ? 0.1908 0.1779 0.1916 0.0134  0.0189  0.0227  309  GLU A O   
2189  C CB  . GLU A 311  ? 0.2299 0.2106 0.2256 0.0134  0.0175  0.0188  309  GLU A CB  
2190  C CG  . GLU A 311  ? 0.2437 0.2207 0.2381 0.0126  0.0166  0.0173  309  GLU A CG  
2191  C CD  . GLU A 311  ? 0.3048 0.2791 0.2992 0.0120  0.0157  0.0158  309  GLU A CD  
2192  O OE1 . GLU A 311  ? 0.2420 0.2167 0.2377 0.0119  0.0156  0.0161  309  GLU A OE1 
2193  O OE2 . GLU A 311  ? 0.3435 0.3157 0.3366 0.0115  0.0150  0.0145  309  GLU A OE2 
2194  N N   . ALA A 312  ? 0.1823 0.1712 0.1820 0.0134  0.0193  0.0249  310  ALA A N   
2195  C CA  . ALA A 312  ? 0.1973 0.1918 0.1981 0.0139  0.0204  0.0272  310  ALA A CA  
2196  C C   . ALA A 312  ? 0.2000 0.1978 0.1991 0.0157  0.0211  0.0250  310  ALA A C   
2197  O O   . ALA A 312  ? 0.2092 0.2110 0.2098 0.0160  0.0218  0.0261  310  ALA A O   
2198  C CB  . ALA A 312  ? 0.1985 0.1963 0.1992 0.0139  0.0209  0.0299  310  ALA A CB  
2199  N N   . ASP A 313  ? 0.2062 0.2027 0.2028 0.0168  0.0207  0.0219  311  ASP A N   
2200  C CA  . ASP A 313  ? 0.2087 0.2083 0.2044 0.0186  0.0210  0.0192  311  ASP A CA  
2201  C C   . ASP A 313  ? 0.2072 0.2043 0.2045 0.0187  0.0204  0.0177  311  ASP A C   
2202  O O   . ASP A 313  ? 0.2325 0.2318 0.2299 0.0203  0.0203  0.0153  311  ASP A O   
2203  C CB  . ASP A 313  ? 0.2293 0.2287 0.2224 0.0200  0.0206  0.0164  311  ASP A CB  
2204  C CG  . ASP A 313  ? 0.3155 0.3084 0.3079 0.0192  0.0192  0.0145  311  ASP A CG  
2205  O OD1 . ASP A 313  ? 0.2830 0.2718 0.2767 0.0177  0.0186  0.0152  311  ASP A OD1 
2206  O OD2 . ASP A 313  ? 0.3459 0.3382 0.3365 0.0201  0.0187  0.0122  311  ASP A OD2 
2207  N N   . ARG A 314  ? 0.1964 0.1894 0.1953 0.0170  0.0197  0.0189  312  ARG A N   
2208  C CA  . ARG A 314  ? 0.1888 0.1799 0.1894 0.0167  0.0190  0.0181  312  ARG A CA  
2209  C C   . ARG A 314  ? 0.2129 0.2062 0.2162 0.0160  0.0196  0.0205  312  ARG A C   
2210  O O   . ARG A 314  ? 0.2088 0.2015 0.2138 0.0160  0.0192  0.0199  312  ARG A O   
2211  C CB  . ARG A 314  ? 0.2206 0.2059 0.2209 0.0153  0.0177  0.0173  312  ARG A CB  
2212  C CG  . ARG A 314  ? 0.2682 0.2515 0.2668 0.0161  0.0168  0.0148  312  ARG A CG  
2213  C CD  . ARG A 314  ? 0.2756 0.2544 0.2733 0.0145  0.0158  0.0146  312  ARG A CD  
2214  N NE  . ARG A 314  ? 0.2605 0.2372 0.2576 0.0150  0.0146  0.0126  312  ARG A NE  
2215  C CZ  . ARG A 314  ? 0.2478 0.2213 0.2439 0.0139  0.0136  0.0122  312  ARG A CZ  
2216  N NH1 . ARG A 314  ? 0.2607 0.2330 0.2561 0.0124  0.0138  0.0132  312  ARG A NH1 
2217  N NH2 . ARG A 314  ? 0.2689 0.2408 0.2653 0.0142  0.0124  0.0107  312  ARG A NH2 
2218  N N   . LEU A 315  ? 0.2027 0.1989 0.2069 0.0154  0.0205  0.0234  313  LEU A N   
2219  C CA  . LEU A 315  ? 0.2137 0.2119 0.2210 0.0145  0.0209  0.0261  313  LEU A CA  
2220  C C   . LEU A 315  ? 0.1969 0.1995 0.2052 0.0158  0.0216  0.0255  313  LEU A C   
2221  O O   . LEU A 315  ? 0.1994 0.2009 0.2098 0.0153  0.0212  0.0255  313  LEU A O   
2222  C CB  . LEU A 315  ? 0.2045 0.2056 0.2128 0.0137  0.0215  0.0296  313  LEU A CB  
2223  C CG  . LEU A 315  ? 0.2095 0.2106 0.2219 0.0120  0.0213  0.0329  313  LEU A CG  
2224  C CD1 . LEU A 315  ? 0.2180 0.2219 0.2317 0.0113  0.0216  0.0365  313  LEU A CD1 
2225  C CD2 . LEU A 315  ? 0.2386 0.2434 0.2532 0.0122  0.0219  0.0338  313  LEU A CD2 
2226  N N   . GLU A 316  ? 0.1829 0.1911 0.1899 0.0175  0.0227  0.0249  314  GLU A N   
2227  C CA  . GLU A 316  ? 0.2034 0.2170 0.2120 0.0188  0.0235  0.0243  314  GLU A CA  
2228  C C   . GLU A 316  ? 0.2248 0.2355 0.2338 0.0199  0.0225  0.0207  314  GLU A C   
2229  O O   . GLU A 316  ? 0.2261 0.2385 0.2375 0.0202  0.0225  0.0207  314  GLU A O   
2230  C CB  . GLU A 316  ? 0.2295 0.2510 0.2367 0.0203  0.0249  0.0244  314  GLU A CB  
2231  C CG  . GLU A 316  ? 0.2473 0.2725 0.2553 0.0189  0.0258  0.0292  314  GLU A CG  
2232  C CD  . GLU A 316  ? 0.2469 0.2810 0.2534 0.0203  0.0272  0.0299  314  GLU A CD  
2233  O OE1 . GLU A 316  ? 0.2727 0.3125 0.2792 0.0221  0.0280  0.0278  314  GLU A OE1 
2234  O OE2 . GLU A 316  ? 0.2450 0.2806 0.2505 0.0195  0.0275  0.0327  314  GLU A OE2 
2235  N N   . LEU A 317  ? 0.2158 0.2220 0.2229 0.0203  0.0213  0.0180  315  LEU A N   
2236  C CA  . LEU A 317  ? 0.2327 0.2356 0.2410 0.0209  0.0200  0.0153  315  LEU A CA  
2237  C C   . LEU A 317  ? 0.2314 0.2305 0.2417 0.0192  0.0191  0.0169  315  LEU A C   
2238  O O   . LEU A 317  ? 0.2289 0.2282 0.2415 0.0197  0.0186  0.0160  315  LEU A O   
2239  C CB  . LEU A 317  ? 0.2469 0.2454 0.2531 0.0212  0.0188  0.0129  315  LEU A CB  
2240  C CG  . LEU A 317  ? 0.2663 0.2611 0.2742 0.0217  0.0170  0.0105  315  LEU A CG  
2241  C CD1 . LEU A 317  ? 0.2824 0.2813 0.2926 0.0240  0.0170  0.0080  315  LEU A CD1 
2242  C CD2 . LEU A 317  ? 0.3025 0.2936 0.3086 0.0217  0.0158  0.0087  315  LEU A CD2 
2243  N N   . SER A 318  ? 0.2017 0.1976 0.2115 0.0172  0.0190  0.0191  316  SER A N   
2244  C CA  . SER A 318  ? 0.1998 0.1926 0.2115 0.0155  0.0181  0.0203  316  SER A CA  
2245  C C   . SER A 318  ? 0.2087 0.2051 0.2233 0.0155  0.0187  0.0220  316  SER A C   
2246  O O   . SER A 318  ? 0.2109 0.2056 0.2276 0.0148  0.0179  0.0221  316  SER A O   
2247  C CB  . SER A 318  ? 0.1906 0.1799 0.2015 0.0136  0.0177  0.0217  316  SER A CB  
2248  O OG  . SER A 318  ? 0.2080 0.2000 0.2200 0.0130  0.0187  0.0243  316  SER A OG  
2249  N N   . LEU A 319  ? 0.1925 0.1943 0.2076 0.0161  0.0202  0.0234  317  LEU A N   
2250  C CA  . LEU A 319  ? 0.2130 0.2192 0.2310 0.0161  0.0210  0.0252  317  LEU A CA  
2251  C C   . LEU A 319  ? 0.2067 0.2148 0.2261 0.0178  0.0208  0.0228  317  LEU A C   
2252  O O   . LEU A 319  ? 0.2083 0.2175 0.2305 0.0175  0.0207  0.0237  317  LEU A O   
2253  C CB  . LEU A 319  ? 0.1937 0.2063 0.2118 0.0164  0.0227  0.0276  317  LEU A CB  
2254  C CG  . LEU A 319  ? 0.2406 0.2517 0.2588 0.0146  0.0227  0.0307  317  LEU A CG  
2255  C CD1 . LEU A 319  ? 0.2318 0.2502 0.2503 0.0150  0.0242  0.0335  317  LEU A CD1 
2256  C CD2 . LEU A 319  ? 0.2387 0.2465 0.2600 0.0126  0.0218  0.0327  317  LEU A CD2 
2257  N N   . ASP A 320  ? 0.2114 0.2198 0.2293 0.0197  0.0205  0.0196  318  ASP A N   
2258  C CA  . ASP A 320  ? 0.2301 0.2397 0.2501 0.0214  0.0199  0.0170  318  ASP A CA  
2259  C C   . ASP A 320  ? 0.2446 0.2484 0.2661 0.0203  0.0181  0.0168  318  ASP A C   
2260  O O   . ASP A 320  ? 0.2484 0.2534 0.2729 0.0209  0.0176  0.0163  318  ASP A O   
2261  C CB  . ASP A 320  ? 0.2245 0.2355 0.2432 0.0237  0.0197  0.0133  318  ASP A CB  
2262  C CG  . ASP A 320  ? 0.2935 0.3124 0.3113 0.0253  0.0216  0.0131  318  ASP A CG  
2263  O OD1 . ASP A 320  ? 0.3002 0.3249 0.3202 0.0259  0.0227  0.0137  318  ASP A OD1 
2264  O OD2 . ASP A 320  ? 0.3401 0.3598 0.3551 0.0257  0.0221  0.0124  318  ASP A OD2 
2265  N N   . LEU A 321  ? 0.2207 0.2190 0.2405 0.0187  0.0170  0.0174  319  LEU A N   
2266  C CA  . LEU A 321  ? 0.2191 0.2130 0.2402 0.0174  0.0153  0.0177  319  LEU A CA  
2267  C C   . LEU A 321  ? 0.2161 0.2106 0.2391 0.0158  0.0156  0.0202  319  LEU A C   
2268  O O   . LEU A 321  ? 0.2424 0.2365 0.2679 0.0156  0.0146  0.0203  319  LEU A O   
2269  C CB  . LEU A 321  ? 0.2342 0.2229 0.2527 0.0160  0.0142  0.0175  319  LEU A CB  
2270  C CG  . LEU A 321  ? 0.2736 0.2606 0.2915 0.0173  0.0131  0.0150  319  LEU A CG  
2271  C CD1 . LEU A 321  ? 0.3066 0.2954 0.3220 0.0184  0.0143  0.0140  319  LEU A CD1 
2272  C CD2 . LEU A 321  ? 0.3510 0.3331 0.3680 0.0156  0.0114  0.0154  319  LEU A CD2 
2273  N N   . LEU A 322  ? 0.2093 0.2049 0.2317 0.0147  0.0166  0.0223  320  LEU A N   
2274  C CA  . LEU A 322  ? 0.2062 0.2025 0.2311 0.0132  0.0167  0.0246  320  LEU A CA  
2275  C C   . LEU A 322  ? 0.2038 0.2047 0.2317 0.0142  0.0173  0.0250  320  LEU A C   
2276  O O   . LEU A 322  ? 0.2233 0.2237 0.2538 0.0134  0.0166  0.0258  320  LEU A O   
2277  C CB  . LEU A 322  ? 0.2130 0.2102 0.2375 0.0121  0.0176  0.0269  320  LEU A CB  
2278  C CG  . LEU A 322  ? 0.2315 0.2292 0.2594 0.0104  0.0174  0.0293  320  LEU A CG  
2279  C CD1 . LEU A 322  ? 0.1971 0.1900 0.2251 0.0089  0.0157  0.0286  320  LEU A CD1 
2280  C CD2 . LEU A 322  ? 0.1994 0.1989 0.2281 0.0096  0.0183  0.0319  320  LEU A CD2 
2281  N N   . GLU A 323  ? 0.2065 0.2123 0.2342 0.0161  0.0187  0.0243  321  GLU A N   
2282  C CA  . GLU A 323  ? 0.2226 0.2338 0.2532 0.0173  0.0195  0.0244  321  GLU A CA  
2283  C C   . GLU A 323  ? 0.2545 0.2638 0.2872 0.0180  0.0180  0.0224  321  GLU A C   
2284  O O   . GLU A 323  ? 0.2222 0.2327 0.2579 0.0176  0.0178  0.0234  321  GLU A O   
2285  C CB  . GLU A 323  ? 0.2376 0.2551 0.2673 0.0194  0.0211  0.0232  321  GLU A CB  
2286  C CG  . GLU A 323  ? 0.3112 0.3351 0.3438 0.0212  0.0219  0.0222  321  GLU A CG  
2287  C CD  . GLU A 323  ? 0.3398 0.3710 0.3738 0.0208  0.0238  0.0253  321  GLU A CD  
2288  O OE1 . GLU A 323  ? 0.3444 0.3758 0.3772 0.0193  0.0245  0.0282  321  GLU A OE1 
2289  O OE2 . GLU A 323  ? 0.3645 0.4015 0.4011 0.0220  0.0245  0.0249  321  GLU A OE2 
2290  N N   . VAL A 324  ? 0.2089 0.2150 0.2403 0.0191  0.0168  0.0197  322  VAL A N   
2291  C CA  . VAL A 324  ? 0.2194 0.2236 0.2534 0.0198  0.0151  0.0180  322  VAL A CA  
2292  C C   . VAL A 324  ? 0.2035 0.2038 0.2385 0.0176  0.0137  0.0200  322  VAL A C   
2293  O O   . VAL A 324  ? 0.2307 0.2317 0.2689 0.0177  0.0129  0.0202  322  VAL A O   
2294  C CB  . VAL A 324  ? 0.2720 0.2733 0.3051 0.0211  0.0138  0.0152  322  VAL A CB  
2295  C CG1 . VAL A 324  ? 0.2621 0.2611 0.2987 0.0216  0.0116  0.0140  322  VAL A CG1 
2296  C CG2 . VAL A 324  ? 0.2648 0.2707 0.2973 0.0235  0.0150  0.0127  322  VAL A CG2 
2297  N N   . LEU A 325  ? 0.1944 0.1909 0.2269 0.0157  0.0133  0.0212  323  LEU A N   
2298  C CA  . LEU A 325  ? 0.2188 0.2121 0.2519 0.0136  0.0119  0.0226  323  LEU A CA  
2299  C C   . LEU A 325  ? 0.2121 0.2081 0.2480 0.0128  0.0125  0.0245  323  LEU A C   
2300  O O   . LEU A 325  ? 0.2018 0.1973 0.2400 0.0121  0.0112  0.0250  323  LEU A O   
2301  C CB  . LEU A 325  ? 0.2040 0.1937 0.2340 0.0119  0.0115  0.0231  323  LEU A CB  
2302  C CG  . LEU A 325  ? 0.2470 0.2338 0.2745 0.0124  0.0107  0.0215  323  LEU A CG  
2303  C CD1 . LEU A 325  ? 0.2390 0.2236 0.2633 0.0111  0.0109  0.0218  323  LEU A CD1 
2304  C CD2 . LEU A 325  ? 0.2392 0.2237 0.2680 0.0119  0.0085  0.0214  323  LEU A CD2 
2305  N N   . CYS A 326  ? 0.2177 0.2168 0.2536 0.0127  0.0142  0.0258  324  CYS A N   
2306  C CA  . CYS A 326  ? 0.1868 0.1884 0.2258 0.0117  0.0146  0.0280  324  CYS A CA  
2307  C C   . CYS A 326  ? 0.2222 0.2280 0.2646 0.0130  0.0149  0.0278  324  CYS A C   
2308  O O   . CYS A 326  ? 0.2252 0.2321 0.2705 0.0121  0.0146  0.0293  324  CYS A O   
2309  C CB  . CYS A 326  ? 0.1944 0.1985 0.2333 0.0110  0.0161  0.0301  324  CYS A CB  
2310  S SG  . CYS A 326  ? 0.2712 0.2703 0.3078 0.0091  0.0153  0.0305  324  CYS A SG  
2311  N N   . LEU A 327  ? 0.2043 0.2124 0.2465 0.0153  0.0154  0.0257  325  LEU A N   
2312  C CA  . LEU A 327  ? 0.2087 0.2209 0.2542 0.0169  0.0156  0.0249  325  LEU A CA  
2313  C C   . LEU A 327  ? 0.2164 0.2254 0.2637 0.0174  0.0134  0.0232  325  LEU A C   
2314  O O   . LEU A 327  ? 0.2447 0.2567 0.2954 0.0187  0.0132  0.0224  325  LEU A O   
2315  C CB  . LEU A 327  ? 0.2134 0.2310 0.2585 0.0194  0.0172  0.0231  325  LEU A CB  
2316  C CG  . LEU A 327  ? 0.2913 0.3138 0.3353 0.0189  0.0194  0.0253  325  LEU A CG  
2317  C CD1 . LEU A 327  ? 0.2742 0.3025 0.3172 0.0214  0.0209  0.0231  325  LEU A CD1 
2318  C CD2 . LEU A 327  ? 0.3180 0.3442 0.3652 0.0177  0.0201  0.0283  325  LEU A CD2 
2319  N N   . ASP A 328  ? 0.2180 0.2215 0.2633 0.0164  0.0118  0.0230  326  ASP A N   
2320  C CA  . ASP A 328  ? 0.1942 0.1947 0.2412 0.0166  0.0095  0.0220  326  ASP A CA  
2321  C C   . ASP A 328  ? 0.1996 0.1995 0.2489 0.0150  0.0083  0.0239  326  ASP A C   
2322  O O   . ASP A 328  ? 0.2086 0.2063 0.2563 0.0128  0.0079  0.0254  326  ASP A O   
2323  C CB  . ASP A 328  ? 0.2335 0.2290 0.2774 0.0158  0.0082  0.0215  326  ASP A CB  
2324  C CG  . ASP A 328  ? 0.2733 0.2661 0.3193 0.0162  0.0057  0.0207  326  ASP A CG  
2325  O OD1 . ASP A 328  ? 0.2789 0.2719 0.3280 0.0158  0.0044  0.0216  326  ASP A OD1 
2326  O OD2 . ASP A 328  ? 0.3340 0.3245 0.3789 0.0169  0.0049  0.0193  326  ASP A OD2 
2327  N N   . GLY A 329  ? 0.1948 0.1968 0.2482 0.0161  0.0076  0.0234  327  GLY A N   
2328  C CA  . GLY A 329  ? 0.2102 0.2123 0.2661 0.0147  0.0066  0.0252  327  GLY A CA  
2329  C C   . GLY A 329  ? 0.2372 0.2349 0.2919 0.0128  0.0043  0.0262  327  GLY A C   
2330  O O   . GLY A 329  ? 0.2221 0.2197 0.2775 0.0111  0.0036  0.0277  327  GLY A O   
2331  N N   . ASP A 330  ? 0.2183 0.2128 0.2713 0.0130  0.0031  0.0253  328  ASP A N   
2332  C CA  . ASP A 330  ? 0.2208 0.2121 0.2725 0.0111  0.0009  0.0265  328  ASP A CA  
2333  C C   . ASP A 330  ? 0.2098 0.2002 0.2580 0.0089  0.0015  0.0275  328  ASP A C   
2334  O O   . ASP A 330  ? 0.2102 0.1994 0.2576 0.0071  0.0000  0.0286  328  ASP A O   
2335  C CB  . ASP A 330  ? 0.2371 0.2254 0.2878 0.0116  -0.0005 0.0258  328  ASP A CB  
2336  C CG  . ASP A 330  ? 0.3071 0.2955 0.3623 0.0135  -0.0020 0.0248  328  ASP A CG  
2337  O OD1 . ASP A 330  ? 0.3466 0.3370 0.4057 0.0140  -0.0025 0.0251  328  ASP A OD1 
2338  O OD2 . ASP A 330  ? 0.2879 0.2744 0.3432 0.0145  -0.0028 0.0235  328  ASP A OD2 
2339  N N   . LEU A 331  ? 0.1898 0.1811 0.2361 0.0091  0.0037  0.0271  329  LEU A N   
2340  C CA  . LEU A 331  ? 0.2024 0.1928 0.2461 0.0072  0.0041  0.0277  329  LEU A CA  
2341  C C   . LEU A 331  ? 0.2174 0.2100 0.2634 0.0064  0.0048  0.0288  329  LEU A C   
2342  O O   . LEU A 331  ? 0.2238 0.2159 0.2687 0.0050  0.0051  0.0291  329  LEU A O   
2343  C CB  . LEU A 331  ? 0.2067 0.1962 0.2472 0.0077  0.0057  0.0269  329  LEU A CB  
2344  C CG  . LEU A 331  ? 0.2082 0.1949 0.2459 0.0079  0.0048  0.0260  329  LEU A CG  
2345  C CD1 . LEU A 331  ? 0.2240 0.2104 0.2591 0.0088  0.0064  0.0250  329  LEU A CD1 
2346  C CD2 . LEU A 331  ? 0.2109 0.1959 0.2467 0.0058  0.0033  0.0265  329  LEU A CD2 
2347  N N   . SER A 332  ? 0.2164 0.2116 0.2661 0.0072  0.0049  0.0293  330  SER A N   
2348  C CA  . SER A 332  ? 0.2439 0.2416 0.2963 0.0065  0.0056  0.0305  330  SER A CA  
2349  C C   . SER A 332  ? 0.2141 0.2107 0.2670 0.0044  0.0040  0.0311  330  SER A C   
2350  O O   . SER A 332  ? 0.2691 0.2642 0.3211 0.0037  0.0021  0.0308  330  SER A O   
2351  C CB  . SER A 332  ? 0.2471 0.2484 0.3034 0.0080  0.0061  0.0308  330  SER A CB  
2352  O OG  . SER A 332  ? 0.2765 0.2773 0.3348 0.0079  0.0042  0.0308  330  SER A OG  
2353  N N   . GLY A 333  ? 0.2164 0.2141 0.2711 0.0033  0.0044  0.0319  331  GLY A N   
2354  C CA  . GLY A 333  ? 0.2231 0.2201 0.2787 0.0014  0.0028  0.0320  331  GLY A CA  
2355  C C   . GLY A 333  ? 0.2388 0.2335 0.2914 0.0002  0.0024  0.0309  331  GLY A C   
2356  O O   . GLY A 333  ? 0.2757 0.2701 0.3290 -0.0013 0.0010  0.0303  331  GLY A O   
2357  N N   . TRP A 334  ? 0.2104 0.2035 0.2597 0.0009  0.0035  0.0303  332  TRP A N   
2358  C CA  . TRP A 334  ? 0.2409 0.2320 0.2873 0.0000  0.0032  0.0291  332  TRP A CA  
2359  C C   . TRP A 334  ? 0.2025 0.1934 0.2491 0.0004  0.0049  0.0295  332  TRP A C   
2360  O O   . TRP A 334  ? 0.2233 0.2150 0.2692 0.0018  0.0064  0.0301  332  TRP A O   
2361  C CB  . TRP A 334  ? 0.2073 0.1968 0.2498 0.0005  0.0028  0.0282  332  TRP A CB  
2362  C CG  . TRP A 334  ? 0.1949 0.1827 0.2340 -0.0001 0.0029  0.0269  332  TRP A CG  
2363  C CD1 . TRP A 334  ? 0.1874 0.1750 0.2257 -0.0015 0.0018  0.0257  332  TRP A CD1 
2364  C CD2 . TRP A 334  ? 0.2102 0.1965 0.2462 0.0008  0.0039  0.0265  332  TRP A CD2 
2365  N NE1 . TRP A 334  ? 0.1916 0.1777 0.2266 -0.0015 0.0022  0.0246  332  TRP A NE1 
2366  C CE2 . TRP A 334  ? 0.1917 0.1769 0.2252 -0.0001 0.0035  0.0252  332  TRP A CE2 
2367  C CE3 . TRP A 334  ? 0.2126 0.1988 0.2480 0.0025  0.0052  0.0268  332  TRP A CE3 
2368  C CZ2 . TRP A 334  ? 0.1852 0.1688 0.2156 0.0004  0.0043  0.0246  332  TRP A CZ2 
2369  C CZ3 . TRP A 334  ? 0.2102 0.1948 0.2425 0.0030  0.0059  0.0260  332  TRP A CZ3 
2370  C CH2 . TRP A 334  ? 0.2163 0.1996 0.2461 0.0019  0.0055  0.0251  332  TRP A CH2 
2371  N N   . ASN A 335  ? 0.1943 0.1845 0.2421 -0.0008 0.0045  0.0291  333  ASN A N   
2372  C CA  . ASN A 335  ? 0.1896 0.1795 0.2381 -0.0007 0.0057  0.0298  333  ASN A CA  
2373  C C   . ASN A 335  ? 0.1967 0.1842 0.2418 -0.0008 0.0056  0.0282  333  ASN A C   
2374  O O   . ASN A 335  ? 0.2115 0.1984 0.2577 -0.0011 0.0060  0.0285  333  ASN A O   
2375  C CB  . ASN A 335  ? 0.2074 0.1982 0.2611 -0.0019 0.0051  0.0309  333  ASN A CB  
2376  C CG  . ASN A 335  ? 0.2412 0.2350 0.2986 -0.0015 0.0059  0.0333  333  ASN A CG  
2377  O OD1 . ASN A 335  ? 0.2090 0.2046 0.2651 -0.0002 0.0074  0.0343  333  ASN A OD1 
2378  N ND2 . ASN A 335  ? 0.3229 0.3175 0.3850 -0.0027 0.0048  0.0341  333  ASN A ND2 
2379  N N   . GLY A 336  ? 0.2034 0.1898 0.2448 -0.0008 0.0049  0.0266  334  GLY A N   
2380  C CA  . GLY A 336  ? 0.1800 0.1647 0.2183 -0.0010 0.0048  0.0249  334  GLY A CA  
2381  C C   . GLY A 336  ? 0.1777 0.1613 0.2130 0.0001  0.0063  0.0252  334  GLY A C   
2382  O O   . GLY A 336  ? 0.1826 0.1648 0.2156 -0.0001 0.0062  0.0239  334  GLY A O   
2383  N N   . MET A 337  ? 0.1867 0.1714 0.2221 0.0014  0.0075  0.0266  335  MET A N   
2384  C CA  A MET A 337  ? 0.1966 0.1807 0.2292 0.0025  0.0088  0.0265  335  MET A CA  
2385  C CA  B MET A 337  ? 0.1967 0.1808 0.2293 0.0025  0.0088  0.0265  335  MET A CA  
2386  C C   . MET A 337  ? 0.1952 0.1792 0.2288 0.0023  0.0096  0.0271  335  MET A C   
2387  O O   . MET A 337  ? 0.2070 0.1926 0.2442 0.0019  0.0099  0.0289  335  MET A O   
2388  C CB  A MET A 337  ? 0.2262 0.2124 0.2592 0.0041  0.0100  0.0274  335  MET A CB  
2389  C CB  B MET A 337  ? 0.2260 0.2120 0.2588 0.0041  0.0099  0.0273  335  MET A CB  
2390  C CG  A MET A 337  ? 0.2566 0.2426 0.2867 0.0054  0.0111  0.0268  335  MET A CG  
2391  C CG  B MET A 337  ? 0.2583 0.2444 0.2885 0.0054  0.0113  0.0270  335  MET A CG  
2392  S SD  A MET A 337  ? 0.3321 0.3151 0.3584 0.0055  0.0100  0.0249  335  MET A SD  
2393  S SD  B MET A 337  ? 0.2906 0.2770 0.3193 0.0071  0.0113  0.0259  335  MET A SD  
2394  C CE  A MET A 337  ? 0.2917 0.2757 0.3196 0.0065  0.0092  0.0249  335  MET A CE  
2395  C CE  B MET A 337  ? 0.2514 0.2346 0.2781 0.0060  0.0093  0.0247  335  MET A CE  
2396  N N   . GLY A 338  ? 0.1962 0.1784 0.2269 0.0023  0.0097  0.0260  336  GLY A N   
2397  C CA  . GLY A 338  ? 0.2240 0.2057 0.2556 0.0021  0.0102  0.0265  336  GLY A CA  
2398  C C   . GLY A 338  ? 0.2109 0.1926 0.2395 0.0033  0.0115  0.0267  336  GLY A C   
2399  O O   . GLY A 338  ? 0.1989 0.1802 0.2243 0.0041  0.0117  0.0257  336  GLY A O   
2400  N N   . PHE A 339  ? 0.1944 0.1766 0.2242 0.0033  0.0121  0.0281  337  PHE A N   
2401  C CA  . PHE A 339  ? 0.1938 0.1769 0.2210 0.0044  0.0134  0.0285  337  PHE A CA  
2402  C C   . PHE A 339  ? 0.1915 0.1739 0.2201 0.0039  0.0134  0.0296  337  PHE A C   
2403  O O   . PHE A 339  ? 0.1962 0.1794 0.2291 0.0030  0.0130  0.0315  337  PHE A O   
2404  C CB  . PHE A 339  ? 0.1863 0.1732 0.2141 0.0055  0.0148  0.0303  337  PHE A CB  
2405  C CG  . PHE A 339  ? 0.2065 0.1950 0.2312 0.0070  0.0161  0.0301  337  PHE A CG  
2406  C CD1 . PHE A 339  ? 0.2092 0.1971 0.2308 0.0082  0.0161  0.0279  337  PHE A CD1 
2407  C CD2 . PHE A 339  ? 0.2126 0.2036 0.2379 0.0071  0.0170  0.0322  337  PHE A CD2 
2408  C CE1 . PHE A 339  ? 0.2102 0.1998 0.2293 0.0097  0.0171  0.0273  337  PHE A CE1 
2409  C CE2 . PHE A 339  ? 0.2227 0.2158 0.2449 0.0086  0.0182  0.0318  337  PHE A CE2 
2410  C CZ  . PHE A 339  ? 0.2208 0.2131 0.2399 0.0099  0.0182  0.0291  337  PHE A CZ  
2411  N N   . VAL A 340  ? 0.1822 0.1631 0.2077 0.0043  0.0135  0.0284  338  VAL A N   
2412  C CA  . VAL A 340  ? 0.2070 0.1871 0.2341 0.0039  0.0133  0.0293  338  VAL A CA  
2413  C C   . VAL A 340  ? 0.1742 0.1574 0.2011 0.0046  0.0147  0.0319  338  VAL A C   
2414  O O   . VAL A 340  ? 0.2130 0.1981 0.2366 0.0059  0.0159  0.0316  338  VAL A O   
2415  C CB  . VAL A 340  ? 0.1964 0.1737 0.2203 0.0040  0.0128  0.0266  338  VAL A CB  
2416  C CG1 . VAL A 340  ? 0.2022 0.1788 0.2279 0.0037  0.0125  0.0274  338  VAL A CG1 
2417  C CG2 . VAL A 340  ? 0.1999 0.1754 0.2238 0.0031  0.0115  0.0241  338  VAL A CG2 
2418  N N   . VAL A 341  ? 0.1902 0.1742 0.2209 0.0039  0.0144  0.0345  339  VAL A N   
2419  C CA  . VAL A 341  ? 0.1989 0.1861 0.2295 0.0044  0.0155  0.0374  339  VAL A CA  
2420  C C   . VAL A 341  ? 0.2060 0.1912 0.2382 0.0038  0.0146  0.0380  339  VAL A C   
2421  O O   . VAL A 341  ? 0.1991 0.1816 0.2354 0.0027  0.0130  0.0378  339  VAL A O   
2422  C CB  . VAL A 341  ? 0.2213 0.2131 0.2555 0.0040  0.0161  0.0413  339  VAL A CB  
2423  C CG1 . VAL A 341  ? 0.2822 0.2787 0.3150 0.0047  0.0175  0.0439  339  VAL A CG1 
2424  C CG2 . VAL A 341  ? 0.2407 0.2343 0.2742 0.0045  0.0168  0.0403  339  VAL A CG2 
2425  N N   . GLN A 342  ? 0.1927 0.1792 0.2219 0.0047  0.0154  0.0385  340  GLN A N   
2426  C CA  . GLN A 342  ? 0.2050 0.1893 0.2349 0.0044  0.0146  0.0386  340  GLN A CA  
2427  C C   . GLN A 342  ? 0.1838 0.1713 0.2174 0.0038  0.0146  0.0433  340  GLN A C   
2428  O O   . GLN A 342  ? 0.2087 0.2007 0.2401 0.0045  0.0160  0.0454  340  GLN A O   
2429  C CB  . GLN A 342  ? 0.2014 0.1851 0.2256 0.0056  0.0154  0.0361  340  GLN A CB  
2430  C CG  . GLN A 342  ? 0.2000 0.1804 0.2208 0.0059  0.0151  0.0319  340  GLN A CG  
2431  C CD  . GLN A 342  ? 0.2051 0.1864 0.2207 0.0073  0.0161  0.0302  340  GLN A CD  
2432  O OE1 . GLN A 342  ? 0.2143 0.1992 0.2285 0.0082  0.0173  0.0313  340  GLN A OE1 
2433  N NE2 . GLN A 342  ? 0.2046 0.1829 0.2174 0.0074  0.0156  0.0273  340  GLN A NE2 
2434  N N   . ALA A 343  ? 0.1728 0.1584 0.2124 0.0025  0.0129  0.0449  341  ALA A N   
2435  C CA  . ALA A 343  ? 0.1973 0.1857 0.2417 0.0017  0.0125  0.0500  341  ALA A CA  
2436  C C   . ALA A 343  ? 0.2153 0.2049 0.2578 0.0022  0.0127  0.0514  341  ALA A C   
2437  O O   . ALA A 343  ? 0.2105 0.2040 0.2558 0.0016  0.0128  0.0562  341  ALA A O   
2438  C CB  . ALA A 343  ? 0.2204 0.2057 0.2725 0.0002  0.0101  0.0509  341  ALA A CB  
2439  N N   . TYR A 344  ? 0.1985 0.1852 0.2366 0.0032  0.0129  0.0476  342  TYR A N   
2440  C CA  . TYR A 344  ? 0.2011 0.1893 0.2369 0.0038  0.0132  0.0488  342  TYR A CA  
2441  C C   . TYR A 344  ? 0.2363 0.2302 0.2671 0.0048  0.0153  0.0501  342  TYR A C   
2442  O O   . TYR A 344  ? 0.2313 0.2278 0.2603 0.0053  0.0157  0.0517  342  TYR A O   
2443  C CB  . TYR A 344  ? 0.2109 0.1946 0.2443 0.0044  0.0126  0.0447  342  TYR A CB  
2444  C CG  . TYR A 344  ? 0.1787 0.1611 0.2054 0.0055  0.0137  0.0401  342  TYR A CG  
2445  C CD1 . TYR A 344  ? 0.1975 0.1819 0.2208 0.0062  0.0150  0.0391  342  TYR A CD1 
2446  C CD2 . TYR A 344  ? 0.2000 0.1791 0.2246 0.0060  0.0131  0.0369  342  TYR A CD2 
2447  C CE1 . TYR A 344  ? 0.1943 0.1771 0.2125 0.0071  0.0156  0.0352  342  TYR A CE1 
2448  C CE2 . TYR A 344  ? 0.2257 0.2035 0.2450 0.0068  0.0139  0.0332  342  TYR A CE2 
2449  C CZ  . TYR A 344  ? 0.2132 0.1928 0.2295 0.0073  0.0150  0.0324  342  TYR A CZ  
2450  O OH  . TYR A 344  ? 0.2020 0.1801 0.2138 0.0080  0.0154  0.0291  342  TYR A OH  
2451  N N   . GLY A 345  ? 0.1989 0.1951 0.2278 0.0053  0.0165  0.0493  343  GLY A N   
2452  C CA  . GLY A 345  ? 0.2035 0.2053 0.2279 0.0066  0.0184  0.0495  343  GLY A CA  
2453  C C   . GLY A 345  ? 0.2264 0.2351 0.2537 0.0060  0.0191  0.0546  343  GLY A C   
2454  O O   . GLY A 345  ? 0.2145 0.2234 0.2467 0.0047  0.0185  0.0571  343  GLY A O   
2455  N N   . LYS A 346  ? 0.2158 0.2306 0.2400 0.0069  0.0204  0.0562  344  LYS A N   
2456  C CA  . LYS A 346  ? 0.2080 0.2307 0.2346 0.0063  0.0212  0.0615  344  LYS A CA  
2457  C C   . LYS A 346  ? 0.2363 0.2630 0.2632 0.0066  0.0224  0.0614  344  LYS A C   
2458  O O   . LYS A 346  ? 0.2246 0.2573 0.2550 0.0057  0.0228  0.0661  344  LYS A O   
2459  C CB  . LYS A 346  ? 0.2299 0.2592 0.2525 0.0074  0.0223  0.0626  344  LYS A CB  
2460  C CG  . LYS A 346  ? 0.2471 0.2731 0.2697 0.0071  0.0211  0.0632  344  LYS A CG  
2461  C CD  . LYS A 346  ? 0.2298 0.2624 0.2480 0.0083  0.0222  0.0639  344  LYS A CD  
2462  C CE  . LYS A 346  ? 0.2346 0.2649 0.2541 0.0076  0.0208  0.0660  344  LYS A CE  
2463  N NZ  . LYS A 346  ? 0.2600 0.2961 0.2746 0.0090  0.0218  0.0656  344  LYS A NZ  
2464  N N   . ARG A 347  ? 0.1857 0.2095 0.2094 0.0079  0.0228  0.0563  345  ARG A N   
2465  C CA  . ARG A 347  ? 0.2098 0.2370 0.2339 0.0084  0.0239  0.0557  345  ARG A CA  
2466  C C   . ARG A 347  ? 0.1965 0.2193 0.2253 0.0069  0.0227  0.0563  345  ARG A C   
2467  O O   . ARG A 347  ? 0.2105 0.2365 0.2407 0.0069  0.0234  0.0568  345  ARG A O   
2468  C CB  . ARG A 347  ? 0.2003 0.2268 0.2193 0.0105  0.0247  0.0501  345  ARG A CB  
2469  C CG  . ARG A 347  ? 0.2032 0.2356 0.2179 0.0122  0.0259  0.0492  345  ARG A CG  
2470  C CD  . ARG A 347  ? 0.1963 0.2262 0.2068 0.0142  0.0260  0.0433  345  ARG A CD  
2471  N NE  . ARG A 347  ? 0.2031 0.2249 0.2122 0.0139  0.0247  0.0409  345  ARG A NE  
2472  C CZ  . ARG A 347  ? 0.2081 0.2256 0.2144 0.0150  0.0243  0.0363  345  ARG A CZ  
2473  N NH1 . ARG A 347  ? 0.2221 0.2420 0.2270 0.0166  0.0249  0.0332  345  ARG A NH1 
2474  N NH2 . ARG A 347  ? 0.1976 0.2085 0.2029 0.0144  0.0232  0.0346  345  ARG A NH2 
2475  N N   . CYS A 348  ? 0.1972 0.2132 0.2288 0.0056  0.0209  0.0563  346  CYS A N   
2476  C CA  . CYS A 348  ? 0.2098 0.2211 0.2456 0.0043  0.0196  0.0557  346  CYS A CA  
2477  C C   . CYS A 348  ? 0.2086 0.2243 0.2489 0.0033  0.0199  0.0594  346  CYS A C   
2478  O O   . CYS A 348  ? 0.2188 0.2335 0.2595 0.0035  0.0200  0.0574  346  CYS A O   
2479  C CB  . CYS A 348  ? 0.2418 0.2471 0.2812 0.0030  0.0175  0.0561  346  CYS A CB  
2480  S SG  . CYS A 348  ? 0.2940 0.2929 0.3369 0.0021  0.0158  0.0531  346  CYS A SG  
2481  N N   . PRO A 349  ? 0.2166 0.2374 0.2610 0.0022  0.0199  0.0649  347  PRO A N   
2482  C CA  . PRO A 349  ? 0.2051 0.2302 0.2543 0.0010  0.0200  0.0686  347  PRO A CA  
2483  C C   . PRO A 349  ? 0.1931 0.2242 0.2390 0.0025  0.0221  0.0674  347  PRO A C   
2484  O O   . PRO A 349  ? 0.2199 0.2519 0.2686 0.0020  0.0221  0.0677  347  PRO A O   
2485  C CB  . PRO A 349  ? 0.2187 0.2486 0.2724 -0.0005 0.0196  0.0753  347  PRO A CB  
2486  C CG  . PRO A 349  ? 0.2376 0.2683 0.2871 0.0004  0.0200  0.0749  347  PRO A CG  
2487  C CD  . PRO A 349  ? 0.2134 0.2368 0.2582 0.0018  0.0197  0.0685  347  PRO A CD  
2488  N N   . PHE A 350  ? 0.2188 0.2541 0.2591 0.0043  0.0237  0.0655  348  PHE A N   
2489  C CA  . PHE A 350  ? 0.2149 0.2562 0.2522 0.0060  0.0256  0.0636  348  PHE A CA  
2490  C C   . PHE A 350  ? 0.1951 0.2307 0.2301 0.0072  0.0253  0.0579  348  PHE A C   
2491  O O   . PHE A 350  ? 0.2007 0.2393 0.2362 0.0079  0.0261  0.0568  348  PHE A O   
2492  C CB  . PHE A 350  ? 0.2095 0.2571 0.2420 0.0077  0.0271  0.0631  348  PHE A CB  
2493  C CG  . PHE A 350  ? 0.2210 0.2741 0.2556 0.0064  0.0271  0.0690  348  PHE A CG  
2494  C CD1 . PHE A 350  ? 0.2294 0.2914 0.2674 0.0054  0.0281  0.0742  348  PHE A CD1 
2495  C CD2 . PHE A 350  ? 0.2349 0.2843 0.2687 0.0059  0.0261  0.0697  348  PHE A CD2 
2496  C CE1 . PHE A 350  ? 0.2746 0.3421 0.3150 0.0040  0.0279  0.0803  348  PHE A CE1 
2497  C CE2 . PHE A 350  ? 0.2629 0.3173 0.2992 0.0046  0.0259  0.0756  348  PHE A CE2 
2498  C CZ  . PHE A 350  ? 0.2854 0.3489 0.3251 0.0035  0.0268  0.0811  348  PHE A CZ  
2499  N N   . VAL A 351  ? 0.1865 0.2142 0.2193 0.0073  0.0241  0.0545  349  VAL A N   
2500  C CA  . VAL A 351  ? 0.1981 0.2200 0.2295 0.0080  0.0235  0.0499  349  VAL A CA  
2501  C C   . VAL A 351  ? 0.2076 0.2273 0.2438 0.0064  0.0224  0.0512  349  VAL A C   
2502  O O   . VAL A 351  ? 0.2157 0.2352 0.2520 0.0070  0.0225  0.0492  349  VAL A O   
2503  C CB  . VAL A 351  ? 0.1946 0.2094 0.2232 0.0080  0.0223  0.0469  349  VAL A CB  
2504  C CG1 . VAL A 351  ? 0.2065 0.2157 0.2341 0.0083  0.0214  0.0429  349  VAL A CG1 
2505  C CG2 . VAL A 351  ? 0.2233 0.2402 0.2471 0.0097  0.0233  0.0452  349  VAL A CG2 
2506  N N   . LEU A 352  ? 0.2175 0.2354 0.2583 0.0045  0.0212  0.0545  350  LEU A N   
2507  C CA  . LEU A 352  ? 0.2083 0.2243 0.2543 0.0030  0.0200  0.0557  350  LEU A CA  
2508  C C   . LEU A 352  ? 0.2195 0.2423 0.2677 0.0030  0.0212  0.0583  350  LEU A C   
2509  O O   . LEU A 352  ? 0.2225 0.2443 0.2726 0.0028  0.0208  0.0572  350  LEU A O   
2510  C CB  . LEU A 352  ? 0.2026 0.2159 0.2539 0.0010  0.0183  0.0588  350  LEU A CB  
2511  C CG  . LEU A 352  ? 0.2364 0.2424 0.2867 0.0008  0.0167  0.0556  350  LEU A CG  
2512  C CD1 . LEU A 352  ? 0.2700 0.2740 0.3264 -0.0009 0.0149  0.0587  350  LEU A CD1 
2513  C CD2 . LEU A 352  ? 0.2495 0.2506 0.2987 0.0010  0.0158  0.0512  350  LEU A CD2 
2514  N N   . ASP A 353  ? 0.2187 0.2492 0.2669 0.0033  0.0227  0.0618  351  ASP A N   
2515  C CA  . ASP A 353  ? 0.2145 0.2527 0.2646 0.0035  0.0241  0.0640  351  ASP A CA  
2516  C C   . ASP A 353  ? 0.2038 0.2424 0.2504 0.0055  0.0250  0.0592  351  ASP A C   
2517  O O   . ASP A 353  ? 0.2070 0.2474 0.2561 0.0054  0.0251  0.0593  351  ASP A O   
2518  C CB  . ASP A 353  ? 0.2070 0.2544 0.2564 0.0038  0.0257  0.0679  351  ASP A CB  
2519  C CG  . ASP A 353  ? 0.2682 0.3168 0.3225 0.0015  0.0248  0.0739  351  ASP A CG  
2520  O OD1 . ASP A 353  ? 0.2770 0.3211 0.3369 -0.0004 0.0229  0.0757  351  ASP A OD1 
2521  O OD2 . ASP A 353  ? 0.3124 0.3667 0.3654 0.0016  0.0256  0.0768  351  ASP A OD2 
2522  N N   . PHE A 354  ? 0.1959 0.2326 0.2370 0.0074  0.0255  0.0552  352  PHE A N   
2523  C CA  . PHE A 354  ? 0.1897 0.2263 0.2281 0.0094  0.0259  0.0506  352  PHE A CA  
2524  C C   . PHE A 354  ? 0.1882 0.2177 0.2281 0.0087  0.0243  0.0484  352  PHE A C   
2525  O O   . PHE A 354  ? 0.2058 0.2368 0.2470 0.0093  0.0245  0.0471  352  PHE A O   
2526  C CB  . PHE A 354  ? 0.1894 0.2244 0.2224 0.0112  0.0263  0.0468  352  PHE A CB  
2527  C CG  . PHE A 354  ? 0.2113 0.2438 0.2421 0.0130  0.0260  0.0418  352  PHE A CG  
2528  C CD1 . PHE A 354  ? 0.2242 0.2631 0.2546 0.0150  0.0272  0.0400  352  PHE A CD1 
2529  C CD2 . PHE A 354  ? 0.2488 0.2731 0.2786 0.0126  0.0244  0.0391  352  PHE A CD2 
2530  C CE1 . PHE A 354  ? 0.2602 0.2965 0.2896 0.0167  0.0266  0.0356  352  PHE A CE1 
2531  C CE2 . PHE A 354  ? 0.2416 0.2636 0.2700 0.0140  0.0239  0.0352  352  PHE A CE2 
2532  C CZ  . PHE A 354  ? 0.2457 0.2734 0.2742 0.0161  0.0249  0.0335  352  PHE A CZ  
2533  N N   . ILE A 355  ? 0.1810 0.2033 0.2210 0.0074  0.0227  0.0479  353  ILE A N   
2534  C CA  . ILE A 355  ? 0.1842 0.2004 0.2254 0.0067  0.0212  0.0456  353  ILE A CA  
2535  C C   . ILE A 355  ? 0.2081 0.2259 0.2545 0.0053  0.0207  0.0482  353  ILE A C   
2536  O O   . ILE A 355  ? 0.2002 0.2168 0.2476 0.0054  0.0201  0.0465  353  ILE A O   
2537  C CB  . ILE A 355  ? 0.2138 0.2231 0.2540 0.0057  0.0196  0.0443  353  ILE A CB  
2538  C CG1 . ILE A 355  ? 0.2272 0.2345 0.2621 0.0071  0.0200  0.0414  353  ILE A CG1 
2539  C CG2 . ILE A 355  ? 0.2072 0.2116 0.2491 0.0047  0.0180  0.0425  353  ILE A CG2 
2540  C CD1 . ILE A 355  ? 0.2337 0.2354 0.2676 0.0062  0.0187  0.0403  353  ILE A CD1 
2541  N N   . ILE A 356  ? 0.2301 0.2505 0.2805 0.0038  0.0206  0.0525  354  ILE A N   
2542  C CA  . ILE A 356  ? 0.1951 0.2173 0.2512 0.0023  0.0200  0.0553  354  ILE A CA  
2543  C C   . ILE A 356  ? 0.2071 0.2356 0.2635 0.0035  0.0215  0.0554  354  ILE A C   
2544  O O   . ILE A 356  ? 0.2083 0.2363 0.2674 0.0031  0.0209  0.0549  354  ILE A O   
2545  C CB  . ILE A 356  ? 0.2066 0.2309 0.2676 0.0004  0.0196  0.0603  354  ILE A CB  
2546  C CG1 . ILE A 356  ? 0.2300 0.2472 0.2922 -0.0007 0.0176  0.0595  354  ILE A CG1 
2547  C CG2 . ILE A 356  ? 0.2434 0.2716 0.3106 -0.0010 0.0193  0.0639  354  ILE A CG2 
2548  C CD1 . ILE A 356  ? 0.2444 0.2632 0.3110 -0.0023 0.0170  0.0643  354  ILE A CD1 
2549  N N   . ASP A 357  ? 0.1828 0.2175 0.2364 0.0050  0.0234  0.0557  355  ASP A N   
2550  C CA  . ASP A 357  ? 0.1957 0.2371 0.2496 0.0065  0.0249  0.0551  355  ASP A CA  
2551  C C   . ASP A 357  ? 0.2052 0.2426 0.2567 0.0080  0.0243  0.0502  355  ASP A C   
2552  O O   . ASP A 357  ? 0.2130 0.2526 0.2668 0.0084  0.0244  0.0497  355  ASP A O   
2553  C CB  . ASP A 357  ? 0.2471 0.2966 0.2983 0.0080  0.0270  0.0559  355  ASP A CB  
2554  C CG  . ASP A 357  ? 0.2301 0.2866 0.2812 0.0100  0.0284  0.0541  355  ASP A CG  
2555  O OD1 . ASP A 357  ? 0.2844 0.3472 0.3395 0.0093  0.0291  0.0573  355  ASP A OD1 
2556  O OD2 . ASP A 357  ? 0.2488 0.3045 0.2964 0.0122  0.0287  0.0495  355  ASP A OD2 
2557  N N   . LEU A 358  ? 0.2032 0.2348 0.2505 0.0088  0.0236  0.0467  356  LEU A N   
2558  C CA  . LEU A 358  ? 0.1821 0.2096 0.2277 0.0100  0.0228  0.0426  356  LEU A CA  
2559  C C   . LEU A 358  ? 0.1998 0.2229 0.2484 0.0084  0.0211  0.0428  356  LEU A C   
2560  O O   . LEU A 358  ? 0.2058 0.2289 0.2554 0.0091  0.0207  0.0411  356  LEU A O   
2561  C CB  . LEU A 358  ? 0.1852 0.2075 0.2261 0.0108  0.0222  0.0395  356  LEU A CB  
2562  C CG  . LEU A 358  ? 0.1988 0.2162 0.2382 0.0116  0.0209  0.0358  356  LEU A CG  
2563  C CD1 . LEU A 358  ? 0.2525 0.2741 0.2926 0.0137  0.0215  0.0338  356  LEU A CD1 
2564  C CD2 . LEU A 358  ? 0.2150 0.2276 0.2502 0.0119  0.0204  0.0335  356  LEU A CD2 
2565  N N   . ALA A 359  ? 0.2134 0.2330 0.2640 0.0064  0.0200  0.0447  357  ALA A N   
2566  C CA  . ALA A 359  ? 0.2017 0.2177 0.2555 0.0048  0.0183  0.0448  357  ALA A CA  
2567  C C   . ALA A 359  ? 0.2043 0.2253 0.2626 0.0046  0.0187  0.0469  357  ALA A C   
2568  O O   . ALA A 359  ? 0.2169 0.2365 0.2767 0.0045  0.0178  0.0457  357  ALA A O   
2569  C CB  . ALA A 359  ? 0.2326 0.2449 0.2885 0.0028  0.0170  0.0463  357  ALA A CB  
2570  N N   . ARG A 360  ? 0.2113 0.2387 0.2718 0.0044  0.0202  0.0504  358  ARG A N   
2571  C CA  . ARG A 360  ? 0.2152 0.2483 0.2800 0.0042  0.0208  0.0527  358  ARG A CA  
2572  C C   . ARG A 360  ? 0.2316 0.2677 0.2948 0.0064  0.0217  0.0498  358  ARG A C   
2573  O O   . ARG A 360  ? 0.2641 0.3009 0.3303 0.0063  0.0211  0.0496  358  ARG A O   
2574  C CB  . ARG A 360  ? 0.2483 0.2885 0.3155 0.0035  0.0223  0.0572  358  ARG A CB  
2575  C CG  . ARG A 360  ? 0.2887 0.3265 0.3594 0.0011  0.0211  0.0608  358  ARG A CG  
2576  C CD  . ARG A 360  ? 0.3232 0.3691 0.3976 0.0002  0.0223  0.0663  358  ARG A CD  
2577  N NE  . ARG A 360  ? 0.3771 0.4205 0.4545 -0.0019 0.0211  0.0697  358  ARG A NE  
2578  C CZ  . ARG A 360  ? 0.4519 0.4921 0.5353 -0.0041 0.0191  0.0720  358  ARG A CZ  
2579  N NH1 . ARG A 360  ? 0.4610 0.5008 0.5481 -0.0047 0.0182  0.0716  358  ARG A NH1 
2580  N NH2 . ARG A 360  ? 0.4058 0.4433 0.4922 -0.0057 0.0177  0.0746  358  ARG A NH2 
2581  N N   . ARG A 361  ? 0.2238 0.2619 0.2829 0.0085  0.0229  0.0475  359  ARG A N   
2582  C CA  . ARG A 361  ? 0.2142 0.2553 0.2725 0.0109  0.0235  0.0444  359  ARG A CA  
2583  C C   . ARG A 361  ? 0.2323 0.2669 0.2903 0.0110  0.0216  0.0413  359  ARG A C   
2584  O O   . ARG A 361  ? 0.2490 0.2854 0.3092 0.0119  0.0213  0.0403  359  ARG A O   
2585  C CB  . ARG A 361  ? 0.2622 0.3058 0.3162 0.0130  0.0247  0.0420  359  ARG A CB  
2586  C CG  . ARG A 361  ? 0.2828 0.3352 0.3369 0.0134  0.0269  0.0446  359  ARG A CG  
2587  C CD  . ARG A 361  ? 0.2945 0.3500 0.3446 0.0159  0.0279  0.0413  359  ARG A CD  
2588  N NE  . ARG A 361  ? 0.2763 0.3261 0.3225 0.0156  0.0273  0.0405  359  ARG A NE  
2589  C CZ  . ARG A 361  ? 0.2703 0.3153 0.3132 0.0170  0.0266  0.0364  359  ARG A CZ  
2590  N NH1 . ARG A 361  ? 0.2477 0.2918 0.2911 0.0188  0.0259  0.0327  359  ARG A NH1 
2591  N NH2 . ARG A 361  ? 0.2633 0.3046 0.3028 0.0167  0.0263  0.0361  359  ARG A NH2 
2592  N N   . SER A 362  ? 0.2158 0.2433 0.2709 0.0103  0.0202  0.0400  360  SER A N   
2593  C CA  . SER A 362  ? 0.2127 0.2346 0.2671 0.0104  0.0184  0.0373  360  SER A CA  
2594  C C   . SER A 362  ? 0.2247 0.2441 0.2824 0.0084  0.0169  0.0387  360  SER A C   
2595  O O   . SER A 362  ? 0.2418 0.2583 0.2997 0.0085  0.0154  0.0370  360  SER A O   
2596  C CB  . SER A 362  ? 0.2221 0.2383 0.2722 0.0103  0.0176  0.0355  360  SER A CB  
2597  O OG  . SER A 362  ? 0.2111 0.2245 0.2611 0.0083  0.0172  0.0373  360  SER A OG  
2598  N N   . GLY A 363  ? 0.2237 0.2440 0.2840 0.0066  0.0170  0.0417  361  GLY A N   
2599  C CA  . GLY A 363  ? 0.2418 0.2593 0.3054 0.0046  0.0152  0.0425  361  GLY A CA  
2600  C C   . GLY A 363  ? 0.2648 0.2758 0.3260 0.0036  0.0135  0.0407  361  GLY A C   
2601  O O   . GLY A 363  ? 0.2674 0.2761 0.3308 0.0022  0.0118  0.0405  361  GLY A O   
2602  N N   . ARG A 364  ? 0.2160 0.2245 0.2728 0.0042  0.0138  0.0392  362  ARG A N   
2603  C CA  . ARG A 364  ? 0.2186 0.2216 0.2729 0.0033  0.0124  0.0374  362  ARG A CA  
2604  C C   . ARG A 364  ? 0.2341 0.2362 0.2898 0.0020  0.0123  0.0389  362  ARG A C   
2605  O O   . ARG A 364  ? 0.2542 0.2585 0.3095 0.0024  0.0137  0.0405  362  ARG A O   
2606  C CB  . ARG A 364  ? 0.2606 0.2618 0.3099 0.0047  0.0127  0.0352  362  ARG A CB  
2607  C CG  . ARG A 364  ? 0.3263 0.3286 0.3747 0.0064  0.0128  0.0337  362  ARG A CG  
2608  C CD  . ARG A 364  ? 0.2320 0.2308 0.2795 0.0059  0.0109  0.0321  362  ARG A CD  
2609  N NE  . ARG A 364  ? 0.2224 0.2228 0.2710 0.0074  0.0107  0.0313  362  ARG A NE  
2610  C CZ  . ARG A 364  ? 0.2285 0.2279 0.2751 0.0088  0.0104  0.0296  362  ARG A CZ  
2611  N NH1 . ARG A 364  ? 0.1941 0.1905 0.2370 0.0088  0.0103  0.0285  362  ARG A NH1 
2612  N NH2 . ARG A 364  ? 0.2171 0.2183 0.2658 0.0103  0.0102  0.0289  362  ARG A NH2 
2613  N N   . ARG A 365  ? 0.2098 0.2087 0.2671 0.0004  0.0105  0.0382  363  ARG A N   
2614  C CA  . ARG A 365  ? 0.2039 0.2013 0.2633 -0.0008 0.0100  0.0392  363  ARG A CA  
2615  C C   . ARG A 365  ? 0.2226 0.2169 0.2773 -0.0003 0.0101  0.0371  363  ARG A C   
2616  O O   . ARG A 365  ? 0.2273 0.2183 0.2805 -0.0008 0.0087  0.0346  363  ARG A O   
2617  C CB  . ARG A 365  ? 0.2101 0.2058 0.2739 -0.0024 0.0080  0.0388  363  ARG A CB  
2618  C CG  . ARG A 365  ? 0.2283 0.2225 0.2955 -0.0036 0.0071  0.0398  363  ARG A CG  
2619  C CD  . ARG A 365  ? 0.2720 0.2661 0.3456 -0.0052 0.0053  0.0405  363  ARG A CD  
2620  N NE  . ARG A 365  ? 0.2479 0.2406 0.3261 -0.0063 0.0042  0.0418  363  ARG A NE  
2621  C CZ  . ARG A 365  ? 0.2491 0.2384 0.3287 -0.0069 0.0023  0.0390  363  ARG A CZ  
2622  N NH1 . ARG A 365  ? 0.2546 0.2421 0.3313 -0.0068 0.0012  0.0350  363  ARG A NH1 
2623  N NH2 . ARG A 365  ? 0.2291 0.2171 0.3133 -0.0077 0.0013  0.0403  363  ARG A NH2 
2624  N N   . ILE A 366  ? 0.1936 0.1893 0.2457 0.0008  0.0117  0.0380  364  ILE A N   
2625  C CA  . ILE A 366  ? 0.2093 0.2023 0.2568 0.0015  0.0119  0.0360  364  ILE A CA  
2626  C C   . ILE A 366  ? 0.2266 0.2166 0.2755 0.0002  0.0107  0.0355  364  ILE A C   
2627  O O   . ILE A 366  ? 0.1941 0.1848 0.2471 -0.0007 0.0104  0.0378  364  ILE A O   
2628  C CB  . ILE A 366  ? 0.1969 0.1926 0.2418 0.0029  0.0138  0.0371  364  ILE A CB  
2629  C CG1 . ILE A 366  ? 0.2133 0.2121 0.2572 0.0044  0.0148  0.0366  364  ILE A CG1 
2630  C CG2 . ILE A 366  ? 0.2321 0.2250 0.2725 0.0034  0.0139  0.0352  364  ILE A CG2 
2631  C CD1 . ILE A 366  ? 0.2254 0.2283 0.2675 0.0059  0.0167  0.0374  364  ILE A CD1 
2632  N N   . MET A 367  ? 0.1980 0.1849 0.2438 0.0002  0.0098  0.0326  365  MET A N   
2633  C CA  . MET A 367  ? 0.2002 0.1844 0.2469 -0.0007 0.0086  0.0314  365  MET A CA  
2634  C C   . MET A 367  ? 0.2172 0.2011 0.2615 0.0001  0.0098  0.0321  365  MET A C   
2635  O O   . MET A 367  ? 0.2541 0.2378 0.2936 0.0011  0.0107  0.0309  365  MET A O   
2636  C CB  . MET A 367  ? 0.2124 0.1945 0.2567 -0.0010 0.0073  0.0279  365  MET A CB  
2637  C CG  . MET A 367  ? 0.2208 0.2037 0.2666 -0.0016 0.0062  0.0273  365  MET A CG  
2638  S SD  . MET A 367  ? 0.2481 0.2299 0.2910 -0.0022 0.0046  0.0236  365  MET A SD  
2639  C CE  . MET A 367  ? 0.2697 0.2507 0.3174 -0.0034 0.0027  0.0216  365  MET A CE  
2640  N N   . VAL A 368  ? 0.1769 0.1610 0.2248 -0.0005 0.0096  0.0342  366  VAL A N   
2641  C CA  . VAL A 368  ? 0.1677 0.1523 0.2137 0.0002  0.0107  0.0354  366  VAL A CA  
2642  C C   . VAL A 368  ? 0.1934 0.1748 0.2406 -0.0004 0.0094  0.0339  366  VAL A C   
2643  O O   . VAL A 368  ? 0.2019 0.1826 0.2548 -0.0015 0.0080  0.0349  366  VAL A O   
2644  C CB  . VAL A 368  ? 0.1933 0.1817 0.2425 0.0000  0.0117  0.0397  366  VAL A CB  
2645  C CG1 . VAL A 368  ? 0.2232 0.2122 0.2703 0.0006  0.0127  0.0410  366  VAL A CG1 
2646  C CG2 . VAL A 368  ? 0.2403 0.2325 0.2883 0.0008  0.0131  0.0408  366  VAL A CG2 
2647  N N   . ARG A 369  ? 0.1844 0.1640 0.2269 0.0003  0.0097  0.0315  367  ARG A N   
2648  C CA  . ARG A 369  ? 0.2047 0.1818 0.2482 -0.0001 0.0085  0.0298  367  ARG A CA  
2649  C C   . ARG A 369  ? 0.2176 0.1954 0.2613 0.0003  0.0094  0.0323  367  ARG A C   
2650  O O   . ARG A 369  ? 0.2226 0.2014 0.2616 0.0014  0.0108  0.0326  367  ARG A O   
2651  C CB  . ARG A 369  ? 0.2155 0.1909 0.2541 0.0004  0.0084  0.0260  367  ARG A CB  
2652  C CG  . ARG A 369  ? 0.2222 0.1954 0.2621 0.0001  0.0072  0.0239  367  ARG A CG  
2653  C CD  . ARG A 369  ? 0.2190 0.1914 0.2536 0.0007  0.0076  0.0211  367  ARG A CD  
2654  N NE  . ARG A 369  ? 0.2090 0.1818 0.2414 0.0004  0.0070  0.0187  367  ARG A NE  
2655  C CZ  . ARG A 369  ? 0.2276 0.2006 0.2550 0.0007  0.0076  0.0174  367  ARG A CZ  
2656  N NH1 . ARG A 369  ? 0.2448 0.2173 0.2686 0.0015  0.0087  0.0178  367  ARG A NH1 
2657  N NH2 . ARG A 369  ? 0.2175 0.1914 0.2435 0.0002  0.0069  0.0159  367  ARG A NH2 
2658  N N   . LEU A 370  ? 0.1871 0.1644 0.2365 -0.0005 0.0082  0.0343  368  LEU A N   
2659  C CA  . LEU A 370  ? 0.1916 0.1697 0.2419 -0.0004 0.0086  0.0371  368  LEU A CA  
2660  C C   . LEU A 370  ? 0.1753 0.1503 0.2248 -0.0001 0.0076  0.0342  368  LEU A C   
2661  O O   . LEU A 370  ? 0.1975 0.1701 0.2509 -0.0007 0.0058  0.0319  368  LEU A O   
2662  C CB  . LEU A 370  ? 0.2077 0.1870 0.2654 -0.0016 0.0076  0.0412  368  LEU A CB  
2663  C CG  . LEU A 370  ? 0.2250 0.2060 0.2843 -0.0016 0.0079  0.0451  368  LEU A CG  
2664  C CD1 . LEU A 370  ? 0.2308 0.2165 0.2851 -0.0007 0.0104  0.0475  368  LEU A CD1 
2665  C CD2 . LEU A 370  ? 0.2267 0.2082 0.2946 -0.0032 0.0062  0.0490  368  LEU A CD2 
2666  N N   . VAL A 371  ? 0.1761 0.1514 0.2209 0.0008  0.0089  0.0341  369  VAL A N   
2667  C CA  . VAL A 371  ? 0.1819 0.1548 0.2257 0.0011  0.0082  0.0317  369  VAL A CA  
2668  C C   . VAL A 371  ? 0.1798 0.1539 0.2240 0.0014  0.0087  0.0350  369  VAL A C   
2669  O O   . VAL A 371  ? 0.2185 0.1959 0.2625 0.0015  0.0098  0.0387  369  VAL A O   
2670  C CB  . VAL A 371  ? 0.1910 0.1631 0.2281 0.0020  0.0090  0.0280  369  VAL A CB  
2671  C CG1 . VAL A 371  ? 0.1932 0.1649 0.2294 0.0017  0.0086  0.0255  369  VAL A CG1 
2672  C CG2 . VAL A 371  ? 0.1995 0.1737 0.2313 0.0030  0.0110  0.0296  369  VAL A CG2 
2673  N N   . LYS A 372  ? 0.2002 0.1722 0.2448 0.0016  0.0078  0.0335  370  LYS A N   
2674  C CA  . LYS A 372  ? 0.2252 0.1986 0.2693 0.0020  0.0084  0.0364  370  LYS A CA  
2675  C C   . LYS A 372  ? 0.2098 0.1845 0.2463 0.0032  0.0103  0.0352  370  LYS A C   
2676  O O   . LYS A 372  ? 0.2639 0.2420 0.2980 0.0037  0.0117  0.0379  370  LYS A O   
2677  C CB  . LYS A 372  ? 0.2292 0.2001 0.2784 0.0017  0.0064  0.0362  370  LYS A CB  
2678  C CG  . LYS A 372  ? 0.2193 0.1897 0.2771 0.0004  0.0045  0.0387  370  LYS A CG  
2679  C CD  . LYS A 372  ? 0.2594 0.2271 0.3238 0.0001  0.0021  0.0384  370  LYS A CD  
2680  C CE  . LYS A 372  ? 0.2657 0.2326 0.3391 -0.0012 -0.0001 0.0402  370  LYS A CE  
2681  N NZ  . LYS A 372  ? 0.2536 0.2175 0.3347 -0.0014 -0.0030 0.0391  370  LYS A NZ  
2682  N N   . GLY A 373  ? 0.2116 0.1840 0.2443 0.0037  0.0103  0.0311  371  GLY A N   
2683  C CA  . GLY A 373  ? 0.1901 0.1634 0.2162 0.0048  0.0118  0.0297  371  GLY A CA  
2684  C C   . GLY A 373  ? 0.2051 0.1762 0.2286 0.0052  0.0114  0.0267  371  GLY A C   
2685  O O   . GLY A 373  ? 0.2274 0.1973 0.2538 0.0050  0.0104  0.0267  371  GLY A O   
2686  N N   . ALA A 374  ? 0.2039 0.1748 0.2224 0.0057  0.0122  0.0242  372  ALA A N   
2687  C CA  . ALA A 374  ? 0.2002 0.1692 0.2165 0.0058  0.0117  0.0209  372  ALA A CA  
2688  C C   . ALA A 374  ? 0.2288 0.1983 0.2410 0.0067  0.0125  0.0208  372  ALA A C   
2689  O O   . ALA A 374  ? 0.2525 0.2207 0.2631 0.0068  0.0122  0.0185  372  ALA A O   
2690  C CB  . ALA A 374  ? 0.2336 0.2021 0.2477 0.0055  0.0116  0.0182  372  ALA A CB  
2691  N N   . TYR A 375  ? 0.2181 0.1897 0.2286 0.0074  0.0136  0.0231  373  TYR A N   
2692  C CA  . TYR A 375  ? 0.2163 0.1886 0.2226 0.0084  0.0143  0.0225  373  TYR A CA  
2693  C C   . TYR A 375  ? 0.1891 0.1631 0.1961 0.0088  0.0146  0.0250  373  TYR A C   
2694  O O   . TYR A 375  ? 0.2131 0.1892 0.2170 0.0098  0.0154  0.0253  373  TYR A O   
2695  C CB  . TYR A 375  ? 0.2211 0.1951 0.2244 0.0092  0.0153  0.0223  373  TYR A CB  
2696  C CG  . TYR A 375  ? 0.2142 0.1868 0.2167 0.0087  0.0150  0.0204  373  TYR A CG  
2697  C CD1 . TYR A 375  ? 0.2209 0.1938 0.2262 0.0081  0.0148  0.0212  373  TYR A CD1 
2698  C CD2 . TYR A 375  ? 0.2656 0.2370 0.2650 0.0089  0.0149  0.0181  373  TYR A CD2 
2699  C CE1 . TYR A 375  ? 0.2409 0.2128 0.2455 0.0076  0.0144  0.0197  373  TYR A CE1 
2700  C CE2 . TYR A 375  ? 0.2863 0.2569 0.2853 0.0084  0.0145  0.0169  373  TYR A CE2 
2701  C CZ  . TYR A 375  ? 0.2796 0.2505 0.2811 0.0078  0.0143  0.0177  373  TYR A CZ  
2702  O OH  . TYR A 375  ? 0.2936 0.2639 0.2946 0.0073  0.0138  0.0167  373  TYR A OH  
2703  N N   . TRP A 376  ? 0.1984 0.1719 0.2100 0.0082  0.0136  0.0267  374  TRP A N   
2704  C CA  . TRP A 376  ? 0.2144 0.1902 0.2275 0.0083  0.0137  0.0302  374  TRP A CA  
2705  C C   . TRP A 376  ? 0.2154 0.1917 0.2250 0.0092  0.0140  0.0294  374  TRP A C   
2706  O O   . TRP A 376  ? 0.2173 0.1972 0.2247 0.0099  0.0149  0.0313  374  TRP A O   
2707  C CB  . TRP A 376  ? 0.2344 0.2089 0.2539 0.0074  0.0121  0.0321  374  TRP A CB  
2708  C CG  . TRP A 376  ? 0.2334 0.2107 0.2549 0.0074  0.0120  0.0364  374  TRP A CG  
2709  C CD1 . TRP A 376  ? 0.2394 0.2206 0.2623 0.0071  0.0126  0.0406  374  TRP A CD1 
2710  C CD2 . TRP A 376  ? 0.2300 0.2069 0.2523 0.0076  0.0113  0.0371  374  TRP A CD2 
2711  N NE1 . TRP A 376  ? 0.2214 0.2052 0.2460 0.0070  0.0122  0.0442  374  TRP A NE1 
2712  C CE2 . TRP A 376  ? 0.2406 0.2215 0.2648 0.0073  0.0113  0.0421  374  TRP A CE2 
2713  C CE3 . TRP A 376  ? 0.2742 0.2483 0.2959 0.0079  0.0105  0.0342  374  TRP A CE3 
2714  C CZ2 . TRP A 376  ? 0.2755 0.2573 0.3012 0.0074  0.0106  0.0444  374  TRP A CZ2 
2715  C CZ3 . TRP A 376  ? 0.3007 0.2755 0.3239 0.0081  0.0098  0.0362  374  TRP A CZ3 
2716  C CH2 . TRP A 376  ? 0.2873 0.2657 0.3125 0.0078  0.0098  0.0413  374  TRP A CH2 
2717  N N   . ASP A 377  ? 0.2414 0.2148 0.2505 0.0092  0.0133  0.0267  375  ASP A N   
2718  C CA  A ASP A 377  ? 0.2442 0.2180 0.2504 0.0100  0.0134  0.0259  375  ASP A CA  
2719  C CA  B ASP A 377  ? 0.2440 0.2180 0.2502 0.0100  0.0135  0.0262  375  ASP A CA  
2720  C C   . ASP A 377  ? 0.2354 0.2111 0.2364 0.0109  0.0146  0.0248  375  ASP A C   
2721  O O   . ASP A 377  ? 0.2450 0.2229 0.2437 0.0117  0.0151  0.0255  375  ASP A O   
2722  C CB  A ASP A 377  ? 0.2985 0.2692 0.3047 0.0098  0.0126  0.0225  375  ASP A CB  
2723  C CB  B ASP A 377  ? 0.3026 0.2737 0.3099 0.0098  0.0124  0.0237  375  ASP A CB  
2724  C CG  A ASP A 377  ? 0.3146 0.2835 0.3263 0.0091  0.0112  0.0228  375  ASP A CG  
2725  C CG  B ASP A 377  ? 0.3017 0.2706 0.3078 0.0094  0.0123  0.0200  375  ASP A CG  
2726  O OD1 A ASP A 377  ? 0.3891 0.3589 0.4043 0.0090  0.0106  0.0260  375  ASP A OD1 
2727  O OD1 B ASP A 377  ? 0.3389 0.3081 0.3422 0.0095  0.0130  0.0192  375  ASP A OD1 
2728  O OD2 A ASP A 377  ? 0.4094 0.3763 0.4223 0.0088  0.0105  0.0198  375  ASP A OD2 
2729  O OD2 B ASP A 377  ? 0.3463 0.3135 0.3544 0.0091  0.0114  0.0180  375  ASP A OD2 
2730  N N   . ALA A 378  ? 0.2289 0.2036 0.2283 0.0108  0.0150  0.0228  376  ALA A N   
2731  C CA  . ALA A 378  ? 0.2174 0.1934 0.2128 0.0118  0.0158  0.0213  376  ALA A CA  
2732  C C   . ALA A 378  ? 0.2305 0.2107 0.2253 0.0126  0.0167  0.0234  376  ALA A C   
2733  O O   . ALA A 378  ? 0.2259 0.2083 0.2177 0.0137  0.0172  0.0225  376  ALA A O   
2734  C CB  . ALA A 378  ? 0.2378 0.2118 0.2324 0.0114  0.0156  0.0191  376  ALA A CB  
2735  N N   . GLU A 379  ? 0.2173 0.1991 0.2150 0.0121  0.0169  0.0261  377  GLU A N   
2736  C CA  . GLU A 379  ? 0.2012 0.1882 0.1986 0.0128  0.0179  0.0284  377  GLU A CA  
2737  C C   . GLU A 379  ? 0.2079 0.1982 0.2046 0.0132  0.0180  0.0305  377  GLU A C   
2738  O O   . GLU A 379  ? 0.2291 0.2242 0.2234 0.0143  0.0189  0.0308  377  GLU A O   
2739  C CB  . GLU A 379  ? 0.2026 0.1909 0.2038 0.0118  0.0179  0.0312  377  GLU A CB  
2740  C CG  . GLU A 379  ? 0.2336 0.2193 0.2357 0.0114  0.0178  0.0295  377  GLU A CG  
2741  C CD  . GLU A 379  ? 0.2571 0.2442 0.2562 0.0125  0.0186  0.0272  377  GLU A CD  
2742  O OE1 . GLU A 379  ? 0.2552 0.2458 0.2517 0.0138  0.0193  0.0268  377  GLU A OE1 
2743  O OE2 . GLU A 379  ? 0.2423 0.2271 0.2419 0.0121  0.0183  0.0258  377  GLU A OE2 
2744  N N   . ILE A 380  ? 0.2193 0.2076 0.2183 0.0124  0.0171  0.0319  378  ILE A N   
2745  C CA  . ILE A 380  ? 0.2323 0.2239 0.2310 0.0128  0.0170  0.0342  378  ILE A CA  
2746  C C   . ILE A 380  ? 0.2221 0.2141 0.2160 0.0141  0.0173  0.0311  378  ILE A C   
2747  O O   . ILE A 380  ? 0.2179 0.2150 0.2096 0.0150  0.0180  0.0319  378  ILE A O   
2748  C CB  . ILE A 380  ? 0.2488 0.2374 0.2515 0.0118  0.0156  0.0359  378  ILE A CB  
2749  C CG1 . ILE A 380  ? 0.2492 0.2372 0.2574 0.0105  0.0150  0.0389  378  ILE A CG1 
2750  C CG2 . ILE A 380  ? 0.2420 0.2339 0.2443 0.0121  0.0154  0.0385  378  ILE A CG2 
2751  C CD1 . ILE A 380  ? 0.2445 0.2383 0.2541 0.0102  0.0157  0.0434  378  ILE A CD1 
2752  N N   . LYS A 381  ? 0.2081 0.1955 0.2008 0.0141  0.0168  0.0276  379  LYS A N   
2753  C CA  . LYS A 381  ? 0.2170 0.2044 0.2060 0.0151  0.0169  0.0247  379  LYS A CA  
2754  C C   . LYS A 381  ? 0.2331 0.2239 0.2193 0.0164  0.0177  0.0231  379  LYS A C   
2755  O O   . LYS A 381  ? 0.2200 0.2141 0.2037 0.0175  0.0180  0.0223  379  LYS A O   
2756  C CB  . LYS A 381  ? 0.2194 0.2016 0.2079 0.0146  0.0162  0.0215  379  LYS A CB  
2757  C CG  . LYS A 381  ? 0.2258 0.2078 0.2110 0.0155  0.0160  0.0187  379  LYS A CG  
2758  C CD  . LYS A 381  ? 0.2354 0.2129 0.2206 0.0148  0.0153  0.0163  379  LYS A CD  
2759  C CE  . LYS A 381  ? 0.2733 0.2506 0.2558 0.0155  0.0150  0.0138  379  LYS A CE  
2760  N NZ  . LYS A 381  ? 0.2315 0.2051 0.2141 0.0146  0.0143  0.0119  379  LYS A NZ  
2761  N N   . ARG A 382  ? 0.2209 0.2112 0.2079 0.0162  0.0181  0.0225  380  ARG A N   
2762  C CA  . ARG A 382  ? 0.2314 0.2244 0.2164 0.0176  0.0187  0.0205  380  ARG A CA  
2763  C C   . ARG A 382  ? 0.2250 0.2251 0.2091 0.0186  0.0196  0.0223  380  ARG A C   
2764  O O   . ARG A 382  ? 0.2421 0.2456 0.2238 0.0201  0.0198  0.0200  380  ARG A O   
2765  C CB  . ARG A 382  ? 0.2599 0.2514 0.2465 0.0171  0.0188  0.0201  380  ARG A CB  
2766  C CG  . ARG A 382  ? 0.3342 0.3278 0.3196 0.0185  0.0191  0.0175  380  ARG A CG  
2767  C CD  . ARG A 382  ? 0.4735 0.4630 0.4577 0.0188  0.0181  0.0140  380  ARG A CD  
2768  N NE  . ARG A 382  ? 0.5059 0.4978 0.4880 0.0203  0.0180  0.0119  380  ARG A NE  
2769  C CZ  . ARG A 382  ? 0.5278 0.5167 0.5089 0.0205  0.0170  0.0093  380  ARG A CZ  
2770  N NH1 . ARG A 382  ? 0.6041 0.5878 0.5859 0.0192  0.0161  0.0089  380  ARG A NH1 
2771  N NH2 . ARG A 382  ? 0.4423 0.4338 0.4218 0.0220  0.0167  0.0072  380  ARG A NH2 
2772  N N   . ALA A 383  ? 0.2163 0.2192 0.2027 0.0178  0.0200  0.0263  381  ALA A N   
2773  C CA  . ALA A 383  ? 0.2174 0.2282 0.2032 0.0185  0.0209  0.0287  381  ALA A CA  
2774  C C   . ALA A 383  ? 0.2242 0.2379 0.2077 0.0193  0.0208  0.0287  381  ALA A C   
2775  O O   . ALA A 383  ? 0.2323 0.2526 0.2135 0.0206  0.0214  0.0281  381  ALA A O   
2776  C CB  . ALA A 383  ? 0.2178 0.2306 0.2071 0.0171  0.0212  0.0337  381  ALA A CB  
2777  N N   . GLN A 384  ? 0.2172 0.2264 0.2012 0.0184  0.0198  0.0293  382  GLN A N   
2778  C CA  . GLN A 384  ? 0.2261 0.2377 0.2081 0.0190  0.0194  0.0292  382  GLN A CA  
2779  C C   . GLN A 384  ? 0.2281 0.2397 0.2067 0.0206  0.0194  0.0243  382  GLN A C   
2780  O O   . GLN A 384  ? 0.2449 0.2620 0.2210 0.0219  0.0196  0.0235  382  GLN A O   
2781  C CB  . GLN A 384  ? 0.2175 0.2240 0.2015 0.0178  0.0183  0.0306  382  GLN A CB  
2782  C CG  . GLN A 384  ? 0.2038 0.2113 0.1918 0.0164  0.0180  0.0357  382  GLN A CG  
2783  C CD  . GLN A 384  ? 0.2373 0.2403 0.2278 0.0155  0.0166  0.0367  382  GLN A CD  
2784  O OE1 . GLN A 384  ? 0.2606 0.2590 0.2500 0.0157  0.0161  0.0333  382  GLN A OE1 
2785  N NE2 . GLN A 384  ? 0.2518 0.2564 0.2461 0.0145  0.0160  0.0414  382  GLN A NE2 
2786  N N   . LEU A 385  ? 0.2235 0.2289 0.2020 0.0205  0.0189  0.0209  383  LEU A N   
2787  C CA  . LEU A 385  ? 0.2363 0.2412 0.2126 0.0219  0.0184  0.0164  383  LEU A CA  
2788  C C   . LEU A 385  ? 0.2615 0.2724 0.2366 0.0236  0.0191  0.0146  383  LEU A C   
2789  O O   . LEU A 385  ? 0.2609 0.2748 0.2339 0.0251  0.0188  0.0116  383  LEU A O   
2790  C CB  . LEU A 385  ? 0.2413 0.2392 0.2185 0.0212  0.0177  0.0139  383  LEU A CB  
2791  C CG  . LEU A 385  ? 0.2822 0.2745 0.2600 0.0199  0.0169  0.0140  383  LEU A CG  
2792  C CD1 . LEU A 385  ? 0.2906 0.2777 0.2693 0.0191  0.0163  0.0120  383  LEU A CD1 
2793  C CD2 . LEU A 385  ? 0.2926 0.2852 0.2686 0.0205  0.0162  0.0124  383  LEU A CD2 
2794  N N   . ASP A 386  ? 0.2507 0.2637 0.2271 0.0234  0.0200  0.0160  384  ASP A N   
2795  C CA  . ASP A 386  ? 0.2682 0.2870 0.2440 0.0252  0.0206  0.0138  384  ASP A CA  
2796  C C   . ASP A 386  ? 0.2617 0.2899 0.2361 0.0260  0.0216  0.0160  384  ASP A C   
2797  O O   . ASP A 386  ? 0.2700 0.3046 0.2437 0.0276  0.0223  0.0141  384  ASP A O   
2798  C CB  . ASP A 386  ? 0.2722 0.2892 0.2502 0.0247  0.0210  0.0141  384  ASP A CB  
2799  C CG  . ASP A 386  ? 0.3646 0.3740 0.3436 0.0244  0.0199  0.0112  384  ASP A CG  
2800  O OD1 . ASP A 386  ? 0.4015 0.4077 0.3795 0.0247  0.0189  0.0085  384  ASP A OD1 
2801  O OD2 . ASP A 386  ? 0.3896 0.3965 0.3705 0.0237  0.0200  0.0117  384  ASP A OD2 
2802  N N   . GLY A 387  ? 0.2603 0.2899 0.2346 0.0249  0.0217  0.0200  385  GLY A N   
2803  C CA  . GLY A 387  ? 0.2530 0.2921 0.2261 0.0254  0.0225  0.0228  385  GLY A CA  
2804  C C   . GLY A 387  ? 0.2395 0.2848 0.2139 0.0253  0.0238  0.0255  385  GLY A C   
2805  O O   . GLY A 387  ? 0.2498 0.3045 0.2226 0.0266  0.0247  0.0253  385  GLY A O   
2806  N N   . LEU A 388  ? 0.2427 0.2834 0.2201 0.0238  0.0238  0.0280  386  LEU A N   
2807  C CA  . LEU A 388  ? 0.2494 0.2957 0.2285 0.0237  0.0250  0.0302  386  LEU A CA  
2808  C C   . LEU A 388  ? 0.2558 0.3076 0.2367 0.0222  0.0254  0.0369  386  LEU A C   
2809  O O   . LEU A 388  ? 0.2829 0.3332 0.2642 0.0211  0.0246  0.0399  386  LEU A O   
2810  C CB  . LEU A 388  ? 0.2521 0.2916 0.2337 0.0230  0.0248  0.0291  386  LEU A CB  
2811  C CG  . LEU A 388  ? 0.2605 0.2953 0.2407 0.0244  0.0242  0.0230  386  LEU A CG  
2812  C CD1 . LEU A 388  ? 0.2868 0.3152 0.2695 0.0236  0.0239  0.0223  386  LEU A CD1 
2813  C CD2 . LEU A 388  ? 0.2838 0.3260 0.2620 0.0268  0.0248  0.0192  386  LEU A CD2 
2814  N N   . ALA A 389  ? 0.2664 0.3253 0.2485 0.0221  0.0266  0.0394  387  ALA A N   
2815  C CA  . ALA A 389  ? 0.2964 0.3629 0.2800 0.0209  0.0270  0.0459  387  ALA A CA  
2816  C C   . ALA A 389  ? 0.2863 0.3463 0.2742 0.0184  0.0259  0.0510  387  ALA A C   
2817  O O   . ALA A 389  ? 0.2860 0.3492 0.2754 0.0172  0.0254  0.0561  387  ALA A O   
2818  C CB  . ALA A 389  ? 0.3063 0.3817 0.2906 0.0213  0.0285  0.0474  387  ALA A CB  
2819  N N   . ASP A 390  ? 0.2523 0.3036 0.2427 0.0176  0.0253  0.0495  388  ASP A N   
2820  C CA  . ASP A 390  ? 0.2627 0.3081 0.2579 0.0153  0.0241  0.0536  388  ASP A CA  
2821  C C   . ASP A 390  ? 0.2405 0.2760 0.2367 0.0152  0.0234  0.0495  388  ASP A C   
2822  O O   . ASP A 390  ? 0.2408 0.2744 0.2340 0.0166  0.0238  0.0444  388  ASP A O   
2823  C CB  . ASP A 390  ? 0.2865 0.3379 0.2858 0.0139  0.0246  0.0595  388  ASP A CB  
2824  C CG  . ASP A 390  ? 0.2865 0.3348 0.2912 0.0117  0.0230  0.0652  388  ASP A CG  
2825  O OD1 . ASP A 390  ? 0.3015 0.3406 0.3084 0.0110  0.0216  0.0636  388  ASP A OD1 
2826  O OD2 . ASP A 390  ? 0.3490 0.4044 0.3563 0.0105  0.0231  0.0713  388  ASP A OD2 
2827  N N   . PHE A 391  ? 0.2442 0.2739 0.2446 0.0135  0.0223  0.0518  389  PHE A N   
2828  C CA  . PHE A 391  ? 0.2372 0.2584 0.2385 0.0132  0.0216  0.0482  389  PHE A CA  
2829  C C   . PHE A 391  ? 0.2348 0.2567 0.2385 0.0127  0.0221  0.0488  389  PHE A C   
2830  O O   . PHE A 391  ? 0.2333 0.2610 0.2394 0.0120  0.0227  0.0531  389  PHE A O   
2831  C CB  . PHE A 391  ? 0.2314 0.2461 0.2365 0.0117  0.0199  0.0496  389  PHE A CB  
2832  C CG  . PHE A 391  ? 0.2076 0.2216 0.2109 0.0121  0.0193  0.0493  389  PHE A CG  
2833  C CD1 . PHE A 391  ? 0.2269 0.2372 0.2263 0.0132  0.0192  0.0444  389  PHE A CD1 
2834  C CD2 . PHE A 391  ? 0.2240 0.2416 0.2297 0.0113  0.0186  0.0542  389  PHE A CD2 
2835  C CE1 . PHE A 391  ? 0.2539 0.2638 0.2516 0.0136  0.0187  0.0439  389  PHE A CE1 
2836  C CE2 . PHE A 391  ? 0.2547 0.2719 0.2587 0.0118  0.0180  0.0538  389  PHE A CE2 
2837  C CZ  . PHE A 391  ? 0.2628 0.2762 0.2628 0.0130  0.0181  0.0486  389  PHE A CZ  
2838  N N   . PRO A 392  ? 0.2254 0.2418 0.2283 0.0131  0.0220  0.0446  390  PRO A N   
2839  C CA  . PRO A 392  ? 0.2152 0.2315 0.2207 0.0125  0.0223  0.0451  390  PRO A CA  
2840  C C   . PRO A 392  ? 0.2131 0.2240 0.2235 0.0106  0.0209  0.0470  390  PRO A C   
2841  O O   . PRO A 392  ? 0.2353 0.2452 0.2482 0.0100  0.0209  0.0472  390  PRO A O   
2842  C CB  . PRO A 392  ? 0.2022 0.2150 0.2045 0.0138  0.0225  0.0396  390  PRO A CB  
2843  C CG  . PRO A 392  ? 0.2121 0.2193 0.2126 0.0138  0.0215  0.0371  390  PRO A CG  
2844  C CD  . PRO A 392  ? 0.2068 0.2176 0.2065 0.0139  0.0215  0.0396  390  PRO A CD  
2845  N N   . VAL A 393  ? 0.2321 0.2395 0.2443 0.0098  0.0197  0.0480  391  VAL A N   
2846  C CA  . VAL A 393  ? 0.2138 0.2163 0.2313 0.0082  0.0181  0.0495  391  VAL A CA  
2847  C C   . VAL A 393  ? 0.2194 0.2241 0.2407 0.0073  0.0172  0.0544  391  VAL A C   
2848  O O   . VAL A 393  ? 0.2294 0.2381 0.2483 0.0079  0.0177  0.0558  391  VAL A O   
2849  C CB  . VAL A 393  ? 0.2009 0.1962 0.2175 0.0083  0.0171  0.0450  391  VAL A CB  
2850  C CG1 . VAL A 393  ? 0.2322 0.2252 0.2460 0.0089  0.0176  0.0409  391  VAL A CG1 
2851  C CG2 . VAL A 393  ? 0.2268 0.2215 0.2398 0.0092  0.0171  0.0434  391  VAL A CG2 
2852  N N   . PHE A 394  ? 0.2210 0.2231 0.2487 0.0057  0.0156  0.0569  392  PHE A N   
2853  C CA  . PHE A 394  ? 0.2137 0.2167 0.2462 0.0046  0.0142  0.0615  392  PHE A CA  
2854  C C   . PHE A 394  ? 0.2427 0.2414 0.2741 0.0052  0.0132  0.0590  392  PHE A C   
2855  O O   . PHE A 394  ? 0.2403 0.2345 0.2684 0.0060  0.0133  0.0538  392  PHE A O   
2856  C CB  . PHE A 394  ? 0.2193 0.2199 0.2598 0.0029  0.0125  0.0643  392  PHE A CB  
2857  C CG  . PHE A 394  ? 0.2018 0.2070 0.2438 0.0023  0.0134  0.0671  392  PHE A CG  
2858  C CD1 . PHE A 394  ? 0.2567 0.2699 0.2987 0.0020  0.0144  0.0724  392  PHE A CD1 
2859  C CD2 . PHE A 394  ? 0.2332 0.2354 0.2764 0.0021  0.0134  0.0645  392  PHE A CD2 
2860  C CE1 . PHE A 394  ? 0.2429 0.2611 0.2863 0.0014  0.0154  0.0750  392  PHE A CE1 
2861  C CE2 . PHE A 394  ? 0.2116 0.2182 0.2563 0.0015  0.0142  0.0672  392  PHE A CE2 
2862  C CZ  . PHE A 394  ? 0.2220 0.2367 0.2668 0.0012  0.0153  0.0724  392  PHE A CZ  
2863  N N   . THR A 395  ? 0.2161 0.2167 0.2504 0.0046  0.0122  0.0631  393  THR A N   
2864  C CA  . THR A 395  ? 0.2509 0.2479 0.2846 0.0051  0.0112  0.0611  393  THR A CA  
2865  C C   . THR A 395  ? 0.2540 0.2466 0.2957 0.0039  0.0085  0.0629  393  THR A C   
2866  O O   . THR A 395  ? 0.2605 0.2495 0.3026 0.0044  0.0074  0.0606  393  THR A O   
2867  C CB  . THR A 395  ? 0.2457 0.2481 0.2756 0.0058  0.0119  0.0634  393  THR A CB  
2868  O OG1 . THR A 395  ? 0.2618 0.2700 0.2959 0.0046  0.0115  0.0703  393  THR A OG1 
2869  C CG2 . THR A 395  ? 0.2940 0.3001 0.3161 0.0073  0.0143  0.0603  393  THR A CG2 
2870  N N   . ARG A 396  ? 0.2474 0.2405 0.2960 0.0025  0.0074  0.0667  394  ARG A N   
2871  C CA  . ARG A 396  ? 0.2530 0.2414 0.3102 0.0015  0.0045  0.0675  394  ARG A CA  
2872  C C   . ARG A 396  ? 0.2472 0.2315 0.3071 0.0011  0.0040  0.0641  394  ARG A C   
2873  O O   . ARG A 396  ? 0.2468 0.2336 0.3060 0.0007  0.0051  0.0653  394  ARG A O   
2874  C CB  . ARG A 396  ? 0.2602 0.2521 0.3247 -0.0001 0.0030  0.0751  394  ARG A CB  
2875  C CG  . ARG A 396  ? 0.2763 0.2727 0.3389 0.0001  0.0031  0.0790  394  ARG A CG  
2876  C CD  . ARG A 396  ? 0.3442 0.3438 0.4152 -0.0017 0.0011  0.0870  394  ARG A CD  
2877  N NE  . ARG A 396  ? 0.3685 0.3740 0.4371 -0.0017 0.0015  0.0915  394  ARG A NE  
2878  C CZ  . ARG A 396  ? 0.4133 0.4184 0.4877 -0.0024 -0.0009 0.0956  394  ARG A CZ  
2879  N NH1 . ARG A 396  ? 0.4356 0.4346 0.5192 -0.0033 -0.0040 0.0958  394  ARG A NH1 
2880  N NH2 . ARG A 396  ? 0.3922 0.4034 0.4633 -0.0023 -0.0003 0.0994  394  ARG A NH2 
2881  N N   . LYS A 397  ? 0.2515 0.2300 0.3143 0.0013  0.0023  0.0596  395  LYS A N   
2882  C CA  . LYS A 397  ? 0.2383 0.2131 0.3033 0.0011  0.0017  0.0557  395  LYS A CA  
2883  C C   . LYS A 397  ? 0.2495 0.2254 0.3220 -0.0004 0.0004  0.0599  395  LYS A C   
2884  O O   . LYS A 397  ? 0.2459 0.2217 0.3180 -0.0007 0.0010  0.0585  395  LYS A O   
2885  C CB  . LYS A 397  ? 0.2822 0.2518 0.3504 0.0016  -0.0002 0.0506  395  LYS A CB  
2886  C CG  . LYS A 397  ? 0.2887 0.2553 0.3561 0.0018  -0.0003 0.0449  395  LYS A CG  
2887  C CD  . LYS A 397  ? 0.2774 0.2420 0.3541 0.0008  -0.0027 0.0455  395  LYS A CD  
2888  C CE  . LYS A 397  ? 0.3090 0.2713 0.3848 0.0010  -0.0029 0.0396  395  LYS A CE  
2889  N NZ  . LYS A 397  ? 0.3204 0.2808 0.4057 0.0001  -0.0056 0.0396  395  LYS A NZ  
2890  N N   . ILE A 398  ? 0.2405 0.2175 0.3202 -0.0015 -0.0015 0.0655  396  ILE A N   
2891  C CA  . ILE A 398  ? 0.2714 0.2492 0.3593 -0.0032 -0.0031 0.0699  396  ILE A CA  
2892  C C   . ILE A 398  ? 0.2391 0.2226 0.3231 -0.0036 -0.0007 0.0733  396  ILE A C   
2893  O O   . ILE A 398  ? 0.2571 0.2410 0.3455 -0.0047 -0.0013 0.0749  396  ILE A O   
2894  C CB  . ILE A 398  ? 0.2745 0.2525 0.3716 -0.0043 -0.0059 0.0756  396  ILE A CB  
2895  C CG1 . ILE A 398  ? 0.3348 0.3120 0.4423 -0.0061 -0.0083 0.0792  396  ILE A CG1 
2896  C CG2 . ILE A 398  ? 0.2886 0.2729 0.3820 -0.0046 -0.0044 0.0817  396  ILE A CG2 
2897  C CD1 . ILE A 398  ? 0.3838 0.3589 0.5022 -0.0072 -0.0120 0.0832  396  ILE A CD1 
2898  N N   . HIS A 399  ? 0.2414 0.2296 0.3171 -0.0027 0.0019  0.0742  397  HIS A N   
2899  C CA  . HIS A 399  ? 0.2634 0.2576 0.3350 -0.0028 0.0043  0.0766  397  HIS A CA  
2900  C C   . HIS A 399  ? 0.2364 0.2282 0.3045 -0.0022 0.0055  0.0713  397  HIS A C   
2901  O O   . HIS A 399  ? 0.2341 0.2284 0.3039 -0.0029 0.0060  0.0732  397  HIS A O   
2902  C CB  . HIS A 399  ? 0.2580 0.2577 0.3215 -0.0017 0.0067  0.0774  397  HIS A CB  
2903  C CG  . HIS A 399  ? 0.2367 0.2406 0.3031 -0.0024 0.0059  0.0836  397  HIS A CG  
2904  N ND1 . HIS A 399  ? 0.2835 0.2923 0.3436 -0.0014 0.0075  0.0845  397  HIS A ND1 
2905  C CD2 . HIS A 399  ? 0.3203 0.3244 0.3958 -0.0041 0.0034  0.0893  397  HIS A CD2 
2906  C CE1 . HIS A 399  ? 0.2897 0.3019 0.3544 -0.0025 0.0061  0.0907  397  HIS A CE1 
2907  N NE2 . HIS A 399  ? 0.2789 0.2881 0.3531 -0.0042 0.0035  0.0939  397  HIS A NE2 
2908  N N   . THR A 400  ? 0.2310 0.2183 0.2944 -0.0009 0.0058  0.0649  398  THR A N   
2909  C CA  . THR A 400  ? 0.2189 0.2037 0.2796 -0.0005 0.0065  0.0601  398  THR A CA  
2910  C C   . THR A 400  ? 0.2220 0.2039 0.2906 -0.0017 0.0044  0.0602  398  THR A C   
2911  O O   . THR A 400  ? 0.2172 0.1998 0.2855 -0.0020 0.0050  0.0595  398  THR A O   
2912  C CB  . THR A 400  ? 0.2238 0.2046 0.2791 0.0009  0.0068  0.0538  398  THR A CB  
2913  O OG1 . THR A 400  ? 0.2247 0.2086 0.2726 0.0020  0.0089  0.0536  398  THR A OG1 
2914  C CG2 . THR A 400  ? 0.1979 0.1761 0.2512 0.0011  0.0071  0.0491  398  THR A CG2 
2915  N N   . ASP A 401  ? 0.2207 0.1994 0.2969 -0.0025 0.0017  0.0609  399  ASP A N   
2916  C CA  . ASP A 401  ? 0.2550 0.2308 0.3395 -0.0037 -0.0007 0.0607  399  ASP A CA  
2917  C C   . ASP A 401  ? 0.2200 0.2001 0.3089 -0.0051 -0.0006 0.0668  399  ASP A C   
2918  O O   . ASP A 401  ? 0.2298 0.2092 0.3213 -0.0057 -0.0010 0.0659  399  ASP A O   
2919  C CB  . ASP A 401  ? 0.2309 0.2027 0.3236 -0.0041 -0.0039 0.0603  399  ASP A CB  
2920  C CG  . ASP A 401  ? 0.2942 0.2619 0.3837 -0.0027 -0.0042 0.0535  399  ASP A CG  
2921  O OD1 . ASP A 401  ? 0.3123 0.2794 0.3952 -0.0018 -0.0026 0.0486  399  ASP A OD1 
2922  O OD2 . ASP A 401  ? 0.3203 0.2857 0.4140 -0.0025 -0.0061 0.0531  399  ASP A OD2 
2923  N N   . VAL A 402  ? 0.2349 0.2196 0.3245 -0.0057 -0.0001 0.0731  400  VAL A N   
2924  C CA  . VAL A 402  ? 0.2429 0.2330 0.3364 -0.0072 0.0002  0.0794  400  VAL A CA  
2925  C C   . VAL A 402  ? 0.1937 0.1873 0.2802 -0.0065 0.0030  0.0778  400  VAL A C   
2926  O O   . VAL A 402  ? 0.2141 0.2091 0.3040 -0.0075 0.0029  0.0793  400  VAL A O   
2927  C CB  . VAL A 402  ? 0.2602 0.2557 0.3552 -0.0080 0.0003  0.0865  400  VAL A CB  
2928  C CG1 . VAL A 402  ? 0.2222 0.2246 0.3200 -0.0095 0.0011  0.0930  400  VAL A CG1 
2929  C CG2 . VAL A 402  ? 0.2804 0.2723 0.3842 -0.0089 -0.0031 0.0888  400  VAL A CG2 
2930  N N   . SER A 403  ? 0.2353 0.2305 0.3124 -0.0048 0.0055  0.0747  401  SER A N   
2931  C CA  . SER A 403  ? 0.2356 0.2338 0.3061 -0.0039 0.0081  0.0726  401  SER A CA  
2932  C C   . SER A 403  ? 0.2395 0.2332 0.3114 -0.0040 0.0073  0.0682  401  SER A C   
2933  O O   . SER A 403  ? 0.2342 0.2305 0.3067 -0.0044 0.0081  0.0692  401  SER A O   
2934  C CB  . SER A 403  ? 0.2485 0.2473 0.3098 -0.0019 0.0101  0.0688  401  SER A CB  
2935  O OG  . SER A 403  ? 0.2329 0.2336 0.2884 -0.0009 0.0122  0.0660  401  SER A OG  
2936  N N   . TYR A 404  ? 0.2107 0.1982 0.2835 -0.0036 0.0058  0.0634  402  TYR A N   
2937  C CA  . TYR A 404  ? 0.2206 0.2043 0.2945 -0.0037 0.0049  0.0590  402  TYR A CA  
2938  C C   . TYR A 404  ? 0.1996 0.1838 0.2820 -0.0054 0.0032  0.0623  402  TYR A C   
2939  O O   . TYR A 404  ? 0.2247 0.2099 0.3069 -0.0056 0.0037  0.0614  402  TYR A O   
2940  C CB  . TYR A 404  ? 0.2065 0.1846 0.2808 -0.0032 0.0033  0.0537  402  TYR A CB  
2941  C CG  . TYR A 404  ? 0.2250 0.2000 0.2983 -0.0030 0.0028  0.0483  402  TYR A CG  
2942  C CD1 . TYR A 404  ? 0.2256 0.1989 0.3062 -0.0041 0.0006  0.0479  402  TYR A CD1 
2943  C CD2 . TYR A 404  ? 0.2171 0.1913 0.2826 -0.0017 0.0042  0.0437  402  TYR A CD2 
2944  C CE1 . TYR A 404  ? 0.2344 0.2055 0.3139 -0.0038 0.0001  0.0429  402  TYR A CE1 
2945  C CE2 . TYR A 404  ? 0.2094 0.1815 0.2740 -0.0017 0.0037  0.0391  402  TYR A CE2 
2946  C CZ  . TYR A 404  ? 0.2198 0.1906 0.2912 -0.0027 0.0017  0.0387  402  TYR A CZ  
2947  O OH  . TYR A 404  ? 0.2445 0.2140 0.3149 -0.0026 0.0011  0.0341  402  TYR A OH  
2948  N N   . ILE A 405  ? 0.2106 0.1943 0.3011 -0.0067 0.0010  0.0663  403  ILE A N   
2949  C CA  . ILE A 405  ? 0.2251 0.2089 0.3248 -0.0084 -0.0010 0.0695  403  ILE A CA  
2950  C C   . ILE A 405  ? 0.1923 0.1826 0.2914 -0.0091 0.0008  0.0747  403  ILE A C   
2951  O O   . ILE A 405  ? 0.2317 0.2225 0.3340 -0.0099 0.0004  0.0749  403  ILE A O   
2952  C CB  . ILE A 405  ? 0.2193 0.2008 0.3286 -0.0096 -0.0042 0.0727  403  ILE A CB  
2953  C CG1 . ILE A 405  ? 0.2931 0.2684 0.4032 -0.0086 -0.0060 0.0664  403  ILE A CG1 
2954  C CG2 . ILE A 405  ? 0.2603 0.2421 0.3798 -0.0116 -0.0065 0.0765  403  ILE A CG2 
2955  C CD1 . ILE A 405  ? 0.3761 0.3489 0.4946 -0.0093 -0.0090 0.0686  403  ILE A CD1 
2956  N N   . ALA A 406  ? 0.2184 0.2142 0.3129 -0.0088 0.0030  0.0784  404  ALA A N   
2957  C CA  . ALA A 406  ? 0.2121 0.2152 0.3052 -0.0092 0.0051  0.0829  404  ALA A CA  
2958  C C   . ALA A 406  ? 0.2285 0.2320 0.3155 -0.0080 0.0070  0.0784  404  ALA A C   
2959  O O   . ALA A 406  ? 0.2417 0.2487 0.3310 -0.0087 0.0075  0.0806  404  ALA A O   
2960  C CB  . ALA A 406  ? 0.2399 0.2492 0.3280 -0.0085 0.0071  0.0863  404  ALA A CB  
2961  N N   . CYS A 407  ? 0.2444 0.2447 0.3240 -0.0062 0.0081  0.0725  405  CYS A N   
2962  C CA  . CYS A 407  ? 0.2252 0.2256 0.2995 -0.0051 0.0096  0.0684  405  CYS A CA  
2963  C C   . CYS A 407  ? 0.2310 0.2273 0.3100 -0.0060 0.0078  0.0659  405  CYS A C   
2964  O O   . CYS A 407  ? 0.2178 0.2159 0.2958 -0.0058 0.0087  0.0652  405  CYS A O   
2965  C CB  . CYS A 407  ? 0.2460 0.2441 0.3119 -0.0032 0.0109  0.0632  405  CYS A CB  
2966  S SG  . CYS A 407  ? 0.3143 0.3189 0.3742 -0.0020 0.0134  0.0657  405  CYS A SG  
2967  N N   . ALA A 408  ? 0.2183 0.2094 0.3027 -0.0068 0.0052  0.0645  406  ALA A N   
2968  C CA  . ALA A 408  ? 0.2235 0.2112 0.3131 -0.0076 0.0032  0.0622  406  ALA A CA  
2969  C C   . ALA A 408  ? 0.2146 0.2059 0.3113 -0.0092 0.0026  0.0674  406  ALA A C   
2970  O O   . ALA A 408  ? 0.2435 0.2345 0.3417 -0.0096 0.0022  0.0660  406  ALA A O   
2971  C CB  . ALA A 408  ? 0.2445 0.2266 0.3392 -0.0079 0.0003  0.0593  406  ALA A CB  
2972  N N   . ALA A 409  ? 0.2191 0.2139 0.3202 -0.0103 0.0023  0.0736  407  ALA A N   
2973  C CA  . ALA A 409  ? 0.2495 0.2485 0.3572 -0.0121 0.0019  0.0793  407  ALA A CA  
2974  C C   . ALA A 409  ? 0.2245 0.2291 0.3270 -0.0114 0.0047  0.0797  407  ALA A C   
2975  O O   . ALA A 409  ? 0.2368 0.2429 0.3433 -0.0123 0.0043  0.0809  407  ALA A O   
2976  C CB  . ALA A 409  ? 0.2526 0.2555 0.3655 -0.0134 0.0013  0.0865  407  ALA A CB  
2977  N N   . LYS A 410  ? 0.2328 0.2403 0.3264 -0.0096 0.0074  0.0783  408  LYS A N   
2978  C CA  . LYS A 410  ? 0.2217 0.2344 0.3104 -0.0086 0.0100  0.0778  408  LYS A CA  
2979  C C   . LYS A 410  ? 0.2020 0.2105 0.2888 -0.0080 0.0097  0.0723  408  LYS A C   
2980  O O   . LYS A 410  ? 0.2291 0.2405 0.3174 -0.0083 0.0102  0.0731  408  LYS A O   
2981  C CB  . LYS A 410  ? 0.2455 0.2615 0.3257 -0.0067 0.0126  0.0767  408  LYS A CB  
2982  C CG  . LYS A 410  ? 0.2701 0.2917 0.3452 -0.0054 0.0152  0.0757  408  LYS A CG  
2983  C CD  . LYS A 410  ? 0.2799 0.3045 0.3472 -0.0034 0.0173  0.0740  408  LYS A CD  
2984  C CE  . LYS A 410  ? 0.2821 0.3128 0.3505 -0.0040 0.0179  0.0795  408  LYS A CE  
2985  N NZ  . LYS A 410  ? 0.3147 0.3547 0.3852 -0.0045 0.0194  0.0841  408  LYS A NZ  
2986  N N   . LEU A 411  ? 0.1983 0.2004 0.2821 -0.0072 0.0087  0.0670  409  LEU A N   
2987  C CA  . LEU A 411  ? 0.2000 0.1986 0.2820 -0.0067 0.0082  0.0619  409  LEU A CA  
2988  C C   . LEU A 411  ? 0.2157 0.2128 0.3057 -0.0084 0.0060  0.0627  409  LEU A C   
2989  O O   . LEU A 411  ? 0.1987 0.1964 0.2886 -0.0084 0.0061  0.0613  409  LEU A O   
2990  C CB  . LEU A 411  ? 0.2034 0.1965 0.2812 -0.0058 0.0075  0.0566  409  LEU A CB  
2991  C CG  . LEU A 411  ? 0.2048 0.1989 0.2739 -0.0039 0.0098  0.0544  409  LEU A CG  
2992  C CD1 . LEU A 411  ? 0.2292 0.2184 0.2951 -0.0033 0.0090  0.0502  409  LEU A CD1 
2993  C CD2 . LEU A 411  ? 0.2127 0.2084 0.2774 -0.0029 0.0112  0.0523  409  LEU A CD2 
2994  N N   . LEU A 412  ? 0.2133 0.2084 0.3108 -0.0098 0.0036  0.0651  410  LEU A N   
2995  C CA  . LEU A 412  ? 0.2112 0.2044 0.3171 -0.0114 0.0011  0.0653  410  LEU A CA  
2996  C C   . LEU A 412  ? 0.2153 0.2139 0.3253 -0.0125 0.0017  0.0704  410  LEU A C   
2997  O O   . LEU A 412  ? 0.2619 0.2595 0.3772 -0.0136 0.0001  0.0700  410  LEU A O   
2998  C CB  . LEU A 412  ? 0.2606 0.2499 0.3741 -0.0125 -0.0019 0.0660  410  LEU A CB  
2999  C CG  . LEU A 412  ? 0.2199 0.2035 0.3309 -0.0115 -0.0032 0.0597  410  LEU A CG  
3000  C CD1 . LEU A 412  ? 0.2758 0.2563 0.3944 -0.0123 -0.0059 0.0608  410  LEU A CD1 
3001  C CD2 . LEU A 412  ? 0.2537 0.2347 0.3648 -0.0113 -0.0044 0.0543  410  LEU A CD2 
3002  N N   . ALA A 413  ? 0.2071 0.2117 0.3146 -0.0124 0.0040  0.0749  411  ALA A N   
3003  C CA  . ALA A 413  ? 0.2448 0.2557 0.3554 -0.0132 0.0051  0.0795  411  ALA A CA  
3004  C C   . ALA A 413  ? 0.2501 0.2630 0.3548 -0.0118 0.0071  0.0762  411  ALA A C   
3005  O O   . ALA A 413  ? 0.2718 0.2898 0.3787 -0.0124 0.0080  0.0791  411  ALA A O   
3006  C CB  . ALA A 413  ? 0.2451 0.2631 0.3556 -0.0136 0.0068  0.0857  411  ALA A CB  
3007  N N   . ALA A 414  ? 0.2467 0.2557 0.3442 -0.0101 0.0077  0.0704  412  ALA A N   
3008  C CA  . ALA A 414  ? 0.2397 0.2507 0.3315 -0.0086 0.0095  0.0675  412  ALA A CA  
3009  C C   . ALA A 414  ? 0.2605 0.2658 0.3507 -0.0082 0.0081  0.0619  412  ALA A C   
3010  O O   . ALA A 414  ? 0.2127 0.2178 0.2969 -0.0067 0.0093  0.0585  412  ALA A O   
3011  C CB  . ALA A 414  ? 0.2782 0.2919 0.3620 -0.0066 0.0121  0.0665  412  ALA A CB  
3012  N N   . THR A 415  ? 0.2485 0.2495 0.3444 -0.0096 0.0054  0.0608  413  THR A N   
3013  C CA  . THR A 415  ? 0.2507 0.2472 0.3450 -0.0093 0.0039  0.0554  413  THR A CA  
3014  C C   . THR A 415  ? 0.2513 0.2498 0.3450 -0.0091 0.0044  0.0545  413  THR A C   
3015  O O   . THR A 415  ? 0.2551 0.2510 0.3457 -0.0085 0.0037  0.0501  413  THR A O   
3016  C CB  . THR A 415  ? 0.2862 0.2784 0.3874 -0.0106 0.0008  0.0540  413  THR A CB  
3017  O OG1 . THR A 415  ? 0.2984 0.2925 0.4081 -0.0123 -0.0006 0.0581  413  THR A OG1 
3018  C CG2 . THR A 415  ? 0.2577 0.2474 0.3592 -0.0105 0.0002  0.0542  413  THR A CG2 
3019  N N   . ASP A 416  ? 0.2584 0.2619 0.3551 -0.0095 0.0054  0.0586  414  ASP A N   
3020  C CA  . ASP A 416  ? 0.2397 0.2452 0.3355 -0.0091 0.0059  0.0575  414  ASP A CA  
3021  C C   . ASP A 416  ? 0.2316 0.2382 0.3193 -0.0071 0.0080  0.0550  414  ASP A C   
3022  O O   . ASP A 416  ? 0.3259 0.3320 0.4116 -0.0065 0.0079  0.0524  414  ASP A O   
3023  C CB  . ASP A 416  ? 0.2917 0.3028 0.3932 -0.0102 0.0065  0.0625  414  ASP A CB  
3024  C CG  . ASP A 416  ? 0.3691 0.3859 0.4690 -0.0096 0.0089  0.0665  414  ASP A CG  
3025  O OD1 . ASP A 416  ? 0.3758 0.3916 0.4746 -0.0096 0.0090  0.0676  414  ASP A OD1 
3026  O OD2 . ASP A 416  ? 0.4699 0.4925 0.5694 -0.0091 0.0107  0.0685  414  ASP A OD2 
3027  N N   . VAL A 417  ? 0.2277 0.2356 0.3109 -0.0059 0.0098  0.0556  415  VAL A N   
3028  C CA  . VAL A 417  ? 0.2571 0.2663 0.3335 -0.0039 0.0117  0.0533  415  VAL A CA  
3029  C C   . VAL A 417  ? 0.2402 0.2450 0.3107 -0.0029 0.0116  0.0497  415  VAL A C   
3030  O O   . VAL A 417  ? 0.2669 0.2715 0.3323 -0.0014 0.0125  0.0471  415  VAL A O   
3031  C CB  . VAL A 417  ? 0.3022 0.3182 0.3776 -0.0029 0.0141  0.0563  415  VAL A CB  
3032  C CG1 . VAL A 417  ? 0.3373 0.3583 0.4185 -0.0039 0.0143  0.0599  415  VAL A CG1 
3033  C CG2 . VAL A 417  ? 0.2851 0.3022 0.3598 -0.0031 0.0148  0.0586  415  VAL A CG2 
3034  N N   . VAL A 418  ? 0.2082 0.2097 0.2798 -0.0037 0.0105  0.0496  416  VAL A N   
3035  C CA  . VAL A 418  ? 0.1884 0.1857 0.2550 -0.0030 0.0102  0.0461  416  VAL A CA  
3036  C C   . VAL A 418  ? 0.2081 0.2009 0.2779 -0.0043 0.0078  0.0441  416  VAL A C   
3037  O O   . VAL A 418  ? 0.2217 0.2145 0.2980 -0.0057 0.0063  0.0460  416  VAL A O   
3038  C CB  . VAL A 418  ? 0.1801 0.1783 0.2435 -0.0022 0.0116  0.0472  416  VAL A CB  
3039  C CG1 . VAL A 418  ? 0.2298 0.2326 0.2892 -0.0006 0.0139  0.0479  416  VAL A CG1 
3040  C CG2 . VAL A 418  ? 0.1929 0.1922 0.2615 -0.0035 0.0111  0.0511  416  VAL A CG2 
3041  N N   . PHE A 419  ? 0.1775 0.1669 0.2430 -0.0037 0.0072  0.0403  417  PHE A N   
3042  C CA  . PHE A 419  ? 0.2108 0.1966 0.2787 -0.0046 0.0051  0.0375  417  PHE A CA  
3043  C C   . PHE A 419  ? 0.1875 0.1714 0.2537 -0.0042 0.0052  0.0371  417  PHE A C   
3044  O O   . PHE A 419  ? 0.1946 0.1774 0.2548 -0.0032 0.0061  0.0349  417  PHE A O   
3045  C CB  . PHE A 419  ? 0.2012 0.1856 0.2656 -0.0043 0.0043  0.0335  417  PHE A CB  
3046  C CG  . PHE A 419  ? 0.2152 0.1968 0.2810 -0.0050 0.0022  0.0299  417  PHE A CG  
3047  C CD1 . PHE A 419  ? 0.2393 0.2202 0.3120 -0.0061 0.0001  0.0297  417  PHE A CD1 
3048  C CD2 . PHE A 419  ? 0.2060 0.1862 0.2666 -0.0044 0.0022  0.0266  417  PHE A CD2 
3049  C CE1 . PHE A 419  ? 0.2148 0.1938 0.2894 -0.0065 -0.0019 0.0258  417  PHE A CE1 
3050  C CE2 . PHE A 419  ? 0.2009 0.1796 0.2629 -0.0048 0.0003  0.0230  417  PHE A CE2 
3051  C CZ  . PHE A 419  ? 0.2043 0.1824 0.2732 -0.0058 -0.0017 0.0223  417  PHE A CZ  
3052  N N   . PRO A 420  ? 0.1855 0.1689 0.2570 -0.0051 0.0043  0.0393  418  PRO A N   
3053  C CA  . PRO A 420  ? 0.1928 0.1745 0.2631 -0.0047 0.0044  0.0391  418  PRO A CA  
3054  C C   . PRO A 420  ? 0.1921 0.1703 0.2617 -0.0046 0.0027  0.0343  418  PRO A C   
3055  O O   . PRO A 420  ? 0.2099 0.1868 0.2834 -0.0053 0.0007  0.0320  418  PRO A O   
3056  C CB  . PRO A 420  ? 0.1789 0.1613 0.2566 -0.0058 0.0034  0.0433  418  PRO A CB  
3057  C CG  . PRO A 420  ? 0.1871 0.1730 0.2681 -0.0066 0.0038  0.0466  418  PRO A CG  
3058  C CD  . PRO A 420  ? 0.1891 0.1741 0.2684 -0.0064 0.0033  0.0429  418  PRO A CD  
3059  N N   . GLN A 421  ? 0.1807 0.1577 0.2453 -0.0037 0.0036  0.0328  419  GLN A N   
3060  C CA  . GLN A 421  ? 0.2048 0.1793 0.2678 -0.0035 0.0024  0.0282  419  GLN A CA  
3061  C C   . GLN A 421  ? 0.2028 0.1760 0.2662 -0.0031 0.0024  0.0289  419  GLN A C   
3062  O O   . GLN A 421  ? 0.2197 0.1935 0.2780 -0.0023 0.0042  0.0299  419  GLN A O   
3063  C CB  . GLN A 421  ? 0.1885 0.1634 0.2441 -0.0027 0.0035  0.0255  419  GLN A CB  
3064  C CG  . GLN A 421  ? 0.1903 0.1667 0.2455 -0.0030 0.0035  0.0253  419  GLN A CG  
3065  C CD  . GLN A 421  ? 0.2015 0.1785 0.2500 -0.0022 0.0047  0.0239  419  GLN A CD  
3066  O OE1 . GLN A 421  ? 0.2323 0.2099 0.2770 -0.0013 0.0063  0.0255  419  GLN A OE1 
3067  N NE2 . GLN A 421  ? 0.2106 0.1877 0.2576 -0.0026 0.0036  0.0210  419  GLN A NE2 
3068  N N   . PHE A 422  ? 0.1894 0.1607 0.2593 -0.0038 0.0003  0.0282  420  PHE A N   
3069  C CA  . PHE A 422  ? 0.1878 0.1579 0.2596 -0.0036 0.0000  0.0295  420  PHE A CA  
3070  C C   . PHE A 422  ? 0.1784 0.1466 0.2472 -0.0028 -0.0006 0.0247  420  PHE A C   
3071  O O   . PHE A 422  ? 0.2064 0.1731 0.2797 -0.0030 -0.0027 0.0212  420  PHE A O   
3072  C CB  . PHE A 422  ? 0.2045 0.1738 0.2858 -0.0047 -0.0022 0.0321  420  PHE A CB  
3073  C CG  . PHE A 422  ? 0.2174 0.1892 0.3016 -0.0056 -0.0016 0.0372  420  PHE A CG  
3074  C CD1 . PHE A 422  ? 0.2345 0.2092 0.3157 -0.0053 0.0005  0.0418  420  PHE A CD1 
3075  C CD2 . PHE A 422  ? 0.1981 0.1701 0.2878 -0.0065 -0.0031 0.0372  420  PHE A CD2 
3076  C CE1 . PHE A 422  ? 0.2436 0.2217 0.3273 -0.0061 0.0013  0.0464  420  PHE A CE1 
3077  C CE2 . PHE A 422  ? 0.2432 0.2180 0.3356 -0.0074 -0.0024 0.0420  420  PHE A CE2 
3078  C CZ  . PHE A 422  ? 0.2194 0.1975 0.3088 -0.0072 -0.0002 0.0467  420  PHE A CZ  
3079  N N   . ALA A 423  ? 0.1929 0.1616 0.2547 -0.0019 0.0013  0.0244  421  ALA A N   
3080  C CA  . ALA A 423  ? 0.1974 0.1649 0.2556 -0.0012 0.0012  0.0203  421  ALA A CA  
3081  C C   . ALA A 423  ? 0.2370 0.2031 0.2984 -0.0010 0.0004  0.0212  421  ALA A C   
3082  O O   . ALA A 423  ? 0.2420 0.2086 0.3016 -0.0007 0.0017  0.0248  421  ALA A O   
3083  C CB  . ALA A 423  ? 0.1831 0.1518 0.2329 -0.0004 0.0033  0.0199  421  ALA A CB  
3084  N N   . THR A 424  ? 0.2108 0.1752 0.2772 -0.0010 -0.0017 0.0179  422  THR A N   
3085  C CA  . THR A 424  ? 0.2171 0.1799 0.2871 -0.0007 -0.0027 0.0184  422  THR A CA  
3086  C C   . THR A 424  ? 0.2321 0.1936 0.3063 -0.0004 -0.0050 0.0130  422  THR A C   
3087  O O   . THR A 424  ? 0.2342 0.1959 0.3120 -0.0008 -0.0066 0.0101  422  THR A O   
3088  C CB  . THR A 424  ? 0.2591 0.2216 0.3360 -0.0015 -0.0036 0.0238  422  THR A CB  
3089  O OG1 . THR A 424  ? 0.2521 0.2132 0.3321 -0.0012 -0.0046 0.0246  422  THR A OG1 
3090  C CG2 . THR A 424  ? 0.2659 0.2275 0.3512 -0.0025 -0.0061 0.0234  422  THR A CG2 
3091  N N   . HIS A 425  ? 0.2132 0.1738 0.2871 0.0003  -0.0053 0.0114  423  HIS A N   
3092  C CA  . HIS A 425  ? 0.2079 0.1674 0.2871 0.0008  -0.0076 0.0064  423  HIS A CA  
3093  C C   . HIS A 425  ? 0.2444 0.2016 0.3329 0.0006  -0.0100 0.0085  423  HIS A C   
3094  O O   . HIS A 425  ? 0.2848 0.2409 0.3789 0.0012  -0.0122 0.0044  423  HIS A O   
3095  C CB  . HIS A 425  ? 0.2087 0.1692 0.2819 0.0018  -0.0066 0.0027  423  HIS A CB  
3096  C CG  . HIS A 425  ? 0.2459 0.2088 0.3108 0.0018  -0.0047 0.0007  423  HIS A CG  
3097  N ND1 . HIS A 425  ? 0.2742 0.2381 0.3311 0.0023  -0.0025 0.0013  423  HIS A ND1 
3098  C CD2 . HIS A 425  ? 0.2591 0.2238 0.3228 0.0014  -0.0048 -0.0014 423  HIS A CD2 
3099  C CE1 . HIS A 425  ? 0.2864 0.2524 0.3379 0.0020  -0.0015 -0.0003 423  HIS A CE1 
3100  N NE2 . HIS A 425  ? 0.2341 0.2008 0.2894 0.0015  -0.0028 -0.0019 423  HIS A NE2 
3101  N N   . ASN A 426  ? 0.2449 0.2017 0.3355 -0.0001 -0.0096 0.0149  424  ASN A N   
3102  C CA  . ASN A 426  ? 0.2787 0.2336 0.3779 -0.0005 -0.0117 0.0181  424  ASN A CA  
3103  C C   . ASN A 426  ? 0.2596 0.2133 0.3687 -0.0015 -0.0145 0.0185  424  ASN A C   
3104  O O   . ASN A 426  ? 0.2645 0.2194 0.3739 -0.0025 -0.0139 0.0222  424  ASN A O   
3105  C CB  . ASN A 426  ? 0.2724 0.2286 0.3687 -0.0009 -0.0099 0.0250  424  ASN A CB  
3106  C CG  . ASN A 426  ? 0.2744 0.2291 0.3789 -0.0014 -0.0120 0.0292  424  ASN A CG  
3107  O OD1 . ASN A 426  ? 0.2822 0.2352 0.3966 -0.0022 -0.0149 0.0295  424  ASN A OD1 
3108  N ND2 . ASN A 426  ? 0.2592 0.2148 0.3601 -0.0011 -0.0107 0.0324  424  ASN A ND2 
3109  N N   . ALA A 427  ? 0.2311 0.1827 0.3488 -0.0012 -0.0177 0.0147  425  ALA A N   
3110  C CA  . ALA A 427  ? 0.2679 0.2182 0.3958 -0.0020 -0.0208 0.0142  425  ALA A CA  
3111  C C   . ALA A 427  ? 0.2417 0.1913 0.3764 -0.0036 -0.0218 0.0220  425  ALA A C   
3112  O O   . ALA A 427  ? 0.2508 0.2003 0.3914 -0.0047 -0.0232 0.0236  425  ALA A O   
3113  C CB  . ALA A 427  ? 0.2759 0.2240 0.4122 -0.0011 -0.0243 0.0081  425  ALA A CB  
3114  N N   . GLN A 428  ? 0.2573 0.2069 0.3917 -0.0037 -0.0212 0.0272  426  GLN A N   
3115  C CA  . GLN A 428  ? 0.2842 0.2345 0.4244 -0.0053 -0.0218 0.0354  426  GLN A CA  
3116  C C   . GLN A 428  ? 0.2564 0.2101 0.3899 -0.0061 -0.0188 0.0395  426  GLN A C   
3117  O O   . GLN A 428  ? 0.2719 0.2265 0.4111 -0.0076 -0.0197 0.0436  426  GLN A O   
3118  C CB  . GLN A 428  ? 0.2675 0.2179 0.4080 -0.0052 -0.0217 0.0399  426  GLN A CB  
3119  C CG  . GLN A 428  ? 0.2944 0.2454 0.4439 -0.0070 -0.0235 0.0483  426  GLN A CG  
3120  C CD  . GLN A 428  ? 0.3463 0.3017 0.4909 -0.0082 -0.0207 0.0548  426  GLN A CD  
3121  O OE1 . GLN A 428  ? 0.3664 0.3246 0.4999 -0.0075 -0.0171 0.0547  426  GLN A OE1 
3122  N NE2 . GLN A 428  ? 0.3288 0.2850 0.4822 -0.0100 -0.0226 0.0606  426  GLN A NE2 
3123  N N   . THR A 429  ? 0.2600 0.2158 0.3817 -0.0052 -0.0153 0.0382  427  THR A N   
3124  C CA  . THR A 429  ? 0.2493 0.2084 0.3643 -0.0056 -0.0124 0.0409  427  THR A CA  
3125  C C   . THR A 429  ? 0.2267 0.1856 0.3444 -0.0061 -0.0133 0.0383  427  THR A C   
3126  O O   . THR A 429  ? 0.2624 0.2232 0.3823 -0.0073 -0.0130 0.0425  427  THR A O   
3127  C CB  . THR A 429  ? 0.2592 0.2198 0.3621 -0.0042 -0.0091 0.0383  427  THR A CB  
3128  O OG1 . THR A 429  ? 0.2823 0.2428 0.3830 -0.0036 -0.0086 0.0398  427  THR A OG1 
3129  C CG2 . THR A 429  ? 0.2653 0.2295 0.3620 -0.0045 -0.0063 0.0417  427  THR A CG2 
3130  N N   . LEU A 430  ? 0.2297 0.1867 0.3469 -0.0053 -0.0144 0.0312  428  LEU A N   
3131  C CA  . LEU A 430  ? 0.2464 0.2034 0.3658 -0.0057 -0.0154 0.0280  428  LEU A CA  
3132  C C   . LEU A 430  ? 0.2296 0.1856 0.3609 -0.0072 -0.0185 0.0311  428  LEU A C   
3133  O O   . LEU A 430  ? 0.2433 0.2007 0.3759 -0.0082 -0.0182 0.0335  428  LEU A O   
3134  C CB  . LEU A 430  ? 0.2409 0.1966 0.3596 -0.0045 -0.0167 0.0198  428  LEU A CB  
3135  C CG  . LEU A 430  ? 0.2679 0.2245 0.3857 -0.0045 -0.0173 0.0147  428  LEU A CG  
3136  C CD1 . LEU A 430  ? 0.3429 0.2996 0.4575 -0.0031 -0.0176 0.0074  428  LEU A CD1 
3137  C CD2 . LEU A 430  ? 0.3197 0.2751 0.4487 -0.0055 -0.0206 0.0144  428  LEU A CD2 
3138  N N   . ALA A 431  ? 0.2867 0.2399 0.4272 -0.0073 -0.0215 0.0311  429  ALA A N   
3139  C CA  . ALA A 431  ? 0.2679 0.2197 0.4210 -0.0087 -0.0250 0.0338  429  ALA A CA  
3140  C C   . ALA A 431  ? 0.2466 0.2010 0.4012 -0.0104 -0.0239 0.0427  429  ALA A C   
3141  O O   . ALA A 431  ? 0.2373 0.1923 0.3978 -0.0118 -0.0251 0.0449  429  ALA A O   
3142  C CB  . ALA A 431  ? 0.2593 0.2078 0.4221 -0.0085 -0.0285 0.0329  429  ALA A CB  
3143  N N   . ALA A 432  ? 0.2641 0.2206 0.4130 -0.0103 -0.0214 0.0476  430  ALA A N   
3144  C CA  . ALA A 432  ? 0.2770 0.2374 0.4264 -0.0118 -0.0200 0.0560  430  ALA A CA  
3145  C C   . ALA A 432  ? 0.2611 0.2244 0.4053 -0.0121 -0.0178 0.0561  430  ALA A C   
3146  O O   . ALA A 432  ? 0.2934 0.2588 0.4430 -0.0137 -0.0183 0.0611  430  ALA A O   
3147  C CB  . ALA A 432  ? 0.2758 0.2387 0.4181 -0.0113 -0.0174 0.0598  430  ALA A CB  
3148  N N   . ILE A 433  ? 0.2566 0.2201 0.3909 -0.0107 -0.0154 0.0508  431  ILE A N   
3149  C CA  . ILE A 433  ? 0.2613 0.2275 0.3904 -0.0108 -0.0133 0.0507  431  ILE A CA  
3150  C C   . ILE A 433  ? 0.2314 0.1959 0.3672 -0.0115 -0.0158 0.0477  431  ILE A C   
3151  O O   . ILE A 433  ? 0.2552 0.2221 0.3929 -0.0126 -0.0155 0.0506  431  ILE A O   
3152  C CB  . ILE A 433  ? 0.2509 0.2179 0.3678 -0.0091 -0.0103 0.0463  431  ILE A CB  
3153  C CG1 . ILE A 433  ? 0.2888 0.2581 0.3996 -0.0085 -0.0078 0.0500  431  ILE A CG1 
3154  C CG2 . ILE A 433  ? 0.2737 0.2428 0.3860 -0.0091 -0.0086 0.0452  431  ILE A CG2 
3155  C CD1 . ILE A 433  ? 0.3197 0.2895 0.4196 -0.0070 -0.0051 0.0462  431  ILE A CD1 
3156  N N   . TYR A 434  ? 0.2584 0.2194 0.3980 -0.0109 -0.0184 0.0416  432  TYR A N   
3157  C CA  . TYR A 434  ? 0.2654 0.2250 0.4120 -0.0115 -0.0211 0.0380  432  TYR A CA  
3158  C C   . TYR A 434  ? 0.2676 0.2273 0.4253 -0.0135 -0.0235 0.0438  432  TYR A C   
3159  O O   . TYR A 434  ? 0.2805 0.2414 0.4410 -0.0144 -0.0240 0.0442  432  TYR A O   
3160  C CB  . TYR A 434  ? 0.2596 0.2158 0.4101 -0.0105 -0.0239 0.0309  432  TYR A CB  
3161  C CG  . TYR A 434  ? 0.2993 0.2539 0.4592 -0.0110 -0.0276 0.0268  432  TYR A CG  
3162  C CD1 . TYR A 434  ? 0.3039 0.2600 0.4607 -0.0109 -0.0272 0.0231  432  TYR A CD1 
3163  C CD2 . TYR A 434  ? 0.3021 0.2536 0.4745 -0.0115 -0.0316 0.0267  432  TYR A CD2 
3164  C CE1 . TYR A 434  ? 0.3046 0.2596 0.4701 -0.0113 -0.0307 0.0191  432  TYR A CE1 
3165  C CE2 . TYR A 434  ? 0.3442 0.2943 0.5259 -0.0119 -0.0352 0.0225  432  TYR A CE2 
3166  C CZ  . TYR A 434  ? 0.3414 0.2933 0.5193 -0.0118 -0.0347 0.0186  432  TYR A CZ  
3167  O OH  . TYR A 434  ? 0.3790 0.3297 0.5662 -0.0121 -0.0384 0.0142  432  TYR A OH  
3168  N N   . HIS A 435  ? 0.2576 0.2166 0.4221 -0.0142 -0.0249 0.0486  433  HIS A N   
3169  C CA  . HIS A 435  ? 0.2988 0.2582 0.4745 -0.0163 -0.0273 0.0550  433  HIS A CA  
3170  C C   . HIS A 435  ? 0.3054 0.2700 0.4771 -0.0174 -0.0243 0.0625  433  HIS A C   
3171  O O   . HIS A 435  ? 0.2970 0.2633 0.4753 -0.0191 -0.0254 0.0663  433  HIS A O   
3172  C CB  . HIS A 435  ? 0.3394 0.2962 0.5249 -0.0169 -0.0304 0.0578  433  HIS A CB  
3173  C CG  . HIS A 435  ? 0.3433 0.2952 0.5366 -0.0161 -0.0344 0.0507  433  HIS A CG  
3174  N ND1 . HIS A 435  ? 0.3506 0.3004 0.5557 -0.0172 -0.0383 0.0493  433  HIS A ND1 
3175  C CD2 . HIS A 435  ? 0.3114 0.2607 0.5024 -0.0143 -0.0350 0.0441  433  HIS A CD2 
3176  C CE1 . HIS A 435  ? 0.3383 0.2844 0.5482 -0.0159 -0.0413 0.0419  433  HIS A CE1 
3177  N NE2 . HIS A 435  ? 0.3313 0.2772 0.5328 -0.0142 -0.0393 0.0387  433  HIS A NE2 
3178  N N   . MET A 436  ? 0.2843 0.2518 0.4455 -0.0165 -0.0206 0.0642  434  MET A N   
3179  C CA  . MET A 436  ? 0.2650 0.2382 0.4215 -0.0172 -0.0175 0.0702  434  MET A CA  
3180  C C   . MET A 436  ? 0.2694 0.2441 0.4231 -0.0172 -0.0164 0.0679  434  MET A C   
3181  O O   . MET A 436  ? 0.3021 0.2810 0.4581 -0.0184 -0.0156 0.0730  434  MET A O   
3182  C CB  . MET A 436  ? 0.2996 0.2754 0.4449 -0.0157 -0.0138 0.0707  434  MET A CB  
3183  C CG  . MET A 436  ? 0.3049 0.2873 0.4452 -0.0161 -0.0106 0.0763  434  MET A CG  
3184  S SD  . MET A 436  ? 0.3256 0.3108 0.4524 -0.0140 -0.0065 0.0752  434  MET A SD  
3185  C CE  . MET A 436  ? 0.3169 0.3013 0.4477 -0.0145 -0.0080 0.0791  434  MET A CE  
3186  N N   . ALA A 437  ? 0.2595 0.2316 0.4082 -0.0158 -0.0163 0.0603  435  ALA A N   
3187  C CA  . ALA A 437  ? 0.2803 0.2538 0.4256 -0.0157 -0.0152 0.0579  435  ALA A CA  
3188  C C   . ALA A 437  ? 0.3024 0.2750 0.4585 -0.0173 -0.0184 0.0585  435  ALA A C   
3189  O O   . ALA A 437  ? 0.3021 0.2772 0.4576 -0.0178 -0.0176 0.0595  435  ALA A O   
3190  C CB  . ALA A 437  ? 0.3070 0.2783 0.4442 -0.0139 -0.0145 0.0501  435  ALA A CB  
3191  N N   . GLY A 438  ? 0.3383 0.3073 0.5045 -0.0180 -0.0221 0.0579  436  GLY A N   
3192  C CA  . GLY A 438  ? 0.3726 0.3405 0.5503 -0.0197 -0.0256 0.0588  436  GLY A CA  
3193  C C   . GLY A 438  ? 0.3474 0.3129 0.5259 -0.0190 -0.0274 0.0508  436  GLY A C   
3194  O O   . GLY A 438  ? 0.3459 0.3106 0.5161 -0.0173 -0.0262 0.0445  436  GLY A O   
3195  N N   . LYS A 439  ? 0.4129 0.3777 0.6019 -0.0204 -0.0306 0.0515  437  LYS A N   
3196  C CA  . LYS A 439  ? 0.4212 0.3836 0.6138 -0.0200 -0.0333 0.0441  437  LYS A CA  
3197  C C   . LYS A 439  ? 0.3878 0.3530 0.5729 -0.0196 -0.0312 0.0415  437  LYS A C   
3198  O O   . LYS A 439  ? 0.4755 0.4395 0.6592 -0.0187 -0.0325 0.0343  437  LYS A O   
3199  C CB  . LYS A 439  ? 0.4689 0.4292 0.6769 -0.0218 -0.0380 0.0457  437  LYS A CB  
3200  N N   . ASP A 440  ? 0.3963 0.3652 0.5768 -0.0202 -0.0282 0.0471  438  ASP A N   
3201  C CA  . ASP A 440  ? 0.4074 0.3789 0.5809 -0.0198 -0.0263 0.0449  438  ASP A CA  
3202  C C   . ASP A 440  ? 0.4122 0.3840 0.5730 -0.0177 -0.0234 0.0405  438  ASP A C   
3203  O O   . ASP A 440  ? 0.4191 0.3924 0.5728 -0.0171 -0.0203 0.0436  438  ASP A O   
3204  C CB  . ASP A 440  ? 0.4305 0.4065 0.6035 -0.0209 -0.0240 0.0521  438  ASP A CB  
3205  C CG  . ASP A 440  ? 0.5151 0.4915 0.7002 -0.0230 -0.0268 0.0558  438  ASP A CG  
3206  O OD1 . ASP A 440  ? 0.4960 0.4690 0.6899 -0.0235 -0.0308 0.0522  438  ASP A OD1 
3207  O OD2 . ASP A 440  ? 0.5576 0.5381 0.7436 -0.0241 -0.0252 0.0620  438  ASP A OD2 
3208  N N   . PHE A 441  ? 0.3666 0.3373 0.5245 -0.0168 -0.0244 0.0334  439  PHE A N   
3209  C CA  . PHE A 441  ? 0.3609 0.3323 0.5071 -0.0151 -0.0218 0.0296  439  PHE A CA  
3210  C C   . PHE A 441  ? 0.3475 0.3205 0.4896 -0.0148 -0.0218 0.0253  439  PHE A C   
3211  O O   . PHE A 441  ? 0.3452 0.3179 0.4936 -0.0154 -0.0246 0.0222  439  PHE A O   
3212  C CB  . PHE A 441  ? 0.3168 0.2856 0.4618 -0.0140 -0.0228 0.0248  439  PHE A CB  
3213  C CG  . PHE A 441  ? 0.3419 0.3117 0.4751 -0.0124 -0.0201 0.0217  439  PHE A CG  
3214  C CD1 . PHE A 441  ? 0.2999 0.2703 0.4261 -0.0119 -0.0169 0.0254  439  PHE A CD1 
3215  C CD2 . PHE A 441  ? 0.3075 0.2781 0.4365 -0.0117 -0.0206 0.0154  439  PHE A CD2 
3216  C CE1 . PHE A 441  ? 0.2452 0.2165 0.3612 -0.0106 -0.0146 0.0229  439  PHE A CE1 
3217  C CE2 . PHE A 441  ? 0.2978 0.2697 0.4163 -0.0105 -0.0182 0.0133  439  PHE A CE2 
3218  C CZ  . PHE A 441  ? 0.2871 0.2589 0.3993 -0.0100 -0.0152 0.0171  439  PHE A CZ  
3219  N N   . HIS A 442  ? 0.2961 0.2711 0.4279 -0.0138 -0.0187 0.0253  440  HIS A N   
3220  C CA  . HIS A 442  ? 0.3033 0.2799 0.4295 -0.0133 -0.0185 0.0210  440  HIS A CA  
3221  C C   . HIS A 442  ? 0.3421 0.3192 0.4576 -0.0119 -0.0159 0.0194  440  HIS A C   
3222  O O   . HIS A 442  ? 0.2740 0.2509 0.3857 -0.0114 -0.0136 0.0229  440  HIS A O   
3223  C CB  . HIS A 442  ? 0.3307 0.3099 0.4572 -0.0140 -0.0177 0.0243  440  HIS A CB  
3224  C CG  . HIS A 442  ? 0.2541 0.2352 0.3757 -0.0137 -0.0144 0.0298  440  HIS A CG  
3225  N ND1 . HIS A 442  ? 0.3270 0.3088 0.4534 -0.0145 -0.0137 0.0356  440  HIS A ND1 
3226  C CD2 . HIS A 442  ? 0.2947 0.2774 0.4073 -0.0127 -0.0116 0.0301  440  HIS A CD2 
3227  C CE1 . HIS A 442  ? 0.3126 0.2969 0.4329 -0.0139 -0.0106 0.0390  440  HIS A CE1 
3228  N NE2 . HIS A 442  ? 0.2960 0.2806 0.4082 -0.0127 -0.0093 0.0356  440  HIS A NE2 
3229  N N   . VAL A 443  ? 0.3615 0.3396 0.4724 -0.0113 -0.0164 0.0142  441  VAL A N   
3230  C CA  . VAL A 443  ? 0.3661 0.3450 0.4671 -0.0102 -0.0141 0.0129  441  VAL A CA  
3231  C C   . VAL A 443  ? 0.3006 0.2810 0.3966 -0.0100 -0.0114 0.0175  441  VAL A C   
3232  O O   . VAL A 443  ? 0.3192 0.3013 0.4166 -0.0106 -0.0115 0.0190  441  VAL A O   
3233  C CB  . VAL A 443  ? 0.3826 0.3633 0.4800 -0.0098 -0.0153 0.0071  441  VAL A CB  
3234  C CG1 . VAL A 443  ? 0.3485 0.3305 0.4359 -0.0090 -0.0129 0.0071  441  VAL A CG1 
3235  C CG2 . VAL A 443  ? 0.4203 0.4000 0.5216 -0.0095 -0.0176 0.0021  441  VAL A CG2 
3236  N N   . GLY A 444  ? 0.2792 0.2592 0.3696 -0.0092 -0.0090 0.0195  442  GLY A N   
3237  C CA  . GLY A 444  ? 0.2541 0.2355 0.3406 -0.0088 -0.0065 0.0237  442  GLY A CA  
3238  C C   . GLY A 444  ? 0.2416 0.2230 0.3315 -0.0091 -0.0054 0.0286  442  GLY A C   
3239  O O   . GLY A 444  ? 0.2517 0.2348 0.3379 -0.0085 -0.0031 0.0317  442  GLY A O   
3240  N N   . LYS A 445  ? 0.2140 0.1940 0.3114 -0.0099 -0.0072 0.0295  443  LYS A N   
3241  C CA  . LYS A 445  ? 0.2051 0.1858 0.3058 -0.0103 -0.0062 0.0348  443  LYS A CA  
3242  C C   . LYS A 445  ? 0.2374 0.2173 0.3329 -0.0093 -0.0045 0.0354  443  LYS A C   
3243  O O   . LYS A 445  ? 0.2308 0.2129 0.3229 -0.0088 -0.0021 0.0389  443  LYS A O   
3244  C CB  . LYS A 445  ? 0.2348 0.2142 0.3458 -0.0117 -0.0089 0.0362  443  LYS A CB  
3245  C CG  . LYS A 445  ? 0.2858 0.2673 0.4009 -0.0125 -0.0079 0.0428  443  LYS A CG  
3246  C CD  . LYS A 445  ? 0.3624 0.3425 0.4883 -0.0141 -0.0108 0.0450  443  LYS A CD  
3247  C CE  . LYS A 445  ? 0.3925 0.3762 0.5228 -0.0153 -0.0098 0.0522  443  LYS A CE  
3248  N NZ  . LYS A 445  ? 0.4549 0.4373 0.5965 -0.0170 -0.0128 0.0552  443  LYS A NZ  
3249  N N   . TYR A 446  ? 0.2268 0.2041 0.3221 -0.0090 -0.0057 0.0317  444  TYR A N   
3250  C CA  . TYR A 446  ? 0.2344 0.2107 0.3243 -0.0079 -0.0043 0.0313  444  TYR A CA  
3251  C C   . TYR A 446  ? 0.2187 0.1928 0.3075 -0.0075 -0.0059 0.0255  444  TYR A C   
3252  O O   . TYR A 446  ? 0.2305 0.2041 0.3233 -0.0080 -0.0081 0.0222  444  TYR A O   
3253  C CB  . TYR A 446  ? 0.2232 0.1992 0.3171 -0.0083 -0.0042 0.0356  444  TYR A CB  
3254  C CG  . TYR A 446  ? 0.2573 0.2308 0.3602 -0.0092 -0.0072 0.0350  444  TYR A CG  
3255  C CD1 . TYR A 446  ? 0.3146 0.2885 0.4263 -0.0107 -0.0091 0.0377  444  TYR A CD1 
3256  C CD2 . TYR A 446  ? 0.2812 0.2521 0.3844 -0.0087 -0.0084 0.0317  444  TYR A CD2 
3257  C CE1 . TYR A 446  ? 0.3134 0.2847 0.4342 -0.0115 -0.0122 0.0370  444  TYR A CE1 
3258  C CE2 . TYR A 446  ? 0.3510 0.3195 0.4632 -0.0093 -0.0114 0.0307  444  TYR A CE2 
3259  C CZ  . TYR A 446  ? 0.3424 0.3110 0.4635 -0.0107 -0.0134 0.0334  444  TYR A CZ  
3260  O OH  . TYR A 446  ? 0.5226 0.4886 0.6535 -0.0114 -0.0168 0.0323  444  TYR A OH  
3261  N N   . GLU A 447  ? 0.2007 0.1738 0.2843 -0.0066 -0.0048 0.0242  445  GLU A N   
3262  C CA  . GLU A 447  ? 0.2001 0.1719 0.2831 -0.0061 -0.0062 0.0189  445  GLU A CA  
3263  C C   . GLU A 447  ? 0.2236 0.1938 0.3051 -0.0055 -0.0056 0.0195  445  GLU A C   
3264  O O   . GLU A 447  ? 0.2047 0.1753 0.2840 -0.0053 -0.0037 0.0236  445  GLU A O   
3265  C CB  . GLU A 447  ? 0.2068 0.1800 0.2826 -0.0056 -0.0055 0.0153  445  GLU A CB  
3266  C CG  . GLU A 447  ? 0.2269 0.2007 0.2945 -0.0048 -0.0028 0.0170  445  GLU A CG  
3267  C CD  . GLU A 447  ? 0.2234 0.1988 0.2846 -0.0045 -0.0022 0.0143  445  GLU A CD  
3268  O OE1 . GLU A 447  ? 0.2498 0.2265 0.3124 -0.0050 -0.0037 0.0118  445  GLU A OE1 
3269  O OE2 . GLU A 447  ? 0.2231 0.1986 0.2780 -0.0038 -0.0005 0.0149  445  GLU A OE2 
3270  N N   . PHE A 448  ? 0.1920 0.1609 0.2750 -0.0051 -0.0071 0.0151  446  PHE A N   
3271  C CA  . PHE A 448  ? 0.2104 0.1782 0.2905 -0.0043 -0.0064 0.0146  446  PHE A CA  
3272  C C   . PHE A 448  ? 0.1830 0.1520 0.2544 -0.0035 -0.0049 0.0115  446  PHE A C   
3273  O O   . PHE A 448  ? 0.2069 0.1777 0.2755 -0.0036 -0.0049 0.0092  446  PHE A O   
3274  C CB  . PHE A 448  ? 0.2276 0.1934 0.3149 -0.0042 -0.0090 0.0117  446  PHE A CB  
3275  C CG  . PHE A 448  ? 0.2284 0.1927 0.3249 -0.0051 -0.0107 0.0154  446  PHE A CG  
3276  C CD1 . PHE A 448  ? 0.2375 0.2011 0.3349 -0.0052 -0.0099 0.0204  446  PHE A CD1 
3277  C CD2 . PHE A 448  ? 0.2586 0.2224 0.3630 -0.0059 -0.0133 0.0142  446  PHE A CD2 
3278  C CE1 . PHE A 448  ? 0.2490 0.2117 0.3553 -0.0063 -0.0116 0.0247  446  PHE A CE1 
3279  C CE2 . PHE A 448  ? 0.2812 0.2436 0.3949 -0.0070 -0.0151 0.0182  446  PHE A CE2 
3280  C CZ  . PHE A 448  ? 0.2701 0.2321 0.3848 -0.0072 -0.0143 0.0236  446  PHE A CZ  
3281  N N   . GLN A 449  ? 0.1867 0.1551 0.2541 -0.0027 -0.0036 0.0117  447  GLN A N   
3282  C CA  . GLN A 449  ? 0.1978 0.1672 0.2577 -0.0021 -0.0025 0.0088  447  GLN A CA  
3283  C C   . GLN A 449  ? 0.2187 0.1871 0.2786 -0.0014 -0.0028 0.0066  447  GLN A C   
3284  O O   . GLN A 449  ? 0.2219 0.1885 0.2856 -0.0013 -0.0032 0.0087  447  GLN A O   
3285  C CB  . GLN A 449  ? 0.2036 0.1739 0.2566 -0.0018 0.0000  0.0118  447  GLN A CB  
3286  C CG  . GLN A 449  ? 0.1997 0.1714 0.2526 -0.0023 0.0004  0.0138  447  GLN A CG  
3287  C CD  . GLN A 449  ? 0.2499 0.2227 0.2958 -0.0018 0.0024  0.0151  447  GLN A CD  
3288  O OE1 . GLN A 449  ? 0.2537 0.2261 0.2952 -0.0011 0.0037  0.0152  447  GLN A OE1 
3289  N NE2 . GLN A 449  ? 0.2114 0.1855 0.2568 -0.0021 0.0026  0.0160  447  GLN A NE2 
3290  N N   . CYS A 450  ? 0.2119 0.1818 0.2675 -0.0010 -0.0027 0.0026  448  CYS A N   
3291  C CA  . CYS A 450  ? 0.2112 0.1807 0.2662 -0.0003 -0.0029 0.0001  448  CYS A CA  
3292  C C   . CYS A 450  ? 0.2311 0.2029 0.2784 -0.0001 -0.0015 -0.0019 448  CYS A C   
3293  O O   . CYS A 450  ? 0.2286 0.2023 0.2719 -0.0005 -0.0009 -0.0017 448  CYS A O   
3294  C CB  . CYS A 450  ? 0.2276 0.1969 0.2895 -0.0002 -0.0055 -0.0043 448  CYS A CB  
3295  S SG  . CYS A 450  ? 0.2624 0.2358 0.3230 -0.0003 -0.0066 -0.0104 448  CYS A SG  
3296  N N   . LEU A 451  ? 0.2079 0.1795 0.2536 0.0006  -0.0012 -0.0035 449  LEU A N   
3297  C CA  . LEU A 451  ? 0.2512 0.2251 0.2901 0.0007  -0.0001 -0.0052 449  LEU A CA  
3298  C C   . LEU A 451  ? 0.2294 0.2067 0.2691 0.0008  -0.0014 -0.0106 449  LEU A C   
3299  O O   . LEU A 451  ? 0.2646 0.2417 0.3100 0.0012  -0.0031 -0.0139 449  LEU A O   
3300  C CB  . LEU A 451  ? 0.2568 0.2293 0.2934 0.0014  0.0010  -0.0041 449  LEU A CB  
3301  C CG  . LEU A 451  ? 0.3293 0.3039 0.3594 0.0015  0.0022  -0.0052 449  LEU A CG  
3302  C CD1 . LEU A 451  ? 0.3163 0.2919 0.3410 0.0010  0.0035  -0.0028 449  LEU A CD1 
3303  C CD2 . LEU A 451  ? 0.3106 0.2833 0.3396 0.0022  0.0030  -0.0041 449  LEU A CD2 
3304  N N   . HIS A 452  ? 0.2304 0.2112 0.2649 0.0003  -0.0008 -0.0117 450  HIS A N   
3305  C CA  . HIS A 452  ? 0.2445 0.2300 0.2787 0.0003  -0.0018 -0.0167 450  HIS A CA  
3306  C C   . HIS A 452  ? 0.2663 0.2523 0.3012 0.0011  -0.0020 -0.0197 450  HIS A C   
3307  O O   . HIS A 452  ? 0.2938 0.2779 0.3259 0.0014  -0.0007 -0.0175 450  HIS A O   
3308  C CB  . HIS A 452  ? 0.2431 0.2325 0.2707 -0.0005 -0.0008 -0.0160 450  HIS A CB  
3309  C CG  . HIS A 452  ? 0.2361 0.2315 0.2622 -0.0006 -0.0014 -0.0206 450  HIS A CG  
3310  N ND1 . HIS A 452  ? 0.2631 0.2627 0.2913 -0.0009 -0.0029 -0.0244 450  HIS A ND1 
3311  C CD2 . HIS A 452  ? 0.2976 0.2959 0.3204 -0.0004 -0.0007 -0.0222 450  HIS A CD2 
3312  C CE1 . HIS A 452  ? 0.2761 0.2815 0.3021 -0.0008 -0.0031 -0.0281 450  HIS A CE1 
3313  N NE2 . HIS A 452  ? 0.2778 0.2826 0.3006 -0.0006 -0.0017 -0.0268 450  HIS A NE2 
3314  N N   . GLY A 453  ? 0.3207 0.3097 0.3596 0.0016  -0.0036 -0.0250 451  GLY A N   
3315  C CA  . GLY A 453  ? 0.3228 0.3131 0.3626 0.0025  -0.0039 -0.0284 451  GLY A CA  
3316  C C   . GLY A 453  ? 0.4084 0.3933 0.4526 0.0032  -0.0042 -0.0268 451  GLY A C   
3317  O O   . GLY A 453  ? 0.4330 0.4182 0.4768 0.0040  -0.0039 -0.0281 451  GLY A O   
3318  N N   . MET A 454  ? 0.3103 0.2909 0.3589 0.0030  -0.0048 -0.0237 452  MET A N   
3319  C CA  . MET A 454  ? 0.2817 0.2577 0.3352 0.0036  -0.0054 -0.0214 452  MET A CA  
3320  C C   . MET A 454  ? 0.3040 0.2774 0.3655 0.0033  -0.0073 -0.0207 452  MET A C   
3321  O O   . MET A 454  ? 0.3262 0.2977 0.3953 0.0039  -0.0094 -0.0224 452  MET A O   
3322  C CB  . MET A 454  ? 0.3026 0.2760 0.3511 0.0033  -0.0032 -0.0156 452  MET A CB  
3323  C CG  . MET A 454  ? 0.3377 0.3071 0.3911 0.0037  -0.0037 -0.0125 452  MET A CG  
3324  S SD  . MET A 454  ? 0.4646 0.4337 0.5223 0.0048  -0.0051 -0.0164 452  MET A SD  
3325  C CE  . MET A 454  ? 0.4248 0.3959 0.4732 0.0051  -0.0026 -0.0160 452  MET A CE  
3326  N N   . GLY A 455  ? 0.2900 0.2633 0.3505 0.0024  -0.0070 -0.0181 453  GLY A N   
3327  C CA  . GLY A 455  ? 0.2752 0.2459 0.3431 0.0020  -0.0087 -0.0165 453  GLY A CA  
3328  C C   . GLY A 455  ? 0.3062 0.2787 0.3797 0.0020  -0.0111 -0.0214 453  GLY A C   
3329  O O   . GLY A 455  ? 0.3050 0.2753 0.3862 0.0016  -0.0130 -0.0204 453  GLY A O   
3330  N N   . GLU A 456  ? 0.3152 0.2924 0.3854 0.0022  -0.0112 -0.0264 454  GLU A N   
3331  C CA  . GLU A 456  ? 0.3381 0.3178 0.4131 0.0022  -0.0135 -0.0314 454  GLU A CA  
3332  C C   . GLU A 456  ? 0.3455 0.3234 0.4310 0.0030  -0.0166 -0.0352 454  GLU A C   
3333  O O   . GLU A 456  ? 0.3463 0.3236 0.4385 0.0027  -0.0188 -0.0365 454  GLU A O   
3334  C CB  . GLU A 456  ? 0.3548 0.3411 0.4242 0.0024  -0.0130 -0.0362 454  GLU A CB  
3335  C CG  . GLU A 456  ? 0.4238 0.4122 0.4844 0.0014  -0.0107 -0.0327 454  GLU A CG  
3336  C CD  . GLU A 456  ? 0.4090 0.3979 0.4623 0.0015  -0.0084 -0.0305 454  GLU A CD  
3337  O OE1 . GLU A 456  ? 0.3737 0.3598 0.4286 0.0022  -0.0082 -0.0300 454  GLU A OE1 
3338  O OE2 . GLU A 456  ? 0.4132 0.4052 0.4595 0.0008  -0.0069 -0.0291 454  GLU A OE2 
3339  N N   . PRO A 457  ? 0.3038 0.2808 0.3917 0.0041  -0.0171 -0.0373 455  PRO A N   
3340  C CA  . PRO A 457  ? 0.3245 0.2993 0.4235 0.0049  -0.0204 -0.0408 455  PRO A CA  
3341  C C   . PRO A 457  ? 0.3470 0.3166 0.4535 0.0040  -0.0219 -0.0357 455  PRO A C   
3342  O O   . PRO A 457  ? 0.3406 0.3093 0.4563 0.0041  -0.0249 -0.0385 455  PRO A O   
3343  C CB  . PRO A 457  ? 0.3519 0.3261 0.4510 0.0060  -0.0202 -0.0421 455  PRO A CB  
3344  C CG  . PRO A 457  ? 0.3611 0.3395 0.4494 0.0060  -0.0172 -0.0424 455  PRO A CG  
3345  C CD  . PRO A 457  ? 0.3426 0.3208 0.4240 0.0047  -0.0150 -0.0370 455  PRO A CD  
3346  N N   . LEU A 458  ? 0.3221 0.2887 0.4252 0.0032  -0.0198 -0.0283 456  LEU A N   
3347  C CA  . LEU A 458  ? 0.2933 0.2560 0.4032 0.0022  -0.0210 -0.0229 456  LEU A CA  
3348  C C   . LEU A 458  ? 0.2840 0.2478 0.3945 0.0012  -0.0214 -0.0225 456  LEU A C   
3349  O O   . LEU A 458  ? 0.2572 0.2192 0.3769 0.0007  -0.0241 -0.0226 456  LEU A O   
3350  C CB  . LEU A 458  ? 0.2837 0.2443 0.3888 0.0016  -0.0185 -0.0154 456  LEU A CB  
3351  C CG  . LEU A 458  ? 0.2974 0.2553 0.4075 0.0004  -0.0189 -0.0087 456  LEU A CG  
3352  C CD1 . LEU A 458  ? 0.2920 0.2469 0.4148 0.0003  -0.0226 -0.0089 456  LEU A CD1 
3353  C CD2 . LEU A 458  ? 0.2985 0.2557 0.4025 0.0001  -0.0161 -0.0021 456  LEU A CD2 
3354  N N   . TYR A 459  ? 0.2864 0.2531 0.3876 0.0008  -0.0189 -0.0219 457  TYR A N   
3355  C CA  . TYR A 459  ? 0.2780 0.2456 0.3794 -0.0002 -0.0190 -0.0204 457  TYR A CA  
3356  C C   . TYR A 459  ? 0.2738 0.2443 0.3792 0.0000  -0.0214 -0.0271 457  TYR A C   
3357  O O   . TYR A 459  ? 0.3008 0.2713 0.4093 -0.0008 -0.0224 -0.0263 457  TYR A O   
3358  C CB  . TYR A 459  ? 0.2493 0.2185 0.3404 -0.0007 -0.0157 -0.0165 457  TYR A CB  
3359  C CG  . TYR A 459  ? 0.2372 0.2035 0.3275 -0.0012 -0.0140 -0.0094 457  TYR A CG  
3360  C CD1 . TYR A 459  ? 0.2698 0.2344 0.3649 -0.0022 -0.0145 -0.0048 457  TYR A CD1 
3361  C CD2 . TYR A 459  ? 0.2544 0.2199 0.3394 -0.0006 -0.0120 -0.0073 457  TYR A CD2 
3362  C CE1 . TYR A 459  ? 0.2436 0.2067 0.3380 -0.0026 -0.0130 0.0016  457  TYR A CE1 
3363  C CE2 . TYR A 459  ? 0.2521 0.2158 0.3364 -0.0010 -0.0106 -0.0010 457  TYR A CE2 
3364  C CZ  . TYR A 459  ? 0.2484 0.2110 0.3373 -0.0020 -0.0110 0.0034  457  TYR A CZ  
3365  O OH  . TYR A 459  ? 0.2540 0.2160 0.3422 -0.0024 -0.0096 0.0096  457  TYR A OH  
3366  N N   . GLU A 460  ? 0.2969 0.2700 0.4027 0.0012  -0.0225 -0.0337 458  GLU A N   
3367  C CA  . GLU A 460  ? 0.3438 0.3196 0.4557 0.0016  -0.0255 -0.0406 458  GLU A CA  
3368  C C   . GLU A 460  ? 0.3534 0.3251 0.4782 0.0016  -0.0290 -0.0410 458  GLU A C   
3369  O O   . GLU A 460  ? 0.3686 0.3418 0.4998 0.0017  -0.0318 -0.0459 458  GLU A O   
3370  C CB  . GLU A 460  ? 0.3971 0.3778 0.5063 0.0030  -0.0257 -0.0479 458  GLU A CB  
3371  C CG  . GLU A 460  ? 0.4457 0.4319 0.5436 0.0027  -0.0231 -0.0485 458  GLU A CG  
3372  C CD  . GLU A 460  ? 0.5994 0.5918 0.6950 0.0039  -0.0233 -0.0558 458  GLU A CD  
3373  O OE1 . GLU A 460  ? 0.6271 0.6191 0.7296 0.0052  -0.0255 -0.0606 458  GLU A OE1 
3374  O OE2 . GLU A 460  ? 0.6553 0.6532 0.7423 0.0036  -0.0215 -0.0565 458  GLU A OE2 
3375  N N   . GLU A 461  ? 0.3156 0.2825 0.4446 0.0013  -0.0292 -0.0358 459  GLU A N   
3376  C CA  . GLU A 461  ? 0.3604 0.3231 0.5019 0.0008  -0.0325 -0.0342 459  GLU A CA  
3377  C C   . GLU A 461  ? 0.3481 0.3088 0.4905 -0.0009 -0.0318 -0.0269 459  GLU A C   
3378  O O   . GLU A 461  ? 0.3548 0.3121 0.5073 -0.0017 -0.0343 -0.0240 459  GLU A O   
3379  C CB  . GLU A 461  ? 0.3131 0.2721 0.4597 0.0014  -0.0333 -0.0322 459  GLU A CB  
3380  C CG  . GLU A 461  ? 0.3597 0.3208 0.5051 0.0031  -0.0337 -0.0388 459  GLU A CG  
3381  C CD  . GLU A 461  ? 0.4100 0.3733 0.5632 0.0043  -0.0372 -0.0479 459  GLU A CD  
3382  O OE1 . GLU A 461  ? 0.4264 0.3880 0.5890 0.0037  -0.0403 -0.0486 459  GLU A OE1 
3383  O OE2 . GLU A 461  ? 0.4549 0.4220 0.6049 0.0058  -0.0370 -0.0544 459  GLU A OE2 
3384  N N   . VAL A 462  ? 0.3043 0.2673 0.4367 -0.0015 -0.0286 -0.0239 460  VAL A N   
3385  C CA  . VAL A 462  ? 0.2983 0.2601 0.4302 -0.0030 -0.0274 -0.0170 460  VAL A CA  
3386  C C   . VAL A 462  ? 0.3048 0.2697 0.4341 -0.0035 -0.0273 -0.0190 460  VAL A C   
3387  O O   . VAL A 462  ? 0.3266 0.2905 0.4623 -0.0045 -0.0290 -0.0173 460  VAL A O   
3388  C CB  . VAL A 462  ? 0.3030 0.2645 0.4259 -0.0032 -0.0236 -0.0106 460  VAL A CB  
3389  C CG1 . VAL A 462  ? 0.2887 0.2501 0.4109 -0.0046 -0.0223 -0.0041 460  VAL A CG1 
3390  C CG2 . VAL A 462  ? 0.2991 0.2578 0.4252 -0.0028 -0.0239 -0.0081 460  VAL A CG2 
3391  N N   . VAL A 463  ? 0.2956 0.2643 0.4156 -0.0029 -0.0255 -0.0225 461  VAL A N   
3392  C CA  . VAL A 463  ? 0.3117 0.2836 0.4278 -0.0035 -0.0251 -0.0236 461  VAL A CA  
3393  C C   . VAL A 463  ? 0.3750 0.3487 0.4989 -0.0033 -0.0286 -0.0301 461  VAL A C   
3394  O O   . VAL A 463  ? 0.4005 0.3750 0.5283 -0.0022 -0.0306 -0.0362 461  VAL A O   
3395  C CB  . VAL A 463  ? 0.3135 0.2894 0.4180 -0.0030 -0.0223 -0.0251 461  VAL A CB  
3396  C CG1 . VAL A 463  ? 0.3306 0.3103 0.4315 -0.0036 -0.0222 -0.0264 461  VAL A CG1 
3397  C CG2 . VAL A 463  ? 0.3216 0.2956 0.4191 -0.0031 -0.0190 -0.0188 461  VAL A CG2 
3398  N N   . GLY A 464  ? 0.3688 0.3431 0.4950 -0.0042 -0.0295 -0.0291 462  GLY A N   
3399  C CA  . GLY A 464  ? 0.4259 0.4027 0.5583 -0.0040 -0.0327 -0.0356 462  GLY A CA  
3400  C C   . GLY A 464  ? 0.4104 0.3834 0.5557 -0.0047 -0.0361 -0.0347 462  GLY A C   
3401  O O   . GLY A 464  ? 0.3790 0.3477 0.5302 -0.0050 -0.0367 -0.0308 462  GLY A O   
3402  N N   . ARG A 465  ? 0.3885 0.3634 0.5386 -0.0051 -0.0386 -0.0383 463  ARG A N   
3403  C CA  . ARG A 465  ? 0.3857 0.3573 0.5487 -0.0059 -0.0421 -0.0375 463  ARG A CA  
3404  C C   . ARG A 465  ? 0.4288 0.3975 0.6022 -0.0050 -0.0454 -0.0414 463  ARG A C   
3405  O O   . ARG A 465  ? 0.4709 0.4353 0.6549 -0.0058 -0.0478 -0.0380 463  ARG A O   
3406  C CB  . ARG A 465  ? 0.4368 0.4116 0.6027 -0.0063 -0.0443 -0.0417 463  ARG A CB  
3407  N N   . GLY A 466  ? 0.3796 0.3508 0.5504 -0.0033 -0.0457 -0.0482 464  GLY A N   
3408  C CA  . GLY A 466  ? 0.3821 0.3508 0.5629 -0.0023 -0.0488 -0.0522 464  GLY A CA  
3409  C C   . GLY A 466  ? 0.4307 0.3950 0.6116 -0.0023 -0.0474 -0.0464 464  GLY A C   
3410  O O   . GLY A 466  ? 0.4263 0.3878 0.6162 -0.0015 -0.0502 -0.0487 464  GLY A O   
3411  N N   . LYS A 467  ? 0.4097 0.3735 0.5809 -0.0032 -0.0434 -0.0390 465  LYS A N   
3412  C CA  . LYS A 467  ? 0.3555 0.3159 0.5257 -0.0032 -0.0417 -0.0333 465  LYS A CA  
3413  C C   . LYS A 467  ? 0.4029 0.3605 0.5753 -0.0051 -0.0408 -0.0239 465  LYS A C   
3414  O O   . LYS A 467  ? 0.4049 0.3603 0.5879 -0.0061 -0.0438 -0.0224 465  LYS A O   
3415  C CB  . LYS A 467  ? 0.3644 0.3274 0.5219 -0.0022 -0.0380 -0.0340 465  LYS A CB  
3416  C CG  . LYS A 467  ? 0.3892 0.3559 0.5453 -0.0005 -0.0390 -0.0432 465  LYS A CG  
3417  C CD  . LYS A 467  ? 0.4125 0.3764 0.5787 0.0006  -0.0422 -0.0467 465  LYS A CD  
3418  C CE  . LYS A 467  ? 0.4434 0.4118 0.6069 0.0026  -0.0425 -0.0555 465  LYS A CE  
3419  N NZ  . LYS A 467  ? 0.4416 0.4072 0.6144 0.0038  -0.0452 -0.0587 465  LYS A NZ  
3420  N N   . LEU A 468  ? 0.3769 0.3347 0.5399 -0.0055 -0.0369 -0.0176 466  LEU A N   
3421  C CA  . LEU A 468  ? 0.3547 0.3111 0.5187 -0.0072 -0.0357 -0.0089 466  LEU A CA  
3422  C C   . LEU A 468  ? 0.3498 0.3090 0.5077 -0.0079 -0.0337 -0.0073 466  LEU A C   
3423  O O   . LEU A 468  ? 0.3316 0.2903 0.4909 -0.0093 -0.0329 -0.0007 466  LEU A O   
3424  C CB  . LEU A 468  ? 0.3498 0.3053 0.5077 -0.0071 -0.0326 -0.0029 466  LEU A CB  
3425  C CG  . LEU A 468  ? 0.3673 0.3200 0.5305 -0.0064 -0.0342 -0.0037 466  LEU A CG  
3426  C CD1 . LEU A 468  ? 0.3558 0.3081 0.5132 -0.0065 -0.0313 0.0030  466  LEU A CD1 
3427  C CD2 . LEU A 468  ? 0.4199 0.3695 0.5983 -0.0071 -0.0388 -0.0033 466  LEU A CD2 
3428  N N   . ASP A 469  ? 0.3595 0.3219 0.5110 -0.0071 -0.0331 -0.0132 467  ASP A N   
3429  C CA  . ASP A 469  ? 0.3385 0.3037 0.4843 -0.0078 -0.0316 -0.0123 467  ASP A CA  
3430  C C   . ASP A 469  ? 0.3200 0.2856 0.4575 -0.0083 -0.0277 -0.0052 467  ASP A C   
3431  O O   . ASP A 469  ? 0.2816 0.2478 0.4195 -0.0094 -0.0270 -0.0008 467  ASP A O   
3432  C CB  . ASP A 469  ? 0.3578 0.3226 0.5131 -0.0089 -0.0346 -0.0124 467  ASP A CB  
3433  C CG  . ASP A 469  ? 0.4087 0.3773 0.5589 -0.0091 -0.0339 -0.0146 467  ASP A CG  
3434  O OD1 . ASP A 469  ? 0.4193 0.3910 0.5599 -0.0083 -0.0320 -0.0178 467  ASP A OD1 
3435  O OD2 . ASP A 469  ? 0.5018 0.4703 0.6577 -0.0103 -0.0354 -0.0127 467  ASP A OD2 
3436  N N   . ARG A 470  ? 0.3143 0.2798 0.4446 -0.0074 -0.0252 -0.0042 468  ARG A N   
3437  C CA  . ARG A 470  ? 0.2713 0.2376 0.3928 -0.0076 -0.0215 0.0012  468  ARG A CA  
3438  C C   . ARG A 470  ? 0.2876 0.2562 0.3983 -0.0065 -0.0193 -0.0021 468  ARG A C   
3439  O O   . ARG A 470  ? 0.2926 0.2614 0.4024 -0.0056 -0.0200 -0.0068 468  ARG A O   
3440  C CB  . ARG A 470  ? 0.2687 0.2327 0.3918 -0.0077 -0.0206 0.0068  468  ARG A CB  
3441  C CG  . ARG A 470  ? 0.2510 0.2132 0.3846 -0.0091 -0.0226 0.0116  468  ARG A CG  
3442  C CD  . ARG A 470  ? 0.2897 0.2538 0.4233 -0.0102 -0.0216 0.0159  468  ARG A CD  
3443  N NE  . ARG A 470  ? 0.2811 0.2440 0.4253 -0.0117 -0.0236 0.0207  468  ARG A NE  
3444  C CZ  . ARG A 470  ? 0.2878 0.2499 0.4415 -0.0125 -0.0269 0.0189  468  ARG A CZ  
3445  N NH1 . ARG A 470  ? 0.3046 0.2672 0.4584 -0.0120 -0.0285 0.0123  468  ARG A NH1 
3446  N NH2 . ARG A 470  ? 0.3174 0.2785 0.4810 -0.0140 -0.0288 0.0241  468  ARG A NH2 
3447  N N   . PRO A 471  ? 0.2636 0.2342 0.3666 -0.0067 -0.0168 0.0002  469  PRO A N   
3448  C CA  . PRO A 471  ? 0.2272 0.2002 0.3207 -0.0059 -0.0150 -0.0026 469  PRO A CA  
3449  C C   . PRO A 471  ? 0.2583 0.2302 0.3463 -0.0052 -0.0128 -0.0005 469  PRO A C   
3450  O O   . PRO A 471  ? 0.2414 0.2113 0.3308 -0.0053 -0.0118 0.0042  469  PRO A O   
3451  C CB  . PRO A 471  ? 0.2640 0.2389 0.3528 -0.0064 -0.0135 0.0002  469  PRO A CB  
3452  C CG  . PRO A 471  ? 0.2652 0.2385 0.3583 -0.0071 -0.0129 0.0061  469  PRO A CG  
3453  C CD  . PRO A 471  ? 0.2670 0.2381 0.3704 -0.0076 -0.0158 0.0054  469  PRO A CD  
3454  N N   . CYS A 472  ? 0.2368 0.2105 0.3184 -0.0045 -0.0120 -0.0041 470  CYS A N   
3455  C CA  . CYS A 472  ? 0.2452 0.2182 0.3209 -0.0038 -0.0099 -0.0027 470  CYS A CA  
3456  C C   . CYS A 472  ? 0.2471 0.2229 0.3139 -0.0036 -0.0082 -0.0037 470  CYS A C   
3457  O O   . CYS A 472  ? 0.2707 0.2495 0.3361 -0.0036 -0.0091 -0.0078 470  CYS A O   
3458  C CB  . CYS A 472  ? 0.2481 0.2203 0.3267 -0.0030 -0.0112 -0.0065 470  CYS A CB  
3459  S SG  . CYS A 472  ? 0.2765 0.2476 0.3485 -0.0022 -0.0087 -0.0045 470  CYS A SG  
3460  N N   . ARG A 473  ? 0.2190 0.1942 0.2802 -0.0034 -0.0058 0.0003  471  ARG A N   
3461  C CA  . ARG A 473  ? 0.2075 0.1849 0.2608 -0.0032 -0.0042 0.0000  471  ARG A CA  
3462  C C   . ARG A 473  ? 0.2313 0.2083 0.2808 -0.0025 -0.0033 -0.0013 471  ARG A C   
3463  O O   . ARG A 473  ? 0.2105 0.1851 0.2605 -0.0021 -0.0025 0.0010  471  ARG A O   
3464  C CB  . ARG A 473  ? 0.2312 0.2082 0.2811 -0.0033 -0.0024 0.0046  471  ARG A CB  
3465  C CG  . ARG A 473  ? 0.2255 0.2044 0.2682 -0.0033 -0.0013 0.0045  471  ARG A CG  
3466  C CD  . ARG A 473  ? 0.2141 0.1927 0.2548 -0.0032 0.0002  0.0085  471  ARG A CD  
3467  N NE  . ARG A 473  ? 0.2191 0.1979 0.2644 -0.0038 -0.0007 0.0098  471  ARG A NE  
3468  C CZ  . ARG A 473  ? 0.2657 0.2466 0.3115 -0.0044 -0.0017 0.0086  471  ARG A CZ  
3469  N NH1 . ARG A 473  ? 0.2467 0.2299 0.2882 -0.0046 -0.0020 0.0066  471  ARG A NH1 
3470  N NH2 . ARG A 473  ? 0.2540 0.2349 0.3047 -0.0049 -0.0026 0.0097  471  ARG A NH2 
3471  N N   . ILE A 474  ? 0.2323 0.2123 0.2780 -0.0025 -0.0035 -0.0048 472  ILE A N   
3472  C CA  . ILE A 474  ? 0.2079 0.1884 0.2503 -0.0019 -0.0029 -0.0066 472  ILE A CA  
3473  C C   . ILE A 474  ? 0.2318 0.2125 0.2671 -0.0019 -0.0009 -0.0037 472  ILE A C   
3474  O O   . ILE A 474  ? 0.2221 0.2052 0.2539 -0.0025 -0.0006 -0.0033 472  ILE A O   
3475  C CB  . ILE A 474  ? 0.2110 0.1956 0.2533 -0.0019 -0.0042 -0.0121 472  ILE A CB  
3476  C CG1 . ILE A 474  ? 0.2495 0.2336 0.2995 -0.0017 -0.0066 -0.0156 472  ILE A CG1 
3477  C CG2 . ILE A 474  ? 0.2296 0.2153 0.2679 -0.0014 -0.0034 -0.0137 472  ILE A CG2 
3478  C CD1 . ILE A 474  ? 0.2699 0.2590 0.3204 -0.0016 -0.0081 -0.0217 472  ILE A CD1 
3479  N N   . TYR A 475  ? 0.2399 0.2181 0.2737 -0.0013 0.0004  -0.0016 473  TYR A N   
3480  C CA  . TYR A 475  ? 0.2432 0.2215 0.2708 -0.0012 0.0021  0.0006  473  TYR A CA  
3481  C C   . TYR A 475  ? 0.2272 0.2084 0.2513 -0.0013 0.0020  -0.0023 473  TYR A C   
3482  O O   . TYR A 475  ? 0.2335 0.2147 0.2586 -0.0008 0.0017  -0.0047 473  TYR A O   
3483  C CB  . TYR A 475  ? 0.2511 0.2264 0.2787 -0.0005 0.0033  0.0035  473  TYR A CB  
3484  C CG  . TYR A 475  ? 0.2377 0.2126 0.2598 -0.0002 0.0049  0.0059  473  TYR A CG  
3485  C CD1 . TYR A 475  ? 0.3016 0.2771 0.3199 0.0000  0.0055  0.0048  473  TYR A CD1 
3486  C CD2 . TYR A 475  ? 0.2430 0.2173 0.2644 -0.0001 0.0057  0.0090  473  TYR A CD2 
3487  C CE1 . TYR A 475  ? 0.2804 0.2554 0.2945 0.0003  0.0066  0.0069  473  TYR A CE1 
3488  C CE2 . TYR A 475  ? 0.2501 0.2241 0.2673 0.0004  0.0069  0.0107  473  TYR A CE2 
3489  C CZ  . TYR A 475  ? 0.3065 0.2807 0.3202 0.0005  0.0073  0.0096  473  TYR A CZ  
3490  O OH  . TYR A 475  ? 0.3360 0.3097 0.3462 0.0010  0.0081  0.0111  473  TYR A OH  
3491  N N   . ALA A 476  ? 0.2227 0.2066 0.2427 -0.0020 0.0022  -0.0020 474  ALA A N   
3492  C CA  . ALA A 476  ? 0.2372 0.2255 0.2544 -0.0024 0.0018  -0.0048 474  ALA A CA  
3493  C C   . ALA A 476  ? 0.2248 0.2135 0.2367 -0.0027 0.0029  -0.0026 474  ALA A C   
3494  O O   . ALA A 476  ? 0.2301 0.2197 0.2396 -0.0033 0.0030  -0.0003 474  ALA A O   
3495  C CB  . ALA A 476  ? 0.2286 0.2209 0.2462 -0.0033 0.0006  -0.0062 474  ALA A CB  
3496  N N   . PRO A 477  ? 0.2474 0.2356 0.2579 -0.0022 0.0036  -0.0033 475  PRO A N   
3497  C CA  . PRO A 477  ? 0.2545 0.2433 0.2604 -0.0025 0.0044  -0.0013 475  PRO A CA  
3498  C C   . PRO A 477  ? 0.2252 0.2196 0.2285 -0.0037 0.0038  -0.0024 475  PRO A C   
3499  O O   . PRO A 477  ? 0.2312 0.2298 0.2356 -0.0039 0.0030  -0.0058 475  PRO A O   
3500  C CB  . PRO A 477  ? 0.2858 0.2732 0.2915 -0.0017 0.0051  -0.0025 475  PRO A CB  
3501  C CG  . PRO A 477  ? 0.3199 0.3048 0.3304 -0.0009 0.0046  -0.0040 475  PRO A CG  
3502  C CD  . PRO A 477  ? 0.2772 0.2641 0.2905 -0.0013 0.0034  -0.0058 475  PRO A CD  
3503  N N   . VAL A 478  ? 0.2183 0.2134 0.2186 -0.0044 0.0040  0.0006  476  VAL A N   
3504  C CA  . VAL A 478  ? 0.2310 0.2318 0.2288 -0.0058 0.0034  0.0008  476  VAL A CA  
3505  C C   . VAL A 478  ? 0.2756 0.2764 0.2704 -0.0063 0.0039  0.0033  476  VAL A C   
3506  O O   . VAL A 478  ? 0.3196 0.3162 0.3141 -0.0060 0.0042  0.0062  476  VAL A O   
3507  C CB  . VAL A 478  ? 0.2614 0.2631 0.2596 -0.0066 0.0025  0.0028  476  VAL A CB  
3508  C CG1 . VAL A 478  ? 0.2658 0.2740 0.2616 -0.0082 0.0017  0.0036  476  VAL A CG1 
3509  C CG2 . VAL A 478  ? 0.2635 0.2648 0.2652 -0.0061 0.0019  0.0005  476  VAL A CG2 
3510  N N   . GLY A 479  ? 0.2963 0.3019 0.2891 -0.0070 0.0038  0.0020  477  GLY A N   
3511  C CA  . GLY A 479  ? 0.3419 0.3479 0.3323 -0.0077 0.0041  0.0047  477  GLY A CA  
3512  C C   . GLY A 479  ? 0.3132 0.3243 0.3021 -0.0082 0.0044  0.0025  477  GLY A C   
3513  O O   . GLY A 479  ? 0.2992 0.3132 0.2890 -0.0076 0.0044  -0.0015 477  GLY A O   
3514  N N   . THR A 480  ? 0.3649 0.3771 0.3517 -0.0091 0.0044  0.0051  478  THR A N   
3515  C CA  . THR A 480  ? 0.3892 0.4071 0.3743 -0.0098 0.0047  0.0039  478  THR A CA  
3516  C C   . THR A 480  ? 0.4483 0.4630 0.4340 -0.0084 0.0056  0.0014  478  THR A C   
3517  O O   . THR A 480  ? 0.4845 0.4926 0.4717 -0.0069 0.0061  0.0012  478  THR A O   
3518  C CB  . THR A 480  ? 0.4180 0.4382 0.4014 -0.0115 0.0042  0.0083  478  THR A CB  
3519  O OG1 . THR A 480  ? 0.5460 0.5592 0.5300 -0.0108 0.0044  0.0105  478  THR A OG1 
3520  C CG2 . THR A 480  ? 0.4020 0.4251 0.3853 -0.0130 0.0030  0.0113  478  THR A CG2 
3521  N N   . HIS A 481  ? 0.4322 0.4522 0.4168 -0.0088 0.0060  -0.0003 479  HIS A N   
3522  C CA  . HIS A 481  ? 0.5377 0.5552 0.5229 -0.0075 0.0067  -0.0026 479  HIS A CA  
3523  C C   . HIS A 481  ? 0.5594 0.5703 0.5443 -0.0071 0.0071  0.0005  479  HIS A C   
3524  O O   . HIS A 481  ? 0.5706 0.5764 0.5567 -0.0056 0.0077  -0.0007 479  HIS A O   
3525  C CB  . HIS A 481  ? 0.4499 0.4750 0.4337 -0.0082 0.0070  -0.0045 479  HIS A CB  
3526  C CG  . HIS A 481  ? 0.4958 0.5285 0.4800 -0.0084 0.0066  -0.0082 479  HIS A CG  
3527  N ND1 . HIS A 481  ? 0.4995 0.5409 0.4824 -0.0091 0.0068  -0.0103 479  HIS A ND1 
3528  C CD2 . HIS A 481  ? 0.4492 0.4826 0.4350 -0.0080 0.0060  -0.0105 479  HIS A CD2 
3529  C CE1 . HIS A 481  ? 0.4670 0.5144 0.4506 -0.0090 0.0063  -0.0140 479  HIS A CE1 
3530  N NE2 . HIS A 481  ? 0.4983 0.5407 0.4837 -0.0083 0.0057  -0.0142 479  HIS A NE2 
3531  N N   . GLU A 482  ? 0.5595 0.5707 0.5430 -0.0084 0.0067  0.0045  480  GLU A N   
3532  C CA  . GLU A 482  ? 0.5872 0.5924 0.5707 -0.0080 0.0068  0.0070  480  GLU A CA  
3533  C C   . GLU A 482  ? 0.5772 0.5757 0.5622 -0.0065 0.0070  0.0071  480  GLU A C   
3534  O O   . GLU A 482  ? 0.5905 0.5843 0.5759 -0.0052 0.0076  0.0068  480  GLU A O   
3535  C CB  . GLU A 482  ? 0.5889 0.5957 0.5717 -0.0097 0.0059  0.0112  480  GLU A CB  
3536  N N   . THR A 483  ? 0.5253 0.5237 0.5111 -0.0066 0.0066  0.0076  481  THR A N   
3537  C CA  . THR A 483  ? 0.5724 0.5652 0.5598 -0.0054 0.0067  0.0081  481  THR A CA  
3538  C C   . THR A 483  ? 0.5247 0.5154 0.5136 -0.0039 0.0075  0.0051  481  THR A C   
3539  O O   . THR A 483  ? 0.5320 0.5180 0.5218 -0.0026 0.0080  0.0056  481  THR A O   
3540  C CB  . THR A 483  ? 0.4749 0.4687 0.4630 -0.0061 0.0060  0.0096  481  THR A CB  
3541  N N   . LEU A 484  ? 0.4926 0.4871 0.4820 -0.0040 0.0074  0.0021  482  LEU A N   
3542  C CA  . LEU A 484  ? 0.4750 0.4675 0.4670 -0.0027 0.0076  -0.0006 482  LEU A CA  
3543  C C   . LEU A 484  ? 0.5005 0.4900 0.4926 -0.0016 0.0083  -0.0011 482  LEU A C   
3544  O O   . LEU A 484  ? 0.5266 0.5120 0.5207 -0.0005 0.0085  -0.0011 482  LEU A O   
3545  C CB  . LEU A 484  ? 0.5454 0.5430 0.5385 -0.0030 0.0071  -0.0043 482  LEU A CB  
3546  N N   . LEU A 485  ? 0.5226 0.5145 0.5129 -0.0021 0.0085  -0.0014 483  LEU A N   
3547  C CA  . LEU A 485  ? 0.4991 0.4888 0.4897 -0.0011 0.0090  -0.0022 483  LEU A CA  
3548  C C   . LEU A 485  ? 0.5219 0.5065 0.5120 -0.0003 0.0094  0.0004  483  LEU A C   
3549  O O   . LEU A 485  ? 0.5073 0.4894 0.4980 0.0007  0.0098  -0.0001 483  LEU A O   
3550  C CB  . LEU A 485  ? 0.4702 0.4642 0.4590 -0.0018 0.0091  -0.0030 483  LEU A CB  
3551  C CG  . LEU A 485  ? 0.4933 0.4934 0.4828 -0.0022 0.0088  -0.0065 483  LEU A CG  
3552  C CD1 . LEU A 485  ? 0.5038 0.5092 0.4911 -0.0033 0.0090  -0.0064 483  LEU A CD1 
3553  C CD2 . LEU A 485  ? 0.4541 0.4527 0.4467 -0.0007 0.0088  -0.0100 483  LEU A CD2 
3554  N N   . ALA A 486  ? 0.5412 0.5243 0.5303 -0.0008 0.0093  0.0030  484  ALA A N   
3555  C CA  . ALA A 486  ? 0.5203 0.4995 0.5088 0.0000  0.0096  0.0051  484  ALA A CA  
3556  C C   . ALA A 486  ? 0.5290 0.5049 0.5191 0.0015  0.0101  0.0048  484  ALA A C   
3557  O O   . ALA A 486  ? 0.5405 0.5144 0.5301 0.0024  0.0106  0.0050  484  ALA A O   
3558  C CB  . ALA A 486  ? 0.5190 0.4975 0.5071 -0.0006 0.0091  0.0074  484  ALA A CB  
3559  N N   . TYR A 487  ? 0.5396 0.5151 0.5318 0.0017  0.0101  0.0045  485  TYR A N   
3560  C CA  . TYR A 487  ? 0.4841 0.4570 0.4783 0.0028  0.0105  0.0049  485  TYR A CA  
3561  C C   . TYR A 487  ? 0.5073 0.4809 0.5046 0.0030  0.0100  0.0029  485  TYR A C   
3562  O O   . TYR A 487  ? 0.4509 0.4228 0.4509 0.0035  0.0100  0.0035  485  TYR A O   
3563  C CB  . TYR A 487  ? 0.4956 0.4670 0.4903 0.0031  0.0106  0.0069  485  TYR A CB  
3564  N N   . LEU A 488  ? 0.5087 0.4849 0.5061 0.0025  0.0096  0.0003  486  LEU A N   
3565  C CA  . LEU A 488  ? 0.4886 0.4656 0.4896 0.0028  0.0090  -0.0022 486  LEU A CA  
3566  C C   . LEU A 488  ? 0.4743 0.4487 0.4778 0.0038  0.0090  -0.0021 486  LEU A C   
3567  O O   . LEU A 488  ? 0.3855 0.3590 0.3931 0.0042  0.0082  -0.0030 486  LEU A O   
3568  C CB  . LEU A 488  ? 0.4848 0.4662 0.4853 0.0022  0.0085  -0.0054 486  LEU A CB  
3569  C CG  . LEU A 488  ? 0.5248 0.5077 0.5293 0.0026  0.0076  -0.0090 486  LEU A CG  
3570  C CD1 . LEU A 488  ? 0.5043 0.4861 0.5116 0.0024  0.0069  -0.0086 486  LEU A CD1 
3571  C CD2 . LEU A 488  ? 0.4318 0.4203 0.4353 0.0020  0.0073  -0.0123 486  LEU A CD2 
3572  N N   . VAL A 489  ? 0.4958 0.4691 0.4970 0.0043  0.0096  -0.0010 487  VAL A N   
3573  C CA  . VAL A 489  ? 0.4500 0.4212 0.4534 0.0052  0.0096  -0.0004 487  VAL A CA  
3574  C C   . VAL A 489  ? 0.4853 0.4543 0.4911 0.0056  0.0095  0.0021  487  VAL A C   
3575  O O   . VAL A 489  ? 0.4795 0.4474 0.4896 0.0060  0.0088  0.0020  487  VAL A O   
3576  C CB  . VAL A 489  ? 0.4776 0.4483 0.4777 0.0056  0.0103  0.0006  487  VAL A CB  
3577  C CG1 . VAL A 489  ? 0.4906 0.4592 0.4925 0.0065  0.0103  0.0021  487  VAL A CG1 
3578  C CG2 . VAL A 489  ? 0.4501 0.4232 0.4489 0.0053  0.0101  -0.0019 487  VAL A CG2 
3579  N N   . ARG A 490  ? 0.4814 0.4498 0.4849 0.0055  0.0102  0.0044  488  ARG A N   
3580  C CA  . ARG A 490  ? 0.5033 0.4706 0.5092 0.0057  0.0104  0.0069  488  ARG A CA  
3581  C C   . ARG A 490  ? 0.5081 0.4754 0.5183 0.0053  0.0094  0.0060  488  ARG A C   
3582  O O   . ARG A 490  ? 0.5037 0.4700 0.5179 0.0055  0.0089  0.0074  488  ARG A O   
3583  C CB  . ARG A 490  ? 0.5266 0.4940 0.5294 0.0058  0.0112  0.0088  488  ARG A CB  
3584  C CG  . ARG A 490  ? 0.4587 0.4258 0.4635 0.0061  0.0115  0.0114  488  ARG A CG  
3585  C CD  . ARG A 490  ? 0.4691 0.4367 0.4715 0.0062  0.0122  0.0125  488  ARG A CD  
3586  N NE  . ARG A 490  ? 0.4909 0.4589 0.4933 0.0053  0.0117  0.0115  488  ARG A NE  
3587  C CZ  . ARG A 490  ? 0.4665 0.4349 0.4666 0.0052  0.0118  0.0116  488  ARG A CZ  
3588  N NH1 . ARG A 490  ? 0.4709 0.4391 0.4686 0.0059  0.0124  0.0123  488  ARG A NH1 
3589  N NH2 . ARG A 490  ? 0.4229 0.3921 0.4234 0.0043  0.0113  0.0109  488  ARG A NH2 
3590  N N   . ARG A 491  ? 0.4312 0.4001 0.4410 0.0046  0.0089  0.0037  489  ARG A N   
3591  C CA  . ARG A 491  ? 0.4934 0.4627 0.5073 0.0042  0.0079  0.0026  489  ARG A CA  
3592  C C   . ARG A 491  ? 0.5814 0.5502 0.6003 0.0045  0.0066  0.0004  489  ARG A C   
3593  O O   . ARG A 491  ? 0.5366 0.5047 0.5604 0.0044  0.0055  0.0003  489  ARG A O   
3594  C CB  . ARG A 491  ? 0.5376 0.5093 0.5494 0.0034  0.0077  0.0005  489  ARG A CB  
3595  N N   . LEU A 492  ? 0.5525 0.5217 0.5705 0.0050  0.0066  -0.0014 490  LEU A N   
3596  C CA  . LEU A 492  ? 0.5670 0.5360 0.5902 0.0055  0.0052  -0.0039 490  LEU A CA  
3597  C C   . LEU A 492  ? 0.5665 0.5327 0.5936 0.0060  0.0048  -0.0010 490  LEU A C   
3598  O O   . LEU A 492  ? 0.4819 0.4471 0.5153 0.0061  0.0032  -0.0018 490  LEU A O   
3599  C CB  . LEU A 492  ? 0.5343 0.5054 0.5554 0.0058  0.0053  -0.0071 490  LEU A CB  
3600  C CG  . LEU A 492  ? 0.5628 0.5379 0.5813 0.0052  0.0054  -0.0103 490  LEU A CG  
3601  C CD1 . LEU A 492  ? 0.5368 0.5143 0.5520 0.0053  0.0060  -0.0120 490  LEU A CD1 
3602  C CD2 . LEU A 492  ? 0.5879 0.5646 0.6114 0.0052  0.0038  -0.0140 490  LEU A CD2 
3603  N N   . LEU A 493  ? 0.5068 0.4722 0.5305 0.0062  0.0060  0.0024  491  LEU A N   
3604  C CA  . LEU A 493  ? 0.4769 0.4406 0.5038 0.0065  0.0057  0.0057  491  LEU A CA  
3605  C C   . LEU A 493  ? 0.5203 0.4833 0.5513 0.0060  0.0051  0.0082  491  LEU A C   
3606  O O   . LEU A 493  ? 0.5902 0.5521 0.6272 0.0059  0.0038  0.0098  491  LEU A O   
3607  C CB  . LEU A 493  ? 0.5538 0.5177 0.5758 0.0069  0.0072  0.0086  491  LEU A CB  
3608  C CG  . LEU A 493  ? 0.5660 0.5304 0.5838 0.0073  0.0078  0.0067  491  LEU A CG  
3609  C CD1 . LEU A 493  ? 0.5136 0.4781 0.5282 0.0078  0.0088  0.0097  491  LEU A CD1 
3610  C CD2 . LEU A 493  ? 0.5620 0.5263 0.5835 0.0076  0.0065  0.0038  491  LEU A CD2 
3611  N N   . GLY A 496  ? 0.5571 0.5182 0.6037 0.0064  0.0003  0.0020  494  GLY A N   
3612  C CA  . GLY A 496  ? 0.5550 0.5160 0.6041 0.0072  -0.0008 -0.0012 494  GLY A CA  
3613  C C   . GLY A 496  ? 0.5958 0.5556 0.6457 0.0076  -0.0008 0.0021  494  GLY A C   
3614  O O   . GLY A 496  ? 0.5772 0.5368 0.6288 0.0084  -0.0016 -0.0002 494  GLY A O   
3615  N N   . ALA A 497  ? 0.5756 0.5348 0.6240 0.0072  0.0001  0.0073  495  ALA A N   
3616  C CA  . ALA A 497  ? 0.5222 0.4808 0.5716 0.0075  0.0000  0.0111  495  ALA A CA  
3617  C C   . ALA A 497  ? 0.4494 0.4063 0.5085 0.0074  -0.0026 0.0125  495  ALA A C   
3618  O O   . ALA A 497  ? 0.4543 0.4103 0.5191 0.0069  -0.0042 0.0116  495  ALA A O   
3619  C CB  . ALA A 497  ? 0.4376 0.3974 0.4826 0.0071  0.0017  0.0161  495  ALA A CB  
3620  N N   . ASN A 498  ? 0.4580 0.4143 0.5194 0.0077  -0.0034 0.0149  496  ASN A N   
3621  C CA  . ASN A 498  ? 0.4484 0.4029 0.5197 0.0076  -0.0062 0.0163  496  ASN A CA  
3622  C C   . ASN A 498  ? 0.4282 0.3823 0.5046 0.0065  -0.0072 0.0207  496  ASN A C   
3623  O O   . ASN A 498  ? 0.4685 0.4208 0.5543 0.0062  -0.0099 0.0205  496  ASN A O   
3624  C CB  . ASN A 498  ? 0.4917 0.4461 0.5641 0.0080  -0.0067 0.0193  496  ASN A CB  
3625  N N   . SER A 499  ? 0.4560 0.4120 0.5271 0.0058  -0.0051 0.0246  497  SER A N   
3626  C CA  . SER A 499  ? 0.4156 0.3721 0.4909 0.0047  -0.0056 0.0290  497  SER A CA  
3627  C C   . SER A 499  ? 0.3697 0.3258 0.4455 0.0043  -0.0056 0.0260  497  SER A C   
3628  O O   . SER A 499  ? 0.3741 0.3303 0.4548 0.0033  -0.0065 0.0292  497  SER A O   
3629  C CB  . SER A 499  ? 0.4338 0.3935 0.5034 0.0043  -0.0034 0.0345  497  SER A CB  
3630  O OG  . SER A 499  ? 0.5043 0.4653 0.5642 0.0050  -0.0007 0.0320  497  SER A OG  
3631  N N   . SER A 500  ? 0.3380 0.2940 0.4090 0.0049  -0.0048 0.0203  498  SER A N   
3632  C CA  . SER A 500  ? 0.3274 0.2836 0.3982 0.0046  -0.0047 0.0175  498  SER A CA  
3633  C C   . SER A 500  ? 0.3843 0.3386 0.4648 0.0044  -0.0077 0.0148  498  SER A C   
3634  O O   . SER A 500  ? 0.3658 0.3188 0.4511 0.0051  -0.0096 0.0117  498  SER A O   
3635  C CB  . SER A 500  ? 0.4111 0.3683 0.4743 0.0052  -0.0031 0.0124  498  SER A CB  
3636  O OG  . SER A 500  ? 0.4638 0.4227 0.5186 0.0053  -0.0005 0.0145  498  SER A OG  
3637  N N   . PHE A 501  ? 0.3177 0.2720 0.4011 0.0035  -0.0083 0.0158  499  PHE A N   
3638  C CA  . PHE A 501  ? 0.3284 0.2811 0.4212 0.0033  -0.0113 0.0129  499  PHE A CA  
3639  C C   . PHE A 501  ? 0.3822 0.3350 0.4747 0.0044  -0.0121 0.0052  499  PHE A C   
3640  O O   . PHE A 501  ? 0.3974 0.3489 0.4982 0.0049  -0.0149 0.0019  499  PHE A O   
3641  C CB  . PHE A 501  ? 0.3112 0.2643 0.4055 0.0022  -0.0113 0.0145  499  PHE A CB  
3642  C CG  . PHE A 501  ? 0.3099 0.2614 0.4138 0.0020  -0.0146 0.0111  499  PHE A CG  
3643  C CD1 . PHE A 501  ? 0.3225 0.2720 0.4370 0.0013  -0.0173 0.0146  499  PHE A CD1 
3644  C CD2 . PHE A 501  ? 0.3780 0.3304 0.4809 0.0026  -0.0150 0.0045  499  PHE A CD2 
3645  C CE1 . PHE A 501  ? 0.3322 0.2801 0.4564 0.0012  -0.0206 0.0112  499  PHE A CE1 
3646  C CE2 . PHE A 501  ? 0.3253 0.2766 0.4374 0.0025  -0.0181 0.0008  499  PHE A CE2 
3647  C CZ  . PHE A 501  ? 0.3397 0.2885 0.4626 0.0019  -0.0210 0.0041  499  PHE A CZ  
3648  N N   . VAL A 502  ? 0.3838 0.3389 0.4675 0.0047  -0.0098 0.0022  500  VAL A N   
3649  C CA  . VAL A 502  ? 0.4054 0.3620 0.4885 0.0055  -0.0104 -0.0049 500  VAL A CA  
3650  C C   . VAL A 502  ? 0.4282 0.3844 0.5126 0.0066  -0.0111 -0.0074 500  VAL A C   
3651  O O   . VAL A 502  ? 0.5104 0.4673 0.5994 0.0075  -0.0129 -0.0131 500  VAL A O   
3652  C CB  . VAL A 502  ? 0.4244 0.3839 0.4979 0.0054  -0.0079 -0.0066 500  VAL A CB  
3653  N N   . HIS A 503  ? 0.3995 0.3551 0.4803 0.0067  -0.0097 -0.0034 501  HIS A N   
3654  C CA  . HIS A 503  ? 0.4018 0.3568 0.4850 0.0077  -0.0106 -0.0051 501  HIS A CA  
3655  C C   . HIS A 503  ? 0.4454 0.3977 0.5403 0.0079  -0.0140 -0.0046 501  HIS A C   
3656  O O   . HIS A 503  ? 0.4240 0.3761 0.5244 0.0089  -0.0160 -0.0093 501  HIS A O   
3657  C CB  . HIS A 503  ? 0.4396 0.3947 0.5163 0.0077  -0.0085 -0.0007 501  HIS A CB  
3658  C CG  . HIS A 503  ? 0.4664 0.4207 0.5458 0.0087  -0.0095 -0.0015 501  HIS A CG  
3659  N ND1 . HIS A 503  ? 0.4715 0.4237 0.5574 0.0086  -0.0112 0.0027  501  HIS A ND1 
3660  C CD2 . HIS A 503  ? 0.4722 0.4279 0.5489 0.0097  -0.0091 -0.0058 501  HIS A CD2 
3661  C CE1 . HIS A 503  ? 0.4720 0.4240 0.5591 0.0095  -0.0118 0.0009  501  HIS A CE1 
3662  N NE2 . HIS A 503  ? 0.4546 0.4087 0.5361 0.0102  -0.0105 -0.0044 501  HIS A NE2 
3663  N N   . ARG A 504  ? 0.3756 0.3261 0.4749 0.0068  -0.0149 0.0011  502  ARG A N   
3664  C CA  . ARG A 504  ? 0.3844 0.3323 0.4954 0.0067  -0.0182 0.0029  502  ARG A CA  
3665  C C   . ARG A 504  ? 0.4211 0.3681 0.5410 0.0070  -0.0213 -0.0026 502  ARG A C   
3666  O O   . ARG A 504  ? 0.3942 0.3393 0.5237 0.0077  -0.0244 -0.0047 502  ARG A O   
3667  C CB  . ARG A 504  ? 0.4042 0.3514 0.5172 0.0052  -0.0181 0.0112  502  ARG A CB  
3668  C CG  . ARG A 504  ? 0.4244 0.3728 0.5308 0.0051  -0.0159 0.0164  502  ARG A CG  
3669  C CD  . ARG A 504  ? 0.3997 0.3492 0.5046 0.0037  -0.0147 0.0238  502  ARG A CD  
3670  N NE  . ARG A 504  ? 0.4134 0.3614 0.5294 0.0026  -0.0177 0.0275  502  ARG A NE  
3671  C CZ  . ARG A 504  ? 0.4593 0.4060 0.5834 0.0023  -0.0201 0.0315  502  ARG A CZ  
3672  N NH1 . ARG A 504  ? 0.4927 0.4395 0.6152 0.0030  -0.0200 0.0322  502  ARG A NH1 
3673  N NH2 . ARG A 504  ? 0.4516 0.3969 0.5860 0.0011  -0.0229 0.0352  502  ARG A NH2 
3674  N N   . ILE A 505  ? 0.4174 0.3659 0.5345 0.0066  -0.0205 -0.0053 503  ILE A N   
3675  C CA  . ILE A 505  ? 0.4011 0.3494 0.5261 0.0070  -0.0234 -0.0112 503  ILE A CA  
3676  C C   . ILE A 505  ? 0.4320 0.3815 0.5589 0.0088  -0.0246 -0.0189 503  ILE A C   
3677  O O   . ILE A 505  ? 0.4879 0.4365 0.6249 0.0095  -0.0280 -0.0235 503  ILE A O   
3678  C CB  . ILE A 505  ? 0.4071 0.3575 0.5272 0.0064  -0.0221 -0.0128 503  ILE A CB  
3679  C CG1 . ILE A 505  ? 0.4560 0.4064 0.5850 0.0067  -0.0253 -0.0185 503  ILE A CG1 
3680  C CG2 . ILE A 505  ? 0.4764 0.4304 0.5851 0.0069  -0.0190 -0.0161 503  ILE A CG2 
3681  C CD1 . ILE A 505  ? 0.3614 0.3086 0.5011 0.0056  -0.0281 -0.0145 503  ILE A CD1 
3682  N N   . ASN A 506  ? 0.4099 0.3619 0.5278 0.0095  -0.0220 -0.0204 504  ASN A N   
3683  C CA  . ASN A 506  ? 0.4678 0.4219 0.5866 0.0111  -0.0227 -0.0275 504  ASN A CA  
3684  C C   . ASN A 506  ? 0.4747 0.4266 0.5983 0.0119  -0.0241 -0.0263 504  ASN A C   
3685  O O   . ASN A 506  ? 0.5199 0.4736 0.6455 0.0134  -0.0249 -0.0322 504  ASN A O   
3686  C CB  . ASN A 506  ? 0.4988 0.4572 0.6055 0.0113  -0.0193 -0.0300 504  ASN A CB  
3687  C CG  . ASN A 506  ? 0.5297 0.4912 0.6329 0.0108  -0.0186 -0.0330 504  ASN A CG  
3688  O OD1 . ASN A 506  ? 0.5950 0.5567 0.7053 0.0110  -0.0211 -0.0368 504  ASN A OD1 
3689  N ND2 . ASN A 506  ? 0.6149 0.5788 0.7073 0.0101  -0.0154 -0.0312 504  ASN A ND2 
3690  N N   . ASP A 507  ? 0.4359 0.3846 0.5614 0.0110  -0.0242 -0.0189 505  ASP A N   
3691  C CA  . ASP A 507  ? 0.4724 0.4192 0.6030 0.0117  -0.0257 -0.0172 505  ASP A CA  
3692  C C   . ASP A 507  ? 0.5276 0.4714 0.6727 0.0122  -0.0303 -0.0189 505  ASP A C   
3693  O O   . ASP A 507  ? 0.4617 0.4032 0.6132 0.0109  -0.0320 -0.0145 505  ASP A O   
3694  C CB  . ASP A 507  ? 0.4380 0.3834 0.5646 0.0105  -0.0241 -0.0083 505  ASP A CB  
3695  C CG  . ASP A 507  ? 0.5366 0.4807 0.6667 0.0112  -0.0252 -0.0062 505  ASP A CG  
3696  O OD1 . ASP A 507  ? 0.5725 0.5149 0.7127 0.0122  -0.0286 -0.0095 505  ASP A OD1 
3697  O OD2 . ASP A 507  ? 0.5132 0.4579 0.6363 0.0108  -0.0229 -0.0013 505  ASP A OD2 
3698  N N   . PRO A 508  ? 0.5366 0.4807 0.6880 0.0139  -0.0325 -0.0251 506  PRO A N   
3699  C CA  . PRO A 508  ? 0.5727 0.5137 0.7392 0.0144  -0.0373 -0.0271 506  PRO A CA  
3700  C C   . PRO A 508  ? 0.5062 0.4432 0.6802 0.0133  -0.0394 -0.0187 506  PRO A C   
3701  O O   . PRO A 508  ? 0.5705 0.5044 0.7567 0.0129  -0.0432 -0.0176 506  PRO A O   
3702  C CB  . PRO A 508  ? 0.5559 0.4987 0.7257 0.0167  -0.0387 -0.0353 506  PRO A CB  
3703  C CG  . PRO A 508  ? 0.6071 0.5547 0.7632 0.0171  -0.0345 -0.0384 506  PRO A CG  
3704  C CD  . PRO A 508  ? 0.5248 0.4721 0.6703 0.0154  -0.0309 -0.0304 506  PRO A CD  
3705  N N   . LYS A 509  ? 0.4938 0.4309 0.6611 0.0128  -0.0371 -0.0127 507  LYS A N   
3706  C CA  . LYS A 509  ? 0.5046 0.4389 0.6781 0.0118  -0.0389 -0.0044 507  LYS A CA  
3707  C C   . LYS A 509  ? 0.5035 0.4371 0.6766 0.0096  -0.0383 0.0035  507  LYS A C   
3708  O O   . LYS A 509  ? 0.5220 0.4543 0.7000 0.0084  -0.0396 0.0112  507  LYS A O   
3709  C CB  . LYS A 509  ? 0.5752 0.5106 0.7411 0.0121  -0.0366 -0.0012 507  LYS A CB  
3710  N N   . VAL A 510  ? 0.4619 0.3971 0.6296 0.0089  -0.0364 0.0019  508  VAL A N   
3711  C CA  . VAL A 510  ? 0.4342 0.3694 0.6011 0.0069  -0.0356 0.0089  508  VAL A CA  
3712  C C   . VAL A 510  ? 0.4010 0.3342 0.5789 0.0065  -0.0391 0.0066  508  VAL A C   
3713  O O   . VAL A 510  ? 0.4601 0.3942 0.6369 0.0074  -0.0391 -0.0007 508  VAL A O   
3714  C CB  . VAL A 510  ? 0.4380 0.3764 0.5903 0.0065  -0.0309 0.0095  508  VAL A CB  
3715  C CG1 . VAL A 510  ? 0.4061 0.3449 0.5582 0.0046  -0.0302 0.0162  508  VAL A CG1 
3716  C CG2 . VAL A 510  ? 0.4334 0.3736 0.5755 0.0070  -0.0278 0.0115  508  VAL A CG2 
3717  N N   . SER A 511  ? 0.3975 0.3283 0.5862 0.0052  -0.0422 0.0128  509  SER A N   
3718  C CA  . SER A 511  ? 0.3905 0.3191 0.5910 0.0046  -0.0459 0.0110  509  SER A CA  
3719  C C   . SER A 511  ? 0.4161 0.3464 0.6112 0.0032  -0.0438 0.0131  509  SER A C   
3720  O O   . SER A 511  ? 0.4114 0.3443 0.5953 0.0024  -0.0398 0.0177  509  SER A O   
3721  C CB  . SER A 511  ? 0.4423 0.3678 0.6569 0.0034  -0.0502 0.0178  509  SER A CB  
3722  O OG  . SER A 511  ? 0.4539 0.3810 0.6648 0.0013  -0.0483 0.0280  509  SER A OG  
3723  N N   . ILE A 512  ? 0.3854 0.3143 0.5890 0.0031  -0.0466 0.0092  510  ILE A N   
3724  C CA  . ILE A 512  ? 0.4022 0.3324 0.6028 0.0016  -0.0452 0.0114  510  ILE A CA  
3725  C C   . ILE A 512  ? 0.4455 0.3758 0.6484 -0.0007 -0.0450 0.0224  510  ILE A C   
3726  O O   . ILE A 512  ? 0.3921 0.3250 0.5863 -0.0018 -0.0417 0.0266  510  ILE A O   
3727  C CB  . ILE A 512  ? 0.4038 0.3325 0.6142 0.0020  -0.0488 0.0049  510  ILE A CB  
3728  C CG1 . ILE A 512  ? 0.3920 0.3223 0.5980 0.0043  -0.0482 -0.0060 510  ILE A CG1 
3729  C CG2 . ILE A 512  ? 0.4196 0.3495 0.6280 0.0003  -0.0477 0.0078  510  ILE A CG2 
3730  C CD1 . ILE A 512  ? 0.4450 0.3745 0.6609 0.0050  -0.0519 -0.0136 510  ILE A CD1 
3731  N N   . ASP A 513  ? 0.4212 0.3491 0.6357 -0.0014 -0.0486 0.0274  511  ASP A N   
3732  C CA  . ASP A 513  ? 0.4258 0.3547 0.6427 -0.0037 -0.0485 0.0384  511  ASP A CA  
3733  C C   . ASP A 513  ? 0.4370 0.3698 0.6396 -0.0040 -0.0436 0.0434  511  ASP A C   
3734  O O   . ASP A 513  ? 0.4131 0.3488 0.6115 -0.0056 -0.0414 0.0501  511  ASP A O   
3735  C CB  . ASP A 513  ? 0.4843 0.4102 0.7160 -0.0044 -0.0533 0.0430  511  ASP A CB  
3736  C CG  . ASP A 513  ? 0.5426 0.4680 0.7871 -0.0046 -0.0579 0.0387  511  ASP A CG  
3737  O OD1 . ASP A 513  ? 0.5575 0.4830 0.8033 -0.0054 -0.0580 0.0377  511  ASP A OD1 
3738  O OD2 . ASP A 513  ? 0.6647 0.5899 0.9182 -0.0039 -0.0614 0.0361  511  ASP A OD2 
3739  N N   . GLU A 514  ? 0.4044 0.3377 0.5996 -0.0023 -0.0417 0.0398  512  GLU A N   
3740  C CA  . GLU A 514  ? 0.3934 0.3304 0.5747 -0.0022 -0.0371 0.0432  512  GLU A CA  
3741  C C   . GLU A 514  ? 0.3922 0.3317 0.5621 -0.0022 -0.0332 0.0406  512  GLU A C   
3742  O O   . GLU A 514  ? 0.3979 0.3408 0.5595 -0.0030 -0.0300 0.0458  512  GLU A O   
3743  C CB  . GLU A 514  ? 0.4342 0.3708 0.6106 -0.0004 -0.0363 0.0391  512  GLU A CB  
3744  C CG  . GLU A 514  ? 0.5038 0.4389 0.6887 -0.0006 -0.0391 0.0436  512  GLU A CG  
3745  C CD  . GLU A 514  ? 0.5844 0.5185 0.7667 0.0015  -0.0391 0.0380  512  GLU A CD  
3746  O OE1 . GLU A 514  ? 0.5741 0.5068 0.7571 0.0031  -0.0397 0.0291  512  GLU A OE1 
3747  O OE2 . GLU A 514  ? 0.7127 0.6480 0.8922 0.0015  -0.0383 0.0423  512  GLU A OE2 
3748  N N   . LEU A 515  ? 0.4043 0.3425 0.5739 -0.0012 -0.0336 0.0325  513  LEU A N   
3749  C CA  . LEU A 515  ? 0.3688 0.3094 0.5278 -0.0010 -0.0302 0.0298  513  LEU A CA  
3750  C C   . LEU A 515  ? 0.3766 0.3183 0.5382 -0.0028 -0.0302 0.0346  513  LEU A C   
3751  O O   . LEU A 515  ? 0.3517 0.2961 0.5040 -0.0031 -0.0269 0.0357  513  LEU A O   
3752  C CB  . LEU A 515  ? 0.3438 0.2837 0.5019 0.0005  -0.0308 0.0199  513  LEU A CB  
3753  C CG  . LEU A 515  ? 0.3830 0.3233 0.5352 0.0023  -0.0296 0.0145  513  LEU A CG  
3754  C CD1 . LEU A 515  ? 0.3753 0.3155 0.5291 0.0037  -0.0309 0.0049  513  LEU A CD1 
3755  C CD2 . LEU A 515  ? 0.3623 0.3054 0.5002 0.0025  -0.0250 0.0164  513  LEU A CD2 
3756  N N   . ILE A 516  ? 0.3359 0.2755 0.5106 -0.0040 -0.0340 0.0375  514  ILE A N   
3757  C CA  . ILE A 516  ? 0.3426 0.2833 0.5209 -0.0059 -0.0344 0.0423  514  ILE A CA  
3758  C C   . ILE A 516  ? 0.3883 0.3315 0.5679 -0.0077 -0.0338 0.0528  514  ILE A C   
3759  O O   . ILE A 516  ? 0.3905 0.3352 0.5745 -0.0094 -0.0343 0.0580  514  ILE A O   
3760  C CB  . ILE A 516  ? 0.3615 0.2990 0.5534 -0.0063 -0.0389 0.0392  514  ILE A CB  
3761  C CG1 . ILE A 516  ? 0.4235 0.3580 0.6291 -0.0068 -0.0433 0.0425  514  ILE A CG1 
3762  C CG2 . ILE A 516  ? 0.3898 0.3260 0.5796 -0.0045 -0.0393 0.0285  514  ILE A CG2 
3763  C CD1 . ILE A 516  ? 0.4182 0.3493 0.6388 -0.0074 -0.0483 0.0401  514  ILE A CD1 
3764  N N   . ALA A 517  ? 0.3382 0.2825 0.5144 -0.0073 -0.0328 0.0561  515  ALA A N   
3765  C CA  . ALA A 517  ? 0.3427 0.2907 0.5188 -0.0089 -0.0319 0.0659  515  ALA A CA  
3766  C C   . ALA A 517  ? 0.3866 0.3392 0.5533 -0.0096 -0.0280 0.0687  515  ALA A C   
3767  O O   . ALA A 517  ? 0.3429 0.2964 0.4988 -0.0083 -0.0248 0.0637  515  ALA A O   
3768  C CB  . ALA A 517  ? 0.4079 0.3570 0.5788 -0.0080 -0.0306 0.0676  515  ALA A CB  
3769  N N   . ASP A 518  ? 0.3618 0.3175 0.5333 -0.0116 -0.0284 0.0768  516  ASP A N   
3770  C CA  . ASP A 518  ? 0.3603 0.3209 0.5247 -0.0124 -0.0251 0.0799  516  ASP A CA  
3771  C C   . ASP A 518  ? 0.3158 0.2817 0.4697 -0.0120 -0.0214 0.0839  516  ASP A C   
3772  O O   . ASP A 518  ? 0.3398 0.3089 0.4970 -0.0131 -0.0220 0.0914  516  ASP A O   
3773  C CB  . ASP A 518  ? 0.3821 0.3444 0.5569 -0.0148 -0.0273 0.0871  516  ASP A CB  
3774  C CG  . ASP A 518  ? 0.3620 0.3295 0.5306 -0.0156 -0.0241 0.0899  516  ASP A CG  
3775  O OD1 . ASP A 518  ? 0.3464 0.3161 0.5028 -0.0142 -0.0203 0.0865  516  ASP A OD1 
3776  O OD2 . ASP A 518  ? 0.4424 0.4119 0.6189 -0.0176 -0.0256 0.0957  516  ASP A OD2 
3777  N N   . PRO A 519  ? 0.3453 0.3125 0.4868 -0.0104 -0.0178 0.0792  517  PRO A N   
3778  C CA  . PRO A 519  ? 0.3329 0.3052 0.4647 -0.0098 -0.0145 0.0823  517  PRO A CA  
3779  C C   . PRO A 519  ? 0.2868 0.2659 0.4190 -0.0115 -0.0132 0.0908  517  PRO A C   
3780  O O   . PRO A 519  ? 0.3148 0.2986 0.4435 -0.0116 -0.0119 0.0955  517  PRO A O   
3781  C CB  . PRO A 519  ? 0.3316 0.3035 0.4517 -0.0080 -0.0112 0.0753  517  PRO A CB  
3782  C CG  . PRO A 519  ? 0.3695 0.3384 0.4927 -0.0083 -0.0122 0.0711  517  PRO A CG  
3783  C CD  . PRO A 519  ? 0.3077 0.2724 0.4438 -0.0092 -0.0165 0.0714  517  PRO A CD  
3784  N N   . VAL A 520  ? 0.3151 0.2954 0.4516 -0.0127 -0.0136 0.0927  518  VAL A N   
3785  C CA  . VAL A 520  ? 0.2923 0.2799 0.4293 -0.0143 -0.0123 0.1006  518  VAL A CA  
3786  C C   . VAL A 520  ? 0.3400 0.3299 0.4861 -0.0162 -0.0149 0.1090  518  VAL A C   
3787  O O   . VAL A 520  ? 0.3421 0.3391 0.4850 -0.0167 -0.0132 0.1152  518  VAL A O   
3788  C CB  . VAL A 520  ? 0.3189 0.3067 0.4598 -0.0154 -0.0126 0.1007  518  VAL A CB  
3789  C CG1 . VAL A 520  ? 0.3431 0.3393 0.4849 -0.0171 -0.0112 0.1091  518  VAL A CG1 
3790  C CG2 . VAL A 520  ? 0.3081 0.2940 0.4400 -0.0137 -0.0101 0.0928  518  VAL A CG2 
3791  N N   . GLU A 521  ? 0.3678 0.3521 0.5256 -0.0171 -0.0191 0.1092  519  GLU A N   
3792  C CA  . GLU A 521  ? 0.3411 0.3272 0.5090 -0.0190 -0.0221 0.1175  519  GLU A CA  
3793  C C   . GLU A 521  ? 0.3649 0.3512 0.5291 -0.0179 -0.0219 0.1180  519  GLU A C   
3794  O O   . GLU A 521  ? 0.4201 0.4114 0.5875 -0.0193 -0.0226 0.1261  519  GLU A O   
3795  C CB  . GLU A 521  ? 0.4090 0.3888 0.5915 -0.0202 -0.0270 0.1173  519  GLU A CB  
3796  C CG  . GLU A 521  ? 0.4371 0.4177 0.6246 -0.0217 -0.0275 0.1187  519  GLU A CG  
3797  C CD  . GLU A 521  ? 0.5037 0.4935 0.6901 -0.0236 -0.0255 0.1278  519  GLU A CD  
3798  O OE1 . GLU A 521  ? 0.5275 0.5232 0.7157 -0.0245 -0.0262 0.1338  519  GLU A OE1 
3799  O OE2 . GLU A 521  ? 0.5125 0.5053 0.6947 -0.0238 -0.0232 0.1273  519  GLU A OE2 
3800  N N   . VAL A 522  ? 0.3258 0.3074 0.4835 -0.0156 -0.0210 0.1097  520  VAL A N   
3801  C CA  . VAL A 522  ? 0.3181 0.3000 0.4719 -0.0146 -0.0207 0.1099  520  VAL A CA  
3802  C C   . VAL A 522  ? 0.4066 0.3968 0.5498 -0.0144 -0.0168 0.1139  520  VAL A C   
3803  O O   . VAL A 522  ? 0.3708 0.3653 0.5146 -0.0150 -0.0172 0.1199  520  VAL A O   
3804  C CB  . VAL A 522  ? 0.3781 0.3535 0.5275 -0.0122 -0.0206 0.1000  520  VAL A CB  
3805  C CG1 . VAL A 522  ? 0.3975 0.3737 0.5420 -0.0111 -0.0199 0.1002  520  VAL A CG1 
3806  C CG2 . VAL A 522  ? 0.3699 0.3380 0.5308 -0.0123 -0.0248 0.0961  520  VAL A CG2 
3807  N N   . VAL A 523  ? 0.3418 0.3348 0.4753 -0.0134 -0.0132 0.1105  521  VAL A N   
3808  C CA  . VAL A 523  ? 0.3176 0.3188 0.4412 -0.0130 -0.0096 0.1134  521  VAL A CA  
3809  C C   . VAL A 523  ? 0.3577 0.3671 0.4863 -0.0153 -0.0099 0.1235  521  VAL A C   
3810  O O   . VAL A 523  ? 0.3650 0.3813 0.4899 -0.0154 -0.0087 0.1285  521  VAL A O   
3811  C CB  . VAL A 523  ? 0.3188 0.3207 0.4322 -0.0115 -0.0060 0.1073  521  VAL A CB  
3812  C CG1 . VAL A 523  ? 0.3292 0.3405 0.4343 -0.0112 -0.0026 0.1108  521  VAL A CG1 
3813  C CG2 . VAL A 523  ? 0.3163 0.3120 0.4233 -0.0092 -0.0054 0.0985  521  VAL A CG2 
3814  N N   . ARG A 524  ? 0.3576 0.3668 0.4946 -0.0171 -0.0115 0.1268  522  ARG A N   
3815  C CA  . ARG A 524  ? 0.3647 0.3823 0.5068 -0.0195 -0.0118 0.1368  522  ARG A CA  
3816  C C   . ARG A 524  ? 0.4347 0.4545 0.5836 -0.0209 -0.0144 0.1443  522  ARG A C   
3817  O O   . ARG A 524  ? 0.4697 0.4991 0.6180 -0.0222 -0.0135 0.1520  522  ARG A O   
3818  C CB  . ARG A 524  ? 0.4024 0.4180 0.5541 -0.0213 -0.0138 0.1388  522  ARG A CB  
3819  C CG  . ARG A 524  ? 0.4331 0.4577 0.5913 -0.0240 -0.0145 0.1491  522  ARG A CG  
3820  C CD  . ARG A 524  ? 0.4809 0.5028 0.6510 -0.0256 -0.0181 0.1496  522  ARG A CD  
3821  N NE  . ARG A 524  ? 0.4534 0.4688 0.6225 -0.0250 -0.0173 0.1440  522  ARG A NE  
3822  C CZ  . ARG A 524  ? 0.3729 0.3927 0.5364 -0.0250 -0.0142 0.1439  522  ARG A CZ  
3823  N NH1 . ARG A 524  ? 0.4655 0.4959 0.6242 -0.0256 -0.0114 0.1498  522  ARG A NH1 
3824  N NH2 . ARG A 524  ? 0.4059 0.4202 0.5684 -0.0241 -0.0140 0.1368  522  ARG A NH2 
3825  N N   . ALA A 525  ? 0.3969 0.4087 0.5520 -0.0205 -0.0177 0.1417  523  ALA A N   
3826  C CA  . ALA A 525  ? 0.4441 0.4578 0.6063 -0.0216 -0.0207 0.1467  523  ALA A CA  
3827  C C   . ALA A 525  ? 0.4560 0.4713 0.6106 -0.0202 -0.0193 0.1470  523  ALA A C   
3828  O O   . ALA A 525  ? 0.4822 0.5001 0.6416 -0.0209 -0.0216 0.1506  523  ALA A O   
3829  C CB  . ALA A 525  ? 0.4083 0.4133 0.5825 -0.0218 -0.0254 0.1433  523  ALA A CB  
3830  N N   . MET A 526  ? 0.4374 0.4527 0.5796 -0.0179 -0.0156 0.1406  524  MET A N   
3831  C CA  A MET A 526  ? 0.4463 0.4640 0.5803 -0.0164 -0.0141 0.1395  524  MET A CA  
3832  C CA  B MET A 526  ? 0.4460 0.4636 0.5803 -0.0165 -0.0141 0.1396  524  MET A CA  
3833  C C   . MET A 526  ? 0.4582 0.4874 0.5901 -0.0177 -0.0128 0.1486  524  MET A C   
3834  O O   . MET A 526  ? 0.4209 0.4574 0.5531 -0.0191 -0.0115 0.1536  524  MET A O   
3835  C CB  A MET A 526  ? 0.4755 0.4918 0.5965 -0.0138 -0.0103 0.1303  524  MET A CB  
3836  C CB  B MET A 526  ? 0.4758 0.4915 0.5973 -0.0138 -0.0105 0.1301  524  MET A CB  
3837  C CG  A MET A 526  ? 0.4546 0.4605 0.5761 -0.0123 -0.0112 0.1210  524  MET A CG  
3838  C CG  B MET A 526  ? 0.4564 0.4618 0.5784 -0.0121 -0.0119 0.1214  524  MET A CG  
3839  S SD  A MET A 526  ? 0.5276 0.5265 0.6540 -0.0115 -0.0144 0.1187  524  MET A SD  
3840  S SD  B MET A 526  ? 0.4703 0.4727 0.5800 -0.0096 -0.0082 0.1108  524  MET A SD  
3841  C CE  A MET A 526  ? 0.4273 0.4323 0.5417 -0.0100 -0.0114 0.1189  524  MET A CE  
3842  C CE  B MET A 526  ? 0.4419 0.4362 0.5502 -0.0077 -0.0094 0.1034  524  MET A CE  
3843  N N   . PRO A 527  ? 0.5056 0.5375 0.6353 -0.0173 -0.0132 0.1510  525  PRO A N   
3844  C CA  . PRO A 527  ? 0.5064 0.5506 0.6340 -0.0186 -0.0121 0.1593  525  PRO A CA  
3845  C C   . PRO A 527  ? 0.4763 0.5292 0.5921 -0.0175 -0.0075 0.1582  525  PRO A C   
3846  O O   . PRO A 527  ? 0.4138 0.4770 0.5300 -0.0190 -0.0065 0.1643  525  PRO A O   
3847  C CB  . PRO A 527  ? 0.5038 0.5475 0.6305 -0.0179 -0.0134 0.1599  525  PRO A CB  
3848  C CG  . PRO A 527  ? 0.5066 0.5397 0.6294 -0.0155 -0.0132 0.1501  525  PRO A CG  
3849  C CD  . PRO A 527  ? 0.5014 0.5262 0.6304 -0.0157 -0.0146 0.1459  525  PRO A CD  
3850  N N   . VAL A 528  ? 0.4867 0.5364 0.5923 -0.0148 -0.0048 0.1490  526  VAL A N   
3851  C CA  . VAL A 528  ? 0.3732 0.4295 0.4682 -0.0134 -0.0007 0.1457  526  VAL A CA  
3852  C C   . VAL A 528  ? 0.4004 0.4485 0.4937 -0.0123 0.0001  0.1375  526  VAL A C   
3853  O O   . VAL A 528  ? 0.4294 0.4690 0.5197 -0.0105 0.0000  0.1297  526  VAL A O   
3854  C CB  . VAL A 528  ? 0.4110 0.4714 0.4953 -0.0113 0.0016  0.1421  526  VAL A CB  
3855  C CG1 . VAL A 528  ? 0.4424 0.5089 0.5167 -0.0096 0.0055  0.1377  526  VAL A CG1 
3856  C CG2 . VAL A 528  ? 0.4578 0.5270 0.5437 -0.0125 0.0007  0.1504  526  VAL A CG2 
3857  N N   . VAL A 529  ? 0.3686 0.4196 0.4641 -0.0133 0.0010  0.1392  527  VAL A N   
3858  C CA  . VAL A 529  ? 0.3647 0.4085 0.4591 -0.0123 0.0016  0.1320  527  VAL A CA  
3859  C C   . VAL A 529  ? 0.3886 0.4327 0.4709 -0.0096 0.0050  0.1241  527  VAL A C   
3860  O O   . VAL A 529  ? 0.3845 0.4377 0.4599 -0.0089 0.0077  0.1251  527  VAL A O   
3861  C CB  . VAL A 529  ? 0.3749 0.4226 0.4743 -0.0141 0.0018  0.1361  527  VAL A CB  
3862  C CG1 . VAL A 529  ? 0.3483 0.3892 0.4454 -0.0129 0.0027  0.1285  527  VAL A CG1 
3863  C CG2 . VAL A 529  ? 0.4188 0.4648 0.5313 -0.0169 -0.0020 0.1437  527  VAL A CG2 
3864  N N   . GLY A 530  ? 0.3353 0.3699 0.4152 -0.0081 0.0047  0.1162  528  GLY A N   
3865  C CA  . GLY A 530  ? 0.3274 0.3613 0.3971 -0.0057 0.0074  0.1086  528  GLY A CA  
3866  C C   . GLY A 530  ? 0.2979 0.3338 0.3604 -0.0041 0.0085  0.1064  528  GLY A C   
3867  O O   . GLY A 530  ? 0.3318 0.3694 0.3858 -0.0022 0.0109  0.1013  528  GLY A O   
3868  N N   . ALA A 531  ? 0.3147 0.3504 0.3806 -0.0047 0.0066  0.1102  529  ALA A N   
3869  C CA  . ALA A 531  ? 0.3053 0.3428 0.3645 -0.0032 0.0074  0.1080  529  ALA A CA  
3870  C C   . ALA A 531  ? 0.2908 0.3202 0.3447 -0.0012 0.0081  0.0989  529  ALA A C   
3871  O O   . ALA A 531  ? 0.3447 0.3656 0.4024 -0.0014 0.0066  0.0953  529  ALA A O   
3872  C CB  . ALA A 531  ? 0.3393 0.3766 0.4044 -0.0043 0.0048  0.1133  529  ALA A CB  
3873  N N   . LYS A 532  ? 0.3101 0.3427 0.3552 0.0006  0.0102  0.0952  530  LYS A N   
3874  C CA  . LYS A 532  ? 0.3140 0.3398 0.3538 0.0024  0.0107  0.0874  530  LYS A CA  
3875  C C   . LYS A 532  ? 0.3346 0.3532 0.3789 0.0021  0.0082  0.0866  530  LYS A C   
3876  O O   . LYS A 532  ? 0.3001 0.3204 0.3495 0.0010  0.0064  0.0920  530  LYS A O   
3877  C CB  . LYS A 532  ? 0.3433 0.3748 0.3745 0.0041  0.0127  0.0851  530  LYS A CB  
3878  C CG  . LYS A 532  ? 0.4145 0.4399 0.4403 0.0059  0.0131  0.0777  530  LYS A CG  
3879  C CD  . LYS A 532  ? 0.3650 0.3964 0.3832 0.0075  0.0148  0.0757  530  LYS A CD  
3880  C CE  . LYS A 532  ? 0.3807 0.4172 0.3995 0.0072  0.0139  0.0805  530  LYS A CE  
3881  N NZ  . LYS A 532  ? 0.3506 0.3799 0.3728 0.0068  0.0117  0.0799  530  LYS A NZ  
3882  N N   . HIS A 533  ? 0.2983 0.3092 0.3411 0.0030  0.0080  0.0799  531  HIS A N   
3883  C CA  . HIS A 533  ? 0.2739 0.2785 0.3198 0.0031  0.0060  0.0780  531  HIS A CA  
3884  C C   . HIS A 533  ? 0.3180 0.3262 0.3606 0.0038  0.0060  0.0795  531  HIS A C   
3885  O O   . HIS A 533  ? 0.3061 0.3182 0.3410 0.0051  0.0081  0.0773  531  HIS A O   
3886  C CB  . HIS A 533  ? 0.3036 0.3014 0.3463 0.0043  0.0064  0.0702  531  HIS A CB  
3887  C CG  . HIS A 533  ? 0.3318 0.3230 0.3794 0.0042  0.0041  0.0678  531  HIS A CG  
3888  N ND1 . HIS A 533  ? 0.3413 0.3320 0.3885 0.0048  0.0033  0.0677  531  HIS A ND1 
3889  C CD2 . HIS A 533  ? 0.3904 0.3757 0.4439 0.0038  0.0024  0.0653  531  HIS A CD2 
3890  C CE1 . HIS A 533  ? 0.4433 0.4280 0.4958 0.0048  0.0012  0.0651  531  HIS A CE1 
3891  N NE2 . HIS A 533  ? 0.4564 0.4380 0.5128 0.0042  0.0006  0.0635  531  HIS A NE2 
3892  N N   . ASP A 534  ? 0.3122 0.3189 0.3610 0.0030  0.0036  0.0830  532  ASP A N   
3893  C CA  . ASP A 534  ? 0.3432 0.3536 0.3898 0.0035  0.0033  0.0852  532  ASP A CA  
3894  C C   . ASP A 534  ? 0.3453 0.3525 0.3851 0.0053  0.0043  0.0785  532  ASP A C   
3895  O O   . ASP A 534  ? 0.3883 0.4000 0.4230 0.0061  0.0052  0.0789  532  ASP A O   
3896  C CB  . ASP A 534  ? 0.3726 0.3810 0.4284 0.0023  0.0001  0.0901  532  ASP A CB  
3897  N N   . ARG A 535  ? 0.3168 0.3167 0.3566 0.0059  0.0042  0.0724  533  ARG A N   
3898  C CA  . ARG A 535  ? 0.3251 0.3217 0.3598 0.0073  0.0047  0.0665  533  ARG A CA  
3899  C C   . ARG A 535  ? 0.3118 0.3090 0.3385 0.0084  0.0072  0.0614  533  ARG A C   
3900  O O   . ARG A 535  ? 0.3507 0.3445 0.3736 0.0094  0.0076  0.0562  533  ARG A O   
3901  C CB  . ARG A 535  ? 0.4097 0.3989 0.4497 0.0073  0.0028  0.0630  533  ARG A CB  
3902  C CG  . ARG A 535  ? 0.4965 0.4847 0.5455 0.0063  -0.0001 0.0676  533  ARG A CG  
3903  C CD  . ARG A 535  ? 0.5816 0.5634 0.6347 0.0068  -0.0020 0.0633  533  ARG A CD  
3904  N NE  . ARG A 535  ? 0.6402 0.6174 0.6931 0.0071  -0.0016 0.0574  533  ARG A NE  
3905  C CZ  . ARG A 535  ? 0.6620 0.6361 0.7216 0.0064  -0.0030 0.0572  533  ARG A CZ  
3906  N NH1 . ARG A 535  ? 0.7009 0.6756 0.7687 0.0052  -0.0052 0.0626  533  ARG A NH1 
3907  N NH2 . ARG A 535  ? 0.6514 0.6221 0.7098 0.0067  -0.0025 0.0515  533  ARG A NH2 
3908  N N   . ILE A 536  ? 0.2986 0.3001 0.3230 0.0083  0.0088  0.0630  534  ILE A N   
3909  C CA  . ILE A 536  ? 0.3136 0.3161 0.3311 0.0094  0.0109  0.0585  534  ILE A CA  
3910  C C   . ILE A 536  ? 0.3071 0.3180 0.3200 0.0101  0.0123  0.0610  534  ILE A C   
3911  O O   . ILE A 536  ? 0.3334 0.3499 0.3486 0.0092  0.0125  0.0661  534  ILE A O   
3912  C CB  . ILE A 536  ? 0.3003 0.3005 0.3190 0.0090  0.0115  0.0570  534  ILE A CB  
3913  C CG1 . ILE A 536  ? 0.3373 0.3299 0.3602 0.0085  0.0100  0.0540  534  ILE A CG1 
3914  C CG2 . ILE A 536  ? 0.3027 0.3044 0.3148 0.0102  0.0135  0.0529  534  ILE A CG2 
3915  C CD1 . ILE A 536  ? 0.3487 0.3392 0.3736 0.0079  0.0102  0.0528  534  ILE A CD1 
3916  N N   . ALA A 537  ? 0.2785 0.2906 0.2853 0.0115  0.0133  0.0573  535  ALA A N   
3917  C CA  . ALA A 537  ? 0.2751 0.2956 0.2775 0.0124  0.0145  0.0588  535  ALA A CA  
3918  C C   . ALA A 537  ? 0.2719 0.2956 0.2711 0.0131  0.0163  0.0567  535  ALA A C   
3919  O O   . ALA A 537  ? 0.2828 0.3016 0.2804 0.0136  0.0168  0.0519  535  ALA A O   
3920  C CB  . ALA A 537  ? 0.2924 0.3130 0.2900 0.0137  0.0146  0.0552  535  ALA A CB  
3921  N N   . LEU A 538  ? 0.2664 0.2986 0.2651 0.0130  0.0173  0.0605  536  LEU A N   
3922  C CA  . LEU A 538  ? 0.2908 0.3275 0.2857 0.0142  0.0191  0.0578  536  LEU A CA  
3923  C C   . LEU A 538  ? 0.2673 0.3041 0.2564 0.0161  0.0196  0.0520  536  LEU A C   
3924  O O   . LEU A 538  ? 0.2753 0.3123 0.2628 0.0165  0.0189  0.0517  536  LEU A O   
3925  C CB  . LEU A 538  ? 0.2634 0.3110 0.2583 0.0140  0.0200  0.0628  536  LEU A CB  
3926  C CG  . LEU A 538  ? 0.2804 0.3294 0.2809 0.0121  0.0198  0.0686  536  LEU A CG  
3927  C CD1 . LEU A 538  ? 0.3423 0.4034 0.3424 0.0118  0.0207  0.0738  536  LEU A CD1 
3928  C CD2 . LEU A 538  ? 0.2999 0.3446 0.3012 0.0122  0.0205  0.0654  536  LEU A CD2 
3929  N N   . PRO A 539  ? 0.2574 0.2936 0.2437 0.0174  0.0206  0.0473  537  PRO A N   
3930  C CA  . PRO A 539  ? 0.2653 0.3010 0.2471 0.0192  0.0208  0.0416  537  PRO A CA  
3931  C C   . PRO A 539  ? 0.2511 0.2951 0.2296 0.0203  0.0211  0.0421  537  PRO A C   
3932  O O   . PRO A 539  ? 0.2690 0.3112 0.2452 0.0211  0.0204  0.0392  537  PRO A O   
3933  C CB  . PRO A 539  ? 0.2582 0.2938 0.2388 0.0202  0.0218  0.0377  537  PRO A CB  
3934  C CG  . PRO A 539  ? 0.2600 0.2908 0.2447 0.0186  0.0216  0.0400  537  PRO A CG  
3935  C CD  . PRO A 539  ? 0.2619 0.2963 0.2500 0.0170  0.0213  0.0465  537  PRO A CD  
3936  N N   . ALA A 540  ? 0.2676 0.3211 0.2461 0.0202  0.0219  0.0461  538  ALA A N   
3937  C CA  . ALA A 540  ? 0.3010 0.3637 0.2763 0.0213  0.0222  0.0468  538  ALA A CA  
3938  C C   . ALA A 540  ? 0.3250 0.3863 0.3013 0.0203  0.0208  0.0501  538  ALA A C   
3939  O O   . ALA A 540  ? 0.3197 0.3868 0.2929 0.0213  0.0207  0.0495  538  ALA A O   
3940  C CB  . ALA A 540  ? 0.3028 0.3768 0.2782 0.0212  0.0234  0.0511  538  ALA A CB  
3941  N N   . GLU A 541  ? 0.2877 0.3417 0.2684 0.0186  0.0197  0.0532  539  GLU A N   
3942  C CA  . GLU A 541  ? 0.3074 0.3607 0.2901 0.0175  0.0182  0.0572  539  GLU A CA  
3943  C C   . GLU A 541  ? 0.3001 0.3435 0.2832 0.0176  0.0170  0.0534  539  GLU A C   
3944  O O   . GLU A 541  ? 0.2863 0.3270 0.2724 0.0166  0.0156  0.0564  539  GLU A O   
3945  C CB  . GLU A 541  ? 0.3089 0.3631 0.2975 0.0154  0.0175  0.0644  539  GLU A CB  
3946  C CG  . GLU A 541  ? 0.3746 0.4397 0.3630 0.0152  0.0187  0.0688  539  GLU A CG  
3947  C CD  . GLU A 541  ? 0.5331 0.5995 0.5278 0.0129  0.0178  0.0766  539  GLU A CD  
3948  O OE1 . GLU A 541  ? 0.6535 0.7163 0.6522 0.0117  0.0159  0.0800  539  GLU A OE1 
3949  O OE2 . GLU A 541  ? 0.6069 0.6780 0.6030 0.0123  0.0188  0.0792  539  GLU A OE2 
3950  N N   . LEU A 542  ? 0.2749 0.3135 0.2553 0.0188  0.0175  0.0471  540  LEU A N   
3951  C CA  . LEU A 542  ? 0.3092 0.3390 0.2899 0.0187  0.0164  0.0436  540  LEU A CA  
3952  C C   . LEU A 542  ? 0.2939 0.3248 0.2736 0.0190  0.0154  0.0440  540  LEU A C   
3953  O O   . LEU A 542  ? 0.3224 0.3469 0.3041 0.0184  0.0143  0.0434  540  LEU A O   
3954  C CB  . LEU A 542  ? 0.3200 0.3465 0.2974 0.0200  0.0170  0.0371  540  LEU A CB  
3955  C CG  . LEU A 542  ? 0.3518 0.3729 0.3308 0.0195  0.0175  0.0352  540  LEU A CG  
3956  C CD1 . LEU A 542  ? 0.3179 0.3349 0.2943 0.0206  0.0175  0.0292  540  LEU A CD1 
3957  C CD2 . LEU A 542  ? 0.3467 0.3613 0.3302 0.0179  0.0166  0.0375  540  LEU A CD2 
3958  N N   . PHE A 543  ? 0.2857 0.3248 0.2621 0.0200  0.0158  0.0448  541  PHE A N   
3959  C CA  . PHE A 543  ? 0.2991 0.3399 0.2741 0.0204  0.0148  0.0450  541  PHE A CA  
3960  C C   . PHE A 543  ? 0.3095 0.3562 0.2869 0.0194  0.0141  0.0519  541  PHE A C   
3961  O O   . PHE A 543  ? 0.3268 0.3765 0.3031 0.0197  0.0132  0.0529  541  PHE A O   
3962  C CB  . PHE A 543  ? 0.2675 0.3133 0.2372 0.0224  0.0153  0.0402  541  PHE A CB  
3963  C CG  . PHE A 543  ? 0.2871 0.3278 0.2553 0.0233  0.0158  0.0340  541  PHE A CG  
3964  C CD1 . PHE A 543  ? 0.3200 0.3512 0.2896 0.0228  0.0151  0.0313  541  PHE A CD1 
3965  C CD2 . PHE A 543  ? 0.2769 0.3225 0.2425 0.0247  0.0169  0.0309  541  PHE A CD2 
3966  C CE1 . PHE A 543  ? 0.3058 0.3324 0.2743 0.0234  0.0154  0.0262  541  PHE A CE1 
3967  C CE2 . PHE A 543  ? 0.2699 0.3104 0.2348 0.0255  0.0171  0.0255  541  PHE A CE2 
3968  C CZ  . PHE A 543  ? 0.2750 0.3059 0.2413 0.0248  0.0163  0.0234  541  PHE A CZ  
3969  N N   . GLY A 544  ? 0.2939 0.3426 0.2750 0.0180  0.0143  0.0569  542  GLY A N   
3970  C CA  . GLY A 544  ? 0.3277 0.3812 0.3123 0.0167  0.0132  0.0642  542  GLY A CA  
3971  C C   . GLY A 544  ? 0.3514 0.4161 0.3321 0.0175  0.0136  0.0663  542  GLY A C   
3972  O O   . GLY A 544  ? 0.3186 0.3904 0.2950 0.0187  0.0151  0.0640  542  GLY A O   
3973  N N   . ASP A 545  ? 0.3483 0.4151 0.3308 0.0168  0.0121  0.0704  543  ASP A N   
3974  C CA  . ASP A 545  ? 0.3983 0.4766 0.3776 0.0173  0.0122  0.0735  543  ASP A CA  
3975  C C   . ASP A 545  ? 0.3737 0.4550 0.3465 0.0195  0.0128  0.0669  543  ASP A C   
3976  O O   . ASP A 545  ? 0.4040 0.4963 0.3732 0.0202  0.0133  0.0680  543  ASP A O   
3977  C CB  . ASP A 545  ? 0.4396 0.5189 0.4230 0.0159  0.0101  0.0799  543  ASP A CB  
3978  C CG  . ASP A 545  ? 0.5471 0.6249 0.5379 0.0137  0.0090  0.0872  543  ASP A CG  
3979  O OD1 . ASP A 545  ? 0.5386 0.6186 0.5303 0.0131  0.0102  0.0887  543  ASP A OD1 
3980  O OD2 . ASP A 545  ? 0.6873 0.7615 0.6833 0.0125  0.0069  0.0913  543  ASP A OD2 
3981  N N   . ALA A 546  ? 0.3173 0.3896 0.2889 0.0204  0.0127  0.0603  544  ALA A N   
3982  C CA  . ALA A 546  ? 0.3586 0.4328 0.3249 0.0223  0.0129  0.0541  544  ALA A CA  
3983  C C   . ALA A 546  ? 0.3610 0.4432 0.3229 0.0240  0.0145  0.0506  544  ALA A C   
3984  O O   . ALA A 546  ? 0.3526 0.4432 0.3105 0.0253  0.0146  0.0488  544  ALA A O   
3985  C CB  . ALA A 546  ? 0.3271 0.3899 0.2937 0.0228  0.0124  0.0483  544  ALA A CB  
3986  N N   . ARG A 547  ? 0.3051 0.3852 0.2679 0.0239  0.0157  0.0494  545  ARG A N   
3987  C CA  . ARG A 547  ? 0.3236 0.4109 0.2829 0.0255  0.0172  0.0456  545  ARG A CA  
3988  C C   . ARG A 547  ? 0.2734 0.3570 0.2351 0.0249  0.0183  0.0458  545  ARG A C   
3989  O O   . ARG A 547  ? 0.2730 0.3474 0.2385 0.0234  0.0178  0.0475  545  ARG A O   
3990  C CB  . ARG A 547  ? 0.3291 0.4147 0.2849 0.0277  0.0170  0.0374  545  ARG A CB  
3991  C CG  . ARG A 547  ? 0.3496 0.4226 0.3070 0.0276  0.0166  0.0331  545  ARG A CG  
3992  C CD  . ARG A 547  ? 0.3570 0.4285 0.3116 0.0295  0.0161  0.0257  545  ARG A CD  
3993  N NE  . ARG A 547  ? 0.2993 0.3591 0.2557 0.0288  0.0152  0.0233  545  ARG A NE  
3994  C CZ  . ARG A 547  ? 0.2796 0.3321 0.2372 0.0288  0.0154  0.0197  545  ARG A CZ  
3995  N NH1 . ARG A 547  ? 0.2895 0.3445 0.2467 0.0297  0.0164  0.0176  545  ARG A NH1 
3996  N NH2 . ARG A 547  ? 0.3108 0.3537 0.2700 0.0279  0.0145  0.0184  545  ARG A NH2 
3997  N N   . THR A 548  ? 0.2642 0.3555 0.2238 0.0261  0.0197  0.0439  546  THR A N   
3998  C CA  . THR A 548  ? 0.2576 0.3471 0.2193 0.0257  0.0208  0.0441  546  THR A CA  
3999  C C   . THR A 548  ? 0.2377 0.3195 0.1984 0.0271  0.0209  0.0365  546  THR A C   
4000  O O   . THR A 548  ? 0.2453 0.3298 0.2028 0.0291  0.0208  0.0308  546  THR A O   
4001  C CB  . THR A 548  ? 0.2976 0.4002 0.2576 0.0264  0.0223  0.0459  546  THR A CB  
4002  O OG1 . THR A 548  ? 0.3486 0.4591 0.3096 0.0249  0.0220  0.0535  546  THR A OG1 
4003  C CG2 . THR A 548  ? 0.3036 0.4045 0.2659 0.0260  0.0234  0.0462  546  THR A CG2 
4004  N N   . ASN A 549  ? 0.2360 0.3082 0.1998 0.0259  0.0208  0.0366  547  ASN A N   
4005  C CA  . ASN A 549  ? 0.2433 0.3082 0.2067 0.0269  0.0207  0.0303  547  ASN A CA  
4006  C C   . ASN A 549  ? 0.2462 0.3178 0.2080 0.0287  0.0219  0.0270  547  ASN A C   
4007  O O   . ASN A 549  ? 0.2627 0.3423 0.2249 0.0284  0.0231  0.0305  547  ASN A O   
4008  C CB  . ASN A 549  ? 0.2465 0.3013 0.2136 0.0252  0.0204  0.0319  547  ASN A CB  
4009  C CG  . ASN A 549  ? 0.2526 0.2988 0.2195 0.0258  0.0200  0.0261  547  ASN A CG  
4010  O OD1 . ASN A 549  ? 0.2532 0.2993 0.2178 0.0273  0.0196  0.0211  547  ASN A OD1 
4011  N ND2 . ASN A 549  ? 0.2486 0.2878 0.2184 0.0245  0.0200  0.0269  547  ASN A ND2 
4012  N N   . SER A 550  ? 0.2554 0.3245 0.2159 0.0304  0.0216  0.0202  548  SER A N   
4013  C CA  . SER A 550  ? 0.2491 0.3232 0.2090 0.0322  0.0224  0.0164  548  SER A CA  
4014  C C   . SER A 550  ? 0.2315 0.3010 0.1943 0.0310  0.0231  0.0182  548  SER A C   
4015  O O   . SER A 550  ? 0.2489 0.3091 0.2140 0.0293  0.0226  0.0202  548  SER A O   
4016  C CB  . SER A 550  ? 0.2263 0.2968 0.1854 0.0341  0.0214  0.0088  548  SER A CB  
4017  O OG  . SER A 550  ? 0.2468 0.3052 0.2077 0.0330  0.0204  0.0078  548  SER A OG  
4018  N N   . ALA A 551  ? 0.2557 0.3323 0.2186 0.0321  0.0243  0.0175  549  ALA A N   
4019  C CA  . ALA A 551  ? 0.2908 0.3643 0.2564 0.0312  0.0250  0.0190  549  ALA A CA  
4020  C C   . ALA A 551  ? 0.2738 0.3437 0.2401 0.0329  0.0247  0.0125  549  ALA A C   
4021  O O   . ALA A 551  ? 0.2695 0.3446 0.2343 0.0352  0.0245  0.0073  549  ALA A O   
4022  C CB  . ALA A 551  ? 0.2979 0.3822 0.2638 0.0310  0.0266  0.0232  549  ALA A CB  
4023  N N   . GLY A 552  ? 0.2605 0.3216 0.2293 0.0317  0.0244  0.0128  550  GLY A N   
4024  C CA  . GLY A 552  ? 0.2663 0.3239 0.2364 0.0329  0.0240  0.0078  550  GLY A CA  
4025  C C   . GLY A 552  ? 0.2762 0.3384 0.2481 0.0331  0.0252  0.0090  550  GLY A C   
4026  O O   . GLY A 552  ? 0.2716 0.3423 0.2432 0.0328  0.0266  0.0128  550  GLY A O   
4027  N N   . LEU A 553  ? 0.2787 0.3356 0.2526 0.0336  0.0247  0.0058  551  LEU A N   
4028  C CA  . LEU A 553  ? 0.2468 0.3071 0.2227 0.0339  0.0257  0.0063  551  LEU A CA  
4029  C C   . LEU A 553  ? 0.2748 0.3250 0.2534 0.0323  0.0250  0.0070  551  LEU A C   
4030  O O   . LEU A 553  ? 0.2982 0.3402 0.2772 0.0321  0.0236  0.0044  551  LEU A O   
4031  C CB  . LEU A 553  ? 0.2883 0.3543 0.2645 0.0368  0.0256  0.0002  551  LEU A CB  
4032  C CG  . LEU A 553  ? 0.2867 0.3648 0.2603 0.0387  0.0265  -0.0013 551  LEU A CG  
4033  C CD1 . LEU A 553  ? 0.3530 0.4355 0.3276 0.0418  0.0260  -0.0084 551  LEU A CD1 
4034  C CD2 . LEU A 553  ? 0.2892 0.3766 0.2624 0.0377  0.0284  0.0045  551  LEU A CD2 
4035  N N   . ASP A 554  ? 0.2416 0.2929 0.2222 0.0312  0.0260  0.0105  552  ASP A N   
4036  C CA  . ASP A 554  ? 0.2686 0.3111 0.2517 0.0296  0.0253  0.0116  552  ASP A CA  
4037  C C   . ASP A 554  ? 0.2463 0.2884 0.2313 0.0311  0.0250  0.0075  552  ASP A C   
4038  O O   . ASP A 554  ? 0.2356 0.2836 0.2219 0.0317  0.0261  0.0081  552  ASP A O   
4039  C CB  . ASP A 554  ? 0.2431 0.2864 0.2278 0.0274  0.0262  0.0176  552  ASP A CB  
4040  C CG  . ASP A 554  ? 0.2664 0.3010 0.2537 0.0257  0.0255  0.0186  552  ASP A CG  
4041  O OD1 . ASP A 554  ? 0.2923 0.3206 0.2797 0.0261  0.0244  0.0150  552  ASP A OD1 
4042  O OD2 . ASP A 554  ? 0.3010 0.3350 0.2901 0.0238  0.0259  0.0231  552  ASP A OD2 
4043  N N   . LEU A 555  ? 0.2406 0.2760 0.2261 0.0316  0.0234  0.0035  553  LEU A N   
4044  C CA  . LEU A 555  ? 0.2449 0.2795 0.2329 0.0331  0.0227  -0.0004 553  LEU A CA  
4045  C C   . LEU A 555  ? 0.2425 0.2722 0.2332 0.0315  0.0226  0.0020  553  LEU A C   
4046  O O   . LEU A 555  ? 0.2775 0.3054 0.2705 0.0325  0.0218  -0.0008 553  LEU A O   
4047  C CB  . LEU A 555  ? 0.2637 0.2935 0.2521 0.0343  0.0208  -0.0053 553  LEU A CB  
4048  C CG  . LEU A 555  ? 0.2669 0.3021 0.2531 0.0361  0.0207  -0.0083 553  LEU A CG  
4049  C CD1 . LEU A 555  ? 0.3401 0.3707 0.3277 0.0374  0.0185  -0.0134 553  LEU A CD1 
4050  C CD2 . LEU A 555  ? 0.3007 0.3471 0.2866 0.0383  0.0221  -0.0097 553  LEU A CD2 
4051  N N   . SER A 556  ? 0.2322 0.2597 0.2227 0.0292  0.0233  0.0069  554  SER A N   
4052  C CA  . SER A 556  ? 0.2662 0.2908 0.2592 0.0278  0.0234  0.0093  554  SER A CA  
4053  C C   . SER A 556  ? 0.2609 0.2929 0.2548 0.0276  0.0251  0.0124  554  SER A C   
4054  O O   . SER A 556  ? 0.2834 0.3139 0.2797 0.0265  0.0253  0.0146  554  SER A O   
4055  C CB  . SER A 556  ? 0.2717 0.2886 0.2647 0.0252  0.0227  0.0122  554  SER A CB  
4056  O OG  . SER A 556  ? 0.2984 0.3178 0.2908 0.0239  0.0237  0.0164  554  SER A OG  
4057  N N   . ASN A 557  ? 0.2446 0.2851 0.2370 0.0287  0.0263  0.0129  555  ASN A N   
4058  C CA  . ASN A 557  ? 0.2362 0.2850 0.2295 0.0284  0.0279  0.0165  555  ASN A CA  
4059  C C   . ASN A 557  ? 0.2433 0.2992 0.2375 0.0309  0.0286  0.0130  555  ASN A C   
4060  O O   . ASN A 557  ? 0.2424 0.3027 0.2351 0.0332  0.0285  0.0087  555  ASN A O   
4061  C CB  . ASN A 557  ? 0.2619 0.3167 0.2528 0.0281  0.0287  0.0195  555  ASN A CB  
4062  C CG  . ASN A 557  ? 0.2459 0.3098 0.2379 0.0275  0.0303  0.0242  555  ASN A CG  
4063  O OD1 . ASN A 557  ? 0.2823 0.3534 0.2752 0.0288  0.0313  0.0230  555  ASN A OD1 
4064  N ND2 . ASN A 557  ? 0.2720 0.3358 0.2645 0.0253  0.0305  0.0298  555  ASN A ND2 
4065  N N   . GLU A 558  ? 0.2373 0.2945 0.2343 0.0304  0.0291  0.0144  556  GLU A N   
4066  C CA  . GLU A 558  ? 0.2709 0.3344 0.2695 0.0328  0.0296  0.0107  556  GLU A CA  
4067  C C   . GLU A 558  ? 0.2512 0.3274 0.2481 0.0345  0.0312  0.0103  556  GLU A C   
4068  O O   . GLU A 558  ? 0.2694 0.3511 0.2665 0.0372  0.0312  0.0052  556  GLU A O   
4069  C CB  . GLU A 558  ? 0.2877 0.3506 0.2897 0.0319  0.0299  0.0127  556  GLU A CB  
4070  C CG  . GLU A 558  ? 0.2893 0.3412 0.2931 0.0307  0.0282  0.0120  556  GLU A CG  
4071  C CD  . GLU A 558  ? 0.2943 0.3422 0.2989 0.0328  0.0266  0.0061  556  GLU A CD  
4072  O OE1 . GLU A 558  ? 0.2600 0.3136 0.2645 0.0354  0.0267  0.0018  556  GLU A OE1 
4073  O OE2 . GLU A 558  ? 0.2871 0.3260 0.2929 0.0316  0.0250  0.0059  556  GLU A OE2 
4074  N N   . GLU A 559  ? 0.2354 0.3167 0.2312 0.0329  0.0324  0.0158  557  GLU A N   
4075  C CA  . GLU A 559  ? 0.2554 0.3496 0.2492 0.0343  0.0339  0.0160  557  GLU A CA  
4076  C C   . GLU A 559  ? 0.2301 0.3253 0.2208 0.0363  0.0332  0.0111  557  GLU A C   
4077  O O   . GLU A 559  ? 0.2688 0.3731 0.2586 0.0389  0.0338  0.0069  557  GLU A O   
4078  C CB  . GLU A 559  ? 0.3060 0.4045 0.2994 0.0318  0.0350  0.0235  557  GLU A CB  
4079  C CG  . GLU A 559  ? 0.3251 0.4252 0.3219 0.0298  0.0358  0.0289  557  GLU A CG  
4080  C CD  . GLU A 559  ? 0.4485 0.5507 0.4458 0.0270  0.0361  0.0366  557  GLU A CD  
4081  O OE1 . GLU A 559  ? 0.4867 0.5900 0.4814 0.0269  0.0359  0.0376  557  GLU A OE1 
4082  O OE2 . GLU A 559  ? 0.4796 0.5822 0.4803 0.0250  0.0364  0.0416  557  GLU A OE2 
4083  N N   . THR A 560  ? 0.2444 0.3304 0.2337 0.0352  0.0319  0.0114  558  THR A N   
4084  C CA  . THR A 560  ? 0.2511 0.3371 0.2377 0.0369  0.0310  0.0069  558  THR A CA  
4085  C C   . THR A 560  ? 0.2291 0.3133 0.2171 0.0396  0.0299  -0.0005 558  THR A C   
4086  O O   . THR A 560  ? 0.2684 0.3592 0.2552 0.0421  0.0298  -0.0053 558  THR A O   
4087  C CB  . THR A 560  ? 0.2552 0.3310 0.2405 0.0349  0.0298  0.0089  558  THR A CB  
4088  O OG1 . THR A 560  ? 0.2931 0.3710 0.2779 0.0326  0.0306  0.0156  558  THR A OG1 
4089  C CG2 . THR A 560  ? 0.2699 0.3454 0.2527 0.0366  0.0288  0.0043  558  THR A CG2 
4090  N N   . LEU A 561  ? 0.2479 0.3236 0.2388 0.0390  0.0288  -0.0015 559  LEU A N   
4091  C CA  . LEU A 561  ? 0.2142 0.2876 0.2075 0.0414  0.0273  -0.0080 559  LEU A CA  
4092  C C   . LEU A 561  ? 0.2333 0.3180 0.2279 0.0441  0.0284  -0.0115 559  LEU A C   
4093  O O   . LEU A 561  ? 0.2639 0.3514 0.2594 0.0470  0.0274  -0.0179 559  LEU A O   
4094  C CB  . LEU A 561  ? 0.2193 0.2822 0.2156 0.0400  0.0260  -0.0074 559  LEU A CB  
4095  C CG  . LEU A 561  ? 0.2325 0.2844 0.2278 0.0379  0.0246  -0.0057 559  LEU A CG  
4096  C CD1 . LEU A 561  ? 0.2481 0.2913 0.2463 0.0365  0.0235  -0.0047 559  LEU A CD1 
4097  C CD2 . LEU A 561  ? 0.2444 0.2937 0.2387 0.0394  0.0230  -0.0105 559  LEU A CD2 
4098  N N   . ALA A 562  ? 0.2659 0.3574 0.2612 0.0434  0.0302  -0.0076 560  ALA A N   
4099  C CA  . ALA A 562  ? 0.2645 0.3677 0.2611 0.0459  0.0314  -0.0108 560  ALA A CA  
4100  C C   . ALA A 562  ? 0.2630 0.3776 0.2565 0.0479  0.0323  -0.0132 560  ALA A C   
4101  O O   . ALA A 562  ? 0.2613 0.3827 0.2557 0.0511  0.0320  -0.0197 560  ALA A O   
4102  C CB  . ALA A 562  ? 0.2709 0.3790 0.2689 0.0443  0.0332  -0.0053 560  ALA A CB  
4103  N N   . SER A 563  ? 0.2777 0.3947 0.2677 0.0461  0.0332  -0.0081 561  SER A N   
4104  C CA  A SER A 563  ? 0.2940 0.4222 0.2807 0.0477  0.0340  -0.0098 561  SER A CA  
4105  C CA  B SER A 563  ? 0.2940 0.4223 0.2807 0.0477  0.0340  -0.0100 561  SER A CA  
4106  C C   . SER A 563  ? 0.2762 0.4003 0.2621 0.0498  0.0321  -0.0167 561  SER A C   
4107  O O   . SER A 563  ? 0.2971 0.4306 0.2821 0.0527  0.0321  -0.0221 561  SER A O   
4108  C CB  A SER A 563  ? 0.2955 0.4258 0.2792 0.0449  0.0351  -0.0022 561  SER A CB  
4109  C CB  B SER A 563  ? 0.2958 0.4274 0.2796 0.0451  0.0352  -0.0023 561  SER A CB  
4110  O OG  A SER A 563  ? 0.3305 0.4706 0.3107 0.0463  0.0356  -0.0036 561  SER A OG  
4111  O OG  B SER A 563  ? 0.3398 0.4592 0.3227 0.0429  0.0339  0.0001  561  SER A OG  
4112  N N   . LEU A 564  ? 0.2833 0.3938 0.2697 0.0484  0.0302  -0.0165 562  LEU A N   
4113  C CA  . LEU A 564  ? 0.2663 0.3722 0.2524 0.0501  0.0282  -0.0225 562  LEU A CA  
4114  C C   . LEU A 564  ? 0.2762 0.3830 0.2664 0.0532  0.0268  -0.0302 562  LEU A C   
4115  O O   . LEU A 564  ? 0.2905 0.4013 0.2806 0.0559  0.0257  -0.0366 562  LEU A O   
4116  C CB  . LEU A 564  ? 0.2682 0.3598 0.2543 0.0477  0.0266  -0.0201 562  LEU A CB  
4117  C CG  . LEU A 564  ? 0.3685 0.4545 0.3540 0.0485  0.0245  -0.0244 562  LEU A CG  
4118  C CD1 . LEU A 564  ? 0.3400 0.4348 0.3216 0.0495  0.0252  -0.0250 562  LEU A CD1 
4119  C CD2 . LEU A 564  ? 0.3186 0.3916 0.3040 0.0457  0.0234  -0.0207 562  LEU A CD2 
4120  N N   . THR A 565  ? 0.2493 0.3525 0.2430 0.0530  0.0267  -0.0299 563  THR A N   
4121  C CA  . THR A 565  ? 0.2601 0.3643 0.2584 0.0560  0.0253  -0.0370 563  THR A CA  
4122  C C   . THR A 565  ? 0.2498 0.3688 0.2476 0.0594  0.0263  -0.0422 563  THR A C   
4123  O O   . THR A 565  ? 0.2782 0.3990 0.2782 0.0624  0.0245  -0.0498 563  THR A O   
4124  C CB  . THR A 565  ? 0.2831 0.3836 0.2851 0.0552  0.0254  -0.0350 563  THR A CB  
4125  O OG1 . THR A 565  ? 0.2747 0.3614 0.2775 0.0524  0.0241  -0.0314 563  THR A OG1 
4126  C CG2 . THR A 565  ? 0.3253 0.4282 0.3325 0.0586  0.0240  -0.0424 563  THR A CG2 
4127  N N   . GLU A 566  ? 0.2668 0.3971 0.2619 0.0589  0.0290  -0.0382 564  GLU A N   
4128  C CA  . GLU A 566  ? 0.2677 0.4138 0.2621 0.0620  0.0302  -0.0428 564  GLU A CA  
4129  C C   . GLU A 566  ? 0.2703 0.4205 0.2615 0.0634  0.0294  -0.0464 564  GLU A C   
4130  O O   . GLU A 566  ? 0.2935 0.4504 0.2862 0.0669  0.0284  -0.0544 564  GLU A O   
4131  C CB  . GLU A 566  ? 0.3076 0.4653 0.3000 0.0607  0.0332  -0.0367 564  GLU A CB  
4132  C CG  . GLU A 566  ? 0.4084 0.5636 0.4044 0.0597  0.0339  -0.0340 564  GLU A CG  
4133  C CD  . GLU A 566  ? 0.4401 0.5947 0.4414 0.0629  0.0324  -0.0418 564  GLU A CD  
4134  O OE1 . GLU A 566  ? 0.4527 0.6182 0.4548 0.0664  0.0324  -0.0487 564  GLU A OE1 
4135  O OE2 . GLU A 566  ? 0.4758 0.6190 0.4807 0.0619  0.0310  -0.0413 564  GLU A OE2 
4136  N N   . ALA A 567  ? 0.2736 0.4197 0.2608 0.0608  0.0297  -0.0409 565  ALA A N   
4137  C CA  . ALA A 567  ? 0.2861 0.4358 0.2701 0.0619  0.0290  -0.0439 565  ALA A CA  
4138  C C   . ALA A 567  ? 0.2622 0.4035 0.2492 0.0640  0.0259  -0.0517 565  ALA A C   
4139  O O   . ALA A 567  ? 0.2783 0.4264 0.2650 0.0668  0.0250  -0.0582 565  ALA A O   
4140  C CB  . ALA A 567  ? 0.2996 0.4449 0.2794 0.0585  0.0296  -0.0362 565  ALA A CB  
4141  N N   . LEU A 568  ? 0.2551 0.3820 0.2455 0.0625  0.0241  -0.0509 566  LEU A N   
4142  C CA  . LEU A 568  ? 0.2452 0.3635 0.2394 0.0641  0.0210  -0.0574 566  LEU A CA  
4143  C C   . LEU A 568  ? 0.2584 0.3833 0.2572 0.0681  0.0198  -0.0661 566  LEU A C   
4144  O O   . LEU A 568  ? 0.2742 0.4008 0.2748 0.0708  0.0177  -0.0733 566  LEU A O   
4145  C CB  . LEU A 568  ? 0.2583 0.3610 0.2552 0.0615  0.0195  -0.0540 566  LEU A CB  
4146  C CG  . LEU A 568  ? 0.2534 0.3479 0.2463 0.0578  0.0200  -0.0467 566  LEU A CG  
4147  C CD1 . LEU A 568  ? 0.2452 0.3259 0.2411 0.0555  0.0186  -0.0438 566  LEU A CD1 
4148  C CD2 . LEU A 568  ? 0.2766 0.3705 0.2669 0.0582  0.0189  -0.0488 566  LEU A CD2 
4149  N N   . ARG A 569  ? 0.2585 0.3875 0.2599 0.0687  0.0210  -0.0656 567  ARG A N   
4150  C CA  . ARG A 569  ? 0.2812 0.4180 0.2873 0.0727  0.0201  -0.0740 567  ARG A CA  
4151  C C   . ARG A 569  ? 0.2818 0.4341 0.2851 0.0756  0.0210  -0.0790 567  ARG A C   
4152  O O   . ARG A 569  ? 0.3147 0.4704 0.3214 0.0792  0.0189  -0.0879 567  ARG A O   
4153  C CB  . ARG A 569  ? 0.3112 0.4513 0.3198 0.0726  0.0217  -0.0718 567  ARG A CB  
4154  C CG  . ARG A 569  ? 0.3283 0.4540 0.3411 0.0707  0.0201  -0.0691 567  ARG A CG  
4155  C CD  . ARG A 569  ? 0.3905 0.5200 0.4054 0.0705  0.0218  -0.0665 567  ARG A CD  
4156  N NE  . ARG A 569  ? 0.4270 0.5431 0.4451 0.0681  0.0205  -0.0628 567  ARG A NE  
4157  C CZ  . ARG A 569  ? 0.4865 0.6024 0.5059 0.0668  0.0218  -0.0588 567  ARG A CZ  
4158  N NH1 . ARG A 569  ? 0.5607 0.6890 0.5789 0.0675  0.0245  -0.0576 567  ARG A NH1 
4159  N NH2 . ARG A 569  ? 0.5439 0.6475 0.5662 0.0648  0.0203  -0.0557 567  ARG A NH2 
4160  N N   . GLU A 570  ? 0.2663 0.4281 0.2636 0.0742  0.0240  -0.0734 568  GLU A N   
4161  C CA  . GLU A 570  ? 0.2783 0.4560 0.2723 0.0767  0.0251  -0.0774 568  GLU A CA  
4162  C C   . GLU A 570  ? 0.3554 0.5302 0.3484 0.0778  0.0228  -0.0821 568  GLU A C   
4163  O O   . GLU A 570  ? 0.3310 0.5165 0.3244 0.0812  0.0221  -0.0898 568  GLU A O   
4164  C CB  . GLU A 570  ? 0.3197 0.5074 0.3079 0.0743  0.0285  -0.0690 568  GLU A CB  
4165  C CG  . GLU A 570  ? 0.3774 0.5724 0.3670 0.0739  0.0309  -0.0657 568  GLU A CG  
4166  C CD  . GLU A 570  ? 0.4652 0.6668 0.4500 0.0707  0.0339  -0.0557 568  GLU A CD  
4167  O OE1 . GLU A 570  ? 0.5515 0.7481 0.5326 0.0681  0.0339  -0.0502 568  GLU A OE1 
4168  O OE2 . GLU A 570  ? 0.6050 0.8170 0.5901 0.0707  0.0361  -0.0533 568  GLU A OE2 
4169  N N   . SER A 571  ? 0.3047 0.4656 0.2967 0.0749  0.0215  -0.0779 569  SER A N   
4170  C CA  . SER A 571  ? 0.3148 0.4722 0.3062 0.0758  0.0192  -0.0822 569  SER A CA  
4171  C C   . SER A 571  ? 0.2919 0.4454 0.2900 0.0791  0.0158  -0.0920 569  SER A C   
4172  O O   . SER A 571  ? 0.3160 0.4734 0.3146 0.0815  0.0140  -0.0987 569  SER A O   
4173  C CB  . SER A 571  ? 0.2737 0.4169 0.2630 0.0720  0.0186  -0.0754 569  SER A CB  
4174  O OG  . SER A 571  ? 0.3108 0.4394 0.3052 0.0710  0.0164  -0.0756 569  SER A OG  
4175  N N   . ALA A 572  ? 0.3078 0.4538 0.3117 0.0793  0.0146  -0.0931 570  ALA A N   
4176  C CA  . ALA A 572  ? 0.3213 0.4632 0.3327 0.0824  0.0110  -0.1021 570  ALA A CA  
4177  C C   . ALA A 572  ? 0.3538 0.5107 0.3676 0.0870  0.0111  -0.1110 570  ALA A C   
4178  O O   . ALA A 572  ? 0.3944 0.5500 0.4147 0.0901  0.0078  -0.1198 570  ALA A O   
4179  C CB  . ALA A 572  ? 0.3684 0.4974 0.3855 0.0810  0.0095  -0.1000 570  ALA A CB  
4180  N N   . ALA A 573  ? 0.3383 0.5097 0.3477 0.0874  0.0145  -0.1090 571  ALA A N   
4181  C CA  . ALA A 573  ? 0.3778 0.5659 0.3886 0.0918  0.0150  -0.1173 571  ALA A CA  
4182  C C   . ALA A 573  ? 0.4300 0.6278 0.4360 0.0921  0.0147  -0.1191 571  ALA A C   
4183  O O   . ALA A 573  ? 0.4302 0.6396 0.4369 0.0936  0.0138  -0.1236 571  ALA A O   
4184  C CB  . ALA A 573  ? 0.3559 0.5548 0.3651 0.0915  0.0185  -0.1134 571  ALA A CB  
4185  N N   . MET A 574  ? 0.3601 0.5535 0.3613 0.0905  0.0152  -0.1156 572  MET A N   
4186  C CA  . MET A 574  ? 0.3841 0.5860 0.3809 0.0905  0.0147  -0.1168 572  MET A CA  
4187  C C   . MET A 574  ? 0.4199 0.6166 0.4219 0.0925  0.0100  -0.1254 572  MET A C   
4188  O O   . MET A 574  ? 0.3460 0.5293 0.3536 0.0929  0.0074  -0.1283 572  MET A O   
4189  C CB  . MET A 574  ? 0.4067 0.6062 0.3963 0.0877  0.0170  -0.1087 572  MET A CB  
4190  C CG  . MET A 574  ? 0.3875 0.5930 0.3723 0.0849  0.0210  -0.0989 572  MET A CG  
4191  S SD  . MET A 574  ? 0.4225 0.6206 0.4007 0.0799  0.0224  -0.0870 572  MET A SD  
4192  C CE  . MET A 574  ? 0.4924 0.6989 0.4675 0.0773  0.0265  -0.0773 572  MET A CE  
4193  N N   . LYS A 575  ? 0.4073 0.6153 0.4081 0.0936  0.0087  -0.1295 573  LYS A N   
4194  C CA  . LYS A 575  ? 0.3838 0.5892 0.3898 0.0955  0.0042  -0.1380 573  LYS A CA  
4195  C C   . LYS A 575  ? 0.3774 0.5779 0.3796 0.0943  0.0036  -0.1364 573  LYS A C   
4196  O O   . LYS A 575  ? 0.3788 0.5886 0.3778 0.0947  0.0031  -0.1377 573  LYS A O   
4197  C CB  . LYS A 575  ? 0.4092 0.6297 0.4168 0.0977  0.0029  -0.1440 573  LYS A CB  
4198  N N   . TRP A 576  ? 0.3359 0.5217 0.3388 0.0930  0.0034  -0.1334 574  TRP A N   
4199  C CA  . TRP A 576  ? 0.2928 0.4726 0.2919 0.0916  0.0031  -0.1312 574  TRP A CA  
4200  C C   . TRP A 576  ? 0.2603 0.4389 0.2640 0.0932  -0.0014 -0.1388 574  TRP A C   
4201  O O   . TRP A 576  ? 0.3012 0.4732 0.3131 0.0946  -0.0050 -0.1449 574  TRP A O   
4202  C CB  . TRP A 576  ? 0.2996 0.4633 0.2999 0.0898  0.0033  -0.1268 574  TRP A CB  
4203  C CG  . TRP A 576  ? 0.2921 0.4535 0.2885 0.0864  0.0067  -0.1166 574  TRP A CG  
4204  C CD1 . TRP A 576  ? 0.2613 0.4159 0.2615 0.0855  0.0071  -0.1140 574  TRP A CD1 
4205  C CD2 . TRP A 576  ? 0.2707 0.4364 0.2593 0.0835  0.0100  -0.1075 574  TRP A CD2 
4206  N NE1 . TRP A 576  ? 0.3023 0.4569 0.2974 0.0822  0.0104  -0.1042 574  TRP A NE1 
4207  C CE2 . TRP A 576  ? 0.2694 0.4305 0.2576 0.0809  0.0122  -0.1000 574  TRP A CE2 
4208  C CE3 . TRP A 576  ? 0.2669 0.4399 0.2491 0.0827  0.0112  -0.1050 574  TRP A CE3 
4209  C CZ2 . TRP A 576  ? 0.2970 0.4602 0.2791 0.0776  0.0153  -0.0903 574  TRP A CZ2 
4210  C CZ3 . TRP A 576  ? 0.2789 0.4540 0.2551 0.0794  0.0143  -0.0950 574  TRP A CZ3 
4211  C CH2 . TRP A 576  ? 0.3371 0.5073 0.3135 0.0769  0.0163  -0.0878 574  TRP A CH2 
4212  N N   . THR A 577  ? 0.2714 0.4562 0.2702 0.0928  -0.0013 -0.1383 575  THR A N   
4213  C CA  . THR A 577  ? 0.2986 0.4819 0.3013 0.0940  -0.0054 -0.1450 575  THR A CA  
4214  C C   . THR A 577  ? 0.3186 0.4983 0.3159 0.0923  -0.0049 -0.1413 575  THR A C   
4215  O O   . THR A 577  ? 0.3082 0.4904 0.2979 0.0905  -0.0013 -0.1339 575  THR A O   
4216  C CB  . THR A 577  ? 0.3053 0.5038 0.3095 0.0963  -0.0069 -0.1511 575  THR A CB  
4217  O OG1 . THR A 577  ? 0.3337 0.5456 0.3297 0.0954  -0.0037 -0.1464 575  THR A OG1 
4218  C CG2 . THR A 577  ? 0.3299 0.5326 0.3398 0.0981  -0.0077 -0.1553 575  THR A CG2 
4219  N N   . ALA A 578  ? 0.2953 0.4689 0.2970 0.0930  -0.0088 -0.1465 576  ALA A N   
4220  C CA  . ALA A 578  ? 0.2700 0.4412 0.2676 0.0918  -0.0092 -0.1446 576  ALA A CA  
4221  C C   . ALA A 578  ? 0.3260 0.5036 0.3276 0.0937  -0.0129 -0.1522 576  ALA A C   
4222  O O   . ALA A 578  ? 0.3050 0.4778 0.3151 0.0952  -0.0168 -0.1588 576  ALA A O   
4223  C CB  . ALA A 578  ? 0.2966 0.4504 0.2965 0.0903  -0.0104 -0.1428 576  ALA A CB  
4224  N N   . LEU A 579  ? 0.3040 0.4927 0.2998 0.0937  -0.0118 -0.1511 577  LEU A N   
4225  C CA  . LEU A 579  ? 0.3013 0.4984 0.3002 0.0956  -0.0150 -0.1580 577  LEU A CA  
4226  C C   . LEU A 579  ? 0.3353 0.5307 0.3299 0.0945  -0.0154 -0.1560 577  LEU A C   
4227  O O   . LEU A 579  ? 0.3019 0.4948 0.2893 0.0923  -0.0123 -0.1485 577  LEU A O   
4228  C CB  . LEU A 579  ? 0.2948 0.5104 0.2912 0.0971  -0.0136 -0.1593 577  LEU A CB  
4229  C CG  . LEU A 579  ? 0.3629 0.5832 0.3616 0.0981  -0.0123 -0.1600 577  LEU A CG  
4230  C CD1 . LEU A 579  ? 0.3684 0.6079 0.3645 0.0995  -0.0113 -0.1614 577  LEU A CD1 
4231  C CD2 . LEU A 579  ? 0.3994 0.6114 0.4083 0.0998  -0.0162 -0.1673 577  LEU A CD2 
4232  N N   . PRO A 580  ? 0.3133 0.5102 0.3125 0.0959  -0.0192 -0.1625 578  PRO A N   
4233  C CA  . PRO A 580  ? 0.2850 0.4834 0.2797 0.0950  -0.0194 -0.1609 578  PRO A CA  
4234  C C   . PRO A 580  ? 0.3731 0.5879 0.3601 0.0949  -0.0163 -0.1570 578  PRO A C   
4235  O O   . PRO A 580  ? 0.3743 0.6027 0.3628 0.0969  -0.0172 -0.1616 578  PRO A O   
4236  C CB  . PRO A 580  ? 0.3727 0.5712 0.3755 0.0971  -0.0243 -0.1697 578  PRO A CB  
4237  C CG  . PRO A 580  ? 0.3413 0.5335 0.3533 0.0984  -0.0270 -0.1750 578  PRO A CG  
4238  C CD  . PRO A 580  ? 0.3303 0.5280 0.3392 0.0984  -0.0235 -0.1716 578  PRO A CD  
4239  N N   . GLN A 581  ? 0.2792 0.4929 0.2582 0.0925  -0.0127 -0.1484 579  GLN A N   
4240  C CA  . GLN A 581  ? 0.3116 0.5399 0.2831 0.0918  -0.0096 -0.1430 579  GLN A CA  
4241  C C   . GLN A 581  ? 0.3276 0.5586 0.2955 0.0912  -0.0104 -0.1419 579  GLN A C   
4242  O O   . GLN A 581  ? 0.3209 0.5464 0.2833 0.0889  -0.0087 -0.1353 579  GLN A O   
4243  C CB  . GLN A 581  ? 0.2925 0.5184 0.2582 0.0895  -0.0054 -0.1337 579  GLN A CB  
4244  C CG  . GLN A 581  ? 0.3087 0.5324 0.2777 0.0900  -0.0043 -0.1343 579  GLN A CG  
4245  C CD  . GLN A 581  ? 0.3403 0.5801 0.3101 0.0917  -0.0038 -0.1368 579  GLN A CD  
4246  O OE1 . GLN A 581  ? 0.3598 0.6128 0.3277 0.0924  -0.0042 -0.1380 579  GLN A OE1 
4247  N NE2 . GLN A 581  ? 0.3284 0.5675 0.3012 0.0923  -0.0029 -0.1375 579  GLN A NE2 
4248  N N   . LEU A 582  ? 0.3288 0.5685 0.3001 0.0933  -0.0132 -0.1488 580  LEU A N   
4249  C CA  . LEU A 582  ? 0.3501 0.5944 0.3183 0.0930  -0.0141 -0.1483 580  LEU A CA  
4250  C C   . LEU A 582  ? 0.3263 0.5855 0.2871 0.0920  -0.0109 -0.1415 580  LEU A C   
4251  O O   . LEU A 582  ? 0.3722 0.6395 0.3310 0.0918  -0.0084 -0.1382 580  LEU A O   
4252  C CB  . LEU A 582  ? 0.3194 0.5682 0.2944 0.0958  -0.0183 -0.1581 580  LEU A CB  
4253  C CG  . LEU A 582  ? 0.4351 0.6687 0.4169 0.0961  -0.0221 -0.1634 580  LEU A CG  
4254  C CD1 . LEU A 582  ? 0.4144 0.6360 0.4018 0.0962  -0.0228 -0.1652 580  LEU A CD1 
4255  C CD2 . LEU A 582  ? 0.4677 0.7076 0.4557 0.0987  -0.0261 -0.1724 580  LEU A CD2 
4256  N N   . ALA A 583  ? 0.3248 0.5876 0.2817 0.0912  -0.0111 -0.1391 581  ALA A N   
4257  C CA  . ALA A 583  ? 0.3245 0.6015 0.2750 0.0900  -0.0085 -0.1323 581  ALA A CA  
4258  C C   . ALA A 583  ? 0.3600 0.6547 0.3125 0.0922  -0.0087 -0.1363 581  ALA A C   
4259  O O   . ALA A 583  ? 0.4576 0.7645 0.4058 0.0912  -0.0061 -0.1302 581  ALA A O   
4260  C CB  . ALA A 583  ? 0.3245 0.6024 0.2716 0.0891  -0.0093 -0.1302 581  ALA A CB  
4261  N N   . THR A 584  ? 0.3414 0.6378 0.3007 0.0951  -0.0119 -0.1463 582  THR A N   
4262  C CA  . THR A 584  ? 0.4118 0.7251 0.3740 0.0976  -0.0127 -0.1517 582  THR A CA  
4263  C C   . THR A 584  ? 0.4469 0.7618 0.4120 0.0985  -0.0119 -0.1533 582  THR A C   
4264  O O   . THR A 584  ? 0.4453 0.7745 0.4129 0.1006  -0.0124 -0.1578 582  THR A O   
4265  C CB  . THR A 584  ? 0.4289 0.7435 0.3977 0.1004  -0.0170 -0.1621 582  THR A CB  
4266  O OG1 . THR A 584  ? 0.4552 0.7527 0.4298 0.1008  -0.0195 -0.1668 582  THR A OG1 
4267  C CG2 . THR A 584  ? 0.4156 0.7334 0.3813 0.0999  -0.0178 -0.1609 582  THR A CG2 
4268  N N   . GLY A 585  ? 0.4080 0.7091 0.3731 0.0970  -0.0105 -0.1500 583  GLY A N   
4269  C CA  . GLY A 585  ? 0.3983 0.6994 0.3664 0.0978  -0.0097 -0.1515 583  GLY A CA  
4270  C C   . GLY A 585  ? 0.4227 0.7077 0.3975 0.0987  -0.0122 -0.1572 583  GLY A C   
4271  O O   . GLY A 585  ? 0.4164 0.6908 0.3940 0.0988  -0.0148 -0.1605 583  GLY A O   
4272  N N   . PRO A 586  ? 0.3893 0.6723 0.3672 0.0993  -0.0116 -0.1584 584  PRO A N   
4273  C CA  . PRO A 586  ? 0.3684 0.6363 0.3534 0.1000  -0.0141 -0.1635 584  PRO A CA  
4274  C C   . PRO A 586  ? 0.4494 0.7181 0.4423 0.1027  -0.0189 -0.1737 584  PRO A C   
4275  O O   . PRO A 586  ? 0.4110 0.6943 0.4056 0.1048  -0.0202 -0.1787 584  PRO A O   
4276  C CB  . PRO A 586  ? 0.4410 0.7118 0.4278 0.1006  -0.0126 -0.1634 584  PRO A CB  
4277  C CG  . PRO A 586  ? 0.4678 0.7523 0.4472 0.0993  -0.0087 -0.1561 584  PRO A CG  
4278  C CD  . PRO A 586  ? 0.4163 0.7120 0.3921 0.0995  -0.0090 -0.1558 584  PRO A CD  
4279  N N   . ALA A 587  ? 0.3873 0.6403 0.3855 0.1025  -0.0216 -0.1766 585  ALA A N   
4280  C CA  . ALA A 587  ? 0.4169 0.6685 0.4235 0.1048  -0.0265 -0.1858 585  ALA A CA  
4281  C C   . ALA A 587  ? 0.4402 0.6832 0.4559 0.1060  -0.0292 -0.1911 585  ALA A C   
4282  O O   . ALA A 587  ? 0.4236 0.6565 0.4390 0.1046  -0.0275 -0.1871 585  ALA A O   
4283  C CB  . ALA A 587  ? 0.4385 0.6794 0.4451 0.1035  -0.0283 -0.1851 585  ALA A CB  
4284  N N   . ALA A 588  ? 0.4410 0.6886 0.4651 0.1087  -0.0333 -0.2002 586  ALA A N   
4285  C CA  . ALA A 588  ? 0.4185 0.6580 0.4523 0.1099  -0.0364 -0.2055 586  ALA A CA  
4286  C C   . ALA A 588  ? 0.4219 0.6431 0.4611 0.1086  -0.0393 -0.2056 586  ALA A C   
4287  O O   . ALA A 588  ? 0.4760 0.6925 0.5128 0.1074  -0.0398 -0.2037 586  ALA A O   
4288  C CB  . ALA A 588  ? 0.3888 0.6402 0.4303 0.1133  -0.0401 -0.2154 586  ALA A CB  
4289  N N   . GLY A 589  ? 0.4042 0.6152 0.4511 0.1087  -0.0415 -0.2078 587  GLY A N   
4290  C CA  . GLY A 589  ? 0.4030 0.5969 0.4562 0.1074  -0.0445 -0.2076 587  GLY A CA  
4291  C C   . GLY A 589  ? 0.4402 0.6250 0.5013 0.1075  -0.0463 -0.2090 587  GLY A C   
4292  O O   . GLY A 589  ? 0.4460 0.6383 0.5084 0.1090  -0.0455 -0.2112 587  GLY A O   
4293  N N   . GLU A 590  ? 0.4423 0.6110 0.5089 0.1059  -0.0487 -0.2076 588  GLU A N   
4294  C CA  . GLU A 590  ? 0.4350 0.5936 0.5097 0.1057  -0.0507 -0.2081 588  GLU A CA  
4295  C C   . GLU A 590  ? 0.4125 0.5679 0.4804 0.1041  -0.0460 -0.2010 588  GLU A C   
4296  O O   . GLU A 590  ? 0.3791 0.5289 0.4392 0.1018  -0.0427 -0.1939 588  GLU A O   
4297  C CB  . GLU A 590  ? 0.4512 0.5940 0.5336 0.1040  -0.0546 -0.2076 588  GLU A CB  
4298  N N   . THR A 591  ? 0.3770 0.5361 0.4481 0.1054  -0.0457 -0.2030 589  THR A N   
4299  C CA  . THR A 591  ? 0.3597 0.5178 0.4250 0.1042  -0.0413 -0.1969 589  THR A CA  
4300  C C   . THR A 591  ? 0.3689 0.5134 0.4420 0.1034  -0.0433 -0.1959 589  THR A C   
4301  O O   . THR A 591  ? 0.4010 0.5434 0.4846 0.1048  -0.0478 -0.2018 589  THR A O   
4302  C CB  . THR A 591  ? 0.4368 0.6112 0.4987 0.1063  -0.0390 -0.1994 589  THR A CB  
4303  O OG1 . THR A 591  ? 0.4170 0.6042 0.4710 0.1067  -0.0369 -0.1990 589  THR A OG1 
4304  C CG2 . THR A 591  ? 0.3717 0.5449 0.4289 0.1052  -0.0348 -0.1935 589  THR A CG2 
4305  N N   . ARG A 592  ? 0.3340 0.4695 0.4024 0.1011  -0.0401 -0.1884 590  ARG A N   
4306  C CA  . ARG A 592  ? 0.3845 0.5078 0.4595 0.1002  -0.0415 -0.1865 590  ARG A CA  
4307  C C   . ARG A 592  ? 0.3729 0.4952 0.4403 0.0989  -0.0364 -0.1795 590  ARG A C   
4308  O O   . ARG A 592  ? 0.3460 0.4744 0.4033 0.0982  -0.0321 -0.1752 590  ARG A O   
4309  C CB  . ARG A 592  ? 0.3900 0.4979 0.4706 0.0981  -0.0448 -0.1846 590  ARG A CB  
4310  C CG  . ARG A 592  ? 0.3929 0.4946 0.4649 0.0957  -0.0416 -0.1774 590  ARG A CG  
4311  C CD  . ARG A 592  ? 0.4377 0.5233 0.5156 0.0933  -0.0445 -0.1743 590  ARG A CD  
4312  N NE  . ARG A 592  ? 0.4704 0.5511 0.5404 0.0912  -0.0420 -0.1686 590  ARG A NE  
4313  C CZ  . ARG A 592  ? 0.4561 0.5333 0.5189 0.0897  -0.0378 -0.1618 590  ARG A CZ  
4314  N NH1 . ARG A 592  ? 0.4294 0.5066 0.4919 0.0899  -0.0357 -0.1596 590  ARG A NH1 
4315  N NH2 . ARG A 592  ? 0.4321 0.5058 0.4880 0.0879  -0.0358 -0.1574 590  ARG A NH2 
4316  N N   . THR A 593  ? 0.3639 0.4787 0.4367 0.0985  -0.0370 -0.1781 591  THR A N   
4317  C CA  . THR A 593  ? 0.3748 0.4879 0.4415 0.0974  -0.0324 -0.1715 591  THR A CA  
4318  C C   . THR A 593  ? 0.3682 0.4688 0.4314 0.0946  -0.0311 -0.1645 591  THR A C   
4319  O O   . THR A 593  ? 0.3793 0.4698 0.4473 0.0935  -0.0344 -0.1646 591  THR A O   
4320  C CB  . THR A 593  ? 0.3928 0.5024 0.4667 0.0980  -0.0336 -0.1725 591  THR A CB  
4321  O OG1 . THR A 593  ? 0.4003 0.4970 0.4844 0.0972  -0.0385 -0.1737 591  THR A OG1 
4322  C CG2 . THR A 593  ? 0.3688 0.4918 0.4453 0.1007  -0.0343 -0.1790 591  THR A CG2 
4323  N N   . VAL A 594  ? 0.3075 0.4095 0.3625 0.0936  -0.0262 -0.1583 592  VAL A N   
4324  C CA  . VAL A 594  ? 0.3050 0.3958 0.3567 0.0912  -0.0245 -0.1514 592  VAL A CA  
4325  C C   . VAL A 594  ? 0.3280 0.4127 0.3830 0.0908  -0.0237 -0.1483 592  VAL A C   
4326  O O   . VAL A 594  ? 0.3261 0.4191 0.3786 0.0918  -0.0209 -0.1479 592  VAL A O   
4327  C CB  . VAL A 594  ? 0.2924 0.3896 0.3324 0.0902  -0.0197 -0.1463 592  VAL A CB  
4328  C CG1 . VAL A 594  ? 0.2805 0.3651 0.3170 0.0851  -0.0185 -0.1354 592  VAL A CG1 
4329  C CG2 . VAL A 594  ? 0.3441 0.4486 0.3809 0.0908  -0.0206 -0.1497 592  VAL A CG2 
4330  N N   . LEU A 595  ? 0.3091 0.3798 0.3701 0.0886  -0.0265 -0.1452 593  LEU A N   
4331  C CA  . LEU A 595  ? 0.3170 0.3810 0.3823 0.0874  -0.0266 -0.1414 593  LEU A CA  
4332  C C   . LEU A 595  ? 0.2898 0.3454 0.3488 0.0825  -0.0238 -0.1298 593  LEU A C   
4333  O O   . LEU A 595  ? 0.3420 0.3921 0.3974 0.0797  -0.0238 -0.1253 593  LEU A O   
4334  C CB  . LEU A 595  ? 0.3166 0.3711 0.3944 0.0885  -0.0321 -0.1460 593  LEU A CB  
4335  C CG  . LEU A 595  ? 0.3394 0.4004 0.4241 0.0906  -0.0359 -0.1539 593  LEU A CG  
4336  C CD1 . LEU A 595  ? 0.3760 0.4269 0.4730 0.0900  -0.0413 -0.1554 593  LEU A CD1 
4337  C CD2 . LEU A 595  ? 0.3374 0.4115 0.4195 0.0929  -0.0334 -0.1571 593  LEU A CD2 
4338  N N   . ASN A 596  ? 0.2812 0.3362 0.3392 0.0815  -0.0216 -0.1253 594  ASN A N   
4339  C CA  . ASN A 596  ? 0.2780 0.3254 0.3310 0.0770  -0.0192 -0.1148 594  ASN A CA  
4340  C C   . ASN A 596  ? 0.2562 0.2899 0.3154 0.0745  -0.0229 -0.1121 594  ASN A C   
4341  O O   . ASN A 596  ? 0.2859 0.3151 0.3543 0.0757  -0.0263 -0.1153 594  ASN A O   
4342  C CB  . ASN A 596  ? 0.2769 0.3271 0.3293 0.0770  -0.0168 -0.1121 594  ASN A CB  
4343  C CG  . ASN A 596  ? 0.3045 0.3483 0.3514 0.0726  -0.0140 -0.1017 594  ASN A CG  
4344  O OD1 . ASN A 596  ? 0.2959 0.3300 0.3426 0.0695  -0.0151 -0.0968 594  ASN A OD1 
4345  N ND2 . ASN A 596  ? 0.3080 0.3577 0.3506 0.0724  -0.0105 -0.0985 594  ASN A ND2 
4346  N N   . PRO A 597  ? 0.2947 0.3219 0.3498 0.0711  -0.0225 -0.1061 595  PRO A N   
4347  C CA  . PRO A 597  ? 0.2592 0.2743 0.3205 0.0686  -0.0261 -0.1034 595  PRO A CA  
4348  C C   . PRO A 597  ? 0.2848 0.2931 0.3497 0.0667  -0.0264 -0.0984 595  PRO A C   
4349  O O   . PRO A 597  ? 0.2755 0.2752 0.3481 0.0655  -0.0302 -0.0977 595  PRO A O   
4350  C CB  . PRO A 597  ? 0.2908 0.3026 0.3451 0.0653  -0.0244 -0.0974 595  PRO A CB  
4351  C CG  . PRO A 597  ? 0.2821 0.3019 0.3264 0.0651  -0.0195 -0.0943 595  PRO A CG  
4352  C CD  . PRO A 597  ? 0.2578 0.2887 0.3028 0.0693  -0.0189 -0.1015 595  PRO A CD  
4353  N N   . GLY A 598  ? 0.2421 0.2543 0.3020 0.0662  -0.0228 -0.0947 596  GLY A N   
4354  C CA  . GLY A 598  ? 0.2364 0.2429 0.2994 0.0645  -0.0230 -0.0902 596  GLY A CA  
4355  C C   . GLY A 598  ? 0.2903 0.2991 0.3613 0.0676  -0.0251 -0.0958 596  GLY A C   
4356  O O   . GLY A 598  ? 0.3099 0.3138 0.3849 0.0664  -0.0260 -0.0925 596  GLY A O   
4357  N N   . ASP A 599  ? 0.2766 0.2933 0.3503 0.0717  -0.0261 -0.1044 597  ASP A N   
4358  C CA  . ASP A 599  ? 0.2925 0.3127 0.3742 0.0752  -0.0281 -0.1109 597  ASP A CA  
4359  C C   . ASP A 599  ? 0.2889 0.3176 0.3729 0.0795  -0.0295 -0.1208 597  ASP A C   
4360  O O   . ASP A 599  ? 0.2733 0.3130 0.3509 0.0814  -0.0262 -0.1233 597  ASP A O   
4361  C CB  . ASP A 599  ? 0.2976 0.3240 0.3751 0.0756  -0.0243 -0.1086 597  ASP A CB  
4362  C CG  . ASP A 599  ? 0.3510 0.3797 0.4374 0.0788  -0.0265 -0.1143 597  ASP A CG  
4363  O OD1 . ASP A 599  ? 0.3225 0.3510 0.4176 0.0817  -0.0306 -0.1220 597  ASP A OD1 
4364  O OD2 . ASP A 599  ? 0.3641 0.3949 0.4491 0.0783  -0.0243 -0.1112 597  ASP A OD2 
4365  N N   . HIS A 600  ? 0.2725 0.2965 0.3659 0.0810  -0.0345 -0.1264 598  HIS A N   
4366  C CA  . HIS A 600  ? 0.3237 0.3553 0.4197 0.0849  -0.0362 -0.1362 598  HIS A CA  
4367  C C   . HIS A 600  ? 0.3461 0.3890 0.4441 0.0889  -0.0355 -0.1433 598  HIS A C   
4368  O O   . HIS A 600  ? 0.3787 0.4309 0.4752 0.0907  -0.0358 -0.1490 598  HIS A O   
4369  C CB  . HIS A 600  ? 0.3485 0.3719 0.4547 0.0850  -0.0421 -0.1398 598  HIS A CB  
4370  C CG  . HIS A 600  ? 0.3687 0.3842 0.4718 0.0816  -0.0426 -0.1343 598  HIS A CG  
4371  N ND1 . HIS A 600  ? 0.4092 0.4169 0.5208 0.0811  -0.0476 -0.1363 598  HIS A ND1 
4372  C CD2 . HIS A 600  ? 0.3325 0.3470 0.4251 0.0781  -0.0387 -0.1265 598  HIS A CD2 
4373  C CE1 . HIS A 600  ? 0.3782 0.3808 0.4844 0.0775  -0.0466 -0.1300 598  HIS A CE1 
4374  N NE2 . HIS A 600  ? 0.3752 0.3818 0.4699 0.0757  -0.0413 -0.1241 598  HIS A NE2 
4375  N N   . ARG A 601  ? 0.3038 0.3466 0.4041 0.0893  -0.0346 -0.1417 599  ARG A N   
4376  C CA  . ARG A 601  ? 0.3109 0.3651 0.4116 0.0919  -0.0334 -0.1464 599  ARG A CA  
4377  C C   . ARG A 601  ? 0.3688 0.4353 0.4584 0.0929  -0.0278 -0.1458 599  ARG A C   
4378  O O   . ARG A 601  ? 0.3590 0.4372 0.4476 0.0950  -0.0267 -0.1502 599  ARG A O   
4379  C CB  . ARG A 601  ? 0.3173 0.3675 0.4234 0.0918  -0.0338 -0.1442 599  ARG A CB  
4380  C CG  . ARG A 601  ? 0.3515 0.3902 0.4690 0.0905  -0.0394 -0.1440 599  ARG A CG  
4381  C CD  . ARG A 601  ? 0.3443 0.3780 0.4658 0.0899  -0.0394 -0.1400 599  ARG A CD  
4382  N NE  . ARG A 601  ? 0.3544 0.3851 0.4674 0.0871  -0.0351 -0.1313 599  ARG A NE  
4383  C CZ  . ARG A 601  ? 0.4073 0.4348 0.5203 0.0853  -0.0339 -0.1255 599  ARG A CZ  
4384  N NH1 . ARG A 601  ? 0.3658 0.3924 0.4881 0.0873  -0.0365 -0.1287 599  ARG A NH1 
4385  N NH2 . ARG A 601  ? 0.3789 0.4042 0.4826 0.0813  -0.0301 -0.1163 599  ARG A NH2 
4386  N N   . ASP A 602  ? 0.3171 0.3812 0.3977 0.0900  -0.0244 -0.1384 600  ASP A N   
4387  C CA  . ASP A 602  ? 0.3363 0.4112 0.4061 0.0896  -0.0193 -0.1354 600  ASP A CA  
4388  C C   . ASP A 602  ? 0.3463 0.4276 0.4122 0.0909  -0.0193 -0.1397 600  ASP A C   
4389  O O   . ASP A 602  ? 0.3164 0.3914 0.3785 0.0882  -0.0195 -0.1354 600  ASP A O   
4390  C CB  . ASP A 602  ? 0.3251 0.3937 0.3874 0.0848  -0.0160 -0.1239 600  ASP A CB  
4391  C CG  . ASP A 602  ? 0.3702 0.4494 0.4221 0.0841  -0.0109 -0.1201 600  ASP A CG  
4392  O OD1 . ASP A 602  ? 0.3535 0.4458 0.4043 0.0873  -0.0095 -0.1255 600  ASP A OD1 
4393  O OD2 . ASP A 602  ? 0.3356 0.4104 0.3806 0.0803  -0.0085 -0.1116 600  ASP A OD2 
4394  N N   . VAL A 603  ? 0.3159 0.4096 0.3821 0.0942  -0.0194 -0.1471 601  VAL A N   
4395  C CA  . VAL A 603  ? 0.3346 0.4357 0.3963 0.0947  -0.0194 -0.1501 601  VAL A CA  
4396  C C   . VAL A 603  ? 0.3160 0.4259 0.3664 0.0940  -0.0140 -0.1451 601  VAL A C   
4397  O O   . VAL A 603  ? 0.3430 0.4623 0.3897 0.0947  -0.0106 -0.1436 601  VAL A O   
4398  C CB  . VAL A 603  ? 0.3341 0.4455 0.4003 0.0972  -0.0219 -0.1580 601  VAL A CB  
4399  C CG1 . VAL A 603  ? 0.3419 0.4612 0.4037 0.0977  -0.0222 -0.1610 601  VAL A CG1 
4400  C CG2 . VAL A 603  ? 0.3955 0.4982 0.4735 0.0977  -0.0275 -0.1625 601  VAL A CG2 
4401  N N   . VAL A 604  ? 0.2851 0.3915 0.3299 0.0921  -0.0133 -0.1415 602  VAL A N   
4402  C CA  . VAL A 604  ? 0.2761 0.3884 0.3103 0.0896  -0.0088 -0.1339 602  VAL A CA  
4403  C C   . VAL A 604  ? 0.2947 0.4224 0.3242 0.0924  -0.0075 -0.1392 602  VAL A C   
4404  O O   . VAL A 604  ? 0.3134 0.4519 0.3357 0.0920  -0.0036 -0.1356 602  VAL A O   
4405  C CB  . VAL A 604  ? 0.2779 0.3780 0.3084 0.0852  -0.0088 -0.1257 602  VAL A CB  
4406  C CG1 . VAL A 604  ? 0.2946 0.4004 0.3150 0.0827  -0.0043 -0.1177 602  VAL A CG1 
4407  C CG2 . VAL A 604  ? 0.2803 0.3660 0.3157 0.0825  -0.0102 -0.1207 602  VAL A CG2 
4408  N N   . GLY A 605  ? 0.2833 0.4113 0.3167 0.0936  -0.0112 -0.1456 603  GLY A N   
4409  C CA  . GLY A 605  ? 0.2992 0.4406 0.3285 0.0946  -0.0108 -0.1485 603  GLY A CA  
4410  C C   . GLY A 605  ? 0.2895 0.4291 0.3250 0.0958  -0.0157 -0.1556 603  GLY A C   
4411  O O   . GLY A 605  ? 0.3327 0.4623 0.3769 0.0961  -0.0197 -0.1589 603  GLY A O   
4412  N N   . SER A 606  ? 0.3017 0.4511 0.3327 0.0963  -0.0156 -0.1574 604  SER A N   
4413  C CA  A SER A 606  ? 0.3026 0.4526 0.3392 0.0976  -0.0201 -0.1644 604  SER A CA  
4414  C CA  B SER A 606  ? 0.3028 0.4531 0.3393 0.0977  -0.0200 -0.1645 604  SER A CA  
4415  C C   . SER A 606  ? 0.3255 0.4775 0.3557 0.0966  -0.0193 -0.1625 604  SER A C   
4416  O O   . SER A 606  ? 0.3610 0.5220 0.3824 0.0960  -0.0155 -0.1580 604  SER A O   
4417  C CB  A SER A 606  ? 0.2932 0.4570 0.3329 0.1003  -0.0215 -0.1712 604  SER A CB  
4418  C CB  B SER A 606  ? 0.2930 0.4579 0.3320 0.1002  -0.0211 -0.1709 604  SER A CB  
4419  O OG  A SER A 606  ? 0.2857 0.4470 0.3324 0.1013  -0.0227 -0.1737 604  SER A OG  
4420  O OG  B SER A 606  ? 0.2950 0.4637 0.3374 0.1016  -0.0247 -0.1771 604  SER A OG  
4421  N N   . VAL A 607  ? 0.2862 0.4297 0.3212 0.0964  -0.0231 -0.1654 605  VAL A N   
4422  C CA  . VAL A 607  ? 0.3025 0.4471 0.3326 0.0956  -0.0231 -0.1643 605  VAL A CA  
4423  C C   . VAL A 607  ? 0.3235 0.4740 0.3592 0.0976  -0.0273 -0.1722 605  VAL A C   
4424  O O   . VAL A 607  ? 0.3181 0.4630 0.3636 0.0986  -0.0316 -0.1776 605  VAL A O   
4425  C CB  . VAL A 607  ? 0.3062 0.4354 0.3362 0.0933  -0.0236 -0.1599 605  VAL A CB  
4426  C CG1 . VAL A 607  ? 0.3425 0.4588 0.3834 0.0932  -0.0283 -0.1633 605  VAL A CG1 
4427  C CG2 . VAL A 607  ? 0.3054 0.4362 0.3304 0.0925  -0.0237 -0.1592 605  VAL A CG2 
4428  N N   . THR A 608  ? 0.2853 0.4476 0.3151 0.0981  -0.0262 -0.1728 606  THR A N   
4429  C CA  . THR A 608  ? 0.3259 0.4935 0.3600 0.0998  -0.0300 -0.1797 606  THR A CA  
4430  C C   . THR A 608  ? 0.3042 0.4643 0.3357 0.0981  -0.0306 -0.1772 606  THR A C   
4431  O O   . THR A 608  ? 0.3119 0.4746 0.3343 0.0966  -0.0271 -0.1713 606  THR A O   
4432  C CB  . THR A 608  ? 0.3342 0.5206 0.3638 0.1015  -0.0284 -0.1820 606  THR A CB  
4433  O OG1 . THR A 608  ? 0.3300 0.5232 0.3620 0.1029  -0.0276 -0.1840 606  THR A OG1 
4434  C CG2 . THR A 608  ? 0.3592 0.5519 0.3937 0.1035  -0.0324 -0.1896 606  THR A CG2 
4435  N N   . GLU A 609  ? 0.3172 0.4677 0.3569 0.0981  -0.0351 -0.1811 607  GLU A N   
4436  C CA  . GLU A 609  ? 0.3442 0.4860 0.3823 0.0963  -0.0360 -0.1787 607  GLU A CA  
4437  C C   . GLU A 609  ? 0.3611 0.5124 0.3979 0.0975  -0.0376 -0.1827 607  GLU A C   
4438  O O   . GLU A 609  ? 0.3179 0.4802 0.3584 0.1000  -0.0395 -0.1891 607  GLU A O   
4439  C CB  . GLU A 609  ? 0.3645 0.4901 0.4117 0.0952  -0.0398 -0.1793 607  GLU A CB  
4440  C CG  . GLU A 609  ? 0.4207 0.5363 0.4668 0.0935  -0.0374 -0.1733 607  GLU A CG  
4441  C CD  . GLU A 609  ? 0.4907 0.5900 0.5452 0.0919  -0.0409 -0.1723 607  GLU A CD  
4442  O OE1 . GLU A 609  ? 0.5575 0.6539 0.6217 0.0927  -0.0457 -0.1776 607  GLU A OE1 
4443  O OE2 . GLU A 609  ? 0.4759 0.5657 0.5276 0.0898  -0.0388 -0.1661 607  GLU A OE2 
4444  N N   . THR A 610  ? 0.3414 0.4890 0.3727 0.0958  -0.0366 -0.1788 608  THR A N   
4445  C CA  . THR A 610  ? 0.3442 0.5011 0.3724 0.0966  -0.0372 -0.1810 608  THR A CA  
4446  C C   . THR A 610  ? 0.3858 0.5373 0.4232 0.0973  -0.0426 -0.1871 608  THR A C   
4447  O O   . THR A 610  ? 0.3985 0.5359 0.4411 0.0958  -0.0448 -0.1860 608  THR A O   
4448  C CB  . THR A 610  ? 0.3588 0.5132 0.3771 0.0942  -0.0339 -0.1737 608  THR A CB  
4449  O OG1 . THR A 610  ? 0.3368 0.4948 0.3473 0.0932  -0.0291 -0.1673 608  THR A OG1 
4450  C CG2 . THR A 610  ? 0.3486 0.5137 0.3629 0.0949  -0.0342 -0.1752 608  THR A CG2 
4451  N N   . SER A 611  ? 0.3541 0.5173 0.3942 0.0997  -0.0447 -0.1935 609  SER A N   
4452  C CA  . SER A 611  ? 0.3843 0.5437 0.4325 0.1004  -0.0496 -0.1990 609  SER A CA  
4453  C C   . SER A 611  ? 0.3981 0.5536 0.4408 0.0985  -0.0489 -0.1952 609  SER A C   
4454  O O   . SER A 611  ? 0.3852 0.5463 0.4176 0.0976  -0.0450 -0.1901 609  SER A O   
4455  C CB  . SER A 611  ? 0.4115 0.5856 0.4639 0.1036  -0.0519 -0.2070 609  SER A CB  
4456  O OG  . SER A 611  ? 0.4248 0.6116 0.4687 0.1041  -0.0495 -0.2059 609  SER A OG  
4457  N N   . GLU A 612  ? 0.4085 0.5542 0.4584 0.0980  -0.0530 -0.1975 610  GLU A N   
4458  C CA  . GLU A 612  ? 0.4180 0.5600 0.4636 0.0963  -0.0529 -0.1946 610  GLU A CA  
4459  C C   . GLU A 612  ? 0.4155 0.5725 0.4557 0.0979  -0.0520 -0.1969 610  GLU A C   
4460  O O   . GLU A 612  ? 0.4090 0.5671 0.4410 0.0965  -0.0497 -0.1923 610  GLU A O   
4461  C CB  . GLU A 612  ? 0.4914 0.6210 0.5469 0.0955  -0.0578 -0.1970 610  GLU A CB  
4462  C CG  . GLU A 612  ? 0.5472 0.6604 0.6043 0.0926  -0.0576 -0.1913 610  GLU A CG  
4463  C CD  . GLU A 612  ? 0.6000 0.7029 0.6703 0.0924  -0.0628 -0.1946 610  GLU A CD  
4464  O OE1 . GLU A 612  ? 0.6838 0.7879 0.7609 0.0938  -0.0644 -0.1980 610  GLU A OE1 
4465  O OE2 . GLU A 612  ? 0.6562 0.7501 0.7305 0.0907  -0.0654 -0.1936 610  GLU A OE2 
4466  N N   . GLU A 613  ? 0.4417 0.6106 0.4865 0.1009  -0.0539 -0.2039 611  GLU A N   
4467  C CA  . GLU A 613  ? 0.4520 0.6367 0.4917 0.1025  -0.0528 -0.2059 611  GLU A CA  
4468  C C   . GLU A 613  ? 0.3790 0.5720 0.4067 0.1015  -0.0473 -0.1992 611  GLU A C   
4469  O O   . GLU A 613  ? 0.3470 0.5459 0.3671 0.1007  -0.0454 -0.1958 611  GLU A O   
4470  C CB  . GLU A 613  ? 0.4748 0.6713 0.5221 0.1060  -0.0558 -0.2148 611  GLU A CB  
4471  N N   . ASP A 614  ? 0.3699 0.5634 0.3960 0.1014  -0.0449 -0.1968 612  ASP A N   
4472  C CA  . ASP A 614  ? 0.3286 0.5304 0.3441 0.1004  -0.0398 -0.1901 612  ASP A CA  
4473  C C   . ASP A 614  ? 0.3506 0.5423 0.3585 0.0972  -0.0369 -0.1815 612  ASP A C   
4474  O O   . ASP A 614  ? 0.3182 0.5172 0.3169 0.0961  -0.0333 -0.1757 612  ASP A O   
4475  C CB  . ASP A 614  ? 0.3947 0.5996 0.4111 0.1011  -0.0380 -0.1900 612  ASP A CB  
4476  C CG  . ASP A 614  ? 0.3900 0.6091 0.4116 0.1043  -0.0399 -0.1976 612  ASP A CG  
4477  O OD1 . ASP A 614  ? 0.4433 0.6747 0.4636 0.1057  -0.0406 -0.2007 612  ASP A OD1 
4478  O OD2 . ASP A 614  ? 0.4700 0.6882 0.4969 0.1054  -0.0407 -0.2006 612  ASP A OD2 
4479  N N   . ALA A 615  ? 0.3287 0.5041 0.3406 0.0956  -0.0386 -0.1805 613  ALA A N   
4480  C CA  . ALA A 615  ? 0.3109 0.4769 0.3163 0.0928  -0.0363 -0.1731 613  ALA A CA  
4481  C C   . ALA A 615  ? 0.3263 0.4969 0.3271 0.0923  -0.0366 -0.1723 613  ALA A C   
4482  O O   . ALA A 615  ? 0.3149 0.4884 0.3067 0.0908  -0.0333 -0.1658 613  ALA A O   
4483  C CB  . ALA A 615  ? 0.3264 0.4747 0.3381 0.0913  -0.0386 -0.1728 613  ALA A CB  
4484  N N   . ARG A 616  ? 0.3449 0.5166 0.3522 0.0938  -0.0407 -0.1788 614  ARG A N   
4485  C CA  . ARG A 616  ? 0.3793 0.5564 0.3828 0.0936  -0.0411 -0.1786 614  ARG A CA  
4486  C C   . ARG A 616  ? 0.3254 0.5201 0.3217 0.0946  -0.0383 -0.1771 614  ARG A C   
4487  O O   . ARG A 616  ? 0.3113 0.5098 0.2999 0.0933  -0.0362 -0.1721 614  ARG A O   
4488  C CB  . ARG A 616  ? 0.4206 0.5959 0.4335 0.0951  -0.0462 -0.1863 614  ARG A CB  
4489  C CG  . ARG A 616  ? 0.4448 0.6031 0.4625 0.0932  -0.0488 -0.1855 614  ARG A CG  
4490  C CD  . ARG A 616  ? 0.5098 0.6667 0.5370 0.0945  -0.0539 -0.1926 614  ARG A CD  
4491  N NE  . ARG A 616  ? 0.5710 0.7303 0.6081 0.0969  -0.0569 -0.1995 614  ARG A NE  
4492  C CZ  . ARG A 616  ? 0.5588 0.7071 0.6039 0.0964  -0.0590 -0.2004 614  ARG A CZ  
4493  N NH1 . ARG A 616  ? 0.5713 0.7054 0.6154 0.0936  -0.0582 -0.1948 614  ARG A NH1 
4494  N NH2 . ARG A 616  ? 0.5288 0.6804 0.5831 0.0988  -0.0620 -0.2071 614  ARG A NH2 
4495  N N   . ARG A 617  ? 0.3038 0.5092 0.3024 0.0968  -0.0381 -0.1809 615  ARG A N   
4496  C CA  . ARG A 617  ? 0.3114 0.5341 0.3035 0.0976  -0.0353 -0.1790 615  ARG A CA  
4497  C C   . ARG A 617  ? 0.3439 0.5668 0.3263 0.0952  -0.0306 -0.1692 615  ARG A C   
4498  O O   . ARG A 617  ? 0.3303 0.5631 0.3056 0.0945  -0.0284 -0.1647 615  ARG A O   
4499  C CB  . ARG A 617  ? 0.3752 0.6088 0.3723 0.1004  -0.0361 -0.1849 615  ARG A CB  
4500  C CG  . ARG A 617  ? 0.4388 0.6916 0.4306 0.1015  -0.0339 -0.1840 615  ARG A CG  
4501  C CD  . ARG A 617  ? 0.4547 0.7189 0.4536 0.1048  -0.0363 -0.1927 615  ARG A CD  
4502  N NE  . ARG A 617  ? 0.4354 0.6950 0.4389 0.1054  -0.0364 -0.1947 615  ARG A NE  
4503  C CZ  . ARG A 617  ? 0.5264 0.7940 0.5265 0.1054  -0.0334 -0.1917 615  ARG A CZ  
4504  N NH1 . ARG A 617  ? 0.5656 0.8458 0.5576 0.1047  -0.0299 -0.1861 615  ARG A NH1 
4505  N NH2 . ARG A 617  ? 0.5113 0.7743 0.5164 0.1062  -0.0340 -0.1942 615  ARG A NH2 
4506  N N   . ALA A 618  ? 0.2980 0.5101 0.2803 0.0938  -0.0290 -0.1657 616  ALA A N   
4507  C CA  . ALA A 618  ? 0.3213 0.5330 0.2950 0.0914  -0.0246 -0.1564 616  ALA A CA  
4508  C C   . ALA A 618  ? 0.2831 0.4903 0.2507 0.0892  -0.0238 -0.1507 616  ALA A C   
4509  O O   . ALA A 618  ? 0.2949 0.5093 0.2548 0.0878  -0.0207 -0.1437 616  ALA A O   
4510  C CB  . ALA A 618  ? 0.3120 0.5120 0.2877 0.0905  -0.0235 -0.1544 616  ALA A CB  
4511  N N   . VAL A 619  ? 0.2908 0.4863 0.2621 0.0887  -0.0267 -0.1533 617  VAL A N   
4512  C CA  . VAL A 619  ? 0.3039 0.4951 0.2699 0.0867  -0.0262 -0.1484 617  VAL A CA  
4513  C C   . VAL A 619  ? 0.3030 0.5084 0.2651 0.0873  -0.0261 -0.1482 617  VAL A C   
4514  O O   . VAL A 619  ? 0.3295 0.5382 0.2841 0.0856  -0.0238 -0.1412 617  VAL A O   
4515  C CB  . VAL A 619  ? 0.3363 0.5123 0.3079 0.0861  -0.0296 -0.1515 617  VAL A CB  
4516  C CG1 . VAL A 619  ? 0.3397 0.5120 0.3057 0.0840  -0.0293 -0.1468 617  VAL A CG1 
4517  C CG2 . VAL A 619  ? 0.3017 0.4640 0.2766 0.0851  -0.0293 -0.1505 617  VAL A CG2 
4518  N N   . ARG A 620  ? 0.3029 0.5172 0.2702 0.0899  -0.0287 -0.1556 618  ARG A N   
4519  C CA  . ARG A 620  ? 0.3483 0.5771 0.3123 0.0907  -0.0286 -0.1558 618  ARG A CA  
4520  C C   . ARG A 620  ? 0.3055 0.5473 0.2623 0.0901  -0.0247 -0.1492 618  ARG A C   
4521  O O   . ARG A 620  ? 0.3678 0.6169 0.3185 0.0889  -0.0232 -0.1438 618  ARG A O   
4522  C CB  . ARG A 620  ? 0.3689 0.6052 0.3404 0.0938  -0.0321 -0.1655 618  ARG A CB  
4523  C CG  . ARG A 620  ? 0.4215 0.6473 0.3994 0.0941  -0.0362 -0.1710 618  ARG A CG  
4524  C CD  . ARG A 620  ? 0.5108 0.7448 0.4964 0.0972  -0.0398 -0.1806 618  ARG A CD  
4525  N NE  . ARG A 620  ? 0.5577 0.7843 0.5527 0.0986  -0.0425 -0.1868 618  ARG A NE  
4526  C CZ  . ARG A 620  ? 0.5049 0.7398 0.5040 0.1009  -0.0429 -0.1915 618  ARG A CZ  
4527  N NH1 . ARG A 620  ? 0.5409 0.7927 0.5361 0.1022  -0.0408 -0.1913 618  ARG A NH1 
4528  N NH2 . ARG A 620  ? 0.5580 0.7846 0.5658 0.1018  -0.0455 -0.1965 618  ARG A NH2 
4529  N N   . LEU A 621  ? 0.2795 0.5243 0.2375 0.0907  -0.0230 -0.1492 619  LEU A N   
4530  C CA  . LEU A 621  ? 0.3100 0.5668 0.2619 0.0899  -0.0193 -0.1425 619  LEU A CA  
4531  C C   . LEU A 621  ? 0.3234 0.5738 0.2681 0.0867  -0.0163 -0.1322 619  LEU A C   
4532  O O   . LEU A 621  ? 0.3201 0.5804 0.2589 0.0854  -0.0140 -0.1253 619  LEU A O   
4533  C CB  . LEU A 621  ? 0.3192 0.5789 0.2743 0.0911  -0.0184 -0.1448 619  LEU A CB  
4534  C CG  . LEU A 621  ? 0.3546 0.6237 0.3166 0.0944  -0.0211 -0.1544 619  LEU A CG  
4535  C CD1 . LEU A 621  ? 0.3302 0.5970 0.2964 0.0954  -0.0207 -0.1570 619  LEU A CD1 
4536  C CD2 . LEU A 621  ? 0.3635 0.6522 0.3226 0.0954  -0.0202 -0.1539 619  LEU A CD2 
4537  N N   . ALA A 622  ? 0.3111 0.5453 0.2565 0.0853  -0.0164 -0.1308 620  ALA A N   
4538  C CA  . ALA A 622  ? 0.2987 0.5261 0.2378 0.0825  -0.0139 -0.1216 620  ALA A CA  
4539  C C   . ALA A 622  ? 0.2978 0.5280 0.2328 0.0813  -0.0145 -0.1184 620  ALA A C   
4540  O O   . ALA A 622  ? 0.3383 0.5727 0.2671 0.0793  -0.0121 -0.1098 620  ALA A O   
4541  C CB  . ALA A 622  ? 0.3050 0.5145 0.2465 0.0815  -0.0145 -0.1221 620  ALA A CB  
4542  N N   . ALA A 623  ? 0.2915 0.5192 0.2302 0.0826  -0.0179 -0.1249 621  ALA A N   
4543  C CA  . ALA A 623  ? 0.3166 0.5470 0.2519 0.0816  -0.0187 -0.1224 621  ALA A CA  
4544  C C   . ALA A 623  ? 0.3047 0.5528 0.2362 0.0819  -0.0173 -0.1191 621  ALA A C   
4545  O O   . ALA A 623  ? 0.3486 0.6003 0.2746 0.0800  -0.0160 -0.1117 621  ALA A O   
4546  C CB  . ALA A 623  ? 0.3419 0.5667 0.2828 0.0831  -0.0228 -0.1307 621  ALA A CB  
4547  N N   . ASP A 624  ? 0.3121 0.5719 0.2468 0.0842  -0.0177 -0.1244 622  ASP A N   
4548  C CA  . ASP A 624  ? 0.3863 0.6640 0.3179 0.0845  -0.0163 -0.1215 622  ASP A CA  
4549  C C   . ASP A 624  ? 0.3509 0.6330 0.2770 0.0821  -0.0126 -0.1111 622  ASP A C   
4550  O O   . ASP A 624  ? 0.4314 0.7244 0.3534 0.0810  -0.0113 -0.1049 622  ASP A O   
4551  C CB  . ASP A 624  ? 0.4323 0.7216 0.3691 0.0875  -0.0175 -0.1297 622  ASP A CB  
4552  C CG  . ASP A 624  ? 0.5027 0.7899 0.4456 0.0899  -0.0215 -0.1398 622  ASP A CG  
4553  O OD1 . ASP A 624  ? 0.5858 0.8692 0.5277 0.0893  -0.0230 -0.1397 622  ASP A OD1 
4554  O OD2 . ASP A 624  ? 0.5299 0.8192 0.4791 0.0924  -0.0232 -0.1478 622  ASP A OD2 
4555  N N   . ALA A 625  ? 0.3894 0.6628 0.3155 0.0813  -0.0109 -0.1087 623  ALA A N   
4556  C CA  . ALA A 625  ? 0.4217 0.6982 0.3434 0.0791  -0.0075 -0.0991 623  ALA A CA  
4557  C C   . ALA A 625  ? 0.4068 0.6736 0.3239 0.0761  -0.0063 -0.0903 623  ALA A C   
4558  O O   . ALA A 625  ? 0.4473 0.7173 0.3608 0.0740  -0.0037 -0.0812 623  ALA A O   
4559  C CB  . ALA A 625  ? 0.4272 0.6990 0.3516 0.0797  -0.0062 -0.1008 623  ALA A CB  
4560  N N   . ALA A 626  ? 0.3765 0.6314 0.2940 0.0759  -0.0084 -0.0928 624  ALA A N   
4561  C CA  . ALA A 626  ? 0.3234 0.5682 0.2370 0.0733  -0.0075 -0.0852 624  ALA A CA  
4562  C C   . ALA A 626  ? 0.3712 0.6249 0.2798 0.0711  -0.0060 -0.0752 624  ALA A C   
4563  O O   . ALA A 626  ? 0.3666 0.6167 0.2723 0.0688  -0.0038 -0.0665 624  ALA A O   
4564  C CB  . ALA A 626  ? 0.3558 0.5879 0.2711 0.0736  -0.0103 -0.0902 624  ALA A CB  
4565  N N   . PRO A 627  ? 0.3871 0.6525 0.2950 0.0716  -0.0070 -0.0755 625  PRO A N   
4566  C CA  . PRO A 627  ? 0.3956 0.6692 0.2996 0.0693  -0.0057 -0.0652 625  PRO A CA  
4567  C C   . PRO A 627  ? 0.3899 0.6710 0.2927 0.0678  -0.0028 -0.0575 625  PRO A C   
4568  O O   . PRO A 627  ? 0.4076 0.6871 0.3078 0.0651  -0.0014 -0.0474 625  PRO A O   
4569  C CB  . PRO A 627  ? 0.3889 0.6754 0.2934 0.0707  -0.0074 -0.0690 625  PRO A CB  
4570  C CG  . PRO A 627  ? 0.4172 0.6970 0.3254 0.0731  -0.0102 -0.0801 625  PRO A CG  
4571  C CD  . PRO A 627  ? 0.4024 0.6735 0.3136 0.0741  -0.0097 -0.0849 625  PRO A CD  
4572  N N   . ASP A 628  ? 0.3412 0.6305 0.2465 0.0696  -0.0020 -0.0620 626  ASP A N   
4573  C CA  . ASP A 628  ? 0.4041 0.7017 0.3087 0.0682  0.0007  -0.0550 626  ASP A CA  
4574  C C   . ASP A 628  ? 0.4047 0.6899 0.3083 0.0663  0.0025  -0.0492 626  ASP A C   
4575  O O   . ASP A 628  ? 0.4008 0.6893 0.3029 0.0639  0.0045  -0.0395 626  ASP A O   
4576  C CB  . ASP A 628  ? 0.3798 0.6873 0.2876 0.0708  0.0009  -0.0622 626  ASP A CB  
4577  C CG  . ASP A 628  ? 0.4865 0.8066 0.3958 0.0730  -0.0011 -0.0688 626  ASP A CG  
4578  O OD1 . ASP A 628  ? 0.5058 0.8202 0.4161 0.0743  -0.0035 -0.0752 626  ASP A OD1 
4579  O OD2 . ASP A 628  ? 0.5737 0.9096 0.4833 0.0735  -0.0002 -0.0675 626  ASP A OD2 
4580  N N   . TRP A 629  ? 0.3359 0.6071 0.2408 0.0672  0.0018  -0.0549 627  TRP A N   
4581  C CA  . TRP A 629  ? 0.3447 0.6045 0.2488 0.0656  0.0036  -0.0499 627  TRP A CA  
4582  C C   . TRP A 629  ? 0.3230 0.5736 0.2252 0.0628  0.0034  -0.0416 627  TRP A C   
4583  O O   . TRP A 629  ? 0.3296 0.5757 0.2324 0.0601  0.0051  -0.0325 627  TRP A O   
4584  C CB  . TRP A 629  ? 0.3316 0.5798 0.2387 0.0675  0.0028  -0.0587 627  TRP A CB  
4585  C CG  . TRP A 629  ? 0.3152 0.5487 0.2250 0.0651  0.0042  -0.0530 627  TRP A CG  
4586  C CD1 . TRP A 629  ? 0.2781 0.4931 0.1917 0.0636  0.0031  -0.0531 627  TRP A CD1 
4587  C CD2 . TRP A 629  ? 0.2857 0.5216 0.1950 0.0635  0.0069  -0.0459 627  TRP A CD2 
4588  N NE1 . TRP A 629  ? 0.2790 0.4850 0.1945 0.0614  0.0049  -0.0469 627  TRP A NE1 
4589  C CE2 . TRP A 629  ? 0.2680 0.4862 0.1811 0.0613  0.0072  -0.0425 627  TRP A CE2 
4590  C CE3 . TRP A 629  ? 0.2632 0.5150 0.1695 0.0637  0.0091  -0.0422 627  TRP A CE3 
4591  C CZ2 . TRP A 629  ? 0.2807 0.4962 0.1948 0.0593  0.0094  -0.0357 627  TRP A CZ2 
4592  C CZ3 . TRP A 629  ? 0.3062 0.5550 0.2136 0.0617  0.0113  -0.0352 627  TRP A CZ3 
4593  C CH2 . TRP A 629  ? 0.2922 0.5228 0.2036 0.0595  0.0114  -0.0321 627  TRP A CH2 
4594  N N   . ALA A 630  ? 0.3269 0.5731 0.2291 0.0630  0.0010  -0.0442 628  ALA A N   
4595  C CA  . ALA A 630  ? 0.3448 0.5816 0.2477 0.0599  0.0005  -0.0360 628  ALA A CA  
4596  C C   . ALA A 630  ? 0.3755 0.6240 0.2750 0.0580  0.0018  -0.0257 628  ALA A C   
4597  O O   . ALA A 630  ? 0.3789 0.6196 0.2798 0.0551  0.0020  -0.0168 628  ALA A O   
4598  C CB  . ALA A 630  ? 0.3282 0.5608 0.2315 0.0607  -0.0023 -0.0411 628  ALA A CB  
4599  N N   . ALA A 631  ? 0.3491 0.6154 0.2460 0.0594  0.0024  -0.0266 629  ALA A N   
4600  C CA  . ALA A 631  ? 0.3831 0.6602 0.2794 0.0571  0.0033  -0.0165 629  ALA A CA  
4601  C C   . ALA A 631  ? 0.3903 0.6678 0.2874 0.0551  0.0057  -0.0085 629  ALA A C   
4602  O O   . ALA A 631  ? 0.3734 0.6565 0.2707 0.0526  0.0063  0.0015  629  ALA A O   
4603  C CB  . ALA A 631  ? 0.3995 0.6931 0.2966 0.0586  0.0028  -0.0199 629  ALA A CB  
4604  N N   . VAL A 632  ? 0.3504 0.6221 0.2485 0.0561  0.0070  -0.0124 630  VAL A N   
4605  C CA  . VAL A 632  ? 0.3182 0.5888 0.2172 0.0541  0.0093  -0.0048 630  VAL A CA  
4606  C C   . VAL A 632  ? 0.3016 0.5567 0.2029 0.0511  0.0088  0.0028  630  VAL A C   
4607  O O   . VAL A 632  ? 0.3132 0.5527 0.2172 0.0512  0.0077  -0.0015 630  VAL A O   
4608  C CB  . VAL A 632  ? 0.3416 0.6089 0.2420 0.0559  0.0106  -0.0114 630  VAL A CB  
4609  C CG1 . VAL A 632  ? 0.3128 0.5777 0.2146 0.0536  0.0128  -0.0034 630  VAL A CG1 
4610  C CG2 . VAL A 632  ? 0.3281 0.6084 0.2299 0.0584  0.0103  -0.0190 630  VAL A CG2 
4611  N N   . PRO A 633  ? 0.3171 0.5753 0.2188 0.0483  0.0094  0.0140  631  PRO A N   
4612  C CA  . PRO A 633  ? 0.2898 0.5330 0.1952 0.0455  0.0085  0.0207  631  PRO A CA  
4613  C C   . PRO A 633  ? 0.3076 0.5336 0.2171 0.0449  0.0092  0.0185  631  PRO A C   
4614  O O   . PRO A 633  ? 0.2989 0.5260 0.2088 0.0457  0.0108  0.0161  631  PRO A O   
4615  C CB  . PRO A 633  ? 0.3301 0.5820 0.2359 0.0428  0.0092  0.0327  631  PRO A CB  
4616  C CG  . PRO A 633  ? 0.3652 0.6375 0.2674 0.0441  0.0099  0.0321  631  PRO A CG  
4617  C CD  . PRO A 633  ? 0.3582 0.6325 0.2592 0.0472  0.0107  0.0209  631  PRO A CD  
4618  N N   . PRO A 634  ? 0.2584 0.4686 0.1710 0.0436  0.0079  0.0192  632  PRO A N   
4619  C CA  . PRO A 634  ? 0.2689 0.4632 0.1854 0.0430  0.0084  0.0173  632  PRO A CA  
4620  C C   . PRO A 634  ? 0.2677 0.4621 0.1861 0.0414  0.0104  0.0232  632  PRO A C   
4621  O O   . PRO A 634  ? 0.2697 0.4578 0.1896 0.0420  0.0114  0.0191  632  PRO A O   
4622  C CB  . PRO A 634  ? 0.2948 0.4755 0.2141 0.0412  0.0069  0.0201  632  PRO A CB  
4623  C CG  . PRO A 634  ? 0.3034 0.4912 0.2201 0.0421  0.0051  0.0189  632  PRO A CG  
4624  C CD  . PRO A 634  ? 0.2887 0.4956 0.2015 0.0429  0.0058  0.0213  632  PRO A CD  
4625  N N   . SER A 635  ? 0.2938 0.4951 0.2127 0.0393  0.0107  0.0329  633  SER A N   
4626  C CA  . SER A 635  ? 0.2995 0.5011 0.2209 0.0376  0.0124  0.0390  633  SER A CA  
4627  C C   . SER A 635  ? 0.2744 0.4864 0.1933 0.0395  0.0142  0.0347  633  SER A C   
4628  O O   . SER A 635  ? 0.2711 0.4779 0.1922 0.0391  0.0156  0.0345  633  SER A O   
4629  C CB  . SER A 635  ? 0.3925 0.6013 0.3151 0.0351  0.0121  0.0503  633  SER A CB  
4630  N N   . GLU A 636  ? 0.2763 0.5033 0.1908 0.0416  0.0143  0.0308  634  GLU A N   
4631  C CA  . GLU A 636  ? 0.3230 0.5611 0.2354 0.0437  0.0160  0.0259  634  GLU A CA  
4632  C C   . GLU A 636  ? 0.2885 0.5174 0.2016 0.0461  0.0158  0.0150  634  GLU A C   
4633  O O   . GLU A 636  ? 0.2993 0.5295 0.2132 0.0471  0.0173  0.0122  634  GLU A O   
4634  C CB  . GLU A 636  ? 0.3420 0.6004 0.2496 0.0453  0.0161  0.0252  634  GLU A CB  
4635  C CG  . GLU A 636  ? 0.4182 0.6887 0.3243 0.0476  0.0177  0.0192  634  GLU A CG  
4636  C CD  . GLU A 636  ? 0.4833 0.7535 0.3918 0.0462  0.0198  0.0244  634  GLU A CD  
4637  O OE1 . GLU A 636  ? 0.5118 0.7839 0.4224 0.0431  0.0201  0.0349  634  GLU A OE1 
4638  O OE2 . GLU A 636  ? 0.4265 0.6942 0.3354 0.0479  0.0209  0.0179  634  GLU A OE2 
4639  N N   . ARG A 637  ? 0.2904 0.5100 0.2037 0.0471  0.0140  0.0092  635  ARG A N   
4640  C CA  . ARG A 637  ? 0.2388 0.4473 0.1541 0.0488  0.0135  0.0001  635  ARG A CA  
4641  C C   . ARG A 637  ? 0.2559 0.4506 0.1752 0.0470  0.0145  0.0032  635  ARG A C   
4642  O O   . ARG A 637  ? 0.2576 0.4494 0.1782 0.0482  0.0152  -0.0017 635  ARG A O   
4643  C CB  . ARG A 637  ? 0.2449 0.4452 0.1603 0.0496  0.0112  -0.0052 635  ARG A CB  
4644  C CG  . ARG A 637  ? 0.2821 0.4964 0.1936 0.0515  0.0102  -0.0085 635  ARG A CG  
4645  C CD  . ARG A 637  ? 0.2932 0.5005 0.2051 0.0531  0.0078  -0.0165 635  ARG A CD  
4646  N NE  . ARG A 637  ? 0.2884 0.4810 0.2028 0.0509  0.0067  -0.0129 635  ARG A NE  
4647  C CZ  . ARG A 637  ? 0.3311 0.5241 0.2445 0.0501  0.0052  -0.0104 635  ARG A CZ  
4648  N NH1 . ARG A 637  ? 0.3178 0.5253 0.2275 0.0511  0.0047  -0.0102 635  ARG A NH1 
4649  N NH2 . ARG A 637  ? 0.2784 0.4573 0.1946 0.0484  0.0042  -0.0082 635  ARG A NH2 
4650  N N   . ALA A 638  ? 0.2674 0.4535 0.1888 0.0441  0.0142  0.0111  636  ALA A N   
4651  C CA  . ALA A 638  ? 0.2684 0.4420 0.1937 0.0423  0.0150  0.0142  636  ALA A CA  
4652  C C   . ALA A 638  ? 0.2784 0.4596 0.2040 0.0419  0.0171  0.0176  636  ALA A C   
4653  O O   . ALA A 638  ? 0.2474 0.4207 0.1755 0.0417  0.0179  0.0161  636  ALA A O   
4654  C CB  . ALA A 638  ? 0.2645 0.4293 0.1923 0.0394  0.0142  0.0220  636  ALA A CB  
4655  N N   . ALA A 639  ? 0.2427 0.4395 0.1659 0.0418  0.0179  0.0222  637  ALA A N   
4656  C CA  . ALA A 639  ? 0.2571 0.4627 0.1806 0.0415  0.0199  0.0253  637  ALA A CA  
4657  C C   . ALA A 639  ? 0.2652 0.4740 0.1877 0.0444  0.0208  0.0161  637  ALA A C   
4658  O O   . ALA A 639  ? 0.2919 0.4999 0.2162 0.0442  0.0222  0.0167  637  ALA A O   
4659  C CB  . ALA A 639  ? 0.2666 0.4897 0.1876 0.0408  0.0205  0.0323  637  ALA A CB  
4660  N N   . CYS A 640  ? 0.2544 0.4669 0.1745 0.0472  0.0197  0.0075  638  CYS A N   
4661  C CA  . CYS A 640  ? 0.2800 0.4940 0.2003 0.0501  0.0201  -0.0020 638  CYS A CA  
4662  C C   . CYS A 640  ? 0.2591 0.4558 0.1833 0.0496  0.0198  -0.0046 638  CYS A C   
4663  O O   . CYS A 640  ? 0.2628 0.4595 0.1887 0.0505  0.0209  -0.0073 638  CYS A O   
4664  C CB  . CYS A 640  ? 0.2814 0.5003 0.1994 0.0531  0.0184  -0.0111 638  CYS A CB  
4665  S SG  . CYS A 640  ? 0.3110 0.5524 0.2238 0.0544  0.0187  -0.0103 638  CYS A SG  
4666  N N   . LEU A 641  ? 0.2443 0.4268 0.1703 0.0482  0.0183  -0.0037 639  LEU A N   
4667  C CA  . LEU A 641  ? 0.2475 0.4140 0.1772 0.0475  0.0180  -0.0057 639  LEU A CA  
4668  C C   . LEU A 641  ? 0.2361 0.3999 0.1680 0.0454  0.0197  0.0009  639  LEU A C   
4669  O O   . LEU A 641  ? 0.2515 0.4098 0.1856 0.0459  0.0202  -0.0020 639  LEU A O   
4670  C CB  . LEU A 641  ? 0.2456 0.3989 0.1766 0.0461  0.0163  -0.0048 639  LEU A CB  
4671  C CG  . LEU A 641  ? 0.2562 0.4046 0.1874 0.0480  0.0143  -0.0134 639  LEU A CG  
4672  C CD1 . LEU A 641  ? 0.2600 0.4216 0.1878 0.0504  0.0136  -0.0179 639  LEU A CD1 
4673  C CD2 . LEU A 641  ? 0.2491 0.3846 0.1818 0.0462  0.0129  -0.0113 639  LEU A CD2 
4674  N N   . ASP A 642  ? 0.2457 0.4133 0.1774 0.0431  0.0203  0.0099  640  ASP A N   
4675  C CA  . ASP A 642  ? 0.2567 0.4218 0.1909 0.0410  0.0217  0.0165  640  ASP A CA  
4676  C C   . ASP A 642  ? 0.2309 0.4070 0.1645 0.0424  0.0235  0.0148  640  ASP A C   
4677  O O   . ASP A 642  ? 0.2493 0.4203 0.1856 0.0417  0.0244  0.0155  640  ASP A O   
4678  C CB  . ASP A 642  ? 0.2655 0.4333 0.2004 0.0382  0.0217  0.0265  640  ASP A CB  
4679  C CG  . ASP A 642  ? 0.2945 0.4484 0.2318 0.0364  0.0201  0.0290  640  ASP A CG  
4680  O OD1 . ASP A 642  ? 0.3146 0.4555 0.2536 0.0366  0.0196  0.0245  640  ASP A OD1 
4681  O OD2 . ASP A 642  ? 0.3244 0.4806 0.2619 0.0348  0.0195  0.0355  640  ASP A OD2 
4682  N N   . ARG A 643  ? 0.2610 0.4528 0.1913 0.0443  0.0240  0.0124  641  ARG A N   
4683  C CA  . ARG A 643  ? 0.2553 0.4584 0.1850 0.0460  0.0257  0.0099  641  ARG A CA  
4684  C C   . ARG A 643  ? 0.2609 0.4568 0.1923 0.0483  0.0254  0.0006  641  ARG A C   
4685  O O   . ARG A 643  ? 0.2700 0.4671 0.2032 0.0486  0.0266  0.0000  641  ARG A O   
4686  C CB  . ARG A 643  ? 0.2636 0.4858 0.1892 0.0478  0.0261  0.0086  641  ARG A CB  
4687  C CG  . ARG A 643  ? 0.2820 0.5151 0.2064 0.0454  0.0270  0.0190  641  ARG A CG  
4688  C CD  . ARG A 643  ? 0.3086 0.5626 0.2288 0.0473  0.0278  0.0175  641  ARG A CD  
4689  N NE  . ARG A 643  ? 0.3110 0.5675 0.2282 0.0493  0.0262  0.0112  641  ARG A NE  
4690  C CZ  . ARG A 643  ? 0.2964 0.5560 0.2117 0.0481  0.0251  0.0158  641  ARG A CZ  
4691  N NH1 . ARG A 643  ? 0.3138 0.5736 0.2302 0.0448  0.0252  0.0267  641  ARG A NH1 
4692  N NH2 . ARG A 643  ? 0.3521 0.6148 0.2647 0.0502  0.0236  0.0093  641  ARG A NH2 
4693  N N   . ALA A 644  ? 0.2326 0.4214 0.1640 0.0499  0.0235  -0.0065 642  ALA A N   
4694  C CA  . ALA A 644  ? 0.2525 0.4332 0.1864 0.0518  0.0228  -0.0148 642  ALA A CA  
4695  C C   . ALA A 644  ? 0.2417 0.4081 0.1793 0.0497  0.0231  -0.0116 642  ALA A C   
4696  O O   . ALA A 644  ? 0.2546 0.4185 0.1945 0.0508  0.0235  -0.0154 642  ALA A O   
4697  C CB  . ALA A 644  ? 0.2477 0.4226 0.1815 0.0534  0.0204  -0.0220 642  ALA A CB  
4698  N N   . ALA A 645  ? 0.2378 0.3947 0.1762 0.0468  0.0227  -0.0050 643  ALA A N   
4699  C CA  . ALA A 645  ? 0.2236 0.3675 0.1654 0.0448  0.0229  -0.0019 643  ALA A CA  
4700  C C   . ALA A 645  ? 0.2497 0.3993 0.1926 0.0441  0.0249  0.0023  643  ALA A C   
4701  O O   . ALA A 645  ? 0.2486 0.3915 0.1942 0.0440  0.0252  0.0008  643  ALA A O   
4702  C CB  . ALA A 645  ? 0.2352 0.3698 0.1777 0.0420  0.0222  0.0044  643  ALA A CB  
4703  N N   . GLU A 646  ? 0.2558 0.4180 0.1970 0.0433  0.0261  0.0081  644  GLU A N   
4704  C CA  . GLU A 646  ? 0.2707 0.4399 0.2130 0.0427  0.0280  0.0122  644  GLU A CA  
4705  C C   . GLU A 646  ? 0.2689 0.4442 0.2113 0.0455  0.0287  0.0048  644  GLU A C   
4706  O O   . GLU A 646  ? 0.2664 0.4395 0.2113 0.0452  0.0297  0.0054  644  GLU A O   
4707  C CB  . GLU A 646  ? 0.3279 0.5116 0.2681 0.0416  0.0290  0.0194  644  GLU A CB  
4708  C CG  . GLU A 646  ? 0.3949 0.5737 0.3364 0.0384  0.0284  0.0284  644  GLU A CG  
4709  C CD  . GLU A 646  ? 0.4969 0.6648 0.4426 0.0358  0.0286  0.0336  644  GLU A CD  
4710  O OE1 . GLU A 646  ? 0.5442 0.7140 0.4916 0.0360  0.0299  0.0333  644  GLU A OE1 
4711  O OE2 . GLU A 646  ? 0.5160 0.6737 0.4637 0.0337  0.0274  0.0377  644  GLU A OE2 
4712  N N   . LEU A 647  ? 0.2683 0.4515 0.2083 0.0485  0.0281  -0.0025 645  LEU A N   
4713  C CA  . LEU A 647  ? 0.2509 0.4402 0.1916 0.0515  0.0286  -0.0103 645  LEU A CA  
4714  C C   . LEU A 647  ? 0.2844 0.4589 0.2288 0.0520  0.0274  -0.0154 645  LEU A C   
4715  O O   . LEU A 647  ? 0.3019 0.4772 0.2486 0.0531  0.0282  -0.0181 645  LEU A O   
4716  C CB  . LEU A 647  ? 0.2804 0.4809 0.2182 0.0546  0.0278  -0.0175 645  LEU A CB  
4717  C CG  . LEU A 647  ? 0.3080 0.5269 0.2420 0.0547  0.0292  -0.0135 645  LEU A CG  
4718  C CD1 . LEU A 647  ? 0.3034 0.5317 0.2344 0.0576  0.0280  -0.0207 645  LEU A CD1 
4719  C CD2 . LEU A 647  ? 0.3383 0.5694 0.2728 0.0553  0.0314  -0.0122 645  LEU A CD2 
4720  N N   . MET A 648  ? 0.2702 0.4314 0.2154 0.0513  0.0256  -0.0167 646  MET A N   
4721  C CA  . MET A 648  ? 0.2549 0.4022 0.2037 0.0514  0.0244  -0.0208 646  MET A CA  
4722  C C   . MET A 648  ? 0.2605 0.4006 0.2118 0.0490  0.0255  -0.0149 646  MET A C   
4723  O O   . MET A 648  ? 0.2840 0.4193 0.2382 0.0497  0.0254  -0.0180 646  MET A O   
4724  C CB  . MET A 648  ? 0.2349 0.3706 0.1840 0.0509  0.0222  -0.0228 646  MET A CB  
4725  C CG  . MET A 648  ? 0.3169 0.4569 0.2654 0.0538  0.0206  -0.0310 646  MET A CG  
4726  S SD  . MET A 648  ? 0.3171 0.4411 0.2674 0.0531  0.0179  -0.0338 646  MET A SD  
4727  C CE  . MET A 648  ? 0.3369 0.4694 0.2861 0.0565  0.0161  -0.0428 646  MET A CE  
4728  N N   . GLN A 649  ? 0.2718 0.4108 0.2223 0.0461  0.0263  -0.0064 647  GLN A N   
4729  C CA  . GLN A 649  ? 0.2350 0.3678 0.1881 0.0438  0.0272  -0.0008 647  GLN A CA  
4730  C C   . GLN A 649  ? 0.2440 0.3861 0.1981 0.0448  0.0289  -0.0011 647  GLN A C   
4731  O O   . GLN A 649  ? 0.2972 0.4332 0.2542 0.0444  0.0292  -0.0015 647  GLN A O   
4732  C CB  . GLN A 649  ? 0.2746 0.4065 0.2274 0.0408  0.0276  0.0081  647  GLN A CB  
4733  C CG  . GLN A 649  ? 0.2630 0.3872 0.2190 0.0383  0.0282  0.0136  647  GLN A CG  
4734  C CD  . GLN A 649  ? 0.2610 0.3694 0.2191 0.0373  0.0268  0.0119  647  GLN A CD  
4735  O OE1 . GLN A 649  ? 0.2722 0.3737 0.2301 0.0360  0.0258  0.0138  647  GLN A OE1 
4736  N NE2 . GLN A 649  ? 0.2981 0.4012 0.2585 0.0379  0.0268  0.0083  647  GLN A NE2 
4737  N N   . ALA A 650  ? 0.2598 0.4174 0.2114 0.0461  0.0301  -0.0008 648  ALA A N   
4738  C CA  . ALA A 650  ? 0.2695 0.4377 0.2220 0.0470  0.0319  -0.0009 648  ALA A CA  
4739  C C   . ALA A 650  ? 0.3155 0.4825 0.2698 0.0501  0.0313  -0.0100 648  ALA A C   
4740  O O   . ALA A 650  ? 0.3641 0.5324 0.3208 0.0504  0.0323  -0.0104 648  ALA A O   
4741  C CB  . ALA A 650  ? 0.2871 0.4732 0.2362 0.0478  0.0332  0.0013  648  ALA A CB  
4742  N N   . ARG A 651  ? 0.2735 0.4380 0.2272 0.0523  0.0296  -0.0174 649  ARG A N   
4743  C CA  . ARG A 651  ? 0.2637 0.4279 0.2198 0.0554  0.0286  -0.0266 649  ARG A CA  
4744  C C   . ARG A 651  ? 0.2749 0.4223 0.2347 0.0548  0.0268  -0.0288 649  ARG A C   
4745  O O   . ARG A 651  ? 0.2858 0.4308 0.2484 0.0572  0.0255  -0.0362 649  ARG A O   
4746  C CB  . ARG A 651  ? 0.2986 0.4707 0.2527 0.0584  0.0274  -0.0338 649  ARG A CB  
4747  C CG  . ARG A 651  ? 0.3893 0.5666 0.3459 0.0622  0.0266  -0.0436 649  ARG A CG  
4748  C CD  . ARG A 651  ? 0.3592 0.5526 0.3129 0.0651  0.0267  -0.0488 649  ARG A CD  
4749  N NE  . ARG A 651  ? 0.3956 0.5925 0.3525 0.0690  0.0253  -0.0594 649  ARG A NE  
4750  C CZ  . ARG A 651  ? 0.4149 0.6200 0.3740 0.0711  0.0263  -0.0630 649  ARG A CZ  
4751  N NH1 . ARG A 651  ? 0.4361 0.6460 0.3947 0.0695  0.0288  -0.0566 649  ARG A NH1 
4752  N NH2 . ARG A 651  ? 0.4652 0.6735 0.4276 0.0749  0.0246  -0.0733 649  ARG A NH2 
4753  N N   . MET A 652  ? 0.2773 0.4133 0.2374 0.0516  0.0267  -0.0226 650  MET A N   
4754  C CA  . MET A 652  ? 0.2801 0.4006 0.2433 0.0507  0.0250  -0.0242 650  MET A CA  
4755  C C   . MET A 652  ? 0.2722 0.3903 0.2394 0.0522  0.0246  -0.0287 650  MET A C   
4756  O O   . MET A 652  ? 0.2645 0.3754 0.2342 0.0536  0.0226  -0.0345 650  MET A O   
4757  C CB  . MET A 652  ? 0.2935 0.4041 0.2566 0.0471  0.0253  -0.0164 650  MET A CB  
4758  C CG  . MET A 652  ? 0.2915 0.3875 0.2578 0.0461  0.0238  -0.0177 650  MET A CG  
4759  S SD  . MET A 652  ? 0.3200 0.4053 0.2864 0.0421  0.0240  -0.0095 650  MET A SD  
4760  C CE  . MET A 652  ? 0.2808 0.3645 0.2443 0.0417  0.0230  -0.0091 650  MET A CE  
4761  N N   . PRO A 653  ? 0.2839 0.4075 0.2520 0.0521  0.0264  -0.0263 651  PRO A N   
4762  C CA  . PRO A 653  ? 0.3143 0.4348 0.2866 0.0536  0.0258  -0.0306 651  PRO A CA  
4763  C C   . PRO A 653  ? 0.2843 0.4092 0.2585 0.0573  0.0243  -0.0401 651  PRO A C   
4764  O O   . PRO A 653  ? 0.2743 0.3908 0.2525 0.0582  0.0223  -0.0447 651  PRO A O   
4765  C CB  . PRO A 653  ? 0.2793 0.4085 0.2517 0.0530  0.0282  -0.0264 651  PRO A CB  
4766  C CG  . PRO A 653  ? 0.3355 0.4649 0.3052 0.0499  0.0295  -0.0177 651  PRO A CG  
4767  C CD  . PRO A 653  ? 0.2931 0.4246 0.2594 0.0503  0.0287  -0.0188 651  PRO A CD  
4768  N N   . THR A 654  ? 0.2528 0.3912 0.2245 0.0595  0.0250  -0.0430 652  THR A N   
4769  C CA  . THR A 654  ? 0.2563 0.3997 0.2299 0.0632  0.0233  -0.0527 652  THR A CA  
4770  C C   . THR A 654  ? 0.2863 0.4193 0.2610 0.0634  0.0205  -0.0564 652  THR A C   
4771  O O   . THR A 654  ? 0.2746 0.4028 0.2538 0.0654  0.0182  -0.0632 652  THR A O   
4772  C CB  . THR A 654  ? 0.2725 0.4334 0.2426 0.0653  0.0248  -0.0546 652  THR A CB  
4773  O OG1 . THR A 654  ? 0.3118 0.4826 0.2813 0.0649  0.0274  -0.0505 652  THR A OG1 
4774  C CG2 . THR A 654  ? 0.2998 0.4667 0.2723 0.0695  0.0230  -0.0654 652  THR A CG2 
4775  N N   . LEU A 655  ? 0.2585 0.3879 0.2296 0.0612  0.0206  -0.0518 653  LEU A N   
4776  C CA  . LEU A 655  ? 0.2644 0.3838 0.2365 0.0611  0.0180  -0.0547 653  LEU A CA  
4777  C C   . LEU A 655  ? 0.3126 0.4172 0.2892 0.0598  0.0163  -0.0546 653  LEU A C   
4778  O O   . LEU A 655  ? 0.2742 0.3725 0.2543 0.0609  0.0136  -0.0601 653  LEU A O   
4779  C CB  . LEU A 655  ? 0.2723 0.3905 0.2399 0.0587  0.0185  -0.0489 653  LEU A CB  
4780  C CG  . LEU A 655  ? 0.2663 0.3990 0.2294 0.0598  0.0199  -0.0487 653  LEU A CG  
4781  C CD1 . LEU A 655  ? 0.3080 0.4384 0.2674 0.0572  0.0202  -0.0423 653  LEU A CD1 
4782  C CD2 . LEU A 655  ? 0.3003 0.4398 0.2643 0.0634  0.0181  -0.0580 653  LEU A CD2 
4783  N N   . LEU A 656  ? 0.2828 0.3821 0.2597 0.0572  0.0177  -0.0483 654  LEU A N   
4784  C CA  . LEU A 656  ? 0.2668 0.3531 0.2478 0.0559  0.0162  -0.0478 654  LEU A CA  
4785  C C   . LEU A 656  ? 0.3084 0.3945 0.2946 0.0587  0.0143  -0.0552 654  LEU A C   
4786  O O   . LEU A 656  ? 0.2975 0.3743 0.2877 0.0588  0.0116  -0.0582 654  LEU A O   
4787  C CB  . LEU A 656  ? 0.2838 0.3669 0.2643 0.0533  0.0181  -0.0408 654  LEU A CB  
4788  C CG  . LEU A 656  ? 0.3067 0.3888 0.2833 0.0503  0.0198  -0.0330 654  LEU A CG  
4789  C CD1 . LEU A 656  ? 0.3096 0.3869 0.2875 0.0480  0.0210  -0.0275 654  LEU A CD1 
4790  C CD2 . LEU A 656  ? 0.2892 0.3627 0.2647 0.0488  0.0183  -0.0322 654  LEU A CD2 
4791  N N   . GLY A 657  ? 0.2850 0.3817 0.2719 0.0610  0.0155  -0.0581 655  GLY A N   
4792  C CA  . GLY A 657  ? 0.3063 0.4031 0.2990 0.0638  0.0136  -0.0651 655  GLY A CA  
4793  C C   . GLY A 657  ? 0.2552 0.3513 0.2506 0.0663  0.0106  -0.0729 655  GLY A C   
4794  O O   . GLY A 657  ? 0.3036 0.3926 0.3049 0.0673  0.0079  -0.0773 655  GLY A O   
4795  N N   . LEU A 658  ? 0.2620 0.3657 0.2536 0.0672  0.0110  -0.0746 656  LEU A N   
4796  C CA  . LEU A 658  ? 0.2600 0.3633 0.2541 0.0696  0.0081  -0.0821 656  LEU A CA  
4797  C C   . LEU A 658  ? 0.2577 0.3465 0.2540 0.0674  0.0056  -0.0804 656  LEU A C   
4798  O O   . LEU A 658  ? 0.2733 0.3561 0.2755 0.0687  0.0024  -0.0858 656  LEU A O   
4799  C CB  . LEU A 658  ? 0.2639 0.3792 0.2528 0.0709  0.0092  -0.0837 656  LEU A CB  
4800  C CG  . LEU A 658  ? 0.2884 0.4049 0.2796 0.0734  0.0062  -0.0917 656  LEU A CG  
4801  C CD1 . LEU A 658  ? 0.2945 0.4128 0.2927 0.0770  0.0038  -0.1009 656  LEU A CD1 
4802  C CD2 . LEU A 658  ? 0.2770 0.4066 0.2623 0.0745  0.0077  -0.0925 656  LEU A CD2 
4803  N N   . ILE A 659  ? 0.2683 0.3515 0.2603 0.0639  0.0070  -0.0728 657  ILE A N   
4804  C CA  . ILE A 659  ? 0.2448 0.3151 0.2384 0.0616  0.0050  -0.0706 657  ILE A CA  
4805  C C   . ILE A 659  ? 0.2597 0.3200 0.2591 0.0608  0.0033  -0.0705 657  ILE A C   
4806  O O   . ILE A 659  ? 0.2559 0.3081 0.2599 0.0607  0.0003  -0.0730 657  ILE A O   
4807  C CB  . ILE A 659  ? 0.2575 0.3250 0.2454 0.0582  0.0071  -0.0625 657  ILE A CB  
4808  C CG1 . ILE A 659  ? 0.2749 0.3513 0.2579 0.0591  0.0080  -0.0631 657  ILE A CG1 
4809  C CG2 . ILE A 659  ? 0.2590 0.3133 0.2486 0.0556  0.0054  -0.0596 657  ILE A CG2 
4810  C CD1 . ILE A 659  ? 0.2640 0.3402 0.2417 0.0562  0.0102  -0.0553 657  ILE A CD1 
4811  N N   . ILE A 660  ? 0.2553 0.3164 0.2548 0.0602  0.0051  -0.0672 658  ILE A N   
4812  C CA  . ILE A 660  ? 0.2590 0.3115 0.2640 0.0594  0.0036  -0.0667 658  ILE A CA  
4813  C C   . ILE A 660  ? 0.2904 0.3424 0.3025 0.0624  0.0002  -0.0748 658  ILE A C   
4814  O O   . ILE A 660  ? 0.2843 0.3266 0.3014 0.0616  -0.0026 -0.0754 658  ILE A O   
4815  C CB  . ILE A 660  ? 0.2447 0.3002 0.2486 0.0587  0.0062  -0.0627 658  ILE A CB  
4816  C CG1 . ILE A 660  ? 0.2623 0.3144 0.2610 0.0551  0.0086  -0.0543 658  ILE A CG1 
4817  C CG2 . ILE A 660  ? 0.2775 0.3271 0.2878 0.0590  0.0043  -0.0643 658  ILE A CG2 
4818  C CD1 . ILE A 660  ? 0.3338 0.3908 0.3309 0.0545  0.0113  -0.0502 658  ILE A CD1 
4819  N N   . ARG A 661  ? 0.2610 0.3236 0.2738 0.0659  0.0004  -0.0811 659  ARG A N   
4820  C CA  . ARG A 661  ? 0.2808 0.3437 0.3012 0.0691  -0.0028 -0.0893 659  ARG A CA  
4821  C C   . ARG A 661  ? 0.3053 0.3661 0.3282 0.0703  -0.0060 -0.0946 659  ARG A C   
4822  O O   . ARG A 661  ? 0.3023 0.3572 0.3328 0.0715  -0.0097 -0.0993 659  ARG A O   
4823  C CB  . ARG A 661  ? 0.2887 0.3645 0.3096 0.0726  -0.0015 -0.0945 659  ARG A CB  
4824  C CG  . ARG A 661  ? 0.2955 0.3720 0.3167 0.0718  0.0006  -0.0905 659  ARG A CG  
4825  C CD  . ARG A 661  ? 0.2814 0.3721 0.3020 0.0750  0.0025  -0.0948 659  ARG A CD  
4826  N NE  . ARG A 661  ? 0.2983 0.3934 0.3256 0.0791  -0.0004 -0.1048 659  ARG A NE  
4827  C CZ  . ARG A 661  ? 0.3280 0.4354 0.3541 0.0824  -0.0001 -0.1114 659  ARG A CZ  
4828  N NH1 . ARG A 661  ? 0.3383 0.4551 0.3567 0.0819  0.0028  -0.1088 659  ARG A NH1 
4829  N NH2 . ARG A 661  ? 0.3028 0.4133 0.3359 0.0863  -0.0030 -0.1210 659  ARG A NH2 
4830  N N   . GLU A 662  ? 0.2659 0.3315 0.2831 0.0701  -0.0048 -0.0941 660  GLU A N   
4831  C CA  . GLU A 662  ? 0.3036 0.3678 0.3231 0.0714  -0.0078 -0.0995 660  GLU A CA  
4832  C C   . GLU A 662  ? 0.2752 0.3263 0.2964 0.0682  -0.0098 -0.0953 660  GLU A C   
4833  O O   . GLU A 662  ? 0.3092 0.3552 0.3367 0.0691  -0.0135 -0.0999 660  GLU A O   
4834  C CB  . GLU A 662  ? 0.3194 0.3944 0.3323 0.0725  -0.0059 -0.1008 660  GLU A CB  
4835  C CG  . GLU A 662  ? 0.3116 0.3867 0.3271 0.0742  -0.0091 -0.1073 660  GLU A CG  
4836  C CD  . GLU A 662  ? 0.3168 0.4033 0.3258 0.0754  -0.0074 -0.1087 660  GLU A CD  
4837  O OE1 . GLU A 662  ? 0.3095 0.4001 0.3112 0.0734  -0.0039 -0.1020 660  GLU A OE1 
4838  O OE2 . GLU A 662  ? 0.3143 0.4057 0.3258 0.0782  -0.0097 -0.1165 660  GLU A OE2 
4839  N N   . ALA A 663  ? 0.2541 0.3000 0.2703 0.0646  -0.0075 -0.0869 661  ALA A N   
4840  C CA  . ALA A 663  ? 0.2374 0.2730 0.2537 0.0616  -0.0089 -0.0828 661  ALA A CA  
4841  C C   . ALA A 663  ? 0.2992 0.3245 0.3184 0.0587  -0.0094 -0.0774 661  ALA A C   
4842  O O   . ALA A 663  ? 0.3376 0.3549 0.3563 0.0559  -0.0101 -0.0731 661  ALA A O   
4843  C CB  . ALA A 663  ? 0.3070 0.3452 0.3154 0.0597  -0.0063 -0.0780 661  ALA A CB  
4844  N N   . GLY A 664  ? 0.3126 0.3382 0.3347 0.0593  -0.0091 -0.0774 662  GLY A N   
4845  C CA  . GLY A 664  ? 0.3211 0.3374 0.3460 0.0566  -0.0097 -0.0724 662  GLY A CA  
4846  C C   . GLY A 664  ? 0.2957 0.3094 0.3143 0.0532  -0.0066 -0.0642 662  GLY A C   
4847  O O   . GLY A 664  ? 0.3552 0.3606 0.3751 0.0505  -0.0073 -0.0596 662  GLY A O   
4848  N N   . LYS A 665  ? 0.2741 0.2951 0.2861 0.0533  -0.0033 -0.0622 663  LYS A N   
4849  C CA  . LYS A 665  ? 0.2655 0.2842 0.2720 0.0502  -0.0006 -0.0547 663  LYS A CA  
4850  C C   . LYS A 665  ? 0.2382 0.2582 0.2443 0.0496  0.0014  -0.0514 663  LYS A C   
4851  O O   . LYS A 665  ? 0.2491 0.2759 0.2563 0.0520  0.0021  -0.0545 663  LYS A O   
4852  C CB  . LYS A 665  ? 0.2839 0.3095 0.2840 0.0504  0.0017  -0.0536 663  LYS A CB  
4853  C CG  . LYS A 665  ? 0.3261 0.3515 0.3260 0.0510  -0.0001 -0.0568 663  LYS A CG  
4854  C CD  . LYS A 665  ? 0.3401 0.3553 0.3415 0.0484  -0.0018 -0.0540 663  LYS A CD  
4855  C CE  . LYS A 665  ? 0.4003 0.4160 0.4005 0.0487  -0.0031 -0.0562 663  LYS A CE  
4856  N NZ  . LYS A 665  ? 0.3824 0.3887 0.3857 0.0466  -0.0054 -0.0547 663  LYS A NZ  
4857  N N   . SER A 666  ? 0.3118 0.3255 0.3163 0.0465  0.0024  -0.0453 664  SER A N   
4858  C CA  . SER A 666  ? 0.2833 0.2985 0.2865 0.0456  0.0046  -0.0413 664  SER A CA  
4859  C C   . SER A 666  ? 0.2768 0.3003 0.2745 0.0458  0.0077  -0.0391 664  SER A C   
4860  O O   . SER A 666  ? 0.2751 0.3015 0.2694 0.0460  0.0082  -0.0394 664  SER A O   
4861  C CB  . SER A 666  ? 0.3279 0.3348 0.3307 0.0422  0.0047  -0.0356 664  SER A CB  
4862  O OG  . SER A 666  ? 0.3293 0.3353 0.3273 0.0403  0.0061  -0.0319 664  SER A OG  
4863  N N   . ALA A 667  ? 0.2794 0.3065 0.2763 0.0456  0.0097  -0.0366 665  ALA A N   
4864  C CA  . ALA A 667  ? 0.2571 0.2922 0.2494 0.0454  0.0126  -0.0336 665  ALA A CA  
4865  C C   . ALA A 667  ? 0.3004 0.3318 0.2888 0.0428  0.0135  -0.0284 665  ALA A C   
4866  O O   . ALA A 667  ? 0.2665 0.3036 0.2513 0.0430  0.0146  -0.0275 665  ALA A O   
4867  C CB  . ALA A 667  ? 0.3067 0.3454 0.2996 0.0452  0.0144  -0.0311 665  ALA A CB  
4868  N N   . LEU A 668  ? 0.2834 0.3060 0.2725 0.0402  0.0129  -0.0249 666  LEU A N   
4869  C CA  . LEU A 668  ? 0.2896 0.3086 0.2756 0.0378  0.0136  -0.0204 666  LEU A CA  
4870  C C   . LEU A 668  ? 0.3182 0.3372 0.3026 0.0384  0.0125  -0.0227 666  LEU A C   
4871  O O   . LEU A 668  ? 0.3138 0.3355 0.2948 0.0377  0.0136  -0.0202 666  LEU A O   
4872  C CB  . LEU A 668  ? 0.3337 0.3435 0.3212 0.0353  0.0128  -0.0175 666  LEU A CB  
4873  C CG  . LEU A 668  ? 0.4461 0.4549 0.4338 0.0337  0.0142  -0.0133 666  LEU A CG  
4874  C CD1 . LEU A 668  ? 0.3817 0.3820 0.3710 0.0315  0.0131  -0.0114 666  LEU A CD1 
4875  C CD2 . LEU A 668  ? 0.4572 0.4698 0.4416 0.0326  0.0163  -0.0091 666  LEU A CD2 
4876  N N   . ASN A 669  ? 0.2815 0.2976 0.2688 0.0396  0.0102  -0.0273 667  ASN A N   
4877  C CA  . ASN A 669  ? 0.3094 0.3252 0.2955 0.0401  0.0090  -0.0296 667  ASN A CA  
4878  C C   . ASN A 669  ? 0.2883 0.3139 0.2723 0.0426  0.0097  -0.0327 667  ASN A C   
4879  O O   . ASN A 669  ? 0.2765 0.3039 0.2579 0.0426  0.0097  -0.0328 667  ASN A O   
4880  C CB  . ASN A 669  ? 0.3756 0.3853 0.3661 0.0404  0.0061  -0.0332 667  ASN A CB  
4881  C CG  . ASN A 669  ? 0.3808 0.3816 0.3729 0.0377  0.0053  -0.0295 667  ASN A CG  
4882  O OD1 . ASN A 669  ? 0.4467 0.4429 0.4432 0.0376  0.0034  -0.0310 667  ASN A OD1 
4883  N ND2 . ASN A 669  ? 0.4622 0.4609 0.4510 0.0354  0.0068  -0.0247 667  ASN A ND2 
4884  N N   . ALA A 670  ? 0.2581 0.2905 0.2431 0.0447  0.0104  -0.0353 668  ALA A N   
4885  C CA  . ALA A 670  ? 0.2546 0.2978 0.2372 0.0470  0.0113  -0.0380 668  ALA A CA  
4886  C C   . ALA A 670  ? 0.2616 0.3099 0.2395 0.0455  0.0139  -0.0323 668  ALA A C   
4887  O O   . ALA A 670  ? 0.2598 0.3146 0.2346 0.0463  0.0143  -0.0328 668  ALA A O   
4888  C CB  . ALA A 670  ? 0.2619 0.3119 0.2471 0.0496  0.0115  -0.0424 668  ALA A CB  
4889  N N   . ILE A 671  ? 0.2552 0.3007 0.2328 0.0434  0.0154  -0.0269 669  ILE A N   
4890  C CA  . ILE A 671  ? 0.2561 0.3053 0.2304 0.0418  0.0174  -0.0210 669  ILE A CA  
4891  C C   . ILE A 671  ? 0.2656 0.3109 0.2377 0.0404  0.0167  -0.0192 669  ILE A C   
4892  O O   . ILE A 671  ? 0.2768 0.3283 0.2459 0.0405  0.0176  -0.0175 669  ILE A O   
4893  C CB  . ILE A 671  ? 0.2676 0.3127 0.2428 0.0396  0.0186  -0.0158 669  ILE A CB  
4894  C CG1 . ILE A 671  ? 0.2604 0.3116 0.2373 0.0409  0.0196  -0.0168 669  ILE A CG1 
4895  C CG2 . ILE A 671  ? 0.2930 0.3392 0.2657 0.0375  0.0199  -0.0096 669  ILE A CG2 
4896  C CD1 . ILE A 671  ? 0.2926 0.3387 0.2714 0.0390  0.0203  -0.0129 669  ILE A CD1 
4897  N N   . ALA A 672  ? 0.2698 0.3052 0.2435 0.0391  0.0152  -0.0195 670  ALA A N   
4898  C CA  . ALA A 672  ? 0.2660 0.2973 0.2381 0.0378  0.0145  -0.0181 670  ALA A CA  
4899  C C   . ALA A 672  ? 0.2475 0.2841 0.2181 0.0398  0.0136  -0.0222 670  ALA A C   
4900  O O   . ALA A 672  ? 0.2882 0.3267 0.2562 0.0393  0.0139  -0.0202 670  ALA A O   
4901  C CB  . ALA A 672  ? 0.2694 0.2903 0.2439 0.0364  0.0129  -0.0185 670  ALA A CB  
4902  N N   . GLU A 673  ? 0.2488 0.2880 0.2215 0.0422  0.0124  -0.0281 671  GLU A N   
4903  C CA  . GLU A 673  ? 0.2498 0.2944 0.2217 0.0444  0.0112  -0.0330 671  GLU A CA  
4904  C C   . GLU A 673  ? 0.2632 0.3190 0.2311 0.0453  0.0130  -0.0316 671  GLU A C   
4905  O O   . GLU A 673  ? 0.2569 0.3159 0.2223 0.0455  0.0127  -0.0316 671  GLU A O   
4906  C CB  . GLU A 673  ? 0.2741 0.3195 0.2498 0.0469  0.0095  -0.0398 671  GLU A CB  
4907  C CG  . GLU A 673  ? 0.3372 0.3886 0.3128 0.0495  0.0080  -0.0460 671  GLU A CG  
4908  C CD  . GLU A 673  ? 0.3510 0.3949 0.3284 0.0489  0.0056  -0.0479 671  GLU A CD  
4909  O OE1 . GLU A 673  ? 0.3877 0.4217 0.3671 0.0467  0.0048  -0.0453 671  GLU A OE1 
4910  O OE2 . GLU A 673  ? 0.3225 0.3707 0.2992 0.0505  0.0044  -0.0520 671  GLU A OE2 
4911  N N   . VAL A 674  ? 0.2317 0.2941 0.1992 0.0458  0.0148  -0.0300 672  VAL A N   
4912  C CA  . VAL A 674  ? 0.2433 0.3175 0.2074 0.0465  0.0165  -0.0281 672  VAL A CA  
4913  C C   . VAL A 674  ? 0.2511 0.3241 0.2126 0.0439  0.0176  -0.0209 672  VAL A C   
4914  O O   . VAL A 674  ? 0.2287 0.3087 0.1872 0.0442  0.0180  -0.0195 672  VAL A O   
4915  C CB  . VAL A 674  ? 0.2282 0.3102 0.1930 0.0477  0.0181  -0.0283 672  VAL A CB  
4916  C CG1 . VAL A 674  ? 0.2630 0.3583 0.2242 0.0483  0.0199  -0.0258 672  VAL A CG1 
4917  C CG2 . VAL A 674  ? 0.2407 0.3239 0.2087 0.0506  0.0167  -0.0362 672  VAL A CG2 
4918  N N   . ARG A 675  ? 0.2418 0.3062 0.2047 0.0415  0.0180  -0.0163 673  ARG A N   
4919  C CA  . ARG A 675  ? 0.2129 0.2751 0.1742 0.0391  0.0186  -0.0100 673  ARG A CA  
4920  C C   . ARG A 675  ? 0.2129 0.2727 0.1728 0.0390  0.0172  -0.0111 673  ARG A C   
4921  O O   . ARG A 675  ? 0.2336 0.2976 0.1913 0.0384  0.0177  -0.0076 673  ARG A O   
4922  C CB  . ARG A 675  ? 0.2180 0.2707 0.1816 0.0367  0.0188  -0.0062 673  ARG A CB  
4923  C CG  . ARG A 675  ? 0.2345 0.2898 0.1993 0.0363  0.0203  -0.0035 673  ARG A CG  
4924  C CD  . ARG A 675  ? 0.2717 0.3178 0.2385 0.0337  0.0203  0.0007  673  ARG A CD  
4925  N NE  . ARG A 675  ? 0.2587 0.3043 0.2247 0.0319  0.0205  0.0058  673  ARG A NE  
4926  C CZ  . ARG A 675  ? 0.2653 0.3029 0.2327 0.0298  0.0202  0.0089  673  ARG A CZ  
4927  N NH1 . ARG A 675  ? 0.2364 0.2663 0.2059 0.0291  0.0197  0.0076  673  ARG A NH1 
4928  N NH2 . ARG A 675  ? 0.2426 0.2804 0.2099 0.0284  0.0202  0.0133  673  ARG A NH2 
4929  N N   . GLU A 676  ? 0.2263 0.2793 0.1878 0.0396  0.0155  -0.0158 674  GLU A N   
4930  C CA  . GLU A 676  ? 0.2311 0.2814 0.1916 0.0394  0.0141  -0.0170 674  GLU A CA  
4931  C C   . GLU A 676  ? 0.2342 0.2947 0.1920 0.0414  0.0140  -0.0194 674  GLU A C   
4932  O O   . GLU A 676  ? 0.2323 0.2944 0.1880 0.0408  0.0138  -0.0173 674  GLU A O   
4933  C CB  . GLU A 676  ? 0.2360 0.2780 0.1992 0.0397  0.0121  -0.0217 674  GLU A CB  
4934  C CG  . GLU A 676  ? 0.2748 0.3126 0.2377 0.0392  0.0106  -0.0226 674  GLU A CG  
4935  C CD  . GLU A 676  ? 0.3955 0.4247 0.3589 0.0365  0.0106  -0.0181 674  GLU A CD  
4936  O OE1 . GLU A 676  ? 0.4470 0.4743 0.4107 0.0350  0.0120  -0.0139 674  GLU A OE1 
4937  O OE2 . GLU A 676  ? 0.4068 0.4315 0.3704 0.0359  0.0093  -0.0190 674  GLU A OE2 
4938  N N   . ALA A 677  ? 0.2420 0.3103 0.1999 0.0438  0.0141  -0.0239 675  ALA A N   
4939  C CA  . ALA A 677  ? 0.2215 0.3009 0.1766 0.0458  0.0141  -0.0265 675  ALA A CA  
4940  C C   . ALA A 677  ? 0.2499 0.3371 0.2019 0.0447  0.0158  -0.0200 675  ALA A C   
4941  O O   . ALA A 677  ? 0.2368 0.3287 0.1863 0.0448  0.0155  -0.0190 675  ALA A O   
4942  C CB  . ALA A 677  ? 0.2134 0.3004 0.1696 0.0487  0.0140  -0.0327 675  ALA A CB  
4943  N N   . ILE A 678  ? 0.2210 0.3096 0.1735 0.0435  0.0176  -0.0153 676  ILE A N   
4944  C CA  . ILE A 678  ? 0.2050 0.3004 0.1556 0.0421  0.0191  -0.0082 676  ILE A CA  
4945  C C   . ILE A 678  ? 0.2209 0.3100 0.1711 0.0399  0.0184  -0.0037 676  ILE A C   
4946  O O   . ILE A 678  ? 0.2241 0.3196 0.1721 0.0395  0.0185  -0.0002 676  ILE A O   
4947  C CB  . ILE A 678  ? 0.2080 0.3034 0.1602 0.0409  0.0207  -0.0041 676  ILE A CB  
4948  C CG1 . ILE A 678  ? 0.2478 0.3525 0.2001 0.0432  0.0216  -0.0081 676  ILE A CG1 
4949  C CG2 . ILE A 678  ? 0.2638 0.3630 0.2155 0.0387  0.0218  0.0043  676  ILE A CG2 
4950  C CD1 . ILE A 678  ? 0.2331 0.3352 0.1879 0.0423  0.0228  -0.0058 676  ILE A CD1 
4951  N N   . ASP A 679  ? 0.2174 0.2940 0.1699 0.0385  0.0176  -0.0036 677  ASP A N   
4952  C CA  . ASP A 679  ? 0.2092 0.2794 0.1619 0.0365  0.0169  0.0004  677  ASP A CA  
4953  C C   . ASP A 679  ? 0.2460 0.3178 0.1968 0.0375  0.0155  -0.0026 677  ASP A C   
4954  O O   . ASP A 679  ? 0.2358 0.3091 0.1856 0.0365  0.0153  0.0014  677  ASP A O   
4955  C CB  . ASP A 679  ? 0.2293 0.2870 0.1848 0.0349  0.0164  0.0005  677  ASP A CB  
4956  C CG  . ASP A 679  ? 0.2903 0.3459 0.2478 0.0336  0.0176  0.0042  677  ASP A CG  
4957  O OD1 . ASP A 679  ? 0.2898 0.3515 0.2470 0.0330  0.0187  0.0090  677  ASP A OD1 
4958  O OD2 . ASP A 679  ? 0.3271 0.3748 0.2866 0.0331  0.0173  0.0024  677  ASP A OD2 
4959  N N   . PHE A 680  ? 0.2202 0.2917 0.1710 0.0394  0.0143  -0.0095 678  PHE A N   
4960  C CA  . PHE A 680  ? 0.2200 0.2943 0.1691 0.0406  0.0129  -0.0126 678  PHE A CA  
4961  C C   . PHE A 680  ? 0.2123 0.2993 0.1582 0.0413  0.0136  -0.0104 678  PHE A C   
4962  O O   . PHE A 680  ? 0.2283 0.3169 0.1726 0.0408  0.0130  -0.0081 678  PHE A O   
4963  C CB  . PHE A 680  ? 0.2204 0.2942 0.1705 0.0428  0.0115  -0.0207 678  PHE A CB  
4964  C CG  . PHE A 680  ? 0.2123 0.2741 0.1654 0.0420  0.0099  -0.0231 678  PHE A CG  
4965  C CD1 . PHE A 680  ? 0.2360 0.2910 0.1893 0.0403  0.0091  -0.0208 678  PHE A CD1 
4966  C CD2 . PHE A 680  ? 0.2433 0.3010 0.1993 0.0429  0.0092  -0.0277 678  PHE A CD2 
4967  C CE1 . PHE A 680  ? 0.2666 0.3115 0.2226 0.0395  0.0077  -0.0229 678  PHE A CE1 
4968  C CE2 . PHE A 680  ? 0.2560 0.3034 0.2149 0.0420  0.0077  -0.0294 678  PHE A CE2 
4969  C CZ  . PHE A 680  ? 0.2357 0.2770 0.1946 0.0403  0.0070  -0.0270 678  PHE A CZ  
4970  N N   . LEU A 681  ? 0.2083 0.3049 0.1532 0.0427  0.0149  -0.0112 679  LEU A N   
4971  C CA  . LEU A 681  ? 0.1987 0.3088 0.1404 0.0434  0.0156  -0.0090 679  LEU A CA  
4972  C C   . LEU A 681  ? 0.2339 0.3444 0.1752 0.0409  0.0162  -0.0003 679  LEU A C   
4973  O O   . LEU A 681  ? 0.2301 0.3465 0.1693 0.0408  0.0157  0.0019  679  LEU A O   
4974  C CB  . LEU A 681  ? 0.2367 0.3569 0.1779 0.0449  0.0171  -0.0105 679  LEU A CB  
4975  C CG  . LEU A 681  ? 0.2360 0.3586 0.1777 0.0479  0.0163  -0.0197 679  LEU A CG  
4976  C CD1 . LEU A 681  ? 0.2360 0.3643 0.1786 0.0490  0.0178  -0.0208 679  LEU A CD1 
4977  C CD2 . LEU A 681  ? 0.2288 0.3619 0.1677 0.0501  0.0153  -0.0240 679  LEU A CD2 
4978  N N   . ARG A 682  ? 0.2045 0.3088 0.1482 0.0389  0.0171  0.0047  680  ARG A N   
4979  C CA  . ARG A 682  ? 0.2124 0.3174 0.1567 0.0366  0.0175  0.0130  680  ARG A CA  
4980  C C   . ARG A 682  ? 0.2349 0.3312 0.1802 0.0353  0.0160  0.0144  680  ARG A C   
4981  O O   . ARG A 682  ? 0.2351 0.3346 0.1800 0.0342  0.0156  0.0197  680  ARG A O   
4982  C CB  . ARG A 682  ? 0.2061 0.3074 0.1533 0.0349  0.0187  0.0176  680  ARG A CB  
4983  C CG  . ARG A 682  ? 0.2166 0.3285 0.1629 0.0357  0.0203  0.0181  680  ARG A CG  
4984  C CD  . ARG A 682  ? 0.2509 0.3578 0.2004 0.0342  0.0213  0.0217  680  ARG A CD  
4985  N NE  . ARG A 682  ? 0.2420 0.3599 0.1908 0.0348  0.0229  0.0231  680  ARG A NE  
4986  C CZ  . ARG A 682  ? 0.2551 0.3709 0.2063 0.0340  0.0239  0.0248  680  ARG A CZ  
4987  N NH1 . ARG A 682  ? 0.2613 0.3649 0.2156 0.0326  0.0235  0.0254  680  ARG A NH1 
4988  N NH2 . ARG A 682  ? 0.2621 0.3890 0.2127 0.0348  0.0254  0.0257  680  ARG A NH2 
4989  N N   . TYR A 683  ? 0.2050 0.2907 0.1515 0.0355  0.0151  0.0098  681  TYR A N   
4990  C CA  . TYR A 683  ? 0.1958 0.2735 0.1434 0.0343  0.0137  0.0107  681  TYR A CA  
4991  C C   . TYR A 683  ? 0.2431 0.3267 0.1880 0.0355  0.0126  0.0087  681  TYR A C   
4992  O O   . TYR A 683  ? 0.2308 0.3146 0.1758 0.0344  0.0119  0.0128  681  TYR A O   
4993  C CB  . TYR A 683  ? 0.2164 0.2825 0.1660 0.0342  0.0131  0.0063  681  TYR A CB  
4994  C CG  . TYR A 683  ? 0.2151 0.2735 0.1657 0.0331  0.0118  0.0066  681  TYR A CG  
4995  C CD1 . TYR A 683  ? 0.2249 0.2778 0.1778 0.0311  0.0118  0.0118  681  TYR A CD1 
4996  C CD2 . TYR A 683  ? 0.1993 0.2562 0.1490 0.0342  0.0104  0.0016  681  TYR A CD2 
4997  C CE1 . TYR A 683  ? 0.2234 0.2698 0.1774 0.0302  0.0106  0.0118  681  TYR A CE1 
4998  C CE2 . TYR A 683  ? 0.2118 0.2624 0.1626 0.0332  0.0092  0.0020  681  TYR A CE2 
4999  C CZ  . TYR A 683  ? 0.2458 0.2912 0.1986 0.0313  0.0094  0.0070  681  TYR A CZ  
5000  O OH  . TYR A 683  ? 0.2569 0.2964 0.2109 0.0304  0.0083  0.0071  681  TYR A OH  
5001  N N   . TYR A 684  ? 0.2265 0.3151 0.1695 0.0378  0.0122  0.0023  682  TYR A N   
5002  C CA  . TYR A 684  ? 0.2180 0.3125 0.1585 0.0390  0.0110  0.0000  682  TYR A CA  
5003  C C   . TYR A 684  ? 0.2270 0.3338 0.1651 0.0388  0.0116  0.0052  682  TYR A C   
5004  O O   . TYR A 684  ? 0.2241 0.3340 0.1609 0.0387  0.0106  0.0068  682  TYR A O   
5005  C CB  . TYR A 684  ? 0.2093 0.3065 0.1489 0.0415  0.0101  -0.0085 682  TYR A CB  
5006  C CG  . TYR A 684  ? 0.1982 0.2834 0.1407 0.0415  0.0090  -0.0132 682  TYR A CG  
5007  C CD1 . TYR A 684  ? 0.2103 0.2855 0.1544 0.0398  0.0081  -0.0114 682  TYR A CD1 
5008  C CD2 . TYR A 684  ? 0.2339 0.3180 0.1776 0.0431  0.0088  -0.0191 682  TYR A CD2 
5009  C CE1 . TYR A 684  ? 0.2506 0.3157 0.1973 0.0395  0.0071  -0.0151 682  TYR A CE1 
5010  C CE2 . TYR A 684  ? 0.2216 0.2952 0.1684 0.0428  0.0076  -0.0227 682  TYR A CE2 
5011  C CZ  . TYR A 684  ? 0.2466 0.3109 0.1947 0.0409  0.0068  -0.0205 682  TYR A CZ  
5012  O OH  . TYR A 684  ? 0.2375 0.2921 0.1886 0.0405  0.0056  -0.0237 682  TYR A OH  
5013  N N   . ALA A 685  ? 0.2156 0.3296 0.1534 0.0387  0.0132  0.0082  683  ALA A N   
5014  C CA  . ALA A 685  ? 0.2169 0.3426 0.1529 0.0381  0.0138  0.0144  683  ALA A CA  
5015  C C   . ALA A 685  ? 0.2619 0.3825 0.2001 0.0356  0.0132  0.0220  683  ALA A C   
5016  O O   . ALA A 685  ? 0.2386 0.3653 0.1755 0.0353  0.0124  0.0255  683  ALA A O   
5017  C CB  . ALA A 685  ? 0.2381 0.3715 0.1741 0.0382  0.0157  0.0168  683  ALA A CB  
5018  N N   . GLU A 686  ? 0.2375 0.3471 0.1793 0.0339  0.0134  0.0246  684  GLU A N   
5019  C CA  . GLU A 686  ? 0.2547 0.3590 0.1994 0.0316  0.0127  0.0313  684  GLU A CA  
5020  C C   . GLU A 686  ? 0.2628 0.3618 0.2074 0.0317  0.0110  0.0293  684  GLU A C   
5021  O O   . GLU A 686  ? 0.2473 0.3485 0.1925 0.0308  0.0100  0.0342  684  GLU A O   
5022  C CB  . GLU A 686  ? 0.2922 0.3861 0.2410 0.0300  0.0132  0.0334  684  GLU A CB  
5023  C CG  . GLU A 686  ? 0.3349 0.4220 0.2875 0.0279  0.0121  0.0391  684  GLU A CG  
5024  C CD  . GLU A 686  ? 0.3976 0.4930 0.3514 0.0266  0.0118  0.0473  684  GLU A CD  
5025  O OE1 . GLU A 686  ? 0.3893 0.4958 0.3413 0.0269  0.0128  0.0497  684  GLU A OE1 
5026  O OE2 . GLU A 686  ? 0.3739 0.4651 0.3310 0.0252  0.0105  0.0517  684  GLU A OE2 
5027  N N   . GLN A 687  ? 0.2319 0.3241 0.1759 0.0329  0.0104  0.0222  685  GLN A N   
5028  C CA  . GLN A 687  ? 0.2276 0.3151 0.1716 0.0330  0.0088  0.0200  685  GLN A CA  
5029  C C   . GLN A 687  ? 0.2510 0.3493 0.1918 0.0341  0.0080  0.0201  685  GLN A C   
5030  O O   . GLN A 687  ? 0.2347 0.3322 0.1759 0.0335  0.0068  0.0223  685  GLN A O   
5031  C CB  . GLN A 687  ? 0.2222 0.3020 0.1664 0.0341  0.0084  0.0125  685  GLN A CB  
5032  C CG  . GLN A 687  ? 0.2352 0.3033 0.1826 0.0327  0.0088  0.0127  685  GLN A CG  
5033  C CD  . GLN A 687  ? 0.3027 0.3644 0.2530 0.0308  0.0082  0.0176  685  GLN A CD  
5034  O OE1 . GLN A 687  ? 0.2757 0.3352 0.2262 0.0307  0.0070  0.0171  685  GLN A OE1 
5035  N NE2 . GLN A 687  ? 0.3166 0.3756 0.2696 0.0293  0.0090  0.0222  685  GLN A NE2 
5036  N N   . THR A 688  ? 0.2170 0.3260 0.1547 0.0358  0.0088  0.0176  686  THR A N   
5037  C CA  . THR A 688  ? 0.1989 0.3199 0.1333 0.0368  0.0081  0.0178  686  THR A CA  
5038  C C   . THR A 688  ? 0.2175 0.3442 0.1526 0.0350  0.0080  0.0269  686  THR A C   
5039  O O   . THR A 688  ? 0.2504 0.3803 0.1848 0.0348  0.0067  0.0291  686  THR A O   
5040  C CB  . THR A 688  ? 0.2228 0.3551 0.1540 0.0390  0.0091  0.0134  686  THR A CB  
5041  O OG1 . THR A 688  ? 0.2460 0.3735 0.1771 0.0408  0.0085  0.0046  686  THR A OG1 
5042  C CG2 . THR A 688  ? 0.2257 0.3725 0.1533 0.0399  0.0086  0.0148  686  THR A CG2 
5043  N N   . ARG A 689  ? 0.2317 0.3595 0.1686 0.0337  0.0093  0.0325  687  ARG A N   
5044  C CA  . ARG A 689  ? 0.2382 0.3712 0.1768 0.0317  0.0090  0.0418  687  ARG A CA  
5045  C C   . ARG A 689  ? 0.2481 0.3713 0.1905 0.0301  0.0074  0.0453  687  ARG A C   
5046  O O   . ARG A 689  ? 0.2759 0.4037 0.2195 0.0289  0.0064  0.0520  687  ARG A O   
5047  C CB  . ARG A 689  ? 0.2677 0.4027 0.2085 0.0305  0.0105  0.0468  687  ARG A CB  
5048  C CG  . ARG A 689  ? 0.2832 0.4320 0.2203 0.0318  0.0120  0.0457  687  ARG A CG  
5049  C CD  . ARG A 689  ? 0.3150 0.4661 0.2548 0.0302  0.0133  0.0521  687  ARG A CD  
5050  N NE  . ARG A 689  ? 0.3160 0.4545 0.2589 0.0297  0.0139  0.0498  687  ARG A NE  
5051  C CZ  . ARG A 689  ? 0.3548 0.4934 0.2966 0.0309  0.0154  0.0449  687  ARG A CZ  
5052  N NH1 . ARG A 689  ? 0.3337 0.4841 0.2718 0.0329  0.0164  0.0412  687  ARG A NH1 
5053  N NH2 . ARG A 689  ? 0.3300 0.4571 0.2749 0.0302  0.0157  0.0434  687  ARG A NH2 
5054  N N   . ARG A 690  ? 0.2452 0.3554 0.1896 0.0301  0.0071  0.0411  688  ARG A N   
5055  C CA  . ARG A 690  ? 0.2849 0.3859 0.2328 0.0288  0.0056  0.0434  688  ARG A CA  
5056  C C   . ARG A 690  ? 0.2705 0.3726 0.2165 0.0298  0.0041  0.0403  688  ARG A C   
5057  O O   . ARG A 690  ? 0.2645 0.3625 0.2133 0.0287  0.0027  0.0436  688  ARG A O   
5058  C CB  . ARG A 690  ? 0.2570 0.3446 0.2079 0.0283  0.0059  0.0400  688  ARG A CB  
5059  C CG  . ARG A 690  ? 0.2741 0.3584 0.2280 0.0271  0.0070  0.0434  688  ARG A CG  
5060  C CD  . ARG A 690  ? 0.3010 0.3845 0.2597 0.0251  0.0062  0.0515  688  ARG A CD  
5061  N NE  . ARG A 690  ? 0.3303 0.4043 0.2924 0.0244  0.0047  0.0514  688  ARG A NE  
5062  C CZ  . ARG A 690  ? 0.3428 0.4184 0.3064 0.0239  0.0031  0.0548  688  ARG A CZ  
5063  N NH1 . ARG A 690  ? 0.3230 0.4094 0.2849 0.0240  0.0026  0.0590  688  ARG A NH1 
5064  N NH2 . ARG A 690  ? 0.2875 0.3542 0.2545 0.0235  0.0018  0.0539  688  ARG A NH2 
5065  N N   . THR A 691  ? 0.2326 0.3399 0.1743 0.0318  0.0042  0.0340  689  THR A N   
5066  C CA  . THR A 691  ? 0.2223 0.3275 0.1630 0.0326  0.0026  0.0298  689  THR A CA  
5067  C C   . THR A 691  ? 0.2843 0.4017 0.2207 0.0342  0.0019  0.0281  689  THR A C   
5068  O O   . THR A 691  ? 0.3129 0.4321 0.2492 0.0340  0.0004  0.0297  689  THR A O   
5069  C CB  . THR A 691  ? 0.2617 0.3571 0.2027 0.0335  0.0026  0.0221  689  THR A CB  
5070  O OG1 . THR A 691  ? 0.2892 0.3887 0.2277 0.0351  0.0036  0.0170  689  THR A OG1 
5071  C CG2 . THR A 691  ? 0.2827 0.3657 0.2279 0.0319  0.0030  0.0236  689  THR A CG2 
5072  N N   . LEU A 692  ? 0.2434 0.3697 0.1764 0.0358  0.0029  0.0245  690  LEU A N   
5073  C CA  . LEU A 692  ? 0.2663 0.4023 0.1953 0.0378  0.0021  0.0196  690  LEU A CA  
5074  C C   . LEU A 692  ? 0.2997 0.4486 0.2266 0.0374  0.0016  0.0256  690  LEU A C   
5075  O O   . LEU A 692  ? 0.3121 0.4685 0.2389 0.0365  0.0026  0.0319  690  LEU A O   
5076  C CB  . LEU A 692  ? 0.2608 0.4019 0.1874 0.0399  0.0031  0.0128  690  LEU A CB  
5077  C CG  . LEU A 692  ? 0.2883 0.4174 0.2169 0.0405  0.0031  0.0058  690  LEU A CG  
5078  C CD1 . LEU A 692  ? 0.2992 0.4342 0.2259 0.0429  0.0036  -0.0016 690  LEU A CD1 
5079  C CD2 . LEU A 692  ? 0.3051 0.4260 0.2350 0.0406  0.0012  0.0023  690  LEU A CD2 
5080  N N   . GLY A 693  ? 0.2837 0.4354 0.2092 0.0381  -0.0002 0.0238  691  GLY A N   
5081  C CA  . GLY A 693  ? 0.3177 0.4819 0.2411 0.0379  -0.0010 0.0290  691  GLY A CA  
5082  C C   . GLY A 693  ? 0.3421 0.5153 0.2613 0.0402  -0.0021 0.0223  691  GLY A C   
5083  O O   . GLY A 693  ? 0.3623 0.5321 0.2807 0.0420  -0.0022 0.0135  691  GLY A O   
5084  N N   . PRO A 694  ? 0.3465 0.5315 0.2633 0.0401  -0.0030 0.0264  692  PRO A N   
5085  C CA  . PRO A 694  ? 0.3949 0.5910 0.3075 0.0424  -0.0040 0.0202  692  PRO A CA  
5086  C C   . PRO A 694  ? 0.3872 0.5744 0.3005 0.0435  -0.0058 0.0126  692  PRO A C   
5087  O O   . PRO A 694  ? 0.4099 0.6025 0.3206 0.0458  -0.0064 0.0044  692  PRO A O   
5088  C CB  . PRO A 694  ? 0.4309 0.6396 0.3417 0.0414  -0.0049 0.0280  692  PRO A CB  
5089  C CG  . PRO A 694  ? 0.3934 0.6012 0.3070 0.0389  -0.0038 0.0380  692  PRO A CG  
5090  C CD  . PRO A 694  ? 0.3413 0.5315 0.2595 0.0379  -0.0032 0.0372  692  PRO A CD  
5091  N N   . GLY A 695  ? 0.3305 0.5047 0.2476 0.0420  -0.0067 0.0150  693  GLY A N   
5092  C CA  . GLY A 695  ? 0.3831 0.5488 0.3013 0.0427  -0.0083 0.0086  693  GLY A CA  
5093  C C   . GLY A 695  ? 0.3866 0.5413 0.3067 0.0435  -0.0079 0.0012  693  GLY A C   
5094  O O   . GLY A 695  ? 0.3594 0.5071 0.2808 0.0441  -0.0093 -0.0042 693  GLY A O   
5095  N N   . HIS A 696  ? 0.3284 0.4813 0.2490 0.0435  -0.0060 0.0011  694  HIS A N   
5096  C CA  . HIS A 696  ? 0.3266 0.4694 0.2492 0.0441  -0.0056 -0.0055 694  HIS A CA  
5097  C C   . HIS A 696  ? 0.3681 0.5204 0.2881 0.0467  -0.0055 -0.0128 694  HIS A C   
5098  O O   . HIS A 696  ? 0.3757 0.5317 0.2949 0.0472  -0.0038 -0.0131 694  HIS A O   
5099  C CB  . HIS A 696  ? 0.3455 0.4796 0.2709 0.0424  -0.0038 -0.0011 694  HIS A CB  
5100  C CG  . HIS A 696  ? 0.2822 0.4095 0.2104 0.0400  -0.0040 0.0065  694  HIS A CG  
5101  N ND1 . HIS A 696  ? 0.3375 0.4685 0.2662 0.0385  -0.0030 0.0147  694  HIS A ND1 
5102  C CD2 . HIS A 696  ? 0.3286 0.4462 0.2597 0.0390  -0.0052 0.0071  694  HIS A CD2 
5103  C CE1 . HIS A 696  ? 0.3074 0.4307 0.2396 0.0367  -0.0037 0.0197  694  HIS A CE1 
5104  N NE2 . HIS A 696  ? 0.3331 0.4484 0.2665 0.0370  -0.0049 0.0151  694  HIS A NE2 
5105  N N   . GLY A 697  ? 0.3494 0.5058 0.2680 0.0485  -0.0074 -0.0191 695  GLY A N   
5106  C CA  . GLY A 697  ? 0.3556 0.5225 0.2719 0.0512  -0.0077 -0.0265 695  GLY A CA  
5107  C C   . GLY A 697  ? 0.3019 0.4608 0.2209 0.0523  -0.0076 -0.0337 695  GLY A C   
5108  O O   . GLY A 697  ? 0.3028 0.4483 0.2255 0.0515  -0.0083 -0.0354 695  GLY A O   
5109  N N   . PRO A 698  ? 0.3101 0.4775 0.2278 0.0543  -0.0068 -0.0381 696  PRO A N   
5110  C CA  . PRO A 698  ? 0.3351 0.4954 0.2559 0.0555  -0.0069 -0.0450 696  PRO A CA  
5111  C C   . PRO A 698  ? 0.3066 0.4625 0.2298 0.0571  -0.0097 -0.0535 696  PRO A C   
5112  O O   . PRO A 698  ? 0.3080 0.4702 0.2296 0.0580  -0.0114 -0.0558 696  PRO A O   
5113  C CB  . PRO A 698  ? 0.3449 0.5183 0.2632 0.0576  -0.0056 -0.0479 696  PRO A CB  
5114  C CG  . PRO A 698  ? 0.3820 0.5708 0.2958 0.0583  -0.0057 -0.0458 696  PRO A CG  
5115  C CD  . PRO A 698  ? 0.3851 0.5696 0.2984 0.0555  -0.0057 -0.0368 696  PRO A CD  
5116  N N   . LEU A 699  ? 0.2864 0.4311 0.2139 0.0572  -0.0103 -0.0578 697  LEU A N   
5117  C CA  . LEU A 699  ? 0.3001 0.4406 0.2309 0.0586  -0.0132 -0.0662 697  LEU A CA  
5118  C C   . LEU A 699  ? 0.3037 0.4568 0.2335 0.0620  -0.0144 -0.0746 697  LEU A C   
5119  O O   . LEU A 699  ? 0.2928 0.4489 0.2231 0.0635  -0.0169 -0.0804 697  LEU A O   
5120  C CB  . LEU A 699  ? 0.2637 0.3903 0.1998 0.0579  -0.0136 -0.0684 697  LEU A CB  
5121  C CG  . LEU A 699  ? 0.2953 0.4089 0.2332 0.0547  -0.0129 -0.0616 697  LEU A CG  
5122  C CD1 . LEU A 699  ? 0.2906 0.3924 0.2335 0.0542  -0.0133 -0.0642 697  LEU A CD1 
5123  C CD2 . LEU A 699  ? 0.3215 0.4322 0.2596 0.0538  -0.0146 -0.0606 697  LEU A CD2 
5124  N N   . GLY A 700  ? 0.2805 0.4414 0.2088 0.0634  -0.0127 -0.0757 698  GLY A N   
5125  C CA  . GLY A 700  ? 0.2674 0.4389 0.1958 0.0668  -0.0138 -0.0849 698  GLY A CA  
5126  C C   . GLY A 700  ? 0.2667 0.4332 0.1990 0.0678  -0.0134 -0.0888 698  GLY A C   
5127  O O   . GLY A 700  ? 0.2946 0.4526 0.2279 0.0657  -0.0115 -0.0831 698  GLY A O   
5128  N N   . PRO A 701  ? 0.2897 0.4614 0.2245 0.0710  -0.0152 -0.0987 699  PRO A N   
5129  C CA  . PRO A 701  ? 0.2500 0.4174 0.1889 0.0721  -0.0150 -0.1028 699  PRO A CA  
5130  C C   . PRO A 701  ? 0.2456 0.3949 0.1897 0.0698  -0.0157 -0.1004 699  PRO A C   
5131  O O   . PRO A 701  ? 0.2711 0.4117 0.2187 0.0692  -0.0182 -0.1026 699  PRO A O   
5132  C CB  . PRO A 701  ? 0.2972 0.4719 0.2391 0.0759  -0.0179 -0.1147 699  PRO A CB  
5133  C CG  . PRO A 701  ? 0.2928 0.4821 0.2295 0.0772  -0.0181 -0.1156 699  PRO A CG  
5134  C CD  . PRO A 701  ? 0.2977 0.4809 0.2316 0.0739  -0.0175 -0.1067 699  PRO A CD  
5135  N N   . ILE A 702  ? 0.2822 0.4262 0.2268 0.0684  -0.0134 -0.0957 700  ILE A N   
5136  C CA  A ILE A 702  ? 0.2616 0.3896 0.2108 0.0662  -0.0137 -0.0930 700  ILE A CA  
5137  C CA  B ILE A 702  ? 0.2617 0.3896 0.2108 0.0661  -0.0137 -0.0929 700  ILE A CA  
5138  C C   . ILE A 702  ? 0.2450 0.3705 0.1991 0.0679  -0.0144 -0.0988 700  ILE A C   
5139  O O   . ILE A 702  ? 0.2580 0.3917 0.2103 0.0693  -0.0126 -0.0995 700  ILE A O   
5140  C CB  A ILE A 702  ? 0.2494 0.3718 0.1957 0.0628  -0.0108 -0.0824 700  ILE A CB  
5141  C CB  B ILE A 702  ? 0.2484 0.3715 0.1946 0.0629  -0.0106 -0.0824 700  ILE A CB  
5142  C CG1 A ILE A 702  ? 0.2521 0.3738 0.1954 0.0610  -0.0110 -0.0774 700  ILE A CG1 
5143  C CG1 B ILE A 702  ? 0.2615 0.3871 0.2035 0.0612  -0.0101 -0.0764 700  ILE A CG1 
5144  C CG2 A ILE A 702  ? 0.2667 0.3745 0.2176 0.0609  -0.0108 -0.0803 700  ILE A CG2 
5145  C CG2 B ILE A 702  ? 0.2660 0.3734 0.2168 0.0607  -0.0109 -0.0799 700  ILE A CG2 
5146  C CD1 A ILE A 702  ? 0.2629 0.3786 0.2044 0.0578  -0.0087 -0.0676 700  ILE A CD1 
5147  C CD1 B ILE A 702  ? 0.2703 0.3862 0.2149 0.0599  -0.0124 -0.0769 700  ILE A CD1 
5148  N N   . VAL A 703  ? 0.2469 0.3613 0.2073 0.0677  -0.0171 -0.1027 701  VAL A N   
5149  C CA  . VAL A 703  ? 0.2577 0.3676 0.2239 0.0690  -0.0182 -0.1076 701  VAL A CA  
5150  C C   . VAL A 703  ? 0.2276 0.3262 0.1948 0.0660  -0.0164 -0.1002 701  VAL A C   
5151  O O   . VAL A 703  ? 0.2476 0.3357 0.2160 0.0633  -0.0168 -0.0957 701  VAL A O   
5152  C CB  . VAL A 703  ? 0.2924 0.3966 0.2657 0.0704  -0.0225 -0.1155 701  VAL A CB  
5153  C CG1 . VAL A 703  ? 0.2796 0.3767 0.2599 0.0710  -0.0239 -0.1191 701  VAL A CG1 
5154  C CG2 . VAL A 703  ? 0.3080 0.4249 0.2806 0.0738  -0.0243 -0.1239 701  VAL A CG2 
5155  N N   . CYS A 704  ? 0.2298 0.3311 0.1963 0.0665  -0.0142 -0.0989 702  CYS A N   
5156  C CA  . CYS A 704  ? 0.2426 0.3343 0.2100 0.0639  -0.0124 -0.0924 702  CYS A CA  
5157  C C   . CYS A 704  ? 0.2675 0.3534 0.2417 0.0651  -0.0143 -0.0976 702  CYS A C   
5158  O O   . CYS A 704  ? 0.2462 0.3395 0.2215 0.0677  -0.0142 -0.1025 702  CYS A O   
5159  C CB  . CYS A 704  ? 0.2748 0.3735 0.2367 0.0632  -0.0087 -0.0863 702  CYS A CB  
5160  S SG  . CYS A 704  ? 0.2615 0.3670 0.2162 0.0616  -0.0067 -0.0794 702  CYS A SG  
5161  N N   . ILE A 705  ? 0.2450 0.3181 0.2240 0.0631  -0.0161 -0.0962 703  ILE A N   
5162  C CA  . ILE A 705  ? 0.2528 0.3191 0.2392 0.0638  -0.0183 -0.1003 703  ILE A CA  
5163  C C   . ILE A 705  ? 0.2313 0.2885 0.2179 0.0608  -0.0164 -0.0930 703  ILE A C   
5164  O O   . ILE A 705  ? 0.2367 0.2868 0.2217 0.0578  -0.0157 -0.0868 703  ILE A O   
5165  C CB  . ILE A 705  ? 0.2470 0.3066 0.2398 0.0639  -0.0225 -0.1050 703  ILE A CB  
5166  C CG1 . ILE A 705  ? 0.2828 0.3520 0.2758 0.0671  -0.0245 -0.1131 703  ILE A CG1 
5167  C CG2 . ILE A 705  ? 0.2320 0.2832 0.2329 0.0640  -0.0249 -0.1077 703  ILE A CG2 
5168  C CD1 . ILE A 705  ? 0.2846 0.3478 0.2831 0.0669  -0.0285 -0.1169 703  ILE A CD1 
5169  N N   . SER A 706  ? 0.2461 0.3039 0.2347 0.0617  -0.0157 -0.0939 704  SER A N   
5170  C CA  . SER A 706  ? 0.2486 0.3002 0.2362 0.0592  -0.0134 -0.0869 704  SER A CA  
5171  C C   . SER A 706  ? 0.2462 0.2898 0.2410 0.0592  -0.0154 -0.0890 704  SER A C   
5172  O O   . SER A 706  ? 0.2540 0.2992 0.2543 0.0618  -0.0182 -0.0963 704  SER A O   
5173  C CB  . SER A 706  ? 0.2664 0.3269 0.2485 0.0598  -0.0098 -0.0840 704  SER A CB  
5174  O OG  . SER A 706  ? 0.2655 0.3351 0.2491 0.0632  -0.0103 -0.0908 704  SER A OG  
5175  N N   . PRO A 707  ? 0.2702 0.3055 0.2654 0.0564  -0.0143 -0.0828 705  PRO A N   
5176  C CA  . PRO A 707  ? 0.2666 0.2940 0.2687 0.0559  -0.0164 -0.0837 705  PRO A CA  
5177  C C   . PRO A 707  ? 0.2358 0.2671 0.2381 0.0573  -0.0148 -0.0843 705  PRO A C   
5178  O O   . PRO A 707  ? 0.2720 0.3111 0.2688 0.0580  -0.0117 -0.0826 705  PRO A O   
5179  C CB  . PRO A 707  ? 0.2675 0.2856 0.2686 0.0520  -0.0154 -0.0760 705  PRO A CB  
5180  C CG  . PRO A 707  ? 0.2643 0.2870 0.2576 0.0509  -0.0117 -0.0706 705  PRO A CG  
5181  C CD  . PRO A 707  ? 0.2327 0.2651 0.2225 0.0533  -0.0115 -0.0745 705  PRO A CD  
5182  N N   . TRP A 708  ? 0.2579 0.2839 0.2672 0.0577  -0.0170 -0.0867 706  TRP A N   
5183  C CA  . TRP A 708  ? 0.2571 0.2865 0.2672 0.0592  -0.0157 -0.0877 706  TRP A CA  
5184  C C   . TRP A 708  ? 0.2754 0.3015 0.2818 0.0564  -0.0126 -0.0797 706  TRP A C   
5185  O O   . TRP A 708  ? 0.2860 0.3173 0.2905 0.0574  -0.0104 -0.0791 706  TRP A O   
5186  C CB  . TRP A 708  ? 0.2478 0.2728 0.2671 0.0607  -0.0193 -0.0929 706  TRP A CB  
5187  C CG  . TRP A 708  ? 0.2793 0.2928 0.3027 0.0576  -0.0207 -0.0879 706  TRP A CG  
5188  C CD1 . TRP A 708  ? 0.2668 0.2723 0.2948 0.0559  -0.0237 -0.0873 706  TRP A CD1 
5189  C CD2 . TRP A 708  ? 0.2675 0.2769 0.2908 0.0557  -0.0190 -0.0825 706  TRP A CD2 
5190  N NE1 . TRP A 708  ? 0.2806 0.2778 0.3110 0.0530  -0.0239 -0.0816 706  TRP A NE1 
5191  C CE2 . TRP A 708  ? 0.2684 0.2677 0.2959 0.0529  -0.0211 -0.0788 706  TRP A CE2 
5192  C CE3 . TRP A 708  ? 0.2738 0.2875 0.2938 0.0561  -0.0160 -0.0804 706  TRP A CE3 
5193  C CZ2 . TRP A 708  ? 0.2654 0.2590 0.2936 0.0505  -0.0203 -0.0732 706  TRP A CZ2 
5194  C CZ3 . TRP A 708  ? 0.2820 0.2894 0.3029 0.0537  -0.0152 -0.0749 706  TRP A CZ3 
5195  C CH2 . TRP A 708  ? 0.2801 0.2777 0.3050 0.0510  -0.0174 -0.0715 706  TRP A CH2 
5196  N N   . ASN A 709  ? 0.2450 0.2629 0.2504 0.0531  -0.0124 -0.0737 707  ASN A N   
5197  C CA  . ASN A 709  ? 0.2645 0.2775 0.2690 0.0506  -0.0105 -0.0675 707  ASN A CA  
5198  C C   . ASN A 709  ? 0.2852 0.3031 0.2824 0.0497  -0.0066 -0.0623 707  ASN A C   
5199  O O   . ASN A 709  ? 0.2900 0.3064 0.2863 0.0485  -0.0048 -0.0584 707  ASN A O   
5200  C CB  . ASN A 709  ? 0.2540 0.2569 0.2610 0.0475  -0.0120 -0.0634 707  ASN A CB  
5201  C CG  . ASN A 709  ? 0.3057 0.3078 0.3078 0.0456  -0.0109 -0.0598 707  ASN A CG  
5202  O OD1 . ASN A 709  ? 0.3129 0.3178 0.3145 0.0468  -0.0120 -0.0630 707  ASN A OD1 
5203  N ND2 . ASN A 709  ? 0.2620 0.2605 0.2609 0.0429  -0.0088 -0.0533 707  ASN A ND2 
5204  N N   . PHE A 710  ? 0.2747 0.2981 0.2670 0.0500  -0.0054 -0.0619 708  PHE A N   
5205  C CA  . PHE A 710  ? 0.2572 0.2870 0.2433 0.0496  -0.0020 -0.0577 708  PHE A CA  
5206  C C   . PHE A 710  ? 0.2826 0.3236 0.2667 0.0527  -0.0018 -0.0628 708  PHE A C   
5207  O O   . PHE A 710  ? 0.2733 0.3189 0.2538 0.0529  -0.0015 -0.0629 708  PHE A O   
5208  C CB  . PHE A 710  ? 0.2597 0.2863 0.2417 0.0469  -0.0008 -0.0520 708  PHE A CB  
5209  C CG  . PHE A 710  ? 0.3250 0.3416 0.3086 0.0439  -0.0010 -0.0473 708  PHE A CG  
5210  C CD1 . PHE A 710  ? 0.3406 0.3538 0.3260 0.0431  -0.0003 -0.0452 708  PHE A CD1 
5211  C CD2 . PHE A 710  ? 0.3196 0.3307 0.3028 0.0419  -0.0017 -0.0451 708  PHE A CD2 
5212  C CE1 . PHE A 710  ? 0.3615 0.3665 0.3482 0.0403  -0.0004 -0.0409 708  PHE A CE1 
5213  C CE2 . PHE A 710  ? 0.3181 0.3211 0.3026 0.0392  -0.0018 -0.0409 708  PHE A CE2 
5214  C CZ  . PHE A 710  ? 0.3421 0.3422 0.3282 0.0384  -0.0011 -0.0389 708  PHE A CZ  
5215  N N   . PRO A 711  ? 0.2712 0.3174 0.2579 0.0551  -0.0020 -0.0673 709  PRO A N   
5216  C CA  . PRO A 711  ? 0.2706 0.3271 0.2572 0.0586  -0.0027 -0.0742 709  PRO A CA  
5217  C C   . PRO A 711  ? 0.2691 0.3371 0.2493 0.0592  0.0002  -0.0720 709  PRO A C   
5218  O O   . PRO A 711  ? 0.2677 0.3452 0.2467 0.0617  -0.0003 -0.0771 709  PRO A O   
5219  C CB  . PRO A 711  ? 0.2900 0.3476 0.2819 0.0608  -0.0038 -0.0792 709  PRO A CB  
5220  C CG  . PRO A 711  ? 0.2665 0.3193 0.2579 0.0586  -0.0018 -0.0730 709  PRO A CG  
5221  C CD  . PRO A 711  ? 0.2659 0.3089 0.2559 0.0550  -0.0017 -0.0666 709  PRO A CD  
5222  N N   . LEU A 712  ? 0.2758 0.3437 0.2522 0.0569  0.0030  -0.0647 710  LEU A N   
5223  C CA  . LEU A 712  ? 0.2496 0.3279 0.2203 0.0569  0.0055  -0.0613 710  LEU A CA  
5224  C C   . LEU A 712  ? 0.2573 0.3318 0.2243 0.0542  0.0063  -0.0550 710  LEU A C   
5225  O O   . LEU A 712  ? 0.2342 0.3158 0.1976 0.0547  0.0067  -0.0547 710  LEU A O   
5226  C CB  . LEU A 712  ? 0.2471 0.3302 0.2167 0.0567  0.0081  -0.0578 710  LEU A CB  
5227  C CG  . LEU A 712  ? 0.2741 0.3688 0.2383 0.0566  0.0107  -0.0537 710  LEU A CG  
5228  C CD1 . LEU A 712  ? 0.2608 0.3682 0.2236 0.0598  0.0101  -0.0601 710  LEU A CD1 
5229  C CD2 . LEU A 712  ? 0.2898 0.3878 0.2534 0.0557  0.0132  -0.0489 710  LEU A CD2 
5230  N N   . ALA A 713  ? 0.2351 0.2986 0.2033 0.0515  0.0063  -0.0503 711  ALA A N   
5231  C CA  . ALA A 713  ? 0.2190 0.2791 0.1841 0.0488  0.0073  -0.0440 711  ALA A CA  
5232  C C   . ALA A 713  ? 0.2498 0.3088 0.2142 0.0491  0.0054  -0.0463 711  ALA A C   
5233  O O   . ALA A 713  ? 0.2591 0.3239 0.2198 0.0489  0.0062  -0.0441 711  ALA A O   
5234  C CB  . ALA A 713  ? 0.2320 0.2811 0.1988 0.0461  0.0076  -0.0393 711  ALA A CB  
5235  N N   . ILE A 714  ? 0.2291 0.2808 0.1975 0.0492  0.0029  -0.0503 712  ILE A N   
5236  C CA  . ILE A 714  ? 0.2124 0.2625 0.1805 0.0493  0.0011  -0.0523 712  ILE A CA  
5237  C C   . ILE A 714  ? 0.2531 0.3141 0.2197 0.0521  0.0005  -0.0576 712  ILE A C   
5238  O O   . ILE A 714  ? 0.2493 0.3140 0.2129 0.0521  0.0003  -0.0571 712  ILE A O   
5239  C CB  . ILE A 714  ? 0.2650 0.3050 0.2383 0.0486  -0.0016 -0.0550 712  ILE A CB  
5240  C CG1 . ILE A 714  ? 0.2896 0.3203 0.2633 0.0454  -0.0007 -0.0488 712  ILE A CG1 
5241  C CG2 . ILE A 714  ? 0.2688 0.3089 0.2428 0.0493  -0.0039 -0.0586 712  ILE A CG2 
5242  C CD1 . ILE A 714  ? 0.3855 0.4069 0.3632 0.0441  -0.0030 -0.0497 712  ILE A CD1 
5243  N N   . PHE A 715  ? 0.2546 0.3211 0.2233 0.0547  0.0000  -0.0631 713  PHE A N   
5244  C CA  . PHE A 715  ? 0.2350 0.3135 0.2020 0.0577  -0.0003 -0.0686 713  PHE A CA  
5245  C C   . PHE A 715  ? 0.2855 0.3736 0.2463 0.0572  0.0021  -0.0637 713  PHE A C   
5246  O O   . PHE A 715  ? 0.2504 0.3441 0.2086 0.0579  0.0015  -0.0649 713  PHE A O   
5247  C CB  . PHE A 715  ? 0.2481 0.3315 0.2179 0.0603  -0.0004 -0.0737 713  PHE A CB  
5248  C CG  . PHE A 715  ? 0.2726 0.3695 0.2410 0.0636  -0.0006 -0.0799 713  PHE A CG  
5249  C CD1 . PHE A 715  ? 0.2735 0.3716 0.2449 0.0659  -0.0036 -0.0878 713  PHE A CD1 
5250  C CD2 . PHE A 715  ? 0.2862 0.3951 0.2503 0.0643  0.0021  -0.0778 713  PHE A CD2 
5251  C CE1 . PHE A 715  ? 0.3021 0.4135 0.2722 0.0691  -0.0039 -0.0941 713  PHE A CE1 
5252  C CE2 . PHE A 715  ? 0.2964 0.4190 0.2589 0.0674  0.0020  -0.0836 713  PHE A CE2 
5253  C CZ  . PHE A 715  ? 0.2974 0.4213 0.2628 0.0699  -0.0010 -0.0920 713  PHE A CZ  
5254  N N   . THR A 716  ? 0.2450 0.3350 0.2037 0.0559  0.0048  -0.0579 714  THR A N   
5255  C CA  . THR A 716  ? 0.2444 0.3435 0.1979 0.0552  0.0070  -0.0524 714  THR A CA  
5256  C C   . THR A 716  ? 0.2432 0.3376 0.1946 0.0529  0.0068  -0.0473 714  THR A C   
5257  O O   . THR A 716  ? 0.2473 0.3498 0.1952 0.0532  0.0071  -0.0460 714  THR A O   
5258  C CB  . THR A 716  ? 0.2647 0.3649 0.2176 0.0539  0.0096  -0.0467 714  THR A CB  
5259  O OG1 . THR A 716  ? 0.2704 0.3764 0.2252 0.0562  0.0098  -0.0516 714  THR A OG1 
5260  C CG2 . THR A 716  ? 0.2668 0.3761 0.2152 0.0528  0.0116  -0.0403 714  THR A CG2 
5261  N N   . GLY A 717  ? 0.2258 0.3076 0.1796 0.0506  0.0063  -0.0445 715  GLY A N   
5262  C CA  . GLY A 717  ? 0.2454 0.3224 0.1976 0.0484  0.0061  -0.0397 715  GLY A CA  
5263  C C   . GLY A 717  ? 0.2635 0.3436 0.2146 0.0496  0.0043  -0.0435 715  GLY A C   
5264  O O   . GLY A 717  ? 0.2481 0.3332 0.1960 0.0490  0.0047  -0.0402 715  GLY A O   
5265  N N   . GLN A 718  ? 0.2165 0.2940 0.1708 0.0512  0.0020  -0.0506 716  GLN A N   
5266  C CA  . GLN A 718  ? 0.2385 0.3183 0.1923 0.0523  -0.0001 -0.0545 716  GLN A CA  
5267  C C   . GLN A 718  ? 0.2590 0.3530 0.2089 0.0544  0.0005  -0.0562 716  GLN A C   
5268  O O   . GLN A 718  ? 0.2370 0.3352 0.1840 0.0541  0.0003  -0.0546 716  GLN A O   
5269  C CB  . GLN A 718  ? 0.2171 0.2918 0.1759 0.0538  -0.0029 -0.0620 716  GLN A CB  
5270  C CG  . GLN A 718  ? 0.2316 0.2928 0.1945 0.0515  -0.0039 -0.0601 716  GLN A CG  
5271  C CD  . GLN A 718  ? 0.2669 0.3231 0.2352 0.0527  -0.0071 -0.0668 716  GLN A CD  
5272  O OE1 . GLN A 718  ? 0.2685 0.3161 0.2393 0.0510  -0.0087 -0.0660 716  GLN A OE1 
5273  N NE2 . GLN A 718  ? 0.2717 0.3334 0.2422 0.0556  -0.0083 -0.0736 716  GLN A NE2 
5274  N N   . ILE A 719  ? 0.2316 0.3339 0.1814 0.0564  0.0013  -0.0595 717  ILE A N   
5275  C CA  . ILE A 719  ? 0.2477 0.3650 0.1939 0.0587  0.0019  -0.0618 717  ILE A CA  
5276  C C   . ILE A 719  ? 0.2452 0.3688 0.1867 0.0569  0.0042  -0.0535 717  ILE A C   
5277  O O   . ILE A 719  ? 0.2579 0.3904 0.1960 0.0574  0.0040  -0.0530 717  ILE A O   
5278  C CB  . ILE A 719  ? 0.2900 0.4146 0.2375 0.0612  0.0024  -0.0669 717  ILE A CB  
5279  C CG1 . ILE A 719  ? 0.2627 0.3831 0.2153 0.0635  -0.0005 -0.0762 717  ILE A CG1 
5280  C CG2 . ILE A 719  ? 0.3431 0.4845 0.2862 0.0629  0.0039  -0.0672 717  ILE A CG2 
5281  C CD1 . ILE A 719  ? 0.3410 0.4625 0.2969 0.0651  -0.0002 -0.0800 717  ILE A CD1 
5282  N N   . ALA A 720  ? 0.2472 0.3663 0.1887 0.0547  0.0062  -0.0467 718  ALA A N   
5283  C CA  . ALA A 720  ? 0.2753 0.3999 0.2134 0.0528  0.0081  -0.0384 718  ALA A CA  
5284  C C   . ALA A 720  ? 0.2432 0.3642 0.1800 0.0512  0.0072  -0.0348 718  ALA A C   
5285  O O   . ALA A 720  ? 0.2339 0.3640 0.1674 0.0510  0.0076  -0.0313 718  ALA A O   
5286  C CB  . ALA A 720  ? 0.2476 0.3657 0.1871 0.0506  0.0099  -0.0323 718  ALA A CB  
5287  N N   . ALA A 721  ? 0.2254 0.3335 0.1650 0.0500  0.0058  -0.0355 719  ALA A N   
5288  C CA  . ALA A 721  ? 0.2243 0.3282 0.1632 0.0485  0.0048  -0.0325 719  ALA A CA  
5289  C C   . ALA A 721  ? 0.2385 0.3513 0.1752 0.0504  0.0033  -0.0369 719  ALA A C   
5290  O O   . ALA A 721  ? 0.2353 0.3538 0.1692 0.0498  0.0034  -0.0328 719  ALA A O   
5291  C CB  . ALA A 721  ? 0.2296 0.3192 0.1721 0.0472  0.0035  -0.0336 719  ALA A CB  
5292  N N   . ALA A 722  ? 0.2230 0.3373 0.1612 0.0529  0.0016  -0.0453 720  ALA A N   
5293  C CA  . ALA A 722  ? 0.2308 0.3534 0.1673 0.0549  -0.0001 -0.0503 720  ALA A CA  
5294  C C   . ALA A 722  ? 0.2675 0.4061 0.1994 0.0559  0.0013  -0.0484 720  ALA A C   
5295  O O   . ALA A 722  ? 0.2469 0.3921 0.1760 0.0559  0.0008  -0.0467 720  ALA A O   
5296  C CB  . ALA A 722  ? 0.2307 0.3521 0.1705 0.0574  -0.0022 -0.0601 720  ALA A CB  
5297  N N   . LEU A 723  ? 0.2212 0.3666 0.1525 0.0568  0.0031  -0.0483 721  LEU A N   
5298  C CA  . LEU A 723  ? 0.2213 0.3829 0.1484 0.0577  0.0046  -0.0461 721  LEU A CA  
5299  C C   . LEU A 723  ? 0.2384 0.4017 0.1628 0.0550  0.0057  -0.0361 721  LEU A C   
5300  O O   . LEU A 723  ? 0.2285 0.4033 0.1495 0.0554  0.0057  -0.0342 721  LEU A O   
5301  C CB  . LEU A 723  ? 0.2411 0.4079 0.1686 0.0586  0.0064  -0.0467 721  LEU A CB  
5302  C CG  . LEU A 723  ? 0.2137 0.3831 0.1435 0.0618  0.0054  -0.0568 721  LEU A CG  
5303  C CD1 . LEU A 723  ? 0.2577 0.4301 0.1882 0.0620  0.0076  -0.0555 721  LEU A CD1 
5304  C CD2 . LEU A 723  ? 0.2652 0.4495 0.1922 0.0647  0.0044  -0.0629 721  LEU A CD2 
5305  N N   . VAL A 724  ? 0.2553 0.4080 0.1817 0.0524  0.0068  -0.0295 722  VAL A N   
5306  C CA  . VAL A 724  ? 0.2313 0.3864 0.1561 0.0499  0.0078  -0.0200 722  VAL A CA  
5307  C C   . VAL A 724  ? 0.2282 0.3808 0.1524 0.0492  0.0060  -0.0186 722  VAL A C   
5308  O O   . VAL A 724  ? 0.2761 0.4353 0.1982 0.0480  0.0063  -0.0122 722  VAL A O   
5309  C CB  . VAL A 724  ? 0.2205 0.3658 0.1480 0.0474  0.0092  -0.0137 722  VAL A CB  
5310  C CG1 . VAL A 724  ? 0.2587 0.3878 0.1893 0.0459  0.0080  -0.0137 722  VAL A CG1 
5311  C CG2 . VAL A 724  ? 0.2548 0.4071 0.1810 0.0455  0.0105  -0.0042 722  VAL A CG2 
5312  N N   . ALA A 725  ? 0.2365 0.3800 0.1626 0.0498  0.0042  -0.0243 723  ALA A N   
5313  C CA  . ALA A 725  ? 0.2591 0.4009 0.1846 0.0494  0.0024  -0.0243 723  ALA A CA  
5314  C C   . ALA A 725  ? 0.2624 0.4183 0.1844 0.0517  0.0014  -0.0283 723  ALA A C   
5315  O O   . ALA A 725  ? 0.2835 0.4397 0.2048 0.0516  -0.0002 -0.0287 723  ALA A O   
5316  C CB  . ALA A 725  ? 0.2455 0.3738 0.1744 0.0494  0.0007  -0.0293 723  ALA A CB  
5317  N N   . GLY A 726  ? 0.2564 0.4244 0.1765 0.0537  0.0023  -0.0315 724  GLY A N   
5318  C CA  . GLY A 726  ? 0.2759 0.4589 0.1924 0.0558  0.0015  -0.0352 724  GLY A CA  
5319  C C   . GLY A 726  ? 0.2744 0.4587 0.1919 0.0589  -0.0004 -0.0464 724  GLY A C   
5320  O O   . GLY A 726  ? 0.2892 0.4852 0.2041 0.0607  -0.0015 -0.0503 724  GLY A O   
5321  N N   . ASN A 727  ? 0.2731 0.4464 0.1947 0.0594  -0.0010 -0.0516 725  ASN A N   
5322  C CA  . ASN A 727  ? 0.2546 0.4277 0.1785 0.0622  -0.0033 -0.0622 725  ASN A CA  
5323  C C   . ASN A 727  ? 0.2728 0.4534 0.1974 0.0646  -0.0025 -0.0679 725  ASN A C   
5324  O O   . ASN A 727  ? 0.2572 0.4337 0.1830 0.0638  -0.0007 -0.0650 725  ASN A O   
5325  C CB  . ASN A 727  ? 0.2705 0.4263 0.1994 0.0611  -0.0049 -0.0643 725  ASN A CB  
5326  C CG  . ASN A 727  ? 0.2612 0.4084 0.1902 0.0585  -0.0055 -0.0586 725  ASN A CG  
5327  O OD1 . ASN A 727  ? 0.2780 0.4276 0.2062 0.0590  -0.0073 -0.0608 725  ASN A OD1 
5328  N ND2 . ASN A 727  ? 0.2647 0.4021 0.1948 0.0558  -0.0040 -0.0516 725  ASN A ND2 
5329  N N   . PRO A 728  ? 0.2506 0.4417 0.1747 0.0678  -0.0039 -0.0765 726  PRO A N   
5330  C CA  . PRO A 728  ? 0.2505 0.4463 0.1768 0.0705  -0.0037 -0.0836 726  PRO A CA  
5331  C C   . PRO A 728  ? 0.2573 0.4375 0.1898 0.0706  -0.0055 -0.0884 726  PRO A C   
5332  O O   . PRO A 728  ? 0.2685 0.4381 0.2037 0.0697  -0.0077 -0.0896 726  PRO A O   
5333  C CB  . PRO A 728  ? 0.2380 0.4488 0.1625 0.0739  -0.0053 -0.0921 726  PRO A CB  
5334  C CG  . PRO A 728  ? 0.2775 0.4844 0.2016 0.0732  -0.0076 -0.0922 726  PRO A CG  
5335  C CD  . PRO A 728  ? 0.2653 0.4631 0.1878 0.0693  -0.0062 -0.0811 726  PRO A CD  
5336  N N   . VAL A 729  ? 0.2587 0.4378 0.1939 0.0716  -0.0047 -0.0908 727  VAL A N   
5337  C CA  . VAL A 729  ? 0.2504 0.4144 0.1916 0.0711  -0.0059 -0.0933 727  VAL A CA  
5338  C C   . VAL A 729  ? 0.2319 0.3998 0.1776 0.0747  -0.0078 -0.1039 727  VAL A C   
5339  O O   . VAL A 729  ? 0.2713 0.4521 0.2153 0.0770  -0.0066 -0.1072 727  VAL A O   
5340  C CB  . VAL A 729  ? 0.2580 0.4144 0.1993 0.0684  -0.0033 -0.0852 727  VAL A CB  
5341  C CG1 . VAL A 729  ? 0.2690 0.4129 0.2165 0.0685  -0.0045 -0.0886 727  VAL A CG1 
5342  C CG2 . VAL A 729  ? 0.2953 0.4446 0.2343 0.0649  -0.0023 -0.0759 727  VAL A CG2 
5343  N N   . LEU A 730  ? 0.2458 0.4024 0.1975 0.0751  -0.0108 -0.1093 728  LEU A N   
5344  C CA  . LEU A 730  ? 0.2741 0.4295 0.2320 0.0778  -0.0129 -0.1183 728  LEU A CA  
5345  C C   . LEU A 730  ? 0.2415 0.3823 0.2036 0.0756  -0.0125 -0.1143 728  LEU A C   
5346  O O   . LEU A 730  ? 0.2615 0.3891 0.2261 0.0732  -0.0137 -0.1111 728  LEU A O   
5347  C CB  . LEU A 730  ? 0.2733 0.4262 0.2359 0.0797  -0.0170 -0.1270 728  LEU A CB  
5348  C CG  . LEU A 730  ? 0.2730 0.4397 0.2320 0.0819  -0.0180 -0.1318 728  LEU A CG  
5349  C CD1 . LEU A 730  ? 0.2724 0.4552 0.2290 0.0833  -0.0160 -0.1316 728  LEU A CD1 
5350  C CD2 . LEU A 730  ? 0.2663 0.4315 0.2203 0.0792  -0.0173 -0.1244 728  LEU A CD2 
5351  N N   . ALA A 731  ? 0.2652 0.4089 0.2278 0.0764  -0.0106 -0.1140 729  ALA A N   
5352  C CA  . ALA A 731  ? 0.2524 0.3840 0.2183 0.0743  -0.0098 -0.1096 729  ALA A CA  
5353  C C   . ALA A 731  ? 0.2698 0.3959 0.2437 0.0765  -0.0129 -0.1179 729  ALA A C   
5354  O O   . ALA A 731  ? 0.3017 0.4368 0.2775 0.0797  -0.0132 -0.1247 729  ALA A O   
5355  C CB  . ALA A 731  ? 0.2693 0.4073 0.2312 0.0736  -0.0061 -0.1039 729  ALA A CB  
5356  N N   . LYS A 732  ? 0.2355 0.3473 0.2146 0.0747  -0.0152 -0.1172 730  LYS A N   
5357  C CA  . LYS A 732  ? 0.2472 0.3524 0.2350 0.0763  -0.0185 -0.1241 730  LYS A CA  
5358  C C   . LYS A 732  ? 0.2470 0.3406 0.2373 0.0737  -0.0175 -0.1181 730  LYS A C   
5359  O O   . LYS A 732  ? 0.2557 0.3375 0.2477 0.0708  -0.0183 -0.1133 730  LYS A O   
5360  C CB  . LYS A 732  ? 0.3007 0.3992 0.2933 0.0763  -0.0225 -0.1284 730  LYS A CB  
5361  C CG  . LYS A 732  ? 0.2679 0.3672 0.2689 0.0798  -0.0265 -0.1391 730  LYS A CG  
5362  C CD  . LYS A 732  ? 0.2697 0.3611 0.2775 0.0797  -0.0274 -0.1397 730  LYS A CD  
5363  C CE  . LYS A 732  ? 0.2818 0.3574 0.2935 0.0761  -0.0287 -0.1337 730  LYS A CE  
5364  N NZ  . LYS A 732  ? 0.2936 0.3616 0.3117 0.0758  -0.0295 -0.1334 730  LYS A NZ  
5365  N N   . PRO A 733  ? 0.2438 0.3409 0.2344 0.0747  -0.0158 -0.1181 731  PRO A N   
5366  C CA  . PRO A 733  ? 0.2673 0.3539 0.2604 0.0723  -0.0149 -0.1126 731  PRO A CA  
5367  C C   . PRO A 733  ? 0.2563 0.3331 0.2588 0.0729  -0.0188 -0.1174 731  PRO A C   
5368  O O   . PRO A 733  ? 0.2729 0.3524 0.2806 0.0758  -0.0220 -0.1261 731  PRO A O   
5369  C CB  . PRO A 733  ? 0.2602 0.3558 0.2510 0.0738  -0.0121 -0.1125 731  PRO A CB  
5370  C CG  . PRO A 733  ? 0.2892 0.3974 0.2812 0.0780  -0.0135 -0.1220 731  PRO A CG  
5371  C CD  . PRO A 733  ? 0.2749 0.3864 0.2638 0.0781  -0.0145 -0.1234 731  PRO A CD  
5372  N N   . ALA A 734  ? 0.2575 0.3228 0.2622 0.0700  -0.0186 -0.1115 732  ALA A N   
5373  C CA  . ALA A 734  ? 0.2569 0.3124 0.2706 0.0700  -0.0222 -0.1146 732  ALA A CA  
5374  C C   . ALA A 734  ? 0.2632 0.3242 0.2825 0.0737  -0.0238 -0.1226 732  ALA A C   
5375  O O   . ALA A 734  ? 0.2917 0.3614 0.3077 0.0752  -0.0211 -0.1230 732  ALA A O   
5376  C CB  . ALA A 734  ? 0.2489 0.2939 0.2630 0.0664  -0.0210 -0.1065 732  ALA A CB  
5377  N N   . GLU A 735  ? 0.2900 0.3461 0.3183 0.0752  -0.0282 -0.1290 733  GLU A N   
5378  C CA  . GLU A 735  ? 0.3199 0.3809 0.3547 0.0789  -0.0303 -0.1374 733  GLU A CA  
5379  C C   . GLU A 735  ? 0.2930 0.3513 0.3296 0.0784  -0.0288 -0.1342 733  GLU A C   
5380  O O   . GLU A 735  ? 0.2986 0.3641 0.3377 0.0816  -0.0288 -0.1399 733  GLU A O   
5381  C CB  . GLU A 735  ? 0.3164 0.3713 0.3618 0.0803  -0.0358 -0.1444 733  GLU A CB  
5382  C CG  . GLU A 735  ? 0.3218 0.3618 0.3728 0.0768  -0.0382 -0.1389 733  GLU A CG  
5383  C CD  . GLU A 735  ? 0.3807 0.4156 0.4294 0.0740  -0.0388 -0.1350 733  GLU A CD  
5384  O OE1 . GLU A 735  ? 0.3460 0.3870 0.3860 0.0736  -0.0359 -0.1328 733  GLU A OE1 
5385  O OE2 . GLU A 735  ? 0.3777 0.4025 0.4336 0.0723  -0.0423 -0.1341 733  GLU A OE2 
5386  N N   . GLU A 736  ? 0.2875 0.3362 0.3225 0.0746  -0.0274 -0.1253 734  GLU A N   
5387  C CA  . GLU A 736  ? 0.2528 0.2985 0.2897 0.0739  -0.0262 -0.1222 734  GLU A CA  
5388  C C   . GLU A 736  ? 0.2928 0.3480 0.3218 0.0743  -0.0215 -0.1192 734  GLU A C   
5389  O O   . GLU A 736  ? 0.3139 0.3713 0.3451 0.0755  -0.0207 -0.1201 734  GLU A O   
5390  C CB  . GLU A 736  ? 0.2885 0.3214 0.3265 0.0697  -0.0263 -0.1138 734  GLU A CB  
5391  C CG  . GLU A 736  ? 0.3163 0.3392 0.3629 0.0687  -0.0310 -0.1154 734  GLU A CG  
5392  C CD  . GLU A 736  ? 0.3727 0.3930 0.4165 0.0669  -0.0316 -0.1134 734  GLU A CD  
5393  O OE1 . GLU A 736  ? 0.3172 0.3448 0.3534 0.0674  -0.0291 -0.1133 734  GLU A OE1 
5394  O OE2 . GLU A 736  ? 0.3414 0.3523 0.3908 0.0648  -0.0346 -0.1117 734  GLU A OE2 
5395  N N   . THR A 737  ? 0.2955 0.3565 0.3158 0.0733  -0.0184 -0.1154 735  THR A N   
5396  C CA  . THR A 737  ? 0.2856 0.3541 0.2984 0.0727  -0.0139 -0.1104 735  THR A CA  
5397  C C   . THR A 737  ? 0.2752 0.3575 0.2818 0.0748  -0.0121 -0.1131 735  THR A C   
5398  O O   . THR A 737  ? 0.2779 0.3634 0.2772 0.0728  -0.0092 -0.1070 735  THR A O   
5399  C CB  . THR A 737  ? 0.2769 0.3374 0.2851 0.0684  -0.0116 -0.1002 735  THR A CB  
5400  O OG1 . THR A 737  ? 0.2777 0.3339 0.2838 0.0666  -0.0125 -0.0982 735  THR A OG1 
5401  C CG2 . THR A 737  ? 0.2865 0.3357 0.3001 0.0665  -0.0128 -0.0972 735  THR A CG2 
5402  N N   . PRO A 738  ? 0.2640 0.3554 0.2737 0.0788  -0.0138 -0.1224 736  PRO A N   
5403  C CA  . PRO A 738  ? 0.2942 0.4000 0.2979 0.0808  -0.0121 -0.1252 736  PRO A CA  
5404  C C   . PRO A 738  ? 0.2818 0.3988 0.2796 0.0811  -0.0080 -0.1217 736  PRO A C   
5405  O O   . PRO A 738  ? 0.2758 0.4034 0.2669 0.0813  -0.0058 -0.1201 736  PRO A O   
5406  C CB  . PRO A 738  ? 0.2975 0.4091 0.3075 0.0851  -0.0156 -0.1369 736  PRO A CB  
5407  C CG  . PRO A 738  ? 0.2873 0.3925 0.3054 0.0860  -0.0174 -0.1395 736  PRO A CG  
5408  C CD  . PRO A 738  ? 0.2927 0.3826 0.3117 0.0817  -0.0174 -0.1309 736  PRO A CD  
5409  N N   . LEU A 739  ? 0.2611 0.3766 0.2615 0.0811  -0.0069 -0.1204 737  LEU A N   
5410  C CA  . LEU A 739  ? 0.2614 0.3892 0.2573 0.0820  -0.0034 -0.1186 737  LEU A CA  
5411  C C   . LEU A 739  ? 0.2566 0.3850 0.2448 0.0784  0.0003  -0.1080 737  LEU A C   
5412  O O   . LEU A 739  ? 0.2721 0.4133 0.2545 0.0789  0.0029  -0.1063 737  LEU A O   
5413  C CB  . LEU A 739  ? 0.2593 0.3848 0.2604 0.0829  -0.0034 -0.1199 737  LEU A CB  
5414  C CG  . LEU A 739  ? 0.2919 0.4169 0.3019 0.0865  -0.0071 -0.1303 737  LEU A CG  
5415  C CD1 . LEU A 739  ? 0.2366 0.3571 0.2516 0.0866  -0.0070 -0.1296 737  LEU A CD1 
5416  C CD2 . LEU A 739  ? 0.3086 0.4497 0.3181 0.0905  -0.0073 -0.1387 737  LEU A CD2 
5417  N N   . ILE A 740  ? 0.2372 0.3523 0.2254 0.0748  0.0005  -0.1008 738  ILE A N   
5418  C CA  . ILE A 740  ? 0.2407 0.3558 0.2223 0.0715  0.0036  -0.0911 738  ILE A CA  
5419  C C   . ILE A 740  ? 0.2474 0.3669 0.2241 0.0710  0.0037  -0.0900 738  ILE A C   
5420  O O   . ILE A 740  ? 0.2731 0.4000 0.2439 0.0698  0.0064  -0.0844 738  ILE A O   
5421  C CB  . ILE A 740  ? 0.2921 0.3925 0.2753 0.0679  0.0037  -0.0843 738  ILE A CB  
5422  C CG1 . ILE A 740  ? 0.2851 0.3861 0.2624 0.0648  0.0069  -0.0747 738  ILE A CG1 
5423  C CG2 . ILE A 740  ? 0.2835 0.3723 0.2696 0.0668  0.0008  -0.0854 738  ILE A CG2 
5424  C CD1 . ILE A 740  ? 0.3308 0.4433 0.3052 0.0654  0.0099  -0.0724 738  ILE A CD1 
5425  N N   . ALA A 741  ? 0.2817 0.3974 0.2610 0.0721  0.0007  -0.0955 739  ALA A N   
5426  C CA  . ALA A 741  ? 0.2763 0.3972 0.2513 0.0721  0.0005  -0.0956 739  ALA A CA  
5427  C C   . ALA A 741  ? 0.2529 0.3915 0.2242 0.0749  0.0019  -0.0992 739  ALA A C   
5428  O O   . ALA A 741  ? 0.2730 0.4192 0.2382 0.0739  0.0038  -0.0946 739  ALA A O   
5429  C CB  . ALA A 741  ? 0.2960 0.4099 0.2757 0.0731  -0.0034 -0.1017 739  ALA A CB  
5430  N N   . ALA A 742  ? 0.2466 0.3923 0.2216 0.0785  0.0009  -0.1075 740  ALA A N   
5431  C CA  . ALA A 742  ? 0.2555 0.4193 0.2270 0.0813  0.0023  -0.1114 740  ALA A CA  
5432  C C   . ALA A 742  ? 0.2667 0.4384 0.2327 0.0795  0.0063  -0.1031 740  ALA A C   
5433  O O   . ALA A 742  ? 0.2826 0.4676 0.2431 0.0798  0.0081  -0.1013 740  ALA A O   
5434  C CB  . ALA A 742  ? 0.2614 0.4312 0.2387 0.0854  0.0006  -0.1218 740  ALA A CB  
5435  N N   . GLU A 743  ? 0.2581 0.4219 0.2256 0.0774  0.0077  -0.0976 741  GLU A N   
5436  C CA  . GLU A 743  ? 0.2891 0.4594 0.2521 0.0755  0.0113  -0.0893 741  GLU A CA  
5437  C C   . GLU A 743  ? 0.2558 0.4237 0.2136 0.0721  0.0126  -0.0804 741  GLU A C   
5438  O O   . GLU A 743  ? 0.2749 0.4539 0.2278 0.0713  0.0150  -0.0752 741  GLU A O   
5439  C CB  . GLU A 743  ? 0.2762 0.4379 0.2427 0.0741  0.0122  -0.0861 741  GLU A CB  
5440  C CG  . GLU A 743  ? 0.3185 0.4845 0.2813 0.0716  0.0156  -0.0769 741  GLU A CG  
5441  C CD  . GLU A 743  ? 0.2627 0.4471 0.2229 0.0737  0.0178  -0.0781 741  GLU A CD  
5442  O OE1 . GLU A 743  ? 0.2922 0.4867 0.2535 0.0773  0.0168  -0.0868 741  GLU A OE1 
5443  O OE2 . GLU A 743  ? 0.3721 0.5613 0.3294 0.0716  0.0205  -0.0703 741  GLU A OE2 
5444  N N   . GLY A 744  ? 0.2586 0.4127 0.2175 0.0701  0.0108  -0.0785 742  GLY A N   
5445  C CA  . GLY A 744  ? 0.2577 0.4096 0.2122 0.0672  0.0117  -0.0710 742  GLY A CA  
5446  C C   . GLY A 744  ? 0.2533 0.4181 0.2036 0.0687  0.0116  -0.0730 742  GLY A C   
5447  O O   . GLY A 744  ? 0.2703 0.4418 0.2159 0.0670  0.0134  -0.0662 742  GLY A O   
5448  N N   . VAL A 745  ? 0.2555 0.4239 0.2076 0.0718  0.0092  -0.0823 743  VAL A N   
5449  C CA  . VAL A 745  ? 0.2740 0.4562 0.2222 0.0736  0.0090  -0.0853 743  VAL A CA  
5450  C C   . VAL A 745  ? 0.3017 0.5016 0.2463 0.0747  0.0117  -0.0839 743  VAL A C   
5451  O O   . VAL A 745  ? 0.3036 0.5143 0.2430 0.0741  0.0130  -0.0799 743  VAL A O   
5452  C CB  . VAL A 745  ? 0.2983 0.4807 0.2503 0.0769  0.0057  -0.0965 743  VAL A CB  
5453  C CG1 . VAL A 745  ? 0.3279 0.5277 0.2760 0.0795  0.0056  -0.1012 743  VAL A CG1 
5454  C CG2 . VAL A 745  ? 0.2838 0.4510 0.2382 0.0752  0.0031  -0.0962 743  VAL A CG2 
5455  N N   . ARG A 746  ? 0.2801 0.4834 0.2273 0.0763  0.0126  -0.0869 744  ARG A N   
5456  C CA  . ARG A 746  ? 0.2759 0.4964 0.2198 0.0773  0.0153  -0.0852 744  ARG A CA  
5457  C C   . ARG A 746  ? 0.2615 0.4830 0.2012 0.0735  0.0180  -0.0730 744  ARG A C   
5458  O O   . ARG A 746  ? 0.2956 0.5318 0.2308 0.0733  0.0197  -0.0694 744  ARG A O   
5459  C CB  . ARG A 746  ? 0.2992 0.5208 0.2476 0.0791  0.0158  -0.0896 744  ARG A CB  
5460  C CG  . ARG A 746  ? 0.3099 0.5476 0.2577 0.0794  0.0171  -0.0881 744  ARG A CG  
5461  C CD  . ARG A 746  ? 0.2974 0.5344 0.2489 0.0801  0.0182  -0.0892 744  ARG A CD  
5462  N NE  . ARG A 746  ? 0.3257 0.5546 0.2755 0.0779  0.0210  -0.0815 744  ARG A NE  
5463  C CZ  . ARG A 746  ? 0.3483 0.5826 0.2943 0.0751  0.0237  -0.0717 744  ARG A CZ  
5464  N NH1 . ARG A 746  ? 0.3929 0.6420 0.3357 0.0746  0.0245  -0.0685 744  ARG A NH1 
5465  N NH2 . ARG A 746  ? 0.3367 0.5589 0.2839 0.0718  0.0246  -0.0639 744  ARG A NH2 
5466  N N   . ILE A 747  ? 0.2607 0.4670 0.2024 0.0703  0.0183  -0.0665 745  ILE A N   
5467  C CA  . ILE A 747  ? 0.2560 0.4615 0.1948 0.0667  0.0204  -0.0552 745  ILE A CA  
5468  C C   . ILE A 747  ? 0.2536 0.4616 0.1883 0.0653  0.0200  -0.0509 745  ILE A C   
5469  O O   . ILE A 747  ? 0.2519 0.4701 0.1831 0.0638  0.0217  -0.0439 745  ILE A O   
5470  C CB  . ILE A 747  ? 0.2579 0.4458 0.2001 0.0640  0.0204  -0.0506 745  ILE A CB  
5471  C CG1 . ILE A 747  ? 0.2632 0.4520 0.2086 0.0650  0.0215  -0.0525 745  ILE A CG1 
5472  C CG2 . ILE A 747  ? 0.3079 0.4918 0.2479 0.0601  0.0217  -0.0395 745  ILE A CG2 
5473  C CD1 . ILE A 747  ? 0.2839 0.4556 0.2334 0.0632  0.0208  -0.0510 745  ILE A CD1 
5474  N N   . LEU A 748  ? 0.2594 0.4583 0.1951 0.0655  0.0176  -0.0547 746  LEU A N   
5475  C CA  . LEU A 748  ? 0.2537 0.4549 0.1858 0.0644  0.0170  -0.0512 746  LEU A CA  
5476  C C   . LEU A 748  ? 0.2885 0.5093 0.2165 0.0664  0.0176  -0.0534 746  LEU A C   
5477  O O   . LEU A 748  ? 0.2712 0.4996 0.1954 0.0648  0.0185  -0.0465 746  LEU A O   
5478  C CB  . LEU A 748  ? 0.2556 0.4444 0.1897 0.0646  0.0142  -0.0560 746  LEU A CB  
5479  C CG  . LEU A 748  ? 0.2974 0.4685 0.2338 0.0614  0.0138  -0.0503 746  LEU A CG  
5480  C CD1 . LEU A 748  ? 0.3473 0.5066 0.2868 0.0621  0.0109  -0.0564 746  LEU A CD1 
5481  C CD2 . LEU A 748  ? 0.3218 0.4935 0.2550 0.0585  0.0147  -0.0409 746  LEU A CD2 
5482  N N   . ARG A 749  ? 0.2590 0.4887 0.1879 0.0701  0.0169  -0.0629 747  ARG A N   
5483  C CA  . ARG A 749  ? 0.2558 0.5037 0.1824 0.0716  0.0170  -0.0647 747  ARG A CA  
5484  C C   . ARG A 749  ? 0.2513 0.5104 0.1764 0.0698  0.0196  -0.0566 747  ARG A C   
5485  O O   . ARG A 749  ? 0.2906 0.5611 0.2134 0.0687  0.0198  -0.0516 747  ARG A O   
5486  C CB  . ARG A 749  ? 0.2934 0.5448 0.2246 0.0750  0.0146  -0.0760 747  ARG A CB  
5487  C CG  . ARG A 749  ? 0.3530 0.5977 0.2858 0.0765  0.0114  -0.0834 747  ARG A CG  
5488  C CD  . ARG A 749  ? 0.4178 0.6664 0.3561 0.0797  0.0088  -0.0941 747  ARG A CD  
5489  N NE  . ARG A 749  ? 0.3636 0.6074 0.3042 0.0811  0.0055  -0.1011 747  ARG A NE  
5490  C CZ  . ARG A 749  ? 0.4136 0.6631 0.3587 0.0838  0.0027  -0.1100 747  ARG A CZ  
5491  N NH1 . ARG A 749  ? 0.3785 0.6387 0.3262 0.0854  0.0028  -0.1132 747  ARG A NH1 
5492  N NH2 . ARG A 749  ? 0.3485 0.5929 0.2959 0.0848  -0.0004 -0.1158 747  ARG A NH2 
5493  N N   . GLU A 750  ? 0.2554 0.5114 0.1822 0.0695  0.0214  -0.0548 748  GLU A N   
5494  C CA  . GLU A 750  ? 0.2964 0.5621 0.2223 0.0675  0.0238  -0.0464 748  GLU A CA  
5495  C C   . GLU A 750  ? 0.2619 0.5265 0.1842 0.0640  0.0251  -0.0351 748  GLU A C   
5496  O O   . GLU A 750  ? 0.3005 0.5764 0.2218 0.0623  0.0259  -0.0281 748  GLU A O   
5497  C CB  . GLU A 750  ? 0.2769 0.5380 0.2054 0.0676  0.0255  -0.0464 748  GLU A CB  
5498  C CG  . GLU A 750  ? 0.3229 0.5941 0.2510 0.0655  0.0277  -0.0379 748  GLU A CG  
5499  C CD  . GLU A 750  ? 0.3933 0.6595 0.3240 0.0654  0.0295  -0.0373 748  GLU A CD  
5500  O OE1 . GLU A 750  ? 0.4716 0.7306 0.4052 0.0678  0.0287  -0.0454 748  GLU A OE1 
5501  O OE2 . GLU A 750  ? 0.4063 0.6758 0.3366 0.0629  0.0315  -0.0284 748  GLU A OE2 
5502  N N   . ALA A 751  ? 0.2451 0.4942 0.1675 0.0625  0.0243  -0.0330 749  ALA A N   
5503  C CA  . ALA A 751  ? 0.2736 0.5183 0.1948 0.0588  0.0246  -0.0223 749  ALA A CA  
5504  C C   . ALA A 751  ? 0.2893 0.5439 0.2065 0.0589  0.0238  -0.0208 749  ALA A C   
5505  O O   . ALA A 751  ? 0.3167 0.5703 0.2329 0.0560  0.0239  -0.0116 749  ALA A O   
5506  C CB  . ALA A 751  ? 0.2685 0.4920 0.1931 0.0568  0.0232  -0.0208 749  ALA A CB  
5507  N N   . GLY A 752  ? 0.2758 0.5388 0.1921 0.0619  0.0224  -0.0293 750  GLY A N   
5508  C CA  . GLY A 752  ? 0.2967 0.5690 0.2112 0.0616  0.0210  -0.0279 750  GLY A CA  
5509  C C   . GLY A 752  ? 0.3055 0.5720 0.2193 0.0633  0.0186  -0.0353 750  GLY A C   
5510  O O   . GLY A 752  ? 0.3135 0.5877 0.2258 0.0633  0.0173  -0.0347 750  GLY A O   
5511  N N   . ILE A 753  ? 0.3039 0.5574 0.2188 0.0648  0.0178  -0.0420 751  ILE A N   
5512  C CA  . ILE A 753  ? 0.3022 0.5502 0.2176 0.0665  0.0151  -0.0494 751  ILE A CA  
5513  C C   . ILE A 753  ? 0.3025 0.5619 0.2202 0.0693  0.0135  -0.0581 751  ILE A C   
5514  O O   . ILE A 753  ? 0.3109 0.5719 0.2319 0.0711  0.0135  -0.0637 751  ILE A O   
5515  C CB  . ILE A 753  ? 0.2807 0.5089 0.2010 0.0662  0.0135  -0.0534 751  ILE A CB  
5516  C CG1 . ILE A 753  ? 0.2824 0.4959 0.2042 0.0624  0.0142  -0.0440 751  ILE A CG1 
5517  C CG2 . ILE A 753  ? 0.3102 0.5334 0.2314 0.0677  0.0106  -0.0606 751  ILE A CG2 
5518  C CD1 . ILE A 753  ? 0.2770 0.4872 0.1969 0.0601  0.0135  -0.0378 751  ILE A CD1 
5519  N N   . PRO A 754  ? 0.3144 0.5818 0.2310 0.0698  0.0118  -0.0594 752  PRO A N   
5520  C CA  . PRO A 754  ? 0.3213 0.6001 0.2407 0.0725  0.0102  -0.0676 752  PRO A CA  
5521  C C   . PRO A 754  ? 0.2930 0.5628 0.2167 0.0753  0.0078  -0.0788 752  PRO A C   
5522  O O   . PRO A 754  ? 0.2812 0.5368 0.2052 0.0751  0.0068  -0.0807 752  PRO A O   
5523  C CB  . PRO A 754  ? 0.3371 0.6240 0.2542 0.0722  0.0089  -0.0660 752  PRO A CB  
5524  C CG  . PRO A 754  ? 0.3140 0.5960 0.2270 0.0689  0.0102  -0.0553 752  PRO A CG  
5525  C CD  . PRO A 754  ? 0.3086 0.5751 0.2217 0.0679  0.0113  -0.0536 752  PRO A CD  
5526  N N   . ALA A 755  ? 0.3073 0.5860 0.2347 0.0778  0.0067  -0.0862 753  ALA A N   
5527  C CA  . ALA A 755  ? 0.3128 0.5839 0.2456 0.0805  0.0041  -0.0969 753  ALA A CA  
5528  C C   . ALA A 755  ? 0.2897 0.5549 0.2232 0.0812  0.0012  -0.1015 753  ALA A C   
5529  O O   . ALA A 755  ? 0.3153 0.5678 0.2525 0.0821  -0.0008 -0.1073 753  ALA A O   
5530  C CB  . ALA A 755  ? 0.3569 0.6408 0.2936 0.0831  0.0031  -0.1038 753  ALA A CB  
5531  N N   . SER A 756  ? 0.2882 0.5622 0.2185 0.0806  0.0009  -0.0988 754  SER A N   
5532  C CA  . SER A 756  ? 0.2914 0.5602 0.2223 0.0811  -0.0018 -0.1029 754  SER A CA  
5533  C C   . SER A 756  ? 0.2897 0.5427 0.2182 0.0791  -0.0015 -0.0987 754  SER A C   
5534  O O   . SER A 756  ? 0.3443 0.5882 0.2748 0.0797  -0.0041 -0.1037 754  SER A O   
5535  C CB  . SER A 756  ? 0.3256 0.6085 0.2535 0.0810  -0.0020 -0.1005 754  SER A CB  
5536  O OG  . SER A 756  ? 0.3471 0.6334 0.2696 0.0781  0.0006  -0.0895 754  SER A OG  
5537  N N   . ALA A 757  ? 0.3073 0.5568 0.2319 0.0766  0.0014  -0.0896 755  ALA A N   
5538  C CA  . ALA A 757  ? 0.2758 0.5112 0.1980 0.0746  0.0018  -0.0852 755  ALA A CA  
5539  C C   . ALA A 757  ? 0.2864 0.5073 0.2122 0.0750  0.0016  -0.0887 755  ALA A C   
5540  O O   . ALA A 757  ? 0.2808 0.4861 0.2090 0.0728  0.0005  -0.0858 755  ALA A O   
5541  C CB  . ALA A 757  ? 0.2753 0.5133 0.1923 0.0717  0.0047  -0.0734 755  ALA A CB  
5542  N N   . LEU A 758  ? 0.2475 0.4706 0.1769 0.0766  0.0019  -0.0929 756  LEU A N   
5543  C CA  . LEU A 758  ? 0.2390 0.4482 0.1730 0.0766  0.0017  -0.0951 756  LEU A CA  
5544  C C   . LEU A 758  ? 0.2946 0.5072 0.2342 0.0798  -0.0002 -0.1051 756  LEU A C   
5545  O O   . LEU A 758  ? 0.3084 0.5305 0.2489 0.0806  0.0010  -0.1053 756  LEU A O   
5546  C CB  . LEU A 758  ? 0.2706 0.4760 0.2037 0.0739  0.0047  -0.0860 756  LEU A CB  
5547  C CG  . LEU A 758  ? 0.3091 0.4999 0.2477 0.0733  0.0043  -0.0870 756  LEU A CG  
5548  C CD1 . LEU A 758  ? 0.2819 0.4559 0.2243 0.0720  0.0017  -0.0880 756  LEU A CD1 
5549  C CD2 . LEU A 758  ? 0.3208 0.5089 0.2581 0.0705  0.0073  -0.0774 756  LEU A CD2 
5550  N N   . GLN A 759  ? 0.2688 0.4728 0.2135 0.0811  -0.0035 -0.1126 757  GLN A N   
5551  C CA  . GLN A 759  ? 0.2860 0.4905 0.2380 0.0837  -0.0062 -0.1216 757  GLN A CA  
5552  C C   . GLN A 759  ? 0.2950 0.4841 0.2520 0.0836  -0.0071 -0.1239 757  GLN A C   
5553  O O   . GLN A 759  ? 0.3092 0.4854 0.2664 0.0821  -0.0078 -0.1218 757  GLN A O   
5554  C CB  . GLN A 759  ? 0.2782 0.4857 0.2336 0.0852  -0.0098 -0.1286 757  GLN A CB  
5555  C CG  . GLN A 759  ? 0.3033 0.5275 0.2549 0.0857  -0.0092 -0.1274 757  GLN A CG  
5556  C CD  . GLN A 759  ? 0.2850 0.5118 0.2395 0.0872  -0.0127 -0.1339 757  GLN A CD  
5557  O OE1 . GLN A 759  ? 0.2800 0.5134 0.2400 0.0896  -0.0150 -0.1415 757  GLN A OE1 
5558  N NE2 . GLN A 759  ? 0.2786 0.5003 0.2299 0.0857  -0.0131 -0.1310 757  GLN A NE2 
5559  N N   . LEU A 760  ? 0.3060 0.4961 0.2675 0.0850  -0.0071 -0.1272 758  LEU A N   
5560  C CA  . LEU A 760  ? 0.3120 0.4885 0.2792 0.0851  -0.0082 -0.1295 758  LEU A CA  
5561  C C   . LEU A 760  ? 0.2924 0.4658 0.2684 0.0872  -0.0127 -0.1388 758  LEU A C   
5562  O O   . LEU A 760  ? 0.2910 0.4752 0.2699 0.0892  -0.0140 -0.1439 758  LEU A O   
5563  C CB  . LEU A 760  ? 0.2740 0.4531 0.2412 0.0852  -0.0055 -0.1269 758  LEU A CB  
5564  C CG  . LEU A 760  ? 0.2785 0.4442 0.2519 0.0854  -0.0067 -0.1292 758  LEU A CG  
5565  C CD1 . LEU A 760  ? 0.3089 0.4596 0.2816 0.0810  -0.0057 -0.1194 758  LEU A CD1 
5566  C CD2 . LEU A 760  ? 0.2927 0.4644 0.2682 0.0865  -0.0052 -0.1298 758  LEU A CD2 
5567  N N   . LEU A 761  ? 0.2714 0.4305 0.2520 0.0867  -0.0153 -0.1408 759  LEU A N   
5568  C CA  A LEU A 761  ? 0.3050 0.4596 0.2947 0.0882  -0.0200 -0.1488 759  LEU A CA  
5569  C CA  B LEU A 761  ? 0.3051 0.4596 0.2948 0.0882  -0.0200 -0.1488 759  LEU A CA  
5570  C C   . LEU A 761  ? 0.2945 0.4348 0.2910 0.0878  -0.0215 -0.1496 759  LEU A C   
5571  O O   . LEU A 761  ? 0.2858 0.4133 0.2846 0.0864  -0.0231 -0.1485 759  LEU A O   
5572  C CB  A LEU A 761  ? 0.3008 0.4529 0.2905 0.0878  -0.0225 -0.1505 759  LEU A CB  
5573  C CB  B LEU A 761  ? 0.3009 0.4523 0.2908 0.0878  -0.0226 -0.1505 759  LEU A CB  
5574  C CG  A LEU A 761  ? 0.3054 0.4716 0.2878 0.0880  -0.0208 -0.1486 759  LEU A CG  
5575  C CG  B LEU A 761  ? 0.3039 0.4685 0.2881 0.0882  -0.0219 -0.1502 759  LEU A CG  
5576  C CD1 A LEU A 761  ? 0.2988 0.4611 0.2790 0.0869  -0.0221 -0.1476 759  LEU A CD1 
5577  C CD1 B LEU A 761  ? 0.2955 0.4756 0.2807 0.0905  -0.0218 -0.1541 759  LEU A CD1 
5578  C CD2 A LEU A 761  ? 0.2973 0.4770 0.2834 0.0906  -0.0224 -0.1552 759  LEU A CD2 
5579  C CD2 B LEU A 761  ? 0.3081 0.4746 0.2824 0.0860  -0.0179 -0.1415 759  LEU A CD2 
5580  N N   . PRO A 762  ? 0.2887 0.4310 0.2889 0.0889  -0.0212 -0.1513 760  PRO A N   
5581  C CA  . PRO A 762  ? 0.2876 0.4167 0.2948 0.0885  -0.0228 -0.1519 760  PRO A CA  
5582  C C   . PRO A 762  ? 0.3463 0.4679 0.3634 0.0892  -0.0281 -0.1581 760  PRO A C   
5583  O O   . PRO A 762  ? 0.3373 0.4660 0.3573 0.0908  -0.0307 -0.1638 760  PRO A O   
5584  C CB  . PRO A 762  ? 0.2754 0.4113 0.2842 0.0899  -0.0214 -0.1531 760  PRO A CB  
5585  C CG  . PRO A 762  ? 0.2947 0.4461 0.2953 0.0903  -0.0179 -0.1507 760  PRO A CG  
5586  C CD  . PRO A 762  ? 0.2702 0.4271 0.2682 0.0905  -0.0192 -0.1523 760  PRO A CD  
5587  N N   . GLY A 763  ? 0.2908 0.3980 0.3132 0.0879  -0.0299 -0.1568 761  GLY A N   
5588  C CA  . GLY A 763  ? 0.3163 0.4154 0.3492 0.0881  -0.0351 -0.1617 761  GLY A CA  
5589  C C   . GLY A 763  ? 0.3613 0.4450 0.3961 0.0856  -0.0361 -0.1575 761  GLY A C   
5590  O O   . GLY A 763  ? 0.2964 0.3758 0.3249 0.0831  -0.0328 -0.1498 761  GLY A O   
5591  N N   . ASP A 764  ? 0.3538 0.4298 0.3979 0.0853  -0.0409 -0.1609 762  ASP A N   
5592  C CA  . ASP A 764  ? 0.3709 0.4320 0.4190 0.0827  -0.0427 -0.1570 762  ASP A CA  
5593  C C   . ASP A 764  ? 0.3631 0.4218 0.4076 0.0811  -0.0431 -0.1551 762  ASP A C   
5594  O O   . ASP A 764  ? 0.3028 0.3708 0.3394 0.0818  -0.0409 -0.1554 762  ASP A O   
5595  C CB  . ASP A 764  ? 0.4091 0.4627 0.4701 0.0828  -0.0477 -0.1603 762  ASP A CB  
5596  C CG  . ASP A 764  ? 0.4075 0.4664 0.4755 0.0845  -0.0520 -0.1674 762  ASP A CG  
5597  O OD1 . ASP A 764  ? 0.4128 0.4772 0.4766 0.0849  -0.0518 -0.1690 762  ASP A OD1 
5598  O OD2 . ASP A 764  ? 0.5057 0.5635 0.5836 0.0855  -0.0556 -0.1714 762  ASP A OD2 
5599  N N   . GLY A 765  ? 0.3250 0.3715 0.3752 0.0784  -0.0460 -0.1520 763  GLY A N   
5600  C CA  . GLY A 765  ? 0.3380 0.3815 0.3854 0.0761  -0.0463 -0.1487 763  GLY A CA  
5601  C C   . GLY A 765  ? 0.3275 0.3785 0.3759 0.0790  -0.0489 -0.1572 763  GLY A C   
5602  O O   . GLY A 765  ? 0.3305 0.3834 0.3734 0.0777  -0.0480 -0.1548 763  GLY A O   
5603  N N   . ARG A 766  ? 0.3444 0.4008 0.4002 0.0813  -0.0519 -0.1637 764  ARG A N   
5604  C CA  . ARG A 766  ? 0.3696 0.4349 0.4268 0.0831  -0.0541 -0.1695 764  ARG A CA  
5605  C C   . ARG A 766  ? 0.3511 0.4294 0.3971 0.0844  -0.0500 -0.1693 764  ARG A C   
5606  O O   . ARG A 766  ? 0.3316 0.4151 0.3749 0.0847  -0.0506 -0.1710 764  ARG A O   
5607  C CB  . ARG A 766  ? 0.4014 0.4714 0.4683 0.0855  -0.0576 -0.1763 764  ARG A CB  
5608  C CG  . ARG A 766  ? 0.4908 0.5504 0.5705 0.0846  -0.0628 -0.1779 764  ARG A CG  
5609  C CD  . ARG A 766  ? 0.4513 0.5172 0.5394 0.0873  -0.0657 -0.1846 764  ARG A CD  
5610  N NE  . ARG A 766  ? 0.4741 0.5428 0.5595 0.0880  -0.0627 -0.1833 764  ARG A NE  
5611  C CZ  . ARG A 766  ? 0.4746 0.5542 0.5611 0.0908  -0.0626 -0.1884 764  ARG A CZ  
5612  N NH1 . ARG A 766  ? 0.5487 0.6382 0.6386 0.0933  -0.0650 -0.1953 764  ARG A NH1 
5613  N NH2 . ARG A 766  ? 0.5183 0.5992 0.6026 0.0912  -0.0600 -0.1866 764  ARG A NH2 
5614  N N   . VAL A 767  ? 0.3059 0.3903 0.3458 0.0850  -0.0460 -0.1671 765  VAL A N   
5615  C CA  . VAL A 767  ? 0.3451 0.4421 0.3744 0.0859  -0.0421 -0.1656 765  VAL A CA  
5616  C C   . VAL A 767  ? 0.2957 0.3886 0.3166 0.0837  -0.0396 -0.1595 765  VAL A C   
5617  O O   . VAL A 767  ? 0.3118 0.4126 0.3267 0.0839  -0.0386 -0.1593 765  VAL A O   
5618  C CB  . VAL A 767  ? 0.3035 0.4076 0.3289 0.0869  -0.0385 -0.1641 765  VAL A CB  
5619  C CG1 . VAL A 767  ? 0.3326 0.4508 0.3477 0.0876  -0.0346 -0.1621 765  VAL A CG1 
5620  C CG2 . VAL A 767  ? 0.3582 0.4657 0.3925 0.0891  -0.0413 -0.1704 765  VAL A CG2 
5621  N N   . GLY A 768  ? 0.3087 0.3895 0.3298 0.0807  -0.0386 -0.1527 766  GLY A N   
5622  C CA  . GLY A 768  ? 0.2975 0.3732 0.3127 0.0770  -0.0366 -0.1439 766  GLY A CA  
5623  C C   . GLY A 768  ? 0.2741 0.3480 0.2916 0.0768  -0.0397 -0.1468 766  GLY A C   
5624  O O   . GLY A 768  ? 0.2903 0.3688 0.3012 0.0760  -0.0382 -0.1440 766  GLY A O   
5625  N N   . ALA A 769  ? 0.3014 0.3685 0.3288 0.0776  -0.0444 -0.1527 767  ALA A N   
5626  C CA  . ALA A 769  ? 0.2963 0.3604 0.3268 0.0771  -0.0477 -0.1551 767  ALA A CA  
5627  C C   . ALA A 769  ? 0.2985 0.3756 0.3259 0.0802  -0.0483 -0.1620 767  ALA A C   
5628  O O   . ALA A 769  ? 0.3277 0.4062 0.3518 0.0795  -0.0488 -0.1615 767  ALA A O   
5629  C CB  . ALA A 769  ? 0.3142 0.3683 0.3570 0.0771  -0.0529 -0.1595 767  ALA A CB  
5630  N N   . ALA A 770  ? 0.3212 0.4086 0.3502 0.0827  -0.0482 -0.1663 768  ALA A N   
5631  C CA  . ALA A 770  ? 0.3305 0.4315 0.3571 0.0848  -0.0486 -0.1705 768  ALA A CA  
5632  C C   . ALA A 770  ? 0.3106 0.4196 0.3249 0.0843  -0.0443 -0.1657 768  ALA A C   
5633  O O   . ALA A 770  ? 0.3306 0.4468 0.3419 0.0847  -0.0447 -0.1670 768  ALA A O   
5634  C CB  . ALA A 770  ? 0.3181 0.4289 0.3489 0.0876  -0.0492 -0.1759 768  ALA A CB  
5635  N N   . LEU A 771  ? 0.3042 0.4124 0.3119 0.0832  -0.0402 -0.1600 769  LEU A N   
5636  C CA  . LEU A 771  ? 0.2915 0.4068 0.2878 0.0824  -0.0361 -0.1544 769  LEU A CA  
5637  C C   . LEU A 771  ? 0.3198 0.4272 0.3143 0.0791  -0.0364 -0.1482 769  LEU A C   
5638  O O   . LEU A 771  ? 0.3321 0.4468 0.3207 0.0791  -0.0355 -0.1469 769  LEU A O   
5639  C CB  . LEU A 771  ? 0.2798 0.3942 0.2720 0.0808  -0.0319 -0.1469 769  LEU A CB  
5640  C CG  . LEU A 771  ? 0.2855 0.4102 0.2778 0.0837  -0.0307 -0.1514 769  LEU A CG  
5641  C CD1 . LEU A 771  ? 0.2943 0.4160 0.2834 0.0820  -0.0270 -0.1441 769  LEU A CD1 
5642  C CD2 . LEU A 771  ? 0.3099 0.4509 0.2971 0.0852  -0.0295 -0.1524 769  LEU A CD2 
5643  N N   . VAL A 772  ? 0.2951 0.3879 0.2945 0.0763  -0.0375 -0.1440 770  VAL A N   
5644  C CA  . VAL A 772  ? 0.2915 0.3764 0.2901 0.0731  -0.0379 -0.1384 770  VAL A CA  
5645  C C   . VAL A 772  ? 0.3401 0.4289 0.3408 0.0747  -0.0414 -0.1449 770  VAL A C   
5646  O O   . VAL A 772  ? 0.3715 0.4620 0.3675 0.0734  -0.0407 -0.1414 770  VAL A O   
5647  C CB  . VAL A 772  ? 0.2810 0.3508 0.2859 0.0702  -0.0391 -0.1341 770  VAL A CB  
5648  C CG1 . VAL A 772  ? 0.3526 0.4148 0.3580 0.0673  -0.0402 -0.1298 770  VAL A CG1 
5649  C CG2 . VAL A 772  ? 0.2963 0.3627 0.2976 0.0682  -0.0352 -0.1264 770  VAL A CG2 
5650  N N   . ALA A 773  ? 0.3574 0.4476 0.3657 0.0776  -0.0453 -0.1547 771  ALA A N   
5651  C CA  . ALA A 773  ? 0.3150 0.4077 0.3268 0.0792  -0.0492 -0.1617 771  ALA A CA  
5652  C C   . ALA A 773  ? 0.3861 0.4944 0.3922 0.0812  -0.0481 -0.1640 771  ALA A C   
5653  O O   . ALA A 773  ? 0.4152 0.5265 0.4233 0.0817  -0.0505 -0.1671 771  ALA A O   
5654  C CB  . ALA A 773  ? 0.3439 0.4323 0.3682 0.0803  -0.0537 -0.1679 771  ALA A CB  
5655  N N   . ALA A 774  ? 0.3890 0.5074 0.3886 0.0822  -0.0444 -0.1621 772  ALA A N   
5656  C CA  . ALA A 774  ? 0.3853 0.5195 0.3806 0.0841  -0.0435 -0.1640 772  ALA A CA  
5657  C C   . ALA A 774  ? 0.3690 0.5063 0.3566 0.0828  -0.0424 -0.1599 772  ALA A C   
5658  O O   . ALA A 774  ? 0.3434 0.4749 0.3249 0.0806  -0.0401 -0.1535 772  ALA A O   
5659  C CB  . ALA A 774  ? 0.3311 0.4754 0.3215 0.0852  -0.0399 -0.1620 772  ALA A CB  
5660  N N   . ALA A 775  ? 0.4260 0.5730 0.4142 0.0842  -0.0441 -0.1637 773  ALA A N   
5661  C CA  . ALA A 775  ? 0.4069 0.5553 0.3897 0.0830  -0.0440 -0.1608 773  ALA A CA  
5662  C C   . ALA A 775  ? 0.3444 0.4987 0.3161 0.0817  -0.0397 -0.1528 773  ALA A C   
5663  O O   . ALA A 775  ? 0.3819 0.5319 0.3488 0.0797  -0.0392 -0.1481 773  ALA A O   
5664  C CB  . ALA A 775  ? 0.4200 0.5785 0.4058 0.0850  -0.0466 -0.1666 773  ALA A CB  
5665  N N   . GLU A 776  ? 0.3298 0.4940 0.2977 0.0826  -0.0367 -0.1509 774  GLU A N   
5666  C CA  . GLU A 776  ? 0.2843 0.4552 0.2423 0.0812  -0.0327 -0.1428 774  GLU A CA  
5667  C C   . GLU A 776  ? 0.2990 0.4594 0.2547 0.0786  -0.0299 -0.1351 774  GLU A C   
5668  O O   . GLU A 776  ? 0.3360 0.4998 0.2855 0.0767  -0.0267 -0.1264 774  GLU A O   
5669  C CB  . GLU A 776  ? 0.3681 0.5553 0.3237 0.0829  -0.0307 -0.1429 774  GLU A CB  
5670  C CG  . GLU A 776  ? 0.4121 0.6107 0.3707 0.0850  -0.0331 -0.1490 774  GLU A CG  
5671  C CD  . GLU A 776  ? 0.4592 0.6583 0.4269 0.0876  -0.0359 -0.1580 774  GLU A CD  
5672  O OE1 . GLU A 776  ? 0.3709 0.5591 0.3438 0.0875  -0.0367 -0.1599 774  GLU A OE1 
5673  O OE2 . GLU A 776  ? 0.5318 0.7428 0.5020 0.0898  -0.0373 -0.1631 774  GLU A OE2 
5674  N N   . THR A 777  ? 0.2888 0.4358 0.2512 0.0778  -0.0312 -0.1361 775  THR A N   
5675  C CA  . THR A 777  ? 0.3109 0.4468 0.2731 0.0745  -0.0286 -0.1271 775  THR A CA  
5676  C C   . THR A 777  ? 0.3070 0.4359 0.2666 0.0711  -0.0279 -0.1189 775  THR A C   
5677  O O   . THR A 777  ? 0.3410 0.4629 0.3041 0.0704  -0.0305 -0.1206 775  THR A O   
5678  C CB  . THR A 777  ? 0.3060 0.4295 0.2764 0.0744  -0.0306 -0.1305 775  THR A CB  
5679  O OG1 . THR A 777  ? 0.2946 0.4249 0.2672 0.0774  -0.0308 -0.1372 775  THR A OG1 
5680  C CG2 . THR A 777  ? 0.2771 0.3885 0.2473 0.0708  -0.0282 -0.1212 775  THR A CG2 
5681  N N   . ALA A 778  ? 0.2793 0.4102 0.2331 0.0692  -0.0244 -0.1100 776  ALA A N   
5682  C CA  . ALA A 778  ? 0.2567 0.3831 0.2075 0.0663  -0.0234 -0.1021 776  ALA A CA  
5683  C C   . ALA A 778  ? 0.2743 0.3867 0.2271 0.0630  -0.0220 -0.0950 776  ALA A C   
5684  O O   . ALA A 778  ? 0.2975 0.4044 0.2492 0.0606  -0.0216 -0.0890 776  ALA A O   
5685  C CB  . ALA A 778  ? 0.2781 0.4168 0.2216 0.0662  -0.0209 -0.0966 776  ALA A CB  
5686  N N   . GLY A 779  ? 0.2677 0.3751 0.2236 0.0631  -0.0213 -0.0956 777  GLY A N   
5687  C CA  . GLY A 779  ? 0.2594 0.3541 0.2172 0.0601  -0.0200 -0.0894 777  GLY A CA  
5688  C C   . GLY A 779  ? 0.2411 0.3321 0.2028 0.0609  -0.0199 -0.0922 777  GLY A C   
5689  O O   . GLY A 779  ? 0.2534 0.3530 0.2147 0.0635  -0.0197 -0.0970 777  GLY A O   
5690  N N   . VAL A 780  ? 0.2549 0.3335 0.2206 0.0587  -0.0202 -0.0893 778  VAL A N   
5691  C CA  . VAL A 780  ? 0.2454 0.3189 0.2155 0.0591  -0.0204 -0.0915 778  VAL A CA  
5692  C C   . VAL A 780  ? 0.2388 0.3045 0.2077 0.0562  -0.0177 -0.0833 778  VAL A C   
5693  O O   . VAL A 780  ? 0.2511 0.3094 0.2200 0.0535  -0.0175 -0.0783 778  VAL A O   
5694  C CB  . VAL A 780  ? 0.2644 0.3303 0.2422 0.0595  -0.0242 -0.0974 778  VAL A CB  
5695  C CG1 . VAL A 780  ? 0.2551 0.3159 0.2379 0.0599  -0.0246 -0.0992 778  VAL A CG1 
5696  C CG2 . VAL A 780  ? 0.2755 0.3493 0.2549 0.0626  -0.0271 -0.1060 778  VAL A CG2 
5697  N N   . MET A 781  ? 0.2197 0.2877 0.1877 0.0567  -0.0158 -0.0823 779  MET A N   
5698  C CA  . MET A 781  ? 0.2224 0.2829 0.1905 0.0542  -0.0136 -0.0757 779  MET A CA  
5699  C C   . MET A 781  ? 0.2518 0.3066 0.2257 0.0548  -0.0150 -0.0795 779  MET A C   
5700  O O   . MET A 781  ? 0.2494 0.3103 0.2243 0.0573  -0.0152 -0.0842 779  MET A O   
5701  C CB  . MET A 781  ? 0.2595 0.3269 0.2220 0.0540  -0.0102 -0.0706 779  MET A CB  
5702  C CG  . MET A 781  ? 0.2501 0.3246 0.2073 0.0537  -0.0092 -0.0671 779  MET A CG  
5703  S SD  . MET A 781  ? 0.2596 0.3441 0.2112 0.0536  -0.0056 -0.0614 779  MET A SD  
5704  C CE  . MET A 781  ? 0.2648 0.3379 0.2171 0.0501  -0.0037 -0.0532 779  MET A CE  
5705  N N   . PHE A 782  ? 0.2547 0.2984 0.2328 0.0526  -0.0162 -0.0775 780  PHE A N   
5706  C CA  . PHE A 782  ? 0.2612 0.2986 0.2457 0.0529  -0.0180 -0.0804 780  PHE A CA  
5707  C C   . PHE A 782  ? 0.2516 0.2810 0.2362 0.0501  -0.0162 -0.0738 780  PHE A C   
5708  O O   . PHE A 782  ? 0.2389 0.2629 0.2222 0.0474  -0.0155 -0.0685 780  PHE A O   
5709  C CB  . PHE A 782  ? 0.2574 0.2887 0.2481 0.0527  -0.0219 -0.0844 780  PHE A CB  
5710  C CG  . PHE A 782  ? 0.2489 0.2730 0.2469 0.0525  -0.0240 -0.0865 780  PHE A CG  
5711  C CD1 . PHE A 782  ? 0.2714 0.2991 0.2736 0.0554  -0.0258 -0.0933 780  PHE A CD1 
5712  C CD2 . PHE A 782  ? 0.2411 0.2553 0.2419 0.0494  -0.0243 -0.0814 780  PHE A CD2 
5713  C CE1 . PHE A 782  ? 0.2840 0.3050 0.2934 0.0553  -0.0280 -0.0951 780  PHE A CE1 
5714  C CE2 . PHE A 782  ? 0.2528 0.2608 0.2604 0.0491  -0.0264 -0.0827 780  PHE A CE2 
5715  C CZ  . PHE A 782  ? 0.2527 0.2637 0.2649 0.0521  -0.0284 -0.0895 780  PHE A CZ  
5716  N N   . THR A 783  ? 0.2235 0.2526 0.2100 0.0508  -0.0156 -0.0745 781  THR A N   
5717  C CA  . THR A 783  ? 0.2602 0.2810 0.2484 0.0483  -0.0147 -0.0695 781  THR A CA  
5718  C C   . THR A 783  ? 0.2585 0.2754 0.2537 0.0494  -0.0173 -0.0740 781  THR A C   
5719  O O   . THR A 783  ? 0.2504 0.2730 0.2471 0.0522  -0.0179 -0.0793 781  THR A O   
5720  C CB  . THR A 783  ? 0.2670 0.2910 0.2502 0.0477  -0.0111 -0.0645 781  THR A CB  
5721  O OG1 . THR A 783  ? 0.2507 0.2783 0.2282 0.0468  -0.0091 -0.0603 781  THR A OG1 
5722  C CG2 . THR A 783  ? 0.2708 0.2865 0.2559 0.0452  -0.0103 -0.0596 781  THR A CG2 
5723  N N   . GLY A 784  ? 0.2479 0.2557 0.2479 0.0472  -0.0191 -0.0720 782  GLY A N   
5724  C CA  . GLY A 784  ? 0.2528 0.2562 0.2607 0.0480  -0.0223 -0.0761 782  GLY A CA  
5725  C C   . GLY A 784  ? 0.2493 0.2435 0.2618 0.0451  -0.0244 -0.0730 782  GLY A C   
5726  O O   . GLY A 784  ? 0.2533 0.2444 0.2624 0.0424  -0.0227 -0.0671 782  GLY A O   
5727  N N   . SER A 785  ? 0.2575 0.2477 0.2781 0.0456  -0.0281 -0.0769 783  SER A N   
5728  C CA  . SER A 785  ? 0.2628 0.2447 0.2887 0.0428  -0.0304 -0.0737 783  SER A CA  
5729  C C   . SER A 785  ? 0.2870 0.2682 0.3124 0.0417  -0.0316 -0.0735 783  SER A C   
5730  O O   . SER A 785  ? 0.2676 0.2541 0.2915 0.0438  -0.0322 -0.0781 783  SER A O   
5731  C CB  . SER A 785  ? 0.2915 0.2696 0.3272 0.0437  -0.0346 -0.0778 783  SER A CB  
5732  O OG  . SER A 785  ? 0.2873 0.2689 0.3267 0.0466  -0.0375 -0.0855 783  SER A OG  
5733  N N   . THR A 786  ? 0.2357 0.2108 0.2624 0.0384  -0.0318 -0.0680 784  THR A N   
5734  C CA  . THR A 786  ? 0.2550 0.2290 0.2821 0.0371  -0.0330 -0.0674 784  THR A CA  
5735  C C   . THR A 786  ? 0.2522 0.2259 0.2866 0.0387  -0.0375 -0.0738 784  THR A C   
5736  O O   . THR A 786  ? 0.2674 0.2438 0.3006 0.0394  -0.0383 -0.0763 784  THR A O   
5737  C CB  . THR A 786  ? 0.2797 0.2476 0.3079 0.0332  -0.0327 -0.0606 784  THR A CB  
5738  O OG1 . THR A 786  ? 0.3027 0.2715 0.3243 0.0320  -0.0287 -0.0554 784  THR A OG1 
5739  C CG2 . THR A 786  ? 0.3007 0.2678 0.3291 0.0317  -0.0337 -0.0596 784  THR A CG2 
5740  N N   . GLU A 787  ? 0.3065 0.2769 0.3489 0.0394  -0.0406 -0.0766 785  GLU A N   
5741  C CA  . GLU A 787  ? 0.2900 0.2595 0.3407 0.0409  -0.0453 -0.0828 785  GLU A CA  
5742  C C   . GLU A 787  ? 0.2704 0.2476 0.3188 0.0448  -0.0456 -0.0905 785  GLU A C   
5743  O O   . GLU A 787  ? 0.2802 0.2588 0.3313 0.0458  -0.0482 -0.0950 785  GLU A O   
5744  C CB  . GLU A 787  ? 0.3387 0.3030 0.3991 0.0407  -0.0488 -0.0839 785  GLU A CB  
5745  N N   . VAL A 788  ? 0.2891 0.2719 0.3325 0.0470  -0.0428 -0.0921 786  VAL A N   
5746  C CA  . VAL A 788  ? 0.2682 0.2597 0.3087 0.0507  -0.0427 -0.0991 786  VAL A CA  
5747  C C   . VAL A 788  ? 0.2713 0.2675 0.3039 0.0503  -0.0404 -0.0973 786  VAL A C   
5748  O O   . VAL A 788  ? 0.2666 0.2676 0.2993 0.0522  -0.0420 -0.1027 786  VAL A O   
5749  C CB  . VAL A 788  ? 0.2712 0.2682 0.3087 0.0531  -0.0404 -0.1011 786  VAL A CB  
5750  C CG1 . VAL A 788  ? 0.2990 0.3067 0.3318 0.0566  -0.0395 -0.1071 786  VAL A CG1 
5751  C CG2 . VAL A 788  ? 0.2918 0.2850 0.3386 0.0543  -0.0436 -0.1049 786  VAL A CG2 
5752  N N   . ALA A 789  ? 0.2593 0.2542 0.2853 0.0477  -0.0367 -0.0897 787  ALA A N   
5753  C CA  . ALA A 789  ? 0.2468 0.2454 0.2659 0.0471  -0.0348 -0.0875 787  ALA A CA  
5754  C C   . ALA A 789  ? 0.2307 0.2264 0.2542 0.0463  -0.0380 -0.0893 787  ALA A C   
5755  O O   . ALA A 789  ? 0.2470 0.2478 0.2674 0.0475  -0.0382 -0.0918 787  ALA A O   
5756  C CB  . ALA A 789  ? 0.2221 0.2182 0.2353 0.0442  -0.0310 -0.0791 787  ALA A CB  
5757  N N   . ARG A 790  ? 0.2388 0.2266 0.2697 0.0443  -0.0408 -0.0879 788  ARG A N   
5758  C CA  . ARG A 790  ? 0.2627 0.2476 0.2987 0.0433  -0.0441 -0.0893 788  ARG A CA  
5759  C C   . ARG A 790  ? 0.2566 0.2457 0.2970 0.0466  -0.0477 -0.0983 788  ARG A C   
5760  O O   . ARG A 790  ? 0.2709 0.2619 0.3116 0.0469  -0.0493 -0.1007 788  ARG A O   
5761  C CB  . ARG A 790  ? 0.3028 0.2789 0.3465 0.0403  -0.0465 -0.0855 788  ARG A CB  
5762  C CG  . ARG A 790  ? 0.2821 0.2546 0.3310 0.0384  -0.0496 -0.0852 788  ARG A CG  
5763  C CD  . ARG A 790  ? 0.3031 0.2678 0.3585 0.0349  -0.0512 -0.0797 788  ARG A CD  
5764  N NE  . ARG A 790  ? 0.2966 0.2599 0.3458 0.0321  -0.0472 -0.0718 788  ARG A NE  
5765  C CZ  . ARG A 790  ? 0.2789 0.2392 0.3280 0.0306  -0.0457 -0.0673 788  ARG A CZ  
5766  N NH1 . ARG A 790  ? 0.3306 0.2887 0.3856 0.0315  -0.0478 -0.0694 788  ARG A NH1 
5767  N NH2 . ARG A 790  ? 0.3333 0.2930 0.3766 0.0282  -0.0422 -0.0608 788  ARG A NH2 
5768  N N   . LEU A 791  ? 0.2695 0.2606 0.3136 0.0493  -0.0490 -0.1037 789  LEU A N   
5769  C CA  . LEU A 791  ? 0.2869 0.2835 0.3348 0.0529  -0.0521 -0.1131 789  LEU A CA  
5770  C C   . LEU A 791  ? 0.3021 0.3088 0.3413 0.0551  -0.0496 -0.1155 789  LEU A C   
5771  O O   . LEU A 791  ? 0.2825 0.2933 0.3229 0.0568  -0.0519 -0.1212 789  LEU A O   
5772  C CB  . LEU A 791  ? 0.2813 0.2786 0.3345 0.0554  -0.0536 -0.1182 789  LEU A CB  
5773  C CG  . LEU A 791  ? 0.3568 0.3447 0.4202 0.0537  -0.0569 -0.1168 789  LEU A CG  
5774  C CD1 . LEU A 791  ? 0.3935 0.3828 0.4610 0.0563  -0.0576 -0.1212 789  LEU A CD1 
5775  C CD2 . LEU A 791  ? 0.3560 0.3399 0.4289 0.0535  -0.0622 -0.1207 789  LEU A CD2 
5776  N N   . ILE A 792  ? 0.2728 0.2837 0.3032 0.0549  -0.0450 -0.1112 790  ILE A N   
5777  C CA  . ILE A 792  ? 0.2926 0.3133 0.3145 0.0566  -0.0425 -0.1124 790  ILE A CA  
5778  C C   . ILE A 792  ? 0.3004 0.3203 0.3193 0.0547  -0.0424 -0.1090 790  ILE A C   
5779  O O   . ILE A 792  ? 0.2949 0.3216 0.3114 0.0564  -0.0431 -0.1130 790  ILE A O   
5780  C CB  . ILE A 792  ? 0.2706 0.2956 0.2849 0.0566  -0.0379 -0.1078 790  ILE A CB  
5781  C CG1 . ILE A 792  ? 0.2753 0.3037 0.2926 0.0594  -0.0384 -0.1130 790  ILE A CG1 
5782  C CG2 . ILE A 792  ? 0.2937 0.3280 0.2990 0.0574  -0.0351 -0.1066 790  ILE A CG2 
5783  C CD1 . ILE A 792  ? 0.2665 0.2963 0.2786 0.0588  -0.0343 -0.1079 790  ILE A CD1 
5784  N N   . GLN A 793  ? 0.2400 0.2519 0.2591 0.0511  -0.0414 -0.1018 791  GLN A N   
5785  C CA  . GLN A 793  ? 0.2464 0.2567 0.2636 0.0491  -0.0415 -0.0985 791  GLN A CA  
5786  C C   . GLN A 793  ? 0.2631 0.2735 0.2865 0.0502  -0.0460 -0.1048 791  GLN A C   
5787  O O   . GLN A 793  ? 0.2837 0.2985 0.3040 0.0507  -0.0462 -0.1059 791  GLN A O   
5788  C CB  . GLN A 793  ? 0.2805 0.2820 0.2989 0.0453  -0.0405 -0.0908 791  GLN A CB  
5789  C CG  . GLN A 793  ? 0.2612 0.2606 0.2786 0.0430  -0.0406 -0.0872 791  GLN A CG  
5790  C CD  . GLN A 793  ? 0.3007 0.2914 0.3215 0.0394  -0.0406 -0.0811 791  GLN A CD  
5791  O OE1 . GLN A 793  ? 0.3389 0.3244 0.3665 0.0386  -0.0427 -0.0815 791  GLN A OE1 
5792  N NE2 . GLN A 793  ? 0.3291 0.3189 0.3456 0.0371  -0.0383 -0.0753 791  GLN A NE2 
5793  N N   . ALA A 794  ? 0.2873 0.2930 0.3199 0.0507  -0.0497 -0.1090 792  ALA A N   
5794  C CA  . ALA A 794  ? 0.3178 0.3231 0.3576 0.0518  -0.0544 -0.1153 792  ALA A CA  
5795  C C   . ALA A 794  ? 0.2995 0.3150 0.3369 0.0557  -0.0552 -0.1235 792  ALA A C   
5796  O O   . ALA A 794  ? 0.3370 0.3554 0.3749 0.0564  -0.0573 -0.1269 792  ALA A O   
5797  C CB  . ALA A 794  ? 0.3069 0.3050 0.3578 0.0515  -0.0585 -0.1179 792  ALA A CB  
5798  N N   . GLN A 795  ? 0.3203 0.3417 0.3551 0.0584  -0.0537 -0.1267 793  GLN A N   
5799  C CA  . GLN A 795  ? 0.3114 0.3441 0.3431 0.0622  -0.0540 -0.1343 793  GLN A CA  
5800  C C   . GLN A 795  ? 0.3299 0.3694 0.3526 0.0619  -0.0515 -0.1314 793  GLN A C   
5801  O O   . GLN A 795  ? 0.3482 0.3941 0.3705 0.0639  -0.0534 -0.1370 793  GLN A O   
5802  C CB  . GLN A 795  ? 0.3434 0.3819 0.3720 0.0645  -0.0516 -0.1360 793  GLN A CB  
5803  C CG  . GLN A 795  ? 0.4519 0.4908 0.4888 0.0674  -0.0549 -0.1442 793  GLN A CG  
5804  C CD  . GLN A 795  ? 0.4283 0.4747 0.4608 0.0697  -0.0519 -0.1456 793  GLN A CD  
5805  O OE1 . GLN A 795  ? 0.4503 0.4938 0.4790 0.0679  -0.0485 -0.1388 793  GLN A OE1 
5806  N NE2 . GLN A 795  ? 0.3460 0.4025 0.3790 0.0737  -0.0532 -0.1545 793  GLN A NE2 
5807  N N   . LEU A 796  ? 0.2839 0.3221 0.2993 0.0595  -0.0472 -0.1227 794  LEU A N   
5808  C CA  . LEU A 796  ? 0.3275 0.3722 0.3345 0.0592  -0.0447 -0.1193 794  LEU A CA  
5809  C C   . LEU A 796  ? 0.3125 0.3533 0.3211 0.0573  -0.0465 -0.1177 794  LEU A C   
5810  O O   . LEU A 796  ? 0.3681 0.4153 0.3713 0.0576  -0.0456 -0.1170 794  LEU A O   
5811  C CB  . LEU A 796  ? 0.3068 0.3508 0.3067 0.0571  -0.0400 -0.1106 794  LEU A CB  
5812  C CG  . LEU A 796  ? 0.2874 0.3377 0.2839 0.0591  -0.0375 -0.1114 794  LEU A CG  
5813  C CD1 . LEU A 796  ? 0.2905 0.3394 0.2807 0.0568  -0.0331 -0.1025 794  LEU A CD1 
5814  C CD2 . LEU A 796  ? 0.3250 0.3884 0.3177 0.0625  -0.0377 -0.1175 794  LEU A CD2 
5815  N N   . ALA A 797  ? 0.3231 0.3541 0.3392 0.0552  -0.0491 -0.1167 795  ALA A N   
5816  C CA  . ALA A 797  ? 0.3488 0.3763 0.3665 0.0532  -0.0507 -0.1149 795  ALA A CA  
5817  C C   . ALA A 797  ? 0.3655 0.3994 0.3850 0.0557  -0.0540 -0.1227 795  ALA A C   
5818  O O   . ALA A 797  ? 0.4889 0.5238 0.5068 0.0548  -0.0545 -0.1213 795  ALA A O   
5819  C CB  . ALA A 797  ? 0.3671 0.3834 0.3929 0.0504  -0.0529 -0.1121 795  ALA A CB  
5820  N N   . ASP A 798  ? 0.4096 0.4485 0.4325 0.0590  -0.0563 -0.1310 796  ASP A N   
5821  C CA  . ASP A 798  ? 0.4554 0.5017 0.4799 0.0619  -0.0594 -0.1394 796  ASP A CA  
5822  C C   . ASP A 798  ? 0.4524 0.5105 0.4671 0.0635  -0.0567 -0.1393 796  ASP A C   
5823  O O   . ASP A 798  ? 0.4660 0.5308 0.4805 0.0653  -0.0589 -0.1448 796  ASP A O   
5824  C CB  . ASP A 798  ? 0.4246 0.4739 0.4552 0.0653  -0.0623 -0.1486 796  ASP A CB  
5825  C CG  . ASP A 798  ? 0.5780 0.6167 0.6199 0.0642  -0.0659 -0.1501 796  ASP A CG  
5826  O OD1 . ASP A 798  ? 0.6333 0.6636 0.6794 0.0611  -0.0675 -0.1459 796  ASP A OD1 
5827  O OD2 . ASP A 798  ? 0.5955 0.6344 0.6421 0.0663  -0.0673 -0.1552 796  ASP A OD2 
5828  N N   . ARG A 799  ? 0.3886 0.4497 0.3955 0.0629  -0.0522 -0.1332 797  ARG A N   
5829  C CA  A ARG A 799  ? 0.3805 0.4541 0.3788 0.0649  -0.0496 -0.1336 797  ARG A CA  
5830  C CA  B ARG A 799  ? 0.3806 0.4543 0.3790 0.0649  -0.0497 -0.1338 797  ARG A CA  
5831  C C   . ARG A 799  ? 0.3319 0.4068 0.3230 0.0627  -0.0468 -0.1256 797  ARG A C   
5832  O O   . ARG A 799  ? 0.3224 0.3885 0.3133 0.0595  -0.0452 -0.1182 797  ARG A O   
5833  C CB  A ARG A 799  ? 0.4026 0.4793 0.3978 0.0659  -0.0466 -0.1323 797  ARG A CB  
5834  C CB  B ARG A 799  ? 0.4023 0.4805 0.3975 0.0663  -0.0469 -0.1336 797  ARG A CB  
5835  C CG  A ARG A 799  ? 0.3764 0.4495 0.3794 0.0675  -0.0490 -0.1387 797  ARG A CG  
5836  C CG  B ARG A 799  ? 0.3857 0.4664 0.3871 0.0695  -0.0496 -0.1429 797  ARG A CG  
5837  C CD  A ARG A 799  ? 0.3902 0.4737 0.3951 0.0716  -0.0517 -0.1493 797  ARG A CD  
5838  C CD  B ARG A 799  ? 0.3875 0.4754 0.3843 0.0712  -0.0465 -0.1427 797  ARG A CD  
5839  N NE  A ARG A 799  ? 0.3914 0.4881 0.3877 0.0736  -0.0485 -0.1492 797  ARG A NE  
5840  N NE  B ARG A 799  ? 0.3921 0.4927 0.3798 0.0722  -0.0437 -0.1409 797  ARG A NE  
5841  C CZ  A ARG A 799  ? 0.3638 0.4638 0.3572 0.0742  -0.0456 -0.1475 797  ARG A CZ  
5842  C CZ  B ARG A 799  ? 0.3690 0.4745 0.3499 0.0717  -0.0396 -0.1353 797  ARG A CZ  
5843  N NH1 A ARG A 799  ? 0.4046 0.4957 0.4028 0.0733  -0.0455 -0.1461 797  ARG A NH1 
5844  N NH1 B ARG A 799  ? 0.3373 0.4365 0.3192 0.0705  -0.0376 -0.1313 797  ARG A NH1 
5845  N NH2 A ARG A 799  ? 0.3959 0.5087 0.3815 0.0758  -0.0428 -0.1469 797  ARG A NH2 
5846  N NH2 B ARG A 799  ? 0.3643 0.4814 0.3376 0.0724  -0.0376 -0.1333 797  ARG A NH2 
5847  N N   . LEU A 800  ? 0.3565 0.4427 0.3418 0.0644  -0.0464 -0.1273 798  LEU A N   
5848  C CA  . LEU A 800  ? 0.3373 0.4270 0.3152 0.0628  -0.0435 -0.1199 798  LEU A CA  
5849  C C   . LEU A 800  ? 0.3187 0.4221 0.2894 0.0650  -0.0413 -0.1204 798  LEU A C   
5850  O O   . LEU A 800  ? 0.3682 0.4803 0.3395 0.0681  -0.0427 -0.1282 798  LEU A O   
5851  C CB  . LEU A 800  ? 0.3670 0.4570 0.3455 0.0622  -0.0458 -0.1206 798  LEU A CB  
5852  C CG  . LEU A 800  ? 0.3313 0.4088 0.3159 0.0595  -0.0477 -0.1183 798  LEU A CG  
5853  C CD1 . LEU A 800  ? 0.3631 0.4431 0.3482 0.0594  -0.0502 -0.1202 798  LEU A CD1 
5854  C CD2 . LEU A 800  ? 0.3530 0.4226 0.3354 0.0562  -0.0444 -0.1087 798  LEU A CD2 
5855  N N   . SER A 801  ? 0.3539 0.4595 0.3181 0.0633  -0.0378 -0.1120 799  SER A N   
5856  C CA  . SER A 801  ? 0.3766 0.4958 0.3337 0.0649  -0.0357 -0.1109 799  SER A CA  
5857  C C   . SER A 801  ? 0.4159 0.5453 0.3708 0.0665  -0.0378 -0.1150 799  SER A C   
5858  O O   . SER A 801  ? 0.3991 0.5238 0.3574 0.0660  -0.0405 -0.1172 799  SER A O   
5859  C CB  . SER A 801  ? 0.3942 0.5118 0.3462 0.0623  -0.0320 -0.1003 799  SER A CB  
5860  O OG  . SER A 801  ? 0.3887 0.5030 0.3401 0.0603  -0.0326 -0.0959 799  SER A OG  
5861  N N   . PRO A 802  ? 0.3936 0.5375 0.3427 0.0685  -0.0366 -0.1160 800  PRO A N   
5862  C CA  . PRO A 802  ? 0.4275 0.5820 0.3736 0.0699  -0.0383 -0.1189 800  PRO A CA  
5863  C C   . PRO A 802  ? 0.4221 0.5726 0.3665 0.0673  -0.0382 -0.1119 800  PRO A C   
5864  O O   . PRO A 802  ? 0.4950 0.6498 0.4394 0.0681  -0.0407 -0.1151 800  PRO A O   
5865  C CB  . PRO A 802  ? 0.4548 0.6254 0.3943 0.0717  -0.0361 -0.1184 800  PRO A CB  
5866  C CG  . PRO A 802  ? 0.4705 0.6396 0.4120 0.0728  -0.0348 -0.1208 800  PRO A CG  
5867  C CD  . PRO A 802  ? 0.4030 0.5552 0.3487 0.0699  -0.0340 -0.1156 800  PRO A CD  
5868  N N   . ALA A 803  ? 0.4242 0.5666 0.3673 0.0644  -0.0356 -0.1026 801  ALA A N   
5869  C CA  . ALA A 803  ? 0.4335 0.5703 0.3762 0.0619  -0.0357 -0.0962 801  ALA A CA  
5870  C C   . ALA A 803  ? 0.4877 0.6110 0.4371 0.0605  -0.0379 -0.0981 801  ALA A C   
5871  O O   . ALA A 803  ? 0.5065 0.6243 0.4563 0.0583  -0.0380 -0.0932 801  ALA A O   
5872  C CB  . ALA A 803  ? 0.4836 0.6175 0.4230 0.0594  -0.0321 -0.0859 801  ALA A CB  
5873  N N   . GLY A 804  ? 0.4649 0.5831 0.4198 0.0615  -0.0397 -0.1049 802  GLY A N   
5874  C CA  . GLY A 804  ? 0.3911 0.4967 0.3529 0.0599  -0.0419 -0.1062 802  GLY A CA  
5875  C C   . GLY A 804  ? 0.3962 0.4897 0.3596 0.0569  -0.0398 -0.0989 802  GLY A C   
5876  O O   . GLY A 804  ? 0.4131 0.4982 0.3798 0.0547  -0.0408 -0.0964 802  GLY A O   
5877  N N   . ARG A 805  ? 0.3858 0.4785 0.3473 0.0566  -0.0370 -0.0956 803  ARG A N   
5878  C CA  . ARG A 805  ? 0.3978 0.4798 0.3606 0.0538  -0.0348 -0.0890 803  ARG A CA  
5879  C C   . ARG A 805  ? 0.3211 0.3985 0.2873 0.0543  -0.0346 -0.0916 803  ARG A C   
5880  O O   . ARG A 805  ? 0.3123 0.3965 0.2783 0.0569  -0.0351 -0.0973 803  ARG A O   
5881  C CB  . ARG A 805  ? 0.4003 0.4853 0.3572 0.0525  -0.0314 -0.0806 803  ARG A CB  
5882  C CG  . ARG A 805  ? 0.3834 0.4722 0.3374 0.0518  -0.0317 -0.0770 803  ARG A CG  
5883  C CD  . ARG A 805  ? 0.4341 0.5140 0.3927 0.0500  -0.0336 -0.0769 803  ARG A CD  
5884  N NE  . ARG A 805  ? 0.4040 0.4874 0.3601 0.0494  -0.0340 -0.0736 803  ARG A NE  
5885  C CZ  . ARG A 805  ? 0.4692 0.5572 0.4259 0.0505  -0.0367 -0.0779 803  ARG A CZ  
5886  N NH1 . ARG A 805  ? 0.4489 0.5386 0.4088 0.0524  -0.0394 -0.0860 803  ARG A NH1 
5887  N NH2 . ARG A 805  ? 0.5287 0.6197 0.4832 0.0498  -0.0368 -0.0740 803  ARG A NH2 
5888  N N   . PRO A 806  ? 0.3461 0.4125 0.3158 0.0520  -0.0339 -0.0879 804  PRO A N   
5889  C CA  . PRO A 806  ? 0.3267 0.3883 0.3002 0.0523  -0.0339 -0.0903 804  PRO A CA  
5890  C C   . PRO A 806  ? 0.3412 0.4092 0.3102 0.0536  -0.0311 -0.0890 804  PRO A C   
5891  O O   . PRO A 806  ? 0.3161 0.3881 0.2795 0.0529  -0.0283 -0.0832 804  PRO A O   
5892  C CB  . PRO A 806  ? 0.3384 0.3883 0.3149 0.0491  -0.0331 -0.0846 804  PRO A CB  
5893  C CG  . PRO A 806  ? 0.3846 0.4323 0.3617 0.0476  -0.0343 -0.0827 804  PRO A CG  
5894  C CD  . PRO A 806  ? 0.3625 0.4204 0.3337 0.0490  -0.0335 -0.0822 804  PRO A CD  
5895  N N   . ILE A 807  ? 0.2688 0.3376 0.2408 0.0554  -0.0320 -0.0945 805  ILE A N   
5896  C CA  . ILE A 807  ? 0.2806 0.3549 0.2493 0.0566  -0.0295 -0.0939 805  ILE A CA  
5897  C C   . ILE A 807  ? 0.2950 0.3607 0.2637 0.0540  -0.0269 -0.0868 805  ILE A C   
5898  O O   . ILE A 807  ? 0.2885 0.3445 0.2625 0.0527  -0.0280 -0.0870 805  ILE A O   
5899  C CB  . ILE A 807  ? 0.2866 0.3639 0.2594 0.0595  -0.0316 -0.1024 805  ILE A CB  
5900  C CG1 . ILE A 807  ? 0.3284 0.4145 0.3017 0.0622  -0.0344 -0.1102 805  ILE A CG1 
5901  C CG2 . ILE A 807  ? 0.3044 0.3875 0.2739 0.0607  -0.0288 -0.1016 805  ILE A CG2 
5902  C CD1 . ILE A 807  ? 0.3502 0.4494 0.3159 0.0635  -0.0327 -0.1090 805  ILE A CD1 
5903  N N   . PRO A 808  ? 0.2855 0.3545 0.2487 0.0531  -0.0237 -0.0804 806  PRO A N   
5904  C CA  . PRO A 808  ? 0.2738 0.3347 0.2372 0.0507  -0.0213 -0.0739 806  PRO A CA  
5905  C C   . PRO A 808  ? 0.2641 0.3215 0.2310 0.0513  -0.0213 -0.0765 806  PRO A C   
5906  O O   . PRO A 808  ? 0.2792 0.3435 0.2454 0.0537  -0.0213 -0.0809 806  PRO A O   
5907  C CB  . PRO A 808  ? 0.2771 0.3447 0.2344 0.0503  -0.0183 -0.0679 806  PRO A CB  
5908  C CG  . PRO A 808  ? 0.3094 0.3857 0.2635 0.0515  -0.0192 -0.0692 806  PRO A CG  
5909  C CD  . PRO A 808  ? 0.2814 0.3615 0.2384 0.0541  -0.0221 -0.0783 806  PRO A CD  
5910  N N   . LEU A 809  ? 0.2754 0.3222 0.2459 0.0491  -0.0213 -0.0737 807  LEU A N   
5911  C CA  . LEU A 809  ? 0.2599 0.3021 0.2341 0.0492  -0.0213 -0.0751 807  LEU A CA  
5912  C C   . LEU A 809  ? 0.2732 0.3093 0.2460 0.0466  -0.0186 -0.0678 807  LEU A C   
5913  O O   . LEU A 809  ? 0.2686 0.2979 0.2423 0.0442  -0.0186 -0.0637 807  LEU A O   
5914  C CB  . LEU A 809  ? 0.2658 0.3008 0.2473 0.0490  -0.0248 -0.0795 807  LEU A CB  
5915  C CG  . LEU A 809  ? 0.2662 0.2947 0.2523 0.0485  -0.0250 -0.0798 807  LEU A CG  
5916  C CD1 . LEU A 809  ? 0.2655 0.3006 0.2514 0.0514  -0.0248 -0.0846 807  LEU A CD1 
5917  C CD2 . LEU A 809  ? 0.3198 0.3406 0.3135 0.0477  -0.0286 -0.0826 807  LEU A CD2 
5918  N N   . ILE A 810  ? 0.2404 0.2793 0.2111 0.0471  -0.0164 -0.0662 808  ILE A N   
5919  C CA  . ILE A 810  ? 0.2633 0.2957 0.2340 0.0450  -0.0144 -0.0607 808  ILE A CA  
5920  C C   . ILE A 810  ? 0.2707 0.2983 0.2467 0.0454  -0.0158 -0.0641 808  ILE A C   
5921  O O   . ILE A 810  ? 0.2672 0.2997 0.2440 0.0477  -0.0162 -0.0687 808  ILE A O   
5922  C CB  . ILE A 810  ? 0.2516 0.2899 0.2173 0.0451  -0.0112 -0.0564 808  ILE A CB  
5923  C CG1 . ILE A 810  ? 0.2702 0.3144 0.2312 0.0449  -0.0102 -0.0533 808  ILE A CG1 
5924  C CG2 . ILE A 810  ? 0.2611 0.2923 0.2272 0.0428  -0.0093 -0.0509 808  ILE A CG2 
5925  C CD1 . ILE A 810  ? 0.3179 0.3675 0.2747 0.0447  -0.0073 -0.0481 808  ILE A CD1 
5926  N N   . ALA A 811  ? 0.2452 0.2636 0.2251 0.0432  -0.0166 -0.0619 809  ALA A N   
5927  C CA  . ALA A 811  ? 0.2545 0.2675 0.2402 0.0432  -0.0184 -0.0646 809  ALA A CA  
5928  C C   . ALA A 811  ? 0.2696 0.2761 0.2553 0.0406  -0.0166 -0.0587 809  ALA A C   
5929  O O   . ALA A 811  ? 0.2598 0.2606 0.2464 0.0382  -0.0166 -0.0549 809  ALA A O   
5930  C CB  . ALA A 811  ? 0.2783 0.2870 0.2698 0.0430  -0.0220 -0.0683 809  ALA A CB  
5931  N N   . GLU A 812  ? 0.2351 0.2431 0.2199 0.0413  -0.0149 -0.0580 810  GLU A N   
5932  C CA  . GLU A 812  ? 0.2510 0.2538 0.2356 0.0391  -0.0131 -0.0528 810  GLU A CA  
5933  C C   . GLU A 812  ? 0.2411 0.2392 0.2316 0.0392  -0.0150 -0.0551 810  GLU A C   
5934  O O   . GLU A 812  ? 0.2396 0.2411 0.2317 0.0414  -0.0156 -0.0593 810  GLU A O   
5935  C CB  . GLU A 812  ? 0.2783 0.2862 0.2577 0.0395  -0.0099 -0.0497 810  GLU A CB  
5936  C CG  . GLU A 812  ? 0.2589 0.2714 0.2332 0.0393  -0.0084 -0.0469 810  GLU A CG  
5937  C CD  . GLU A 812  ? 0.3327 0.3396 0.3070 0.0368  -0.0083 -0.0428 810  GLU A CD  
5938  O OE1 . GLU A 812  ? 0.3235 0.3267 0.2970 0.0349  -0.0065 -0.0380 810  GLU A OE1 
5939  O OE2 . GLU A 812  ? 0.3299 0.3363 0.3052 0.0367  -0.0100 -0.0445 810  GLU A OE2 
5940  N N   . THR A 813  ? 0.2441 0.2348 0.2381 0.0367  -0.0161 -0.0524 811  THR A N   
5941  C CA  . THR A 813  ? 0.2490 0.2350 0.2499 0.0367  -0.0189 -0.0549 811  THR A CA  
5942  C C   . THR A 813  ? 0.2609 0.2413 0.2632 0.0343  -0.0180 -0.0502 811  THR A C   
5943  O O   . THR A 813  ? 0.2751 0.2565 0.2730 0.0336  -0.0151 -0.0463 811  THR A O   
5944  C CB  . THR A 813  ? 0.2544 0.2376 0.2599 0.0362  -0.0222 -0.0574 811  THR A CB  
5945  O OG1 . THR A 813  ? 0.2915 0.2724 0.2949 0.0338  -0.0213 -0.0530 811  THR A OG1 
5946  C CG2 . THR A 813  ? 0.2467 0.2361 0.2517 0.0392  -0.0235 -0.0635 811  THR A CG2 
5947  N N   . GLY A 814  ? 0.2618 0.2367 0.2706 0.0332  -0.0207 -0.0504 812  GLY A N   
5948  C CA  . GLY A 814  ? 0.2538 0.2244 0.2646 0.0314  -0.0203 -0.0468 812  GLY A CA  
5949  C C   . GLY A 814  ? 0.2784 0.2460 0.2867 0.0283  -0.0185 -0.0406 812  GLY A C   
5950  O O   . GLY A 814  ? 0.2829 0.2511 0.2883 0.0273  -0.0177 -0.0389 812  GLY A O   
5951  N N   . GLY A 815  ? 0.2661 0.2307 0.2756 0.0267  -0.0179 -0.0372 813  GLY A N   
5952  C CA  . GLY A 815  ? 0.2582 0.2203 0.2658 0.0238  -0.0164 -0.0317 813  GLY A CA  
5953  C C   . GLY A 815  ? 0.2482 0.2058 0.2615 0.0217  -0.0184 -0.0293 813  GLY A C   
5954  O O   . GLY A 815  ? 0.3048 0.2608 0.3232 0.0226  -0.0207 -0.0316 813  GLY A O   
5955  N N   . GLN A 816  ? 0.2391 0.1950 0.2515 0.0189  -0.0176 -0.0247 814  GLN A N   
5956  C CA  . GLN A 816  ? 0.2587 0.2114 0.2752 0.0164  -0.0189 -0.0212 814  GLN A CA  
5957  C C   . GLN A 816  ? 0.2418 0.1953 0.2533 0.0147  -0.0158 -0.0169 814  GLN A C   
5958  O O   . GLN A 816  ? 0.2705 0.2237 0.2816 0.0123  -0.0154 -0.0136 814  GLN A O   
5959  C CB  . GLN A 816  ? 0.2652 0.2156 0.2869 0.0145  -0.0218 -0.0201 814  GLN A CB  
5960  C CG  . GLN A 816  ? 0.3037 0.2512 0.3308 0.0120  -0.0237 -0.0165 814  GLN A CG  
5961  C CD  . GLN A 816  ? 0.3515 0.2970 0.3843 0.0134  -0.0262 -0.0189 814  GLN A CD  
5962  O OE1 . GLN A 816  ? 0.3144 0.2605 0.3453 0.0147  -0.0248 -0.0195 814  GLN A OE1 
5963  N NE2 . GLN A 816  ? 0.3441 0.2872 0.3844 0.0133  -0.0301 -0.0204 814  GLN A NE2 
5964  N N   . ASN A 817  ? 0.2284 0.1834 0.2365 0.0160  -0.0136 -0.0171 815  ASN A N   
5965  C CA  . ASN A 817  ? 0.2110 0.1677 0.2137 0.0152  -0.0104 -0.0144 815  ASN A CA  
5966  C C   . ASN A 817  ? 0.2236 0.1787 0.2271 0.0127  -0.0101 -0.0103 815  ASN A C   
5967  O O   . ASN A 817  ? 0.2379 0.1916 0.2447 0.0125  -0.0112 -0.0098 815  ASN A O   
5968  C CB  . ASN A 817  ? 0.2234 0.1824 0.2225 0.0175  -0.0084 -0.0162 815  ASN A CB  
5969  C CG  . ASN A 817  ? 0.2297 0.1911 0.2284 0.0201  -0.0091 -0.0204 815  ASN A CG  
5970  O OD1 . ASN A 817  ? 0.2049 0.1674 0.2022 0.0201  -0.0092 -0.0211 815  ASN A OD1 
5971  N ND2 . ASN A 817  ? 0.2313 0.1939 0.2312 0.0222  -0.0096 -0.0234 815  ASN A ND2 
5972  N N   . ALA A 818  ? 0.2161 0.1722 0.2170 0.0109  -0.0085 -0.0076 816  ALA A N   
5973  C CA  . ALA A 818  ? 0.2330 0.1889 0.2342 0.0085  -0.0081 -0.0038 816  ALA A CA  
5974  C C   . ALA A 818  ? 0.2150 0.1725 0.2116 0.0086  -0.0051 -0.0027 816  ALA A C   
5975  O O   . ALA A 818  ? 0.2148 0.1737 0.2079 0.0100  -0.0034 -0.0040 816  ALA A O   
5976  C CB  . ALA A 818  ? 0.2075 0.1640 0.2097 0.0062  -0.0086 -0.0017 816  ALA A CB  
5977  N N   . MET A 819  ? 0.2253 0.1827 0.2223 0.0071  -0.0048 -0.0002 817  MET A N   
5978  C CA  . MET A 819  ? 0.2189 0.1781 0.2124 0.0066  -0.0023 0.0012  817  MET A CA  
5979  C C   . MET A 819  ? 0.2253 0.1856 0.2196 0.0039  -0.0025 0.0043  817  MET A C   
5980  O O   . MET A 819  ? 0.2324 0.1920 0.2299 0.0025  -0.0042 0.0061  817  MET A O   
5981  C CB  . MET A 819  ? 0.2399 0.1986 0.2328 0.0076  -0.0016 0.0011  817  MET A CB  
5982  C CG  . MET A 819  ? 0.2518 0.2121 0.2417 0.0071  0.0007  0.0024  817  MET A CG  
5983  S SD  . MET A 819  ? 0.2787 0.2385 0.2688 0.0078  0.0012  0.0028  817  MET A SD  
5984  C CE  . MET A 819  ? 0.2939 0.2539 0.2828 0.0108  0.0018  -0.0001 817  MET A CE  
5985  N N   . ILE A 820  ? 0.2044 0.1669 0.1960 0.0032  -0.0009 0.0048  818  ILE A N   
5986  C CA  . ILE A 820  ? 0.2198 0.1848 0.2116 0.0008  -0.0007 0.0073  818  ILE A CA  
5987  C C   . ILE A 820  ? 0.1996 0.1660 0.1893 0.0007  0.0011  0.0078  818  ILE A C   
5988  O O   . ILE A 820  ? 0.2166 0.1830 0.2038 0.0022  0.0027  0.0063  818  ILE A O   
5989  C CB  . ILE A 820  ? 0.2219 0.1890 0.2129 0.0001  -0.0003 0.0071  818  ILE A CB  
5990  C CG1 . ILE A 820  ? 0.2214 0.1871 0.2152 0.0000  -0.0023 0.0067  818  ILE A CG1 
5991  C CG2 . ILE A 820  ? 0.2588 0.2297 0.2498 -0.0022 0.0002  0.0093  818  ILE A CG2 
5992  C CD1 . ILE A 820  ? 0.2217 0.1894 0.2150 -0.0006 -0.0020 0.0065  818  ILE A CD1 
5993  N N   . VAL A 821  ? 0.2111 0.1788 0.2019 -0.0011 0.0006  0.0101  819  VAL A N   
5994  C CA  . VAL A 821  ? 0.2272 0.1965 0.2163 -0.0014 0.0019  0.0106  819  VAL A CA  
5995  C C   . VAL A 821  ? 0.2320 0.2056 0.2209 -0.0037 0.0021  0.0125  819  VAL A C   
5996  O O   . VAL A 821  ? 0.2537 0.2286 0.2448 -0.0056 0.0006  0.0149  819  VAL A O   
5997  C CB  . VAL A 821  ? 0.2526 0.2199 0.2433 -0.0012 0.0010  0.0116  819  VAL A CB  
5998  C CG1 . VAL A 821  ? 0.2508 0.2199 0.2399 -0.0016 0.0023  0.0121  819  VAL A CG1 
5999  C CG2 . VAL A 821  ? 0.2431 0.2070 0.2342 0.0011  0.0007  0.0095  819  VAL A CG2 
6000  N N   . ASP A 822  ? 0.2404 0.2167 0.2271 -0.0035 0.0038  0.0114  820  ASP A N   
6001  C CA  . ASP A 822  ? 0.2641 0.2455 0.2504 -0.0055 0.0041  0.0126  820  ASP A CA  
6002  C C   . ASP A 822  ? 0.2425 0.2257 0.2281 -0.0061 0.0046  0.0132  820  ASP A C   
6003  O O   . ASP A 822  ? 0.2462 0.2264 0.2318 -0.0049 0.0047  0.0128  820  ASP A O   
6004  C CB  . ASP A 822  ? 0.2817 0.2660 0.2668 -0.0053 0.0052  0.0108  820  ASP A CB  
6005  C CG  . ASP A 822  ? 0.2804 0.2644 0.2638 -0.0036 0.0068  0.0081  820  ASP A CG  
6006  O OD1 . ASP A 822  ? 0.2835 0.2660 0.2666 -0.0029 0.0072  0.0078  820  ASP A OD1 
6007  O OD2 . ASP A 822  ? 0.2866 0.2721 0.2697 -0.0031 0.0075  0.0063  820  ASP A OD2 
6008  N N   . SER A 823  ? 0.2648 0.2537 0.2499 -0.0078 0.0049  0.0141  821  SER A N   
6009  C CA  . SER A 823  ? 0.2799 0.2713 0.2644 -0.0085 0.0052  0.0148  821  SER A CA  
6010  C C   . SER A 823  ? 0.2792 0.2701 0.2623 -0.0069 0.0066  0.0117  821  SER A C   
6011  O O   . SER A 823  ? 0.3270 0.3197 0.3098 -0.0073 0.0068  0.0119  821  SER A O   
6012  C CB  . SER A 823  ? 0.2775 0.2761 0.2620 -0.0110 0.0049  0.0166  821  SER A CB  
6013  O OG  . SER A 823  ? 0.3354 0.3379 0.3188 -0.0108 0.0060  0.0145  821  SER A OG  
6014  N N   . SER A 824  ? 0.2708 0.2595 0.2534 -0.0051 0.0075  0.0092  822  SER A N   
6015  C CA  . SER A 824  ? 0.2763 0.2640 0.2584 -0.0036 0.0086  0.0067  822  SER A CA  
6016  C C   . SER A 824  ? 0.2903 0.2727 0.2727 -0.0021 0.0086  0.0068  822  SER A C   
6017  O O   . SER A 824  ? 0.2790 0.2604 0.2614 -0.0011 0.0092  0.0055  822  SER A O   
6018  C CB  . SER A 824  ? 0.2956 0.2840 0.2777 -0.0025 0.0093  0.0042  822  SER A CB  
6019  O OG  . SER A 824  ? 0.2791 0.2632 0.2612 -0.0013 0.0092  0.0042  822  SER A OG  
6020  N N   . ALA A 825  ? 0.2705 0.2497 0.2534 -0.0019 0.0077  0.0083  823  ALA A N   
6021  C CA  . ALA A 825  ? 0.2655 0.2405 0.2486 -0.0003 0.0078  0.0081  823  ALA A CA  
6022  C C   . ALA A 825  ? 0.2916 0.2666 0.2752 -0.0007 0.0076  0.0092  823  ALA A C   
6023  O O   . ALA A 825  ? 0.3075 0.2851 0.2914 -0.0024 0.0070  0.0107  823  ALA A O   
6024  C CB  . ALA A 825  ? 0.2740 0.2463 0.2579 0.0001  0.0067  0.0088  823  ALA A CB  
6025  N N   . LEU A 826  ? 0.2790 0.2516 0.2626 0.0008  0.0082  0.0085  824  LEU A N   
6026  C CA  . LEU A 826  ? 0.3094 0.2815 0.2936 0.0006  0.0080  0.0094  824  LEU A CA  
6027  C C   . LEU A 826  ? 0.3133 0.2831 0.2987 0.0008  0.0069  0.0107  824  LEU A C   
6028  O O   . LEU A 826  ? 0.2989 0.2664 0.2846 0.0023  0.0069  0.0100  824  LEU A O   
6029  C CB  . LEU A 826  ? 0.3531 0.3240 0.3374 0.0020  0.0091  0.0083  824  LEU A CB  
6030  N N   . ALA A 827  ? 0.2964 0.2673 0.2829 -0.0007 0.0058  0.0126  825  ALA A N   
6031  C CA  . ALA A 827  ? 0.2760 0.2448 0.2646 -0.0007 0.0042  0.0139  825  ALA A CA  
6032  C C   . ALA A 827  ? 0.2900 0.2560 0.2793 0.0013  0.0044  0.0128  825  ALA A C   
6033  O O   . ALA A 827  ? 0.2705 0.2343 0.2611 0.0024  0.0037  0.0121  825  ALA A O   
6034  C CB  . ALA A 827  ? 0.3362 0.3069 0.3262 -0.0027 0.0029  0.0165  825  ALA A CB  
6035  N N   . GLU A 828  ? 0.2944 0.2607 0.2833 0.0018  0.0054  0.0125  826  GLU A N   
6036  C CA  . GLU A 828  ? 0.3014 0.2659 0.2910 0.0036  0.0057  0.0118  826  GLU A CA  
6037  C C   . GLU A 828  ? 0.2898 0.2533 0.2785 0.0054  0.0065  0.0100  826  GLU A C   
6038  O O   . GLU A 828  ? 0.2951 0.2575 0.2847 0.0069  0.0062  0.0091  826  GLU A O   
6039  C CB  . GLU A 828  ? 0.3469 0.3122 0.3362 0.0037  0.0067  0.0120  826  GLU A CB  
6040  C CG  . GLU A 828  ? 0.3850 0.3514 0.3755 0.0022  0.0058  0.0136  826  GLU A CG  
6041  C CD  . GLU A 828  ? 0.4879 0.4570 0.4775 0.0002  0.0055  0.0146  826  GLU A CD  
6042  O OE1 . GLU A 828  ? 0.4443 0.4146 0.4324 0.0000  0.0062  0.0136  826  GLU A OE1 
6043  O OE2 . GLU A 828  ? 0.5554 0.5260 0.5460 -0.0012 0.0045  0.0163  826  GLU A OE2 
6044  N N   . GLN A 829  ? 0.2950 0.2593 0.2819 0.0054  0.0075  0.0094  827  GLN A N   
6045  C CA  . GLN A 829  ? 0.2865 0.2503 0.2724 0.0069  0.0082  0.0080  827  GLN A CA  
6046  C C   . GLN A 829  ? 0.2790 0.2418 0.2655 0.0072  0.0070  0.0074  827  GLN A C   
6047  O O   . GLN A 829  ? 0.2850 0.2472 0.2716 0.0088  0.0069  0.0061  827  GLN A O   
6048  C CB  . GLN A 829  ? 0.3083 0.2733 0.2929 0.0065  0.0092  0.0077  827  GLN A CB  
6049  C CG  . GLN A 829  ? 0.3877 0.3525 0.3713 0.0080  0.0099  0.0068  827  GLN A CG  
6050  C CD  . GLN A 829  ? 0.4428 0.4084 0.4259 0.0077  0.0107  0.0066  827  GLN A CD  
6051  O OE1 . GLN A 829  ? 0.4332 0.3998 0.4164 0.0064  0.0105  0.0064  827  GLN A OE1 
6052  N NE2 . GLN A 829  ? 0.5129 0.4788 0.4960 0.0089  0.0115  0.0066  827  GLN A NE2 
6053  N N   . VAL A 830  ? 0.2436 0.2067 0.2306 0.0056  0.0060  0.0082  828  VAL A N   
6054  C CA  . VAL A 830  ? 0.2605 0.2225 0.2489 0.0056  0.0045  0.0079  828  VAL A CA  
6055  C C   . VAL A 830  ? 0.2600 0.2204 0.2509 0.0066  0.0032  0.0074  828  VAL A C   
6056  O O   . VAL A 830  ? 0.2387 0.1982 0.2305 0.0080  0.0026  0.0057  828  VAL A O   
6057  C CB  . VAL A 830  ? 0.2599 0.2230 0.2490 0.0033  0.0035  0.0096  828  VAL A CB  
6058  C CG1 . VAL A 830  ? 0.2650 0.2267 0.2566 0.0031  0.0015  0.0097  828  VAL A CG1 
6059  C CG2 . VAL A 830  ? 0.2948 0.2599 0.2817 0.0027  0.0047  0.0092  828  VAL A CG2 
6060  N N   . VAL A 831  ? 0.2374 0.1977 0.2299 0.0059  0.0027  0.0088  829  VAL A N   
6061  C CA  . VAL A 831  ? 0.2289 0.1876 0.2245 0.0067  0.0011  0.0084  829  VAL A CA  
6062  C C   . VAL A 831  ? 0.2450 0.2036 0.2401 0.0093  0.0019  0.0059  829  VAL A C   
6063  O O   . VAL A 831  ? 0.2509 0.2087 0.2482 0.0107  0.0007  0.0040  829  VAL A O   
6064  C CB  . VAL A 831  ? 0.2536 0.2123 0.2510 0.0055  0.0003  0.0105  829  VAL A CB  
6065  C CG1 . VAL A 831  ? 0.2671 0.2242 0.2682 0.0068  -0.0012 0.0097  829  VAL A CG1 
6066  C CG2 . VAL A 831  ? 0.2956 0.2551 0.2940 0.0029  -0.0010 0.0131  829  VAL A CG2 
6067  N N   . GLY A 832  ? 0.2535 0.2135 0.2461 0.0099  0.0040  0.0058  830  GLY A N   
6068  C CA  . GLY A 832  ? 0.2381 0.1992 0.2301 0.0122  0.0049  0.0040  830  GLY A CA  
6069  C C   . GLY A 832  ? 0.2342 0.1957 0.2253 0.0135  0.0048  0.0020  830  GLY A C   
6070  O O   . GLY A 832  ? 0.2516 0.2137 0.2438 0.0153  0.0043  -0.0002 830  GLY A O   
6071  N N   . ASP A 833  ? 0.2474 0.2089 0.2366 0.0125  0.0052  0.0025  831  ASP A N   
6072  C CA  . ASP A 833  ? 0.2603 0.2223 0.2486 0.0136  0.0051  0.0007  831  ASP A CA  
6073  C C   . ASP A 833  ? 0.2330 0.1935 0.2240 0.0138  0.0029  -0.0007 831  ASP A C   
6074  O O   . ASP A 833  ? 0.2320 0.1932 0.2231 0.0154  0.0024  -0.0031 831  ASP A O   
6075  C CB  . ASP A 833  ? 0.2419 0.2043 0.2280 0.0125  0.0060  0.0017  831  ASP A CB  
6076  C CG  . ASP A 833  ? 0.2743 0.2382 0.2584 0.0127  0.0079  0.0026  831  ASP A CG  
6077  O OD1 . ASP A 833  ? 0.3115 0.2766 0.2954 0.0140  0.0086  0.0024  831  ASP A OD1 
6078  O OD2 . ASP A 833  ? 0.2810 0.2450 0.2640 0.0117  0.0085  0.0035  831  ASP A OD2 
6079  N N   . VAL A 834  ? 0.2188 0.1775 0.2124 0.0121  0.0014  0.0008  832  VAL A N   
6080  C CA  . VAL A 834  ? 0.2197 0.1766 0.2170 0.0121  -0.0011 -0.0001 832  VAL A CA  
6081  C C   . VAL A 834  ? 0.2469 0.2035 0.2472 0.0141  -0.0023 -0.0024 832  VAL A C   
6082  O O   . VAL A 834  ? 0.2478 0.2041 0.2502 0.0155  -0.0037 -0.0052 832  VAL A O   
6083  C CB  . VAL A 834  ? 0.2338 0.1895 0.2332 0.0095  -0.0025 0.0028  832  VAL A CB  
6084  C CG1 . VAL A 834  ? 0.2483 0.2019 0.2529 0.0093  -0.0055 0.0025  832  VAL A CG1 
6085  C CG2 . VAL A 834  ? 0.2322 0.1889 0.2292 0.0078  -0.0017 0.0043  832  VAL A CG2 
6086  N N   . ILE A 835  ? 0.2364 0.1933 0.2371 0.0142  -0.0017 -0.0015 833  ILE A N   
6087  C CA  . ILE A 835  ? 0.2441 0.2012 0.2478 0.0162  -0.0027 -0.0038 833  ILE A CA  
6088  C C   . ILE A 835  ? 0.2612 0.2209 0.2631 0.0188  -0.0016 -0.0072 833  ILE A C   
6089  O O   . ILE A 835  ? 0.2719 0.2318 0.2766 0.0206  -0.0032 -0.0105 833  ILE A O   
6090  C CB  . ILE A 835  ? 0.2530 0.2104 0.2570 0.0158  -0.0019 -0.0021 833  ILE A CB  
6091  C CG1 . ILE A 835  ? 0.3006 0.2558 0.3073 0.0134  -0.0035 0.0009  833  ILE A CG1 
6092  C CG2 . ILE A 835  ? 0.3090 0.2676 0.3152 0.0183  -0.0022 -0.0050 833  ILE A CG2 
6093  C CD1 . ILE A 835  ? 0.3472 0.3002 0.3598 0.0138  -0.0066 0.0002  833  ILE A CD1 
6094  N N   . THR A 836  ? 0.2390 0.2010 0.2364 0.0189  0.0008  -0.0065 834  THR A N   
6095  C CA  . THR A 836  ? 0.2589 0.2244 0.2543 0.0212  0.0019  -0.0091 834  THR A CA  
6096  C C   . THR A 836  ? 0.2430 0.2083 0.2388 0.0218  0.0006  -0.0114 834  THR A C   
6097  O O   . THR A 836  ? 0.2799 0.2470 0.2771 0.0239  -0.0003 -0.0149 834  THR A O   
6098  C CB  . THR A 836  ? 0.3050 0.2727 0.2961 0.0208  0.0045  -0.0071 834  THR A CB  
6099  O OG1 . THR A 836  ? 0.3626 0.3309 0.3538 0.0205  0.0056  -0.0054 834  THR A OG1 
6100  C CG2 . THR A 836  ? 0.3472 0.3192 0.3362 0.0229  0.0056  -0.0091 834  THR A CG2 
6101  N N   . SER A 837  ? 0.2304 0.1936 0.2252 0.0199  0.0004  -0.0096 835  SER A N   
6102  C CA  . SER A 837  ? 0.2360 0.1993 0.2308 0.0204  -0.0007 -0.0115 835  SER A CA  
6103  C C   . SER A 837  ? 0.2248 0.1861 0.2246 0.0210  -0.0036 -0.0140 835  SER A C   
6104  O O   . SER A 837  ? 0.2417 0.2041 0.2423 0.0226  -0.0047 -0.0172 835  SER A O   
6105  C CB  . SER A 837  ? 0.2272 0.1891 0.2202 0.0182  -0.0003 -0.0089 835  SER A CB  
6106  O OG  . SER A 837  ? 0.2464 0.2101 0.2355 0.0179  0.0022  -0.0072 835  SER A OG  
6107  N N   . ALA A 838  ? 0.2233 0.1818 0.2269 0.0198  -0.0052 -0.0125 836  ALA A N   
6108  C CA  . ALA A 838  ? 0.2301 0.1862 0.2395 0.0200  -0.0084 -0.0143 836  ALA A CA  
6109  C C   . ALA A 838  ? 0.2754 0.2325 0.2881 0.0226  -0.0096 -0.0180 836  ALA A C   
6110  O O   . ALA A 838  ? 0.2517 0.2083 0.2686 0.0240  -0.0120 -0.0215 836  ALA A O   
6111  C CB  . ALA A 838  ? 0.2499 0.2027 0.2625 0.0173  -0.0100 -0.0106 836  ALA A CB  
6112  N N   . PHE A 839  ? 0.2550 0.2138 0.2665 0.0233  -0.0080 -0.0176 837  PHE A N   
6113  C CA  . PHE A 839  ? 0.2633 0.2229 0.2789 0.0255  -0.0093 -0.0208 837  PHE A CA  
6114  C C   . PHE A 839  ? 0.2754 0.2401 0.2880 0.0281  -0.0072 -0.0237 837  PHE A C   
6115  O O   . PHE A 839  ? 0.2755 0.2418 0.2917 0.0304  -0.0084 -0.0274 837  PHE A O   
6116  C CB  . PHE A 839  ? 0.2718 0.2288 0.2906 0.0241  -0.0101 -0.0179 837  PHE A CB  
6117  C CG  . PHE A 839  ? 0.2378 0.1906 0.2598 0.0214  -0.0123 -0.0147 837  PHE A CG  
6118  C CD1 . PHE A 839  ? 0.2673 0.2177 0.2948 0.0215  -0.0156 -0.0164 837  PHE A CD1 
6119  C CD2 . PHE A 839  ? 0.2760 0.2278 0.2958 0.0186  -0.0112 -0.0099 837  PHE A CD2 
6120  C CE1 . PHE A 839  ? 0.2569 0.2041 0.2878 0.0188  -0.0177 -0.0129 837  PHE A CE1 
6121  C CE2 . PHE A 839  ? 0.2852 0.2343 0.3078 0.0160  -0.0132 -0.0066 837  PHE A CE2 
6122  C CZ  . PHE A 839  ? 0.2772 0.2240 0.3054 0.0160  -0.0164 -0.0078 837  PHE A CZ  
6123  N N   . ASP A 840  ? 0.2888 0.2564 0.2955 0.0279  -0.0043 -0.0221 838  ASP A N   
6124  C CA  . ASP A 840  ? 0.2984 0.2719 0.3024 0.0304  -0.0025 -0.0247 838  ASP A CA  
6125  C C   . ASP A 840  ? 0.3076 0.2833 0.3138 0.0328  -0.0043 -0.0300 838  ASP A C   
6126  O O   . ASP A 840  ? 0.2799 0.2534 0.2873 0.0324  -0.0060 -0.0310 838  ASP A O   
6127  C CB  . ASP A 840  ? 0.3270 0.3028 0.3250 0.0295  0.0002  -0.0219 838  ASP A CB  
6128  C CG  . ASP A 840  ? 0.4142 0.3967 0.4092 0.0316  0.0022  -0.0235 838  ASP A CG  
6129  O OD1 . ASP A 840  ? 0.4027 0.3886 0.3969 0.0333  0.0018  -0.0268 838  ASP A OD1 
6130  O OD2 . ASP A 840  ? 0.4892 0.4738 0.4826 0.0314  0.0041  -0.0214 838  ASP A OD2 
6131  N N   . SER A 841  ? 0.2734 0.2539 0.2807 0.0355  -0.0041 -0.0337 839  SER A N   
6132  C CA  . SER A 841  ? 0.2868 0.2704 0.2967 0.0383  -0.0059 -0.0397 839  SER A CA  
6133  C C   . SER A 841  ? 0.2570 0.2352 0.2737 0.0381  -0.0097 -0.0419 839  SER A C   
6134  O O   . SER A 841  ? 0.2560 0.2350 0.2748 0.0395  -0.0117 -0.0460 839  SER A O   
6135  C CB  . SER A 841  ? 0.3225 0.3103 0.3277 0.0389  -0.0047 -0.0406 839  SER A CB  
6136  O OG  . SER A 841  ? 0.3703 0.3627 0.3698 0.0387  -0.0014 -0.0377 839  SER A OG  
6137  N N   . ALA A 842  ? 0.2582 0.2311 0.2785 0.0363  -0.0110 -0.0389 840  ALA A N   
6138  C CA  . ALA A 842  ? 0.2309 0.1983 0.2583 0.0356  -0.0148 -0.0397 840  ALA A CA  
6139  C C   . ALA A 842  ? 0.2292 0.1939 0.2560 0.0341  -0.0159 -0.0389 840  ALA A C   
6140  O O   . ALA A 842  ? 0.2626 0.2251 0.2950 0.0346  -0.0192 -0.0419 840  ALA A O   
6141  C CB  . ALA A 842  ? 0.2526 0.2213 0.2866 0.0386  -0.0176 -0.0459 840  ALA A CB  
6142  N N   . GLY A 843  ? 0.2388 0.2039 0.2595 0.0321  -0.0134 -0.0349 841  GLY A N   
6143  C CA  . GLY A 843  ? 0.2314 0.1945 0.2512 0.0307  -0.0141 -0.0339 841  GLY A CA  
6144  C C   . GLY A 843  ? 0.2374 0.2039 0.2565 0.0329  -0.0147 -0.0388 841  GLY A C   
6145  O O   . GLY A 843  ? 0.2520 0.2169 0.2715 0.0320  -0.0159 -0.0387 841  GLY A O   
6146  N N   . GLN A 844  ? 0.2254 0.1974 0.2436 0.0359  -0.0139 -0.0430 842  GLN A N   
6147  C CA  . GLN A 844  ? 0.2199 0.1962 0.2374 0.0383  -0.0145 -0.0481 842  GLN A CA  
6148  C C   . GLN A 844  ? 0.2625 0.2437 0.2722 0.0383  -0.0113 -0.0464 842  GLN A C   
6149  O O   . GLN A 844  ? 0.2723 0.2602 0.2793 0.0406  -0.0100 -0.0495 842  GLN A O   
6150  C CB  . GLN A 844  ? 0.2248 0.2050 0.2463 0.0417  -0.0159 -0.0542 842  GLN A CB  
6151  C CG  . GLN A 844  ? 0.2409 0.2158 0.2712 0.0417  -0.0198 -0.0562 842  GLN A CG  
6152  C CD  . GLN A 844  ? 0.2576 0.2358 0.2922 0.0448  -0.0209 -0.0614 842  GLN A CD  
6153  O OE1 . GLN A 844  ? 0.2449 0.2234 0.2857 0.0470  -0.0241 -0.0672 842  GLN A OE1 
6154  N NE2 . GLN A 844  ? 0.2838 0.2648 0.3155 0.0451  -0.0183 -0.0596 842  GLN A NE2 
6155  N N   . ARG A 845  ? 0.2501 0.2282 0.2566 0.0355  -0.0100 -0.0414 843  ARG A N   
6156  C CA  . ARG A 845  ? 0.2531 0.2345 0.2535 0.0352  -0.0077 -0.0395 843  ARG A CA  
6157  C C   . ARG A 845  ? 0.2431 0.2208 0.2444 0.0336  -0.0093 -0.0388 843  ARG A C   
6158  O O   . ARG A 845  ? 0.2586 0.2307 0.2634 0.0315  -0.0108 -0.0367 843  ARG A O   
6159  C CB  . ARG A 845  ? 0.2809 0.2619 0.2770 0.0332  -0.0047 -0.0340 843  ARG A CB  
6160  C CG  . ARG A 845  ? 0.2629 0.2477 0.2577 0.0344  -0.0028 -0.0337 843  ARG A CG  
6161  C CD  . ARG A 845  ? 0.3399 0.3237 0.3310 0.0323  -0.0002 -0.0282 843  ARG A CD  
6162  N NE  . ARG A 845  ? 0.4173 0.4054 0.4068 0.0333  0.0018  -0.0275 843  ARG A NE  
6163  C CZ  . ARG A 845  ? 0.4482 0.4422 0.4337 0.0342  0.0038  -0.0269 843  ARG A CZ  
6164  N NH1 . ARG A 845  ? 0.3983 0.3947 0.3809 0.0342  0.0042  -0.0267 843  ARG A NH1 
6165  N NH2 . ARG A 845  ? 0.5089 0.5069 0.4936 0.0349  0.0055  -0.0260 843  ARG A NH2 
6166  N N   . CYS A 846  ? 0.2222 0.2034 0.2205 0.0344  -0.0089 -0.0403 844  CYS A N   
6167  C CA  . CYS A 846  ? 0.2461 0.2240 0.2451 0.0329  -0.0103 -0.0395 844  CYS A CA  
6168  C C   . CYS A 846  ? 0.2198 0.1940 0.2167 0.0299  -0.0087 -0.0337 844  CYS A C   
6169  O O   . CYS A 846  ? 0.2337 0.2039 0.2328 0.0280  -0.0101 -0.0322 844  CYS A O   
6170  C CB  . CYS A 846  ? 0.2468 0.2297 0.2425 0.0344  -0.0099 -0.0418 844  CYS A CB  
6171  S SG  . CYS A 846  ? 0.2909 0.2799 0.2793 0.0348  -0.0061 -0.0390 844  CYS A SG  
6172  N N   . SER A 847  ? 0.2285 0.2043 0.2214 0.0294  -0.0060 -0.0305 845  SER A N   
6173  C CA  . SER A 847  ? 0.2044 0.1776 0.1951 0.0269  -0.0043 -0.0255 845  SER A CA  
6174  C C   . SER A 847  ? 0.2169 0.1858 0.2106 0.0251  -0.0049 -0.0232 845  SER A C   
6175  O O   . SER A 847  ? 0.2264 0.1934 0.2186 0.0230  -0.0036 -0.0194 845  SER A O   
6176  C CB  . SER A 847  ? 0.2173 0.1943 0.2033 0.0273  -0.0014 -0.0234 845  SER A CB  
6177  O OG  . SER A 847  ? 0.2507 0.2300 0.2372 0.0288  -0.0009 -0.0247 845  SER A OG  
6178  N N   . ALA A 848  ? 0.2355 0.2031 0.2336 0.0260  -0.0068 -0.0255 846  ALA A N   
6179  C CA  . ALA A 848  ? 0.2164 0.1807 0.2172 0.0245  -0.0072 -0.0231 846  ALA A CA  
6180  C C   . ALA A 848  ? 0.2177 0.1780 0.2202 0.0216  -0.0082 -0.0197 846  ALA A C   
6181  O O   . ALA A 848  ? 0.2284 0.1875 0.2324 0.0210  -0.0098 -0.0203 846  ALA A O   
6182  C CB  . ALA A 848  ? 0.2370 0.2007 0.2432 0.0261  -0.0095 -0.0264 846  ALA A CB  
6183  N N   . LEU A 849  ? 0.2355 0.1943 0.2377 0.0198  -0.0073 -0.0161 847  LEU A N   
6184  C CA  . LEU A 849  ? 0.2086 0.1647 0.2123 0.0169  -0.0081 -0.0126 847  LEU A CA  
6185  C C   . LEU A 849  ? 0.2154 0.1686 0.2255 0.0164  -0.0115 -0.0132 847  LEU A C   
6186  O O   . LEU A 849  ? 0.2507 0.2029 0.2642 0.0171  -0.0126 -0.0139 847  LEU A O   
6187  C CB  . LEU A 849  ? 0.2348 0.1908 0.2364 0.0154  -0.0063 -0.0091 847  LEU A CB  
6188  C CG  . LEU A 849  ? 0.2151 0.1694 0.2183 0.0124  -0.0071 -0.0054 847  LEU A CG  
6189  C CD1 . LEU A 849  ? 0.2314 0.1864 0.2325 0.0112  -0.0066 -0.0046 847  LEU A CD1 
6190  C CD2 . LEU A 849  ? 0.2513 0.2060 0.2526 0.0112  -0.0054 -0.0026 847  LEU A CD2 
6191  N N   . ARG A 850  ? 0.2087 0.1605 0.2210 0.0151  -0.0132 -0.0127 848  ARG A N   
6192  C CA  . ARG A 850  ? 0.2498 0.1989 0.2691 0.0143  -0.0168 -0.0128 848  ARG A CA  
6193  C C   . ARG A 850  ? 0.2574 0.2050 0.2786 0.0109  -0.0175 -0.0077 848  ARG A C   
6194  O O   . ARG A 850  ? 0.2516 0.1969 0.2787 0.0098  -0.0203 -0.0064 848  ARG A O   
6195  C CB  . ARG A 850  ? 0.2360 0.1848 0.2575 0.0152  -0.0187 -0.0159 848  ARG A CB  
6196  C CG  . ARG A 850  ? 0.2549 0.2063 0.2740 0.0185  -0.0179 -0.0210 848  ARG A CG  
6197  C CD  . ARG A 850  ? 0.2854 0.2370 0.3072 0.0206  -0.0187 -0.0238 848  ARG A CD  
6198  N NE  . ARG A 850  ? 0.2616 0.2165 0.2818 0.0238  -0.0184 -0.0290 848  ARG A NE  
6199  C CZ  . ARG A 850  ? 0.2589 0.2159 0.2800 0.0263  -0.0183 -0.0323 848  ARG A CZ  
6200  N NH1 . ARG A 850  ? 0.2668 0.2222 0.2906 0.0261  -0.0187 -0.0311 848  ARG A NH1 
6201  N NH2 . ARG A 850  ? 0.2723 0.2334 0.2915 0.0291  -0.0178 -0.0369 848  ARG A NH2 
6202  N N   . VAL A 851  ? 0.2372 0.1865 0.2539 0.0092  -0.0153 -0.0050 849  VAL A N   
6203  C CA  . VAL A 851  ? 0.2539 0.2032 0.2720 0.0060  -0.0159 -0.0005 849  VAL A CA  
6204  C C   . VAL A 851  ? 0.2362 0.1878 0.2487 0.0050  -0.0127 0.0019  849  VAL A C   
6205  O O   . VAL A 851  ? 0.2465 0.1999 0.2543 0.0055  -0.0105 0.0011  849  VAL A O   
6206  C CB  . VAL A 851  ? 0.2904 0.2399 0.3098 0.0047  -0.0170 0.0000  849  VAL A CB  
6207  C CG1 . VAL A 851  ? 0.3283 0.2786 0.3495 0.0012  -0.0177 0.0050  849  VAL A CG1 
6208  C CG2 . VAL A 851  ? 0.3498 0.2970 0.3747 0.0059  -0.0202 -0.0031 849  VAL A CG2 
6209  N N   . LEU A 852  ? 0.2349 0.1865 0.2483 0.0036  -0.0127 0.0047  850  LEU A N   
6210  C CA  . LEU A 852  ? 0.2230 0.1769 0.2318 0.0025  -0.0101 0.0070  850  LEU A CA  
6211  C C   . LEU A 852  ? 0.2097 0.1656 0.2195 -0.0006 -0.0106 0.0108  850  LEU A C   
6212  O O   . LEU A 852  ? 0.2275 0.1828 0.2420 -0.0024 -0.0131 0.0134  850  LEU A O   
6213  C CB  . LEU A 852  ? 0.2229 0.1764 0.2323 0.0028  -0.0099 0.0077  850  LEU A CB  
6214  C CG  . LEU A 852  ? 0.2230 0.1789 0.2286 0.0016  -0.0077 0.0100  850  LEU A CG  
6215  C CD1 . LEU A 852  ? 0.2129 0.1702 0.2133 0.0030  -0.0048 0.0080  850  LEU A CD1 
6216  C CD2 . LEU A 852  ? 0.2200 0.1750 0.2272 0.0018  -0.0081 0.0109  850  LEU A CD2 
6217  N N   . CYS A 853  ? 0.2307 0.1894 0.2363 -0.0013 -0.0085 0.0113  851  CYS A N   
6218  C CA  . CYS A 853  ? 0.2388 0.2005 0.2447 -0.0040 -0.0086 0.0144  851  CYS A CA  
6219  C C   . CYS A 853  ? 0.2024 0.1674 0.2049 -0.0050 -0.0065 0.0160  851  CYS A C   
6220  O O   . CYS A 853  ? 0.2325 0.1985 0.2310 -0.0038 -0.0041 0.0141  851  CYS A O   
6221  C CB  . CYS A 853  ? 0.2586 0.2215 0.2632 -0.0039 -0.0081 0.0131  851  CYS A CB  
6222  S SG  . CYS A 853  ? 0.2831 0.2424 0.2909 -0.0022 -0.0102 0.0102  851  CYS A SG  
6223  N N   . LEU A 854  ? 0.2289 0.1956 0.2334 -0.0072 -0.0075 0.0195  852  LEU A N   
6224  C CA  . LEU A 854  ? 0.2330 0.2029 0.2349 -0.0082 -0.0059 0.0209  852  LEU A CA  
6225  C C   . LEU A 854  ? 0.2254 0.2007 0.2267 -0.0108 -0.0057 0.0236  852  LEU A C   
6226  O O   . LEU A 854  ? 0.2411 0.2177 0.2460 -0.0129 -0.0077 0.0268  852  LEU A O   
6227  C CB  . LEU A 854  ? 0.2279 0.1965 0.2325 -0.0086 -0.0074 0.0228  852  LEU A CB  
6228  C CG  . LEU A 854  ? 0.2149 0.1789 0.2202 -0.0060 -0.0077 0.0201  852  LEU A CG  
6229  C CD1 . LEU A 854  ? 0.2399 0.2031 0.2481 -0.0067 -0.0091 0.0224  852  LEU A CD1 
6230  C CD2 . LEU A 854  ? 0.2393 0.2033 0.2399 -0.0039 -0.0049 0.0170  852  LEU A CD2 
6231  N N   . GLN A 855  ? 0.2276 0.2064 0.2249 -0.0107 -0.0033 0.0224  853  GLN A N   
6232  C CA  . GLN A 855  ? 0.2374 0.2225 0.2340 -0.0131 -0.0029 0.0246  853  GLN A CA  
6233  C C   . GLN A 855  ? 0.2493 0.2373 0.2479 -0.0154 -0.0042 0.0287  853  GLN A C   
6234  O O   . GLN A 855  ? 0.2629 0.2492 0.2614 -0.0148 -0.0043 0.0288  853  GLN A O   
6235  C CB  . GLN A 855  ? 0.2409 0.2293 0.2335 -0.0122 -0.0003 0.0220  853  GLN A CB  
6236  C CG  . GLN A 855  ? 0.2413 0.2369 0.2332 -0.0143 0.0002  0.0234  853  GLN A CG  
6237  C CD  . GLN A 855  ? 0.2956 0.2948 0.2842 -0.0134 0.0025  0.0204  853  GLN A CD  
6238  O OE1 . GLN A 855  ? 0.3017 0.2978 0.2888 -0.0112 0.0037  0.0170  853  GLN A OE1 
6239  N NE2 . GLN A 855  ? 0.3537 0.3602 0.3415 -0.0152 0.0030  0.0217  853  GLN A NE2 
6240  N N   . GLU A 856  ? 0.2572 0.2498 0.2578 -0.0181 -0.0054 0.0323  854  GLU A N   
6241  C CA  . GLU A 856  ? 0.2976 0.2927 0.3013 -0.0206 -0.0073 0.0371  854  GLU A CA  
6242  C C   . GLU A 856  ? 0.3278 0.3261 0.3290 -0.0208 -0.0062 0.0374  854  GLU A C   
6243  O O   . GLU A 856  ? 0.3128 0.3096 0.3162 -0.0214 -0.0077 0.0398  854  GLU A O   
6244  C CB  . GLU A 856  ? 0.2914 0.2925 0.2971 -0.0236 -0.0083 0.0410  854  GLU A CB  
6245  C CG  . GLU A 856  ? 0.3605 0.3658 0.3692 -0.0266 -0.0103 0.0468  854  GLU A CG  
6246  C CD  . GLU A 856  ? 0.4699 0.4687 0.4839 -0.0265 -0.0133 0.0488  854  GLU A CD  
6247  O OE1 . GLU A 856  ? 0.4564 0.4492 0.4734 -0.0252 -0.0146 0.0472  854  GLU A OE1 
6248  O OE2 . GLU A 856  ? 0.4851 0.4852 0.5005 -0.0277 -0.0144 0.0519  854  GLU A OE2 
6249  N N   . ASP A 857  ? 0.3096 0.3120 0.3064 -0.0202 -0.0037 0.0348  855  ASP A N   
6250  C CA  . ASP A 857  ? 0.3177 0.3244 0.3122 -0.0207 -0.0028 0.0350  855  ASP A CA  
6251  C C   . ASP A 857  ? 0.3195 0.3206 0.3137 -0.0187 -0.0026 0.0332  855  ASP A C   
6252  O O   . ASP A 857  ? 0.3601 0.3637 0.3536 -0.0194 -0.0026 0.0344  855  ASP A O   
6253  C CB  . ASP A 857  ? 0.3943 0.4064 0.3850 -0.0201 -0.0003 0.0317  855  ASP A CB  
6254  N N   . VAL A 858  ? 0.2612 0.2553 0.2558 -0.0163 -0.0025 0.0304  856  VAL A N   
6255  C CA  . VAL A 858  ? 0.2804 0.2696 0.2747 -0.0143 -0.0023 0.0287  856  VAL A CA  
6256  C C   . VAL A 858  ? 0.2784 0.2618 0.2766 -0.0137 -0.0044 0.0297  856  VAL A C   
6257  O O   . VAL A 858  ? 0.2752 0.2548 0.2738 -0.0120 -0.0043 0.0283  856  VAL A O   
6258  C CB  . VAL A 858  ? 0.2933 0.2802 0.2846 -0.0117 -0.0001 0.0241  856  VAL A CB  
6259  C CG1 . VAL A 858  ? 0.3205 0.3129 0.3088 -0.0122 0.0017  0.0227  856  VAL A CG1 
6260  C CG2 . VAL A 858  ? 0.2791 0.2631 0.2706 -0.0105 0.0001  0.0222  856  VAL A CG2 
6261  N N   . ALA A 859  ? 0.2562 0.2391 0.2578 -0.0150 -0.0063 0.0320  857  ALA A N   
6262  C CA  . ALA A 859  ? 0.2583 0.2354 0.2641 -0.0140 -0.0085 0.0319  857  ALA A CA  
6263  C C   . ALA A 859  ? 0.3042 0.2798 0.3130 -0.0142 -0.0101 0.0340  857  ALA A C   
6264  O O   . ALA A 859  ? 0.2597 0.2303 0.2701 -0.0121 -0.0107 0.0319  857  ALA A O   
6265  C CB  . ALA A 859  ? 0.2836 0.2610 0.2932 -0.0156 -0.0106 0.0342  857  ALA A CB  
6266  N N   . ASP A 860  ? 0.3034 0.2834 0.3129 -0.0168 -0.0109 0.0380  858  ASP A N   
6267  C CA  . ASP A 860  ? 0.3216 0.3002 0.3345 -0.0172 -0.0128 0.0404  858  ASP A CA  
6268  C C   . ASP A 860  ? 0.3068 0.2834 0.3169 -0.0150 -0.0111 0.0374  858  ASP A C   
6269  O O   . ASP A 860  ? 0.2926 0.2649 0.3056 -0.0136 -0.0123 0.0368  858  ASP A O   
6270  C CB  . ASP A 860  ? 0.3040 0.2888 0.3179 -0.0205 -0.0139 0.0457  858  ASP A CB  
6271  C CG  . ASP A 860  ? 0.3794 0.3653 0.3980 -0.0229 -0.0165 0.0499  858  ASP A CG  
6272  O OD1 . ASP A 860  ? 0.4635 0.4439 0.4870 -0.0221 -0.0187 0.0495  858  ASP A OD1 
6273  O OD2 . ASP A 860  ? 0.5566 0.5493 0.5743 -0.0256 -0.0165 0.0534  858  ASP A OD2 
6274  N N   . ARG A 861  ? 0.2696 0.2494 0.2746 -0.0146 -0.0084 0.0354  859  ARG A N   
6275  C CA  . ARG A 861  ? 0.2868 0.2650 0.2895 -0.0127 -0.0068 0.0328  859  ARG A CA  
6276  C C   . ARG A 861  ? 0.2591 0.2317 0.2620 -0.0098 -0.0063 0.0290  859  ARG A C   
6277  O O   . ARG A 861  ? 0.2914 0.2611 0.2954 -0.0083 -0.0064 0.0280  859  ARG A O   
6278  C CB  . ARG A 861  ? 0.3721 0.3548 0.3701 -0.0129 -0.0044 0.0312  859  ARG A CB  
6279  C CG  . ARG A 861  ? 0.4245 0.4052 0.4205 -0.0109 -0.0027 0.0283  859  ARG A CG  
6280  C CD  . ARG A 861  ? 0.5373 0.5229 0.5300 -0.0115 -0.0011 0.0273  859  ARG A CD  
6281  N NE  . ARG A 861  ? 0.6520 0.6354 0.6437 -0.0097 0.0001  0.0250  859  ARG A NE  
6282  C CZ  . ARG A 861  ? 0.5519 0.5330 0.5420 -0.0077 0.0017  0.0218  859  ARG A CZ  
6283  N NH1 . ARG A 861  ? 0.5683 0.5489 0.5572 -0.0071 0.0025  0.0201  859  ARG A NH1 
6284  N NH2 . ARG A 861  ? 0.5576 0.5369 0.5474 -0.0064 0.0025  0.0204  859  ARG A NH2 
6285  N N   . ILE A 862  ? 0.2396 0.2111 0.2414 -0.0089 -0.0055 0.0269  860  ILE A N   
6286  C CA  . ILE A 862  ? 0.2602 0.2272 0.2619 -0.0061 -0.0050 0.0234  860  ILE A CA  
6287  C C   . ILE A 862  ? 0.2631 0.2264 0.2697 -0.0054 -0.0075 0.0237  860  ILE A C   
6288  O O   . ILE A 862  ? 0.2472 0.2077 0.2545 -0.0032 -0.0073 0.0214  860  ILE A O   
6289  C CB  . ILE A 862  ? 0.2489 0.2162 0.2484 -0.0055 -0.0038 0.0213  860  ILE A CB  
6290  C CG1 . ILE A 862  ? 0.2779 0.2481 0.2730 -0.0053 -0.0013 0.0199  860  ILE A CG1 
6291  C CG2 . ILE A 862  ? 0.2662 0.2295 0.2663 -0.0029 -0.0038 0.0181  860  ILE A CG2 
6292  C CD1 . ILE A 862  ? 0.3152 0.2862 0.3083 -0.0049 -0.0002 0.0182  860  ILE A CD1 
6293  N N   . LEU A 863  ? 0.2390 0.2024 0.2495 -0.0072 -0.0099 0.0265  861  LEU A N   
6294  C CA  A LEU A 863  ? 0.2600 0.2197 0.2763 -0.0066 -0.0128 0.0266  861  LEU A CA  
6295  C CA  B LEU A 863  ? 0.2598 0.2195 0.2762 -0.0066 -0.0128 0.0266  861  LEU A CA  
6296  C C   . LEU A 863  ? 0.2615 0.2201 0.2801 -0.0062 -0.0136 0.0275  861  LEU A C   
6297  O O   . LEU A 863  ? 0.2390 0.1943 0.2605 -0.0041 -0.0147 0.0252  861  LEU A O   
6298  C CB  A LEU A 863  ? 0.2862 0.2466 0.3070 -0.0091 -0.0155 0.0303  861  LEU A CB  
6299  C CB  B LEU A 863  ? 0.2863 0.2467 0.3069 -0.0091 -0.0154 0.0302  861  LEU A CB  
6300  C CG  A LEU A 863  ? 0.3051 0.2636 0.3276 -0.0086 -0.0164 0.0286  861  LEU A CG  
6301  C CG  B LEU A 863  ? 0.3131 0.2694 0.3407 -0.0085 -0.0188 0.0301  861  LEU A CG  
6302  C CD1 A LEU A 863  ? 0.3068 0.2671 0.3335 -0.0116 -0.0189 0.0331  861  LEU A CD1 
6303  C CD1 B LEU A 863  ? 0.3038 0.2567 0.3311 -0.0053 -0.0183 0.0248  861  LEU A CD1 
6304  C CD2 A LEU A 863  ? 0.3192 0.2729 0.3456 -0.0059 -0.0181 0.0251  861  LEU A CD2 
6305  C CD2 B LEU A 863  ? 0.3286 0.2862 0.3601 -0.0112 -0.0211 0.0339  861  LEU A CD2 
6306  N N   . THR A 864  ? 0.2503 0.2122 0.2676 -0.0081 -0.0133 0.0307  862  THR A N   
6307  C CA  . THR A 864  ? 0.2730 0.2343 0.2922 -0.0078 -0.0140 0.0315  862  THR A CA  
6308  C C   . THR A 864  ? 0.2494 0.2089 0.2658 -0.0049 -0.0118 0.0274  862  THR A C   
6309  O O   . THR A 864  ? 0.2385 0.1954 0.2579 -0.0033 -0.0128 0.0261  862  THR A O   
6310  C CB  . THR A 864  ? 0.2761 0.2421 0.2934 -0.0103 -0.0136 0.0352  862  THR A CB  
6311  O OG1 . THR A 864  ? 0.3024 0.2706 0.3229 -0.0131 -0.0159 0.0397  862  THR A OG1 
6312  C CG2 . THR A 864  ? 0.2552 0.2207 0.2737 -0.0098 -0.0140 0.0358  862  THR A CG2 
6313  N N   . MET A 865  ? 0.2376 0.1988 0.2486 -0.0043 -0.0089 0.0253  863  MET A N   
6314  C CA  . MET A 865  ? 0.2239 0.1838 0.2325 -0.0018 -0.0069 0.0220  863  MET A CA  
6315  C C   . MET A 865  ? 0.2263 0.1830 0.2368 0.0007  -0.0074 0.0188  863  MET A C   
6316  O O   . MET A 865  ? 0.2145 0.1701 0.2260 0.0027  -0.0072 0.0168  863  MET A O   
6317  C CB  . MET A 865  ? 0.2556 0.2179 0.2589 -0.0018 -0.0041 0.0207  863  MET A CB  
6318  C CG  . MET A 865  ? 0.3093 0.2709 0.3103 0.0004  -0.0021 0.0181  863  MET A CG  
6319  S SD  . MET A 865  ? 0.3443 0.3086 0.3405 0.0000  0.0006  0.0171  863  MET A SD  
6320  C CE  . MET A 865  ? 0.3038 0.2718 0.2998 -0.0030 -0.0003 0.0203  863  MET A CE  
6321  N N   . LEU A 866  ? 0.2299 0.1859 0.2412 0.0006  -0.0082 0.0182  864  LEU A N   
6322  C CA  . LEU A 866  ? 0.2235 0.1770 0.2366 0.0030  -0.0089 0.0147  864  LEU A CA  
6323  C C   . LEU A 866  ? 0.2135 0.1647 0.2325 0.0039  -0.0115 0.0144  864  LEU A C   
6324  O O   . LEU A 866  ? 0.2423 0.1925 0.2624 0.0065  -0.0114 0.0111  864  LEU A O   
6325  C CB  . LEU A 866  ? 0.2244 0.1777 0.2378 0.0023  -0.0096 0.0146  864  LEU A CB  
6326  C CG  . LEU A 866  ? 0.3014 0.2525 0.3169 0.0047  -0.0106 0.0109  864  LEU A CG  
6327  C CD1 . LEU A 866  ? 0.2942 0.2462 0.3056 0.0072  -0.0080 0.0075  864  LEU A CD1 
6328  C CD2 . LEU A 866  ? 0.3054 0.2563 0.3216 0.0036  -0.0116 0.0112  864  LEU A CD2 
6329  N N   . LYS A 867  ? 0.2378 0.1885 0.2612 0.0018  -0.0141 0.0179  865  LYS A N   
6330  C CA  . LYS A 867  ? 0.2391 0.1874 0.2690 0.0026  -0.0170 0.0177  865  LYS A CA  
6331  C C   . LYS A 867  ? 0.2428 0.1914 0.2722 0.0039  -0.0160 0.0169  865  LYS A C   
6332  O O   . LYS A 867  ? 0.2389 0.1859 0.2719 0.0062  -0.0171 0.0142  865  LYS A O   
6333  C CB  . LYS A 867  ? 0.2764 0.2243 0.3112 -0.0003 -0.0201 0.0225  865  LYS A CB  
6334  C CG  . LYS A 867  ? 0.2935 0.2408 0.3305 -0.0015 -0.0217 0.0232  865  LYS A CG  
6335  C CD  . LYS A 867  ? 0.3005 0.2485 0.3422 -0.0048 -0.0246 0.0288  865  LYS A CD  
6336  C CE  . LYS A 867  ? 0.3911 0.3388 0.4350 -0.0062 -0.0261 0.0298  865  LYS A CE  
6337  N NZ  . LYS A 867  ? 0.4312 0.3806 0.4792 -0.0098 -0.0287 0.0360  865  LYS A NZ  
6338  N N   . GLY A 868  ? 0.2371 0.1881 0.2622 0.0026  -0.0140 0.0191  866  GLY A N   
6339  C CA  . GLY A 868  ? 0.2501 0.2017 0.2745 0.0038  -0.0129 0.0184  866  GLY A CA  
6340  C C   . GLY A 868  ? 0.2299 0.1815 0.2521 0.0068  -0.0108 0.0139  866  GLY A C   
6341  O O   . GLY A 868  ? 0.2433 0.1945 0.2677 0.0087  -0.0110 0.0121  866  GLY A O   
6342  N N   . ALA A 869  ? 0.2162 0.1686 0.2341 0.0072  -0.0088 0.0123  867  ALA A N   
6343  C CA  . ALA A 869  ? 0.2197 0.1729 0.2352 0.0099  -0.0069 0.0086  867  ALA A CA  
6344  C C   . ALA A 869  ? 0.2362 0.1881 0.2559 0.0122  -0.0087 0.0052  867  ALA A C   
6345  O O   . ALA A 869  ? 0.2375 0.1904 0.2574 0.0146  -0.0079 0.0023  867  ALA A O   
6346  C CB  . ALA A 869  ? 0.2328 0.1872 0.2432 0.0096  -0.0047 0.0081  867  ALA A CB  
6347  N N   . LEU A 870  ? 0.2293 0.1792 0.2526 0.0114  -0.0112 0.0055  868  LEU A N   
6348  C CA  . LEU A 870  ? 0.2530 0.2013 0.2811 0.0136  -0.0134 0.0019  868  LEU A CA  
6349  C C   . LEU A 870  ? 0.2541 0.2021 0.2869 0.0152  -0.0147 0.0007  868  LEU A C   
6350  O O   . LEU A 870  ? 0.2674 0.2161 0.3020 0.0180  -0.0149 -0.0036 868  LEU A O   
6351  C CB  . LEU A 870  ? 0.2519 0.1978 0.2845 0.0120  -0.0165 0.0035  868  LEU A CB  
6352  C CG  . LEU A 870  ? 0.3091 0.2532 0.3475 0.0139  -0.0193 -0.0002 868  LEU A CG  
6353  C CD1 . LEU A 870  ? 0.3405 0.2856 0.3752 0.0151  -0.0180 -0.0033 868  LEU A CD1 
6354  C CD2 . LEU A 870  ? 0.3402 0.2813 0.3854 0.0118  -0.0232 0.0026  868  LEU A CD2 
6355  N N   . HIS A 871  ? 0.2297 0.1769 0.2645 0.0134  -0.0157 0.0043  869  HIS A N   
6356  C CA  . HIS A 871  ? 0.2729 0.2195 0.3130 0.0147  -0.0174 0.0034  869  HIS A CA  
6357  C C   . HIS A 871  ? 0.2817 0.2309 0.3187 0.0166  -0.0148 0.0014  869  HIS A C   
6358  O O   . HIS A 871  ? 0.2986 0.2479 0.3399 0.0182  -0.0159 -0.0001 869  HIS A O   
6359  C CB  . HIS A 871  ? 0.3196 0.2647 0.3635 0.0121  -0.0197 0.0081  869  HIS A CB  
6360  C CG  . HIS A 871  ? 0.3369 0.2794 0.3864 0.0107  -0.0233 0.0098  869  HIS A CG  
6361  N ND1 . HIS A 871  ? 0.3443 0.2843 0.4014 0.0124  -0.0266 0.0071  869  HIS A ND1 
6362  C CD2 . HIS A 871  ? 0.3320 0.2741 0.3810 0.0077  -0.0241 0.0138  869  HIS A CD2 
6363  C CE1 . HIS A 871  ? 0.3822 0.3202 0.4435 0.0104  -0.0294 0.0096  869  HIS A CE1 
6364  N NE2 . HIS A 871  ? 0.3808 0.3202 0.4371 0.0075  -0.0279 0.0139  869  HIS A NE2 
6365  N N   . GLU A 872  ? 0.2355 0.1871 0.2658 0.0166  -0.0114 0.0013  870  GLU A N   
6366  C CA  . GLU A 872  ? 0.2783 0.2329 0.3059 0.0183  -0.0089 -0.0003 870  GLU A CA  
6367  C C   . GLU A 872  ? 0.2640 0.2209 0.2909 0.0213  -0.0079 -0.0050 870  GLU A C   
6368  O O   . GLU A 872  ? 0.2617 0.2218 0.2864 0.0228  -0.0058 -0.0063 870  GLU A O   
6369  C CB  . GLU A 872  ? 0.2460 0.2021 0.2674 0.0166  -0.0060 0.0024  870  GLU A CB  
6370  C CG  . GLU A 872  ? 0.2608 0.2159 0.2825 0.0139  -0.0066 0.0066  870  GLU A CG  
6371  C CD  . GLU A 872  ? 0.3085 0.2635 0.3339 0.0143  -0.0077 0.0073  870  GLU A CD  
6372  O OE1 . GLU A 872  ? 0.3157 0.2724 0.3419 0.0166  -0.0068 0.0047  870  GLU A OE1 
6373  O OE2 . GLU A 872  ? 0.2975 0.2513 0.3252 0.0122  -0.0094 0.0105  870  GLU A OE2 
6374  N N   . LEU A 873  ? 0.2451 0.2008 0.2739 0.0221  -0.0096 -0.0074 871  LEU A N   
6375  C CA  . LEU A 873  ? 0.2213 0.1799 0.2492 0.0250  -0.0088 -0.0121 871  LEU A CA  
6376  C C   . LEU A 873  ? 0.2341 0.1938 0.2678 0.0277  -0.0105 -0.0161 871  LEU A C   
6377  O O   . LEU A 873  ? 0.2805 0.2371 0.3206 0.0275  -0.0137 -0.0162 871  LEU A O   
6378  C CB  . LEU A 873  ? 0.2496 0.2068 0.2776 0.0248  -0.0099 -0.0134 871  LEU A CB  
6379  C CG  . LEU A 873  ? 0.2765 0.2330 0.2992 0.0223  -0.0083 -0.0100 871  LEU A CG  
6380  C CD1 . LEU A 873  ? 0.2833 0.2383 0.3069 0.0222  -0.0099 -0.0114 871  LEU A CD1 
6381  C CD2 . LEU A 873  ? 0.3030 0.2632 0.3194 0.0228  -0.0047 -0.0098 871  LEU A CD2 
6382  N N   . HIS A 874  ? 0.2524 0.2169 0.2841 0.0303  -0.0086 -0.0195 872  HIS A N   
6383  C CA  . HIS A 874  ? 0.2538 0.2206 0.2904 0.0333  -0.0099 -0.0242 872  HIS A CA  
6384  C C   . HIS A 874  ? 0.2525 0.2212 0.2903 0.0356  -0.0110 -0.0293 872  HIS A C   
6385  O O   . HIS A 874  ? 0.2466 0.2190 0.2790 0.0363  -0.0087 -0.0303 872  HIS A O   
6386  C CB  . HIS A 874  ? 0.2674 0.2395 0.3011 0.0347  -0.0070 -0.0246 872  HIS A CB  
6387  C CG  . HIS A 874  ? 0.3064 0.2821 0.3451 0.0379  -0.0080 -0.0295 872  HIS A CG  
6388  N ND1 . HIS A 874  ? 0.3874 0.3684 0.4245 0.0393  -0.0057 -0.0302 872  HIS A ND1 
6389  C CD2 . HIS A 874  ? 0.3677 0.3426 0.4131 0.0401  -0.0112 -0.0342 872  HIS A CD2 
6390  C CE1 . HIS A 874  ? 0.3730 0.3568 0.4155 0.0423  -0.0073 -0.0352 872  HIS A CE1 
6391  N NE2 . HIS A 874  ? 0.3283 0.3083 0.3760 0.0429  -0.0106 -0.0379 872  HIS A NE2 
6392  N N   . ILE A 875  ? 0.2690 0.2352 0.3140 0.0368  -0.0146 -0.0325 873  ILE A N   
6393  C CA  . ILE A 875  ? 0.2615 0.2290 0.3088 0.0391  -0.0163 -0.0379 873  ILE A CA  
6394  C C   . ILE A 875  ? 0.2932 0.2650 0.3452 0.0428  -0.0171 -0.0440 873  ILE A C   
6395  O O   . ILE A 875  ? 0.2755 0.2456 0.3334 0.0433  -0.0190 -0.0443 873  ILE A O   
6396  C CB  . ILE A 875  ? 0.2690 0.2304 0.3221 0.0377  -0.0201 -0.0373 873  ILE A CB  
6397  C CG1 . ILE A 875  ? 0.3369 0.2956 0.3849 0.0345  -0.0191 -0.0326 873  ILE A CG1 
6398  C CG2 . ILE A 875  ? 0.2998 0.2624 0.3575 0.0405  -0.0226 -0.0439 873  ILE A CG2 
6399  C CD1 . ILE A 875  ? 0.3388 0.2956 0.3829 0.0313  -0.0173 -0.0261 873  ILE A CD1 
6400  N N   . GLY A 876  ? 0.2628 0.2407 0.3123 0.0455  -0.0158 -0.0488 874  GLY A N   
6401  C CA  . GLY A 876  ? 0.2595 0.2427 0.3134 0.0492  -0.0166 -0.0552 874  GLY A CA  
6402  C C   . GLY A 876  ? 0.2822 0.2735 0.3314 0.0518  -0.0145 -0.0596 874  GLY A C   
6403  O O   . GLY A 876  ? 0.2588 0.2512 0.3020 0.0507  -0.0127 -0.0580 874  GLY A O   
6404  N N   . ARG A 877  ? 0.2552 0.2528 0.3075 0.0553  -0.0147 -0.0655 875  ARG A N   
6405  C CA  . ARG A 877  ? 0.2725 0.2797 0.3205 0.0579  -0.0125 -0.0698 875  ARG A CA  
6406  C C   . ARG A 877  ? 0.2687 0.2800 0.3078 0.0561  -0.0079 -0.0644 875  ARG A C   
6407  O O   . ARG A 877  ? 0.2643 0.2747 0.3021 0.0546  -0.0063 -0.0600 875  ARG A O   
6408  C CB  . ARG A 877  ? 0.3150 0.3289 0.3681 0.0618  -0.0132 -0.0765 875  ARG A CB  
6409  C CG  . ARG A 877  ? 0.3208 0.3445 0.3720 0.0651  -0.0125 -0.0831 875  ARG A CG  
6410  C CD  . ARG A 877  ? 0.3736 0.4037 0.4309 0.0691  -0.0137 -0.0902 875  ARG A CD  
6411  N NE  . ARG A 877  ? 0.3477 0.3859 0.4011 0.0697  -0.0100 -0.0887 875  ARG A NE  
6412  C CZ  . ARG A 877  ? 0.4276 0.4738 0.4846 0.0732  -0.0100 -0.0946 875  ARG A CZ  
6413  N NH1 . ARG A 877  ? 0.3822 0.4293 0.4472 0.0765  -0.0136 -0.1028 875  ARG A NH1 
6414  N NH2 . ARG A 877  ? 0.4102 0.4641 0.4633 0.0734  -0.0065 -0.0925 875  ARG A NH2 
6415  N N   . THR A 878  ? 0.2645 0.2802 0.2977 0.0562  -0.0062 -0.0646 876  THR A N   
6416  C CA  . THR A 878  ? 0.2456 0.2627 0.2710 0.0537  -0.0026 -0.0583 876  THR A CA  
6417  C C   . THR A 878  ? 0.2577 0.2844 0.2792 0.0549  0.0007  -0.0579 876  THR A C   
6418  O O   . THR A 878  ? 0.2783 0.3070 0.2937 0.0530  0.0036  -0.0529 876  THR A O   
6419  C CB  . THR A 878  ? 0.2684 0.2852 0.2895 0.0529  -0.0024 -0.0579 876  THR A CB  
6420  O OG1 . THR A 878  ? 0.2989 0.3225 0.3209 0.0561  -0.0033 -0.0647 876  THR A OG1 
6421  C CG2 . THR A 878  ? 0.3170 0.3239 0.3407 0.0506  -0.0050 -0.0559 876  THR A CG2 
6422  N N   . ASP A 879  ? 0.2426 0.2754 0.2678 0.0579  0.0004  -0.0629 877  ASP A N   
6423  C CA  . ASP A 879  ? 0.2849 0.3275 0.3069 0.0589  0.0036  -0.0622 877  ASP A CA  
6424  C C   . ASP A 879  ? 0.2681 0.3078 0.2907 0.0570  0.0048  -0.0571 877  ASP A C   
6425  O O   . ASP A 879  ? 0.2534 0.3002 0.2762 0.0584  0.0065  -0.0577 877  ASP A O   
6426  C CB  . ASP A 879  ? 0.2547 0.3069 0.2800 0.0632  0.0029  -0.0702 877  ASP A CB  
6427  C CG  . ASP A 879  ? 0.3572 0.4058 0.3909 0.0650  0.0000  -0.0745 877  ASP A CG  
6428  O OD1 . ASP A 879  ? 0.3905 0.4285 0.4283 0.0633  -0.0027 -0.0730 877  ASP A OD1 
6429  O OD2 . ASP A 879  ? 0.3438 0.4005 0.3802 0.0679  0.0004  -0.0791 877  ASP A OD2 
6430  N N   . ARG A 880  ? 0.2729 0.3026 0.2957 0.0539  0.0040  -0.0521 878  ARG A N   
6431  C CA  . ARG A 880  ? 0.2705 0.2968 0.2930 0.0516  0.0052  -0.0466 878  ARG A CA  
6432  C C   . ARG A 880  ? 0.2370 0.2582 0.2543 0.0481  0.0065  -0.0402 878  ARG A C   
6433  O O   . ARG A 880  ? 0.2545 0.2694 0.2716 0.0469  0.0049  -0.0398 878  ARG A O   
6434  C CB  . ARG A 880  ? 0.3119 0.3307 0.3409 0.0513  0.0023  -0.0472 878  ARG A CB  
6435  C CG  . ARG A 880  ? 0.3630 0.3862 0.3981 0.0546  0.0010  -0.0529 878  ARG A CG  
6436  C CD  . ARG A 880  ? 0.3984 0.4134 0.4403 0.0540  -0.0022 -0.0527 878  ARG A CD  
6437  N NE  . ARG A 880  ? 0.5897 0.6085 0.6384 0.0573  -0.0039 -0.0584 878  ARG A NE  
6438  C CZ  . ARG A 880  ? 0.5911 0.6102 0.6430 0.0575  -0.0038 -0.0574 878  ARG A CZ  
6439  N NH1 . ARG A 880  ? 0.5991 0.6147 0.6482 0.0545  -0.0023 -0.0509 878  ARG A NH1 
6440  N NH2 . ARG A 880  ? 0.6250 0.6479 0.6834 0.0608  -0.0054 -0.0633 878  ARG A NH2 
6441  N N   . LEU A 881  ? 0.2360 0.2599 0.2494 0.0465  0.0093  -0.0354 879  LEU A N   
6442  C CA  . LEU A 881  ? 0.2156 0.2349 0.2247 0.0433  0.0105  -0.0295 879  LEU A CA  
6443  C C   . LEU A 881  ? 0.2256 0.2349 0.2369 0.0410  0.0086  -0.0271 879  LEU A C   
6444  O O   . LEU A 881  ? 0.2453 0.2500 0.2540 0.0388  0.0085  -0.0242 879  LEU A O   
6445  C CB  . LEU A 881  ? 0.2491 0.2727 0.2555 0.0421  0.0134  -0.0250 879  LEU A CB  
6446  C CG  . LEU A 881  ? 0.2839 0.3041 0.2863 0.0391  0.0147  -0.0192 879  LEU A CG  
6447  C CD1 . LEU A 881  ? 0.3109 0.3339 0.3094 0.0393  0.0153  -0.0194 879  LEU A CD1 
6448  C CD2 . LEU A 881  ? 0.3001 0.3239 0.3017 0.0380  0.0169  -0.0150 879  LEU A CD2 
6449  N N   . SER A 882  ? 0.2266 0.2330 0.2429 0.0414  0.0068  -0.0283 880  SER A N   
6450  C CA  . SER A 882  ? 0.2431 0.2408 0.2615 0.0391  0.0049  -0.0256 880  SER A CA  
6451  C C   . SER A 882  ? 0.2841 0.2768 0.3046 0.0389  0.0022  -0.0276 880  SER A C   
6452  O O   . SER A 882  ? 0.2740 0.2601 0.2959 0.0367  0.0007  -0.0248 880  SER A O   
6453  C CB  . SER A 882  ? 0.2538 0.2503 0.2773 0.0396  0.0037  -0.0260 880  SER A CB  
6454  O OG  . SER A 882  ? 0.3082 0.3069 0.3369 0.0426  0.0017  -0.0317 880  SER A OG  
6455  N N   . VAL A 883  ? 0.2589 0.2549 0.2797 0.0412  0.0016  -0.0321 881  VAL A N   
6456  C CA  . VAL A 883  ? 0.2598 0.2510 0.2832 0.0411  -0.0012 -0.0343 881  VAL A CA  
6457  C C   . VAL A 883  ? 0.2546 0.2436 0.2730 0.0390  -0.0002 -0.0311 881  VAL A C   
6458  O O   . VAL A 883  ? 0.3056 0.2993 0.3191 0.0393  0.0021  -0.0307 881  VAL A O   
6459  C CB  . VAL A 883  ? 0.2809 0.2765 0.3076 0.0446  -0.0027 -0.0411 881  VAL A CB  
6460  C CG1 . VAL A 883  ? 0.2658 0.2571 0.2942 0.0444  -0.0053 -0.0429 881  VAL A CG1 
6461  C CG2 . VAL A 883  ? 0.3013 0.2973 0.3348 0.0466  -0.0047 -0.0445 881  VAL A CG2 
6462  N N   . ASP A 884  ? 0.2438 0.2259 0.2637 0.0367  -0.0020 -0.0287 882  ASP A N   
6463  C CA  . ASP A 884  ? 0.2527 0.2324 0.2683 0.0346  -0.0013 -0.0258 882  ASP A CA  
6464  C C   . ASP A 884  ? 0.3097 0.2888 0.3265 0.0356  -0.0032 -0.0293 882  ASP A C   
6465  O O   . ASP A 884  ? 0.3421 0.3228 0.3546 0.0353  -0.0019 -0.0289 882  ASP A O   
6466  C CB  . ASP A 884  ? 0.2767 0.2503 0.2928 0.0314  -0.0021 -0.0212 882  ASP A CB  
6467  C CG  . ASP A 884  ? 0.2407 0.2148 0.2556 0.0303  -0.0004 -0.0178 882  ASP A CG  
6468  O OD1 . ASP A 884  ? 0.2968 0.2742 0.3072 0.0301  0.0023  -0.0162 882  ASP A OD1 
6469  O OD2 . ASP A 884  ? 0.2654 0.2367 0.2842 0.0296  -0.0019 -0.0167 882  ASP A OD2 
6470  N N   . VAL A 885  ? 0.2502 0.2269 0.2733 0.0367  -0.0063 -0.0325 883  VAL A N   
6471  C CA  . VAL A 885  ? 0.2732 0.2480 0.2988 0.0373  -0.0088 -0.0355 883  VAL A CA  
6472  C C   . VAL A 885  ? 0.2588 0.2368 0.2895 0.0407  -0.0107 -0.0420 883  VAL A C   
6473  O O   . VAL A 885  ? 0.2592 0.2360 0.2954 0.0416  -0.0124 -0.0433 883  VAL A O   
6474  C CB  . VAL A 885  ? 0.3027 0.2703 0.3322 0.0347  -0.0115 -0.0326 883  VAL A CB  
6475  C CG1 . VAL A 885  ? 0.2947 0.2605 0.3272 0.0353  -0.0141 -0.0356 883  VAL A CG1 
6476  C CG2 . VAL A 885  ? 0.3039 0.2691 0.3284 0.0314  -0.0095 -0.0265 883  VAL A CG2 
6477  N N   . GLY A 886  ? 0.2635 0.2459 0.2927 0.0428  -0.0105 -0.0463 884  GLY A N   
6478  C CA  . GLY A 886  ? 0.2400 0.2264 0.2739 0.0464  -0.0124 -0.0533 884  GLY A CA  
6479  C C   . GLY A 886  ? 0.2664 0.2482 0.3070 0.0468  -0.0165 -0.0566 884  GLY A C   
6480  O O   . GLY A 886  ? 0.2537 0.2287 0.2963 0.0441  -0.0183 -0.0530 884  GLY A O   
6481  N N   . PRO A 887  ? 0.2559 0.2419 0.3002 0.0502  -0.0183 -0.0637 885  PRO A N   
6482  C CA  . PRO A 887  ? 0.2459 0.2278 0.2980 0.0510  -0.0227 -0.0677 885  PRO A CA  
6483  C C   . PRO A 887  ? 0.2414 0.2222 0.2906 0.0500  -0.0230 -0.0676 885  PRO A C   
6484  O O   . PRO A 887  ? 0.2539 0.2384 0.2953 0.0494  -0.0199 -0.0656 885  PRO A O   
6485  C CB  . PRO A 887  ? 0.2518 0.2403 0.3081 0.0554  -0.0239 -0.0760 885  PRO A CB  
6486  C CG  . PRO A 887  ? 0.2711 0.2687 0.3188 0.0566  -0.0195 -0.0764 885  PRO A CG  
6487  C CD  . PRO A 887  ? 0.2820 0.2775 0.3239 0.0535  -0.0162 -0.0685 885  PRO A CD  
6488  N N   . VAL A 888  ? 0.2382 0.2139 0.2945 0.0498  -0.0271 -0.0697 886  VAL A N   
6489  C CA  . VAL A 888  ? 0.2222 0.1983 0.2775 0.0500  -0.0282 -0.0720 886  VAL A CA  
6490  C C   . VAL A 888  ? 0.2557 0.2388 0.3129 0.0542  -0.0292 -0.0807 886  VAL A C   
6491  O O   . VAL A 888  ? 0.2708 0.2569 0.3329 0.0570  -0.0303 -0.0855 886  VAL A O   
6492  C CB  . VAL A 888  ? 0.2764 0.2445 0.3382 0.0477  -0.0320 -0.0699 886  VAL A CB  
6493  C CG1 . VAL A 888  ? 0.2956 0.2583 0.3545 0.0435  -0.0306 -0.0613 886  VAL A CG1 
6494  C CG2 . VAL A 888  ? 0.2848 0.2496 0.3577 0.0493  -0.0367 -0.0741 886  VAL A CG2 
6495  N N   . ILE A 889  ? 0.2607 0.2472 0.3141 0.0549  -0.0287 -0.0830 887  ILE A N   
6496  C CA  . ILE A 889  ? 0.2789 0.2747 0.3308 0.0587  -0.0281 -0.0903 887  ILE A CA  
6497  C C   . ILE A 889  ? 0.3008 0.2970 0.3627 0.0620  -0.0326 -0.0987 887  ILE A C   
6498  O O   . ILE A 889  ? 0.2795 0.2835 0.3422 0.0656  -0.0323 -0.1050 887  ILE A O   
6499  C CB  . ILE A 889  ? 0.2661 0.2657 0.3111 0.0584  -0.0265 -0.0902 887  ILE A CB  
6500  C CG1 . ILE A 889  ? 0.2863 0.2972 0.3283 0.0622  -0.0253 -0.0969 887  ILE A CG1 
6501  C CG2 . ILE A 889  ? 0.2741 0.2676 0.3239 0.0573  -0.0301 -0.0911 887  ILE A CG2 
6502  C CD1 . ILE A 889  ? 0.2585 0.2765 0.2956 0.0632  -0.0215 -0.0956 887  ILE A CD1 
6503  N N   . THR A 890  ? 0.2438 0.2321 0.3139 0.0609  -0.0369 -0.0990 888  THR A N   
6504  C CA  . THR A 890  ? 0.2495 0.2376 0.3301 0.0640  -0.0417 -0.1071 888  THR A CA  
6505  C C   . THR A 890  ? 0.2531 0.2310 0.3436 0.0618  -0.0459 -0.1043 888  THR A C   
6506  O O   . THR A 890  ? 0.2695 0.2408 0.3583 0.0579  -0.0454 -0.0963 888  THR A O   
6507  C CB  . THR A 890  ? 0.3024 0.2929 0.3840 0.0655  -0.0438 -0.1129 888  THR A CB  
6508  O OG1 . THR A 890  ? 0.3080 0.2914 0.3893 0.0619  -0.0447 -0.1073 888  THR A OG1 
6509  C CG2 . THR A 890  ? 0.3081 0.3095 0.3804 0.0677  -0.0400 -0.1160 888  THR A CG2 
6510  N N   . SER A 891  ? 0.2786 0.2556 0.3799 0.0646  -0.0504 -0.1111 889  SER A N   
6511  C CA  A SER A 891  ? 0.3123 0.2800 0.4248 0.0629  -0.0553 -0.1091 889  SER A CA  
6512  C CA  B SER A 891  ? 0.3122 0.2799 0.4245 0.0628  -0.0552 -0.1089 889  SER A CA  
6513  C C   . SER A 891  ? 0.3003 0.2619 0.4146 0.0600  -0.0575 -0.1058 889  SER A C   
6514  O O   . SER A 891  ? 0.3292 0.2830 0.4481 0.0566  -0.0596 -0.0994 889  SER A O   
6515  C CB  A SER A 891  ? 0.3298 0.2984 0.4542 0.0669  -0.0600 -0.1182 889  SER A CB  
6516  C CB  B SER A 891  ? 0.3301 0.2984 0.4543 0.0667  -0.0598 -0.1176 889  SER A CB  
6517  O OG  A SER A 891  ? 0.3164 0.2896 0.4407 0.0693  -0.0584 -0.1207 889  SER A OG  
6518  O OG  B SER A 891  ? 0.3571 0.3303 0.4833 0.0699  -0.0617 -0.1263 889  SER A OG  
6519  N N   . GLU A 892  ? 0.2946 0.2602 0.4055 0.0612  -0.0573 -0.1100 890  GLU A N   
6520  C CA  . GLU A 892  ? 0.3153 0.2757 0.4280 0.0585  -0.0595 -0.1072 890  GLU A CA  
6521  C C   . GLU A 892  ? 0.3250 0.2826 0.4286 0.0541  -0.0556 -0.0972 890  GLU A C   
6522  O O   . GLU A 892  ? 0.3417 0.2926 0.4487 0.0507  -0.0576 -0.0917 890  GLU A O   
6523  C CB  . GLU A 892  ? 0.3378 0.3037 0.4488 0.0611  -0.0600 -0.1143 890  GLU A CB  
6524  C CG  . GLU A 892  ? 0.4551 0.4259 0.5736 0.0660  -0.0632 -0.1253 890  GLU A CG  
6525  C CD  . GLU A 892  ? 0.5092 0.4907 0.6192 0.0693  -0.0589 -0.1296 890  GLU A CD  
6526  O OE1 . GLU A 892  ? 0.6271 0.6152 0.7289 0.0701  -0.0563 -0.1314 890  GLU A OE1 
6527  O OE2 . GLU A 892  ? 0.4398 0.4236 0.5513 0.0709  -0.0581 -0.1309 890  GLU A OE2 
6528  N N   . ALA A 893  ? 0.3098 0.2728 0.4022 0.0542  -0.0503 -0.0949 891  ALA A N   
6529  C CA  . ALA A 893  ? 0.3242 0.2847 0.4085 0.0502  -0.0467 -0.0858 891  ALA A CA  
6530  C C   . ALA A 893  ? 0.3195 0.2735 0.4082 0.0474  -0.0477 -0.0794 891  ALA A C   
6531  O O   . ALA A 893  ? 0.3206 0.2694 0.4095 0.0437  -0.0481 -0.0728 891  ALA A O   
6532  C CB  . ALA A 893  ? 0.2631 0.2308 0.3359 0.0510  -0.0411 -0.0848 891  ALA A CB  
6533  N N   . LYS A 894  ? 0.2921 0.2469 0.3848 0.0492  -0.0483 -0.0815 892  LYS A N   
6534  C CA  . LYS A 894  ? 0.3364 0.2853 0.4343 0.0469  -0.0498 -0.0760 892  LYS A CA  
6535  C C   . LYS A 894  ? 0.3512 0.2930 0.4594 0.0448  -0.0550 -0.0742 892  LYS A C   
6536  O O   . LYS A 894  ? 0.3425 0.2794 0.4512 0.0410  -0.0553 -0.0665 892  LYS A O   
6537  C CB  . LYS A 894  ? 0.2792 0.2304 0.3816 0.0499  -0.0505 -0.0802 892  LYS A CB  
6538  C CG  . LYS A 894  ? 0.3200 0.2654 0.4288 0.0477  -0.0525 -0.0750 892  LYS A CG  
6539  C CD  . LYS A 894  ? 0.3482 0.2963 0.4611 0.0509  -0.0530 -0.0795 892  LYS A CD  
6540  C CE  . LYS A 894  ? 0.3820 0.3243 0.5022 0.0489  -0.0555 -0.0744 892  LYS A CE  
6541  N NZ  . LYS A 894  ? 0.5184 0.4630 0.6444 0.0522  -0.0567 -0.0794 892  LYS A NZ  
6542  N N   . ASP A 895  ? 0.3270 0.2684 0.4437 0.0473  -0.0593 -0.0812 893  ASP A N   
6543  C CA  . ASP A 895  ? 0.3855 0.3201 0.5130 0.0453  -0.0646 -0.0796 893  ASP A CA  
6544  C C   . ASP A 895  ? 0.3355 0.2677 0.4584 0.0415  -0.0636 -0.0733 893  ASP A C   
6545  O O   . ASP A 895  ? 0.3714 0.2981 0.4994 0.0379  -0.0660 -0.0669 893  ASP A O   
6546  C CB  . ASP A 895  ? 0.3570 0.2923 0.4939 0.0489  -0.0693 -0.0890 893  ASP A CB  
6547  C CG  . ASP A 895  ? 0.4696 0.4057 0.6148 0.0524  -0.0718 -0.0949 893  ASP A CG  
6548  O OD1 . ASP A 895  ? 0.5749 0.5092 0.7211 0.0513  -0.0712 -0.0907 893  ASP A OD1 
6549  O OD2 . ASP A 895  ? 0.4855 0.4244 0.6367 0.0562  -0.0746 -0.1042 893  ASP A OD2 
6550  N N   . ASN A 896  ? 0.3241 0.2608 0.4378 0.0421  -0.0603 -0.0750 894  ASN A N   
6551  C CA  . ASN A 896  ? 0.3625 0.2974 0.4718 0.0388  -0.0593 -0.0696 894  ASN A CA  
6552  C C   . ASN A 896  ? 0.3543 0.2874 0.4577 0.0349  -0.0561 -0.0603 894  ASN A C   
6553  O O   . ASN A 896  ? 0.3362 0.2653 0.4417 0.0313  -0.0574 -0.0543 894  ASN A O   
6554  C CB  . ASN A 896  ? 0.3724 0.3131 0.4728 0.0405  -0.0561 -0.0735 894  ASN A CB  
6555  C CG  . ASN A 896  ? 0.4727 0.4121 0.5674 0.0372  -0.0544 -0.0678 894  ASN A CG  
6556  O OD1 . ASN A 896  ? 0.4910 0.4324 0.5760 0.0355  -0.0498 -0.0629 894  ASN A OD1 
6557  N ND2 . ASN A 896  ? 0.4839 0.4202 0.5850 0.0361  -0.0581 -0.0684 894  ASN A ND2 
6558  N N   . ILE A 897  ? 0.3257 0.2620 0.4217 0.0356  -0.0520 -0.0592 895  ILE A N   
6559  C CA  . ILE A 897  ? 0.3141 0.2491 0.4045 0.0322  -0.0490 -0.0510 895  ILE A CA  
6560  C C   . ILE A 897  ? 0.3580 0.2878 0.4572 0.0298  -0.0525 -0.0463 895  ILE A C   
6561  O O   . ILE A 897  ? 0.3377 0.2649 0.4363 0.0260  -0.0524 -0.0392 895  ILE A O   
6562  C CB  . ILE A 897  ? 0.2847 0.2244 0.3665 0.0337  -0.0444 -0.0513 895  ILE A CB  
6563  C CG1 . ILE A 897  ? 0.2892 0.2346 0.3623 0.0356  -0.0409 -0.0548 895  ILE A CG1 
6564  C CG2 . ILE A 897  ? 0.3107 0.2489 0.3876 0.0303  -0.0417 -0.0434 895  ILE A CG2 
6565  C CD1 . ILE A 897  ? 0.2753 0.2263 0.3429 0.0384  -0.0376 -0.0577 895  ILE A CD1 
6566  N N   . GLU A 898  ? 0.3295 0.2579 0.4371 0.0320  -0.0557 -0.0502 896  GLU A N   
6567  C CA  . GLU A 898  ? 0.3509 0.2745 0.4672 0.0298  -0.0591 -0.0454 896  GLU A CA  
6568  C C   . GLU A 898  ? 0.3335 0.2525 0.4581 0.0271  -0.0636 -0.0423 896  GLU A C   
6569  O O   . GLU A 898  ? 0.3777 0.2935 0.5057 0.0235  -0.0651 -0.0351 896  GLU A O   
6570  C CB  . GLU A 898  ? 0.3707 0.2941 0.4944 0.0329  -0.0616 -0.0504 896  GLU A CB  
6571  C CG  . GLU A 898  ? 0.4036 0.3316 0.5191 0.0348  -0.0570 -0.0514 896  GLU A CG  
6572  C CD  . GLU A 898  ? 0.4552 0.3837 0.5778 0.0380  -0.0591 -0.0565 896  GLU A CD  
6573  O OE1 . GLU A 898  ? 0.4961 0.4231 0.6286 0.0404  -0.0636 -0.0624 896  GLU A OE1 
6574  O OE2 . GLU A 898  ? 0.5824 0.5129 0.7008 0.0383  -0.0563 -0.0548 896  GLU A OE2 
6575  N N   . LYS A 899  ? 0.3507 0.2696 0.4786 0.0286  -0.0658 -0.0476 897  LYS A N   
6576  C CA  . LYS A 899  ? 0.3575 0.2724 0.4930 0.0259  -0.0699 -0.0445 897  LYS A CA  
6577  C C   . LYS A 899  ? 0.3793 0.2947 0.5073 0.0217  -0.0669 -0.0365 897  LYS A C   
6578  O O   . LYS A 899  ? 0.3765 0.2887 0.5101 0.0181  -0.0695 -0.0302 897  LYS A O   
6579  C CB  . LYS A 899  ? 0.4005 0.3160 0.5397 0.0285  -0.0723 -0.0522 897  LYS A CB  
6580  N N   . HIS A 900  ? 0.3088 0.2283 0.4243 0.0221  -0.0615 -0.0365 898  HIS A N   
6581  C CA  . HIS A 900  ? 0.3552 0.2756 0.4634 0.0183  -0.0584 -0.0294 898  HIS A CA  
6582  C C   . HIS A 900  ? 0.3167 0.2362 0.4246 0.0154  -0.0576 -0.0220 898  HIS A C   
6583  O O   . HIS A 900  ? 0.3887 0.3070 0.4978 0.0116  -0.0584 -0.0152 898  HIS A O   
6584  C CB  . HIS A 900  ? 0.3231 0.2481 0.4190 0.0197  -0.0531 -0.0314 898  HIS A CB  
6585  C CG  . HIS A 900  ? 0.3334 0.2598 0.4214 0.0163  -0.0496 -0.0246 898  HIS A CG  
6586  N ND1 . HIS A 900  ? 0.3419 0.2677 0.4301 0.0136  -0.0502 -0.0212 898  HIS A ND1 
6587  C CD2 . HIS A 900  ? 0.3448 0.2732 0.4251 0.0152  -0.0456 -0.0206 898  HIS A CD2 
6588  C CE1 . HIS A 900  ? 0.3442 0.2720 0.4249 0.0111  -0.0466 -0.0158 898  HIS A CE1 
6589  N NE2 . HIS A 900  ? 0.3184 0.2477 0.3944 0.0120  -0.0439 -0.0154 898  HIS A NE2 
6590  N N   . ILE A 901  ? 0.3086 0.2291 0.4143 0.0172  -0.0560 -0.0233 899  ILE A N   
6591  C CA  . ILE A 901  ? 0.3543 0.2742 0.4597 0.0147  -0.0553 -0.0168 899  ILE A CA  
6592  C C   . ILE A 901  ? 0.3899 0.3058 0.5069 0.0121  -0.0606 -0.0124 899  ILE A C   
6593  O O   . ILE A 901  ? 0.4014 0.3172 0.5182 0.0084  -0.0605 -0.0048 899  ILE A O   
6594  C CB  . ILE A 901  ? 0.3265 0.2480 0.4295 0.0174  -0.0534 -0.0198 899  ILE A CB  
6595  C CG1 . ILE A 901  ? 0.3294 0.2554 0.4206 0.0193  -0.0480 -0.0226 899  ILE A CG1 
6596  C CG2 . ILE A 901  ? 0.3754 0.2958 0.4797 0.0150  -0.0536 -0.0134 899  ILE A CG2 
6597  C CD1 . ILE A 901  ? 0.3317 0.2599 0.4206 0.0223  -0.0461 -0.0264 899  ILE A CD1 
6598  N N   . GLU A 902  ? 0.3863 0.2992 0.5140 0.0141  -0.0653 -0.0170 900  GLU A N   
6599  C CA  . GLU A 902  ? 0.4153 0.3239 0.5552 0.0118  -0.0709 -0.0127 900  GLU A CA  
6600  C C   . GLU A 902  ? 0.3952 0.3029 0.5377 0.0081  -0.0726 -0.0074 900  GLU A C   
6601  O O   . GLU A 902  ? 0.4559 0.3622 0.6038 0.0044  -0.0750 0.0001  900  GLU A O   
6602  C CB  . GLU A 902  ? 0.4447 0.3503 0.5962 0.0152  -0.0757 -0.0196 900  GLU A CB  
6603  C CG  . GLU A 902  ? 0.4916 0.3978 0.6435 0.0179  -0.0750 -0.0225 900  GLU A CG  
6604  C CD  . GLU A 902  ? 0.5380 0.4441 0.6886 0.0148  -0.0741 -0.0144 900  GLU A CD  
6605  O OE1 . GLU A 902  ? 0.5903 0.4933 0.7497 0.0117  -0.0782 -0.0084 900  GLU A OE1 
6606  O OE2 . GLU A 902  ? 0.5714 0.4807 0.7121 0.0153  -0.0694 -0.0138 900  GLU A OE2 
6607  N N   . ARG A 903  ? 0.4042 0.3130 0.5431 0.0089  -0.0716 -0.0110 901  ARG A N   
6608  C CA  . ARG A 903  ? 0.4418 0.3506 0.5816 0.0053  -0.0724 -0.0059 901  ARG A CA  
6609  C C   . ARG A 903  ? 0.5002 0.4120 0.6321 0.0015  -0.0688 0.0024  901  ARG A C   
6610  O O   . ARG A 903  ? 0.4773 0.3887 0.6141 -0.0024 -0.0711 0.0097  901  ARG A O   
6611  C CB  . ARG A 903  ? 0.4742 0.3845 0.6092 0.0071  -0.0709 -0.0113 901  ARG A CB  
6612  N N   . MET A 904  ? 0.4563 0.3716 0.5764 0.0026  -0.0634 0.0014  902  MET A N   
6613  C CA  . MET A 904  ? 0.4565 0.3750 0.5690 -0.0006 -0.0598 0.0083  902  MET A CA  
6614  C C   . MET A 904  ? 0.4430 0.3606 0.5610 -0.0029 -0.0620 0.0145  902  MET A C   
6615  O O   . MET A 904  ? 0.4605 0.3799 0.5789 -0.0069 -0.0623 0.0219  902  MET A O   
6616  C CB  . MET A 904  ? 0.3955 0.3174 0.4958 0.0015  -0.0541 0.0054  902  MET A CB  
6617  C CG  . MET A 904  ? 0.3947 0.3183 0.4884 0.0035  -0.0515 0.0004  902  MET A CG  
6618  S SD  . MET A 904  ? 0.5540 0.4795 0.6453 0.0001  -0.0508 0.0049  902  MET A SD  
6619  C CE  . MET A 904  ? 0.5325 0.4544 0.6342 0.0009  -0.0561 0.0011  902  MET A CE  
6620  N N   . ARG A 905  ? 0.4227 0.3382 0.5451 -0.0006 -0.0636 0.0115  903  ARG A N   
6621  C CA  . ARG A 905  ? 0.4201 0.3346 0.5483 -0.0027 -0.0659 0.0172  903  ARG A CA  
6622  C C   . ARG A 905  ? 0.5172 0.4291 0.6573 -0.0057 -0.0715 0.0223  903  ARG A C   
6623  O O   . ARG A 905  ? 0.4568 0.3699 0.5994 -0.0094 -0.0727 0.0302  903  ARG A O   
6624  C CB  . ARG A 905  ? 0.4605 0.3729 0.5921 0.0008  -0.0669 0.0123  903  ARG A CB  
6625  C CG  . ARG A 905  ? 0.4991 0.4115 0.6335 -0.0011 -0.0679 0.0180  903  ARG A CG  
6626  C CD  . ARG A 905  ? 0.4854 0.3951 0.6263 0.0023  -0.0702 0.0132  903  ARG A CD  
6627  N NE  . ARG A 905  ? 0.4769 0.3881 0.6107 0.0065  -0.0666 0.0052  903  ARG A NE  
6628  C CZ  . ARG A 905  ? 0.4946 0.4088 0.6196 0.0075  -0.0622 0.0048  903  ARG A CZ  
6629  N NH1 . ARG A 905  ? 0.4580 0.3739 0.5794 0.0047  -0.0606 0.0114  903  ARG A NH1 
6630  N NH2 . ARG A 905  ? 0.4919 0.4076 0.6116 0.0114  -0.0594 -0.0024 903  ARG A NH2 
6631  N N   . GLY A 906  ? 0.4620 0.3707 0.6096 -0.0043 -0.0751 0.0179  904  GLY A N   
6632  C CA  . GLY A 906  ? 0.5415 0.4474 0.7015 -0.0071 -0.0808 0.0224  904  GLY A CA  
6633  C C   . GLY A 906  ? 0.5511 0.4601 0.7084 -0.0116 -0.0799 0.0297  904  GLY A C   
6634  O O   . GLY A 906  ? 0.6020 0.5098 0.7691 -0.0149 -0.0843 0.0357  904  GLY A O   
6635  N N   . LEU A 907  ? 0.5266 0.4398 0.6715 -0.0117 -0.0745 0.0293  905  LEU A N   
6636  C CA  . LEU A 907  ? 0.5122 0.4294 0.6534 -0.0158 -0.0731 0.0359  905  LEU A CA  
6637  C C   . LEU A 907  ? 0.5145 0.4363 0.6502 -0.0188 -0.0705 0.0432  905  LEU A C   
6638  O O   . LEU A 907  ? 0.5490 0.4752 0.6811 -0.0222 -0.0690 0.0489  905  LEU A O   
6639  C CB  . LEU A 907  ? 0.5355 0.4550 0.6670 -0.0143 -0.0689 0.0314  905  LEU A CB  
6640  C CG  . LEU A 907  ? 0.5928 0.5088 0.7294 -0.0117 -0.0714 0.0246  905  LEU A CG  
6641  C CD1 . LEU A 907  ? 0.6268 0.5457 0.7535 -0.0105 -0.0672 0.0209  905  LEU A CD1 
6642  C CD2 . LEU A 907  ? 0.6153 0.5287 0.7648 -0.0144 -0.0773 0.0285  905  LEU A CD2 
6643  N N   . GLY A 908  ? 0.4888 0.4100 0.6237 -0.0176 -0.0699 0.0431  906  GLY A N   
6644  C CA  . GLY A 908  ? 0.5135 0.4391 0.6432 -0.0203 -0.0677 0.0495  906  GLY A CA  
6645  C C   . GLY A 908  ? 0.4051 0.3345 0.5212 -0.0187 -0.0615 0.0468  906  GLY A C   
6646  O O   . GLY A 908  ? 0.4574 0.3908 0.5687 -0.0207 -0.0594 0.0515  906  GLY A O   
6647  N N   . ARG A 909  ? 0.4321 0.3605 0.5424 -0.0153 -0.0587 0.0394  907  ARG A N   
6648  C CA  . ARG A 909  ? 0.3839 0.3156 0.4819 -0.0139 -0.0531 0.0369  907  ARG A CA  
6649  C C   . ARG A 909  ? 0.4016 0.3326 0.4979 -0.0121 -0.0520 0.0357  907  ARG A C   
6650  O O   . ARG A 909  ? 0.4215 0.3487 0.5247 -0.0100 -0.0549 0.0328  907  ARG A O   
6651  C CB  . ARG A 909  ? 0.4075 0.3382 0.5007 -0.0106 -0.0508 0.0296  907  ARG A CB  
6652  C CG  . ARG A 909  ? 0.4142 0.3448 0.5101 -0.0118 -0.0523 0.0297  907  ARG A CG  
6653  C CD  . ARG A 909  ? 0.4623 0.3979 0.5527 -0.0153 -0.0500 0.0352  907  ARG A CD  
6654  N NE  . ARG A 909  ? 0.4821 0.4180 0.5731 -0.0158 -0.0504 0.0342  907  ARG A NE  
6655  C CZ  . ARG A 909  ? 0.6161 0.5520 0.7146 -0.0187 -0.0539 0.0384  907  ARG A CZ  
6656  N NH1 . ARG A 909  ? 0.5787 0.5143 0.6852 -0.0214 -0.0574 0.0445  907  ARG A NH1 
6657  N NH2 . ARG A 909  ? 0.5679 0.5042 0.6663 -0.0188 -0.0539 0.0369  907  ARG A NH2 
6658  N N   . LYS A 910  ? 0.3324 0.2676 0.4201 -0.0129 -0.0480 0.0377  908  LYS A N   
6659  C CA  . LYS A 910  ? 0.3557 0.2908 0.4411 -0.0115 -0.0467 0.0368  908  LYS A CA  
6660  C C   . LYS A 910  ? 0.3831 0.3161 0.4648 -0.0070 -0.0445 0.0290  908  LYS A C   
6661  O O   . LYS A 910  ? 0.3408 0.2753 0.4152 -0.0057 -0.0413 0.0256  908  LYS A O   
6662  C CB  . LYS A 910  ? 0.4167 0.3570 0.4939 -0.0135 -0.0431 0.0408  908  LYS A CB  
6663  C CG  . LYS A 910  ? 0.4419 0.3853 0.5231 -0.0177 -0.0453 0.0489  908  LYS A CG  
6664  C CD  . LYS A 910  ? 0.5061 0.4550 0.5791 -0.0192 -0.0417 0.0518  908  LYS A CD  
6665  C CE  . LYS A 910  ? 0.4886 0.4364 0.5580 -0.0166 -0.0397 0.0483  908  LYS A CE  
6666  N NZ  . LYS A 910  ? 0.5844 0.5375 0.6476 -0.0184 -0.0371 0.0517  908  LYS A NZ  
6667  N N   . VAL A 911  ? 0.3479 0.2780 0.4346 -0.0048 -0.0464 0.0262  909  VAL A N   
6668  C CA  . VAL A 911  ? 0.3254 0.2541 0.4100 -0.0005 -0.0450 0.0187  909  VAL A CA  
6669  C C   . VAL A 911  ? 0.3424 0.2719 0.4246 0.0007  -0.0434 0.0184  909  VAL A C   
6670  O O   . VAL A 911  ? 0.3627 0.2906 0.4514 0.0000  -0.0462 0.0210  909  VAL A O   
6671  C CB  . VAL A 911  ? 0.3647 0.2894 0.4589 0.0016  -0.0493 0.0143  909  VAL A CB  
6672  C CG1 . VAL A 911  ? 0.3894 0.3138 0.4813 0.0061  -0.0477 0.0066  909  VAL A CG1 
6673  C CG2 . VAL A 911  ? 0.3745 0.2984 0.4709 0.0005  -0.0509 0.0143  909  VAL A CG2 
6674  N N   . GLU A 912  ? 0.3349 0.2667 0.4081 0.0024  -0.0389 0.0155  910  GLU A N   
6675  C CA  . GLU A 912  ? 0.3369 0.2698 0.4071 0.0039  -0.0369 0.0145  910  GLU A CA  
6676  C C   . GLU A 912  ? 0.3597 0.2920 0.4295 0.0081  -0.0361 0.0073  910  GLU A C   
6677  O O   . GLU A 912  ? 0.3240 0.2574 0.3892 0.0095  -0.0341 0.0037  910  GLU A O   
6678  C CB  . GLU A 912  ? 0.3453 0.2820 0.4058 0.0025  -0.0325 0.0168  910  GLU A CB  
6679  C CG  . GLU A 912  ? 0.3642 0.3022 0.4217 0.0035  -0.0305 0.0167  910  GLU A CG  
6680  C CD  . GLU A 912  ? 0.4208 0.3588 0.4825 0.0010  -0.0327 0.0221  910  GLU A CD  
6681  O OE1 . GLU A 912  ? 0.4081 0.3461 0.4734 -0.0019 -0.0350 0.0267  910  GLU A OE1 
6682  O OE2 . GLU A 912  ? 0.3933 0.3316 0.4549 0.0019  -0.0321 0.0219  910  GLU A OE2 
6683  N N   . GLN A 913  ? 0.3430 0.2742 0.4177 0.0100  -0.0376 0.0052  911  GLN A N   
6684  C CA  . GLN A 913  ? 0.3074 0.2390 0.3821 0.0141  -0.0369 -0.0018 911  GLN A CA  
6685  C C   . GLN A 913  ? 0.3863 0.3192 0.4600 0.0155  -0.0355 -0.0024 911  GLN A C   
6686  O O   . GLN A 913  ? 0.3851 0.3168 0.4632 0.0140  -0.0374 0.0013  911  GLN A O   
6687  C CB  . GLN A 913  ? 0.3331 0.2618 0.4178 0.0159  -0.0415 -0.0058 911  GLN A CB  
6688  C CG  . GLN A 913  ? 0.3423 0.2696 0.4286 0.0151  -0.0431 -0.0063 911  GLN A CG  
6689  C CD  . GLN A 913  ? 0.3809 0.3056 0.4768 0.0175  -0.0474 -0.0115 911  GLN A CD  
6690  O OE1 . GLN A 913  ? 0.4290 0.3508 0.5344 0.0173  -0.0515 -0.0106 911  GLN A OE1 
6691  N NE2 . GLN A 913  ? 0.3499 0.2760 0.4437 0.0199  -0.0466 -0.0172 911  GLN A NE2 
6692  N N   . ILE A 914  ? 0.3642 0.3000 0.4323 0.0182  -0.0323 -0.0068 912  ILE A N   
6693  C CA  . ILE A 914  ? 0.3479 0.2854 0.4157 0.0199  -0.0310 -0.0081 912  ILE A CA  
6694  C C   . ILE A 914  ? 0.3831 0.3188 0.4602 0.0224  -0.0347 -0.0121 912  ILE A C   
6695  O O   . ILE A 914  ? 0.3714 0.3060 0.4534 0.0241  -0.0372 -0.0163 912  ILE A O   
6696  C CB  . ILE A 914  ? 0.4441 0.3857 0.5037 0.0220  -0.0266 -0.0114 912  ILE A CB  
6697  N N   . GLY A 915  ? 0.3871 0.3227 0.4674 0.0227  -0.0354 -0.0110 913  GLY A N   
6698  C CA  . GLY A 915  ? 0.4149 0.3493 0.5043 0.0254  -0.0387 -0.0152 913  GLY A CA  
6699  C C   . GLY A 915  ? 0.4135 0.3520 0.5001 0.0294  -0.0364 -0.0221 913  GLY A C   
6700  O O   . GLY A 915  ? 0.4545 0.3967 0.5337 0.0298  -0.0324 -0.0218 913  GLY A O   
6701  N N   . LEU A 916  ? 0.3726 0.3110 0.4657 0.0324  -0.0391 -0.0282 914  LEU A N   
6702  C CA  . LEU A 916  ? 0.4101 0.3535 0.5011 0.0363  -0.0371 -0.0353 914  LEU A CA  
6703  C C   . LEU A 916  ? 0.4380 0.3827 0.5348 0.0388  -0.0383 -0.0382 914  LEU A C   
6704  O O   . LEU A 916  ? 0.4332 0.3740 0.5392 0.0386  -0.0424 -0.0375 914  LEU A O   
6705  C CB  . LEU A 916  ? 0.4006 0.3440 0.4954 0.0385  -0.0394 -0.0412 914  LEU A CB  
6706  C CG  . LEU A 916  ? 0.3914 0.3342 0.4803 0.0366  -0.0381 -0.0393 914  LEU A CG  
6707  C CD1 . LEU A 916  ? 0.4160 0.3598 0.5084 0.0392  -0.0401 -0.0460 914  LEU A CD1 
6708  C CD2 . LEU A 916  ? 0.4326 0.3795 0.5099 0.0358  -0.0327 -0.0370 914  LEU A CD2 
6709  N N   . ALA A 917  ? 0.3760 0.3263 0.4675 0.0412  -0.0348 -0.0414 915  ALA A N   
6710  C CA  . ALA A 917  ? 0.4137 0.3664 0.5103 0.0439  -0.0355 -0.0449 915  ALA A CA  
6711  C C   . ALA A 917  ? 0.4024 0.3556 0.5080 0.0475  -0.0393 -0.0526 915  ALA A C   
6712  O O   . ALA A 917  ? 0.4075 0.3615 0.5128 0.0486  -0.0399 -0.0565 915  ALA A O   
6713  C CB  . ALA A 917  ? 0.4283 0.3879 0.5169 0.0454  -0.0307 -0.0463 915  ALA A CB  
6714  N N   . SER A 918  ? 0.4094 0.3622 0.5235 0.0495  -0.0419 -0.0551 916  SER A N   
6715  C CA  . SER A 918  ? 0.4248 0.3781 0.5487 0.0532  -0.0458 -0.0630 916  SER A CA  
6716  C C   . SER A 918  ? 0.4115 0.3727 0.5310 0.0569  -0.0433 -0.0706 916  SER A C   
6717  O O   . SER A 918  ? 0.3962 0.3581 0.5213 0.0596  -0.0460 -0.0773 916  SER A O   
6718  C CB  . SER A 918  ? 0.3979 0.3502 0.5314 0.0548  -0.0488 -0.0645 916  SER A CB  
6719  O OG  . SER A 918  ? 0.5109 0.4690 0.6393 0.0561  -0.0450 -0.0650 916  SER A OG  
6720  N N   . GLU A 919  ? 0.4005 0.3677 0.5101 0.0570  -0.0381 -0.0696 917  GLU A N   
6721  C CA  . GLU A 919  ? 0.3808 0.3567 0.4856 0.0603  -0.0353 -0.0759 917  GLU A CA  
6722  C C   . GLU A 919  ? 0.3905 0.3665 0.4918 0.0601  -0.0353 -0.0777 917  GLU A C   
6723  O O   . GLU A 919  ? 0.3922 0.3750 0.4921 0.0633  -0.0345 -0.0843 917  GLU A O   
6724  C CB  . GLU A 919  ? 0.3973 0.3791 0.4922 0.0597  -0.0299 -0.0727 917  GLU A CB  
6725  C CG  . GLU A 919  ? 0.4852 0.4701 0.5830 0.0612  -0.0293 -0.0734 917  GLU A CG  
6726  C CD  . GLU A 919  ? 0.5824 0.5608 0.6818 0.0579  -0.0301 -0.0661 917  GLU A CD  
6727  O OE1 . GLU A 919  ? 0.5522 0.5233 0.6525 0.0547  -0.0320 -0.0612 917  GLU A OE1 
6728  O OE2 . GLU A 919  ? 0.6772 0.6582 0.7769 0.0584  -0.0287 -0.0652 917  GLU A OE2 
6729  N N   . THR A 920  ? 0.3799 0.3493 0.4797 0.0565  -0.0362 -0.0720 918  THR A N   
6730  C CA  . THR A 920  ? 0.3778 0.3471 0.4747 0.0563  -0.0364 -0.0736 918  THR A CA  
6731  C C   . THR A 920  ? 0.3489 0.3168 0.4557 0.0589  -0.0412 -0.0808 918  THR A C   
6732  O O   . THR A 920  ? 0.3283 0.2981 0.4333 0.0598  -0.0414 -0.0842 918  THR A O   
6733  C CB  . THR A 920  ? 0.3395 0.3024 0.4326 0.0517  -0.0361 -0.0656 918  THR A CB  
6734  O OG1 . THR A 920  ? 0.3729 0.3284 0.4747 0.0498  -0.0403 -0.0623 918  THR A OG1 
6735  C CG2 . THR A 920  ? 0.3282 0.2929 0.4115 0.0493  -0.0313 -0.0593 918  THR A CG2 
6736  N N   . GLY A 921  ? 0.3776 0.3427 0.4953 0.0604  -0.0453 -0.0833 919  GLY A N   
6737  C CA  . GLY A 921  ? 0.3756 0.3388 0.5040 0.0629  -0.0504 -0.0903 919  GLY A CA  
6738  C C   . GLY A 921  ? 0.3484 0.3199 0.4760 0.0674  -0.0498 -0.0999 919  GLY A C   
6739  O O   . GLY A 921  ? 0.3916 0.3621 0.5256 0.0691  -0.0534 -0.1055 919  GLY A O   
6740  N N   . VAL A 922  ? 0.3640 0.3443 0.4841 0.0693  -0.0453 -0.1019 920  VAL A N   
6741  C CA  . VAL A 922  ? 0.3054 0.2951 0.4239 0.0735  -0.0444 -0.1108 920  VAL A CA  
6742  C C   . VAL A 922  ? 0.3414 0.3339 0.4509 0.0725  -0.0419 -0.1101 920  VAL A C   
6743  O O   . VAL A 922  ? 0.3435 0.3437 0.4519 0.0757  -0.0416 -0.1174 920  VAL A O   
6744  C CB  . VAL A 922  ? 0.3206 0.3198 0.4353 0.0761  -0.0408 -0.1134 920  VAL A CB  
6745  C CG1 . VAL A 922  ? 0.3622 0.3599 0.4875 0.0781  -0.0439 -0.1165 920  VAL A CG1 
6746  C CG2 . VAL A 922  ? 0.3363 0.3365 0.4399 0.0728  -0.0355 -0.1048 920  VAL A CG2 
6747  N N   . GLY A 923  ? 0.2961 0.2831 0.3993 0.0682  -0.0402 -0.1017 921  GLY A N   
6748  C CA  . GLY A 923  ? 0.3116 0.3002 0.4070 0.0670  -0.0381 -0.1005 921  GLY A CA  
6749  C C   . GLY A 923  ? 0.2798 0.2593 0.3783 0.0639  -0.0411 -0.0966 921  GLY A C   
6750  O O   . GLY A 923  ? 0.3184 0.2909 0.4266 0.0632  -0.0455 -0.0961 921  GLY A O   
6751  N N   . THR A 924  ? 0.2779 0.2577 0.3689 0.0620  -0.0390 -0.0937 922  THR A N   
6752  C CA  . THR A 924  ? 0.2865 0.2585 0.3796 0.0589  -0.0415 -0.0898 922  THR A CA  
6753  C C   . THR A 924  ? 0.2963 0.2654 0.3809 0.0547  -0.0379 -0.0804 922  THR A C   
6754  O O   . THR A 924  ? 0.2917 0.2645 0.3671 0.0540  -0.0344 -0.0786 922  THR A O   
6755  C CB  . THR A 924  ? 0.2698 0.2444 0.3624 0.0604  -0.0426 -0.0950 922  THR A CB  
6756  O OG1 . THR A 924  ? 0.2683 0.2513 0.3506 0.0616  -0.0381 -0.0961 922  THR A OG1 
6757  C CG2 . THR A 924  ? 0.3170 0.2931 0.4201 0.0643  -0.0472 -0.1043 922  THR A CG2 
6758  N N   . PHE A 925  ? 0.2752 0.2380 0.3632 0.0519  -0.0391 -0.0745 923  PHE A N   
6759  C CA  . PHE A 925  ? 0.2591 0.2194 0.3398 0.0481  -0.0360 -0.0659 923  PHE A CA  
6760  C C   . PHE A 925  ? 0.2617 0.2143 0.3465 0.0445  -0.0389 -0.0607 923  PHE A C   
6761  O O   . PHE A 925  ? 0.3125 0.2606 0.4073 0.0445  -0.0435 -0.0618 923  PHE A O   
6762  C CB  . PHE A 925  ? 0.2330 0.1936 0.3128 0.0476  -0.0343 -0.0627 923  PHE A CB  
6763  C CG  . PHE A 925  ? 0.2681 0.2367 0.3427 0.0503  -0.0307 -0.0660 923  PHE A CG  
6764  C CD1 . PHE A 925  ? 0.2658 0.2388 0.3459 0.0543  -0.0322 -0.0733 923  PHE A CD1 
6765  C CD2 . PHE A 925  ? 0.2509 0.2229 0.3156 0.0490  -0.0260 -0.0619 923  PHE A CD2 
6766  C CE1 . PHE A 925  ? 0.2737 0.2549 0.3490 0.0567  -0.0289 -0.0762 923  PHE A CE1 
6767  C CE2 . PHE A 925  ? 0.2547 0.2345 0.3150 0.0513  -0.0228 -0.0645 923  PHE A CE2 
6768  C CZ  . PHE A 925  ? 0.2431 0.2277 0.3084 0.0551  -0.0242 -0.0715 923  PHE A CZ  
6769  N N   . VAL A 926  ? 0.2558 0.2074 0.3330 0.0414  -0.0361 -0.0549 924  VAL A N   
6770  C CA  . VAL A 926  ? 0.2647 0.2103 0.3438 0.0375  -0.0378 -0.0485 924  VAL A CA  
6771  C C   . VAL A 926  ? 0.2672 0.2127 0.3395 0.0348  -0.0344 -0.0417 924  VAL A C   
6772  O O   . VAL A 926  ? 0.2850 0.2345 0.3486 0.0349  -0.0302 -0.0409 924  VAL A O   
6773  C CB  . VAL A 926  ? 0.2790 0.2240 0.3555 0.0364  -0.0379 -0.0484 924  VAL A CB  
6774  C CG1 . VAL A 926  ? 0.2955 0.2356 0.3727 0.0321  -0.0389 -0.0411 924  VAL A CG1 
6775  C CG2 . VAL A 926  ? 0.2971 0.2419 0.3812 0.0390  -0.0419 -0.0553 924  VAL A CG2 
6776  N N   . PRO A 927  ? 0.2755 0.2170 0.3520 0.0324  -0.0360 -0.0367 925  PRO A N   
6777  C CA  . PRO A 927  ? 0.2959 0.2378 0.3660 0.0299  -0.0328 -0.0306 925  PRO A CA  
6778  C C   . PRO A 927  ? 0.2940 0.2358 0.3572 0.0271  -0.0306 -0.0264 925  PRO A C   
6779  O O   . PRO A 927  ? 0.2934 0.2327 0.3593 0.0257  -0.0327 -0.0255 925  PRO A O   
6780  C CB  . PRO A 927  ? 0.3486 0.2862 0.4262 0.0279  -0.0361 -0.0264 925  PRO A CB  
6781  C CG  . PRO A 927  ? 0.3566 0.2905 0.4431 0.0278  -0.0408 -0.0281 925  PRO A CG  
6782  C CD  . PRO A 927  ? 0.3411 0.2777 0.4285 0.0316  -0.0411 -0.0360 925  PRO A CD  
6783  N N   . PRO A 928  ? 0.2985 0.2431 0.3532 0.0264  -0.0264 -0.0241 926  PRO A N   
6784  C CA  . PRO A 928  ? 0.2849 0.2292 0.3336 0.0235  -0.0244 -0.0196 926  PRO A CA  
6785  C C   . PRO A 928  ? 0.2661 0.2065 0.3192 0.0202  -0.0270 -0.0145 926  PRO A C   
6786  O O   . PRO A 928  ? 0.2817 0.2204 0.3391 0.0192  -0.0287 -0.0119 926  PRO A O   
6787  C CB  . PRO A 928  ? 0.2671 0.2143 0.3086 0.0232  -0.0204 -0.0173 926  PRO A CB  
6788  C CG  . PRO A 928  ? 0.2950 0.2457 0.3364 0.0266  -0.0194 -0.0223 926  PRO A CG  
6789  C CD  . PRO A 928  ? 0.2941 0.2427 0.3445 0.0283  -0.0234 -0.0256 926  PRO A CD  
6790  N N   . THR A 929  ? 0.2806 0.2201 0.3328 0.0185  -0.0275 -0.0129 927  THR A N   
6791  C CA  . THR A 929  ? 0.2900 0.2264 0.3476 0.0155  -0.0306 -0.0087 927  THR A CA  
6792  C C   . THR A 929  ? 0.3007 0.2383 0.3523 0.0127  -0.0284 -0.0045 927  THR A C   
6793  O O   . THR A 929  ? 0.2727 0.2120 0.3189 0.0135  -0.0262 -0.0066 927  THR A O   
6794  C CB  . THR A 929  ? 0.3092 0.2432 0.3744 0.0167  -0.0345 -0.0121 927  THR A CB  
6795  O OG1 . THR A 929  ? 0.3039 0.2371 0.3753 0.0195  -0.0368 -0.0166 927  THR A OG1 
6796  C CG2 . THR A 929  ? 0.2931 0.2241 0.3643 0.0133  -0.0379 -0.0071 927  THR A CG2 
6797  N N   . ILE A 930  ? 0.2805 0.2175 0.3330 0.0095  -0.0290 0.0012  928  ILE A N   
6798  C CA  . ILE A 930  ? 0.2943 0.2328 0.3425 0.0066  -0.0275 0.0053  928  ILE A CA  
6799  C C   . ILE A 930  ? 0.2959 0.2325 0.3511 0.0041  -0.0313 0.0088  928  ILE A C   
6800  O O   . ILE A 930  ? 0.3391 0.2739 0.4006 0.0030  -0.0342 0.0115  928  ILE A O   
6801  C CB  . ILE A 930  ? 0.2533 0.1941 0.2962 0.0049  -0.0248 0.0093  928  ILE A CB  
6802  C CG1 . ILE A 930  ? 0.3016 0.2443 0.3381 0.0072  -0.0212 0.0062  928  ILE A CG1 
6803  C CG2 . ILE A 930  ? 0.3346 0.2775 0.3740 0.0018  -0.0237 0.0134  928  ILE A CG2 
6804  C CD1 . ILE A 930  ? 0.3252 0.2698 0.3580 0.0059  -0.0191 0.0094  928  ILE A CD1 
6805  N N   . ILE A 931  ? 0.2773 0.2142 0.3317 0.0032  -0.0314 0.0088  929  ILE A N   
6806  C CA  . ILE A 931  ? 0.3081 0.2435 0.3691 0.0007  -0.0349 0.0121  929  ILE A CA  
6807  C C   . ILE A 931  ? 0.3401 0.2787 0.3961 -0.0023 -0.0329 0.0165  929  ILE A C   
6808  O O   . ILE A 931  ? 0.3281 0.2685 0.3780 -0.0016 -0.0302 0.0144  929  ILE A O   
6809  C CB  . ILE A 931  ? 0.3314 0.2644 0.3972 0.0025  -0.0375 0.0076  929  ILE A CB  
6810  C CG1 . ILE A 931  ? 0.3237 0.2542 0.3948 0.0058  -0.0395 0.0025  929  ILE A CG1 
6811  C CG2 . ILE A 931  ? 0.3303 0.2620 0.4032 -0.0004 -0.0411 0.0115  929  ILE A CG2 
6812  C CD1 . ILE A 931  ? 0.3446 0.2730 0.4216 0.0076  -0.0426 -0.0023 929  ILE A CD1 
6813  N N   . GLU A 932  ? 0.3310 0.2708 0.3897 -0.0056 -0.0343 0.0225  930  GLU A N   
6814  C CA  . GLU A 932  ? 0.3426 0.2864 0.3970 -0.0086 -0.0325 0.0267  930  GLU A CA  
6815  C C   . GLU A 932  ? 0.2990 0.2423 0.3583 -0.0103 -0.0351 0.0283  930  GLU A C   
6816  O O   . GLU A 932  ? 0.3503 0.2918 0.4180 -0.0119 -0.0391 0.0313  930  GLU A O   
6817  C CB  . GLU A 932  ? 0.3241 0.2707 0.3784 -0.0113 -0.0325 0.0324  930  GLU A CB  
6818  C CG  . GLU A 932  ? 0.3566 0.3043 0.4049 -0.0097 -0.0294 0.0308  930  GLU A CG  
6819  C CD  . GLU A 932  ? 0.4385 0.3885 0.4880 -0.0120 -0.0300 0.0357  930  GLU A CD  
6820  O OE1 . GLU A 932  ? 0.3884 0.3424 0.4370 -0.0151 -0.0299 0.0406  930  GLU A OE1 
6821  O OE2 . GLU A 932  ? 0.4252 0.3733 0.4763 -0.0105 -0.0305 0.0347  930  GLU A OE2 
6822  N N   . LEU A 933  ? 0.3186 0.2635 0.3734 -0.0099 -0.0330 0.0263  931  LEU A N   
6823  C CA  . LEU A 933  ? 0.3223 0.2670 0.3811 -0.0113 -0.0352 0.0273  931  LEU A CA  
6824  C C   . LEU A 933  ? 0.4328 0.3825 0.4895 -0.0150 -0.0341 0.0329  931  LEU A C   
6825  O O   . LEU A 933  ? 0.4101 0.3637 0.4603 -0.0157 -0.0310 0.0344  931  LEU A O   
6826  C CB  . LEU A 933  ? 0.3568 0.3005 0.4120 -0.0087 -0.0337 0.0216  931  LEU A CB  
6827  C CG  . LEU A 933  ? 0.4270 0.3670 0.4839 -0.0049 -0.0346 0.0153  931  LEU A CG  
6828  C CD1 . LEU A 933  ? 0.4414 0.3816 0.4950 -0.0029 -0.0333 0.0107  931  LEU A CD1 
6829  C CD2 . LEU A 933  ? 0.4212 0.3573 0.4884 -0.0050 -0.0395 0.0154  931  LEU A CD2 
6830  N N   . GLU A 934  ? 0.4049 0.3547 0.4674 -0.0172 -0.0370 0.0357  932  GLU A N   
6831  C CA  . GLU A 934  ? 0.4954 0.4506 0.5565 -0.0206 -0.0362 0.0408  932  GLU A CA  
6832  C C   . GLU A 934  ? 0.5433 0.5005 0.5985 -0.0197 -0.0334 0.0376  932  GLU A C   
6833  O O   . GLU A 934  ? 0.5607 0.5230 0.6098 -0.0209 -0.0303 0.0391  932  GLU A O   
6834  C CB  . GLU A 934  ? 0.5208 0.4755 0.5915 -0.0237 -0.0407 0.0459  932  GLU A CB  
6835  N N   . LYS A 935  ? 0.5079 0.4613 0.5649 -0.0175 -0.0345 0.0331  933  LYS A N   
6836  C CA  . LYS A 935  ? 0.5602 0.5151 0.6121 -0.0165 -0.0321 0.0299  933  LYS A CA  
6837  C C   . LYS A 935  ? 0.5956 0.5463 0.6461 -0.0125 -0.0318 0.0231  933  LYS A C   
6838  O O   . LYS A 935  ? 0.5728 0.5194 0.6283 -0.0109 -0.0344 0.0208  933  LYS A O   
6839  C CB  . LYS A 935  ? 0.5918 0.5481 0.6483 -0.0189 -0.0342 0.0326  933  LYS A CB  
6840  N N   . LEU A 936  ? 0.5602 0.5125 0.6041 -0.0109 -0.0287 0.0199  934  LEU A N   
6841  C CA  . LEU A 936  ? 0.5847 0.5343 0.6264 -0.0073 -0.0282 0.0137  934  LEU A CA  
6842  C C   . LEU A 936  ? 0.6098 0.5563 0.6581 -0.0065 -0.0318 0.0112  934  LEU A C   
6843  O O   . LEU A 936  ? 0.5881 0.5321 0.6369 -0.0035 -0.0324 0.0061  934  LEU A O   
6844  C CB  . LEU A 936  ? 0.5629 0.5152 0.5968 -0.0061 -0.0245 0.0116  934  LEU A CB  
6845  C CG  . LEU A 936  ? 0.6111 0.5628 0.6392 -0.0029 -0.0218 0.0076  934  LEU A CG  
6846  C CD1 . LEU A 936  ? 0.5166 0.4714 0.5378 -0.0025 -0.0184 0.0068  934  LEU A CD1 
6847  C CD2 . LEU A 936  ? 0.5413 0.4900 0.5717 0.0000  -0.0235 0.0025  934  LEU A CD2 
6848  N N   . SER A 937  ? 0.6346 0.5816 0.6882 -0.0092 -0.0342 0.0146  935  SER A N   
6849  C CA  . SER A 937  ? 0.6119 0.5558 0.6730 -0.0088 -0.0381 0.0125  935  SER A CA  
6850  C C   . SER A 937  ? 0.5901 0.5299 0.6591 -0.0081 -0.0419 0.0117  935  SER A C   
6851  O O   . SER A 937  ? 0.6347 0.5714 0.7104 -0.0071 -0.0454 0.0087  935  SER A O   
6852  C CB  . SER A 937  ? 0.6334 0.5793 0.6986 -0.0123 -0.0398 0.0171  935  SER A CB  
6853  O OG  . SER A 937  ? 0.6170 0.5656 0.6833 -0.0156 -0.0397 0.0236  935  SER A OG  
6854  N N   . ASP A 938  ? 0.6023 0.5419 0.6711 -0.0084 -0.0414 0.0139  936  ASP A N   
6855  C CA  . ASP A 938  ? 0.6002 0.5358 0.6763 -0.0073 -0.0448 0.0126  936  ASP A CA  
6856  C C   . ASP A 938  ? 0.6188 0.5522 0.6940 -0.0030 -0.0448 0.0050  936  ASP A C   
6857  O O   . ASP A 938  ? 0.6010 0.5310 0.6837 -0.0016 -0.0483 0.0024  936  ASP A O   
6858  C CB  . ASP A 938  ? 0.6340 0.5704 0.7090 -0.0085 -0.0439 0.0165  936  ASP A CB  
6859  C CG  . ASP A 938  ? 0.6568 0.5961 0.7336 -0.0128 -0.0444 0.0243  936  ASP A CG  
6860  O OD1 . ASP A 938  ? 0.6596 0.6002 0.7392 -0.0150 -0.0457 0.0267  936  ASP A OD1 
6861  O OD2 . ASP A 938  ? 0.6101 0.5510 0.6856 -0.0141 -0.0435 0.0279  936  ASP A OD2 
6862  N N   . LEU A 939  ? 0.5626 0.4981 0.6291 -0.0009 -0.0410 0.0014  937  LEU A N   
6863  C CA  . LEU A 939  ? 0.5592 0.4940 0.6242 0.0032  -0.0407 -0.0056 937  LEU A CA  
6864  C C   . LEU A 939  ? 0.5795 0.5139 0.6463 0.0043  -0.0423 -0.0096 937  LEU A C   
6865  O O   . LEU A 939  ? 0.6088 0.5451 0.6729 0.0028  -0.0412 -0.0077 937  LEU A O   
6866  C CB  . LEU A 939  ? 0.5399 0.4775 0.5947 0.0049  -0.0358 -0.0070 937  LEU A CB  
6867  C CG  . LEU A 939  ? 0.4928 0.4309 0.5451 0.0043  -0.0340 -0.0041 937  LEU A CG  
6868  C CD1 . LEU A 939  ? 0.4837 0.4242 0.5277 0.0068  -0.0300 -0.0070 937  LEU A CD1 
6869  C CD2 . LEU A 939  ? 0.4958 0.4308 0.5559 0.0050  -0.0374 -0.0049 937  LEU A CD2 
6870  N N   . GLN A 940  ? 0.5321 0.4646 0.6038 0.0071  -0.0449 -0.0153 938  GLN A N   
6871  C CA  . GLN A 940  ? 0.5215 0.4541 0.5951 0.0087  -0.0466 -0.0200 938  GLN A CA  
6872  C C   . GLN A 940  ? 0.5509 0.4867 0.6165 0.0121  -0.0434 -0.0254 938  GLN A C   
6873  O O   . GLN A 940  ? 0.6229 0.5613 0.6812 0.0118  -0.0404 -0.0246 938  GLN A O   
6874  C CB  . GLN A 940  ? 0.5800 0.5090 0.6647 0.0097  -0.0520 -0.0234 938  GLN A CB  
6875  N N   . ARG A 941  ? 0.5296 0.4654 0.5965 0.0154  -0.0441 -0.0307 939  ARG A N   
6876  C CA  . ARG A 941  ? 0.4590 0.3986 0.5190 0.0187  -0.0414 -0.0358 939  ARG A CA  
6877  C C   . ARG A 941  ? 0.3822 0.3234 0.4369 0.0197  -0.0382 -0.0351 939  ARG A C   
6878  O O   . ARG A 941  ? 0.4234 0.3625 0.4806 0.0183  -0.0386 -0.0316 939  ARG A O   
6879  C CB  . ARG A 941  ? 0.4630 0.4028 0.5284 0.0219  -0.0446 -0.0433 939  ARG A CB  
6880  N N   . GLU A 942  ? 0.3558 0.3011 0.4032 0.0221  -0.0351 -0.0381 940  GLU A N   
6881  C CA  . GLU A 942  ? 0.3757 0.3232 0.4181 0.0235  -0.0321 -0.0381 940  GLU A CA  
6882  C C   . GLU A 942  ? 0.3195 0.2655 0.3684 0.0251  -0.0346 -0.0410 940  GLU A C   
6883  O O   . GLU A 942  ? 0.3464 0.2922 0.4010 0.0273  -0.0377 -0.0464 940  GLU A O   
6884  C CB  . GLU A 942  ? 0.3184 0.2710 0.3539 0.0261  -0.0294 -0.0418 940  GLU A CB  
6885  C CG  . GLU A 942  ? 0.3056 0.2615 0.3368 0.0281  -0.0267 -0.0428 940  GLU A CG  
6886  C CD  . GLU A 942  ? 0.3050 0.2666 0.3307 0.0309  -0.0249 -0.0470 940  GLU A CD  
6887  O OE1 . GLU A 942  ? 0.3565 0.3199 0.3854 0.0331  -0.0272 -0.0525 940  GLU A OE1 
6888  O OE2 . GLU A 942  ? 0.2800 0.2446 0.2986 0.0308  -0.0213 -0.0446 940  GLU A OE2 
6889  N N   . VAL A 943  ? 0.3275 0.2723 0.3759 0.0241  -0.0334 -0.0375 941  VAL A N   
6890  C CA  . VAL A 943  ? 0.2967 0.2406 0.3505 0.0257  -0.0352 -0.0399 941  VAL A CA  
6891  C C   . VAL A 943  ? 0.3175 0.2656 0.3646 0.0279  -0.0315 -0.0414 941  VAL A C   
6892  O O   . VAL A 943  ? 0.2888 0.2374 0.3307 0.0264  -0.0285 -0.0369 941  VAL A O   
6893  C CB  . VAL A 943  ? 0.3255 0.2650 0.3848 0.0229  -0.0371 -0.0346 941  VAL A CB  
6894  C CG1 . VAL A 943  ? 0.3253 0.2638 0.3900 0.0247  -0.0388 -0.0370 941  VAL A CG1 
6895  C CG2 . VAL A 943  ? 0.3520 0.2879 0.4184 0.0206  -0.0409 -0.0327 941  VAL A CG2 
6896  N N   . PHE A 944  ? 0.3020 0.2537 0.3494 0.0314  -0.0319 -0.0477 942  PHE A N   
6897  C CA  . PHE A 944  ? 0.2872 0.2443 0.3276 0.0335  -0.0282 -0.0494 942  PHE A CA  
6898  C C   . PHE A 944  ? 0.2943 0.2513 0.3374 0.0346  -0.0283 -0.0499 942  PHE A C   
6899  O O   . PHE A 944  ? 0.3098 0.2696 0.3560 0.0376  -0.0294 -0.0555 942  PHE A O   
6900  C CB  . PHE A 944  ? 0.2683 0.2305 0.3072 0.0366  -0.0284 -0.0558 942  PHE A CB  
6901  C CG  . PHE A 944  ? 0.2548 0.2233 0.2851 0.0380  -0.0243 -0.0559 942  PHE A CG  
6902  C CD1 . PHE A 944  ? 0.2578 0.2269 0.2811 0.0360  -0.0213 -0.0512 942  PHE A CD1 
6903  C CD2 . PHE A 944  ? 0.2512 0.2253 0.2807 0.0411  -0.0235 -0.0605 942  PHE A CD2 
6904  C CE1 . PHE A 944  ? 0.2271 0.2019 0.2432 0.0371  -0.0178 -0.0509 942  PHE A CE1 
6905  C CE2 . PHE A 944  ? 0.2650 0.2454 0.2868 0.0421  -0.0198 -0.0599 942  PHE A CE2 
6906  C CZ  . PHE A 944  ? 0.2431 0.2236 0.2585 0.0400  -0.0171 -0.0549 942  PHE A CZ  
6907  N N   . GLY A 945  ? 0.2700 0.2241 0.3122 0.0320  -0.0272 -0.0441 943  GLY A N   
6908  C CA  . GLY A 945  ? 0.2698 0.2234 0.3147 0.0326  -0.0273 -0.0438 943  GLY A CA  
6909  C C   . GLY A 945  ? 0.2972 0.2490 0.3384 0.0296  -0.0250 -0.0370 943  GLY A C   
6910  O O   . GLY A 945  ? 0.2713 0.2228 0.3074 0.0274  -0.0230 -0.0331 943  GLY A O   
6911  N N   . PRO A 946  ? 0.2561 0.2069 0.2999 0.0297  -0.0252 -0.0358 944  PRO A N   
6912  C CA  . PRO A 946  ? 0.2576 0.2076 0.2974 0.0272  -0.0228 -0.0300 944  PRO A CA  
6913  C C   . PRO A 946  ? 0.2536 0.1990 0.2972 0.0238  -0.0249 -0.0248 944  PRO A C   
6914  O O   . PRO A 946  ? 0.2770 0.2202 0.3244 0.0226  -0.0262 -0.0222 944  PRO A O   
6915  C CB  . PRO A 946  ? 0.2350 0.1865 0.2765 0.0290  -0.0224 -0.0316 944  PRO A CB  
6916  C CG  . PRO A 946  ? 0.3133 0.2634 0.3634 0.0311  -0.0264 -0.0365 944  PRO A CG  
6917  C CD  . PRO A 946  ? 0.2771 0.2280 0.3275 0.0322  -0.0276 -0.0403 944  PRO A CD  
6918  N N   . VAL A 947  ? 0.2767 0.2210 0.3193 0.0220  -0.0253 -0.0232 945  VAL A N   
6919  C CA  . VAL A 947  ? 0.3023 0.2432 0.3492 0.0188  -0.0276 -0.0186 945  VAL A CA  
6920  C C   . VAL A 947  ? 0.2722 0.2141 0.3126 0.0163  -0.0250 -0.0144 945  VAL A C   
6921  O O   . VAL A 947  ? 0.2747 0.2176 0.3125 0.0164  -0.0244 -0.0157 945  VAL A O   
6922  C CB  . VAL A 947  ? 0.3091 0.2473 0.3639 0.0190  -0.0319 -0.0209 945  VAL A CB  
6923  C CG1 . VAL A 947  ? 0.3024 0.2376 0.3619 0.0154  -0.0343 -0.0152 945  VAL A CG1 
6924  C CG2 . VAL A 947  ? 0.2890 0.2264 0.3506 0.0220  -0.0347 -0.0261 945  VAL A CG2 
6925  N N   . LEU A 948  ? 0.2903 0.2323 0.3284 0.0140  -0.0235 -0.0096 946  LEU A N   
6926  C CA  . LEU A 948  ? 0.2751 0.2185 0.3076 0.0116  -0.0211 -0.0057 946  LEU A CA  
6927  C C   . LEU A 948  ? 0.2801 0.2218 0.3169 0.0084  -0.0235 -0.0013 946  LEU A C   
6928  O O   . LEU A 948  ? 0.3084 0.2486 0.3504 0.0071  -0.0257 0.0013  946  LEU A O   
6929  C CB  . LEU A 948  ? 0.2507 0.1958 0.2783 0.0111  -0.0181 -0.0034 946  LEU A CB  
6930  C CG  . LEU A 948  ? 0.2636 0.2105 0.2859 0.0087  -0.0158 0.0002  946  LEU A CG  
6931  C CD1 . LEU A 948  ? 0.2640 0.2124 0.2818 0.0098  -0.0140 -0.0021 946  LEU A CD1 
6932  C CD2 . LEU A 948  ? 0.3075 0.2558 0.3259 0.0084  -0.0134 0.0021  946  LEU A CD2 
6933  N N   . HIS A 949  ? 0.2380 0.1805 0.2729 0.0071  -0.0231 -0.0003 947  HIS A N   
6934  C CA  . HIS A 949  ? 0.2637 0.2058 0.3019 0.0038  -0.0249 0.0043  947  HIS A CA  
6935  C C   . HIS A 949  ? 0.2712 0.2164 0.3033 0.0016  -0.0219 0.0080  947  HIS A C   
6936  O O   . HIS A 949  ? 0.2821 0.2293 0.3078 0.0027  -0.0188 0.0064  947  HIS A O   
6937  C CB  . HIS A 949  ? 0.2676 0.2089 0.3088 0.0036  -0.0269 0.0028  947  HIS A CB  
6938  C CG  . HIS A 949  ? 0.2883 0.2269 0.3355 0.0061  -0.0299 -0.0018 947  HIS A CG  
6939  N ND1 . HIS A 949  ? 0.2960 0.2354 0.3404 0.0094  -0.0287 -0.0074 947  HIS A ND1 
6940  C CD2 . HIS A 949  ? 0.3392 0.2749 0.3954 0.0058  -0.0341 -0.0017 947  HIS A CD2 
6941  C CE1 . HIS A 949  ? 0.3471 0.2844 0.3984 0.0112  -0.0321 -0.0112 947  HIS A CE1 
6942  N NE2 . HIS A 949  ? 0.3197 0.2543 0.3784 0.0091  -0.0355 -0.0079 947  HIS A NE2 
6943  N N   . VAL A 950  ? 0.2519 0.1980 0.2862 -0.0014 -0.0229 0.0131  948  VAL A N   
6944  C CA  . VAL A 950  ? 0.2885 0.2382 0.3175 -0.0034 -0.0202 0.0164  948  VAL A CA  
6945  C C   . VAL A 950  ? 0.3125 0.2642 0.3435 -0.0065 -0.0214 0.0204  948  VAL A C   
6946  O O   . VAL A 950  ? 0.3175 0.2682 0.3549 -0.0083 -0.0246 0.0235  948  VAL A O   
6947  C CB  . VAL A 950  ? 0.2714 0.2218 0.3000 -0.0041 -0.0198 0.0189  948  VAL A CB  
6948  C CG1 . VAL A 950  ? 0.2881 0.2429 0.3115 -0.0062 -0.0171 0.0218  948  VAL A CG1 
6949  C CG2 . VAL A 950  ? 0.2954 0.2443 0.3222 -0.0011 -0.0185 0.0150  948  VAL A CG2 
6950  N N   . ILE A 951  ? 0.2769 0.2317 0.3028 -0.0071 -0.0190 0.0204  949  ILE A N   
6951  C CA  . ILE A 951  ? 0.2914 0.2494 0.3182 -0.0100 -0.0194 0.0241  949  ILE A CA  
6952  C C   . ILE A 951  ? 0.3242 0.2870 0.3454 -0.0114 -0.0165 0.0260  949  ILE A C   
6953  O O   . ILE A 951  ? 0.2750 0.2381 0.2910 -0.0096 -0.0138 0.0235  949  ILE A O   
6954  C CB  . ILE A 951  ? 0.3337 0.2913 0.3602 -0.0094 -0.0195 0.0218  949  ILE A CB  
6955  N N   . ARG A 952  ? 0.2928 0.2597 0.3153 -0.0145 -0.0172 0.0306  950  ARG A N   
6956  C CA  . ARG A 952  ? 0.2555 0.2280 0.2733 -0.0159 -0.0146 0.0323  950  ARG A CA  
6957  C C   . ARG A 952  ? 0.2777 0.2543 0.2941 -0.0172 -0.0137 0.0328  950  ARG A C   
6958  O O   . ARG A 952  ? 0.3173 0.2934 0.3377 -0.0183 -0.0158 0.0342  950  ARG A O   
6959  C CB  . ARG A 952  ? 0.2955 0.2713 0.3159 -0.0187 -0.0161 0.0375  950  ARG A CB  
6960  C CG  . ARG A 952  ? 0.3276 0.2993 0.3511 -0.0178 -0.0177 0.0377  950  ARG A CG  
6961  C CD  . ARG A 952  ? 0.4135 0.3877 0.4417 -0.0209 -0.0203 0.0436  950  ARG A CD  
6962  N NE  . ARG A 952  ? 0.4229 0.4030 0.4471 -0.0224 -0.0185 0.0460  950  ARG A NE  
6963  C CZ  . ARG A 952  ? 0.3880 0.3679 0.4117 -0.0221 -0.0183 0.0466  950  ARG A CZ  
6964  N NH1 . ARG A 952  ? 0.4135 0.3876 0.4403 -0.0203 -0.0198 0.0451  950  ARG A NH1 
6965  N NH2 . ARG A 952  ? 0.3887 0.3746 0.4088 -0.0236 -0.0168 0.0486  950  ARG A NH2 
6966  N N   . TYR A 953  ? 0.2510 0.2316 0.2619 -0.0169 -0.0108 0.0314  951  TYR A N   
6967  C CA  . TYR A 953  ? 0.2649 0.2498 0.2744 -0.0180 -0.0098 0.0315  951  TYR A CA  
6968  C C   . TYR A 953  ? 0.2464 0.2382 0.2521 -0.0192 -0.0076 0.0325  951  TYR A C   
6969  O O   . TYR A 953  ? 0.2680 0.2601 0.2706 -0.0182 -0.0060 0.0311  951  TYR A O   
6970  C CB  . TYR A 953  ? 0.2772 0.2589 0.2845 -0.0153 -0.0086 0.0269  951  TYR A CB  
6971  C CG  . TYR A 953  ? 0.2680 0.2495 0.2701 -0.0131 -0.0058 0.0234  951  TYR A CG  
6972  C CD1 . TYR A 953  ? 0.2512 0.2284 0.2525 -0.0109 -0.0055 0.0213  951  TYR A CD1 
6973  C CD2 . TYR A 953  ? 0.2475 0.2335 0.2462 -0.0131 -0.0036 0.0222  951  TYR A CD2 
6974  C CE1 . TYR A 953  ? 0.2602 0.2373 0.2573 -0.0091 -0.0031 0.0185  951  TYR A CE1 
6975  C CE2 . TYR A 953  ? 0.2363 0.2219 0.2312 -0.0112 -0.0013 0.0191  951  TYR A CE2 
6976  C CZ  . TYR A 953  ? 0.2437 0.2248 0.2379 -0.0092 -0.0012 0.0175  951  TYR A CZ  
6977  O OH  . TYR A 953  ? 0.2518 0.2326 0.2428 -0.0074 0.0009  0.0149  951  TYR A OH  
6978  N N   . ARG A 954  ? 0.2923 0.2901 0.2984 -0.0214 -0.0075 0.0347  952  ARG A N   
6979  C CA  . ARG A 954  ? 0.3021 0.3074 0.3045 -0.0223 -0.0052 0.0347  952  ARG A CA  
6980  C C   . ARG A 954  ? 0.2758 0.2809 0.2746 -0.0200 -0.0029 0.0298  952  ARG A C   
6981  O O   . ARG A 954  ? 0.2773 0.2790 0.2769 -0.0189 -0.0032 0.0280  952  ARG A O   
6982  C CB  . ARG A 954  ? 0.3484 0.3613 0.3531 -0.0256 -0.0061 0.0391  952  ARG A CB  
6983  N N   . ARG A 955  ? 0.2818 0.2905 0.2770 -0.0192 -0.0007 0.0276  953  ARG A N   
6984  C CA  . ARG A 955  ? 0.2948 0.3023 0.2871 -0.0167 0.0013  0.0229  953  ARG A CA  
6985  C C   . ARG A 955  ? 0.2651 0.2752 0.2579 -0.0171 0.0015  0.0222  953  ARG A C   
6986  O O   . ARG A 955  ? 0.3058 0.3121 0.2979 -0.0150 0.0020  0.0191  953  ARG A O   
6987  C CB  . ARG A 955  ? 0.3320 0.3437 0.3213 -0.0162 0.0032  0.0208  953  ARG A CB  
6988  C CG  . ARG A 955  ? 0.4020 0.4124 0.3892 -0.0137 0.0049  0.0161  953  ARG A CG  
6989  C CD  . ARG A 955  ? 0.4512 0.4533 0.4385 -0.0113 0.0046  0.0142  953  ARG A CD  
6990  N NE  . ARG A 955  ? 0.4728 0.4736 0.4586 -0.0091 0.0060  0.0104  953  ARG A NE  
6991  C CZ  . ARG A 955  ? 0.4687 0.4705 0.4547 -0.0086 0.0064  0.0090  953  ARG A CZ  
6992  N NH1 . ARG A 955  ? 0.4123 0.4168 0.3998 -0.0102 0.0055  0.0108  953  ARG A NH1 
6993  N NH2 . ARG A 955  ? 0.4548 0.4551 0.4399 -0.0065 0.0074  0.0057  953  ARG A NH2 
6994  N N   . ASP A 956  ? 0.2852 0.3023 0.2793 -0.0197 0.0011  0.0252  954  ASP A N   
6995  C CA  . ASP A 956  ? 0.2976 0.3178 0.2925 -0.0201 0.0013  0.0247  954  ASP A CA  
6996  C C   . ASP A 956  ? 0.3278 0.3416 0.3254 -0.0196 -0.0004 0.0251  954  ASP A C   
6997  O O   . ASP A 956  ? 0.3350 0.3492 0.3328 -0.0191 -0.0001 0.0234  954  ASP A O   
6998  C CB  . ASP A 956  ? 0.3092 0.3389 0.3052 -0.0232 0.0012  0.0283  954  ASP A CB  
6999  C CG  . ASP A 956  ? 0.3839 0.4216 0.3770 -0.0233 0.0032  0.0267  954  ASP A CG  
7000  O OD1 . ASP A 956  ? 0.3945 0.4303 0.3851 -0.0208 0.0048  0.0222  954  ASP A OD1 
7001  O OD2 . ASP A 956  ? 0.4350 0.4813 0.4286 -0.0259 0.0031  0.0299  954  ASP A OD2 
7002  N N   . ASP A 957  ? 0.2816 0.2898 0.2815 -0.0198 -0.0023 0.0269  955  ASP A N   
7003  C CA  . ASP A 957  ? 0.2929 0.2952 0.2959 -0.0192 -0.0043 0.0269  955  ASP A CA  
7004  C C   . ASP A 957  ? 0.2872 0.2825 0.2884 -0.0159 -0.0038 0.0226  955  ASP A C   
7005  O O   . ASP A 957  ? 0.3032 0.2933 0.3069 -0.0151 -0.0056 0.0221  955  ASP A O   
7006  C CB  . ASP A 957  ? 0.3308 0.3312 0.3384 -0.0212 -0.0071 0.0310  955  ASP A CB  
7007  C CG  . ASP A 957  ? 0.4230 0.4304 0.4333 -0.0248 -0.0081 0.0361  955  ASP A CG  
7008  O OD1 . ASP A 957  ? 0.4370 0.4497 0.4467 -0.0256 -0.0072 0.0361  955  ASP A OD1 
7009  O OD2 . ASP A 957  ? 0.4479 0.4560 0.4613 -0.0267 -0.0099 0.0402  955  ASP A OD2 
7010  N N   . LEU A 958  ? 0.2480 0.2434 0.2453 -0.0141 -0.0016 0.0196  956  LEU A N   
7011  C CA  . LEU A 958  ? 0.2511 0.2406 0.2467 -0.0111 -0.0011 0.0161  956  LEU A CA  
7012  C C   . LEU A 958  ? 0.2807 0.2678 0.2771 -0.0099 -0.0016 0.0142  956  LEU A C   
7013  O O   . LEU A 958  ? 0.2664 0.2484 0.2636 -0.0084 -0.0027 0.0129  956  LEU A O   
7014  C CB  . LEU A 958  ? 0.2589 0.2498 0.2510 -0.0096 0.0013  0.0136  956  LEU A CB  
7015  C CG  . LEU A 958  ? 0.2755 0.2612 0.2658 -0.0067 0.0020  0.0105  956  LEU A CG  
7016  C CD1 . LEU A 958  ? 0.2607 0.2414 0.2520 -0.0059 0.0007  0.0109  956  LEU A CD1 
7017  C CD2 . LEU A 958  ? 0.3262 0.3134 0.3139 -0.0055 0.0040  0.0084  956  LEU A CD2 
7018  N N   . ASP A 959  ? 0.2481 0.2393 0.2444 -0.0106 -0.0010 0.0140  957  ASP A N   
7019  C CA  . ASP A 959  ? 0.2563 0.2454 0.2532 -0.0095 -0.0015 0.0122  957  ASP A CA  
7020  C C   . ASP A 959  ? 0.2673 0.2535 0.2681 -0.0104 -0.0042 0.0137  957  ASP A C   
7021  O O   . ASP A 959  ? 0.2524 0.2344 0.2537 -0.0087 -0.0051 0.0116  957  ASP A O   
7022  C CB  . ASP A 959  ? 0.2945 0.2889 0.2909 -0.0102 -0.0004 0.0117  957  ASP A CB  
7023  C CG  . ASP A 959  ? 0.3488 0.3409 0.3450 -0.0084 -0.0005 0.0092  957  ASP A CG  
7024  O OD1 . ASP A 959  ? 0.3059 0.2944 0.3001 -0.0060 0.0001  0.0066  957  ASP A OD1 
7025  O OD2 . ASP A 959  ? 0.3770 0.3713 0.3753 -0.0096 -0.0014 0.0099  957  ASP A OD2 
7026  N N   . ARG A 960  ? 0.2588 0.2475 0.2628 -0.0131 -0.0056 0.0174  958  ARG A N   
7027  C CA  . ARG A 960  ? 0.2882 0.2739 0.2970 -0.0141 -0.0085 0.0192  958  ARG A CA  
7028  C C   . ARG A 960  ? 0.2902 0.2698 0.2997 -0.0123 -0.0097 0.0176  958  ARG A C   
7029  O O   . ARG A 960  ? 0.3212 0.2968 0.3335 -0.0113 -0.0117 0.0162  958  ARG A O   
7030  C CB  . ARG A 960  ? 0.2885 0.2784 0.3007 -0.0176 -0.0098 0.0242  958  ARG A CB  
7031  C CG  . ARG A 960  ? 0.3307 0.3181 0.3492 -0.0192 -0.0133 0.0268  958  ARG A CG  
7032  C CD  . ARG A 960  ? 0.4852 0.4679 0.5063 -0.0189 -0.0152 0.0277  958  ARG A CD  
7033  N NE  . ARG A 960  ? 0.5215 0.5067 0.5399 -0.0193 -0.0136 0.0291  958  ARG A NE  
7034  C CZ  . ARG A 960  ? 0.4793 0.4606 0.4978 -0.0182 -0.0141 0.0286  958  ARG A CZ  
7035  N NH1 . ARG A 960  ? 0.5463 0.5215 0.5676 -0.0165 -0.0160 0.0265  958  ARG A NH1 
7036  N NH2 . ARG A 960  ? 0.5301 0.5142 0.5459 -0.0187 -0.0126 0.0299  958  ARG A NH2 
7037  N N   . LEU A 961  ? 0.2602 0.2393 0.2674 -0.0117 -0.0085 0.0176  959  LEU A N   
7038  C CA  . LEU A 961  ? 0.2855 0.2594 0.2932 -0.0098 -0.0093 0.0160  959  LEU A CA  
7039  C C   . LEU A 961  ? 0.2950 0.2657 0.3005 -0.0068 -0.0087 0.0117  959  LEU A C   
7040  O O   . LEU A 961  ? 0.2741 0.2411 0.2819 -0.0054 -0.0105 0.0099  959  LEU A O   
7041  C CB  . LEU A 961  ? 0.2482 0.2229 0.2534 -0.0097 -0.0079 0.0166  959  LEU A CB  
7042  C CG  . LEU A 961  ? 0.2446 0.2146 0.2495 -0.0074 -0.0081 0.0145  959  LEU A CG  
7043  C CD1 . LEU A 961  ? 0.3325 0.2993 0.3429 -0.0079 -0.0113 0.0156  959  LEU A CD1 
7044  C CD2 . LEU A 961  ? 0.2841 0.2553 0.2861 -0.0073 -0.0064 0.0151  959  LEU A CD2 
7045  N N   . VAL A 962  ? 0.2502 0.2229 0.2516 -0.0057 -0.0064 0.0099  960  VAL A N   
7046  C CA  . VAL A 962  ? 0.2694 0.2398 0.2688 -0.0030 -0.0058 0.0064  960  VAL A CA  
7047  C C   . VAL A 962  ? 0.3270 0.2961 0.3294 -0.0030 -0.0079 0.0055  960  VAL A C   
7048  O O   . VAL A 962  ? 0.2825 0.2488 0.2851 -0.0010 -0.0088 0.0028  960  VAL A O   
7049  C CB  . VAL A 962  ? 0.2975 0.2703 0.2929 -0.0022 -0.0033 0.0052  960  VAL A CB  
7050  C CG1 . VAL A 962  ? 0.3218 0.2928 0.3154 0.0003  -0.0030 0.0022  960  VAL A CG1 
7051  C CG2 . VAL A 962  ? 0.2908 0.2643 0.2837 -0.0019 -0.0015 0.0056  960  VAL A CG2 
7052  N N   . ASP A 963  ? 0.2993 0.2709 0.3041 -0.0052 -0.0088 0.0076  961  ASP A N   
7053  C CA  . ASP A 963  ? 0.3240 0.2944 0.3326 -0.0055 -0.0112 0.0071  961  ASP A CA  
7054  C C   . ASP A 963  ? 0.3064 0.2728 0.3192 -0.0052 -0.0139 0.0068  961  ASP A C   
7055  O O   . ASP A 963  ? 0.3579 0.3217 0.3723 -0.0036 -0.0155 0.0039  961  ASP A O   
7056  C CB  . ASP A 963  ? 0.3330 0.3071 0.3442 -0.0084 -0.0118 0.0103  961  ASP A CB  
7057  C CG  . ASP A 963  ? 0.4031 0.3812 0.4112 -0.0084 -0.0096 0.0096  961  ASP A CG  
7058  O OD1 . ASP A 963  ? 0.4772 0.4543 0.4818 -0.0060 -0.0082 0.0066  961  ASP A OD1 
7059  O OD2 . ASP A 963  ? 0.5238 0.5064 0.5331 -0.0107 -0.0094 0.0123  961  ASP A OD2 
7060  N N   . ASP A 964  ? 0.2920 0.2581 0.3069 -0.0067 -0.0146 0.0095  962  ASP A N   
7061  C CA  . ASP A 964  ? 0.3355 0.2979 0.3554 -0.0064 -0.0175 0.0093  962  ASP A CA  
7062  C C   . ASP A 964  ? 0.3677 0.3270 0.3856 -0.0031 -0.0172 0.0050  962  ASP A C   
7063  O O   . ASP A 964  ? 0.3312 0.2875 0.3528 -0.0019 -0.0196 0.0026  962  ASP A O   
7064  C CB  . ASP A 964  ? 0.3452 0.3082 0.3673 -0.0086 -0.0181 0.0133  962  ASP A CB  
7065  C CG  . ASP A 964  ? 0.3922 0.3589 0.4175 -0.0121 -0.0191 0.0180  962  ASP A CG  
7066  O OD1 . ASP A 964  ? 0.4338 0.4016 0.4606 -0.0128 -0.0198 0.0179  962  ASP A OD1 
7067  O OD2 . ASP A 964  ? 0.4789 0.4477 0.5050 -0.0142 -0.0191 0.0218  962  ASP A OD2 
7068  N N   . VAL A 965  ? 0.3072 0.2674 0.3196 -0.0017 -0.0143 0.0040  963  VAL A N   
7069  C CA  . VAL A 965  ? 0.3045 0.2628 0.3147 0.0013  -0.0137 0.0002  963  VAL A CA  
7070  C C   . VAL A 965  ? 0.3235 0.2817 0.3332 0.0031  -0.0143 -0.0032 963  VAL A C   
7071  O O   . VAL A 965  ? 0.3148 0.2712 0.3263 0.0051  -0.0158 -0.0064 963  VAL A O   
7072  C CB  . VAL A 965  ? 0.2875 0.2472 0.2923 0.0022  -0.0106 0.0003  963  VAL A CB  
7073  C CG1 . VAL A 965  ? 0.2653 0.2240 0.2677 0.0053  -0.0099 -0.0033 963  VAL A CG1 
7074  C CG2 . VAL A 965  ? 0.2915 0.2514 0.2970 0.0007  -0.0103 0.0032  963  VAL A CG2 
7075  N N   . ASN A 966  ? 0.2752 0.2356 0.2826 0.0025  -0.0130 -0.0027 964  ASN A N   
7076  C CA  . ASN A 966  ? 0.3022 0.2628 0.3091 0.0040  -0.0136 -0.0056 964  ASN A CA  
7077  C C   . ASN A 966  ? 0.3318 0.2907 0.3445 0.0036  -0.0170 -0.0065 964  ASN A C   
7078  O O   . ASN A 966  ? 0.3185 0.2767 0.3317 0.0055  -0.0182 -0.0101 964  ASN A O   
7079  C CB  . ASN A 966  ? 0.3134 0.2768 0.3176 0.0032  -0.0119 -0.0045 964  ASN A CB  
7080  C CG  . ASN A 966  ? 0.2954 0.2605 0.2944 0.0042  -0.0088 -0.0045 964  ASN A CG  
7081  O OD1 . ASN A 966  ? 0.2855 0.2497 0.2823 0.0061  -0.0080 -0.0059 964  ASN A OD1 
7082  N ND2 . ASN A 966  ? 0.2857 0.2532 0.2830 0.0031  -0.0073 -0.0031 964  ASN A ND2 
7083  N N   . ALA A 967  ? 0.3139 0.2721 0.3312 0.0010  -0.0188 -0.0034 965  ALA A N   
7084  C CA  . ALA A 967  ? 0.3479 0.3045 0.3717 0.0001  -0.0223 -0.0037 965  ALA A CA  
7085  C C   . ALA A 967  ? 0.3635 0.3169 0.3912 0.0020  -0.0249 -0.0071 965  ALA A C   
7086  O O   . ALA A 967  ? 0.3859 0.3378 0.4191 0.0020  -0.0280 -0.0086 965  ALA A O   
7087  C CB  . ALA A 967  ? 0.3879 0.3452 0.4161 -0.0034 -0.0236 0.0013  965  ALA A CB  
7088  N N   . THR A 968  ? 0.3049 0.2574 0.3304 0.0038  -0.0238 -0.0085 966  THR A N   
7089  C CA  . THR A 968  ? 0.3191 0.2693 0.3484 0.0060  -0.0262 -0.0125 966  THR A CA  
7090  C C   . THR A 968  ? 0.3173 0.2684 0.3453 0.0086  -0.0267 -0.0175 966  THR A C   
7091  O O   . THR A 968  ? 0.3333 0.2829 0.3659 0.0102  -0.0295 -0.0212 966  THR A O   
7092  C CB  . THR A 968  ? 0.3060 0.2560 0.3327 0.0076  -0.0246 -0.0133 966  THR A CB  
7093  O OG1 . THR A 968  ? 0.3110 0.2635 0.3304 0.0094  -0.0213 -0.0148 966  THR A OG1 
7094  C CG2 . THR A 968  ? 0.3060 0.2556 0.3333 0.0051  -0.0239 -0.0084 966  THR A CG2 
7095  N N   . GLY A 969  ? 0.3006 0.2544 0.3227 0.0091  -0.0241 -0.0177 967  GLY A N   
7096  C CA  . GLY A 969  ? 0.3109 0.2663 0.3307 0.0117  -0.0242 -0.0220 967  GLY A CA  
7097  C C   . GLY A 969  ? 0.2571 0.2145 0.2719 0.0144  -0.0220 -0.0246 967  GLY A C   
7098  O O   . GLY A 969  ? 0.2672 0.2271 0.2787 0.0164  -0.0214 -0.0274 967  GLY A O   
7099  N N   . TYR A 970  ? 0.2657 0.2222 0.2800 0.0146  -0.0211 -0.0236 968  TYR A N   
7100  C CA  . TYR A 970  ? 0.2447 0.2035 0.2542 0.0169  -0.0188 -0.0253 968  TYR A CA  
7101  C C   . TYR A 970  ? 0.2382 0.1990 0.2416 0.0162  -0.0153 -0.0223 968  TYR A C   
7102  O O   . TYR A 970  ? 0.2901 0.2505 0.2932 0.0140  -0.0147 -0.0191 968  TYR A O   
7103  C CB  . TYR A 970  ? 0.2438 0.2011 0.2554 0.0173  -0.0191 -0.0253 968  TYR A CB  
7104  C CG  . TYR A 970  ? 0.2754 0.2310 0.2933 0.0186  -0.0226 -0.0291 968  TYR A CG  
7105  C CD1 . TYR A 970  ? 0.2721 0.2301 0.2897 0.0217  -0.0231 -0.0343 968  TYR A CD1 
7106  C CD2 . TYR A 970  ? 0.3147 0.2667 0.3394 0.0166  -0.0255 -0.0274 968  TYR A CD2 
7107  C CE1 . TYR A 970  ? 0.2986 0.2552 0.3227 0.0231  -0.0265 -0.0383 968  TYR A CE1 
7108  C CE2 . TYR A 970  ? 0.3008 0.2509 0.3323 0.0178  -0.0290 -0.0310 968  TYR A CE2 
7109  C CZ  . TYR A 970  ? 0.3405 0.2928 0.3718 0.0211  -0.0296 -0.0367 968  TYR A CZ  
7110  O OH  . TYR A 970  ? 0.4264 0.3769 0.4650 0.0225  -0.0333 -0.0408 968  TYR A OH  
7111  N N   . GLY A 971  ? 0.2048 0.1681 0.2037 0.0181  -0.0132 -0.0233 969  GLY A N   
7112  C CA  . GLY A 971  ? 0.2304 0.1954 0.2243 0.0177  -0.0103 -0.0206 969  GLY A CA  
7113  C C   . GLY A 971  ? 0.2104 0.1781 0.2004 0.0197  -0.0084 -0.0215 969  GLY A C   
7114  O O   . GLY A 971  ? 0.2257 0.1964 0.2121 0.0207  -0.0070 -0.0216 969  GLY A O   
7115  N N   . LEU A 972  ? 0.1963 0.1634 0.1874 0.0203  -0.0084 -0.0220 970  LEU A N   
7116  C CA  . LEU A 972  ? 0.2143 0.1845 0.2023 0.0223  -0.0067 -0.0229 970  LEU A CA  
7117  C C   . LEU A 972  ? 0.2350 0.2049 0.2203 0.0212  -0.0042 -0.0193 970  LEU A C   
7118  O O   . LEU A 972  ? 0.2322 0.2037 0.2145 0.0209  -0.0025 -0.0174 970  LEU A O   
7119  C CB  . LEU A 972  ? 0.2198 0.1904 0.2106 0.0240  -0.0082 -0.0264 970  LEU A CB  
7120  C CG  . LEU A 972  ? 0.2505 0.2256 0.2382 0.0264  -0.0067 -0.0281 970  LEU A CG  
7121  C CD1 . LEU A 972  ? 0.2161 0.1959 0.2001 0.0277  -0.0059 -0.0290 970  LEU A CD1 
7122  C CD2 . LEU A 972  ? 0.2596 0.2354 0.2508 0.0284  -0.0086 -0.0324 970  LEU A CD2 
7123  N N   . THR A 973  ? 0.2151 0.1831 0.2021 0.0206  -0.0041 -0.0183 971  THR A N   
7124  C CA  . THR A 973  ? 0.2070 0.1747 0.1920 0.0195  -0.0020 -0.0150 971  THR A CA  
7125  C C   . THR A 973  ? 0.2132 0.1778 0.2001 0.0169  -0.0024 -0.0124 971  THR A C   
7126  O O   . THR A 973  ? 0.2215 0.1839 0.2120 0.0160  -0.0044 -0.0128 971  THR A O   
7127  C CB  . THR A 973  ? 0.1889 0.1575 0.1737 0.0206  -0.0012 -0.0154 971  THR A CB  
7128  O OG1 . THR A 973  ? 0.2189 0.1851 0.2077 0.0206  -0.0032 -0.0168 971  THR A OG1 
7129  C CG2 . THR A 973  ? 0.2129 0.1858 0.1952 0.0230  -0.0005 -0.0175 971  THR A CG2 
7130  N N   . PHE A 974  ? 0.2074 0.1722 0.1922 0.0158  -0.0005 -0.0097 972  PHE A N   
7131  C CA  . PHE A 974  ? 0.2017 0.1647 0.1877 0.0134  -0.0006 -0.0072 972  PHE A CA  
7132  C C   . PHE A 974  ? 0.1868 0.1504 0.1708 0.0129  0.0014  -0.0052 972  PHE A C   
7133  O O   . PHE A 974  ? 0.2279 0.1931 0.2094 0.0138  0.0030  -0.0050 972  PHE A O   
7134  C CB  . PHE A 974  ? 0.2222 0.1857 0.2081 0.0123  -0.0008 -0.0066 972  PHE A CB  
7135  C CG  . PHE A 974  ? 0.2095 0.1727 0.1961 0.0099  -0.0004 -0.0041 972  PHE A CG  
7136  C CD1 . PHE A 974  ? 0.2099 0.1720 0.1997 0.0083  -0.0021 -0.0031 972  PHE A CD1 
7137  C CD2 . PHE A 974  ? 0.2254 0.1899 0.2099 0.0094  0.0014  -0.0028 972  PHE A CD2 
7138  C CE1 . PHE A 974  ? 0.2489 0.2118 0.2392 0.0060  -0.0018 -0.0006 972  PHE A CE1 
7139  C CE2 . PHE A 974  ? 0.2163 0.1815 0.2014 0.0073  0.0017  -0.0009 972  PHE A CE2 
7140  C CZ  . PHE A 974  ? 0.2354 0.2001 0.2232 0.0056  0.0002  0.0003  972  PHE A CZ  
7141  N N   . GLY A 975  ? 0.2186 0.1811 0.2040 0.0114  0.0013  -0.0035 973  GLY A N   
7142  C CA  . GLY A 975  ? 0.2342 0.1972 0.2182 0.0109  0.0030  -0.0019 973  GLY A CA  
7143  C C   . GLY A 975  ? 0.1871 0.1504 0.1715 0.0086  0.0031  0.0001  973  GLY A C   
7144  O O   . GLY A 975  ? 0.1971 0.1599 0.1836 0.0072  0.0017  0.0008  973  GLY A O   
7145  N N   . LEU A 976  ? 0.2026 0.1670 0.1854 0.0083  0.0047  0.0009  974  LEU A N   
7146  C CA  . LEU A 976  ? 0.2010 0.1667 0.1840 0.0064  0.0051  0.0022  974  LEU A CA  
7147  C C   . LEU A 976  ? 0.1999 0.1659 0.1822 0.0064  0.0063  0.0029  974  LEU A C   
7148  O O   . LEU A 976  ? 0.2186 0.1847 0.1997 0.0076  0.0073  0.0025  974  LEU A O   
7149  C CB  . LEU A 976  ? 0.2080 0.1752 0.1902 0.0062  0.0056  0.0018  974  LEU A CB  
7150  C CG  . LEU A 976  ? 0.2219 0.1915 0.2042 0.0046  0.0063  0.0025  974  LEU A CG  
7151  C CD1 . LEU A 976  ? 0.2676 0.2381 0.2514 0.0026  0.0051  0.0040  974  LEU A CD1 
7152  C CD2 . LEU A 976  ? 0.2828 0.2538 0.2647 0.0050  0.0068  0.0015  974  LEU A CD2 
7153  N N   . HIS A 977  ? 0.2165 0.1831 0.1997 0.0048  0.0059  0.0043  975  HIS A N   
7154  C CA  . HIS A 977  ? 0.2314 0.1987 0.2141 0.0045  0.0069  0.0049  975  HIS A CA  
7155  C C   . HIS A 977  ? 0.2214 0.1915 0.2040 0.0029  0.0072  0.0053  975  HIS A C   
7156  O O   . HIS A 977  ? 0.2170 0.1887 0.2005 0.0012  0.0064  0.0066  975  HIS A O   
7157  C CB  . HIS A 977  ? 0.2249 0.1910 0.2087 0.0042  0.0062  0.0059  975  HIS A CB  
7158  C CG  . HIS A 977  ? 0.2557 0.2202 0.2392 0.0061  0.0066  0.0051  975  HIS A CG  
7159  N ND1 . HIS A 977  ? 0.3341 0.2989 0.3173 0.0064  0.0076  0.0055  975  HIS A ND1 
7160  C CD2 . HIS A 977  ? 0.3271 0.2905 0.3108 0.0077  0.0062  0.0039  975  HIS A CD2 
7161  C CE1 . HIS A 977  ? 0.2906 0.2545 0.2737 0.0081  0.0078  0.0048  975  HIS A CE1 
7162  N NE2 . HIS A 977  ? 0.3075 0.2708 0.2908 0.0089  0.0070  0.0038  975  HIS A NE2 
7163  N N   . THR A 978  ? 0.2065 0.1778 0.1884 0.0034  0.0083  0.0042  976  THR A N   
7164  C CA  . THR A 978  ? 0.2146 0.1892 0.1966 0.0022  0.0088  0.0039  976  THR A CA  
7165  C C   . THR A 978  ? 0.2161 0.1909 0.1982 0.0032  0.0097  0.0025  976  THR A C   
7166  O O   . THR A 978  ? 0.2389 0.2115 0.2209 0.0047  0.0100  0.0021  976  THR A O   
7167  C CB  . THR A 978  ? 0.2238 0.2003 0.2059 0.0016  0.0085  0.0035  976  THR A CB  
7168  O OG1 . THR A 978  ? 0.2364 0.2171 0.2187 0.0006  0.0090  0.0028  976  THR A OG1 
7169  C CG2 . THR A 978  ? 0.2470 0.2220 0.2289 0.0032  0.0087  0.0022  976  THR A CG2 
7170  N N   . ARG A 979  ? 0.2299 0.2076 0.2124 0.0024  0.0101  0.0018  977  ARG A N   
7171  C CA  . ARG A 979  ? 0.2471 0.2252 0.2306 0.0033  0.0107  0.0000  977  ARG A CA  
7172  C C   . ARG A 979  ? 0.2336 0.2142 0.2179 0.0034  0.0108  -0.0018 977  ARG A C   
7173  O O   . ARG A 979  ? 0.2822 0.2631 0.2680 0.0043  0.0110  -0.0035 977  ARG A O   
7174  C CB  . ARG A 979  ? 0.2384 0.2183 0.2225 0.0027  0.0108  -0.0003 977  ARG A CB  
7175  C CG  . ARG A 979  ? 0.3221 0.2995 0.3058 0.0028  0.0107  0.0013  977  ARG A CG  
7176  C CD  . ARG A 979  ? 0.4237 0.4033 0.4079 0.0019  0.0107  0.0010  977  ARG A CD  
7177  N NE  . ARG A 979  ? 0.4505 0.4274 0.4348 0.0023  0.0107  0.0023  977  ARG A NE  
7178  C CZ  . ARG A 979  ? 0.4945 0.4726 0.4794 0.0018  0.0107  0.0024  977  ARG A CZ  
7179  N NH1 . ARG A 979  ? 0.4303 0.4123 0.4154 0.0009  0.0106  0.0010  977  ARG A NH1 
7180  N NH2 . ARG A 979  ? 0.4476 0.4232 0.4327 0.0022  0.0107  0.0036  977  ARG A NH2 
7181  N N   . LEU A 980  ? 0.1942 0.1765 0.1778 0.0026  0.0105  -0.0014 978  LEU A N   
7182  C CA  . LEU A 980  ? 0.2093 0.1954 0.1937 0.0023  0.0107  -0.0032 978  LEU A CA  
7183  C C   . LEU A 980  ? 0.2178 0.2020 0.2025 0.0035  0.0106  -0.0037 978  LEU A C   
7184  O O   . LEU A 980  ? 0.2268 0.2095 0.2106 0.0033  0.0101  -0.0024 978  LEU A O   
7185  C CB  . LEU A 980  ? 0.2149 0.2052 0.1985 0.0004  0.0105  -0.0022 978  LEU A CB  
7186  C CG  . LEU A 980  ? 0.2168 0.2096 0.1999 -0.0009 0.0104  -0.0013 978  LEU A CG  
7187  C CD1 . LEU A 980  ? 0.2574 0.2548 0.2400 -0.0030 0.0101  0.0005  978  LEU A CD1 
7188  C CD2 . LEU A 980  ? 0.2550 0.2505 0.2391 -0.0004 0.0110  -0.0039 978  LEU A CD2 
7189  N N   . ASP A 981  ? 0.2370 0.2217 0.2235 0.0046  0.0107  -0.0057 979  ASP A N   
7190  C CA  . ASP A 981  ? 0.2302 0.2133 0.2172 0.0057  0.0105  -0.0060 979  ASP A CA  
7191  C C   . ASP A 981  ? 0.2226 0.2080 0.2090 0.0049  0.0103  -0.0060 979  ASP A C   
7192  O O   . ASP A 981  ? 0.2383 0.2217 0.2242 0.0054  0.0099  -0.0053 979  ASP A O   
7193  C CB  . ASP A 981  ? 0.2395 0.2232 0.2294 0.0069  0.0104  -0.0082 979  ASP A CB  
7194  C CG  . ASP A 981  ? 0.2803 0.2608 0.2715 0.0078  0.0103  -0.0077 979  ASP A CG  
7195  O OD1 . ASP A 981  ? 0.3238 0.3017 0.3134 0.0079  0.0104  -0.0056 979  ASP A OD1 
7196  O OD2 . ASP A 981  ? 0.3059 0.2870 0.3003 0.0086  0.0101  -0.0095 979  ASP A OD2 
7197  N N   . GLU A 982  ? 0.2216 0.2117 0.2081 0.0036  0.0105  -0.0067 980  GLU A N   
7198  C CA  . GLU A 982  ? 0.2254 0.2182 0.2117 0.0026  0.0103  -0.0063 980  GLU A CA  
7199  C C   . GLU A 982  ? 0.2263 0.2165 0.2113 0.0018  0.0096  -0.0037 980  GLU A C   
7200  O O   . GLU A 982  ? 0.2367 0.2261 0.2217 0.0018  0.0091  -0.0032 980  GLU A O   
7201  C CB  . GLU A 982  ? 0.2579 0.2572 0.2444 0.0010  0.0107  -0.0070 980  GLU A CB  
7202  C CG  . GLU A 982  ? 0.2809 0.2836 0.2675 -0.0002 0.0104  -0.0062 980  GLU A CG  
7203  C CD  . GLU A 982  ? 0.3770 0.3866 0.3634 -0.0022 0.0107  -0.0056 980  GLU A CD  
7204  O OE1 . GLU A 982  ? 0.4202 0.4304 0.4057 -0.0034 0.0106  -0.0038 980  GLU A OE1 
7205  O OE2 . GLU A 982  ? 0.3419 0.3568 0.3291 -0.0026 0.0110  -0.0068 980  GLU A OE2 
7206  N N   . THR A 983  ? 0.2121 0.2006 0.1961 0.0012  0.0095  -0.0021 981  THR A N   
7207  C CA  . THR A 983  ? 0.2060 0.1920 0.1895 0.0005  0.0086  0.0001  981  THR A CA  
7208  C C   . THR A 983  ? 0.2211 0.2025 0.2043 0.0023  0.0083  -0.0002 981  THR A C   
7209  O O   . THR A 983  ? 0.2299 0.2098 0.2132 0.0022  0.0074  0.0004  981  THR A O   
7210  C CB  . THR A 983  ? 0.2253 0.2111 0.2085 -0.0005 0.0084  0.0017  981  THR A CB  
7211  O OG1 . THR A 983  ? 0.2559 0.2471 0.2393 -0.0023 0.0086  0.0022  981  THR A OG1 
7212  C CG2 . THR A 983  ? 0.2419 0.2247 0.2255 -0.0009 0.0072  0.0036  981  THR A CG2 
7213  N N   . ILE A 984  ? 0.2095 0.1888 0.1924 0.0038  0.0089  -0.0010 982  ILE A N   
7214  C CA  . ILE A 984  ? 0.2223 0.1985 0.2048 0.0054  0.0087  -0.0011 982  ILE A CA  
7215  C C   . ILE A 984  ? 0.2309 0.2076 0.2137 0.0059  0.0083  -0.0019 982  ILE A C   
7216  O O   . ILE A 984  ? 0.2281 0.2032 0.2104 0.0065  0.0077  -0.0017 982  ILE A O   
7217  C CB  . ILE A 984  ? 0.2234 0.1982 0.2061 0.0067  0.0093  -0.0014 982  ILE A CB  
7218  C CG1 . ILE A 984  ? 0.2873 0.2612 0.2696 0.0063  0.0096  -0.0005 982  ILE A CG1 
7219  C CG2 . ILE A 984  ? 0.2498 0.2226 0.2320 0.0083  0.0092  -0.0012 982  ILE A CG2 
7220  C CD1 . ILE A 984  ? 0.2753 0.2485 0.2583 0.0072  0.0101  -0.0007 982  ILE A CD1 
7221  N N   . ALA A 985  ? 0.2027 0.1820 0.1866 0.0058  0.0087  -0.0031 983  ALA A N   
7222  C CA  . ALA A 985  ? 0.2327 0.2127 0.2173 0.0064  0.0084  -0.0040 983  ALA A CA  
7223  C C   . ALA A 985  ? 0.2177 0.1985 0.2021 0.0052  0.0076  -0.0033 983  ALA A C   
7224  O O   . ALA A 985  ? 0.2545 0.2340 0.2387 0.0059  0.0069  -0.0033 983  ALA A O   
7225  C CB  . ALA A 985  ? 0.2590 0.2420 0.2454 0.0065  0.0088  -0.0057 983  ALA A CB  
7226  N N   . HIS A 986  ? 0.2282 0.2115 0.2129 0.0034  0.0076  -0.0025 984  HIS A N   
7227  C CA  . HIS A 986  ? 0.2427 0.2271 0.2279 0.0020  0.0067  -0.0014 984  HIS A CA  
7228  C C   . HIS A 986  ? 0.2482 0.2287 0.2332 0.0024  0.0055  -0.0005 984  HIS A C   
7229  O O   . HIS A 986  ? 0.2428 0.2223 0.2283 0.0028  0.0046  -0.0009 984  HIS A O   
7230  C CB  . HIS A 986  ? 0.2332 0.2213 0.2189 -0.0001 0.0068  -0.0001 984  HIS A CB  
7231  C CG  . HIS A 986  ? 0.2572 0.2463 0.2441 -0.0019 0.0056  0.0019  984  HIS A CG  
7232  N ND1 . HIS A 986  ? 0.3353 0.3275 0.3229 -0.0041 0.0053  0.0040  984  HIS A ND1 
7233  C CD2 . HIS A 986  ? 0.2728 0.2605 0.2609 -0.0021 0.0044  0.0024  984  HIS A CD2 
7234  C CE1 . HIS A 986  ? 0.3792 0.3716 0.3685 -0.0055 0.0039  0.0060  984  HIS A CE1 
7235  N NE2 . HIS A 986  ? 0.3008 0.2903 0.2906 -0.0043 0.0033  0.0048  984  HIS A NE2 
7236  N N   . VAL A 987  ? 0.2385 0.2169 0.2229 0.0025  0.0055  0.0002  985  VAL A N   
7237  C CA  . VAL A 987  ? 0.2431 0.2184 0.2279 0.0029  0.0043  0.0007  985  VAL A CA  
7238  C C   . VAL A 987  ? 0.2482 0.2214 0.2320 0.0049  0.0042  -0.0008 985  VAL A C   
7239  O O   . VAL A 987  ? 0.2503 0.2223 0.2348 0.0053  0.0029  -0.0012 985  VAL A O   
7240  C CB  . VAL A 987  ? 0.1985 0.1724 0.1830 0.0027  0.0044  0.0017  985  VAL A CB  
7241  C CG1 . VAL A 987  ? 0.2152 0.1859 0.2003 0.0036  0.0031  0.0014  985  VAL A CG1 
7242  C CG2 . VAL A 987  ? 0.2527 0.2291 0.2384 0.0004  0.0041  0.0035  985  VAL A CG2 
7243  N N   . THR A 988  ? 0.2397 0.2127 0.2222 0.0063  0.0053  -0.0014 986  THR A N   
7244  C CA  . THR A 988  ? 0.2556 0.2273 0.2372 0.0082  0.0051  -0.0023 986  THR A CA  
7245  C C   . THR A 988  ? 0.3105 0.2832 0.2925 0.0084  0.0045  -0.0031 986  THR A C   
7246  O O   . THR A 988  ? 0.3078 0.2798 0.2892 0.0097  0.0038  -0.0039 986  THR A O   
7247  C CB  . THR A 988  ? 0.2844 0.2559 0.2650 0.0094  0.0062  -0.0022 986  THR A CB  
7248  O OG1 . THR A 988  ? 0.2957 0.2687 0.2771 0.0092  0.0069  -0.0024 986  THR A OG1 
7249  C CG2 . THR A 988  ? 0.2692 0.2397 0.2495 0.0093  0.0067  -0.0014 986  THR A CG2 
7250  N N   . SER A 989  ? 0.2631 0.2378 0.2461 0.0073  0.0048  -0.0031 987  SER A N   
7251  C CA  . SER A 989  ? 0.3029 0.2788 0.2866 0.0075  0.0042  -0.0038 987  SER A CA  
7252  C C   . SER A 989  ? 0.3406 0.3163 0.3255 0.0065  0.0027  -0.0037 987  SER A C   
7253  O O   . SER A 989  ? 0.4070 0.3829 0.3923 0.0070  0.0019  -0.0045 987  SER A O   
7254  C CB  . SER A 989  ? 0.3173 0.2961 0.3021 0.0068  0.0049  -0.0041 987  SER A CB  
7255  O OG  . SER A 989  ? 0.3832 0.3643 0.3690 0.0049  0.0050  -0.0034 987  SER A OG  
7256  N N   . ARG A 990  ? 0.2464 0.2216 0.2321 0.0051  0.0022  -0.0026 988  ARG A N   
7257  C CA  . ARG A 990  ? 0.2758 0.2508 0.2637 0.0039  0.0005  -0.0021 988  ARG A CA  
7258  C C   . ARG A 990  ? 0.2592 0.2313 0.2477 0.0047  -0.0009 -0.0027 988  ARG A C   
7259  O O   . ARG A 990  ? 0.2805 0.2518 0.2711 0.0044  -0.0027 -0.0032 988  ARG A O   
7260  C CB  . ARG A 990  ? 0.2814 0.2585 0.2708 0.0015  0.0005  -0.0001 988  ARG A CB  
7261  C CG  . ARG A 990  ? 0.3870 0.3682 0.3761 0.0007  0.0018  0.0000  988  ARG A CG  
7262  C CD  . ARG A 990  ? 0.4178 0.4012 0.4085 0.0000  0.0012  -0.0002 988  ARG A CD  
7263  N NE  . ARG A 990  ? 0.3841 0.3701 0.3770 -0.0025 0.0004  0.0020  988  ARG A NE  
7264  C CZ  . ARG A 990  ? 0.3990 0.3874 0.3939 -0.0037 -0.0005 0.0026  988  ARG A CZ  
7265  N NH1 . ARG A 990  ? 0.4034 0.3915 0.3983 -0.0025 -0.0006 0.0009  988  ARG A NH1 
7266  N NH2 . ARG A 990  ? 0.3903 0.3817 0.3875 -0.0062 -0.0012 0.0052  988  ARG A NH2 
7267  N N   . ILE A 991  ? 0.2443 0.2148 0.2314 0.0058  -0.0003 -0.0029 989  ILE A N   
7268  C CA  . ILE A 991  ? 0.2320 0.2001 0.2198 0.0068  -0.0016 -0.0040 989  ILE A CA  
7269  C C   . ILE A 991  ? 0.2565 0.2247 0.2433 0.0088  -0.0021 -0.0062 989  ILE A C   
7270  O O   . ILE A 991  ? 0.2755 0.2450 0.2602 0.0097  -0.0009 -0.0065 989  ILE A O   
7271  C CB  . ILE A 991  ? 0.2396 0.2069 0.2262 0.0075  -0.0006 -0.0036 989  ILE A CB  
7272  C CG1 . ILE A 991  ? 0.2735 0.2387 0.2617 0.0083  -0.0021 -0.0047 989  ILE A CG1 
7273  C CG2 . ILE A 991  ? 0.2565 0.2245 0.2402 0.0091  0.0011  -0.0042 989  ILE A CG2 
7274  C CD1 . ILE A 991  ? 0.2981 0.2622 0.2899 0.0064  -0.0039 -0.0034 989  ILE A CD1 
7275  N N   . LYS A 992  ? 0.2333 0.2002 0.2219 0.0094  -0.0039 -0.0077 990  LYS A N   
7276  C CA  . LYS A 992  ? 0.2556 0.2232 0.2433 0.0114  -0.0046 -0.0102 990  LYS A CA  
7277  C C   . LYS A 992  ? 0.2471 0.2139 0.2346 0.0131  -0.0051 -0.0120 990  LYS A C   
7278  O O   . LYS A 992  ? 0.2783 0.2439 0.2687 0.0133  -0.0072 -0.0136 990  LYS A O   
7279  C CB  . LYS A 992  ? 0.2593 0.2267 0.2499 0.0107  -0.0067 -0.0111 990  LYS A CB  
7280  C CG  . LYS A 992  ? 0.3244 0.2930 0.3155 0.0089  -0.0063 -0.0094 990  LYS A CG  
7281  C CD  . LYS A 992  ? 0.4361 0.4044 0.4308 0.0080  -0.0086 -0.0100 990  LYS A CD  
7282  C CE  . LYS A 992  ? 0.4892 0.4594 0.4846 0.0062  -0.0082 -0.0082 990  LYS A CE  
7283  N NZ  . LYS A 992  ? 0.6328 0.6028 0.6326 0.0047  -0.0106 -0.0081 990  LYS A NZ  
7284  N N   . ALA A 993  ? 0.2487 0.2167 0.2332 0.0144  -0.0034 -0.0118 991  ALA A N   
7285  C CA  . ALA A 993  ? 0.2347 0.2031 0.2187 0.0161  -0.0035 -0.0135 991  ALA A CA  
7286  C C   . ALA A 993  ? 0.2267 0.1978 0.2071 0.0178  -0.0019 -0.0135 991  ALA A C   
7287  O O   . ALA A 993  ? 0.2604 0.2322 0.2391 0.0172  -0.0004 -0.0115 991  ALA A O   
7288  C CB  . ALA A 993  ? 0.2341 0.2006 0.2192 0.0154  -0.0032 -0.0123 991  ALA A CB  
7289  N N   . GLY A 994  ? 0.2127 0.1858 0.1922 0.0197  -0.0022 -0.0156 992  GLY A N   
7290  C CA  . GLY A 994  ? 0.2443 0.2210 0.2206 0.0212  -0.0008 -0.0153 992  GLY A CA  
7291  C C   . GLY A 994  ? 0.2153 0.1925 0.1900 0.0212  0.0011  -0.0130 992  GLY A C   
7292  O O   . GLY A 994  ? 0.2229 0.2025 0.1955 0.0216  0.0024  -0.0113 992  GLY A O   
7293  N N   . ASN A 995  ? 0.2193 0.1944 0.1953 0.0206  0.0013  -0.0126 993  ASN A N   
7294  C CA  . ASN A 995  ? 0.2188 0.1944 0.1937 0.0206  0.0030  -0.0106 993  ASN A CA  
7295  C C   . ASN A 995  ? 0.2244 0.1965 0.2009 0.0187  0.0033  -0.0089 993  ASN A C   
7296  O O   . ASN A 995  ? 0.2108 0.1809 0.1895 0.0181  0.0022  -0.0097 993  ASN A O   
7297  C CB  . ASN A 995  ? 0.2207 0.1985 0.1954 0.0223  0.0030  -0.0124 993  ASN A CB  
7298  C CG  . ASN A 995  ? 0.2307 0.2135 0.2030 0.0241  0.0034  -0.0132 993  ASN A CG  
7299  O OD1 . ASN A 995  ? 0.2389 0.2236 0.2111 0.0252  0.0022  -0.0158 993  ASN A OD1 
7300  N ND2 . ASN A 995  ? 0.2273 0.2126 0.1977 0.0244  0.0051  -0.0108 993  ASN A ND2 
7301  N N   . LEU A 996  ? 0.2030 0.1749 0.1788 0.0176  0.0045  -0.0065 994  LEU A N   
7302  C CA  . LEU A 996  ? 0.2227 0.1923 0.1997 0.0159  0.0049  -0.0050 994  LEU A CA  
7303  C C   . LEU A 996  ? 0.1958 0.1657 0.1722 0.0160  0.0063  -0.0035 994  LEU A C   
7304  O O   . LEU A 996  ? 0.2040 0.1758 0.1790 0.0170  0.0072  -0.0027 994  LEU A O   
7305  C CB  . LEU A 996  ? 0.2135 0.1829 0.1906 0.0147  0.0052  -0.0040 994  LEU A CB  
7306  C CG  . LEU A 996  ? 0.2254 0.1952 0.2028 0.0147  0.0041  -0.0052 994  LEU A CG  
7307  C CD1 . LEU A 996  ? 0.2839 0.2540 0.2616 0.0137  0.0046  -0.0042 994  LEU A CD1 
7308  C CD2 . LEU A 996  ? 0.2501 0.2185 0.2294 0.0141  0.0025  -0.0064 994  LEU A CD2 
7309  N N   . TYR A 997  ? 0.1892 0.1574 0.1667 0.0148  0.0063  -0.0028 995  TYR A N   
7310  C CA  . TYR A 997  ? 0.2082 0.1764 0.1855 0.0148  0.0074  -0.0015 995  TYR A CA  
7311  C C   . TYR A 997  ? 0.2070 0.1738 0.1853 0.0130  0.0076  -0.0003 995  TYR A C   
7312  O O   . TYR A 997  ? 0.2244 0.1902 0.2039 0.0118  0.0067  -0.0005 995  TYR A O   
7313  C CB  . TYR A 997  ? 0.2005 0.1687 0.1783 0.0157  0.0070  -0.0025 995  TYR A CB  
7314  C CG  . TYR A 997  ? 0.2110 0.1814 0.1880 0.0177  0.0066  -0.0043 995  TYR A CG  
7315  C CD1 . TYR A 997  ? 0.2311 0.2011 0.2091 0.0181  0.0051  -0.0065 995  TYR A CD1 
7316  C CD2 . TYR A 997  ? 0.2466 0.2200 0.2221 0.0190  0.0078  -0.0039 995  TYR A CD2 
7317  C CE1 . TYR A 997  ? 0.2621 0.2347 0.2395 0.0200  0.0046  -0.0088 995  TYR A CE1 
7318  C CE2 . TYR A 997  ? 0.2522 0.2288 0.2267 0.0208  0.0074  -0.0057 995  TYR A CE2 
7319  C CZ  . TYR A 997  ? 0.2503 0.2264 0.2256 0.0214  0.0058  -0.0084 995  TYR A CZ  
7320  O OH  . TYR A 997  ? 0.3003 0.2801 0.2748 0.0233  0.0054  -0.0108 995  TYR A OH  
7321  N N   . ILE A 998  ? 0.1990 0.1664 0.1771 0.0127  0.0088  0.0009  996  ILE A N   
7322  C CA  A ILE A 998  ? 0.2151 0.1820 0.1940 0.0112  0.0090  0.0016  996  ILE A CA  
7323  C CA  B ILE A 998  ? 0.2151 0.1819 0.1940 0.0112  0.0090  0.0016  996  ILE A CA  
7324  C C   . ILE A 998  ? 0.2137 0.1803 0.1930 0.0111  0.0097  0.0025  996  ILE A C   
7325  O O   . ILE A 998  ? 0.2069 0.1740 0.1860 0.0119  0.0105  0.0032  996  ILE A O   
7326  C CB  A ILE A 998  ? 0.2280 0.1957 0.2072 0.0109  0.0095  0.0017  996  ILE A CB  
7327  C CB  B ILE A 998  ? 0.2281 0.1958 0.2073 0.0109  0.0095  0.0016  996  ILE A CB  
7328  C CG1 A ILE A 998  ? 0.2417 0.2099 0.2205 0.0113  0.0089  0.0008  996  ILE A CG1 
7329  C CG1 B ILE A 998  ? 0.2364 0.2045 0.2154 0.0108  0.0087  0.0007  996  ILE A CG1 
7330  C CG2 A ILE A 998  ? 0.2295 0.1976 0.2096 0.0094  0.0097  0.0017  996  ILE A CG2 
7331  C CG2 B ILE A 998  ? 0.2264 0.1945 0.2066 0.0096  0.0098  0.0018  996  ILE A CG2 
7332  C CD1 A ILE A 998  ? 0.2312 0.1992 0.2105 0.0101  0.0080  0.0002  996  ILE A CD1 
7333  C CD1 B ILE A 998  ? 0.2581 0.2271 0.2376 0.0108  0.0090  0.0005  996  ILE A CD1 
7334  N N   . ASN A 999  ? 0.2047 0.1707 0.1847 0.0099  0.0093  0.0028  997  ASN A N   
7335  C CA  . ASN A 999  ? 0.2109 0.1767 0.1913 0.0096  0.0098  0.0036  997  ASN A CA  
7336  C C   . ASN A 999  ? 0.1990 0.1647 0.1792 0.0110  0.0101  0.0038  997  ASN A C   
7337  O O   . ASN A 999  ? 0.2218 0.1879 0.2024 0.0112  0.0109  0.0046  997  ASN A O   
7338  C CB  . ASN A 999  ? 0.1968 0.1633 0.1777 0.0091  0.0106  0.0040  997  ASN A CB  
7339  C CG  . ASN A 999  ? 0.2074 0.1750 0.1887 0.0076  0.0103  0.0035  997  ASN A CG  
7340  O OD1 . ASN A 999  ? 0.2356 0.2033 0.2169 0.0066  0.0096  0.0038  997  ASN A OD1 
7341  N ND2 . ASN A 999  ? 0.2315 0.2000 0.2133 0.0076  0.0107  0.0029  997  ASN A ND2 
7342  N N   . ARG A 1000 ? 0.2207 0.1863 0.2007 0.0120  0.0094  0.0028  998  ARG A N   
7343  C CA  . ARG A 1000 ? 0.2202 0.1866 0.2000 0.0135  0.0097  0.0024  998  ARG A CA  
7344  C C   . ARG A 1000 ? 0.2340 0.1999 0.2146 0.0142  0.0083  0.0007  998  ARG A C   
7345  O O   . ARG A 1000 ? 0.2388 0.2034 0.2202 0.0133  0.0072  0.0003  998  ARG A O   
7346  C CB  . ARG A 1000 ? 0.2256 0.1942 0.2042 0.0148  0.0106  0.0027  998  ARG A CB  
7347  C CG  . ARG A 1000 ? 0.2103 0.1793 0.1880 0.0151  0.0102  0.0020  998  ARG A CG  
7348  C CD  . ARG A 1000 ? 0.2294 0.2012 0.2059 0.0167  0.0107  0.0020  998  ARG A CD  
7349  N NE  . ARG A 1000 ? 0.2234 0.1967 0.1996 0.0180  0.0103  0.0003  998  ARG A NE  
7350  C CZ  . ARG A 1000 ? 0.2528 0.2297 0.2279 0.0196  0.0108  0.0000  998  ARG A CZ  
7351  N NH1 . ARG A 1000 ? 0.2561 0.2353 0.2301 0.0198  0.0115  0.0017  998  ARG A NH1 
7352  N NH2 . ARG A 1000 ? 0.2396 0.2180 0.2149 0.0210  0.0103  -0.0022 998  ARG A NH2 
7353  N N   . ASN A 1001 ? 0.2263 0.1934 0.2071 0.0157  0.0084  -0.0003 999  ASN A N   
7354  C CA  . ASN A 1001 ? 0.2363 0.2031 0.2185 0.0167  0.0069  -0.0026 999  ASN A CA  
7355  C C   . ASN A 1001 ? 0.2492 0.2171 0.2303 0.0175  0.0065  -0.0040 999  ASN A C   
7356  O O   . ASN A 1001 ? 0.2224 0.1917 0.2015 0.0176  0.0075  -0.0031 999  ASN A O   
7357  C CB  . ASN A 1001 ? 0.2508 0.2192 0.2338 0.0183  0.0069  -0.0038 999  ASN A CB  
7358  C CG  . ASN A 1001 ? 0.2872 0.2595 0.2681 0.0200  0.0083  -0.0042 999  ASN A CG  
7359  O OD1 . ASN A 1001 ? 0.2695 0.2435 0.2490 0.0208  0.0083  -0.0050 999  ASN A OD1 
7360  N ND2 . ASN A 1001 ? 0.3598 0.3339 0.3407 0.0206  0.0093  -0.0034 999  ASN A ND2 
7361  N N   . ILE A 1002 ? 0.2084 0.1757 0.1911 0.0182  0.0048  -0.0063 1000 ILE A N   
7362  C CA  . ILE A 1002 ? 0.2208 0.1889 0.2029 0.0189  0.0041  -0.0079 1000 ILE A CA  
7363  C C   . ILE A 1002 ? 0.2347 0.2059 0.2165 0.0213  0.0037  -0.0108 1000 ILE A C   
7364  O O   . ILE A 1002 ? 0.2478 0.2197 0.2300 0.0221  0.0025  -0.0130 1000 ILE A O   
7365  C CB  . ILE A 1002 ? 0.2139 0.1793 0.1984 0.0175  0.0022  -0.0082 1000 ILE A CB  
7366  C CG1 . ILE A 1002 ? 0.2410 0.2047 0.2292 0.0180  0.0001  -0.0101 1000 ILE A CG1 
7367  C CG2 . ILE A 1002 ? 0.2261 0.1898 0.2105 0.0152  0.0027  -0.0054 1000 ILE A CG2 
7368  C CD1 . ILE A 1002 ? 0.2335 0.1949 0.2248 0.0167  -0.0021 -0.0103 1000 ILE A CD1 
7369  N N   . ILE A 1003 ? 0.2269 0.2005 0.2082 0.0225  0.0047  -0.0110 1001 ILE A N   
7370  C CA  . ILE A 1003 ? 0.2649 0.2424 0.2460 0.0249  0.0044  -0.0142 1001 ILE A CA  
7371  C C   . ILE A 1003 ? 0.3825 0.3651 0.3603 0.0259  0.0063  -0.0131 1001 ILE A C   
7372  O O   . ILE A 1003 ? 0.3505 0.3378 0.3276 0.0278  0.0065  -0.0151 1001 ILE A O   
7373  C CB  . ILE A 1003 ? 0.2468 0.2243 0.2307 0.0259  0.0036  -0.0161 1001 ILE A CB  
7374  C CG1 . ILE A 1003 ? 0.3016 0.2790 0.2851 0.0252  0.0052  -0.0134 1001 ILE A CG1 
7375  C CG2 . ILE A 1003 ? 0.2468 0.2197 0.2347 0.0251  0.0012  -0.0173 1001 ILE A CG2 
7376  C CD1 . ILE A 1003 ? 0.3568 0.3352 0.3428 0.0265  0.0047  -0.0154 1001 ILE A CD1 
7377  N N   . GLY A 1004 ? 0.3822 0.3641 0.3581 0.0245  0.0073  -0.0101 1002 GLY A N   
7378  C CA  . GLY A 1004 ? 0.3032 0.2895 0.2766 0.0251  0.0088  -0.0083 1002 GLY A CA  
7379  C C   . GLY A 1004 ? 0.3514 0.3410 0.3232 0.0263  0.0083  -0.0100 1002 GLY A C   
7380  O O   . GLY A 1004 ? 0.3587 0.3460 0.3309 0.0257  0.0072  -0.0108 1002 GLY A O   
7381  N N   . ALA A 1005 ? 0.2733 0.2690 0.2436 0.0280  0.0089  -0.0107 1003 ALA A N   
7382  C CA  . ALA A 1005 ? 0.3518 0.3518 0.3202 0.0292  0.0085  -0.0122 1003 ALA A CA  
7383  C C   . ALA A 1005 ? 0.3492 0.3558 0.3153 0.0298  0.0100  -0.0095 1003 ALA A C   
7384  O O   . ALA A 1005 ? 0.3760 0.3891 0.3405 0.0315  0.0100  -0.0114 1003 ALA A O   
7385  C CB  . ALA A 1005 ? 0.3324 0.3345 0.3018 0.0312  0.0069  -0.0173 1003 ALA A CB  
7386  N N   . VAL A 1006 ? 0.2827 0.2881 0.2488 0.0284  0.0113  -0.0052 1004 VAL A N   
7387  C CA  . VAL A 1006 ? 0.2539 0.2657 0.2186 0.0287  0.0126  -0.0020 1004 VAL A CA  
7388  C C   . VAL A 1006 ? 0.2447 0.2605 0.2074 0.0292  0.0122  -0.0014 1004 VAL A C   
7389  O O   . VAL A 1006 ? 0.2405 0.2526 0.2035 0.0281  0.0116  -0.0002 1004 VAL A O   
7390  C CB  . VAL A 1006 ? 0.2548 0.2639 0.2208 0.0269  0.0136  0.0026  1004 VAL A CB  
7391  C CG1 . VAL A 1006 ? 0.2713 0.2869 0.2364 0.0270  0.0147  0.0065  1004 VAL A CG1 
7392  C CG2 . VAL A 1006 ? 0.2385 0.2449 0.2061 0.0267  0.0140  0.0018  1004 VAL A CG2 
7393  N N   . VAL A 1007 ? 0.2281 0.2519 0.1889 0.0308  0.0125  -0.0024 1005 VAL A N   
7394  C CA  . VAL A 1007 ? 0.2152 0.2441 0.1740 0.0315  0.0120  -0.0022 1005 VAL A CA  
7395  C C   . VAL A 1007 ? 0.2312 0.2593 0.1902 0.0298  0.0124  0.0033  1005 VAL A C   
7396  O O   . VAL A 1007 ? 0.2511 0.2803 0.2111 0.0289  0.0135  0.0075  1005 VAL A O   
7397  C CB  . VAL A 1007 ? 0.2205 0.2595 0.1771 0.0334  0.0126  -0.0037 1005 VAL A CB  
7398  C CG1 . VAL A 1007 ? 0.2530 0.2985 0.2074 0.0340  0.0122  -0.0026 1005 VAL A CG1 
7399  C CG2 . VAL A 1007 ? 0.2585 0.2980 0.2157 0.0353  0.0118  -0.0100 1005 VAL A CG2 
7400  N N   . GLY A 1008 ? 0.2308 0.2572 0.1895 0.0295  0.0114  0.0034  1006 GLY A N   
7401  C CA  . GLY A 1008 ? 0.2228 0.2484 0.1823 0.0281  0.0115  0.0083  1006 GLY A CA  
7402  C C   . GLY A 1008 ? 0.2429 0.2608 0.2054 0.0263  0.0116  0.0104  1006 GLY A C   
7403  O O   . GLY A 1008 ? 0.2658 0.2824 0.2298 0.0252  0.0114  0.0142  1006 GLY A O   
7404  N N   . VAL A 1009 ? 0.2324 0.2453 0.1959 0.0261  0.0118  0.0080  1007 VAL A N   
7405  C CA  . VAL A 1009 ? 0.2555 0.2616 0.2214 0.0244  0.0119  0.0094  1007 VAL A CA  
7406  C C   . VAL A 1009 ? 0.2265 0.2266 0.1931 0.0241  0.0111  0.0059  1007 VAL A C   
7407  O O   . VAL A 1009 ? 0.2435 0.2393 0.2115 0.0229  0.0107  0.0066  1007 VAL A O   
7408  C CB  . VAL A 1009 ? 0.2498 0.2561 0.2169 0.0241  0.0130  0.0109  1007 VAL A CB  
7409  C CG1 . VAL A 1009 ? 0.2467 0.2465 0.2164 0.0225  0.0130  0.0120  1007 VAL A CG1 
7410  C CG2 . VAL A 1009 ? 0.2254 0.2380 0.1922 0.0242  0.0138  0.0150  1007 VAL A CG2 
7411  N N   . GLN A 1010 ? 0.2417 0.2419 0.2075 0.0250  0.0107  0.0021  1008 GLN A N   
7412  C CA  . GLN A 1010 ? 0.2380 0.2339 0.2044 0.0249  0.0095  -0.0012 1008 GLN A CA  
7413  C C   . GLN A 1010 ? 0.2374 0.2374 0.2022 0.0266  0.0086  -0.0044 1008 GLN A C   
7414  O O   . GLN A 1010 ? 0.2847 0.2857 0.2497 0.0277  0.0081  -0.0076 1008 GLN A O   
7415  C CB  . GLN A 1010 ? 0.2530 0.2449 0.2209 0.0244  0.0094  -0.0028 1008 GLN A CB  
7416  C CG  . GLN A 1010 ? 0.2634 0.2516 0.2328 0.0228  0.0102  -0.0001 1008 GLN A CG  
7417  C CD  . GLN A 1010 ? 0.2812 0.2715 0.2508 0.0231  0.0113  0.0011  1008 GLN A CD  
7418  O OE1 . GLN A 1010 ? 0.2698 0.2627 0.2389 0.0244  0.0113  -0.0009 1008 GLN A OE1 
7419  N NE2 . GLN A 1010 ? 0.2593 0.2486 0.2299 0.0220  0.0122  0.0043  1008 GLN A NE2 
7420  N N   . PRO A 1011 ? 0.2459 0.2488 0.2095 0.0269  0.0082  -0.0036 1009 PRO A N   
7421  C CA  . PRO A 1011 ? 0.2525 0.2588 0.2149 0.0284  0.0071  -0.0072 1009 PRO A CA  
7422  C C   . PRO A 1011 ? 0.2089 0.2104 0.1732 0.0283  0.0057  -0.0110 1009 PRO A C   
7423  O O   . PRO A 1011 ? 0.2184 0.2142 0.1843 0.0268  0.0054  -0.0103 1009 PRO A O   
7424  C CB  . PRO A 1011 ? 0.2341 0.2415 0.1958 0.0280  0.0066  -0.0053 1009 PRO A CB  
7425  C CG  . PRO A 1011 ? 0.2415 0.2491 0.2035 0.0269  0.0078  -0.0004 1009 PRO A CG  
7426  C CD  . PRO A 1011 ? 0.2391 0.2419 0.2029 0.0259  0.0086  0.0003  1009 PRO A CD  
7427  N N   . PHE A 1012 ? 0.2177 0.2217 0.1820 0.0299  0.0048  -0.0150 1010 PHE A N   
7428  C CA  . PHE A 1012 ? 0.2206 0.2200 0.1877 0.0298  0.0035  -0.0182 1010 PHE A CA  
7429  C C   . PHE A 1012 ? 0.2346 0.2342 0.2026 0.0307  0.0015  -0.0221 1010 PHE A C   
7430  O O   . PHE A 1012 ? 0.2398 0.2450 0.2063 0.0325  0.0010  -0.0246 1010 PHE A O   
7431  C CB  . PHE A 1012 ? 0.2251 0.2263 0.1929 0.0310  0.0038  -0.0201 1010 PHE A CB  
7432  C CG  . PHE A 1012 ? 0.2138 0.2099 0.1852 0.0307  0.0023  -0.0226 1010 PHE A CG  
7433  C CD1 . PHE A 1012 ? 0.2639 0.2545 0.2369 0.0288  0.0027  -0.0201 1010 PHE A CD1 
7434  C CD2 . PHE A 1012 ? 0.2524 0.2492 0.2259 0.0322  0.0003  -0.0275 1010 PHE A CD2 
7435  C CE1 . PHE A 1012 ? 0.2181 0.2041 0.1945 0.0283  0.0012  -0.0218 1010 PHE A CE1 
7436  C CE2 . PHE A 1012 ? 0.2562 0.2480 0.2337 0.0317  -0.0014 -0.0294 1010 PHE A CE2 
7437  C CZ  . PHE A 1012 ? 0.2215 0.2079 0.2005 0.0297  -0.0010 -0.0263 1010 PHE A CZ  
7438  N N   . GLY A 1013 ? 0.2139 0.2078 0.1847 0.0294  0.0001  -0.0228 1011 GLY A N   
7439  C CA  . GLY A 1013 ? 0.2318 0.2251 0.2043 0.0300  -0.0021 -0.0265 1011 GLY A CA  
7440  C C   . GLY A 1013 ? 0.2265 0.2144 0.2011 0.0279  -0.0029 -0.0250 1011 GLY A C   
7441  O O   . GLY A 1013 ? 0.2355 0.2218 0.2089 0.0264  -0.0017 -0.0214 1011 GLY A O   
7442  N N   . GLY A 1014 ? 0.2512 0.2365 0.2292 0.0279  -0.0052 -0.0279 1012 GLY A N   
7443  C CA  . GLY A 1014 ? 0.2529 0.2334 0.2335 0.0257  -0.0062 -0.0265 1012 GLY A CA  
7444  C C   . GLY A 1014 ? 0.2416 0.2224 0.2234 0.0258  -0.0080 -0.0285 1012 GLY A C   
7445  O O   . GLY A 1014 ? 0.2674 0.2523 0.2473 0.0275  -0.0084 -0.0306 1012 GLY A O   
7446  N N   . ARG A 1015 ? 0.2170 0.1937 0.2020 0.0239  -0.0093 -0.0276 1013 ARG A N   
7447  C CA  . ARG A 1015 ? 0.2334 0.2097 0.2199 0.0234  -0.0109 -0.0285 1013 ARG A CA  
7448  C C   . ARG A 1015 ? 0.2315 0.2042 0.2236 0.0225  -0.0137 -0.0301 1013 ARG A C   
7449  O O   . ARG A 1015 ? 0.2305 0.2011 0.2251 0.0222  -0.0142 -0.0302 1013 ARG A O   
7450  C CB  . ARG A 1015 ? 0.2676 0.2428 0.2527 0.0214  -0.0096 -0.0247 1013 ARG A CB  
7451  C CG  . ARG A 1015 ? 0.2717 0.2434 0.2586 0.0191  -0.0090 -0.0217 1013 ARG A CG  
7452  C CD  . ARG A 1015 ? 0.3215 0.2926 0.3081 0.0172  -0.0081 -0.0188 1013 ARG A CD  
7453  N NE  . ARG A 1015 ? 0.3672 0.3393 0.3546 0.0173  -0.0094 -0.0201 1013 ARG A NE  
7454  C CZ  . ARG A 1015 ? 0.3873 0.3579 0.3786 0.0164  -0.0118 -0.0213 1013 ARG A CZ  
7455  N NH1 . ARG A 1015 ? 0.3693 0.3372 0.3643 0.0154  -0.0132 -0.0212 1013 ARG A NH1 
7456  N NH2 . ARG A 1015 ? 0.3479 0.3198 0.3398 0.0166  -0.0129 -0.0225 1013 ARG A NH2 
7457  N N   . GLY A 1016 ? 0.2574 0.2296 0.2519 0.0219  -0.0155 -0.0311 1014 GLY A N   
7458  C CA  . GLY A 1016 ? 0.2468 0.2155 0.2473 0.0209  -0.0185 -0.0323 1014 GLY A CA  
7459  C C   . GLY A 1016 ? 0.2620 0.2312 0.2654 0.0231  -0.0205 -0.0369 1014 GLY A C   
7460  O O   . GLY A 1016 ? 0.2627 0.2358 0.2639 0.0255  -0.0205 -0.0405 1014 GLY A O   
7461  N N   . LEU A 1017 ? 0.2447 0.2104 0.2531 0.0222  -0.0222 -0.0367 1015 LEU A N   
7462  C CA  . LEU A 1017 ? 0.2452 0.2110 0.2573 0.0243  -0.0243 -0.0412 1015 LEU A CA  
7463  C C   . LEU A 1017 ? 0.2318 0.2008 0.2396 0.0264  -0.0220 -0.0424 1015 LEU A C   
7464  O O   . LEU A 1017 ? 0.2389 0.2090 0.2492 0.0286  -0.0235 -0.0466 1015 LEU A O   
7465  C CB  . LEU A 1017 ? 0.2539 0.2148 0.2727 0.0226  -0.0266 -0.0399 1015 LEU A CB  
7466  C CG  . LEU A 1017 ? 0.2793 0.2372 0.3037 0.0204  -0.0294 -0.0387 1015 LEU A CG  
7467  C CD1 . LEU A 1017 ? 0.2836 0.2372 0.3143 0.0183  -0.0314 -0.0359 1015 LEU A CD1 
7468  C CD2 . LEU A 1017 ? 0.2753 0.2343 0.3035 0.0223  -0.0326 -0.0443 1015 LEU A CD2 
7469  N N   . SER A 1018 ? 0.2079 0.1785 0.2098 0.0259  -0.0187 -0.0388 1016 SER A N   
7470  C CA  . SER A 1018 ? 0.2234 0.1970 0.2216 0.0274  -0.0164 -0.0390 1016 SER A CA  
7471  C C   . SER A 1018 ? 0.2254 0.2050 0.2187 0.0296  -0.0150 -0.0409 1016 SER A C   
7472  O O   . SER A 1018 ? 0.2396 0.2227 0.2301 0.0312  -0.0134 -0.0415 1016 SER A O   
7473  C CB  . SER A 1018 ? 0.2450 0.2168 0.2404 0.0255  -0.0137 -0.0337 1016 SER A CB  
7474  O OG  . SER A 1018 ? 0.2304 0.1976 0.2302 0.0236  -0.0149 -0.0318 1016 SER A OG  
7475  N N   . GLY A 1019 ? 0.2271 0.2085 0.2192 0.0298  -0.0156 -0.0417 1017 GLY A N   
7476  C CA  . GLY A 1019 ? 0.2436 0.2312 0.2309 0.0317  -0.0143 -0.0431 1017 GLY A CA  
7477  C C   . GLY A 1019 ? 0.2296 0.2188 0.2156 0.0314  -0.0148 -0.0430 1017 GLY A C   
7478  O O   . GLY A 1019 ? 0.2837 0.2690 0.2711 0.0293  -0.0152 -0.0405 1017 GLY A O   
7479  N N   . THR A 1020 ? 0.2400 0.2353 0.2233 0.0336  -0.0149 -0.0458 1018 THR A N   
7480  C CA  . THR A 1020 ? 0.2679 0.2659 0.2487 0.0335  -0.0149 -0.0451 1018 THR A CA  
7481  C C   . THR A 1020 ? 0.2508 0.2516 0.2264 0.0331  -0.0120 -0.0405 1018 THR A C   
7482  O O   . THR A 1020 ? 0.2764 0.2779 0.2504 0.0323  -0.0118 -0.0385 1018 THR A O   
7483  C CB  . THR A 1020 ? 0.2556 0.2598 0.2359 0.0361  -0.0166 -0.0505 1018 THR A CB  
7484  O OG1 . THR A 1020 ? 0.2547 0.2650 0.2318 0.0382  -0.0151 -0.0517 1018 THR A OG1 
7485  C CG2 . THR A 1020 ? 0.2983 0.2997 0.2845 0.0368  -0.0199 -0.0557 1018 THR A CG2 
7486  N N   . GLY A 1021 ? 0.2742 0.2770 0.2476 0.0336  -0.0101 -0.0390 1019 GLY A N   
7487  C CA  . GLY A 1021 ? 0.2736 0.2806 0.2426 0.0337  -0.0077 -0.0353 1019 GLY A CA  
7488  C C   . GLY A 1021 ? 0.2703 0.2853 0.2364 0.0358  -0.0081 -0.0376 1019 GLY A C   
7489  O O   . GLY A 1021 ? 0.2660 0.2833 0.2335 0.0373  -0.0102 -0.0426 1019 GLY A O   
7490  N N   . PRO A 1022 ? 0.2555 0.2753 0.2178 0.0359  -0.0063 -0.0339 1020 PRO A N   
7491  C CA  . PRO A 1022 ? 0.2575 0.2753 0.2187 0.0343  -0.0040 -0.0283 1020 PRO A CA  
7492  C C   . PRO A 1022 ? 0.2748 0.2920 0.2363 0.0345  -0.0028 -0.0281 1020 PRO A C   
7493  O O   . PRO A 1022 ? 0.2770 0.2967 0.2392 0.0361  -0.0035 -0.0322 1020 PRO A O   
7494  C CB  . PRO A 1022 ? 0.2468 0.2716 0.2045 0.0349  -0.0031 -0.0254 1020 PRO A CB  
7495  C CG  . PRO A 1022 ? 0.2603 0.2928 0.2164 0.0373  -0.0042 -0.0300 1020 PRO A CG  
7496  C CD  . PRO A 1022 ? 0.2575 0.2861 0.2167 0.0377  -0.0065 -0.0353 1020 PRO A CD  
7497  N N   . LYS A 1023 ? 0.2439 0.2580 0.2053 0.0330  -0.0011 -0.0236 1021 LYS A N   
7498  C CA  . LYS A 1023 ? 0.2365 0.2495 0.1984 0.0329  0.0001  -0.0230 1021 LYS A CA  
7499  C C   . LYS A 1023 ? 0.2503 0.2713 0.2096 0.0346  0.0012  -0.0230 1021 LYS A C   
7500  O O   . LYS A 1023 ? 0.2384 0.2646 0.1951 0.0347  0.0021  -0.0200 1021 LYS A O   
7501  C CB  . LYS A 1023 ? 0.2211 0.2295 0.1833 0.0309  0.0017  -0.0181 1021 LYS A CB  
7502  C CG  . LYS A 1023 ? 0.2088 0.2096 0.1738 0.0291  0.0010  -0.0179 1021 LYS A CG  
7503  C CD  . LYS A 1023 ? 0.2183 0.2163 0.1833 0.0274  0.0026  -0.0133 1021 LYS A CD  
7504  C CE  . LYS A 1023 ? 0.2230 0.2144 0.1905 0.0256  0.0023  -0.0128 1021 LYS A CE  
7505  N NZ  . LYS A 1023 ? 0.2433 0.2321 0.2123 0.0254  0.0023  -0.0140 1021 LYS A NZ  
7506  N N   . ALA A 1024 ? 0.2608 0.2832 0.2210 0.0359  0.0012  -0.0262 1022 ALA A N   
7507  C CA  . ALA A 1024 ? 0.2725 0.3021 0.2306 0.0371  0.0026  -0.0256 1022 ALA A CA  
7508  C C   . ALA A 1024 ? 0.2711 0.2991 0.2287 0.0355  0.0047  -0.0197 1022 ALA A C   
7509  O O   . ALA A 1024 ? 0.2698 0.2904 0.2293 0.0337  0.0049  -0.0177 1022 ALA A O   
7510  C CB  . ALA A 1024 ? 0.2478 0.2780 0.2079 0.0387  0.0020  -0.0304 1022 ALA A CB  
7511  N N   . GLY A 1025 ? 0.2483 0.2838 0.2034 0.0360  0.0060  -0.0170 1023 GLY A N   
7512  C CA  . GLY A 1025 ? 0.2467 0.2812 0.2018 0.0344  0.0077  -0.0113 1023 GLY A CA  
7513  C C   . GLY A 1025 ? 0.2579 0.2879 0.2135 0.0326  0.0077  -0.0071 1023 GLY A C   
7514  O O   . GLY A 1025 ? 0.2381 0.2647 0.1949 0.0310  0.0086  -0.0030 1023 GLY A O   
7515  N N   . GLY A 1026 ? 0.2283 0.2584 0.1833 0.0327  0.0064  -0.0082 1024 GLY A N   
7516  C CA  . GLY A 1026 ? 0.2234 0.2503 0.1791 0.0312  0.0062  -0.0045 1024 GLY A CA  
7517  C C   . GLY A 1026 ? 0.2250 0.2586 0.1786 0.0320  0.0056  -0.0034 1024 GLY A C   
7518  O O   . GLY A 1026 ? 0.2196 0.2604 0.1710 0.0336  0.0053  -0.0059 1024 GLY A O   
7519  N N   . PRO A 1027 ? 0.2078 0.2393 0.1623 0.0307  0.0053  0.0002  1025 PRO A N   
7520  C CA  . PRO A 1027 ? 0.2211 0.2593 0.1739 0.0311  0.0049  0.0030  1025 PRO A CA  
7521  C C   . PRO A 1027 ? 0.2036 0.2439 0.1553 0.0321  0.0034  -0.0005 1025 PRO A C   
7522  O O   . PRO A 1027 ? 0.2226 0.2696 0.1726 0.0326  0.0029  0.0013  1025 PRO A O   
7523  C CB  . PRO A 1027 ? 0.2486 0.2827 0.2039 0.0293  0.0050  0.0083  1025 PRO A CB  
7524  C CG  . PRO A 1027 ? 0.2643 0.2890 0.2221 0.0283  0.0049  0.0062  1025 PRO A CG  
7525  C CD  . PRO A 1027 ? 0.2143 0.2378 0.1716 0.0289  0.0055  0.0026  1025 PRO A CD  
7526  N N   . LEU A 1028 ? 0.2268 0.2617 0.1794 0.0323  0.0024  -0.0053 1026 LEU A N   
7527  C CA  . LEU A 1028 ? 0.2316 0.2685 0.1835 0.0333  0.0007  -0.0090 1026 LEU A CA  
7528  C C   . LEU A 1028 ? 0.2103 0.2533 0.1605 0.0354  0.0002  -0.0141 1026 LEU A C   
7529  O O   . LEU A 1028 ? 0.2391 0.2850 0.1886 0.0365  -0.0013 -0.0176 1026 LEU A O   
7530  C CB  . LEU A 1028 ? 0.2234 0.2519 0.1779 0.0324  -0.0003 -0.0113 1026 LEU A CB  
7531  C CG  . LEU A 1028 ? 0.2685 0.2917 0.2249 0.0306  -0.0001 -0.0073 1026 LEU A CG  
7532  C CD1 . LEU A 1028 ? 0.2768 0.2928 0.2357 0.0296  -0.0010 -0.0098 1026 LEU A CD1 
7533  C CD2 . LEU A 1028 ? 0.3513 0.3792 0.3066 0.0307  -0.0007 -0.0046 1026 LEU A CD2 
7534  N N   . TYR A 1029 ? 0.2137 0.2588 0.1634 0.0360  0.0013  -0.0148 1027 TYR A N   
7535  C CA  . TYR A 1029 ? 0.2379 0.2873 0.1870 0.0381  0.0006  -0.0207 1027 TYR A CA  
7536  C C   . TYR A 1029 ? 0.2458 0.3062 0.1919 0.0399  0.0002  -0.0220 1027 TYR A C   
7537  O O   . TYR A 1029 ? 0.2387 0.3016 0.1847 0.0414  -0.0015 -0.0274 1027 TYR A O   
7538  C CB  . TYR A 1029 ? 0.2222 0.2719 0.1718 0.0383  0.0021  -0.0205 1027 TYR A CB  
7539  C CG  . TYR A 1029 ? 0.2108 0.2614 0.1615 0.0401  0.0013  -0.0268 1027 TYR A CG  
7540  C CD1 . TYR A 1029 ? 0.2305 0.2731 0.1845 0.0399  -0.0002 -0.0306 1027 TYR A CD1 
7541  C CD2 . TYR A 1029 ? 0.2252 0.2846 0.1742 0.0420  0.0021  -0.0287 1027 TYR A CD2 
7542  C CE1 . TYR A 1029 ? 0.2257 0.2687 0.1817 0.0416  -0.0012 -0.0363 1027 TYR A CE1 
7543  C CE2 . TYR A 1029 ? 0.2488 0.3090 0.1994 0.0438  0.0013  -0.0347 1027 TYR A CE2 
7544  C CZ  . TYR A 1029 ? 0.2290 0.2807 0.1835 0.0436  -0.0005 -0.0385 1027 TYR A CZ  
7545  O OH  . TYR A 1029 ? 0.2608 0.3131 0.2177 0.0454  -0.0016 -0.0444 1027 TYR A OH  
7546  N N   . LEU A 1030 ? 0.2241 0.2916 0.1678 0.0396  0.0016  -0.0171 1028 LEU A N   
7547  C CA  . LEU A 1030 ? 0.2186 0.2981 0.1591 0.0413  0.0013  -0.0180 1028 LEU A CA  
7548  C C   . LEU A 1030 ? 0.2466 0.3269 0.1865 0.0415  -0.0005 -0.0193 1028 LEU A C   
7549  O O   . LEU A 1030 ? 0.2593 0.3474 0.1972 0.0434  -0.0016 -0.0235 1028 LEU A O   
7550  C CB  . LEU A 1030 ? 0.2454 0.3323 0.1839 0.0406  0.0029  -0.0114 1028 LEU A CB  
7551  C CG  . LEU A 1030 ? 0.2749 0.3635 0.2136 0.0405  0.0048  -0.0097 1028 LEU A CG  
7552  C CD1 . LEU A 1030 ? 0.2863 0.3828 0.2234 0.0396  0.0060  -0.0025 1028 LEU A CD1 
7553  C CD2 . LEU A 1030 ? 0.2886 0.3833 0.2263 0.0430  0.0047  -0.0164 1028 LEU A CD2 
7554  N N   . GLY A 1031 ? 0.2334 0.3059 0.1750 0.0397  -0.0010 -0.0160 1029 GLY A N   
7555  C CA  . GLY A 1031 ? 0.2255 0.2988 0.1668 0.0398  -0.0027 -0.0167 1029 GLY A CA  
7556  C C   . GLY A 1031 ? 0.2501 0.3221 0.1923 0.0412  -0.0046 -0.0241 1029 GLY A C   
7557  O O   . GLY A 1031 ? 0.2681 0.3436 0.2093 0.0418  -0.0061 -0.0258 1029 GLY A O   
7558  N N   . ARG A 1032 ? 0.2340 0.3009 0.1784 0.0416  -0.0047 -0.0285 1030 ARG A N   
7559  C CA  . ARG A 1032 ? 0.2248 0.2902 0.1709 0.0430  -0.0069 -0.0356 1030 ARG A CA  
7560  C C   . ARG A 1032 ? 0.2570 0.3332 0.2010 0.0456  -0.0075 -0.0407 1030 ARG A C   
7561  O O   . ARG A 1032 ? 0.2612 0.3384 0.2065 0.0471  -0.0097 -0.0468 1030 ARG A O   
7562  C CB  . ARG A 1032 ? 0.2670 0.3232 0.2169 0.0424  -0.0070 -0.0379 1030 ARG A CB  
7563  C CG  . ARG A 1032 ? 0.2420 0.2943 0.1952 0.0432  -0.0095 -0.0442 1030 ARG A CG  
7564  C CD  . ARG A 1032 ? 0.2523 0.2990 0.2072 0.0416  -0.0108 -0.0429 1030 ARG A CD  
7565  N NE  . ARG A 1032 ? 0.2733 0.3147 0.2324 0.0418  -0.0132 -0.0481 1030 ARG A NE  
7566  C CZ  . ARG A 1032 ? 0.3082 0.3510 0.2684 0.0425  -0.0155 -0.0518 1030 ARG A CZ  
7567  N NH1 . ARG A 1032 ? 0.3352 0.3847 0.2923 0.0432  -0.0158 -0.0512 1030 ARG A NH1 
7568  N NH2 . ARG A 1032 ? 0.3400 0.3774 0.3049 0.0425  -0.0178 -0.0562 1030 ARG A NH2 
7569  N N   . LEU A 1033 ? 0.2262 0.3109 0.1672 0.0463  -0.0058 -0.0384 1031 LEU A N   
7570  C CA  . LEU A 1033 ? 0.2308 0.3268 0.1698 0.0490  -0.0061 -0.0434 1031 LEU A CA  
7571  C C   . LEU A 1033 ? 0.2709 0.3784 0.2059 0.0497  -0.0062 -0.0416 1031 LEU A C   
7572  O O   . LEU A 1033 ? 0.2609 0.3800 0.1933 0.0517  -0.0060 -0.0444 1031 LEU A O   
7573  C CB  . LEU A 1033 ? 0.2409 0.3401 0.1794 0.0494  -0.0040 -0.0425 1031 LEU A CB  
7574  C CG  . LEU A 1033 ? 0.2290 0.3164 0.1713 0.0484  -0.0038 -0.0430 1031 LEU A CG  
7575  C CD1 . LEU A 1033 ? 0.2189 0.3093 0.1608 0.0487  -0.0017 -0.0416 1031 LEU A CD1 
7576  C CD2 . LEU A 1033 ? 0.2806 0.3633 0.2267 0.0497  -0.0062 -0.0507 1031 LEU A CD2 
7577  N N   . VAL A 1034 ? 0.2521 0.3571 0.1866 0.0481  -0.0067 -0.0371 1032 VAL A N   
7578  C CA  . VAL A 1034 ? 0.2409 0.3560 0.1720 0.0485  -0.0072 -0.0350 1032 VAL A CA  
7579  C C   . VAL A 1034 ? 0.2760 0.3861 0.2086 0.0482  -0.0094 -0.0369 1032 VAL A C   
7580  O O   . VAL A 1034 ? 0.2850 0.3836 0.2211 0.0469  -0.0101 -0.0375 1032 VAL A O   
7581  C CB  . VAL A 1034 ? 0.2528 0.3713 0.1821 0.0467  -0.0054 -0.0258 1032 VAL A CB  
7582  C CG1 . VAL A 1034 ? 0.2822 0.4076 0.2099 0.0472  -0.0033 -0.0238 1032 VAL A CG1 
7583  C CG2 . VAL A 1034 ? 0.2462 0.3520 0.1786 0.0442  -0.0051 -0.0206 1032 VAL A CG2 
7584  N N   . THR A 1035 ? 0.2882 0.4078 0.2182 0.0492  -0.0106 -0.0377 1033 THR A N   
7585  C CA  . THR A 1035 ? 0.2966 0.4125 0.2279 0.0491  -0.0129 -0.0401 1033 THR A CA  
7586  C C   . THR A 1035 ? 0.3632 0.4715 0.2958 0.0466  -0.0126 -0.0332 1033 THR A C   
7587  O O   . THR A 1035 ? 0.3990 0.4990 0.3345 0.0458  -0.0140 -0.0348 1033 THR A O   
7588  C CB  . THR A 1035 ? 0.3425 0.4712 0.2707 0.0511  -0.0144 -0.0436 1033 THR A CB  
7589  O OG1 . THR A 1035 ? 0.4563 0.5953 0.3806 0.0507  -0.0131 -0.0371 1033 THR A OG1 
7590  C CG2 . THR A 1035 ? 0.3383 0.4733 0.2663 0.0538  -0.0150 -0.0519 1033 THR A CG2 
7591  N N   . THR A 1036 ? 0.3039 0.4150 0.2350 0.0453  -0.0110 -0.0255 1034 THR A N   
7592  C CA  . THR A 1036 ? 0.3148 0.4190 0.2478 0.0430  -0.0108 -0.0189 1034 THR A CA  
7593  C C   . THR A 1036 ? 0.3047 0.4033 0.2391 0.0415  -0.0086 -0.0142 1034 THR A C   
7594  O O   . THR A 1036 ? 0.3369 0.4424 0.2693 0.0416  -0.0072 -0.0105 1034 THR A O   
7595  C CB  . THR A 1036 ? 0.3792 0.4922 0.3098 0.0427  -0.0113 -0.0136 1034 THR A CB  
7596  O OG1 . THR A 1036 ? 0.4192 0.5386 0.3481 0.0443  -0.0133 -0.0185 1034 THR A OG1 
7597  C CG2 . THR A 1036 ? 0.4426 0.5480 0.3760 0.0406  -0.0114 -0.0074 1034 THR A CG2 
7598  N N   . ALA A 1037 ? 0.3177 0.4044 0.2556 0.0402  -0.0085 -0.0142 1035 ALA A N   
7599  C CA  . ALA A 1037 ? 0.3081 0.3890 0.2475 0.0389  -0.0066 -0.0108 1035 ALA A CA  
7600  C C   . ALA A 1037 ? 0.3091 0.3915 0.2488 0.0374  -0.0057 -0.0027 1035 ALA A C   
7601  O O   . ALA A 1037 ? 0.3089 0.3898 0.2497 0.0366  -0.0068 0.0003  1035 ALA A O   
7602  C CB  . ALA A 1037 ? 0.3538 0.4224 0.2968 0.0378  -0.0068 -0.0129 1035 ALA A CB  
7603  N N   . PRO A 1038 ? 0.2596 0.3449 0.1987 0.0370  -0.0041 0.0012  1036 PRO A N   
7604  C CA  . PRO A 1038 ? 0.2526 0.3376 0.1933 0.0353  -0.0035 0.0091  1036 PRO A CA  
7605  C C   . PRO A 1038 ? 0.2669 0.3398 0.2117 0.0337  -0.0033 0.0105  1036 PRO A C   
7606  O O   . PRO A 1038 ? 0.2693 0.3346 0.2154 0.0338  -0.0032 0.0059  1036 PRO A O   
7607  C CB  . PRO A 1038 ? 0.2748 0.3663 0.2140 0.0355  -0.0018 0.0117  1036 PRO A CB  
7608  C CG  . PRO A 1038 ? 0.3069 0.3953 0.2457 0.0366  -0.0011 0.0052  1036 PRO A CG  
7609  C CD  . PRO A 1038 ? 0.2743 0.3624 0.2122 0.0380  -0.0027 -0.0016 1036 PRO A CD  
7610  N N   . VAL A 1039 ? 0.2628 0.3344 0.2101 0.0323  -0.0032 0.0170  1037 VAL A N   
7611  C CA  . VAL A 1039 ? 0.2488 0.3101 0.2002 0.0308  -0.0029 0.0188  1037 VAL A CA  
7612  C C   . VAL A 1039 ? 0.2289 0.2888 0.1809 0.0303  -0.0011 0.0202  1037 VAL A C   
7613  O O   . VAL A 1039 ? 0.2502 0.3158 0.2020 0.0299  -0.0006 0.0252  1037 VAL A O   
7614  C CB  . VAL A 1039 ? 0.2689 0.3294 0.2235 0.0296  -0.0039 0.0248  1037 VAL A CB  
7615  C CG1 . VAL A 1039 ? 0.2730 0.3238 0.2322 0.0282  -0.0035 0.0263  1037 VAL A CG1 
7616  C CG2 . VAL A 1039 ? 0.2932 0.3552 0.2474 0.0301  -0.0057 0.0233  1037 VAL A CG2 
7617  N N   . PRO A 1040 ? 0.2348 0.2877 0.1875 0.0302  -0.0003 0.0162  1038 PRO A N   
7618  C CA  . PRO A 1040 ? 0.2466 0.2984 0.1997 0.0298  0.0013  0.0174  1038 PRO A CA  
7619  C C   . PRO A 1040 ? 0.2302 0.2789 0.1870 0.0282  0.0015  0.0235  1038 PRO A C   
7620  O O   . PRO A 1040 ? 0.2425 0.2870 0.2022 0.0274  0.0005  0.0255  1038 PRO A O   
7621  C CB  . PRO A 1040 ? 0.2460 0.2898 0.1997 0.0299  0.0016  0.0120  1038 PRO A CB  
7622  C CG  . PRO A 1040 ? 0.2943 0.3380 0.2469 0.0308  0.0003  0.0073  1038 PRO A CG  
7623  C CD  . PRO A 1040 ? 0.2762 0.3224 0.2293 0.0305  -0.0009 0.0106  1038 PRO A CD  
7624  N N   . PRO A 1041 ? 0.2437 0.2943 0.2010 0.0278  0.0028  0.0264  1039 PRO A N   
7625  C CA  . PRO A 1041 ? 0.2308 0.2772 0.1924 0.0262  0.0028  0.0316  1039 PRO A CA  
7626  C C   . PRO A 1041 ? 0.2360 0.2720 0.2007 0.0255  0.0027  0.0291  1039 PRO A C   
7627  O O   . PRO A 1041 ? 0.2482 0.2800 0.2116 0.0259  0.0032  0.0240  1039 PRO A O   
7628  C CB  . PRO A 1041 ? 0.2896 0.3391 0.2507 0.0260  0.0043  0.0333  1039 PRO A CB  
7629  C CG  . PRO A 1041 ? 0.3080 0.3660 0.2643 0.0276  0.0049  0.0305  1039 PRO A CG  
7630  C CD  . PRO A 1041 ? 0.2558 0.3118 0.2101 0.0287  0.0041  0.0245  1039 PRO A CD  
7631  N N   . GLN A 1042 ? 0.2316 0.2638 0.2006 0.0244  0.0018  0.0327  1040 GLN A N   
7632  C CA  . GLN A 1042 ? 0.2447 0.2681 0.2174 0.0236  0.0016  0.0310  1040 GLN A CA  
7633  C C   . GLN A 1042 ? 0.2547 0.2745 0.2262 0.0241  0.0010  0.0260  1040 GLN A C   
7634  O O   . GLN A 1042 ? 0.2512 0.2644 0.2249 0.0236  0.0011  0.0238  1040 GLN A O   
7635  C CB  . GLN A 1042 ? 0.2808 0.2998 0.2544 0.0231  0.0029  0.0300  1040 GLN A CB  
7636  C CG  . GLN A 1042 ? 0.3812 0.4035 0.3564 0.0225  0.0034  0.0348  1040 GLN A CG  
7637  C CD  . GLN A 1042 ? 0.4181 0.4358 0.3943 0.0219  0.0046  0.0336  1040 GLN A CD  
7638  O OE1 . GLN A 1042 ? 0.5313 0.5438 0.5119 0.0210  0.0043  0.0346  1040 GLN A OE1 
7639  N NE2 . GLN A 1042 ? 0.4868 0.5068 0.4595 0.0226  0.0059  0.0310  1040 GLN A NE2 
7640  N N   . HIS A 1043 ? 0.2241 0.2484 0.1924 0.0251  0.0005  0.0241  1041 HIS A N   
7641  C CA  . HIS A 1043 ? 0.2325 0.2537 0.1995 0.0256  0.0000  0.0190  1041 HIS A CA  
7642  C C   . HIS A 1043 ? 0.2183 0.2383 0.1877 0.0254  -0.0015 0.0200  1041 HIS A C   
7643  O O   . HIS A 1043 ? 0.2429 0.2679 0.2110 0.0260  -0.0025 0.0211  1041 HIS A O   
7644  C CB  . HIS A 1043 ? 0.2194 0.2462 0.1820 0.0269  0.0000  0.0157  1041 HIS A CB  
7645  C CG  . HIS A 1043 ? 0.2355 0.2595 0.1973 0.0274  -0.0008 0.0106  1041 HIS A CG  
7646  N ND1 . HIS A 1043 ? 0.2385 0.2580 0.2002 0.0273  -0.0004 0.0064  1041 HIS A ND1 
7647  C CD2 . HIS A 1043 ? 0.2341 0.2594 0.1956 0.0278  -0.0022 0.0093  1041 HIS A CD2 
7648  C CE1 . HIS A 1043 ? 0.2504 0.2684 0.2119 0.0276  -0.0014 0.0029  1041 HIS A CE1 
7649  N NE2 . HIS A 1043 ? 0.2519 0.2735 0.2132 0.0279  -0.0025 0.0044  1041 HIS A NE2 
7650  N N   . SER A 1044 ? 0.2093 0.2229 0.1824 0.0245  -0.0016 0.0196  1042 SER A N   
7651  C CA  . SER A 1044 ? 0.2109 0.2226 0.1868 0.0244  -0.0029 0.0199  1042 SER A CA  
7652  C C   . SER A 1044 ? 0.2238 0.2288 0.2027 0.0236  -0.0025 0.0175  1042 SER A C   
7653  O O   . SER A 1044 ? 0.2495 0.2515 0.2285 0.0231  -0.0013 0.0167  1042 SER A O   
7654  C CB  . SER A 1044 ? 0.2357 0.2498 0.2149 0.0241  -0.0040 0.0253  1042 SER A CB  
7655  O OG  . SER A 1044 ? 0.2448 0.2557 0.2277 0.0233  -0.0035 0.0277  1042 SER A OG  
7656  N N   . SER A 1045 ? 0.2049 0.2078 0.1862 0.0235  -0.0034 0.0165  1043 SER A N   
7657  C CA  . SER A 1045 ? 0.2290 0.2266 0.2134 0.0228  -0.0031 0.0145  1043 SER A CA  
7658  C C   . SER A 1045 ? 0.2024 0.1994 0.1911 0.0229  -0.0045 0.0154  1043 SER A C   
7659  O O   . SER A 1045 ? 0.2170 0.2165 0.2050 0.0234  -0.0056 0.0155  1043 SER A O   
7660  C CB  . SER A 1045 ? 0.2398 0.2355 0.2220 0.0226  -0.0025 0.0099  1043 SER A CB  
7661  O OG  . SER A 1045 ? 0.2485 0.2402 0.2337 0.0219  -0.0023 0.0082  1043 SER A OG  
7662  N N   . VAL A 1046 ? 0.2297 0.2234 0.2230 0.0225  -0.0046 0.0159  1044 VAL A N   
7663  C CA  . VAL A 1046 ? 0.2386 0.2316 0.2368 0.0226  -0.0059 0.0161  1044 VAL A CA  
7664  C C   . VAL A 1046 ? 0.2431 0.2343 0.2414 0.0225  -0.0057 0.0119  1044 VAL A C   
7665  O O   . VAL A 1046 ? 0.2704 0.2613 0.2725 0.0228  -0.0068 0.0114  1044 VAL A O   
7666  C CB  . VAL A 1046 ? 0.2625 0.2532 0.2667 0.0225  -0.0065 0.0181  1044 VAL A CB  
7667  C CG1 . VAL A 1046 ? 0.2879 0.2808 0.2928 0.0224  -0.0071 0.0232  1044 VAL A CG1 
7668  C CG2 . VAL A 1046 ? 0.2480 0.2353 0.2530 0.0219  -0.0052 0.0153  1044 VAL A CG2 
7669  N N   . HIS A 1047 ? 0.2285 0.2188 0.2232 0.0221  -0.0044 0.0089  1045 HIS A N   
7670  C CA  . HIS A 1047 ? 0.2748 0.2637 0.2698 0.0216  -0.0041 0.0053  1045 HIS A CA  
7671  C C   . HIS A 1047 ? 0.2369 0.2279 0.2294 0.0219  -0.0049 0.0041  1045 HIS A C   
7672  O O   . HIS A 1047 ? 0.2544 0.2474 0.2434 0.0223  -0.0051 0.0048  1045 HIS A O   
7673  C CB  . HIS A 1047 ? 0.2976 0.2845 0.2907 0.0208  -0.0026 0.0034  1045 HIS A CB  
7674  C CG  . HIS A 1047 ? 0.3466 0.3317 0.3421 0.0206  -0.0020 0.0044  1045 HIS A CG  
7675  N ND1 . HIS A 1047 ? 0.3863 0.3702 0.3865 0.0205  -0.0023 0.0038  1045 HIS A ND1 
7676  C CD2 . HIS A 1047 ? 0.3685 0.3530 0.3625 0.0204  -0.0012 0.0060  1045 HIS A CD2 
7677  C CE1 . HIS A 1047 ? 0.3955 0.3779 0.3972 0.0203  -0.0018 0.0047  1045 HIS A CE1 
7678  N NE2 . HIS A 1047 ? 0.3659 0.3487 0.3639 0.0202  -0.0011 0.0063  1045 HIS A NE2 
7679  N N   . THR A 1048 ? 0.2364 0.2273 0.2312 0.0217  -0.0054 0.0023  1046 THR A N   
7680  C CA  . THR A 1048 ? 0.2544 0.2471 0.2476 0.0219  -0.0063 0.0009  1046 THR A CA  
7681  C C   . THR A 1048 ? 0.2496 0.2412 0.2427 0.0209  -0.0057 -0.0022 1046 THR A C   
7682  O O   . THR A 1048 ? 0.2624 0.2530 0.2585 0.0204  -0.0051 -0.0033 1046 THR A O   
7683  C CB  . THR A 1048 ? 0.2392 0.2334 0.2357 0.0225  -0.0078 0.0020  1046 THR A CB  
7684  O OG1 . THR A 1048 ? 0.2713 0.2667 0.2688 0.0232  -0.0085 0.0056  1046 THR A OG1 
7685  C CG2 . THR A 1048 ? 0.2649 0.2613 0.2595 0.0228  -0.0088 0.0008  1046 THR A CG2 
7686  N N   . ASP A 1049 ? 0.2356 0.2276 0.2257 0.0206  -0.0058 -0.0036 1047 ASP A N   
7687  C CA  . ASP A 1049 ? 0.2110 0.2021 0.2012 0.0195  -0.0054 -0.0060 1047 ASP A CA  
7688  C C   . ASP A 1049 ? 0.2197 0.2119 0.2131 0.0192  -0.0061 -0.0069 1047 ASP A C   
7689  O O   . ASP A 1049 ? 0.2217 0.2156 0.2156 0.0200  -0.0073 -0.0066 1047 ASP A O   
7690  C CB  . ASP A 1049 ? 0.1928 0.1842 0.1801 0.0194  -0.0060 -0.0073 1047 ASP A CB  
7691  C CG  . ASP A 1049 ? 0.2600 0.2503 0.2481 0.0180  -0.0060 -0.0091 1047 ASP A CG  
7692  O OD1 . ASP A 1049 ? 0.2554 0.2469 0.2453 0.0176  -0.0068 -0.0101 1047 ASP A OD1 
7693  O OD2 . ASP A 1049 ? 0.2597 0.2485 0.2470 0.0172  -0.0052 -0.0094 1047 ASP A OD2 
7694  N N   . PRO A 1050 ? 0.2107 0.2026 0.2063 0.0183  -0.0053 -0.0081 1048 PRO A N   
7695  C CA  . PRO A 1050 ? 0.2321 0.2257 0.2311 0.0182  -0.0057 -0.0091 1048 PRO A CA  
7696  C C   . PRO A 1050 ? 0.2198 0.2148 0.2185 0.0175  -0.0067 -0.0103 1048 PRO A C   
7697  O O   . PRO A 1050 ? 0.2291 0.2258 0.2301 0.0178  -0.0075 -0.0108 1048 PRO A O   
7698  C CB  . PRO A 1050 ? 0.2552 0.2489 0.2563 0.0173  -0.0044 -0.0102 1048 PRO A CB  
7699  C CG  . PRO A 1050 ? 0.2518 0.2437 0.2499 0.0164  -0.0034 -0.0100 1048 PRO A CG  
7700  C CD  . PRO A 1050 ? 0.2245 0.2150 0.2198 0.0173  -0.0038 -0.0085 1048 PRO A CD  
7701  N N   . VAL A 1051 ? 0.2241 0.2181 0.2204 0.0167  -0.0067 -0.0108 1049 VAL A N   
7702  C CA  . VAL A 1051 ? 0.2248 0.2198 0.2214 0.0161  -0.0079 -0.0119 1049 VAL A CA  
7703  C C   . VAL A 1051 ? 0.2060 0.2020 0.2013 0.0174  -0.0094 -0.0117 1049 VAL A C   
7704  O O   . VAL A 1051 ? 0.2107 0.2083 0.2074 0.0174  -0.0107 -0.0125 1049 VAL A O   
7705  C CB  . VAL A 1051 ? 0.2430 0.2367 0.2384 0.0148  -0.0079 -0.0125 1049 VAL A CB  
7706  C CG1 . VAL A 1051 ? 0.2927 0.2872 0.2891 0.0141  -0.0095 -0.0136 1049 VAL A CG1 
7707  C CG2 . VAL A 1051 ? 0.2485 0.2421 0.2452 0.0133  -0.0064 -0.0123 1049 VAL A CG2 
7708  N N   . LEU A 1052 ? 0.1973 0.1927 0.1900 0.0186  -0.0094 -0.0107 1050 LEU A N   
7709  C CA  . LEU A 1052 ? 0.2060 0.2034 0.1974 0.0199  -0.0107 -0.0101 1050 LEU A CA  
7710  C C   . LEU A 1052 ? 0.2169 0.2158 0.2112 0.0205  -0.0113 -0.0092 1050 LEU A C   
7711  O O   . LEU A 1052 ? 0.1915 0.1924 0.1863 0.0209  -0.0127 -0.0096 1050 LEU A O   
7712  C CB  . LEU A 1052 ? 0.2144 0.2119 0.2030 0.0209  -0.0103 -0.0086 1050 LEU A CB  
7713  C CG  . LEU A 1052 ? 0.2053 0.2059 0.1922 0.0223  -0.0115 -0.0073 1050 LEU A CG  
7714  C CD1 . LEU A 1052 ? 0.2210 0.2227 0.2104 0.0229  -0.0118 -0.0048 1050 LEU A CD1 
7715  C CD2 . LEU A 1052 ? 0.2302 0.2328 0.2160 0.0226  -0.0131 -0.0094 1050 LEU A CD2 
7716  N N   . LEU A 1053 ? 0.2144 0.2125 0.2110 0.0205  -0.0103 -0.0081 1051 LEU A N   
7717  C CA  . LEU A 1053 ? 0.2206 0.2201 0.2208 0.0211  -0.0111 -0.0074 1051 LEU A CA  
7718  C C   . LEU A 1053 ? 0.1999 0.2007 0.2025 0.0205  -0.0116 -0.0093 1051 LEU A C   
7719  O O   . LEU A 1053 ? 0.2271 0.2298 0.2314 0.0211  -0.0130 -0.0091 1051 LEU A O   
7720  C CB  . LEU A 1053 ? 0.2087 0.2069 0.2118 0.0213  -0.0101 -0.0066 1051 LEU A CB  
7721  C CG  . LEU A 1053 ? 0.2609 0.2581 0.2629 0.0220  -0.0099 -0.0041 1051 LEU A CG  
7722  C CD1 . LEU A 1053 ? 0.2788 0.2744 0.2842 0.0221  -0.0091 -0.0039 1051 LEU A CD1 
7723  C CD2 . LEU A 1053 ? 0.2650 0.2642 0.2673 0.0231  -0.0116 -0.0017 1051 LEU A CD2 
7724  N N   . ASP A 1054 ? 0.2189 0.2192 0.2218 0.0191  -0.0107 -0.0109 1052 ASP A N   
7725  C CA  . ASP A 1054 ? 0.2295 0.2317 0.2348 0.0183  -0.0112 -0.0124 1052 ASP A CA  
7726  C C   . ASP A 1054 ? 0.1959 0.1989 0.1997 0.0183  -0.0129 -0.0129 1052 ASP A C   
7727  O O   . ASP A 1054 ? 0.2202 0.2253 0.2263 0.0184  -0.0140 -0.0135 1052 ASP A O   
7728  C CB  . ASP A 1054 ? 0.2075 0.2096 0.2132 0.0165  -0.0100 -0.0135 1052 ASP A CB  
7729  C CG  . ASP A 1054 ? 0.2901 0.2926 0.2978 0.0164  -0.0084 -0.0136 1052 ASP A CG  
7730  O OD1 . ASP A 1054 ? 0.2696 0.2722 0.2793 0.0177  -0.0085 -0.0133 1052 ASP A OD1 
7731  O OD2 . ASP A 1054 ? 0.3273 0.3300 0.3348 0.0150  -0.0073 -0.0141 1052 ASP A OD2 
7732  N N   . PHE A 1055 ? 0.2084 0.2103 0.2089 0.0184  -0.0132 -0.0130 1053 PHE A N   
7733  C CA  . PHE A 1055 ? 0.2102 0.2132 0.2095 0.0187  -0.0150 -0.0139 1053 PHE A CA  
7734  C C   . PHE A 1055 ? 0.2053 0.2104 0.2043 0.0202  -0.0163 -0.0130 1053 PHE A C   
7735  O O   . PHE A 1055 ? 0.2228 0.2299 0.2230 0.0204  -0.0178 -0.0138 1053 PHE A O   
7736  C CB  . PHE A 1055 ? 0.2084 0.2100 0.2044 0.0188  -0.0151 -0.0146 1053 PHE A CB  
7737  C CG  . PHE A 1055 ? 0.2121 0.2150 0.2070 0.0193  -0.0171 -0.0163 1053 PHE A CG  
7738  C CD1 . PHE A 1055 ? 0.2534 0.2568 0.2508 0.0183  -0.0184 -0.0179 1053 PHE A CD1 
7739  C CD2 . PHE A 1055 ? 0.2232 0.2273 0.2148 0.0207  -0.0177 -0.0164 1053 PHE A CD2 
7740  C CE1 . PHE A 1055 ? 0.2720 0.2767 0.2689 0.0188  -0.0205 -0.0198 1053 PHE A CE1 
7741  C CE2 . PHE A 1055 ? 0.2491 0.2550 0.2398 0.0213  -0.0196 -0.0186 1053 PHE A CE2 
7742  C CZ  . PHE A 1055 ? 0.2403 0.2462 0.2337 0.0203  -0.0211 -0.0204 1053 PHE A CZ  
7743  N N   . ALA A 1056 ? 0.2084 0.2136 0.2065 0.0213  -0.0158 -0.0109 1054 ALA A N   
7744  C CA  . ALA A 1056 ? 0.2197 0.2273 0.2181 0.0226  -0.0171 -0.0093 1054 ALA A CA  
7745  C C   . ALA A 1056 ? 0.2334 0.2421 0.2361 0.0226  -0.0178 -0.0094 1054 ALA A C   
7746  O O   . ALA A 1056 ? 0.2347 0.2457 0.2379 0.0232  -0.0195 -0.0092 1054 ALA A O   
7747  C CB  . ALA A 1056 ? 0.2557 0.2629 0.2533 0.0234  -0.0165 -0.0065 1054 ALA A CB  
7748  N N   . LYS A 1057 ? 0.2295 0.2370 0.2354 0.0219  -0.0166 -0.0099 1055 LYS A N   
7749  C CA  . LYS A 1057 ? 0.2623 0.2713 0.2725 0.0220  -0.0172 -0.0105 1055 LYS A CA  
7750  C C   . LYS A 1057 ? 0.2338 0.2444 0.2445 0.0212  -0.0181 -0.0124 1055 LYS A C   
7751  O O   . LYS A 1057 ? 0.2566 0.2693 0.2697 0.0216  -0.0195 -0.0126 1055 LYS A O   
7752  C CB  . LYS A 1057 ? 0.2746 0.2829 0.2881 0.0216  -0.0157 -0.0112 1055 LYS A CB  
7753  C CG  . LYS A 1057 ? 0.2954 0.3025 0.3105 0.0226  -0.0154 -0.0095 1055 LYS A CG  
7754  C CD  . LYS A 1057 ? 0.2777 0.2849 0.2969 0.0224  -0.0142 -0.0110 1055 LYS A CD  
7755  C CE  . LYS A 1057 ? 0.2859 0.2922 0.3032 0.0210  -0.0124 -0.0124 1055 LYS A CE  
7756  N NZ  . LYS A 1057 ? 0.3245 0.3309 0.3451 0.0212  -0.0112 -0.0135 1055 LYS A NZ  
7757  N N   . TRP A 1058 ? 0.2321 0.2417 0.2411 0.0199  -0.0175 -0.0137 1056 TRP A N   
7758  C CA  . TRP A 1058 ? 0.2628 0.2736 0.2726 0.0189  -0.0187 -0.0153 1056 TRP A CA  
7759  C C   . TRP A 1058 ? 0.2472 0.2594 0.2554 0.0199  -0.0208 -0.0155 1056 TRP A C   
7760  O O   . TRP A 1058 ? 0.2567 0.2709 0.2670 0.0198  -0.0222 -0.0163 1056 TRP A O   
7761  C CB  . TRP A 1058 ? 0.2529 0.2619 0.2615 0.0173  -0.0179 -0.0163 1056 TRP A CB  
7762  C CG  . TRP A 1058 ? 0.2562 0.2661 0.2662 0.0161  -0.0194 -0.0177 1056 TRP A CG  
7763  C CD1 . TRP A 1058 ? 0.3268 0.3382 0.3403 0.0146  -0.0193 -0.0181 1056 TRP A CD1 
7764  C CD2 . TRP A 1058 ? 0.2874 0.2969 0.2957 0.0163  -0.0212 -0.0189 1056 TRP A CD2 
7765  N NE1 . TRP A 1058 ? 0.3238 0.3355 0.3383 0.0137  -0.0211 -0.0192 1056 TRP A NE1 
7766  C CE2 . TRP A 1058 ? 0.3385 0.3488 0.3499 0.0148  -0.0224 -0.0200 1056 TRP A CE2 
7767  C CE3 . TRP A 1058 ? 0.2757 0.2847 0.2805 0.0176  -0.0220 -0.0193 1056 TRP A CE3 
7768  C CZ2 . TRP A 1058 ? 0.3335 0.3436 0.3449 0.0147  -0.0245 -0.0217 1056 TRP A CZ2 
7769  C CZ3 . TRP A 1058 ? 0.2989 0.3082 0.3033 0.0176  -0.0240 -0.0214 1056 TRP A CZ3 
7770  C CH2 . TRP A 1058 ? 0.3245 0.3340 0.3324 0.0162  -0.0254 -0.0226 1056 TRP A CH2 
7771  N N   . LEU A 1059 ? 0.2275 0.2392 0.2319 0.0208  -0.0210 -0.0148 1057 LEU A N   
7772  C CA  . LEU A 1059 ? 0.2613 0.2753 0.2637 0.0219  -0.0229 -0.0151 1057 LEU A CA  
7773  C C   . LEU A 1059 ? 0.2657 0.2823 0.2703 0.0229  -0.0241 -0.0137 1057 LEU A C   
7774  O O   . LEU A 1059 ? 0.2732 0.2921 0.2784 0.0231  -0.0259 -0.0146 1057 LEU A O   
7775  C CB  . LEU A 1059 ? 0.2282 0.2424 0.2264 0.0229  -0.0227 -0.0142 1057 LEU A CB  
7776  C CG  . LEU A 1059 ? 0.2421 0.2545 0.2379 0.0224  -0.0224 -0.0162 1057 LEU A CG  
7777  C CD1 . LEU A 1059 ? 0.2309 0.2438 0.2228 0.0234  -0.0217 -0.0151 1057 LEU A CD1 
7778  C CD2 . LEU A 1059 ? 0.2770 0.2909 0.2729 0.0223  -0.0244 -0.0190 1057 LEU A CD2 
7779  N N   . ASP A 1060 ? 0.2486 0.2647 0.2549 0.0234  -0.0232 -0.0115 1058 ASP A N   
7780  C CA  . ASP A 1060 ? 0.3090 0.3273 0.3183 0.0243  -0.0245 -0.0100 1058 ASP A CA  
7781  C C   . ASP A 1060 ? 0.2955 0.3147 0.3088 0.0237  -0.0250 -0.0117 1058 ASP A C   
7782  O O   . ASP A 1060 ? 0.3357 0.3574 0.3503 0.0242  -0.0268 -0.0117 1058 ASP A O   
7783  C CB  . ASP A 1060 ? 0.3023 0.3194 0.3137 0.0250  -0.0237 -0.0076 1058 ASP A CB  
7784  C CG  . ASP A 1060 ? 0.3146 0.3329 0.3235 0.0260  -0.0243 -0.0046 1058 ASP A CG  
7785  O OD1 . ASP A 1060 ? 0.3660 0.3874 0.3728 0.0266  -0.0259 -0.0040 1058 ASP A OD1 
7786  O OD2 . ASP A 1060 ? 0.3533 0.3699 0.3624 0.0262  -0.0233 -0.0027 1058 ASP A OD2 
7787  N N   . GLY A 1061 ? 0.3099 0.3277 0.3250 0.0224  -0.0236 -0.0132 1059 GLY A N   
7788  C CA  . GLY A 1061 ? 0.2991 0.3185 0.3180 0.0216  -0.0239 -0.0148 1059 GLY A CA  
7789  C C   . GLY A 1061 ? 0.3509 0.3717 0.3690 0.0210  -0.0256 -0.0162 1059 GLY A C   
7790  O O   . GLY A 1061 ? 0.3236 0.3466 0.3448 0.0209  -0.0268 -0.0170 1059 GLY A O   
7791  N N   . LYS A 1062 ? 0.2847 0.3043 0.2991 0.0208  -0.0259 -0.0169 1060 LYS A N   
7792  C CA  . LYS A 1062 ? 0.3237 0.3444 0.3376 0.0204  -0.0278 -0.0187 1060 LYS A CA  
7793  C C   . LYS A 1062 ? 0.3353 0.3586 0.3475 0.0219  -0.0299 -0.0184 1060 LYS A C   
7794  O O   . LYS A 1062 ? 0.3784 0.4032 0.3905 0.0218  -0.0318 -0.0202 1060 LYS A O   
7795  C CB  . LYS A 1062 ? 0.3349 0.3534 0.3460 0.0197  -0.0276 -0.0201 1060 LYS A CB  
7796  C CG  . LYS A 1062 ? 0.3368 0.3533 0.3499 0.0177  -0.0262 -0.0205 1060 LYS A CG  
7797  C CD  . LYS A 1062 ? 0.4166 0.4347 0.4338 0.0163  -0.0273 -0.0215 1060 LYS A CD  
7798  C CE  . LYS A 1062 ? 0.4469 0.4640 0.4664 0.0142  -0.0259 -0.0213 1060 LYS A CE  
7799  N NZ  . LYS A 1062 ? 0.4587 0.4780 0.4826 0.0126  -0.0270 -0.0218 1060 LYS A NZ  
7800  N N   . GLY A 1063 ? 0.3121 0.3364 0.3234 0.0233  -0.0297 -0.0161 1061 GLY A N   
7801  C CA  . GLY A 1063 ? 0.3576 0.3850 0.3671 0.0246  -0.0316 -0.0151 1061 GLY A CA  
7802  C C   . GLY A 1063 ? 0.3682 0.3966 0.3726 0.0254  -0.0319 -0.0151 1061 GLY A C   
7803  O O   . GLY A 1063 ? 0.3780 0.4101 0.3806 0.0265  -0.0335 -0.0144 1061 GLY A O   
7804  N N   . ALA A 1064 ? 0.3188 0.3446 0.3211 0.0249  -0.0303 -0.0159 1062 ALA A N   
7805  C CA  . ALA A 1064 ? 0.2929 0.3197 0.2904 0.0257  -0.0304 -0.0161 1062 ALA A CA  
7806  C C   . ALA A 1064 ? 0.2888 0.3162 0.2848 0.0265  -0.0293 -0.0125 1062 ALA A C   
7807  O O   . ALA A 1064 ? 0.2753 0.3003 0.2700 0.0263  -0.0275 -0.0117 1062 ALA A O   
7808  C CB  . ALA A 1064 ? 0.3108 0.3346 0.3074 0.0248  -0.0294 -0.0186 1062 ALA A CB  
7809  N N   . ARG A 1065 ? 0.2562 0.2869 0.2528 0.0275  -0.0305 -0.0100 1063 ARG A N   
7810  C CA  A ARG A 1065 ? 0.2804 0.3115 0.2773 0.0280  -0.0298 -0.0059 1063 ARG A CA  
7811  C CA  B ARG A 1065 ? 0.2805 0.3115 0.2775 0.0280  -0.0298 -0.0059 1063 ARG A CA  
7812  C C   . ARG A 1065 ? 0.2781 0.3108 0.2704 0.0286  -0.0291 -0.0047 1063 ARG A C   
7813  O O   . ARG A 1065 ? 0.2895 0.3199 0.2817 0.0284  -0.0276 -0.0027 1063 ARG A O   
7814  C CB  A ARG A 1065 ? 0.3165 0.3510 0.3156 0.0288  -0.0318 -0.0033 1063 ARG A CB  
7815  C CB  B ARG A 1065 ? 0.3165 0.3509 0.3156 0.0288  -0.0317 -0.0032 1063 ARG A CB  
7816  C CG  A ARG A 1065 ? 0.3526 0.3865 0.3561 0.0284  -0.0327 -0.0049 1063 ARG A CG  
7817  C CG  B ARG A 1065 ? 0.3523 0.3863 0.3557 0.0284  -0.0328 -0.0049 1063 ARG A CG  
7818  C CD  A ARG A 1065 ? 0.3550 0.3846 0.3629 0.0277  -0.0311 -0.0050 1063 ARG A CD  
7819  C CD  B ARG A 1065 ? 0.3544 0.3839 0.3619 0.0275  -0.0311 -0.0058 1063 ARG A CD  
7820  N NE  A ARG A 1065 ? 0.3530 0.3827 0.3652 0.0273  -0.0319 -0.0066 1063 ARG A NE  
7821  N NE  B ARG A 1065 ? 0.3600 0.3881 0.3703 0.0279  -0.0304 -0.0027 1063 ARG A NE  
7822  C CZ  A ARG A 1065 ? 0.3462 0.3740 0.3631 0.0271  -0.0311 -0.0066 1063 ARG A CZ  
7823  C CZ  B ARG A 1065 ? 0.3432 0.3686 0.3579 0.0275  -0.0294 -0.0032 1063 ARG A CZ  
7824  N NH1 A ARG A 1065 ? 0.4035 0.4288 0.4217 0.0271  -0.0296 -0.0053 1063 ARG A NH1 
7825  N NH1 B ARG A 1065 ? 0.3938 0.4181 0.4104 0.0266  -0.0287 -0.0062 1063 ARG A NH1 
7826  N NH2 A ARG A 1065 ? 0.3459 0.3747 0.3666 0.0268  -0.0318 -0.0082 1063 ARG A NH2 
7827  N NH2 B ARG A 1065 ? 0.3791 0.4032 0.3966 0.0280  -0.0290 -0.0006 1063 ARG A NH2 
7828  N N   . ALA A 1066 ? 0.2843 0.3214 0.2728 0.0293  -0.0304 -0.0061 1064 ALA A N   
7829  C CA  . ALA A 1066 ? 0.2765 0.3162 0.2605 0.0299  -0.0297 -0.0052 1064 ALA A CA  
7830  C C   . ALA A 1066 ? 0.2547 0.2901 0.2376 0.0293  -0.0277 -0.0073 1064 ALA A C   
7831  O O   . ALA A 1066 ? 0.2683 0.3035 0.2493 0.0294  -0.0263 -0.0053 1064 ALA A O   
7832  C CB  . ALA A 1066 ? 0.2770 0.3230 0.2573 0.0309  -0.0314 -0.0071 1064 ALA A CB  
7833  N N   . GLU A 1067 ? 0.2470 0.2789 0.2313 0.0285  -0.0277 -0.0111 1065 GLU A N   
7834  C CA  . GLU A 1067 ? 0.2522 0.2800 0.2359 0.0278  -0.0260 -0.0129 1065 GLU A CA  
7835  C C   . GLU A 1067 ? 0.2467 0.2704 0.2326 0.0270  -0.0241 -0.0103 1065 GLU A C   
7836  O O   . GLU A 1067 ? 0.2493 0.2710 0.2337 0.0268  -0.0225 -0.0099 1065 GLU A O   
7837  C CB  . GLU A 1067 ? 0.2775 0.3030 0.2631 0.0270  -0.0268 -0.0170 1065 GLU A CB  
7838  C CG  . GLU A 1067 ? 0.2820 0.3109 0.2654 0.0279  -0.0288 -0.0206 1065 GLU A CG  
7839  C CD  . GLU A 1067 ? 0.3720 0.4052 0.3561 0.0285  -0.0310 -0.0208 1065 GLU A CD  
7840  O OE1 . GLU A 1067 ? 0.2937 0.3267 0.2803 0.0282  -0.0311 -0.0183 1065 GLU A OE1 
7841  O OE2 . GLU A 1067 ? 0.4038 0.4408 0.3860 0.0294  -0.0327 -0.0237 1065 GLU A OE2 
7842  N N   . ALA A 1068 ? 0.2728 0.2952 0.2626 0.0266  -0.0242 -0.0089 1066 ALA A N   
7843  C CA  . ALA A 1068 ? 0.2265 0.2456 0.2188 0.0261  -0.0226 -0.0068 1066 ALA A CA  
7844  C C   . ALA A 1068 ? 0.2457 0.2660 0.2365 0.0268  -0.0220 -0.0032 1066 ALA A C   
7845  O O   . ALA A 1068 ? 0.2431 0.2606 0.2339 0.0264  -0.0204 -0.0023 1066 ALA A O   
7846  C CB  . ALA A 1068 ? 0.2636 0.2823 0.2607 0.0259  -0.0232 -0.0061 1066 ALA A CB  
7847  N N   . GLU A 1069 ? 0.2650 0.2897 0.2546 0.0277  -0.0234 -0.0009 1067 GLU A N   
7848  C CA  . GLU A 1069 ? 0.2513 0.2781 0.2396 0.0282  -0.0231 0.0030  1067 GLU A CA  
7849  C C   . GLU A 1069 ? 0.2521 0.2793 0.2360 0.0283  -0.0218 0.0020  1067 GLU A C   
7850  O O   . GLU A 1069 ? 0.2671 0.2930 0.2509 0.0281  -0.0205 0.0043  1067 GLU A O   
7851  C CB  . GLU A 1069 ? 0.2916 0.3242 0.2792 0.0291  -0.0250 0.0058  1067 GLU A CB  
7852  C CG  . GLU A 1069 ? 0.3560 0.3921 0.3417 0.0294  -0.0249 0.0103  1067 GLU A CG  
7853  C CD  . GLU A 1069 ? 0.4237 0.4572 0.4141 0.0291  -0.0248 0.0145  1067 GLU A CD  
7854  O OE1 . GLU A 1069 ? 0.5091 0.5382 0.5041 0.0287  -0.0246 0.0135  1067 GLU A OE1 
7855  O OE2 . GLU A 1069 ? 0.5337 0.5700 0.5236 0.0292  -0.0248 0.0189  1067 GLU A OE2 
7856  N N   . ALA A 1070 ? 0.2720 0.3010 0.2527 0.0286  -0.0223 -0.0016 1068 ALA A N   
7857  C CA  . ALA A 1070 ? 0.2496 0.2791 0.2266 0.0288  -0.0212 -0.0032 1068 ALA A CA  
7858  C C   . ALA A 1070 ? 0.2455 0.2690 0.2239 0.0278  -0.0193 -0.0043 1068 ALA A C   
7859  O O   . ALA A 1070 ? 0.2419 0.2648 0.2185 0.0278  -0.0180 -0.0036 1068 ALA A O   
7860  C CB  . ALA A 1070 ? 0.2579 0.2902 0.2323 0.0294  -0.0224 -0.0075 1068 ALA A CB  
7861  N N   . ALA A 1071 ? 0.2303 0.2498 0.2120 0.0269  -0.0193 -0.0060 1069 ALA A N   
7862  C CA  . ALA A 1071 ? 0.2108 0.2253 0.1939 0.0258  -0.0176 -0.0068 1069 ALA A CA  
7863  C C   . ALA A 1071 ? 0.2361 0.2489 0.2206 0.0257  -0.0163 -0.0033 1069 ALA A C   
7864  O O   . ALA A 1071 ? 0.2037 0.2145 0.1871 0.0254  -0.0148 -0.0031 1069 ALA A O   
7865  C CB  . ALA A 1071 ? 0.2214 0.2332 0.2079 0.0248  -0.0179 -0.0088 1069 ALA A CB  
7866  N N   . ARG A 1072 ? 0.2308 0.2447 0.2181 0.0260  -0.0171 -0.0007 1070 ARG A N   
7867  C CA  . ARG A 1072 ? 0.2353 0.2478 0.2248 0.0259  -0.0163 0.0026  1070 ARG A CA  
7868  C C   . ARG A 1072 ? 0.2378 0.2525 0.2241 0.0264  -0.0157 0.0050  1070 ARG A C   
7869  O O   . ARG A 1072 ? 0.2540 0.2665 0.2407 0.0260  -0.0144 0.0063  1070 ARG A O   
7870  C CB  . ARG A 1072 ? 0.2436 0.2571 0.2372 0.0263  -0.0176 0.0051  1070 ARG A CB  
7871  C CG  . ARG A 1072 ? 0.2704 0.2813 0.2682 0.0259  -0.0177 0.0030  1070 ARG A CG  
7872  C CD  . ARG A 1072 ? 0.3101 0.3219 0.3128 0.0264  -0.0191 0.0054  1070 ARG A CD  
7873  N NE  . ARG A 1072 ? 0.3142 0.3301 0.3160 0.0271  -0.0210 0.0066  1070 ARG A NE  
7874  C CZ  . ARG A 1072 ? 0.3207 0.3377 0.3233 0.0271  -0.0221 0.0045  1070 ARG A CZ  
7875  N NH1 . ARG A 1072 ? 0.3065 0.3212 0.3110 0.0265  -0.0214 0.0013  1070 ARG A NH1 
7876  N NH2 . ARG A 1072 ? 0.3427 0.3638 0.3443 0.0278  -0.0239 0.0059  1070 ARG A NH2 
7877  N N   . ASN A 1073 ? 0.2296 0.2493 0.2126 0.0272  -0.0168 0.0056  1071 ASN A N   
7878  C CA  . ASN A 1073 ? 0.2308 0.2540 0.2105 0.0276  -0.0162 0.0078  1071 ASN A CA  
7879  C C   . ASN A 1073 ? 0.2420 0.2629 0.2191 0.0274  -0.0146 0.0051  1071 ASN A C   
7880  O O   . ASN A 1073 ? 0.2642 0.2849 0.2405 0.0273  -0.0134 0.0072  1071 ASN A O   
7881  C CB  . ASN A 1073 ? 0.2563 0.2862 0.2327 0.0286  -0.0177 0.0081  1071 ASN A CB  
7882  C CG  . ASN A 1073 ? 0.3255 0.3585 0.3043 0.0288  -0.0193 0.0122  1071 ASN A CG  
7883  O OD1 . ASN A 1073 ? 0.3511 0.3816 0.3340 0.0283  -0.0193 0.0155  1071 ASN A OD1 
7884  N ND2 . ASN A 1073 ? 0.3600 0.3985 0.3367 0.0295  -0.0208 0.0119  1071 ASN A ND2 
7885  N N   . ALA A 1074 ? 0.2192 0.2381 0.1954 0.0272  -0.0146 0.0007  1072 ALA A N   
7886  C CA  . ALA A 1074 ? 0.2374 0.2538 0.2118 0.0269  -0.0133 -0.0018 1072 ALA A CA  
7887  C C   . ALA A 1074 ? 0.2406 0.2521 0.2176 0.0259  -0.0118 -0.0006 1072 ALA A C   
7888  O O   . ALA A 1074 ? 0.2228 0.2332 0.1983 0.0258  -0.0105 -0.0003 1072 ALA A O   
7889  C CB  . ALA A 1074 ? 0.2539 0.2691 0.2282 0.0267  -0.0141 -0.0064 1072 ALA A CB  
7890  N N   . GLY A 1075 ? 0.2234 0.2321 0.2040 0.0252  -0.0119 -0.0002 1073 GLY A N   
7891  C CA  . GLY A 1075 ? 0.2267 0.2313 0.2099 0.0244  -0.0106 0.0006  1073 GLY A CA  
7892  C C   . GLY A 1075 ? 0.2194 0.2245 0.2028 0.0247  -0.0099 0.0041  1073 GLY A C   
7893  O O   . GLY A 1075 ? 0.2416 0.2441 0.2250 0.0242  -0.0086 0.0043  1073 GLY A O   
7894  N N   . SER A 1076 ? 0.2341 0.2427 0.2179 0.0253  -0.0110 0.0074  1074 SER A N   
7895  C CA  . SER A 1076 ? 0.2590 0.2688 0.2436 0.0254  -0.0107 0.0115  1074 SER A CA  
7896  C C   . SER A 1076 ? 0.2815 0.2939 0.2616 0.0257  -0.0098 0.0118  1074 SER A C   
7897  O O   . SER A 1076 ? 0.2790 0.2905 0.2595 0.0254  -0.0088 0.0138  1074 SER A O   
7898  C CB  . SER A 1076 ? 0.3020 0.3152 0.2886 0.0259  -0.0124 0.0153  1074 SER A CB  
7899  O OG  . SER A 1076 ? 0.3963 0.4068 0.3880 0.0257  -0.0132 0.0155  1074 SER A OG  
7900  N N   . SER A 1077 ? 0.2315 0.2478 0.2078 0.0264  -0.0103 0.0098  1075 SER A N   
7901  C CA  A SER A 1077 ? 0.2606 0.2807 0.2329 0.0269  -0.0096 0.0098  1075 SER A CA  
7902  C CA  B SER A 1077 ? 0.2607 0.2808 0.2329 0.0270  -0.0096 0.0097  1075 SER A CA  
7903  C C   . SER A 1077 ? 0.2411 0.2574 0.2123 0.0266  -0.0081 0.0068  1075 SER A C   
7904  O O   . SER A 1077 ? 0.2581 0.2762 0.2271 0.0269  -0.0071 0.0074  1075 SER A O   
7905  C CB  A SER A 1077 ? 0.2746 0.3004 0.2436 0.0280  -0.0108 0.0078  1075 SER A CB  
7906  C CB  B SER A 1077 ? 0.2742 0.2997 0.2432 0.0280  -0.0108 0.0074  1075 SER A CB  
7907  O OG  A SER A 1077 ? 0.3145 0.3450 0.2839 0.0283  -0.0120 0.0116  1075 SER A OG  
7908  O OG  B SER A 1077 ? 0.3265 0.3559 0.2915 0.0287  -0.0102 0.0061  1075 SER A OG  
7909  N N   . SER A 1078 ? 0.2215 0.2329 0.1943 0.0259  -0.0080 0.0037  1076 SER A N   
7910  C CA  . SER A 1078 ? 0.2567 0.2645 0.2289 0.0254  -0.0068 0.0012  1076 SER A CA  
7911  C C   . SER A 1078 ? 0.2282 0.2340 0.2013 0.0249  -0.0054 0.0038  1076 SER A C   
7912  O O   . SER A 1078 ? 0.2350 0.2395 0.2111 0.0245  -0.0054 0.0066  1076 SER A O   
7913  C CB  . SER A 1078 ? 0.2291 0.2324 0.2037 0.0245  -0.0069 -0.0013 1076 SER A CB  
7914  O OG  . SER A 1078 ? 0.2158 0.2157 0.1902 0.0238  -0.0059 -0.0030 1076 SER A OG  
7915  N N   . ALA A 1079 ? 0.2062 0.2119 0.1773 0.0250  -0.0044 0.0028  1077 ALA A N   
7916  C CA  . ALA A 1079 ? 0.1956 0.1991 0.1676 0.0245  -0.0030 0.0048  1077 ALA A CA  
7917  C C   . ALA A 1079 ? 0.2334 0.2317 0.2068 0.0235  -0.0022 0.0026  1077 ALA A C   
7918  O O   . ALA A 1079 ? 0.2091 0.2054 0.1828 0.0230  -0.0011 0.0035  1077 ALA A O   
7919  C CB  . ALA A 1079 ? 0.2147 0.2220 0.1838 0.0252  -0.0023 0.0058  1077 ALA A CB  
7920  N N   . LEU A 1080 ? 0.2143 0.2105 0.1885 0.0230  -0.0028 -0.0001 1078 LEU A N   
7921  C CA  . LEU A 1080 ? 0.2152 0.2072 0.1911 0.0219  -0.0022 -0.0017 1078 LEU A CA  
7922  C C   . LEU A 1080 ? 0.2147 0.2046 0.1932 0.0212  -0.0013 0.0004  1078 LEU A C   
7923  O O   . LEU A 1080 ? 0.2267 0.2173 0.2074 0.0214  -0.0019 0.0021  1078 LEU A O   
7924  C CB  . LEU A 1080 ? 0.2099 0.2011 0.1871 0.0214  -0.0031 -0.0038 1078 LEU A CB  
7925  C CG  . LEU A 1080 ? 0.2137 0.2016 0.1930 0.0200  -0.0025 -0.0050 1078 LEU A CG  
7926  C CD1 . LEU A 1080 ? 0.2564 0.2428 0.2343 0.0195  -0.0023 -0.0067 1078 LEU A CD1 
7927  C CD2 . LEU A 1080 ? 0.2287 0.2167 0.2098 0.0195  -0.0034 -0.0063 1078 LEU A CD2 
7928  N N   . GLY A 1081 ? 0.2133 0.2008 0.1920 0.0206  -0.0002 0.0001  1079 GLY A N   
7929  C CA  . GLY A 1081 ? 0.2384 0.2242 0.2198 0.0200  0.0004  0.0016  1079 GLY A CA  
7930  C C   . GLY A 1081 ? 0.2364 0.2229 0.2176 0.0204  0.0010  0.0044  1079 GLY A C   
7931  O O   . GLY A 1081 ? 0.2506 0.2354 0.2345 0.0200  0.0014  0.0055  1079 GLY A O   
7932  N N   . LEU A 1082 ? 0.2011 0.1906 0.1797 0.0212  0.0008  0.0054  1080 LEU A N   
7933  C CA  A LEU A 1082 ? 0.2028 0.1936 0.1811 0.0215  0.0015  0.0082  1080 LEU A CA  
7934  C CA  B LEU A 1082 ? 0.2036 0.1944 0.1818 0.0215  0.0015  0.0082  1080 LEU A CA  
7935  C C   . LEU A 1082 ? 0.2336 0.2214 0.2121 0.0207  0.0027  0.0073  1080 LEU A C   
7936  O O   . LEU A 1082 ? 0.2270 0.2132 0.2040 0.0204  0.0030  0.0047  1080 LEU A O   
7937  C CB  A LEU A 1082 ? 0.2221 0.2173 0.1967 0.0224  0.0014  0.0084  1080 LEU A CB  
7938  C CB  B LEU A 1082 ? 0.2221 0.2173 0.1966 0.0224  0.0014  0.0084  1080 LEU A CB  
7939  C CG  A LEU A 1082 ? 0.2204 0.2183 0.1942 0.0227  0.0021  0.0113  1080 LEU A CG  
7940  C CG  B LEU A 1082 ? 0.2206 0.2188 0.1943 0.0227  0.0021  0.0113  1080 LEU A CG  
7941  C CD1 A LEU A 1082 ? 0.2261 0.2244 0.2033 0.0223  0.0017  0.0155  1080 LEU A CD1 
7942  C CD1 B LEU A 1082 ? 0.2337 0.2380 0.2046 0.0238  0.0016  0.0123  1080 LEU A CD1 
7943  C CD2 A LEU A 1082 ? 0.2331 0.2366 0.2033 0.0238  0.0020  0.0110  1080 LEU A CD2 
7944  C CD2 B LEU A 1082 ? 0.2235 0.2202 0.1957 0.0226  0.0033  0.0096  1080 LEU A CD2 
7945  N N   . ASP A 1083 ? 0.2179 0.2049 0.1986 0.0204  0.0031  0.0098  1081 ASP A N   
7946  C CA  . ASP A 1083 ? 0.2717 0.2559 0.2531 0.0197  0.0041  0.0090  1081 ASP A CA  
7947  C C   . ASP A 1083 ? 0.2704 0.2556 0.2531 0.0197  0.0044  0.0123  1081 ASP A C   
7948  O O   . ASP A 1083 ? 0.3030 0.2875 0.2894 0.0195  0.0038  0.0144  1081 ASP A O   
7949  C CB  . ASP A 1083 ? 0.2802 0.2614 0.2647 0.0189  0.0039  0.0075  1081 ASP A CB  
7950  C CG  . ASP A 1083 ? 0.4126 0.3914 0.3976 0.0181  0.0048  0.0064  1081 ASP A CG  
7951  O OD1 . ASP A 1083 ? 0.4105 0.3894 0.3934 0.0181  0.0056  0.0065  1081 ASP A OD1 
7952  O OD2 . ASP A 1083 ? 0.4484 0.4257 0.4363 0.0176  0.0048  0.0053  1081 ASP A OD2 
7953  N N   . LEU A 1084 ? 0.2553 0.2422 0.2353 0.0200  0.0052  0.0128  1082 LEU A N   
7954  C CA  . LEU A 1084 ? 0.2496 0.2385 0.2304 0.0200  0.0055  0.0162  1082 LEU A CA  
7955  C C   . LEU A 1084 ? 0.2428 0.2299 0.2233 0.0195  0.0066  0.0155  1082 LEU A C   
7956  O O   . LEU A 1084 ? 0.2619 0.2475 0.2404 0.0195  0.0072  0.0126  1082 LEU A O   
7957  C CB  . LEU A 1084 ? 0.2857 0.2800 0.2635 0.0209  0.0056  0.0177  1082 LEU A CB  
7958  C CG  . LEU A 1084 ? 0.2909 0.2884 0.2682 0.0215  0.0045  0.0187  1082 LEU A CG  
7959  C CD1 . LEU A 1084 ? 0.3026 0.3062 0.2760 0.0225  0.0047  0.0191  1082 LEU A CD1 
7960  C CD2 . LEU A 1084 ? 0.3222 0.3198 0.3037 0.0210  0.0035  0.0227  1082 LEU A CD2 
7961  N N   . GLU A 1085 ? 0.2511 0.2384 0.2341 0.0191  0.0068  0.0185  1083 GLU A N   
7962  C CA  . GLU A 1085 ? 0.2209 0.2076 0.2035 0.0188  0.0079  0.0186  1083 GLU A CA  
7963  C C   . GLU A 1085 ? 0.2558 0.2474 0.2366 0.0193  0.0083  0.0214  1083 GLU A C   
7964  O O   . GLU A 1085 ? 0.2882 0.2828 0.2708 0.0193  0.0077  0.0251  1083 GLU A O   
7965  C CB  . GLU A 1085 ? 0.2573 0.2408 0.2442 0.0179  0.0077  0.0198  1083 GLU A CB  
7966  C CG  . GLU A 1085 ? 0.3021 0.2854 0.2886 0.0175  0.0087  0.0201  1083 GLU A CG  
7967  C CD  . GLU A 1085 ? 0.3941 0.3737 0.3842 0.0166  0.0086  0.0198  1083 GLU A CD  
7968  O OE1 . GLU A 1085 ? 0.4189 0.3961 0.4119 0.0163  0.0079  0.0187  1083 GLU A OE1 
7969  O OE2 . GLU A 1085 ? 0.4109 0.3906 0.4010 0.0163  0.0094  0.0206  1083 GLU A OE2 
7970  N N   . LEU A 1086 ? 0.2602 0.2534 0.2379 0.0198  0.0092  0.0196  1084 LEU A N   
7971  C CA  . LEU A 1086 ? 0.2490 0.2479 0.2246 0.0205  0.0098  0.0215  1084 LEU A CA  
7972  C C   . LEU A 1086 ? 0.2973 0.2964 0.2747 0.0199  0.0106  0.0239  1084 LEU A C   
7973  O O   . LEU A 1086 ? 0.2694 0.2644 0.2477 0.0194  0.0110  0.0222  1084 LEU A O   
7974  C CB  . LEU A 1086 ? 0.2715 0.2723 0.2432 0.0216  0.0102  0.0177  1084 LEU A CB  
7975  C CG  . LEU A 1086 ? 0.3183 0.3187 0.2885 0.0222  0.0092  0.0149  1084 LEU A CG  
7976  C CD1 . LEU A 1086 ? 0.2823 0.2847 0.2495 0.0234  0.0093  0.0110  1084 LEU A CD1 
7977  C CD2 . LEU A 1086 ? 0.3327 0.3370 0.3030 0.0225  0.0085  0.0176  1084 LEU A CD2 
7978  N N   . PRO A 1087 ? 0.2892 0.2933 0.2672 0.0199  0.0107  0.0280  1085 PRO A N   
7979  C CA  . PRO A 1087 ? 0.3248 0.3295 0.3048 0.0192  0.0114  0.0307  1085 PRO A CA  
7980  C C   . PRO A 1087 ? 0.2874 0.2925 0.2648 0.0198  0.0126  0.0276  1085 PRO A C   
7981  O O   . PRO A 1087 ? 0.3267 0.3351 0.3005 0.0210  0.0130  0.0250  1085 PRO A O   
7982  C CB  . PRO A 1087 ? 0.3507 0.3624 0.3311 0.0192  0.0114  0.0356  1085 PRO A CB  
7983  C CG  . PRO A 1087 ? 0.3700 0.3833 0.3500 0.0195  0.0103  0.0363  1085 PRO A CG  
7984  C CD  . PRO A 1087 ? 0.2959 0.3056 0.2732 0.0203  0.0101  0.0309  1085 PRO A CD  
7985  N N   . GLY A 1088 ? 0.3008 0.3027 0.2803 0.0190  0.0131  0.0278  1086 GLY A N   
7986  C CA  . GLY A 1088 ? 0.3018 0.3036 0.2794 0.0195  0.0140  0.0253  1086 GLY A CA  
7987  C C   . GLY A 1088 ? 0.2268 0.2263 0.2075 0.0184  0.0144  0.0270  1086 GLY A C   
7988  O O   . GLY A 1088 ? 0.2656 0.2650 0.2498 0.0175  0.0140  0.0307  1086 GLY A O   
7989  N N   . PRO A 1089 ? 0.2566 0.2540 0.2363 0.0186  0.0150  0.0242  1087 PRO A N   
7990  C CA  . PRO A 1089 ? 0.2479 0.2433 0.2302 0.0177  0.0154  0.0255  1087 PRO A CA  
7991  C C   . PRO A 1089 ? 0.2907 0.2803 0.2762 0.0165  0.0145  0.0254  1087 PRO A C   
7992  O O   . PRO A 1089 ? 0.2640 0.2506 0.2491 0.0164  0.0139  0.0233  1087 PRO A O   
7993  C CB  . PRO A 1089 ? 0.2917 0.2863 0.2719 0.0183  0.0160  0.0221  1087 PRO A CB  
7994  C CG  . PRO A 1089 ? 0.3307 0.3236 0.3084 0.0190  0.0154  0.0184  1087 PRO A CG  
7995  C CD  . PRO A 1089 ? 0.2674 0.2641 0.2440 0.0196  0.0151  0.0198  1087 PRO A CD  
7996  N N   . VAL A 1090 ? 0.2532 0.2418 0.2421 0.0155  0.0145  0.0276  1088 VAL A N   
7997  C CA  . VAL A 1090 ? 0.2220 0.2055 0.2141 0.0145  0.0137  0.0267  1088 VAL A CA  
7998  C C   . VAL A 1090 ? 0.2453 0.2255 0.2353 0.0145  0.0139  0.0225  1088 VAL A C   
7999  O O   . VAL A 1090 ? 0.2469 0.2282 0.2339 0.0151  0.0146  0.0209  1088 VAL A O   
8000  C CB  . VAL A 1090 ? 0.2579 0.2411 0.2544 0.0136  0.0135  0.0294  1088 VAL A CB  
8001  C CG1 . VAL A 1090 ? 0.2749 0.2616 0.2742 0.0133  0.0130  0.0342  1088 VAL A CG1 
8002  C CG2 . VAL A 1090 ? 0.2735 0.2579 0.2686 0.0136  0.0145  0.0291  1088 VAL A CG2 
8003  N N   . GLY A 1091 ? 0.2384 0.2149 0.2302 0.0138  0.0132  0.0209  1089 GLY A N   
8004  C CA  . GLY A 1091 ? 0.2893 0.2632 0.2795 0.0136  0.0133  0.0176  1089 GLY A CA  
8005  C C   . GLY A 1091 ? 0.2365 0.2104 0.2232 0.0141  0.0133  0.0152  1089 GLY A C   
8006  O O   . GLY A 1091 ? 0.2463 0.2188 0.2316 0.0139  0.0134  0.0130  1089 GLY A O   
8007  N N   . GLU A 1092 ? 0.2320 0.2076 0.2178 0.0148  0.0131  0.0159  1090 GLU A N   
8008  C CA  . GLU A 1092 ? 0.2671 0.2428 0.2502 0.0154  0.0129  0.0137  1090 GLU A CA  
8009  C C   . GLU A 1092 ? 0.2491 0.2254 0.2329 0.0156  0.0123  0.0144  1090 GLU A C   
8010  O O   . GLU A 1092 ? 0.2686 0.2466 0.2542 0.0157  0.0121  0.0172  1090 GLU A O   
8011  C CB  . GLU A 1092 ? 0.2894 0.2681 0.2697 0.0165  0.0134  0.0134  1090 GLU A CB  
8012  C CG  . GLU A 1092 ? 0.3465 0.3245 0.3245 0.0169  0.0131  0.0104  1090 GLU A CG  
8013  C CD  . GLU A 1092 ? 0.3735 0.3545 0.3498 0.0182  0.0135  0.0096  1090 GLU A CD  
8014  O OE1 . GLU A 1092 ? 0.3187 0.3034 0.2936 0.0192  0.0136  0.0101  1090 GLU A OE1 
8015  O OE2 . GLU A 1092 ? 0.3903 0.3704 0.3666 0.0182  0.0137  0.0085  1090 GLU A OE2 
8016  N N   . ARG A 1093 ? 0.2194 0.1942 0.2021 0.0156  0.0118  0.0122  1091 ARG A N   
8017  C CA  . ARG A 1093 ? 0.2596 0.2353 0.2425 0.0160  0.0112  0.0125  1091 ARG A CA  
8018  C C   . ARG A 1093 ? 0.2378 0.2149 0.2175 0.0167  0.0111  0.0108  1091 ARG A C   
8019  O O   . ARG A 1093 ? 0.2423 0.2179 0.2208 0.0165  0.0110  0.0084  1091 ARG A O   
8020  C CB  . ARG A 1093 ? 0.2846 0.2579 0.2699 0.0153  0.0106  0.0113  1091 ARG A CB  
8021  C CG  . ARG A 1093 ? 0.4160 0.3886 0.4055 0.0149  0.0101  0.0131  1091 ARG A CG  
8022  C CD  . ARG A 1093 ? 0.5309 0.5023 0.5230 0.0148  0.0093  0.0118  1091 ARG A CD  
8023  N NE  . ARG A 1093 ? 0.5898 0.5601 0.5808 0.0143  0.0094  0.0086  1091 ARG A NE  
8024  C CZ  . ARG A 1093 ? 0.5993 0.5685 0.5917 0.0135  0.0096  0.0071  1091 ARG A CZ  
8025  N NH1 . ARG A 1093 ? 0.5664 0.5350 0.5618 0.0133  0.0094  0.0080  1091 ARG A NH1 
8026  N NH2 . ARG A 1093 ? 0.6093 0.5784 0.6003 0.0130  0.0097  0.0046  1091 ARG A NH2 
8027  N N   . ASN A 1094 ? 0.2249 0.2053 0.2035 0.0176  0.0110  0.0121  1092 ASN A N   
8028  C CA  . ASN A 1094 ? 0.2046 0.1870 0.1804 0.0186  0.0108  0.0103  1092 ASN A CA  
8029  C C   . ASN A 1094 ? 0.2103 0.1934 0.1861 0.0189  0.0100  0.0104  1092 ASN A C   
8030  O O   . ASN A 1094 ? 0.2343 0.2197 0.2110 0.0191  0.0098  0.0131  1092 ASN A O   
8031  C CB  . ASN A 1094 ? 0.2028 0.1893 0.1768 0.0196  0.0113  0.0111  1092 ASN A CB  
8032  C CG  . ASN A 1094 ? 0.2310 0.2166 0.2048 0.0195  0.0120  0.0101  1092 ASN A CG  
8033  O OD1 . ASN A 1094 ? 0.2397 0.2234 0.2127 0.0196  0.0117  0.0073  1092 ASN A OD1 
8034  N ND2 . ASN A 1094 ? 0.2587 0.2455 0.2337 0.0193  0.0127  0.0126  1092 ASN A ND2 
8035  N N   . LEU A 1095 ? 0.2178 0.1990 0.1930 0.0187  0.0094  0.0078  1093 LEU A N   
8036  C CA  . LEU A 1095 ? 0.2292 0.2105 0.2049 0.0187  0.0086  0.0077  1093 LEU A CA  
8037  C C   . LEU A 1095 ? 0.2427 0.2262 0.2160 0.0197  0.0080  0.0058  1093 LEU A C   
8038  O O   . LEU A 1095 ? 0.2407 0.2240 0.2126 0.0200  0.0080  0.0036  1093 LEU A O   
8039  C CB  . LEU A 1095 ? 0.2562 0.2341 0.2336 0.0177  0.0083  0.0061  1093 LEU A CB  
8040  C CG  . LEU A 1095 ? 0.2956 0.2716 0.2756 0.0168  0.0088  0.0071  1093 LEU A CG  
8041  C CD1 . LEU A 1095 ? 0.3572 0.3310 0.3386 0.0159  0.0086  0.0052  1093 LEU A CD1 
8042  C CD2 . LEU A 1095 ? 0.3320 0.3090 0.3145 0.0171  0.0086  0.0099  1093 LEU A CD2 
8043  N N   . TYR A 1096 ? 0.2269 0.2123 0.2001 0.0202  0.0074  0.0065  1094 TYR A N   
8044  C CA  . TYR A 1096 ? 0.2150 0.2029 0.1860 0.0211  0.0066  0.0047  1094 TYR A CA  
8045  C C   . TYR A 1096 ? 0.2224 0.2096 0.1945 0.0209  0.0057  0.0045  1094 TYR A C   
8046  O O   . TYR A 1096 ? 0.2483 0.2360 0.2221 0.0207  0.0056  0.0069  1094 TYR A O   
8047  C CB  . TYR A 1096 ? 0.2211 0.2144 0.1904 0.0223  0.0068  0.0065  1094 TYR A CB  
8048  C CG  . TYR A 1096 ? 0.2421 0.2392 0.2093 0.0234  0.0060  0.0048  1094 TYR A CG  
8049  C CD1 . TYR A 1096 ? 0.2297 0.2284 0.1950 0.0244  0.0057  0.0015  1094 TYR A CD1 
8050  C CD2 . TYR A 1096 ? 0.2307 0.2300 0.1980 0.0236  0.0052  0.0063  1094 TYR A CD2 
8051  C CE1 . TYR A 1096 ? 0.2622 0.2647 0.2257 0.0256  0.0048  -0.0005 1094 TYR A CE1 
8052  C CE2 . TYR A 1096 ? 0.2445 0.2477 0.2097 0.0247  0.0043  0.0046  1094 TYR A CE2 
8053  C CZ  . TYR A 1096 ? 0.2245 0.2294 0.1878 0.0257  0.0041  0.0011  1094 TYR A CZ  
8054  O OH  . TYR A 1096 ? 0.2593 0.2685 0.2207 0.0270  0.0031  -0.0011 1094 TYR A OH  
8055  N N   . THR A 1097 ? 0.2236 0.2094 0.1953 0.0208  0.0050  0.0017  1095 THR A N   
8056  C CA  . THR A 1097 ? 0.2137 0.1985 0.1868 0.0203  0.0043  0.0012  1095 THR A CA  
8057  C C   . THR A 1097 ? 0.2328 0.2191 0.2045 0.0210  0.0032  -0.0012 1095 THR A C   
8058  O O   . THR A 1097 ? 0.2355 0.2221 0.2059 0.0214  0.0029  -0.0033 1095 THR A O   
8059  C CB  . THR A 1097 ? 0.2947 0.2758 0.2698 0.0190  0.0045  0.0003  1095 THR A CB  
8060  O OG1 . THR A 1097 ? 0.3263 0.3058 0.3007 0.0185  0.0044  -0.0017 1095 THR A OG1 
8061  C CG2 . THR A 1097 ? 0.2671 0.2469 0.2439 0.0184  0.0054  0.0021  1095 THR A CG2 
8062  N N   . LEU A 1098 ? 0.2188 0.2061 0.1911 0.0211  0.0023  -0.0010 1096 LEU A N   
8063  C CA  . LEU A 1098 ? 0.2382 0.2269 0.2096 0.0217  0.0011  -0.0033 1096 LEU A CA  
8064  C C   . LEU A 1098 ? 0.2026 0.1885 0.1760 0.0206  0.0006  -0.0046 1096 LEU A C   
8065  O O   . LEU A 1098 ? 0.2102 0.1956 0.1855 0.0201  0.0007  -0.0033 1096 LEU A O   
8066  C CB  . LEU A 1098 ? 0.2231 0.2160 0.1934 0.0228  0.0004  -0.0021 1096 LEU A CB  
8067  C CG  . LEU A 1098 ? 0.2078 0.2048 0.1759 0.0238  0.0009  -0.0007 1096 LEU A CG  
8068  C CD1 . LEU A 1098 ? 0.2283 0.2301 0.1952 0.0248  0.0001  0.0006  1096 LEU A CD1 
8069  C CD2 . LEU A 1098 ? 0.2280 0.2258 0.1943 0.0246  0.0009  -0.0038 1096 LEU A CD2 
8070  N N   . HIS A 1099 ? 0.2076 0.1923 0.1812 0.0202  -0.0002 -0.0070 1097 HIS A N   
8071  C CA  . HIS A 1099 ? 0.2141 0.1967 0.1897 0.0189  -0.0008 -0.0081 1097 HIS A CA  
8072  C C   . HIS A 1099 ? 0.2296 0.2134 0.2053 0.0194  -0.0024 -0.0103 1097 HIS A C   
8073  O O   . HIS A 1099 ? 0.2287 0.2148 0.2027 0.0208  -0.0031 -0.0114 1097 HIS A O   
8074  C CB  . HIS A 1099 ? 0.2516 0.2315 0.2282 0.0177  -0.0004 -0.0086 1097 HIS A CB  
8075  C CG  . HIS A 1099 ? 0.2831 0.2618 0.2598 0.0172  0.0011  -0.0069 1097 HIS A CG  
8076  N ND1 . HIS A 1099 ? 0.3313 0.3088 0.3096 0.0159  0.0017  -0.0061 1097 HIS A ND1 
8077  C CD2 . HIS A 1099 ? 0.3013 0.2803 0.2767 0.0179  0.0020  -0.0059 1097 HIS A CD2 
8078  C CE1 . HIS A 1099 ? 0.3402 0.3170 0.3183 0.0158  0.0029  -0.0049 1097 HIS A CE1 
8079  N NE2 . HIS A 1099 ? 0.3265 0.3040 0.3030 0.0169  0.0030  -0.0045 1097 HIS A NE2 
8080  N N   . ALA A 1100 ? 0.2397 0.2224 0.2175 0.0183  -0.0031 -0.0109 1098 ALA A N   
8081  C CA  . ALA A 1100 ? 0.2376 0.2208 0.2161 0.0184  -0.0049 -0.0131 1098 ALA A CA  
8082  C C   . ALA A 1100 ? 0.2536 0.2357 0.2325 0.0185  -0.0057 -0.0151 1098 ALA A C   
8083  O O   . ALA A 1100 ? 0.2679 0.2480 0.2471 0.0179  -0.0050 -0.0145 1098 ALA A O   
8084  C CB  . ALA A 1100 ? 0.2461 0.2284 0.2273 0.0168  -0.0053 -0.0130 1098 ALA A CB  
8085  N N   . ARG A 1101 ? 0.2417 0.2250 0.2207 0.0195  -0.0075 -0.0176 1099 ARG A N   
8086  C CA  A ARG A 1101 ? 0.2627 0.2448 0.2431 0.0198  -0.0087 -0.0200 1099 ARG A CA  
8087  C CA  B ARG A 1101 ? 0.2627 0.2449 0.2431 0.0198  -0.0087 -0.0200 1099 ARG A CA  
8088  C C   . ARG A 1101 ? 0.2464 0.2255 0.2306 0.0178  -0.0099 -0.0201 1099 ARG A C   
8089  O O   . ARG A 1101 ? 0.2690 0.2459 0.2550 0.0173  -0.0104 -0.0204 1099 ARG A O   
8090  C CB  A ARG A 1101 ? 0.2658 0.2508 0.2456 0.0216  -0.0104 -0.0232 1099 ARG A CB  
8091  C CB  B ARG A 1101 ? 0.2658 0.2508 0.2456 0.0216  -0.0104 -0.0232 1099 ARG A CB  
8092  C CG  A ARG A 1101 ? 0.2802 0.2692 0.2562 0.0236  -0.0094 -0.0232 1099 ARG A CG  
8093  C CG  B ARG A 1101 ? 0.2842 0.2730 0.2605 0.0236  -0.0095 -0.0234 1099 ARG A CG  
8094  C CD  A ARG A 1101 ? 0.2669 0.2597 0.2424 0.0255  -0.0112 -0.0270 1099 ARG A CD  
8095  C CD  B ARG A 1101 ? 0.2926 0.2828 0.2692 0.0251  -0.0109 -0.0273 1099 ARG A CD  
8096  N NE  A ARG A 1101 ? 0.2657 0.2578 0.2427 0.0263  -0.0123 -0.0302 1099 ARG A NE  
8097  N NE  B ARG A 1101 ? 0.2776 0.2717 0.2510 0.0268  -0.0096 -0.0273 1099 ARG A NE  
8098  C CZ  A ARG A 1101 ? 0.2854 0.2797 0.2605 0.0277  -0.0114 -0.0309 1099 ARG A CZ  
8099  C CZ  B ARG A 1101 ? 0.2963 0.2932 0.2694 0.0286  -0.0105 -0.0308 1099 ARG A CZ  
8100  N NH1 A ARG A 1101 ? 0.2888 0.2863 0.2604 0.0282  -0.0094 -0.0283 1099 ARG A NH1 
8101  N NH1 B ARG A 1101 ? 0.2966 0.2923 0.2728 0.0290  -0.0128 -0.0348 1099 ARG A NH1 
8102  N NH2 A ARG A 1101 ? 0.2974 0.2911 0.2746 0.0285  -0.0126 -0.0343 1099 ARG A NH2 
8103  N NH2 B ARG A 1101 ? 0.2879 0.2891 0.2578 0.0300  -0.0091 -0.0303 1099 ARG A NH2 
8104  N N   . GLY A 1102 ? 0.2391 0.2184 0.2249 0.0168  -0.0106 -0.0196 1100 GLY A N   
8105  C CA  . GLY A 1102 ? 0.2758 0.2531 0.2655 0.0148  -0.0118 -0.0193 1100 GLY A CA  
8106  C C   . GLY A 1102 ? 0.2390 0.2174 0.2306 0.0146  -0.0136 -0.0205 1100 GLY A C   
8107  O O   . GLY A 1102 ? 0.2647 0.2450 0.2549 0.0149  -0.0129 -0.0199 1100 GLY A O   
8108  N N   . ARG A 1103 ? 0.2446 0.2216 0.2399 0.0141  -0.0160 -0.0223 1101 ARG A N   
8109  C CA  . ARG A 1103 ? 0.2163 0.1943 0.2139 0.0139  -0.0180 -0.0237 1101 ARG A CA  
8110  C C   . ARG A 1103 ? 0.2185 0.1980 0.2154 0.0163  -0.0197 -0.0276 1101 ARG A C   
8111  O O   . ARG A 1103 ? 0.2487 0.2271 0.2471 0.0171  -0.0210 -0.0298 1101 ARG A O   
8112  C CB  . ARG A 1103 ? 0.2620 0.2380 0.2650 0.0116  -0.0199 -0.0230 1101 ARG A CB  
8113  C CG  . ARG A 1103 ? 0.2655 0.2428 0.2711 0.0111  -0.0217 -0.0238 1101 ARG A CG  
8114  C CD  . ARG A 1103 ? 0.3064 0.2825 0.3175 0.0083  -0.0232 -0.0219 1101 ARG A CD  
8115  N NE  . ARG A 1103 ? 0.3400 0.3167 0.3504 0.0063  -0.0210 -0.0182 1101 ARG A NE  
8116  C CZ  . ARG A 1103 ? 0.3859 0.3650 0.3960 0.0053  -0.0197 -0.0163 1101 ARG A CZ  
8117  N NH1 . ARG A 1103 ? 0.3178 0.2987 0.3279 0.0059  -0.0204 -0.0176 1101 ARG A NH1 
8118  N NH2 . ARG A 1103 ? 0.4162 0.3963 0.4259 0.0036  -0.0178 -0.0134 1101 ARG A NH2 
8119  N N   . ILE A 1104 ? 0.2182 0.2006 0.2129 0.0174  -0.0197 -0.0284 1102 ILE A N   
8120  C CA  . ILE A 1104 ? 0.2224 0.2075 0.2159 0.0197  -0.0211 -0.0320 1102 ILE A CA  
8121  C C   . ILE A 1104 ? 0.1965 0.1815 0.1940 0.0193  -0.0241 -0.0344 1102 ILE A C   
8122  O O   . ILE A 1104 ? 0.2222 0.2072 0.2212 0.0179  -0.0242 -0.0328 1102 ILE A O   
8123  C CB  . ILE A 1104 ? 0.2381 0.2270 0.2268 0.0212  -0.0196 -0.0311 1102 ILE A CB  
8124  C CG1 . ILE A 1104 ? 0.2297 0.2184 0.2151 0.0212  -0.0168 -0.0281 1102 ILE A CG1 
8125  C CG2 . ILE A 1104 ? 0.2391 0.2319 0.2260 0.0236  -0.0210 -0.0349 1102 ILE A CG2 
8126  C CD1 . ILE A 1104 ? 0.2512 0.2396 0.2355 0.0223  -0.0164 -0.0294 1102 ILE A CD1 
8127  N N   . LEU A 1105 ? 0.2104 0.1954 0.2102 0.0205  -0.0265 -0.0384 1103 LEU A N   
8128  C CA  . LEU A 1105 ? 0.2273 0.2126 0.2312 0.0205  -0.0296 -0.0414 1103 LEU A CA  
8129  C C   . LEU A 1105 ? 0.2290 0.2189 0.2293 0.0223  -0.0297 -0.0431 1103 LEU A C   
8130  O O   . LEU A 1105 ? 0.2444 0.2378 0.2409 0.0245  -0.0292 -0.0450 1103 LEU A O   
8131  C CB  . LEU A 1105 ? 0.2492 0.2332 0.2570 0.0215  -0.0323 -0.0456 1103 LEU A CB  
8132  C CG  . LEU A 1105 ? 0.2558 0.2401 0.2684 0.0218  -0.0360 -0.0495 1103 LEU A CG  
8133  C CD1 . LEU A 1105 ? 0.2651 0.2463 0.2830 0.0189  -0.0372 -0.0467 1103 LEU A CD1 
8134  C CD2 . LEU A 1105 ? 0.2602 0.2437 0.2767 0.0234  -0.0387 -0.0544 1103 LEU A CD2 
8135  N N   . LEU A 1106 ? 0.2165 0.2070 0.2183 0.0213  -0.0305 -0.0422 1104 LEU A N   
8136  C CA  . LEU A 1106 ? 0.2292 0.2242 0.2284 0.0228  -0.0310 -0.0436 1104 LEU A CA  
8137  C C   . LEU A 1106 ? 0.2500 0.2454 0.2535 0.0232  -0.0346 -0.0479 1104 LEU A C   
8138  O O   . LEU A 1106 ? 0.2465 0.2389 0.2552 0.0213  -0.0363 -0.0475 1104 LEU A O   
8139  C CB  . LEU A 1106 ? 0.2317 0.2272 0.2296 0.0216  -0.0294 -0.0398 1104 LEU A CB  
8140  C CG  . LEU A 1106 ? 0.3197 0.3147 0.3143 0.0210  -0.0261 -0.0356 1104 LEU A CG  
8141  C CD1 . LEU A 1106 ? 0.2523 0.2491 0.2457 0.0207  -0.0252 -0.0330 1104 LEU A CD1 
8142  C CD2 . LEU A 1106 ? 0.2687 0.2655 0.2587 0.0228  -0.0245 -0.0357 1104 LEU A CD2 
8143  N N   . VAL A 1107 ? 0.2289 0.2285 0.2304 0.0257  -0.0359 -0.0521 1105 VAL A N   
8144  C CA  . VAL A 1107 ? 0.2536 0.2544 0.2590 0.0264  -0.0395 -0.0568 1105 VAL A CA  
8145  C C   . VAL A 1107 ? 0.2369 0.2433 0.2385 0.0278  -0.0395 -0.0575 1105 VAL A C   
8146  O O   . VAL A 1107 ? 0.2571 0.2686 0.2552 0.0302  -0.0399 -0.0607 1105 VAL A O   
8147  C CB  . VAL A 1107 ? 0.2340 0.2352 0.2415 0.0282  -0.0415 -0.0621 1105 VAL A CB  
8148  C CG1 . VAL A 1107 ? 0.2620 0.2633 0.2751 0.0287  -0.0456 -0.0671 1105 VAL A CG1 
8149  C CG2 . VAL A 1107 ? 0.2577 0.2535 0.2680 0.0269  -0.0408 -0.0604 1105 VAL A CG2 
8150  N N   . PRO A 1108 ? 0.2254 0.2315 0.2275 0.0264  -0.0393 -0.0546 1106 PRO A N   
8151  C CA  . PRO A 1108 ? 0.2531 0.2646 0.2518 0.0276  -0.0394 -0.0548 1106 PRO A CA  
8152  C C   . PRO A 1108 ? 0.2896 0.3032 0.2916 0.0284  -0.0430 -0.0597 1106 PRO A C   
8153  O O   . PRO A 1108 ? 0.2857 0.2959 0.2936 0.0275  -0.0455 -0.0622 1106 PRO A O   
8154  C CB  . PRO A 1108 ? 0.2553 0.2648 0.2542 0.0256  -0.0377 -0.0497 1106 PRO A CB  
8155  C CG  . PRO A 1108 ? 0.2636 0.2677 0.2683 0.0232  -0.0385 -0.0490 1106 PRO A CG  
8156  C CD  . PRO A 1108 ? 0.2559 0.2575 0.2615 0.0236  -0.0386 -0.0507 1106 PRO A CD  
8157  N N   . ALA A 1109 ? 0.2358 0.2553 0.2342 0.0301  -0.0435 -0.0608 1107 ALA A N   
8158  C CA  . ALA A 1109 ? 0.2554 0.2778 0.2564 0.0308  -0.0468 -0.0651 1107 ALA A CA  
8159  C C   . ALA A 1109 ? 0.3103 0.3343 0.3110 0.0299  -0.0468 -0.0623 1107 ALA A C   
8160  O O   . ALA A 1109 ? 0.3347 0.3581 0.3397 0.0293  -0.0495 -0.0643 1107 ALA A O   
8161  C CB  . ALA A 1109 ? 0.2711 0.3004 0.2685 0.0338  -0.0480 -0.0699 1107 ALA A CB  
8162  N N   . THR A 1110 ? 0.2720 0.2976 0.2681 0.0299  -0.0440 -0.0576 1108 THR A N   
8163  C CA  . THR A 1110 ? 0.2568 0.2843 0.2526 0.0293  -0.0440 -0.0548 1108 THR A CA  
8164  C C   . THR A 1110 ? 0.2568 0.2804 0.2524 0.0275  -0.0411 -0.0492 1108 THR A C   
8165  O O   . THR A 1110 ? 0.2414 0.2622 0.2358 0.0270  -0.0389 -0.0472 1108 THR A O   
8166  C CB  . THR A 1110 ? 0.2923 0.3271 0.2827 0.0314  -0.0439 -0.0547 1108 THR A CB  
8167  O OG1 . THR A 1110 ? 0.2698 0.3058 0.2555 0.0320  -0.0410 -0.0515 1108 THR A OG1 
8168  C CG2 . THR A 1110 ? 0.2903 0.3303 0.2802 0.0334  -0.0467 -0.0608 1108 THR A CG2 
8169  N N   . GLU A 1111 ? 0.2555 0.2793 0.2528 0.0264  -0.0412 -0.0469 1109 GLU A N   
8170  C CA  . GLU A 1111 ? 0.2401 0.2611 0.2376 0.0250  -0.0386 -0.0420 1109 GLU A CA  
8171  C C   . GLU A 1111 ? 0.2644 0.2871 0.2569 0.0260  -0.0361 -0.0389 1109 GLU A C   
8172  O O   . GLU A 1111 ? 0.2451 0.2646 0.2372 0.0252  -0.0338 -0.0362 1109 GLU A O   
8173  C CB  . GLU A 1111 ? 0.2785 0.3004 0.2785 0.0241  -0.0394 -0.0405 1109 GLU A CB  
8174  C CG  . GLU A 1111 ? 0.2905 0.3109 0.2905 0.0231  -0.0368 -0.0360 1109 GLU A CG  
8175  C CD  . GLU A 1111 ? 0.3485 0.3698 0.3518 0.0222  -0.0375 -0.0348 1109 GLU A CD  
8176  O OE1 . GLU A 1111 ? 0.3463 0.3655 0.3540 0.0205  -0.0384 -0.0356 1109 GLU A OE1 
8177  O OE2 . GLU A 1111 ? 0.3624 0.3866 0.3640 0.0232  -0.0373 -0.0330 1109 GLU A OE2 
8178  N N   . SER A 1112 ? 0.2631 0.2914 0.2520 0.0278  -0.0366 -0.0390 1110 SER A N   
8179  C CA  . SER A 1112 ? 0.2623 0.2926 0.2469 0.0287  -0.0345 -0.0356 1110 SER A CA  
8180  C C   . SER A 1112 ? 0.2659 0.2948 0.2484 0.0291  -0.0331 -0.0364 1110 SER A C   
8181  O O   . SER A 1112 ? 0.2626 0.2897 0.2438 0.0287  -0.0308 -0.0330 1110 SER A O   
8182  C CB  . SER A 1112 ? 0.3166 0.3539 0.2979 0.0304  -0.0356 -0.0353 1110 SER A CB  
8183  O OG  . SER A 1112 ? 0.3189 0.3583 0.2969 0.0309  -0.0337 -0.0313 1110 SER A OG  
8184  N N   . GLY A 1113 ? 0.2713 0.3012 0.2540 0.0299  -0.0347 -0.0410 1111 GLY A N   
8185  C CA  . GLY A 1113 ? 0.2205 0.2489 0.2017 0.0304  -0.0335 -0.0420 1111 GLY A CA  
8186  C C   . GLY A 1113 ? 0.2161 0.2377 0.2001 0.0284  -0.0319 -0.0400 1111 GLY A C   
8187  O O   . GLY A 1113 ? 0.2265 0.2467 0.2086 0.0284  -0.0297 -0.0380 1111 GLY A O   
8188  N N   . LEU A 1114 ? 0.2353 0.2531 0.2238 0.0267  -0.0329 -0.0403 1112 LEU A N   
8189  C CA  . LEU A 1114 ? 0.2405 0.2529 0.2317 0.0248  -0.0313 -0.0381 1112 LEU A CA  
8190  C C   . LEU A 1114 ? 0.2224 0.2342 0.2115 0.0243  -0.0286 -0.0334 1112 LEU A C   
8191  O O   . LEU A 1114 ? 0.2309 0.2399 0.2195 0.0236  -0.0266 -0.0316 1112 LEU A O   
8192  C CB  . LEU A 1114 ? 0.2287 0.2383 0.2251 0.0229  -0.0329 -0.0387 1112 LEU A CB  
8193  C CG  . LEU A 1114 ? 0.2597 0.2650 0.2588 0.0206  -0.0313 -0.0358 1112 LEU A CG  
8194  C CD1 . LEU A 1114 ? 0.2464 0.2486 0.2454 0.0204  -0.0305 -0.0362 1112 LEU A CD1 
8195  C CD2 . LEU A 1114 ? 0.2988 0.3026 0.3032 0.0187  -0.0329 -0.0360 1112 LEU A CD2 
8196  N N   . TYR A 1115 ? 0.2337 0.2482 0.2222 0.0246  -0.0286 -0.0315 1113 TYR A N   
8197  C CA  . TYR A 1115 ? 0.2260 0.2399 0.2137 0.0243  -0.0264 -0.0274 1113 TYR A CA  
8198  C C   . TYR A 1115 ? 0.2279 0.2430 0.2116 0.0254  -0.0247 -0.0258 1113 TYR A C   
8199  O O   . TYR A 1115 ? 0.2429 0.2555 0.2265 0.0247  -0.0227 -0.0231 1113 TYR A O   
8200  C CB  . TYR A 1115 ? 0.2255 0.2423 0.2138 0.0246  -0.0271 -0.0258 1113 TYR A CB  
8201  C CG  . TYR A 1115 ? 0.2149 0.2305 0.2073 0.0233  -0.0283 -0.0267 1113 TYR A CG  
8202  C CD1 . TYR A 1115 ? 0.2144 0.2264 0.2101 0.0216  -0.0283 -0.0277 1113 TYR A CD1 
8203  C CD2 . TYR A 1115 ? 0.2689 0.2875 0.2623 0.0237  -0.0296 -0.0262 1113 TYR A CD2 
8204  C CE1 . TYR A 1115 ? 0.2559 0.2676 0.2557 0.0203  -0.0294 -0.0281 1113 TYR A CE1 
8205  C CE2 . TYR A 1115 ? 0.2614 0.2793 0.2587 0.0226  -0.0306 -0.0269 1113 TYR A CE2 
8206  C CZ  . TYR A 1115 ? 0.3003 0.3150 0.3009 0.0208  -0.0305 -0.0278 1113 TYR A CZ  
8207  O OH  . TYR A 1115 ? 0.2924 0.3071 0.2971 0.0195  -0.0316 -0.0282 1113 TYR A OH  
8208  N N   . HIS A 1116 ? 0.2166 0.2360 0.1971 0.0270  -0.0257 -0.0273 1114 HIS A N   
8209  C CA  . HIS A 1116 ? 0.2365 0.2579 0.2134 0.0280  -0.0242 -0.0258 1114 HIS A CA  
8210  C C   . HIS A 1116 ? 0.2317 0.2492 0.2088 0.0275  -0.0231 -0.0271 1114 HIS A C   
8211  O O   . HIS A 1116 ? 0.2317 0.2481 0.2074 0.0274  -0.0211 -0.0245 1114 HIS A O   
8212  C CB  . HIS A 1116 ? 0.2446 0.2725 0.2182 0.0299  -0.0255 -0.0277 1114 HIS A CB  
8213  C CG  . HIS A 1116 ? 0.2673 0.3000 0.2394 0.0306  -0.0260 -0.0248 1114 HIS A CG  
8214  N ND1 . HIS A 1116 ? 0.3057 0.3402 0.2794 0.0306  -0.0279 -0.0257 1114 HIS A ND1 
8215  C CD2 . HIS A 1116 ? 0.2733 0.3096 0.2431 0.0311  -0.0250 -0.0208 1114 HIS A CD2 
8216  C CE1 . HIS A 1116 ? 0.3078 0.3467 0.2800 0.0312  -0.0280 -0.0224 1114 HIS A CE1 
8217  N NE2 . HIS A 1116 ? 0.3412 0.3813 0.3112 0.0315  -0.0263 -0.0192 1114 HIS A NE2 
8218  N N   . GLN A 1117 ? 0.2109 0.2266 0.1901 0.0273  -0.0245 -0.0309 1115 GLN A N   
8219  C CA  . GLN A 1117 ? 0.2149 0.2267 0.1949 0.0267  -0.0237 -0.0319 1115 GLN A CA  
8220  C C   . GLN A 1117 ? 0.1966 0.2037 0.1785 0.0248  -0.0219 -0.0287 1115 GLN A C   
8221  O O   . GLN A 1117 ? 0.2070 0.2121 0.1879 0.0246  -0.0201 -0.0274 1115 GLN A O   
8222  C CB  . GLN A 1117 ? 0.2266 0.2369 0.2099 0.0265  -0.0261 -0.0362 1115 GLN A CB  
8223  C CG  . GLN A 1117 ? 0.2309 0.2458 0.2126 0.0286  -0.0280 -0.0405 1115 GLN A CG  
8224  C CD  . GLN A 1117 ? 0.2924 0.3051 0.2785 0.0284  -0.0306 -0.0450 1115 GLN A CD  
8225  O OE1 . GLN A 1117 ? 0.2471 0.2553 0.2375 0.0265  -0.0312 -0.0443 1115 GLN A OE1 
8226  N NE2 . GLN A 1117 ? 0.2376 0.2539 0.2229 0.0303  -0.0323 -0.0495 1115 GLN A NE2 
8227  N N   . LEU A 1118 ? 0.2075 0.2131 0.1923 0.0235  -0.0222 -0.0277 1116 LEU A N   
8228  C CA  . LEU A 1118 ? 0.2155 0.2177 0.2022 0.0218  -0.0205 -0.0250 1116 LEU A CA  
8229  C C   . LEU A 1118 ? 0.2119 0.2146 0.1963 0.0222  -0.0184 -0.0217 1116 LEU A C   
8230  O O   . LEU A 1118 ? 0.2238 0.2240 0.2083 0.0215  -0.0166 -0.0201 1116 LEU A O   
8231  C CB  . LEU A 1118 ? 0.2478 0.2497 0.2378 0.0206  -0.0214 -0.0247 1116 LEU A CB  
8232  C CG  . LEU A 1118 ? 0.3248 0.3243 0.3187 0.0189  -0.0227 -0.0263 1116 LEU A CG  
8233  C CD1 . LEU A 1118 ? 0.3375 0.3382 0.3344 0.0181  -0.0237 -0.0261 1116 LEU A CD1 
8234  C CD2 . LEU A 1118 ? 0.3479 0.3441 0.3429 0.0174  -0.0210 -0.0247 1116 LEU A CD2 
8235  N N   . ALA A 1119 ? 0.2268 0.2331 0.2095 0.0235  -0.0187 -0.0206 1117 ALA A N   
8236  C CA  . ALA A 1119 ? 0.2418 0.2487 0.2232 0.0238  -0.0171 -0.0171 1117 ALA A CA  
8237  C C   . ALA A 1119 ? 0.2386 0.2452 0.2173 0.0244  -0.0158 -0.0167 1117 ALA A C   
8238  O O   . ALA A 1119 ? 0.2357 0.2401 0.2147 0.0238  -0.0141 -0.0145 1117 ALA A O   
8239  C CB  . ALA A 1119 ? 0.2492 0.2604 0.2294 0.0250  -0.0181 -0.0157 1117 ALA A CB  
8240  N N   . ALA A 1120 ? 0.2022 0.2113 0.1786 0.0255  -0.0166 -0.0190 1118 ALA A N   
8241  C CA  . ALA A 1120 ? 0.1883 0.1975 0.1623 0.0261  -0.0154 -0.0187 1118 ALA A CA  
8242  C C   . ALA A 1120 ? 0.2364 0.2407 0.2121 0.0247  -0.0143 -0.0190 1118 ALA A C   
8243  O O   . ALA A 1120 ? 0.2209 0.2237 0.1957 0.0245  -0.0126 -0.0169 1118 ALA A O   
8244  C CB  . ALA A 1120 ? 0.2082 0.2214 0.1800 0.0276  -0.0167 -0.0220 1118 ALA A CB  
8245  N N   . ALA A 1121 ? 0.2230 0.2245 0.2013 0.0238  -0.0153 -0.0213 1119 ALA A N   
8246  C CA  . ALA A 1121 ? 0.2124 0.2097 0.1924 0.0224  -0.0146 -0.0214 1119 ALA A CA  
8247  C C   . ALA A 1121 ? 0.1842 0.1793 0.1655 0.0211  -0.0128 -0.0184 1119 ALA A C   
8248  O O   . ALA A 1121 ? 0.1983 0.1912 0.1794 0.0205  -0.0113 -0.0173 1119 ALA A O   
8249  C CB  . ALA A 1121 ? 0.2521 0.2477 0.2354 0.0215  -0.0164 -0.0241 1119 ALA A CB  
8250  N N   . LEU A 1122 ? 0.2065 0.2021 0.1895 0.0206  -0.0131 -0.0175 1120 LEU A N   
8251  C CA  . LEU A 1122 ? 0.1868 0.1810 0.1715 0.0195  -0.0116 -0.0153 1120 LEU A CA  
8252  C C   . LEU A 1122 ? 0.2079 0.2025 0.1909 0.0203  -0.0101 -0.0129 1120 LEU A C   
8253  O O   . LEU A 1122 ? 0.2072 0.2000 0.1910 0.0196  -0.0087 -0.0116 1120 LEU A O   
8254  C CB  . LEU A 1122 ? 0.2094 0.2047 0.1965 0.0190  -0.0123 -0.0152 1120 LEU A CB  
8255  C CG  . LEU A 1122 ? 0.2297 0.2244 0.2192 0.0178  -0.0137 -0.0171 1120 LEU A CG  
8256  C CD1 . LEU A 1122 ? 0.2526 0.2492 0.2444 0.0176  -0.0145 -0.0169 1120 LEU A CD1 
8257  C CD2 . LEU A 1122 ? 0.2182 0.2106 0.2096 0.0160  -0.0129 -0.0168 1120 LEU A CD2 
8258  N N   . ALA A 1123 ? 0.2079 0.2055 0.1889 0.0217  -0.0107 -0.0121 1121 ALA A N   
8259  C CA  . ALA A 1123 ? 0.2015 0.1998 0.1815 0.0224  -0.0096 -0.0093 1121 ALA A CA  
8260  C C   . ALA A 1123 ? 0.2058 0.2025 0.1843 0.0222  -0.0082 -0.0089 1121 ALA A C   
8261  O O   . ALA A 1123 ? 0.2171 0.2132 0.1958 0.0222  -0.0071 -0.0066 1121 ALA A O   
8262  C CB  . ALA A 1123 ? 0.2000 0.2026 0.1779 0.0238  -0.0105 -0.0082 1121 ALA A CB  
8263  N N   . THR A 1124 ? 0.1841 0.1800 0.1614 0.0222  -0.0085 -0.0113 1122 THR A N   
8264  C CA  . THR A 1124 ? 0.1753 0.1697 0.1514 0.0221  -0.0073 -0.0112 1122 THR A CA  
8265  C C   . THR A 1124 ? 0.2098 0.2005 0.1880 0.0205  -0.0068 -0.0119 1122 THR A C   
8266  O O   . THR A 1124 ? 0.2048 0.1939 0.1824 0.0203  -0.0062 -0.0123 1122 THR A O   
8267  C CB  . THR A 1124 ? 0.2333 0.2301 0.2071 0.0233  -0.0081 -0.0133 1122 THR A CB  
8268  O OG1 . THR A 1124 ? 0.2201 0.2172 0.1949 0.0234  -0.0099 -0.0163 1122 THR A OG1 
8269  C CG2 . THR A 1124 ? 0.2235 0.2251 0.1947 0.0248  -0.0082 -0.0117 1122 THR A CG2 
8270  N N   . GLY A 1125 ? 0.1989 0.1885 0.1796 0.0194  -0.0069 -0.0118 1123 GLY A N   
8271  C CA  . GLY A 1125 ? 0.2025 0.1897 0.1851 0.0178  -0.0061 -0.0117 1123 GLY A CA  
8272  C C   . GLY A 1125 ? 0.2223 0.2082 0.2063 0.0167  -0.0072 -0.0135 1123 GLY A C   
8273  O O   . GLY A 1125 ? 0.2332 0.2175 0.2187 0.0152  -0.0066 -0.0130 1123 GLY A O   
8274  N N   . ASN A 1126 ? 0.2165 0.2032 0.2002 0.0174  -0.0089 -0.0154 1124 ASN A N   
8275  C CA  . ASN A 1126 ? 0.2120 0.1972 0.1976 0.0166  -0.0103 -0.0172 1124 ASN A CA  
8276  C C   . ASN A 1126 ? 0.2052 0.1906 0.1940 0.0152  -0.0114 -0.0174 1124 ASN A C   
8277  O O   . ASN A 1126 ? 0.2332 0.2203 0.2222 0.0154  -0.0114 -0.0169 1124 ASN A O   
8278  C CB  . ASN A 1126 ? 0.1958 0.1823 0.1802 0.0182  -0.0119 -0.0198 1124 ASN A CB  
8279  C CG  . ASN A 1126 ? 0.2080 0.1952 0.1895 0.0196  -0.0109 -0.0197 1124 ASN A CG  
8280  O OD1 . ASN A 1126 ? 0.2269 0.2121 0.2087 0.0192  -0.0103 -0.0196 1124 ASN A OD1 
8281  N ND2 . ASN A 1126 ? 0.1947 0.1852 0.1736 0.0212  -0.0107 -0.0197 1124 ASN A ND2 
8282  N N   . SER A 1127 ? 0.2131 0.1967 0.2045 0.0137  -0.0124 -0.0179 1125 SER A N   
8283  C CA  . SER A 1127 ? 0.2159 0.1999 0.2107 0.0125  -0.0141 -0.0184 1125 SER A CA  
8284  C C   . SER A 1127 ? 0.2058 0.1899 0.2014 0.0136  -0.0165 -0.0213 1125 SER A C   
8285  O O   . SER A 1127 ? 0.2280 0.2120 0.2215 0.0153  -0.0168 -0.0230 1125 SER A O   
8286  C CB  . SER A 1127 ? 0.2270 0.2096 0.2251 0.0101  -0.0143 -0.0170 1125 SER A CB  
8287  O OG  . SER A 1127 ? 0.2943 0.2746 0.2929 0.0100  -0.0149 -0.0175 1125 SER A OG  
8288  N N   . VAL A 1128 ? 0.2395 0.2241 0.2383 0.0128  -0.0184 -0.0222 1126 VAL A N   
8289  C CA  . VAL A 1128 ? 0.2374 0.2223 0.2373 0.0140  -0.0210 -0.0255 1126 VAL A CA  
8290  C C   . VAL A 1128 ? 0.2528 0.2361 0.2582 0.0121  -0.0234 -0.0259 1126 VAL A C   
8291  O O   . VAL A 1128 ? 0.2503 0.2335 0.2583 0.0100  -0.0231 -0.0236 1126 VAL A O   
8292  C CB  . VAL A 1128 ? 0.2293 0.2173 0.2273 0.0155  -0.0215 -0.0266 1126 VAL A CB  
8293  C CG1 . VAL A 1128 ? 0.2521 0.2419 0.2453 0.0172  -0.0195 -0.0257 1126 VAL A CG1 
8294  C CG2 . VAL A 1128 ? 0.2613 0.2503 0.2617 0.0140  -0.0216 -0.0251 1126 VAL A CG2 
8295  N N   . ALA A 1129 ? 0.2472 0.2295 0.2547 0.0130  -0.0259 -0.0291 1127 ALA A N   
8296  C CA  . ALA A 1129 ? 0.2635 0.2447 0.2768 0.0117  -0.0289 -0.0302 1127 ALA A CA  
8297  C C   . ALA A 1129 ? 0.2219 0.2052 0.2350 0.0137  -0.0310 -0.0341 1127 ALA A C   
8298  O O   . ALA A 1129 ? 0.2648 0.2490 0.2756 0.0160  -0.0314 -0.0372 1127 ALA A O   
8299  C CB  . ALA A 1129 ? 0.3013 0.2793 0.3186 0.0110  -0.0305 -0.0308 1127 ALA A CB  
8300  N N   . ILE A 1130 ? 0.2241 0.2087 0.2393 0.0128  -0.0321 -0.0339 1128 ILE A N   
8301  C CA  . ILE A 1130 ? 0.2497 0.2369 0.2644 0.0146  -0.0339 -0.0374 1128 ILE A CA  
8302  C C   . ILE A 1130 ? 0.2809 0.2665 0.3019 0.0140  -0.0378 -0.0403 1128 ILE A C   
8303  O O   . ILE A 1130 ? 0.2850 0.2687 0.3113 0.0116  -0.0389 -0.0383 1128 ILE A O   
8304  C CB  . ILE A 1130 ? 0.2328 0.2227 0.2462 0.0142  -0.0330 -0.0356 1128 ILE A CB  
8305  C CG1 . ILE A 1130 ? 0.2663 0.2571 0.2749 0.0144  -0.0295 -0.0323 1128 ILE A CG1 
8306  C CG2 . ILE A 1130 ? 0.2473 0.2403 0.2593 0.0163  -0.0349 -0.0391 1128 ILE A CG2 
8307  C CD1 . ILE A 1130 ? 0.2687 0.2618 0.2771 0.0138  -0.0287 -0.0305 1128 ILE A CD1 
8308  N N   . ASP A 1131 ? 0.2616 0.2485 0.2824 0.0163  -0.0398 -0.0450 1129 ASP A N   
8309  C CA  . ASP A 1131 ? 0.2429 0.2286 0.2702 0.0162  -0.0438 -0.0487 1129 ASP A CA  
8310  C C   . ASP A 1131 ? 0.2693 0.2554 0.3005 0.0145  -0.0455 -0.0477 1129 ASP A C   
8311  O O   . ASP A 1131 ? 0.2870 0.2765 0.3155 0.0155  -0.0453 -0.0485 1129 ASP A O   
8312  C CB  . ASP A 1131 ? 0.2550 0.2435 0.2804 0.0194  -0.0455 -0.0544 1129 ASP A CB  
8313  C CG  . ASP A 1131 ? 0.3544 0.3417 0.3869 0.0196  -0.0499 -0.0590 1129 ASP A CG  
8314  O OD1 . ASP A 1131 ? 0.3128 0.2960 0.3519 0.0174  -0.0517 -0.0576 1129 ASP A OD1 
8315  O OD2 . ASP A 1131 ? 0.3300 0.3208 0.3616 0.0220  -0.0517 -0.0639 1129 ASP A OD2 
8316  N N   . ALA A 1132 ? 0.2817 0.2648 0.3197 0.0118  -0.0472 -0.0457 1130 ALA A N   
8317  C CA  . ALA A 1132 ? 0.3180 0.3017 0.3605 0.0099  -0.0489 -0.0445 1130 ALA A CA  
8318  C C   . ALA A 1132 ? 0.3622 0.3472 0.4079 0.0114  -0.0526 -0.0497 1130 ALA A C   
8319  O O   . ALA A 1132 ? 0.3646 0.3515 0.4117 0.0108  -0.0536 -0.0496 1130 ALA A O   
8320  C CB  . ALA A 1132 ? 0.3194 0.3001 0.3688 0.0066  -0.0500 -0.0408 1130 ALA A CB  
8321  N N   . ALA A 1133 ? 0.3443 0.3284 0.3912 0.0135  -0.0548 -0.0546 1131 ALA A N   
8322  C CA  . ALA A 1133 ? 0.3850 0.3707 0.4350 0.0152  -0.0585 -0.0603 1131 ALA A CA  
8323  C C   . ALA A 1133 ? 0.3539 0.3449 0.3973 0.0176  -0.0573 -0.0624 1131 ALA A C   
8324  O O   . ALA A 1133 ? 0.3778 0.3711 0.4231 0.0190  -0.0602 -0.0669 1131 ALA A O   
8325  C CB  . ALA A 1133 ? 0.3559 0.3400 0.4095 0.0169  -0.0612 -0.0654 1131 ALA A CB  
8326  N N   . SER A 1134 ? 0.3356 0.3287 0.3715 0.0181  -0.0533 -0.0592 1132 SER A N   
8327  C CA  . SER A 1134 ? 0.3048 0.3029 0.3347 0.0201  -0.0523 -0.0602 1132 SER A CA  
8328  C C   . SER A 1134 ? 0.2964 0.2959 0.3284 0.0187  -0.0532 -0.0588 1132 SER A C   
8329  O O   . SER A 1134 ? 0.3125 0.3163 0.3413 0.0204  -0.0535 -0.0606 1132 SER A O   
8330  C CB  . SER A 1134 ? 0.3137 0.3132 0.3363 0.0206  -0.0480 -0.0564 1132 SER A CB  
8331  O OG  . SER A 1134 ? 0.3137 0.3110 0.3370 0.0180  -0.0458 -0.0510 1132 SER A OG  
8332  N N   . GLY A 1135 ? 0.3048 0.3013 0.3421 0.0158  -0.0535 -0.0554 1133 GLY A N   
8333  C CA  . GLY A 1135 ? 0.3140 0.3121 0.3534 0.0144  -0.0541 -0.0537 1133 GLY A CA  
8334  C C   . GLY A 1135 ? 0.3169 0.3178 0.3504 0.0147  -0.0508 -0.0503 1133 GLY A C   
8335  O O   . GLY A 1135 ? 0.3532 0.3565 0.3874 0.0144  -0.0513 -0.0499 1133 GLY A O   
8336  N N   . LEU A 1136 ? 0.2824 0.2831 0.3106 0.0152  -0.0474 -0.0478 1134 LEU A N   
8337  C CA  . LEU A 1136 ? 0.3059 0.3092 0.3289 0.0158  -0.0444 -0.0449 1134 LEU A CA  
8338  C C   . LEU A 1136 ? 0.3074 0.3093 0.3315 0.0135  -0.0420 -0.0401 1134 LEU A C   
8339  O O   . LEU A 1136 ? 0.2992 0.3025 0.3194 0.0139  -0.0393 -0.0376 1134 LEU A O   
8340  C CB  . LEU A 1136 ? 0.2965 0.3013 0.3129 0.0181  -0.0424 -0.0454 1134 LEU A CB  
8341  C CG  . LEU A 1136 ? 0.2892 0.2976 0.3031 0.0208  -0.0444 -0.0498 1134 LEU A CG  
8342  C CD1 . LEU A 1136 ? 0.2929 0.3031 0.3007 0.0228  -0.0422 -0.0497 1134 LEU A CD1 
8343  C CD2 . LEU A 1136 ? 0.3337 0.3462 0.3470 0.0215  -0.0455 -0.0503 1134 LEU A CD2 
8344  N N   . GLN A 1137 ? 0.3168 0.3163 0.3466 0.0109  -0.0430 -0.0388 1135 GLN A N   
8345  C CA  . GLN A 1137 ? 0.3488 0.3480 0.3798 0.0086  -0.0407 -0.0345 1135 GLN A CA  
8346  C C   . GLN A 1137 ? 0.3163 0.3187 0.3459 0.0087  -0.0393 -0.0328 1135 GLN A C   
8347  O O   . GLN A 1137 ? 0.3258 0.3290 0.3530 0.0084  -0.0364 -0.0300 1135 GLN A O   
8348  C CB  . GLN A 1137 ? 0.3472 0.3445 0.3852 0.0057  -0.0426 -0.0332 1135 GLN A CB  
8349  C CG  . GLN A 1137 ? 0.3426 0.3363 0.3824 0.0051  -0.0432 -0.0333 1135 GLN A CG  
8350  C CD  . GLN A 1137 ? 0.3178 0.3098 0.3603 0.0065  -0.0467 -0.0379 1135 GLN A CD  
8351  O OE1 . GLN A 1137 ? 0.3550 0.3489 0.3966 0.0083  -0.0484 -0.0413 1135 GLN A OE1 
8352  N NE2 . GLN A 1137 ? 0.3792 0.3678 0.4252 0.0056  -0.0481 -0.0381 1135 GLN A NE2 
8353  N N   . ALA A 1138 ? 0.3183 0.3229 0.3497 0.0092  -0.0415 -0.0347 1136 ALA A N   
8354  C CA  . ALA A 1138 ? 0.3154 0.3232 0.3462 0.0093  -0.0404 -0.0331 1136 ALA A CA  
8355  C C   . ALA A 1138 ? 0.3829 0.3922 0.4077 0.0115  -0.0382 -0.0325 1136 ALA A C   
8356  O O   . ALA A 1138 ? 0.3955 0.4071 0.4200 0.0116  -0.0370 -0.0309 1136 ALA A O   
8357  C CB  . ALA A 1138 ? 0.3865 0.3963 0.4207 0.0093  -0.0434 -0.0353 1136 ALA A CB  
8358  N N   . SER A 1139 ? 0.3228 0.3311 0.3433 0.0132  -0.0376 -0.0337 1137 SER A N   
8359  C CA  . SER A 1139 ? 0.3528 0.3627 0.3682 0.0152  -0.0356 -0.0326 1137 SER A CA  
8360  C C   . SER A 1139 ? 0.3026 0.3111 0.3165 0.0145  -0.0325 -0.0295 1137 SER A C   
8361  O O   . SER A 1139 ? 0.3366 0.3463 0.3471 0.0158  -0.0309 -0.0281 1137 SER A O   
8362  C CB  . SER A 1139 ? 0.3061 0.3165 0.3174 0.0173  -0.0364 -0.0351 1137 SER A CB  
8363  O OG  . SER A 1139 ? 0.3759 0.3886 0.3880 0.0183  -0.0393 -0.0383 1137 SER A OG  
8364  N N   . LEU A 1140 ? 0.2987 0.3050 0.3152 0.0124  -0.0317 -0.0283 1138 LEU A N   
8365  C CA  . LEU A 1140 ? 0.3183 0.3236 0.3335 0.0118  -0.0288 -0.0257 1138 LEU A CA  
8366  C C   . LEU A 1140 ? 0.3413 0.3477 0.3604 0.0096  -0.0280 -0.0238 1138 LEU A C   
8367  O O   . LEU A 1140 ? 0.4195 0.4250 0.4395 0.0080  -0.0265 -0.0221 1138 LEU A O   
8368  C CB  . LEU A 1140 ? 0.3395 0.3417 0.3534 0.0115  -0.0282 -0.0259 1138 LEU A CB  
8369  C CG  . LEU A 1140 ? 0.3745 0.3760 0.3837 0.0137  -0.0278 -0.0270 1138 LEU A CG  
8370  C CD1 . LEU A 1140 ? 0.3647 0.3633 0.3735 0.0129  -0.0266 -0.0263 1138 LEU A CD1 
8371  C CD2 . LEU A 1140 ? 0.3142 0.3176 0.3199 0.0152  -0.0260 -0.0255 1138 LEU A CD2 
8372  N N   . LYS A 1141 ? 0.3217 0.3309 0.3432 0.0094  -0.0289 -0.0239 1139 LYS A N   
8373  C CA  . LYS A 1141 ? 0.3838 0.3951 0.4090 0.0074  -0.0280 -0.0221 1139 LYS A CA  
8374  C C   . LYS A 1141 ? 0.3693 0.3821 0.3929 0.0080  -0.0252 -0.0207 1139 LYS A C   
8375  O O   . LYS A 1141 ? 0.3418 0.3548 0.3627 0.0101  -0.0247 -0.0209 1139 LYS A O   
8376  C CB  . LYS A 1141 ? 0.3884 0.4024 0.4170 0.0072  -0.0300 -0.0230 1139 LYS A CB  
8377  N N   . ASN A 1142 ? 0.3597 0.3740 0.3854 0.0062  -0.0236 -0.0191 1140 ASN A N   
8378  C CA  . ASN A 1142 ? 0.3553 0.3718 0.3806 0.0066  -0.0212 -0.0182 1140 ASN A CA  
8379  C C   . ASN A 1142 ? 0.3470 0.3611 0.3683 0.0082  -0.0195 -0.0180 1140 ASN A C   
8380  O O   . ASN A 1142 ? 0.3335 0.3485 0.3540 0.0097  -0.0185 -0.0180 1140 ASN A O   
8381  C CB  . ASN A 1142 ? 0.4176 0.4372 0.4447 0.0077  -0.0216 -0.0188 1140 ASN A CB  
8382  C CG  . ASN A 1142 ? 0.4729 0.4947 0.5038 0.0064  -0.0236 -0.0192 1140 ASN A CG  
8383  O OD1 . ASN A 1142 ? 0.4770 0.4989 0.5081 0.0075  -0.0255 -0.0203 1140 ASN A OD1 
8384  N ND2 . ASN A 1142 ? 0.4662 0.4902 0.5005 0.0039  -0.0233 -0.0180 1140 ASN A ND2 
8385  N N   . LEU A 1143 ? 0.3503 0.3613 0.3694 0.0079  -0.0195 -0.0179 1141 LEU A N   
8386  C CA  . LEU A 1143 ? 0.3632 0.3721 0.3787 0.0092  -0.0179 -0.0175 1141 LEU A CA  
8387  C C   . LEU A 1143 ? 0.3512 0.3618 0.3675 0.0086  -0.0155 -0.0165 1141 LEU A C   
8388  O O   . LEU A 1143 ? 0.3263 0.3392 0.3450 0.0066  -0.0149 -0.0159 1141 LEU A O   
8389  C CB  . LEU A 1143 ? 0.3212 0.3267 0.3347 0.0088  -0.0182 -0.0176 1141 LEU A CB  
8390  C CG  . LEU A 1143 ? 0.3381 0.3417 0.3495 0.0103  -0.0201 -0.0191 1141 LEU A CG  
8391  C CD1 . LEU A 1143 ? 0.3271 0.3278 0.3376 0.0097  -0.0203 -0.0194 1141 LEU A CD1 
8392  C CD2 . LEU A 1143 ? 0.3180 0.3219 0.3261 0.0126  -0.0196 -0.0192 1141 LEU A CD2 
8393  N N   . PRO A 1144 ? 0.3397 0.3497 0.3541 0.0102  -0.0142 -0.0164 1142 PRO A N   
8394  C CA  . PRO A 1144 ? 0.3663 0.3775 0.3811 0.0097  -0.0121 -0.0160 1142 PRO A CA  
8395  C C   . PRO A 1144 ? 0.3304 0.3404 0.3443 0.0080  -0.0114 -0.0151 1142 PRO A C   
8396  O O   . PRO A 1144 ? 0.3123 0.3190 0.3242 0.0079  -0.0122 -0.0150 1142 PRO A O   
8397  C CB  . PRO A 1144 ? 0.3743 0.3835 0.3869 0.0118  -0.0114 -0.0159 1142 PRO A CB  
8398  C CG  . PRO A 1144 ? 0.3745 0.3829 0.3862 0.0134  -0.0131 -0.0161 1142 PRO A CG  
8399  C CD  . PRO A 1144 ? 0.3373 0.3453 0.3489 0.0124  -0.0148 -0.0166 1142 PRO A CD  
8400  N N   . GLN A 1145 ? 0.3098 0.3227 0.3253 0.0065  -0.0099 -0.0146 1143 GLN A N   
8401  C CA  . GLN A 1145 ? 0.3124 0.3248 0.3274 0.0047  -0.0093 -0.0134 1143 GLN A CA  
8402  C C   . GLN A 1145 ? 0.3068 0.3150 0.3183 0.0057  -0.0087 -0.0132 1143 GLN A C   
8403  O O   . GLN A 1145 ? 0.2939 0.2999 0.3045 0.0046  -0.0091 -0.0124 1143 GLN A O   
8404  C CB  . GLN A 1145 ? 0.3832 0.4005 0.4000 0.0033  -0.0075 -0.0130 1143 GLN A CB  
8405  N N   . THR A 1146 ? 0.2955 0.3025 0.3053 0.0077  -0.0079 -0.0139 1144 THR A N   
8406  C CA  . THR A 1146 ? 0.3185 0.3220 0.3252 0.0086  -0.0073 -0.0136 1144 THR A CA  
8407  C C   . THR A 1146 ? 0.2941 0.2943 0.2988 0.0091  -0.0089 -0.0137 1144 THR A C   
8408  O O   . THR A 1146 ? 0.2852 0.2829 0.2880 0.0090  -0.0088 -0.0133 1144 THR A O   
8409  C CB  . THR A 1146 ? 0.3301 0.3331 0.3361 0.0106  -0.0065 -0.0139 1144 THR A CB  
8410  O OG1 . THR A 1146 ? 0.3272 0.3307 0.3341 0.0119  -0.0078 -0.0144 1144 THR A OG1 
8411  C CG2 . THR A 1146 ? 0.3014 0.3072 0.3094 0.0103  -0.0050 -0.0144 1144 THR A CG2 
8412  N N   . VAL A 1147 ? 0.2863 0.2870 0.2916 0.0099  -0.0105 -0.0144 1145 VAL A N   
8413  C CA  . VAL A 1147 ? 0.2524 0.2509 0.2561 0.0106  -0.0121 -0.0151 1145 VAL A CA  
8414  C C   . VAL A 1147 ? 0.2693 0.2672 0.2749 0.0088  -0.0134 -0.0152 1145 VAL A C   
8415  O O   . VAL A 1147 ? 0.2727 0.2682 0.2773 0.0088  -0.0142 -0.0156 1145 VAL A O   
8416  C CB  . VAL A 1147 ? 0.2547 0.2544 0.2583 0.0122  -0.0135 -0.0159 1145 VAL A CB  
8417  C CG1 . VAL A 1147 ? 0.2572 0.2556 0.2589 0.0131  -0.0152 -0.0170 1145 VAL A CG1 
8418  C CG2 . VAL A 1147 ? 0.2766 0.2770 0.2793 0.0138  -0.0125 -0.0152 1145 VAL A CG2 
8419  N N   . GLY A 1148 ? 0.2639 0.2644 0.2729 0.0072  -0.0138 -0.0148 1146 GLY A N   
8420  C CA  . GLY A 1148 ? 0.2719 0.2720 0.2836 0.0051  -0.0152 -0.0144 1146 GLY A CA  
8421  C C   . GLY A 1148 ? 0.3007 0.2989 0.3119 0.0039  -0.0145 -0.0132 1146 GLY A C   
8422  O O   . GLY A 1148 ? 0.2969 0.2931 0.3096 0.0031  -0.0162 -0.0132 1146 GLY A O   
8423  N N   . LEU A 1149 ? 0.2548 0.2537 0.2642 0.0040  -0.0123 -0.0123 1147 LEU A N   
8424  C CA  . LEU A 1149 ? 0.3034 0.3008 0.3122 0.0029  -0.0116 -0.0110 1147 LEU A CA  
8425  C C   . LEU A 1149 ? 0.2658 0.2590 0.2724 0.0042  -0.0124 -0.0120 1147 LEU A C   
8426  O O   . LEU A 1149 ? 0.3361 0.3275 0.3433 0.0032  -0.0128 -0.0113 1147 LEU A O   
8427  C CB  . LEU A 1149 ? 0.3170 0.3160 0.3242 0.0030  -0.0091 -0.0104 1147 LEU A CB  
8428  C CG  . LEU A 1149 ? 0.3789 0.3828 0.3884 0.0013  -0.0079 -0.0093 1147 LEU A CG  
8429  C CD1 . LEU A 1149 ? 0.4089 0.4142 0.4167 0.0019  -0.0057 -0.0095 1147 LEU A CD1 
8430  C CD2 . LEU A 1149 ? 0.4184 0.4235 0.4305 -0.0015 -0.0088 -0.0072 1147 LEU A CD2 
8431  N N   . ARG A 1150 ? 0.2636 0.2558 0.2678 0.0065  -0.0127 -0.0136 1148 ARG A N   
8432  C CA  . ARG A 1150 ? 0.2611 0.2506 0.2631 0.0080  -0.0134 -0.0149 1148 ARG A CA  
8433  C C   . ARG A 1150 ? 0.2724 0.2611 0.2761 0.0082  -0.0161 -0.0167 1148 ARG A C   
8434  O O   . ARG A 1150 ? 0.2754 0.2623 0.2778 0.0095  -0.0169 -0.0182 1148 ARG A O   
8435  C CB  . ARG A 1150 ? 0.2597 0.2495 0.2581 0.0103  -0.0124 -0.0154 1148 ARG A CB  
8436  C CG  . ARG A 1150 ? 0.3162 0.3061 0.3130 0.0105  -0.0101 -0.0140 1148 ARG A CG  
8437  C CD  . ARG A 1150 ? 0.3171 0.3053 0.3108 0.0119  -0.0095 -0.0140 1148 ARG A CD  
8438  N NE  . ARG A 1150 ? 0.3033 0.2916 0.2958 0.0124  -0.0075 -0.0128 1148 ARG A NE  
8439  C CZ  . ARG A 1150 ? 0.2778 0.2662 0.2683 0.0140  -0.0070 -0.0124 1148 ARG A CZ  
8440  N NH1 . ARG A 1150 ? 0.2566 0.2455 0.2454 0.0155  -0.0081 -0.0131 1148 ARG A NH1 
8441  N NH2 . ARG A 1150 ? 0.2675 0.2559 0.2580 0.0142  -0.0055 -0.0113 1148 ARG A NH2 
8442  N N   . VAL A 1151 ? 0.2294 0.2195 0.2362 0.0072  -0.0175 -0.0168 1149 VAL A N   
8443  C CA  . VAL A 1151 ? 0.2546 0.2443 0.2634 0.0076  -0.0202 -0.0190 1149 VAL A CA  
8444  C C   . VAL A 1151 ? 0.3068 0.2954 0.3205 0.0053  -0.0221 -0.0183 1149 VAL A C   
8445  O O   . VAL A 1151 ? 0.3297 0.3201 0.3461 0.0032  -0.0217 -0.0161 1149 VAL A O   
8446  C CB  . VAL A 1151 ? 0.2612 0.2534 0.2701 0.0085  -0.0208 -0.0198 1149 VAL A CB  
8447  C CG1 . VAL A 1151 ? 0.3094 0.3014 0.3208 0.0087  -0.0238 -0.0222 1149 VAL A CG1 
8448  C CG2 . VAL A 1151 ? 0.2693 0.2625 0.2738 0.0108  -0.0194 -0.0202 1149 VAL A CG2 
8449  N N   . SER A 1152 ? 0.2663 0.2525 0.2815 0.0057  -0.0242 -0.0202 1150 SER A N   
8450  C CA  . SER A 1152 ? 0.3168 0.3017 0.3378 0.0038  -0.0268 -0.0199 1150 SER A CA  
8451  C C   . SER A 1152 ? 0.3356 0.3198 0.3583 0.0052  -0.0298 -0.0236 1150 SER A C   
8452  O O   . SER A 1152 ? 0.2977 0.2822 0.3167 0.0078  -0.0297 -0.0264 1150 SER A O   
8453  C CB  . SER A 1152 ? 0.3243 0.3065 0.3469 0.0027  -0.0270 -0.0186 1150 SER A CB  
8454  O OG  . SER A 1152 ? 0.3631 0.3432 0.3832 0.0049  -0.0273 -0.0213 1150 SER A OG  
8455  N N   . TRP A 1153 ? 0.2835 0.2673 0.3120 0.0036  -0.0325 -0.0237 1151 TRP A N   
8456  C CA  . TRP A 1153 ? 0.3211 0.3041 0.3525 0.0047  -0.0359 -0.0275 1151 TRP A CA  
8457  C C   . TRP A 1153 ? 0.3276 0.3072 0.3644 0.0038  -0.0385 -0.0282 1151 TRP A C   
8458  O O   . TRP A 1153 ? 0.3684 0.3470 0.4093 0.0012  -0.0388 -0.0248 1151 TRP A O   
8459  C CB  . TRP A 1153 ? 0.3237 0.3087 0.3586 0.0036  -0.0374 -0.0273 1151 TRP A CB  
8460  C CG  . TRP A 1153 ? 0.3297 0.3179 0.3600 0.0050  -0.0355 -0.0276 1151 TRP A CG  
8461  C CD1 . TRP A 1153 ? 0.3556 0.3462 0.3837 0.0042  -0.0327 -0.0246 1151 TRP A CD1 
8462  C CD2 . TRP A 1153 ? 0.3043 0.2941 0.3319 0.0075  -0.0365 -0.0310 1151 TRP A CD2 
8463  N NE1 . TRP A 1153 ? 0.3825 0.3754 0.4070 0.0061  -0.0320 -0.0259 1151 TRP A NE1 
8464  C CE2 . TRP A 1153 ? 0.3234 0.3161 0.3474 0.0081  -0.0342 -0.0296 1151 TRP A CE2 
8465  C CE3 . TRP A 1153 ? 0.3238 0.3133 0.3520 0.0095  -0.0391 -0.0354 1151 TRP A CE3 
8466  C CZ2 . TRP A 1153 ? 0.3089 0.3040 0.3299 0.0103  -0.0346 -0.0317 1151 TRP A CZ2 
8467  C CZ3 . TRP A 1153 ? 0.3165 0.3090 0.3411 0.0117  -0.0393 -0.0377 1151 TRP A CZ3 
8468  C CH2 . TRP A 1153 ? 0.3465 0.3416 0.3676 0.0120  -0.0370 -0.0356 1151 TRP A CH2 
8469  N N   . SER A 1154 ? 0.3158 0.2941 0.3528 0.0061  -0.0405 -0.0326 1152 SER A N   
8470  C CA  . SER A 1154 ? 0.3073 0.2821 0.3492 0.0058  -0.0430 -0.0338 1152 SER A CA  
8471  C C   . SER A 1154 ? 0.3485 0.3226 0.3960 0.0066  -0.0473 -0.0382 1152 SER A C   
8472  O O   . SER A 1154 ? 0.3009 0.2768 0.3456 0.0093  -0.0479 -0.0427 1152 SER A O   
8473  C CB  . SER A 1154 ? 0.3023 0.2763 0.3396 0.0080  -0.0414 -0.0355 1152 SER A CB  
8474  O OG  . SER A 1154 ? 0.3349 0.3057 0.3776 0.0079  -0.0440 -0.0371 1152 SER A OG  
8475  N N   . LYS A 1155 ? 0.3266 0.2984 0.3822 0.0042  -0.0503 -0.0369 1153 LYS A N   
8476  C CA  . LYS A 1155 ? 0.3654 0.3357 0.4278 0.0049  -0.0549 -0.0413 1153 LYS A CA  
8477  C C   . LYS A 1155 ? 0.4045 0.3716 0.4703 0.0062  -0.0570 -0.0443 1153 LYS A C   
8478  O O   . LYS A 1155 ? 0.4950 0.4619 0.5631 0.0085  -0.0598 -0.0501 1153 LYS A O   
8479  C CB  . LYS A 1155 ? 0.4013 0.3708 0.4721 0.0016  -0.0577 -0.0384 1153 LYS A CB  
8480  N N   . ASP A 1156 ? 0.3986 0.3635 0.4646 0.0048  -0.0556 -0.0407 1154 ASP A N   
8481  C CA  . ASP A 1156 ? 0.3987 0.3605 0.4682 0.0058  -0.0575 -0.0428 1154 ASP A CA  
8482  C C   . ASP A 1156 ? 0.3567 0.3195 0.4179 0.0074  -0.0533 -0.0422 1154 ASP A C   
8483  O O   . ASP A 1156 ? 0.3429 0.3050 0.4024 0.0055  -0.0509 -0.0372 1154 ASP A O   
8484  C CB  . ASP A 1156 ? 0.4213 0.3797 0.4995 0.0023  -0.0598 -0.0383 1154 ASP A CB  
8485  C CG  . ASP A 1156 ? 0.4985 0.4532 0.5816 0.0032  -0.0622 -0.0404 1154 ASP A CG  
8486  O OD1 . ASP A 1156 ? 0.5213 0.4764 0.6006 0.0065  -0.0616 -0.0452 1154 ASP A OD1 
8487  O OD2 . ASP A 1156 ? 0.5258 0.4776 0.6171 0.0005  -0.0648 -0.0370 1154 ASP A OD2 
8488  N N   . TRP A 1157 ? 0.3276 0.2925 0.3835 0.0108  -0.0525 -0.0472 1155 TRP A N   
8489  C CA  . TRP A 1157 ? 0.3109 0.2773 0.3586 0.0124  -0.0485 -0.0464 1155 TRP A CA  
8490  C C   . TRP A 1157 ? 0.3344 0.2977 0.3842 0.0116  -0.0483 -0.0445 1155 TRP A C   
8491  O O   . TRP A 1157 ? 0.3597 0.3233 0.4044 0.0111  -0.0448 -0.0409 1155 TRP A O   
8492  C CB  . TRP A 1157 ? 0.3019 0.2715 0.3449 0.0161  -0.0483 -0.0521 1155 TRP A CB  
8493  C CG  . TRP A 1157 ? 0.2809 0.2542 0.3215 0.0172  -0.0487 -0.0544 1155 TRP A CG  
8494  C CD1 . TRP A 1157 ? 0.3035 0.2775 0.3444 0.0154  -0.0485 -0.0516 1155 TRP A CD1 
8495  C CD2 . TRP A 1157 ? 0.2714 0.2486 0.3089 0.0205  -0.0494 -0.0601 1155 TRP A CD2 
8496  N NE1 . TRP A 1157 ? 0.3023 0.2802 0.3407 0.0173  -0.0491 -0.0551 1155 TRP A NE1 
8497  C CE2 . TRP A 1157 ? 0.2939 0.2739 0.3300 0.0204  -0.0497 -0.0603 1155 TRP A CE2 
8498  C CE3 . TRP A 1157 ? 0.2924 0.2716 0.3283 0.0235  -0.0498 -0.0651 1155 TRP A CE3 
8499  C CZ2 . TRP A 1157 ? 0.3109 0.2957 0.3438 0.0232  -0.0504 -0.0651 1155 TRP A CZ2 
8500  C CZ3 . TRP A 1157 ? 0.2854 0.2698 0.3180 0.0263  -0.0505 -0.0699 1155 TRP A CZ3 
8501  C CH2 . TRP A 1157 ? 0.3037 0.2908 0.3348 0.0261  -0.0508 -0.0698 1155 TRP A CH2 
8502  N N   . ALA A 1158 ? 0.3333 0.2935 0.3908 0.0117  -0.0521 -0.0470 1156 ALA A N   
8503  C CA  . ALA A 1158 ? 0.3602 0.3174 0.4202 0.0112  -0.0522 -0.0454 1156 ALA A CA  
8504  C C   . ALA A 1158 ? 0.4230 0.3786 0.4846 0.0075  -0.0510 -0.0382 1156 ALA A C   
8505  O O   . ALA A 1158 ? 0.5038 0.4580 0.5645 0.0069  -0.0496 -0.0357 1156 ALA A O   
8506  C CB  . ALA A 1158 ? 0.3875 0.3418 0.4566 0.0122  -0.0570 -0.0499 1156 ALA A CB  
8507  N N   . ALA A 1159 ? 0.3766 0.3329 0.4406 0.0049  -0.0515 -0.0349 1157 ALA A N   
8508  C CA  . ALA A 1159 ? 0.4226 0.3787 0.4879 0.0012  -0.0503 -0.0280 1157 ALA A CA  
8509  C C   . ALA A 1159 ? 0.4233 0.3824 0.4797 0.0010  -0.0453 -0.0249 1157 ALA A C   
8510  O O   . ALA A 1159 ? 0.4444 0.4038 0.5003 -0.0013 -0.0436 -0.0199 1157 ALA A O   
8511  C CB  . ALA A 1159 ? 0.4177 0.3741 0.4897 -0.0015 -0.0529 -0.0257 1157 ALA A CB  
8512  N N   . ASP A 1160 ? 0.4038 0.3656 0.4534 0.0034  -0.0431 -0.0278 1158 ASP A N   
8513  C CA  . ASP A 1160 ? 0.4005 0.3652 0.4427 0.0032  -0.0389 -0.0250 1158 ASP A CA  
8514  C C   . ASP A 1160 ? 0.3445 0.3096 0.3799 0.0055  -0.0359 -0.0262 1158 ASP A C   
8515  O O   . ASP A 1160 ? 0.3756 0.3430 0.4049 0.0057  -0.0326 -0.0246 1158 ASP A O   
8516  C CB  . ASP A 1160 ? 0.3929 0.3604 0.4330 0.0037  -0.0386 -0.0263 1158 ASP A CB  
8517  C CG  . ASP A 1160 ? 0.4388 0.4062 0.4858 0.0013  -0.0414 -0.0248 1158 ASP A CG  
8518  O OD1 . ASP A 1160 ? 0.4975 0.4635 0.5499 -0.0015 -0.0426 -0.0212 1158 ASP A OD1 
8519  O OD2 . ASP A 1160 ? 0.4284 0.3974 0.4759 0.0020  -0.0425 -0.0271 1158 ASP A OD2 
8520  N N   . GLY A 1161 ? 0.3581 0.3211 0.3947 0.0072  -0.0372 -0.0291 1159 GLY A N   
8521  C CA  . GLY A 1161 ? 0.3549 0.3184 0.3857 0.0092  -0.0345 -0.0299 1159 GLY A CA  
8522  C C   . GLY A 1161 ? 0.3757 0.3379 0.4061 0.0073  -0.0328 -0.0255 1159 GLY A C   
8523  O O   . GLY A 1161 ? 0.4081 0.3699 0.4418 0.0044  -0.0331 -0.0215 1159 GLY A O   
8524  N N   . PRO A 1162 ? 0.3607 0.3228 0.3871 0.0089  -0.0308 -0.0262 1160 PRO A N   
8525  C CA  . PRO A 1162 ? 0.3235 0.2870 0.3458 0.0122  -0.0302 -0.0306 1160 PRO A CA  
8526  C C   . PRO A 1162 ? 0.3458 0.3127 0.3617 0.0133  -0.0276 -0.0306 1160 PRO A C   
8527  O O   . PRO A 1162 ? 0.3349 0.3028 0.3479 0.0119  -0.0252 -0.0270 1160 PRO A O   
8528  C CB  . PRO A 1162 ? 0.3408 0.3032 0.3615 0.0126  -0.0287 -0.0296 1160 PRO A CB  
8529  C CG  . PRO A 1162 ? 0.4172 0.3790 0.4373 0.0098  -0.0268 -0.0242 1160 PRO A CG  
8530  C CD  . PRO A 1162 ? 0.3849 0.3460 0.4105 0.0073  -0.0290 -0.0223 1160 PRO A CD  
8531  N N   . PHE A 1163 ? 0.2797 0.2489 0.2937 0.0158  -0.0283 -0.0347 1161 PHE A N   
8532  C CA  . PHE A 1163 ? 0.2400 0.2128 0.2480 0.0171  -0.0259 -0.0346 1161 PHE A CA  
8533  C C   . PHE A 1163 ? 0.2767 0.2510 0.2797 0.0190  -0.0236 -0.0348 1161 PHE A C   
8534  O O   . PHE A 1163 ? 0.3071 0.2800 0.3113 0.0196  -0.0240 -0.0360 1161 PHE A O   
8535  C CB  . PHE A 1163 ? 0.2388 0.2140 0.2472 0.0187  -0.0279 -0.0383 1161 PHE A CB  
8536  C CG  . PHE A 1163 ? 0.2624 0.2361 0.2763 0.0168  -0.0305 -0.0381 1161 PHE A CG  
8537  C CD1 . PHE A 1163 ? 0.3011 0.2747 0.3148 0.0146  -0.0293 -0.0342 1161 PHE A CD1 
8538  C CD2 . PHE A 1163 ? 0.2532 0.2257 0.2728 0.0173  -0.0341 -0.0419 1161 PHE A CD2 
8539  C CE1 . PHE A 1163 ? 0.3309 0.3036 0.3498 0.0127  -0.0315 -0.0337 1161 PHE A CE1 
8540  C CE2 . PHE A 1163 ? 0.3071 0.2781 0.3323 0.0154  -0.0366 -0.0413 1161 PHE A CE2 
8541  C CZ  . PHE A 1163 ? 0.2908 0.2621 0.3155 0.0130  -0.0352 -0.0370 1161 PHE A CZ  
8542  N N   . ALA A 1164 ? 0.2520 0.2293 0.2498 0.0197  -0.0212 -0.0335 1162 ALA A N   
8543  C CA  . ALA A 1164 ? 0.2600 0.2392 0.2531 0.0212  -0.0189 -0.0331 1162 ALA A CA  
8544  C C   . ALA A 1164 ? 0.2645 0.2485 0.2540 0.0237  -0.0189 -0.0357 1162 ALA A C   
8545  O O   . ALA A 1164 ? 0.2831 0.2698 0.2686 0.0249  -0.0170 -0.0350 1162 ALA A O   
8546  C CB  . ALA A 1164 ? 0.2841 0.2627 0.2745 0.0199  -0.0160 -0.0286 1162 ALA A CB  
8547  N N   . GLY A 1165 ? 0.2347 0.2202 0.2258 0.0243  -0.0211 -0.0384 1163 GLY A N   
8548  C CA  . GLY A 1165 ? 0.2473 0.2381 0.2354 0.0266  -0.0214 -0.0411 1163 GLY A CA  
8549  C C   . GLY A 1165 ? 0.2473 0.2386 0.2379 0.0264  -0.0238 -0.0431 1163 GLY A C   
8550  O O   . GLY A 1165 ? 0.2308 0.2184 0.2254 0.0244  -0.0250 -0.0421 1163 GLY A O   
8551  N N   . ALA A 1166 ? 0.2315 0.2279 0.2196 0.0284  -0.0245 -0.0458 1164 ALA A N   
8552  C CA  . ALA A 1166 ? 0.2266 0.2240 0.2170 0.0283  -0.0269 -0.0479 1164 ALA A CA  
8553  C C   . ALA A 1166 ? 0.2263 0.2300 0.2121 0.0300  -0.0263 -0.0483 1164 ALA A C   
8554  O O   . ALA A 1166 ? 0.2624 0.2705 0.2441 0.0317  -0.0251 -0.0487 1164 ALA A O   
8555  C CB  . ALA A 1166 ? 0.2289 0.2255 0.2243 0.0292  -0.0303 -0.0533 1164 ALA A CB  
8556  N N   . LEU A 1167 ? 0.2184 0.2226 0.2050 0.0293  -0.0273 -0.0477 1165 LEU A N   
8557  C CA  . LEU A 1167 ? 0.2164 0.2265 0.1994 0.0307  -0.0275 -0.0482 1165 LEU A CA  
8558  C C   . LEU A 1167 ? 0.2393 0.2504 0.2258 0.0311  -0.0308 -0.0525 1165 LEU A C   
8559  O O   . LEU A 1167 ? 0.2399 0.2467 0.2309 0.0294  -0.0321 -0.0521 1165 LEU A O   
8560  C CB  . LEU A 1167 ? 0.2261 0.2360 0.2071 0.0294  -0.0256 -0.0430 1165 LEU A CB  
8561  C CG  . LEU A 1167 ? 0.2205 0.2289 0.1989 0.0288  -0.0225 -0.0386 1165 LEU A CG  
8562  C CD1 . LEU A 1167 ? 0.2417 0.2494 0.2195 0.0275  -0.0212 -0.0342 1165 LEU A CD1 
8563  C CD2 . LEU A 1167 ? 0.2425 0.2561 0.2166 0.0308  -0.0214 -0.0390 1165 LEU A CD2 
8564  N N   . VAL A 1168 ? 0.2418 0.2589 0.2263 0.0335  -0.0321 -0.0565 1166 VAL A N   
8565  C CA  . VAL A 1168 ? 0.2429 0.2616 0.2308 0.0343  -0.0355 -0.0617 1166 VAL A CA  
8566  C C   . VAL A 1168 ? 0.2367 0.2624 0.2206 0.0357  -0.0358 -0.0620 1166 VAL A C   
8567  O O   . VAL A 1168 ? 0.2263 0.2577 0.2050 0.0370  -0.0340 -0.0608 1166 VAL A O   
8568  C CB  . VAL A 1168 ? 0.2470 0.2669 0.2371 0.0362  -0.0374 -0.0677 1166 VAL A CB  
8569  C CG1 . VAL A 1168 ? 0.2636 0.2850 0.2580 0.0372  -0.0413 -0.0736 1166 VAL A CG1 
8570  C CG2 . VAL A 1168 ? 0.2391 0.2522 0.2332 0.0349  -0.0371 -0.0668 1166 VAL A CG2 
8571  N N   . GLU A 1169 ? 0.2141 0.2397 0.2008 0.0351  -0.0380 -0.0634 1167 GLU A N   
8572  C CA  . GLU A 1169 ? 0.2329 0.2653 0.2166 0.0364  -0.0389 -0.0643 1167 GLU A CA  
8573  C C   . GLU A 1169 ? 0.2701 0.3047 0.2574 0.0378  -0.0426 -0.0712 1167 GLU A C   
8574  O O   . GLU A 1169 ? 0.2562 0.2854 0.2496 0.0366  -0.0448 -0.0731 1167 GLU A O   
8575  C CB  . GLU A 1169 ? 0.2411 0.2715 0.2251 0.0346  -0.0383 -0.0597 1167 GLU A CB  
8576  C CG  . GLU A 1169 ? 0.2429 0.2799 0.2244 0.0358  -0.0396 -0.0605 1167 GLU A CG  
8577  C CD  . GLU A 1169 ? 0.2482 0.2828 0.2317 0.0340  -0.0397 -0.0570 1167 GLU A CD  
8578  O OE1 . GLU A 1169 ? 0.2559 0.2839 0.2430 0.0319  -0.0390 -0.0547 1167 GLU A OE1 
8579  O OE2 . GLU A 1169 ? 0.2490 0.2887 0.2303 0.0347  -0.0404 -0.0565 1167 GLU A OE2 
8580  N N   . GLY A 1170 ? 0.2366 0.2794 0.2205 0.0402  -0.0435 -0.0748 1168 GLY A N   
8581  C CA  . GLY A 1170 ? 0.2743 0.3200 0.2616 0.0417  -0.0472 -0.0816 1168 GLY A CA  
8582  C C   . GLY A 1170 ? 0.2615 0.3172 0.2445 0.0447  -0.0477 -0.0861 1168 GLY A C   
8583  O O   . GLY A 1170 ? 0.2979 0.3582 0.2755 0.0456  -0.0452 -0.0838 1168 GLY A O   
8584  N N   . ASP A 1171 ? 0.2764 0.3357 0.2621 0.0462  -0.0512 -0.0927 1169 ASP A N   
8585  C CA  . ASP A 1171 ? 0.2919 0.3612 0.2744 0.0493  -0.0521 -0.0984 1169 ASP A CA  
8586  C C   . ASP A 1171 ? 0.3210 0.3892 0.3054 0.0507  -0.0521 -0.1025 1169 ASP A C   
8587  O O   . ASP A 1171 ? 0.2838 0.3432 0.2725 0.0491  -0.0517 -0.1010 1169 ASP A O   
8588  C CB  . ASP A 1171 ? 0.3132 0.3877 0.2977 0.0507  -0.0559 -0.1044 1169 ASP A CB  
8589  C CG  . ASP A 1171 ? 0.3614 0.4293 0.3549 0.0504  -0.0597 -0.1100 1169 ASP A CG  
8590  O OD1 . ASP A 1171 ? 0.3353 0.3962 0.3333 0.0497  -0.0599 -0.1108 1169 ASP A OD1 
8591  O OD2 . ASP A 1171 ? 0.4613 0.5311 0.4576 0.0507  -0.0628 -0.1136 1169 ASP A OD2 
8592  N N   . ALA A 1172 ? 0.2997 0.3776 0.2812 0.0536  -0.0526 -0.1078 1170 ALA A N   
8593  C CA  . ALA A 1172 ? 0.2972 0.3756 0.2797 0.0552  -0.0522 -0.1115 1170 ALA A CA  
8594  C C   . ALA A 1172 ? 0.3072 0.3769 0.2987 0.0548  -0.0552 -0.1163 1170 ALA A C   
8595  O O   . ALA A 1172 ? 0.2932 0.3569 0.2871 0.0542  -0.0542 -0.1151 1170 ALA A O   
8596  C CB  . ALA A 1172 ? 0.3277 0.4190 0.3062 0.0586  -0.0527 -0.1176 1170 ALA A CB  
8597  N N   . GLU A 1173 ? 0.3240 0.3930 0.3210 0.0553  -0.0592 -0.1216 1171 GLU A N   
8598  C CA  . GLU A 1173 ? 0.3422 0.4034 0.3486 0.0549  -0.0625 -0.1262 1171 GLU A CA  
8599  C C   . GLU A 1173 ? 0.3099 0.3593 0.3204 0.0513  -0.0617 -0.1194 1171 GLU A C   
8600  O O   . GLU A 1173 ? 0.3218 0.3641 0.3383 0.0505  -0.0628 -0.1202 1171 GLU A O   
8601  C CB  . GLU A 1173 ? 0.3901 0.4542 0.4020 0.0565  -0.0673 -0.1342 1171 GLU A CB  
8602  C CG  . GLU A 1173 ? 0.4351 0.5105 0.4447 0.0605  -0.0686 -0.1426 1171 GLU A CG  
8603  C CD  . GLU A 1173 ? 0.5033 0.5794 0.5137 0.0623  -0.0677 -0.1456 1171 GLU A CD  
8604  O OE1 . GLU A 1173 ? 0.4723 0.5389 0.4896 0.0611  -0.0688 -0.1456 1171 GLU A OE1 
8605  O OE2 . GLU A 1173 ? 0.4731 0.5594 0.4772 0.0647  -0.0658 -0.1478 1171 GLU A OE2 
8606  N N   . ARG A 1174 ? 0.2836 0.3312 0.2910 0.0490  -0.0600 -0.1128 1172 ARG A N   
8607  C CA  . ARG A 1174 ? 0.2674 0.3051 0.2775 0.0456  -0.0586 -0.1059 1172 ARG A CA  
8608  C C   . ARG A 1174 ? 0.2964 0.3315 0.3036 0.0450  -0.0551 -0.1016 1172 ARG A C   
8609  O O   . ARG A 1174 ? 0.2535 0.2808 0.2655 0.0432  -0.0552 -0.0997 1172 ARG A O   
8610  C CB  . ARG A 1174 ? 0.2895 0.3274 0.2963 0.0436  -0.0571 -0.1000 1172 ARG A CB  
8611  C CG  . ARG A 1174 ? 0.2840 0.3133 0.2924 0.0402  -0.0551 -0.0927 1172 ARG A CG  
8612  C CD  . ARG A 1174 ? 0.3460 0.3677 0.3637 0.0385  -0.0582 -0.0942 1172 ARG A CD  
8613  N NE  . ARG A 1174 ? 0.2962 0.3109 0.3153 0.0352  -0.0563 -0.0872 1172 ARG A NE  
8614  C CZ  . ARG A 1174 ? 0.3293 0.3371 0.3558 0.0331  -0.0580 -0.0864 1172 ARG A CZ  
8615  N NH1 . ARG A 1174 ? 0.3203 0.3262 0.3539 0.0339  -0.0618 -0.0919 1172 ARG A NH1 
8616  N NH2 . ARG A 1174 ? 0.2974 0.3003 0.3243 0.0302  -0.0559 -0.0799 1172 ARG A NH2 
8617  N N   . ILE A 1175 ? 0.2618 0.3036 0.2612 0.0464  -0.0520 -0.1000 1173 ILE A N   
8618  C CA  . ILE A 1175 ? 0.2673 0.3071 0.2638 0.0460  -0.0487 -0.0961 1173 ILE A CA  
8619  C C   . ILE A 1175 ? 0.2599 0.2974 0.2615 0.0473  -0.0504 -0.1013 1173 ILE A C   
8620  O O   . ILE A 1175 ? 0.2998 0.3305 0.3038 0.0457  -0.0493 -0.0983 1173 ILE A O   
8621  C CB  . ILE A 1175 ? 0.2809 0.3295 0.2688 0.0475  -0.0457 -0.0940 1173 ILE A CB  
8622  C CG1 . ILE A 1175 ? 0.2698 0.3190 0.2535 0.0458  -0.0437 -0.0873 1173 ILE A CG1 
8623  C CG2 . ILE A 1175 ? 0.2739 0.3216 0.2596 0.0477  -0.0428 -0.0917 1173 ILE A CG2 
8624  C CD1 . ILE A 1175 ? 0.2987 0.3577 0.2748 0.0473  -0.0417 -0.0855 1173 ILE A CD1 
8625  N N   . ARG A 1176 ? 0.2866 0.3299 0.2903 0.0501  -0.0533 -0.1094 1174 ARG A N   
8626  C CA  . ARG A 1176 ? 0.2778 0.3192 0.2871 0.0516  -0.0552 -0.1150 1174 ARG A CA  
8627  C C   . ARG A 1176 ? 0.2741 0.3047 0.2924 0.0493  -0.0578 -0.1143 1174 ARG A C   
8628  O O   . ARG A 1176 ? 0.3061 0.3312 0.3277 0.0486  -0.0575 -0.1132 1174 ARG A O   
8629  C CB  . ARG A 1176 ? 0.2703 0.3201 0.2808 0.0552  -0.0583 -0.1245 1174 ARG A CB  
8630  C CG  . ARG A 1176 ? 0.3739 0.4247 0.3879 0.0576  -0.0592 -0.1303 1174 ARG A CG  
8631  C CD  . ARG A 1176 ? 0.4039 0.4618 0.4217 0.0610  -0.0632 -0.1408 1174 ARG A CD  
8632  N NE  . ARG A 1176 ? 0.3715 0.4410 0.3819 0.0629  -0.0623 -0.1427 1174 ARG A NE  
8633  C CZ  . ARG A 1176 ? 0.4408 0.5209 0.4449 0.0655  -0.0602 -0.1449 1174 ARG A CZ  
8634  N NH1 . ARG A 1176 ? 0.4180 0.4984 0.4217 0.0664  -0.0584 -0.1451 1174 ARG A NH1 
8635  N NH2 . ARG A 1176 ? 0.4237 0.5148 0.4219 0.0671  -0.0600 -0.1467 1174 ARG A NH2 
8636  N N   . ALA A 1177 ? 0.2754 0.3032 0.2979 0.0479  -0.0604 -0.1145 1175 ALA A N   
8637  C CA  . ALA A 1177 ? 0.3059 0.3243 0.3375 0.0455  -0.0631 -0.1134 1175 ALA A CA  
8638  C C   . ALA A 1177 ? 0.2762 0.2877 0.3066 0.0423  -0.0600 -0.1048 1175 ALA A C   
8639  O O   . ALA A 1177 ? 0.2972 0.3020 0.3335 0.0409  -0.0610 -0.1037 1175 ALA A O   
8640  C CB  . ALA A 1177 ? 0.2841 0.3016 0.3198 0.0445  -0.0662 -0.1148 1175 ALA A CB  
8641  N N   . VAL A 1178 ? 0.2509 0.2641 0.2739 0.0410  -0.0563 -0.0987 1176 VAL A N   
8642  C CA  . VAL A 1178 ? 0.2441 0.2516 0.2656 0.0381  -0.0532 -0.0909 1176 VAL A CA  
8643  C C   . VAL A 1178 ? 0.2640 0.2706 0.2837 0.0388  -0.0511 -0.0902 1176 VAL A C   
8644  O O   . VAL A 1178 ? 0.2822 0.2825 0.3053 0.0368  -0.0506 -0.0866 1176 VAL A O   
8645  C CB  . VAL A 1178 ? 0.2365 0.2466 0.2510 0.0371  -0.0500 -0.0853 1176 VAL A CB  
8646  C CG1 . VAL A 1178 ? 0.2460 0.2512 0.2584 0.0346  -0.0466 -0.0780 1176 VAL A CG1 
8647  C CG2 . VAL A 1178 ? 0.2565 0.2660 0.2739 0.0358  -0.0521 -0.0853 1176 VAL A CG2 
8648  N N   . ASN A 1179 ? 0.2599 0.2735 0.2747 0.0417  -0.0499 -0.0936 1177 ASN A N   
8649  C CA  . ASN A 1179 ? 0.2696 0.2831 0.2826 0.0426  -0.0479 -0.0932 1177 ASN A CA  
8650  C C   . ASN A 1179 ? 0.3147 0.3228 0.3362 0.0427  -0.0509 -0.0968 1177 ASN A C   
8651  O O   . ASN A 1179 ? 0.2974 0.3010 0.3200 0.0416  -0.0496 -0.0937 1177 ASN A O   
8652  C CB  . ASN A 1179 ? 0.3482 0.3714 0.3552 0.0458  -0.0467 -0.0970 1177 ASN A CB  
8653  C CG  . ASN A 1179 ? 0.3716 0.3965 0.3728 0.0460  -0.0427 -0.0931 1177 ASN A CG  
8654  O OD1 . ASN A 1179 ? 0.4445 0.4637 0.4451 0.0436  -0.0405 -0.0868 1177 ASN A OD1 
8655  N ND2 . ASN A 1179 ? 0.4308 0.4641 0.4279 0.0488  -0.0419 -0.0967 1177 ASN A ND2 
8656  N N   . LYS A 1180 ? 0.2961 0.3047 0.3241 0.0440  -0.0552 -0.1034 1178 LYS A N   
8657  C CA  . LYS A 1180 ? 0.3009 0.3039 0.3384 0.0440  -0.0588 -0.1068 1178 LYS A CA  
8658  C C   . LYS A 1180 ? 0.2783 0.2722 0.3208 0.0401  -0.0592 -0.1005 1178 LYS A C   
8659  O O   . LYS A 1180 ? 0.2973 0.2861 0.3442 0.0392  -0.0595 -0.0990 1178 LYS A O   
8660  C CB  . LYS A 1180 ? 0.3294 0.3347 0.3734 0.0461  -0.0636 -0.1152 1178 LYS A CB  
8661  C CG  . LYS A 1180 ? 0.3510 0.3657 0.3914 0.0502  -0.0637 -0.1227 1178 LYS A CG  
8662  C CD  . LYS A 1180 ? 0.3541 0.3728 0.3989 0.0523  -0.0680 -0.1306 1178 LYS A CD  
8663  C CE  . LYS A 1180 ? 0.4743 0.4861 0.5317 0.0519  -0.0733 -0.1349 1178 LYS A CE  
8664  N NZ  . LYS A 1180 ? 0.4989 0.5148 0.5612 0.0541  -0.0778 -0.1433 1178 LYS A NZ  
8665  N N   . ALA A 1181 ? 0.2947 0.2870 0.3368 0.0378  -0.0590 -0.0966 1179 ALA A N   
8666  C CA  . ALA A 1181 ? 0.2832 0.2682 0.3297 0.0340  -0.0592 -0.0902 1179 ALA A CA  
8667  C C   . ALA A 1181 ? 0.2887 0.2717 0.3301 0.0324  -0.0549 -0.0835 1179 ALA A C   
8668  O O   . ALA A 1181 ? 0.2736 0.2510 0.3195 0.0302  -0.0553 -0.0799 1179 ALA A O   
8669  C CB  . ALA A 1181 ? 0.2853 0.2703 0.3318 0.0321  -0.0596 -0.0877 1179 ALA A CB  
8670  N N   . ILE A 1182 ? 0.2746 0.2624 0.3067 0.0335  -0.0510 -0.0817 1180 ILE A N   
8671  C CA  . ILE A 1182 ? 0.2721 0.2582 0.2996 0.0321  -0.0470 -0.0758 1180 ILE A CA  
8672  C C   . ILE A 1182 ? 0.2596 0.2439 0.2893 0.0332  -0.0472 -0.0775 1180 ILE A C   
8673  O O   . ILE A 1182 ? 0.2869 0.2668 0.3179 0.0312  -0.0460 -0.0730 1180 ILE A O   
8674  C CB  . ILE A 1182 ? 0.2863 0.2779 0.3042 0.0330  -0.0432 -0.0735 1180 ILE A CB  
8675  C CG1 . ILE A 1182 ? 0.2544 0.2464 0.2707 0.0314  -0.0428 -0.0704 1180 ILE A CG1 
8676  C CG2 . ILE A 1182 ? 0.2954 0.2858 0.3089 0.0323  -0.0395 -0.0688 1180 ILE A CG2 
8677  C CD1 . ILE A 1182 ? 0.2923 0.2899 0.3003 0.0324  -0.0396 -0.0684 1180 ILE A CD1 
8678  N N   . ALA A 1183 ? 0.2711 0.2596 0.3014 0.0364  -0.0488 -0.0842 1181 ALA A N   
8679  C CA  . ALA A 1183 ? 0.2848 0.2723 0.3176 0.0377  -0.0491 -0.0864 1181 ALA A CA  
8680  C C   . ALA A 1183 ? 0.2967 0.2767 0.3391 0.0358  -0.0523 -0.0859 1181 ALA A C   
8681  O O   . ALA A 1183 ? 0.2905 0.2676 0.3350 0.0355  -0.0519 -0.0845 1181 ALA A O   
8682  C CB  . ALA A 1183 ? 0.3070 0.3010 0.3395 0.0416  -0.0505 -0.0945 1181 ALA A CB  
8683  N N   . ALA A 1184 ? 0.2854 0.2626 0.3341 0.0345  -0.0557 -0.0866 1182 ALA A N   
8684  C CA  . ALA A 1184 ? 0.3055 0.2759 0.3643 0.0325  -0.0593 -0.0857 1182 ALA A CA  
8685  C C   . ALA A 1184 ? 0.2919 0.2576 0.3506 0.0285  -0.0574 -0.0772 1182 ALA A C   
8686  O O   . ALA A 1184 ? 0.3033 0.2637 0.3700 0.0265  -0.0599 -0.0752 1182 ALA A O   
8687  C CB  . ALA A 1184 ? 0.3074 0.2770 0.3738 0.0324  -0.0639 -0.0897 1182 ALA A CB  
8688  N N   . LEU A 1185 ? 0.2694 0.2370 0.3197 0.0274  -0.0531 -0.0722 1183 LEU A N   
8689  C CA  . LEU A 1185 ? 0.2938 0.2578 0.3438 0.0238  -0.0512 -0.0646 1183 LEU A CA  
8690  C C   . LEU A 1185 ? 0.2806 0.2419 0.3317 0.0235  -0.0503 -0.0626 1183 LEU A C   
8691  O O   . LEU A 1185 ? 0.2964 0.2601 0.3437 0.0260  -0.0488 -0.0654 1183 LEU A O   
8692  C CB  . LEU A 1185 ? 0.2539 0.2209 0.2949 0.0231  -0.0469 -0.0605 1183 LEU A CB  
8693  C CG  . LEU A 1185 ? 0.2841 0.2539 0.3236 0.0233  -0.0475 -0.0617 1183 LEU A CG  
8694  C CD1 . LEU A 1185 ? 0.2824 0.2553 0.3133 0.0229  -0.0433 -0.0579 1183 LEU A CD1 
8695  C CD2 . LEU A 1185 ? 0.3027 0.2691 0.3499 0.0206  -0.0506 -0.0601 1183 LEU A CD2 
8696  N N   . PRO A 1186 ? 0.3187 0.2753 0.3747 0.0204  -0.0512 -0.0576 1184 PRO A N   
8697  C CA  . PRO A 1186 ? 0.2981 0.2524 0.3550 0.0199  -0.0503 -0.0553 1184 PRO A CA  
8698  C C   . PRO A 1186 ? 0.2680 0.2247 0.3153 0.0200  -0.0452 -0.0518 1184 PRO A C   
8699  O O   . PRO A 1186 ? 0.2876 0.2466 0.3289 0.0192  -0.0425 -0.0492 1184 PRO A O   
8700  C CB  . PRO A 1186 ? 0.3343 0.2842 0.3982 0.0161  -0.0522 -0.0497 1184 PRO A CB  
8701  C CG  . PRO A 1186 ? 0.3723 0.3235 0.4348 0.0142  -0.0518 -0.0472 1184 PRO A CG  
8702  C CD  . PRO A 1186 ? 0.3295 0.2838 0.3901 0.0171  -0.0527 -0.0534 1184 PRO A CD  
8703  N N   . GLY A 1187 ? 0.2780 0.2341 0.3244 0.0209  -0.0441 -0.0519 1185 GLY A N   
8704  C CA  . GLY A 1187 ? 0.3158 0.2731 0.3547 0.0205  -0.0398 -0.0478 1185 GLY A CA  
8705  C C   . GLY A 1187 ? 0.2584 0.2206 0.2898 0.0234  -0.0371 -0.0509 1185 GLY A C   
8706  O O   . GLY A 1187 ? 0.3000 0.2642 0.3323 0.0263  -0.0382 -0.0562 1185 GLY A O   
8707  N N   . PRO A 1188 ? 0.2581 0.2226 0.2823 0.0228  -0.0334 -0.0475 1186 PRO A N   
8708  C CA  . PRO A 1188 ? 0.2508 0.2198 0.2679 0.0252  -0.0305 -0.0489 1186 PRO A CA  
8709  C C   . PRO A 1188 ? 0.2569 0.2305 0.2723 0.0278  -0.0315 -0.0540 1186 PRO A C   
8710  O O   . PRO A 1188 ? 0.2683 0.2421 0.2859 0.0274  -0.0334 -0.0553 1186 PRO A O   
8711  C CB  . PRO A 1188 ? 0.2950 0.2645 0.3064 0.0234  -0.0270 -0.0434 1186 PRO A CB  
8712  C CG  . PRO A 1188 ? 0.3200 0.2874 0.3344 0.0210  -0.0284 -0.0412 1186 PRO A CG  
8713  C CD  . PRO A 1188 ? 0.2876 0.2510 0.3102 0.0200  -0.0320 -0.0422 1186 PRO A CD  
8714  N N   . LEU A 1189 ? 0.2515 0.2295 0.2632 0.0304  -0.0302 -0.0569 1187 LEU A N   
8715  C CA  . LEU A 1189 ? 0.2585 0.2425 0.2668 0.0329  -0.0304 -0.0609 1187 LEU A CA  
8716  C C   . LEU A 1189 ? 0.2668 0.2527 0.2694 0.0317  -0.0279 -0.0567 1187 LEU A C   
8717  O O   . LEU A 1189 ? 0.3150 0.2999 0.3139 0.0303  -0.0250 -0.0517 1187 LEU A O   
8718  C CB  . LEU A 1189 ? 0.2528 0.2421 0.2578 0.0357  -0.0291 -0.0641 1187 LEU A CB  
8719  C CG  . LEU A 1189 ? 0.2803 0.2701 0.2909 0.0380  -0.0321 -0.0704 1187 LEU A CG  
8720  C CD1 . LEU A 1189 ? 0.3026 0.2860 0.3189 0.0366  -0.0332 -0.0689 1187 LEU A CD1 
8721  C CD2 . LEU A 1189 ? 0.3450 0.3422 0.3511 0.0411  -0.0306 -0.0740 1187 LEU A CD2 
8722  N N   . LEU A 1190 ? 0.2596 0.2481 0.2619 0.0322  -0.0292 -0.0588 1188 LEU A N   
8723  C CA  . LEU A 1190 ? 0.2621 0.2523 0.2597 0.0313  -0.0273 -0.0551 1188 LEU A CA  
8724  C C   . LEU A 1190 ? 0.2551 0.2527 0.2469 0.0337  -0.0259 -0.0568 1188 LEU A C   
8725  O O   . LEU A 1190 ? 0.2876 0.2895 0.2800 0.0360  -0.0277 -0.0621 1188 LEU A O   
8726  C CB  . LEU A 1190 ? 0.2692 0.2577 0.2703 0.0300  -0.0295 -0.0555 1188 LEU A CB  
8727  C CG  . LEU A 1190 ? 0.2856 0.2677 0.2927 0.0273  -0.0310 -0.0532 1188 LEU A CG  
8728  C CD1 . LEU A 1190 ? 0.3231 0.3046 0.3321 0.0259  -0.0324 -0.0524 1188 LEU A CD1 
8729  C CD2 . LEU A 1190 ? 0.3129 0.2922 0.3180 0.0253  -0.0282 -0.0476 1188 LEU A CD2 
8730  N N   . LEU A 1191 ? 0.2568 0.2562 0.2434 0.0331  -0.0228 -0.0522 1189 LEU A N   
8731  C CA  . LEU A 1191 ? 0.2763 0.2828 0.2575 0.0349  -0.0216 -0.0525 1189 LEU A CA  
8732  C C   . LEU A 1191 ? 0.2470 0.2550 0.2283 0.0346  -0.0229 -0.0529 1189 LEU A C   
8733  O O   . LEU A 1191 ? 0.2625 0.2677 0.2435 0.0327  -0.0221 -0.0488 1189 LEU A O   
8734  C CB  . LEU A 1191 ? 0.2546 0.2620 0.2314 0.0342  -0.0182 -0.0471 1189 LEU A CB  
8735  C CG  . LEU A 1191 ? 0.2597 0.2750 0.2313 0.0360  -0.0167 -0.0468 1189 LEU A CG  
8736  C CD1 . LEU A 1191 ? 0.2688 0.2834 0.2376 0.0350  -0.0137 -0.0415 1189 LEU A CD1 
8737  C CD2 . LEU A 1191 ? 0.2630 0.2826 0.2323 0.0364  -0.0172 -0.0464 1189 LEU A CD2 
8738  N N   . VAL A 1192 ? 0.2532 0.2658 0.2350 0.0366  -0.0251 -0.0581 1190 VAL A N   
8739  C CA  . VAL A 1192 ? 0.2443 0.2588 0.2266 0.0367  -0.0269 -0.0594 1190 VAL A CA  
8740  C C   . VAL A 1192 ? 0.2501 0.2725 0.2265 0.0381  -0.0256 -0.0586 1190 VAL A C   
8741  O O   . VAL A 1192 ? 0.2778 0.3065 0.2513 0.0402  -0.0251 -0.0607 1190 VAL A O   
8742  C CB  . VAL A 1192 ? 0.3007 0.3154 0.2880 0.0380  -0.0306 -0.0661 1190 VAL A CB  
8743  C CG1 . VAL A 1192 ? 0.2947 0.3111 0.2828 0.0379  -0.0326 -0.0674 1190 VAL A CG1 
8744  C CG2 . VAL A 1192 ? 0.3278 0.3349 0.3215 0.0365  -0.0321 -0.0666 1190 VAL A CG2 
8745  N N   . GLN A 1193 ? 0.2401 0.2628 0.2151 0.0371  -0.0253 -0.0554 1191 GLN A N   
8746  C CA  . GLN A 1193 ? 0.1953 0.2256 0.1657 0.0383  -0.0248 -0.0546 1191 GLN A CA  
8747  C C   . GLN A 1193 ? 0.2263 0.2579 0.1986 0.0385  -0.0274 -0.0573 1191 GLN A C   
8748  O O   . GLN A 1193 ? 0.2328 0.2587 0.2084 0.0366  -0.0283 -0.0560 1191 GLN A O   
8749  C CB  . GLN A 1193 ? 0.2285 0.2582 0.1958 0.0369  -0.0222 -0.0478 1191 GLN A CB  
8750  C CG  . GLN A 1193 ? 0.2516 0.2796 0.2174 0.0364  -0.0196 -0.0445 1191 GLN A CG  
8751  C CD  . GLN A 1193 ? 0.2471 0.2764 0.2099 0.0355  -0.0174 -0.0384 1191 GLN A CD  
8752  O OE1 . GLN A 1193 ? 0.2691 0.3054 0.2284 0.0366  -0.0170 -0.0371 1191 GLN A OE1 
8753  N NE2 . GLN A 1193 ? 0.2537 0.2766 0.2181 0.0335  -0.0162 -0.0346 1191 GLN A NE2 
8754  N N   . ALA A 1194 ? 0.2158 0.2553 0.1859 0.0407  -0.0287 -0.0611 1192 ALA A N   
8755  C CA  . ALA A 1194 ? 0.2188 0.2602 0.1906 0.0410  -0.0314 -0.0643 1192 ALA A CA  
8756  C C   . ALA A 1194 ? 0.2380 0.2875 0.2048 0.0419  -0.0308 -0.0622 1192 ALA A C   
8757  O O   . ALA A 1194 ? 0.2435 0.2993 0.2057 0.0430  -0.0291 -0.0605 1192 ALA A O   
8758  C CB  . ALA A 1194 ? 0.2299 0.2736 0.2048 0.0431  -0.0343 -0.0721 1192 ALA A CB  
8759  N N   . ALA A 1195 ? 0.2308 0.2804 0.1987 0.0414  -0.0325 -0.0623 1193 ALA A N   
8760  C CA  . ALA A 1195 ? 0.2763 0.3337 0.2401 0.0422  -0.0325 -0.0605 1193 ALA A CA  
8761  C C   . ALA A 1195 ? 0.2610 0.3191 0.2274 0.0424  -0.0355 -0.0642 1193 ALA A C   
8762  O O   . ALA A 1195 ? 0.2667 0.3177 0.2382 0.0411  -0.0369 -0.0655 1193 ALA A O   
8763  C CB  . ALA A 1195 ? 0.2418 0.2970 0.2036 0.0404  -0.0301 -0.0528 1193 ALA A CB  
8764  N N   . SER A 1196 ? 0.2438 0.3109 0.2071 0.0440  -0.0366 -0.0659 1194 SER A N   
8765  C CA  . SER A 1196 ? 0.2742 0.3424 0.2397 0.0441  -0.0394 -0.0686 1194 SER A CA  
8766  C C   . SER A 1196 ? 0.2576 0.3229 0.2230 0.0422  -0.0385 -0.0624 1194 SER A C   
8767  O O   . SER A 1196 ? 0.2650 0.3292 0.2280 0.0412  -0.0360 -0.0563 1194 SER A O   
8768  C CB  . SER A 1196 ? 0.3180 0.3976 0.2799 0.0466  -0.0409 -0.0725 1194 SER A CB  
8769  O OG  . SER A 1196 ? 0.2924 0.3786 0.2488 0.0466  -0.0389 -0.0669 1194 SER A OG  
8770  N N   . SER A 1197 ? 0.2602 0.3242 0.2286 0.0417  -0.0409 -0.0642 1195 SER A N   
8771  C CA  . SER A 1197 ? 0.2568 0.3189 0.2253 0.0401  -0.0404 -0.0589 1195 SER A CA  
8772  C C   . SER A 1197 ? 0.2580 0.3282 0.2213 0.0409  -0.0393 -0.0548 1195 SER A C   
8773  O O   . SER A 1197 ? 0.2718 0.3401 0.2342 0.0397  -0.0374 -0.0486 1195 SER A O   
8774  C CB  . SER A 1197 ? 0.2903 0.3511 0.2629 0.0397  -0.0433 -0.0620 1195 SER A CB  
8775  O OG  . SER A 1197 ? 0.2939 0.3471 0.2721 0.0386  -0.0445 -0.0649 1195 SER A OG  
8776  N N   . GLY A 1198 ? 0.2861 0.3658 0.2460 0.0430  -0.0405 -0.0582 1196 GLY A N   
8777  C CA  . GLY A 1198 ? 0.2871 0.3756 0.2421 0.0438  -0.0396 -0.0539 1196 GLY A CA  
8778  C C   . GLY A 1198 ? 0.3321 0.4207 0.2841 0.0434  -0.0365 -0.0488 1196 GLY A C   
8779  O O   . GLY A 1198 ? 0.3026 0.3935 0.2527 0.0427  -0.0353 -0.0424 1196 GLY A O   
8780  N N   . GLU A 1199 ? 0.2961 0.3824 0.2483 0.0438  -0.0354 -0.0514 1197 GLU A N   
8781  C CA  . GLU A 1199 ? 0.3069 0.3927 0.2569 0.0434  -0.0325 -0.0467 1197 GLU A CA  
8782  C C   . GLU A 1199 ? 0.3009 0.3780 0.2532 0.0411  -0.0309 -0.0406 1197 GLU A C   
8783  O O   . GLU A 1199 ? 0.2818 0.3603 0.2321 0.0405  -0.0291 -0.0345 1197 GLU A O   
8784  C CB  . GLU A 1199 ? 0.2858 0.3698 0.2364 0.0442  -0.0320 -0.0512 1197 GLU A CB  
8785  C CG  . GLU A 1199 ? 0.3761 0.4609 0.3241 0.0440  -0.0291 -0.0471 1197 GLU A CG  
8786  C CD  . GLU A 1199 ? 0.4783 0.5624 0.4269 0.0452  -0.0289 -0.0522 1197 GLU A CD  
8787  O OE1 . GLU A 1199 ? 0.4353 0.5185 0.3867 0.0462  -0.0311 -0.0590 1197 GLU A OE1 
8788  O OE2 . GLU A 1199 ? 0.5445 0.6291 0.4914 0.0451  -0.0266 -0.0496 1197 GLU A OE2 
8789  N N   . ILE A 1200 ? 0.2632 0.3316 0.2199 0.0398  -0.0316 -0.0420 1198 ILE A N   
8790  C CA  . ILE A 1200 ? 0.2829 0.3437 0.2420 0.0378  -0.0301 -0.0369 1198 ILE A CA  
8791  C C   . ILE A 1200 ? 0.3067 0.3710 0.2650 0.0374  -0.0304 -0.0320 1198 ILE A C   
8792  O O   . ILE A 1200 ? 0.2916 0.3536 0.2501 0.0364  -0.0287 -0.0265 1198 ILE A O   
8793  C CB  . ILE A 1200 ? 0.2583 0.3109 0.2224 0.0365  -0.0311 -0.0396 1198 ILE A CB  
8794  C CG1 . ILE A 1200 ? 0.2735 0.3219 0.2390 0.0365  -0.0307 -0.0431 1198 ILE A CG1 
8795  C CG2 . ILE A 1200 ? 0.2741 0.3205 0.2407 0.0345  -0.0299 -0.0347 1198 ILE A CG2 
8796  C CD1 . ILE A 1200 ? 0.2638 0.3054 0.2344 0.0353  -0.0322 -0.0461 1198 ILE A CD1 
8797  N N   . ALA A 1201 ? 0.2901 0.3601 0.2477 0.0383  -0.0326 -0.0341 1199 ALA A N   
8798  C CA  . ALA A 1201 ? 0.3117 0.3852 0.2688 0.0380  -0.0331 -0.0295 1199 ALA A CA  
8799  C C   . ALA A 1201 ? 0.3137 0.3945 0.2669 0.0386  -0.0320 -0.0247 1199 ALA A C   
8800  O O   . ALA A 1201 ? 0.3264 0.4072 0.2802 0.0378  -0.0314 -0.0188 1199 ALA A O   
8801  C CB  . ALA A 1201 ? 0.3033 0.3814 0.2606 0.0389  -0.0359 -0.0332 1199 ALA A CB  
8802  N N   . ARG A 1202 ? 0.2862 0.3736 0.2358 0.0400  -0.0317 -0.0271 1200 ARG A N   
8803  C CA  . ARG A 1202 ? 0.2942 0.3902 0.2398 0.0406  -0.0307 -0.0226 1200 ARG A CA  
8804  C C   . ARG A 1202 ? 0.3351 0.4277 0.2806 0.0397  -0.0281 -0.0182 1200 ARG A C   
8805  O O   . ARG A 1202 ? 0.3409 0.4375 0.2853 0.0393  -0.0273 -0.0119 1200 ARG A O   
8806  C CB  . ARG A 1202 ? 0.2655 0.3721 0.2071 0.0426  -0.0317 -0.0272 1200 ARG A CB  
8807  C CG  . ARG A 1202 ? 0.2799 0.3923 0.2210 0.0436  -0.0344 -0.0309 1200 ARG A CG  
8808  C CD  . ARG A 1202 ? 0.3189 0.4430 0.2558 0.0458  -0.0352 -0.0355 1200 ARG A CD  
8809  N NE  . ARG A 1202 ? 0.3600 0.4814 0.2975 0.0468  -0.0348 -0.0419 1200 ARG A NE  
8810  C CZ  . ARG A 1202 ? 0.3687 0.4886 0.3083 0.0478  -0.0368 -0.0497 1200 ARG A CZ  
8811  N NH1 . ARG A 1202 ? 0.3351 0.4569 0.2758 0.0482  -0.0394 -0.0526 1200 ARG A NH1 
8812  N NH2 . ARG A 1202 ? 0.3683 0.4844 0.3094 0.0485  -0.0364 -0.0546 1200 ARG A NH2 
8813  N N   . ASN A 1203 ? 0.2880 0.3736 0.2350 0.0394  -0.0269 -0.0211 1201 ASN A N   
8814  C CA  . ASN A 1203 ? 0.3008 0.3845 0.2471 0.0389  -0.0245 -0.0179 1201 ASN A CA  
8815  C C   . ASN A 1203 ? 0.3483 0.4208 0.2986 0.0372  -0.0233 -0.0160 1201 ASN A C   
8816  O O   . ASN A 1203 ? 0.3294 0.3953 0.2818 0.0369  -0.0234 -0.0203 1201 ASN A O   
8817  C CB  . ASN A 1203 ? 0.3105 0.3971 0.2545 0.0403  -0.0240 -0.0230 1201 ASN A CB  
8818  C CG  . ASN A 1203 ? 0.3700 0.4554 0.3133 0.0398  -0.0215 -0.0198 1201 ASN A CG  
8819  O OD1 . ASN A 1203 ? 0.3720 0.4549 0.3162 0.0385  -0.0203 -0.0136 1201 ASN A OD1 
8820  N ND2 . ASN A 1203 ? 0.3911 0.4783 0.3330 0.0409  -0.0209 -0.0241 1201 ASN A ND2 
8821  N N   . PRO A 1204 ? 0.3419 0.4123 0.2935 0.0360  -0.0223 -0.0097 1202 PRO A N   
8822  C CA  . PRO A 1204 ? 0.3959 0.4564 0.3513 0.0345  -0.0211 -0.0083 1202 PRO A CA  
8823  C C   . PRO A 1204 ? 0.3547 0.4107 0.3099 0.0344  -0.0194 -0.0106 1202 PRO A C   
8824  O O   . PRO A 1204 ? 0.3709 0.4189 0.3291 0.0333  -0.0188 -0.0114 1202 PRO A O   
8825  C CB  . PRO A 1204 ? 0.4144 0.4755 0.3709 0.0337  -0.0204 -0.0012 1202 PRO A CB  
8826  C CG  . PRO A 1204 ? 0.4411 0.5111 0.3956 0.0345  -0.0220 0.0010  1202 PRO A CG  
8827  C CD  . PRO A 1204 ? 0.3753 0.4524 0.3255 0.0360  -0.0224 -0.0037 1202 PRO A CD  
8828  N N   . ASP A 1205 ? 0.3516 0.4131 0.3035 0.0354  -0.0188 -0.0119 1203 ASP A N   
8829  C CA  . ASP A 1205 ? 0.3547 0.4126 0.3065 0.0354  -0.0173 -0.0141 1203 ASP A CA  
8830  C C   . ASP A 1205 ? 0.3260 0.3853 0.2771 0.0367  -0.0184 -0.0211 1203 ASP A C   
8831  O O   . ASP A 1205 ? 0.3658 0.4259 0.3158 0.0374  -0.0176 -0.0234 1203 ASP A O   
8832  C CB  . ASP A 1205 ? 0.4158 0.4783 0.3652 0.0356  -0.0156 -0.0103 1203 ASP A CB  
8833  C CG  . ASP A 1205 ? 0.4890 0.5499 0.4401 0.0343  -0.0148 -0.0033 1203 ASP A CG  
8834  O OD1 . ASP A 1205 ? 0.4703 0.5241 0.4248 0.0332  -0.0150 -0.0022 1203 ASP A OD1 
8835  O OD2 . ASP A 1205 ? 0.5453 0.6122 0.4946 0.0345  -0.0142 0.0009  1203 ASP A OD2 
8836  N N   . ALA A 1206 ? 0.3129 0.3727 0.2650 0.0371  -0.0205 -0.0246 1204 ALA A N   
8837  C CA  . ALA A 1206 ? 0.3293 0.3894 0.2820 0.0383  -0.0221 -0.0315 1204 ALA A CA  
8838  C C   . ALA A 1206 ? 0.3149 0.3675 0.2700 0.0376  -0.0212 -0.0336 1204 ALA A C   
8839  O O   . ALA A 1206 ? 0.3549 0.4091 0.3096 0.0388  -0.0215 -0.0380 1204 ALA A O   
8840  C CB  . ALA A 1206 ? 0.3154 0.3741 0.2704 0.0381  -0.0244 -0.0342 1204 ALA A CB  
8841  N N   . TYR A 1207 ? 0.2608 0.3054 0.2187 0.0357  -0.0202 -0.0306 1205 TYR A N   
8842  C CA  . TYR A 1207 ? 0.2795 0.3172 0.2393 0.0348  -0.0190 -0.0311 1205 TYR A CA  
8843  C C   . TYR A 1207 ? 0.2828 0.3198 0.2413 0.0341  -0.0166 -0.0259 1205 TYR A C   
8844  O O   . TYR A 1207 ? 0.3867 0.4221 0.3458 0.0331  -0.0159 -0.0214 1205 TYR A O   
8845  C CB  . TYR A 1207 ? 0.2800 0.3100 0.2440 0.0332  -0.0197 -0.0317 1205 TYR A CB  
8846  C CG  . TYR A 1207 ? 0.2646 0.2949 0.2308 0.0336  -0.0224 -0.0365 1205 TYR A CG  
8847  C CD1 . TYR A 1207 ? 0.2599 0.2915 0.2270 0.0348  -0.0238 -0.0418 1205 TYR A CD1 
8848  C CD2 . TYR A 1207 ? 0.2592 0.2888 0.2272 0.0329  -0.0236 -0.0358 1205 TYR A CD2 
8849  C CE1 . TYR A 1207 ? 0.2533 0.2849 0.2230 0.0353  -0.0265 -0.0464 1205 TYR A CE1 
8850  C CE2 . TYR A 1207 ? 0.2708 0.3007 0.2411 0.0332  -0.0261 -0.0401 1205 TYR A CE2 
8851  C CZ  . TYR A 1207 ? 0.2445 0.2754 0.2158 0.0344  -0.0277 -0.0454 1205 TYR A CZ  
8852  O OH  . TYR A 1207 ? 0.2664 0.2974 0.2407 0.0347  -0.0305 -0.0500 1205 TYR A OH  
8853  N N   . CYS A 1208 ? 0.2670 0.3049 0.2241 0.0347  -0.0154 -0.0266 1206 CYS A N   
8854  C CA  . CYS A 1208 ? 0.2713 0.3094 0.2271 0.0342  -0.0132 -0.0219 1206 CYS A CA  
8855  C C   . CYS A 1208 ? 0.2669 0.2964 0.2256 0.0325  -0.0120 -0.0204 1206 CYS A C   
8856  O O   . CYS A 1208 ? 0.2605 0.2857 0.2210 0.0323  -0.0123 -0.0236 1206 CYS A O   
8857  C CB  . CYS A 1208 ? 0.3212 0.3652 0.2743 0.0357  -0.0125 -0.0235 1206 CYS A CB  
8858  S SG  . CYS A 1208 ? 0.3573 0.4017 0.3091 0.0350  -0.0099 -0.0179 1206 CYS A SG  
8859  N N   . LEU A 1209 ? 0.2260 0.2531 0.1854 0.0313  -0.0109 -0.0156 1207 LEU A N   
8860  C CA  . LEU A 1209 ? 0.2308 0.2506 0.1930 0.0297  -0.0099 -0.0143 1207 LEU A CA  
8861  C C   . LEU A 1209 ? 0.2375 0.2557 0.1991 0.0296  -0.0083 -0.0139 1207 LEU A C   
8862  O O   . LEU A 1209 ? 0.2511 0.2635 0.2148 0.0284  -0.0076 -0.0139 1207 LEU A O   
8863  C CB  . LEU A 1209 ? 0.2359 0.2540 0.1996 0.0287  -0.0093 -0.0098 1207 LEU A CB  
8864  C CG  . LEU A 1209 ? 0.2415 0.2612 0.2062 0.0287  -0.0109 -0.0097 1207 LEU A CG  
8865  C CD1 . LEU A 1209 ? 0.2640 0.2816 0.2310 0.0278  -0.0104 -0.0055 1207 LEU A CD1 
8866  C CD2 . LEU A 1209 ? 0.2705 0.2869 0.2371 0.0283  -0.0121 -0.0137 1207 LEU A CD2 
8867  N N   . ASN A 1210 ? 0.2587 0.2825 0.2176 0.0308  -0.0077 -0.0137 1208 ASN A N   
8868  C CA  . ASN A 1210 ? 0.2618 0.2844 0.2202 0.0309  -0.0063 -0.0137 1208 ASN A CA  
8869  C C   . ASN A 1210 ? 0.2412 0.2593 0.2014 0.0308  -0.0069 -0.0181 1208 ASN A C   
8870  O O   . ASN A 1210 ? 0.2805 0.2944 0.2418 0.0300  -0.0058 -0.0176 1208 ASN A O   
8871  C CB  . ASN A 1210 ? 0.2853 0.3159 0.2405 0.0325  -0.0059 -0.0139 1208 ASN A CB  
8872  C CG  . ASN A 1210 ? 0.3365 0.3723 0.2902 0.0324  -0.0052 -0.0086 1208 ASN A CG  
8873  O OD1 . ASN A 1210 ? 0.3998 0.4335 0.3550 0.0314  -0.0054 -0.0052 1208 ASN A OD1 
8874  N ND2 . ASN A 1210 ? 0.4074 0.4505 0.3584 0.0335  -0.0046 -0.0079 1208 ASN A ND2 
8875  N N   . TRP A 1211 ? 0.2378 0.2568 0.1986 0.0315  -0.0088 -0.0223 1209 TRP A N   
8876  C CA  . TRP A 1211 ? 0.2523 0.2677 0.2154 0.0316  -0.0098 -0.0266 1209 TRP A CA  
8877  C C   . TRP A 1211 ? 0.2512 0.2599 0.2177 0.0298  -0.0105 -0.0266 1209 TRP A C   
8878  O O   . TRP A 1211 ? 0.2788 0.2842 0.2480 0.0296  -0.0117 -0.0296 1209 TRP A O   
8879  C CB  . TRP A 1211 ? 0.2552 0.2757 0.2177 0.0336  -0.0117 -0.0317 1209 TRP A CB  
8880  C CG  . TRP A 1211 ? 0.2706 0.2996 0.2292 0.0353  -0.0110 -0.0313 1209 TRP A CG  
8881  C CD1 . TRP A 1211 ? 0.2584 0.2942 0.2150 0.0366  -0.0122 -0.0326 1209 TRP A CD1 
8882  C CD2 . TRP A 1211 ? 0.2734 0.3058 0.2297 0.0358  -0.0091 -0.0290 1209 TRP A CD2 
8883  N NE1 . TRP A 1211 ? 0.2900 0.3336 0.2431 0.0378  -0.0110 -0.0311 1209 TRP A NE1 
8884  C CE2 . TRP A 1211 ? 0.2715 0.3132 0.2245 0.0373  -0.0091 -0.0289 1209 TRP A CE2 
8885  C CE3 . TRP A 1211 ? 0.2806 0.3095 0.2374 0.0350  -0.0074 -0.0270 1209 TRP A CE3 
8886  C CZ2 . TRP A 1211 ? 0.2755 0.3231 0.2257 0.0379  -0.0075 -0.0265 1209 TRP A CZ2 
8887  C CZ3 . TRP A 1211 ? 0.2800 0.3144 0.2342 0.0358  -0.0058 -0.0249 1209 TRP A CZ3 
8888  C CH2 . TRP A 1211 ? 0.2723 0.3160 0.2234 0.0372  -0.0058 -0.0246 1209 TRP A CH2 
8889  N N   . LEU A 1212 ? 0.2248 0.2318 0.1917 0.0286  -0.0100 -0.0232 1210 LEU A N   
8890  C CA  . LEU A 1212 ? 0.2186 0.2203 0.1887 0.0268  -0.0104 -0.0228 1210 LEU A CA  
8891  C C   . LEU A 1212 ? 0.2199 0.2175 0.1909 0.0253  -0.0086 -0.0196 1210 LEU A C   
8892  O O   . LEU A 1212 ? 0.2245 0.2184 0.1979 0.0237  -0.0087 -0.0190 1210 LEU A O   
8893  C CB  . LEU A 1212 ? 0.2023 0.2055 0.1728 0.0266  -0.0114 -0.0221 1210 LEU A CB  
8894  C CG  . LEU A 1212 ? 0.2126 0.2186 0.1833 0.0278  -0.0136 -0.0261 1210 LEU A CG  
8895  C CD1 . LEU A 1212 ? 0.2325 0.2417 0.2025 0.0280  -0.0143 -0.0249 1210 LEU A CD1 
8896  C CD2 . LEU A 1212 ? 0.2457 0.2473 0.2204 0.0267  -0.0151 -0.0287 1210 LEU A CD2 
8897  N N   . VAL A 1213 ? 0.2279 0.2265 0.1970 0.0257  -0.0070 -0.0175 1211 VAL A N   
8898  C CA  . VAL A 1213 ? 0.2275 0.2225 0.1975 0.0244  -0.0054 -0.0151 1211 VAL A CA  
8899  C C   . VAL A 1213 ? 0.2255 0.2194 0.1953 0.0247  -0.0050 -0.0166 1211 VAL A C   
8900  O O   . VAL A 1213 ? 0.2487 0.2454 0.2174 0.0261  -0.0058 -0.0192 1211 VAL A O   
8901  C CB  . VAL A 1213 ? 0.2318 0.2282 0.2007 0.0244  -0.0039 -0.0112 1211 VAL A CB  
8902  C CG1 . VAL A 1213 ? 0.2381 0.2348 0.2082 0.0240  -0.0044 -0.0097 1211 VAL A CG1 
8903  C CG2 . VAL A 1213 ? 0.2477 0.2491 0.2138 0.0259  -0.0036 -0.0105 1211 VAL A CG2 
8904  N N   . GLU A 1214 ? 0.2374 0.2275 0.2085 0.0234  -0.0040 -0.0151 1212 GLU A N   
8905  C CA  . GLU A 1214 ? 0.2683 0.2568 0.2398 0.0234  -0.0036 -0.0160 1212 GLU A CA  
8906  C C   . GLU A 1214 ? 0.2287 0.2171 0.1989 0.0232  -0.0016 -0.0130 1212 GLU A C   
8907  O O   . GLU A 1214 ? 0.2258 0.2124 0.1968 0.0220  -0.0008 -0.0105 1212 GLU A O   
8908  C CB  . GLU A 1214 ? 0.2979 0.2819 0.2723 0.0217  -0.0042 -0.0165 1212 GLU A CB  
8909  C CG  . GLU A 1214 ? 0.4205 0.4026 0.3962 0.0217  -0.0046 -0.0181 1212 GLU A CG  
8910  C CD  . GLU A 1214 ? 0.4405 0.4189 0.4196 0.0198  -0.0057 -0.0182 1212 GLU A CD  
8911  O OE1 . GLU A 1214 ? 0.4682 0.4444 0.4478 0.0183  -0.0045 -0.0158 1212 GLU A OE1 
8912  O OE2 . GLU A 1214 ? 0.4553 0.4332 0.4367 0.0199  -0.0077 -0.0205 1212 GLU A OE2 
8913  N N   . GLU A 1215 ? 0.2224 0.2132 0.1911 0.0243  -0.0011 -0.0134 1213 GLU A N   
8914  C CA  . GLU A 1215 ? 0.2028 0.1936 0.1707 0.0240  0.0006  -0.0105 1213 GLU A CA  
8915  C C   . GLU A 1215 ? 0.2244 0.2109 0.1940 0.0229  0.0011  -0.0106 1213 GLU A C   
8916  O O   . GLU A 1215 ? 0.2242 0.2092 0.1950 0.0229  0.0002  -0.0131 1213 GLU A O   
8917  C CB  . GLU A 1215 ? 0.2135 0.2091 0.1792 0.0257  0.0011  -0.0109 1213 GLU A CB  
8918  C CG  . GLU A 1215 ? 0.2223 0.2234 0.1860 0.0269  0.0006  -0.0107 1213 GLU A CG  
8919  C CD  . GLU A 1215 ? 0.2676 0.2744 0.2292 0.0287  0.0008  -0.0123 1213 GLU A CD  
8920  O OE1 . GLU A 1215 ? 0.2501 0.2579 0.2119 0.0297  -0.0004 -0.0164 1213 GLU A OE1 
8921  O OE2 . GLU A 1215 ? 0.2487 0.2593 0.2089 0.0289  0.0020  -0.0094 1213 GLU A OE2 
8922  N N   . VAL A 1216 ? 0.2133 0.1980 0.1835 0.0218  0.0024  -0.0079 1214 VAL A N   
8923  C CA  . VAL A 1216 ? 0.2225 0.2038 0.1939 0.0207  0.0029  -0.0075 1214 VAL A CA  
8924  C C   . VAL A 1216 ? 0.2243 0.2064 0.1949 0.0208  0.0044  -0.0051 1214 VAL A C   
8925  O O   . VAL A 1216 ? 0.2304 0.2136 0.2010 0.0207  0.0050  -0.0028 1214 VAL A O   
8926  C CB  . VAL A 1216 ? 0.2395 0.2176 0.2128 0.0189  0.0028  -0.0070 1214 VAL A CB  
8927  C CG1 . VAL A 1216 ? 0.2304 0.2060 0.2047 0.0178  0.0035  -0.0064 1214 VAL A CG1 
8928  C CG2 . VAL A 1216 ? 0.2606 0.2380 0.2351 0.0186  0.0012  -0.0091 1214 VAL A CG2 
8929  N N   . SER A 1217 ? 0.2328 0.2146 0.2033 0.0210  0.0048  -0.0056 1215 SER A N   
8930  C CA  . SER A 1217 ? 0.2312 0.2136 0.2014 0.0210  0.0062  -0.0034 1215 SER A CA  
8931  C C   . SER A 1217 ? 0.2115 0.1900 0.1833 0.0195  0.0066  -0.0030 1215 SER A C   
8932  O O   . SER A 1217 ? 0.2282 0.2046 0.2009 0.0190  0.0058  -0.0046 1215 SER A O   
8933  C CB  . SER A 1217 ? 0.2699 0.2555 0.2389 0.0224  0.0064  -0.0044 1215 SER A CB  
8934  O OG  . SER A 1217 ? 0.2952 0.2805 0.2644 0.0221  0.0076  -0.0027 1215 SER A OG  
8935  N N   . ALA A 1218 ? 0.2113 0.1890 0.1838 0.0188  0.0075  -0.0007 1216 ALA A N   
8936  C CA  . ALA A 1218 ? 0.2286 0.2035 0.2025 0.0175  0.0079  -0.0002 1216 ALA A CA  
8937  C C   . ALA A 1218 ? 0.2250 0.2005 0.1990 0.0176  0.0090  0.0017  1216 ALA A C   
8938  O O   . ALA A 1218 ? 0.2581 0.2350 0.2325 0.0178  0.0094  0.0036  1216 ALA A O   
8939  C CB  . ALA A 1218 ? 0.2257 0.1991 0.2010 0.0162  0.0078  0.0001  1216 ALA A CB  
8940  N N   . SER A 1219 ? 0.2086 0.1830 0.1829 0.0173  0.0093  0.0013  1217 SER A N   
8941  C CA  . SER A 1219 ? 0.2210 0.1959 0.1957 0.0173  0.0102  0.0030  1217 SER A CA  
8942  C C   . SER A 1219 ? 0.2151 0.1873 0.1912 0.0159  0.0104  0.0033  1217 SER A C   
8943  O O   . SER A 1219 ? 0.2178 0.1885 0.1941 0.0153  0.0100  0.0021  1217 SER A O   
8944  C CB  . SER A 1219 ? 0.2392 0.2160 0.2129 0.0184  0.0104  0.0022  1217 SER A CB  
8945  O OG  . SER A 1219 ? 0.2443 0.2219 0.2185 0.0183  0.0113  0.0041  1217 SER A OG  
8946  N N   . ILE A 1220 ? 0.2078 0.1797 0.1852 0.0153  0.0109  0.0048  1218 ILE A N   
8947  C CA  . ILE A 1220 ? 0.2341 0.2042 0.2131 0.0140  0.0111  0.0048  1218 ILE A CA  
8948  C C   . ILE A 1220 ? 0.2142 0.1844 0.1941 0.0140  0.0117  0.0062  1218 ILE A C   
8949  O O   . ILE A 1220 ? 0.2213 0.1926 0.2021 0.0144  0.0120  0.0080  1218 ILE A O   
8950  C CB  . ILE A 1220 ? 0.2305 0.2003 0.2111 0.0135  0.0108  0.0047  1218 ILE A CB  
8951  C CG1 . ILE A 1220 ? 0.3156 0.2856 0.2953 0.0136  0.0102  0.0034  1218 ILE A CG1 
8952  C CG2 . ILE A 1220 ? 0.2687 0.2374 0.2506 0.0123  0.0110  0.0041  1218 ILE A CG2 
8953  C CD1 . ILE A 1220 ? 0.4158 0.3863 0.3970 0.0137  0.0099  0.0036  1218 ILE A CD1 
8954  N N   . ASN A 1221 ? 0.2146 0.1838 0.1946 0.0134  0.0118  0.0058  1219 ASN A N   
8955  C CA  . ASN A 1221 ? 0.2371 0.2063 0.2181 0.0132  0.0124  0.0070  1219 ASN A CA  
8956  C C   . ASN A 1221 ? 0.2476 0.2159 0.2309 0.0122  0.0123  0.0072  1219 ASN A C   
8957  O O   . ASN A 1221 ? 0.2684 0.2360 0.2519 0.0112  0.0121  0.0060  1219 ASN A O   
8958  C CB  . ASN A 1221 ? 0.2525 0.2210 0.2330 0.0129  0.0123  0.0064  1219 ASN A CB  
8959  C CG  . ASN A 1221 ? 0.2657 0.2341 0.2475 0.0125  0.0128  0.0075  1219 ASN A CG  
8960  O OD1 . ASN A 1221 ? 0.2403 0.2093 0.2234 0.0126  0.0132  0.0089  1219 ASN A OD1 
8961  N ND2 . ASN A 1221 ? 0.3070 0.2746 0.2887 0.0121  0.0126  0.0070  1219 ASN A ND2 
8962  N N   . THR A 1222 ? 0.2279 0.1967 0.2130 0.0125  0.0124  0.0086  1220 THR A N   
8963  C CA  . THR A 1222 ? 0.2631 0.2311 0.2511 0.0118  0.0121  0.0083  1220 THR A CA  
8964  C C   . THR A 1222 ? 0.3123 0.2799 0.3022 0.0113  0.0122  0.0090  1220 THR A C   
8965  O O   . THR A 1222 ? 0.3419 0.3090 0.3347 0.0109  0.0118  0.0085  1220 THR A O   
8966  C CB  . THR A 1222 ? 0.2932 0.2616 0.2834 0.0124  0.0116  0.0096  1220 THR A CB  
8967  O OG1 . THR A 1222 ? 0.2750 0.2447 0.2657 0.0129  0.0119  0.0123  1220 THR A OG1 
8968  C CG2 . THR A 1222 ? 0.2868 0.2557 0.2754 0.0129  0.0114  0.0088  1220 THR A CG2 
8969  N N   . ALA A 1223 ? 0.2688 0.2367 0.2572 0.0114  0.0128  0.0098  1221 ALA A N   
8970  C CA  . ALA A 1223 ? 0.3200 0.2875 0.3098 0.0109  0.0129  0.0102  1221 ALA A CA  
8971  C C   . ALA A 1223 ? 0.3769 0.3440 0.3653 0.0101  0.0129  0.0086  1221 ALA A C   
8972  O O   . ALA A 1223 ? 0.4384 0.4053 0.4276 0.0096  0.0129  0.0089  1221 ALA A O   
8973  C CB  . ALA A 1223 ? 0.3293 0.2981 0.3189 0.0115  0.0135  0.0123  1221 ALA A CB  
8974  N N   . ALA A 1224 ? 0.3829 0.3498 0.3695 0.0099  0.0126  0.0072  1222 ALA A N   
8975  C CA  . ALA A 1224 ? 0.3937 0.3605 0.3791 0.0090  0.0124  0.0064  1222 ALA A CA  
8976  C C   . ALA A 1224 ? 0.4387 0.4060 0.4253 0.0079  0.0122  0.0056  1222 ALA A C   
8977  O O   . ALA A 1224 ? 0.5200 0.4876 0.5062 0.0071  0.0120  0.0056  1222 ALA A O   
8978  C CB  . ALA A 1224 ? 0.3982 0.3650 0.3819 0.0089  0.0120  0.0055  1222 ALA A CB  
8979  N N   . ALA A 1225 ? 0.4320 0.3998 0.4206 0.0078  0.0120  0.0047  1223 ALA A N   
8980  C CA  . ALA A 1225 ? 0.5095 0.4785 0.4995 0.0069  0.0117  0.0033  1223 ALA A CA  
8981  C C   . ALA A 1225 ? 0.5498 0.5184 0.5415 0.0068  0.0118  0.0041  1223 ALA A C   
8982  O O   . ALA A 1225 ? 0.5387 0.5086 0.5314 0.0060  0.0114  0.0029  1223 ALA A O   
8983  C CB  . ALA A 1225 ? 0.5147 0.4845 0.5070 0.0071  0.0114  0.0015  1223 ALA A CB  
8984  N N   . GLY A 1226 ? 0.4688 0.4362 0.4607 0.0074  0.0121  0.0060  1224 GLY A N   
8985  C CA  . GLY A 1226 ? 0.5387 0.5059 0.5323 0.0073  0.0121  0.0070  1224 GLY A CA  
8986  C C   . GLY A 1226 ? 0.5844 0.5510 0.5810 0.0078  0.0121  0.0084  1224 GLY A C   
8987  O O   . GLY A 1226 ? 0.5138 0.4804 0.5122 0.0077  0.0121  0.0095  1224 GLY A O   
8988  N N   . GLY A 1227 ? 0.4308 0.3971 0.4284 0.0084  0.0119  0.0086  1225 GLY A N   
8989  C CA  . GLY A 1227 ? 0.4874 0.4534 0.4884 0.0088  0.0116  0.0106  1225 GLY A CA  
8990  C C   . GLY A 1227 ? 0.4585 0.4246 0.4596 0.0094  0.0115  0.0113  1225 GLY A C   
8991  O O   . GLY A 1227 ? 0.4818 0.4481 0.4804 0.0097  0.0116  0.0099  1225 GLY A O   
8992  N N   . ASN A 1228 ? 0.3532 0.3194 0.3575 0.0097  0.0111  0.0137  1226 ASN A N   
8993  C CA  . ASN A 1228 ? 0.4310 0.3976 0.4358 0.0103  0.0108  0.0151  1226 ASN A CA  
8994  C C   . ASN A 1228 ? 0.4558 0.4213 0.4661 0.0101  0.0094  0.0147  1226 ASN A C   
8995  O O   . ASN A 1228 ? 0.4735 0.4385 0.4883 0.0098  0.0087  0.0165  1226 ASN A O   
8996  C CB  . ASN A 1228 ? 0.4443 0.4129 0.4486 0.0107  0.0114  0.0188  1226 ASN A CB  
8997  C CG  . ASN A 1228 ? 0.4784 0.4483 0.4822 0.0113  0.0113  0.0204  1226 ASN A CG  
8998  O OD1 . ASN A 1228 ? 0.4820 0.4508 0.4882 0.0113  0.0103  0.0200  1226 ASN A OD1 
8999  N ND2 . ASN A 1228 ? 0.4533 0.4258 0.4540 0.0119  0.0122  0.0222  1226 ASN A ND2 
9000  N N   . ALA A 1229 ? 0.4607 0.4257 0.4711 0.0104  0.0089  0.0124  1227 ALA A N   
9001  C CA  . ALA A 1229 ? 0.4767 0.4407 0.4927 0.0105  0.0074  0.0114  1227 ALA A CA  
9002  C C   . ALA A 1229 ? 0.5287 0.4926 0.5486 0.0107  0.0065  0.0151  1227 ALA A C   
9003  O O   . ALA A 1229 ? 0.5066 0.4695 0.5327 0.0104  0.0051  0.0159  1227 ALA A O   
9004  C CB  . ALA A 1229 ? 0.4387 0.4029 0.4537 0.0108  0.0072  0.0081  1227 ALA A CB  
9005  N N   . SER A 1230 ? 0.4802 0.4455 0.4970 0.0111  0.0071  0.0176  1228 SER A N   
9006  C CA  . SER A 1230 ? 0.5151 0.4812 0.5354 0.0112  0.0063  0.0216  1228 SER A CA  
9007  C C   . SER A 1230 ? 0.5675 0.5342 0.5909 0.0106  0.0061  0.0252  1228 SER A C   
9008  O O   . SER A 1230 ? 0.5884 0.5548 0.6179 0.0102  0.0045  0.0280  1228 SER A O   
9009  C CB  . SER A 1230 ? 0.5248 0.4932 0.5403 0.0118  0.0072  0.0234  1228 SER A CB  
9010  N N   . LEU A 1231 ? 0.4662 0.4338 0.4861 0.0103  0.0074  0.0252  1229 LEU A N   
9011  C CA  . LEU A 1231 ? 0.5409 0.5096 0.5636 0.0097  0.0074  0.0286  1229 LEU A CA  
9012  C C   . LEU A 1231 ? 0.5414 0.5077 0.5696 0.0090  0.0061  0.0272  1229 LEU A C   
9013  O O   . LEU A 1231 ? 0.5456 0.5124 0.5777 0.0083  0.0057  0.0302  1229 LEU A O   
9014  C CB  . LEU A 1231 ? 0.4745 0.4454 0.4916 0.0098  0.0093  0.0290  1229 LEU A CB  
9015  C CG  . LEU A 1231 ? 0.4796 0.4544 0.4928 0.0105  0.0103  0.0316  1229 LEU A CG  
9016  C CD1 . LEU A 1231 ? 0.3868 0.3640 0.3961 0.0107  0.0119  0.0318  1229 LEU A CD1 
9017  C CD2 . LEU A 1231 ? 0.5293 0.5064 0.5466 0.0101  0.0095  0.0366  1229 LEU A CD2 
9018  N N   . MET A 1232 ? 0.5571 0.5212 0.5861 0.0092  0.0055  0.0226  1230 MET A N   
9019  C CA  . MET A 1232 ? 0.5801 0.5423 0.6150 0.0087  0.0040  0.0208  1230 MET A CA  
9020  C C   . MET A 1232 ? 0.5561 0.5173 0.5991 0.0085  0.0018  0.0234  1230 MET A C   
9021  O O   . MET A 1232 ? 0.5321 0.4921 0.5813 0.0079  0.0004  0.0236  1230 MET A O   
9022  C CB  . MET A 1232 ? 0.5289 0.4902 0.5629 0.0090  0.0038  0.0152  1230 MET A CB  
9023  C CG  . MET A 1232 ? 0.5292 0.4913 0.5569 0.0089  0.0054  0.0128  1230 MET A CG  
9024  S SD  . MET A 1232 ? 0.5991 0.5615 0.6257 0.0091  0.0052  0.0069  1230 MET A SD  
9025  C CE  . MET A 1232 ? 0.5275 0.4889 0.5624 0.0090  0.0030  0.0044  1230 MET A CE  
9026  N N   . ALA A 1233 ? 0.6278 0.5895 0.6714 0.0089  0.0013  0.0255  1231 ALA A N   
9027  C CA  . ALA A 1233 ? 0.6464 0.6073 0.6980 0.0086  -0.0009 0.0287  1231 ALA A CA  
9028  C C   . ALA A 1233 ? 0.6925 0.6558 0.7455 0.0078  -0.0008 0.0353  1231 ALA A C   
9029  O O   . ALA A 1233 ? 0.6865 0.6494 0.7467 0.0073  -0.0029 0.0390  1231 ALA A O   
9030  C CB  . ALA A 1233 ? 0.6453 0.6059 0.6974 0.0094  -0.0017 0.0281  1231 ALA A CB  
9031  N N   . ILE A 1234 ? 0.6916 0.6576 0.7381 0.0077  0.0014  0.0369  1232 ILE A N   
9032  C CA  . ILE A 1234 ? 0.6842 0.6537 0.7311 0.0070  0.0019  0.0429  1232 ILE A CA  
9033  C C   . ILE A 1234 ? 0.6687 0.6381 0.7184 0.0061  0.0019  0.0438  1232 ILE A C   
9034  O O   . ILE A 1234 ? 0.6379 0.6074 0.6828 0.0063  0.0035  0.0411  1232 ILE A O   
9035  C CB  . ILE A 1234 ? 0.5902 0.5636 0.6288 0.0077  0.0042  0.0439  1232 ILE A CB  
9036  C CG1 . ILE A 1234 ? 0.6211 0.5950 0.6582 0.0084  0.0038  0.0440  1232 ILE A CG1 
9037  C CG2 . ILE A 1234 ? 0.4913 0.4694 0.5299 0.0070  0.0050  0.0494  1232 ILE A CG2 
9038  C CD1 . ILE A 1234 ? 0.5383 0.5171 0.5695 0.0088  0.0054  0.0467  1232 ILE A CD1 
9039  N N   . GLY A 1235 ? 0.6079 0.5770 0.6656 0.0051  -0.0001 0.0478  1233 GLY A N   
9040  C CA  . GLY A 1235 ? 0.5183 0.4877 0.5797 0.0041  -0.0004 0.0494  1233 GLY A CA  
9041  C C   . GLY A 1235 ? 0.5015 0.4739 0.5684 0.0029  -0.0014 0.0568  1233 GLY A C   
9042  O O   . GLY A 1235 ? 0.5526 0.5251 0.6240 0.0026  -0.0031 0.0600  1233 GLY A O   
9043  O OXT . GLY A 1235 ? 0.3372 0.3123 0.4046 0.0020  -0.0007 0.0599  1233 GLY A OXT 
9044  N N   . ALA B 16   ? 0.5654 0.4779 0.5548 0.0609  -0.0123 -0.0254 14   ALA B N   
9045  C CA  . ALA B 16   ? 0.5684 0.4853 0.5589 0.0557  -0.0125 -0.0247 14   ALA B CA  
9046  C C   . ALA B 16   ? 0.5502 0.4593 0.5342 0.0517  -0.0136 -0.0254 14   ALA B C   
9047  O O   . ALA B 16   ? 0.5898 0.4929 0.5691 0.0523  -0.0129 -0.0273 14   ALA B O   
9048  C CB  . ALA B 16   ? 0.4969 0.4219 0.4912 0.0554  -0.0101 -0.0256 14   ALA B CB  
9049  N N   . PRO B 17   ? 0.5580 0.4676 0.5419 0.0475  -0.0151 -0.0238 15   PRO B N   
9050  C CA  . PRO B 17   ? 0.5201 0.4232 0.4982 0.0432  -0.0161 -0.0242 15   PRO B CA  
9051  C C   . PRO B 17   ? 0.4987 0.4034 0.4755 0.0413  -0.0145 -0.0260 15   PRO B C   
9052  O O   . PRO B 17   ? 0.4937 0.4062 0.4747 0.0412  -0.0128 -0.0262 15   PRO B O   
9053  C CB  . PRO B 17   ? 0.5484 0.4547 0.5282 0.0394  -0.0176 -0.0221 15   PRO B CB  
9054  C CG  . PRO B 17   ? 0.5683 0.4839 0.5548 0.0409  -0.0168 -0.0212 15   PRO B CG  
9055  C CD  . PRO B 17   ? 0.5185 0.4346 0.5071 0.0463  -0.0160 -0.0217 15   PRO B CD  
9056  N N   . ALA B 18   ? 0.4618 0.3586 0.4325 0.0399  -0.0149 -0.0273 16   ALA B N   
9057  C CA  . ALA B 18   ? 0.4274 0.3249 0.3961 0.0379  -0.0136 -0.0291 16   ALA B CA  
9058  C C   . ALA B 18   ? 0.3773 0.2816 0.3488 0.0335  -0.0135 -0.0280 16   ALA B C   
9059  O O   . ALA B 18   ? 0.3929 0.2972 0.3645 0.0307  -0.0150 -0.0263 16   ALA B O   
9060  C CB  . ALA B 18   ? 0.4538 0.3412 0.4152 0.0362  -0.0148 -0.0303 16   ALA B CB  
9061  N N   . PRO B 19   ? 0.3573 0.2674 0.3308 0.0331  -0.0118 -0.0290 17   PRO B N   
9062  C CA  . PRO B 19   ? 0.3517 0.2684 0.3279 0.0293  -0.0116 -0.0280 17   PRO B CA  
9063  C C   . PRO B 19   ? 0.3268 0.2395 0.2991 0.0247  -0.0131 -0.0276 17   PRO B C   
9064  O O   . PRO B 19   ? 0.3439 0.2505 0.3111 0.0236  -0.0136 -0.0288 17   PRO B O   
9065  C CB  . PRO B 19   ? 0.3379 0.2594 0.3155 0.0300  -0.0095 -0.0294 17   PRO B CB  
9066  C CG  . PRO B 19   ? 0.3876 0.3083 0.3658 0.0348  -0.0083 -0.0304 17   PRO B CG  
9067  C CD  . PRO B 19   ? 0.3954 0.3069 0.3691 0.0363  -0.0097 -0.0308 17   PRO B CD  
9068  N N   . PHE B 20   ? 0.3302 0.2462 0.3045 0.0221  -0.0140 -0.0258 18   PHE B N   
9069  C CA  . PHE B 20   ? 0.3119 0.2262 0.2835 0.0175  -0.0152 -0.0250 18   PHE B CA  
9070  C C   . PHE B 20   ? 0.3681 0.2734 0.3345 0.0164  -0.0170 -0.0247 18   PHE B C   
9071  O O   . PHE B 20   ? 0.3716 0.2746 0.3351 0.0124  -0.0180 -0.0243 18   PHE B O   
9072  C CB  . PHE B 20   ? 0.3090 0.2256 0.2796 0.0150  -0.0143 -0.0261 18   PHE B CB  
9073  C CG  . PHE B 20   ? 0.2759 0.2011 0.2513 0.0157  -0.0126 -0.0262 18   PHE B CG  
9074  C CD1 . PHE B 20   ? 0.2662 0.1974 0.2451 0.0139  -0.0126 -0.0247 18   PHE B CD1 
9075  C CD2 . PHE B 20   ? 0.2856 0.2126 0.2617 0.0180  -0.0110 -0.0277 18   PHE B CD2 
9076  C CE1 . PHE B 20   ? 0.2936 0.2321 0.2767 0.0144  -0.0112 -0.0247 18   PHE B CE1 
9077  C CE2 . PHE B 20   ? 0.2917 0.2263 0.2720 0.0184  -0.0095 -0.0276 18   PHE B CE2 
9078  C CZ  . PHE B 20   ? 0.2843 0.2244 0.2681 0.0166  -0.0097 -0.0261 18   PHE B CZ  
9079  N N   . ALA B 21   ? 0.3958 0.2958 0.3610 0.0197  -0.0175 -0.0249 19   ALA B N   
9080  C CA  . ALA B 21   ? 0.4229 0.3134 0.3827 0.0188  -0.0194 -0.0246 19   ALA B CA  
9081  C C   . ALA B 21   ? 0.4458 0.3359 0.4053 0.0157  -0.0210 -0.0223 19   ALA B C   
9082  O O   . ALA B 21   ? 0.5025 0.3856 0.4573 0.0131  -0.0226 -0.0217 19   ALA B O   
9083  C CB  . ALA B 21   ? 0.4616 0.3468 0.4204 0.0238  -0.0195 -0.0252 19   ALA B CB  
9084  N N   . ASP B 22   ? 0.3603 0.2576 0.3245 0.0156  -0.0206 -0.0208 20   ASP B N   
9085  C CA  . ASP B 22   ? 0.3996 0.2974 0.3635 0.0127  -0.0219 -0.0187 20   ASP B CA  
9086  C C   . ASP B 22   ? 0.3224 0.2289 0.2899 0.0101  -0.0210 -0.0181 20   ASP B C   
9087  O O   . ASP B 22   ? 0.3565 0.2671 0.3266 0.0097  -0.0212 -0.0166 20   ASP B O   
9088  C CB  . ASP B 22   ? 0.4206 0.3173 0.3859 0.0155  -0.0229 -0.0172 20   ASP B CB  
9089  N N   . PHE B 23   ? 0.2817 0.1910 0.2494 0.0085  -0.0199 -0.0193 21   PHE B N   
9090  C CA  . PHE B 23   ? 0.2722 0.1899 0.2436 0.0069  -0.0187 -0.0190 21   PHE B CA  
9091  C C   . PHE B 23   ? 0.2737 0.1930 0.2446 0.0032  -0.0196 -0.0172 21   PHE B C   
9092  O O   . PHE B 23   ? 0.2734 0.1980 0.2474 0.0033  -0.0193 -0.0162 21   PHE B O   
9093  C CB  . PHE B 23   ? 0.2912 0.2110 0.2624 0.0058  -0.0176 -0.0206 21   PHE B CB  
9094  C CG  . PHE B 23   ? 0.2658 0.1937 0.2404 0.0040  -0.0166 -0.0202 21   PHE B CG  
9095  C CD1 . PHE B 23   ? 0.2676 0.2016 0.2468 0.0062  -0.0155 -0.0201 21   PHE B CD1 
9096  C CD2 . PHE B 23   ? 0.2822 0.2114 0.2554 0.0002  -0.0168 -0.0198 21   PHE B CD2 
9097  C CE1 . PHE B 23   ? 0.2566 0.1974 0.2386 0.0047  -0.0146 -0.0198 21   PHE B CE1 
9098  C CE2 . PHE B 23   ? 0.2906 0.2272 0.2669 -0.0011 -0.0158 -0.0194 21   PHE B CE2 
9099  C CZ  . PHE B 23   ? 0.2685 0.2105 0.2491 0.0012  -0.0147 -0.0194 21   PHE B CZ  
9100  N N   . ALA B 24   ? 0.2860 0.2008 0.2529 -0.0001 -0.0206 -0.0167 22   ALA B N   
9101  C CA  . ALA B 24   ? 0.2692 0.1860 0.2356 -0.0038 -0.0212 -0.0149 22   ALA B CA  
9102  C C   . ALA B 24   ? 0.2894 0.1988 0.2506 -0.0068 -0.0227 -0.0140 22   ALA B C   
9103  O O   . ALA B 24   ? 0.3083 0.2187 0.2681 -0.0107 -0.0229 -0.0136 22   ALA B O   
9104  C CB  . ALA B 24   ? 0.3159 0.2400 0.2846 -0.0060 -0.0199 -0.0151 22   ALA B CB  
9105  N N   . PRO B 25   ? 0.3000 0.2020 0.2583 -0.0053 -0.0240 -0.0136 23   PRO B N   
9106  C CA  . PRO B 25   ? 0.3452 0.2392 0.2983 -0.0083 -0.0257 -0.0128 23   PRO B CA  
9107  C C   . PRO B 25   ? 0.3477 0.2442 0.3002 -0.0124 -0.0262 -0.0105 23   PRO B C   
9108  O O   . PRO B 25   ? 0.3363 0.2372 0.2913 -0.0118 -0.0259 -0.0092 23   PRO B O   
9109  C CB  . PRO B 25   ? 0.3639 0.2506 0.3149 -0.0050 -0.0268 -0.0126 23   PRO B CB  
9110  C CG  . PRO B 25   ? 0.3628 0.2551 0.3184 -0.0015 -0.0261 -0.0123 23   PRO B CG  
9111  C CD  . PRO B 25   ? 0.3225 0.2232 0.2824 -0.0009 -0.0242 -0.0136 23   PRO B CD  
9112  N N   . PRO B 26   ? 0.3305 0.2246 0.2800 -0.0168 -0.0269 -0.0099 24   PRO B N   
9113  C CA  . PRO B 26   ? 0.3346 0.2315 0.2835 -0.0209 -0.0272 -0.0076 24   PRO B CA  
9114  C C   . PRO B 26   ? 0.3421 0.2333 0.2883 -0.0208 -0.0286 -0.0056 24   PRO B C   
9115  O O   . PRO B 26   ? 0.3559 0.2392 0.2993 -0.0186 -0.0298 -0.0059 24   PRO B O   
9116  C CB  . PRO B 26   ? 0.3798 0.2744 0.3258 -0.0254 -0.0278 -0.0076 24   PRO B CB  
9117  C CG  . PRO B 26   ? 0.3710 0.2573 0.3137 -0.0238 -0.0287 -0.0094 24   PRO B CG  
9118  C CD  . PRO B 26   ? 0.3428 0.2313 0.2887 -0.0184 -0.0275 -0.0113 24   PRO B CD  
9119  N N   . VAL B 27   ? 0.3352 0.2307 0.2820 -0.0231 -0.0285 -0.0035 25   VAL B N   
9120  C CA  . VAL B 27   ? 0.3311 0.2217 0.2750 -0.0235 -0.0299 -0.0012 25   VAL B CA  
9121  C C   . VAL B 27   ? 0.3424 0.2231 0.2808 -0.0260 -0.0317 -0.0004 25   VAL B C   
9122  O O   . VAL B 27   ? 0.3955 0.2687 0.3310 -0.0244 -0.0332 0.0004  25   VAL B O   
9123  C CB  . VAL B 27   ? 0.3363 0.2336 0.2814 -0.0261 -0.0292 0.0009  25   VAL B CB  
9124  C CG1 . VAL B 27   ? 0.3744 0.2659 0.3155 -0.0274 -0.0308 0.0035  25   VAL B CG1 
9125  C CG2 . VAL B 27   ? 0.3189 0.2241 0.2687 -0.0229 -0.0278 0.0001  25   VAL B CG2 
9126  N N   . ARG B 28   ? 0.3451 0.2255 0.2820 -0.0300 -0.0318 -0.0007 26   ARG B N   
9127  C CA  . ARG B 28   ? 0.3563 0.2272 0.2877 -0.0331 -0.0336 0.0001  26   ARG B CA  
9128  C C   . ARG B 28   ? 0.3936 0.2646 0.3246 -0.0354 -0.0334 -0.0017 26   ARG B C   
9129  O O   . ARG B 28   ? 0.3785 0.2580 0.3134 -0.0355 -0.0319 -0.0028 26   ARG B O   
9130  C CB  . ARG B 28   ? 0.4061 0.2769 0.3352 -0.0378 -0.0343 0.0032  26   ARG B CB  
9131  C CG  . ARG B 28   ? 0.4056 0.2857 0.3372 -0.0420 -0.0330 0.0040  26   ARG B CG  
9132  C CD  . ARG B 28   ? 0.4469 0.3276 0.3764 -0.0464 -0.0335 0.0073  26   ARG B CD  
9133  N NE  . ARG B 28   ? 0.4441 0.3286 0.3752 -0.0441 -0.0328 0.0086  26   ARG B NE  
9134  C CZ  . ARG B 28   ? 0.4993 0.3775 0.4274 -0.0429 -0.0341 0.0101  26   ARG B CZ  
9135  N NH1 . ARG B 28   ? 0.4897 0.3572 0.4130 -0.0437 -0.0362 0.0107  26   ARG B NH1 
9136  N NH2 . ARG B 28   ? 0.4805 0.3631 0.4103 -0.0408 -0.0335 0.0111  26   ARG B NH2 
9137  N N   . PRO B 29   ? 0.3918 0.2531 0.3179 -0.0370 -0.0351 -0.0021 27   PRO B N   
9138  C CA  . PRO B 29   ? 0.3978 0.2590 0.3228 -0.0400 -0.0352 -0.0036 27   PRO B CA  
9139  C C   . PRO B 29   ? 0.4032 0.2722 0.3299 -0.0453 -0.0348 -0.0018 27   PRO B C   
9140  O O   . PRO B 29   ? 0.3960 0.2652 0.3216 -0.0484 -0.0353 0.0009  27   PRO B O   
9141  C CB  . PRO B 29   ? 0.4469 0.2952 0.3654 -0.0415 -0.0375 -0.0037 27   PRO B CB  
9142  C CG  . PRO B 29   ? 0.4580 0.2999 0.3751 -0.0369 -0.0381 -0.0034 27   PRO B CG  
9143  C CD  . PRO B 29   ? 0.4236 0.2733 0.3446 -0.0360 -0.0370 -0.0014 27   PRO B CD  
9144  N N   . GLN B 30   ? 0.3724 0.2481 0.3019 -0.0463 -0.0337 -0.0032 28   GLN B N   
9145  C CA  . GLN B 30   ? 0.3995 0.2844 0.3317 -0.0505 -0.0330 -0.0017 28   GLN B CA  
9146  C C   . GLN B 30   ? 0.3713 0.2518 0.2996 -0.0565 -0.0347 -0.0006 28   GLN B C   
9147  O O   . GLN B 30   ? 0.3738 0.2498 0.2998 -0.0576 -0.0357 -0.0023 28   GLN B O   
9148  C CB  . GLN B 30   ? 0.3632 0.2573 0.3002 -0.0488 -0.0312 -0.0036 28   GLN B CB  
9149  C CG  . GLN B 30   ? 0.3375 0.2360 0.2785 -0.0431 -0.0295 -0.0048 28   GLN B CG  
9150  C CD  . GLN B 30   ? 0.3618 0.2665 0.3054 -0.0429 -0.0285 -0.0027 28   GLN B CD  
9151  O OE1 . GLN B 30   ? 0.3688 0.2823 0.3155 -0.0448 -0.0273 -0.0018 28   GLN B OE1 
9152  N NE2 . GLN B 30   ? 0.3488 0.2489 0.2911 -0.0405 -0.0290 -0.0019 28   GLN B NE2 
9153  N N   . SER B 31   ? 0.3760 0.2576 0.3034 -0.0606 -0.0351 0.0024  29   SER B N   
9154  C CA  . SER B 31   ? 0.3585 0.2366 0.2824 -0.0669 -0.0368 0.0040  29   SER B CA  
9155  C C   . SER B 31   ? 0.3446 0.2316 0.2717 -0.0700 -0.0362 0.0035  29   SER B C   
9156  O O   . SER B 31   ? 0.3482 0.2446 0.2803 -0.0675 -0.0343 0.0024  29   SER B O   
9157  C CB  . SER B 31   ? 0.3694 0.2486 0.2924 -0.0703 -0.0369 0.0075  29   SER B CB  
9158  O OG  . SER B 31   ? 0.3539 0.2456 0.2820 -0.0707 -0.0348 0.0087  29   SER B OG  
9159  N N   . THR B 32   ? 0.3667 0.2506 0.2909 -0.0758 -0.0379 0.0045  30   THR B N   
9160  C CA  . THR B 32   ? 0.3679 0.2605 0.2950 -0.0794 -0.0376 0.0045  30   THR B CA  
9161  C C   . THR B 32   ? 0.3478 0.2536 0.2806 -0.0797 -0.0353 0.0063  30   THR B C   
9162  O O   . THR B 32   ? 0.3453 0.2604 0.2827 -0.0784 -0.0339 0.0052  30   THR B O   
9163  C CB  . THR B 32   ? 0.3981 0.2852 0.3210 -0.0862 -0.0400 0.0059  30   THR B CB  
9164  O OG1 . THR B 32   ? 0.4509 0.3262 0.3686 -0.0855 -0.0419 0.0036  30   THR B OG1 
9165  C CG2 . THR B 32   ? 0.4577 0.3553 0.3842 -0.0906 -0.0397 0.0067  30   THR B CG2 
9166  N N   . LEU B 33   ? 0.3451 0.2517 0.2774 -0.0811 -0.0349 0.0090  31   LEU B N   
9167  C CA  . LEU B 33   ? 0.3585 0.2774 0.2958 -0.0812 -0.0327 0.0107  31   LEU B CA  
9168  C C   . LEU B 33   ? 0.3217 0.2460 0.2631 -0.0748 -0.0306 0.0088  31   LEU B C   
9169  O O   . LEU B 33   ? 0.3032 0.2383 0.2494 -0.0741 -0.0288 0.0087  31   LEU B O   
9170  C CB  . LEU B 33   ? 0.3272 0.2449 0.2624 -0.0840 -0.0328 0.0140  31   LEU B CB  
9171  C CG  . LEU B 33   ? 0.3957 0.3101 0.3277 -0.0910 -0.0346 0.0162  31   LEU B CG  
9172  C CD1 . LEU B 33   ? 0.3738 0.2851 0.3029 -0.0937 -0.0349 0.0195  31   LEU B CD1 
9173  C CD2 . LEU B 33   ? 0.3954 0.3212 0.3317 -0.0947 -0.0339 0.0169  31   LEU B CD2 
9174  N N   . ARG B 34   ? 0.2997 0.2168 0.2393 -0.0702 -0.0309 0.0074  32   ARG B N   
9175  C CA  . ARG B 34   ? 0.3046 0.2267 0.2480 -0.0644 -0.0290 0.0056  32   ARG B CA  
9176  C C   . ARG B 34   ? 0.2806 0.2068 0.2269 -0.0628 -0.0284 0.0031  32   ARG B C   
9177  O O   . ARG B 34   ? 0.2756 0.2106 0.2265 -0.0601 -0.0266 0.0023  32   ARG B O   
9178  C CB  . ARG B 34   ? 0.3072 0.2207 0.2482 -0.0601 -0.0296 0.0047  32   ARG B CB  
9179  C CG  . ARG B 34   ? 0.3226 0.2333 0.2615 -0.0606 -0.0299 0.0072  32   ARG B CG  
9180  C CD  . ARG B 34   ? 0.3274 0.2477 0.2702 -0.0589 -0.0278 0.0081  32   ARG B CD  
9181  N NE  . ARG B 34   ? 0.3319 0.2546 0.2777 -0.0532 -0.0266 0.0058  32   ARG B NE  
9182  C CZ  . ARG B 34   ? 0.3425 0.2614 0.2877 -0.0494 -0.0268 0.0056  32   ARG B CZ  
9183  N NH1 . ARG B 34   ? 0.3465 0.2587 0.2879 -0.0502 -0.0281 0.0074  32   ARG B NH1 
9184  N NH2 . ARG B 34   ? 0.3195 0.2414 0.2679 -0.0446 -0.0257 0.0035  32   ARG B NH2 
9185  N N   . ARG B 35   ? 0.3172 0.2372 0.2607 -0.0643 -0.0301 0.0017  33   ARG B N   
9186  C CA  . ARG B 35   ? 0.3016 0.2252 0.2473 -0.0629 -0.0297 -0.0006 33   ARG B CA  
9187  C C   . ARG B 35   ? 0.2862 0.2210 0.2359 -0.0659 -0.0288 0.0004  33   ARG B C   
9188  O O   . ARG B 35   ? 0.2909 0.2325 0.2443 -0.0635 -0.0275 -0.0010 33   ARG B O   
9189  C CB  . ARG B 35   ? 0.3352 0.2493 0.2762 -0.0643 -0.0318 -0.0022 33   ARG B CB  
9190  C CG  . ARG B 35   ? 0.3693 0.2734 0.3071 -0.0599 -0.0323 -0.0040 33   ARG B CG  
9191  C CD  . ARG B 35   ? 0.4458 0.3401 0.3787 -0.0610 -0.0342 -0.0058 33   ARG B CD  
9192  N NE  . ARG B 35   ? 0.5389 0.4236 0.4686 -0.0567 -0.0346 -0.0072 33   ARG B NE  
9193  C CZ  . ARG B 35   ? 0.5806 0.4657 0.5121 -0.0512 -0.0334 -0.0095 33   ARG B CZ  
9194  N NH1 . ARG B 35   ? 0.6375 0.5312 0.5732 -0.0495 -0.0319 -0.0107 33   ARG B NH1 
9195  N NH2 . ARG B 35   ? 0.5425 0.4193 0.4713 -0.0474 -0.0338 -0.0104 33   ARG B NH2 
9196  N N   . ALA B 36   ? 0.2916 0.2285 0.2406 -0.0711 -0.0294 0.0029  34   ALA B N   
9197  C CA  . ALA B 36   ? 0.3068 0.2550 0.2600 -0.0739 -0.0285 0.0041  34   ALA B CA  
9198  C C   . ALA B 36   ? 0.2789 0.2368 0.2369 -0.0705 -0.0259 0.0046  34   ALA B C   
9199  O O   . ALA B 36   ? 0.3108 0.2780 0.2730 -0.0700 -0.0247 0.0043  34   ALA B O   
9200  C CB  . ALA B 36   ? 0.3196 0.2681 0.2710 -0.0804 -0.0296 0.0070  34   ALA B CB  
9201  N N   . ILE B 37   ? 0.2878 0.2432 0.2450 -0.0681 -0.0251 0.0052  35   ILE B N   
9202  C CA  . ILE B 37   ? 0.2439 0.2070 0.2050 -0.0643 -0.0228 0.0052  35   ILE B CA  
9203  C C   . ILE B 37   ? 0.2909 0.2558 0.2547 -0.0595 -0.0220 0.0024  35   ILE B C   
9204  O O   . ILE B 37   ? 0.2568 0.2307 0.2248 -0.0582 -0.0205 0.0021  35   ILE B O   
9205  C CB  . ILE B 37   ? 0.2513 0.2100 0.2103 -0.0626 -0.0226 0.0062  35   ILE B CB  
9206  C CG1 . ILE B 37   ? 0.2541 0.2129 0.2110 -0.0675 -0.0230 0.0093  35   ILE B CG1 
9207  C CG2 . ILE B 37   ? 0.2571 0.2220 0.2196 -0.0580 -0.0205 0.0055  35   ILE B CG2 
9208  C CD1 . ILE B 37   ? 0.2844 0.2361 0.2376 -0.0666 -0.0235 0.0105  35   ILE B CD1 
9209  N N   . THR B 38   ? 0.2561 0.2126 0.2175 -0.0568 -0.0229 0.0005  36   THR B N   
9210  C CA  . THR B 38   ? 0.2654 0.2232 0.2291 -0.0521 -0.0221 -0.0019 36   THR B CA  
9211  C C   . THR B 38   ? 0.2720 0.2354 0.2380 -0.0533 -0.0220 -0.0029 36   THR B C   
9212  O O   . THR B 38   ? 0.2525 0.2220 0.2221 -0.0503 -0.0206 -0.0040 36   THR B O   
9213  C CB  . THR B 38   ? 0.2800 0.2276 0.2404 -0.0495 -0.0232 -0.0036 36   THR B CB  
9214  O OG1 . THR B 38   ? 0.2634 0.2060 0.2216 -0.0488 -0.0235 -0.0025 36   THR B OG1 
9215  C CG2 . THR B 38   ? 0.3241 0.2734 0.2870 -0.0445 -0.0221 -0.0060 36   THR B CG2 
9216  N N   . ALA B 39   ? 0.2667 0.2278 0.2303 -0.0577 -0.0236 -0.0023 37   ALA B N   
9217  C CA  . ALA B 39   ? 0.2988 0.2649 0.2642 -0.0591 -0.0239 -0.0031 37   ALA B CA  
9218  C C   . ALA B 39   ? 0.2839 0.2620 0.2544 -0.0594 -0.0222 -0.0020 37   ALA B C   
9219  O O   . ALA B 39   ? 0.2898 0.2735 0.2630 -0.0584 -0.0218 -0.0029 37   ALA B O   
9220  C CB  . ALA B 39   ? 0.3043 0.2657 0.2661 -0.0645 -0.0262 -0.0026 37   ALA B CB  
9221  N N   . ALA B 40   ? 0.2484 0.2307 0.2202 -0.0604 -0.0212 0.0001  38   ALA B N   
9222  C CA  . ALA B 40   ? 0.2732 0.2669 0.2495 -0.0606 -0.0196 0.0014  38   ALA B CA  
9223  C C   . ALA B 40   ? 0.2454 0.2435 0.2249 -0.0554 -0.0174 0.0004  38   ALA B C   
9224  O O   . ALA B 40   ? 0.2385 0.2459 0.2218 -0.0548 -0.0159 0.0011  38   ALA B O   
9225  C CB  . ALA B 40   ? 0.2536 0.2502 0.2295 -0.0647 -0.0194 0.0042  38   ALA B CB  
9226  N N   . TYR B 41   ? 0.2480 0.2397 0.2260 -0.0516 -0.0174 -0.0012 39   TYR B N   
9227  C CA  . TYR B 41   ? 0.2296 0.2241 0.2099 -0.0471 -0.0156 -0.0018 39   TYR B CA  
9228  C C   . TYR B 41   ? 0.2398 0.2434 0.2245 -0.0451 -0.0141 -0.0023 39   TYR B C   
9229  O O   . TYR B 41   ? 0.2313 0.2412 0.2184 -0.0438 -0.0124 -0.0015 39   TYR B O   
9230  C CB  . TYR B 41   ? 0.2259 0.2125 0.2044 -0.0435 -0.0160 -0.0037 39   TYR B CB  
9231  C CG  . TYR B 41   ? 0.2564 0.2426 0.2357 -0.0397 -0.0149 -0.0040 39   TYR B CG  
9232  C CD1 . TYR B 41   ? 0.2404 0.2339 0.2227 -0.0381 -0.0132 -0.0035 39   TYR B CD1 
9233  C CD2 . TYR B 41   ? 0.2597 0.2381 0.2367 -0.0375 -0.0156 -0.0050 39   TYR B CD2 
9234  C CE1 . TYR B 41   ? 0.2381 0.2307 0.2207 -0.0348 -0.0123 -0.0040 39   TYR B CE1 
9235  C CE2 . TYR B 41   ? 0.2559 0.2340 0.2337 -0.0342 -0.0148 -0.0052 39   TYR B CE2 
9236  C CZ  . TYR B 41   ? 0.2552 0.2402 0.2357 -0.0329 -0.0133 -0.0048 39   TYR B CZ  
9237  O OH  . TYR B 41   ? 0.2621 0.2464 0.2430 -0.0298 -0.0127 -0.0051 39   TYR B OH  
9238  N N   . ARG B 42   ? 0.2520 0.2562 0.2376 -0.0447 -0.0146 -0.0036 40   ARG B N   
9239  C CA  . ARG B 42   ? 0.2394 0.2516 0.2289 -0.0426 -0.0134 -0.0041 40   ARG B CA  
9240  C C   . ARG B 42   ? 0.2393 0.2562 0.2300 -0.0458 -0.0143 -0.0035 40   ARG B C   
9241  O O   . ARG B 42   ? 0.2753 0.2959 0.2681 -0.0442 -0.0141 -0.0045 40   ARG B O   
9242  C CB  . ARG B 42   ? 0.2547 0.2645 0.2450 -0.0381 -0.0129 -0.0062 40   ARG B CB  
9243  C CG  . ARG B 42   ? 0.2775 0.2845 0.2675 -0.0351 -0.0119 -0.0065 40   ARG B CG  
9244  C CD  . ARG B 42   ? 0.2471 0.2508 0.2374 -0.0310 -0.0116 -0.0084 40   ARG B CD  
9245  N NE  . ARG B 42   ? 0.2447 0.2440 0.2338 -0.0291 -0.0114 -0.0085 40   ARG B NE  
9246  C CZ  . ARG B 42   ? 0.2251 0.2276 0.2158 -0.0271 -0.0101 -0.0081 40   ARG B CZ  
9247  N NH1 . ARG B 42   ? 0.2372 0.2471 0.2308 -0.0263 -0.0088 -0.0078 40   ARG B NH1 
9248  N NH2 . ARG B 42   ? 0.2408 0.2389 0.2300 -0.0258 -0.0102 -0.0081 40   ARG B NH2 
9249  N N   . ARG B 43   ? 0.2354 0.2524 0.2247 -0.0505 -0.0153 -0.0019 41   ARG B N   
9250  C CA  . ARG B 43   ? 0.2424 0.2637 0.2325 -0.0541 -0.0165 -0.0012 41   ARG B CA  
9251  C C   . ARG B 43   ? 0.2630 0.2955 0.2581 -0.0528 -0.0151 -0.0005 41   ARG B C   
9252  O O   . ARG B 43   ? 0.2452 0.2830 0.2426 -0.0512 -0.0132 0.0004  41   ARG B O   
9253  C CB  . ARG B 43   ? 0.2499 0.2702 0.2381 -0.0595 -0.0176 0.0009  41   ARG B CB  
9254  C CG  . ARG B 43   ? 0.2339 0.2586 0.2229 -0.0641 -0.0191 0.0019  41   ARG B CG  
9255  C CD  . ARG B 43   ? 0.2866 0.3069 0.2723 -0.0695 -0.0207 0.0036  41   ARG B CD  
9256  N NE  . ARG B 43   ? 0.3026 0.3107 0.2831 -0.0698 -0.0224 0.0022  41   ARG B NE  
9257  C CZ  . ARG B 43   ? 0.3543 0.3551 0.3310 -0.0725 -0.0233 0.0032  41   ARG B CZ  
9258  N NH1 . ARG B 43   ? 0.3044 0.3089 0.2817 -0.0754 -0.0228 0.0057  41   ARG B NH1 
9259  N NH2 . ARG B 43   ? 0.3171 0.3067 0.2890 -0.0721 -0.0249 0.0016  41   ARG B NH2 
9260  N N   . PRO B 44   ? 0.2660 0.3022 0.2627 -0.0532 -0.0158 -0.0010 42   PRO B N   
9261  C CA  . PRO B 44   ? 0.2530 0.2999 0.2545 -0.0518 -0.0146 -0.0003 42   PRO B CA  
9262  C C   . PRO B 44   ? 0.2436 0.2982 0.2474 -0.0544 -0.0137 0.0022  42   PRO B C   
9263  O O   . PRO B 44   ? 0.2315 0.2850 0.2336 -0.0591 -0.0148 0.0036  42   PRO B O   
9264  C CB  . PRO B 44   ? 0.2772 0.3257 0.2790 -0.0534 -0.0163 -0.0008 42   PRO B CB  
9265  C CG  . PRO B 44   ? 0.3041 0.3419 0.3015 -0.0526 -0.0175 -0.0029 42   PRO B CG  
9266  C CD  . PRO B 44   ? 0.2933 0.3236 0.2873 -0.0541 -0.0178 -0.0026 42   PRO B CD  
9267  N N   . GLU B 45   ? 0.2264 0.2888 0.2339 -0.0513 -0.0116 0.0026  43   GLU B N   
9268  C CA  . GLU B 45   ? 0.2378 0.3081 0.2476 -0.0531 -0.0103 0.0049  43   GLU B CA  
9269  C C   . GLU B 45   ? 0.2614 0.3384 0.2731 -0.0579 -0.0116 0.0067  43   GLU B C   
9270  O O   . GLU B 45   ? 0.2699 0.3501 0.2817 -0.0616 -0.0115 0.0088  43   GLU B O   
9271  C CB  . GLU B 45   ? 0.2852 0.3623 0.2985 -0.0483 -0.0079 0.0047  43   GLU B CB  
9272  C CG  . GLU B 45   ? 0.3373 0.4175 0.3508 -0.0482 -0.0060 0.0060  43   GLU B CG  
9273  C CD  . GLU B 45   ? 0.2293 0.3119 0.2444 -0.0427 -0.0037 0.0050  43   GLU B CD  
9274  O OE1 . GLU B 45   ? 0.2442 0.3236 0.2594 -0.0390 -0.0037 0.0031  43   GLU B OE1 
9275  O OE2 . GLU B 45   ? 0.2447 0.3324 0.2607 -0.0424 -0.0019 0.0062  43   GLU B OE2 
9276  N N   . THR B 46   ? 0.2438 0.3229 0.2568 -0.0580 -0.0129 0.0060  44   THR B N   
9277  C CA  . THR B 46   ? 0.2486 0.3340 0.2634 -0.0628 -0.0144 0.0077  44   THR B CA  
9278  C C   . THR B 46   ? 0.2436 0.3219 0.2543 -0.0684 -0.0167 0.0082  44   THR B C   
9279  O O   . THR B 46   ? 0.2890 0.3723 0.3009 -0.0733 -0.0179 0.0101  44   THR B O   
9280  C CB  . THR B 46   ? 0.2579 0.3464 0.2746 -0.0614 -0.0156 0.0067  44   THR B CB  
9281  O OG1 . THR B 46   ? 0.2772 0.3555 0.2900 -0.0599 -0.0167 0.0043  44   THR B OG1 
9282  C CG2 . THR B 46   ? 0.2707 0.3676 0.2920 -0.0564 -0.0134 0.0067  44   THR B CG2 
9283  N N   . GLU B 47   ? 0.2722 0.3389 0.2781 -0.0678 -0.0175 0.0066  45   GLU B N   
9284  C CA  . GLU B 47   ? 0.2748 0.3337 0.2764 -0.0728 -0.0195 0.0072  45   GLU B CA  
9285  C C   . GLU B 47   ? 0.2536 0.3115 0.2541 -0.0746 -0.0185 0.0090  45   GLU B C   
9286  O O   . GLU B 47   ? 0.2925 0.3487 0.2910 -0.0800 -0.0199 0.0106  45   GLU B O   
9287  C CB  . GLU B 47   ? 0.2780 0.3248 0.2748 -0.0713 -0.0209 0.0046  45   GLU B CB  
9288  C CG  . GLU B 47   ? 0.3432 0.3899 0.3402 -0.0703 -0.0222 0.0029  45   GLU B CG  
9289  C CD  . GLU B 47   ? 0.4118 0.4469 0.4041 -0.0682 -0.0231 0.0003  45   GLU B CD  
9290  O OE1 . GLU B 47   ? 0.4471 0.4734 0.4353 -0.0694 -0.0236 0.0001  45   GLU B OE1 
9291  O OE2 . GLU B 47   ? 0.4644 0.4993 0.4570 -0.0653 -0.0232 -0.0014 45   GLU B OE2 
9292  N N   . CYS B 48   ? 0.2418 0.3008 0.2432 -0.0705 -0.0161 0.0088  46   CYS B N   
9293  C CA  . CYS B 48   ? 0.2600 0.3178 0.2600 -0.0719 -0.0151 0.0104  46   CYS B CA  
9294  C C   . CYS B 48   ? 0.2663 0.3349 0.2695 -0.0753 -0.0142 0.0132  46   CYS B C   
9295  O O   . CYS B 48   ? 0.2511 0.3185 0.2525 -0.0794 -0.0145 0.0153  46   CYS B O   
9296  C CB  . CYS B 48   ? 0.2437 0.3002 0.2438 -0.0664 -0.0129 0.0093  46   CYS B CB  
9297  S SG  . CYS B 48   ? 0.2678 0.3122 0.2641 -0.0624 -0.0137 0.0064  46   CYS B SG  
9298  N N   . LEU B 49   ? 0.2456 0.3249 0.2539 -0.0735 -0.0130 0.0135  47   LEU B N   
9299  C CA  . LEU B 49   ? 0.2447 0.3353 0.2566 -0.0754 -0.0114 0.0162  47   LEU B CA  
9300  C C   . LEU B 49   ? 0.2426 0.3369 0.2550 -0.0823 -0.0131 0.0186  47   LEU B C   
9301  O O   . LEU B 49   ? 0.2433 0.3416 0.2560 -0.0852 -0.0121 0.0210  47   LEU B O   
9302  C CB  . LEU B 49   ? 0.2325 0.3336 0.2497 -0.0708 -0.0093 0.0158  47   LEU B CB  
9303  C CG  . LEU B 49   ? 0.2301 0.3325 0.2477 -0.0658 -0.0065 0.0153  47   LEU B CG  
9304  C CD1 . LEU B 49   ? 0.2421 0.3482 0.2592 -0.0686 -0.0050 0.0178  47   LEU B CD1 
9305  C CD2 . LEU B 49   ? 0.2472 0.3381 0.2607 -0.0624 -0.0067 0.0129  47   LEU B CD2 
9306  N N   . PRO B 50   ? 0.2687 0.3621 0.2810 -0.0852 -0.0156 0.0183  48   PRO B N   
9307  C CA  . PRO B 50   ? 0.2830 0.3814 0.2964 -0.0920 -0.0172 0.0208  48   PRO B CA  
9308  C C   . PRO B 50   ? 0.2918 0.3836 0.3010 -0.0969 -0.0180 0.0225  48   PRO B C   
9309  O O   . PRO B 50   ? 0.3066 0.4058 0.3178 -0.1010 -0.0174 0.0254  48   PRO B O   
9310  C CB  . PRO B 50   ? 0.2728 0.3678 0.2852 -0.0937 -0.0202 0.0193  48   PRO B CB  
9311  C CG  . PRO B 50   ? 0.2776 0.3735 0.2918 -0.0872 -0.0191 0.0169  48   PRO B CG  
9312  C CD  . PRO B 50   ? 0.2748 0.3654 0.2872 -0.0823 -0.0168 0.0158  48   PRO B CD  
9313  N N   . PRO B 51   ? 0.2942 0.3726 0.2977 -0.0966 -0.0192 0.0210  49   PRO B N   
9314  C CA  . PRO B 51   ? 0.2952 0.3677 0.2948 -0.1011 -0.0198 0.0229  49   PRO B CA  
9315  C C   . PRO B 51   ? 0.2842 0.3617 0.2850 -0.0997 -0.0169 0.0247  49   PRO B C   
9316  O O   . PRO B 51   ? 0.2950 0.3735 0.2946 -0.1045 -0.0169 0.0274  49   PRO B O   
9317  C CB  . PRO B 51   ? 0.3245 0.3816 0.3180 -0.0999 -0.0215 0.0206  49   PRO B CB  
9318  C CG  . PRO B 51   ? 0.3382 0.3944 0.3329 -0.0934 -0.0206 0.0176  49   PRO B CG  
9319  C CD  . PRO B 51   ? 0.2912 0.3590 0.2913 -0.0930 -0.0203 0.0178  49   PRO B CD  
9320  N N   . LEU B 52   ? 0.2920 0.3724 0.2947 -0.0935 -0.0144 0.0233  50   LEU B N   
9321  C CA  . LEU B 52   ? 0.2368 0.3223 0.2404 -0.0919 -0.0116 0.0248  50   LEU B CA  
9322  C C   . LEU B 52   ? 0.2877 0.3876 0.2964 -0.0943 -0.0101 0.0275  50   LEU B C   
9323  O O   . LEU B 52   ? 0.2652 0.3687 0.2736 -0.0970 -0.0088 0.0300  50   LEU B O   
9324  C CB  . LEU B 52   ? 0.2406 0.3253 0.2447 -0.0846 -0.0095 0.0224  50   LEU B CB  
9325  C CG  . LEU B 52   ? 0.2553 0.3268 0.2549 -0.0817 -0.0107 0.0199  50   LEU B CG  
9326  C CD1 . LEU B 52   ? 0.2452 0.3179 0.2464 -0.0747 -0.0088 0.0176  50   LEU B CD1 
9327  C CD2 . LEU B 52   ? 0.2919 0.3551 0.2866 -0.0840 -0.0112 0.0211  50   LEU B CD2 
9328  N N   . VAL B 53   ? 0.2428 0.3513 0.2563 -0.0932 -0.0101 0.0270  51   VAL B N   
9329  C CA  . VAL B 53   ? 0.2362 0.3590 0.2550 -0.0956 -0.0089 0.0296  51   VAL B CA  
9330  C C   . VAL B 53   ? 0.3219 0.4450 0.3395 -0.1035 -0.0105 0.0326  51   VAL B C   
9331  O O   . VAL B 53   ? 0.2840 0.4152 0.3035 -0.1061 -0.0089 0.0355  51   VAL B O   
9332  C CB  . VAL B 53   ? 0.2562 0.3865 0.2799 -0.0936 -0.0094 0.0286  51   VAL B CB  
9333  C CG1 . VAL B 53   ? 0.3015 0.4461 0.3306 -0.0975 -0.0090 0.0316  51   VAL B CG1 
9334  C CG2 . VAL B 53   ? 0.2513 0.3839 0.2770 -0.0859 -0.0072 0.0264  51   VAL B CG2 
9335  N N   . GLU B 54   ? 0.2810 0.3950 0.2952 -0.1074 -0.0139 0.0320  52   GLU B N   
9336  C CA  . GLU B 54   ? 0.3163 0.4293 0.3288 -0.1153 -0.0158 0.0347  52   GLU B CA  
9337  C C   . GLU B 54   ? 0.3441 0.4526 0.3529 -0.1172 -0.0147 0.0366  52   GLU B C   
9338  O O   . GLU B 54   ? 0.3373 0.4524 0.3473 -0.1222 -0.0142 0.0399  52   GLU B O   
9339  C CB  . GLU B 54   ? 0.3310 0.4330 0.3395 -0.1185 -0.0196 0.0332  52   GLU B CB  
9340  N N   . ALA B 55   ? 0.3102 0.4077 0.3144 -0.1133 -0.0143 0.0347  53   ALA B N   
9341  C CA  . ALA B 55   ? 0.3167 0.4089 0.3168 -0.1149 -0.0135 0.0364  53   ALA B CA  
9342  C C   . ALA B 55   ? 0.3033 0.4067 0.3065 -0.1130 -0.0099 0.0383  53   ALA B C   
9343  O O   . ALA B 55   ? 0.3485 0.4524 0.3498 -0.1165 -0.0091 0.0410  53   ALA B O   
9344  C CB  . ALA B 55   ? 0.3422 0.4205 0.3370 -0.1108 -0.0141 0.0338  53   ALA B CB  
9345  N N   . ALA B 56   ? 0.3048 0.4170 0.3126 -0.1074 -0.0076 0.0369  54   ALA B N   
9346  C CA  . ALA B 56   ? 0.2859 0.4086 0.2966 -0.1048 -0.0040 0.0382  54   ALA B CA  
9347  C C   . ALA B 56   ? 0.3083 0.4458 0.3245 -0.1085 -0.0029 0.0412  54   ALA B C   
9348  O O   . ALA B 56   ? 0.3420 0.4892 0.3607 -0.1067 0.0003  0.0426  54   ALA B O   
9349  C CB  . ALA B 56   ? 0.3025 0.4272 0.3153 -0.0969 -0.0020 0.0352  54   ALA B CB  
9350  N N   . THR B 57   ? 0.2985 0.4381 0.3165 -0.1137 -0.0054 0.0422  55   THR B N   
9351  C CA  . THR B 57   ? 0.3434 0.4980 0.3673 -0.1170 -0.0045 0.0450  55   THR B CA  
9352  C C   . THR B 57   ? 0.3540 0.5127 0.3770 -0.1223 -0.0033 0.0488  55   THR B C   
9353  O O   . THR B 57   ? 0.3718 0.5206 0.3895 -0.1268 -0.0050 0.0499  55   THR B O   
9354  C CB  . THR B 57   ? 0.3468 0.5017 0.3724 -0.1215 -0.0079 0.0451  55   THR B CB  
9355  O OG1 . THR B 57   ? 0.3496 0.5038 0.3771 -0.1162 -0.0085 0.0419  55   THR B OG1 
9356  C CG2 . THR B 57   ? 0.3460 0.5161 0.3775 -0.1263 -0.0074 0.0485  55   THR B CG2 
9357  N N   . GLN B 58   ? 0.4097 0.5830 0.4377 -0.1215 -0.0002 0.0509  56   GLN B N   
9358  C CA  . GLN B 58   ? 0.3468 0.5265 0.3749 -0.1266 0.0013  0.0548  56   GLN B CA  
9359  C C   . GLN B 58   ? 0.3604 0.5569 0.3958 -0.1297 0.0021  0.0575  56   GLN B C   
9360  O O   . GLN B 58   ? 0.3661 0.5706 0.4067 -0.1263 0.0024  0.0562  56   GLN B O   
9361  C CB  . GLN B 58   ? 0.3957 0.5768 0.4219 -0.1221 0.0051  0.0549  56   GLN B CB  
9362  C CG  . GLN B 58   ? 0.3843 0.5508 0.4045 -0.1172 0.0047  0.0517  56   GLN B CG  
9363  C CD  . GLN B 58   ? 0.4323 0.5973 0.4486 -0.1159 0.0074  0.0528  56   GLN B CD  
9364  O OE1 . GLN B 58   ? 0.4656 0.6290 0.4791 -0.1215 0.0071  0.0559  56   GLN B OE1 
9365  N NE2 . GLN B 58   ? 0.4354 0.6005 0.4513 -0.1088 0.0098  0.0504  56   GLN B NE2 
9366  N N   . SER B 59   ? 0.4161 0.6178 0.4518 -0.1365 0.0024  0.0615  57   SER B N   
9367  C CA  . SER B 59   ? 0.4157 0.6336 0.4583 -0.1404 0.0029  0.0646  57   SER B CA  
9368  C C   . SER B 59   ? 0.3995 0.6323 0.4478 -0.1343 0.0072  0.0646  57   SER B C   
9369  O O   . SER B 59   ? 0.4036 0.6343 0.4498 -0.1281 0.0100  0.0629  57   SER B O   
9370  C CB  . SER B 59   ? 0.4605 0.6807 0.5016 -0.1486 0.0028  0.0690  57   SER B CB  
9371  O OG  . SER B 59   ? 0.4444 0.6658 0.4831 -0.1465 0.0064  0.0701  57   SER B OG  
9372  N N   . LYS B 60   ? 0.3902 0.6383 0.4458 -0.1360 0.0076  0.0666  58   LYS B N   
9373  C CA  . LYS B 60   ? 0.4265 0.6892 0.4877 -0.1302 0.0117  0.0669  58   LYS B CA  
9374  C C   . LYS B 60   ? 0.3777 0.6432 0.4365 -0.1298 0.0153  0.0688  58   LYS B C   
9375  O O   . LYS B 60   ? 0.4096 0.6807 0.4695 -0.1236 0.0191  0.0678  58   LYS B O   
9376  C CB  . LYS B 60   ? 0.3626 0.6369 0.4298 -0.1309 0.0107  0.0682  58   LYS B CB  
9377  N N   . GLU B 61   ? 0.3867 0.6479 0.4417 -0.1361 0.0141  0.0715  59   GLU B N   
9378  C CA  . GLU B 61   ? 0.3722 0.6360 0.4247 -0.1361 0.0173  0.0736  59   GLU B CA  
9379  C C   . GLU B 61   ? 0.4020 0.6582 0.4496 -0.1326 0.0196  0.0719  59   GLU B C   
9380  O O   . GLU B 61   ? 0.3998 0.6625 0.4479 -0.1274 0.0236  0.0716  59   GLU B O   
9381  C CB  . GLU B 61   ? 0.4304 0.6891 0.4792 -0.1440 0.0150  0.0767  59   GLU B CB  
9382  N N   . ILE B 62   ? 0.4170 0.6568 0.4588 -0.1335 0.0165  0.0699  60   ILE B N   
9383  C CA  . ILE B 62   ? 0.4004 0.6283 0.4359 -0.1280 0.0175  0.0671  60   ILE B CA  
9384  C C   . ILE B 62   ? 0.3835 0.6145 0.4215 -0.1188 0.0195  0.0634  60   ILE B C   
9385  O O   . ILE B 62   ? 0.4110 0.6409 0.4465 -0.1134 0.0224  0.0621  60   ILE B O   
9386  C CB  . ILE B 62   ? 0.4178 0.6273 0.4467 -0.1306 0.0135  0.0656  60   ILE B CB  
9387  N N   . ARG B 63   ? 0.3706 0.6054 0.4136 -0.1170 0.0180  0.0618  61   ARG B N   
9388  C CA  . ARG B 63   ? 0.3571 0.5943 0.4024 -0.1084 0.0197  0.0583  61   ARG B CA  
9389  C C   . ARG B 63   ? 0.4089 0.6608 0.4583 -0.1043 0.0243  0.0594  61   ARG B C   
9390  O O   . ARG B 63   ? 0.3922 0.6426 0.4400 -0.0973 0.0267  0.0570  61   ARG B O   
9391  C CB  . ARG B 63   ? 0.4020 0.6402 0.4515 -0.1077 0.0170  0.0567  61   ARG B CB  
9392  C CG  . ARG B 63   ? 0.4116 0.6334 0.4562 -0.1086 0.0131  0.0542  61   ARG B CG  
9393  C CD  . ARG B 63   ? 0.4446 0.6672 0.4929 -0.1070 0.0107  0.0522  61   ARG B CD  
9394  N NE  . ARG B 63   ? 0.4152 0.6452 0.4676 -0.1136 0.0085  0.0547  61   ARG B NE  
9395  C CZ  . ARG B 63   ? 0.4474 0.6912 0.5068 -0.1128 0.0090  0.0557  61   ARG B CZ  
9396  N NH1 . ARG B 63   ? 0.4797 0.7318 0.5430 -0.1057 0.0119  0.0544  61   ARG B NH1 
9397  N NH2 . ARG B 63   ? 0.4146 0.6639 0.4773 -0.1194 0.0065  0.0580  61   ARG B NH2 
9398  N N   . ASP B 64   ? 0.3434 0.6098 0.3982 -0.1085 0.0255  0.0630  62   ASP B N   
9399  C CA  . ASP B 64   ? 0.3731 0.6540 0.4316 -0.1048 0.0301  0.0643  62   ASP B CA  
9400  C C   . ASP B 64   ? 0.2972 0.5737 0.3497 -0.1037 0.0329  0.0646  62   ASP B C   
9401  O O   . ASP B 64   ? 0.3950 0.6750 0.4471 -0.0970 0.0363  0.0630  62   ASP B O   
9402  C CB  . ASP B 64   ? 0.3475 0.6414 0.4115 -0.1092 0.0301  0.0678  62   ASP B CB  
9403  C CG  . ASP B 64   ? 0.4805 0.7796 0.5504 -0.1088 0.0276  0.0671  62   ASP B CG  
9404  O OD1 . ASP B 64   ? 0.4503 0.7461 0.5214 -0.1054 0.0266  0.0644  62   ASP B OD1 
9405  O OD2 . ASP B 64   ? 0.4674 0.7740 0.5409 -0.1120 0.0265  0.0694  62   ASP B OD2 
9406  N N   . ALA B 65   ? 0.3181 0.5867 0.3656 -0.1101 0.0313  0.0668  63   ALA B N   
9407  C CA  . ALA B 65   ? 0.3266 0.5909 0.3680 -0.1096 0.0337  0.0674  63   ALA B CA  
9408  C C   . ALA B 65   ? 0.3891 0.6412 0.4252 -0.1024 0.0339  0.0631  63   ALA B C   
9409  O O   . ALA B 65   ? 0.3870 0.6406 0.4205 -0.0981 0.0372  0.0625  63   ALA B O   
9410  C CB  . ALA B 65   ? 0.3506 0.6070 0.3873 -0.1180 0.0314  0.0704  63   ALA B CB  
9411  N N   . ALA B 66   ? 0.3900 0.6303 0.4246 -0.1012 0.0305  0.0602  64   ALA B N   
9412  C CA  . ALA B 66   ? 0.3530 0.5818 0.3829 -0.0947 0.0304  0.0562  64   ALA B CA  
9413  C C   . ALA B 66   ? 0.3232 0.5599 0.3567 -0.0866 0.0333  0.0537  64   ALA B C   
9414  O O   . ALA B 66   ? 0.3635 0.5961 0.3932 -0.0812 0.0353  0.0516  64   ALA B O   
9415  C CB  . ALA B 66   ? 0.3491 0.5644 0.3770 -0.0955 0.0261  0.0539  64   ALA B CB  
9416  N N   . ALA B 67   ? 0.3388 0.5867 0.3794 -0.0857 0.0336  0.0540  65   ALA B N   
9417  C CA  . ALA B 67   ? 0.3489 0.6045 0.3930 -0.0780 0.0365  0.0519  65   ALA B CA  
9418  C C   . ALA B 67   ? 0.3805 0.6457 0.4242 -0.0757 0.0411  0.0532  65   ALA B C   
9419  O O   . ALA B 67   ? 0.3686 0.6340 0.4111 -0.0686 0.0436  0.0507  65   ALA B O   
9420  C CB  . ALA B 67   ? 0.3485 0.6150 0.4005 -0.0780 0.0357  0.0524  65   ALA B CB  
9421  N N   . SER B 68   ? 0.3704 0.6432 0.4148 -0.0816 0.0422  0.0572  66   SER B N   
9422  C CA  . SER B 68   ? 0.3325 0.6141 0.3759 -0.0799 0.0467  0.0587  66   SER B CA  
9423  C C   . SER B 68   ? 0.3919 0.6615 0.4268 -0.0781 0.0474  0.0572  66   SER B C   
9424  O O   . SER B 68   ? 0.3991 0.6715 0.4319 -0.0726 0.0508  0.0559  66   SER B O   
9425  C CB  . SER B 68   ? 0.4151 0.7078 0.4614 -0.0873 0.0476  0.0637  66   SER B CB  
9426  N N   . THR B 69   ? 0.3668 0.6230 0.3965 -0.0826 0.0441  0.0574  67   THR B N   
9427  C CA  . THR B 69   ? 0.3436 0.5879 0.3652 -0.0808 0.0443  0.0560  67   THR B CA  
9428  C C   . THR B 69   ? 0.3901 0.6273 0.4099 -0.0728 0.0444  0.0513  67   THR B C   
9429  O O   . THR B 69   ? 0.3461 0.5811 0.3615 -0.0685 0.0467  0.0498  67   THR B O   
9430  C CB  . THR B 69   ? 0.4169 0.6481 0.4339 -0.0870 0.0404  0.0571  67   THR B CB  
9431  O OG1 . THR B 69   ? 0.4096 0.6466 0.4271 -0.0945 0.0406  0.0616  67   THR B OG1 
9432  C CG2 . THR B 69   ? 0.3692 0.5873 0.3781 -0.0845 0.0401  0.0552  67   THR B CG2 
9433  N N   . ALA B 70   ? 0.3373 0.5706 0.3602 -0.0709 0.0418  0.0490  68   ALA B N   
9434  C CA  . ALA B 70   ? 0.3535 0.5803 0.3751 -0.0635 0.0418  0.0447  68   ALA B CA  
9435  C C   . ALA B 70   ? 0.3788 0.6162 0.4029 -0.0571 0.0459  0.0436  68   ALA B C   
9436  O O   . ALA B 70   ? 0.3406 0.5728 0.3609 -0.0513 0.0472  0.0407  68   ALA B O   
9437  C CB  . ALA B 70   ? 0.3352 0.5575 0.3602 -0.0631 0.0384  0.0428  68   ALA B CB  
9438  N N   . ARG B 71   ? 0.3722 0.6244 0.4026 -0.0579 0.0479  0.0458  69   ARG B N   
9439  C CA  . ARG B 71   ? 0.4099 0.6730 0.4427 -0.0517 0.0521  0.0450  69   ARG B CA  
9440  C C   . ARG B 71   ? 0.3040 0.5673 0.3311 -0.0505 0.0553  0.0454  69   ARG B C   
9441  O O   . ARG B 71   ? 0.3646 0.6271 0.3892 -0.0439 0.0577  0.0427  69   ARG B O   
9442  C CB  . ARG B 71   ? 0.4081 0.6877 0.4489 -0.0534 0.0535  0.0478  69   ARG B CB  
9443  C CG  . ARG B 71   ? 0.4082 0.7000 0.4518 -0.0470 0.0581  0.0472  69   ARG B CG  
9444  C CD  . ARG B 71   ? 0.4977 0.8063 0.5499 -0.0484 0.0593  0.0500  69   ARG B CD  
9445  N NE  . ARG B 71   ? 0.4762 0.7849 0.5337 -0.0475 0.0564  0.0489  69   ARG B NE  
9446  C CZ  . ARG B 71   ? 0.5101 0.8192 0.5699 -0.0404 0.0569  0.0459  69   ARG B CZ  
9447  N NH1 . ARG B 71   ? 0.5525 0.8607 0.6092 -0.0333 0.0599  0.0434  69   ARG B NH1 
9448  N NH2 . ARG B 71   ? 0.5706 0.8808 0.6354 -0.0404 0.0541  0.0455  69   ARG B NH2 
9449  N N   . LYS B 72   ? 0.3493 0.6131 0.3738 -0.0569 0.0553  0.0488  70   LYS B N   
9450  C CA  . LYS B 72   ? 0.3703 0.6342 0.3890 -0.0564 0.0583  0.0496  70   LYS B CA  
9451  C C   . LYS B 72   ? 0.3927 0.6418 0.4038 -0.0526 0.0573  0.0461  70   LYS B C   
9452  O O   . LYS B 72   ? 0.3957 0.6452 0.4026 -0.0483 0.0602  0.0448  70   LYS B O   
9453  C CB  . LYS B 72   ? 0.3434 0.6090 0.3607 -0.0648 0.0578  0.0540  70   LYS B CB  
9454  C CG  . LYS B 72   ? 0.4072 0.6726 0.4180 -0.0652 0.0606  0.0553  70   LYS B CG  
9455  C CD  . LYS B 72   ? 0.3745 0.6425 0.3845 -0.0738 0.0601  0.0601  70   LYS B CD  
9456  C CE  . LYS B 72   ? 0.4369 0.7034 0.4398 -0.0746 0.0625  0.0616  70   LYS B CE  
9457  N NZ  . LYS B 72   ? 0.3883 0.6682 0.3924 -0.0704 0.0678  0.0619  70   LYS B NZ  
9458  N N   . LEU B 73   ? 0.3742 0.6104 0.3836 -0.0540 0.0531  0.0445  71   LEU B N   
9459  C CA  . LEU B 73   ? 0.3654 0.5879 0.3682 -0.0506 0.0519  0.0414  71   LEU B CA  
9460  C C   . LEU B 73   ? 0.3420 0.5640 0.3455 -0.0425 0.0531  0.0373  71   LEU B C   
9461  O O   . LEU B 73   ? 0.3961 0.6127 0.3942 -0.0383 0.0544  0.0350  71   LEU B O   
9462  C CB  . LEU B 73   ? 0.3351 0.5446 0.3361 -0.0543 0.0472  0.0410  71   LEU B CB  
9463  C CG  . LEU B 73   ? 0.3269 0.5339 0.3258 -0.0622 0.0455  0.0447  71   LEU B CG  
9464  C CD1 . LEU B 73   ? 0.3220 0.5176 0.3207 -0.0655 0.0409  0.0441  71   LEU B CD1 
9465  C CD2 . LEU B 73   ? 0.3802 0.5826 0.3718 -0.0629 0.0468  0.0456  71   LEU B CD2 
9466  N N   . ILE B 74   ? 0.3394 0.5666 0.3494 -0.0403 0.0527  0.0364  72   ILE B N   
9467  C CA  . ILE B 74   ? 0.3793 0.6048 0.3900 -0.0329 0.0533  0.0325  72   ILE B CA  
9468  C C   . ILE B 74   ? 0.4107 0.6457 0.4212 -0.0277 0.0579  0.0320  72   ILE B C   
9469  O O   . ILE B 74   ? 0.3880 0.6178 0.3945 -0.0220 0.0590  0.0288  72   ILE B O   
9470  C CB  . ILE B 74   ? 0.3778 0.6059 0.3953 -0.0324 0.0513  0.0319  72   ILE B CB  
9471  C CG1 . ILE B 74   ? 0.3562 0.5720 0.3723 -0.0360 0.0468  0.0314  72   ILE B CG1 
9472  C CG2 . ILE B 74   ? 0.3779 0.6069 0.3970 -0.0246 0.0526  0.0286  72   ILE B CG2 
9473  C CD1 . ILE B 74   ? 0.3925 0.6122 0.4150 -0.0387 0.0445  0.0324  72   ILE B CD1 
9474  N N   . GLU B 75   ? 0.3991 0.6482 0.4140 -0.0295 0.0606  0.0350  73   GLU B N   
9475  C CA  . GLU B 75   ? 0.4231 0.6818 0.4375 -0.0248 0.0652  0.0348  73   GLU B CA  
9476  C C   . GLU B 75   ? 0.4543 0.7062 0.4601 -0.0240 0.0667  0.0339  73   GLU B C   
9477  O O   . GLU B 75   ? 0.4324 0.6833 0.4349 -0.0178 0.0691  0.0312  73   GLU B O   
9478  C CB  . GLU B 75   ? 0.4041 0.6790 0.4243 -0.0281 0.0677  0.0387  73   GLU B CB  
9479  C CG  . GLU B 75   ? 0.4329 0.7160 0.4619 -0.0282 0.0665  0.0394  73   GLU B CG  
9480  C CD  . GLU B 75   ? 0.4608 0.7609 0.4960 -0.0314 0.0689  0.0434  73   GLU B CD  
9481  O OE1 . GLU B 75   ? 0.5146 0.8190 0.5475 -0.0354 0.0708  0.0463  73   GLU B OE1 
9482  O OE2 . GLU B 75   ? 0.4602 0.7695 0.5028 -0.0299 0.0689  0.0439  73   GLU B OE2 
9483  N N   . ALA B 76   ? 0.3813 0.6277 0.3832 -0.0302 0.0650  0.0362  74   ALA B N   
9484  C CA  . ALA B 76   ? 0.4129 0.6516 0.4063 -0.0299 0.0658  0.0356  74   ALA B CA  
9485  C C   . ALA B 76   ? 0.4149 0.6406 0.4037 -0.0247 0.0641  0.0311  74   ALA B C   
9486  O O   . ALA B 76   ? 0.4469 0.6702 0.4302 -0.0203 0.0662  0.0290  74   ALA B O   
9487  C CB  . ALA B 76   ? 0.3974 0.6308 0.3877 -0.0376 0.0635  0.0388  74   ALA B CB  
9488  N N   . LEU B 77   ? 0.4118 0.6291 0.4026 -0.0251 0.0603  0.0296  75   LEU B N   
9489  C CA  . LEU B 77   ? 0.4198 0.6249 0.4067 -0.0206 0.0585  0.0255  75   LEU B CA  
9490  C C   . LEU B 77   ? 0.4257 0.6347 0.4137 -0.0130 0.0610  0.0224  75   LEU B C   
9491  O O   . LEU B 77   ? 0.4291 0.6316 0.4115 -0.0086 0.0617  0.0195  75   LEU B O   
9492  C CB  . LEU B 77   ? 0.3892 0.5857 0.3786 -0.0227 0.0541  0.0248  75   LEU B CB  
9493  C CG  . LEU B 77   ? 0.4333 0.6215 0.4200 -0.0291 0.0508  0.0268  75   LEU B CG  
9494  C CD1 . LEU B 77   ? 0.3721 0.5545 0.3626 -0.0310 0.0470  0.0262  75   LEU B CD1 
9495  C CD2 . LEU B 77   ? 0.4334 0.6107 0.4122 -0.0281 0.0500  0.0252  75   LEU B CD2 
9496  N N   . ARG B 78   ? 0.3675 0.5867 0.3625 -0.0113 0.0623  0.0229  76   ARG B N   
9497  C CA  . ARG B 78   ? 0.4094 0.6322 0.4060 -0.0039 0.0645  0.0201  76   ARG B CA  
9498  C C   . ARG B 78   ? 0.4470 0.6773 0.4405 -0.0003 0.0691  0.0200  76   ARG B C   
9499  O O   . ARG B 78   ? 0.4532 0.6842 0.4460 0.0063  0.0710  0.0171  76   ARG B O   
9500  C CB  . ARG B 78   ? 0.4659 0.6977 0.4711 -0.0032 0.0643  0.0209  76   ARG B CB  
9501  C CG  . ARG B 78   ? 0.4787 0.7026 0.4866 -0.0055 0.0600  0.0203  76   ARG B CG  
9502  C CD  . ARG B 78   ? 0.4758 0.7072 0.4912 -0.0031 0.0598  0.0202  76   ARG B CD  
9503  N NE  . ARG B 78   ? 0.4763 0.6974 0.4919 -0.0011 0.0566  0.0175  76   ARG B NE  
9504  C CZ  . ARG B 78   ? 0.4977 0.7219 0.5191 0.0006  0.0554  0.0172  76   ARG B CZ  
9505  N NH1 . ARG B 78   ? 0.5508 0.7882 0.5787 0.0003  0.0569  0.0194  76   ARG B NH1 
9506  N NH2 . ARG B 78   ? 0.4990 0.7131 0.5197 0.0025  0.0527  0.0147  76   ARG B NH2 
9507  N N   . GLY B 79   ? 0.4032 0.6389 0.3948 -0.0045 0.0708  0.0230  77   GLY B N   
9508  C CA  . GLY B 79   ? 0.4268 0.6705 0.4154 -0.0016 0.0754  0.0233  77   GLY B CA  
9509  C C   . GLY B 79   ? 0.4801 0.7147 0.4593 -0.0002 0.0759  0.0215  77   GLY B C   
9510  O O   . GLY B 79   ? 0.4398 0.6803 0.4156 0.0021  0.0798  0.0216  77   GLY B O   
9511  N N   . LYS B 80   ? 0.4753 0.6958 0.4501 -0.0014 0.0722  0.0197  78   LYS B N   
9512  C CA  . LYS B 80   ? 0.4619 0.6734 0.4276 -0.0007 0.0723  0.0182  78   LYS B CA  
9513  C C   . LYS B 80   ? 0.4380 0.6358 0.4004 0.0028  0.0693  0.0141  78   LYS B C   
9514  O O   . LYS B 80   ? 0.5000 0.6958 0.4672 0.0048  0.0674  0.0125  78   LYS B O   
9515  C CB  . LYS B 80   ? 0.4876 0.6961 0.4501 -0.0078 0.0707  0.0215  78   LYS B CB  
9516  C CG  . LYS B 80   ? 0.4588 0.6592 0.4238 -0.0126 0.0660  0.0224  78   LYS B CG  
9517  C CD  . LYS B 80   ? 0.4608 0.6604 0.4238 -0.0199 0.0648  0.0264  78   LYS B CD  
9518  C CE  . LYS B 80   ? 0.4061 0.5960 0.3705 -0.0241 0.0600  0.0268  78   LYS B CE  
9519  N NZ  . LYS B 80   ? 0.4584 0.6467 0.4207 -0.0312 0.0587  0.0307  78   LYS B NZ  
9520  N N   . GLY B 85   ? 0.5584 0.6672 0.4864 0.0222  0.0514  -0.0114 83   GLY B N   
9521  C CA  . GLY B 85   ? 0.5098 0.6100 0.4299 0.0245  0.0506  -0.0143 83   GLY B CA  
9522  C C   . GLY B 85   ? 0.5177 0.6116 0.4379 0.0290  0.0496  -0.0181 83   GLY B C   
9523  O O   . GLY B 85   ? 0.5254 0.6178 0.4408 0.0335  0.0514  -0.0208 83   GLY B O   
9524  N N   . VAL B 86   ? 0.5346 0.6243 0.4599 0.0280  0.0466  -0.0182 84   VAL B N   
9525  C CA  . VAL B 86   ? 0.5223 0.6060 0.4481 0.0319  0.0455  -0.0214 84   VAL B CA  
9526  C C   . VAL B 86   ? 0.4993 0.5899 0.4280 0.0368  0.0487  -0.0224 84   VAL B C   
9527  O O   . VAL B 86   ? 0.4977 0.5841 0.4235 0.0414  0.0493  -0.0256 84   VAL B O   
9528  C CB  . VAL B 86   ? 0.5427 0.6213 0.4735 0.0295  0.0418  -0.0210 84   VAL B CB  
9529  C CG1 . VAL B 86   ? 0.5480 0.6226 0.4810 0.0335  0.0411  -0.0237 84   VAL B CG1 
9530  C CG2 . VAL B 86   ? 0.5737 0.6436 0.5005 0.0262  0.0384  -0.0209 84   VAL B CG2 
9531  N N   . GLU B 87   ? 0.5104 0.6114 0.4446 0.0358  0.0509  -0.0198 85   GLU B N   
9532  C CA  . GLU B 87   ? 0.5565 0.6652 0.4939 0.0404  0.0541  -0.0204 85   GLU B CA  
9533  C C   . GLU B 87   ? 0.4963 0.6057 0.4271 0.0449  0.0572  -0.0227 85   GLU B C   
9534  O O   . GLU B 87   ? 0.4743 0.5826 0.4044 0.0503  0.0585  -0.0253 85   GLU B O   
9535  C CB  . GLU B 87   ? 0.5977 0.7184 0.5417 0.0379  0.0559  -0.0169 85   GLU B CB  
9536  N N   . GLY B 88   ? 0.4911 0.6018 0.4165 0.0429  0.0584  -0.0217 86   GLY B N   
9537  C CA  . GLY B 88   ? 0.5025 0.6138 0.4210 0.0470  0.0615  -0.0239 86   GLY B CA  
9538  C C   . GLY B 88   ? 0.4758 0.5752 0.3877 0.0502  0.0597  -0.0279 86   GLY B C   
9539  O O   . GLY B 88   ? 0.4795 0.5782 0.3874 0.0554  0.0620  -0.0307 86   GLY B O   
9540  N N   . LEU B 89   ? 0.4587 0.5486 0.3694 0.0470  0.0556  -0.0283 87   LEU B N   
9541  C CA  . LEU B 89   ? 0.4735 0.5520 0.3785 0.0494  0.0534  -0.0320 87   LEU B CA  
9542  C C   . LEU B 89   ? 0.4031 0.4794 0.3115 0.0539  0.0534  -0.0342 87   LEU B C   
9543  O O   . LEU B 89   ? 0.4091 0.4802 0.3124 0.0585  0.0541  -0.0376 87   LEU B O   
9544  C CB  . LEU B 89   ? 0.4512 0.5213 0.3554 0.0447  0.0490  -0.0314 87   LEU B CB  
9545  C CG  . LEU B 89   ? 0.4938 0.5519 0.3931 0.0462  0.0460  -0.0348 87   LEU B CG  
9546  C CD1 . LEU B 89   ? 0.5241 0.5786 0.4140 0.0486  0.0473  -0.0372 87   LEU B CD1 
9547  C CD2 . LEU B 89   ? 0.5517 0.6036 0.4522 0.0413  0.0417  -0.0335 87   LEU B CD2 
9548  N N   . VAL B 90   ? 0.4315 0.5114 0.3482 0.0527  0.0525  -0.0325 88   VAL B N   
9549  C CA  . VAL B 90   ? 0.4298 0.5084 0.3503 0.0568  0.0524  -0.0342 88   VAL B CA  
9550  C C   . VAL B 90   ? 0.4602 0.5452 0.3799 0.0626  0.0566  -0.0354 88   VAL B C   
9551  O O   . VAL B 90   ? 0.4364 0.5164 0.3539 0.0674  0.0569  -0.0384 88   VAL B O   
9552  C CB  . VAL B 90   ? 0.4300 0.5126 0.3596 0.0541  0.0508  -0.0316 88   VAL B CB  
9553  C CG1 . VAL B 90   ? 0.4381 0.5214 0.3720 0.0586  0.0514  -0.0329 88   VAL B CG1 
9554  C CG2 . VAL B 90   ? 0.3951 0.4697 0.3251 0.0494  0.0466  -0.0311 88   VAL B CG2 
9555  N N   . GLN B 91   ? 0.4430 0.5389 0.3641 0.0621  0.0599  -0.0332 89   GLN B N   
9556  C CA  . GLN B 91   ? 0.4805 0.5834 0.4011 0.0678  0.0641  -0.0342 89   GLN B CA  
9557  C C   . GLN B 91   ? 0.4451 0.5421 0.3560 0.0715  0.0656  -0.0376 89   GLN B C   
9558  O O   . GLN B 91   ? 0.5076 0.6033 0.4163 0.0774  0.0674  -0.0402 89   GLN B O   
9559  C CB  . GLN B 91   ? 0.5531 0.6700 0.4782 0.0660  0.0672  -0.0307 89   GLN B CB  
9560  N N   . GLU B 92   ? 0.4453 0.5382 0.3498 0.0682  0.0646  -0.0375 90   GLU B N   
9561  C CA  . GLU B 92   ? 0.4750 0.5626 0.3697 0.0714  0.0661  -0.0406 90   GLU B CA  
9562  C C   . GLU B 92   ? 0.4337 0.5091 0.3241 0.0749  0.0639  -0.0447 90   GLU B C   
9563  O O   . GLU B 92   ? 0.4527 0.5254 0.3374 0.0802  0.0660  -0.0478 90   GLU B O   
9564  C CB  . GLU B 92   ? 0.5056 0.5910 0.3945 0.0667  0.0650  -0.0395 90   GLU B CB  
9565  C CG  . GLU B 92   ? 0.5403 0.6192 0.4184 0.0697  0.0660  -0.0429 90   GLU B CG  
9566  C CD  . GLU B 92   ? 0.5437 0.6212 0.4157 0.0652  0.0653  -0.0415 90   GLU B CD  
9567  O OE1 . GLU B 92   ? 0.6206 0.7012 0.4968 0.0597  0.0637  -0.0381 90   GLU B OE1 
9568  O OE2 . GLU B 92   ? 0.5354 0.6084 0.3983 0.0673  0.0662  -0.0440 90   GLU B OE2 
9569  N N   . TYR B 93   ? 0.4425 0.5102 0.3355 0.0720  0.0596  -0.0447 91   TYR B N   
9570  C CA  . TYR B 93   ? 0.4485 0.5042 0.3376 0.0745  0.0572  -0.0483 91   TYR B CA  
9571  C C   . TYR B 93   ? 0.4285 0.4838 0.3241 0.0773  0.0566  -0.0487 91   TYR B C   
9572  O O   . TYR B 93   ? 0.4252 0.4705 0.3189 0.0786  0.0541  -0.0511 91   TYR B O   
9573  C CB  . TYR B 93   ? 0.3838 0.4298 0.2696 0.0697  0.0528  -0.0486 91   TYR B CB  
9574  C CG  . TYR B 93   ? 0.3756 0.4198 0.2529 0.0683  0.0532  -0.0492 91   TYR B CG  
9575  C CD1 . TYR B 93   ? 0.3972 0.4337 0.2654 0.0717  0.0535  -0.0529 91   TYR B CD1 
9576  C CD2 . TYR B 93   ? 0.4178 0.4678 0.2960 0.0637  0.0534  -0.0460 91   TYR B CD2 
9577  C CE1 . TYR B 93   ? 0.4433 0.4781 0.3033 0.0705  0.0539  -0.0535 91   TYR B CE1 
9578  C CE2 . TYR B 93   ? 0.4523 0.5007 0.3225 0.0624  0.0539  -0.0463 91   TYR B CE2 
9579  C CZ  . TYR B 93   ? 0.4699 0.5109 0.3311 0.0658  0.0541  -0.0501 91   TYR B CZ  
9580  O OH  . TYR B 93   ? 0.4821 0.5213 0.3348 0.0646  0.0545  -0.0506 91   TYR B OH  
9581  N N   . SER B 94   ? 0.3663 0.4324 0.2695 0.0781  0.0589  -0.0462 92   SER B N   
9582  C CA  . SER B 94   ? 0.3836 0.4507 0.2932 0.0809  0.0586  -0.0462 92   SER B CA  
9583  C C   . SER B 94   ? 0.3685 0.4267 0.2806 0.0778  0.0541  -0.0464 92   SER B C   
9584  O O   . SER B 94   ? 0.3722 0.4231 0.2837 0.0808  0.0527  -0.0486 92   SER B O   
9585  C CB  . SER B 94   ? 0.3938 0.4586 0.2998 0.0881  0.0609  -0.0494 92   SER B CB  
9586  O OG  . SER B 94   ? 0.4366 0.5101 0.3403 0.0911  0.0653  -0.0493 92   SER B OG  
9587  N N   . LEU B 95   ? 0.3162 0.3749 0.2308 0.0718  0.0517  -0.0440 93   LEU B N   
9588  C CA  . LEU B 95   ? 0.3224 0.3731 0.2391 0.0687  0.0476  -0.0439 93   LEU B CA  
9589  C C   . LEU B 95   ? 0.3484 0.4037 0.2740 0.0686  0.0471  -0.0420 93   LEU B C   
9590  O O   . LEU B 95   ? 0.3521 0.4179 0.2832 0.0678  0.0490  -0.0394 93   LEU B O   
9591  C CB  . LEU B 95   ? 0.3259 0.3754 0.2421 0.0625  0.0452  -0.0420 93   LEU B CB  
9592  C CG  . LEU B 95   ? 0.3358 0.3809 0.2433 0.0617  0.0453  -0.0434 93   LEU B CG  
9593  C CD1 . LEU B 95   ? 0.3387 0.3818 0.2462 0.0558  0.0424  -0.0414 93   LEU B CD1 
9594  C CD2 . LEU B 95   ? 0.3752 0.4097 0.2759 0.0651  0.0442  -0.0474 93   LEU B CD2 
9595  N N   . SER B 96   ? 0.3046 0.3522 0.2314 0.0692  0.0444  -0.0433 94   SER B N   
9596  C CA  . SER B 96   ? 0.3176 0.3681 0.2523 0.0676  0.0430  -0.0412 94   SER B CA  
9597  C C   . SER B 96   ? 0.3290 0.3804 0.2665 0.0613  0.0407  -0.0387 94   SER B C   
9598  O O   . SER B 96   ? 0.2968 0.3449 0.2298 0.0584  0.0398  -0.0389 94   SER B O   
9599  C CB  . SER B 96   ? 0.3436 0.3848 0.2783 0.0695  0.0407  -0.0432 94   SER B CB  
9600  O OG  . SER B 96   ? 0.2911 0.3227 0.2218 0.0664  0.0375  -0.0443 94   SER B OG  
9601  N N   . SER B 97   ? 0.2811 0.3367 0.2259 0.0592  0.0398  -0.0364 95   SER B N   
9602  C CA  . SER B 97   ? 0.2779 0.3337 0.2254 0.0535  0.0375  -0.0342 95   SER B CA  
9603  C C   . SER B 97   ? 0.2742 0.3192 0.2181 0.0513  0.0341  -0.0356 95   SER B C   
9604  O O   . SER B 97   ? 0.2763 0.3194 0.2178 0.0476  0.0328  -0.0349 95   SER B O   
9605  C CB  . SER B 97   ? 0.3346 0.3956 0.2900 0.0520  0.0368  -0.0319 95   SER B CB  
9606  O OG  . SER B 97   ? 0.4198 0.4918 0.3787 0.0527  0.0397  -0.0300 95   SER B OG  
9607  N N   . GLN B 98   ? 0.2712 0.3091 0.2148 0.0536  0.0326  -0.0376 96   GLN B N   
9608  C CA  . GLN B 98   ? 0.2614 0.2894 0.2020 0.0515  0.0294  -0.0389 96   GLN B CA  
9609  C C   . GLN B 98   ? 0.2456 0.2688 0.1783 0.0515  0.0294  -0.0407 96   GLN B C   
9610  O O   . GLN B 98   ? 0.2505 0.2686 0.1809 0.0482  0.0269  -0.0407 96   GLN B O   
9611  C CB  . GLN B 98   ? 0.2688 0.2903 0.2101 0.0541  0.0280  -0.0406 96   GLN B CB  
9612  C CG  . GLN B 98   ? 0.2649 0.2890 0.2135 0.0530  0.0270  -0.0388 96   GLN B CG  
9613  C CD  . GLN B 98   ? 0.3087 0.3314 0.2599 0.0480  0.0244  -0.0371 96   GLN B CD  
9614  O OE1 . GLN B 98   ? 0.3195 0.3480 0.2730 0.0450  0.0248  -0.0350 96   GLN B OE1 
9615  N NE2 . GLN B 98   ? 0.2796 0.2945 0.2303 0.0469  0.0217  -0.0380 96   GLN B NE2 
9616  N N   . GLU B 99   ? 0.2551 0.2801 0.1836 0.0554  0.0321  -0.0423 97   GLU B N   
9617  C CA  . GLU B 99   ? 0.2739 0.2949 0.1945 0.0555  0.0323  -0.0440 97   GLU B CA  
9618  C C   . GLU B 99   ? 0.2981 0.3240 0.2183 0.0515  0.0325  -0.0417 97   GLU B C   
9619  O O   . GLU B 99   ? 0.3067 0.3276 0.2222 0.0490  0.0307  -0.0421 97   GLU B O   
9620  C CB  . GLU B 99   ? 0.2964 0.3184 0.2125 0.0608  0.0354  -0.0462 97   GLU B CB  
9621  C CG  . GLU B 99   ? 0.3019 0.3158 0.2158 0.0647  0.0346  -0.0491 97   GLU B CG  
9622  C CD  . GLU B 99   ? 0.3138 0.3299 0.2246 0.0705  0.0381  -0.0510 97   GLU B CD  
9623  O OE1 . GLU B 99   ? 0.3314 0.3563 0.2424 0.0716  0.0412  -0.0499 97   GLU B OE1 
9624  O OE2 . GLU B 99   ? 0.3228 0.3318 0.2307 0.0741  0.0376  -0.0536 97   GLU B OE2 
9625  N N   . GLY B 100  ? 0.2805 0.3163 0.2056 0.0507  0.0347  -0.0391 98   GLY B N   
9626  C CA  . GLY B 100  ? 0.2739 0.3141 0.1989 0.0465  0.0348  -0.0366 98   GLY B CA  
9627  C C   . GLY B 100  ? 0.2862 0.3217 0.2130 0.0418  0.0311  -0.0353 98   GLY B C   
9628  O O   . GLY B 100  ? 0.2746 0.3079 0.1977 0.0389  0.0299  -0.0348 98   GLY B O   
9629  N N   . VAL B 101  ? 0.2558 0.2897 0.1882 0.0412  0.0293  -0.0349 99   VAL B N   
9630  C CA  . VAL B 101  ? 0.2617 0.2911 0.1961 0.0371  0.0259  -0.0338 99   VAL B CA  
9631  C C   . VAL B 101  ? 0.2692 0.2894 0.1979 0.0368  0.0234  -0.0359 99   VAL B C   
9632  O O   . VAL B 101  ? 0.2529 0.2705 0.1796 0.0335  0.0215  -0.0351 99   VAL B O   
9633  C CB  . VAL B 101  ? 0.2523 0.2819 0.1935 0.0370  0.0247  -0.0332 99   VAL B CB  
9634  C CG1 . VAL B 101  ? 0.2628 0.2869 0.2054 0.0334  0.0212  -0.0325 99   VAL B CG1 
9635  C CG2 . VAL B 101  ? 0.2796 0.3185 0.2264 0.0365  0.0267  -0.0307 99   VAL B CG2 
9636  N N   . ALA B 102  ? 0.2503 0.2652 0.1761 0.0402  0.0234  -0.0387 100  ALA B N   
9637  C CA  . ALA B 102  ? 0.2698 0.2756 0.1902 0.0399  0.0209  -0.0409 100  ALA B CA  
9638  C C   . ALA B 102  ? 0.2840 0.2892 0.1976 0.0390  0.0213  -0.0413 100  ALA B C   
9639  O O   . ALA B 102  ? 0.2873 0.2872 0.1978 0.0365  0.0186  -0.0415 100  ALA B O   
9640  C CB  . ALA B 102  ? 0.2626 0.2632 0.1805 0.0440  0.0212  -0.0439 100  ALA B CB  
9641  N N   . LEU B 103  ? 0.2558 0.2666 0.1669 0.0411  0.0246  -0.0412 101  LEU B N   
9642  C CA  . LEU B 103  ? 0.2772 0.2880 0.1815 0.0404  0.0253  -0.0415 101  LEU B CA  
9643  C C   . LEU B 103  ? 0.3067 0.3197 0.2123 0.0356  0.0238  -0.0386 101  LEU B C   
9644  O O   . LEU B 103  ? 0.3059 0.3148 0.2064 0.0337  0.0221  -0.0388 101  LEU B O   
9645  C CB  . LEU B 103  ? 0.3005 0.3181 0.2028 0.0436  0.0295  -0.0417 101  LEU B CB  
9646  C CG  . LEU B 103  ? 0.3230 0.3419 0.2183 0.0430  0.0308  -0.0417 101  LEU B CG  
9647  C CD1 . LEU B 103  ? 0.3318 0.3414 0.2190 0.0442  0.0291  -0.0448 101  LEU B CD1 
9648  C CD2 . LEU B 103  ? 0.3067 0.3339 0.2014 0.0461  0.0353  -0.0414 101  LEU B CD2 
9649  N N   . MET B 104  ? 0.2718 0.2911 0.1842 0.0337  0.0244  -0.0358 102  MET B N   
9650  C CA  . MET B 104  ? 0.3090 0.3298 0.2225 0.0293  0.0229  -0.0330 102  MET B CA  
9651  C C   . MET B 104  ? 0.3274 0.3410 0.2414 0.0268  0.0189  -0.0332 102  MET B C   
9652  O O   . MET B 104  ? 0.3065 0.3180 0.2179 0.0239  0.0171  -0.0321 102  MET B O   
9653  C CB  . MET B 104  ? 0.2862 0.3149 0.2066 0.0277  0.0244  -0.0301 102  MET B CB  
9654  C CG  . MET B 104  ? 0.2733 0.3104 0.1936 0.0297  0.0284  -0.0295 102  MET B CG  
9655  S SD  . MET B 104  ? 0.4424 0.4810 0.3543 0.0295  0.0303  -0.0294 102  MET B SD  
9656  C CE  . MET B 104  ? 0.4814 0.5215 0.3949 0.0237  0.0285  -0.0257 102  MET B CE  
9657  N N   . CYS B 105  ? 0.2704 0.2801 0.1877 0.0280  0.0174  -0.0346 103  CYS B N   
9658  C CA  . CYS B 105  ? 0.2820 0.2850 0.1997 0.0258  0.0137  -0.0349 103  CYS B CA  
9659  C C   . CYS B 105  ? 0.3017 0.2986 0.2120 0.0259  0.0121  -0.0367 103  CYS B C   
9660  O O   . CYS B 105  ? 0.3283 0.3221 0.2373 0.0231  0.0094  -0.0359 103  CYS B O   
9661  C CB  . CYS B 105  ? 0.2724 0.2723 0.1944 0.0273  0.0127  -0.0361 103  CYS B CB  
9662  S SG  . CYS B 105  ? 0.2899 0.2958 0.2208 0.0266  0.0135  -0.0338 103  CYS B SG  
9663  N N   . LEU B 106  ? 0.2893 0.2842 0.1945 0.0292  0.0136  -0.0394 104  LEU B N   
9664  C CA  . LEU B 106  ? 0.2744 0.2635 0.1719 0.0293  0.0123  -0.0413 104  LEU B CA  
9665  C C   . LEU B 106  ? 0.3251 0.3169 0.2186 0.0271  0.0126  -0.0396 104  LEU B C   
9666  O O   . LEU B 106  ? 0.3323 0.3197 0.2217 0.0251  0.0100  -0.0397 104  LEU B O   
9667  C CB  . LEU B 106  ? 0.3082 0.2953 0.2007 0.0336  0.0144  -0.0444 104  LEU B CB  
9668  C CG  . LEU B 106  ? 0.3389 0.3203 0.2221 0.0341  0.0135  -0.0467 104  LEU B CG  
9669  C CD1 . LEU B 106  ? 0.3813 0.3546 0.2633 0.0323  0.0093  -0.0480 104  LEU B CD1 
9670  C CD2 . LEU B 106  ? 0.3417 0.3224 0.2200 0.0387  0.0164  -0.0496 104  LEU B CD2 
9671  N N   . ALA B 107  ? 0.3070 0.3062 0.2016 0.0274  0.0158  -0.0379 105  ALA B N   
9672  C CA  . ALA B 107  ? 0.3139 0.3161 0.2047 0.0253  0.0164  -0.0360 105  ALA B CA  
9673  C C   . ALA B 107  ? 0.3446 0.3457 0.2383 0.0211  0.0134  -0.0334 105  ALA B C   
9674  O O   . ALA B 107  ? 0.3681 0.3666 0.2571 0.0191  0.0117  -0.0328 105  ALA B O   
9675  C CB  . ALA B 107  ? 0.3168 0.3277 0.2093 0.0262  0.0204  -0.0344 105  ALA B CB  
9676  N N   . GLU B 108  ? 0.3224 0.3253 0.2237 0.0199  0.0127  -0.0319 106  GLU B N   
9677  C CA  . GLU B 108  ? 0.3396 0.3410 0.2440 0.0163  0.0097  -0.0296 106  GLU B CA  
9678  C C   . GLU B 108  ? 0.3758 0.3698 0.2770 0.0155  0.0061  -0.0310 106  GLU B C   
9679  O O   . GLU B 108  ? 0.3847 0.3770 0.2839 0.0130  0.0040  -0.0295 106  GLU B O   
9680  C CB  . GLU B 108  ? 0.3631 0.3666 0.2758 0.0158  0.0095  -0.0285 106  GLU B CB  
9681  C CG  . GLU B 108  ? 0.3939 0.3947 0.3101 0.0128  0.0063  -0.0268 106  GLU B CG  
9682  C CD  . GLU B 108  ? 0.4570 0.4583 0.3805 0.0129  0.0058  -0.0266 106  GLU B CD  
9683  O OE1 . GLU B 108  ? 0.4260 0.4311 0.3525 0.0148  0.0081  -0.0270 106  GLU B OE1 
9684  O OE2 . GLU B 108  ? 0.4998 0.4979 0.4260 0.0112  0.0030  -0.0260 106  GLU B OE2 
9685  N N   . ALA B 109  ? 0.3510 0.3405 0.2518 0.0176  0.0052  -0.0337 107  ALA B N   
9686  C CA  . ALA B 109  ? 0.3838 0.3665 0.2816 0.0167  0.0016  -0.0351 107  ALA B CA  
9687  C C   . ALA B 109  ? 0.3837 0.3641 0.2732 0.0164  0.0012  -0.0358 107  ALA B C   
9688  O O   . ALA B 109  ? 0.3689 0.3461 0.2562 0.0142  -0.0018 -0.0351 107  ALA B O   
9689  C CB  . ALA B 109  ? 0.3948 0.3732 0.2938 0.0188  0.0009  -0.0378 107  ALA B CB  
9690  N N   . LEU B 110  ? 0.3345 0.3167 0.2189 0.0188  0.0042  -0.0372 108  LEU B N   
9691  C CA  . LEU B 110  ? 0.3528 0.3329 0.2286 0.0187  0.0040  -0.0380 108  LEU B CA  
9692  C C   . LEU B 110  ? 0.3942 0.3772 0.2690 0.0157  0.0035  -0.0349 108  LEU B C   
9693  O O   . LEU B 110  ? 0.4181 0.3980 0.2869 0.0144  0.0016  -0.0349 108  LEU B O   
9694  C CB  . LEU B 110  ? 0.3323 0.3143 0.2031 0.0221  0.0077  -0.0400 108  LEU B CB  
9695  C CG  . LEU B 110  ? 0.3564 0.3333 0.2257 0.0252  0.0075  -0.0436 108  LEU B CG  
9696  C CD1 . LEU B 110  ? 0.3704 0.3504 0.2366 0.0290  0.0117  -0.0453 108  LEU B CD1 
9697  C CD2 . LEU B 110  ? 0.3993 0.3683 0.2621 0.0244  0.0041  -0.0458 108  LEU B CD2 
9698  N N   . LEU B 111  ? 0.3666 0.3554 0.2469 0.0145  0.0051  -0.0321 109  LEU B N   
9699  C CA  . LEU B 111  ? 0.4249 0.4161 0.3044 0.0115  0.0047  -0.0289 109  LEU B CA  
9700  C C   . LEU B 111  ? 0.4612 0.4485 0.3430 0.0088  0.0005  -0.0275 109  LEU B C   
9701  O O   . LEU B 111  ? 0.4749 0.4625 0.3546 0.0064  -0.0006 -0.0251 109  LEU B O   
9702  C CB  . LEU B 111  ? 0.4387 0.4371 0.3231 0.0109  0.0076  -0.0264 109  LEU B CB  
9703  C CG  . LEU B 111  ? 0.3948 0.3982 0.2760 0.0132  0.0118  -0.0271 109  LEU B CG  
9704  C CD1 . LEU B 111  ? 0.4385 0.4492 0.3259 0.0126  0.0145  -0.0248 109  LEU B CD1 
9705  C CD2 . LEU B 111  ? 0.4751 0.4786 0.3482 0.0125  0.0124  -0.0266 109  LEU B CD2 
9706  N N   . ARG B 112  ? 0.4324 0.4162 0.3184 0.0091  -0.0017 -0.0287 110  ARG B N   
9707  C CA  . ARG B 112  ? 0.4809 0.4609 0.3686 0.0069  -0.0057 -0.0277 110  ARG B CA  
9708  C C   . ARG B 112  ? 0.4959 0.4712 0.3764 0.0064  -0.0082 -0.0288 110  ARG B C   
9709  O O   . ARG B 112  ? 0.5248 0.4976 0.4055 0.0044  -0.0115 -0.0275 110  ARG B O   
9710  C CB  . ARG B 112  ? 0.4472 0.4253 0.3417 0.0073  -0.0073 -0.0286 110  ARG B CB  
9711  C CG  . ARG B 112  ? 0.4792 0.4619 0.3809 0.0075  -0.0051 -0.0273 110  ARG B CG  
9712  C CD  . ARG B 112  ? 0.5907 0.5716 0.4991 0.0073  -0.0070 -0.0274 110  ARG B CD  
9713  N NE  . ARG B 112  ? 0.6019 0.5804 0.5110 0.0095  -0.0068 -0.0302 110  ARG B NE  
9714  C CZ  . ARG B 112  ? 0.5731 0.5542 0.4860 0.0113  -0.0045 -0.0309 110  ARG B CZ  
9715  N NH1 . ARG B 112  ? 0.5991 0.5854 0.5157 0.0111  -0.0022 -0.0291 110  ARG B NH1 
9716  N NH2 . ARG B 112  ? 0.6631 0.6412 0.5761 0.0132  -0.0046 -0.0334 110  ARG B NH2 
9717  N N   . ILE B 113  ? 0.4657 0.4397 0.3397 0.0083  -0.0068 -0.0313 111  ILE B N   
9718  C CA  . ILE B 113  ? 0.4785 0.4484 0.3445 0.0079  -0.0089 -0.0324 111  ILE B CA  
9719  C C   . ILE B 113  ? 0.5066 0.4796 0.3682 0.0065  -0.0077 -0.0299 111  ILE B C   
9720  O O   . ILE B 113  ? 0.5189 0.4957 0.3777 0.0077  -0.0040 -0.0299 111  ILE B O   
9721  C CB  . ILE B 113  ? 0.5110 0.4779 0.3712 0.0106  -0.0077 -0.0361 111  ILE B CB  
9722  C CG1 . ILE B 113  ? 0.4794 0.4427 0.3438 0.0117  -0.0090 -0.0384 111  ILE B CG1 
9723  C CG2 . ILE B 113  ? 0.5199 0.4827 0.3710 0.0100  -0.0097 -0.0372 111  ILE B CG2 
9724  C CD1 . ILE B 113  ? 0.4700 0.4304 0.3296 0.0148  -0.0074 -0.0420 111  ILE B CD1 
9725  N N   . PRO B 114  ? 0.5866 0.5583 0.4475 0.0039  -0.0106 -0.0276 112  PRO B N   
9726  C CA  . PRO B 114  ? 0.5295 0.5042 0.3869 0.0023  -0.0095 -0.0247 112  PRO B CA  
9727  C C   . PRO B 114  ? 0.5172 0.4912 0.3648 0.0030  -0.0083 -0.0259 112  PRO B C   
9728  O O   . PRO B 114  ? 0.5790 0.5570 0.4238 0.0027  -0.0055 -0.0242 112  PRO B O   
9729  C CB  . PRO B 114  ? 0.4711 0.4437 0.3306 -0.0003 -0.0134 -0.0221 112  PRO B CB  
9730  C CG  . PRO B 114  ? 0.5252 0.4930 0.3858 0.0001  -0.0169 -0.0243 112  PRO B CG  
9731  C CD  . PRO B 114  ? 0.5354 0.5032 0.3992 0.0024  -0.0150 -0.0272 112  PRO B CD  
9732  N N   . ASP B 115  ? 0.5489 0.5179 0.3912 0.0039  -0.0104 -0.0287 113  ASP B N   
9733  C CA  . ASP B 115  ? 0.6109 0.5786 0.4432 0.0046  -0.0097 -0.0299 113  ASP B CA  
9734  C C   . ASP B 115  ? 0.6116 0.5814 0.4413 0.0077  -0.0053 -0.0325 113  ASP B C   
9735  O O   . ASP B 115  ? 0.6022 0.5696 0.4334 0.0098  -0.0052 -0.0355 113  ASP B O   
9736  C CB  . ASP B 115  ? 0.5779 0.5391 0.4052 0.0041  -0.0139 -0.0320 113  ASP B CB  
9737  C CG  . ASP B 115  ? 0.6549 0.6142 0.4713 0.0047  -0.0134 -0.0335 113  ASP B CG  
9738  O OD1 . ASP B 115  ? 0.7496 0.7112 0.5617 0.0034  -0.0126 -0.0311 113  ASP B OD1 
9739  O OD2 . ASP B 115  ? 0.7014 0.6565 0.5131 0.0065  -0.0138 -0.0372 113  ASP B OD2 
9740  N N   . THR B 116  ? 0.6055 0.5798 0.4311 0.0080  -0.0019 -0.0313 114  THR B N   
9741  C CA  . THR B 116  ? 0.6519 0.6291 0.4751 0.0112  0.0025  -0.0335 114  THR B CA  
9742  C C   . THR B 116  ? 0.6612 0.6327 0.4771 0.0136  0.0019  -0.0378 114  THR B C   
9743  O O   . THR B 116  ? 0.6170 0.5882 0.4338 0.0167  0.0040  -0.0406 114  THR B O   
9744  C CB  . THR B 116  ? 0.6498 0.6328 0.4689 0.0107  0.0060  -0.0312 114  THR B CB  
9745  O OG1 . THR B 116  ? 0.7295 0.7178 0.5559 0.0085  0.0069  -0.0274 114  THR B OG1 
9746  C CG2 . THR B 116  ? 0.6680 0.6543 0.4840 0.0143  0.0107  -0.0336 114  THR B CG2 
9747  N N   . ALA B 117  ? 0.6665 0.6331 0.4751 0.0123  -0.0012 -0.0384 115  ALA B N   
9748  C CA  . ALA B 117  ? 0.6490 0.6097 0.4500 0.0144  -0.0021 -0.0425 115  ALA B CA  
9749  C C   . ALA B 117  ? 0.6004 0.5561 0.4061 0.0151  -0.0045 -0.0450 115  ALA B C   
9750  O O   . ALA B 117  ? 0.6448 0.5976 0.4480 0.0181  -0.0032 -0.0485 115  ALA B O   
9751  C CB  . ALA B 117  ? 0.6565 0.6131 0.4489 0.0124  -0.0053 -0.0423 115  ALA B CB  
9752  N N   . THR B 118  ? 0.6343 0.5891 0.4469 0.0126  -0.0080 -0.0431 116  THR B N   
9753  C CA  . THR B 118  ? 0.5926 0.5432 0.4103 0.0130  -0.0103 -0.0451 116  THR B CA  
9754  C C   . THR B 118  ? 0.6090 0.5627 0.4327 0.0157  -0.0068 -0.0460 116  THR B C   
9755  O O   . THR B 118  ? 0.5912 0.5409 0.4153 0.0176  -0.0070 -0.0489 116  THR B O   
9756  C CB  . THR B 118  ? 0.6063 0.5565 0.4307 0.0099  -0.0143 -0.0425 116  THR B CB  
9757  O OG1 . THR B 118  ? 0.6760 0.6234 0.4947 0.0076  -0.0178 -0.0417 116  THR B OG1 
9758  C CG2 . THR B 118  ? 0.5912 0.5376 0.4210 0.0102  -0.0166 -0.0444 116  THR B CG2 
9759  N N   . ARG B 119  ? 0.5834 0.5440 0.4117 0.0158  -0.0035 -0.0434 117  ARG B N   
9760  C CA  . ARG B 119  ? 0.5504 0.5147 0.3849 0.0182  -0.0003 -0.0438 117  ARG B CA  
9761  C C   . ARG B 119  ? 0.5608 0.5247 0.3894 0.0220  0.0032  -0.0470 117  ARG B C   
9762  O O   . ARG B 119  ? 0.5307 0.4922 0.3612 0.0245  0.0038  -0.0495 117  ARG B O   
9763  C CB  . ARG B 119  ? 0.4828 0.4546 0.3232 0.0169  0.0021  -0.0401 117  ARG B CB  
9764  C CG  . ARG B 119  ? 0.4860 0.4622 0.3337 0.0189  0.0051  -0.0401 117  ARG B CG  
9765  C CD  . ARG B 119  ? 0.4781 0.4622 0.3299 0.0178  0.0079  -0.0367 117  ARG B CD  
9766  N NE  . ARG B 119  ? 0.5012 0.4857 0.3561 0.0140  0.0053  -0.0334 117  ARG B NE  
9767  C CZ  . ARG B 119  ? 0.5595 0.5474 0.4122 0.0119  0.0060  -0.0305 117  ARG B CZ  
9768  N NH1 . ARG B 119  ? 0.5162 0.5079 0.3636 0.0129  0.0093  -0.0304 117  ARG B NH1 
9769  N NH2 . ARG B 119  ? 0.5629 0.5504 0.4187 0.0087  0.0034  -0.0276 117  ARG B NH2 
9770  N N   . ASP B 120  ? 0.5565 0.5226 0.3778 0.0226  0.0055  -0.0468 118  ASP B N   
9771  C CA  . ASP B 120  ? 0.5950 0.5611 0.4102 0.0265  0.0090  -0.0498 118  ASP B CA  
9772  C C   . ASP B 120  ? 0.6194 0.5767 0.4287 0.0282  0.0067  -0.0540 118  ASP B C   
9773  O O   . ASP B 120  ? 0.5796 0.5353 0.3869 0.0319  0.0090  -0.0570 118  ASP B O   
9774  C CB  . ASP B 120  ? 0.5838 0.5539 0.3919 0.0265  0.0116  -0.0488 118  ASP B CB  
9775  C CG  . ASP B 120  ? 0.6744 0.6534 0.4881 0.0251  0.0143  -0.0447 118  ASP B CG  
9776  O OD1 . ASP B 120  ? 0.6952 0.6775 0.5181 0.0248  0.0148  -0.0432 118  ASP B OD1 
9777  O OD2 . ASP B 120  ? 0.7387 0.7213 0.5475 0.0241  0.0160  -0.0430 118  ASP B OD2 
9778  N N   . ALA B 121  ? 0.6006 0.5520 0.4072 0.0254  0.0021  -0.0543 119  ALA B N   
9779  C CA  . ALA B 121  ? 0.6421 0.5849 0.4435 0.0264  -0.0006 -0.0582 119  ALA B CA  
9780  C C   . ALA B 121  ? 0.6008 0.5410 0.4093 0.0275  -0.0014 -0.0594 119  ALA B C   
9781  O O   . ALA B 121  ? 0.6223 0.5575 0.4274 0.0303  -0.0008 -0.0629 119  ALA B O   
9782  C CB  . ALA B 121  ? 0.6407 0.5785 0.4380 0.0229  -0.0055 -0.0578 119  ALA B CB  
9783  N N   . LEU B 122  ? 0.5832 0.5265 0.4014 0.0253  -0.0026 -0.0566 120  LEU B N   
9784  C CA  . LEU B 122  ? 0.5539 0.4952 0.3790 0.0262  -0.0033 -0.0575 120  LEU B CA  
9785  C C   . LEU B 122  ? 0.5470 0.4914 0.3737 0.0303  0.0012  -0.0587 120  LEU B C   
9786  O O   . LEU B 122  ? 0.5549 0.4951 0.3826 0.0324  0.0012  -0.0612 120  LEU B O   
9787  C CB  . LEU B 122  ? 0.5528 0.4977 0.3878 0.0232  -0.0051 -0.0541 120  LEU B CB  
9788  C CG  . LEU B 122  ? 0.5707 0.5137 0.4131 0.0236  -0.0061 -0.0547 120  LEU B CG  
9789  C CD1 . LEU B 122  ? 0.6133 0.5480 0.4529 0.0224  -0.0103 -0.0570 120  LEU B CD1 
9790  C CD2 . LEU B 122  ? 0.5237 0.4718 0.3759 0.0215  -0.0065 -0.0512 120  LEU B CD2 
9791  N N   . ILE B 123  ? 0.5013 0.4532 0.3285 0.0313  0.0051  -0.0570 121  ILE B N   
9792  C CA  . ILE B 123  ? 0.5499 0.5060 0.3791 0.0353  0.0095  -0.0578 121  ILE B CA  
9793  C C   . ILE B 123  ? 0.5971 0.5478 0.4177 0.0392  0.0109  -0.0620 121  ILE B C   
9794  O O   . ILE B 123  ? 0.5721 0.5201 0.3940 0.0422  0.0119  -0.0642 121  ILE B O   
9795  C CB  . ILE B 123  ? 0.5089 0.4745 0.3401 0.0351  0.0132  -0.0548 121  ILE B CB  
9796  C CG1 . ILE B 123  ? 0.4235 0.3939 0.2642 0.0318  0.0121  -0.0509 121  ILE B CG1 
9797  C CG2 . ILE B 123  ? 0.5186 0.4888 0.3501 0.0396  0.0180  -0.0560 121  ILE B CG2 
9798  C CD1 . ILE B 123  ? 0.4031 0.3818 0.2450 0.0306  0.0148  -0.0477 121  ILE B CD1 
9799  N N   . ARG B 124  ? 0.5557 0.5046 0.3669 0.0392  0.0111  -0.0631 122  ARG B N   
9800  C CA  . ARG B 124  ? 0.6318 0.5758 0.4339 0.0431  0.0128  -0.0671 122  ARG B CA  
9801  C C   . ARG B 124  ? 0.6661 0.5996 0.4651 0.0434  0.0092  -0.0705 122  ARG B C   
9802  O O   . ARG B 124  ? 0.7206 0.6499 0.5158 0.0473  0.0108  -0.0738 122  ARG B O   
9803  C CB  . ARG B 124  ? 0.6427 0.5873 0.4352 0.0427  0.0136  -0.0673 122  ARG B CB  
9804  N N   . ASP B 125  ? 0.6376 0.5669 0.4385 0.0393  0.0045  -0.0697 123  ASP B N   
9805  C CA  . ASP B 125  ? 0.6922 0.6114 0.4889 0.0389  0.0007  -0.0728 123  ASP B CA  
9806  C C   . ASP B 125  ? 0.6960 0.6128 0.5010 0.0382  -0.0013 -0.0726 123  ASP B C   
9807  O O   . ASP B 125  ? 0.7539 0.6624 0.5557 0.0391  -0.0032 -0.0756 123  ASP B O   
9808  C CB  . ASP B 125  ? 0.7767 0.6922 0.5685 0.0348  -0.0036 -0.0724 123  ASP B CB  
9809  C CG  . ASP B 125  ? 0.8213 0.7386 0.6040 0.0353  -0.0020 -0.0726 123  ASP B CG  
9810  O OD1 . ASP B 125  ? 0.8467 0.7640 0.6235 0.0392  0.0017  -0.0750 123  ASP B OD1 
9811  O OD2 . ASP B 125  ? 0.8882 0.8071 0.6697 0.0318  -0.0043 -0.0704 123  ASP B OD2 
9812  N N   . LYS B 126  ? 0.6376 0.5608 0.4527 0.0367  -0.0009 -0.0692 124  LYS B N   
9813  C CA  . LYS B 126  ? 0.6291 0.5501 0.4519 0.0358  -0.0029 -0.0688 124  LYS B CA  
9814  C C   . LYS B 126  ? 0.6595 0.5866 0.4904 0.0382  0.0005  -0.0674 124  LYS B C   
9815  O O   . LYS B 126  ? 0.6905 0.6142 0.5247 0.0396  0.0002  -0.0686 124  LYS B O   
9816  C CB  . LYS B 126  ? 0.6671 0.5886 0.4950 0.0309  -0.0070 -0.0661 124  LYS B CB  
9817  N N   . ILE B 127  ? 0.6091 0.5449 0.4432 0.0385  0.0037  -0.0648 125  ILE B N   
9818  C CA  . ILE B 127  ? 0.5686 0.5109 0.4108 0.0404  0.0067  -0.0632 125  ILE B CA  
9819  C C   . ILE B 127  ? 0.6008 0.5438 0.4397 0.0455  0.0107  -0.0655 125  ILE B C   
9820  O O   . ILE B 127  ? 0.6061 0.5488 0.4492 0.0480  0.0118  -0.0662 125  ILE B O   
9821  C CB  . ILE B 127  ? 0.5022 0.4537 0.3500 0.0381  0.0080  -0.0592 125  ILE B CB  
9822  C CG1 . ILE B 127  ? 0.5608 0.5112 0.4110 0.0333  0.0040  -0.0571 125  ILE B CG1 
9823  C CG2 . ILE B 127  ? 0.4918 0.4493 0.3487 0.0393  0.0102  -0.0574 125  ILE B CG2 
9824  C CD1 . ILE B 127  ? 0.5844 0.5310 0.4407 0.0316  0.0008  -0.0569 125  ILE B CD1 
9825  N N   . ALA B 128  ? 0.5338 0.4780 0.3650 0.0473  0.0130  -0.0667 126  ALA B N   
9826  C CA  . ALA B 128  ? 0.5499 0.4957 0.3779 0.0526  0.0172  -0.0688 126  ALA B CA  
9827  C C   . ALA B 128  ? 0.6187 0.5552 0.4428 0.0557  0.0163  -0.0726 126  ALA B C   
9828  O O   . ALA B 128  ? 0.6380 0.5755 0.4626 0.0602  0.0193  -0.0740 126  ALA B O   
9829  C CB  . ALA B 128  ? 0.5569 0.5054 0.3767 0.0537  0.0197  -0.0694 126  ALA B CB  
9830  N N   . ASP B 129  ? 0.6741 0.6016 0.4943 0.0533  0.0121  -0.0743 127  ASP B N   
9831  C CA  . ASP B 129  ? 0.7622 0.6799 0.5787 0.0555  0.0106  -0.0778 127  ASP B CA  
9832  C C   . ASP B 129  ? 0.8117 0.7287 0.6371 0.0552  0.0095  -0.0767 127  ASP B C   
9833  O O   . ASP B 129  ? 0.9089 0.8173 0.7323 0.0561  0.0075  -0.0791 127  ASP B O   
9834  C CB  . ASP B 129  ? 0.7965 0.7048 0.6055 0.0527  0.0063  -0.0799 127  ASP B CB  
9835  N N   . GLY B 130  ? 0.7857 0.7113 0.6205 0.0540  0.0106  -0.0732 128  GLY B N   
9836  C CA  . GLY B 130  ? 0.7959 0.7218 0.6391 0.0538  0.0099  -0.0719 128  GLY B CA  
9837  C C   . GLY B 130  ? 0.7997 0.7234 0.6479 0.0488  0.0056  -0.0702 128  GLY B C   
9838  O O   . GLY B 130  ? 0.7653 0.6934 0.6221 0.0475  0.0055  -0.0676 128  GLY B O   
9839  N N   . ASN B 131  ? 0.8796 0.7968 0.7224 0.0460  0.0021  -0.0714 129  ASN B N   
9840  C CA  . ASN B 131  ? 0.8586 0.7734 0.7058 0.0414  -0.0021 -0.0699 129  ASN B CA  
9841  C C   . ASN B 131  ? 0.8463 0.7695 0.7001 0.0382  -0.0022 -0.0661 129  ASN B C   
9842  O O   . ASN B 131  ? 0.9173 0.8403 0.7693 0.0349  -0.0046 -0.0651 129  ASN B O   
9843  C CB  . ASN B 131  ? 0.8886 0.7951 0.7281 0.0392  -0.0058 -0.0721 129  ASN B CB  
9844  N N   . TRP B 132  ? 0.7236 0.6540 0.5850 0.0392  0.0003  -0.0638 130  TRP B N   
9845  C CA  . TRP B 132  ? 0.6478 0.5858 0.5153 0.0363  0.0004  -0.0602 130  TRP B CA  
9846  C C   . TRP B 132  ? 0.6695 0.6071 0.5446 0.0331  -0.0026 -0.0583 130  TRP B C   
9847  O O   . TRP B 132  ? 0.7232 0.6645 0.6017 0.0300  -0.0039 -0.0558 130  TRP B O   
9848  C CB  . TRP B 132  ? 0.5962 0.5428 0.4677 0.0387  0.0046  -0.0586 130  TRP B CB  
9849  C CG  . TRP B 132  ? 0.5199 0.4678 0.3977 0.0410  0.0060  -0.0584 130  TRP B CG  
9850  C CD1 . TRP B 132  ? 0.4996 0.4463 0.3756 0.0453  0.0085  -0.0605 130  TRP B CD1 
9851  C CD2 . TRP B 132  ? 0.4644 0.4151 0.3510 0.0391  0.0050  -0.0561 130  TRP B CD2 
9852  N NE1 . TRP B 132  ? 0.4742 0.4227 0.3573 0.0462  0.0090  -0.0594 130  TRP B NE1 
9853  C CE2 . TRP B 132  ? 0.4028 0.3538 0.2924 0.0423  0.0069  -0.0568 130  TRP B CE2 
9854  C CE3 . TRP B 132  ? 0.4350 0.3879 0.3270 0.0351  0.0027  -0.0535 130  TRP B CE3 
9855  C CZ2 . TRP B 132  ? 0.3818 0.3352 0.2794 0.0416  0.0065  -0.0549 130  TRP B CZ2 
9856  C CZ3 . TRP B 132  ? 0.3959 0.3511 0.2958 0.0345  0.0025  -0.0518 130  TRP B CZ3 
9857  C CH2 . TRP B 132  ? 0.3973 0.3528 0.2998 0.0376  0.0043  -0.0525 130  TRP B CH2 
9858  N N   . LYS B 133  ? 0.6908 0.6238 0.5682 0.0339  -0.0036 -0.0594 131  LYS B N   
9859  C CA  . LYS B 133  ? 0.7200 0.6529 0.6047 0.0311  -0.0061 -0.0576 131  LYS B CA  
9860  C C   . LYS B 133  ? 0.8380 0.7677 0.7212 0.0272  -0.0101 -0.0573 131  LYS B C   
9861  O O   . LYS B 133  ? 0.8736 0.8075 0.7613 0.0244  -0.0113 -0.0547 131  LYS B O   
9862  C CB  . LYS B 133  ? 0.7050 0.6330 0.5915 0.0328  -0.0065 -0.0591 131  LYS B CB  
9863  N N   . SER B 134  ? 0.8945 0.8166 0.7711 0.0270  -0.0123 -0.0599 132  SER B N   
9864  C CA  . SER B 134  ? 0.8999 0.8187 0.7746 0.0233  -0.0164 -0.0598 132  SER B CA  
9865  C C   . SER B 134  ? 0.8950 0.8157 0.7639 0.0227  -0.0162 -0.0596 132  SER B C   
9866  O O   . SER B 134  ? 0.9467 0.8622 0.8077 0.0225  -0.0177 -0.0617 132  SER B O   
9867  C CB  . SER B 134  ? 0.9255 0.8352 0.7956 0.0230  -0.0190 -0.0626 132  SER B CB  
9868  N N   . HIS B 135  ? 0.8616 0.7897 0.7342 0.0222  -0.0144 -0.0569 133  HIS B N   
9869  C CA  . HIS B 135  ? 0.8595 0.7902 0.7272 0.0215  -0.0141 -0.0561 133  HIS B CA  
9870  C C   . HIS B 135  ? 0.8597 0.7982 0.7336 0.0200  -0.0130 -0.0525 133  HIS B C   
9871  O O   . HIS B 135  ? 0.8524 0.7929 0.7239 0.0183  -0.0138 -0.0511 133  HIS B O   
9872  C CB  . HIS B 135  ? 0.7959 0.7263 0.6563 0.0249  -0.0108 -0.0583 133  HIS B CB  
9873  N N   . LEU B 136  ? 0.8100 0.7525 0.6915 0.0207  -0.0113 -0.0511 134  LEU B N   
9874  C CA  . LEU B 136  ? 0.7478 0.6970 0.6353 0.0193  -0.0104 -0.0478 134  LEU B CA  
9875  C C   . LEU B 136  ? 0.6705 0.6211 0.5667 0.0185  -0.0111 -0.0464 134  LEU B C   
9876  O O   . LEU B 136  ? 0.6497 0.6052 0.5515 0.0173  -0.0106 -0.0438 134  LEU B O   
9877  C CB  . LEU B 136  ? 0.6985 0.6535 0.5853 0.0214  -0.0062 -0.0472 134  LEU B CB  
9878  C CG  . LEU B 136  ? 0.6521 0.6079 0.5311 0.0219  -0.0049 -0.0476 134  LEU B CG  
9879  C CD1 . LEU B 136  ? 0.5409 0.5030 0.4205 0.0242  -0.0005 -0.0469 134  LEU B CD1 
9880  C CD2 . LEU B 136  ? 0.6682 0.6249 0.5464 0.0186  -0.0072 -0.0454 134  LEU B CD2 
9881  N N   . ARG B 140  ? 0.6101 0.5678 0.5402 0.0114  -0.0169 -0.0384 138  ARG B N   
9882  C CA  . ARG B 140  ? 0.6515 0.6145 0.5843 0.0122  -0.0141 -0.0369 138  ARG B CA  
9883  C C   . ARG B 140  ? 0.5939 0.5579 0.5235 0.0150  -0.0109 -0.0383 138  ARG B C   
9884  O O   . ARG B 140  ? 0.4968 0.4593 0.4202 0.0158  -0.0104 -0.0396 138  ARG B O   
9885  C CB  . ARG B 140  ? 0.6440 0.6099 0.5762 0.0106  -0.0145 -0.0348 138  ARG B CB  
9886  C CG  . ARG B 140  ? 0.5958 0.5671 0.5305 0.0110  -0.0117 -0.0331 138  ARG B CG  
9887  C CD  . ARG B 140  ? 0.7168 0.6900 0.6500 0.0091  -0.0124 -0.0311 138  ARG B CD  
9888  N NE  . ARG B 140  ? 0.6917 0.6696 0.6260 0.0092  -0.0098 -0.0295 138  ARG B NE  
9889  C CZ  . ARG B 140  ? 0.7487 0.7295 0.6879 0.0080  -0.0097 -0.0274 138  ARG B CZ  
9890  N NH1 . ARG B 140  ? 0.7551 0.7346 0.6987 0.0070  -0.0118 -0.0267 138  ARG B NH1 
9891  N NH2 . ARG B 140  ? 0.7568 0.7417 0.6964 0.0079  -0.0074 -0.0261 138  ARG B NH2 
9892  N N   . SER B 141  ? 0.5102 0.4769 0.4441 0.0164  -0.0088 -0.0380 139  SER B N   
9893  C CA  . SER B 141  ? 0.3990 0.3670 0.3306 0.0193  -0.0059 -0.0392 139  SER B CA  
9894  C C   . SER B 141  ? 0.4232 0.3950 0.3513 0.0196  -0.0038 -0.0385 139  SER B C   
9895  O O   . SER B 141  ? 0.4056 0.3811 0.3356 0.0178  -0.0038 -0.0364 139  SER B O   
9896  C CB  . SER B 141  ? 0.4402 0.4114 0.3777 0.0205  -0.0041 -0.0384 139  SER B CB  
9897  O OG  . SER B 141  ? 0.4190 0.3924 0.3550 0.0235  -0.0012 -0.0394 139  SER B OG  
9898  N N   . LEU B 142  ? 0.3590 0.3299 0.2818 0.0220  -0.0021 -0.0404 140  LEU B N   
9899  C CA  . LEU B 142  ? 0.3359 0.3113 0.2557 0.0228  0.0005  -0.0398 140  LEU B CA  
9900  C C   . LEU B 142  ? 0.3017 0.2841 0.2271 0.0230  0.0029  -0.0377 140  LEU B C   
9901  O O   . LEU B 142  ? 0.3122 0.2994 0.2367 0.0224  0.0046  -0.0363 140  LEU B O   
9902  C CB  . LEU B 142  ? 0.3369 0.3104 0.2510 0.0260  0.0024  -0.0424 140  LEU B CB  
9903  C CG  . LEU B 142  ? 0.3884 0.3639 0.2964 0.0264  0.0039  -0.0426 140  LEU B CG  
9904  C CD1 . LEU B 142  ? 0.3906 0.3611 0.2936 0.0242  0.0009  -0.0431 140  LEU B CD1 
9905  C CD2 . LEU B 142  ? 0.3952 0.3702 0.2987 0.0302  0.0066  -0.0449 140  LEU B CD2 
9906  N N   . PHE B 143  ? 0.2991 0.2822 0.2300 0.0237  0.0030  -0.0375 141  PHE B N   
9907  C CA  . PHE B 143  ? 0.2570 0.2465 0.1927 0.0244  0.0055  -0.0360 141  PHE B CA  
9908  C C   . PHE B 143  ? 0.2840 0.2760 0.2256 0.0217  0.0043  -0.0336 141  PHE B C   
9909  O O   . PHE B 143  ? 0.2949 0.2914 0.2411 0.0221  0.0058  -0.0325 141  PHE B O   
9910  C CB  . PHE B 143  ? 0.2648 0.2535 0.2019 0.0276  0.0068  -0.0376 141  PHE B CB  
9911  C CG  . PHE B 143  ? 0.2610 0.2462 0.1919 0.0306  0.0077  -0.0402 141  PHE B CG  
9912  C CD1 . PHE B 143  ? 0.2721 0.2606 0.1988 0.0319  0.0101  -0.0405 141  PHE B CD1 
9913  C CD2 . PHE B 143  ? 0.2597 0.2383 0.1888 0.0319  0.0063  -0.0423 141  PHE B CD2 
9914  C CE1 . PHE B 143  ? 0.2763 0.2615 0.1969 0.0347  0.0111  -0.0430 141  PHE B CE1 
9915  C CE2 . PHE B 143  ? 0.2754 0.2502 0.1983 0.0347  0.0072  -0.0449 141  PHE B CE2 
9916  C CZ  . PHE B 143  ? 0.2833 0.2613 0.2019 0.0362  0.0096  -0.0453 141  PHE B CZ  
9917  N N   . VAL B 144  ? 0.2999 0.2892 0.2413 0.0191  0.0018  -0.0328 142  VAL B N   
9918  C CA  . VAL B 144  ? 0.3047 0.2958 0.2512 0.0166  0.0006  -0.0306 142  VAL B CA  
9919  C C   . VAL B 144  ? 0.3287 0.3261 0.2774 0.0160  0.0028  -0.0287 142  VAL B C   
9920  O O   . VAL B 144  ? 0.3106 0.3105 0.2643 0.0153  0.0029  -0.0274 142  VAL B O   
9921  C CB  . VAL B 144  ? 0.3973 0.3851 0.3422 0.0142  -0.0022 -0.0300 142  VAL B CB  
9922  C CG1 . VAL B 144  ? 0.4030 0.3928 0.3526 0.0119  -0.0031 -0.0277 142  VAL B CG1 
9923  C CG2 . VAL B 144  ? 0.4003 0.3824 0.3443 0.0144  -0.0046 -0.0317 142  VAL B CG2 
9924  N N   . ASN B 145  ? 0.3104 0.3105 0.2552 0.0161  0.0044  -0.0284 143  ASN B N   
9925  C CA  . ASN B 145  ? 0.3254 0.3316 0.2721 0.0151  0.0063  -0.0263 143  ASN B CA  
9926  C C   . ASN B 145  ? 0.3296 0.3409 0.2769 0.0175  0.0094  -0.0267 143  ASN B C   
9927  O O   . ASN B 145  ? 0.3054 0.3221 0.2527 0.0169  0.0114  -0.0252 143  ASN B O   
9928  C CB  . ASN B 145  ? 0.3920 0.3986 0.3347 0.0129  0.0060  -0.0249 143  ASN B CB  
9929  C CG  . ASN B 145  ? 0.4583 0.4617 0.4021 0.0102  0.0032  -0.0236 143  ASN B CG  
9930  O OD1 . ASN B 145  ? 0.4688 0.4726 0.4175 0.0091  0.0024  -0.0226 143  ASN B OD1 
9931  N ND2 . ASN B 145  ? 0.4578 0.4580 0.3970 0.0092  0.0016  -0.0236 143  ASN B ND2 
9932  N N   . ALA B 146  ? 0.2907 0.3004 0.2386 0.0204  0.0099  -0.0287 144  ALA B N   
9933  C CA  . ALA B 146  ? 0.2954 0.3095 0.2434 0.0233  0.0129  -0.0293 144  ALA B CA  
9934  C C   . ALA B 146  ? 0.2798 0.3005 0.2335 0.0227  0.0142  -0.0273 144  ALA B C   
9935  O O   . ALA B 146  ? 0.2980 0.3246 0.2522 0.0243  0.0168  -0.0270 144  ALA B O   
9936  C CB  . ALA B 146  ? 0.3007 0.3107 0.2479 0.0265  0.0128  -0.0318 144  ALA B CB  
9937  N N   . ALA B 147  ? 0.2998 0.3200 0.2580 0.0205  0.0125  -0.0260 145  ALA B N   
9938  C CA  . ALA B 147  ? 0.3239 0.3503 0.2871 0.0195  0.0136  -0.0242 145  ALA B CA  
9939  C C   . ALA B 147  ? 0.3107 0.3423 0.2728 0.0175  0.0150  -0.0222 145  ALA B C   
9940  O O   . ALA B 147  ? 0.3210 0.3593 0.2854 0.0179  0.0171  -0.0212 145  ALA B O   
9941  C CB  . ALA B 147  ? 0.3387 0.3629 0.3061 0.0174  0.0114  -0.0232 145  ALA B CB  
9942  N N   . THR B 148  ? 0.3219 0.3507 0.2805 0.0153  0.0138  -0.0217 146  THR B N   
9943  C CA  . THR B 148  ? 0.3091 0.3421 0.2660 0.0132  0.0150  -0.0197 146  THR B CA  
9944  C C   . THR B 148  ? 0.3061 0.3434 0.2598 0.0155  0.0179  -0.0204 146  THR B C   
9945  O O   . THR B 148  ? 0.3354 0.3796 0.2906 0.0150  0.0200  -0.0189 146  THR B O   
9946  C CB  . THR B 148  ? 0.4279 0.4562 0.3812 0.0106  0.0129  -0.0191 146  THR B CB  
9947  O OG1 . THR B 148  ? 0.4409 0.4655 0.3974 0.0088  0.0104  -0.0185 146  THR B OG1 
9948  C CG2 . THR B 148  ? 0.4727 0.5051 0.4242 0.0081  0.0140  -0.0168 146  THR B CG2 
9949  N N   . TRP B 149  ? 0.2944 0.3276 0.2438 0.0182  0.0180  -0.0228 147  TRP B N   
9950  C CA  . TRP B 149  ? 0.3019 0.3388 0.2480 0.0209  0.0208  -0.0237 147  TRP B CA  
9951  C C   . TRP B 149  ? 0.2828 0.3252 0.2330 0.0238  0.0230  -0.0240 147  TRP B C   
9952  O O   . TRP B 149  ? 0.2909 0.3396 0.2405 0.0252  0.0259  -0.0236 147  TRP B O   
9953  C CB  . TRP B 149  ? 0.3040 0.3346 0.2440 0.0231  0.0202  -0.0264 147  TRP B CB  
9954  C CG  . TRP B 149  ? 0.3088 0.3354 0.2443 0.0205  0.0184  -0.0259 147  TRP B CG  
9955  C CD1 . TRP B 149  ? 0.3302 0.3496 0.2641 0.0194  0.0153  -0.0267 147  TRP B CD1 
9956  C CD2 . TRP B 149  ? 0.3360 0.3658 0.2679 0.0187  0.0195  -0.0243 147  TRP B CD2 
9957  N NE1 . TRP B 149  ? 0.3469 0.3647 0.2764 0.0171  0.0144  -0.0258 147  TRP B NE1 
9958  C CE2 . TRP B 149  ? 0.3620 0.3859 0.2901 0.0166  0.0169  -0.0242 147  TRP B CE2 
9959  C CE3 . TRP B 149  ? 0.3735 0.4107 0.3051 0.0185  0.0225  -0.0227 147  TRP B CE3 
9960  C CZ2 . TRP B 149  ? 0.3935 0.4183 0.3172 0.0145  0.0171  -0.0227 147  TRP B CZ2 
9961  C CZ3 . TRP B 149  ? 0.3894 0.4276 0.3167 0.0162  0.0228  -0.0212 147  TRP B CZ3 
9962  C CH2 . TRP B 149  ? 0.4374 0.4692 0.3607 0.0143  0.0201  -0.0212 147  TRP B CH2 
9963  N N   . GLY B 150  ? 0.2839 0.3242 0.2383 0.0247  0.0218  -0.0247 148  GLY B N   
9964  C CA  . GLY B 150  ? 0.2983 0.3440 0.2569 0.0271  0.0236  -0.0246 148  GLY B CA  
9965  C C   . GLY B 150  ? 0.3082 0.3625 0.2707 0.0249  0.0251  -0.0219 148  GLY B C   
9966  O O   . GLY B 150  ? 0.3145 0.3757 0.2785 0.0269  0.0276  -0.0215 148  GLY B O   
9967  N N   . LEU B 151  ? 0.3043 0.3582 0.2682 0.0207  0.0234  -0.0199 149  LEU B N   
9968  C CA  . LEU B 151  ? 0.3512 0.4126 0.3184 0.0181  0.0245  -0.0173 149  LEU B CA  
9969  C C   . LEU B 151  ? 0.3408 0.4073 0.3046 0.0180  0.0270  -0.0164 149  LEU B C   
9970  O O   . LEU B 151  ? 0.3540 0.4288 0.3204 0.0181  0.0292  -0.0150 149  LEU B O   
9971  C CB  . LEU B 151  ? 0.3673 0.4256 0.3359 0.0137  0.0220  -0.0156 149  LEU B CB  
9972  C CG  . LEU B 151  ? 0.4650 0.5295 0.4375 0.0105  0.0223  -0.0129 149  LEU B CG  
9973  C CD1 . LEU B 151  ? 0.4197 0.4895 0.3975 0.0122  0.0232  -0.0129 149  LEU B CD1 
9974  C CD2 . LEU B 151  ? 0.5168 0.5764 0.4900 0.0068  0.0196  -0.0118 149  LEU B CD2 
9975  N N   . VAL B 152  ? 0.3369 0.3988 0.2948 0.0179  0.0267  -0.0173 150  VAL B N   
9976  C CA  . VAL B 152  ? 0.3680 0.4344 0.3220 0.0179  0.0291  -0.0166 150  VAL B CA  
9977  C C   . VAL B 152  ? 0.3737 0.4453 0.3276 0.0223  0.0322  -0.0179 150  VAL B C   
9978  O O   . VAL B 152  ? 0.3672 0.4470 0.3217 0.0224  0.0349  -0.0165 150  VAL B O   
9979  C CB  . VAL B 152  ? 0.3294 0.3890 0.2768 0.0172  0.0278  -0.0175 150  VAL B CB  
9980  C CG1 . VAL B 152  ? 0.4061 0.4701 0.3487 0.0181  0.0306  -0.0173 150  VAL B CG1 
9981  C CG2 . VAL B 152  ? 0.4022 0.4581 0.3498 0.0128  0.0251  -0.0157 150  VAL B CG2 
9982  N N   . VAL B 153  ? 0.3194 0.3866 0.2726 0.0262  0.0319  -0.0206 151  VAL B N   
9983  C CA  . VAL B 153  ? 0.3374 0.4079 0.2893 0.0309  0.0347  -0.0223 151  VAL B CA  
9984  C C   . VAL B 153  ? 0.3307 0.4088 0.2890 0.0326  0.0362  -0.0214 151  VAL B C   
9985  O O   . VAL B 153  ? 0.3747 0.4605 0.3336 0.0349  0.0393  -0.0211 151  VAL B O   
9986  C CB  . VAL B 153  ? 0.3523 0.4139 0.3000 0.0342  0.0335  -0.0256 151  VAL B CB  
9987  C CG1 . VAL B 153  ? 0.3468 0.4109 0.2937 0.0396  0.0362  -0.0276 151  VAL B CG1 
9988  C CG2 . VAL B 153  ? 0.3119 0.3673 0.2528 0.0329  0.0324  -0.0265 151  VAL B CG2 
9989  N N   . THR B 154  ? 0.3187 0.3952 0.2819 0.0316  0.0342  -0.0210 152  THR B N   
9990  C CA  . THR B 154  ? 0.3542 0.4366 0.3232 0.0335  0.0352  -0.0204 152  THR B CA  
9991  C C   . THR B 154  ? 0.3811 0.4694 0.3558 0.0295  0.0345  -0.0175 152  THR B C   
9992  O O   . THR B 154  ? 0.4200 0.5147 0.3996 0.0307  0.0355  -0.0166 152  THR B O   
9993  C CB  . THR B 154  ? 0.3664 0.4421 0.3367 0.0359  0.0333  -0.0224 152  THR B CB  
9994  O OG1 . THR B 154  ? 0.3778 0.4492 0.3504 0.0322  0.0303  -0.0215 152  THR B OG1 
9995  C CG2 . THR B 154  ? 0.3958 0.4633 0.3600 0.0389  0.0330  -0.0253 152  THR B CG2 
9996  N N   . GLY B 155  ? 0.3416 0.4275 0.3155 0.0249  0.0328  -0.0160 153  GLY B N   
9997  C CA  . GLY B 155  ? 0.3755 0.4655 0.3542 0.0209  0.0318  -0.0135 153  GLY B CA  
9998  C C   . GLY B 155  ? 0.3965 0.4827 0.3791 0.0205  0.0293  -0.0138 153  GLY B C   
9999  O O   . GLY B 155  ? 0.4153 0.5045 0.4018 0.0173  0.0284  -0.0119 153  GLY B O   
10000 N N   . LYS B 156  ? 0.3617 0.4413 0.3430 0.0235  0.0283  -0.0161 154  LYS B N   
10001 C CA  . LYS B 156  ? 0.3933 0.4691 0.3780 0.0233  0.0261  -0.0165 154  LYS B CA  
10002 C C   . LYS B 156  ? 0.4030 0.4691 0.3847 0.0219  0.0236  -0.0176 154  LYS B C   
10003 O O   . LYS B 156  ? 0.3718 0.4332 0.3486 0.0229  0.0236  -0.0191 154  LYS B O   
10004 C CB  . LYS B 156  ? 0.4406 0.5169 0.4270 0.0280  0.0270  -0.0181 154  LYS B CB  
10005 N N   . LEU B 157  ? 0.3620 0.4253 0.3464 0.0196  0.0214  -0.0170 155  LEU B N   
10006 C CA  . LEU B 157  ? 0.3726 0.4276 0.3552 0.0181  0.0189  -0.0178 155  LEU B CA  
10007 C C   . LEU B 157  ? 0.4670 0.5180 0.4516 0.0202  0.0177  -0.0192 155  LEU B C   
10008 O O   . LEU B 157  ? 0.5257 0.5799 0.5145 0.0205  0.0177  -0.0185 155  LEU B O   
10009 C CB  . LEU B 157  ? 0.4261 0.4806 0.4099 0.0137  0.0173  -0.0159 155  LEU B CB  
10010 N N   . THR B 158  ? 0.5146 0.5586 0.4962 0.0216  0.0167  -0.0210 156  THR B N   
10011 C CA  . THR B 158  ? 0.4929 0.5318 0.4760 0.0227  0.0150  -0.0221 156  THR B CA  
10012 C C   . THR B 158  ? 0.4616 0.4946 0.4438 0.0200  0.0126  -0.0220 156  THR B C   
10013 O O   . THR B 158  ? 0.4969 0.5282 0.4760 0.0182  0.0122  -0.0218 156  THR B O   
10014 C CB  . THR B 158  ? 0.5305 0.5660 0.5112 0.0265  0.0156  -0.0242 156  THR B CB  
10015 O OG1 . THR B 158  ? 0.5785 0.6089 0.5542 0.0263  0.0150  -0.0255 156  THR B OG1 
10016 C CG2 . THR B 158  ? 0.5547 0.5961 0.5357 0.0296  0.0182  -0.0244 156  THR B CG2 
10017 N N   . SER B 159  ? 0.4086 0.4384 0.3933 0.0197  0.0111  -0.0222 157  SER B N   
10018 C CA  . SER B 159  ? 0.4216 0.4463 0.4060 0.0174  0.0088  -0.0221 157  SER B CA  
10019 C C   . SER B 159  ? 0.4287 0.4473 0.4098 0.0186  0.0078  -0.0238 157  SER B C   
10020 O O   . SER B 159  ? 0.4097 0.4247 0.3889 0.0168  0.0062  -0.0238 157  SER B O   
10021 C CB  . SER B 159  ? 0.4640 0.4880 0.4524 0.0167  0.0077  -0.0215 157  SER B CB  
10022 O OG  . SER B 159  ? 0.5344 0.5601 0.5249 0.0192  0.0086  -0.0221 157  SER B OG  
10023 N N   . THR B 160  ? 0.3785 0.3956 0.3586 0.0215  0.0085  -0.0253 158  THR B N   
10024 C CA  . THR B 160  ? 0.2950 0.3059 0.2716 0.0226  0.0074  -0.0271 158  THR B CA  
10025 C C   . THR B 160  ? 0.2918 0.3034 0.2649 0.0255  0.0092  -0.0285 158  THR B C   
10026 O O   . THR B 160  ? 0.3536 0.3705 0.3276 0.0270  0.0113  -0.0281 158  THR B O   
10027 C CB  . THR B 160  ? 0.3230 0.3299 0.3018 0.0233  0.0061  -0.0278 158  THR B CB  
10028 O OG1 . THR B 160  ? 0.4076 0.4172 0.3886 0.0257  0.0075  -0.0279 158  THR B OG1 
10029 C CG2 . THR B 160  ? 0.3639 0.3702 0.3460 0.0206  0.0044  -0.0265 158  THR B CG2 
10030 N N   . VAL B 161  ? 0.2411 0.2471 0.2100 0.0262  0.0083  -0.0302 159  VAL B N   
10031 C CA  . VAL B 161  ? 0.2808 0.2861 0.2449 0.0285  0.0096  -0.0318 159  VAL B CA  
10032 C C   . VAL B 161  ? 0.2770 0.2775 0.2397 0.0313  0.0094  -0.0337 159  VAL B C   
10033 O O   . VAL B 161  ? 0.2527 0.2478 0.2158 0.0305  0.0073  -0.0343 159  VAL B O   
10034 C CB  . VAL B 161  ? 0.3230 0.3251 0.2827 0.0265  0.0083  -0.0321 159  VAL B CB  
10035 C CG1 . VAL B 161  ? 0.3879 0.3865 0.3417 0.0288  0.0089  -0.0343 159  VAL B CG1 
10036 C CG2 . VAL B 161  ? 0.4186 0.4258 0.3786 0.0243  0.0091  -0.0302 159  VAL B CG2 
10037 N N   . ASN B 162  ? 0.2402 0.2425 0.2015 0.0347  0.0116  -0.0347 160  ASN B N   
10038 C CA  . ASN B 162  ? 0.2548 0.2514 0.2137 0.0376  0.0113  -0.0368 160  ASN B CA  
10039 C C   . ASN B 162  ? 0.2589 0.2504 0.2113 0.0380  0.0108  -0.0388 160  ASN B C   
10040 O O   . ASN B 162  ? 0.2561 0.2488 0.2046 0.0403  0.0127  -0.0399 160  ASN B O   
10041 C CB  . ASN B 162  ? 0.2857 0.2860 0.2459 0.0414  0.0137  -0.0370 160  ASN B CB  
10042 C CG  . ASN B 162  ? 0.2792 0.2729 0.2369 0.0445  0.0133  -0.0391 160  ASN B CG  
10043 O OD1 . ASN B 162  ? 0.2682 0.2548 0.2218 0.0440  0.0116  -0.0407 160  ASN B OD1 
10044 N ND2 . ASN B 162  ? 0.2945 0.2904 0.2545 0.0476  0.0146  -0.0390 160  ASN B ND2 
10045 N N   . ASP B 163  ? 0.2584 0.2441 0.2095 0.0356  0.0081  -0.0392 161  ASP B N   
10046 C CA  . ASP B 163  ? 0.2247 0.2055 0.1697 0.0353  0.0071  -0.0409 161  ASP B CA  
10047 C C   . ASP B 163  ? 0.2455 0.2206 0.1858 0.0385  0.0075  -0.0436 161  ASP B C   
10048 O O   . ASP B 163  ? 0.2613 0.2336 0.1956 0.0393  0.0076  -0.0452 161  ASP B O   
10049 C CB  . ASP B 163  ? 0.2486 0.2253 0.1939 0.0317  0.0040  -0.0405 161  ASP B CB  
10050 C CG  . ASP B 163  ? 0.3145 0.2880 0.2637 0.0309  0.0022  -0.0402 161  ASP B CG  
10051 O OD1 . ASP B 163  ? 0.2719 0.2488 0.2260 0.0315  0.0032  -0.0390 161  ASP B OD1 
10052 O OD2 . ASP B 163  ? 0.3361 0.3038 0.2835 0.0295  -0.0002 -0.0411 161  ASP B OD2 
10053 N N   . ARG B 164  ? 0.2477 0.2206 0.1901 0.0405  0.0076  -0.0440 162  ARG B N   
10054 C CA  . ARG B 164  ? 0.2263 0.1937 0.1640 0.0440  0.0081  -0.0465 162  ARG B CA  
10055 C C   . ARG B 164  ? 0.2335 0.2054 0.1690 0.0477  0.0114  -0.0471 162  ARG B C   
10056 O O   . ARG B 164  ? 0.2424 0.2105 0.1718 0.0501  0.0121  -0.0494 162  ARG B O   
10057 C CB  . ARG B 164  ? 0.2519 0.2155 0.1924 0.0450  0.0072  -0.0466 162  ARG B CB  
10058 C CG  . ARG B 164  ? 0.2587 0.2172 0.2007 0.0416  0.0041  -0.0462 162  ARG B CG  
10059 C CD  . ARG B 164  ? 0.3259 0.2788 0.2626 0.0396  0.0020  -0.0477 162  ARG B CD  
10060 N NE  . ARG B 164  ? 0.4276 0.3746 0.3577 0.0425  0.0024  -0.0505 162  ARG B NE  
10061 C CZ  . ARG B 164  ? 0.4641 0.4072 0.3880 0.0420  0.0016  -0.0522 162  ARG B CZ  
10062 N NH1 . ARG B 164  ? 0.5080 0.4527 0.4316 0.0387  0.0002  -0.0514 162  ARG B NH1 
10063 N NH2 . ARG B 164  ? 0.4525 0.3898 0.3702 0.0449  0.0021  -0.0549 162  ARG B NH2 
10064 N N   . SER B 165  ? 0.2318 0.2120 0.1723 0.0483  0.0134  -0.0452 163  SER B N   
10065 C CA  . SER B 165  ? 0.2262 0.2122 0.1655 0.0515  0.0166  -0.0454 163  SER B CA  
10066 C C   . SER B 165  ? 0.2433 0.2310 0.1780 0.0505  0.0174  -0.0458 163  SER B C   
10067 O O   . SER B 165  ? 0.2359 0.2241 0.1660 0.0536  0.0195  -0.0473 163  SER B O   
10068 C CB  . SER B 165  ? 0.2317 0.2266 0.1777 0.0514  0.0181  -0.0428 163  SER B CB  
10069 O OG  . SER B 165  ? 0.2577 0.2597 0.2032 0.0539  0.0212  -0.0426 163  SER B OG  
10070 N N   . LEU B 166  ? 0.2450 0.2338 0.1807 0.0463  0.0158  -0.0443 164  LEU B N   
10071 C CA  . LEU B 166  ? 0.2505 0.2408 0.1818 0.0450  0.0163  -0.0443 164  LEU B CA  
10072 C C   . LEU B 166  ? 0.2713 0.2536 0.1952 0.0457  0.0151  -0.0471 164  LEU B C   
10073 O O   . LEU B 166  ? 0.2542 0.2371 0.1727 0.0471  0.0166  -0.0482 164  LEU B O   
10074 C CB  . LEU B 166  ? 0.2427 0.2354 0.1770 0.0403  0.0146  -0.0420 164  LEU B CB  
10075 C CG  . LEU B 166  ? 0.2423 0.2437 0.1827 0.0396  0.0163  -0.0394 164  LEU B CG  
10076 C CD1 . LEU B 166  ? 0.2836 0.2860 0.2270 0.0352  0.0144  -0.0372 164  LEU B CD1 
10077 C CD2 . LEU B 166  ? 0.2306 0.2387 0.1690 0.0413  0.0195  -0.0390 164  LEU B CD2 
10078 N N   . ALA B 167  ? 0.2429 0.2175 0.1662 0.0446  0.0122  -0.0481 165  ALA B N   
10079 C CA  . ALA B 167  ? 0.2551 0.2215 0.1712 0.0452  0.0108  -0.0508 165  ALA B CA  
10080 C C   . ALA B 167  ? 0.2864 0.2508 0.1979 0.0501  0.0131  -0.0533 165  ALA B C   
10081 O O   . ALA B 167  ? 0.2817 0.2434 0.1863 0.0514  0.0137  -0.0552 165  ALA B O   
10082 C CB  . ALA B 167  ? 0.3025 0.2617 0.2198 0.0431  0.0074  -0.0513 165  ALA B CB  
10083 N N   . ALA B 168  ? 0.2699 0.2356 0.1850 0.0530  0.0144  -0.0532 166  ALA B N   
10084 C CA  . ALA B 168  ? 0.2733 0.2377 0.1847 0.0581  0.0168  -0.0553 166  ALA B CA  
10085 C C   . ALA B 168  ? 0.2524 0.2240 0.1617 0.0600  0.0202  -0.0551 166  ALA B C   
10086 O O   . ALA B 168  ? 0.2627 0.2316 0.1655 0.0631  0.0216  -0.0575 166  ALA B O   
10087 C CB  . ALA B 168  ? 0.2815 0.2478 0.1985 0.0605  0.0177  -0.0545 166  ALA B CB  
10088 N N   . ALA B 169  ? 0.2545 0.2353 0.1692 0.0581  0.0214  -0.0523 167  ALA B N   
10089 C CA  . ALA B 169  ? 0.2507 0.2393 0.1640 0.0595  0.0246  -0.0517 167  ALA B CA  
10090 C C   . ALA B 169  ? 0.2767 0.2628 0.1830 0.0581  0.0243  -0.0528 167  ALA B C   
10091 O O   . ALA B 169  ? 0.2630 0.2510 0.1644 0.0609  0.0269  -0.0541 167  ALA B O   
10092 C CB  . ALA B 169  ? 0.2558 0.2541 0.1764 0.0569  0.0254  -0.0483 167  ALA B CB  
10093 N N   . LEU B 170  ? 0.2704 0.2522 0.1758 0.0538  0.0211  -0.0524 168  LEU B N   
10094 C CA  . LEU B 170  ? 0.2664 0.2459 0.1651 0.0522  0.0205  -0.0532 168  LEU B CA  
10095 C C   . LEU B 170  ? 0.2935 0.2645 0.1840 0.0552  0.0203  -0.0569 168  LEU B C   
10096 O O   . LEU B 170  ? 0.2888 0.2602 0.1728 0.0567  0.0219  -0.0582 168  LEU B O   
10097 C CB  . LEU B 170  ? 0.2785 0.2555 0.1787 0.0472  0.0170  -0.0518 168  LEU B CB  
10098 C CG  . LEU B 170  ? 0.2853 0.2603 0.1791 0.0450  0.0160  -0.0522 168  LEU B CG  
10099 C CD1 . LEU B 170  ? 0.3043 0.2873 0.1969 0.0454  0.0192  -0.0507 168  LEU B CD1 
10100 C CD2 . LEU B 170  ? 0.3289 0.3018 0.2254 0.0404  0.0125  -0.0505 168  LEU B CD2 
10101 N N   . THR B 171  ? 0.2881 0.2515 0.1785 0.0560  0.0182  -0.0585 169  THR B N   
10102 C CA  . THR B 171  ? 0.2963 0.2512 0.1789 0.0591  0.0180  -0.0621 169  THR B CA  
10103 C C   . THR B 171  ? 0.3151 0.2736 0.1950 0.0644  0.0221  -0.0635 169  THR B C   
10104 O O   . THR B 171  ? 0.3116 0.2668 0.1836 0.0667  0.0232  -0.0660 169  THR B O   
10105 C CB  . THR B 171  ? 0.3118 0.2589 0.1960 0.0592  0.0155  -0.0632 169  THR B CB  
10106 O OG1 . THR B 171  ? 0.3532 0.2971 0.2394 0.0542  0.0117  -0.0621 169  THR B OG1 
10107 C CG2 . THR B 171  ? 0.3499 0.2877 0.2259 0.0625  0.0152  -0.0670 169  THR B CG2 
10108 N N   . ARG B 172  ? 0.2944 0.2597 0.1808 0.0666  0.0244  -0.0619 170  ARG B N   
10109 C CA  . ARG B 172  ? 0.2961 0.2653 0.1808 0.0721  0.0282  -0.0631 170  ARG B CA  
10110 C C   . ARG B 172  ? 0.3045 0.2805 0.1858 0.0723  0.0310  -0.0626 170  ARG B C   
10111 O O   . ARG B 172  ? 0.3072 0.2819 0.1820 0.0761  0.0332  -0.0650 170  ARG B O   
10112 C CB  . ARG B 172  ? 0.2893 0.2654 0.1824 0.0738  0.0298  -0.0610 170  ARG B CB  
10113 C CG  . ARG B 172  ? 0.2815 0.2606 0.1732 0.0800  0.0335  -0.0623 170  ARG B CG  
10114 C CD  . ARG B 172  ? 0.3039 0.2911 0.2044 0.0816  0.0350  -0.0599 170  ARG B CD  
10115 N NE  . ARG B 172  ? 0.2676 0.2511 0.1734 0.0791  0.0320  -0.0588 170  ARG B NE  
10116 C CZ  . ARG B 172  ? 0.2577 0.2461 0.1701 0.0748  0.0306  -0.0558 170  ARG B CZ  
10117 N NH1 . ARG B 172  ? 0.2761 0.2728 0.1908 0.0719  0.0317  -0.0536 170  ARG B NH1 
10118 N NH2 . ARG B 172  ? 0.2531 0.2377 0.1698 0.0731  0.0281  -0.0550 170  ARG B NH2 
10119 N N   . LEU B 173  ? 0.2866 0.2696 0.1720 0.0681  0.0308  -0.0596 171  LEU B N   
10120 C CA  . LEU B 173  ? 0.3002 0.2904 0.1829 0.0682  0.0336  -0.0587 171  LEU B CA  
10121 C C   . LEU B 173  ? 0.3046 0.2884 0.1778 0.0675  0.0326  -0.0610 171  LEU B C   
10122 O O   . LEU B 173  ? 0.3191 0.3056 0.1868 0.0700  0.0355  -0.0620 171  LEU B O   
10123 C CB  . LEU B 173  ? 0.2970 0.2959 0.1863 0.0638  0.0336  -0.0548 171  LEU B CB  
10124 C CG  . LEU B 173  ? 0.3219 0.3181 0.2117 0.0581  0.0301  -0.0532 171  LEU B CG  
10125 C CD1 . LEU B 173  ? 0.3619 0.3592 0.2452 0.0565  0.0308  -0.0531 171  LEU B CD1 
10126 C CD2 . LEU B 173  ? 0.3228 0.3256 0.2215 0.0548  0.0296  -0.0497 171  LEU B CD2 
10127 N N   . ILE B 174  ? 0.3023 0.2779 0.1733 0.0640  0.0286  -0.0616 172  ILE B N   
10128 C CA  . ILE B 174  ? 0.3009 0.2703 0.1627 0.0632  0.0274  -0.0637 172  ILE B CA  
10129 C C   . ILE B 174  ? 0.3445 0.3069 0.1987 0.0681  0.0285  -0.0678 172  ILE B C   
10130 O O   . ILE B 174  ? 0.3601 0.3218 0.2065 0.0699  0.0302  -0.0696 172  ILE B O   
10131 C CB  . ILE B 174  ? 0.3197 0.2826 0.1815 0.0583  0.0227  -0.0633 172  ILE B CB  
10132 C CG1 . ILE B 174  ? 0.3211 0.2910 0.1893 0.0537  0.0219  -0.0594 172  ILE B CG1 
10133 C CG2 . ILE B 174  ? 0.3588 0.3142 0.2106 0.0578  0.0211  -0.0660 172  ILE B CG2 
10134 C CD1 . ILE B 174  ? 0.3649 0.3294 0.2348 0.0492  0.0173  -0.0587 172  ILE B CD1 
10135 N N   . SER B 175  ? 0.3304 0.2873 0.1866 0.0704  0.0276  -0.0692 173  SER B N   
10136 C CA  . SER B 175  ? 0.3360 0.2854 0.1849 0.0752  0.0285  -0.0731 173  SER B CA  
10137 C C   . SER B 175  ? 0.3563 0.3125 0.2037 0.0806  0.0334  -0.0737 173  SER B C   
10138 O O   . SER B 175  ? 0.4144 0.3656 0.2538 0.0846  0.0348  -0.0770 173  SER B O   
10139 C CB  . SER B 175  ? 0.3833 0.3255 0.2351 0.0764  0.0264  -0.0742 173  SER B CB  
10140 O OG  . SER B 175  ? 0.4584 0.3936 0.3104 0.0717  0.0219  -0.0741 173  SER B OG  
10141 N N   . ARG B 176  ? 0.3328 0.3003 0.1879 0.0807  0.0360  -0.0706 174  ARG B N   
10142 C CA  . ARG B 176  ? 0.3395 0.3148 0.1940 0.0857  0.0408  -0.0709 174  ARG B CA  
10143 C C   . ARG B 176  ? 0.3514 0.3326 0.2013 0.0847  0.0430  -0.0702 174  ARG B C   
10144 O O   . ARG B 176  ? 0.3810 0.3631 0.2247 0.0890  0.0462  -0.0723 174  ARG B O   
10145 C CB  . ARG B 176  ? 0.3574 0.3426 0.2225 0.0863  0.0425  -0.0678 174  ARG B CB  
10146 C CG  . ARG B 176  ? 0.3385 0.3321 0.2044 0.0920  0.0473  -0.0679 174  ARG B CG  
10147 C CD  . ARG B 176  ? 0.3355 0.3380 0.2122 0.0922  0.0482  -0.0648 174  ARG B CD  
10148 N NE  . ARG B 176  ? 0.3296 0.3416 0.2123 0.0872  0.0483  -0.0609 174  ARG B NE  
10149 C CZ  . ARG B 176  ? 0.3621 0.3750 0.2516 0.0826  0.0456  -0.0584 174  ARG B CZ  
10150 N NH1 . ARG B 176  ? 0.3319 0.3374 0.2238 0.0821  0.0426  -0.0590 174  ARG B NH1 
10151 N NH2 . ARG B 176  ? 0.4021 0.4234 0.2960 0.0784  0.0459  -0.0551 174  ARG B NH2 
10152 N N   . CYS B 177  ? 0.3627 0.3479 0.2153 0.0791  0.0415  -0.0674 175  CYS B N   
10153 C CA  . CYS B 177  ? 0.3642 0.3568 0.2141 0.0778  0.0438  -0.0659 175  CYS B CA  
10154 C C   . CYS B 177  ? 0.4237 0.4104 0.2664 0.0740  0.0412  -0.0665 175  CYS B C   
10155 O O   . CYS B 177  ? 0.4415 0.4327 0.2796 0.0736  0.0433  -0.0659 175  CYS B O   
10156 C CB  . CYS B 177  ? 0.3871 0.3911 0.2462 0.0747  0.0449  -0.0614 175  CYS B CB  
10157 S SG  . CYS B 177  ? 0.4713 0.4842 0.3395 0.0788  0.0481  -0.0601 175  CYS B SG  
10158 N N   . GLY B 178  ? 0.3854 0.3628 0.2271 0.0710  0.0367  -0.0674 176  GLY B N   
10159 C CA  . GLY B 178  ? 0.4117 0.3827 0.2455 0.0682  0.0341  -0.0686 176  GLY B CA  
10160 C C   . GLY B 178  ? 0.3915 0.3682 0.2268 0.0632  0.0334  -0.0652 176  GLY B C   
10161 O O   . GLY B 178  ? 0.3899 0.3740 0.2335 0.0606  0.0337  -0.0617 176  GLY B O   
10162 N N   . GLU B 179  ? 0.4382 0.4109 0.2650 0.0617  0.0324  -0.0663 177  GLU B N   
10163 C CA  . GLU B 179  ? 0.4675 0.4445 0.2943 0.0571  0.0314  -0.0633 177  GLU B CA  
10164 C C   . GLU B 179  ? 0.3820 0.3710 0.2133 0.0569  0.0353  -0.0599 177  GLU B C   
10165 O O   . GLU B 179  ? 0.4118 0.4051 0.2484 0.0526  0.0340  -0.0564 177  GLU B O   
10166 C CB  . GLU B 179  ? 0.4741 0.4450 0.2901 0.0562  0.0300  -0.0652 177  GLU B CB  
10167 C CG  . GLU B 179  ? 0.5134 0.4869 0.3293 0.0511  0.0280  -0.0621 177  GLU B CG  
10168 C CD  . GLU B 179  ? 0.6653 0.6345 0.4702 0.0505  0.0273  -0.0637 177  GLU B CD  
10169 O OE1 . GLU B 179  ? 0.7101 0.6716 0.5074 0.0531  0.0267  -0.0676 177  GLU B OE1 
10170 O OE2 . GLU B 179  ? 0.7229 0.6965 0.5267 0.0474  0.0273  -0.0609 177  GLU B OE2 
10171 N N   . PRO B 180  ? 0.3889 0.3837 0.2185 0.0612  0.0399  -0.0607 178  PRO B N   
10172 C CA  . PRO B 180  ? 0.4122 0.4189 0.2463 0.0604  0.0434  -0.0572 178  PRO B CA  
10173 C C   . PRO B 180  ? 0.4264 0.4390 0.2718 0.0578  0.0427  -0.0537 178  PRO B C   
10174 O O   . PRO B 180  ? 0.4285 0.4482 0.2774 0.0543  0.0433  -0.0502 178  PRO B O   
10175 C CB  . PRO B 180  ? 0.4608 0.4719 0.2919 0.0662  0.0482  -0.0591 178  PRO B CB  
10176 C CG  . PRO B 180  ? 0.4369 0.4379 0.2580 0.0691  0.0473  -0.0636 178  PRO B CG  
10177 C CD  . PRO B 180  ? 0.4242 0.4151 0.2468 0.0668  0.0422  -0.0647 178  PRO B CD  
10178 N N   . VAL B 181  ? 0.3640 0.3739 0.2151 0.0593  0.0415  -0.0547 179  VAL B N   
10179 C CA  . VAL B 181  ? 0.3487 0.3644 0.2101 0.0568  0.0409  -0.0514 179  VAL B CA  
10180 C C   . VAL B 181  ? 0.3575 0.3694 0.2211 0.0512  0.0367  -0.0495 179  VAL B C   
10181 O O   . VAL B 181  ? 0.3701 0.3879 0.2402 0.0479  0.0365  -0.0460 179  VAL B O   
10182 C CB  . VAL B 181  ? 0.3443 0.3591 0.2114 0.0602  0.0412  -0.0526 179  VAL B CB  
10183 C CG1 . VAL B 181  ? 0.3717 0.3752 0.2373 0.0599  0.0372  -0.0550 179  VAL B CG1 
10184 C CG2 . VAL B 181  ? 0.3723 0.3952 0.2496 0.0581  0.0416  -0.0491 179  VAL B CG2 
10185 N N   . ILE B 182  ? 0.3517 0.3539 0.2101 0.0502  0.0332  -0.0515 180  ILE B N   
10186 C CA  . ILE B 182  ? 0.3616 0.3604 0.2218 0.0452  0.0292  -0.0497 180  ILE B CA  
10187 C C   . ILE B 182  ? 0.3967 0.4003 0.2547 0.0419  0.0297  -0.0470 180  ILE B C   
10188 O O   . ILE B 182  ? 0.3678 0.3745 0.2311 0.0380  0.0283  -0.0438 180  ILE B O   
10189 C CB  . ILE B 182  ? 0.3860 0.3738 0.2407 0.0448  0.0254  -0.0526 180  ILE B CB  
10190 C CG1 . ILE B 182  ? 0.3623 0.3449 0.2192 0.0478  0.0247  -0.0551 180  ILE B CG1 
10191 C CG2 . ILE B 182  ? 0.3632 0.3482 0.2202 0.0398  0.0212  -0.0506 180  ILE B CG2 
10192 C CD1 . ILE B 182  ? 0.4127 0.3845 0.2628 0.0482  0.0217  -0.0585 180  ILE B CD1 
10193 N N   . ARG B 183  ? 0.4295 0.4336 0.2793 0.0434  0.0318  -0.0481 181  ARG B N   
10194 C CA  . ARG B 183  ? 0.4385 0.4474 0.2855 0.0405  0.0327  -0.0455 181  ARG B CA  
10195 C C   . ARG B 183  ? 0.4309 0.4502 0.2853 0.0392  0.0354  -0.0418 181  ARG B C   
10196 O O   . ARG B 183  ? 0.4481 0.4700 0.3052 0.0350  0.0341  -0.0385 181  ARG B O   
10197 C CB  . ARG B 183  ? 0.4393 0.4477 0.2764 0.0432  0.0352  -0.0476 181  ARG B CB  
10198 C CG  . ARG B 183  ? 0.5561 0.5724 0.3909 0.0416  0.0381  -0.0448 181  ARG B CG  
10199 C CD  . ARG B 183  ? 0.6420 0.6547 0.4716 0.0374  0.0351  -0.0433 181  ARG B CD  
10200 N NE  . ARG B 183  ? 0.6198 0.6307 0.4557 0.0331  0.0313  -0.0407 181  ARG B NE  
10201 C CZ  . ARG B 183  ? 0.6176 0.6203 0.4519 0.0312  0.0268  -0.0417 181  ARG B CZ  
10202 N NH1 . ARG B 183  ? 0.6617 0.6569 0.4884 0.0328  0.0253  -0.0451 181  ARG B NH1 
10203 N NH2 . ARG B 183  ? 0.5806 0.5827 0.4211 0.0275  0.0238  -0.0392 181  ARG B NH2 
10204 N N   . ARG B 184  ? 0.4168 0.4420 0.2747 0.0428  0.0389  -0.0423 182  ARG B N   
10205 C CA  . ARG B 184  ? 0.4269 0.4624 0.2921 0.0415  0.0414  -0.0389 182  ARG B CA  
10206 C C   . ARG B 184  ? 0.4387 0.4739 0.3124 0.0381  0.0385  -0.0366 182  ARG B C   
10207 O O   . ARG B 184  ? 0.4176 0.4585 0.2955 0.0345  0.0387  -0.0331 182  ARG B O   
10208 C CB  . ARG B 184  ? 0.4452 0.4868 0.3129 0.0464  0.0455  -0.0401 182  ARG B CB  
10209 C CG  . ARG B 184  ? 0.5142 0.5605 0.3752 0.0493  0.0496  -0.0409 182  ARG B CG  
10210 C CD  . ARG B 184  ? 0.5224 0.5798 0.3864 0.0468  0.0525  -0.0370 182  ARG B CD  
10211 N NE  . ARG B 184  ? 0.5294 0.5961 0.4008 0.0491  0.0556  -0.0359 182  ARG B NE  
10212 C CZ  . ARG B 184  ? 0.5276 0.6013 0.4073 0.0460  0.0556  -0.0324 182  ARG B CZ  
10213 N NH1 . ARG B 184  ? 0.5320 0.6043 0.4138 0.0406  0.0527  -0.0297 182  ARG B NH1 
10214 N NH2 . ARG B 184  ? 0.5597 0.6419 0.4457 0.0485  0.0584  -0.0317 182  ARG B NH2 
10215 N N   . GLY B 185  ? 0.3975 0.4260 0.2737 0.0390  0.0358  -0.0385 183  GLY B N   
10216 C CA  . GLY B 185  ? 0.3454 0.3732 0.2291 0.0358  0.0330  -0.0366 183  GLY B CA  
10217 C C   . GLY B 185  ? 0.3875 0.4124 0.2701 0.0310  0.0299  -0.0345 183  GLY B C   
10218 O O   . GLY B 185  ? 0.3778 0.4061 0.2659 0.0277  0.0291  -0.0315 183  GLY B O   
10219 N N   . VAL B 186  ? 0.3425 0.3608 0.2176 0.0307  0.0280  -0.0361 184  VAL B N   
10220 C CA  . VAL B 186  ? 0.3985 0.4137 0.2720 0.0264  0.0249  -0.0341 184  VAL B CA  
10221 C C   . VAL B 186  ? 0.4044 0.4266 0.2776 0.0238  0.0269  -0.0307 184  VAL B C   
10222 O O   . VAL B 186  ? 0.4086 0.4318 0.2856 0.0201  0.0252  -0.0277 184  VAL B O   
10223 C CB  . VAL B 186  ? 0.3733 0.3804 0.2384 0.0268  0.0226  -0.0366 184  VAL B CB  
10224 C CG1 . VAL B 186  ? 0.3928 0.3983 0.2550 0.0227  0.0201  -0.0343 184  VAL B CG1 
10225 C CG2 . VAL B 186  ? 0.4183 0.4181 0.2850 0.0278  0.0197  -0.0392 184  VAL B CG2 
10226 N N   . ASP B 187  ? 0.4204 0.4474 0.2890 0.0258  0.0305  -0.0310 185  ASP B N   
10227 C CA  . ASP B 187  ? 0.4378 0.4719 0.3061 0.0233  0.0327  -0.0276 185  ASP B CA  
10228 C C   . ASP B 187  ? 0.4717 0.5126 0.3490 0.0215  0.0337  -0.0247 185  ASP B C   
10229 O O   . ASP B 187  ? 0.4038 0.4474 0.2830 0.0176  0.0330  -0.0214 185  ASP B O   
10230 C CB  . ASP B 187  ? 0.4609 0.4996 0.3231 0.0262  0.0368  -0.0287 185  ASP B CB  
10231 C CG  . ASP B 187  ? 0.5700 0.6021 0.4222 0.0271  0.0357  -0.0310 185  ASP B CG  
10232 O OD1 . ASP B 187  ? 0.6271 0.6529 0.4771 0.0242  0.0319  -0.0305 185  ASP B OD1 
10233 O OD2 . ASP B 187  ? 0.5650 0.5981 0.4116 0.0307  0.0385  -0.0333 185  ASP B OD2 
10234 N N   . MET B 188  ? 0.4399 0.4835 0.3227 0.0244  0.0351  -0.0260 186  MET B N   
10235 C CA  . MET B 188  ? 0.4211 0.4710 0.3125 0.0228  0.0358  -0.0235 186  MET B CA  
10236 C C   . MET B 188  ? 0.4240 0.4695 0.3197 0.0190  0.0319  -0.0219 186  MET B C   
10237 O O   . MET B 188  ? 0.4518 0.5013 0.3512 0.0155  0.0317  -0.0187 186  MET B O   
10238 C CB  . MET B 188  ? 0.4675 0.5197 0.3633 0.0269  0.0375  -0.0256 186  MET B CB  
10239 C CG  . MET B 188  ? 0.5101 0.5696 0.4146 0.0258  0.0385  -0.0232 186  MET B CG  
10240 S SD  . MET B 188  ? 0.7091 0.7803 0.6143 0.0242  0.0425  -0.0199 186  MET B SD  
10241 C CE  . MET B 188  ? 0.5854 0.6584 0.4832 0.0293  0.0462  -0.0227 186  MET B CE  
10242 N N   . ALA B 189  ? 0.4097 0.4471 0.3050 0.0197  0.0287  -0.0241 187  ALA B N   
10243 C CA  . ALA B 189  ? 0.4245 0.4579 0.3241 0.0166  0.0251  -0.0227 187  ALA B CA  
10244 C C   . ALA B 189  ? 0.4670 0.4988 0.3634 0.0126  0.0234  -0.0202 187  ALA B C   
10245 O O   . ALA B 189  ? 0.4194 0.4518 0.3201 0.0094  0.0218  -0.0176 187  ALA B O   
10246 C CB  . ALA B 189  ? 0.4344 0.4598 0.3337 0.0182  0.0222  -0.0255 187  ALA B CB  
10247 N N   . MET B 190  ? 0.4429 0.4724 0.3315 0.0129  0.0235  -0.0209 188  MET B N   
10248 C CA  . MET B 190  ? 0.4372 0.4654 0.3221 0.0093  0.0220  -0.0184 188  MET B CA  
10249 C C   . MET B 190  ? 0.4614 0.4969 0.3491 0.0066  0.0241  -0.0147 188  MET B C   
10250 O O   . MET B 190  ? 0.4675 0.5019 0.3570 0.0030  0.0221  -0.0120 188  MET B O   
10251 C CB  . MET B 190  ? 0.4535 0.4792 0.3291 0.0105  0.0225  -0.0198 188  MET B CB  
10252 C CG  . MET B 190  ? 0.5282 0.5498 0.3992 0.0073  0.0197  -0.0180 188  MET B CG  
10253 S SD  . MET B 190  ? 0.6825 0.7021 0.5422 0.0087  0.0206  -0.0196 188  MET B SD  
10254 C CE  . MET B 190  ? 0.5596 0.5758 0.4177 0.0136  0.0213  -0.0246 188  MET B CE  
10255 N N   . ARG B 191  ? 0.4287 0.4716 0.3168 0.0082  0.0280  -0.0146 189  ARG B N   
10256 C CA  . ARG B 191  ? 0.4856 0.5360 0.3764 0.0054  0.0301  -0.0111 189  ARG B CA  
10257 C C   . ARG B 191  ? 0.4911 0.5429 0.3904 0.0034  0.0288  -0.0094 189  ARG B C   
10258 O O   . ARG B 191  ? 0.4514 0.5041 0.3524 -0.0006 0.0278  -0.0063 189  ARG B O   
10259 C CB  . ARG B 191  ? 0.3878 0.4466 0.2780 0.0080  0.0348  -0.0115 189  ARG B CB  
10260 N N   . MET B 192  ? 0.4427 0.4942 0.3469 0.0060  0.0288  -0.0115 190  MET B N   
10261 C CA  . MET B 192  ? 0.4363 0.4893 0.3482 0.0043  0.0277  -0.0102 190  MET B CA  
10262 C C   . MET B 192  ? 0.4605 0.5066 0.3732 0.0012  0.0237  -0.0091 190  MET B C   
10263 O O   . MET B 192  ? 0.4396 0.4872 0.3556 -0.0022 0.0229  -0.0063 190  MET B O   
10264 C CB  . MET B 192  ? 0.4592 0.5125 0.3756 0.0079  0.0281  -0.0128 190  MET B CB  
10265 C CG  . MET B 192  ? 0.4670 0.5274 0.3835 0.0113  0.0321  -0.0138 190  MET B CG  
10266 S SD  . MET B 192  ? 0.6363 0.6972 0.5590 0.0151  0.0323  -0.0162 190  MET B SD  
10267 C CE  . MET B 192  ? 0.4937 0.5594 0.4247 0.0113  0.0316  -0.0130 190  MET B CE  
10268 N N   . MET B 193  ? 0.4378 0.4764 0.3475 0.0024  0.0211  -0.0112 191  MET B N   
10269 C CA  A MET B 193  ? 0.4612 0.4934 0.3720 0.0001  0.0173  -0.0103 191  MET B CA  
10270 C CA  B MET B 193  ? 0.4611 0.4934 0.3719 0.0000  0.0173  -0.0103 191  MET B CA  
10271 C C   . MET B 193  ? 0.4888 0.5193 0.3952 -0.0032 0.0161  -0.0077 191  MET B C   
10272 O O   . MET B 193  ? 0.4594 0.4861 0.3675 -0.0057 0.0133  -0.0061 191  MET B O   
10273 C CB  A MET B 193  ? 0.4644 0.4897 0.3738 0.0023  0.0149  -0.0133 191  MET B CB  
10274 C CB  B MET B 193  ? 0.4642 0.4897 0.3742 0.0023  0.0149  -0.0133 191  MET B CB  
10275 C CG  A MET B 193  ? 0.4459 0.4719 0.3589 0.0057  0.0159  -0.0160 191  MET B CG  
10276 C CG  B MET B 193  ? 0.4517 0.4778 0.3672 0.0048  0.0153  -0.0153 191  MET B CG  
10277 S SD  A MET B 193  ? 0.4387 0.4563 0.3488 0.0080  0.0131  -0.0195 191  MET B SD  
10278 S SD  B MET B 193  ? 0.4772 0.4948 0.3928 0.0061  0.0117  -0.0179 191  MET B SD  
10279 C CE  A MET B 193  ? 0.5105 0.5239 0.4265 0.0059  0.0095  -0.0185 191  MET B CE  
10280 C CE  B MET B 193  ? 0.4481 0.4625 0.3553 0.0085  0.0121  -0.0205 191  MET B CE  
10281 N N   . GLY B 194  ? 0.4460 0.4789 0.3464 -0.0031 0.0180  -0.0073 192  GLY B N   
10282 C CA  . GLY B 194  ? 0.4463 0.4771 0.3417 -0.0061 0.0168  -0.0048 192  GLY B CA  
10283 C C   . GLY B 194  ? 0.4555 0.4924 0.3517 -0.0092 0.0189  -0.0013 192  GLY B C   
10284 O O   . GLY B 194  ? 0.4516 0.4863 0.3456 -0.0124 0.0173  0.0015  192  GLY B O   
10285 N N   . GLU B 195  ? 0.4191 0.4636 0.3185 -0.0083 0.0223  -0.0012 193  GLU B N   
10286 C CA  . GLU B 195  ? 0.4467 0.4979 0.3464 -0.0112 0.0247  0.0021  193  GLU B CA  
10287 C C   . GLU B 195  ? 0.4590 0.5162 0.3662 -0.0122 0.0260  0.0033  193  GLU B C   
10288 O O   . GLU B 195  ? 0.4239 0.4855 0.3323 -0.0156 0.0270  0.0065  193  GLU B O   
10289 C CB  . GLU B 195  ? 0.4538 0.5103 0.3480 -0.0097 0.0282  0.0019  193  GLU B CB  
10290 N N   . GLN B 196  ? 0.4716 0.5291 0.3840 -0.0095 0.0259  0.0009  194  GLN B N   
10291 C CA  . GLN B 196  ? 0.4419 0.5051 0.3614 -0.0103 0.0270  0.0019  194  GLN B CA  
10292 C C   . GLN B 196  ? 0.4348 0.4931 0.3593 -0.0115 0.0239  0.0018  194  GLN B C   
10293 O O   . GLN B 196  ? 0.4819 0.5421 0.4101 -0.0147 0.0234  0.0042  194  GLN B O   
10294 C CB  . GLN B 196  ? 0.4498 0.5189 0.3716 -0.0061 0.0300  -0.0004 194  GLN B CB  
10295 C CG  . GLN B 196  ? 0.5646 0.6392 0.4941 -0.0064 0.0307  0.0002  194  GLN B CG  
10296 C CD  . GLN B 196  ? 0.5790 0.6583 0.5107 -0.0018 0.0333  -0.0023 194  GLN B CD  
10297 O OE1 . GLN B 196  ? 0.6690 0.7483 0.5963 0.0015  0.0349  -0.0043 194  GLN B OE1 
10298 N NE2 . GLN B 196  ? 0.6553 0.7384 0.5937 -0.0014 0.0335  -0.0022 194  GLN B NE2 
10299 N N   . PHE B 197  ? 0.4382 0.4901 0.3628 -0.0090 0.0218  -0.0009 195  PHE B N   
10300 C CA  . PHE B 197  ? 0.4384 0.4854 0.3673 -0.0100 0.0188  -0.0010 195  PHE B CA  
10301 C C   . PHE B 197  ? 0.4699 0.5118 0.3967 -0.0137 0.0162  0.0014  195  PHE B C   
10302 O O   . PHE B 197  ? 0.4658 0.5054 0.3964 -0.0156 0.0143  0.0024  195  PHE B O   
10303 C CB  . PHE B 197  ? 0.4354 0.4770 0.3646 -0.0066 0.0172  -0.0043 195  PHE B CB  
10304 C CG  . PHE B 197  ? 0.4470 0.4927 0.3789 -0.0030 0.0195  -0.0066 195  PHE B CG  
10305 C CD1 . PHE B 197  ? 0.4990 0.5522 0.4354 -0.0031 0.0218  -0.0056 195  PHE B CD1 
10306 C CD2 . PHE B 197  ? 0.4914 0.5333 0.4210 0.0005  0.0191  -0.0097 195  PHE B CD2 
10307 C CE1 . PHE B 197  ? 0.5363 0.5932 0.4751 0.0005  0.0238  -0.0076 195  PHE B CE1 
10308 C CE2 . PHE B 197  ? 0.5115 0.5566 0.4433 0.0041  0.0211  -0.0118 195  PHE B CE2 
10309 C CZ  . PHE B 197  ? 0.5155 0.5681 0.4519 0.0042  0.0234  -0.0107 195  PHE B CZ  
10310 N N   . VAL B 198  ? 0.4231 0.4628 0.3437 -0.0145 0.0159  0.0022  196  VAL B N   
10311 C CA  . VAL B 198  ? 0.4034 0.4384 0.3213 -0.0178 0.0136  0.0047  196  VAL B CA  
10312 C C   . VAL B 198  ? 0.3811 0.4197 0.2939 -0.0198 0.0155  0.0071  196  VAL B C   
10313 O O   . VAL B 198  ? 0.3902 0.4331 0.3001 -0.0179 0.0181  0.0061  196  VAL B O   
10314 C CB  . VAL B 198  ? 0.3401 0.3669 0.2552 -0.0167 0.0102  0.0034  196  VAL B CB  
10315 C CG1 . VAL B 198  ? 0.4282 0.4518 0.3486 -0.0149 0.0084  0.0012  196  VAL B CG1 
10316 C CG2 . VAL B 198  ? 0.4603 0.4864 0.3696 -0.0143 0.0110  0.0015  196  VAL B CG2 
10317 N N   . THR B 199  ? 0.3751 0.4118 0.2867 -0.0237 0.0142  0.0103  197  THR B N   
10318 C CA  A THR B 199  ? 0.3611 0.4002 0.2673 -0.0259 0.0156  0.0128  197  THR B CA  
10319 C CA  B THR B 199  ? 0.3614 0.4005 0.2676 -0.0260 0.0156  0.0129  197  THR B CA  
10320 C C   . THR B 199  ? 0.3977 0.4317 0.2970 -0.0248 0.0142  0.0121  197  THR B C   
10321 O O   . THR B 199  ? 0.4436 0.4802 0.3375 -0.0253 0.0160  0.0132  197  THR B O   
10322 C CB  A THR B 199  ? 0.3434 0.3816 0.2506 -0.0306 0.0145  0.0166  197  THR B CB  
10323 C CB  B THR B 199  ? 0.3441 0.3817 0.2506 -0.0306 0.0143  0.0166  197  THR B CB  
10324 O OG1 A THR B 199  ? 0.3578 0.4004 0.2717 -0.0315 0.0154  0.0168  197  THR B OG1 
10325 O OG1 B THR B 199  ? 0.3135 0.3434 0.2218 -0.0311 0.0106  0.0165  197  THR B OG1 
10326 C CG2 A THR B 199  ? 0.3380 0.3799 0.2402 -0.0334 0.0164  0.0196  197  THR B CG2 
10327 C CG2 B THR B 199  ? 0.3534 0.3982 0.2649 -0.0327 0.0165  0.0182  197  THR B CG2 
10328 N N   . GLY B 200  ? 0.3364 0.3634 0.2358 -0.0233 0.0110  0.0104  198  GLY B N   
10329 C CA  . GLY B 200  ? 0.3906 0.4127 0.2838 -0.0221 0.0093  0.0095  198  GLY B CA  
10330 C C   . GLY B 200  ? 0.3824 0.3978 0.2779 -0.0205 0.0059  0.0076  198  GLY B C   
10331 O O   . GLY B 200  ? 0.3502 0.3645 0.2516 -0.0208 0.0048  0.0075  198  GLY B O   
10332 N N   . GLU B 201  ? 0.4127 0.4240 0.3035 -0.0189 0.0042  0.0061  199  GLU B N   
10333 C CA  . GLU B 201  ? 0.4314 0.4366 0.3241 -0.0175 0.0008  0.0043  199  GLU B CA  
10334 C C   . GLU B 201  ? 0.4054 0.4054 0.2977 -0.0197 -0.0025 0.0068  199  GLU B C   
10335 O O   . GLU B 201  ? 0.4467 0.4425 0.3425 -0.0190 -0.0052 0.0060  199  GLU B O   
10336 C CB  . GLU B 201  ? 0.4616 0.4646 0.3494 -0.0150 0.0001  0.0017  199  GLU B CB  
10337 C CG  . GLU B 201  ? 0.6015 0.6076 0.4905 -0.0119 0.0025  -0.0017 199  GLU B CG  
10338 C CD  . GLU B 201  ? 0.7160 0.7181 0.6006 -0.0095 0.0010  -0.0045 199  GLU B CD  
10339 O OE1 . GLU B 201  ? 0.6723 0.6709 0.5514 -0.0105 -0.0011 -0.0037 199  GLU B OE1 
10340 O OE2 . GLU B 201  ? 0.7027 0.7051 0.5894 -0.0069 0.0017  -0.0075 199  GLU B OE2 
10341 N N   . THR B 202  ? 0.3301 0.3299 0.2179 -0.0223 -0.0025 0.0099  200  THR B N   
10342 C CA  . THR B 202  ? 0.3690 0.3636 0.2559 -0.0245 -0.0055 0.0126  200  THR B CA  
10343 C C   . THR B 202  ? 0.3260 0.3230 0.2131 -0.0279 -0.0040 0.0160  200  THR B C   
10344 O O   . THR B 202  ? 0.3294 0.3323 0.2158 -0.0287 -0.0007 0.0165  200  THR B O   
10345 C CB  . THR B 202  ? 0.3853 0.3764 0.2650 -0.0247 -0.0074 0.0134  200  THR B CB  
10346 O OG1 . THR B 202  ? 0.3838 0.3786 0.2580 -0.0261 -0.0048 0.0150  200  THR B OG1 
10347 C CG2 . THR B 202  ? 0.4417 0.4311 0.3201 -0.0216 -0.0086 0.0100  200  THR B CG2 
10348 N N   . ILE B 203  ? 0.3202 0.3124 0.2080 -0.0300 -0.0065 0.0184  201  ILE B N   
10349 C CA  . ILE B 203  ? 0.3313 0.3249 0.2194 -0.0335 -0.0055 0.0217  201  ILE B CA  
10350 C C   . ILE B 203  ? 0.3288 0.3244 0.2101 -0.0356 -0.0041 0.0243  201  ILE B C   
10351 O O   . ILE B 203  ? 0.3337 0.3341 0.2148 -0.0380 -0.0015 0.0262  201  ILE B O   
10352 C CB  . ILE B 203  ? 0.3237 0.3111 0.2142 -0.0350 -0.0085 0.0235  201  ILE B CB  
10353 C CG1 . ILE B 203  ? 0.3243 0.3131 0.2155 -0.0389 -0.0074 0.0266  201  ILE B CG1 
10354 C CG2 . ILE B 203  ? 0.3621 0.3431 0.2478 -0.0349 -0.0119 0.0249  201  ILE B CG2 
10355 C CD1 . ILE B 203  ? 0.3164 0.3119 0.2128 -0.0392 -0.0044 0.0256  201  ILE B CD1 
10356 N N   . ARG B 204  ? 0.3753 0.3677 0.2507 -0.0348 -0.0057 0.0244  202  ARG B N   
10357 C CA  . ARG B 204  ? 0.3955 0.3899 0.2641 -0.0368 -0.0042 0.0268  202  ARG B CA  
10358 C C   . ARG B 204  ? 0.3538 0.3560 0.2214 -0.0358 -0.0001 0.0253  202  ARG B C   
10359 O O   . ARG B 204  ? 0.3824 0.3889 0.2470 -0.0381 0.0024  0.0277  202  ARG B O   
10360 C CB  . ARG B 204  ? 0.4314 0.4204 0.2936 -0.0363 -0.0071 0.0275  202  ARG B CB  
10361 C CG  . ARG B 204  ? 0.3838 0.3729 0.2440 -0.0329 -0.0075 0.0240  202  ARG B CG  
10362 C CD  . ARG B 204  ? 0.4731 0.4573 0.3264 -0.0328 -0.0104 0.0250  202  ARG B CD  
10363 N NE  . ARG B 204  ? 0.4144 0.3997 0.2642 -0.0301 -0.0099 0.0218  202  ARG B NE  
10364 C CZ  . ARG B 204  ? 0.4936 0.4823 0.3372 -0.0301 -0.0075 0.0217  202  ARG B CZ  
10365 N NH1 . ARG B 204  ? 0.4854 0.4770 0.3254 -0.0328 -0.0053 0.0249  202  ARG B NH1 
10366 N NH2 . ARG B 204  ? 0.4712 0.4602 0.3117 -0.0274 -0.0073 0.0184  202  ARG B NH2 
10367 N N   . GLU B 205  ? 0.3505 0.3546 0.2206 -0.0323 0.0008  0.0214  203  GLU B N   
10368 C CA  . GLU B 205  ? 0.3786 0.3899 0.2481 -0.0309 0.0048  0.0198  203  GLU B CA  
10369 C C   . GLU B 205  ? 0.3690 0.3863 0.2442 -0.0325 0.0075  0.0209  203  GLU B C   
10370 O O   . GLU B 205  ? 0.3705 0.3944 0.2441 -0.0336 0.0109  0.0221  203  GLU B O   
10371 C CB  . GLU B 205  ? 0.3916 0.4027 0.2625 -0.0267 0.0048  0.0154  203  GLU B CB  
10372 C CG  . GLU B 205  ? 0.3990 0.4173 0.2702 -0.0247 0.0090  0.0134  203  GLU B CG  
10373 C CD  . GLU B 205  ? 0.5526 0.5696 0.4237 -0.0206 0.0088  0.0090  203  GLU B CD  
10374 O OE1 . GLU B 205  ? 0.5340 0.5491 0.4108 -0.0190 0.0075  0.0071  203  GLU B OE1 
10375 O OE2 . GLU B 205  ? 0.7023 0.7200 0.5673 -0.0189 0.0100  0.0076  203  GLU B OE2 
10376 N N   . ALA B 206  ? 0.3111 0.3267 0.1929 -0.0327 0.0061  0.0205  204  ALA B N   
10377 C CA  . ALA B 206  ? 0.3030 0.3239 0.1902 -0.0346 0.0082  0.0217  204  ALA B CA  
10378 C C   . ALA B 206  ? 0.3602 0.3825 0.2449 -0.0390 0.0089  0.0260  204  ALA B C   
10379 O O   . ALA B 206  ? 0.3445 0.3740 0.2305 -0.0406 0.0120  0.0273  204  ALA B O   
10380 C CB  . ALA B 206  ? 0.3290 0.3464 0.2228 -0.0342 0.0060  0.0206  204  ALA B CB  
10381 N N   . LEU B 207  ? 0.3052 0.3208 0.1863 -0.0411 0.0060  0.0283  205  LEU B N   
10382 C CA  . LEU B 207  ? 0.3345 0.3506 0.2126 -0.0456 0.0064  0.0326  205  LEU B CA  
10383 C C   . LEU B 207  ? 0.3784 0.4004 0.2509 -0.0461 0.0095  0.0338  205  LEU B C   
10384 O O   . LEU B 207  ? 0.3732 0.4005 0.2457 -0.0493 0.0119  0.0366  205  LEU B O   
10385 C CB  . LEU B 207  ? 0.3554 0.3624 0.2300 -0.0471 0.0024  0.0348  205  LEU B CB  
10386 C CG  . LEU B 207  ? 0.3619 0.3633 0.2418 -0.0475 -0.0004 0.0347  205  LEU B CG  
10387 C CD1 . LEU B 207  ? 0.4011 0.3934 0.2776 -0.0474 -0.0044 0.0358  205  LEU B CD1 
10388 C CD2 . LEU B 207  ? 0.3362 0.3397 0.2191 -0.0516 0.0006  0.0374  205  LEU B CD2 
10389 N N   . LYS B 208  ? 0.3239 0.3453 0.1916 -0.0432 0.0097  0.0318  206  LYS B N   
10390 C CA  . LYS B 208  ? 0.3708 0.3978 0.2328 -0.0433 0.0129  0.0326  206  LYS B CA  
10391 C C   . LYS B 208  ? 0.3849 0.4216 0.2510 -0.0425 0.0172  0.0314  206  LYS B C   
10392 O O   . LYS B 208  ? 0.4316 0.4747 0.2955 -0.0445 0.0203  0.0337  206  LYS B O   
10393 C CB  . LYS B 208  ? 0.4189 0.4428 0.2749 -0.0401 0.0120  0.0301  206  LYS B CB  
10394 N N   . ARG B 209  ? 0.3783 0.4163 0.2503 -0.0394 0.0174  0.0280  207  ARG B N   
10395 C CA  . ARG B 209  ? 0.4005 0.4476 0.2766 -0.0380 0.0213  0.0268  207  ARG B CA  
10396 C C   . ARG B 209  ? 0.4238 0.4758 0.3053 -0.0417 0.0224  0.0297  207  ARG B C   
10397 O O   . ARG B 209  ? 0.4251 0.4858 0.3094 -0.0415 0.0259  0.0297  207  ARG B O   
10398 C CB  . ARG B 209  ? 0.3870 0.4335 0.2674 -0.0336 0.0211  0.0224  207  ARG B CB  
10399 C CG  . ARG B 209  ? 0.3896 0.4328 0.2646 -0.0297 0.0206  0.0193  207  ARG B CG  
10400 C CD  . ARG B 209  ? 0.4246 0.4677 0.3042 -0.0256 0.0207  0.0152  207  ARG B CD  
10401 N NE  . ARG B 209  ? 0.5351 0.5744 0.4098 -0.0221 0.0200  0.0119  207  ARG B NE  
10402 C CZ  . ARG B 209  ? 0.5584 0.5955 0.4359 -0.0186 0.0192  0.0083  207  ARG B CZ  
10403 N NH1 . ARG B 209  ? 0.4414 0.4798 0.3263 -0.0180 0.0191  0.0074  207  ARG B NH1 
10404 N NH2 . ARG B 209  ? 0.6037 0.6372 0.4761 -0.0158 0.0185  0.0055  207  ARG B NH2 
10405 N N   . SER B 210  ? 0.3496 0.3960 0.2322 -0.0452 0.0195  0.0321  208  SER B N   
10406 C CA  . SER B 210  ? 0.3684 0.4184 0.2560 -0.0490 0.0201  0.0347  208  SER B CA  
10407 C C   . SER B 210  ? 0.3726 0.4277 0.2568 -0.0532 0.0223  0.0389  208  SER B C   
10408 O O   . SER B 210  ? 0.3615 0.4220 0.2498 -0.0564 0.0237  0.0410  208  SER B O   
10409 C CB  . SER B 210  ? 0.2970 0.3383 0.1868 -0.0509 0.0161  0.0355  208  SER B CB  
10410 O OG  . SER B 210  ? 0.3734 0.4115 0.2674 -0.0472 0.0144  0.0318  208  SER B OG  
10411 N N   . LYS B 211  ? 0.3732 0.4270 0.2499 -0.0535 0.0227  0.0401  209  LYS B N   
10412 C CA  . LYS B 211  ? 0.3935 0.4515 0.2665 -0.0578 0.0246  0.0444  209  LYS B CA  
10413 C C   . LYS B 211  ? 0.3872 0.4573 0.2636 -0.0582 0.0291  0.0449  209  LYS B C   
10414 O O   . LYS B 211  ? 0.4449 0.5195 0.3226 -0.0627 0.0304  0.0485  209  LYS B O   
10415 C CB  . LYS B 211  ? 0.4125 0.4676 0.2767 -0.0572 0.0246  0.0451  209  LYS B CB  
10416 N N   . GLU B 212  ? 0.3979 0.4732 0.2759 -0.0534 0.0316  0.0413  210  GLU B N   
10417 C CA  . GLU B 212  ? 0.4033 0.4906 0.2839 -0.0531 0.0362  0.0416  210  GLU B CA  
10418 C C   . GLU B 212  ? 0.3901 0.4827 0.2785 -0.0561 0.0366  0.0432  210  GLU B C   
10419 O O   . GLU B 212  ? 0.3844 0.4850 0.2739 -0.0596 0.0391  0.0465  210  GLU B O   
10420 C CB  . GLU B 212  ? 0.4847 0.5751 0.3657 -0.0469 0.0382  0.0370  210  GLU B CB  
10421 C CG  . GLU B 212  ? 0.5715 0.6743 0.4561 -0.0456 0.0429  0.0368  210  GLU B CG  
10422 C CD  . GLU B 212  ? 0.6051 0.7096 0.4923 -0.0395 0.0441  0.0321  210  GLU B CD  
10423 O OE1 . GLU B 212  ? 0.7164 0.8125 0.6019 -0.0365 0.0414  0.0290  210  GLU B OE1 
10424 O OE2 . GLU B 212  ? 0.7274 0.8416 0.6184 -0.0377 0.0477  0.0315  210  GLU B OE2 
10425 N N   . LEU B 213  ? 0.3526 0.4412 0.2467 -0.0548 0.0342  0.0410  211  LEU B N   
10426 C CA  . LEU B 213  ? 0.3801 0.4734 0.2816 -0.0576 0.0343  0.0424  211  LEU B CA  
10427 C C   . LEU B 213  ? 0.3634 0.4517 0.2643 -0.0637 0.0317  0.0463  211  LEU B C   
10428 O O   . LEU B 213  ? 0.3411 0.4352 0.2462 -0.0676 0.0326  0.0489  211  LEU B O   
10429 C CB  . LEU B 213  ? 0.3018 0.3933 0.2094 -0.0540 0.0330  0.0386  211  LEU B CB  
10430 C CG  . LEU B 213  ? 0.3495 0.4481 0.2591 -0.0486 0.0361  0.0352  211  LEU B CG  
10431 C CD1 . LEU B 213  ? 0.3709 0.4684 0.2871 -0.0456 0.0348  0.0320  211  LEU B CD1 
10432 C CD2 . LEU B 213  ? 0.4096 0.5208 0.3208 -0.0497 0.0404  0.0372  211  LEU B CD2 
10433 N N   . GLU B 214  ? 0.3343 0.4121 0.2300 -0.0646 0.0285  0.0470  212  GLU B N   
10434 C CA  . GLU B 214  ? 0.3375 0.4101 0.2318 -0.0702 0.0262  0.0510  212  GLU B CA  
10435 C C   . GLU B 214  ? 0.3798 0.4594 0.2714 -0.0748 0.0288  0.0553  212  GLU B C   
10436 O O   . GLU B 214  ? 0.3798 0.4611 0.2739 -0.0798 0.0285  0.0585  212  GLU B O   
10437 C CB  . GLU B 214  ? 0.3721 0.4324 0.2611 -0.0699 0.0223  0.0510  212  GLU B CB  
10438 C CG  . GLU B 214  ? 0.3549 0.4075 0.2477 -0.0673 0.0190  0.0479  212  GLU B CG  
10439 C CD  . GLU B 214  ? 0.3836 0.4245 0.2717 -0.0672 0.0151  0.0483  212  GLU B CD  
10440 O OE1 . GLU B 214  ? 0.4332 0.4719 0.3147 -0.0681 0.0150  0.0502  212  GLU B OE1 
10441 O OE2 . GLU B 214  ? 0.3643 0.3984 0.2553 -0.0661 0.0122  0.0466  212  GLU B OE2 
10442 N N   . GLU B 215  ? 0.3616 0.4456 0.2481 -0.0731 0.0316  0.0554  213  GLU B N   
10443 C CA  . GLU B 215  ? 0.3569 0.4488 0.2409 -0.0771 0.0346  0.0595  213  GLU B CA  
10444 C C   . GLU B 215  ? 0.3878 0.4916 0.2788 -0.0788 0.0376  0.0604  213  GLU B C   
10445 O O   . GLU B 215  ? 0.4021 0.5116 0.2928 -0.0837 0.0393  0.0645  213  GLU B O   
10446 C CB  . GLU B 215  ? 0.4468 0.5415 0.3240 -0.0742 0.0373  0.0589  213  GLU B CB  
10447 C CG  . GLU B 215  ? 0.4812 0.5650 0.3506 -0.0737 0.0343  0.0591  213  GLU B CG  
10448 C CD  . GLU B 215  ? 0.6666 0.7533 0.5287 -0.0713 0.0369  0.0587  213  GLU B CD  
10449 O OE1 . GLU B 215  ? 0.7290 0.8251 0.5898 -0.0731 0.0407  0.0610  213  GLU B OE1 
10450 O OE2 . GLU B 215  ? 0.6992 0.7790 0.5569 -0.0677 0.0350  0.0560  213  GLU B OE2 
10451 N N   . LYS B 216  ? 0.3646 0.4722 0.2619 -0.0748 0.0383  0.0568  214  LYS B N   
10452 C CA  . LYS B 216  ? 0.3923 0.5111 0.2969 -0.0762 0.0408  0.0576  214  LYS B CA  
10453 C C   . LYS B 216  ? 0.4088 0.5244 0.3186 -0.0806 0.0379  0.0590  214  LYS B C   
10454 O O   . LYS B 216  ? 0.3853 0.5099 0.3009 -0.0829 0.0395  0.0604  214  LYS B O   
10455 C CB  . LYS B 216  ? 0.4036 0.5284 0.3125 -0.0700 0.0430  0.0532  214  LYS B CB  
10456 C CG  . LYS B 216  ? 0.4460 0.5759 0.3503 -0.0656 0.0465  0.0516  214  LYS B CG  
10457 C CD  . LYS B 216  ? 0.5152 0.6495 0.4239 -0.0593 0.0482  0.0471  214  LYS B CD  
10458 C CE  . LYS B 216  ? 0.6092 0.7464 0.5126 -0.0544 0.0513  0.0449  214  LYS B CE  
10459 N NZ  . LYS B 216  ? 0.5991 0.7308 0.5027 -0.0482 0.0502  0.0399  214  LYS B NZ  
10460 N N   . GLY B 217  ? 0.3750 0.4782 0.2828 -0.0815 0.0336  0.0587  215  GLY B N   
10461 C CA  . GLY B 217  ? 0.3132 0.4121 0.2252 -0.0855 0.0307  0.0599  215  GLY B CA  
10462 C C   . GLY B 217  ? 0.3699 0.4628 0.2860 -0.0818 0.0281  0.0559  215  GLY B C   
10463 O O   . GLY B 217  ? 0.3511 0.4406 0.2707 -0.0847 0.0257  0.0565  215  GLY B O   
10464 N N   . PHE B 218  ? 0.3296 0.4212 0.2452 -0.0757 0.0285  0.0520  216  PHE B N   
10465 C CA  . PHE B 218  ? 0.3071 0.3914 0.2255 -0.0725 0.0257  0.0484  216  PHE B CA  
10466 C C   . PHE B 218  ? 0.3170 0.3882 0.2308 -0.0734 0.0218  0.0489  216  PHE B C   
10467 O O   . PHE B 218  ? 0.3276 0.3951 0.2352 -0.0753 0.0214  0.0512  216  PHE B O   
10468 C CB  . PHE B 218  ? 0.3008 0.3872 0.2198 -0.0658 0.0272  0.0442  216  PHE B CB  
10469 C CG  . PHE B 218  ? 0.3300 0.4282 0.2545 -0.0637 0.0306  0.0430  216  PHE B CG  
10470 C CD1 . PHE B 218  ? 0.3359 0.4442 0.2592 -0.0640 0.0345  0.0445  216  PHE B CD1 
10471 C CD2 . PHE B 218  ? 0.3307 0.4300 0.2615 -0.0613 0.0300  0.0403  216  PHE B CD2 
10472 C CE1 . PHE B 218  ? 0.3468 0.4661 0.2752 -0.0617 0.0377  0.0435  216  PHE B CE1 
10473 C CE2 . PHE B 218  ? 0.3600 0.4701 0.2958 -0.0592 0.0330  0.0393  216  PHE B CE2 
10474 C CZ  . PHE B 218  ? 0.3149 0.4352 0.2497 -0.0593 0.0369  0.0409  216  PHE B CZ  
10475 N N   . SER B 219  ? 0.3119 0.3761 0.2286 -0.0721 0.0189  0.0467  217  SER B N   
10476 C CA  . SER B 219  ? 0.3100 0.3621 0.2231 -0.0714 0.0152  0.0462  217  SER B CA  
10477 C C   . SER B 219  ? 0.2871 0.3363 0.2027 -0.0657 0.0143  0.0417  217  SER B C   
10478 O O   . SER B 219  ? 0.2728 0.3289 0.1926 -0.0627 0.0164  0.0392  217  SER B O   
10479 C CB  . SER B 219  ? 0.3091 0.3544 0.2231 -0.0759 0.0122  0.0483  217  SER B CB  
10480 O OG  . SER B 219  ? 0.3375 0.3852 0.2580 -0.0758 0.0119  0.0467  217  SER B OG  
10481 N N   . TYR B 220  ? 0.2921 0.3311 0.2053 -0.0643 0.0111  0.0406  218  TYR B N   
10482 C CA  . TYR B 220  ? 0.2783 0.3142 0.1932 -0.0591 0.0101  0.0366  218  TYR B CA  
10483 C C   . TYR B 220  ? 0.2497 0.2762 0.1661 -0.0590 0.0065  0.0358  218  TYR B C   
10484 O O   . TYR B 220  ? 0.2992 0.3190 0.2130 -0.0621 0.0042  0.0382  218  TYR B O   
10485 C CB  . TYR B 220  ? 0.2634 0.2971 0.1729 -0.0560 0.0102  0.0356  218  TYR B CB  
10486 C CG  . TYR B 220  ? 0.2788 0.3215 0.1878 -0.0538 0.0139  0.0344  218  TYR B CG  
10487 C CD1 . TYR B 220  ? 0.3022 0.3511 0.2082 -0.0564 0.0165  0.0372  218  TYR B CD1 
10488 C CD2 . TYR B 220  ? 0.2533 0.2984 0.1650 -0.0490 0.0149  0.0306  218  TYR B CD2 
10489 C CE1 . TYR B 220  ? 0.2985 0.3557 0.2039 -0.0540 0.0201  0.0361  218  TYR B CE1 
10490 C CE2 . TYR B 220  ? 0.2880 0.3409 0.1991 -0.0466 0.0183  0.0294  218  TYR B CE2 
10491 C CZ  . TYR B 220  ? 0.2675 0.3266 0.1755 -0.0490 0.0210  0.0321  218  TYR B CZ  
10492 O OH  . TYR B 220  ? 0.3471 0.4141 0.2543 -0.0464 0.0245  0.0309  218  TYR B OH  
10493 N N   . SER B 221  ? 0.2396 0.2655 0.1600 -0.0552 0.0060  0.0323  219  SER B N   
10494 C CA  . SER B 221  ? 0.2481 0.2653 0.1698 -0.0538 0.0028  0.0308  219  SER B CA  
10495 C C   . SER B 221  ? 0.2701 0.2866 0.1923 -0.0486 0.0026  0.0273  219  SER B C   
10496 O O   . SER B 221  ? 0.2903 0.3124 0.2160 -0.0461 0.0045  0.0250  219  SER B O   
10497 C CB  . SER B 221  ? 0.2830 0.3010 0.2103 -0.0550 0.0023  0.0303  219  SER B CB  
10498 O OG  . SER B 221  ? 0.2806 0.2903 0.2089 -0.0534 -0.0007 0.0287  219  SER B OG  
10499 N N   . TYR B 222  ? 0.2576 0.2669 0.1761 -0.0472 0.0004  0.0271  220  TYR B N   
10500 C CA  . TYR B 222  ? 0.2599 0.2683 0.1780 -0.0427 0.0001  0.0240  220  TYR B CA  
10501 C C   . TYR B 222  ? 0.2606 0.2648 0.1830 -0.0402 -0.0019 0.0215  220  TYR B C   
10502 O O   . TYR B 222  ? 0.2859 0.2841 0.2090 -0.0414 -0.0043 0.0223  220  TYR B O   
10503 C CB  . TYR B 222  ? 0.2490 0.2527 0.1609 -0.0424 -0.0014 0.0251  220  TYR B CB  
10504 C CG  . TYR B 222  ? 0.2494 0.2579 0.1568 -0.0446 0.0009  0.0274  220  TYR B CG  
10505 C CD1 . TYR B 222  ? 0.2654 0.2806 0.1720 -0.0425 0.0038  0.0258  220  TYR B CD1 
10506 C CD2 . TYR B 222  ? 0.2713 0.2778 0.1753 -0.0487 0.0004  0.0311  220  TYR B CD2 
10507 C CE1 . TYR B 222  ? 0.2629 0.2830 0.1655 -0.0443 0.0062  0.0279  220  TYR B CE1 
10508 C CE2 . TYR B 222  ? 0.2815 0.2930 0.1815 -0.0508 0.0027  0.0334  220  TYR B CE2 
10509 C CZ  . TYR B 222  ? 0.2776 0.2961 0.1770 -0.0485 0.0057  0.0317  220  TYR B CZ  
10510 O OH  . TYR B 222  ? 0.2974 0.3213 0.1928 -0.0504 0.0082  0.0339  220  TYR B OH  
10511 N N   . ASP B 223  ? 0.2622 0.2694 0.1871 -0.0365 -0.0009 0.0184  221  ASP B N   
10512 C CA  . ASP B 223  ? 0.2910 0.2952 0.2201 -0.0338 -0.0023 0.0157  221  ASP B CA  
10513 C C   . ASP B 223  ? 0.3193 0.3206 0.2462 -0.0305 -0.0034 0.0137  221  ASP B C   
10514 O O   . ASP B 223  ? 0.3410 0.3463 0.2669 -0.0285 -0.0017 0.0121  221  ASP B O   
10515 C CB  . ASP B 223  ? 0.3177 0.3282 0.2519 -0.0326 -0.0002 0.0139  221  ASP B CB  
10516 C CG  . ASP B 223  ? 0.3486 0.3570 0.2867 -0.0293 -0.0012 0.0109  221  ASP B CG  
10517 O OD1 . ASP B 223  ? 0.3585 0.3605 0.2966 -0.0286 -0.0038 0.0106  221  ASP B OD1 
10518 O OD2 . ASP B 223  ? 0.3918 0.4051 0.3329 -0.0273 0.0006  0.0090  221  ASP B OD2 
10519 N N   . MET B 224  ? 0.2765 0.2711 0.2026 -0.0300 -0.0064 0.0138  222  MET B N   
10520 C CA  . MET B 224  ? 0.3335 0.3250 0.2575 -0.0273 -0.0079 0.0122  222  MET B CA  
10521 C C   . MET B 224  ? 0.3726 0.3646 0.3010 -0.0240 -0.0081 0.0090  222  MET B C   
10522 O O   . MET B 224  ? 0.4040 0.3931 0.3315 -0.0219 -0.0097 0.0076  222  MET B O   
10523 C CB  . MET B 224  ? 0.3673 0.3518 0.2887 -0.0279 -0.0111 0.0139  222  MET B CB  
10524 C CG  . MET B 224  ? 0.3241 0.3074 0.2405 -0.0311 -0.0112 0.0172  222  MET B CG  
10525 S SD  . MET B 224  ? 0.3776 0.3665 0.2888 -0.0314 -0.0085 0.0175  222  MET B SD  
10526 C CE  . MET B 224  ? 0.3992 0.3849 0.3077 -0.0280 -0.0105 0.0154  222  MET B CE  
10527 N N   . LEU B 225  ? 0.3513 0.3467 0.2844 -0.0238 -0.0066 0.0080  223  LEU B N   
10528 C CA  . LEU B 225  ? 0.3412 0.3384 0.2786 -0.0210 -0.0060 0.0051  223  LEU B CA  
10529 C C   . LEU B 225  ? 0.4117 0.4042 0.3524 -0.0197 -0.0083 0.0040  223  LEU B C   
10530 O O   . LEU B 225  ? 0.4344 0.4281 0.3787 -0.0175 -0.0080 0.0018  223  LEU B O   
10531 C CB  . LEU B 225  ? 0.3783 0.3773 0.3135 -0.0184 -0.0051 0.0030  223  LEU B CB  
10532 C CG  . LEU B 225  ? 0.4323 0.4364 0.3641 -0.0190 -0.0024 0.0035  223  LEU B CG  
10533 C CD1 . LEU B 225  ? 0.4534 0.4581 0.3826 -0.0162 -0.0019 0.0012  223  LEU B CD1 
10534 C CD2 . LEU B 225  ? 0.4154 0.4256 0.3508 -0.0197 0.0002  0.0038  223  LEU B CD2 
10535 N N   . GLY B 226  ? 0.3494 0.3367 0.2892 -0.0209 -0.0106 0.0056  224  GLY B N   
10536 C CA  . GLY B 226  ? 0.3739 0.3573 0.3172 -0.0196 -0.0126 0.0047  224  GLY B CA  
10537 C C   . GLY B 226  ? 0.3372 0.3225 0.2852 -0.0197 -0.0116 0.0039  224  GLY B C   
10538 O O   . GLY B 226  ? 0.3258 0.3131 0.2740 -0.0220 -0.0104 0.0052  224  GLY B O   
10539 N N   . GLU B 227  ? 0.2970 0.2821 0.2488 -0.0174 -0.0120 0.0018  225  GLU B N   
10540 C CA  . GLU B 227  ? 0.2969 0.2836 0.2530 -0.0174 -0.0111 0.0010  225  GLU B CA  
10541 C C   . GLU B 227  ? 0.2682 0.2529 0.2277 -0.0148 -0.0122 -0.0010 225  GLU B C   
10542 O O   . GLU B 227  ? 0.3229 0.3077 0.2823 -0.0128 -0.0127 -0.0023 225  GLU B O   
10543 C CB  . GLU B 227  ? 0.3258 0.3188 0.2831 -0.0174 -0.0084 0.0002  225  GLU B CB  
10544 C CG  . GLU B 227  ? 0.3513 0.3466 0.3128 -0.0176 -0.0076 -0.0004 225  GLU B CG  
10545 C CD  . GLU B 227  ? 0.3847 0.3866 0.3473 -0.0178 -0.0050 -0.0007 225  GLU B CD  
10546 O OE1 . GLU B 227  ? 0.3712 0.3758 0.3309 -0.0183 -0.0038 0.0000  225  GLU B OE1 
10547 O OE2 . GLU B 227  ? 0.4333 0.4378 0.3995 -0.0174 -0.0042 -0.0015 225  GLU B OE2 
10548 N N   . ALA B 228  ? 0.2476 0.2307 0.2101 -0.0150 -0.0127 -0.0011 226  ALA B N   
10549 C CA  . ALA B 228  ? 0.2694 0.2517 0.2357 -0.0127 -0.0133 -0.0030 226  ALA B CA  
10550 C C   . ALA B 228  ? 0.2658 0.2453 0.2317 -0.0108 -0.0151 -0.0035 226  ALA B C   
10551 O O   . ALA B 228  ? 0.2945 0.2756 0.2618 -0.0089 -0.0149 -0.0051 226  ALA B O   
10552 C CB  . ALA B 228  ? 0.2868 0.2740 0.2558 -0.0115 -0.0113 -0.0046 226  ALA B CB  
10553 N N   . ALA B 229  ? 0.2412 0.2165 0.2050 -0.0114 -0.0169 -0.0020 227  ALA B N   
10554 C CA  . ALA B 229  ? 0.2510 0.2236 0.2149 -0.0096 -0.0190 -0.0023 227  ALA B CA  
10555 C C   . ALA B 229  ? 0.2313 0.2043 0.1999 -0.0075 -0.0191 -0.0041 227  ALA B C   
10556 O O   . ALA B 229  ? 0.2562 0.2288 0.2272 -0.0075 -0.0186 -0.0044 227  ALA B O   
10557 C CB  . ALA B 229  ? 0.2535 0.2212 0.2153 -0.0103 -0.0209 -0.0004 227  ALA B CB  
10558 N N   . THR B 230  ? 0.2474 0.2211 0.2169 -0.0059 -0.0198 -0.0052 228  THR B N   
10559 C CA  . THR B 230  ? 0.2603 0.2345 0.2340 -0.0040 -0.0202 -0.0067 228  THR B CA  
10560 C C   . THR B 230  ? 0.2623 0.2335 0.2370 -0.0028 -0.0224 -0.0061 228  THR B C   
10561 O O   . THR B 230  ? 0.2563 0.2271 0.2346 -0.0015 -0.0227 -0.0067 228  THR B O   
10562 C CB  . THR B 230  ? 0.2594 0.2364 0.2337 -0.0030 -0.0195 -0.0083 228  THR B CB  
10563 O OG1 . THR B 230  ? 0.3191 0.2989 0.2923 -0.0038 -0.0174 -0.0087 228  THR B OG1 
10564 C CG2 . THR B 230  ? 0.2460 0.2239 0.2249 -0.0014 -0.0196 -0.0097 228  THR B CG2 
10565 N N   . THR B 231  ? 0.2400 0.2093 0.2115 -0.0032 -0.0241 -0.0049 229  THR B N   
10566 C CA  . THR B 231  ? 0.2203 0.1872 0.1927 -0.0019 -0.0264 -0.0041 229  THR B CA  
10567 C C   . THR B 231  ? 0.2143 0.1776 0.1832 -0.0030 -0.0276 -0.0020 229  THR B C   
10568 O O   . THR B 231  ? 0.2348 0.1978 0.2001 -0.0048 -0.0267 -0.0011 229  THR B O   
10569 C CB  . THR B 231  ? 0.2418 0.2098 0.2139 -0.0012 -0.0279 -0.0046 229  THR B CB  
10570 O OG1 . THR B 231  ? 0.2673 0.2349 0.2344 -0.0026 -0.0282 -0.0038 229  THR B OG1 
10571 C CG2 . THR B 231  ? 0.2407 0.2119 0.2155 -0.0006 -0.0267 -0.0067 229  THR B CG2 
10572 N N   . ALA B 232  ? 0.2329 0.1935 0.2028 -0.0016 -0.0296 -0.0011 230  ALA B N   
10573 C CA  . ALA B 232  ? 0.2515 0.2081 0.2178 -0.0023 -0.0311 0.0010  230  ALA B CA  
10574 C C   . ALA B 232  ? 0.2651 0.2218 0.2268 -0.0036 -0.0318 0.0020  230  ALA B C   
10575 O O   . ALA B 232  ? 0.2823 0.2368 0.2399 -0.0053 -0.0319 0.0037  230  ALA B O   
10576 C CB  . ALA B 232  ? 0.2542 0.2084 0.2227 -0.0001 -0.0333 0.0017  230  ALA B CB  
10577 N N   . ALA B 233  ? 0.2523 0.2116 0.2144 -0.0030 -0.0324 0.0010  231  ALA B N   
10578 C CA  . ALA B 233  ? 0.2637 0.2233 0.2211 -0.0041 -0.0331 0.0018  231  ALA B CA  
10579 C C   . ALA B 233  ? 0.2797 0.2407 0.2338 -0.0061 -0.0307 0.0017  231  ALA B C   
10580 O O   . ALA B 233  ? 0.2619 0.2220 0.2112 -0.0075 -0.0309 0.0031  231  ALA B O   
10581 C CB  . ALA B 233  ? 0.2803 0.2422 0.2387 -0.0031 -0.0342 0.0004  231  ALA B CB  
10582 N N   . ASP B 234  ? 0.2387 0.2025 0.1955 -0.0061 -0.0284 0.0000  232  ASP B N   
10583 C CA  . ASP B 234  ? 0.2491 0.2150 0.2036 -0.0078 -0.0260 0.0001  232  ASP B CA  
10584 C C   . ASP B 234  ? 0.2508 0.2142 0.2028 -0.0097 -0.0259 0.0023  232  ASP B C   
10585 O O   . ASP B 234  ? 0.2439 0.2076 0.1917 -0.0115 -0.0252 0.0035  232  ASP B O   
10586 C CB  . ASP B 234  ? 0.2763 0.2451 0.2347 -0.0074 -0.0238 -0.0017 232  ASP B CB  
10587 C CG  . ASP B 234  ? 0.3154 0.2869 0.2756 -0.0060 -0.0234 -0.0039 232  ASP B CG  
10588 O OD1 . ASP B 234  ? 0.3262 0.2979 0.2836 -0.0058 -0.0242 -0.0042 232  ASP B OD1 
10589 O OD2 . ASP B 234  ? 0.3272 0.3005 0.2913 -0.0051 -0.0223 -0.0053 232  ASP B OD2 
10590 N N   . ALA B 235  ? 0.2426 0.2034 0.1971 -0.0094 -0.0264 0.0027  233  ALA B N   
10591 C CA  . ALA B 235  ? 0.2424 0.2002 0.1947 -0.0113 -0.0264 0.0046  233  ALA B CA  
10592 C C   . ALA B 235  ? 0.2431 0.1974 0.1907 -0.0122 -0.0282 0.0069  233  ALA B C   
10593 O O   . ALA B 235  ? 0.2618 0.2152 0.2058 -0.0145 -0.0277 0.0087  233  ALA B O   
10594 C CB  . ALA B 235  ? 0.2531 0.2081 0.2087 -0.0104 -0.0269 0.0044  233  ALA B CB  
10595 N N   . GLU B 236  ? 0.2417 0.1944 0.1895 -0.0103 -0.0305 0.0071  234  GLU B N   
10596 C CA  . GLU B 236  ? 0.2747 0.2241 0.2180 -0.0109 -0.0325 0.0093  234  GLU B CA  
10597 C C   . GLU B 236  ? 0.2952 0.2471 0.2339 -0.0126 -0.0316 0.0098  234  GLU B C   
10598 O O   . GLU B 236  ? 0.2769 0.2267 0.2111 -0.0145 -0.0319 0.0121  234  GLU B O   
10599 C CB  . GLU B 236  ? 0.2809 0.2289 0.2258 -0.0085 -0.0352 0.0093  234  GLU B CB  
10600 C CG  . GLU B 236  ? 0.3361 0.2800 0.2768 -0.0087 -0.0376 0.0118  234  GLU B CG  
10601 C CD  . GLU B 236  ? 0.4314 0.3744 0.3743 -0.0061 -0.0404 0.0118  234  GLU B CD  
10602 O OE1 . GLU B 236  ? 0.5192 0.4650 0.4669 -0.0043 -0.0402 0.0098  234  GLU B OE1 
10603 O OE2 . GLU B 236  ? 0.4881 0.4277 0.4281 -0.0060 -0.0427 0.0140  234  GLU B OE2 
10604 N N   . ARG B 237  ? 0.2491 0.2051 0.1888 -0.0119 -0.0305 0.0078  235  ARG B N   
10605 C CA  . ARG B 237  ? 0.2825 0.2410 0.2178 -0.0132 -0.0294 0.0079  235  ARG B CA  
10606 C C   . ARG B 237  ? 0.2799 0.2399 0.2133 -0.0156 -0.0269 0.0089  235  ARG B C   
10607 O O   . ARG B 237  ? 0.2828 0.2424 0.2113 -0.0174 -0.0267 0.0108  235  ARG B O   
10608 C CB  . ARG B 237  ? 0.3187 0.2810 0.2556 -0.0118 -0.0285 0.0052  235  ARG B CB  
10609 C CG  . ARG B 237  ? 0.3502 0.3147 0.2821 -0.0127 -0.0273 0.0051  235  ARG B CG  
10610 C CD  . ARG B 237  ? 0.4355 0.4034 0.3689 -0.0113 -0.0261 0.0023  235  ARG B CD  
10611 N NE  . ARG B 237  ? 0.4762 0.4458 0.4043 -0.0120 -0.0249 0.0021  235  ARG B NE  
10612 C CZ  . ARG B 237  ? 0.4950 0.4662 0.4219 -0.0108 -0.0246 0.0000  235  ARG B CZ  
10613 N NH1 . ARG B 237  ? 0.5425 0.5138 0.4733 -0.0092 -0.0254 -0.0021 235  ARG B NH1 
10614 N NH2 . ARG B 237  ? 0.4916 0.4641 0.4131 -0.0114 -0.0234 -0.0001 235  ARG B NH2 
10615 N N   . TYR B 238  ? 0.2551 0.2169 0.1923 -0.0158 -0.0251 0.0079  236  TYR B N   
10616 C CA  . TYR B 238  ? 0.2498 0.2137 0.1858 -0.0182 -0.0228 0.0089  236  TYR B CA  
10617 C C   . TYR B 238  ? 0.2693 0.2289 0.2022 -0.0204 -0.0239 0.0118  236  TYR B C   
10618 O O   . TYR B 238  ? 0.2596 0.2205 0.1890 -0.0229 -0.0227 0.0135  236  TYR B O   
10619 C CB  . TYR B 238  ? 0.2535 0.2198 0.1944 -0.0179 -0.0211 0.0073  236  TYR B CB  
10620 C CG  . TYR B 238  ? 0.2612 0.2320 0.2048 -0.0161 -0.0196 0.0047  236  TYR B CG  
10621 C CD1 . TYR B 238  ? 0.3064 0.2799 0.2473 -0.0156 -0.0188 0.0039  236  TYR B CD1 
10622 C CD2 . TYR B 238  ? 0.2617 0.2335 0.2103 -0.0148 -0.0191 0.0029  236  TYR B CD2 
10623 C CE1 . TYR B 238  ? 0.3688 0.3457 0.3120 -0.0139 -0.0175 0.0014  236  TYR B CE1 
10624 C CE2 . TYR B 238  ? 0.2879 0.2633 0.2389 -0.0132 -0.0178 0.0006  236  TYR B CE2 
10625 C CZ  . TYR B 238  ? 0.3737 0.3516 0.3221 -0.0127 -0.0170 -0.0001 236  TYR B CZ  
10626 O OH  . TYR B 238  ? 0.3995 0.3802 0.3500 -0.0109 -0.0159 -0.0025 236  TYR B OH  
10627 N N   . TYR B 239  ? 0.2523 0.2070 0.1864 -0.0196 -0.0261 0.0124  237  TYR B N   
10628 C CA  . TYR B 239  ? 0.2803 0.2300 0.2111 -0.0215 -0.0275 0.0153  237  TYR B CA  
10629 C C   . TYR B 239  ? 0.2865 0.2354 0.2116 -0.0225 -0.0284 0.0173  237  TYR B C   
10630 O O   . TYR B 239  ? 0.2792 0.2272 0.2004 -0.0253 -0.0278 0.0196  237  TYR B O   
10631 C CB  . TYR B 239  ? 0.2545 0.1988 0.1873 -0.0196 -0.0299 0.0154  237  TYR B CB  
10632 C CG  . TYR B 239  ? 0.3006 0.2389 0.2294 -0.0212 -0.0317 0.0184  237  TYR B CG  
10633 C CD1 . TYR B 239  ? 0.2986 0.2340 0.2270 -0.0233 -0.0311 0.0194  237  TYR B CD1 
10634 C CD2 . TYR B 239  ? 0.3843 0.3194 0.3094 -0.0206 -0.0339 0.0201  237  TYR B CD2 
10635 C CE1 . TYR B 239  ? 0.2709 0.2002 0.1954 -0.0249 -0.0328 0.0222  237  TYR B CE1 
10636 C CE2 . TYR B 239  ? 0.3946 0.3239 0.3159 -0.0221 -0.0356 0.0230  237  TYR B CE2 
10637 C CZ  . TYR B 239  ? 0.3507 0.2769 0.2717 -0.0242 -0.0349 0.0240  237  TYR B CZ  
10638 O OH  . TYR B 239  ? 0.4300 0.3497 0.3469 -0.0258 -0.0366 0.0268  237  TYR B OH  
10639 N N   . ARG B 240  ? 0.2777 0.2267 0.2021 -0.0204 -0.0299 0.0165  238  ARG B N   
10640 C CA  . ARG B 240  ? 0.3045 0.2526 0.2233 -0.0212 -0.0309 0.0183  238  ARG B CA  
10641 C C   . ARG B 240  ? 0.3192 0.2718 0.2347 -0.0232 -0.0283 0.0185  238  ARG B C   
10642 O O   . ARG B 240  ? 0.3294 0.2810 0.2396 -0.0252 -0.0284 0.0208  238  ARG B O   
10643 C CB  . ARG B 240  ? 0.3048 0.2528 0.2238 -0.0187 -0.0331 0.0172  238  ARG B CB  
10644 C CG  . ARG B 240  ? 0.3298 0.2735 0.2514 -0.0167 -0.0359 0.0176  238  ARG B CG  
10645 C CD  . ARG B 240  ? 0.3646 0.3026 0.2825 -0.0179 -0.0377 0.0208  238  ARG B CD  
10646 N NE  . ARG B 240  ? 0.3832 0.3173 0.3039 -0.0156 -0.0402 0.0211  238  ARG B NE  
10647 C CZ  . ARG B 240  ? 0.5117 0.4400 0.4306 -0.0159 -0.0419 0.0235  238  ARG B CZ  
10648 N NH1 . ARG B 240  ? 0.4503 0.3759 0.3645 -0.0187 -0.0415 0.0259  238  ARG B NH1 
10649 N NH2 . ARG B 240  ? 0.5258 0.4510 0.4477 -0.0132 -0.0441 0.0234  238  ARG B NH2 
10650 N N   . ASP B 241  ? 0.3110 0.2687 0.2295 -0.0226 -0.0259 0.0160  239  ASP B N   
10651 C CA  . ASP B 241  ? 0.3323 0.2949 0.2482 -0.0241 -0.0231 0.0160  239  ASP B CA  
10652 C C   . ASP B 241  ? 0.2993 0.2621 0.2139 -0.0274 -0.0217 0.0184  239  ASP B C   
10653 O O   . ASP B 241  ? 0.2938 0.2585 0.2040 -0.0294 -0.0205 0.0202  239  ASP B O   
10654 C CB  . ASP B 241  ? 0.3554 0.3231 0.2751 -0.0225 -0.0209 0.0129  239  ASP B CB  
10655 C CG  . ASP B 241  ? 0.4316 0.3995 0.3514 -0.0198 -0.0221 0.0106  239  ASP B CG  
10656 O OD1 . ASP B 241  ? 0.4829 0.4482 0.3991 -0.0195 -0.0242 0.0115  239  ASP B OD1 
10657 O OD2 . ASP B 241  ? 0.5160 0.4866 0.4397 -0.0181 -0.0210 0.0081  239  ASP B OD2 
10658 N N   . TYR B 242  ? 0.2828 0.2438 0.2011 -0.0280 -0.0218 0.0186  240  TYR B N   
10659 C CA  . TYR B 242  ? 0.2663 0.2269 0.1833 -0.0314 -0.0209 0.0210  240  TYR B CA  
10660 C C   . TYR B 242  ? 0.2797 0.2350 0.1915 -0.0333 -0.0228 0.0242  240  TYR B C   
10661 O O   . TYR B 242  ? 0.2648 0.2212 0.1730 -0.0363 -0.0217 0.0266  240  TYR B O   
10662 C CB  . TYR B 242  ? 0.2729 0.2313 0.1944 -0.0316 -0.0212 0.0204  240  TYR B CB  
10663 C CG  . TYR B 242  ? 0.2312 0.1949 0.1578 -0.0306 -0.0190 0.0178  240  TYR B CG  
10664 C CD1 . TYR B 242  ? 0.2738 0.2443 0.2006 -0.0313 -0.0162 0.0172  240  TYR B CD1 
10665 C CD2 . TYR B 242  ? 0.2543 0.2161 0.1855 -0.0290 -0.0198 0.0161  240  TYR B CD2 
10666 C CE1 . TYR B 242  ? 0.2743 0.2494 0.2058 -0.0303 -0.0144 0.0150  240  TYR B CE1 
10667 C CE2 . TYR B 242  ? 0.2815 0.2477 0.2171 -0.0282 -0.0180 0.0140  240  TYR B CE2 
10668 C CZ  . TYR B 242  ? 0.2958 0.2686 0.2316 -0.0289 -0.0154 0.0134  240  TYR B CZ  
10669 O OH  . TYR B 242  ? 0.2845 0.2616 0.2249 -0.0279 -0.0138 0.0114  240  TYR B OH  
10670 N N   . GLU B 243  ? 0.2886 0.2382 0.1999 -0.0315 -0.0257 0.0245  241  GLU B N   
10671 C CA  . GLU B 243  ? 0.2863 0.2304 0.1927 -0.0329 -0.0279 0.0277  241  GLU B CA  
10672 C C   . GLU B 243  ? 0.3103 0.2568 0.2111 -0.0341 -0.0272 0.0291  241  GLU B C   
10673 O O   . GLU B 243  ? 0.2754 0.2205 0.1717 -0.0370 -0.0271 0.0321  241  GLU B O   
10674 C CB  . GLU B 243  ? 0.2715 0.2103 0.1788 -0.0300 -0.0311 0.0273  241  GLU B CB  
10675 C CG  . GLU B 243  ? 0.3471 0.2798 0.2495 -0.0308 -0.0336 0.0305  241  GLU B CG  
10676 C CD  . GLU B 243  ? 0.4000 0.3288 0.3037 -0.0275 -0.0367 0.0300  241  GLU B CD  
10677 O OE1 . GLU B 243  ? 0.4180 0.3500 0.3248 -0.0248 -0.0369 0.0275  241  GLU B OE1 
10678 O OE2 . GLU B 243  ? 0.4486 0.3710 0.3502 -0.0275 -0.0391 0.0323  241  GLU B OE2 
10679 N N   . SER B 244  ? 0.2768 0.2269 0.1776 -0.0318 -0.0269 0.0269  242  SER B N   
10680 C CA  A SER B 244  ? 0.2878 0.2403 0.1830 -0.0325 -0.0262 0.0278  242  SER B CA  
10681 C CA  B SER B 244  ? 0.2878 0.2402 0.1829 -0.0326 -0.0262 0.0279  242  SER B CA  
10682 C C   . SER B 244  ? 0.2783 0.2360 0.1720 -0.0353 -0.0228 0.0287  242  SER B C   
10683 O O   . SER B 244  ? 0.2802 0.2381 0.1684 -0.0376 -0.0223 0.0313  242  SER B O   
10684 C CB  A SER B 244  ? 0.3113 0.2668 0.2074 -0.0295 -0.0263 0.0248  242  SER B CB  
10685 C CB  B SER B 244  ? 0.3118 0.2670 0.2075 -0.0296 -0.0264 0.0250  242  SER B CB  
10686 O OG  A SER B 244  ? 0.3305 0.2882 0.2209 -0.0300 -0.0255 0.0253  242  SER B OG  
10687 O OG  B SER B 244  ? 0.3190 0.2698 0.2153 -0.0274 -0.0297 0.0248  242  SER B OG  
10688 N N   . ALA B 245  ? 0.2917 0.2538 0.1901 -0.0352 -0.0205 0.0268  243  ALA B N   
10689 C CA  . ALA B 245  ? 0.2975 0.2653 0.1953 -0.0377 -0.0172 0.0277  243  ALA B CA  
10690 C C   . ALA B 245  ? 0.3112 0.2763 0.2069 -0.0417 -0.0174 0.0313  243  ALA B C   
10691 O O   . ALA B 245  ? 0.3033 0.2715 0.1953 -0.0443 -0.0156 0.0334  243  ALA B O   
10692 C CB  . ALA B 245  ? 0.2931 0.2659 0.1969 -0.0366 -0.0150 0.0249  243  ALA B CB  
10693 N N   . ILE B 246  ? 0.2870 0.2463 0.1849 -0.0421 -0.0195 0.0320  244  ILE B N   
10694 C CA  . ILE B 246  ? 0.2725 0.2283 0.1681 -0.0460 -0.0200 0.0354  244  ILE B CA  
10695 C C   . ILE B 246  ? 0.2947 0.2476 0.1834 -0.0477 -0.0211 0.0386  244  ILE B C   
10696 O O   . ILE B 246  ? 0.3112 0.2653 0.1968 -0.0513 -0.0198 0.0414  244  ILE B O   
10697 C CB  . ILE B 246  ? 0.2719 0.2209 0.1704 -0.0457 -0.0224 0.0353  244  ILE B CB  
10698 C CG1 . ILE B 246  ? 0.3060 0.2587 0.2107 -0.0451 -0.0208 0.0328  244  ILE B CG1 
10699 C CG2 . ILE B 246  ? 0.3121 0.2558 0.2070 -0.0496 -0.0234 0.0390  244  ILE B CG2 
10700 C CD1 . ILE B 246  ? 0.3153 0.2616 0.2230 -0.0441 -0.0230 0.0321  244  ILE B CD1 
10701 N N   . HIS B 247  ? 0.3033 0.2524 0.1897 -0.0451 -0.0235 0.0383  245  HIS B N   
10702 C CA  . HIS B 247  ? 0.3113 0.2577 0.1907 -0.0466 -0.0246 0.0413  245  HIS B CA  
10703 C C   . HIS B 247  ? 0.2917 0.2450 0.1677 -0.0481 -0.0216 0.0418  245  HIS B C   
10704 O O   . HIS B 247  ? 0.3297 0.2826 0.2008 -0.0513 -0.0211 0.0452  245  HIS B O   
10705 C CB  . HIS B 247  ? 0.3122 0.2544 0.1900 -0.0433 -0.0276 0.0406  245  HIS B CB  
10706 C CG  . HIS B 247  ? 0.3137 0.2483 0.1934 -0.0423 -0.0308 0.0413  245  HIS B CG  
10707 N ND1 . HIS B 247  ? 0.3300 0.2582 0.2062 -0.0447 -0.0325 0.0449  245  HIS B ND1 
10708 C CD2 . HIS B 247  ? 0.3536 0.2859 0.2380 -0.0390 -0.0325 0.0390  245  HIS B CD2 
10709 C CE1 . HIS B 247  ? 0.3508 0.2729 0.2294 -0.0427 -0.0351 0.0445  245  HIS B CE1 
10710 N NE2 . HIS B 247  ? 0.3760 0.3008 0.2598 -0.0393 -0.0351 0.0410  245  HIS B NE2 
10711 N N   . ALA B 248  ? 0.2964 0.2560 0.1747 -0.0458 -0.0195 0.0387  246  ALA B N   
10712 C CA  . ALA B 248  ? 0.2893 0.2556 0.1642 -0.0468 -0.0164 0.0389  246  ALA B CA  
10713 C C   . ALA B 248  ? 0.2894 0.2604 0.1655 -0.0503 -0.0135 0.0406  246  ALA B C   
10714 O O   . ALA B 248  ? 0.3337 0.3074 0.2052 -0.0531 -0.0119 0.0432  246  ALA B O   
10715 C CB  . ALA B 248  ? 0.3364 0.3076 0.2137 -0.0432 -0.0150 0.0348  246  ALA B CB  
10716 N N   . ILE B 249  ? 0.2909 0.2633 0.1732 -0.0504 -0.0128 0.0392  247  ILE B N   
10717 C CA  . ILE B 249  ? 0.2810 0.2584 0.1652 -0.0539 -0.0102 0.0407  247  ILE B CA  
10718 C C   . ILE B 249  ? 0.3192 0.2918 0.1998 -0.0582 -0.0115 0.0450  247  ILE B C   
10719 O O   . ILE B 249  ? 0.3288 0.3056 0.2073 -0.0618 -0.0094 0.0476  247  ILE B O   
10720 C CB  . ILE B 249  ? 0.2716 0.2509 0.1631 -0.0529 -0.0097 0.0382  247  ILE B CB  
10721 C CG1 . ILE B 249  ? 0.2629 0.2476 0.1575 -0.0489 -0.0080 0.0343  247  ILE B CG1 
10722 C CG2 . ILE B 249  ? 0.3049 0.2884 0.1983 -0.0569 -0.0077 0.0402  247  ILE B CG2 
10723 C CD1 . ILE B 249  ? 0.2943 0.2784 0.1956 -0.0469 -0.0087 0.0315  247  ILE B CD1 
10724 N N   . GLY B 250  ? 0.3136 0.2774 0.1935 -0.0580 -0.0150 0.0458  248  GLY B N   
10725 C CA  . GLY B 250  ? 0.3101 0.2681 0.1864 -0.0619 -0.0165 0.0498  248  GLY B CA  
10726 C C   . GLY B 250  ? 0.3575 0.3154 0.2266 -0.0638 -0.0163 0.0530  248  GLY B C   
10727 O O   . GLY B 250  ? 0.3563 0.3143 0.2225 -0.0682 -0.0155 0.0565  248  GLY B O   
10728 N N   . LYS B 251  ? 0.3362 0.2940 0.2023 -0.0608 -0.0170 0.0519  249  LYS B N   
10729 C CA  . LYS B 251  ? 0.3808 0.3387 0.2396 -0.0625 -0.0167 0.0548  249  LYS B CA  
10730 C C   . LYS B 251  ? 0.3681 0.3355 0.2260 -0.0645 -0.0125 0.0553  249  LYS B C   
10731 O O   . LYS B 251  ? 0.3741 0.3424 0.2273 -0.0682 -0.0115 0.0589  249  LYS B O   
10732 C CB  . LYS B 251  ? 0.3932 0.3488 0.2489 -0.0587 -0.0186 0.0532  249  LYS B CB  
10733 N N   . ALA B 252  ? 0.3640 0.3386 0.2264 -0.0622 -0.0100 0.0518  250  ALA B N   
10734 C CA  . ALA B 252  ? 0.3660 0.3501 0.2283 -0.0637 -0.0058 0.0521  250  ALA B CA  
10735 C C   . ALA B 252  ? 0.3516 0.3382 0.2161 -0.0684 -0.0044 0.0548  250  ALA B C   
10736 O O   . ALA B 252  ? 0.3821 0.3747 0.2441 -0.0713 -0.0017 0.0572  250  ALA B O   
10737 C CB  . ALA B 252  ? 0.3833 0.3738 0.2504 -0.0598 -0.0037 0.0476  250  ALA B CB  
10738 N N   . SER B 253  ? 0.3414 0.3238 0.2106 -0.0692 -0.0062 0.0546  251  SER B N   
10739 C CA  . SER B 253  ? 0.3653 0.3492 0.2364 -0.0739 -0.0053 0.0572  251  SER B CA  
10740 C C   . SER B 253  ? 0.3832 0.3638 0.2479 -0.0785 -0.0059 0.0621  251  SER B C   
10741 O O   . SER B 253  ? 0.4025 0.3887 0.2667 -0.0826 -0.0035 0.0647  251  SER B O   
10742 C CB  . SER B 253  ? 0.3393 0.3170 0.2150 -0.0740 -0.0078 0.0562  251  SER B CB  
10743 O OG  . SER B 253  ? 0.3517 0.3300 0.2287 -0.0789 -0.0073 0.0589  251  SER B OG  
10744 N N   . ALA B 254  ? 0.3740 0.3458 0.2339 -0.0778 -0.0090 0.0634  252  ALA B N   
10745 C CA  . ALA B 254  ? 0.4027 0.3707 0.2555 -0.0815 -0.0098 0.0680  252  ALA B CA  
10746 C C   . ALA B 254  ? 0.4279 0.3945 0.2811 -0.0872 -0.0098 0.0716  252  ALA B C   
10747 O O   . ALA B 254  ? 0.4470 0.4168 0.2964 -0.0914 -0.0081 0.0753  252  ALA B O   
10748 C CB  . ALA B 254  ? 0.3944 0.3692 0.2423 -0.0814 -0.0071 0.0689  252  ALA B CB  
10749 N N   . GLY B 255  ? 0.4495 0.4113 0.3072 -0.0875 -0.0116 0.0706  253  GLY B N   
10750 C CA  . GLY B 255  ? 0.4363 0.3951 0.2943 -0.0929 -0.0122 0.0737  253  GLY B CA  
10751 C C   . GLY B 255  ? 0.4226 0.3913 0.2849 -0.0961 -0.0089 0.0739  253  GLY B C   
10752 O O   . GLY B 255  ? 0.4451 0.4124 0.3071 -0.1014 -0.0091 0.0771  253  GLY B O   
10753 N N   . ARG B 256  ? 0.3669 0.3456 0.2334 -0.0932 -0.0059 0.0708  254  ARG B N   
10754 C CA  . ARG B 256  ? 0.3976 0.3863 0.2689 -0.0959 -0.0028 0.0709  254  ARG B CA  
10755 C C   . ARG B 256  ? 0.3844 0.3706 0.2613 -0.0973 -0.0042 0.0698  254  ARG B C   
10756 O O   . ARG B 256  ? 0.4086 0.4018 0.2891 -0.1008 -0.0023 0.0708  254  ARG B O   
10757 C CB  . ARG B 256  ? 0.3945 0.3938 0.2687 -0.0919 0.0006  0.0677  254  ARG B CB  
10758 C CG  . ARG B 256  ? 0.3918 0.3975 0.2611 -0.0925 0.0034  0.0697  254  ARG B CG  
10759 C CD  . ARG B 256  ? 0.4153 0.4306 0.2874 -0.0881 0.0066  0.0662  254  ARG B CD  
10760 N NE  . ARG B 256  ? 0.4066 0.4171 0.2777 -0.0825 0.0050  0.0626  254  ARG B NE  
10761 C CZ  . ARG B 256  ? 0.3682 0.3840 0.2423 -0.0778 0.0067  0.0586  254  ARG B CZ  
10762 N NH1 . ARG B 256  ? 0.3936 0.4195 0.2722 -0.0776 0.0101  0.0574  254  ARG B NH1 
10763 N NH2 . ARG B 256  ? 0.4011 0.4118 0.2737 -0.0733 0.0049  0.0557  254  ARG B NH2 
10764 N N   . GLY B 257  ? 0.4010 0.3779 0.2788 -0.0947 -0.0074 0.0678  255  GLY B N   
10765 C CA  . GLY B 257  ? 0.3817 0.3554 0.2641 -0.0960 -0.0088 0.0667  255  GLY B CA  
10766 C C   . GLY B 257  ? 0.3396 0.3201 0.2289 -0.0922 -0.0073 0.0623  255  GLY B C   
10767 O O   . GLY B 257  ? 0.3482 0.3362 0.2389 -0.0887 -0.0050 0.0602  255  GLY B O   
10768 N N   . ILE B 258  ? 0.3512 0.3286 0.2445 -0.0930 -0.0087 0.0610  256  ILE B N   
10769 C CA  . ILE B 258  ? 0.3628 0.3446 0.2623 -0.0891 -0.0079 0.0568  256  ILE B CA  
10770 C C   . ILE B 258  ? 0.3267 0.3213 0.2308 -0.0901 -0.0044 0.0564  256  ILE B C   
10771 O O   . ILE B 258  ? 0.3267 0.3264 0.2354 -0.0862 -0.0032 0.0529  256  ILE B O   
10772 C CB  . ILE B 258  ? 0.3907 0.3645 0.2926 -0.0893 -0.0107 0.0554  256  ILE B CB  
10773 C CG1 . ILE B 258  ? 0.3930 0.3662 0.2949 -0.0955 -0.0112 0.0583  256  ILE B CG1 
10774 C CG2 . ILE B 258  ? 0.3741 0.3359 0.2719 -0.0870 -0.0140 0.0554  256  ILE B CG2 
10775 C CD1 . ILE B 258  ? 0.4305 0.3958 0.3342 -0.0960 -0.0138 0.0570  256  ILE B CD1 
10776 N N   . TYR B 259  ? 0.3462 0.3463 0.2492 -0.0952 -0.0028 0.0599  257  TYR B N   
10777 C CA  . TYR B 259  ? 0.3412 0.3540 0.2490 -0.0962 0.0005  0.0596  257  TYR B CA  
10778 C C   . TYR B 259  ? 0.3521 0.3736 0.2583 -0.0941 0.0039  0.0597  257  TYR B C   
10779 O O   . TYR B 259  ? 0.3435 0.3727 0.2536 -0.0902 0.0061  0.0568  257  TYR B O   
10780 C CB  . TYR B 259  ? 0.3502 0.3653 0.2587 -0.1031 0.0006  0.0632  257  TYR B CB  
10781 C CG  . TYR B 259  ? 0.3620 0.3674 0.2711 -0.1053 -0.0029 0.0631  257  TYR B CG  
10782 C CD1 . TYR B 259  ? 0.3797 0.3854 0.2941 -0.1030 -0.0036 0.0597  257  TYR B CD1 
10783 C CD2 . TYR B 259  ? 0.3940 0.3894 0.2979 -0.1094 -0.0055 0.0662  257  TYR B CD2 
10784 C CE1 . TYR B 259  ? 0.4099 0.4065 0.3245 -0.1047 -0.0067 0.0593  257  TYR B CE1 
10785 C CE2 . TYR B 259  ? 0.3817 0.3676 0.2858 -0.1110 -0.0086 0.0658  257  TYR B CE2 
10786 C CZ  . TYR B 259  ? 0.4009 0.3876 0.3103 -0.1087 -0.0092 0.0623  257  TYR B CZ  
10787 O OH  . TYR B 259  ? 0.4311 0.4082 0.3403 -0.1101 -0.0122 0.0617  257  TYR B OH  
10788 N N   . GLU B 260  ? 0.3500 0.3703 0.2504 -0.0965 0.0043  0.0630  258  GLU B N   
10789 C CA  . GLU B 260  ? 0.3587 0.3867 0.2568 -0.0943 0.0074  0.0630  258  GLU B CA  
10790 C C   . GLU B 260  ? 0.4023 0.4261 0.2986 -0.0881 0.0066  0.0596  258  GLU B C   
10791 O O   . GLU B 260  ? 0.4207 0.4517 0.3181 -0.0843 0.0092  0.0573  258  GLU B O   
10792 C CB  . GLU B 260  ? 0.4066 0.4340 0.2986 -0.0988 0.0079  0.0676  258  GLU B CB  
10793 C CG  . GLU B 260  ? 0.5226 0.5570 0.4112 -0.0965 0.0110  0.0677  258  GLU B CG  
10794 C CD  . GLU B 260  ? 0.5135 0.5467 0.3953 -0.1008 0.0114  0.0724  258  GLU B CD  
10795 O OE1 . GLU B 260  ? 0.5853 0.6130 0.4655 -0.1060 0.0094  0.0758  258  GLU B OE1 
10796 O OE2 . GLU B 260  ? 0.5744 0.6119 0.4522 -0.0990 0.0136  0.0726  258  GLU B OE2 
10797 N N   . GLY B 261  ? 0.3398 0.3523 0.2336 -0.0870 0.0031  0.0591  259  GLY B N   
10798 C CA  . GLY B 261  ? 0.3450 0.3531 0.2362 -0.0819 0.0020  0.0566  259  GLY B CA  
10799 C C   . GLY B 261  ? 0.3471 0.3552 0.2436 -0.0771 0.0015  0.0520  259  GLY B C   
10800 O O   . GLY B 261  ? 0.3119 0.3213 0.2137 -0.0776 0.0013  0.0508  259  GLY B O   
10801 N N   . PRO B 262  ? 0.3011 0.3077 0.1960 -0.0723 0.0012  0.0495  260  PRO B N   
10802 C CA  . PRO B 262  ? 0.3159 0.3229 0.2157 -0.0676 0.0009  0.0451  260  PRO B CA  
10803 C C   . PRO B 262  ? 0.3288 0.3266 0.2305 -0.0669 -0.0025 0.0441  260  PRO B C   
10804 O O   . PRO B 262  ? 0.3266 0.3161 0.2248 -0.0688 -0.0052 0.0462  260  PRO B O   
10805 C CB  . PRO B 262  ? 0.3121 0.3193 0.2084 -0.0635 0.0014  0.0433  260  PRO B CB  
10806 C CG  . PRO B 262  ? 0.3372 0.3391 0.2264 -0.0658 0.0000  0.0466  260  PRO B CG  
10807 C CD  . PRO B 262  ? 0.3182 0.3234 0.2067 -0.0713 0.0013  0.0504  260  PRO B CD  
10808 N N   . GLY B 263  ? 0.2884 0.2877 0.1955 -0.0637 -0.0025 0.0406  261  GLY B N   
10809 C CA  . GLY B 263  ? 0.2838 0.2753 0.1931 -0.0622 -0.0054 0.0390  261  GLY B CA  
10810 C C   . GLY B 263  ? 0.2894 0.2812 0.2014 -0.0568 -0.0056 0.0350  261  GLY B C   
10811 O O   . GLY B 263  ? 0.2962 0.2932 0.2076 -0.0543 -0.0037 0.0335  261  GLY B O   
10812 N N   . ILE B 264  ? 0.2771 0.2631 0.1918 -0.0552 -0.0079 0.0334  262  ILE B N   
10813 C CA  . ILE B 264  ? 0.2687 0.2544 0.1863 -0.0505 -0.0083 0.0298  262  ILE B CA  
10814 C C   . ILE B 264  ? 0.2654 0.2516 0.1887 -0.0499 -0.0084 0.0278  262  ILE B C   
10815 O O   . ILE B 264  ? 0.2838 0.2671 0.2080 -0.0528 -0.0093 0.0292  262  ILE B O   
10816 C CB  . ILE B 264  ? 0.2626 0.2403 0.1774 -0.0482 -0.0112 0.0296  262  ILE B CB  
10817 C CG1 . ILE B 264  ? 0.2665 0.2455 0.1836 -0.0436 -0.0112 0.0261  262  ILE B CG1 
10818 C CG2 . ILE B 264  ? 0.3119 0.2816 0.2273 -0.0493 -0.0139 0.0304  262  ILE B CG2 
10819 C CD1 . ILE B 264  ? 0.3019 0.2742 0.2166 -0.0412 -0.0141 0.0257  262  ILE B CD1 
10820 N N   . SER B 265  ? 0.2294 0.2195 0.1565 -0.0463 -0.0073 0.0247  263  SER B N   
10821 C CA  . SER B 265  ? 0.2541 0.2447 0.1865 -0.0452 -0.0075 0.0226  263  SER B CA  
10822 C C   . SER B 265  ? 0.2701 0.2563 0.2039 -0.0411 -0.0092 0.0200  263  SER B C   
10823 O O   . SER B 265  ? 0.2917 0.2787 0.2242 -0.0384 -0.0090 0.0187  263  SER B O   
10824 C CB  . SER B 265  ? 0.2954 0.2952 0.2316 -0.0445 -0.0046 0.0212  263  SER B CB  
10825 O OG  . SER B 265  ? 0.2856 0.2901 0.2221 -0.0484 -0.0031 0.0234  263  SER B OG  
10826 N N   . ILE B 266  ? 0.2319 0.2133 0.1682 -0.0407 -0.0109 0.0192  264  ILE B N   
10827 C CA  . ILE B 266  ? 0.2529 0.2303 0.1910 -0.0370 -0.0126 0.0169  264  ILE B CA  
10828 C C   . ILE B 266  ? 0.2424 0.2216 0.1856 -0.0357 -0.0121 0.0146  264  ILE B C   
10829 O O   . ILE B 266  ? 0.2451 0.2267 0.1902 -0.0380 -0.0112 0.0151  264  ILE B O   
10830 C CB  . ILE B 266  ? 0.2545 0.2232 0.1900 -0.0371 -0.0155 0.0181  264  ILE B CB  
10831 C CG1 . ILE B 266  ? 0.2806 0.2452 0.2167 -0.0396 -0.0164 0.0192  264  ILE B CG1 
10832 C CG2 . ILE B 266  ? 0.2760 0.2428 0.2061 -0.0384 -0.0161 0.0205  264  ILE B CG2 
10833 C CD1 . ILE B 266  ? 0.3416 0.2972 0.2756 -0.0391 -0.0193 0.0200  264  ILE B CD1 
10834 N N   . LYS B 267  ? 0.2487 0.2268 0.1942 -0.0321 -0.0127 0.0122  265  LYS B N   
10835 C CA  . LYS B 267  ? 0.2171 0.1959 0.1673 -0.0306 -0.0126 0.0101  265  LYS B CA  
10836 C C   . LYS B 267  ? 0.2258 0.1977 0.1763 -0.0288 -0.0150 0.0095  265  LYS B C   
10837 O O   . LYS B 267  ? 0.2450 0.2143 0.1943 -0.0268 -0.0162 0.0092  265  LYS B O   
10838 C CB  . LYS B 267  ? 0.2516 0.2359 0.2045 -0.0277 -0.0109 0.0077  265  LYS B CB  
10839 C CG  . LYS B 267  ? 0.2564 0.2481 0.2097 -0.0289 -0.0083 0.0080  265  LYS B CG  
10840 C CD  . LYS B 267  ? 0.3532 0.3495 0.3083 -0.0258 -0.0068 0.0058  265  LYS B CD  
10841 C CE  . LYS B 267  ? 0.3547 0.3586 0.3102 -0.0267 -0.0041 0.0061  265  LYS B CE  
10842 N NZ  . LYS B 267  ? 0.3671 0.3720 0.3183 -0.0293 -0.0035 0.0085  265  LYS B NZ  
10843 N N   . LEU B 268  ? 0.2162 0.1852 0.1683 -0.0298 -0.0157 0.0094  266  LEU B N   
10844 C CA  . LEU B 268  ? 0.2385 0.2010 0.1911 -0.0278 -0.0177 0.0087  266  LEU B CA  
10845 C C   . LEU B 268  ? 0.2508 0.2148 0.2066 -0.0240 -0.0177 0.0063  266  LEU B C   
10846 O O   . LEU B 268  ? 0.2437 0.2036 0.1993 -0.0219 -0.0194 0.0060  266  LEU B O   
10847 C CB  . LEU B 268  ? 0.2393 0.1987 0.1930 -0.0293 -0.0182 0.0087  266  LEU B CB  
10848 C CG  . LEU B 268  ? 0.2575 0.2145 0.2078 -0.0335 -0.0186 0.0112  266  LEU B CG  
10849 C CD1 . LEU B 268  ? 0.2819 0.2343 0.2328 -0.0346 -0.0196 0.0108  266  LEU B CD1 
10850 C CD2 . LEU B 268  ? 0.2933 0.2454 0.2392 -0.0342 -0.0201 0.0134  266  LEU B CD2 
10851 N N   . SER B 269  ? 0.2238 0.1937 0.1826 -0.0230 -0.0159 0.0046  267  SER B N   
10852 C CA  . SER B 269  ? 0.2438 0.2151 0.2055 -0.0196 -0.0159 0.0025  267  SER B CA  
10853 C C   . SER B 269  ? 0.2412 0.2120 0.2009 -0.0182 -0.0167 0.0026  267  SER B C   
10854 O O   . SER B 269  ? 0.2475 0.2177 0.2091 -0.0156 -0.0175 0.0012  267  SER B O   
10855 C CB  . SER B 269  ? 0.2368 0.2141 0.2016 -0.0189 -0.0138 0.0008  267  SER B CB  
10856 O OG  . SER B 269  ? 0.2468 0.2287 0.2101 -0.0196 -0.0123 0.0012  267  SER B OG  
10857 N N   . ALA B 270  ? 0.1981 0.1693 0.1539 -0.0199 -0.0165 0.0043  268  ALA B N   
10858 C CA  . ALA B 270  ? 0.2206 0.1909 0.1739 -0.0188 -0.0175 0.0045  268  ALA B CA  
10859 C C   . ALA B 270  ? 0.2640 0.2282 0.2161 -0.0179 -0.0201 0.0054  268  ALA B C   
10860 O O   . ALA B 270  ? 0.2487 0.2120 0.2000 -0.0163 -0.0214 0.0052  268  ALA B O   
10861 C CB  . ALA B 270  ? 0.2515 0.2236 0.2004 -0.0210 -0.0166 0.0063  268  ALA B CB  
10862 N N   . LEU B 271  ? 0.2350 0.1950 0.1870 -0.0190 -0.0210 0.0065  269  LEU B N   
10863 C CA  . LEU B 271  ? 0.2620 0.2159 0.2119 -0.0186 -0.0234 0.0079  269  LEU B CA  
10864 C C   . LEU B 271  ? 0.2421 0.1932 0.1955 -0.0159 -0.0247 0.0066  269  LEU B C   
10865 O O   . LEU B 271  ? 0.2628 0.2090 0.2150 -0.0149 -0.0267 0.0076  269  LEU B O   
10866 C CB  . LEU B 271  ? 0.2504 0.2004 0.1970 -0.0216 -0.0239 0.0103  269  LEU B CB  
10867 C CG  . LEU B 271  ? 0.2553 0.2075 0.1979 -0.0244 -0.0229 0.0122  269  LEU B CG  
10868 C CD1 . LEU B 271  ? 0.3347 0.2830 0.2745 -0.0277 -0.0233 0.0145  269  LEU B CD1 
10869 C CD2 . LEU B 271  ? 0.2637 0.2148 0.2032 -0.0233 -0.0243 0.0131  269  LEU B CD2 
10870 N N   . HIS B 272  ? 0.2419 0.1962 0.1995 -0.0145 -0.0235 0.0044  270  HIS B N   
10871 C CA  . HIS B 272  ? 0.2460 0.1983 0.2069 -0.0119 -0.0244 0.0031  270  HIS B CA  
10872 C C   . HIS B 272  ? 0.2357 0.1929 0.2007 -0.0104 -0.0229 0.0008  270  HIS B C   
10873 O O   . HIS B 272  ? 0.2543 0.2150 0.2200 -0.0117 -0.0211 0.0003  270  HIS B O   
10874 C CB  . HIS B 272  ? 0.2575 0.2053 0.2183 -0.0125 -0.0248 0.0035  270  HIS B CB  
10875 C CG  . HIS B 272  ? 0.2677 0.2123 0.2308 -0.0096 -0.0261 0.0027  270  HIS B CG  
10876 N ND1 . HIS B 272  ? 0.3022 0.2494 0.2696 -0.0075 -0.0254 0.0007  270  HIS B ND1 
10877 C CD2 . HIS B 272  ? 0.3456 0.2849 0.3074 -0.0083 -0.0281 0.0038  270  HIS B CD2 
10878 C CE1 . HIS B 272  ? 0.2930 0.2370 0.2618 -0.0050 -0.0267 0.0005  270  HIS B CE1 
10879 N NE2 . HIS B 272  ? 0.3296 0.2686 0.2950 -0.0054 -0.0284 0.0023  270  HIS B NE2 
10880 N N   . PRO B 273  ? 0.2340 0.1918 0.2018 -0.0078 -0.0236 -0.0004 271  PRO B N   
10881 C CA  . PRO B 273  ? 0.2356 0.1979 0.2071 -0.0065 -0.0223 -0.0024 271  PRO B CA  
10882 C C   . PRO B 273  ? 0.2345 0.1969 0.2090 -0.0061 -0.0213 -0.0035 271  PRO B C   
10883 O O   . PRO B 273  ? 0.2449 0.2110 0.2222 -0.0053 -0.0200 -0.0051 271  PRO B O   
10884 C CB  . PRO B 273  ? 0.2637 0.2261 0.2369 -0.0042 -0.0237 -0.0030 271  PRO B CB  
10885 C CG  . PRO B 273  ? 0.2614 0.2192 0.2334 -0.0036 -0.0258 -0.0015 271  PRO B CG  
10886 C CD  . PRO B 273  ? 0.2563 0.2113 0.2238 -0.0060 -0.0258 0.0003  271  PRO B CD  
10887 N N   . ARG B 274  ? 0.2265 0.1849 0.2002 -0.0065 -0.0219 -0.0029 272  ARG B N   
10888 C CA  . ARG B 274  ? 0.2598 0.2178 0.2358 -0.0062 -0.0211 -0.0040 272  ARG B CA  
10889 C C   . ARG B 274  ? 0.2589 0.2146 0.2322 -0.0089 -0.0208 -0.0030 272  ARG B C   
10890 O O   . ARG B 274  ? 0.2540 0.2053 0.2267 -0.0089 -0.0214 -0.0029 272  ARG B O   
10891 C CB  . ARG B 274  ? 0.2573 0.2123 0.2353 -0.0036 -0.0221 -0.0045 272  ARG B CB  
10892 C CG  . ARG B 274  ? 0.2727 0.2303 0.2538 -0.0011 -0.0225 -0.0054 272  ARG B CG  
10893 C CD  . ARG B 274  ? 0.2730 0.2358 0.2570 -0.0009 -0.0208 -0.0070 272  ARG B CD  
10894 N NE  . ARG B 274  ? 0.2653 0.2284 0.2508 -0.0010 -0.0195 -0.0080 272  ARG B NE  
10895 C CZ  . ARG B 274  ? 0.2386 0.2011 0.2267 0.0009  -0.0195 -0.0089 272  ARG B CZ  
10896 N NH1 . ARG B 274  ? 0.2639 0.2252 0.2535 0.0031  -0.0206 -0.0088 272  ARG B NH1 
10897 N NH2 . ARG B 274  ? 0.2591 0.2221 0.2481 0.0007  -0.0182 -0.0099 272  ARG B NH2 
10898 N N   . TYR B 275  ? 0.2428 0.2013 0.2144 -0.0113 -0.0198 -0.0023 273  TYR B N   
10899 C CA  . TYR B 275  ? 0.2532 0.2103 0.2225 -0.0143 -0.0195 -0.0011 273  TYR B CA  
10900 C C   . TYR B 275  ? 0.2523 0.2122 0.2242 -0.0147 -0.0181 -0.0025 273  TYR B C   
10901 O O   . TYR B 275  ? 0.2489 0.2142 0.2222 -0.0153 -0.0166 -0.0030 273  TYR B O   
10902 C CB  . TYR B 275  ? 0.2474 0.2071 0.2141 -0.0166 -0.0189 0.0004  273  TYR B CB  
10903 C CG  . TYR B 275  ? 0.2295 0.1890 0.1942 -0.0201 -0.0184 0.0016  273  TYR B CG  
10904 C CD1 . TYR B 275  ? 0.2586 0.2122 0.2213 -0.0216 -0.0197 0.0026  273  TYR B CD1 
10905 C CD2 . TYR B 275  ? 0.2235 0.1888 0.1886 -0.0219 -0.0166 0.0019  273  TYR B CD2 
10906 C CE1 . TYR B 275  ? 0.2570 0.2104 0.2180 -0.0251 -0.0193 0.0037  273  TYR B CE1 
10907 C CE2 . TYR B 275  ? 0.2293 0.1952 0.1931 -0.0253 -0.0162 0.0031  273  TYR B CE2 
10908 C CZ  . TYR B 275  ? 0.2551 0.2149 0.2168 -0.0271 -0.0176 0.0041  273  TYR B CZ  
10909 O OH  . TYR B 275  ? 0.2704 0.2306 0.2307 -0.0308 -0.0174 0.0054  273  TYR B OH  
10910 N N   . SER B 276  ? 0.2283 0.1844 0.2006 -0.0141 -0.0187 -0.0032 274  SER B N   
10911 C CA  . SER B 276  ? 0.2465 0.2047 0.2210 -0.0142 -0.0177 -0.0045 274  SER B CA  
10912 C C   . SER B 276  ? 0.2388 0.1910 0.2119 -0.0145 -0.0187 -0.0047 274  SER B C   
10913 O O   . SER B 276  ? 0.2428 0.1896 0.2143 -0.0133 -0.0201 -0.0043 274  SER B O   
10914 C CB  . SER B 276  ? 0.2981 0.2598 0.2764 -0.0113 -0.0168 -0.0063 274  SER B CB  
10915 O OG  . SER B 276  ? 0.3355 0.2937 0.3146 -0.0087 -0.0178 -0.0069 274  SER B OG  
10916 N N   . ARG B 277  ? 0.2225 0.1758 0.1961 -0.0159 -0.0180 -0.0054 275  ARG B N   
10917 C CA  . ARG B 277  ? 0.2338 0.1813 0.2057 -0.0162 -0.0190 -0.0059 275  ARG B CA  
10918 C C   . ARG B 277  ? 0.2383 0.1831 0.2117 -0.0125 -0.0193 -0.0073 275  ARG B C   
10919 O O   . ARG B 277  ? 0.2495 0.1880 0.2208 -0.0118 -0.0205 -0.0074 275  ARG B O   
10920 C CB  . ARG B 277  ? 0.2356 0.1854 0.2079 -0.0184 -0.0182 -0.0066 275  ARG B CB  
10921 C CG  . ARG B 277  ? 0.2700 0.2141 0.2406 -0.0185 -0.0190 -0.0075 275  ARG B CG  
10922 C CD  . ARG B 277  ? 0.2729 0.2094 0.2392 -0.0202 -0.0207 -0.0063 275  ARG B CD  
10923 N NE  . ARG B 277  ? 0.2661 0.1964 0.2302 -0.0202 -0.0216 -0.0074 275  ARG B NE  
10924 C CZ  . ARG B 277  ? 0.2778 0.2033 0.2416 -0.0169 -0.0220 -0.0085 275  ARG B CZ  
10925 N NH1 . ARG B 277  ? 0.2951 0.2217 0.2610 -0.0134 -0.0218 -0.0088 275  ARG B NH1 
10926 N NH2 . ARG B 277  ? 0.2706 0.1901 0.2317 -0.0172 -0.0228 -0.0095 275  ARG B NH2 
10927 N N   . ALA B 278  ? 0.2493 0.1989 0.2263 -0.0101 -0.0183 -0.0085 276  ALA B N   
10928 C CA  . ALA B 278  ? 0.2522 0.2000 0.2310 -0.0066 -0.0185 -0.0097 276  ALA B CA  
10929 C C   . ALA B 278  ? 0.2577 0.2013 0.2353 -0.0050 -0.0199 -0.0087 276  ALA B C   
10930 O O   . ALA B 278  ? 0.2761 0.2166 0.2542 -0.0024 -0.0204 -0.0094 276  ALA B O   
10931 C CB  . ALA B 278  ? 0.2644 0.2184 0.2473 -0.0047 -0.0172 -0.0107 276  ALA B CB  
10932 N N   . GLN B 279  ? 0.2291 0.1729 0.2051 -0.0063 -0.0205 -0.0072 277  GLN B N   
10933 C CA  . GLN B 279  ? 0.2283 0.1682 0.2028 -0.0050 -0.0221 -0.0060 277  GLN B CA  
10934 C C   . GLN B 279  ? 0.2509 0.1852 0.2209 -0.0075 -0.0233 -0.0043 277  GLN B C   
10935 O O   . GLN B 279  ? 0.2551 0.1878 0.2233 -0.0077 -0.0244 -0.0027 277  GLN B O   
10936 C CB  . GLN B 279  ? 0.2793 0.2235 0.2555 -0.0041 -0.0221 -0.0055 277  GLN B CB  
10937 C CG  . GLN B 279  ? 0.2684 0.2176 0.2489 -0.0019 -0.0211 -0.0071 277  GLN B CG  
10938 C CD  . GLN B 279  ? 0.2813 0.2284 0.2638 0.0013  -0.0216 -0.0079 277  GLN B CD  
10939 O OE1 . GLN B 279  ? 0.3171 0.2594 0.2980 0.0024  -0.0230 -0.0071 277  GLN B OE1 
10940 N NE2 . GLN B 279  ? 0.2737 0.2244 0.2597 0.0029  -0.0204 -0.0094 277  GLN B NE2 
10941 N N   . ALA B 280  ? 0.2509 0.1821 0.2190 -0.0094 -0.0233 -0.0046 278  ALA B N   
10942 C CA  . ALA B 280  ? 0.2619 0.1880 0.2256 -0.0125 -0.0244 -0.0028 278  ALA B CA  
10943 C C   . ALA B 280  ? 0.2770 0.1964 0.2382 -0.0109 -0.0262 -0.0017 278  ALA B C   
10944 O O   . ALA B 280  ? 0.2613 0.1779 0.2192 -0.0129 -0.0272 0.0003  278  ALA B O   
10945 C CB  . ALA B 280  ? 0.2917 0.2148 0.2536 -0.0146 -0.0243 -0.0035 278  ALA B CB  
10946 N N   . ALA B 281  ? 0.2769 0.1937 0.2394 -0.0072 -0.0267 -0.0028 279  ALA B N   
10947 C CA  . ALA B 281  ? 0.3041 0.2147 0.2645 -0.0052 -0.0285 -0.0017 279  ALA B CA  
10948 C C   . ALA B 281  ? 0.2650 0.1781 0.2256 -0.0049 -0.0292 -0.0001 279  ALA B C   
10949 O O   . ALA B 281  ? 0.2895 0.1979 0.2467 -0.0058 -0.0307 0.0019  279  ALA B O   
10950 C CB  . ALA B 281  ? 0.3285 0.2370 0.2910 -0.0009 -0.0286 -0.0033 279  ALA B CB  
10951 N N   . ARG B 282  ? 0.2631 0.1834 0.2275 -0.0038 -0.0282 -0.0008 280  ARG B N   
10952 C CA  . ARG B 282  ? 0.2607 0.1835 0.2250 -0.0038 -0.0289 0.0006  280  ARG B CA  
10953 C C   . ARG B 282  ? 0.2751 0.1986 0.2362 -0.0076 -0.0287 0.0022  280  ARG B C   
10954 O O   . ARG B 282  ? 0.2921 0.2144 0.2508 -0.0082 -0.0298 0.0040  280  ARG B O   
10955 C CB  . ARG B 282  ? 0.2815 0.2114 0.2503 -0.0019 -0.0279 -0.0007 280  ARG B CB  
10956 C CG  . ARG B 282  ? 0.2963 0.2263 0.2686 0.0020  -0.0282 -0.0019 280  ARG B CG  
10957 C CD  . ARG B 282  ? 0.2941 0.2307 0.2703 0.0033  -0.0276 -0.0027 280  ARG B CD  
10958 N NE  . ARG B 282  ? 0.3144 0.2517 0.2893 0.0030  -0.0290 -0.0012 280  ARG B NE  
10959 C CZ  . ARG B 282  ? 0.2770 0.2195 0.2538 0.0031  -0.0287 -0.0015 280  ARG B CZ  
10960 N NH1 . ARG B 282  ? 0.3057 0.2530 0.2858 0.0035  -0.0272 -0.0032 280  ARG B NH1 
10961 N NH2 . ARG B 282  ? 0.3169 0.2594 0.2919 0.0028  -0.0301 -0.0001 280  ARG B NH2 
10962 N N   . VAL B 283  ? 0.2498 0.1757 0.2108 -0.0103 -0.0273 0.0017  281  VAL B N   
10963 C CA  . VAL B 283  ? 0.2638 0.1909 0.2220 -0.0141 -0.0269 0.0034  281  VAL B CA  
10964 C C   . VAL B 283  ? 0.2675 0.1872 0.2209 -0.0159 -0.0286 0.0055  281  VAL B C   
10965 O O   . VAL B 283  ? 0.2939 0.2130 0.2445 -0.0174 -0.0293 0.0075  281  VAL B O   
10966 C CB  . VAL B 283  ? 0.2388 0.1701 0.1982 -0.0165 -0.0251 0.0024  281  VAL B CB  
10967 C CG1 . VAL B 283  ? 0.2625 0.1944 0.2188 -0.0207 -0.0248 0.0044  281  VAL B CG1 
10968 C CG2 . VAL B 283  ? 0.2514 0.1903 0.2149 -0.0149 -0.0235 0.0008  281  VAL B CG2 
10969 N N   . MET B 284  ? 0.2601 0.1738 0.2123 -0.0158 -0.0293 0.0051  282  MET B N   
10970 C CA  . MET B 284  ? 0.2793 0.1850 0.2266 -0.0176 -0.0310 0.0071  282  MET B CA  
10971 C C   . MET B 284  ? 0.3153 0.2170 0.2612 -0.0150 -0.0328 0.0083  282  MET B C   
10972 O O   . MET B 284  ? 0.3378 0.2350 0.2797 -0.0168 -0.0342 0.0107  282  MET B O   
10973 C CB  . MET B 284  ? 0.2744 0.1741 0.2204 -0.0179 -0.0314 0.0060  282  MET B CB  
10974 C CG  . MET B 284  ? 0.2945 0.1976 0.2414 -0.0208 -0.0300 0.0049  282  MET B CG  
10975 S SD  . MET B 284  ? 0.3631 0.2696 0.3077 -0.0264 -0.0294 0.0073  282  MET B SD  
10976 C CE  . MET B 284  ? 0.3712 0.2668 0.3098 -0.0291 -0.0316 0.0094  282  MET B CE  
10977 N N   . GLY B 285  ? 0.2787 0.1822 0.2281 -0.0108 -0.0330 0.0070  283  GLY B N   
10978 C CA  . GLY B 285  ? 0.3214 0.2214 0.2699 -0.0080 -0.0348 0.0081  283  GLY B CA  
10979 C C   . GLY B 285  ? 0.3176 0.2218 0.2660 -0.0082 -0.0352 0.0095  283  GLY B C   
10980 O O   . GLY B 285  ? 0.3534 0.2538 0.2992 -0.0076 -0.0371 0.0114  283  GLY B O   
10981 N N   . GLU B 286  ? 0.2864 0.1983 0.2374 -0.0091 -0.0336 0.0086  284  GLU B N   
10982 C CA  . GLU B 286  ? 0.2805 0.1968 0.2316 -0.0089 -0.0338 0.0093  284  GLU B CA  
10983 C C   . GLU B 286  ? 0.3029 0.2230 0.2519 -0.0126 -0.0326 0.0103  284  GLU B C   
10984 O O   . GLU B 286  ? 0.3535 0.2737 0.2997 -0.0135 -0.0334 0.0120  284  GLU B O   
10985 C CB  . GLU B 286  ? 0.3194 0.2416 0.2756 -0.0059 -0.0331 0.0073  284  GLU B CB  
10986 C CG  . GLU B 286  ? 0.3080 0.2277 0.2670 -0.0021 -0.0340 0.0063  284  GLU B CG  
10987 C CD  . GLU B 286  ? 0.3576 0.2834 0.3220 0.0002  -0.0329 0.0041  284  GLU B CD  
10988 O OE1 . GLU B 286  ? 0.3513 0.2826 0.3169 -0.0006 -0.0322 0.0037  284  GLU B OE1 
10989 O OE2 . GLU B 286  ? 0.4136 0.3384 0.3806 0.0027  -0.0328 0.0028  284  GLU B OE2 
10990 N N   . LEU B 287  ? 0.2859 0.2092 0.2361 -0.0146 -0.0307 0.0092  285  LEU B N   
10991 C CA  . LEU B 287  ? 0.2943 0.2218 0.2428 -0.0179 -0.0293 0.0101  285  LEU B CA  
10992 C C   . LEU B 287  ? 0.3034 0.2261 0.2471 -0.0214 -0.0300 0.0126  285  LEU B C   
10993 O O   . LEU B 287  ? 0.2912 0.2149 0.2318 -0.0233 -0.0300 0.0145  285  LEU B O   
10994 C CB  . LEU B 287  ? 0.2736 0.2065 0.2253 -0.0187 -0.0271 0.0082  285  LEU B CB  
10995 C CG  . LEU B 287  ? 0.3124 0.2523 0.2643 -0.0206 -0.0252 0.0082  285  LEU B CG  
10996 C CD1 . LEU B 287  ? 0.2893 0.2342 0.2451 -0.0203 -0.0233 0.0061  285  LEU B CD1 
10997 C CD2 . LEU B 287  ? 0.3066 0.2459 0.2546 -0.0245 -0.0249 0.0106  285  LEU B CD2 
10998 N N   . LEU B 288  ? 0.3032 0.2206 0.2460 -0.0224 -0.0305 0.0127  286  LEU B N   
10999 C CA  . LEU B 288  ? 0.3000 0.2122 0.2381 -0.0260 -0.0313 0.0151  286  LEU B CA  
11000 C C   . LEU B 288  ? 0.3276 0.2355 0.2616 -0.0262 -0.0331 0.0177  286  LEU B C   
11001 O O   . LEU B 288  ? 0.2952 0.2035 0.2257 -0.0297 -0.0328 0.0199  286  LEU B O   
11002 C CB  . LEU B 288  ? 0.3258 0.2316 0.2633 -0.0264 -0.0320 0.0145  286  LEU B CB  
11003 C CG  . LEU B 288  ? 0.3765 0.2752 0.3088 -0.0300 -0.0333 0.0170  286  LEU B CG  
11004 C CD1 . LEU B 288  ? 0.3720 0.2752 0.3030 -0.0348 -0.0319 0.0185  286  LEU B CD1 
11005 C CD2 . LEU B 288  ? 0.4137 0.3051 0.3451 -0.0297 -0.0343 0.0161  286  LEU B CD2 
11006 N N   . PRO B 289  ? 0.3086 0.2128 0.2426 -0.0227 -0.0349 0.0177  287  PRO B N   
11007 C CA  . PRO B 289  ? 0.3276 0.2281 0.2575 -0.0230 -0.0367 0.0204  287  PRO B CA  
11008 C C   . PRO B 289  ? 0.3018 0.2084 0.2306 -0.0243 -0.0358 0.0214  287  PRO B C   
11009 O O   . PRO B 289  ? 0.3291 0.2335 0.2534 -0.0265 -0.0366 0.0240  287  PRO B O   
11010 C CB  . PRO B 289  ? 0.3905 0.2878 0.3220 -0.0183 -0.0385 0.0197  287  PRO B CB  
11011 C CG  . PRO B 289  ? 0.3725 0.2682 0.3072 -0.0165 -0.0380 0.0174  287  PRO B CG  
11012 C CD  . PRO B 289  ? 0.3262 0.2287 0.2636 -0.0185 -0.0355 0.0156  287  PRO B CD  
11013 N N   . ARG B 290  ? 0.2893 0.2035 0.2218 -0.0231 -0.0341 0.0193  288  ARG B N   
11014 C CA  A ARG B 290  ? 0.3098 0.2298 0.2412 -0.0242 -0.0331 0.0199  288  ARG B CA  
11015 C CA  B ARG B 290  ? 0.3098 0.2298 0.2412 -0.0242 -0.0331 0.0199  288  ARG B CA  
11016 C C   . ARG B 290  ? 0.2671 0.1895 0.1961 -0.0286 -0.0314 0.0213  288  ARG B C   
11017 O O   . ARG B 290  ? 0.2824 0.2056 0.2075 -0.0306 -0.0313 0.0233  288  ARG B O   
11018 C CB  A ARG B 290  ? 0.3143 0.2411 0.2502 -0.0217 -0.0317 0.0171  288  ARG B CB  
11019 C CB  B ARG B 290  ? 0.3145 0.2412 0.2503 -0.0217 -0.0318 0.0171  288  ARG B CB  
11020 C CG  A ARG B 290  ? 0.3307 0.2561 0.2687 -0.0178 -0.0335 0.0162  288  ARG B CG  
11021 C CG  B ARG B 290  ? 0.3308 0.2560 0.2690 -0.0177 -0.0335 0.0161  288  ARG B CG  
11022 C CD  A ARG B 290  ? 0.3685 0.2993 0.3119 -0.0154 -0.0323 0.0132  288  ARG B CD  
11023 C CD  B ARG B 290  ? 0.3686 0.2997 0.3118 -0.0154 -0.0323 0.0132  288  ARG B CD  
11024 N NE  A ARG B 290  ? 0.3418 0.2711 0.2878 -0.0118 -0.0340 0.0124  288  ARG B NE  
11025 N NE  B ARG B 290  ? 0.3459 0.2798 0.2893 -0.0136 -0.0330 0.0129  288  ARG B NE  
11026 C CZ  A ARG B 290  ? 0.3757 0.3082 0.3265 -0.0094 -0.0333 0.0100  288  ARG B CZ  
11027 C CZ  B ARG B 290  ? 0.3639 0.2993 0.3111 -0.0106 -0.0338 0.0113  288  ARG B CZ  
11028 N NH1 A ARG B 290  ? 0.3081 0.2451 0.2615 -0.0101 -0.0311 0.0083  288  ARG B NH1 
11029 N NH1 B ARG B 290  ? 0.4261 0.3604 0.3771 -0.0086 -0.0338 0.0100  288  ARG B NH1 
11030 N NH2 A ARG B 290  ? 0.3682 0.2995 0.3214 -0.0063 -0.0349 0.0096  288  ARG B NH2 
11031 N NH2 B ARG B 290  ? 0.3416 0.2798 0.2886 -0.0095 -0.0346 0.0111  288  ARG B NH2 
11032 N N   . VAL B 291  ? 0.2834 0.2069 0.2144 -0.0302 -0.0300 0.0202  289  VAL B N   
11033 C CA  . VAL B 291  ? 0.2786 0.2046 0.2076 -0.0345 -0.0285 0.0218  289  VAL B CA  
11034 C C   . VAL B 291  ? 0.2825 0.2017 0.2064 -0.0374 -0.0301 0.0249  289  VAL B C   
11035 O O   . VAL B 291  ? 0.2999 0.2209 0.2205 -0.0406 -0.0294 0.0272  289  VAL B O   
11036 C CB  . VAL B 291  ? 0.2771 0.2056 0.2095 -0.0357 -0.0271 0.0201  289  VAL B CB  
11037 C CG1 . VAL B 291  ? 0.3245 0.2567 0.2554 -0.0402 -0.0255 0.0218  289  VAL B CG1 
11038 C CG2 . VAL B 291  ? 0.3212 0.2558 0.2585 -0.0327 -0.0257 0.0171  289  VAL B CG2 
11039 N N   . LYS B 292  ? 0.2757 0.1867 0.1985 -0.0362 -0.0322 0.0252  290  LYS B N   
11040 C CA  . LYS B 292  ? 0.3001 0.2036 0.2177 -0.0389 -0.0340 0.0283  290  LYS B CA  
11041 C C   . LYS B 292  ? 0.3376 0.2411 0.2514 -0.0389 -0.0348 0.0306  290  LYS B C   
11042 O O   . LYS B 292  ? 0.3266 0.2287 0.2362 -0.0426 -0.0348 0.0335  290  LYS B O   
11043 C CB  . LYS B 292  ? 0.3338 0.2282 0.2509 -0.0369 -0.0362 0.0280  290  LYS B CB  
11044 C CG  . LYS B 292  ? 0.4004 0.2860 0.3118 -0.0398 -0.0381 0.0311  290  LYS B CG  
11045 C CD  . LYS B 292  ? 0.4749 0.3558 0.3831 -0.0377 -0.0402 0.0331  290  LYS B CD  
11046 C CE  . LYS B 292  ? 0.4697 0.3416 0.3720 -0.0408 -0.0421 0.0364  290  LYS B CE  
11047 N NZ  . LYS B 292  ? 0.4901 0.3530 0.3917 -0.0399 -0.0436 0.0358  290  LYS B NZ  
11048 N N   . ALA B 293  ? 0.3053 0.2107 0.2207 -0.0351 -0.0354 0.0295  291  ALA B N   
11049 C CA  . ALA B 293  ? 0.3294 0.2347 0.2410 -0.0349 -0.0364 0.0315  291  ALA B CA  
11050 C C   . ALA B 293  ? 0.3355 0.2478 0.2454 -0.0379 -0.0341 0.0324  291  ALA B C   
11051 O O   . ALA B 293  ? 0.3215 0.2324 0.2266 -0.0402 -0.0346 0.0353  291  ALA B O   
11052 C CB  . ALA B 293  ? 0.3258 0.2327 0.2400 -0.0303 -0.0374 0.0298  291  ALA B CB  
11053 N N   . LEU B 294  ? 0.3115 0.2313 0.2253 -0.0378 -0.0317 0.0301  292  LEU B N   
11054 C CA  . LEU B 294  ? 0.3122 0.2390 0.2247 -0.0403 -0.0293 0.0308  292  LEU B CA  
11055 C C   . LEU B 294  ? 0.3053 0.2310 0.2151 -0.0452 -0.0285 0.0333  292  LEU B C   
11056 O O   . LEU B 294  ? 0.3196 0.2475 0.2257 -0.0479 -0.0277 0.0357  292  LEU B O   
11057 C CB  . LEU B 294  ? 0.2965 0.2312 0.2139 -0.0388 -0.0269 0.0277  292  LEU B CB  
11058 C CG  . LEU B 294  ? 0.2943 0.2307 0.2145 -0.0344 -0.0275 0.0251  292  LEU B CG  
11059 C CD1 . LEU B 294  ? 0.3113 0.2544 0.2365 -0.0331 -0.0253 0.0221  292  LEU B CD1 
11060 C CD2 . LEU B 294  ? 0.3086 0.2465 0.2251 -0.0337 -0.0279 0.0260  292  LEU B CD2 
11061 N N   . ALA B 295  ? 0.3111 0.2337 0.2228 -0.0464 -0.0288 0.0329  293  ALA B N   
11062 C CA  . ALA B 295  ? 0.3069 0.2280 0.2161 -0.0514 -0.0284 0.0354  293  ALA B CA  
11063 C C   . ALA B 295  ? 0.3386 0.2525 0.2419 -0.0534 -0.0304 0.0390  293  ALA B C   
11064 O O   . ALA B 295  ? 0.3252 0.2402 0.2252 -0.0576 -0.0296 0.0418  293  ALA B O   
11065 C CB  . ALA B 295  ? 0.3186 0.2366 0.2307 -0.0521 -0.0288 0.0341  293  ALA B CB  
11066 N N   . LEU B 296  ? 0.3198 0.2265 0.2216 -0.0504 -0.0330 0.0391  294  LEU B N   
11067 C CA  . LEU B 296  ? 0.3220 0.2215 0.2180 -0.0520 -0.0351 0.0425  294  LEU B CA  
11068 C C   . LEU B 296  ? 0.3499 0.2539 0.2424 -0.0530 -0.0342 0.0445  294  LEU B C   
11069 O O   . LEU B 296  ? 0.3647 0.2664 0.2523 -0.0567 -0.0345 0.0479  294  LEU B O   
11070 C CB  . LEU B 296  ? 0.3755 0.2672 0.2712 -0.0479 -0.0380 0.0420  294  LEU B CB  
11071 C CG  . LEU B 296  ? 0.4457 0.3285 0.3355 -0.0487 -0.0406 0.0455  294  LEU B CG  
11072 C CD1 . LEU B 296  ? 0.4763 0.3538 0.3627 -0.0537 -0.0408 0.0481  294  LEU B CD1 
11073 C CD2 . LEU B 296  ? 0.5203 0.3963 0.4111 -0.0441 -0.0432 0.0444  294  LEU B CD2 
11074 N N   . LEU B 297  ? 0.3291 0.2394 0.2237 -0.0499 -0.0333 0.0424  295  LEU B N   
11075 C CA  . LEU B 297  ? 0.3319 0.2472 0.2231 -0.0509 -0.0321 0.0438  295  LEU B CA  
11076 C C   . LEU B 297  ? 0.3331 0.2546 0.2238 -0.0552 -0.0292 0.0451  295  LEU B C   
11077 O O   . LEU B 297  ? 0.3494 0.2715 0.2353 -0.0581 -0.0288 0.0480  295  LEU B O   
11078 C CB  . LEU B 297  ? 0.3184 0.2395 0.2124 -0.0469 -0.0314 0.0409  295  LEU B CB  
11079 C CG  . LEU B 297  ? 0.4140 0.3309 0.3077 -0.0428 -0.0341 0.0402  295  LEU B CG  
11080 C CD1 . LEU B 297  ? 0.3754 0.2990 0.2725 -0.0395 -0.0330 0.0369  295  LEU B CD1 
11081 C CD2 . LEU B 297  ? 0.4137 0.3264 0.3012 -0.0437 -0.0360 0.0435  295  LEU B CD2 
11082 N N   . ALA B 298  ? 0.3001 0.2267 0.1956 -0.0557 -0.0273 0.0429  296  ALA B N   
11083 C CA  . ALA B 298  ? 0.3014 0.2348 0.1970 -0.0597 -0.0245 0.0441  296  ALA B CA  
11084 C C   . ALA B 298  ? 0.3454 0.2737 0.2371 -0.0646 -0.0253 0.0478  296  ALA B C   
11085 O O   . ALA B 298  ? 0.3540 0.2861 0.2428 -0.0682 -0.0238 0.0504  296  ALA B O   
11086 C CB  . ALA B 298  ? 0.3164 0.2554 0.2181 -0.0591 -0.0227 0.0411  296  ALA B CB  
11087 N N   . LYS B 299  ? 0.3312 0.2507 0.2227 -0.0649 -0.0278 0.0481  297  LYS B N   
11088 C CA  . LYS B 299  ? 0.3617 0.2750 0.2491 -0.0696 -0.0290 0.0517  297  LYS B CA  
11089 C C   . LYS B 299  ? 0.4000 0.3097 0.2810 -0.0707 -0.0301 0.0551  297  LYS B C   
11090 O O   . LYS B 299  ? 0.4050 0.3149 0.2823 -0.0754 -0.0295 0.0585  297  LYS B O   
11091 C CB  . LYS B 299  ? 0.3839 0.2875 0.2719 -0.0688 -0.0315 0.0510  297  LYS B CB  
11092 C CG  . LYS B 299  ? 0.4377 0.3325 0.3204 -0.0731 -0.0335 0.0547  297  LYS B CG  
11093 C CD  . LYS B 299  ? 0.5322 0.4155 0.4136 -0.0707 -0.0366 0.0543  297  LYS B CD  
11094 C CE  . LYS B 299  ? 0.5145 0.3885 0.3906 -0.0751 -0.0386 0.0579  297  LYS B CE  
11095 N NZ  . LYS B 299  ? 0.5822 0.4543 0.4525 -0.0770 -0.0392 0.0618  297  LYS B NZ  
11096 N N   . ASN B 300  ? 0.3639 0.2707 0.2435 -0.0666 -0.0317 0.0545  298  ASN B N   
11097 C CA  . ASN B 300  ? 0.4001 0.3031 0.2734 -0.0675 -0.0330 0.0579  298  ASN B CA  
11098 C C   . ASN B 300  ? 0.3767 0.2882 0.2477 -0.0700 -0.0303 0.0594  298  ASN B C   
11099 O O   . ASN B 300  ? 0.4026 0.3118 0.2680 -0.0732 -0.0307 0.0631  298  ASN B O   
11100 C CB  . ASN B 300  ? 0.4146 0.3136 0.2873 -0.0625 -0.0354 0.0567  298  ASN B CB  
11101 C CG  . ASN B 300  ? 0.4382 0.3273 0.3116 -0.0603 -0.0384 0.0563  298  ASN B CG  
11102 O OD1 . ASN B 300  ? 0.5245 0.4073 0.3965 -0.0632 -0.0394 0.0579  298  ASN B OD1 
11103 N ND2 . ASN B 300  ? 0.5224 0.4102 0.3980 -0.0553 -0.0400 0.0541  298  ASN B ND2 
11104 N N   . TYR B 301  ? 0.3464 0.2676 0.2214 -0.0685 -0.0275 0.0566  299  TYR B N   
11105 C CA  . TYR B 301  ? 0.3484 0.2782 0.2216 -0.0706 -0.0246 0.0578  299  TYR B CA  
11106 C C   . TYR B 301  ? 0.3332 0.2682 0.2082 -0.0752 -0.0221 0.0590  299  TYR B C   
11107 O O   . TYR B 301  ? 0.3543 0.2970 0.2279 -0.0774 -0.0195 0.0602  299  TYR B O   
11108 C CB  . TYR B 301  ? 0.3174 0.2549 0.1936 -0.0665 -0.0228 0.0542  299  TYR B CB  
11109 C CG  . TYR B 301  ? 0.3539 0.2884 0.2274 -0.0626 -0.0247 0.0535  299  TYR B CG  
11110 C CD1 . TYR B 301  ? 0.3558 0.2896 0.2229 -0.0636 -0.0250 0.0562  299  TYR B CD1 
11111 C CD2 . TYR B 301  ? 0.3286 0.2613 0.2059 -0.0580 -0.0262 0.0501  299  TYR B CD2 
11112 C CE1 . TYR B 301  ? 0.3564 0.2876 0.2210 -0.0602 -0.0270 0.0555  299  TYR B CE1 
11113 C CE2 . TYR B 301  ? 0.3685 0.2989 0.2437 -0.0546 -0.0281 0.0495  299  TYR B CE2 
11114 C CZ  . TYR B 301  ? 0.3592 0.2889 0.2280 -0.0558 -0.0285 0.0522  299  TYR B CZ  
11115 O OH  . TYR B 301  ? 0.3774 0.3050 0.2440 -0.0526 -0.0306 0.0516  299  TYR B OH  
11116 N N   . ASP B 302  ? 0.3279 0.2593 0.2060 -0.0768 -0.0230 0.0585  300  ASP B N   
11117 C CA  . ASP B 302  ? 0.3607 0.2973 0.2414 -0.0810 -0.0210 0.0592  300  ASP B CA  
11118 C C   . ASP B 302  ? 0.3269 0.2756 0.2121 -0.0798 -0.0175 0.0569  300  ASP B C   
11119 O O   . ASP B 302  ? 0.3518 0.3081 0.2365 -0.0831 -0.0149 0.0587  300  ASP B O   
11120 C CB  . ASP B 302  ? 0.3775 0.3121 0.2534 -0.0869 -0.0211 0.0640  300  ASP B CB  
11121 C CG  . ASP B 302  ? 0.4281 0.3647 0.3069 -0.0915 -0.0203 0.0647  300  ASP B CG  
11122 O OD1 . ASP B 302  ? 0.4641 0.3987 0.3472 -0.0901 -0.0212 0.0620  300  ASP B OD1 
11123 O OD2 . ASP B 302  ? 0.4738 0.4145 0.3507 -0.0965 -0.0188 0.0679  300  ASP B OD2 
11124 N N   . ILE B 303  ? 0.3207 0.2714 0.2102 -0.0750 -0.0174 0.0529  301  ILE B N   
11125 C CA  . ILE B 303  ? 0.3157 0.2767 0.2099 -0.0733 -0.0144 0.0502  301  ILE B CA  
11126 C C   . ILE B 303  ? 0.3298 0.2906 0.2299 -0.0723 -0.0147 0.0475  301  ILE B C   
11127 O O   . ILE B 303  ? 0.3210 0.2736 0.2214 -0.0717 -0.0173 0.0470  301  ILE B O   
11128 C CB  . ILE B 303  ? 0.2914 0.2556 0.1853 -0.0684 -0.0137 0.0478  301  ILE B CB  
11129 C CG1 . ILE B 303  ? 0.3246 0.2825 0.2206 -0.0640 -0.0162 0.0449  301  ILE B CG1 
11130 C CG2 . ILE B 303  ? 0.3097 0.2728 0.1971 -0.0693 -0.0138 0.0504  301  ILE B CG2 
11131 C CD1 . ILE B 303  ? 0.3350 0.2969 0.2321 -0.0593 -0.0154 0.0418  301  ILE B CD1 
11132 N N   . GLY B 304  ? 0.2901 0.2603 0.1948 -0.0720 -0.0120 0.0457  302  GLY B N   
11133 C CA  . GLY B 304  ? 0.2841 0.2550 0.1944 -0.0707 -0.0122 0.0429  302  GLY B CA  
11134 C C   . GLY B 304  ? 0.3303 0.2998 0.2431 -0.0650 -0.0129 0.0392  302  GLY B C   
11135 O O   . GLY B 304  ? 0.3196 0.2921 0.2316 -0.0619 -0.0120 0.0380  302  GLY B O   
11136 N N   . LEU B 305  ? 0.2727 0.2374 0.1885 -0.0637 -0.0146 0.0374  303  LEU B N   
11137 C CA  . LEU B 305  ? 0.2848 0.2488 0.2038 -0.0586 -0.0151 0.0338  303  LEU B CA  
11138 C C   . LEU B 305  ? 0.2752 0.2424 0.1996 -0.0585 -0.0144 0.0317  303  LEU B C   
11139 O O   . LEU B 305  ? 0.2959 0.2582 0.2208 -0.0606 -0.0158 0.0321  303  LEU B O   
11140 C CB  . LEU B 305  ? 0.3050 0.2592 0.2220 -0.0565 -0.0182 0.0336  303  LEU B CB  
11141 C CG  . LEU B 305  ? 0.3250 0.2787 0.2453 -0.0514 -0.0188 0.0301  303  LEU B CG  
11142 C CD1 . LEU B 305  ? 0.3608 0.3087 0.2781 -0.0488 -0.0209 0.0305  303  LEU B CD1 
11143 C CD2 . LEU B 305  ? 0.3807 0.3312 0.3048 -0.0507 -0.0197 0.0284  303  LEU B CD2 
11144 N N   . ASN B 306  ? 0.2623 0.2372 0.1904 -0.0561 -0.0122 0.0293  304  ASN B N   
11145 C CA  . ASN B 306  ? 0.2680 0.2473 0.2012 -0.0562 -0.0112 0.0276  304  ASN B CA  
11146 C C   . ASN B 306  ? 0.2600 0.2378 0.1966 -0.0515 -0.0118 0.0241  304  ASN B C   
11147 O O   . ASN B 306  ? 0.2648 0.2438 0.2014 -0.0481 -0.0115 0.0226  304  ASN B O   
11148 C CB  . ASN B 306  ? 0.2714 0.2614 0.2068 -0.0568 -0.0081 0.0276  304  ASN B CB  
11149 C CG  . ASN B 306  ? 0.2862 0.2811 0.2269 -0.0563 -0.0071 0.0256  304  ASN B CG  
11150 O OD1 . ASN B 306  ? 0.3160 0.3112 0.2580 -0.0596 -0.0075 0.0267  304  ASN B OD1 
11151 N ND2 . ASN B 306  ? 0.2632 0.2619 0.2070 -0.0521 -0.0060 0.0228  304  ASN B ND2 
11152 N N   . ILE B 307  ? 0.2546 0.2300 0.1941 -0.0517 -0.0127 0.0229  305  ILE B N   
11153 C CA  . ILE B 307  ? 0.2554 0.2302 0.1985 -0.0476 -0.0131 0.0197  305  ILE B CA  
11154 C C   . ILE B 307  ? 0.2663 0.2498 0.2139 -0.0470 -0.0108 0.0182  305  ILE B C   
11155 O O   . ILE B 307  ? 0.2347 0.2205 0.1841 -0.0497 -0.0105 0.0186  305  ILE B O   
11156 C CB  . ILE B 307  ? 0.2685 0.2355 0.2119 -0.0477 -0.0153 0.0191  305  ILE B CB  
11157 C CG1 . ILE B 307  ? 0.3025 0.2607 0.2415 -0.0476 -0.0177 0.0206  305  ILE B CG1 
11158 C CG2 . ILE B 307  ? 0.2807 0.2485 0.2283 -0.0438 -0.0153 0.0159  305  ILE B CG2 
11159 C CD1 . ILE B 307  ? 0.3489 0.2988 0.2875 -0.0478 -0.0198 0.0203  305  ILE B CD1 
11160 N N   . ASP B 308  ? 0.2461 0.2341 0.1953 -0.0436 -0.0095 0.0163  306  ASP B N   
11161 C CA  . ASP B 308  ? 0.2520 0.2478 0.2054 -0.0424 -0.0074 0.0147  306  ASP B CA  
11162 C C   . ASP B 308  ? 0.2361 0.2302 0.1931 -0.0411 -0.0082 0.0127  306  ASP B C   
11163 O O   . ASP B 308  ? 0.2587 0.2460 0.2154 -0.0397 -0.0101 0.0119  306  ASP B O   
11164 C CB  . ASP B 308  ? 0.2314 0.2308 0.1851 -0.0386 -0.0060 0.0130  306  ASP B CB  
11165 C CG  . ASP B 308  ? 0.2920 0.2946 0.2421 -0.0397 -0.0047 0.0147  306  ASP B CG  
11166 O OD1 . ASP B 308  ? 0.2735 0.2779 0.2218 -0.0434 -0.0042 0.0172  306  ASP B OD1 
11167 O OD2 . ASP B 308  ? 0.2793 0.2827 0.2281 -0.0368 -0.0042 0.0135  306  ASP B OD2 
11168 N N   . ALA B 309  ? 0.2137 0.2141 0.1742 -0.0417 -0.0068 0.0122  307  ALA B N   
11169 C CA  . ALA B 309  ? 0.2006 0.2001 0.1644 -0.0407 -0.0074 0.0104  307  ALA B CA  
11170 C C   . ALA B 309  ? 0.2343 0.2371 0.2012 -0.0364 -0.0063 0.0078  307  ALA B C   
11171 O O   . ALA B 309  ? 0.2257 0.2347 0.1935 -0.0351 -0.0044 0.0075  307  ALA B O   
11172 C CB  . ALA B 309  ? 0.2249 0.2290 0.1907 -0.0440 -0.0068 0.0113  307  ALA B CB  
11173 N N   . GLU B 310  ? 0.2038 0.2023 0.1722 -0.0342 -0.0075 0.0059  308  GLU B N   
11174 C CA  . GLU B 310  ? 0.2115 0.2121 0.1825 -0.0302 -0.0068 0.0036  308  GLU B CA  
11175 C C   . GLU B 310  ? 0.1859 0.1885 0.1606 -0.0295 -0.0066 0.0022  308  GLU B C   
11176 O O   . GLU B 310  ? 0.2009 0.2077 0.1770 -0.0318 -0.0059 0.0029  308  GLU B O   
11177 C CB  . GLU B 310  ? 0.1954 0.1899 0.1649 -0.0277 -0.0083 0.0028  308  GLU B CB  
11178 C CG  . GLU B 310  ? 0.2287 0.2217 0.1942 -0.0284 -0.0085 0.0043  308  GLU B CG  
11179 C CD  . GLU B 310  ? 0.2494 0.2372 0.2135 -0.0260 -0.0100 0.0036  308  GLU B CD  
11180 O OE1 . GLU B 310  ? 0.2685 0.2581 0.2339 -0.0231 -0.0095 0.0020  308  GLU B OE1 
11181 O OE2 . GLU B 310  ? 0.2475 0.2293 0.2092 -0.0269 -0.0118 0.0048  308  GLU B OE2 
11182 N N   . GLU B 311  ? 0.2158 0.2157 0.1922 -0.0265 -0.0072 0.0002  309  GLU B N   
11183 C CA  . GLU B 311  ? 0.1894 0.1914 0.1691 -0.0256 -0.0069 -0.0012 309  GLU B CA  
11184 C C   . GLU B 311  ? 0.2011 0.2001 0.1804 -0.0283 -0.0081 -0.0006 309  GLU B C   
11185 O O   . GLU B 311  ? 0.2113 0.2046 0.1878 -0.0301 -0.0095 0.0005  309  GLU B O   
11186 C CB  . GLU B 311  ? 0.2019 0.2013 0.1832 -0.0220 -0.0073 -0.0032 309  GLU B CB  
11187 C CG  . GLU B 311  ? 0.2521 0.2544 0.2339 -0.0193 -0.0062 -0.0041 309  GLU B CG  
11188 C CD  . GLU B 311  ? 0.3178 0.3164 0.2969 -0.0185 -0.0071 -0.0037 309  GLU B CD  
11189 O OE1 . GLU B 311  ? 0.2371 0.2316 0.2135 -0.0204 -0.0082 -0.0023 309  GLU B OE1 
11190 O OE2 . GLU B 311  ? 0.3402 0.3398 0.3197 -0.0161 -0.0066 -0.0048 309  GLU B OE2 
11191 N N   . ALA B 312  ? 0.1948 0.1976 0.1769 -0.0286 -0.0076 -0.0012 310  ALA B N   
11192 C CA  . ALA B 312  ? 0.1940 0.1944 0.1755 -0.0315 -0.0087 -0.0008 310  ALA B CA  
11193 C C   . ALA B 312  ? 0.1930 0.1851 0.1728 -0.0307 -0.0105 -0.0016 310  ALA B C   
11194 O O   . ALA B 312  ? 0.2137 0.2013 0.1912 -0.0334 -0.0118 -0.0008 310  ALA B O   
11195 C CB  . ALA B 312  ? 0.2099 0.2158 0.1947 -0.0313 -0.0080 -0.0016 310  ALA B CB  
11196 N N   . ASP B 313  ? 0.2027 0.1927 0.1835 -0.0271 -0.0105 -0.0032 311  ASP B N   
11197 C CA  . ASP B 313  ? 0.2282 0.2109 0.2077 -0.0259 -0.0120 -0.0041 311  ASP B CA  
11198 C C   . ASP B 313  ? 0.2386 0.2154 0.2148 -0.0264 -0.0132 -0.0029 311  ASP B C   
11199 O O   . ASP B 313  ? 0.2402 0.2107 0.2151 -0.0253 -0.0145 -0.0035 311  ASP B O   
11200 C CB  . ASP B 313  ? 0.2452 0.2280 0.2272 -0.0221 -0.0116 -0.0061 311  ASP B CB  
11201 C CG  . ASP B 313  ? 0.2963 0.2808 0.2792 -0.0195 -0.0110 -0.0064 311  ASP B CG  
11202 O OD1 . ASP B 313  ? 0.2765 0.2616 0.2578 -0.0202 -0.0109 -0.0052 311  ASP B OD1 
11203 O OD2 . ASP B 313  ? 0.3038 0.2888 0.2890 -0.0166 -0.0107 -0.0079 311  ASP B OD2 
11204 N N   . ARG B 314  ? 0.2137 0.1924 0.1884 -0.0280 -0.0129 -0.0013 312  ARG B N   
11205 C CA  . ARG B 314  ? 0.2387 0.2120 0.2099 -0.0289 -0.0141 0.0002  312  ARG B CA  
11206 C C   . ARG B 314  ? 0.2258 0.1973 0.1941 -0.0332 -0.0147 0.0022  312  ARG B C   
11207 O O   . ARG B 314  ? 0.2377 0.2037 0.2027 -0.0343 -0.0160 0.0036  312  ARG B O   
11208 C CB  . ARG B 314  ? 0.2144 0.1902 0.1852 -0.0275 -0.0134 0.0007  312  ARG B CB  
11209 C CG  . ARG B 314  ? 0.2187 0.1933 0.1911 -0.0235 -0.0136 -0.0010 312  ARG B CG  
11210 C CD  . ARG B 314  ? 0.2387 0.2175 0.2114 -0.0220 -0.0126 -0.0011 312  ARG B CD  
11211 N NE  . ARG B 314  ? 0.2268 0.2032 0.2004 -0.0188 -0.0134 -0.0023 312  ARG B NE  
11212 C CZ  . ARG B 314  ? 0.2453 0.2243 0.2193 -0.0170 -0.0128 -0.0028 312  ARG B CZ  
11213 N NH1 . ARG B 314  ? 0.2534 0.2375 0.2271 -0.0176 -0.0114 -0.0026 312  ARG B NH1 
11214 N NH2 . ARG B 314  ? 0.2560 0.2323 0.2305 -0.0146 -0.0139 -0.0036 312  ARG B NH2 
11215 N N   . LEU B 315  ? 0.2169 0.1930 0.1866 -0.0358 -0.0140 0.0025  313  LEU B N   
11216 C CA  . LEU B 315  ? 0.2181 0.1936 0.1854 -0.0403 -0.0145 0.0047  313  LEU B CA  
11217 C C   . LEU B 315  ? 0.2359 0.2020 0.1997 -0.0418 -0.0166 0.0051  313  LEU B C   
11218 O O   . LEU B 315  ? 0.2405 0.2023 0.2009 -0.0438 -0.0176 0.0070  313  LEU B O   
11219 C CB  . LEU B 315  ? 0.2377 0.2197 0.2075 -0.0426 -0.0136 0.0047  313  LEU B CB  
11220 C CG  . LEU B 315  ? 0.2300 0.2152 0.1986 -0.0474 -0.0134 0.0072  313  LEU B CG  
11221 C CD1 . LEU B 315  ? 0.2455 0.2379 0.2175 -0.0488 -0.0126 0.0068  313  LEU B CD1 
11222 C CD2 . LEU B 315  ? 0.2789 0.2562 0.2435 -0.0510 -0.0154 0.0086  313  LEU B CD2 
11223 N N   . GLU B 316  ? 0.2449 0.2077 0.2095 -0.0407 -0.0174 0.0033  314  GLU B N   
11224 C CA  . GLU B 316  ? 0.2627 0.2165 0.2237 -0.0423 -0.0194 0.0036  314  GLU B CA  
11225 C C   . GLU B 316  ? 0.2621 0.2089 0.2207 -0.0398 -0.0205 0.0037  314  GLU B C   
11226 O O   . GLU B 316  ? 0.2697 0.2095 0.2244 -0.0418 -0.0220 0.0051  314  GLU B O   
11227 C CB  . GLU B 316  ? 0.2881 0.2402 0.2500 -0.0419 -0.0199 0.0016  314  GLU B CB  
11228 C CG  . GLU B 316  ? 0.2643 0.2225 0.2278 -0.0453 -0.0193 0.0020  314  GLU B CG  
11229 C CD  . GLU B 316  ? 0.3139 0.2708 0.2781 -0.0452 -0.0199 0.0001  314  GLU B CD  
11230 O OE1 . GLU B 316  ? 0.3123 0.2609 0.2735 -0.0448 -0.0213 -0.0008 314  GLU B OE1 
11231 O OE2 . GLU B 316  ? 0.2957 0.2597 0.2630 -0.0453 -0.0188 -0.0005 314  GLU B OE2 
11232 N N   . LEU B 317  ? 0.2851 0.2337 0.2459 -0.0356 -0.0198 0.0025  315  LEU B N   
11233 C CA  . LEU B 317  ? 0.2920 0.2352 0.2510 -0.0332 -0.0209 0.0028  315  LEU B CA  
11234 C C   . LEU B 317  ? 0.2949 0.2370 0.2508 -0.0357 -0.0213 0.0054  315  LEU B C   
11235 O O   . LEU B 317  ? 0.2951 0.2301 0.2476 -0.0359 -0.0229 0.0065  315  LEU B O   
11236 C CB  . LEU B 317  ? 0.2927 0.2396 0.2549 -0.0290 -0.0199 0.0013  315  LEU B CB  
11237 C CG  . LEU B 317  ? 0.3129 0.2551 0.2739 -0.0262 -0.0211 0.0015  315  LEU B CG  
11238 C CD1 . LEU B 317  ? 0.3447 0.2785 0.3036 -0.0254 -0.0227 0.0012  315  LEU B CD1 
11239 C CD2 . LEU B 317  ? 0.3303 0.2767 0.2950 -0.0224 -0.0202 -0.0002 315  LEU B CD2 
11240 N N   . SER B 318  ? 0.2681 0.2174 0.2250 -0.0374 -0.0198 0.0064  316  SER B N   
11241 C CA  . SER B 318  ? 0.2664 0.2152 0.2201 -0.0397 -0.0201 0.0090  316  SER B CA  
11242 C C   . SER B 318  ? 0.2683 0.2114 0.2183 -0.0439 -0.0214 0.0109  316  SER B C   
11243 O O   . SER B 318  ? 0.2936 0.2324 0.2400 -0.0454 -0.0224 0.0130  316  SER B O   
11244 C CB  . SER B 318  ? 0.2601 0.2179 0.2155 -0.0408 -0.0180 0.0097  316  SER B CB  
11245 O OG  . SER B 318  ? 0.2570 0.2194 0.2136 -0.0440 -0.0171 0.0101  316  SER B OG  
11246 N N   . LEU B 319  ? 0.2415 0.1841 0.1921 -0.0461 -0.0217 0.0103  317  LEU B N   
11247 C CA  . LEU B 319  ? 0.2652 0.2018 0.2120 -0.0504 -0.0232 0.0121  317  LEU B CA  
11248 C C   . LEU B 319  ? 0.3029 0.2287 0.2461 -0.0490 -0.0253 0.0121  317  LEU B C   
11249 O O   . LEU B 319  ? 0.3108 0.2306 0.2498 -0.0521 -0.0267 0.0143  317  LEU B O   
11250 C CB  . LEU B 319  ? 0.2813 0.2196 0.2296 -0.0528 -0.0231 0.0111  317  LEU B CB  
11251 C CG  . LEU B 319  ? 0.2771 0.2260 0.2289 -0.0547 -0.0212 0.0114  317  LEU B CG  
11252 C CD1 . LEU B 319  ? 0.2839 0.2336 0.2371 -0.0564 -0.0216 0.0101  317  LEU B CD1 
11253 C CD2 . LEU B 319  ? 0.3057 0.2578 0.2558 -0.0590 -0.0208 0.0145  317  LEU B CD2 
11254 N N   . ASP B 320  ? 0.2990 0.2221 0.2436 -0.0445 -0.0256 0.0099  318  ASP B N   
11255 C CA  . ASP B 320  ? 0.3261 0.2394 0.2675 -0.0426 -0.0276 0.0100  318  ASP B CA  
11256 C C   . ASP B 320  ? 0.3123 0.2234 0.2512 -0.0422 -0.0282 0.0122  318  ASP B C   
11257 O O   . ASP B 320  ? 0.3643 0.2669 0.2992 -0.0427 -0.0301 0.0135  318  ASP B O   
11258 C CB  . ASP B 320  ? 0.3086 0.2209 0.2526 -0.0377 -0.0275 0.0072  318  ASP B CB  
11259 C CG  . ASP B 320  ? 0.3314 0.2420 0.2760 -0.0382 -0.0275 0.0053  318  ASP B CG  
11260 O OD1 . ASP B 320  ? 0.3692 0.2726 0.3100 -0.0407 -0.0290 0.0058  318  ASP B OD1 
11261 O OD2 . ASP B 320  ? 0.3385 0.2547 0.2868 -0.0362 -0.0262 0.0033  318  ASP B OD2 
11262 N N   . LEU B 321  ? 0.2720 0.1904 0.2130 -0.0413 -0.0268 0.0126  319  LEU B N   
11263 C CA  . LEU B 321  ? 0.2973 0.2142 0.2355 -0.0414 -0.0275 0.0148  319  LEU B CA  
11264 C C   . LEU B 321  ? 0.3163 0.2325 0.2510 -0.0466 -0.0276 0.0177  319  LEU B C   
11265 O O   . LEU B 321  ? 0.3338 0.2436 0.2642 -0.0478 -0.0291 0.0199  319  LEU B O   
11266 C CB  . LEU B 321  ? 0.3054 0.2298 0.2463 -0.0388 -0.0260 0.0142  319  LEU B CB  
11267 C CG  . LEU B 321  ? 0.3000 0.2238 0.2435 -0.0338 -0.0263 0.0121  319  LEU B CG  
11268 C CD1 . LEU B 321  ? 0.3199 0.2482 0.2678 -0.0321 -0.0250 0.0093  319  LEU B CD1 
11269 C CD2 . LEU B 321  ? 0.3290 0.2568 0.2728 -0.0319 -0.0260 0.0126  319  LEU B CD2 
11270 N N   . LEU B 322  ? 0.2929 0.2156 0.2292 -0.0498 -0.0261 0.0179  320  LEU B N   
11271 C CA  . LEU B 322  ? 0.2878 0.2108 0.2212 -0.0550 -0.0261 0.0209  320  LEU B CA  
11272 C C   . LEU B 322  ? 0.3048 0.2174 0.2339 -0.0576 -0.0284 0.0221  320  LEU B C   
11273 O O   . LEU B 322  ? 0.3396 0.2481 0.2646 -0.0605 -0.0294 0.0249  320  LEU B O   
11274 C CB  . LEU B 322  ? 0.2878 0.2196 0.2243 -0.0578 -0.0243 0.0206  320  LEU B CB  
11275 C CG  . LEU B 322  ? 0.3163 0.2497 0.2504 -0.0636 -0.0241 0.0237  320  LEU B CG  
11276 C CD1 . LEU B 322  ? 0.3096 0.2456 0.2416 -0.0639 -0.0233 0.0260  320  LEU B CD1 
11277 C CD2 . LEU B 322  ? 0.3073 0.2495 0.2451 -0.0661 -0.0225 0.0233  320  LEU B CD2 
11278 N N   . GLU B 323  ? 0.2994 0.2074 0.2292 -0.0564 -0.0294 0.0199  321  GLU B N   
11279 C CA  . GLU B 323  ? 0.3404 0.2377 0.2658 -0.0585 -0.0316 0.0207  321  GLU B CA  
11280 C C   . GLU B 323  ? 0.3696 0.2584 0.2910 -0.0567 -0.0334 0.0221  321  GLU B C   
11281 O O   . GLU B 323  ? 0.3887 0.2708 0.3056 -0.0600 -0.0349 0.0246  321  GLU B O   
11282 C CB  . GLU B 323  ? 0.3701 0.2642 0.2970 -0.0564 -0.0321 0.0176  321  GLU B CB  
11283 C CG  . GLU B 323  ? 0.4485 0.3304 0.3707 -0.0575 -0.0345 0.0178  321  GLU B CG  
11284 C CD  . GLU B 323  ? 0.4741 0.3545 0.3946 -0.0630 -0.0351 0.0184  321  GLU B CD  
11285 O OE1 . GLU B 323  ? 0.4443 0.3336 0.3681 -0.0652 -0.0336 0.0181  321  GLU B OE1 
11286 O OE2 . GLU B 323  ? 0.4469 0.3171 0.3626 -0.0651 -0.0372 0.0192  321  GLU B OE2 
11287 N N   . VAL B 324  ? 0.3318 0.2206 0.2550 -0.0514 -0.0333 0.0207  322  VAL B N   
11288 C CA  . VAL B 324  ? 0.3621 0.2433 0.2819 -0.0491 -0.0351 0.0220  322  VAL B CA  
11289 C C   . VAL B 324  ? 0.3456 0.2280 0.2624 -0.0520 -0.0352 0.0254  322  VAL B C   
11290 O O   . VAL B 324  ? 0.3857 0.2600 0.2978 -0.0535 -0.0370 0.0277  322  VAL B O   
11291 C CB  . VAL B 324  ? 0.3652 0.2477 0.2881 -0.0430 -0.0350 0.0198  322  VAL B CB  
11292 C CG1 . VAL B 324  ? 0.3645 0.2405 0.2843 -0.0407 -0.0369 0.0215  322  VAL B CG1 
11293 C CG2 . VAL B 324  ? 0.4261 0.3062 0.3513 -0.0403 -0.0351 0.0167  322  VAL B CG2 
11294 N N   . LEU B 325  ? 0.3142 0.2065 0.2335 -0.0527 -0.0332 0.0257  323  LEU B N   
11295 C CA  . LEU B 325  ? 0.3618 0.2560 0.2783 -0.0551 -0.0330 0.0287  323  LEU B CA  
11296 C C   . LEU B 325  ? 0.3507 0.2413 0.2632 -0.0610 -0.0336 0.0316  323  LEU B C   
11297 O O   . LEU B 325  ? 0.3642 0.2500 0.2721 -0.0628 -0.0348 0.0346  323  LEU B O   
11298 C CB  . LEU B 325  ? 0.3322 0.2379 0.2521 -0.0547 -0.0304 0.0282  323  LEU B CB  
11299 C CG  . LEU B 325  ? 0.3270 0.2356 0.2502 -0.0491 -0.0301 0.0257  323  LEU B CG  
11300 C CD1 . LEU B 325  ? 0.3768 0.2964 0.3040 -0.0485 -0.0275 0.0243  323  LEU B CD1 
11301 C CD2 . LEU B 325  ? 0.3253 0.2300 0.2454 -0.0471 -0.0315 0.0273  323  LEU B CD2 
11302 N N   . CYS B 326  ? 0.3399 0.2329 0.2540 -0.0642 -0.0329 0.0310  324  CYS B N   
11303 C CA  . CYS B 326  ? 0.3469 0.2370 0.2575 -0.0703 -0.0335 0.0338  324  CYS B CA  
11304 C C   . CYS B 326  ? 0.3677 0.2446 0.2732 -0.0713 -0.0364 0.0349  324  CYS B C   
11305 O O   . CYS B 326  ? 0.3601 0.2328 0.2615 -0.0761 -0.0373 0.0380  324  CYS B O   
11306 C CB  . CYS B 326  ? 0.3715 0.2679 0.2854 -0.0734 -0.0323 0.0327  324  CYS B CB  
11307 S SG  . CYS B 326  ? 0.4140 0.3259 0.3329 -0.0736 -0.0289 0.0325  324  CYS B SG  
11308 N N   . LEU B 327  ? 0.3606 0.2308 0.2663 -0.0669 -0.0377 0.0325  325  LEU B N   
11309 C CA  . LEU B 327  ? 0.4025 0.2595 0.3032 -0.0669 -0.0404 0.0333  325  LEU B CA  
11310 C C   . LEU B 327  ? 0.4526 0.3041 0.3506 -0.0633 -0.0418 0.0346  325  LEU B C   
11311 O O   . LEU B 327  ? 0.4583 0.2986 0.3522 -0.0625 -0.0441 0.0352  325  LEU B O   
11312 C CB  . LEU B 327  ? 0.3609 0.2134 0.2631 -0.0642 -0.0411 0.0299  325  LEU B CB  
11313 C CG  . LEU B 327  ? 0.4475 0.3045 0.3519 -0.0677 -0.0401 0.0285  325  LEU B CG  
11314 C CD1 . LEU B 327  ? 0.5018 0.3542 0.4073 -0.0645 -0.0407 0.0250  325  LEU B CD1 
11315 C CD2 . LEU B 327  ? 0.5134 0.3665 0.4138 -0.0745 -0.0411 0.0313  325  LEU B CD2 
11316 N N   . ASP B 328  ? 0.4052 0.2641 0.3052 -0.0612 -0.0405 0.0350  326  ASP B N   
11317 C CA  . ASP B 328  ? 0.4125 0.2671 0.3102 -0.0577 -0.0419 0.0363  326  ASP B CA  
11318 C C   . ASP B 328  ? 0.4226 0.2730 0.3147 -0.0619 -0.0430 0.0405  326  ASP B C   
11319 O O   . ASP B 328  ? 0.4259 0.2836 0.3180 -0.0650 -0.0414 0.0423  326  ASP B O   
11320 C CB  . ASP B 328  ? 0.3939 0.2582 0.2959 -0.0540 -0.0402 0.0349  326  ASP B CB  
11321 C CG  . ASP B 328  ? 0.4834 0.3438 0.3839 -0.0496 -0.0418 0.0355  326  ASP B CG  
11322 O OD1 . ASP B 328  ? 0.4691 0.3211 0.3647 -0.0505 -0.0439 0.0382  326  ASP B OD1 
11323 O OD2 . ASP B 328  ? 0.5023 0.3681 0.4067 -0.0454 -0.0411 0.0335  326  ASP B OD2 
11324 N N   . GLY B 329  ? 0.4389 0.2774 0.3261 -0.0618 -0.0456 0.0420  327  GLY B N   
11325 C CA  . GLY B 329  ? 0.4372 0.2706 0.3187 -0.0657 -0.0468 0.0462  327  GLY B CA  
11326 C C   . GLY B 329  ? 0.4478 0.2862 0.3285 -0.0647 -0.0463 0.0483  327  GLY B C   
11327 O O   . GLY B 329  ? 0.4536 0.2915 0.3303 -0.0689 -0.0464 0.0518  327  GLY B O   
11328 N N   . ASP B 330  ? 0.4437 0.2870 0.3279 -0.0594 -0.0458 0.0462  328  ASP B N   
11329 C CA  . ASP B 330  ? 0.3921 0.2410 0.2756 -0.0586 -0.0453 0.0479  328  ASP B CA  
11330 C C   . ASP B 330  ? 0.4731 0.3322 0.3575 -0.0628 -0.0426 0.0488  328  ASP B C   
11331 O O   . ASP B 330  ? 0.4566 0.3187 0.3384 -0.0640 -0.0422 0.0512  328  ASP B O   
11332 C CB  . ASP B 330  ? 0.4594 0.3125 0.3470 -0.0524 -0.0451 0.0451  328  ASP B CB  
11333 C CG  . ASP B 330  ? 0.5240 0.3679 0.4103 -0.0479 -0.0478 0.0449  328  ASP B CG  
11334 O OD1 . ASP B 330  ? 0.5444 0.3784 0.4257 -0.0494 -0.0500 0.0474  328  ASP B OD1 
11335 O OD2 . ASP B 330  ? 0.5164 0.3629 0.4067 -0.0429 -0.0479 0.0423  328  ASP B OD2 
11336 N N   . LEU B 331  ? 0.4063 0.2707 0.2942 -0.0650 -0.0408 0.0471  329  LEU B N   
11337 C CA  . LEU B 331  ? 0.4127 0.2874 0.3021 -0.0687 -0.0381 0.0478  329  LEU B CA  
11338 C C   . LEU B 331  ? 0.3778 0.2502 0.2641 -0.0752 -0.0381 0.0507  329  LEU B C   
11339 O O   . LEU B 331  ? 0.4097 0.2907 0.2979 -0.0786 -0.0359 0.0512  329  LEU B O   
11340 C CB  . LEU B 331  ? 0.3616 0.2451 0.2575 -0.0667 -0.0359 0.0441  329  LEU B CB  
11341 C CG  . LEU B 331  ? 0.3817 0.2678 0.2809 -0.0605 -0.0358 0.0412  329  LEU B CG  
11342 C CD1 . LEU B 331  ? 0.3655 0.2595 0.2708 -0.0588 -0.0337 0.0376  329  LEU B CD1 
11343 C CD2 . LEU B 331  ? 0.3566 0.2470 0.2541 -0.0595 -0.0353 0.0426  329  LEU B CD2 
11344 N N   . SER B 332  ? 0.4393 0.3002 0.3206 -0.0770 -0.0407 0.0529  330  SER B N   
11345 C CA  . SER B 332  ? 0.4246 0.2815 0.3027 -0.0833 -0.0412 0.0556  330  SER B CA  
11346 C C   . SER B 332  ? 0.4346 0.3000 0.3117 -0.0882 -0.0391 0.0586  330  SER B C   
11347 O O   . SER B 332  ? 0.4742 0.3420 0.3490 -0.0876 -0.0387 0.0606  330  SER B O   
11348 C CB  . SER B 332  ? 0.5045 0.3477 0.3764 -0.0838 -0.0444 0.0581  330  SER B CB  
11349 O OG  . SER B 332  ? 0.5773 0.4158 0.4455 -0.0903 -0.0451 0.0610  330  SER B OG  
11350 N N   . GLY B 333  ? 0.3995 0.2694 0.2783 -0.0931 -0.0379 0.0590  331  GLY B N   
11351 C CA  . GLY B 333  ? 0.4527 0.3303 0.3305 -0.0983 -0.0359 0.0622  331  GLY B CA  
11352 C C   . GLY B 333  ? 0.4432 0.3346 0.3252 -0.0964 -0.0327 0.0610  331  GLY B C   
11353 O O   . GLY B 333  ? 0.4643 0.3632 0.3459 -0.1004 -0.0307 0.0634  331  GLY B O   
11354 N N   . TRP B 334  ? 0.4318 0.3265 0.3177 -0.0905 -0.0321 0.0573  332  TRP B N   
11355 C CA  . TRP B 334  ? 0.3894 0.2962 0.2789 -0.0883 -0.0291 0.0559  332  TRP B CA  
11356 C C   . TRP B 334  ? 0.3718 0.2874 0.2670 -0.0895 -0.0271 0.0538  332  TRP B C   
11357 O O   . TRP B 334  ? 0.3859 0.2994 0.2843 -0.0875 -0.0278 0.0508  332  TRP B O   
11358 C CB  . TRP B 334  ? 0.3986 0.3045 0.2895 -0.0816 -0.0296 0.0530  332  TRP B CB  
11359 C CG  . TRP B 334  ? 0.3692 0.2864 0.2639 -0.0786 -0.0269 0.0509  332  TRP B CG  
11360 C CD1 . TRP B 334  ? 0.3896 0.3145 0.2830 -0.0798 -0.0247 0.0525  332  TRP B CD1 
11361 C CD2 . TRP B 334  ? 0.3827 0.3038 0.2826 -0.0738 -0.0262 0.0468  332  TRP B CD2 
11362 N NE1 . TRP B 334  ? 0.3276 0.2608 0.2251 -0.0759 -0.0227 0.0495  332  TRP B NE1 
11363 C CE2 . TRP B 334  ? 0.3165 0.2474 0.2179 -0.0723 -0.0236 0.0461  332  TRP B CE2 
11364 C CE3 . TRP B 334  ? 0.3455 0.2628 0.2486 -0.0706 -0.0273 0.0437  332  TRP B CE3 
11365 C CZ2 . TRP B 334  ? 0.3404 0.2770 0.2466 -0.0679 -0.0224 0.0424  332  TRP B CZ2 
11366 C CZ3 . TRP B 334  ? 0.4038 0.3271 0.3117 -0.0663 -0.0260 0.0403  332  TRP B CZ3 
11367 C CH2 . TRP B 334  ? 0.3756 0.3084 0.2851 -0.0651 -0.0236 0.0397  332  TRP B CH2 
11368 N N   . ASN B 335  ? 0.3745 0.2999 0.2708 -0.0928 -0.0245 0.0554  333  ASN B N   
11369 C CA  . ASN B 335  ? 0.3660 0.3007 0.2678 -0.0941 -0.0225 0.0537  333  ASN B CA  
11370 C C   . ASN B 335  ? 0.3327 0.2776 0.2389 -0.0896 -0.0198 0.0509  333  ASN B C   
11371 O O   . ASN B 335  ? 0.3529 0.3073 0.2634 -0.0905 -0.0176 0.0500  333  ASN B O   
11372 C CB  . ASN B 335  ? 0.3775 0.3169 0.2785 -0.1008 -0.0214 0.0572  333  ASN B CB  
11373 C CG  . ASN B 335  ? 0.4492 0.3781 0.3465 -0.1055 -0.0241 0.0594  333  ASN B CG  
11374 O OD1 . ASN B 335  ? 0.3959 0.3164 0.2933 -0.1039 -0.0264 0.0573  333  ASN B OD1 
11375 N ND2 . ASN B 335  ? 0.4503 0.3793 0.3441 -0.1113 -0.0240 0.0635  333  ASN B ND2 
11376 N N   . GLY B 336  ? 0.3271 0.2701 0.2321 -0.0848 -0.0201 0.0496  334  GLY B N   
11377 C CA  . GLY B 336  ? 0.3306 0.2825 0.2390 -0.0807 -0.0178 0.0471  334  GLY B CA  
11378 C C   . GLY B 336  ? 0.3041 0.2564 0.2173 -0.0760 -0.0180 0.0429  334  GLY B C   
11379 O O   . GLY B 336  ? 0.3007 0.2598 0.2167 -0.0724 -0.0162 0.0407  334  GLY B O   
11380 N N   . MET B 337  ? 0.3074 0.2526 0.2215 -0.0758 -0.0201 0.0417  335  MET B N   
11381 C CA  . MET B 337  ? 0.3110 0.2573 0.2298 -0.0715 -0.0200 0.0378  335  MET B CA  
11382 C C   . MET B 337  ? 0.3048 0.2614 0.2286 -0.0725 -0.0176 0.0366  335  MET B C   
11383 O O   . MET B 337  ? 0.3160 0.2744 0.2403 -0.0769 -0.0173 0.0380  335  MET B O   
11384 C CB  . MET B 337  ? 0.3507 0.2872 0.2691 -0.0714 -0.0226 0.0369  335  MET B CB  
11385 C CG  . MET B 337  ? 0.3852 0.3222 0.3080 -0.0668 -0.0227 0.0330  335  MET B CG  
11386 S SD  . MET B 337  ? 0.5223 0.4567 0.4450 -0.0606 -0.0234 0.0312  335  MET B SD  
11387 C CE  . MET B 337  ? 0.4266 0.3728 0.3545 -0.0577 -0.0205 0.0286  335  MET B CE  
11388 N N   . GLY B 338  ? 0.2787 0.2418 0.2059 -0.0684 -0.0159 0.0340  336  GLY B N   
11389 C CA  . GLY B 338  ? 0.2969 0.2699 0.2289 -0.0685 -0.0135 0.0327  336  GLY B CA  
11390 C C   . GLY B 338  ? 0.2903 0.2633 0.2266 -0.0647 -0.0137 0.0291  336  GLY B C   
11391 O O   . GLY B 338  ? 0.2750 0.2431 0.2112 -0.0608 -0.0149 0.0273  336  GLY B O   
11392 N N   . PHE B 339  ? 0.2697 0.2488 0.2101 -0.0659 -0.0126 0.0283  337  PHE B N   
11393 C CA  . PHE B 339  ? 0.2617 0.2409 0.2060 -0.0627 -0.0129 0.0251  337  PHE B CA  
11394 C C   . PHE B 339  ? 0.2602 0.2499 0.2091 -0.0630 -0.0106 0.0243  337  PHE B C   
11395 O O   . PHE B 339  ? 0.2657 0.2600 0.2152 -0.0672 -0.0099 0.0262  337  PHE B O   
11396 C CB  . PHE B 339  ? 0.2718 0.2429 0.2154 -0.0646 -0.0153 0.0249  337  PHE B CB  
11397 C CG  . PHE B 339  ? 0.2676 0.2368 0.2142 -0.0609 -0.0158 0.0217  337  PHE B CG  
11398 C CD1 . PHE B 339  ? 0.2818 0.2445 0.2275 -0.0569 -0.0171 0.0201  337  PHE B CD1 
11399 C CD2 . PHE B 339  ? 0.2648 0.2390 0.2152 -0.0616 -0.0151 0.0204  337  PHE B CD2 
11400 C CE1 . PHE B 339  ? 0.2799 0.2411 0.2285 -0.0536 -0.0175 0.0172  337  PHE B CE1 
11401 C CE2 . PHE B 339  ? 0.2792 0.2516 0.2322 -0.0583 -0.0156 0.0175  337  PHE B CE2 
11402 C CZ  . PHE B 339  ? 0.2839 0.2499 0.2360 -0.0544 -0.0167 0.0159  337  PHE B CZ  
11403 N N   . VAL B 340  ? 0.2490 0.2428 0.2012 -0.0586 -0.0094 0.0217  338  VAL B N   
11404 C CA  . VAL B 340  ? 0.2380 0.2418 0.1946 -0.0581 -0.0072 0.0208  338  VAL B CA  
11405 C C   . VAL B 340  ? 0.2514 0.2546 0.2112 -0.0584 -0.0081 0.0192  338  VAL B C   
11406 O O   . VAL B 340  ? 0.2452 0.2418 0.2050 -0.0563 -0.0097 0.0174  338  VAL B O   
11407 C CB  . VAL B 340  ? 0.2447 0.2525 0.2029 -0.0532 -0.0055 0.0187  338  VAL B CB  
11408 C CG1 . VAL B 340  ? 0.2609 0.2784 0.2236 -0.0521 -0.0034 0.0176  338  VAL B CG1 
11409 C CG2 . VAL B 340  ? 0.2483 0.2568 0.2029 -0.0530 -0.0046 0.0201  338  VAL B CG2 
11410 N N   . VAL B 341  ? 0.2415 0.2521 0.2042 -0.0609 -0.0070 0.0200  339  VAL B N   
11411 C CA  . VAL B 341  ? 0.2403 0.2523 0.2065 -0.0607 -0.0075 0.0183  339  VAL B CA  
11412 C C   . VAL B 341  ? 0.2241 0.2469 0.1948 -0.0589 -0.0051 0.0175  339  VAL B C   
11413 O O   . VAL B 341  ? 0.2318 0.2622 0.2032 -0.0605 -0.0033 0.0193  339  VAL B O   
11414 C CB  . VAL B 341  ? 0.2932 0.3024 0.2585 -0.0659 -0.0092 0.0199  339  VAL B CB  
11415 C CG1 . VAL B 341  ? 0.3369 0.3455 0.3050 -0.0652 -0.0102 0.0178  339  VAL B CG1 
11416 C CG2 . VAL B 341  ? 0.3141 0.3125 0.2744 -0.0677 -0.0114 0.0210  339  VAL B CG2 
11417 N N   . GLN B 342  ? 0.2096 0.2332 0.1834 -0.0556 -0.0051 0.0150  340  GLN B N   
11418 C CA  . GLN B 342  ? 0.2049 0.2374 0.1829 -0.0527 -0.0030 0.0138  340  GLN B CA  
11419 C C   . GLN B 342  ? 0.2134 0.2514 0.1948 -0.0551 -0.0032 0.0141  340  GLN B C   
11420 O O   . GLN B 342  ? 0.2139 0.2479 0.1960 -0.0551 -0.0048 0.0128  340  GLN B O   
11421 C CB  . GLN B 342  ? 0.1899 0.2196 0.1689 -0.0475 -0.0030 0.0109  340  GLN B CB  
11422 C CG  . GLN B 342  ? 0.1797 0.2045 0.1555 -0.0452 -0.0031 0.0106  340  GLN B CG  
11423 C CD  . GLN B 342  ? 0.2044 0.2227 0.1803 -0.0415 -0.0043 0.0081  340  GLN B CD  
11424 O OE1 . GLN B 342  ? 0.2232 0.2361 0.1990 -0.0421 -0.0060 0.0075  340  GLN B OE1 
11425 N NE2 . GLN B 342  ? 0.1944 0.2134 0.1704 -0.0377 -0.0034 0.0068  340  GLN B NE2 
11426 N N   . ALA B 343  ? 0.1927 0.2401 0.1763 -0.0570 -0.0015 0.0158  341  ALA B N   
11427 C CA  . ALA B 343  ? 0.2058 0.2593 0.1928 -0.0597 -0.0017 0.0165  341  ALA B CA  
11428 C C   . ALA B 343  ? 0.2094 0.2669 0.2004 -0.0560 -0.0012 0.0142  341  ALA B C   
11429 O O   . ALA B 343  ? 0.2155 0.2764 0.2091 -0.0579 -0.0019 0.0144  341  ALA B O   
11430 C CB  . ALA B 343  ? 0.2308 0.2939 0.2192 -0.0627 0.0001  0.0192  341  ALA B CB  
11431 N N   . TYR B 344  ? 0.2026 0.2596 0.1940 -0.0508 0.0000  0.0122  342  TYR B N   
11432 C CA  . TYR B 344  ? 0.2179 0.2772 0.2127 -0.0474 0.0001  0.0101  342  TYR B CA  
11433 C C   . TYR B 344  ? 0.2082 0.2593 0.2020 -0.0473 -0.0022 0.0085  342  TYR B C   
11434 O O   . TYR B 344  ? 0.2140 0.2664 0.2104 -0.0450 -0.0023 0.0069  342  TYR B O   
11435 C CB  . TYR B 344  ? 0.1966 0.2582 0.1924 -0.0421 0.0020  0.0084  342  TYR B CB  
11436 C CG  . TYR B 344  ? 0.2246 0.2781 0.2175 -0.0389 0.0015  0.0067  342  TYR B CG  
11437 C CD1 . TYR B 344  ? 0.1831 0.2273 0.1725 -0.0404 -0.0004 0.0068  342  TYR B CD1 
11438 C CD2 . TYR B 344  ? 0.1915 0.2466 0.1852 -0.0344 0.0030  0.0051  342  TYR B CD2 
11439 C CE1 . TYR B 344  ? 0.1811 0.2187 0.1683 -0.0374 -0.0009 0.0053  342  TYR B CE1 
11440 C CE2 . TYR B 344  ? 0.2117 0.2600 0.2030 -0.0317 0.0025  0.0036  342  TYR B CE2 
11441 C CZ  . TYR B 344  ? 0.1995 0.2395 0.1878 -0.0332 0.0005  0.0038  342  TYR B CZ  
11442 O OH  . TYR B 344  ? 0.2010 0.2350 0.1874 -0.0305 0.0000  0.0024  342  TYR B OH  
11443 N N   . GLY B 345  ? 0.2033 0.2459 0.1934 -0.0497 -0.0040 0.0090  343  GLY B N   
11444 C CA  . GLY B 345  ? 0.2110 0.2455 0.1997 -0.0494 -0.0060 0.0075  343  GLY B CA  
11445 C C   . GLY B 345  ? 0.2224 0.2565 0.2111 -0.0539 -0.0077 0.0084  343  GLY B C   
11446 O O   . GLY B 345  ? 0.2186 0.2545 0.2063 -0.0582 -0.0080 0.0106  343  GLY B O   
11447 N N   . LYS B 346  ? 0.2044 0.2360 0.1940 -0.0528 -0.0088 0.0066  344  LYS B N   
11448 C CA  . LYS B 346  ? 0.2187 0.2496 0.2081 -0.0568 -0.0106 0.0071  344  LYS B CA  
11449 C C   . LYS B 346  ? 0.2165 0.2384 0.2013 -0.0604 -0.0125 0.0079  344  LYS B C   
11450 O O   . LYS B 346  ? 0.2420 0.2637 0.2261 -0.0649 -0.0140 0.0090  344  LYS B O   
11451 C CB  . LYS B 346  ? 0.2452 0.2746 0.2358 -0.0543 -0.0113 0.0048  344  LYS B CB  
11452 C CG  . LYS B 346  ? 0.2211 0.2595 0.2162 -0.0512 -0.0096 0.0042  344  LYS B CG  
11453 C CD  . LYS B 346  ? 0.2296 0.2658 0.2255 -0.0484 -0.0102 0.0020  344  LYS B CD  
11454 C CE  . LYS B 346  ? 0.2243 0.2697 0.2247 -0.0458 -0.0087 0.0017  344  LYS B CE  
11455 N NZ  . LYS B 346  ? 0.2190 0.2621 0.2200 -0.0428 -0.0092 -0.0004 344  LYS B NZ  
11456 N N   . ARG B 347  ? 0.2128 0.2271 0.1945 -0.0587 -0.0128 0.0075  345  ARG B N   
11457 C CA  . ARG B 347  ? 0.2396 0.2446 0.2167 -0.0617 -0.0148 0.0083  345  ARG B CA  
11458 C C   . ARG B 347  ? 0.2470 0.2534 0.2225 -0.0656 -0.0145 0.0112  345  ARG B C   
11459 O O   . ARG B 347  ? 0.2505 0.2495 0.2220 -0.0688 -0.0162 0.0123  345  ARG B O   
11460 C CB  . ARG B 347  ? 0.2175 0.2136 0.1922 -0.0580 -0.0153 0.0066  345  ARG B CB  
11461 C CG  . ARG B 347  ? 0.2146 0.2081 0.1902 -0.0549 -0.0158 0.0040  345  ARG B CG  
11462 C CD  . ARG B 347  ? 0.2252 0.2127 0.1997 -0.0505 -0.0158 0.0024  345  ARG B CD  
11463 N NE  . ARG B 347  ? 0.2150 0.2080 0.1921 -0.0469 -0.0139 0.0021  345  ARG B NE  
11464 C CZ  . ARG B 347  ? 0.2320 0.2214 0.2085 -0.0434 -0.0136 0.0012  345  ARG B CZ  
11465 N NH1 . ARG B 347  ? 0.2313 0.2119 0.2049 -0.0425 -0.0151 0.0005  345  ARG B NH1 
11466 N NH2 . ARG B 347  ? 0.2035 0.1980 0.1821 -0.0405 -0.0120 0.0009  345  ARG B NH2 
11467 N N   . CYS B 348  ? 0.2416 0.2571 0.2197 -0.0653 -0.0124 0.0124  346  CYS B N   
11468 C CA  . CYS B 348  ? 0.2405 0.2576 0.2168 -0.0682 -0.0118 0.0151  346  CYS B CA  
11469 C C   . CYS B 348  ? 0.2604 0.2745 0.2341 -0.0744 -0.0135 0.0174  346  CYS B C   
11470 O O   . CYS B 348  ? 0.2581 0.2654 0.2277 -0.0762 -0.0144 0.0188  346  CYS B O   
11471 C CB  . CYS B 348  ? 0.2363 0.2651 0.2163 -0.0671 -0.0091 0.0160  346  CYS B CB  
11472 S SG  . CYS B 348  ? 0.3158 0.3467 0.2933 -0.0693 -0.0078 0.0189  346  CYS B SG  
11473 N N   . PRO B 349  ? 0.2479 0.2666 0.2237 -0.0779 -0.0142 0.0180  347  PRO B N   
11474 C CA  . PRO B 349  ? 0.2635 0.2788 0.2366 -0.0842 -0.0160 0.0203  347  PRO B CA  
11475 C C   . PRO B 349  ? 0.2519 0.2536 0.2199 -0.0850 -0.0186 0.0194  347  PRO B C   
11476 O O   . PRO B 349  ? 0.2670 0.2631 0.2312 -0.0891 -0.0198 0.0214  347  PRO B O   
11477 C CB  . PRO B 349  ? 0.2812 0.3042 0.2579 -0.0871 -0.0164 0.0205  347  PRO B CB  
11478 C CG  . PRO B 349  ? 0.2731 0.2999 0.2534 -0.0821 -0.0155 0.0178  347  PRO B CG  
11479 C CD  . PRO B 349  ? 0.2497 0.2763 0.2302 -0.0765 -0.0136 0.0167  347  PRO B CD  
11480 N N   . PHE B 350  ? 0.2642 0.2605 0.2320 -0.0810 -0.0193 0.0164  348  PHE B N   
11481 C CA  . PHE B 350  ? 0.2770 0.2605 0.2399 -0.0812 -0.0216 0.0154  348  PHE B CA  
11482 C C   . PHE B 350  ? 0.2701 0.2469 0.2298 -0.0788 -0.0215 0.0158  348  PHE B C   
11483 O O   . PHE B 350  ? 0.2780 0.2450 0.2331 -0.0808 -0.0233 0.0166  348  PHE B O   
11484 C CB  . PHE B 350  ? 0.2633 0.2441 0.2271 -0.0777 -0.0222 0.0122  348  PHE B CB  
11485 C CG  . PHE B 350  ? 0.2797 0.2681 0.2470 -0.0796 -0.0223 0.0119  348  PHE B CG  
11486 C CD1 . PHE B 350  ? 0.3163 0.3019 0.2816 -0.0846 -0.0244 0.0124  348  PHE B CD1 
11487 C CD2 . PHE B 350  ? 0.2686 0.2672 0.2409 -0.0765 -0.0202 0.0111  348  PHE B CD2 
11488 C CE1 . PHE B 350  ? 0.3388 0.3320 0.3075 -0.0866 -0.0246 0.0123  348  PHE B CE1 
11489 C CE2 . PHE B 350  ? 0.2871 0.2932 0.2627 -0.0782 -0.0204 0.0110  348  PHE B CE2 
11490 C CZ  . PHE B 350  ? 0.2774 0.2809 0.2512 -0.0833 -0.0226 0.0116  348  PHE B CZ  
11491 N N   . VAL B 351  ? 0.2452 0.2272 0.2072 -0.0747 -0.0194 0.0154  349  VAL B N   
11492 C CA  . VAL B 351  ? 0.2462 0.2231 0.2053 -0.0728 -0.0192 0.0162  349  VAL B CA  
11493 C C   . VAL B 351  ? 0.2756 0.2523 0.2320 -0.0777 -0.0194 0.0195  349  VAL B C   
11494 O O   . VAL B 351  ? 0.2816 0.2497 0.2337 -0.0786 -0.0208 0.0206  349  VAL B O   
11495 C CB  . VAL B 351  ? 0.2387 0.2218 0.2009 -0.0678 -0.0169 0.0151  349  VAL B CB  
11496 C CG1 . VAL B 351  ? 0.2611 0.2396 0.2201 -0.0663 -0.0169 0.0161  349  VAL B CG1 
11497 C CG2 . VAL B 351  ? 0.2530 0.2350 0.2173 -0.0631 -0.0169 0.0119  349  VAL B CG2 
11498 N N   . LEU B 352  ? 0.2448 0.2312 0.2038 -0.0810 -0.0181 0.0214  350  LEU B N   
11499 C CA  . LEU B 352  ? 0.2595 0.2466 0.2162 -0.0861 -0.0182 0.0248  350  LEU B CA  
11500 C C   . LEU B 352  ? 0.2827 0.2602 0.2352 -0.0908 -0.0210 0.0258  350  LEU B C   
11501 O O   . LEU B 352  ? 0.3065 0.2777 0.2547 -0.0934 -0.0220 0.0280  350  LEU B O   
11502 C CB  . LEU B 352  ? 0.2588 0.2588 0.2197 -0.0887 -0.0163 0.0264  350  LEU B CB  
11503 C CG  . LEU B 352  ? 0.2813 0.2905 0.2454 -0.0845 -0.0133 0.0260  350  LEU B CG  
11504 C CD1 . LEU B 352  ? 0.3043 0.3262 0.2726 -0.0870 -0.0115 0.0275  350  LEU B CD1 
11505 C CD2 . LEU B 352  ? 0.3090 0.3152 0.2696 -0.0836 -0.0126 0.0275  350  LEU B CD2 
11506 N N   . ASP B 353  ? 0.3092 0.2850 0.2626 -0.0921 -0.0225 0.0243  351  ASP B N   
11507 C CA  . ASP B 353  ? 0.3109 0.2764 0.2598 -0.0962 -0.0253 0.0248  351  ASP B CA  
11508 C C   . ASP B 353  ? 0.2863 0.2391 0.2303 -0.0935 -0.0267 0.0241  351  ASP B C   
11509 O O   . ASP B 353  ? 0.3200 0.2646 0.2593 -0.0970 -0.0284 0.0260  351  ASP B O   
11510 C CB  . ASP B 353  ? 0.3101 0.2749 0.2603 -0.0967 -0.0266 0.0226  351  ASP B CB  
11511 C CG  . ASP B 353  ? 0.3690 0.3451 0.3234 -0.1004 -0.0260 0.0237  351  ASP B CG  
11512 O OD1 . ASP B 353  ? 0.4032 0.3856 0.3585 -0.1044 -0.0251 0.0267  351  ASP B OD1 
11513 O OD2 . ASP B 353  ? 0.4108 0.3898 0.3678 -0.0993 -0.0263 0.0216  351  ASP B OD2 
11514 N N   . PHE B 354  ? 0.2959 0.2471 0.2410 -0.0874 -0.0261 0.0214  352  PHE B N   
11515 C CA  . PHE B 354  ? 0.3009 0.2413 0.2421 -0.0842 -0.0272 0.0207  352  PHE B CA  
11516 C C   . PHE B 354  ? 0.3118 0.2509 0.2504 -0.0851 -0.0268 0.0234  352  PHE B C   
11517 O O   . PHE B 354  ? 0.3187 0.2476 0.2524 -0.0863 -0.0287 0.0246  352  PHE B O   
11518 C CB  . PHE B 354  ? 0.2818 0.2229 0.2255 -0.0775 -0.0262 0.0175  352  PHE B CB  
11519 C CG  . PHE B 354  ? 0.3130 0.2451 0.2536 -0.0738 -0.0271 0.0170  352  PHE B CG  
11520 C CD1 . PHE B 354  ? 0.3323 0.2532 0.2693 -0.0730 -0.0292 0.0158  352  PHE B CD1 
11521 C CD2 . PHE B 354  ? 0.3206 0.2552 0.2615 -0.0712 -0.0258 0.0179  352  PHE B CD2 
11522 C CE1 . PHE B 354  ? 0.3255 0.2384 0.2598 -0.0694 -0.0300 0.0155  352  PHE B CE1 
11523 C CE2 . PHE B 354  ? 0.3314 0.2581 0.2696 -0.0679 -0.0268 0.0176  352  PHE B CE2 
11524 C CZ  . PHE B 354  ? 0.3231 0.2392 0.2582 -0.0670 -0.0289 0.0165  352  PHE B CZ  
11525 N N   . ILE B 355  ? 0.2793 0.2283 0.2208 -0.0844 -0.0245 0.0245  353  ILE B N   
11526 C CA  . ILE B 355  ? 0.2854 0.2338 0.2243 -0.0849 -0.0240 0.0271  353  ILE B CA  
11527 C C   . ILE B 355  ? 0.2728 0.2186 0.2083 -0.0914 -0.0251 0.0305  353  ILE B C   
11528 O O   . ILE B 355  ? 0.3277 0.2661 0.2586 -0.0925 -0.0262 0.0325  353  ILE B O   
11529 C CB  . ILE B 355  ? 0.2866 0.2464 0.2293 -0.0824 -0.0211 0.0271  353  ILE B CB  
11530 C CG1 . ILE B 355  ? 0.3297 0.2902 0.2750 -0.0759 -0.0203 0.0239  353  ILE B CG1 
11531 C CG2 . ILE B 355  ? 0.2988 0.2590 0.2385 -0.0839 -0.0204 0.0301  353  ILE B CG2 
11532 C CD1 . ILE B 355  ? 0.3008 0.2722 0.2499 -0.0734 -0.0176 0.0235  353  ILE B CD1 
11533 N N   . ILE B 356  ? 0.2943 0.2465 0.2319 -0.0960 -0.0248 0.0315  354  ILE B N   
11534 C CA  . ILE B 356  ? 0.3211 0.2713 0.2558 -0.1027 -0.0259 0.0349  354  ILE B CA  
11535 C C   . ILE B 356  ? 0.3309 0.2667 0.2600 -0.1045 -0.0290 0.0350  354  ILE B C   
11536 O O   . ILE B 356  ? 0.3263 0.2557 0.2508 -0.1080 -0.0302 0.0378  354  ILE B O   
11537 C CB  . ILE B 356  ? 0.3221 0.2823 0.2607 -0.1071 -0.0252 0.0358  354  ILE B CB  
11538 C CG1 . ILE B 356  ? 0.3450 0.3193 0.2884 -0.1056 -0.0219 0.0364  354  ILE B CG1 
11539 C CG2 . ILE B 356  ? 0.3679 0.3247 0.3032 -0.1145 -0.0268 0.0391  354  ILE B CG2 
11540 C CD1 . ILE B 356  ? 0.3372 0.3226 0.2857 -0.1082 -0.0210 0.0364  354  ILE B CD1 
11541 N N   . ASP B 357  ? 0.3258 0.2560 0.2550 -0.1022 -0.0304 0.0319  355  ASP B N   
11542 C CA  . ASP B 357  ? 0.3521 0.2681 0.2759 -0.1032 -0.0333 0.0315  355  ASP B CA  
11543 C C   . ASP B 357  ? 0.3384 0.2459 0.2585 -0.0994 -0.0338 0.0318  355  ASP B C   
11544 O O   . ASP B 357  ? 0.3379 0.2351 0.2526 -0.1018 -0.0358 0.0336  355  ASP B O   
11545 C CB  . ASP B 357  ? 0.3374 0.2500 0.2621 -0.1009 -0.0343 0.0279  355  ASP B CB  
11546 C CG  . ASP B 357  ? 0.3868 0.2843 0.3058 -0.1004 -0.0370 0.0269  355  ASP B CG  
11547 O OD1 . ASP B 357  ? 0.4008 0.2916 0.3159 -0.1058 -0.0391 0.0285  355  ASP B OD1 
11548 O OD2 . ASP B 357  ? 0.3735 0.2657 0.2919 -0.0947 -0.0371 0.0247  355  ASP B OD2 
11549 N N   . LEU B 358  ? 0.3221 0.2336 0.2449 -0.0934 -0.0322 0.0300  356  LEU B N   
11550 C CA  . LEU B 358  ? 0.3109 0.2157 0.2308 -0.0896 -0.0327 0.0303  356  LEU B CA  
11551 C C   . LEU B 358  ? 0.3148 0.2192 0.2314 -0.0932 -0.0326 0.0343  356  LEU B C   
11552 O O   . LEU B 358  ? 0.3328 0.2271 0.2444 -0.0934 -0.0344 0.0357  356  LEU B O   
11553 C CB  . LEU B 358  ? 0.2846 0.1959 0.2086 -0.0834 -0.0307 0.0281  356  LEU B CB  
11554 C CG  . LEU B 358  ? 0.3375 0.2436 0.2592 -0.0791 -0.0311 0.0284  356  LEU B CG  
11555 C CD1 . LEU B 358  ? 0.3495 0.2422 0.2670 -0.0775 -0.0337 0.0276  356  LEU B CD1 
11556 C CD2 . LEU B 358  ? 0.3260 0.2395 0.2523 -0.0735 -0.0292 0.0259  356  LEU B CD2 
11557 N N   . ALA B 359  ? 0.3177 0.2332 0.2370 -0.0961 -0.0306 0.0362  357  ALA B N   
11558 C CA  . ALA B 359  ? 0.3318 0.2478 0.2480 -0.0998 -0.0303 0.0400  357  ALA B CA  
11559 C C   . ALA B 359  ? 0.3759 0.2824 0.2871 -0.1056 -0.0328 0.0425  357  ALA B C   
11560 O O   . ALA B 359  ? 0.3574 0.2559 0.2635 -0.1067 -0.0341 0.0449  357  ALA B O   
11561 C CB  . ALA B 359  ? 0.3655 0.2957 0.2858 -0.1021 -0.0275 0.0415  357  ALA B CB  
11562 N N   . ARG B 360  ? 0.3316 0.2381 0.2437 -0.1094 -0.0337 0.0420  358  ARG B N   
11563 C CA  . ARG B 360  ? 0.3795 0.2767 0.2868 -0.1154 -0.0362 0.0442  358  ARG B CA  
11564 C C   . ARG B 360  ? 0.3477 0.2294 0.2494 -0.1131 -0.0389 0.0434  358  ARG B C   
11565 O O   . ARG B 360  ? 0.3897 0.2628 0.2861 -0.1163 -0.0406 0.0463  358  ARG B O   
11566 C CB  . ARG B 360  ? 0.3781 0.2779 0.2877 -0.1190 -0.0369 0.0429  358  ARG B CB  
11567 C CG  . ARG B 360  ? 0.4590 0.3723 0.3729 -0.1236 -0.0350 0.0449  358  ARG B CG  
11568 C CD  . ARG B 360  ? 0.4614 0.3755 0.3763 -0.1285 -0.0364 0.0445  358  ARG B CD  
11569 N NE  . ARG B 360  ? 0.5177 0.4440 0.4360 -0.1338 -0.0349 0.0473  358  ARG B NE  
11570 C CZ  . ARG B 360  ? 0.5460 0.4851 0.4705 -0.1335 -0.0331 0.0462  358  ARG B CZ  
11571 N NH1 . ARG B 360  ? 0.5871 0.5281 0.5148 -0.1287 -0.0328 0.0424  358  ARG B NH1 
11572 N NH2 . ARG B 360  ? 0.6449 0.5952 0.5723 -0.1382 -0.0316 0.0492  358  ARG B NH2 
11573 N N   . ARG B 361  ? 0.3838 0.2616 0.2866 -0.1074 -0.0393 0.0397  359  ARG B N   
11574 C CA  . ARG B 361  ? 0.3770 0.2400 0.2746 -0.1052 -0.0419 0.0388  359  ARG B CA  
11575 C C   . ARG B 361  ? 0.3634 0.2223 0.2588 -0.1009 -0.0419 0.0398  359  ARG B C   
11576 O O   . ARG B 361  ? 0.4068 0.2533 0.2971 -0.1001 -0.0442 0.0403  359  ARG B O   
11577 C CB  . ARG B 361  ? 0.4531 0.3125 0.3521 -0.1013 -0.0425 0.0346  359  ARG B CB  
11578 C CG  . ARG B 361  ? 0.4140 0.2809 0.3181 -0.0946 -0.0405 0.0317  359  ARG B CG  
11579 C CD  . ARG B 361  ? 0.3778 0.2420 0.2833 -0.0918 -0.0410 0.0277  359  ARG B CD  
11580 N NE  . ARG B 361  ? 0.3770 0.2518 0.2885 -0.0873 -0.0387 0.0253  359  ARG B NE  
11581 C CZ  . ARG B 361  ? 0.3453 0.2201 0.2585 -0.0810 -0.0379 0.0234  359  ARG B CZ  
11582 N NH1 . ARG B 361  ? 0.3907 0.2559 0.3002 -0.0780 -0.0393 0.0236  359  ARG B NH1 
11583 N NH2 . ARG B 361  ? 0.3528 0.2375 0.2715 -0.0776 -0.0358 0.0213  359  ARG B NH2 
11584 N N   . SER B 362  ? 0.3868 0.2558 0.2857 -0.0982 -0.0395 0.0401  360  SER B N   
11585 C CA  . SER B 362  ? 0.3750 0.2407 0.2718 -0.0943 -0.0397 0.0411  360  SER B CA  
11586 C C   . SER B 362  ? 0.3843 0.2508 0.2778 -0.0985 -0.0395 0.0455  360  SER B C   
11587 O O   . SER B 362  ? 0.3922 0.2544 0.2828 -0.0960 -0.0401 0.0468  360  SER B O   
11588 C CB  . SER B 362  ? 0.3798 0.2548 0.2818 -0.0884 -0.0374 0.0387  360  SER B CB  
11589 O OG  . SER B 362  ? 0.3676 0.2555 0.2732 -0.0904 -0.0348 0.0396  360  SER B OG  
11590 N N   . GLY B 363  ? 0.3608 0.2331 0.2547 -0.1047 -0.0387 0.0478  361  GLY B N   
11591 C CA  . GLY B 363  ? 0.3892 0.2632 0.2801 -0.1087 -0.0383 0.0521  361  GLY B CA  
11592 C C   . GLY B 363  ? 0.3829 0.2671 0.2763 -0.1057 -0.0357 0.0524  361  GLY B C   
11593 O O   . GLY B 363  ? 0.4063 0.2888 0.2961 -0.1062 -0.0358 0.0553  361  GLY B O   
11594 N N   . ARG B 364  ? 0.3628 0.2575 0.2621 -0.1025 -0.0335 0.0496  362  ARG B N   
11595 C CA  . ARG B 364  ? 0.3967 0.3017 0.2988 -0.0994 -0.0308 0.0494  362  ARG B CA  
11596 C C   . ARG B 364  ? 0.4104 0.3285 0.3173 -0.1021 -0.0283 0.0494  362  ARG B C   
11597 O O   . ARG B 364  ? 0.4155 0.3363 0.3261 -0.1021 -0.0281 0.0471  362  ARG B O   
11598 C CB  . ARG B 364  ? 0.4018 0.3071 0.3069 -0.0922 -0.0306 0.0455  362  ARG B CB  
11599 C CG  . ARG B 364  ? 0.3870 0.2806 0.2885 -0.0884 -0.0330 0.0449  362  ARG B CG  
11600 C CD  . ARG B 364  ? 0.3864 0.2789 0.2845 -0.0872 -0.0330 0.0473  362  ARG B CD  
11601 N NE  . ARG B 364  ? 0.4000 0.2807 0.2945 -0.0840 -0.0356 0.0471  362  ARG B NE  
11602 C CZ  . ARG B 364  ? 0.3811 0.2604 0.2774 -0.0780 -0.0360 0.0445  362  ARG B CZ  
11603 N NH1 . ARG B 364  ? 0.3724 0.2608 0.2737 -0.0744 -0.0340 0.0418  362  ARG B NH1 
11604 N NH2 . ARG B 364  ? 0.4166 0.2850 0.3096 -0.0754 -0.0385 0.0446  362  ARG B NH2 
11605 N N   . ARG B 365  ? 0.3592 0.2855 0.2661 -0.1042 -0.0262 0.0519  363  ARG B N   
11606 C CA  . ARG B 365  ? 0.3547 0.2947 0.2669 -0.1049 -0.0233 0.0513  363  ARG B CA  
11607 C C   . ARG B 365  ? 0.3589 0.3042 0.2747 -0.0981 -0.0217 0.0479  363  ARG B C   
11608 O O   . ARG B 365  ? 0.3753 0.3195 0.2890 -0.0949 -0.0213 0.0481  363  ARG B O   
11609 C CB  . ARG B 365  ? 0.3584 0.3060 0.2695 -0.1093 -0.0214 0.0551  363  ARG B CB  
11610 C CG  . ARG B 365  ? 0.3681 0.3295 0.2847 -0.1110 -0.0186 0.0549  363  ARG B CG  
11611 C CD  . ARG B 365  ? 0.4093 0.3769 0.3243 -0.1166 -0.0171 0.0592  363  ARG B CD  
11612 N NE  . ARG B 365  ? 0.4108 0.3918 0.3313 -0.1188 -0.0147 0.0594  363  ARG B NE  
11613 C CZ  . ARG B 365  ? 0.3633 0.3558 0.2855 -0.1187 -0.0115 0.0606  363  ARG B CZ  
11614 N NH1 . ARG B 365  ? 0.3880 0.3803 0.3067 -0.1167 -0.0104 0.0618  363  ARG B NH1 
11615 N NH2 . ARG B 365  ? 0.3672 0.3716 0.2946 -0.1206 -0.0095 0.0608  363  ARG B NH2 
11616 N N   . ILE B 366  ? 0.3242 0.2743 0.2450 -0.0960 -0.0210 0.0449  364  ILE B N   
11617 C CA  . ILE B 366  ? 0.3158 0.2706 0.2402 -0.0898 -0.0196 0.0415  364  ILE B CA  
11618 C C   . ILE B 366  ? 0.3161 0.2844 0.2444 -0.0900 -0.0163 0.0417  364  ILE B C   
11619 O O   . ILE B 366  ? 0.2994 0.2744 0.2304 -0.0936 -0.0154 0.0426  364  ILE B O   
11620 C CB  . ILE B 366  ? 0.2951 0.2464 0.2224 -0.0871 -0.0208 0.0380  364  ILE B CB  
11621 C CG1 . ILE B 366  ? 0.3547 0.2924 0.2778 -0.0864 -0.0238 0.0378  364  ILE B CG1 
11622 C CG2 . ILE B 366  ? 0.2731 0.2306 0.2047 -0.0812 -0.0190 0.0348  364  ILE B CG2 
11623 C CD1 . ILE B 366  ? 0.3501 0.2830 0.2750 -0.0847 -0.0252 0.0348  364  ILE B CD1 
11624 N N   . MET B 367  ? 0.2935 0.2661 0.2220 -0.0861 -0.0147 0.0410  365  MET B N   
11625 C CA  . MET B 367  ? 0.3319 0.3169 0.2639 -0.0852 -0.0115 0.0407  365  MET B CA  
11626 C C   . MET B 367  ? 0.3075 0.2967 0.2449 -0.0814 -0.0109 0.0371  365  MET B C   
11627 O O   . MET B 367  ? 0.3043 0.2886 0.2421 -0.0769 -0.0118 0.0344  365  MET B O   
11628 C CB  . MET B 367  ? 0.2998 0.2867 0.2293 -0.0823 -0.0102 0.0411  365  MET B CB  
11629 C CG  . MET B 367  ? 0.3091 0.2896 0.2327 -0.0853 -0.0114 0.0444  365  MET B CG  
11630 S SD  . MET B 367  ? 0.3558 0.3390 0.2759 -0.0822 -0.0098 0.0450  365  MET B SD  
11631 C CE  . MET B 367  ? 0.4653 0.4613 0.3863 -0.0857 -0.0062 0.0475  365  MET B CE  
11632 N N   . VAL B 368  ? 0.2525 0.2504 0.1941 -0.0833 -0.0094 0.0370  366  VAL B N   
11633 C CA  . VAL B 368  ? 0.2627 0.2644 0.2093 -0.0801 -0.0089 0.0338  366  VAL B CA  
11634 C C   . VAL B 368  ? 0.2908 0.3045 0.2411 -0.0779 -0.0058 0.0332  366  VAL B C   
11635 O O   . VAL B 368  ? 0.2779 0.3002 0.2301 -0.0811 -0.0041 0.0351  366  VAL B O   
11636 C CB  . VAL B 368  ? 0.2741 0.2752 0.2227 -0.0838 -0.0103 0.0339  366  VAL B CB  
11637 C CG1 . VAL B 368  ? 0.3161 0.3212 0.2696 -0.0802 -0.0098 0.0306  366  VAL B CG1 
11638 C CG2 . VAL B 368  ? 0.3024 0.2910 0.2469 -0.0859 -0.0134 0.0344  366  VAL B CG2 
11639 N N   . ARG B 369  ? 0.2623 0.2768 0.2138 -0.0724 -0.0049 0.0305  367  ARG B N   
11640 C CA  . ARG B 369  ? 0.2470 0.2720 0.2019 -0.0697 -0.0020 0.0295  367  ARG B CA  
11641 C C   . ARG B 369  ? 0.2481 0.2773 0.2082 -0.0684 -0.0018 0.0273  367  ARG B C   
11642 O O   . ARG B 369  ? 0.2666 0.2910 0.2278 -0.0652 -0.0031 0.0247  367  ARG B O   
11643 C CB  . ARG B 369  ? 0.2460 0.2697 0.1993 -0.0647 -0.0013 0.0277  367  ARG B CB  
11644 C CG  . ARG B 369  ? 0.2708 0.3048 0.2269 -0.0619 0.0018  0.0266  367  ARG B CG  
11645 C CD  . ARG B 369  ? 0.2633 0.2954 0.2188 -0.0565 0.0021  0.0240  367  ARG B CD  
11646 N NE  . ARG B 369  ? 0.2567 0.2841 0.2070 -0.0563 0.0017  0.0251  367  ARG B NE  
11647 C CZ  . ARG B 369  ? 0.2651 0.2868 0.2135 -0.0528 0.0006  0.0233  367  ARG B CZ  
11648 N NH1 . ARG B 369  ? 0.2493 0.2692 0.2006 -0.0491 0.0000  0.0203  367  ARG B NH1 
11649 N NH2 . ARG B 369  ? 0.2863 0.3039 0.2297 -0.0531 0.0001  0.0247  367  ARG B NH2 
11650 N N   . LEU B 370  ? 0.2281 0.2668 0.1916 -0.0708 -0.0003 0.0285  368  LEU B N   
11651 C CA  . LEU B 370  ? 0.2243 0.2684 0.1929 -0.0694 0.0001  0.0267  368  LEU B CA  
11652 C C   . LEU B 370  ? 0.2325 0.2842 0.2037 -0.0645 0.0027  0.0249  368  LEU B C   
11653 O O   . LEU B 370  ? 0.2429 0.3020 0.2141 -0.0647 0.0051  0.0263  368  LEU B O   
11654 C CB  . LEU B 370  ? 0.2397 0.2903 0.2107 -0.0745 0.0003  0.0289  368  LEU B CB  
11655 C CG  . LEU B 370  ? 0.2461 0.3021 0.2224 -0.0736 0.0002  0.0273  368  LEU B CG  
11656 C CD1 . LEU B 370  ? 0.2506 0.2972 0.2262 -0.0730 -0.0025 0.0253  368  LEU B CD1 
11657 C CD2 . LEU B 370  ? 0.2517 0.3160 0.2306 -0.0787 0.0007  0.0299  368  LEU B CD2 
11658 N N   . VAL B 371  ? 0.2002 0.2498 0.1734 -0.0601 0.0023  0.0219  369  VAL B N   
11659 C CA  . VAL B 371  ? 0.1977 0.2533 0.1734 -0.0553 0.0045  0.0199  369  VAL B CA  
11660 C C   . VAL B 371  ? 0.2262 0.2854 0.2066 -0.0541 0.0043  0.0183  369  VAL B C   
11661 O O   . VAL B 371  ? 0.2293 0.2849 0.2105 -0.0563 0.0023  0.0183  369  VAL B O   
11662 C CB  . VAL B 371  ? 0.1952 0.2442 0.1683 -0.0509 0.0041  0.0178  369  VAL B CB  
11663 C CG1 . VAL B 371  ? 0.2179 0.2623 0.1859 -0.0525 0.0037  0.0195  369  VAL B CG1 
11664 C CG2 . VAL B 371  ? 0.2208 0.2617 0.1943 -0.0494 0.0017  0.0157  369  VAL B CG2 
11665 N N   . LYS B 372  ? 0.2041 0.2701 0.1875 -0.0502 0.0064  0.0168  370  LYS B N   
11666 C CA  . LYS B 372  ? 0.2017 0.2699 0.1893 -0.0482 0.0060  0.0150  370  LYS B CA  
11667 C C   . LYS B 372  ? 0.1944 0.2541 0.1810 -0.0447 0.0045  0.0123  370  LYS B C   
11668 O O   . LYS B 372  ? 0.2326 0.2869 0.2194 -0.0458 0.0024  0.0117  370  LYS B O   
11669 C CB  . LYS B 372  ? 0.2168 0.2958 0.2083 -0.0457 0.0086  0.0147  370  LYS B CB  
11670 C CG  . LYS B 372  ? 0.2253 0.3129 0.2184 -0.0499 0.0097  0.0176  370  LYS B CG  
11671 C CD  . LYS B 372  ? 0.2218 0.3209 0.2188 -0.0476 0.0124  0.0177  370  LYS B CD  
11672 C CE  . LYS B 372  ? 0.2376 0.3452 0.2359 -0.0521 0.0136  0.0210  370  LYS B CE  
11673 N NZ  . LYS B 372  ? 0.2525 0.3722 0.2547 -0.0497 0.0165  0.0213  370  LYS B NZ  
11674 N N   . GLY B 373  ? 0.2217 0.2797 0.2069 -0.0407 0.0054  0.0108  371  GLY B N   
11675 C CA  . GLY B 373  ? 0.2069 0.2566 0.1908 -0.0379 0.0039  0.0087  371  GLY B CA  
11676 C C   . GLY B 373  ? 0.2131 0.2645 0.1978 -0.0330 0.0053  0.0065  371  GLY B C   
11677 O O   . GLY B 373  ? 0.2398 0.2985 0.2273 -0.0311 0.0071  0.0061  371  GLY B O   
11678 N N   . ALA B 374  ? 0.1907 0.2352 0.1728 -0.0308 0.0043  0.0052  372  ALA B N   
11679 C CA  . ALA B 374  ? 0.1995 0.2447 0.1811 -0.0266 0.0055  0.0035  372  ALA B CA  
11680 C C   . ALA B 374  ? 0.1870 0.2294 0.1708 -0.0232 0.0048  0.0010  372  ALA B C   
11681 O O   . ALA B 374  ? 0.2167 0.2596 0.2003 -0.0198 0.0057  -0.0005 372  ALA B O   
11682 C CB  . ALA B 374  ? 0.2243 0.2645 0.2014 -0.0265 0.0051  0.0038  372  ALA B CB  
11683 N N   . TYR B 375  ? 0.2004 0.2398 0.1860 -0.0241 0.0033  0.0007  373  TYR B N   
11684 C CA  . TYR B 375  ? 0.2066 0.2424 0.1938 -0.0211 0.0024  -0.0015 373  TYR B CA  
11685 C C   . TYR B 375  ? 0.2039 0.2440 0.1950 -0.0203 0.0029  -0.0021 373  TYR B C   
11686 O O   . TYR B 375  ? 0.1988 0.2355 0.1913 -0.0190 0.0018  -0.0034 373  TYR B O   
11687 C CB  . TYR B 375  ? 0.2227 0.2503 0.2083 -0.0221 0.0002  -0.0017 373  TYR B CB  
11688 C CG  . TYR B 375  ? 0.2172 0.2401 0.1990 -0.0227 -0.0006 -0.0009 373  TYR B CG  
11689 C CD1 . TYR B 375  ? 0.2358 0.2588 0.2151 -0.0261 -0.0007 0.0013  373  TYR B CD1 
11690 C CD2 . TYR B 375  ? 0.2474 0.2656 0.2280 -0.0201 -0.0014 -0.0022 373  TYR B CD2 
11691 C CE1 . TYR B 375  ? 0.2237 0.2420 0.1992 -0.0266 -0.0016 0.0021  373  TYR B CE1 
11692 C CE2 . TYR B 375  ? 0.2724 0.2864 0.2496 -0.0206 -0.0023 -0.0015 373  TYR B CE2 
11693 C CZ  . TYR B 375  ? 0.2626 0.2766 0.2371 -0.0238 -0.0024 0.0007  373  TYR B CZ  
11694 O OH  . TYR B 375  ? 0.2848 0.2944 0.2557 -0.0242 -0.0034 0.0015  373  TYR B OH  
11695 N N   . TRP B 376  ? 0.2017 0.2495 0.1948 -0.0210 0.0044  -0.0012 374  TRP B N   
11696 C CA  . TRP B 376  ? 0.1889 0.2409 0.1856 -0.0211 0.0045  -0.0014 374  TRP B CA  
11697 C C   . TRP B 376  ? 0.1891 0.2399 0.1878 -0.0172 0.0045  -0.0035 374  TRP B C   
11698 O O   . TRP B 376  ? 0.2053 0.2537 0.2053 -0.0174 0.0032  -0.0041 374  TRP B O   
11699 C CB  . TRP B 376  ? 0.1810 0.2422 0.1797 -0.0219 0.0063  0.0000  374  TRP B CB  
11700 C CG  . TRP B 376  ? 0.1851 0.2508 0.1876 -0.0222 0.0060  0.0001  374  TRP B CG  
11701 C CD1 . TRP B 376  ? 0.1612 0.2269 0.1646 -0.0258 0.0046  0.0011  374  TRP B CD1 
11702 C CD2 . TRP B 376  ? 0.1967 0.2670 0.2023 -0.0189 0.0071  -0.0010 374  TRP B CD2 
11703 N NE1 . TRP B 376  ? 0.1793 0.2498 0.1862 -0.0249 0.0047  0.0008  374  TRP B NE1 
11704 C CE2 . TRP B 376  ? 0.1966 0.2701 0.2050 -0.0206 0.0062  -0.0004 374  TRP B CE2 
11705 C CE3 . TRP B 376  ? 0.2301 0.3020 0.2361 -0.0146 0.0086  -0.0023 374  TRP B CE3 
11706 C CZ2 . TRP B 376  ? 0.2021 0.2803 0.2138 -0.0181 0.0067  -0.0011 374  TRP B CZ2 
11707 C CZ3 . TRP B 376  ? 0.2482 0.3246 0.2575 -0.0120 0.0092  -0.0030 374  TRP B CZ3 
11708 C CH2 . TRP B 376  ? 0.2583 0.3379 0.2705 -0.0137 0.0083  -0.0023 374  TRP B CH2 
11709 N N   . ASP B 377  ? 0.2054 0.2576 0.2039 -0.0138 0.0058  -0.0046 375  ASP B N   
11710 C CA  . ASP B 377  ? 0.2119 0.2629 0.2122 -0.0103 0.0058  -0.0064 375  ASP B CA  
11711 C C   . ASP B 377  ? 0.2013 0.2447 0.2007 -0.0102 0.0040  -0.0074 375  ASP B C   
11712 O O   . ASP B 377  ? 0.2126 0.2550 0.2140 -0.0090 0.0034  -0.0083 375  ASP B O   
11713 C CB  . ASP B 377  ? 0.3015 0.3532 0.3006 -0.0069 0.0073  -0.0075 375  ASP B CB  
11714 C CG  . ASP B 377  ? 0.4208 0.4803 0.4209 -0.0062 0.0094  -0.0068 375  ASP B CG  
11715 O OD1 . ASP B 377  ? 0.5075 0.5726 0.5109 -0.0061 0.0099  -0.0063 375  ASP B OD1 
11716 O OD2 . ASP B 377  ? 0.5658 0.6260 0.5635 -0.0055 0.0106  -0.0068 375  ASP B OD2 
11717 N N   . ALA B 378  ? 0.2029 0.2410 0.1993 -0.0112 0.0031  -0.0072 376  ALA B N   
11718 C CA  . ALA B 378  ? 0.1888 0.2201 0.1846 -0.0108 0.0014  -0.0081 376  ALA B CA  
11719 C C   . ALA B 378  ? 0.1864 0.2158 0.1830 -0.0130 0.0001  -0.0077 376  ALA B C   
11720 O O   . ALA B 378  ? 0.1989 0.2246 0.1963 -0.0120 -0.0008 -0.0087 376  ALA B O   
11721 C CB  . ALA B 378  ? 0.2222 0.2488 0.2146 -0.0114 0.0007  -0.0079 376  ALA B CB  
11722 N N   . GLU B 379  ? 0.1772 0.2092 0.1736 -0.0162 0.0001  -0.0062 377  GLU B N   
11723 C CA  . GLU B 379  ? 0.1943 0.2242 0.1911 -0.0185 -0.0013 -0.0058 377  GLU B CA  
11724 C C   . GLU B 379  ? 0.2103 0.2436 0.2101 -0.0173 -0.0011 -0.0066 377  GLU B C   
11725 O O   . GLU B 379  ? 0.1871 0.2170 0.1872 -0.0176 -0.0022 -0.0073 377  GLU B O   
11726 C CB  . GLU B 379  ? 0.2025 0.2340 0.1981 -0.0225 -0.0016 -0.0039 377  GLU B CB  
11727 C CG  . GLU B 379  ? 0.2287 0.2562 0.2208 -0.0241 -0.0020 -0.0028 377  GLU B CG  
11728 C CD  . GLU B 379  ? 0.2546 0.2737 0.2445 -0.0241 -0.0038 -0.0034 377  GLU B CD  
11729 O OE1 . GLU B 379  ? 0.2516 0.2675 0.2425 -0.0231 -0.0047 -0.0046 377  GLU B OE1 
11730 O OE2 . GLU B 379  ? 0.2552 0.2709 0.2423 -0.0250 -0.0043 -0.0025 377  GLU B OE2 
11731 N N   . ILE B 380  ? 0.2028 0.2428 0.2048 -0.0160 0.0004  -0.0065 378  ILE B N   
11732 C CA  . ILE B 380  ? 0.1959 0.2390 0.2007 -0.0146 0.0006  -0.0071 378  ILE B CA  
11733 C C   . ILE B 380  ? 0.1853 0.2240 0.1904 -0.0116 0.0002  -0.0088 378  ILE B C   
11734 O O   . ILE B 380  ? 0.1825 0.2195 0.1884 -0.0114 -0.0006 -0.0094 378  ILE B O   
11735 C CB  . ILE B 380  ? 0.1841 0.2351 0.1912 -0.0132 0.0023  -0.0066 378  ILE B CB  
11736 C CG1 . ILE B 380  ? 0.1811 0.2374 0.1883 -0.0163 0.0028  -0.0047 378  ILE B CG1 
11737 C CG2 . ILE B 380  ? 0.1869 0.2411 0.1969 -0.0114 0.0024  -0.0072 378  ILE B CG2 
11738 C CD1 . ILE B 380  ? 0.2151 0.2717 0.2227 -0.0201 0.0014  -0.0038 378  ILE B CD1 
11739 N N   . LYS B 381  ? 0.1831 0.2199 0.1872 -0.0092 0.0008  -0.0096 379  LYS B N   
11740 C CA  . LYS B 381  ? 0.1777 0.2106 0.1822 -0.0066 0.0005  -0.0110 379  LYS B CA  
11741 C C   . LYS B 381  ? 0.1986 0.2254 0.2021 -0.0076 -0.0010 -0.0114 379  LYS B C   
11742 O O   . LYS B 381  ? 0.1964 0.2216 0.2010 -0.0065 -0.0014 -0.0122 379  LYS B O   
11743 C CB  . LYS B 381  ? 0.2053 0.2367 0.2086 -0.0044 0.0012  -0.0117 379  LYS B CB  
11744 C CG  . LYS B 381  ? 0.2175 0.2446 0.2211 -0.0021 0.0007  -0.0131 379  LYS B CG  
11745 C CD  . LYS B 381  ? 0.1989 0.2251 0.2013 0.0000  0.0013  -0.0138 379  LYS B CD  
11746 C CE  . LYS B 381  ? 0.2226 0.2451 0.2257 0.0021  0.0007  -0.0151 379  LYS B CE  
11747 N NZ  . LYS B 381  ? 0.2155 0.2365 0.2170 0.0038  0.0011  -0.0159 379  LYS B NZ  
11748 N N   . ARG B 382  ? 0.1825 0.2061 0.1837 -0.0097 -0.0018 -0.0107 380  ARG B N   
11749 C CA  . ARG B 382  ? 0.1971 0.2146 0.1972 -0.0101 -0.0032 -0.0112 380  ARG B CA  
11750 C C   . ARG B 382  ? 0.1983 0.2155 0.1990 -0.0114 -0.0039 -0.0112 380  ARG B C   
11751 O O   . ARG B 382  ? 0.1958 0.2097 0.1969 -0.0103 -0.0045 -0.0122 380  ARG B O   
11752 C CB  . ARG B 382  ? 0.2197 0.2338 0.2170 -0.0121 -0.0040 -0.0102 380  ARG B CB  
11753 C CG  . ARG B 382  ? 0.2932 0.3008 0.2892 -0.0123 -0.0054 -0.0106 380  ARG B CG  
11754 C CD  . ARG B 382  ? 0.3190 0.3241 0.3160 -0.0093 -0.0055 -0.0119 380  ARG B CD  
11755 N NE  . ARG B 382  ? 0.4428 0.4421 0.4386 -0.0093 -0.0068 -0.0122 380  ARG B NE  
11756 C CZ  . ARG B 382  ? 0.5258 0.5215 0.5197 -0.0095 -0.0076 -0.0117 380  ARG B CZ  
11757 N NH1 . ARG B 382  ? 0.4635 0.4605 0.4562 -0.0098 -0.0074 -0.0110 380  ARG B NH1 
11758 N NH2 . ARG B 382  ? 0.4942 0.4849 0.4873 -0.0092 -0.0088 -0.0119 380  ARG B NH2 
11759 N N   . ALA B 383  ? 0.1713 0.1923 0.1723 -0.0138 -0.0038 -0.0103 381  ALA B N   
11760 C CA  . ALA B 383  ? 0.1640 0.1847 0.1654 -0.0153 -0.0046 -0.0104 381  ALA B CA  
11761 C C   . ALA B 383  ? 0.1776 0.2005 0.1812 -0.0129 -0.0042 -0.0113 381  ALA B C   
11762 O O   . ALA B 383  ? 0.1922 0.2123 0.1956 -0.0128 -0.0049 -0.0121 381  ALA B O   
11763 C CB  . ALA B 383  ? 0.1895 0.2144 0.1909 -0.0185 -0.0047 -0.0089 381  ALA B CB  
11764 N N   . GLN B 384  ? 0.1601 0.1876 0.1657 -0.0109 -0.0029 -0.0113 382  GLN B N   
11765 C CA  . GLN B 384  ? 0.1901 0.2193 0.1977 -0.0085 -0.0025 -0.0121 382  GLN B CA  
11766 C C   . GLN B 384  ? 0.1790 0.2031 0.1862 -0.0064 -0.0028 -0.0133 382  GLN B C   
11767 O O   . GLN B 384  ? 0.2032 0.2262 0.2109 -0.0058 -0.0031 -0.0139 382  GLN B O   
11768 C CB  . GLN B 384  ? 0.1664 0.2011 0.1758 -0.0066 -0.0012 -0.0119 382  GLN B CB  
11769 C CG  . GLN B 384  ? 0.1726 0.2137 0.1833 -0.0083 -0.0008 -0.0107 382  GLN B CG  
11770 C CD  . GLN B 384  ? 0.1679 0.2144 0.1805 -0.0059 0.0006  -0.0105 382  GLN B CD  
11771 O OE1 . GLN B 384  ? 0.2283 0.2733 0.2406 -0.0034 0.0014  -0.0112 382  GLN B OE1 
11772 N NE2 . GLN B 384  ? 0.1635 0.2165 0.1780 -0.0067 0.0009  -0.0095 382  GLN B NE2 
11773 N N   . LEU B 385  ? 0.1802 0.2015 0.1865 -0.0054 -0.0026 -0.0136 383  LEU B N   
11774 C CA  . LEU B 385  ? 0.1892 0.2060 0.1954 -0.0036 -0.0030 -0.0146 383  LEU B CA  
11775 C C   . LEU B 385  ? 0.1917 0.2045 0.1969 -0.0046 -0.0040 -0.0149 383  LEU B C   
11776 O O   . LEU B 385  ? 0.1944 0.2052 0.2002 -0.0032 -0.0041 -0.0156 383  LEU B O   
11777 C CB  . LEU B 385  ? 0.2057 0.2201 0.2107 -0.0030 -0.0030 -0.0146 383  LEU B CB  
11778 C CG  . LEU B 385  ? 0.2377 0.2549 0.2433 -0.0014 -0.0020 -0.0147 383  LEU B CG  
11779 C CD1 . LEU B 385  ? 0.2439 0.2583 0.2479 -0.0012 -0.0023 -0.0148 383  LEU B CD1 
11780 C CD2 . LEU B 385  ? 0.2692 0.2869 0.2767 0.0010  -0.0016 -0.0155 383  LEU B CD2 
11781 N N   . ASP B 386  ? 0.2019 0.2131 0.2052 -0.0071 -0.0047 -0.0143 384  ASP B N   
11782 C CA  . ASP B 386  ? 0.2033 0.2096 0.2051 -0.0079 -0.0058 -0.0147 384  ASP B CA  
11783 C C   . ASP B 386  ? 0.2168 0.2240 0.2185 -0.0090 -0.0061 -0.0149 384  ASP B C   
11784 O O   . ASP B 386  ? 0.2306 0.2337 0.2308 -0.0095 -0.0069 -0.0155 384  ASP B O   
11785 C CB  . ASP B 386  ? 0.2354 0.2383 0.2347 -0.0099 -0.0066 -0.0140 384  ASP B CB  
11786 C CG  . ASP B 386  ? 0.3150 0.3159 0.3139 -0.0087 -0.0066 -0.0139 384  ASP B CG  
11787 O OD1 . ASP B 386  ? 0.3224 0.3238 0.3230 -0.0062 -0.0061 -0.0146 384  ASP B OD1 
11788 O OD2 . ASP B 386  ? 0.3259 0.3245 0.3228 -0.0102 -0.0072 -0.0131 384  ASP B OD2 
11789 N N   . GLY B 387  ? 0.1982 0.2107 0.2015 -0.0092 -0.0056 -0.0145 385  GLY B N   
11790 C CA  . GLY B 387  ? 0.2243 0.2381 0.2276 -0.0102 -0.0060 -0.0147 385  GLY B CA  
11791 C C   . GLY B 387  ? 0.2445 0.2560 0.2454 -0.0134 -0.0072 -0.0144 385  GLY B C   
11792 O O   . GLY B 387  ? 0.2404 0.2495 0.2400 -0.0141 -0.0080 -0.0150 385  GLY B O   
11793 N N   . LEU B 388  ? 0.2115 0.2237 0.2117 -0.0155 -0.0074 -0.0133 386  LEU B N   
11794 C CA  . LEU B 388  ? 0.2151 0.2243 0.2128 -0.0187 -0.0087 -0.0129 386  LEU B CA  
11795 C C   . LEU B 388  ? 0.2253 0.2394 0.2237 -0.0213 -0.0091 -0.0121 386  LEU B C   
11796 O O   . LEU B 388  ? 0.2262 0.2465 0.2272 -0.0205 -0.0083 -0.0117 386  LEU B O   
11797 C CB  . LEU B 388  ? 0.2228 0.2294 0.2189 -0.0199 -0.0088 -0.0120 386  LEU B CB  
11798 C CG  . LEU B 388  ? 0.2083 0.2097 0.2036 -0.0174 -0.0088 -0.0128 386  LEU B CG  
11799 C CD1 . LEU B 388  ? 0.2757 0.2743 0.2693 -0.0185 -0.0091 -0.0119 386  LEU B CD1 
11800 C CD2 . LEU B 388  ? 0.2502 0.2462 0.2441 -0.0164 -0.0095 -0.0141 386  LEU B CD2 
11801 N N   . ALA B 389  ? 0.2359 0.2468 0.2318 -0.0245 -0.0105 -0.0119 387  ALA B N   
11802 C CA  . ALA B 389  ? 0.2458 0.2605 0.2420 -0.0272 -0.0113 -0.0114 387  ALA B CA  
11803 C C   . ALA B 389  ? 0.2461 0.2687 0.2449 -0.0286 -0.0106 -0.0097 387  ALA B C   
11804 O O   . ALA B 389  ? 0.2656 0.2943 0.2666 -0.0290 -0.0105 -0.0093 387  ALA B O   
11805 C CB  . ALA B 389  ? 0.2679 0.2769 0.2604 -0.0306 -0.0130 -0.0114 387  ALA B CB  
11806 N N   . ASP B 390  ? 0.2211 0.2439 0.2198 -0.0292 -0.0100 -0.0087 388  ASP B N   
11807 C CA  . ASP B 390  ? 0.2266 0.2568 0.2275 -0.0304 -0.0091 -0.0071 388  ASP B CA  
11808 C C   . ASP B 390  ? 0.1671 0.1961 0.1674 -0.0294 -0.0081 -0.0066 388  ASP B C   
11809 O O   . ASP B 390  ? 0.1998 0.2226 0.1983 -0.0278 -0.0083 -0.0075 388  ASP B O   
11810 C CB  . ASP B 390  ? 0.2401 0.2723 0.2403 -0.0351 -0.0104 -0.0057 388  ASP B CB  
11811 C CG  . ASP B 390  ? 0.2570 0.2990 0.2606 -0.0361 -0.0096 -0.0043 388  ASP B CG  
11812 O OD1 . ASP B 390  ? 0.2450 0.2916 0.2505 -0.0343 -0.0079 -0.0036 388  ASP B OD1 
11813 O OD2 . ASP B 390  ? 0.3152 0.3605 0.3195 -0.0387 -0.0107 -0.0037 388  ASP B OD2 
11814 N N   . PHE B 391  ? 0.2020 0.2372 0.2039 -0.0302 -0.0071 -0.0052 389  PHE B N   
11815 C CA  . PHE B 391  ? 0.1893 0.2238 0.1903 -0.0297 -0.0061 -0.0046 389  PHE B CA  
11816 C C   . PHE B 391  ? 0.1838 0.2143 0.1817 -0.0336 -0.0072 -0.0033 389  PHE B C   
11817 O O   . PHE B 391  ? 0.2179 0.2487 0.2152 -0.0371 -0.0084 -0.0025 389  PHE B O   
11818 C CB  . PHE B 391  ? 0.2042 0.2472 0.2078 -0.0288 -0.0044 -0.0036 389  PHE B CB  
11819 C CG  . PHE B 391  ? 0.1858 0.2325 0.1922 -0.0250 -0.0034 -0.0047 389  PHE B CG  
11820 C CD1 . PHE B 391  ? 0.1895 0.2330 0.1957 -0.0213 -0.0027 -0.0060 389  PHE B CD1 
11821 C CD2 . PHE B 391  ? 0.2004 0.2533 0.2095 -0.0252 -0.0034 -0.0044 389  PHE B CD2 
11822 C CE1 . PHE B 391  ? 0.1979 0.2440 0.2063 -0.0180 -0.0019 -0.0070 389  PHE B CE1 
11823 C CE2 . PHE B 391  ? 0.1953 0.2510 0.2067 -0.0216 -0.0025 -0.0053 389  PHE B CE2 
11824 C CZ  . PHE B 391  ? 0.1829 0.2350 0.1939 -0.0181 -0.0018 -0.0066 389  PHE B CZ  
11825 N N   . PRO B 392  ? 0.1869 0.2134 0.1828 -0.0331 -0.0070 -0.0031 390  PRO B N   
11826 C CA  . PRO B 392  ? 0.1782 0.2011 0.1711 -0.0367 -0.0080 -0.0016 390  PRO B CA  
11827 C C   . PRO B 392  ? 0.2000 0.2294 0.1936 -0.0387 -0.0068 0.0004  390  PRO B C   
11828 O O   . PRO B 392  ? 0.2059 0.2330 0.1970 -0.0417 -0.0073 0.0019  390  PRO B O   
11829 C CB  . PRO B 392  ? 0.2033 0.2190 0.1938 -0.0345 -0.0083 -0.0024 390  PRO B CB  
11830 C CG  . PRO B 392  ? 0.2220 0.2412 0.2146 -0.0305 -0.0067 -0.0033 390  PRO B CG  
11831 C CD  . PRO B 392  ? 0.1597 0.1838 0.1555 -0.0292 -0.0062 -0.0042 390  PRO B CD  
11832 N N   . VAL B 393  ? 0.1913 0.2285 0.1881 -0.0367 -0.0051 0.0004  391  VAL B N   
11833 C CA  . VAL B 393  ? 0.1892 0.2340 0.1872 -0.0381 -0.0036 0.0021  391  VAL B CA  
11834 C C   . VAL B 393  ? 0.2018 0.2551 0.2037 -0.0384 -0.0031 0.0025  391  VAL B C   
11835 O O   . VAL B 393  ? 0.1985 0.2518 0.2020 -0.0366 -0.0036 0.0011  391  VAL B O   
11836 C CB  . VAL B 393  ? 0.1893 0.2358 0.1872 -0.0346 -0.0018 0.0017  391  VAL B CB  
11837 C CG1 . VAL B 393  ? 0.2123 0.2509 0.2064 -0.0345 -0.0025 0.0016  391  VAL B CG1 
11838 C CG2 . VAL B 393  ? 0.1932 0.2413 0.1936 -0.0301 -0.0010 -0.0002 391  VAL B CG2 
11839 N N   . PHE B 394  ? 0.1976 0.2583 0.2009 -0.0406 -0.0021 0.0044  392  PHE B N   
11840 C CA  . PHE B 394  ? 0.1828 0.2529 0.1902 -0.0405 -0.0013 0.0049  392  PHE B CA  
11841 C C   . PHE B 394  ? 0.1830 0.2570 0.1927 -0.0353 0.0005  0.0036  392  PHE B C   
11842 O O   . PHE B 394  ? 0.2001 0.2709 0.2083 -0.0324 0.0015  0.0027  392  PHE B O   
11843 C CB  . PHE B 394  ? 0.1878 0.2654 0.1963 -0.0443 -0.0006 0.0075  392  PHE B CB  
11844 C CG  . PHE B 394  ? 0.1875 0.2608 0.1936 -0.0497 -0.0025 0.0089  392  PHE B CG  
11845 C CD1 . PHE B 394  ? 0.2150 0.2867 0.2214 -0.0522 -0.0046 0.0087  392  PHE B CD1 
11846 C CD2 . PHE B 394  ? 0.1986 0.2685 0.2015 -0.0522 -0.0025 0.0103  392  PHE B CD2 
11847 C CE1 . PHE B 394  ? 0.2142 0.2810 0.2179 -0.0571 -0.0065 0.0097  392  PHE B CE1 
11848 C CE2 . PHE B 394  ? 0.2087 0.2737 0.2089 -0.0571 -0.0044 0.0115  392  PHE B CE2 
11849 C CZ  . PHE B 394  ? 0.2028 0.2660 0.2034 -0.0596 -0.0065 0.0112  392  PHE B CZ  
11850 N N   . THR B 395  ? 0.1900 0.2708 0.2034 -0.0343 0.0008  0.0036  393  THR B N   
11851 C CA  . THR B 395  ? 0.1973 0.2818 0.2131 -0.0293 0.0024  0.0024  393  THR B CA  
11852 C C   . THR B 395  ? 0.1774 0.2726 0.1965 -0.0286 0.0043  0.0037  393  THR B C   
11853 O O   . THR B 395  ? 0.1950 0.2930 0.2155 -0.0243 0.0059  0.0028  393  THR B O   
11854 C CB  . THR B 395  ? 0.1963 0.2792 0.2135 -0.0275 0.0013  0.0010  393  THR B CB  
11855 O OG1 . THR B 395  ? 0.1947 0.2830 0.2142 -0.0303 0.0002  0.0022  393  THR B OG1 
11856 C CG2 . THR B 395  ? 0.2103 0.2830 0.2243 -0.0274 -0.0003 -0.0005 393  THR B CG2 
11857 N N   . ARG B 396  ? 0.1860 0.2871 0.2063 -0.0326 0.0043  0.0059  394  ARG B N   
11858 C CA  . ARG B 396  ? 0.1809 0.2927 0.2042 -0.0321 0.0063  0.0074  394  ARG B CA  
11859 C C   . ARG B 396  ? 0.2039 0.3157 0.2248 -0.0345 0.0074  0.0088  394  ARG B C   
11860 O O   . ARG B 396  ? 0.1953 0.3028 0.2138 -0.0389 0.0060  0.0099  394  ARG B O   
11861 C CB  . ARG B 396  ? 0.1814 0.3017 0.2086 -0.0350 0.0056  0.0091  394  ARG B CB  
11862 C CG  . ARG B 396  ? 0.2285 0.3494 0.2580 -0.0329 0.0045  0.0080  394  ARG B CG  
11863 C CD  . ARG B 396  ? 0.2436 0.3745 0.2774 -0.0354 0.0039  0.0098  394  ARG B CD  
11864 N NE  . ARG B 396  ? 0.2876 0.4182 0.3230 -0.0338 0.0025  0.0088  394  ARG B NE  
11865 C CZ  . ARG B 396  ? 0.3352 0.4742 0.3748 -0.0311 0.0031  0.0092  394  ARG B CZ  
11866 N NH1 . ARG B 396  ? 0.3219 0.4709 0.3648 -0.0300 0.0051  0.0107  394  ARG B NH1 
11867 N NH2 . ARG B 396  ? 0.3102 0.4474 0.3505 -0.0294 0.0017  0.0081  394  ARG B NH2 
11868 N N   . LYS B 397  ? 0.2170 0.3333 0.2382 -0.0315 0.0099  0.0089  395  LYS B N   
11869 C CA  . LYS B 397  ? 0.2365 0.3528 0.2550 -0.0334 0.0111  0.0102  395  LYS B CA  
11870 C C   . LYS B 397  ? 0.2279 0.3501 0.2477 -0.0389 0.0108  0.0130  395  LYS B C   
11871 O O   . LYS B 397  ? 0.2364 0.3550 0.2531 -0.0426 0.0103  0.0143  395  LYS B O   
11872 C CB  . LYS B 397  ? 0.2211 0.3421 0.2399 -0.0289 0.0139  0.0096  395  LYS B CB  
11873 C CG  . LYS B 397  ? 0.2435 0.3617 0.2583 -0.0297 0.0150  0.0101  395  LYS B CG  
11874 C CD  . LYS B 397  ? 0.2922 0.4199 0.3084 -0.0323 0.0168  0.0127  395  LYS B CD  
11875 C CE  . LYS B 397  ? 0.2669 0.3921 0.2788 -0.0331 0.0180  0.0134  395  LYS B CE  
11876 N NZ  . LYS B 397  ? 0.2560 0.3906 0.2692 -0.0363 0.0197  0.0162  395  LYS B NZ  
11877 N N   . ILE B 398  ? 0.2007 0.3320 0.2250 -0.0397 0.0109  0.0141  396  ILE B N   
11878 C CA  . ILE B 398  ? 0.2773 0.4149 0.3032 -0.0453 0.0104  0.0169  396  ILE B CA  
11879 C C   . ILE B 398  ? 0.2095 0.3387 0.2326 -0.0504 0.0075  0.0173  396  ILE B C   
11880 O O   . ILE B 398  ? 0.2339 0.3643 0.2561 -0.0555 0.0070  0.0195  396  ILE B O   
11881 C CB  . ILE B 398  ? 0.2842 0.4333 0.3159 -0.0449 0.0109  0.0179  396  ILE B CB  
11882 C CG1 . ILE B 398  ? 0.3379 0.4957 0.3718 -0.0502 0.0111  0.0210  396  ILE B CG1 
11883 C CG2 . ILE B 398  ? 0.2545 0.4005 0.2876 -0.0448 0.0084  0.0166  396  ILE B CG2 
11884 C CD1 . ILE B 398  ? 0.3467 0.5173 0.3866 -0.0495 0.0120  0.0223  396  ILE B CD1 
11885 N N   . HIS B 399  ? 0.2082 0.3285 0.2296 -0.0490 0.0055  0.0151  397  HIS B N   
11886 C CA  . HIS B 399  ? 0.2069 0.3185 0.2251 -0.0533 0.0028  0.0152  397  HIS B CA  
11887 C C   . HIS B 399  ? 0.2084 0.3122 0.2218 -0.0548 0.0028  0.0156  397  HIS B C   
11888 O O   . HIS B 399  ? 0.2301 0.3305 0.2412 -0.0598 0.0013  0.0172  397  HIS B O   
11889 C CB  . HIS B 399  ? 0.1871 0.2916 0.2047 -0.0510 0.0010  0.0128  397  HIS B CB  
11890 C CG  . HIS B 399  ? 0.2200 0.3311 0.2418 -0.0505 0.0004  0.0127  397  HIS B CG  
11891 N ND1 . HIS B 399  ? 0.2367 0.3437 0.2587 -0.0478 -0.0007 0.0105  397  HIS B ND1 
11892 C CD2 . HIS B 399  ? 0.2418 0.3636 0.2678 -0.0525 0.0007  0.0145  397  HIS B CD2 
11893 C CE1 . HIS B 399  ? 0.2423 0.3568 0.2681 -0.0480 -0.0012 0.0111  397  HIS B CE1 
11894 N NE2 . HIS B 399  ? 0.2344 0.3581 0.2628 -0.0508 -0.0004 0.0134  397  HIS B NE2 
11895 N N   . THR B 400  ? 0.2013 0.3021 0.2129 -0.0505 0.0043  0.0143  398  THR B N   
11896 C CA  . THR B 400  ? 0.2179 0.3123 0.2251 -0.0517 0.0044  0.0148  398  THR B CA  
11897 C C   . THR B 400  ? 0.1819 0.2827 0.1890 -0.0555 0.0056  0.0178  398  THR B C   
11898 O O   . THR B 400  ? 0.2094 0.3051 0.2131 -0.0594 0.0046  0.0192  398  THR B O   
11899 C CB  . THR B 400  ? 0.2039 0.2952 0.2095 -0.0463 0.0058  0.0129  398  THR B CB  
11900 O OG1 . THR B 400  ? 0.1997 0.2832 0.2046 -0.0437 0.0043  0.0104  398  THR B OG1 
11901 C CG2 . THR B 400  ? 0.2283 0.3150 0.2296 -0.0473 0.0063  0.0137  398  THR B CG2 
11902 N N   . ASP B 401  ? 0.2247 0.3370 0.2358 -0.0546 0.0078  0.0188  399  ASP B N   
11903 C CA  . ASP B 401  ? 0.2530 0.3727 0.2644 -0.0582 0.0093  0.0217  399  ASP B CA  
11904 C C   . ASP B 401  ? 0.1957 0.3156 0.2074 -0.0648 0.0072  0.0240  399  ASP B C   
11905 O O   . ASP B 401  ? 0.2239 0.3425 0.2330 -0.0691 0.0071  0.0262  399  ASP B O   
11906 C CB  . ASP B 401  ? 0.2557 0.3882 0.2719 -0.0554 0.0120  0.0222  399  ASP B CB  
11907 C CG  . ASP B 401  ? 0.3339 0.4665 0.3488 -0.0496 0.0145  0.0205  399  ASP B CG  
11908 O OD1 . ASP B 401  ? 0.2902 0.4148 0.3005 -0.0487 0.0144  0.0197  399  ASP B OD1 
11909 O OD2 . ASP B 401  ? 0.2873 0.4281 0.3059 -0.0458 0.0164  0.0199  399  ASP B OD2 
11910 N N   . VAL B 402  ? 0.2104 0.3314 0.2249 -0.0658 0.0054  0.0234  400  VAL B N   
11911 C CA  . VAL B 402  ? 0.2269 0.3471 0.2413 -0.0722 0.0030  0.0252  400  VAL B CA  
11912 C C   . VAL B 402  ? 0.2090 0.3159 0.2178 -0.0747 0.0007  0.0249  400  VAL B C   
11913 O O   . VAL B 402  ? 0.2432 0.3481 0.2497 -0.0801 -0.0003 0.0272  400  VAL B O   
11914 C CB  . VAL B 402  ? 0.2472 0.3707 0.2654 -0.0721 0.0014  0.0243  400  VAL B CB  
11915 C CG1 . VAL B 402  ? 0.2817 0.4019 0.2988 -0.0786 -0.0015 0.0257  400  VAL B CG1 
11916 C CG2 . VAL B 402  ? 0.2404 0.3779 0.2645 -0.0700 0.0036  0.0252  400  VAL B CG2 
11917 N N   . SER B 403  ? 0.2196 0.3172 0.2260 -0.0708 -0.0001 0.0221  401  SER B N   
11918 C CA  . SER B 403  ? 0.2400 0.3248 0.2410 -0.0724 -0.0021 0.0216  401  SER B CA  
11919 C C   . SER B 403  ? 0.1976 0.2805 0.1952 -0.0742 -0.0012 0.0236  401  SER B C   
11920 O O   . SER B 403  ? 0.2361 0.3125 0.2301 -0.0786 -0.0029 0.0250  401  SER B O   
11921 C CB  . SER B 403  ? 0.2188 0.2959 0.2185 -0.0671 -0.0025 0.0185  401  SER B CB  
11922 O OG  . SER B 403  ? 0.2354 0.3008 0.2301 -0.0679 -0.0042 0.0180  401  SER B OG  
11923 N N   . TYR B 404  ? 0.2259 0.3142 0.2242 -0.0708 0.0015  0.0236  402  TYR B N   
11924 C CA  . TYR B 404  ? 0.2746 0.3618 0.2695 -0.0723 0.0027  0.0255  402  TYR B CA  
11925 C C   . TYR B 404  ? 0.2309 0.3231 0.2261 -0.0787 0.0025  0.0290  402  TYR B C   
11926 O O   . TYR B 404  ? 0.2376 0.3236 0.2286 -0.0825 0.0014  0.0308  402  TYR B O   
11927 C CB  . TYR B 404  ? 0.2257 0.3196 0.2218 -0.0676 0.0058  0.0249  402  TYR B CB  
11928 C CG  . TYR B 404  ? 0.2269 0.3181 0.2186 -0.0679 0.0069  0.0262  402  TYR B CG  
11929 C CD1 . TYR B 404  ? 0.2839 0.3812 0.2752 -0.0719 0.0082  0.0293  402  TYR B CD1 
11930 C CD2 . TYR B 404  ? 0.2572 0.3398 0.2453 -0.0644 0.0066  0.0243  402  TYR B CD2 
11931 C CE1 . TYR B 404  ? 0.2708 0.3656 0.2578 -0.0722 0.0093  0.0306  402  TYR B CE1 
11932 C CE2 . TYR B 404  ? 0.2359 0.3160 0.2198 -0.0646 0.0074  0.0255  402  TYR B CE2 
11933 C CZ  . TYR B 404  ? 0.2749 0.3609 0.2581 -0.0685 0.0088  0.0286  402  TYR B CZ  
11934 O OH  . TYR B 404  ? 0.2998 0.3834 0.2785 -0.0689 0.0097  0.0299  402  TYR B OH  
11935 N N   . ILE B 405  ? 0.2415 0.3451 0.2416 -0.0801 0.0035  0.0302  403  ILE B N   
11936 C CA  . ILE B 405  ? 0.2780 0.3877 0.2790 -0.0864 0.0035  0.0336  403  ILE B CA  
11937 C C   . ILE B 405  ? 0.2374 0.3388 0.2360 -0.0919 0.0001  0.0344  403  ILE B C   
11938 O O   . ILE B 405  ? 0.2746 0.3737 0.2705 -0.0972 -0.0007 0.0370  403  ILE B O   
11939 C CB  . ILE B 405  ? 0.2843 0.4087 0.2917 -0.0862 0.0054  0.0346  403  ILE B CB  
11940 C CG1 . ILE B 405  ? 0.3059 0.4376 0.3146 -0.0809 0.0090  0.0341  403  ILE B CG1 
11941 C CG2 . ILE B 405  ? 0.2682 0.3994 0.2770 -0.0931 0.0051  0.0383  403  ILE B CG2 
11942 C CD1 . ILE B 405  ? 0.4152 0.5610 0.4302 -0.0791 0.0110  0.0345  403  ILE B CD1 
11943 N N   . ALA B 406  ? 0.2790 0.3752 0.2782 -0.0907 -0.0021 0.0320  404  ALA B N   
11944 C CA  . ALA B 406  ? 0.2753 0.3625 0.2715 -0.0955 -0.0054 0.0323  404  ALA B CA  
11945 C C   . ALA B 406  ? 0.2858 0.3601 0.2757 -0.0962 -0.0067 0.0323  404  ALA B C   
11946 O O   . ALA B 406  ? 0.3028 0.3713 0.2895 -0.1016 -0.0087 0.0341  404  ALA B O   
11947 C CB  . ALA B 406  ? 0.2912 0.3753 0.2889 -0.0932 -0.0072 0.0294  404  ALA B CB  
11948 N N   . CYS B 407  ? 0.2629 0.3324 0.2510 -0.0907 -0.0057 0.0303  405  CYS B N   
11949 C CA  . CYS B 407  ? 0.3085 0.3663 0.2908 -0.0909 -0.0068 0.0304  405  CYS B CA  
11950 C C   . CYS B 407  ? 0.2576 0.3176 0.2377 -0.0941 -0.0056 0.0336  405  CYS B C   
11951 O O   . CYS B 407  ? 0.2938 0.3450 0.2691 -0.0973 -0.0072 0.0350  405  CYS B O   
11952 C CB  . CYS B 407  ? 0.2579 0.3107 0.2393 -0.0843 -0.0062 0.0274  405  CYS B CB  
11953 S SG  . CYS B 407  ? 0.3416 0.3887 0.3244 -0.0813 -0.0082 0.0238  405  CYS B SG  
11954 N N   . ALA B 408  ? 0.2579 0.3296 0.2411 -0.0934 -0.0027 0.0349  406  ALA B N   
11955 C CA  . ALA B 408  ? 0.2932 0.3684 0.2746 -0.0969 -0.0013 0.0382  406  ALA B CA  
11956 C C   . ALA B 408  ? 0.2710 0.3463 0.2518 -0.1044 -0.0031 0.0412  406  ALA B C   
11957 O O   . ALA B 408  ? 0.3325 0.4030 0.3091 -0.1084 -0.0037 0.0437  406  ALA B O   
11958 C CB  . ALA B 408  ? 0.3173 0.4059 0.3025 -0.0944 0.0022  0.0388  406  ALA B CB  
11959 N N   . ALA B 409  ? 0.2910 0.3711 0.2757 -0.1066 -0.0042 0.0410  407  ALA B N   
11960 C CA  . ALA B 409  ? 0.3548 0.4345 0.3391 -0.1140 -0.0062 0.0436  407  ALA B CA  
11961 C C   . ALA B 409  ? 0.3059 0.3701 0.2840 -0.1165 -0.0094 0.0434  407  ALA B C   
11962 O O   . ALA B 409  ? 0.3476 0.4082 0.3225 -0.1223 -0.0106 0.0463  407  ALA B O   
11963 C CB  . ALA B 409  ? 0.2901 0.3771 0.2795 -0.1153 -0.0071 0.0430  407  ALA B CB  
11964 N N   . LYS B 410  ? 0.3209 0.3758 0.2973 -0.1122 -0.0108 0.0401  408  LYS B N   
11965 C CA  . LYS B 410  ? 0.2868 0.3267 0.2573 -0.1137 -0.0137 0.0396  408  LYS B CA  
11966 C C   . LYS B 410  ? 0.3522 0.3864 0.3179 -0.1138 -0.0131 0.0414  408  LYS B C   
11967 O O   . LYS B 410  ? 0.3447 0.3707 0.3059 -0.1184 -0.0151 0.0434  408  LYS B O   
11968 C CB  . LYS B 410  ? 0.3150 0.3476 0.2852 -0.1083 -0.0148 0.0356  408  LYS B CB  
11969 C CG  . LYS B 410  ? 0.3386 0.3558 0.3030 -0.1091 -0.0177 0.0347  408  LYS B CG  
11970 C CD  . LYS B 410  ? 0.3646 0.3754 0.3288 -0.1032 -0.0184 0.0308  408  LYS B CD  
11971 C CE  . LYS B 410  ? 0.4043 0.4194 0.3723 -0.1026 -0.0190 0.0288  408  LYS B CE  
11972 N NZ  . LYS B 410  ? 0.3927 0.4011 0.3582 -0.1076 -0.0220 0.0289  408  LYS B NZ  
11973 N N   . LEU B 411  ? 0.3254 0.3637 0.2918 -0.1088 -0.0106 0.0407  409  LEU B N   
11974 C CA  . LEU B 411  ? 0.3434 0.3768 0.3052 -0.1087 -0.0100 0.0424  409  LEU B CA  
11975 C C   . LEU B 411  ? 0.3221 0.3606 0.2830 -0.1149 -0.0092 0.0466  409  LEU B C   
11976 O O   . LEU B 411  ? 0.3462 0.3767 0.3020 -0.1181 -0.0106 0.0488  409  LEU B O   
11977 C CB  . LEU B 411  ? 0.3082 0.3456 0.2711 -0.1023 -0.0074 0.0406  409  LEU B CB  
11978 C CG  . LEU B 411  ? 0.3169 0.3461 0.2789 -0.0965 -0.0085 0.0370  409  LEU B CG  
11979 C CD1 . LEU B 411  ? 0.3181 0.3537 0.2825 -0.0905 -0.0059 0.0351  409  LEU B CD1 
11980 C CD2 . LEU B 411  ? 0.3307 0.3465 0.2867 -0.0968 -0.0107 0.0373  409  LEU B CD2 
11981 N N   . LEU B 412  ? 0.3445 0.3967 0.3104 -0.1165 -0.0071 0.0480  410  LEU B N   
11982 C CA  . LEU B 412  ? 0.3406 0.3991 0.3060 -0.1223 -0.0060 0.0522  410  LEU B CA  
11983 C C   . LEU B 412  ? 0.3829 0.4350 0.3458 -0.1296 -0.0090 0.0545  410  LEU B C   
11984 O O   . LEU B 412  ? 0.4157 0.4681 0.3760 -0.1347 -0.0088 0.0582  410  LEU B O   
11985 C CB  . LEU B 412  ? 0.3877 0.4628 0.3595 -0.1222 -0.0030 0.0530  410  LEU B CB  
11986 C CG  . LEU B 412  ? 0.3865 0.4688 0.3597 -0.1161 0.0005  0.0519  410  LEU B CG  
11987 C CD1 . LEU B 412  ? 0.3901 0.4881 0.3700 -0.1151 0.0031  0.0521  410  LEU B CD1 
11988 C CD2 . LEU B 412  ? 0.4275 0.5084 0.3961 -0.1174 0.0018  0.0545  410  LEU B CD2 
11989 N N   . ALA B 413  ? 0.3789 0.4251 0.3423 -0.1304 -0.0117 0.0525  411  ALA B N   
11990 C CA  . ALA B 413  ? 0.4464 0.4842 0.4064 -0.1370 -0.0149 0.0543  411  ALA B CA  
11991 C C   . ALA B 413  ? 0.4083 0.4299 0.3611 -0.1366 -0.0172 0.0540  411  ALA B C   
11992 O O   . ALA B 413  ? 0.4520 0.4650 0.4010 -0.1420 -0.0199 0.0557  411  ALA B O   
11993 C CB  . ALA B 413  ? 0.3976 0.4353 0.3604 -0.1382 -0.0170 0.0523  411  ALA B CB  
11994 N N   . ALA B 414  ? 0.3653 0.3826 0.3163 -0.1304 -0.0162 0.0521  412  ALA B N   
11995 C CA  . ALA B 414  ? 0.3596 0.3620 0.3043 -0.1292 -0.0183 0.0517  412  ALA B CA  
11996 C C   . ALA B 414  ? 0.4057 0.4074 0.3471 -0.1278 -0.0167 0.0536  412  ALA B C   
11997 O O   . ALA B 414  ? 0.3963 0.3878 0.3336 -0.1244 -0.0178 0.0525  412  ALA B O   
11998 C CB  . ALA B 414  ? 0.3748 0.3703 0.3197 -0.1230 -0.0194 0.0473  412  ALA B CB  
11999 N N   . THR B 415  ? 0.3731 0.3858 0.3162 -0.1302 -0.0141 0.0565  413  THR B N   
12000 C CA  . THR B 415  ? 0.3999 0.4127 0.3398 -0.1286 -0.0124 0.0582  413  THR B CA  
12001 C C   . THR B 415  ? 0.3925 0.3926 0.3254 -0.1320 -0.0148 0.0607  413  THR B C   
12002 O O   . THR B 415  ? 0.4277 0.4243 0.3568 -0.1297 -0.0141 0.0615  413  THR B O   
12003 C CB  . THR B 415  ? 0.3825 0.4099 0.3254 -0.1307 -0.0090 0.0609  413  THR B CB  
12004 O OG1 . THR B 415  ? 0.4214 0.4513 0.3643 -0.1385 -0.0098 0.0645  413  THR B OG1 
12005 C CG2 . THR B 415  ? 0.3950 0.4347 0.3446 -0.1265 -0.0065 0.0584  413  THR B CG2 
12006 N N   . ASP B 416  ? 0.4524 0.4454 0.3833 -0.1375 -0.0175 0.0620  414  ASP B N   
12007 C CA  . ASP B 416  ? 0.4475 0.4266 0.3714 -0.1403 -0.0202 0.0640  414  ASP B CA  
12008 C C   . ASP B 416  ? 0.4119 0.3785 0.3327 -0.1346 -0.0221 0.0609  414  ASP B C   
12009 O O   . ASP B 416  ? 0.4916 0.4469 0.4066 -0.1353 -0.0240 0.0623  414  ASP B O   
12010 C CB  . ASP B 416  ? 0.4494 0.4240 0.3720 -0.1478 -0.0228 0.0660  414  ASP B CB  
12011 C CG  . ASP B 416  ? 0.5853 0.5612 0.5120 -0.1474 -0.0240 0.0629  414  ASP B CG  
12012 O OD1 . ASP B 416  ? 0.5663 0.5542 0.4990 -0.1448 -0.0218 0.0612  414  ASP B OD1 
12013 O OD2 . ASP B 416  ? 0.6686 0.6331 0.5921 -0.1496 -0.0272 0.0621  414  ASP B OD2 
12014 N N   . VAL B 417  ? 0.4132 0.3818 0.3378 -0.1289 -0.0217 0.0567  415  VAL B N   
12015 C CA  . VAL B 417  ? 0.3857 0.3428 0.3081 -0.1240 -0.0237 0.0535  415  VAL B CA  
12016 C C   . VAL B 417  ? 0.3927 0.3537 0.3172 -0.1166 -0.0218 0.0509  415  VAL B C   
12017 O O   . VAL B 417  ? 0.3765 0.3286 0.2981 -0.1124 -0.0230 0.0495  415  VAL B O   
12018 C CB  . VAL B 417  ? 0.4686 0.4231 0.3932 -0.1244 -0.0255 0.0508  415  VAL B CB  
12019 C CG1 . VAL B 417  ? 0.3914 0.3351 0.3141 -0.1189 -0.0272 0.0474  415  VAL B CG1 
12020 C CG2 . VAL B 417  ? 0.4507 0.4006 0.3728 -0.1321 -0.0277 0.0534  415  VAL B CG2 
12021 N N   . VAL B 418  ? 0.3639 0.3380 0.2934 -0.1149 -0.0188 0.0503  416  VAL B N   
12022 C CA  . VAL B 418  ? 0.3206 0.2989 0.2521 -0.1083 -0.0169 0.0479  416  VAL B CA  
12023 C C   . VAL B 418  ? 0.3543 0.3446 0.2874 -0.1090 -0.0137 0.0499  416  VAL B C   
12024 O O   . VAL B 418  ? 0.3492 0.3464 0.2835 -0.1141 -0.0128 0.0527  416  VAL B O   
12025 C CB  . VAL B 418  ? 0.3589 0.3408 0.2955 -0.1038 -0.0165 0.0438  416  VAL B CB  
12026 C CG1 . VAL B 418  ? 0.3376 0.3073 0.2721 -0.1022 -0.0194 0.0416  416  VAL B CG1 
12027 C CG2 . VAL B 418  ? 0.3196 0.3121 0.2611 -0.1071 -0.0153 0.0442  416  VAL B CG2 
12028 N N   . PHE B 419  ? 0.3214 0.3141 0.2545 -0.1038 -0.0121 0.0486  417  PHE B N   
12029 C CA  . PHE B 419  ? 0.3120 0.3159 0.2464 -0.1034 -0.0088 0.0499  417  PHE B CA  
12030 C C   . PHE B 419  ? 0.2810 0.2942 0.2212 -0.0987 -0.0067 0.0467  417  PHE B C   
12031 O O   . PHE B 419  ? 0.2923 0.3033 0.2327 -0.0930 -0.0065 0.0438  417  PHE B O   
12032 C CB  . PHE B 419  ? 0.3235 0.3232 0.2530 -0.1011 -0.0085 0.0508  417  PHE B CB  
12033 C CG  . PHE B 419  ? 0.3458 0.3562 0.2760 -0.1003 -0.0052 0.0519  417  PHE B CG  
12034 C CD1 . PHE B 419  ? 0.3499 0.3688 0.2807 -0.1052 -0.0033 0.0551  417  PHE B CD1 
12035 C CD2 . PHE B 419  ? 0.3162 0.3282 0.2461 -0.0945 -0.0038 0.0496  417  PHE B CD2 
12036 C CE1 . PHE B 419  ? 0.3555 0.3843 0.2866 -0.1041 0.0000  0.0561  417  PHE B CE1 
12037 C CE2 . PHE B 419  ? 0.2874 0.3088 0.2173 -0.0935 -0.0007 0.0504  417  PHE B CE2 
12038 C CZ  . PHE B 419  ? 0.3210 0.3509 0.2516 -0.0981 0.0013  0.0536  417  PHE B CZ  
12039 N N   . PRO B 420  ? 0.2905 0.3140 0.2353 -0.1008 -0.0051 0.0471  418  PRO B N   
12040 C CA  . PRO B 420  ? 0.2694 0.3013 0.2197 -0.0963 -0.0033 0.0441  418  PRO B CA  
12041 C C   . PRO B 420  ? 0.2708 0.3106 0.2215 -0.0926 -0.0001 0.0438  418  PRO B C   
12042 O O   . PRO B 420  ? 0.2658 0.3108 0.2148 -0.0952 0.0016  0.0467  418  PRO B O   
12043 C CB  . PRO B 420  ? 0.2963 0.3367 0.2512 -0.1005 -0.0028 0.0453  418  PRO B CB  
12044 C CG  . PRO B 420  ? 0.3012 0.3342 0.2526 -0.1069 -0.0054 0.0480  418  PRO B CG  
12045 C CD  . PRO B 420  ? 0.3022 0.3289 0.2478 -0.1076 -0.0056 0.0501  418  PRO B CD  
12046 N N   . GLN B 421  ? 0.2742 0.3145 0.2268 -0.0866 0.0006  0.0404  419  GLN B N   
12047 C CA  . GLN B 421  ? 0.2782 0.3247 0.2309 -0.0824 0.0033  0.0395  419  GLN B CA  
12048 C C   . GLN B 421  ? 0.2700 0.3244 0.2284 -0.0787 0.0049  0.0368  419  GLN B C   
12049 O O   . GLN B 421  ? 0.2600 0.3100 0.2200 -0.0752 0.0036  0.0338  419  GLN B O   
12050 C CB  . GLN B 421  ? 0.2584 0.2960 0.2069 -0.0786 0.0022  0.0380  419  GLN B CB  
12051 C CG  . GLN B 421  ? 0.2702 0.2988 0.2129 -0.0821 0.0002  0.0407  419  GLN B CG  
12052 C CD  . GLN B 421  ? 0.2867 0.3050 0.2260 -0.0784 -0.0018 0.0390  419  GLN B CD  
12053 O OE1 . GLN B 421  ? 0.2996 0.3125 0.2405 -0.0759 -0.0035 0.0364  419  GLN B OE1 
12054 N NE2 . GLN B 421  ? 0.2833 0.2992 0.2179 -0.0780 -0.0016 0.0404  419  GLN B NE2 
12055 N N   . PHE B 422  ? 0.2785 0.3446 0.2401 -0.0794 0.0076  0.0378  420  PHE B N   
12056 C CA  . PHE B 422  ? 0.2527 0.3271 0.2201 -0.0765 0.0090  0.0357  420  PHE B CA  
12057 C C   . PHE B 422  ? 0.2504 0.3285 0.2179 -0.0706 0.0114  0.0335  420  PHE B C   
12058 O O   . PHE B 422  ? 0.2550 0.3414 0.2225 -0.0701 0.0142  0.0346  420  PHE B O   
12059 C CB  . PHE B 422  ? 0.2147 0.2998 0.1861 -0.0806 0.0104  0.0382  420  PHE B CB  
12060 C CG  . PHE B 422  ? 0.2484 0.3292 0.2194 -0.0867 0.0077  0.0403  420  PHE B CG  
12061 C CD1 . PHE B 422  ? 0.2780 0.3531 0.2506 -0.0867 0.0052  0.0384  420  PHE B CD1 
12062 C CD2 . PHE B 422  ? 0.2799 0.3621 0.2486 -0.0925 0.0078  0.0441  420  PHE B CD2 
12063 C CE1 . PHE B 422  ? 0.2937 0.3642 0.2655 -0.0922 0.0026  0.0401  420  PHE B CE1 
12064 C CE2 . PHE B 422  ? 0.2999 0.3776 0.2680 -0.0983 0.0053  0.0459  420  PHE B CE2 
12065 C CZ  . PHE B 422  ? 0.3204 0.3920 0.2900 -0.0980 0.0026  0.0438  420  PHE B CZ  
12066 N N   . ALA B 423  ? 0.2390 0.3108 0.2064 -0.0660 0.0102  0.0303  421  ALA B N   
12067 C CA  . ALA B 423  ? 0.2688 0.3426 0.2360 -0.0604 0.0120  0.0278  421  ALA B CA  
12068 C C   . ALA B 423  ? 0.2641 0.3466 0.2370 -0.0576 0.0137  0.0262  421  ALA B C   
12069 O O   . ALA B 423  ? 0.2734 0.3539 0.2495 -0.0566 0.0122  0.0245  421  ALA B O   
12070 C CB  . ALA B 423  ? 0.2277 0.2909 0.1926 -0.0571 0.0098  0.0254  421  ALA B CB  
12071 N N   . THR B 424  ? 0.2750 0.3671 0.2491 -0.0561 0.0168  0.0267  422  THR B N   
12072 C CA  . THR B 424  ? 0.2515 0.3521 0.2309 -0.0529 0.0185  0.0251  422  THR B CA  
12073 C C   . THR B 424  ? 0.2311 0.3399 0.2099 -0.0501 0.0220  0.0252  422  THR B C   
12074 O O   . THR B 424  ? 0.2848 0.3963 0.2607 -0.0526 0.0234  0.0275  422  THR B O   
12075 C CB  . THR B 424  ? 0.2777 0.3848 0.2619 -0.0568 0.0182  0.0269  422  THR B CB  
12076 O OG1 . THR B 424  ? 0.2832 0.3986 0.2724 -0.0532 0.0198  0.0254  422  THR B OG1 
12077 C CG2 . THR B 424  ? 0.2830 0.3966 0.2666 -0.0619 0.0194  0.0306  422  THR B CG2 
12078 N N   . HIS B 425  ? 0.2443 0.3565 0.2255 -0.0449 0.0235  0.0226  423  HIS B N   
12079 C CA  . HIS B 425  ? 0.2282 0.3492 0.2096 -0.0418 0.0270  0.0224  423  HIS B CA  
12080 C C   . HIS B 425  ? 0.2802 0.4130 0.2676 -0.0418 0.0289  0.0233  423  HIS B C   
12081 O O   . HIS B 425  ? 0.3147 0.4557 0.3031 -0.0387 0.0319  0.0230  423  HIS B O   
12082 C CB  . HIS B 425  ? 0.2503 0.3671 0.2298 -0.0358 0.0275  0.0189  423  HIS B CB  
12083 C CG  . HIS B 425  ? 0.2849 0.3912 0.2585 -0.0356 0.0259  0.0182  423  HIS B CG  
12084 N ND1 . HIS B 425  ? 0.3484 0.4461 0.3209 -0.0325 0.0239  0.0153  423  HIS B ND1 
12085 C CD2 . HIS B 425  ? 0.2773 0.3805 0.2458 -0.0382 0.0258  0.0200  423  HIS B CD2 
12086 C CE1 . HIS B 425  ? 0.3072 0.3973 0.2744 -0.0331 0.0227  0.0154  423  HIS B CE1 
12087 N NE2 . HIS B 425  ? 0.2778 0.3709 0.2424 -0.0365 0.0237  0.0182  423  HIS B NE2 
12088 N N   . ASN B 426  ? 0.2852 0.4191 0.2766 -0.0450 0.0270  0.0243  424  ASN B N   
12089 C CA  . ASN B 426  ? 0.2785 0.4232 0.2761 -0.0449 0.0282  0.0250  424  ASN B CA  
12090 C C   . ASN B 426  ? 0.2873 0.4409 0.2862 -0.0500 0.0296  0.0287  424  ASN B C   
12091 O O   . ASN B 426  ? 0.2561 0.4063 0.2540 -0.0556 0.0275  0.0309  424  ASN B O   
12092 C CB  . ASN B 426  ? 0.2729 0.4136 0.2737 -0.0459 0.0253  0.0240  424  ASN B CB  
12093 C CG  . ASN B 426  ? 0.2972 0.4483 0.3045 -0.0449 0.0262  0.0242  424  ASN B CG  
12094 O OD1 . ASN B 426  ? 0.2785 0.4402 0.2888 -0.0470 0.0280  0.0266  424  ASN B OD1 
12095 N ND2 . ASN B 426  ? 0.2876 0.4357 0.2972 -0.0417 0.0248  0.0218  424  ASN B ND2 
12096 N N   . ALA B 427  ? 0.3142 0.4791 0.3153 -0.0480 0.0330  0.0295  425  ALA B N   
12097 C CA  . ALA B 427  ? 0.3611 0.5355 0.3634 -0.0527 0.0347  0.0332  425  ALA B CA  
12098 C C   . ALA B 427  ? 0.2678 0.4472 0.2754 -0.0575 0.0330  0.0353  425  ALA B C   
12099 O O   . ALA B 427  ? 0.2988 0.4809 0.3061 -0.0635 0.0326  0.0386  425  ALA B O   
12100 C CB  . ALA B 427  ? 0.3417 0.5279 0.3458 -0.0488 0.0389  0.0334  425  ALA B CB  
12101 N N   . GLN B 428  ? 0.2877 0.4682 0.2997 -0.0552 0.0318  0.0335  426  GLN B N   
12102 C CA  . GLN B 428  ? 0.3279 0.5124 0.3446 -0.0598 0.0298  0.0353  426  GLN B CA  
12103 C C   . GLN B 428  ? 0.2872 0.4604 0.3005 -0.0651 0.0261  0.0360  426  GLN B C   
12104 O O   . GLN B 428  ? 0.3128 0.4884 0.3270 -0.0713 0.0250  0.0389  426  GLN B O   
12105 C CB  . GLN B 428  ? 0.3097 0.4973 0.3314 -0.0558 0.0292  0.0331  426  GLN B CB  
12106 C CG  . GLN B 428  ? 0.3128 0.5083 0.3402 -0.0599 0.0278  0.0351  426  GLN B CG  
12107 C CD  . GLN B 428  ? 0.2973 0.4834 0.3231 -0.0652 0.0239  0.0355  426  GLN B CD  
12108 O OE1 . GLN B 428  ? 0.3314 0.5054 0.3536 -0.0637 0.0218  0.0332  426  GLN B OE1 
12109 N NE2 . GLN B 428  ? 0.3606 0.5521 0.3888 -0.0715 0.0228  0.0385  426  GLN B NE2 
12110 N N   . THR B 429  ? 0.2815 0.4421 0.2907 -0.0627 0.0243  0.0333  427  THR B N   
12111 C CA  . THR B 429  ? 0.3042 0.4534 0.3097 -0.0670 0.0210  0.0338  427  THR B CA  
12112 C C   . THR B 429  ? 0.2614 0.4095 0.2628 -0.0719 0.0214  0.0369  427  THR B C   
12113 O O   . THR B 429  ? 0.2854 0.4311 0.2862 -0.0779 0.0193  0.0391  427  THR B O   
12114 C CB  . THR B 429  ? 0.2835 0.4204 0.2852 -0.0630 0.0195  0.0306  427  THR B CB  
12115 O OG1 . THR B 429  ? 0.2611 0.3994 0.2664 -0.0581 0.0194  0.0278  427  THR B OG1 
12116 C CG2 . THR B 429  ? 0.2921 0.4177 0.2907 -0.0670 0.0160  0.0308  427  THR B CG2 
12117 N N   . LEU B 430  ? 0.3117 0.4612 0.3100 -0.0694 0.0239  0.0369  428  LEU B N   
12118 C CA  . LEU B 430  ? 0.2797 0.4284 0.2738 -0.0737 0.0245  0.0399  428  LEU B CA  
12119 C C   . LEU B 430  ? 0.3052 0.4644 0.3028 -0.0794 0.0254  0.0437  428  LEU B C   
12120 O O   . LEU B 430  ? 0.2802 0.4359 0.2756 -0.0855 0.0237  0.0464  428  LEU B O   
12121 C CB  . LEU B 430  ? 0.2939 0.4446 0.2847 -0.0695 0.0276  0.0393  428  LEU B CB  
12122 C CG  . LEU B 430  ? 0.3103 0.4592 0.2956 -0.0725 0.0286  0.0418  428  LEU B CG  
12123 C CD1 . LEU B 430  ? 0.3456 0.4944 0.3275 -0.0668 0.0310  0.0398  428  LEU B CD1 
12124 C CD2 . LEU B 430  ? 0.3740 0.5338 0.3612 -0.0776 0.0305  0.0459  428  LEU B CD2 
12125 N N   . ALA B 431  ? 0.3410 0.5133 0.3441 -0.0774 0.0279  0.0439  429  ALA B N   
12126 C CA  . ALA B 431  ? 0.3503 0.5343 0.3574 -0.0826 0.0290  0.0476  429  ALA B CA  
12127 C C   . ALA B 431  ? 0.3157 0.4969 0.3249 -0.0884 0.0255  0.0489  429  ALA B C   
12128 O O   . ALA B 431  ? 0.3640 0.5481 0.3733 -0.0950 0.0249  0.0524  429  ALA B O   
12129 C CB  . ALA B 431  ? 0.3242 0.5226 0.3372 -0.0786 0.0322  0.0473  429  ALA B CB  
12130 N N   . ALA B 432  ? 0.3066 0.4818 0.3173 -0.0862 0.0230  0.0461  430  ALA B N   
12131 C CA  . ALA B 432  ? 0.2997 0.4712 0.3118 -0.0914 0.0195  0.0469  430  ALA B CA  
12132 C C   . ALA B 432  ? 0.3119 0.4715 0.3180 -0.0966 0.0170  0.0484  430  ALA B C   
12133 O O   . ALA B 432  ? 0.3271 0.4872 0.3335 -0.1032 0.0153  0.0511  430  ALA B O   
12134 C CB  . ALA B 432  ? 0.3172 0.4834 0.3311 -0.0875 0.0174  0.0434  430  ALA B CB  
12135 N N   . ILE B 433  ? 0.3061 0.4549 0.3066 -0.0937 0.0167  0.0467  431  ILE B N   
12136 C CA  . ILE B 433  ? 0.3660 0.5028 0.3605 -0.0980 0.0143  0.0480  431  ILE B CA  
12137 C C   . ILE B 433  ? 0.3271 0.4685 0.3195 -0.1028 0.0159  0.0520  431  ILE B C   
12138 O O   . ILE B 433  ? 0.3152 0.4514 0.3050 -0.1090 0.0138  0.0545  431  ILE B O   
12139 C CB  . ILE B 433  ? 0.3688 0.4935 0.3584 -0.0932 0.0136  0.0451  431  ILE B CB  
12140 C CG1 . ILE B 433  ? 0.3931 0.5116 0.3843 -0.0899 0.0113  0.0416  431  ILE B CG1 
12141 C CG2 . ILE B 433  ? 0.3699 0.4837 0.3530 -0.0970 0.0118  0.0469  431  ILE B CG2 
12142 C CD1 . ILE B 433  ? 0.4003 0.5079 0.3873 -0.0854 0.0105  0.0389  431  ILE B CD1 
12143 N N   . TYR B 434  ? 0.3365 0.4871 0.3297 -0.1000 0.0196  0.0526  432  TYR B N   
12144 C CA  . TYR B 434  ? 0.3322 0.4882 0.3233 -0.1043 0.0215  0.0565  432  TYR B CA  
12145 C C   . TYR B 434  ? 0.3591 0.5224 0.3539 -0.1115 0.0207  0.0600  432  TYR B C   
12146 O O   . TYR B 434  ? 0.3553 0.5152 0.3469 -0.1177 0.0196  0.0633  432  TYR B O   
12147 C CB  . TYR B 434  ? 0.3277 0.4944 0.3201 -0.0995 0.0259  0.0561  432  TYR B CB  
12148 C CG  . TYR B 434  ? 0.3515 0.5270 0.3431 -0.1035 0.0286  0.0602  432  TYR B CG  
12149 C CD1 . TYR B 434  ? 0.3411 0.5096 0.3261 -0.1063 0.0284  0.0622  432  TYR B CD1 
12150 C CD2 . TYR B 434  ? 0.3792 0.5705 0.3767 -0.1043 0.0314  0.0620  432  TYR B CD2 
12151 C CE1 . TYR B 434  ? 0.4071 0.5840 0.3911 -0.1099 0.0310  0.0660  432  TYR B CE1 
12152 C CE2 . TYR B 434  ? 0.3638 0.5639 0.3607 -0.1079 0.0341  0.0658  432  TYR B CE2 
12153 C CZ  . TYR B 434  ? 0.4119 0.6047 0.4020 -0.1108 0.0339  0.0678  432  TYR B CZ  
12154 O OH  . TYR B 434  ? 0.4551 0.6566 0.4443 -0.1145 0.0367  0.0717  432  TYR B OH  
12155 N N   . HIS B 435  ? 0.3823 0.5551 0.3838 -0.1110 0.0209  0.0595  433  HIS B N   
12156 C CA  . HIS B 435  ? 0.3787 0.5592 0.3840 -0.1180 0.0200  0.0628  433  HIS B CA  
12157 C C   . HIS B 435  ? 0.3724 0.5418 0.3760 -0.1228 0.0155  0.0628  433  HIS B C   
12158 O O   . HIS B 435  ? 0.3638 0.5334 0.3669 -0.1302 0.0140  0.0661  433  HIS B O   
12159 C CB  . HIS B 435  ? 0.3886 0.5845 0.4019 -0.1156 0.0221  0.0626  433  HIS B CB  
12160 C CG  . HIS B 435  ? 0.4041 0.6127 0.4192 -0.1129 0.0267  0.0639  433  HIS B CG  
12161 N ND1 . HIS B 435  ? 0.3670 0.5852 0.3832 -0.1182 0.0285  0.0682  433  HIS B ND1 
12162 C CD2 . HIS B 435  ? 0.3907 0.6037 0.4065 -0.1055 0.0298  0.0616  433  HIS B CD2 
12163 C CE1 . HIS B 435  ? 0.4288 0.6572 0.4462 -0.1139 0.0328  0.0684  433  HIS B CE1 
12164 N NE2 . HIS B 435  ? 0.3446 0.5698 0.3617 -0.1062 0.0336  0.0643  433  HIS B NE2 
12165 N N   . MET B 436  ? 0.3835 0.5431 0.3860 -0.1189 0.0133  0.0590  434  MET B N   
12166 C CA  . MET B 436  ? 0.3210 0.4688 0.3211 -0.1228 0.0090  0.0585  434  MET B CA  
12167 C C   . MET B 436  ? 0.3332 0.4702 0.3266 -0.1276 0.0075  0.0608  434  MET B C   
12168 O O   . MET B 436  ? 0.3721 0.5028 0.3637 -0.1336 0.0044  0.0622  434  MET B O   
12169 C CB  . MET B 436  ? 0.3728 0.5114 0.3720 -0.1169 0.0075  0.0540  434  MET B CB  
12170 C CG  . MET B 436  ? 0.4187 0.5437 0.4144 -0.1199 0.0033  0.0531  434  MET B CG  
12171 S SD  . MET B 436  ? 0.4525 0.5673 0.4470 -0.1125 0.0020  0.0479  434  MET B SD  
12172 C CE  . MET B 436  ? 0.3857 0.5127 0.3881 -0.1100 0.0027  0.0464  434  MET B CE  
12173 N N   . ALA B 437  ? 0.3393 0.4734 0.3284 -0.1250 0.0094  0.0611  435  ALA B N   
12174 C CA  . ALA B 437  ? 0.3586 0.4819 0.3409 -0.1290 0.0079  0.0632  435  ALA B CA  
12175 C C   . ALA B 437  ? 0.3834 0.5133 0.3658 -0.1366 0.0085  0.0681  435  ALA B C   
12176 O O   . ALA B 437  ? 0.4194 0.5401 0.3964 -0.1413 0.0067  0.0703  435  ALA B O   
12177 C CB  . ALA B 437  ? 0.4184 0.5370 0.3962 -0.1238 0.0097  0.0620  435  ALA B CB  
12178 N N   . GLY B 438  ? 0.4321 0.5774 0.4204 -0.1379 0.0110  0.0698  436  GLY B N   
12179 C CA  . GLY B 438  ? 0.4527 0.6054 0.4417 -0.1454 0.0116  0.0746  436  GLY B CA  
12180 C C   . GLY B 438  ? 0.4959 0.6521 0.4815 -0.1454 0.0148  0.0771  436  GLY B C   
12181 O O   . GLY B 438  ? 0.4289 0.5827 0.4118 -0.1393 0.0167  0.0751  436  GLY B O   
12182 N N   . LYS B 439  ? 0.4789 0.6406 0.4644 -0.1526 0.0152  0.0817  437  LYS B N   
12183 C CA  . LYS B 439  ? 0.4453 0.6131 0.4284 -0.1534 0.0186  0.0848  437  LYS B CA  
12184 C C   . LYS B 439  ? 0.4705 0.6242 0.4449 -0.1548 0.0173  0.0859  437  LYS B C   
12185 O O   . LYS B 439  ? 0.5179 0.6741 0.4891 -0.1530 0.0201  0.0871  437  LYS B O   
12186 C CB  . LYS B 439  ? 0.4196 0.5998 0.4066 -0.1601 0.0197  0.0892  437  LYS B CB  
12187 N N   . ASP B 440  ? 0.4618 0.6007 0.4321 -0.1579 0.0131  0.0856  438  ASP B N   
12188 C CA  . ASP B 440  ? 0.4991 0.6247 0.4614 -0.1601 0.0115  0.0872  438  ASP B CA  
12189 C C   . ASP B 440  ? 0.4644 0.5802 0.4228 -0.1523 0.0113  0.0832  438  ASP B C   
12190 O O   . ASP B 440  ? 0.4809 0.5888 0.4399 -0.1489 0.0089  0.0795  438  ASP B O   
12191 C CB  . ASP B 440  ? 0.5277 0.6416 0.4872 -0.1667 0.0070  0.0887  438  ASP B CB  
12192 N N   . PHE B 441  ? 0.4431 0.5595 0.3975 -0.1496 0.0137  0.0840  439  PHE B N   
12193 C CA  . PHE B 441  ? 0.4108 0.5186 0.3615 -0.1425 0.0135  0.0804  439  PHE B CA  
12194 C C   . PHE B 441  ? 0.4542 0.5541 0.3971 -0.1436 0.0135  0.0827  439  PHE B C   
12195 O O   . PHE B 441  ? 0.4577 0.5639 0.3989 -0.1475 0.0156  0.0866  439  PHE B O   
12196 C CB  . PHE B 441  ? 0.4021 0.5202 0.3567 -0.1352 0.0171  0.0773  439  PHE B CB  
12197 C CG  . PHE B 441  ? 0.4156 0.5246 0.3665 -0.1282 0.0166  0.0735  439  PHE B CG  
12198 C CD1 . PHE B 441  ? 0.3569 0.4584 0.3093 -0.1244 0.0142  0.0696  439  PHE B CD1 
12199 C CD2 . PHE B 441  ? 0.3804 0.4879 0.3261 -0.1258 0.0184  0.0741  439  PHE B CD2 
12200 C CE1 . PHE B 441  ? 0.3702 0.4634 0.3195 -0.1183 0.0136  0.0663  439  PHE B CE1 
12201 C CE2 . PHE B 441  ? 0.3952 0.4942 0.3375 -0.1197 0.0176  0.0708  439  PHE B CE2 
12202 C CZ  . PHE B 441  ? 0.3796 0.4715 0.3239 -0.1160 0.0152  0.0669  439  PHE B CZ  
12203 N N   . HIS B 442  ? 0.4197 0.5060 0.3579 -0.1400 0.0111  0.0803  440  HIS B N   
12204 C CA  . HIS B 442  ? 0.4265 0.5051 0.3574 -0.1393 0.0111  0.0817  440  HIS B CA  
12205 C C   . HIS B 442  ? 0.4245 0.4949 0.3537 -0.1318 0.0100  0.0773  440  HIS B C   
12206 O O   . HIS B 442  ? 0.3993 0.4653 0.3314 -0.1290 0.0081  0.0739  440  HIS B O   
12207 C CB  . HIS B 442  ? 0.4360 0.5029 0.3616 -0.1457 0.0077  0.0851  440  HIS B CB  
12208 C CG  . HIS B 442  ? 0.5115 0.5667 0.4373 -0.1461 0.0036  0.0830  440  HIS B CG  
12209 N ND1 . HIS B 442  ? 0.5462 0.5885 0.4685 -0.1416 0.0012  0.0801  440  HIS B ND1 
12210 C CD2 . HIS B 442  ? 0.5021 0.5568 0.4313 -0.1504 0.0016  0.0832  440  HIS B CD2 
12211 C CE1 . HIS B 442  ? 0.5004 0.5347 0.4238 -0.1430 -0.0021 0.0787  440  HIS B CE1 
12212 N NE2 . HIS B 442  ? 0.5250 0.5663 0.4523 -0.1483 -0.0019 0.0805  440  HIS B NE2 
12213 N N   . VAL B 443  ? 0.4261 0.4948 0.3505 -0.1286 0.0114  0.0774  441  VAL B N   
12214 C CA  . VAL B 443  ? 0.4094 0.4698 0.3316 -0.1220 0.0102  0.0735  441  VAL B CA  
12215 C C   . VAL B 443  ? 0.4091 0.4545 0.3285 -0.1232 0.0057  0.0730  441  VAL B C   
12216 O O   . VAL B 443  ? 0.4227 0.4610 0.3380 -0.1284 0.0038  0.0763  441  VAL B O   
12217 C CB  . VAL B 443  ? 0.4477 0.5080 0.3643 -0.1193 0.0119  0.0742  441  VAL B CB  
12218 C CG1 . VAL B 443  ? 0.4132 0.4630 0.3269 -0.1136 0.0099  0.0708  441  VAL B CG1 
12219 C CG2 . VAL B 443  ? 0.4512 0.5260 0.3708 -0.1166 0.0164  0.0736  441  VAL B CG2 
12220 N N   . GLY B 444  ? 0.3989 0.4395 0.3207 -0.1183 0.0042  0.0688  442  GLY B N   
12221 C CA  . GLY B 444  ? 0.3742 0.4017 0.2944 -0.1189 0.0002  0.0678  442  GLY B CA  
12222 C C   . GLY B 444  ? 0.3713 0.3998 0.2965 -0.1213 -0.0011 0.0668  442  GLY B C   
12223 O O   . GLY B 444  ? 0.3676 0.3857 0.2920 -0.1207 -0.0042 0.0651  442  GLY B O   
12224 N N   . LYS B 445  ? 0.3634 0.4042 0.2936 -0.1240 0.0011  0.0679  443  LYS B N   
12225 C CA  . LYS B 445  ? 0.3354 0.3782 0.2706 -0.1259 -0.0001 0.0667  443  LYS B CA  
12226 C C   . LYS B 445  ? 0.3592 0.4033 0.2986 -0.1193 0.0001  0.0619  443  LYS B C   
12227 O O   . LYS B 445  ? 0.3546 0.3908 0.2946 -0.1183 -0.0025 0.0595  443  LYS B O   
12228 C CB  . LYS B 445  ? 0.3695 0.4258 0.3090 -0.1308 0.0021  0.0694  443  LYS B CB  
12229 C CG  . LYS B 445  ? 0.4230 0.4811 0.3672 -0.1339 0.0004  0.0688  443  LYS B CG  
12230 C CD  . LYS B 445  ? 0.4705 0.5421 0.4190 -0.1391 0.0024  0.0719  443  LYS B CD  
12231 C CE  . LYS B 445  ? 0.4870 0.5591 0.4395 -0.1430 0.0001  0.0716  443  LYS B CE  
12232 N NZ  . LYS B 445  ? 0.5022 0.5854 0.4578 -0.1498 0.0013  0.0756  443  LYS B NZ  
12233 N N   . TYR B 446  ? 0.3198 0.3738 0.2620 -0.1148 0.0033  0.0604  444  TYR B N   
12234 C CA  . TYR B 446  ? 0.3078 0.3631 0.2534 -0.1081 0.0038  0.0560  444  TYR B CA  
12235 C C   . TYR B 446  ? 0.3118 0.3748 0.2571 -0.1038 0.0072  0.0554  444  TYR B C   
12236 O O   . TYR B 446  ? 0.3214 0.3901 0.2649 -0.1063 0.0093  0.0584  444  TYR B O   
12237 C CB  . TYR B 446  ? 0.3190 0.3814 0.2712 -0.1084 0.0040  0.0545  444  TYR B CB  
12238 C CG  . TYR B 446  ? 0.3584 0.4360 0.3151 -0.1104 0.0071  0.0564  444  TYR B CG  
12239 C CD1 . TYR B 446  ? 0.3207 0.4083 0.2807 -0.1053 0.0103  0.0546  444  TYR B CD1 
12240 C CD2 . TYR B 446  ? 0.3366 0.4185 0.2942 -0.1173 0.0068  0.0600  444  TYR B CD2 
12241 C CE1 . TYR B 446  ? 0.4006 0.5024 0.3649 -0.1068 0.0133  0.0564  444  TYR B CE1 
12242 C CE2 . TYR B 446  ? 0.4092 0.5056 0.3713 -0.1192 0.0097  0.0619  444  TYR B CE2 
12243 C CZ  . TYR B 446  ? 0.3888 0.4952 0.3543 -0.1137 0.0130  0.0601  444  TYR B CZ  
12244 O OH  . TYR B 446  ? 0.4840 0.6052 0.4541 -0.1153 0.0160  0.0620  444  TYR B OH  
12245 N N   . GLU B 447  ? 0.3038 0.3670 0.2510 -0.0975 0.0078  0.0516  445  GLU B N   
12246 C CA  . GLU B 447  ? 0.2909 0.3618 0.2383 -0.0931 0.0111  0.0506  445  GLU B CA  
12247 C C   . GLU B 447  ? 0.2622 0.3382 0.2150 -0.0880 0.0121  0.0469  445  GLU B C   
12248 O O   . GLU B 447  ? 0.2616 0.3339 0.2173 -0.0874 0.0101  0.0449  445  GLU B O   
12249 C CB  . GLU B 447  ? 0.2689 0.3317 0.2103 -0.0901 0.0105  0.0500  445  GLU B CB  
12250 C CG  . GLU B 447  ? 0.2780 0.3311 0.2192 -0.0857 0.0080  0.0464  445  GLU B CG  
12251 C CD  . GLU B 447  ? 0.2729 0.3176 0.2083 -0.0834 0.0070  0.0461  445  GLU B CD  
12252 O OE1 . GLU B 447  ? 0.3116 0.3565 0.2425 -0.0857 0.0078  0.0489  445  GLU B OE1 
12253 O OE2 . GLU B 447  ? 0.2835 0.3216 0.2189 -0.0792 0.0053  0.0431  445  GLU B OE2 
12254 N N   . PHE B 448  ? 0.2572 0.3419 0.2112 -0.0842 0.0153  0.0459  446  PHE B N   
12255 C CA  . PHE B 448  ? 0.2709 0.3587 0.2286 -0.0783 0.0163  0.0421  446  PHE B CA  
12256 C C   . PHE B 448  ? 0.2414 0.3216 0.1950 -0.0734 0.0157  0.0396  446  PHE B C   
12257 O O   . PHE B 448  ? 0.2649 0.3394 0.2130 -0.0744 0.0152  0.0410  446  PHE B O   
12258 C CB  . PHE B 448  ? 0.2971 0.3987 0.2585 -0.0768 0.0200  0.0424  446  PHE B CB  
12259 C CG  . PHE B 448  ? 0.2940 0.4042 0.2603 -0.0813 0.0205  0.0446  446  PHE B CG  
12260 C CD1 . PHE B 448  ? 0.3199 0.4324 0.2917 -0.0805 0.0195  0.0429  446  PHE B CD1 
12261 C CD2 . PHE B 448  ? 0.3241 0.4401 0.2894 -0.0865 0.0218  0.0486  446  PHE B CD2 
12262 C CE1 . PHE B 448  ? 0.3004 0.4210 0.2768 -0.0848 0.0197  0.0451  446  PHE B CE1 
12263 C CE2 . PHE B 448  ? 0.3501 0.4743 0.3201 -0.0909 0.0221  0.0508  446  PHE B CE2 
12264 C CZ  . PHE B 448  ? 0.3201 0.4467 0.2957 -0.0900 0.0209  0.0490  446  PHE B CZ  
12265 N N   . GLN B 449  ? 0.2634 0.3434 0.2197 -0.0682 0.0158  0.0360  447  GLN B N   
12266 C CA  . GLN B 449  ? 0.2543 0.3280 0.2074 -0.0634 0.0154  0.0334  447  GLN B CA  
12267 C C   . GLN B 449  ? 0.2618 0.3421 0.2183 -0.0581 0.0176  0.0304  447  GLN B C   
12268 O O   . GLN B 449  ? 0.2384 0.3251 0.2002 -0.0576 0.0184  0.0297  447  GLN B O   
12269 C CB  . GLN B 449  ? 0.2597 0.3217 0.2117 -0.0627 0.0118  0.0318  447  GLN B CB  
12270 C CG  . GLN B 449  ? 0.2706 0.3249 0.2191 -0.0675 0.0094  0.0345  447  GLN B CG  
12271 C CD  . GLN B 449  ? 0.2597 0.3023 0.2053 -0.0655 0.0064  0.0330  447  GLN B CD  
12272 O OE1 . GLN B 449  ? 0.2903 0.3309 0.2376 -0.0611 0.0060  0.0298  447  GLN B OE1 
12273 N NE2 . GLN B 449  ? 0.2723 0.3073 0.2137 -0.0688 0.0044  0.0353  447  GLN B NE2 
12274 N N   . CYS B 450  ? 0.2470 0.3257 0.2001 -0.0541 0.0186  0.0287  448  CYS B N   
12275 C CA  . CYS B 450  ? 0.2449 0.3280 0.2003 -0.0488 0.0205  0.0257  448  CYS B CA  
12276 C C   . CYS B 450  ? 0.2309 0.3061 0.1823 -0.0449 0.0193  0.0232  448  CYS B C   
12277 O O   . CYS B 450  ? 0.2690 0.3366 0.2159 -0.0464 0.0174  0.0241  448  CYS B O   
12278 C CB  . CYS B 450  ? 0.2685 0.3626 0.2243 -0.0480 0.0243  0.0266  448  CYS B CB  
12279 S SG  . CYS B 450  ? 0.2927 0.3860 0.2410 -0.0480 0.0259  0.0279  448  CYS B SG  
12280 N N   . LEU B 451  ? 0.2637 0.3409 0.2168 -0.0400 0.0205  0.0202  449  LEU B N   
12281 C CA  . LEU B 451  ? 0.2579 0.3284 0.2076 -0.0362 0.0195  0.0176  449  LEU B CA  
12282 C C   . LEU B 451  ? 0.2952 0.3693 0.2404 -0.0343 0.0220  0.0175  449  LEU B C   
12283 O O   . LEU B 451  ? 0.3051 0.3881 0.2518 -0.0335 0.0251  0.0178  449  LEU B O   
12284 C CB  . LEU B 451  ? 0.2866 0.3568 0.2403 -0.0319 0.0193  0.0143  449  LEU B CB  
12285 C CG  . LEU B 451  ? 0.3760 0.4389 0.3275 -0.0281 0.0178  0.0114  449  LEU B CG  
12286 C CD1 . LEU B 451  ? 0.3425 0.3960 0.2911 -0.0301 0.0146  0.0121  449  LEU B CD1 
12287 C CD2 . LEU B 451  ? 0.4140 0.4773 0.3703 -0.0249 0.0175  0.0087  449  LEU B CD2 
12288 N N   . HIS B 452  ? 0.2644 0.3316 0.2042 -0.0338 0.0207  0.0172  450  HIS B N   
12289 C CA  . HIS B 452  ? 0.3376 0.4070 0.2725 -0.0317 0.0228  0.0166  450  HIS B CA  
12290 C C   . HIS B 452  ? 0.3204 0.3942 0.2572 -0.0267 0.0249  0.0135  450  HIS B C   
12291 O O   . HIS B 452  ? 0.3442 0.4150 0.2841 -0.0240 0.0237  0.0110  450  HIS B O   
12292 C CB  . HIS B 452  ? 0.2861 0.3463 0.2155 -0.0310 0.0203  0.0160  450  HIS B CB  
12293 C CG  . HIS B 452  ? 0.3166 0.3777 0.2406 -0.0282 0.0220  0.0146  450  HIS B CG  
12294 N ND1 . HIS B 452  ? 0.3399 0.4045 0.2591 -0.0299 0.0239  0.0168  450  HIS B ND1 
12295 C CD2 . HIS B 452  ? 0.3576 0.4166 0.2801 -0.0238 0.0221  0.0113  450  HIS B CD2 
12296 C CE1 . HIS B 452  ? 0.3772 0.4417 0.2920 -0.0266 0.0251  0.0148  450  HIS B CE1 
12297 N NE2 . HIS B 452  ? 0.3718 0.4327 0.2884 -0.0229 0.0240  0.0114  450  HIS B NE2 
12298 N N   . GLY B 453  ? 0.3729 0.4539 0.3077 -0.0255 0.0282  0.0138  451  GLY B N   
12299 C CA  . GLY B 453  ? 0.4383 0.5230 0.3739 -0.0205 0.0305  0.0108  451  GLY B CA  
12300 C C   . GLY B 453  ? 0.5009 0.5912 0.4435 -0.0190 0.0314  0.0099  451  GLY B C   
12301 O O   . GLY B 453  ? 0.5605 0.6520 0.5042 -0.0145 0.0325  0.0071  451  GLY B O   
12302 N N   . MET B 454  ? 0.3595 0.4527 0.3066 -0.0226 0.0307  0.0122  452  MET B N   
12303 C CA  . MET B 454  ? 0.3499 0.4494 0.3037 -0.0217 0.0316  0.0118  452  MET B CA  
12304 C C   . MET B 454  ? 0.3872 0.4950 0.3437 -0.0260 0.0330  0.0153  452  MET B C   
12305 O O   . MET B 454  ? 0.3816 0.4990 0.3418 -0.0250 0.0356  0.0157  452  MET B O   
12306 C CB  . MET B 454  ? 0.3709 0.4639 0.3282 -0.0218 0.0284  0.0105  452  MET B CB  
12307 C CG  . MET B 454  ? 0.3833 0.4824 0.3474 -0.0217 0.0289  0.0106  452  MET B CG  
12308 S SD  . MET B 454  ? 0.5438 0.6512 0.5103 -0.0161 0.0323  0.0085  452  MET B SD  
12309 C CE  . MET B 454  ? 0.4820 0.5796 0.4455 -0.0113 0.0307  0.0045  452  MET B CE  
12310 N N   . GLY B 455  ? 0.2965 0.4006 0.2511 -0.0310 0.0312  0.0180  453  GLY B N   
12311 C CA  . GLY B 455  ? 0.3077 0.4182 0.2649 -0.0358 0.0319  0.0214  453  GLY B CA  
12312 C C   . GLY B 455  ? 0.3741 0.4917 0.3284 -0.0378 0.0348  0.0240  453  GLY B C   
12313 O O   . GLY B 455  ? 0.3484 0.4735 0.3058 -0.0415 0.0359  0.0269  453  GLY B O   
12314 N N   . GLU B 456  ? 0.3930 0.5087 0.3415 -0.0356 0.0360  0.0233  454  GLU B N   
12315 C CA  . GLU B 456  ? 0.4119 0.5340 0.3571 -0.0376 0.0388  0.0259  454  GLU B CA  
12316 C C   . GLU B 456  ? 0.3991 0.5346 0.3486 -0.0366 0.0426  0.0267  454  GLU B C   
12317 O O   . GLU B 456  ? 0.4226 0.5648 0.3725 -0.0408 0.0441  0.0302  454  GLU B O   
12318 C CB  . GLU B 456  ? 0.4456 0.5630 0.3833 -0.0352 0.0394  0.0247  454  GLU B CB  
12319 C CG  . GLU B 456  ? 0.4949 0.6007 0.4279 -0.0374 0.0358  0.0251  454  GLU B CG  
12320 C CD  . GLU B 456  ? 0.4811 0.5782 0.4144 -0.0338 0.0331  0.0216  454  GLU B CD  
12321 O OE1 . GLU B 456  ? 0.4656 0.5643 0.4045 -0.0317 0.0329  0.0197  454  GLU B OE1 
12322 O OE2 . GLU B 456  ? 0.4492 0.5379 0.3772 -0.0331 0.0312  0.0207  454  GLU B OE2 
12323 N N   . PRO B 457  ? 0.3918 0.5315 0.3446 -0.0315 0.0442  0.0239  455  PRO B N   
12324 C CA  . PRO B 457  ? 0.4016 0.5545 0.3587 -0.0305 0.0479  0.0249  455  PRO B CA  
12325 C C   . PRO B 457  ? 0.3941 0.5535 0.3572 -0.0355 0.0474  0.0281  455  PRO B C   
12326 O O   . PRO B 457  ? 0.3883 0.5584 0.3532 -0.0376 0.0501  0.0308  455  PRO B O   
12327 C CB  . PRO B 457  ? 0.4038 0.5573 0.3637 -0.0241 0.0486  0.0211  455  PRO B CB  
12328 C CG  . PRO B 457  ? 0.4625 0.6046 0.4168 -0.0213 0.0467  0.0181  455  PRO B CG  
12329 C CD  . PRO B 457  ? 0.4305 0.5635 0.3824 -0.0261 0.0432  0.0197  455  PRO B CD  
12330 N N   . LEU B 458  ? 0.3815 0.5351 0.3478 -0.0376 0.0440  0.0279  456  LEU B N   
12331 C CA  . LEU B 458  ? 0.3462 0.5050 0.3175 -0.0428 0.0431  0.0309  456  LEU B CA  
12332 C C   . LEU B 458  ? 0.3342 0.4914 0.3020 -0.0490 0.0425  0.0346  456  LEU B C   
12333 O O   . LEU B 458  ? 0.3360 0.5024 0.3061 -0.0529 0.0441  0.0379  456  LEU B O   
12334 C CB  . LEU B 458  ? 0.3328 0.4849 0.3077 -0.0432 0.0395  0.0294  456  LEU B CB  
12335 C CG  . LEU B 458  ? 0.3106 0.4661 0.2900 -0.0490 0.0380  0.0323  456  LEU B CG  
12336 C CD1 . LEU B 458  ? 0.3279 0.4980 0.3129 -0.0492 0.0409  0.0340  456  LEU B CD1 
12337 C CD2 . LEU B 458  ? 0.3332 0.4816 0.3155 -0.0487 0.0346  0.0304  456  LEU B CD2 
12338 N N   . TYR B 459  ? 0.3274 0.4732 0.2893 -0.0501 0.0401  0.0343  457  TYR B N   
12339 C CA  . TYR B 459  ? 0.3136 0.4563 0.2723 -0.0562 0.0388  0.0379  457  TYR B CA  
12340 C C   . TYR B 459  ? 0.3231 0.4710 0.2772 -0.0573 0.0418  0.0402  457  TYR B C   
12341 O O   . TYR B 459  ? 0.2977 0.4456 0.2498 -0.0628 0.0414  0.0438  457  TYR B O   
12342 C CB  . TYR B 459  ? 0.3257 0.4542 0.2806 -0.0572 0.0348  0.0370  457  TYR B CB  
12343 C CG  . TYR B 459  ? 0.2994 0.4245 0.2592 -0.0588 0.0319  0.0365  457  TYR B CG  
12344 C CD1 . TYR B 459  ? 0.2799 0.4062 0.2418 -0.0648 0.0305  0.0396  457  TYR B CD1 
12345 C CD2 . TYR B 459  ? 0.2972 0.4182 0.2594 -0.0543 0.0306  0.0328  457  TYR B CD2 
12346 C CE1 . TYR B 459  ? 0.2932 0.4163 0.2592 -0.0663 0.0279  0.0389  457  TYR B CE1 
12347 C CE2 . TYR B 459  ? 0.3474 0.4654 0.3139 -0.0558 0.0280  0.0323  457  TYR B CE2 
12348 C CZ  . TYR B 459  ? 0.2814 0.4006 0.2496 -0.0617 0.0267  0.0353  457  TYR B CZ  
12349 O OH  . TYR B 459  ? 0.2730 0.3890 0.2449 -0.0632 0.0241  0.0347  457  TYR B OH  
12350 N N   . GLU B 460  ? 0.3248 0.4771 0.2769 -0.0522 0.0449  0.0382  458  GLU B N   
12351 C CA  . GLU B 460  ? 0.3834 0.5431 0.3321 -0.0534 0.0483  0.0406  458  GLU B CA  
12352 C C   . GLU B 460  ? 0.4477 0.6210 0.4021 -0.0563 0.0509  0.0436  458  GLU B C   
12353 O O   . GLU B 460  ? 0.3846 0.5647 0.3370 -0.0591 0.0534  0.0466  458  GLU B O   
12354 C CB  . GLU B 460  ? 0.3952 0.5557 0.3397 -0.0472 0.0510  0.0377  458  GLU B CB  
12355 C CG  . GLU B 460  ? 0.4640 0.6315 0.4133 -0.0414 0.0532  0.0347  458  GLU B CG  
12356 C CD  . GLU B 460  ? 0.6003 0.7663 0.5446 -0.0353 0.0553  0.0314  458  GLU B CD  
12357 O OE1 . GLU B 460  ? 0.5855 0.7447 0.5226 -0.0356 0.0547  0.0313  458  GLU B OE1 
12358 O OE2 . GLU B 460  ? 0.5557 0.7271 0.5031 -0.0301 0.0574  0.0288  458  GLU B OE2 
12359 N N   . GLU B 461  ? 0.3804 0.5580 0.3421 -0.0560 0.0502  0.0429  459  GLU B N   
12360 C CA  . GLU B 461  ? 0.3930 0.5829 0.3609 -0.0596 0.0518  0.0459  459  GLU B CA  
12361 C C   . GLU B 461  ? 0.4095 0.5960 0.3789 -0.0669 0.0487  0.0491  459  GLU B C   
12362 O O   . GLU B 461  ? 0.3697 0.5654 0.3447 -0.0705 0.0492  0.0516  459  GLU B O   
12363 C CB  . GLU B 461  ? 0.3568 0.5538 0.3319 -0.0552 0.0527  0.0436  459  GLU B CB  
12364 C CG  . GLU B 461  ? 0.3584 0.5571 0.3322 -0.0475 0.0553  0.0399  459  GLU B CG  
12365 C CD  . GLU B 461  ? 0.5090 0.7174 0.4803 -0.0461 0.0599  0.0412  459  GLU B CD  
12366 O OE1 . GLU B 461  ? 0.4823 0.6988 0.4547 -0.0510 0.0613  0.0452  459  GLU B OE1 
12367 O OE2 . GLU B 461  ? 0.5177 0.7256 0.4858 -0.0401 0.0620  0.0383  459  GLU B OE2 
12368 N N   . VAL B 462  ? 0.3703 0.5436 0.3348 -0.0692 0.0452  0.0491  460  VAL B N   
12369 C CA  . VAL B 462  ? 0.3212 0.4887 0.2864 -0.0755 0.0418  0.0515  460  VAL B CA  
12370 C C   . VAL B 462  ? 0.3683 0.5294 0.3267 -0.0802 0.0409  0.0545  460  VAL B C   
12371 O O   . VAL B 462  ? 0.3630 0.5269 0.3219 -0.0865 0.0406  0.0584  460  VAL B O   
12372 C CB  . VAL B 462  ? 0.3585 0.5154 0.3251 -0.0739 0.0379  0.0485  460  VAL B CB  
12373 C CG1 . VAL B 462  ? 0.3237 0.4731 0.2898 -0.0802 0.0342  0.0508  460  VAL B CG1 
12374 C CG2 . VAL B 462  ? 0.3140 0.4777 0.2876 -0.0702 0.0386  0.0461  460  VAL B CG2 
12375 N N   . VAL B 463  ? 0.3057 0.4578 0.2577 -0.0772 0.0403  0.0528  461  VAL B N   
12376 C CA  . VAL B 463  ? 0.3175 0.4625 0.2627 -0.0811 0.0392  0.0555  461  VAL B CA  
12377 C C   . VAL B 463  ? 0.3394 0.4942 0.2824 -0.0831 0.0430  0.0587  461  VAL B C   
12378 O O   . VAL B 463  ? 0.4022 0.5658 0.3458 -0.0789 0.0466  0.0574  461  VAL B O   
12379 C CB  . VAL B 463  ? 0.3446 0.4778 0.2839 -0.0769 0.0374  0.0526  461  VAL B CB  
12380 C CG1 . VAL B 463  ? 0.3600 0.4854 0.2919 -0.0807 0.0360  0.0555  461  VAL B CG1 
12381 C CG2 . VAL B 463  ? 0.3164 0.4407 0.2584 -0.0748 0.0339  0.0495  461  VAL B CG2 
12382 N N   . GLY B 464  ? 0.3624 0.5157 0.3026 -0.0895 0.0422  0.0629  462  GLY B N   
12383 C CA  . GLY B 464  ? 0.4015 0.5630 0.3385 -0.0917 0.0456  0.0662  462  GLY B CA  
12384 C C   . GLY B 464  ? 0.4386 0.6110 0.3805 -0.0977 0.0470  0.0703  462  GLY B C   
12385 O O   . GLY B 464  ? 0.4183 0.5967 0.3674 -0.0981 0.0468  0.0698  462  GLY B O   
12386 N N   . ARG B 465  ? 0.4743 0.6494 0.4121 -0.1026 0.0484  0.0746  463  ARG B N   
12387 C CA  . ARG B 465  ? 0.5199 0.7054 0.4619 -0.1090 0.0497  0.0790  463  ARG B CA  
12388 C C   . ARG B 465  ? 0.5561 0.7580 0.5052 -0.1063 0.0538  0.0784  463  ARG B C   
12389 O O   . ARG B 465  ? 0.5448 0.7553 0.5003 -0.1104 0.0539  0.0807  463  ARG B O   
12390 C CB  . ARG B 465  ? 0.5728 0.7586 0.5086 -0.1141 0.0510  0.0836  463  ARG B CB  
12391 N N   . GLY B 466  ? 0.4947 0.7010 0.4427 -0.0993 0.0569  0.0754  464  GLY B N   
12392 C CA  . GLY B 466  ? 0.5076 0.7288 0.4619 -0.0957 0.0608  0.0744  464  GLY B CA  
12393 C C   . GLY B 466  ? 0.5239 0.7457 0.4849 -0.0913 0.0595  0.0706  464  GLY B C   
12394 O O   . GLY B 466  ? 0.4909 0.7246 0.4572 -0.0875 0.0626  0.0695  464  GLY B O   
12395 N N   . LYS B 467  ? 0.4756 0.6847 0.4363 -0.0916 0.0550  0.0686  465  LYS B N   
12396 C CA  . LYS B 467  ? 0.4336 0.6421 0.4002 -0.0877 0.0535  0.0650  465  LYS B CA  
12397 C C   . LYS B 467  ? 0.4439 0.6495 0.4145 -0.0938 0.0498  0.0669  465  LYS B C   
12398 O O   . LYS B 467  ? 0.4176 0.6320 0.3916 -0.0993 0.0506  0.0707  465  LYS B O   
12399 C CB  . LYS B 467  ? 0.4135 0.6107 0.3761 -0.0813 0.0520  0.0603  465  LYS B CB  
12400 C CG  . LYS B 467  ? 0.4443 0.6450 0.4031 -0.0752 0.0557  0.0582  465  LYS B CG  
12401 C CD  . LYS B 467  ? 0.4719 0.6854 0.4368 -0.0703 0.0591  0.0565  465  LYS B CD  
12402 C CE  . LYS B 467  ? 0.4680 0.6848 0.4286 -0.0643 0.0629  0.0544  465  LYS B CE  
12403 N NZ  . LYS B 467  ? 0.5028 0.7292 0.4690 -0.0582 0.0656  0.0518  465  LYS B NZ  
12404 N N   . LEU B 468  ? 0.3854 0.5788 0.3556 -0.0930 0.0458  0.0644  466  LEU B N   
12405 C CA  . LEU B 468  ? 0.3572 0.5461 0.3300 -0.0988 0.0421  0.0660  466  LEU B CA  
12406 C C   . LEU B 468  ? 0.3553 0.5322 0.3217 -0.1041 0.0392  0.0683  466  LEU B C   
12407 O O   . LEU B 468  ? 0.3369 0.5092 0.3045 -0.1095 0.0361  0.0700  466  LEU B O   
12408 C CB  . LEU B 468  ? 0.3867 0.5699 0.3631 -0.0952 0.0394  0.0620  466  LEU B CB  
12409 C CG  . LEU B 468  ? 0.4031 0.5972 0.3859 -0.0896 0.0419  0.0596  466  LEU B CG  
12410 C CD1 . LEU B 468  ? 0.4131 0.6008 0.3990 -0.0865 0.0390  0.0560  466  LEU B CD1 
12411 C CD2 . LEU B 468  ? 0.4189 0.6286 0.4080 -0.0933 0.0441  0.0629  466  LEU B CD2 
12412 N N   . ASP B 469  ? 0.3480 0.5197 0.3074 -0.1027 0.0402  0.0685  467  ASP B N   
12413 C CA  . ASP B 469  ? 0.4286 0.5886 0.3814 -0.1071 0.0375  0.0708  467  ASP B CA  
12414 C C   . ASP B 469  ? 0.3495 0.4956 0.3017 -0.1074 0.0328  0.0688  467  ASP B C   
12415 O O   . ASP B 469  ? 0.3924 0.5315 0.3429 -0.1131 0.0299  0.0712  467  ASP B O   
12416 C CB  . ASP B 469  ? 0.4326 0.5980 0.3850 -0.1150 0.0381  0.0762  467  ASP B CB  
12417 C CG  . ASP B 469  ? 0.5152 0.6714 0.4594 -0.1182 0.0371  0.0789  467  ASP B CG  
12418 O OD1 . ASP B 469  ? 0.4990 0.6474 0.4378 -0.1137 0.0369  0.0766  467  ASP B OD1 
12419 O OD2 . ASP B 469  ? 0.5945 0.7512 0.5375 -0.1253 0.0365  0.0833  467  ASP B OD2 
12420 N N   . ARG B 470  ? 0.3674 0.5096 0.3209 -0.1011 0.0321  0.0643  468  ARG B N   
12421 C CA  . ARG B 470  ? 0.3468 0.4761 0.2996 -0.1003 0.0280  0.0620  468  ARG B CA  
12422 C C   . ARG B 470  ? 0.3553 0.4755 0.3031 -0.0946 0.0275  0.0589  468  ARG B C   
12423 O O   . ARG B 470  ? 0.3568 0.4821 0.3050 -0.0892 0.0300  0.0565  468  ARG B O   
12424 C CB  . ARG B 470  ? 0.3302 0.4629 0.2900 -0.0984 0.0272  0.0594  468  ARG B CB  
12425 C CG  . ARG B 470  ? 0.3343 0.4747 0.2993 -0.1043 0.0269  0.0622  468  ARG B CG  
12426 C CD  . ARG B 470  ? 0.3161 0.4476 0.2778 -0.1113 0.0237  0.0653  468  ARG B CD  
12427 N NE  . ARG B 470  ? 0.3734 0.5124 0.3397 -0.1174 0.0234  0.0681  468  ARG B NE  
12428 C CZ  . ARG B 470  ? 0.4301 0.5783 0.3969 -0.1223 0.0254  0.0723  468  ARG B CZ  
12429 N NH1 . ARG B 470  ? 0.3891 0.5404 0.3519 -0.1218 0.0282  0.0740  468  ARG B NH1 
12430 N NH2 . ARG B 470  ? 0.4100 0.5645 0.3812 -0.1280 0.0247  0.0747  468  ARG B NH2 
12431 N N   . PRO B 471  ? 0.3281 0.4351 0.2715 -0.0957 0.0240  0.0587  469  PRO B N   
12432 C CA  . PRO B 471  ? 0.3303 0.4288 0.2690 -0.0907 0.0233  0.0561  469  PRO B CA  
12433 C C   . PRO B 471  ? 0.3175 0.4135 0.2598 -0.0850 0.0223  0.0515  469  PRO B C   
12434 O O   . PRO B 471  ? 0.2802 0.3771 0.2276 -0.0855 0.0211  0.0504  469  PRO B O   
12435 C CB  . PRO B 471  ? 0.3100 0.3956 0.2435 -0.0943 0.0197  0.0579  469  PRO B CB  
12436 C CG  . PRO B 471  ? 0.3789 0.4634 0.3160 -0.0991 0.0176  0.0593  469  PRO B CG  
12437 C CD  . PRO B 471  ? 0.3268 0.4256 0.2694 -0.1013 0.0206  0.0608  469  PRO B CD  
12438 N N   . CYS B 472  ? 0.2983 0.3913 0.2377 -0.0797 0.0229  0.0488  470  CYS B N   
12439 C CA  . CYS B 472  ? 0.2697 0.3592 0.2116 -0.0742 0.0219  0.0445  470  CYS B CA  
12440 C C   . CYS B 472  ? 0.2964 0.3750 0.2328 -0.0714 0.0199  0.0429  470  CYS B C   
12441 O O   . CYS B 472  ? 0.3088 0.3873 0.2401 -0.0706 0.0211  0.0437  470  CYS B O   
12442 C CB  . CYS B 472  ? 0.2930 0.3927 0.2384 -0.0696 0.0253  0.0423  470  CYS B CB  
12443 S SG  . CYS B 472  ? 0.3255 0.4211 0.2742 -0.0632 0.0240  0.0372  470  CYS B SG  
12444 N N   . ARG B 473  ? 0.2999 0.3697 0.2373 -0.0701 0.0168  0.0409  471  ARG B N   
12445 C CA  . ARG B 473  ? 0.2991 0.3591 0.2323 -0.0669 0.0148  0.0390  471  ARG B CA  
12446 C C   . ARG B 473  ? 0.2921 0.3539 0.2277 -0.0609 0.0157  0.0349  471  ARG B C   
12447 O O   . ARG B 473  ? 0.2830 0.3468 0.2238 -0.0593 0.0155  0.0329  471  ARG B O   
12448 C CB  . ARG B 473  ? 0.2668 0.3161 0.1996 -0.0687 0.0109  0.0392  471  ARG B CB  
12449 C CG  . ARG B 473  ? 0.2693 0.3086 0.1976 -0.0658 0.0086  0.0378  471  ARG B CG  
12450 C CD  . ARG B 473  ? 0.2716 0.3005 0.1990 -0.0679 0.0050  0.0385  471  ARG B CD  
12451 N NE  . ARG B 473  ? 0.3053 0.3334 0.2310 -0.0738 0.0045  0.0423  471  ARG B NE  
12452 C CZ  . ARG B 473  ? 0.3520 0.3766 0.2722 -0.0765 0.0040  0.0454  471  ARG B CZ  
12453 N NH1 . ARG B 473  ? 0.3210 0.3421 0.2366 -0.0740 0.0037  0.0451  471  ARG B NH1 
12454 N NH2 . ARG B 473  ? 0.3141 0.3387 0.2332 -0.0822 0.0037  0.0489  471  ARG B NH2 
12455 N N   . ILE B 474  ? 0.2901 0.3506 0.2216 -0.0576 0.0164  0.0337  472  ILE B N   
12456 C CA  . ILE B 474  ? 0.2620 0.3235 0.1948 -0.0520 0.0173  0.0299  472  ILE B CA  
12457 C C   . ILE B 474  ? 0.2604 0.3115 0.1923 -0.0498 0.0140  0.0277  472  ILE B C   
12458 O O   . ILE B 474  ? 0.2789 0.3229 0.2060 -0.0504 0.0121  0.0287  472  ILE B O   
12459 C CB  . ILE B 474  ? 0.2917 0.3572 0.2202 -0.0497 0.0199  0.0295  472  ILE B CB  
12460 C CG1 . ILE B 474  ? 0.2912 0.3679 0.2211 -0.0515 0.0235  0.0316  472  ILE B CG1 
12461 C CG2 . ILE B 474  ? 0.3106 0.3755 0.2397 -0.0440 0.0203  0.0255  472  ILE B CG2 
12462 C CD1 . ILE B 474  ? 0.3284 0.4088 0.2531 -0.0499 0.0261  0.0318  472  ILE B CD1 
12463 N N   . TYR B 475  ? 0.2382 0.2888 0.1749 -0.0471 0.0133  0.0250  473  TYR B N   
12464 C CA  . TYR B 475  ? 0.2465 0.2888 0.1832 -0.0443 0.0106  0.0226  473  TYR B CA  
12465 C C   . TYR B 475  ? 0.2776 0.3198 0.2115 -0.0400 0.0115  0.0202  473  TYR B C   
12466 O O   . TYR B 475  ? 0.2768 0.3249 0.2126 -0.0371 0.0138  0.0183  473  TYR B O   
12467 C CB  . TYR B 475  ? 0.2548 0.2977 0.1975 -0.0430 0.0100  0.0206  473  TYR B CB  
12468 C CG  . TYR B 475  ? 0.2532 0.2876 0.1964 -0.0408 0.0071  0.0185  473  TYR B CG  
12469 C CD1 . TYR B 475  ? 0.2686 0.3016 0.2120 -0.0364 0.0071  0.0155  473  TYR B CD1 
12470 C CD2 . TYR B 475  ? 0.2423 0.2701 0.1857 -0.0433 0.0045  0.0196  473  TYR B CD2 
12471 C CE1 . TYR B 475  ? 0.2628 0.2887 0.2071 -0.0345 0.0045  0.0138  473  TYR B CE1 
12472 C CE2 . TYR B 475  ? 0.2511 0.2718 0.1954 -0.0411 0.0021  0.0177  473  TYR B CE2 
12473 C CZ  . TYR B 475  ? 0.2927 0.3127 0.2374 -0.0368 0.0021  0.0149  473  TYR B CZ  
12474 O OH  . TYR B 475  ? 0.3130 0.3265 0.2588 -0.0348 -0.0002 0.0132  473  TYR B OH  
12475 N N   . ALA B 476  ? 0.2641 0.2994 0.1931 -0.0397 0.0096  0.0204  474  ALA B N   
12476 C CA  . ALA B 476  ? 0.2985 0.3337 0.2233 -0.0366 0.0104  0.0189  474  ALA B CA  
12477 C C   . ALA B 476  ? 0.2942 0.3222 0.2189 -0.0335 0.0078  0.0163  474  ALA B C   
12478 O O   . ALA B 476  ? 0.2843 0.3053 0.2064 -0.0345 0.0051  0.0172  474  ALA B O   
12479 C CB  . ALA B 476  ? 0.3083 0.3423 0.2268 -0.0392 0.0105  0.0217  474  ALA B CB  
12480 N N   . PRO B 477  ? 0.2946 0.3241 0.2222 -0.0298 0.0085  0.0131  475  PRO B N   
12481 C CA  . PRO B 477  ? 0.2753 0.2986 0.2026 -0.0269 0.0061  0.0107  475  PRO B CA  
12482 C C   . PRO B 477  ? 0.2618 0.2822 0.1828 -0.0261 0.0055  0.0107  475  PRO B C   
12483 O O   . PRO B 477  ? 0.2997 0.3243 0.2171 -0.0258 0.0078  0.0109  475  PRO B O   
12484 C CB  . PRO B 477  ? 0.3021 0.3291 0.2332 -0.0234 0.0077  0.0076  475  PRO B CB  
12485 C CG  . PRO B 477  ? 0.3119 0.3459 0.2470 -0.0248 0.0099  0.0086  475  PRO B CG  
12486 C CD  . PRO B 477  ? 0.2936 0.3307 0.2253 -0.0281 0.0112  0.0117  475  PRO B CD  
12487 N N   . VAL B 478  ? 0.2614 0.2747 0.1809 -0.0255 0.0025  0.0103  476  VAL B N   
12488 C CA  . VAL B 478  ? 0.2807 0.2906 0.1943 -0.0248 0.0013  0.0103  476  VAL B CA  
12489 C C   . VAL B 478  ? 0.3479 0.3530 0.2627 -0.0220 -0.0011 0.0077  476  VAL B C   
12490 O O   . VAL B 478  ? 0.3363 0.3373 0.2543 -0.0222 -0.0034 0.0077  476  VAL B O   
12491 C CB  . VAL B 478  ? 0.3093 0.3152 0.2191 -0.0280 -0.0005 0.0136  476  VAL B CB  
12492 C CG1 . VAL B 478  ? 0.3447 0.3473 0.2480 -0.0272 -0.0017 0.0136  476  VAL B CG1 
12493 C CG2 . VAL B 478  ? 0.2881 0.2986 0.1971 -0.0314 0.0017  0.0165  476  VAL B CG2 
12494 N N   . GLY B 479  ? 0.3875 0.3929 0.2995 -0.0195 -0.0006 0.0054  477  GLY B N   
12495 C CA  . GLY B 479  ? 0.4371 0.4382 0.3500 -0.0170 -0.0029 0.0030  477  GLY B CA  
12496 C C   . GLY B 479  ? 0.4346 0.4375 0.3457 -0.0142 -0.0015 0.0000  477  GLY B C   
12497 O O   . GLY B 479  ? 0.4072 0.4150 0.3165 -0.0136 0.0015  -0.0003 477  GLY B O   
12498 N N   . THR B 480  ? 0.5078 0.5068 0.4197 -0.0122 -0.0036 -0.0021 478  THR B N   
12499 C CA  . THR B 480  ? 0.5722 0.5709 0.4814 -0.0096 -0.0032 -0.0050 478  THR B CA  
12500 C C   . THR B 480  ? 0.6305 0.6328 0.5438 -0.0074 -0.0008 -0.0072 478  THR B C   
12501 O O   . THR B 480  ? 0.6513 0.6565 0.5697 -0.0080 0.0003  -0.0065 478  THR B O   
12502 C CB  . THR B 480  ? 0.5341 0.5272 0.4430 -0.0087 -0.0067 -0.0063 478  THR B CB  
12503 O OG1 . THR B 480  ? 0.6645 0.6563 0.5799 -0.0084 -0.0079 -0.0067 478  THR B OG1 
12504 C CG2 . THR B 480  ? 0.5498 0.5394 0.4547 -0.0107 -0.0092 -0.0040 478  THR B CG2 
12505 N N   . HIS B 481  ? 0.6942 0.6961 0.6051 -0.0049 -0.0002 -0.0100 479  HIS B N   
12506 C CA  . HIS B 481  ? 0.6678 0.6724 0.5820 -0.0025 0.0019  -0.0122 479  HIS B CA  
12507 C C   . HIS B 481  ? 0.7282 0.7308 0.6488 -0.0020 0.0002  -0.0130 479  HIS B C   
12508 O O   . HIS B 481  ? 0.7185 0.7244 0.6440 -0.0016 0.0018  -0.0130 479  HIS B O   
12509 C CB  . HIS B 481  ? 0.6768 0.6801 0.5862 0.0001  0.0025  -0.0150 479  HIS B CB  
12510 N N   . GLU B 482  ? 0.7338 0.7312 0.6544 -0.0021 -0.0029 -0.0136 480  GLU B N   
12511 C CA  . GLU B 482  ? 0.7015 0.6970 0.6278 -0.0015 -0.0044 -0.0144 480  GLU B CA  
12512 C C   . GLU B 482  ? 0.6771 0.6742 0.6083 -0.0033 -0.0044 -0.0122 480  GLU B C   
12513 O O   . GLU B 482  ? 0.6849 0.6831 0.6214 -0.0026 -0.0040 -0.0128 480  GLU B O   
12514 C CB  . GLU B 482  ? 0.7074 0.6976 0.6327 -0.0015 -0.0079 -0.0151 480  GLU B CB  
12515 N N   . THR B 483  ? 0.7090 0.7060 0.6384 -0.0056 -0.0049 -0.0097 481  THR B N   
12516 C CA  . THR B 483  ? 0.7109 0.7088 0.6443 -0.0074 -0.0050 -0.0077 481  THR B CA  
12517 C C   . THR B 483  ? 0.6548 0.6583 0.5903 -0.0077 -0.0020 -0.0072 481  THR B C   
12518 O O   . THR B 483  ? 0.7355 0.7403 0.6759 -0.0082 -0.0017 -0.0068 481  THR B O   
12519 C CB  . THR B 483  ? 0.6835 0.6789 0.6138 -0.0099 -0.0066 -0.0050 481  THR B CB  
12520 N N   . LEU B 484  ? 0.6919 0.6991 0.6240 -0.0074 0.0004  -0.0073 482  LEU B N   
12521 C CA  . LEU B 484  ? 0.6835 0.6969 0.6177 -0.0077 0.0033  -0.0066 482  LEU B CA  
12522 C C   . LEU B 484  ? 0.6504 0.6658 0.5895 -0.0054 0.0043  -0.0086 482  LEU B C   
12523 O O   . LEU B 484  ? 0.6799 0.6988 0.6233 -0.0062 0.0054  -0.0078 482  LEU B O   
12524 C CB  . LEU B 484  ? 0.6320 0.6492 0.5613 -0.0073 0.0058  -0.0064 482  LEU B CB  
12525 N N   . LEU B 485  ? 0.6310 0.6440 0.5694 -0.0028 0.0039  -0.0112 483  LEU B N   
12526 C CA  . LEU B 485  ? 0.7213 0.7360 0.6636 -0.0004 0.0049  -0.0131 483  LEU B CA  
12527 C C   . LEU B 485  ? 0.6608 0.6746 0.6089 -0.0010 0.0037  -0.0127 483  LEU B C   
12528 O O   . LEU B 485  ? 0.6177 0.6344 0.5697 0.0003  0.0049  -0.0135 483  LEU B O   
12529 C CB  . LEU B 485  ? 0.6874 0.6983 0.6273 0.0022  0.0042  -0.0158 483  LEU B CB  
12530 C CG  . LEU B 485  ? 0.5891 0.6011 0.5232 0.0037  0.0058  -0.0169 483  LEU B CG  
12531 C CD1 . LEU B 485  ? 0.5929 0.5992 0.5232 0.0050  0.0038  -0.0190 483  LEU B CD1 
12532 C CD2 . LEU B 485  ? 0.5814 0.5985 0.5168 0.0061  0.0090  -0.0179 483  LEU B CD2 
12533 N N   . ALA B 486  ? 0.6829 0.6930 0.6316 -0.0030 0.0013  -0.0115 484  ALA B N   
12534 C CA  . ALA B 486  ? 0.6300 0.6380 0.5835 -0.0032 -0.0002 -0.0115 484  ALA B CA  
12535 C C   . ALA B 486  ? 0.6637 0.6757 0.6212 -0.0045 0.0010  -0.0102 484  ALA B C   
12536 O O   . ALA B 486  ? 0.7096 0.7201 0.6710 -0.0046 0.0000  -0.0104 484  ALA B O   
12537 C CB  . ALA B 486  ? 0.6103 0.6132 0.5629 -0.0046 -0.0030 -0.0106 484  ALA B CB  
12538 N N   . TYR B 487  ? 0.6842 0.7011 0.6409 -0.0056 0.0031  -0.0090 485  TYR B N   
12539 C CA  . TYR B 487  ? 0.6158 0.6367 0.5764 -0.0070 0.0041  -0.0078 485  TYR B CA  
12540 C C   . TYR B 487  ? 0.6171 0.6447 0.5770 -0.0073 0.0069  -0.0070 485  TYR B C   
12541 O O   . TYR B 487  ? 0.5247 0.5559 0.4866 -0.0095 0.0076  -0.0052 485  TYR B O   
12542 C CB  . TYR B 487  ? 0.5842 0.6022 0.5450 -0.0101 0.0024  -0.0057 485  TYR B CB  
12543 N N   . LEU B 488  ? 0.6874 0.7167 0.6448 -0.0049 0.0085  -0.0083 486  LEU B N   
12544 C CA  . LEU B 488  ? 0.6877 0.7236 0.6439 -0.0047 0.0113  -0.0077 486  LEU B CA  
12545 C C   . LEU B 488  ? 0.6426 0.6847 0.6036 -0.0041 0.0131  -0.0076 486  LEU B C   
12546 O O   . LEU B 488  ? 0.6857 0.7343 0.6467 -0.0042 0.0155  -0.0066 486  LEU B O   
12547 C CB  . LEU B 488  ? 0.6492 0.6845 0.6012 -0.0018 0.0124  -0.0096 486  LEU B CB  
12548 C CG  . LEU B 488  ? 0.6091 0.6503 0.5583 -0.0011 0.0153  -0.0092 486  LEU B CG  
12549 C CD1 . LEU B 488  ? 0.5696 0.6069 0.5126 0.0000  0.0150  -0.0103 486  LEU B CD1 
12550 C CD2 . LEU B 488  ? 0.5795 0.6260 0.5316 0.0020  0.0177  -0.0106 486  LEU B CD2 
12551 N N   . VAL B 489  ? 0.7269 0.7676 0.6922 -0.0034 0.0120  -0.0084 487  VAL B N   
12552 C CA  . VAL B 489  ? 0.6261 0.6728 0.5961 -0.0030 0.0134  -0.0081 487  VAL B CA  
12553 C C   . VAL B 489  ? 0.7040 0.7554 0.6752 -0.0066 0.0140  -0.0054 487  VAL B C   
12554 O O   . VAL B 489  ? 0.6944 0.7526 0.6687 -0.0065 0.0157  -0.0048 487  VAL B O   
12555 C CB  . VAL B 489  ? 0.6219 0.6654 0.5956 -0.0020 0.0118  -0.0093 487  VAL B CB  
12556 N N   . ARG B 490  ? 0.4857 0.5339 0.4546 -0.0098 0.0126  -0.0037 488  ARG B N   
12557 C CA  . ARG B 490  ? 0.5664 0.6181 0.5365 -0.0136 0.0128  -0.0011 488  ARG B CA  
12558 C C   . ARG B 490  ? 0.5430 0.6022 0.5120 -0.0143 0.0155  0.0003  488  ARG B C   
12559 O O   . ARG B 490  ? 0.5547 0.6203 0.5268 -0.0160 0.0166  0.0018  488  ARG B O   
12560 C CB  . ARG B 490  ? 0.5342 0.5795 0.5018 -0.0167 0.0105  0.0003  488  ARG B CB  
12561 C CG  . ARG B 490  ? 0.4504 0.4896 0.4201 -0.0163 0.0080  -0.0008 488  ARG B CG  
12562 C CD  . ARG B 490  ? 0.4667 0.4993 0.4337 -0.0188 0.0057  0.0005  488  ARG B CD  
12563 N NE  . ARG B 490  ? 0.4354 0.4627 0.4046 -0.0182 0.0036  -0.0006 488  ARG B NE  
12564 C CZ  . ARG B 490  ? 0.3733 0.3938 0.3406 -0.0185 0.0014  -0.0005 488  ARG B CZ  
12565 N NH1 . ARG B 490  ? 0.3828 0.4007 0.3459 -0.0197 0.0008  0.0007  488  ARG B NH1 
12566 N NH2 . ARG B 490  ? 0.4082 0.4247 0.3778 -0.0176 -0.0002 -0.0016 488  ARG B NH2 
12567 N N   . ARG B 491  ? 0.5347 0.5936 0.4993 -0.0130 0.0166  -0.0001 489  ARG B N   
12568 C CA  . ARG B 491  ? 0.5873 0.6536 0.5506 -0.0134 0.0194  0.0012  489  ARG B CA  
12569 C C   . ARG B 491  ? 0.6303 0.7043 0.5977 -0.0108 0.0217  0.0004  489  ARG B C   
12570 O O   . ARG B 491  ? 0.5996 0.6816 0.5685 -0.0120 0.0239  0.0021  489  ARG B O   
12571 C CB  . ARG B 491  ? 0.5484 0.6125 0.5059 -0.0118 0.0202  0.0004  489  ARG B CB  
12572 N N   . LEU B 492  ? 0.6354 0.7074 0.6049 -0.0073 0.0213  -0.0020 490  LEU B N   
12573 C CA  . LEU B 492  ? 0.6248 0.7033 0.5979 -0.0042 0.0234  -0.0030 490  LEU B CA  
12574 C C   . LEU B 492  ? 0.5892 0.6690 0.5679 -0.0047 0.0222  -0.0029 490  LEU B C   
12575 O O   . LEU B 492  ? 0.7040 0.7913 0.6863 -0.0057 0.0235  -0.0015 490  LEU B O   
12576 C CB  . LEU B 492  ? 0.6200 0.6958 0.5906 0.0005  0.0241  -0.0059 490  LEU B CB  
12577 N N   . LEU B 493  ? 0.7351 0.8080 0.7145 -0.0039 0.0200  -0.0044 491  LEU B N   
12578 C CA  . LEU B 493  ? 0.5822 0.6560 0.5665 -0.0039 0.0190  -0.0045 491  LEU B CA  
12579 C C   . LEU B 493  ? 0.5812 0.6575 0.5677 -0.0084 0.0181  -0.0021 491  LEU B C   
12580 O O   . LEU B 493  ? 0.6585 0.7426 0.6481 -0.0094 0.0194  -0.0007 491  LEU B O   
12581 C CB  . LEU B 493  ? 0.5480 0.6137 0.5323 -0.0025 0.0167  -0.0064 491  LEU B CB  
12582 N N   . ALA B 497  ? 0.5046 0.5983 0.5006 0.0015  0.0230  -0.0045 495  ALA B N   
12583 C CA  . ALA B 497  ? 0.5441 0.6431 0.5452 0.0005  0.0226  -0.0034 495  ALA B CA  
12584 C C   . ALA B 497  ? 0.4384 0.5484 0.4423 0.0010  0.0251  -0.0020 495  ALA B C   
12585 O O   . ALA B 497  ? 0.4769 0.5913 0.4796 -0.0011 0.0264  -0.0004 495  ALA B O   
12586 C CB  . ALA B 497  ? 0.4557 0.5520 0.4574 -0.0045 0.0203  -0.0019 495  ALA B CB  
12587 N N   . ASN B 498  ? 0.4695 0.5843 0.4774 0.0038  0.0256  -0.0024 496  ASN B N   
12588 C CA  . ASN B 498  ? 0.4959 0.6218 0.5072 0.0048  0.0280  -0.0010 496  ASN B CA  
12589 C C   . ASN B 498  ? 0.4615 0.5939 0.4755 -0.0004 0.0276  0.0019  496  ASN B C   
12590 O O   . ASN B 498  ? 0.4376 0.5792 0.4533 -0.0008 0.0297  0.0035  496  ASN B O   
12591 C CB  . ASN B 498  ? 0.4668 0.5958 0.4819 0.0089  0.0282  -0.0020 496  ASN B CB  
12592 N N   . SER B 499  ? 0.4184 0.5460 0.4327 -0.0043 0.0250  0.0025  497  SER B N   
12593 C CA  . SER B 499  ? 0.3836 0.5163 0.4003 -0.0095 0.0242  0.0051  497  SER B CA  
12594 C C   . SER B 499  ? 0.3608 0.4926 0.3740 -0.0134 0.0246  0.0067  497  SER B C   
12595 O O   . SER B 499  ? 0.3295 0.4656 0.3443 -0.0180 0.0242  0.0091  497  SER B O   
12596 C CB  . SER B 499  ? 0.4299 0.5569 0.4475 -0.0122 0.0212  0.0050  497  SER B CB  
12597 O OG  . SER B 499  ? 0.4404 0.5566 0.4538 -0.0129 0.0196  0.0038  497  SER B OG  
12598 N N   . SER B 500  ? 0.3757 0.5019 0.3842 -0.0117 0.0253  0.0055  498  SER B N   
12599 C CA  . SER B 500  ? 0.3343 0.4585 0.3389 -0.0153 0.0254  0.0071  498  SER B CA  
12600 C C   . SER B 500  ? 0.3928 0.5269 0.3978 -0.0154 0.0285  0.0088  498  SER B C   
12601 O O   . SER B 500  ? 0.4330 0.5728 0.4393 -0.0112 0.0308  0.0079  498  SER B O   
12602 C CB  . SER B 500  ? 0.4045 0.5189 0.4039 -0.0137 0.0247  0.0052  498  SER B CB  
12603 O OG  . SER B 500  ? 0.4750 0.5905 0.4728 -0.0087 0.0268  0.0033  498  SER B OG  
12604 N N   . PHE B 501  ? 0.3738 0.5097 0.3776 -0.0203 0.0284  0.0113  499  PHE B N   
12605 C CA  . PHE B 501  ? 0.3762 0.5211 0.3798 -0.0209 0.0313  0.0132  499  PHE B CA  
12606 C C   . PHE B 501  ? 0.4212 0.5639 0.4202 -0.0168 0.0334  0.0115  499  PHE B C   
12607 O O   . PHE B 501  ? 0.5039 0.6547 0.5034 -0.0143 0.0365  0.0117  499  PHE B O   
12608 C CB  . PHE B 501  ? 0.3483 0.4936 0.3506 -0.0273 0.0305  0.0163  499  PHE B CB  
12609 C CG  . PHE B 501  ? 0.3746 0.5308 0.3779 -0.0289 0.0334  0.0188  499  PHE B CG  
12610 C CD1 . PHE B 501  ? 0.4194 0.5761 0.4182 -0.0277 0.0357  0.0190  499  PHE B CD1 
12611 C CD2 . PHE B 501  ? 0.3671 0.5332 0.3756 -0.0318 0.0339  0.0212  499  PHE B CD2 
12612 C CE1 . PHE B 501  ? 0.4210 0.5881 0.4206 -0.0292 0.0386  0.0214  499  PHE B CE1 
12613 C CE2 . PHE B 501  ? 0.4141 0.5909 0.4239 -0.0334 0.0366  0.0237  499  PHE B CE2 
12614 C CZ  . PHE B 501  ? 0.3744 0.5518 0.3797 -0.0320 0.0391  0.0238  499  PHE B CZ  
12615 N N   . VAL B 502  ? 0.4700 0.6018 0.4644 -0.0160 0.0318  0.0097  500  VAL B N   
12616 C CA  . VAL B 502  ? 0.5313 0.6600 0.5208 -0.0123 0.0333  0.0079  500  VAL B CA  
12617 C C   . VAL B 502  ? 0.5192 0.6519 0.5104 -0.0064 0.0354  0.0057  500  VAL B C   
12618 O O   . VAL B 502  ? 0.5315 0.6673 0.5200 -0.0034 0.0380  0.0050  500  VAL B O   
12619 C CB  . VAL B 502  ? 0.5090 0.6253 0.4940 -0.0125 0.0307  0.0063  500  VAL B CB  
12620 N N   . HIS B 503  ? 0.4532 0.5858 0.4486 -0.0045 0.0342  0.0045  501  HIS B N   
12621 C CA  . HIS B 503  ? 0.4812 0.6174 0.4785 0.0011  0.0360  0.0026  501  HIS B CA  
12622 C C   . HIS B 503  ? 0.5180 0.6670 0.5201 0.0016  0.0385  0.0044  501  HIS B C   
12623 O O   . HIS B 503  ? 0.4910 0.6453 0.4931 0.0059  0.0412  0.0035  501  HIS B O   
12624 C CB  . HIS B 503  ? 0.5012 0.6311 0.5004 0.0031  0.0337  0.0006  501  HIS B CB  
12625 C CG  . HIS B 503  ? 0.5339 0.6680 0.5361 0.0084  0.0351  -0.0009 501  HIS B CG  
12626 N ND1 . HIS B 503  ? 0.5265 0.6689 0.5345 0.0087  0.0356  0.0003  501  HIS B ND1 
12627 C CD2 . HIS B 503  ? 0.5519 0.6825 0.5518 0.0136  0.0361  -0.0035 501  HIS B CD2 
12628 C CE1 . HIS B 503  ? 0.5229 0.6669 0.5320 0.0140  0.0368  -0.0014 501  HIS B CE1 
12629 N NE2 . HIS B 503  ? 0.5416 0.6782 0.5458 0.0171  0.0372  -0.0038 501  HIS B NE2 
12630 N N   . ARG B 504  ? 0.4612 0.6153 0.4675 -0.0029 0.0375  0.0069  502  ARG B N   
12631 C CA  . ARG B 504  ? 0.3836 0.5502 0.3955 -0.0026 0.0393  0.0087  502  ARG B CA  
12632 C C   . ARG B 504  ? 0.4512 0.6267 0.4622 -0.0027 0.0426  0.0104  502  ARG B C   
12633 O O   . ARG B 504  ? 0.4571 0.6426 0.4716 0.0004  0.0452  0.0107  502  ARG B O   
12634 C CB  . ARG B 504  ? 0.4098 0.5787 0.4260 -0.0077 0.0369  0.0109  502  ARG B CB  
12635 C CG  . ARG B 504  ? 0.4142 0.5774 0.4325 -0.0065 0.0343  0.0092  502  ARG B CG  
12636 C CD  . ARG B 504  ? 0.3690 0.5314 0.3898 -0.0121 0.0315  0.0110  502  ARG B CD  
12637 N NE  . ARG B 504  ? 0.3734 0.5473 0.3988 -0.0153 0.0323  0.0139  502  ARG B NE  
12638 C CZ  . ARG B 504  ? 0.3976 0.5803 0.4284 -0.0133 0.0329  0.0143  502  ARG B CZ  
12639 N NH1 . ARG B 504  ? 0.4037 0.5851 0.4358 -0.0080 0.0330  0.0122  502  ARG B NH1 
12640 N NH2 . ARG B 504  ? 0.3966 0.5897 0.4317 -0.0169 0.0334  0.0172  502  ARG B NH2 
12641 N N   . ILE B 505  ? 0.4152 0.5877 0.4217 -0.0063 0.0427  0.0115  503  ILE B N   
12642 C CA  . ILE B 505  ? 0.4474 0.6282 0.4525 -0.0066 0.0460  0.0132  503  ILE B CA  
12643 C C   . ILE B 505  ? 0.5099 0.6926 0.5128 -0.0001 0.0490  0.0109  503  ILE B C   
12644 O O   . ILE B 505  ? 0.4445 0.6371 0.4482 0.0013  0.0524  0.0120  503  ILE B O   
12645 C CB  . ILE B 505  ? 0.4177 0.5935 0.4177 -0.0116 0.0453  0.0149  503  ILE B CB  
12646 N N   . ASN B 506  ? 0.4405 0.6138 0.4405 0.0041  0.0480  0.0076  504  ASN B N   
12647 C CA  . ASN B 506  ? 0.5369 0.7101 0.5340 0.0104  0.0504  0.0050  504  ASN B CA  
12648 C C   . ASN B 506  ? 0.5519 0.7286 0.5535 0.0155  0.0510  0.0035  504  ASN B C   
12649 O O   . ASN B 506  ? 0.5859 0.7616 0.5851 0.0212  0.0529  0.0010  504  ASN B O   
12650 C CB  . ASN B 506  ? 0.5519 0.7122 0.5422 0.0117  0.0489  0.0023  504  ASN B CB  
12651 C CG  . ASN B 506  ? 0.6102 0.7676 0.5950 0.0079  0.0490  0.0036  504  ASN B CG  
12652 O OD1 . ASN B 506  ? 0.5939 0.7592 0.5782 0.0066  0.0516  0.0056  504  ASN B OD1 
12653 N ND2 . ASN B 506  ? 0.6782 0.8244 0.6591 0.0062  0.0462  0.0026  504  ASN B ND2 
12654 N N   . ASP B 507  ? 0.5007 0.6813 0.5084 0.0138  0.0495  0.0048  505  ASP B N   
12655 C CA  . ASP B 507  ? 0.5339 0.7180 0.5460 0.0185  0.0498  0.0036  505  ASP B CA  
12656 C C   . ASP B 507  ? 0.5926 0.7915 0.6100 0.0193  0.0526  0.0058  505  ASP B C   
12657 O O   . ASP B 507  ? 0.5482 0.7540 0.5701 0.0146  0.0519  0.0087  505  ASP B O   
12658 C CB  . ASP B 507  ? 0.5188 0.6982 0.5344 0.0164  0.0462  0.0036  505  ASP B CB  
12659 C CG  . ASP B 507  ? 0.5650 0.7439 0.5833 0.0218  0.0460  0.0017  505  ASP B CG  
12660 O OD1 . ASP B 507  ? 0.6551 0.8394 0.6739 0.0270  0.0488  0.0008  505  ASP B OD1 
12661 O OD2 . ASP B 507  ? 0.6851 0.8582 0.7049 0.0209  0.0432  0.0011  505  ASP B OD2 
12662 N N   . PRO B 508  ? 0.6470 0.8512 0.6641 0.0251  0.0559  0.0046  506  PRO B N   
12663 C CA  . PRO B 508  ? 0.5945 0.8137 0.6169 0.0261  0.0588  0.0068  506  PRO B CA  
12664 C C   . PRO B 508  ? 0.6143 0.8399 0.6441 0.0265  0.0575  0.0080  506  PRO B C   
12665 O O   . PRO B 508  ? 0.6392 0.8780 0.6745 0.0258  0.0593  0.0105  506  PRO B O   
12666 C CB  . PRO B 508  ? 0.6964 0.9173 0.7156 0.0331  0.0624  0.0046  506  PRO B CB  
12667 C CG  . PRO B 508  ? 0.7244 0.9311 0.7359 0.0346  0.0612  0.0015  506  PRO B CG  
12668 C CD  . PRO B 508  ? 0.6454 0.8421 0.6572 0.0311  0.0570  0.0011  506  PRO B CD  
12669 N N   . LYS B 509  ? 0.6124 0.8296 0.6427 0.0275  0.0546  0.0063  507  LYS B N   
12670 C CA  . LYS B 509  ? 0.5977 0.8201 0.6347 0.0272  0.0529  0.0075  507  LYS B CA  
12671 C C   . LYS B 509  ? 0.6204 0.8453 0.6605 0.0197  0.0504  0.0103  507  LYS B C   
12672 O O   . LYS B 509  ? 0.6642 0.8960 0.7103 0.0186  0.0493  0.0119  507  LYS B O   
12673 C CB  . LYS B 509  ? 0.5783 0.7904 0.6143 0.0306  0.0505  0.0048  507  LYS B CB  
12674 N N   . VAL B 510  ? 0.5914 0.8104 0.6274 0.0146  0.0495  0.0109  508  VAL B N   
12675 C CA  . VAL B 510  ? 0.5750 0.7957 0.6131 0.0073  0.0473  0.0136  508  VAL B CA  
12676 C C   . VAL B 510  ? 0.5366 0.7680 0.5757 0.0042  0.0498  0.0165  508  VAL B C   
12677 O O   . VAL B 510  ? 0.5398 0.7692 0.5740 0.0044  0.0518  0.0162  508  VAL B O   
12678 C CB  . VAL B 510  ? 0.4846 0.6916 0.5176 0.0036  0.0443  0.0126  508  VAL B CB  
12679 N N   . SER B 511  ? 0.5187 0.7616 0.5641 0.0014  0.0498  0.0193  509  SER B N   
12680 C CA  . SER B 511  ? 0.5069 0.7617 0.5543 -0.0014 0.0525  0.0223  509  SER B CA  
12681 C C   . SER B 511  ? 0.5281 0.7793 0.5729 -0.0091 0.0509  0.0245  509  SER B C   
12682 O O   . SER B 511  ? 0.5270 0.7675 0.5694 -0.0125 0.0475  0.0239  509  SER B O   
12683 C CB  . SER B 511  ? 0.5462 0.8154 0.6018 -0.0016 0.0530  0.0247  509  SER B CB  
12684 O OG  . SER B 511  ? 0.5571 0.8266 0.6157 -0.0082 0.0497  0.0268  509  SER B OG  
12685 N N   . ILE B 512  ? 0.4749 0.7354 0.5203 -0.0119 0.0534  0.0272  510  ILE B N   
12686 C CA  . ILE B 512  ? 0.4930 0.7513 0.5362 -0.0195 0.0520  0.0298  510  ILE B CA  
12687 C C   . ILE B 512  ? 0.5455 0.8066 0.5937 -0.0253 0.0489  0.0320  510  ILE B C   
12688 O O   . ILE B 512  ? 0.4723 0.7256 0.5179 -0.0311 0.0461  0.0329  510  ILE B O   
12689 C CB  . ILE B 512  ? 0.4597 0.7272 0.5018 -0.0207 0.0557  0.0321  510  ILE B CB  
12690 C CG1 . ILE B 512  ? 0.4820 0.7435 0.5176 -0.0155 0.0582  0.0295  510  ILE B CG1 
12691 C CG2 . ILE B 512  ? 0.4539 0.7208 0.4946 -0.0291 0.0544  0.0354  510  ILE B CG2 
12692 C CD1 . ILE B 512  ? 0.4378 0.7085 0.4719 -0.0155 0.0623  0.0313  510  ILE B CD1 
12693 N N   . ASP B 513  ? 0.5162 0.7882 0.5714 -0.0238 0.0492  0.0329  511  ASP B N   
12694 C CA  . ASP B 513  ? 0.5005 0.7748 0.5603 -0.0291 0.0459  0.0347  511  ASP B CA  
12695 C C   . ASP B 513  ? 0.4516 0.7116 0.5085 -0.0297 0.0419  0.0324  511  ASP B C   
12696 O O   . ASP B 513  ? 0.4260 0.6816 0.4826 -0.0358 0.0389  0.0336  511  ASP B O   
12697 C CB  . ASP B 513  ? 0.5383 0.8266 0.6060 -0.0264 0.0468  0.0358  511  ASP B CB  
12698 C CG  . ASP B 513  ? 0.5782 0.8823 0.6502 -0.0289 0.0496  0.0394  511  ASP B CG  
12699 O OD1 . ASP B 513  ? 0.5800 0.8846 0.6502 -0.0353 0.0495  0.0418  511  ASP B OD1 
12700 O OD2 . ASP B 513  ? 0.6606 0.9769 0.7379 -0.0245 0.0520  0.0398  511  ASP B OD2 
12701 N N   . GLU B 514  ? 0.4199 0.6725 0.4747 -0.0234 0.0420  0.0290  512  GLU B N   
12702 C CA  . GLU B 514  ? 0.4825 0.7216 0.5345 -0.0238 0.0385  0.0267  512  GLU B CA  
12703 C C   . GLU B 514  ? 0.4501 0.6778 0.4958 -0.0281 0.0370  0.0267  512  GLU B C   
12704 O O   . GLU B 514  ? 0.4380 0.6577 0.4824 -0.0321 0.0337  0.0266  512  GLU B O   
12705 C CB  . GLU B 514  ? 0.4346 0.6681 0.4851 -0.0163 0.0391  0.0233  512  GLU B CB  
12706 C CG  . GLU B 514  ? 0.5576 0.8016 0.6137 -0.0111 0.0407  0.0231  512  GLU B CG  
12707 C CD  . GLU B 514  ? 0.6196 0.8568 0.6736 -0.0038 0.0413  0.0197  512  GLU B CD  
12708 O OE1 . GLU B 514  ? 0.6877 0.9132 0.7388 -0.0037 0.0387  0.0177  512  GLU B OE1 
12709 O OE2 . GLU B 514  ? 0.6244 0.8679 0.6795 0.0017  0.0443  0.0191  512  GLU B OE2 
12710 N N   . LEU B 515  ? 0.4164 0.6430 0.4577 -0.0272 0.0395  0.0267  513  LEU B N   
12711 C CA  . LEU B 515  ? 0.4127 0.6281 0.4478 -0.0306 0.0382  0.0265  513  LEU B CA  
12712 C C   . LEU B 515  ? 0.4015 0.6181 0.4369 -0.0385 0.0365  0.0297  513  LEU B C   
12713 O O   . LEU B 515  ? 0.3711 0.5770 0.4022 -0.0421 0.0341  0.0296  513  LEU B O   
12714 C CB  . LEU B 515  ? 0.3767 0.5916 0.4071 -0.0277 0.0413  0.0259  513  LEU B CB  
12715 C CG  . LEU B 515  ? 0.3870 0.5981 0.4154 -0.0201 0.0427  0.0224  513  LEU B CG  
12716 C CD1 . LEU B 515  ? 0.4585 0.6719 0.4829 -0.0176 0.0461  0.0222  513  LEU B CD1 
12717 C CD2 . LEU B 515  ? 0.3907 0.5871 0.4152 -0.0191 0.0397  0.0196  513  LEU B CD2 
12718 N N   . ILE B 516  ? 0.3475 0.5770 0.3879 -0.0414 0.0376  0.0327  514  ILE B N   
12719 C CA  . ILE B 516  ? 0.3346 0.5659 0.3756 -0.0493 0.0361  0.0359  514  ILE B CA  
12720 C C   . ILE B 516  ? 0.3216 0.5532 0.3667 -0.0528 0.0327  0.0365  514  ILE B C   
12721 O O   . ILE B 516  ? 0.3414 0.5746 0.3872 -0.0596 0.0310  0.0392  514  ILE B O   
12722 C CB  . ILE B 516  ? 0.3975 0.6425 0.4410 -0.0516 0.0392  0.0393  514  ILE B CB  
12723 C CG1 . ILE B 516  ? 0.3984 0.6580 0.4497 -0.0496 0.0405  0.0403  514  ILE B CG1 
12724 C CG2 . ILE B 516  ? 0.3838 0.6283 0.4227 -0.0480 0.0426  0.0386  514  ILE B CG2 
12725 C CD1 . ILE B 516  ? 0.4471 0.7214 0.5017 -0.0518 0.0437  0.0437  514  ILE B CD1 
12726 N N   . ALA B 517  ? 0.3882 0.6181 0.4356 -0.0484 0.0316  0.0341  515  ALA B N   
12727 C CA  . ALA B 517  ? 0.3908 0.6196 0.4412 -0.0514 0.0282  0.0343  515  ALA B CA  
12728 C C   . ALA B 517  ? 0.3461 0.5625 0.3918 -0.0570 0.0249  0.0344  515  ALA B C   
12729 O O   . ALA B 517  ? 0.3245 0.5295 0.3646 -0.0557 0.0246  0.0326  515  ALA B O   
12730 C CB  . ALA B 517  ? 0.3630 0.5886 0.4148 -0.0454 0.0275  0.0312  515  ALA B CB  
12731 N N   . ASP B 518  ? 0.3546 0.5737 0.4026 -0.0632 0.0226  0.0366  516  ASP B N   
12732 C CA  . ASP B 518  ? 0.3486 0.5567 0.3923 -0.0690 0.0195  0.0370  516  ASP B CA  
12733 C C   . ASP B 518  ? 0.2986 0.4967 0.3412 -0.0670 0.0166  0.0341  516  ASP B C   
12734 O O   . ASP B 518  ? 0.3021 0.5046 0.3487 -0.0672 0.0151  0.0340  516  ASP B O   
12735 C CB  . ASP B 518  ? 0.3017 0.5171 0.3484 -0.0764 0.0181  0.0405  516  ASP B CB  
12736 C CG  . ASP B 518  ? 0.3683 0.5722 0.4102 -0.0827 0.0149  0.0412  516  ASP B CG  
12737 O OD1 . ASP B 518  ? 0.3024 0.4929 0.3392 -0.0811 0.0135  0.0388  516  ASP B OD1 
12738 O OD2 . ASP B 518  ? 0.4029 0.6112 0.4463 -0.0893 0.0137  0.0441  516  ASP B OD2 
12739 N N   . PRO B 519  ? 0.2567 0.4417 0.2938 -0.0650 0.0157  0.0318  517  PRO B N   
12740 C CA  . PRO B 519  ? 0.2896 0.4653 0.3256 -0.0631 0.0132  0.0291  517  PRO B CA  
12741 C C   . PRO B 519  ? 0.2682 0.4416 0.3048 -0.0687 0.0098  0.0300  517  PRO B C   
12742 O O   . PRO B 519  ? 0.2664 0.4385 0.3048 -0.0673 0.0080  0.0285  517  PRO B O   
12743 C CB  . PRO B 519  ? 0.3104 0.4731 0.3402 -0.0612 0.0130  0.0271  517  PRO B CB  
12744 C CG  . PRO B 519  ? 0.3203 0.4835 0.3473 -0.0648 0.0141  0.0295  517  PRO B CG  
12745 C CD  . PRO B 519  ? 0.2787 0.4567 0.3103 -0.0650 0.0169  0.0318  517  PRO B CD  
12746 N N   . VAL B 520  ? 0.2897 0.4624 0.3247 -0.0752 0.0087  0.0325  518  VAL B N   
12747 C CA  . VAL B 520  ? 0.2709 0.4401 0.3056 -0.0809 0.0053  0.0333  518  VAL B CA  
12748 C C   . VAL B 520  ? 0.2959 0.4763 0.3368 -0.0817 0.0047  0.0341  518  VAL B C   
12749 O O   . VAL B 520  ? 0.2918 0.4688 0.3332 -0.0821 0.0021  0.0328  518  VAL B O   
12750 C CB  . VAL B 520  ? 0.3010 0.4681 0.3329 -0.0879 0.0046  0.0361  518  VAL B CB  
12751 C CG1 . VAL B 520  ? 0.3269 0.4889 0.3578 -0.0939 0.0008  0.0367  518  VAL B CG1 
12752 C CG2 . VAL B 520  ? 0.2835 0.4398 0.3092 -0.0867 0.0052  0.0354  518  VAL B CG2 
12753 N N   . GLU B 521  ? 0.2839 0.4782 0.3296 -0.0816 0.0071  0.0364  519  GLU B N   
12754 C CA  . GLU B 521  ? 0.2810 0.4869 0.3330 -0.0823 0.0065  0.0375  519  GLU B CA  
12755 C C   . GLU B 521  ? 0.2927 0.5001 0.3473 -0.0755 0.0070  0.0349  519  GLU B C   
12756 O O   . GLU B 521  ? 0.3311 0.5422 0.3889 -0.0760 0.0050  0.0348  519  GLU B O   
12757 C CB  . GLU B 521  ? 0.2884 0.5093 0.3451 -0.0843 0.0090  0.0408  519  GLU B CB  
12758 C CG  . GLU B 521  ? 0.3322 0.5524 0.3868 -0.0920 0.0082  0.0438  519  GLU B CG  
12759 C CD  . GLU B 521  ? 0.4191 0.6340 0.4727 -0.0985 0.0040  0.0444  519  GLU B CD  
12760 O OE1 . GLU B 521  ? 0.4781 0.6968 0.5352 -0.0983 0.0022  0.0438  519  GLU B OE1 
12761 O OE2 . GLU B 521  ? 0.4730 0.6796 0.5220 -0.1039 0.0025  0.0454  519  GLU B OE2 
12762 N N   . VAL B 522  ? 0.3106 0.5146 0.3634 -0.0691 0.0093  0.0328  520  VAL B N   
12763 C CA  . VAL B 522  ? 0.2821 0.4860 0.3367 -0.0627 0.0096  0.0303  520  VAL B CA  
12764 C C   . VAL B 522  ? 0.3361 0.5287 0.3878 -0.0632 0.0063  0.0281  520  VAL B C   
12765 O O   . VAL B 522  ? 0.3315 0.5267 0.3861 -0.0615 0.0050  0.0273  520  VAL B O   
12766 C CB  . VAL B 522  ? 0.3126 0.5148 0.3656 -0.0560 0.0127  0.0285  520  VAL B CB  
12767 C CG1 . VAL B 522  ? 0.3474 0.5485 0.4019 -0.0496 0.0128  0.0260  520  VAL B CG1 
12768 C CG2 . VAL B 522  ? 0.3703 0.5846 0.4263 -0.0552 0.0161  0.0306  520  VAL B CG2 
12769 N N   . VAL B 523  ? 0.2713 0.4514 0.3173 -0.0656 0.0049  0.0272  521  VAL B N   
12770 C CA  . VAL B 523  ? 0.2743 0.4435 0.3174 -0.0662 0.0019  0.0252  521  VAL B CA  
12771 C C   . VAL B 523  ? 0.2964 0.4691 0.3416 -0.0716 -0.0010 0.0265  521  VAL B C   
12772 O O   . VAL B 523  ? 0.3210 0.4915 0.3668 -0.0706 -0.0030 0.0251  521  VAL B O   
12773 C CB  . VAL B 523  ? 0.2988 0.4544 0.3354 -0.0676 0.0010  0.0241  521  VAL B CB  
12774 C CG1 . VAL B 523  ? 0.3066 0.4520 0.3403 -0.0696 -0.0023 0.0225  521  VAL B CG1 
12775 C CG2 . VAL B 523  ? 0.3385 0.4895 0.3730 -0.0616 0.0033  0.0221  521  VAL B CG2 
12776 N N   . ARG B 524  ? 0.3215 0.4992 0.3675 -0.0776 -0.0014 0.0293  522  ARG B N   
12777 C CA  . ARG B 524  ? 0.3534 0.5339 0.4009 -0.0835 -0.0044 0.0308  522  ARG B CA  
12778 C C   . ARG B 524  ? 0.3494 0.5405 0.4028 -0.0813 -0.0047 0.0309  522  ARG B C   
12779 O O   . ARG B 524  ? 0.3796 0.5696 0.4333 -0.0840 -0.0076 0.0306  522  ARG B O   
12780 C CB  . ARG B 524  ? 0.3597 0.5461 0.4081 -0.0900 -0.0043 0.0342  522  ARG B CB  
12781 C CG  . ARG B 524  ? 0.4169 0.6046 0.4660 -0.0970 -0.0077 0.0357  522  ARG B CG  
12782 C CD  . ARG B 524  ? 0.3788 0.5767 0.4309 -0.1030 -0.0071 0.0395  522  ARG B CD  
12783 N NE  . ARG B 524  ? 0.3784 0.5719 0.4268 -0.1044 -0.0053 0.0406  522  ARG B NE  
12784 C CZ  . ARG B 524  ? 0.4474 0.6291 0.4900 -0.1088 -0.0072 0.0407  522  ARG B CZ  
12785 N NH1 . ARG B 524  ? 0.3815 0.5540 0.4209 -0.1122 -0.0108 0.0396  522  ARG B NH1 
12786 N NH2 . ARG B 524  ? 0.4140 0.5929 0.4536 -0.1098 -0.0054 0.0420  522  ARG B NH2 
12787 N N   . ALA B 525  ? 0.3263 0.5272 0.3840 -0.0762 -0.0018 0.0312  523  ALA B N   
12788 C CA  . ALA B 525  ? 0.3823 0.5947 0.4460 -0.0739 -0.0018 0.0317  523  ALA B CA  
12789 C C   . ALA B 525  ? 0.3984 0.6062 0.4617 -0.0677 -0.0021 0.0289  523  ALA B C   
12790 O O   . ALA B 525  ? 0.4134 0.6298 0.4814 -0.0653 -0.0023 0.0292  523  ALA B O   
12791 C CB  . ALA B 525  ? 0.3282 0.5548 0.3972 -0.0718 0.0015  0.0339  523  ALA B CB  
12792 N N   . MET B 526  ? 0.3788 0.5737 0.4369 -0.0650 -0.0021 0.0262  524  MET B N   
12793 C CA  A MET B 526  ? 0.3791 0.5690 0.4366 -0.0595 -0.0024 0.0236  524  MET B CA  
12794 C CA  B MET B 526  ? 0.3790 0.5693 0.4366 -0.0595 -0.0024 0.0237  524  MET B CA  
12795 C C   . MET B 526  ? 0.3272 0.5150 0.3846 -0.0622 -0.0059 0.0232  524  MET B C   
12796 O O   . MET B 526  ? 0.3533 0.5373 0.4085 -0.0682 -0.0083 0.0238  524  MET B O   
12797 C CB  A MET B 526  ? 0.3850 0.5615 0.4368 -0.0569 -0.0019 0.0211  524  MET B CB  
12798 C CB  B MET B 526  ? 0.3851 0.5627 0.4374 -0.0563 -0.0016 0.0212  524  MET B CB  
12799 C CG  A MET B 526  ? 0.4114 0.5889 0.4627 -0.0535 0.0014  0.0211  524  MET B CG  
12800 C CG  B MET B 526  ? 0.4093 0.5892 0.4615 -0.0533 0.0018  0.0215  524  MET B CG  
12801 S SD  A MET B 526  ? 0.4766 0.6651 0.5331 -0.0464 0.0042  0.0210  524  MET B SD  
12802 S SD  B MET B 526  ? 0.4287 0.5942 0.4746 -0.0500 0.0026  0.0188  524  MET B SD  
12803 C CE  A MET B 526  ? 0.3919 0.5720 0.4468 -0.0415 0.0029  0.0180  524  MET B CE  
12804 C CE  B MET B 526  ? 0.3744 0.5400 0.4220 -0.0421 0.0039  0.0164  524  MET B CE  
12805 N N   . PRO B 527  ? 0.4120 0.6018 0.4715 -0.0578 -0.0063 0.0220  525  PRO B N   
12806 C CA  . PRO B 527  ? 0.4371 0.6251 0.4962 -0.0603 -0.0096 0.0216  525  PRO B CA  
12807 C C   . PRO B 527  ? 0.4033 0.5771 0.4561 -0.0629 -0.0117 0.0196  525  PRO B C   
12808 O O   . PRO B 527  ? 0.3637 0.5355 0.4152 -0.0678 -0.0147 0.0200  525  PRO B O   
12809 C CB  . PRO B 527  ? 0.4420 0.6335 0.5038 -0.0541 -0.0090 0.0205  525  PRO B CB  
12810 C CG  . PRO B 527  ? 0.4504 0.6390 0.5114 -0.0483 -0.0059 0.0192  525  PRO B CG  
12811 C CD  . PRO B 527  ? 0.4269 0.6193 0.4883 -0.0505 -0.0038 0.0208  525  PRO B CD  
12812 N N   . VAL B 528  ? 0.3806 0.5444 0.4294 -0.0596 -0.0104 0.0176  526  VAL B N   
12813 C CA  . VAL B 528  ? 0.3208 0.4710 0.3636 -0.0615 -0.0121 0.0158  526  VAL B CA  
12814 C C   . VAL B 528  ? 0.3005 0.4456 0.3405 -0.0622 -0.0105 0.0159  526  VAL B C   
12815 O O   . VAL B 528  ? 0.3458 0.4885 0.3852 -0.0574 -0.0082 0.0148  526  VAL B O   
12816 C CB  . VAL B 528  ? 0.3117 0.4545 0.3524 -0.0566 -0.0123 0.0131  526  VAL B CB  
12817 C CG1 . VAL B 528  ? 0.3341 0.4631 0.3687 -0.0581 -0.0136 0.0112  526  VAL B CG1 
12818 C CG2 . VAL B 528  ? 0.3513 0.4990 0.3944 -0.0562 -0.0141 0.0131  526  VAL B CG2 
12819 N N   . VAL B 529  ? 0.2668 0.4098 0.3048 -0.0681 -0.0117 0.0173  527  VAL B N   
12820 C CA  . VAL B 529  ? 0.2442 0.3825 0.2794 -0.0691 -0.0103 0.0178  527  VAL B CA  
12821 C C   . VAL B 529  ? 0.2851 0.4105 0.3154 -0.0659 -0.0102 0.0152  527  VAL B C   
12822 O O   . VAL B 529  ? 0.2926 0.4092 0.3194 -0.0668 -0.0124 0.0136  527  VAL B O   
12823 C CB  . VAL B 529  ? 0.2788 0.4161 0.3123 -0.0764 -0.0121 0.0198  527  VAL B CB  
12824 C CG1 . VAL B 529  ? 0.2945 0.4252 0.3242 -0.0774 -0.0109 0.0202  527  VAL B CG1 
12825 C CG2 . VAL B 529  ? 0.2995 0.4510 0.3384 -0.0795 -0.0118 0.0227  527  VAL B CG2 
12826 N N   . GLY B 530  ? 0.2436 0.3682 0.2735 -0.0618 -0.0077 0.0146  528  GLY B N   
12827 C CA  . GLY B 530  ? 0.2509 0.3641 0.2765 -0.0590 -0.0075 0.0125  528  GLY B CA  
12828 C C   . GLY B 530  ? 0.2488 0.3591 0.2747 -0.0536 -0.0073 0.0101  528  GLY B C   
12829 O O   . GLY B 530  ? 0.2462 0.3466 0.2685 -0.0517 -0.0077 0.0082  528  GLY B O   
12830 N N   . ALA B 531  ? 0.2355 0.3541 0.2656 -0.0509 -0.0067 0.0102  529  ALA B N   
12831 C CA  . ALA B 531  ? 0.2202 0.3360 0.2505 -0.0458 -0.0064 0.0081  529  ALA B CA  
12832 C C   . ALA B 531  ? 0.2233 0.3347 0.2521 -0.0413 -0.0043 0.0068  529  ALA B C   
12833 O O   . ALA B 531  ? 0.2584 0.3739 0.2881 -0.0405 -0.0023 0.0078  529  ALA B O   
12834 C CB  . ALA B 531  ? 0.2939 0.4203 0.3292 -0.0435 -0.0059 0.0088  529  ALA B CB  
12835 N N   . LYS B 532  ? 0.2014 0.3045 0.2277 -0.0385 -0.0047 0.0047  530  LYS B N   
12836 C CA  . LYS B 532  ? 0.2216 0.3202 0.2466 -0.0341 -0.0030 0.0033  530  LYS B CA  
12837 C C   . LYS B 532  ? 0.2306 0.3373 0.2591 -0.0300 -0.0009 0.0036  530  LYS B C   
12838 O O   . LYS B 532  ? 0.2427 0.3571 0.2748 -0.0293 -0.0009 0.0044  530  LYS B O   
12839 C CB  . LYS B 532  ? 0.2553 0.3456 0.2781 -0.0318 -0.0040 0.0011  530  LYS B CB  
12840 C CG  . LYS B 532  ? 0.2861 0.3722 0.3081 -0.0270 -0.0025 -0.0004 530  LYS B CG  
12841 C CD  . LYS B 532  ? 0.2596 0.3387 0.2800 -0.0249 -0.0035 -0.0023 530  LYS B CD  
12842 C CE  . LYS B 532  ? 0.2327 0.3164 0.2557 -0.0232 -0.0040 -0.0024 530  LYS B CE  
12843 N NZ  . LYS B 532  ? 0.2516 0.3414 0.2777 -0.0190 -0.0022 -0.0022 530  LYS B NZ  
12844 N N   . HIS B 533  ? 0.2162 0.3211 0.2437 -0.0272 0.0010  0.0030  531  HIS B N   
12845 C CA  . HIS B 533  ? 0.2104 0.3211 0.2404 -0.0227 0.0031  0.0029  531  HIS B CA  
12846 C C   . HIS B 533  ? 0.2035 0.3139 0.2351 -0.0192 0.0026  0.0017  531  HIS B C   
12847 O O   . HIS B 533  ? 0.2286 0.3312 0.2579 -0.0184 0.0015  0.0002  531  HIS B O   
12848 C CB  . HIS B 533  ? 0.2278 0.3334 0.2551 -0.0201 0.0046  0.0018  531  HIS B CB  
12849 C CG  . HIS B 533  ? 0.2627 0.3746 0.2920 -0.0162 0.0071  0.0019  531  HIS B CG  
12850 N ND1 . HIS B 533  ? 0.2707 0.3850 0.3021 -0.0118 0.0078  0.0010  531  HIS B ND1 
12851 C CD2 . HIS B 533  ? 0.3279 0.4438 0.3569 -0.0160 0.0090  0.0027  531  HIS B CD2 
12852 C CE1 . HIS B 533  ? 0.3271 0.4464 0.3594 -0.0089 0.0100  0.0012  531  HIS B CE1 
12853 N NE2 . HIS B 533  ? 0.3978 0.5184 0.4288 -0.0113 0.0109  0.0022  531  HIS B NE2 
12854 N N   . ASP B 534  ? 0.2329 0.3521 0.2683 -0.0170 0.0035  0.0025  532  ASP B N   
12855 C CA  . ASP B 534  ? 0.2963 0.4161 0.3333 -0.0138 0.0030  0.0018  532  ASP B CA  
12856 C C   . ASP B 534  ? 0.2674 0.3807 0.3027 -0.0092 0.0039  -0.0002 532  ASP B C   
12857 O O   . ASP B 534  ? 0.2902 0.4009 0.3256 -0.0072 0.0031  -0.0010 532  ASP B O   
12858 C CB  . ASP B 534  ? 0.3109 0.4419 0.3525 -0.0120 0.0040  0.0032  532  ASP B CB  
12859 C CG  . ASP B 534  ? 0.4826 0.6207 0.5266 -0.0165 0.0026  0.0051  532  ASP B CG  
12860 O OD1 . ASP B 534  ? 0.4728 0.6071 0.5155 -0.0198 0.0004  0.0050  532  ASP B OD1 
12861 O OD2 . ASP B 534  ? 0.5650 0.7125 0.6121 -0.0168 0.0038  0.0068  532  ASP B OD2 
12862 N N   . ARG B 535  ? 0.2383 0.3488 0.2717 -0.0077 0.0055  -0.0008 533  ARG B N   
12863 C CA  . ARG B 535  ? 0.2449 0.3499 0.2768 -0.0034 0.0063  -0.0025 533  ARG B CA  
12864 C C   . ARG B 535  ? 0.2614 0.3566 0.2895 -0.0043 0.0057  -0.0038 533  ARG B C   
12865 O O   . ARG B 535  ? 0.2923 0.3828 0.3188 -0.0013 0.0064  -0.0052 533  ARG B O   
12866 C CB  . ARG B 535  ? 0.3008 0.4103 0.3335 -0.0001 0.0087  -0.0025 533  ARG B CB  
12867 N N   . ILE B 536  ? 0.2210 0.3128 0.2474 -0.0085 0.0042  -0.0035 534  ILE B N   
12868 C CA  . ILE B 536  ? 0.2041 0.2867 0.2271 -0.0093 0.0034  -0.0046 534  ILE B CA  
12869 C C   . ILE B 536  ? 0.1948 0.2735 0.2173 -0.0109 0.0015  -0.0051 534  ILE B C   
12870 O O   . ILE B 536  ? 0.2216 0.3027 0.2446 -0.0143 0.0003  -0.0041 534  ILE B O   
12871 C CB  . ILE B 536  ? 0.2010 0.2823 0.2219 -0.0126 0.0034  -0.0038 534  ILE B CB  
12872 C CG1 . ILE B 536  ? 0.2218 0.3072 0.2429 -0.0109 0.0055  -0.0034 534  ILE B CG1 
12873 C CG2 . ILE B 536  ? 0.2350 0.3068 0.2524 -0.0133 0.0024  -0.0049 534  ILE B CG2 
12874 C CD1 . ILE B 536  ? 0.2812 0.3663 0.3003 -0.0142 0.0057  -0.0023 534  ILE B CD1 
12875 N N   . ALA B 537  ? 0.1860 0.2588 0.2074 -0.0086 0.0011  -0.0065 535  ALA B N   
12876 C CA  . ALA B 537  ? 0.1940 0.2631 0.2147 -0.0097 -0.0005 -0.0071 535  ALA B CA  
12877 C C   . ALA B 537  ? 0.1990 0.2616 0.2167 -0.0127 -0.0016 -0.0074 535  ALA B C   
12878 O O   . ALA B 537  ? 0.2062 0.2642 0.2220 -0.0124 -0.0013 -0.0079 535  ALA B O   
12879 C CB  . ALA B 537  ? 0.2297 0.2950 0.2503 -0.0061 -0.0002 -0.0084 535  ALA B CB  
12880 N N   . LEU B 538  ? 0.2013 0.2634 0.2184 -0.0157 -0.0032 -0.0071 536  LEU B N   
12881 C CA  . LEU B 538  ? 0.2182 0.2728 0.2322 -0.0177 -0.0044 -0.0078 536  LEU B CA  
12882 C C   . LEU B 538  ? 0.1934 0.2420 0.2063 -0.0147 -0.0042 -0.0093 536  LEU B C   
12883 O O   . LEU B 538  ? 0.2159 0.2660 0.2304 -0.0119 -0.0037 -0.0098 536  LEU B O   
12884 C CB  . LEU B 538  ? 0.2280 0.2824 0.2413 -0.0206 -0.0061 -0.0076 536  LEU B CB  
12885 C CG  . LEU B 538  ? 0.2462 0.3048 0.2598 -0.0248 -0.0069 -0.0061 536  LEU B CG  
12886 C CD1 . LEU B 538  ? 0.3066 0.3651 0.3195 -0.0273 -0.0087 -0.0062 536  LEU B CD1 
12887 C CD2 . LEU B 538  ? 0.2448 0.2988 0.2557 -0.0273 -0.0071 -0.0057 536  LEU B CD2 
12888 N N   . PRO B 539  ? 0.1774 0.2191 0.1877 -0.0152 -0.0046 -0.0100 537  PRO B N   
12889 C CA  . PRO B 539  ? 0.1946 0.2311 0.2042 -0.0125 -0.0044 -0.0114 537  PRO B CA  
12890 C C   . PRO B 539  ? 0.1972 0.2336 0.2073 -0.0115 -0.0049 -0.0121 537  PRO B C   
12891 O O   . PRO B 539  ? 0.1977 0.2337 0.2088 -0.0085 -0.0042 -0.0127 537  PRO B O   
12892 C CB  . PRO B 539  ? 0.2044 0.2343 0.2113 -0.0139 -0.0052 -0.0118 537  PRO B CB  
12893 C CG  . PRO B 539  ? 0.1904 0.2224 0.1968 -0.0164 -0.0051 -0.0105 537  PRO B CG  
12894 C CD  . PRO B 539  ? 0.1950 0.2337 0.2031 -0.0181 -0.0052 -0.0095 537  PRO B CD  
12895 N N   . ALA B 540  ? 0.2007 0.2374 0.2100 -0.0139 -0.0061 -0.0119 538  ALA B N   
12896 C CA  . ALA B 540  ? 0.2326 0.2691 0.2418 -0.0131 -0.0066 -0.0125 538  ALA B CA  
12897 C C   . ALA B 540  ? 0.2512 0.2938 0.2632 -0.0109 -0.0059 -0.0120 538  ALA B C   
12898 O O   . ALA B 540  ? 0.2150 0.2571 0.2272 -0.0093 -0.0059 -0.0125 538  ALA B O   
12899 C CB  . ALA B 540  ? 0.2352 0.2711 0.2426 -0.0164 -0.0082 -0.0124 538  ALA B CB  
12900 N N   . GLU B 541  ? 0.2278 0.2761 0.2420 -0.0108 -0.0052 -0.0109 539  GLU B N   
12901 C CA  . GLU B 541  ? 0.2103 0.2649 0.2273 -0.0090 -0.0046 -0.0102 539  GLU B CA  
12902 C C   . GLU B 541  ? 0.1851 0.2404 0.2035 -0.0054 -0.0031 -0.0104 539  GLU B C   
12903 O O   . GLU B 541  ? 0.2111 0.2719 0.2318 -0.0037 -0.0024 -0.0097 539  GLU B O   
12904 C CB  . GLU B 541  ? 0.2458 0.3073 0.2643 -0.0115 -0.0051 -0.0088 539  GLU B CB  
12905 C CG  . GLU B 541  ? 0.2964 0.3569 0.3134 -0.0149 -0.0069 -0.0087 539  GLU B CG  
12906 C CD  . GLU B 541  ? 0.4092 0.4759 0.4275 -0.0183 -0.0077 -0.0073 539  GLU B CD  
12907 O OE1 . GLU B 541  ? 0.4223 0.4948 0.4430 -0.0181 -0.0067 -0.0061 539  GLU B OE1 
12908 O OE2 . GLU B 541  ? 0.4532 0.5186 0.4698 -0.0214 -0.0094 -0.0073 539  GLU B OE2 
12909 N N   . LEU B 542  ? 0.1942 0.2440 0.2112 -0.0043 -0.0026 -0.0113 540  LEU B N   
12910 C CA  . LEU B 542  ? 0.2076 0.2574 0.2255 -0.0012 -0.0013 -0.0116 540  LEU B CA  
12911 C C   . LEU B 542  ? 0.1998 0.2515 0.2193 0.0017  -0.0009 -0.0116 540  LEU B C   
12912 O O   . LEU B 542  ? 0.2364 0.2903 0.2571 0.0042  0.0002  -0.0115 540  LEU B O   
12913 C CB  . LEU B 542  ? 0.2284 0.2716 0.2445 -0.0006 -0.0012 -0.0126 540  LEU B CB  
12914 C CG  . LEU B 542  ? 0.2630 0.3038 0.2776 -0.0022 -0.0012 -0.0127 540  LEU B CG  
12915 C CD1 . LEU B 542  ? 0.2361 0.2711 0.2495 -0.0007 -0.0011 -0.0137 540  LEU B CD1 
12916 C CD2 . LEU B 542  ? 0.2440 0.2894 0.2594 -0.0023 -0.0003 -0.0119 540  LEU B CD2 
12917 N N   . PHE B 543  ? 0.1920 0.2427 0.2112 0.0016  -0.0017 -0.0117 541  PHE B N   
12918 C CA  . PHE B 543  ? 0.2205 0.2722 0.2408 0.0042  -0.0014 -0.0116 541  PHE B CA  
12919 C C   . PHE B 543  ? 0.2220 0.2798 0.2439 0.0040  -0.0020 -0.0106 541  PHE B C   
12920 O O   . PHE B 543  ? 0.2283 0.2871 0.2510 0.0059  -0.0020 -0.0103 541  PHE B O   
12921 C CB  . PHE B 543  ? 0.2015 0.2477 0.2203 0.0047  -0.0018 -0.0124 541  PHE B CB  
12922 C CG  . PHE B 543  ? 0.2324 0.2733 0.2500 0.0048  -0.0014 -0.0134 541  PHE B CG  
12923 C CD1 . PHE B 543  ? 0.2442 0.2843 0.2622 0.0066  -0.0005 -0.0136 541  PHE B CD1 
12924 C CD2 . PHE B 543  ? 0.2103 0.2470 0.2261 0.0031  -0.0020 -0.0140 541  PHE B CD2 
12925 C CE1 . PHE B 543  ? 0.2448 0.2803 0.2618 0.0065  -0.0004 -0.0144 541  PHE B CE1 
12926 C CE2 . PHE B 543  ? 0.2185 0.2506 0.2334 0.0033  -0.0018 -0.0147 541  PHE B CE2 
12927 C CZ  . PHE B 543  ? 0.2581 0.2898 0.2736 0.0049  -0.0011 -0.0149 541  PHE B CZ  
12928 N N   . GLY B 544  ? 0.2339 0.2960 0.2565 0.0015  -0.0024 -0.0098 542  GLY B N   
12929 C CA  . GLY B 544  ? 0.2281 0.2968 0.2526 0.0012  -0.0030 -0.0086 542  GLY B CA  
12930 C C   . GLY B 544  ? 0.2490 0.3167 0.2725 0.0006  -0.0043 -0.0087 542  GLY B C   
12931 O O   . GLY B 544  ? 0.2732 0.3360 0.2943 -0.0012 -0.0050 -0.0095 542  GLY B O   
12932 N N   . ASP B 545  ? 0.2870 0.3592 0.3123 0.0023  -0.0045 -0.0078 543  ASP B N   
12933 C CA  . ASP B 545  ? 0.3415 0.4137 0.3659 0.0018  -0.0058 -0.0076 543  ASP B CA  
12934 C C   . ASP B 545  ? 0.2847 0.3506 0.3071 0.0034  -0.0055 -0.0086 543  ASP B C   
12935 O O   . ASP B 545  ? 0.2868 0.3515 0.3076 0.0027  -0.0065 -0.0086 543  ASP B O   
12936 C CB  . ASP B 545  ? 0.3140 0.3931 0.3410 0.0035  -0.0061 -0.0062 543  ASP B CB  
12937 C CG  . ASP B 545  ? 0.4931 0.5797 0.5225 0.0017  -0.0064 -0.0051 543  ASP B CG  
12938 O OD1 . ASP B 545  ? 0.4830 0.5694 0.5115 -0.0019 -0.0071 -0.0052 543  ASP B OD1 
12939 O OD2 . ASP B 545  ? 0.5719 0.6646 0.6042 0.0040  -0.0059 -0.0040 543  ASP B OD2 
12940 N N   . ALA B 546  ? 0.2713 0.3331 0.2935 0.0055  -0.0042 -0.0092 544  ALA B N   
12941 C CA  . ALA B 546  ? 0.2417 0.2983 0.2624 0.0071  -0.0039 -0.0099 544  ALA B CA  
12942 C C   . ALA B 546  ? 0.2648 0.3165 0.2828 0.0049  -0.0045 -0.0109 544  ALA B C   
12943 O O   . ALA B 546  ? 0.2509 0.3004 0.2675 0.0051  -0.0048 -0.0111 544  ALA B O   
12944 C CB  . ALA B 546  ? 0.2513 0.3048 0.2725 0.0094  -0.0026 -0.0103 544  ALA B CB  
12945 N N   . ARG B 547  ? 0.2377 0.2875 0.2549 0.0028  -0.0046 -0.0115 545  ARG B N   
12946 C CA  . ARG B 547  ? 0.2282 0.2729 0.2427 0.0010  -0.0051 -0.0126 545  ARG B CA  
12947 C C   . ARG B 547  ? 0.2261 0.2699 0.2400 -0.0014 -0.0053 -0.0129 545  ARG B C   
12948 O O   . ARG B 547  ? 0.2148 0.2613 0.2304 -0.0013 -0.0048 -0.0124 545  ARG B O   
12949 C CB  . ARG B 547  ? 0.2750 0.3146 0.2888 0.0028  -0.0042 -0.0134 545  ARG B CB  
12950 C CG  . ARG B 547  ? 0.1966 0.2347 0.2115 0.0042  -0.0032 -0.0136 545  ARG B CG  
12951 C CD  . ARG B 547  ? 0.2234 0.2568 0.2377 0.0057  -0.0025 -0.0142 545  ARG B CD  
12952 N NE  . ARG B 547  ? 0.2142 0.2470 0.2299 0.0073  -0.0017 -0.0142 545  ARG B NE  
12953 C CZ  . ARG B 547  ? 0.2358 0.2656 0.2512 0.0071  -0.0014 -0.0149 545  ARG B CZ  
12954 N NH1 . ARG B 547  ? 0.2062 0.2330 0.2201 0.0055  -0.0018 -0.0155 545  ARG B NH1 
12955 N NH2 . ARG B 547  ? 0.2445 0.2741 0.2609 0.0086  -0.0008 -0.0148 545  ARG B NH2 
12956 N N   . THR B 548  ? 0.1964 0.2362 0.2079 -0.0034 -0.0060 -0.0137 546  THR B N   
12957 C CA  . THR B 548  ? 0.1968 0.2344 0.2071 -0.0057 -0.0064 -0.0140 546  THR B CA  
12958 C C   . THR B 548  ? 0.1850 0.2176 0.1947 -0.0045 -0.0056 -0.0149 546  THR B C   
12959 O O   . THR B 548  ? 0.1829 0.2117 0.1916 -0.0031 -0.0053 -0.0156 546  THR B O   
12960 C CB  . THR B 548  ? 0.2171 0.2523 0.2245 -0.0084 -0.0078 -0.0146 546  THR B CB  
12961 O OG1 . THR B 548  ? 0.2694 0.3096 0.2774 -0.0097 -0.0088 -0.0138 546  THR B OG1 
12962 C CG2 . THR B 548  ? 0.2266 0.2588 0.2325 -0.0109 -0.0083 -0.0148 546  THR B CG2 
12963 N N   . ASN B 549  ? 0.1693 0.2021 0.1797 -0.0049 -0.0052 -0.0146 547  ASN B N   
12964 C CA  . ASN B 549  ? 0.1696 0.1978 0.1794 -0.0040 -0.0047 -0.0152 547  ASN B CA  
12965 C C   . ASN B 549  ? 0.1709 0.1937 0.1780 -0.0054 -0.0054 -0.0161 547  ASN B C   
12966 O O   . ASN B 549  ? 0.2087 0.2310 0.2141 -0.0079 -0.0065 -0.0161 547  ASN B O   
12967 C CB  . ASN B 549  ? 0.1883 0.2184 0.1990 -0.0045 -0.0043 -0.0146 547  ASN B CB  
12968 C CG  . ASN B 549  ? 0.1707 0.1968 0.1810 -0.0032 -0.0037 -0.0151 547  ASN B CG  
12969 O OD1 . ASN B 549  ? 0.1880 0.2112 0.1984 -0.0014 -0.0034 -0.0158 547  ASN B OD1 
12970 N ND2 . ASN B 549  ? 0.1903 0.2168 0.2005 -0.0041 -0.0036 -0.0147 547  ASN B ND2 
12971 N N   . SER B 550  ? 0.1799 0.1985 0.1866 -0.0038 -0.0050 -0.0169 548  SER B N   
12972 C CA  . SER B 550  ? 0.1885 0.2017 0.1926 -0.0047 -0.0056 -0.0177 548  SER B CA  
12973 C C   . SER B 550  ? 0.1793 0.1911 0.1824 -0.0067 -0.0062 -0.0173 548  SER B C   
12974 O O   . SER B 550  ? 0.2025 0.2166 0.2069 -0.0068 -0.0058 -0.0166 548  SER B O   
12975 C CB  . SER B 550  ? 0.1781 0.1879 0.1826 -0.0024 -0.0049 -0.0184 548  SER B CB  
12976 O OG  . SER B 550  ? 0.2072 0.2172 0.2131 -0.0015 -0.0044 -0.0180 548  SER B OG  
12977 N N   . ALA B 551  ? 0.2235 0.2312 0.2239 -0.0085 -0.0071 -0.0179 549  ALA B N   
12978 C CA  . ALA B 551  ? 0.2174 0.2229 0.2163 -0.0106 -0.0078 -0.0174 549  ALA B CA  
12979 C C   . ALA B 551  ? 0.2212 0.2209 0.2188 -0.0095 -0.0079 -0.0181 549  ALA B C   
12980 O O   . ALA B 551  ? 0.2275 0.2239 0.2242 -0.0081 -0.0078 -0.0191 549  ALA B O   
12981 C CB  . ALA B 551  ? 0.2544 0.2590 0.2510 -0.0138 -0.0091 -0.0174 549  ALA B CB  
12982 N N   . GLY B 552  ? 0.2181 0.2168 0.2156 -0.0102 -0.0080 -0.0174 550  GLY B N   
12983 C CA  . GLY B 552  ? 0.2437 0.2371 0.2398 -0.0094 -0.0083 -0.0178 550  GLY B CA  
12984 C C   . GLY B 552  ? 0.2239 0.2126 0.2167 -0.0119 -0.0096 -0.0177 550  GLY B C   
12985 O O   . GLY B 552  ? 0.2432 0.2320 0.2345 -0.0141 -0.0103 -0.0177 550  GLY B O   
12986 N N   . LEU B 553  ? 0.2599 0.2442 0.2515 -0.0115 -0.0100 -0.0176 551  LEU B N   
12987 C CA  . LEU B 553  ? 0.2706 0.2497 0.2589 -0.0137 -0.0113 -0.0174 551  LEU B CA  
12988 C C   . LEU B 553  ? 0.2393 0.2179 0.2275 -0.0143 -0.0115 -0.0161 551  LEU B C   
12989 O O   . LEU B 553  ? 0.2667 0.2463 0.2566 -0.0121 -0.0108 -0.0160 551  LEU B O   
12990 C CB  . LEU B 553  ? 0.2778 0.2504 0.2639 -0.0120 -0.0117 -0.0186 551  LEU B CB  
12991 C CG  . LEU B 553  ? 0.2835 0.2556 0.2687 -0.0114 -0.0116 -0.0200 551  LEU B CG  
12992 C CD1 . LEU B 553  ? 0.3407 0.3075 0.3245 -0.0089 -0.0115 -0.0212 551  LEU B CD1 
12993 C CD2 . LEU B 553  ? 0.3316 0.3026 0.3141 -0.0148 -0.0127 -0.0199 551  LEU B CD2 
12994 N N   . ASP B 554  ? 0.2571 0.2343 0.2431 -0.0175 -0.0124 -0.0151 552  ASP B N   
12995 C CA  . ASP B 554  ? 0.2310 0.2082 0.2166 -0.0185 -0.0126 -0.0137 552  ASP B CA  
12996 C C   . ASP B 554  ? 0.2496 0.2194 0.2325 -0.0179 -0.0136 -0.0137 552  ASP B C   
12997 O O   . ASP B 554  ? 0.2619 0.2266 0.2416 -0.0200 -0.0148 -0.0136 552  ASP B O   
12998 C CB  . ASP B 554  ? 0.2700 0.2499 0.2548 -0.0224 -0.0129 -0.0123 552  ASP B CB  
12999 C CG  . ASP B 554  ? 0.2631 0.2434 0.2472 -0.0236 -0.0129 -0.0107 552  ASP B CG  
13000 O OD1 . ASP B 554  ? 0.2834 0.2618 0.2677 -0.0214 -0.0128 -0.0107 552  ASP B OD1 
13001 O OD2 . ASP B 554  ? 0.3017 0.2844 0.2852 -0.0268 -0.0131 -0.0094 552  ASP B OD2 
13002 N N   . LEU B 555  ? 0.2403 0.2094 0.2244 -0.0151 -0.0132 -0.0139 553  LEU B N   
13003 C CA  . LEU B 555  ? 0.2593 0.2219 0.2413 -0.0140 -0.0142 -0.0139 553  LEU B CA  
13004 C C   . LEU B 555  ? 0.2892 0.2495 0.2689 -0.0162 -0.0151 -0.0122 553  LEU B C   
13005 O O   . LEU B 555  ? 0.2668 0.2220 0.2448 -0.0152 -0.0160 -0.0119 553  LEU B O   
13006 C CB  . LEU B 555  ? 0.2485 0.2116 0.2329 -0.0103 -0.0136 -0.0146 553  LEU B CB  
13007 C CG  . LEU B 555  ? 0.2681 0.2328 0.2544 -0.0081 -0.0128 -0.0162 553  LEU B CG  
13008 C CD1 . LEU B 555  ? 0.2987 0.2634 0.2872 -0.0047 -0.0124 -0.0167 553  LEU B CD1 
13009 C CD2 . LEU B 555  ? 0.3224 0.2825 0.3061 -0.0086 -0.0133 -0.0172 553  LEU B CD2 
13010 N N   . SER B 556  ? 0.2710 0.2353 0.2508 -0.0190 -0.0148 -0.0110 554  SER B N   
13011 C CA  . SER B 556  ? 0.2754 0.2373 0.2525 -0.0218 -0.0157 -0.0093 554  SER B CA  
13012 C C   . SER B 556  ? 0.2726 0.2318 0.2470 -0.0255 -0.0166 -0.0087 554  SER B C   
13013 O O   . SER B 556  ? 0.2827 0.2397 0.2546 -0.0282 -0.0174 -0.0071 554  SER B O   
13014 C CB  . SER B 556  ? 0.2917 0.2599 0.2703 -0.0226 -0.0147 -0.0080 554  SER B CB  
13015 O OG  . SER B 556  ? 0.2855 0.2594 0.2655 -0.0246 -0.0139 -0.0078 554  SER B OG  
13016 N N   . ASN B 557  ? 0.2522 0.2116 0.2269 -0.0257 -0.0167 -0.0100 555  ASN B N   
13017 C CA  . ASN B 557  ? 0.2708 0.2279 0.2429 -0.0294 -0.0178 -0.0096 555  ASN B CA  
13018 C C   . ASN B 557  ? 0.2797 0.2274 0.2481 -0.0289 -0.0192 -0.0106 555  ASN B C   
13019 O O   . ASN B 557  ? 0.2687 0.2143 0.2375 -0.0258 -0.0189 -0.0123 555  ASN B O   
13020 C CB  . ASN B 557  ? 0.2666 0.2293 0.2409 -0.0300 -0.0171 -0.0105 555  ASN B CB  
13021 C CG  . ASN B 557  ? 0.2931 0.2540 0.2650 -0.0340 -0.0184 -0.0102 555  ASN B CG  
13022 O OD1 . ASN B 557  ? 0.3077 0.2611 0.2760 -0.0348 -0.0197 -0.0108 555  ASN B OD1 
13023 N ND2 . ASN B 557  ? 0.2894 0.2574 0.2633 -0.0365 -0.0180 -0.0093 555  ASN B ND2 
13024 N N   . GLU B 558  ? 0.2724 0.2145 0.2371 -0.0318 -0.0206 -0.0093 556  GLU B N   
13025 C CA  . GLU B 558  ? 0.3132 0.2457 0.2740 -0.0310 -0.0220 -0.0101 556  GLU B CA  
13026 C C   . GLU B 558  ? 0.3040 0.2337 0.2633 -0.0313 -0.0225 -0.0120 556  GLU B C   
13027 O O   . GLU B 558  ? 0.3042 0.2276 0.2615 -0.0287 -0.0229 -0.0135 556  GLU B O   
13028 C CB  . GLU B 558  ? 0.3262 0.2527 0.2831 -0.0343 -0.0235 -0.0083 556  GLU B CB  
13029 C CG  . GLU B 558  ? 0.3427 0.2693 0.2998 -0.0335 -0.0234 -0.0065 556  GLU B CG  
13030 C CD  . GLU B 558  ? 0.3704 0.2934 0.3278 -0.0288 -0.0234 -0.0074 556  GLU B CD  
13031 O OE1 . GLU B 558  ? 0.3492 0.2681 0.3061 -0.0260 -0.0236 -0.0092 556  GLU B OE1 
13032 O OE2 . GLU B 558  ? 0.3407 0.2654 0.2990 -0.0279 -0.0232 -0.0061 556  GLU B OE2 
13033 N N   . GLU B 559  ? 0.2927 0.2269 0.2526 -0.0345 -0.0225 -0.0119 557  GLU B N   
13034 C CA  . GLU B 559  ? 0.2584 0.1905 0.2168 -0.0347 -0.0230 -0.0137 557  GLU B CA  
13035 C C   . GLU B 559  ? 0.2933 0.2279 0.2543 -0.0301 -0.0216 -0.0156 557  GLU B C   
13036 O O   . GLU B 559  ? 0.3100 0.2395 0.2689 -0.0281 -0.0218 -0.0174 557  GLU B O   
13037 C CB  . GLU B 559  ? 0.3383 0.2765 0.2978 -0.0386 -0.0232 -0.0131 557  GLU B CB  
13038 C CG  . GLU B 559  ? 0.4041 0.3411 0.3614 -0.0439 -0.0245 -0.0112 557  GLU B CG  
13039 C CD  . GLU B 559  ? 0.5141 0.4581 0.4731 -0.0474 -0.0247 -0.0107 557  GLU B CD  
13040 O OE1 . GLU B 559  ? 0.5198 0.4671 0.4804 -0.0458 -0.0242 -0.0123 557  GLU B OE1 
13041 O OE2 . GLU B 559  ? 0.4337 0.3803 0.3927 -0.0516 -0.0253 -0.0087 557  GLU B OE2 
13042 N N   . THR B 560  ? 0.2707 0.2131 0.2362 -0.0284 -0.0200 -0.0151 558  THR B N   
13043 C CA  . THR B 560  ? 0.2658 0.2111 0.2340 -0.0243 -0.0186 -0.0166 558  THR B CA  
13044 C C   . THR B 560  ? 0.2898 0.2294 0.2571 -0.0206 -0.0186 -0.0175 558  THR B C   
13045 O O   . THR B 560  ? 0.2763 0.2138 0.2432 -0.0180 -0.0182 -0.0192 558  THR B O   
13046 C CB  . THR B 560  ? 0.2596 0.2137 0.2325 -0.0234 -0.0172 -0.0158 558  THR B CB  
13047 O OG1 . THR B 560  ? 0.2914 0.2512 0.2654 -0.0265 -0.0172 -0.0150 558  THR B OG1 
13048 C CG2 . THR B 560  ? 0.2856 0.2425 0.2613 -0.0195 -0.0158 -0.0172 558  THR B CG2 
13049 N N   . LEU B 561  ? 0.2513 0.1884 0.2181 -0.0204 -0.0190 -0.0162 559  LEU B N   
13050 C CA  . LEU B 561  ? 0.2539 0.1860 0.2201 -0.0168 -0.0191 -0.0168 559  LEU B CA  
13051 C C   . LEU B 561  ? 0.2898 0.2134 0.2517 -0.0164 -0.0202 -0.0182 559  LEU B C   
13052 O O   . LEU B 561  ? 0.2760 0.1970 0.2380 -0.0127 -0.0197 -0.0196 559  LEU B O   
13053 C CB  . LEU B 561  ? 0.2752 0.2061 0.2413 -0.0170 -0.0197 -0.0150 559  LEU B CB  
13054 C CG  . LEU B 561  ? 0.2384 0.1769 0.2085 -0.0163 -0.0185 -0.0140 559  LEU B CG  
13055 C CD1 . LEU B 561  ? 0.2760 0.2125 0.2451 -0.0168 -0.0193 -0.0122 559  LEU B CD1 
13056 C CD2 . LEU B 561  ? 0.2603 0.2020 0.2339 -0.0123 -0.0173 -0.0153 559  LEU B CD2 
13057 N N   . ALA B 562  ? 0.2698 0.1890 0.2279 -0.0202 -0.0216 -0.0177 560  ALA B N   
13058 C CA  . ALA B 562  ? 0.3039 0.2142 0.2572 -0.0200 -0.0228 -0.0191 560  ALA B CA  
13059 C C   . ALA B 562  ? 0.3269 0.2381 0.2802 -0.0185 -0.0220 -0.0214 560  ALA B C   
13060 O O   . ALA B 562  ? 0.3274 0.2334 0.2787 -0.0153 -0.0219 -0.0230 560  ALA B O   
13061 C CB  . ALA B 562  ? 0.2933 0.1989 0.2425 -0.0250 -0.0246 -0.0180 560  ALA B CB  
13062 N N   . SER B 563  ? 0.2874 0.2053 0.2427 -0.0205 -0.0215 -0.0214 561  SER B N   
13063 C CA  . SER B 563  ? 0.2861 0.2049 0.2410 -0.0192 -0.0208 -0.0234 561  SER B CA  
13064 C C   . SER B 563  ? 0.3172 0.2398 0.2757 -0.0144 -0.0190 -0.0243 561  SER B C   
13065 O O   . SER B 563  ? 0.3092 0.2294 0.2664 -0.0119 -0.0185 -0.0261 561  SER B O   
13066 C CB  . SER B 563  ? 0.3321 0.2573 0.2883 -0.0226 -0.0209 -0.0230 561  SER B CB  
13067 O OG  . SER B 563  ? 0.3863 0.3204 0.3476 -0.0222 -0.0196 -0.0218 561  SER B OG  
13068 N N   . LEU B 564  ? 0.2707 0.1991 0.2336 -0.0133 -0.0181 -0.0230 562  LEU B N   
13069 C CA  . LEU B 564  ? 0.2605 0.1924 0.2270 -0.0091 -0.0165 -0.0236 562  LEU B CA  
13070 C C   . LEU B 564  ? 0.2934 0.2190 0.2582 -0.0057 -0.0166 -0.0244 562  LEU B C   
13071 O O   . LEU B 564  ? 0.2917 0.2174 0.2572 -0.0024 -0.0155 -0.0258 562  LEU B O   
13072 C CB  . LEU B 564  ? 0.2780 0.2168 0.2490 -0.0089 -0.0157 -0.0220 562  LEU B CB  
13073 C CG  . LEU B 564  ? 0.3130 0.2560 0.2880 -0.0051 -0.0142 -0.0224 562  LEU B CG  
13074 C CD1 . LEU B 564  ? 0.3059 0.2523 0.2819 -0.0040 -0.0130 -0.0237 562  LEU B CD1 
13075 C CD2 . LEU B 564  ? 0.2992 0.2478 0.2777 -0.0055 -0.0138 -0.0209 562  LEU B CD2 
13076 N N   . THR B 565  ? 0.2798 0.1999 0.2423 -0.0064 -0.0178 -0.0235 563  THR B N   
13077 C CA  . THR B 565  ? 0.2764 0.1900 0.2371 -0.0031 -0.0182 -0.0242 563  THR B CA  
13078 C C   . THR B 565  ? 0.3128 0.2215 0.2701 -0.0015 -0.0180 -0.0264 563  THR B C   
13079 O O   . THR B 565  ? 0.3101 0.2182 0.2683 0.0025  -0.0169 -0.0276 563  THR B O   
13080 C CB  . THR B 565  ? 0.3276 0.2346 0.2850 -0.0049 -0.0199 -0.0229 563  THR B CB  
13081 O OG1 . THR B 565  ? 0.3232 0.2347 0.2837 -0.0056 -0.0199 -0.0209 563  THR B OG1 
13082 C CG2 . THR B 565  ? 0.3366 0.2360 0.2915 -0.0014 -0.0204 -0.0237 563  THR B CG2 
13083 N N   . GLU B 566  ? 0.3043 0.2099 0.2578 -0.0048 -0.0189 -0.0271 564  GLU B N   
13084 C CA  . GLU B 566  ? 0.3041 0.2043 0.2535 -0.0035 -0.0189 -0.0293 564  GLU B CA  
13085 C C   . GLU B 566  ? 0.3032 0.2095 0.2554 -0.0013 -0.0170 -0.0306 564  GLU B C   
13086 O O   . GLU B 566  ? 0.3142 0.2178 0.2650 0.0022  -0.0161 -0.0323 564  GLU B O   
13087 C CB  . GLU B 566  ? 0.3639 0.2591 0.3084 -0.0079 -0.0206 -0.0297 564  GLU B CB  
13088 C CG  . GLU B 566  ? 0.4372 0.3247 0.3781 -0.0100 -0.0226 -0.0285 564  GLU B CG  
13089 C CD  . GLU B 566  ? 0.5623 0.4434 0.5019 -0.0058 -0.0226 -0.0289 564  GLU B CD  
13090 O OE1 . GLU B 566  ? 0.5995 0.4764 0.5369 -0.0024 -0.0220 -0.0310 564  GLU B OE1 
13091 O OE2 . GLU B 566  ? 0.5407 0.4210 0.4815 -0.0057 -0.0232 -0.0271 564  GLU B OE2 
13092 N N   . ALA B 567  ? 0.2793 0.1938 0.2352 -0.0030 -0.0164 -0.0297 565  ALA B N   
13093 C CA  . ALA B 567  ? 0.2911 0.2114 0.2496 -0.0010 -0.0146 -0.0306 565  ALA B CA  
13094 C C   . ALA B 567  ? 0.2955 0.2183 0.2577 0.0035  -0.0131 -0.0306 565  ALA B C   
13095 O O   . ALA B 567  ? 0.2833 0.2072 0.2458 0.0063  -0.0117 -0.0320 565  ALA B O   
13096 C CB  . ALA B 567  ? 0.2977 0.2260 0.2595 -0.0037 -0.0144 -0.0295 565  ALA B CB  
13097 N N   . LEU B 568  ? 0.2584 0.1824 0.2234 0.0041  -0.0133 -0.0291 566  LEU B N   
13098 C CA  . LEU B 568  ? 0.2672 0.1939 0.2360 0.0080  -0.0120 -0.0290 566  LEU B CA  
13099 C C   . LEU B 568  ? 0.2794 0.1998 0.2455 0.0114  -0.0119 -0.0303 566  LEU B C   
13100 O O   . LEU B 568  ? 0.2615 0.1842 0.2295 0.0148  -0.0104 -0.0312 566  LEU B O   
13101 C CB  . LEU B 568  ? 0.2404 0.1694 0.2122 0.0076  -0.0126 -0.0270 566  LEU B CB  
13102 C CG  . LEU B 568  ? 0.2507 0.1865 0.2256 0.0049  -0.0124 -0.0257 566  LEU B CG  
13103 C CD1 . LEU B 568  ? 0.2713 0.2080 0.2480 0.0043  -0.0132 -0.0239 566  LEU B CD1 
13104 C CD2 . LEU B 568  ? 0.2942 0.2369 0.2730 0.0064  -0.0108 -0.0260 566  LEU B CD2 
13105 N N   . ARG B 569  ? 0.2926 0.2050 0.2543 0.0106  -0.0135 -0.0305 567  ARG B N   
13106 C CA  . ARG B 569  ? 0.2872 0.1927 0.2457 0.0140  -0.0134 -0.0320 567  ARG B CA  
13107 C C   . ARG B 569  ? 0.3295 0.2345 0.2857 0.0154  -0.0122 -0.0342 567  ARG B C   
13108 O O   . ARG B 569  ? 0.3353 0.2402 0.2921 0.0195  -0.0108 -0.0353 567  ARG B O   
13109 C CB  . ARG B 569  ? 0.3308 0.2271 0.2840 0.0122  -0.0155 -0.0319 567  ARG B CB  
13110 C CG  . ARG B 569  ? 0.4123 0.3079 0.3672 0.0121  -0.0166 -0.0298 567  ARG B CG  
13111 C CD  . ARG B 569  ? 0.4032 0.2898 0.3528 0.0096  -0.0187 -0.0294 567  ARG B CD  
13112 N NE  . ARG B 569  ? 0.5066 0.3929 0.4577 0.0093  -0.0198 -0.0272 567  ARG B NE  
13113 C CZ  . ARG B 569  ? 0.5259 0.4061 0.4734 0.0064  -0.0217 -0.0260 567  ARG B CZ  
13114 N NH1 . ARG B 569  ? 0.5435 0.4175 0.4858 0.0033  -0.0228 -0.0268 567  ARG B NH1 
13115 N NH2 . ARG B 569  ? 0.5529 0.4334 0.5019 0.0064  -0.0225 -0.0240 567  ARG B NH2 
13116 N N   . GLU B 570  ? 0.2953 0.2004 0.2490 0.0119  -0.0127 -0.0347 568  GLU B N   
13117 C CA  . GLU B 570  ? 0.3254 0.2299 0.2764 0.0129  -0.0117 -0.0368 568  GLU B CA  
13118 C C   . GLU B 570  ? 0.3229 0.2354 0.2785 0.0155  -0.0094 -0.0368 568  GLU B C   
13119 O O   . GLU B 570  ? 0.3182 0.2301 0.2724 0.0183  -0.0080 -0.0385 568  GLU B O   
13120 C CB  . GLU B 570  ? 0.3407 0.2446 0.2885 0.0083  -0.0129 -0.0371 568  GLU B CB  
13121 C CG  . GLU B 570  ? 0.3805 0.2754 0.3226 0.0056  -0.0151 -0.0375 568  GLU B CG  
13122 C CD  . GLU B 570  ? 0.5130 0.4095 0.4540 0.0002  -0.0166 -0.0367 568  GLU B CD  
13123 O OE1 . GLU B 570  ? 0.4983 0.4026 0.4425 -0.0011 -0.0159 -0.0362 568  GLU B OE1 
13124 O OE2 . GLU B 570  ? 0.5682 0.4582 0.5052 -0.0028 -0.0186 -0.0365 568  GLU B OE2 
13125 N N   . SER B 571  ? 0.2890 0.2091 0.2501 0.0146  -0.0090 -0.0350 569  SER B N   
13126 C CA  . SER B 571  ? 0.2905 0.2181 0.2560 0.0167  -0.0070 -0.0349 569  SER B CA  
13127 C C   . SER B 571  ? 0.3154 0.2427 0.2828 0.0213  -0.0057 -0.0353 569  SER B C   
13128 O O   . SER B 571  ? 0.3351 0.2663 0.3043 0.0237  -0.0038 -0.0359 569  SER B O   
13129 C CB  . SER B 571  ? 0.3086 0.2434 0.2794 0.0149  -0.0070 -0.0329 569  SER B CB  
13130 O OG  . SER B 571  ? 0.3151 0.2503 0.2889 0.0161  -0.0073 -0.0316 569  SER B OG  
13131 N N   . ALA B 572  ? 0.3070 0.2300 0.2741 0.0225  -0.0067 -0.0348 570  ALA B N   
13132 C CA  . ALA B 572  ? 0.3188 0.2419 0.2880 0.0270  -0.0056 -0.0350 570  ALA B CA  
13133 C C   . ALA B 572  ? 0.3413 0.2588 0.3060 0.0300  -0.0048 -0.0372 570  ALA B C   
13134 O O   . ALA B 572  ? 0.3886 0.3078 0.3554 0.0341  -0.0032 -0.0377 570  ALA B O   
13135 C CB  . ALA B 572  ? 0.3350 0.2556 0.3055 0.0275  -0.0070 -0.0336 570  ALA B CB  
13136 N N   . ALA B 573  ? 0.3376 0.2488 0.2964 0.0280  -0.0057 -0.0387 571  ALA B N   
13137 C CA  . ALA B 573  ? 0.3879 0.2932 0.3416 0.0307  -0.0050 -0.0410 571  ALA B CA  
13138 C C   . ALA B 573  ? 0.3652 0.2748 0.3186 0.0312  -0.0031 -0.0423 571  ALA B C   
13139 O O   . ALA B 573  ? 0.3652 0.2710 0.3147 0.0340  -0.0020 -0.0443 571  ALA B O   
13140 C CB  . ALA B 573  ? 0.3863 0.2819 0.3331 0.0282  -0.0071 -0.0421 571  ALA B CB  
13141 N N   . MET B 574  ? 0.3422 0.2593 0.2992 0.0288  -0.0027 -0.0411 572  MET B N   
13142 C CA  . MET B 574  ? 0.3135 0.2346 0.2699 0.0290  -0.0010 -0.0420 572  MET B CA  
13143 C C   . MET B 574  ? 0.3186 0.2455 0.2794 0.0331  0.0015  -0.0418 572  MET B C   
13144 O O   . MET B 574  ? 0.3191 0.2495 0.2849 0.0346  0.0018  -0.0403 572  MET B O   
13145 C CB  . MET B 574  ? 0.3289 0.2560 0.2879 0.0250  -0.0016 -0.0406 572  MET B CB  
13146 C CG  . MET B 574  ? 0.3621 0.2848 0.3172 0.0207  -0.0039 -0.0406 572  MET B CG  
13147 S SD  . MET B 574  ? 0.3853 0.3159 0.3446 0.0166  -0.0045 -0.0386 572  MET B SD  
13148 C CE  . MET B 574  ? 0.3821 0.3067 0.3360 0.0119  -0.0071 -0.0390 572  MET B CE  
13149 N N   . LYS B 575  ? 0.2837 0.2116 0.2422 0.0347  0.0032  -0.0433 573  LYS B N   
13150 C CA  . LYS B 575  ? 0.2915 0.2254 0.2539 0.0383  0.0058  -0.0430 573  LYS B CA  
13151 C C   . LYS B 575  ? 0.2886 0.2311 0.2557 0.0361  0.0065  -0.0413 573  LYS B C   
13152 O O   . LYS B 575  ? 0.3022 0.2461 0.2671 0.0344  0.0069  -0.0417 573  LYS B O   
13153 C CB  . LYS B 575  ? 0.3086 0.2396 0.2660 0.0410  0.0075  -0.0454 573  LYS B CB  
13154 C CG  . LYS B 575  ? 0.3722 0.3095 0.3333 0.0449  0.0105  -0.0452 573  LYS B CG  
13155 C CD  . LYS B 575  ? 0.4721 0.4052 0.4275 0.0481  0.0121  -0.0477 573  LYS B CD  
13156 C CE  . LYS B 575  ? 0.5566 0.4965 0.5157 0.0520  0.0153  -0.0474 573  LYS B CE  
13157 N NZ  . LYS B 575  ? 0.5335 0.4798 0.4935 0.0502  0.0166  -0.0467 573  LYS B NZ  
13158 N N   . TRP B 576  ? 0.2797 0.2274 0.2530 0.0361  0.0065  -0.0393 574  TRP B N   
13159 C CA  . TRP B 576  ? 0.2465 0.2018 0.2244 0.0342  0.0071  -0.0375 574  TRP B CA  
13160 C C   . TRP B 576  ? 0.2458 0.2069 0.2270 0.0371  0.0096  -0.0372 574  TRP B C   
13161 O O   . TRP B 576  ? 0.2533 0.2155 0.2372 0.0402  0.0106  -0.0370 574  TRP B O   
13162 C CB  . TRP B 576  ? 0.2600 0.2177 0.2426 0.0326  0.0057  -0.0356 574  TRP B CB  
13163 C CG  . TRP B 576  ? 0.2426 0.1955 0.2223 0.0295  0.0033  -0.0355 574  TRP B CG  
13164 C CD1 . TRP B 576  ? 0.2798 0.2274 0.2583 0.0295  0.0017  -0.0356 574  TRP B CD1 
13165 C CD2 . TRP B 576  ? 0.2351 0.1884 0.2132 0.0257  0.0022  -0.0353 574  TRP B CD2 
13166 N NE1 . TRP B 576  ? 0.2848 0.2296 0.2609 0.0259  -0.0002 -0.0353 574  TRP B NE1 
13167 C CE2 . TRP B 576  ? 0.2811 0.2296 0.2570 0.0235  0.0001  -0.0352 574  TRP B CE2 
13168 C CE3 . TRP B 576  ? 0.2572 0.2147 0.2355 0.0241  0.0028  -0.0351 574  TRP B CE3 
13169 C CZ2 . TRP B 576  ? 0.2856 0.2338 0.2598 0.0197  -0.0013 -0.0348 574  TRP B CZ2 
13170 C CZ3 . TRP B 576  ? 0.3023 0.2593 0.2789 0.0205  0.0013  -0.0347 574  TRP B CZ3 
13171 C CH2 . TRP B 576  ? 0.3063 0.2590 0.2810 0.0184  -0.0007 -0.0346 574  TRP B CH2 
13172 N N   . THR B 577  ? 0.2524 0.2174 0.2333 0.0360  0.0107  -0.0370 575  THR B N   
13173 C CA  . THR B 577  ? 0.2275 0.1983 0.2113 0.0382  0.0132  -0.0365 575  THR B CA  
13174 C C   . THR B 577  ? 0.2275 0.2042 0.2146 0.0357  0.0134  -0.0347 575  THR B C   
13175 O O   . THR B 577  ? 0.2358 0.2117 0.2217 0.0326  0.0118  -0.0344 575  THR B O   
13176 C CB  . THR B 577  ? 0.2731 0.2417 0.2517 0.0403  0.0150  -0.0385 575  THR B CB  
13177 O OG1 . THR B 577  ? 0.3153 0.2823 0.2896 0.0375  0.0142  -0.0391 575  THR B OG1 
13178 C CG2 . THR B 577  ? 0.2819 0.2436 0.2566 0.0429  0.0147  -0.0405 575  THR B CG2 
13179 N N   . ALA B 578  ? 0.2241 0.2069 0.2155 0.0371  0.0153  -0.0335 576  ALA B N   
13180 C CA  . ALA B 578  ? 0.2107 0.1990 0.2048 0.0351  0.0157  -0.0319 576  ALA B CA  
13181 C C   . ALA B 578  ? 0.2063 0.1987 0.2010 0.0373  0.0185  -0.0318 576  ALA B C   
13182 O O   . ALA B 578  ? 0.2399 0.2343 0.2373 0.0400  0.0198  -0.0316 576  ALA B O   
13183 C CB  . ALA B 578  ? 0.2009 0.1929 0.2010 0.0338  0.0149  -0.0298 576  ALA B CB  
13184 N N   . LEU B 579  ? 0.2333 0.2269 0.2253 0.0362  0.0192  -0.0318 577  LEU B N   
13185 C CA  . LEU B 579  ? 0.2330 0.2300 0.2244 0.0381  0.0219  -0.0318 577  LEU B CA  
13186 C C   . LEU B 579  ? 0.2193 0.2214 0.2131 0.0360  0.0224  -0.0298 577  LEU B C   
13187 O O   . LEU B 579  ? 0.2063 0.2079 0.2001 0.0332  0.0206  -0.0290 577  LEU B O   
13188 C CB  . LEU B 579  ? 0.2512 0.2438 0.2355 0.0390  0.0224  -0.0341 577  LEU B CB  
13189 C CG  . LEU B 579  ? 0.3312 0.3167 0.3114 0.0403  0.0213  -0.0363 577  LEU B CG  
13190 C CD1 . LEU B 579  ? 0.3484 0.3293 0.3210 0.0407  0.0216  -0.0386 577  LEU B CD1 
13191 C CD2 . LEU B 579  ? 0.3382 0.3245 0.3213 0.0438  0.0226  -0.0365 577  LEU B CD2 
13192 N N   . PRO B 580  ? 0.2107 0.2177 0.2061 0.0373  0.0248  -0.0288 578  PRO B N   
13193 C CA  . PRO B 580  ? 0.1829 0.1937 0.1790 0.0353  0.0253  -0.0271 578  PRO B CA  
13194 C C   . PRO B 580  ? 0.2144 0.2221 0.2041 0.0344  0.0250  -0.0283 578  PRO B C   
13195 O O   . PRO B 580  ? 0.2511 0.2579 0.2366 0.0361  0.0266  -0.0296 578  PRO B O   
13196 C CB  . PRO B 580  ? 0.2497 0.2660 0.2485 0.0373  0.0282  -0.0260 578  PRO B CB  
13197 C CG  . PRO B 580  ? 0.2423 0.2586 0.2440 0.0399  0.0287  -0.0267 578  PRO B CG  
13198 C CD  . PRO B 580  ? 0.2242 0.2337 0.2212 0.0406  0.0272  -0.0291 578  PRO B CD  
13199 N N   . GLN B 581  ? 0.2009 0.2067 0.1896 0.0317  0.0227  -0.0280 579  GLN B N   
13200 C CA  . GLN B 581  ? 0.2186 0.2215 0.2015 0.0304  0.0218  -0.0290 579  GLN B CA  
13201 C C   . GLN B 581  ? 0.2475 0.2544 0.2309 0.0290  0.0225  -0.0271 579  GLN B C   
13202 O O   . GLN B 581  ? 0.2381 0.2463 0.2239 0.0269  0.0210  -0.0256 579  GLN B O   
13203 C CB  . GLN B 581  ? 0.2385 0.2376 0.2205 0.0283  0.0190  -0.0296 579  GLN B CB  
13204 C CG  . GLN B 581  ? 0.2425 0.2370 0.2235 0.0294  0.0182  -0.0314 579  GLN B CG  
13205 C CD  . GLN B 581  ? 0.3164 0.3064 0.2911 0.0308  0.0187  -0.0338 579  GLN B CD  
13206 O OE1 . GLN B 581  ? 0.3004 0.2906 0.2710 0.0309  0.0196  -0.0343 579  GLN B OE1 
13207 N NE2 . GLN B 581  ? 0.3723 0.3577 0.3458 0.0321  0.0181  -0.0354 579  GLN B NE2 
13208 N N   . LEU B 582  ? 0.2406 0.2495 0.2217 0.0304  0.0247  -0.0271 580  LEU B N   
13209 C CA  . LEU B 582  ? 0.2230 0.2352 0.2037 0.0292  0.0254  -0.0253 580  LEU B CA  
13210 C C   . LEU B 582  ? 0.2701 0.2794 0.2447 0.0278  0.0240  -0.0263 580  LEU B C   
13211 O O   . LEU B 582  ? 0.2993 0.3042 0.2699 0.0279  0.0228  -0.0285 580  LEU B O   
13212 C CB  . LEU B 582  ? 0.2659 0.2821 0.2470 0.0310  0.0284  -0.0245 580  LEU B CB  
13213 C CG  . LEU B 582  ? 0.3077 0.3287 0.2958 0.0312  0.0296  -0.0223 580  LEU B CG  
13214 C CD1 . LEU B 582  ? 0.3053 0.3254 0.2972 0.0325  0.0291  -0.0231 580  LEU B CD1 
13215 C CD2 . LEU B 582  ? 0.3204 0.3460 0.3088 0.0326  0.0327  -0.0212 580  LEU B CD2 
13216 N N   . ALA B 583  ? 0.2534 0.2654 0.2274 0.0265  0.0240  -0.0245 581  ALA B N   
13217 C CA  . ALA B 583  ? 0.2717 0.2816 0.2403 0.0251  0.0225  -0.0252 581  ALA B CA  
13218 C C   . ALA B 583  ? 0.3259 0.3329 0.2879 0.0265  0.0235  -0.0275 581  ALA B C   
13219 O O   . ALA B 583  ? 0.3552 0.3586 0.3124 0.0255  0.0218  -0.0292 581  ALA B O   
13220 C CB  . ALA B 583  ? 0.2915 0.3048 0.2604 0.0239  0.0227  -0.0227 581  ALA B CB  
13221 N N   . THR B 584  ? 0.2809 0.2895 0.2427 0.0289  0.0263  -0.0278 582  THR B N   
13222 C CA  . THR B 584  ? 0.3019 0.3081 0.2573 0.0307  0.0277  -0.0301 582  THR B CA  
13223 C C   . THR B 584  ? 0.2701 0.2717 0.2243 0.0324  0.0275  -0.0328 582  THR B C   
13224 O O   . THR B 584  ? 0.2886 0.2873 0.2372 0.0342  0.0286  -0.0350 582  THR B O   
13225 C CB  . THR B 584  ? 0.3323 0.3429 0.2880 0.0325  0.0310  -0.0290 582  THR B CB  
13226 O OG1 . THR B 584  ? 0.3531 0.3671 0.3157 0.0336  0.0324  -0.0276 582  THR B OG1 
13227 C CG2 . THR B 584  ? 0.3731 0.3871 0.3282 0.0308  0.0311  -0.0266 582  THR B CG2 
13228 N N   . GLY B 585  ? 0.2804 0.2810 0.2392 0.0320  0.0261  -0.0326 583  GLY B N   
13229 C CA  . GLY B 585  ? 0.2874 0.2833 0.2450 0.0335  0.0257  -0.0350 583  GLY B CA  
13230 C C   . GLY B 585  ? 0.3057 0.3042 0.2698 0.0352  0.0269  -0.0340 583  GLY B C   
13231 O O   . GLY B 585  ? 0.2736 0.2776 0.2430 0.0350  0.0280  -0.0317 583  GLY B O   
13232 N N   . PRO B 586  ? 0.2680 0.2625 0.2319 0.0368  0.0264  -0.0358 584  PRO B N   
13233 C CA  . PRO B 586  ? 0.2364 0.2335 0.2066 0.0385  0.0273  -0.0348 584  PRO B CA  
13234 C C   . PRO B 586  ? 0.2989 0.3005 0.2706 0.0414  0.0306  -0.0344 584  PRO B C   
13235 O O   . PRO B 586  ? 0.2983 0.2986 0.2651 0.0434  0.0323  -0.0360 584  PRO B O   
13236 C CB  . PRO B 586  ? 0.3137 0.3046 0.2818 0.0396  0.0259  -0.0371 584  PRO B CB  
13237 C CG  . PRO B 586  ? 0.3495 0.3351 0.3096 0.0399  0.0257  -0.0395 584  PRO B CG  
13238 C CD  . PRO B 586  ? 0.3152 0.3025 0.2733 0.0369  0.0248  -0.0385 584  PRO B CD  
13239 N N   . ALA B 587  ? 0.2751 0.2821 0.2538 0.0416  0.0314  -0.0322 585  ALA B N   
13240 C CA  . ALA B 587  ? 0.2546 0.2671 0.2361 0.0441  0.0346  -0.0313 585  ALA B CA  
13241 C C   . ALA B 587  ? 0.2717 0.2839 0.2563 0.0471  0.0352  -0.0321 585  ALA B C   
13242 O O   . ALA B 587  ? 0.2683 0.2776 0.2549 0.0466  0.0330  -0.0324 585  ALA B O   
13243 C CB  . ALA B 587  ? 0.2606 0.2796 0.2479 0.0422  0.0351  -0.0281 585  ALA B CB  
13244 N N   . ALA B 588  ? 0.2638 0.2793 0.2487 0.0503  0.0381  -0.0324 586  ALA B N   
13245 C CA  . ALA B 588  ? 0.2654 0.2818 0.2539 0.0534  0.0389  -0.0329 586  ALA B CA  
13246 C C   . ALA B 588  ? 0.2675 0.2901 0.2646 0.0523  0.0386  -0.0301 586  ALA B C   
13247 O O   . ALA B 588  ? 0.2884 0.3155 0.2886 0.0497  0.0388  -0.0278 586  ALA B O   
13248 C CB  . ALA B 588  ? 0.2529 0.2718 0.2396 0.0574  0.0424  -0.0338 586  ALA B CB  
13249 N N   . GLY B 589  ? 0.2797 0.3020 0.2804 0.0542  0.0381  -0.0303 587  GLY B N   
13250 C CA  . GLY B 589  ? 0.2616 0.2896 0.2703 0.0533  0.0377  -0.0278 587  GLY B CA  
13251 C C   . GLY B 589  ? 0.2949 0.3223 0.3067 0.0561  0.0372  -0.0284 587  GLY B C   
13252 O O   . GLY B 589  ? 0.3095 0.3322 0.3174 0.0591  0.0374  -0.0307 587  GLY B O   
13253 N N   . GLU B 590  ? 0.2954 0.3274 0.3143 0.0551  0.0363  -0.0263 588  GLU B N   
13254 C CA  . GLU B 590  ? 0.2976 0.3296 0.3201 0.0575  0.0355  -0.0264 588  GLU B CA  
13255 C C   . GLU B 590  ? 0.2752 0.2998 0.2952 0.0562  0.0323  -0.0276 588  GLU B C   
13256 O O   . GLU B 590  ? 0.2736 0.2967 0.2938 0.0525  0.0302  -0.0268 588  GLU B O   
13257 C CB  . GLU B 590  ? 0.3135 0.3533 0.3443 0.0564  0.0355  -0.0236 588  GLU B CB  
13258 C CG  . GLU B 590  ? 0.4557 0.5038 0.4901 0.0579  0.0387  -0.0222 588  GLU B CG  
13259 C CD  . GLU B 590  ? 0.5163 0.5657 0.5505 0.0630  0.0409  -0.0235 588  GLU B CD  
13260 O OE1 . GLU B 590  ? 0.5617 0.6076 0.5962 0.0652  0.0396  -0.0246 588  GLU B OE1 
13261 O OE2 . GLU B 590  ? 0.6371 0.6908 0.6708 0.0648  0.0441  -0.0234 588  GLU B OE2 
13262 N N   . THR B 591  ? 0.3025 0.3222 0.3200 0.0592  0.0319  -0.0295 589  THR B N   
13263 C CA  . THR B 591  ? 0.3012 0.3130 0.3153 0.0581  0.0290  -0.0307 589  THR B CA  
13264 C C   . THR B 591  ? 0.2874 0.2995 0.3060 0.0595  0.0275  -0.0300 589  THR B C   
13265 O O   . THR B 591  ? 0.2845 0.3002 0.3064 0.0630  0.0289  -0.0297 589  THR B O   
13266 C CB  . THR B 591  ? 0.2944 0.2987 0.3008 0.0601  0.0294  -0.0336 589  THR B CB  
13267 O OG1 . THR B 591  ? 0.3396 0.3439 0.3416 0.0586  0.0306  -0.0342 589  THR B OG1 
13268 C CG2 . THR B 591  ? 0.3177 0.3139 0.3204 0.0586  0.0263  -0.0347 589  THR B CG2 
13269 N N   . ARG B 592  ? 0.2704 0.2790 0.2891 0.0567  0.0246  -0.0295 590  ARG B N   
13270 C CA  . ARG B 592  ? 0.3003 0.3079 0.3221 0.0579  0.0228  -0.0290 590  ARG B CA  
13271 C C   . ARG B 592  ? 0.2928 0.2925 0.3104 0.0558  0.0200  -0.0299 590  ARG B C   
13272 O O   . ARG B 592  ? 0.2751 0.2715 0.2888 0.0529  0.0193  -0.0305 590  ARG B O   
13273 C CB  . ARG B 592  ? 0.3175 0.3323 0.3468 0.0562  0.0223  -0.0264 590  ARG B CB  
13274 C CG  . ARG B 592  ? 0.2968 0.3116 0.3263 0.0516  0.0207  -0.0254 590  ARG B CG  
13275 C CD  . ARG B 592  ? 0.3820 0.4018 0.4179 0.0501  0.0194  -0.0232 590  ARG B CD  
13276 N NE  . ARG B 592  ? 0.3832 0.4035 0.4194 0.0459  0.0182  -0.0222 590  ARG B NE  
13277 C CZ  . ARG B 592  ? 0.4035 0.4194 0.4378 0.0435  0.0159  -0.0224 590  ARG B CZ  
13278 N NH1 . ARG B 592  ? 0.3495 0.3600 0.3814 0.0444  0.0142  -0.0233 590  ARG B NH1 
13279 N NH2 . ARG B 592  ? 0.3685 0.3855 0.4032 0.0401  0.0152  -0.0215 590  ARG B NH2 
13280 N N   . THR B 593  ? 0.2755 0.2724 0.2942 0.0573  0.0184  -0.0299 591  THR B N   
13281 C CA  . THR B 593  ? 0.2803 0.2699 0.2953 0.0553  0.0157  -0.0305 591  THR B CA  
13282 C C   . THR B 593  ? 0.2775 0.2696 0.2958 0.0513  0.0138  -0.0287 591  THR B C   
13283 O O   . THR B 593  ? 0.2806 0.2792 0.3046 0.0508  0.0140  -0.0269 591  THR B O   
13284 C CB  . THR B 593  ? 0.3126 0.2979 0.3271 0.0583  0.0146  -0.0309 591  THR B CB  
13285 O OG1 . THR B 593  ? 0.3432 0.3346 0.3645 0.0596  0.0144  -0.0290 591  THR B OG1 
13286 C CG2 . THR B 593  ? 0.3943 0.3763 0.4050 0.0625  0.0165  -0.0330 591  THR B CG2 
13287 N N   . VAL B 594  ? 0.2366 0.2232 0.2509 0.0485  0.0119  -0.0292 592  VAL B N   
13288 C CA  . VAL B 594  ? 0.2073 0.1948 0.2237 0.0450  0.0099  -0.0278 592  VAL B CA  
13289 C C   . VAL B 594  ? 0.2676 0.2498 0.2827 0.0454  0.0077  -0.0279 592  VAL B C   
13290 O O   . VAL B 594  ? 0.2681 0.2435 0.2780 0.0458  0.0071  -0.0293 592  VAL B O   
13291 C CB  . VAL B 594  ? 0.2486 0.2344 0.2616 0.0415  0.0096  -0.0282 592  VAL B CB  
13292 C CG1 . VAL B 594  ? 0.2630 0.2495 0.2778 0.0382  0.0076  -0.0269 592  VAL B CG1 
13293 C CG2 . VAL B 594  ? 0.2894 0.2799 0.3031 0.0414  0.0117  -0.0281 592  VAL B CG2 
13294 N N   . LEU B 595  ? 0.2855 0.2707 0.3051 0.0453  0.0065  -0.0263 593  LEU B N   
13295 C CA  . LEU B 595  ? 0.2566 0.2375 0.2755 0.0460  0.0045  -0.0260 593  LEU B CA  
13296 C C   . LEU B 595  ? 0.2583 0.2382 0.2772 0.0423  0.0024  -0.0250 593  LEU B C   
13297 O O   . LEU B 595  ? 0.2669 0.2514 0.2885 0.0399  0.0024  -0.0240 593  LEU B O   
13298 C CB  . LEU B 595  ? 0.2784 0.2635 0.3025 0.0490  0.0046  -0.0249 593  LEU B CB  
13299 C CG  . LEU B 595  ? 0.3013 0.2887 0.3263 0.0531  0.0069  -0.0257 593  LEU B CG  
13300 C CD1 . LEU B 595  ? 0.3374 0.3296 0.3681 0.0559  0.0067  -0.0243 593  LEU B CD1 
13301 C CD2 . LEU B 595  ? 0.2807 0.2603 0.2996 0.0553  0.0072  -0.0277 593  LEU B CD2 
13302 N N   . ASN B 596  ? 0.2294 0.2032 0.2449 0.0418  0.0005  -0.0252 594  ASN B N   
13303 C CA  . ASN B 596  ? 0.2426 0.2153 0.2577 0.0385  -0.0014 -0.0242 594  ASN B CA  
13304 C C   . ASN B 596  ? 0.2426 0.2205 0.2631 0.0387  -0.0022 -0.0225 594  ASN B C   
13305 O O   . ASN B 596  ? 0.2285 0.2066 0.2510 0.0413  -0.0027 -0.0220 594  ASN B O   
13306 C CB  . ASN B 596  ? 0.2187 0.1838 0.2293 0.0385  -0.0031 -0.0247 594  ASN B CB  
13307 C CG  . ASN B 596  ? 0.2360 0.1993 0.2451 0.0350  -0.0049 -0.0238 594  ASN B CG  
13308 O OD1 . ASN B 596  ? 0.2445 0.2121 0.2569 0.0334  -0.0055 -0.0226 594  ASN B OD1 
13309 N ND2 . ASN B 596  ? 0.2736 0.2303 0.2776 0.0336  -0.0059 -0.0245 594  ASN B ND2 
13310 N N   . PRO B 597  ? 0.2124 0.1944 0.2353 0.0360  -0.0025 -0.0216 595  PRO B N   
13311 C CA  . PRO B 597  ? 0.2165 0.2030 0.2441 0.0360  -0.0035 -0.0201 595  PRO B CA  
13312 C C   . PRO B 597  ? 0.2167 0.1999 0.2435 0.0361  -0.0057 -0.0193 595  PRO B C   
13313 O O   . PRO B 597  ? 0.2156 0.2020 0.2462 0.0371  -0.0066 -0.0182 595  PRO B O   
13314 C CB  . PRO B 597  ? 0.1805 0.1703 0.2094 0.0328  -0.0035 -0.0196 595  PRO B CB  
13315 C CG  . PRO B 597  ? 0.2140 0.1996 0.2380 0.0307  -0.0033 -0.0206 595  PRO B CG  
13316 C CD  . PRO B 597  ? 0.2184 0.2011 0.2398 0.0330  -0.0020 -0.0219 595  PRO B CD  
13317 N N   . GLY B 598  ? 0.2253 0.2023 0.2473 0.0349  -0.0067 -0.0199 596  GLY B N   
13318 C CA  . GLY B 598  ? 0.2278 0.2013 0.2485 0.0349  -0.0088 -0.0190 596  GLY B CA  
13319 C C   . GLY B 598  ? 0.2626 0.2323 0.2822 0.0384  -0.0091 -0.0193 596  GLY B C   
13320 O O   . GLY B 598  ? 0.2588 0.2259 0.2779 0.0390  -0.0109 -0.0183 596  GLY B O   
13321 N N   . ASP B 599  ? 0.2349 0.2042 0.2541 0.0409  -0.0074 -0.0205 597  ASP B N   
13322 C CA  . ASP B 599  ? 0.2598 0.2255 0.2780 0.0446  -0.0074 -0.0209 597  ASP B CA  
13323 C C   . ASP B 599  ? 0.2662 0.2341 0.2851 0.0472  -0.0050 -0.0222 597  ASP B C   
13324 O O   . ASP B 599  ? 0.2449 0.2091 0.2598 0.0468  -0.0039 -0.0237 597  ASP B O   
13325 C CB  . ASP B 599  ? 0.2723 0.2291 0.2842 0.0439  -0.0086 -0.0216 597  ASP B CB  
13326 C CG  . ASP B 599  ? 0.3170 0.2691 0.3275 0.0478  -0.0092 -0.0218 597  ASP B CG  
13327 O OD1 . ASP B 599  ? 0.3031 0.2586 0.3168 0.0515  -0.0080 -0.0219 597  ASP B OD1 
13328 O OD2 . ASP B 599  ? 0.3380 0.2828 0.3440 0.0471  -0.0108 -0.0217 597  ASP B OD2 
13329 N N   . HIS B 600  ? 0.2528 0.2268 0.2769 0.0499  -0.0040 -0.0215 598  HIS B N   
13330 C CA  . HIS B 600  ? 0.2519 0.2291 0.2773 0.0523  -0.0015 -0.0225 598  HIS B CA  
13331 C C   . HIS B 600  ? 0.2749 0.2458 0.2959 0.0556  -0.0007 -0.0242 598  HIS B C   
13332 O O   . HIS B 600  ? 0.3082 0.2804 0.3286 0.0574  0.0016  -0.0254 598  HIS B O   
13333 C CB  . HIS B 600  ? 0.2799 0.2655 0.3121 0.0543  -0.0007 -0.0213 598  HIS B CB  
13334 C CG  . HIS B 600  ? 0.2746 0.2665 0.3107 0.0509  -0.0008 -0.0201 598  HIS B CG  
13335 N ND1 . HIS B 600  ? 0.3316 0.3315 0.3739 0.0517  -0.0001 -0.0188 598  HIS B ND1 
13336 C CD2 . HIS B 600  ? 0.2905 0.2816 0.3249 0.0469  -0.0014 -0.0200 598  HIS B CD2 
13337 C CE1 . HIS B 600  ? 0.3605 0.3637 0.4045 0.0481  -0.0005 -0.0180 598  HIS B CE1 
13338 N NE2 . HIS B 600  ? 0.3346 0.3327 0.3740 0.0453  -0.0013 -0.0187 598  HIS B NE2 
13339 N N   . ARG B 601  ? 0.2695 0.2333 0.2869 0.0564  -0.0025 -0.0243 599  ARG B N   
13340 C CA  . ARG B 601  ? 0.2511 0.2076 0.2634 0.0592  -0.0020 -0.0260 599  ARG B CA  
13341 C C   . ARG B 601  ? 0.2869 0.2383 0.2934 0.0565  -0.0015 -0.0277 599  ARG B C   
13342 O O   . ARG B 601  ? 0.3233 0.2694 0.3254 0.0586  -0.0006 -0.0295 599  ARG B O   
13343 C CB  . ARG B 601  ? 0.3442 0.2942 0.3542 0.0607  -0.0042 -0.0255 599  ARG B CB  
13344 C CG  . ARG B 601  ? 0.3583 0.3134 0.3740 0.0635  -0.0050 -0.0237 599  ARG B CG  
13345 C CD  . ARG B 601  ? 0.3618 0.3105 0.3752 0.0640  -0.0076 -0.0227 599  ARG B CD  
13346 N NE  . ARG B 601  ? 0.3544 0.3006 0.3656 0.0592  -0.0096 -0.0219 599  ARG B NE  
13347 C CZ  . ARG B 601  ? 0.4324 0.3727 0.4406 0.0585  -0.0119 -0.0209 599  ARG B CZ  
13348 N NH1 . ARG B 601  ? 0.4140 0.3499 0.4213 0.0623  -0.0129 -0.0206 599  ARG B NH1 
13349 N NH2 . ARG B 601  ? 0.3668 0.3056 0.3731 0.0540  -0.0134 -0.0201 599  ARG B NH2 
13350 N N   . ASP B 602  ? 0.2884 0.2410 0.2945 0.0519  -0.0023 -0.0272 600  ASP B N   
13351 C CA  . ASP B 602  ? 0.2839 0.2322 0.2849 0.0489  -0.0021 -0.0285 600  ASP B CA  
13352 C C   . ASP B 602  ? 0.2922 0.2462 0.2948 0.0487  0.0002  -0.0292 600  ASP B C   
13353 O O   . ASP B 602  ? 0.2698 0.2301 0.2762 0.0466  0.0005  -0.0281 600  ASP B O   
13354 C CB  . ASP B 602  ? 0.3064 0.2538 0.3066 0.0444  -0.0041 -0.0273 600  ASP B CB  
13355 C CG  . ASP B 602  ? 0.3441 0.2880 0.3396 0.0411  -0.0041 -0.0284 600  ASP B CG  
13356 O OD1 . ASP B 602  ? 0.3528 0.2922 0.3441 0.0423  -0.0033 -0.0302 600  ASP B OD1 
13357 O OD2 . ASP B 602  ? 0.3347 0.2803 0.3306 0.0374  -0.0049 -0.0276 600  ASP B OD2 
13358 N N   . VAL B 603  ? 0.2861 0.2375 0.2855 0.0510  0.0018  -0.0310 601  VAL B N   
13359 C CA  . VAL B 603  ? 0.2819 0.2380 0.2820 0.0510  0.0041  -0.0318 601  VAL B CA  
13360 C C   . VAL B 603  ? 0.2850 0.2386 0.2811 0.0469  0.0036  -0.0324 601  VAL B C   
13361 O O   . VAL B 603  ? 0.3188 0.2651 0.3092 0.0461  0.0027  -0.0338 601  VAL B O   
13362 C CB  . VAL B 603  ? 0.3013 0.2556 0.2992 0.0552  0.0061  -0.0335 601  VAL B CB  
13363 C CG1 . VAL B 603  ? 0.2813 0.2407 0.2797 0.0549  0.0085  -0.0341 601  VAL B CG1 
13364 C CG2 . VAL B 603  ? 0.3194 0.2765 0.3216 0.0596  0.0066  -0.0327 601  VAL B CG2 
13365 N N   . VAL B 604  ? 0.2574 0.2170 0.2565 0.0442  0.0040  -0.0314 602  VAL B N   
13366 C CA  . VAL B 604  ? 0.2580 0.2161 0.2540 0.0404  0.0034  -0.0318 602  VAL B CA  
13367 C C   . VAL B 604  ? 0.2486 0.2067 0.2415 0.0409  0.0052  -0.0333 602  VAL B C   
13368 O O   . VAL B 604  ? 0.2691 0.2227 0.2570 0.0389  0.0046  -0.0345 602  VAL B O   
13369 C CB  . VAL B 604  ? 0.2643 0.2281 0.2645 0.0374  0.0029  -0.0300 602  VAL B CB  
13370 C CG1 . VAL B 604  ? 0.2497 0.2117 0.2466 0.0336  0.0021  -0.0303 602  VAL B CG1 
13371 C CG2 . VAL B 604  ? 0.2477 0.2115 0.2506 0.0372  0.0012  -0.0286 602  VAL B CG2 
13372 N N   . GLY B 605  ? 0.2312 0.1946 0.2270 0.0433  0.0074  -0.0333 603  GLY B N   
13373 C CA  . GLY B 605  ? 0.2498 0.2138 0.2428 0.0437  0.0092  -0.0346 603  GLY B CA  
13374 C C   . GLY B 605  ? 0.2477 0.2184 0.2448 0.0465  0.0117  -0.0341 603  GLY B C   
13375 O O   . GLY B 605  ? 0.2493 0.2229 0.2507 0.0488  0.0120  -0.0332 603  GLY B O   
13376 N N   . SER B 606  ? 0.2245 0.1978 0.2203 0.0461  0.0134  -0.0346 604  SER B N   
13377 C CA  A SER B 606  ? 0.2486 0.2283 0.2478 0.0485  0.0160  -0.0341 604  SER B CA  
13378 C CA  B SER B 606  ? 0.2484 0.2280 0.2474 0.0485  0.0160  -0.0341 604  SER B CA  
13379 C C   . SER B 606  ? 0.2550 0.2397 0.2554 0.0459  0.0168  -0.0331 604  SER B C   
13380 O O   . SER B 606  ? 0.2668 0.2490 0.2634 0.0433  0.0160  -0.0337 604  SER B O   
13381 C CB  A SER B 606  ? 0.3118 0.2888 0.3069 0.0522  0.0179  -0.0361 604  SER B CB  
13382 C CB  B SER B 606  ? 0.3115 0.2880 0.3060 0.0520  0.0179  -0.0362 604  SER B CB  
13383 O OG  A SER B 606  ? 0.3317 0.3046 0.3206 0.0508  0.0179  -0.0377 604  SER B OG  
13384 O OG  B SER B 606  ? 0.3708 0.3433 0.3647 0.0552  0.0174  -0.0371 604  SER B OG  
13385 N N   . VAL B 607  ? 0.2264 0.2184 0.2323 0.0465  0.0182  -0.0314 605  VAL B N   
13386 C CA  . VAL B 607  ? 0.2082 0.2051 0.2156 0.0442  0.0191  -0.0302 605  VAL B CA  
13387 C C   . VAL B 607  ? 0.2251 0.2270 0.2338 0.0466  0.0221  -0.0301 605  VAL B C   
13388 O O   . VAL B 607  ? 0.2189 0.2242 0.2314 0.0493  0.0232  -0.0296 605  VAL B O   
13389 C CB  . VAL B 607  ? 0.2122 0.2132 0.2250 0.0416  0.0178  -0.0281 605  VAL B CB  
13390 C CG1 . VAL B 607  ? 0.2300 0.2347 0.2486 0.0436  0.0179  -0.0269 605  VAL B CG1 
13391 C CG2 . VAL B 607  ? 0.2260 0.2316 0.2401 0.0396  0.0188  -0.0268 605  VAL B CG2 
13392 N N   . THR B 608  ? 0.2079 0.2104 0.2134 0.0457  0.0233  -0.0304 606  THR B N   
13393 C CA  . THR B 608  ? 0.2299 0.2377 0.2365 0.0473  0.0261  -0.0299 606  THR B CA  
13394 C C   . THR B 608  ? 0.2067 0.2201 0.2172 0.0444  0.0262  -0.0276 606  THR B C   
13395 O O   . THR B 608  ? 0.2260 0.2377 0.2343 0.0416  0.0250  -0.0274 606  THR B O   
13396 C CB  . THR B 608  ? 0.2640 0.2683 0.2637 0.0483  0.0274  -0.0319 606  THR B CB  
13397 O OG1 . THR B 608  ? 0.2827 0.2812 0.2787 0.0511  0.0271  -0.0342 606  THR B OG1 
13398 C CG2 . THR B 608  ? 0.2676 0.2777 0.2681 0.0499  0.0305  -0.0313 606  THR B CG2 
13399 N N   . GLU B 609  ? 0.2163 0.2361 0.2326 0.0452  0.0275  -0.0258 607  GLU B N   
13400 C CA  . GLU B 609  ? 0.2477 0.2721 0.2680 0.0423  0.0272  -0.0235 607  GLU B CA  
13401 C C   . GLU B 609  ? 0.1917 0.2200 0.2110 0.0421  0.0296  -0.0227 607  GLU B C   
13402 O O   . GLU B 609  ? 0.2381 0.2674 0.2552 0.0446  0.0319  -0.0236 607  GLU B O   
13403 C CB  . GLU B 609  ? 0.2524 0.2811 0.2796 0.0423  0.0266  -0.0218 607  GLU B CB  
13404 C CG  . GLU B 609  ? 0.3101 0.3343 0.3375 0.0415  0.0238  -0.0223 607  GLU B CG  
13405 C CD  . GLU B 609  ? 0.3793 0.4071 0.4129 0.0415  0.0228  -0.0208 607  GLU B CD  
13406 O OE1 . GLU B 609  ? 0.4138 0.4473 0.4516 0.0430  0.0244  -0.0197 607  GLU B OE1 
13407 O OE2 . GLU B 609  ? 0.3445 0.3697 0.3788 0.0398  0.0204  -0.0206 607  GLU B OE2 
13408 N N   . THR B 610  ? 0.2123 0.2425 0.2329 0.0390  0.0290  -0.0210 608  THR B N   
13409 C CA  . THR B 610  ? 0.2053 0.2380 0.2239 0.0382  0.0307  -0.0202 608  THR B CA  
13410 C C   . THR B 610  ? 0.2086 0.2484 0.2323 0.0385  0.0329  -0.0180 608  THR B C   
13411 O O   . THR B 610  ? 0.2373 0.2801 0.2664 0.0373  0.0320  -0.0163 608  THR B O   
13412 C CB  . THR B 610  ? 0.2427 0.2738 0.2604 0.0347  0.0289  -0.0192 608  THR B CB  
13413 O OG1 . THR B 610  ? 0.2235 0.2487 0.2377 0.0340  0.0266  -0.0208 608  THR B OG1 
13414 C CG2 . THR B 610  ? 0.2262 0.2588 0.2408 0.0339  0.0304  -0.0184 608  THR B CG2 
13415 N N   . SER B 611  ? 0.2082 0.2508 0.2299 0.0400  0.0356  -0.0180 609  SER B N   
13416 C CA  . SER B 611  ? 0.2424 0.2921 0.2687 0.0398  0.0377  -0.0156 609  SER B CA  
13417 C C   . SER B 611  ? 0.2707 0.3217 0.2980 0.0362  0.0370  -0.0134 609  SER B C   
13418 O O   . SER B 611  ? 0.2228 0.2698 0.2460 0.0345  0.0357  -0.0138 609  SER B O   
13419 C CB  . SER B 611  ? 0.2803 0.3327 0.3038 0.0424  0.0410  -0.0162 609  SER B CB  
13420 O OG  . SER B 611  ? 0.2593 0.3092 0.2769 0.0412  0.0413  -0.0166 609  SER B OG  
13421 N N   . GLU B 612  ? 0.2510 0.3078 0.2839 0.0349  0.0377  -0.0109 610  GLU B N   
13422 C CA  . GLU B 612  ? 0.2638 0.3215 0.2975 0.0316  0.0371  -0.0086 610  GLU B CA  
13423 C C   . GLU B 612  ? 0.2812 0.3386 0.3098 0.0313  0.0387  -0.0084 610  GLU B C   
13424 O O   . GLU B 612  ? 0.2626 0.3174 0.2889 0.0291  0.0374  -0.0076 610  GLU B O   
13425 C CB  . GLU B 612  ? 0.3201 0.3839 0.3606 0.0302  0.0376  -0.0059 610  GLU B CB  
13426 C CG  . GLU B 612  ? 0.3622 0.4258 0.4075 0.0299  0.0354  -0.0060 610  GLU B CG  
13427 C CD  . GLU B 612  ? 0.4538 0.5237 0.5059 0.0285  0.0358  -0.0035 610  GLU B CD  
13428 O OE1 . GLU B 612  ? 0.5871 0.6605 0.6403 0.0266  0.0371  -0.0013 610  GLU B OE1 
13429 O OE2 . GLU B 612  ? 0.4594 0.5309 0.5158 0.0292  0.0348  -0.0036 610  GLU B OE2 
13430 N N   . GLU B 613  ? 0.2794 0.3392 0.3058 0.0338  0.0415  -0.0091 611  GLU B N   
13431 C CA  . GLU B 613  ? 0.2513 0.3105 0.2721 0.0338  0.0430  -0.0091 611  GLU B CA  
13432 C C   . GLU B 613  ? 0.2644 0.3168 0.2791 0.0335  0.0411  -0.0112 611  GLU B C   
13433 O O   . GLU B 613  ? 0.3105 0.3614 0.3217 0.0317  0.0406  -0.0104 611  GLU B O   
13434 C CB  . GLU B 613  ? 0.3470 0.4100 0.3664 0.0368  0.0465  -0.0097 611  GLU B CB  
13435 N N   . ASP B 614  ? 0.2371 0.2854 0.2504 0.0351  0.0398  -0.0138 612  ASP B N   
13436 C CA  . ASP B 614  ? 0.2163 0.2582 0.2239 0.0346  0.0377  -0.0157 612  ASP B CA  
13437 C C   . ASP B 614  ? 0.2454 0.2851 0.2545 0.0316  0.0349  -0.0146 612  ASP B C   
13438 O O   . ASP B 614  ? 0.2354 0.2717 0.2404 0.0303  0.0335  -0.0151 612  ASP B O   
13439 C CB  . ASP B 614  ? 0.2638 0.3016 0.2691 0.0369  0.0371  -0.0186 612  ASP B CB  
13440 C CG  . ASP B 614  ? 0.3488 0.3866 0.3497 0.0400  0.0397  -0.0203 612  ASP B CG  
13441 O OD1 . ASP B 614  ? 0.3595 0.3988 0.3568 0.0397  0.0413  -0.0198 612  ASP B OD1 
13442 O OD2 . ASP B 614  ? 0.3356 0.3718 0.3363 0.0426  0.0401  -0.0222 612  ASP B OD2 
13443 N N   . ALA B 615  ? 0.2343 0.2762 0.2494 0.0305  0.0340  -0.0131 613  ALA B N   
13444 C CA  . ALA B 615  ? 0.2240 0.2641 0.2406 0.0278  0.0316  -0.0120 613  ALA B CA  
13445 C C   . ALA B 615  ? 0.2098 0.2512 0.2249 0.0259  0.0320  -0.0100 613  ALA B C   
13446 O O   . ALA B 615  ? 0.2048 0.2431 0.2173 0.0245  0.0304  -0.0099 613  ALA B O   
13447 C CB  . ALA B 615  ? 0.2623 0.3045 0.2852 0.0270  0.0306  -0.0108 613  ALA B CB  
13448 N N   . ARG B 616  ? 0.2457 0.2917 0.2624 0.0260  0.0344  -0.0081 614  ARG B N   
13449 C CA  . ARG B 616  ? 0.2318 0.2789 0.2467 0.0243  0.0350  -0.0061 614  ARG B CA  
13450 C C   . ARG B 616  ? 0.2446 0.2891 0.2526 0.0250  0.0353  -0.0074 614  ARG B C   
13451 O O   . ARG B 616  ? 0.2304 0.2731 0.2358 0.0234  0.0342  -0.0064 614  ARG B O   
13452 C CB  . ARG B 616  ? 0.2694 0.3223 0.2875 0.0241  0.0375  -0.0037 614  ARG B CB  
13453 C CG  . ARG B 616  ? 0.2932 0.3484 0.3178 0.0222  0.0366  -0.0017 614  ARG B CG  
13454 C CD  . ARG B 616  ? 0.3565 0.4176 0.3842 0.0215  0.0390  0.0009  614  ARG B CD  
13455 N NE  . ARG B 616  ? 0.3763 0.4417 0.4057 0.0239  0.0414  0.0001  614  ARG B NE  
13456 C CZ  . ARG B 616  ? 0.4081 0.4760 0.4427 0.0247  0.0412  -0.0001 614  ARG B CZ  
13457 N NH1 . ARG B 616  ? 0.3668 0.4332 0.4052 0.0230  0.0387  0.0003  614  ARG B NH1 
13458 N NH2 . ARG B 616  ? 0.3612 0.4331 0.3970 0.0273  0.0435  -0.0008 614  ARG B NH2 
13459 N N   . ARG B 617  ? 0.2275 0.2715 0.2323 0.0274  0.0367  -0.0095 615  ARG B N   
13460 C CA  . ARG B 617  ? 0.2561 0.2972 0.2540 0.0280  0.0367  -0.0111 615  ARG B CA  
13461 C C   . ARG B 617  ? 0.2243 0.2605 0.2200 0.0267  0.0336  -0.0122 615  ARG B C   
13462 O O   . ARG B 617  ? 0.2412 0.2758 0.2328 0.0257  0.0328  -0.0120 615  ARG B O   
13463 C CB  . ARG B 617  ? 0.2825 0.3231 0.2774 0.0309  0.0384  -0.0136 615  ARG B CB  
13464 C CG  . ARG B 617  ? 0.2966 0.3340 0.2838 0.0315  0.0385  -0.0153 615  ARG B CG  
13465 C CD  . ARG B 617  ? 0.3483 0.3864 0.3323 0.0345  0.0412  -0.0172 615  ARG B CD  
13466 N NE  . ARG B 617  ? 0.4006 0.4353 0.3845 0.0365  0.0405  -0.0199 615  ARG B NE  
13467 C CZ  . ARG B 617  ? 0.5209 0.5500 0.4997 0.0370  0.0390  -0.0226 615  ARG B CZ  
13468 N NH1 . ARG B 617  ? 0.4842 0.5106 0.4574 0.0356  0.0378  -0.0230 615  ARG B NH1 
13469 N NH2 . ARG B 617  ? 0.5035 0.5296 0.4825 0.0388  0.0385  -0.0247 615  ARG B NH2 
13470 N N   . ALA B 618  ? 0.2135 0.2476 0.2121 0.0267  0.0318  -0.0133 616  ALA B N   
13471 C CA  . ALA B 618  ? 0.1918 0.2217 0.1886 0.0254  0.0290  -0.0142 616  ALA B CA  
13472 C C   . ALA B 618  ? 0.2035 0.2339 0.2013 0.0232  0.0278  -0.0120 616  ALA B C   
13473 O O   . ALA B 618  ? 0.2179 0.2460 0.2122 0.0223  0.0262  -0.0123 616  ALA B O   
13474 C CB  . ALA B 618  ? 0.2043 0.2323 0.2044 0.0257  0.0275  -0.0154 616  ALA B CB  
13475 N N   . VAL B 619  ? 0.2317 0.2650 0.2341 0.0223  0.0283  -0.0097 617  VAL B N   
13476 C CA  . VAL B 619  ? 0.1980 0.2311 0.2012 0.0204  0.0271  -0.0076 617  VAL B CA  
13477 C C   . VAL B 619  ? 0.2235 0.2572 0.2222 0.0201  0.0279  -0.0065 617  VAL B C   
13478 O O   . VAL B 619  ? 0.2415 0.2735 0.2382 0.0191  0.0263  -0.0059 617  VAL B O   
13479 C CB  . VAL B 619  ? 0.2235 0.2590 0.2323 0.0193  0.0273  -0.0054 617  VAL B CB  
13480 C CG1 . VAL B 619  ? 0.2273 0.2621 0.2365 0.0175  0.0261  -0.0033 617  VAL B CG1 
13481 C CG2 . VAL B 619  ? 0.2327 0.2673 0.2454 0.0195  0.0261  -0.0066 617  VAL B CG2 
13482 N N   . ARG B 620  ? 0.2429 0.2791 0.2398 0.0211  0.0304  -0.0064 618  ARG B N   
13483 C CA  . ARG B 620  ? 0.2776 0.3143 0.2697 0.0209  0.0312  -0.0055 618  ARG B CA  
13484 C C   . ARG B 620  ? 0.2409 0.2741 0.2276 0.0213  0.0296  -0.0076 618  ARG B C   
13485 O O   . ARG B 620  ? 0.2475 0.2800 0.2310 0.0203  0.0286  -0.0066 618  ARG B O   
13486 C CB  . ARG B 620  ? 0.2805 0.3206 0.2715 0.0222  0.0343  -0.0052 618  ARG B CB  
13487 C CG  . ARG B 620  ? 0.3609 0.4050 0.3572 0.0214  0.0359  -0.0026 618  ARG B CG  
13488 C CD  . ARG B 620  ? 0.4264 0.4747 0.4215 0.0225  0.0392  -0.0019 618  ARG B CD  
13489 N NE  . ARG B 620  ? 0.5050 0.5572 0.5059 0.0230  0.0407  -0.0013 618  ARG B NE  
13490 C CZ  . ARG B 620  ? 0.4171 0.4706 0.4186 0.0253  0.0422  -0.0033 618  ARG B CZ  
13491 N NH1 . ARG B 620  ? 0.4743 0.5252 0.4706 0.0274  0.0425  -0.0060 618  ARG B NH1 
13492 N NH2 . ARG B 620  ? 0.5112 0.5686 0.5184 0.0257  0.0434  -0.0024 618  ARG B NH2 
13493 N N   . LEU B 621  ? 0.2240 0.2552 0.2094 0.0225  0.0293  -0.0103 619  LEU B N   
13494 C CA  . LEU B 621  ? 0.2320 0.2597 0.2124 0.0225  0.0276  -0.0124 619  LEU B CA  
13495 C C   . LEU B 621  ? 0.2450 0.2710 0.2267 0.0209  0.0248  -0.0118 619  LEU B C   
13496 O O   . LEU B 621  ? 0.2609 0.2856 0.2387 0.0201  0.0234  -0.0120 619  LEU B O   
13497 C CB  . LEU B 621  ? 0.2520 0.2774 0.2313 0.0240  0.0278  -0.0154 619  LEU B CB  
13498 C CG  . LEU B 621  ? 0.2834 0.3099 0.2601 0.0262  0.0305  -0.0165 619  LEU B CG  
13499 C CD1 . LEU B 621  ? 0.2860 0.3098 0.2625 0.0279  0.0305  -0.0192 619  LEU B CD1 
13500 C CD2 . LEU B 621  ? 0.3541 0.3800 0.3241 0.0262  0.0311  -0.0169 619  LEU B CD2 
13501 N N   . ALA B 622  ? 0.2247 0.2508 0.2116 0.0203  0.0239  -0.0112 620  ALA B N   
13502 C CA  . ALA B 622  ? 0.2353 0.2601 0.2236 0.0190  0.0215  -0.0105 620  ALA B CA  
13503 C C   . ALA B 622  ? 0.2221 0.2481 0.2097 0.0180  0.0212  -0.0080 620  ALA B C   
13504 O O   . ALA B 622  ? 0.2154 0.2404 0.2012 0.0173  0.0193  -0.0079 620  ALA B O   
13505 C CB  . ALA B 622  ? 0.2276 0.2523 0.2214 0.0187  0.0208  -0.0104 620  ALA B CB  
13506 N N   . ALA B 623  ? 0.2120 0.2404 0.2011 0.0180  0.0230  -0.0060 621  ALA B N   
13507 C CA  . ALA B 623  ? 0.2255 0.2547 0.2136 0.0171  0.0228  -0.0034 621  ALA B CA  
13508 C C   . ALA B 623  ? 0.2399 0.2688 0.2221 0.0172  0.0226  -0.0037 621  ALA B C   
13509 O O   . ALA B 623  ? 0.2712 0.2995 0.2519 0.0166  0.0210  -0.0025 621  ALA B O   
13510 C CB  . ALA B 623  ? 0.2416 0.2734 0.2321 0.0168  0.0250  -0.0012 621  ALA B CB  
13511 N N   . ASP B 624  ? 0.2651 0.2943 0.2438 0.0182  0.0241  -0.0053 622  ASP B N   
13512 C CA  . ASP B 624  ? 0.2790 0.3078 0.2516 0.0183  0.0239  -0.0057 622  ASP B CA  
13513 C C   . ASP B 624  ? 0.3067 0.3333 0.2775 0.0177  0.0210  -0.0071 622  ASP B C   
13514 O O   . ASP B 624  ? 0.3918 0.4182 0.3590 0.0172  0.0198  -0.0063 622  ASP B O   
13515 C CB  . ASP B 624  ? 0.3403 0.3692 0.3093 0.0197  0.0259  -0.0078 622  ASP B CB  
13516 C CG  . ASP B 624  ? 0.3835 0.4154 0.3537 0.0203  0.0290  -0.0063 622  ASP B CG  
13517 O OD1 . ASP B 624  ? 0.4664 0.5002 0.4387 0.0194  0.0295  -0.0034 622  ASP B OD1 
13518 O OD2 . ASP B 624  ? 0.4601 0.4925 0.4292 0.0218  0.0309  -0.0080 622  ASP B OD2 
13519 N N   . ALA B 625  ? 0.2847 0.3095 0.2578 0.0178  0.0199  -0.0090 623  ALA B N   
13520 C CA  . ALA B 625  ? 0.3463 0.3694 0.3180 0.0171  0.0174  -0.0103 623  ALA B CA  
13521 C C   . ALA B 625  ? 0.3109 0.3343 0.2861 0.0162  0.0155  -0.0088 623  ALA B C   
13522 O O   . ALA B 625  ? 0.3013 0.3239 0.2757 0.0155  0.0133  -0.0095 623  ALA B O   
13523 C CB  . ALA B 625  ? 0.3995 0.4203 0.3715 0.0175  0.0172  -0.0131 623  ALA B CB  
13524 N N   . ALA B 626  ? 0.2733 0.2978 0.2524 0.0162  0.0162  -0.0066 624  ALA B N   
13525 C CA  . ALA B 626  ? 0.2642 0.2886 0.2467 0.0157  0.0145  -0.0054 624  ALA B CA  
13526 C C   . ALA B 626  ? 0.2625 0.2872 0.2425 0.0153  0.0126  -0.0044 624  ALA B C   
13527 O O   . ALA B 626  ? 0.2617 0.2862 0.2431 0.0150  0.0107  -0.0049 624  ALA B O   
13528 C CB  . ALA B 626  ? 0.2392 0.2642 0.2258 0.0156  0.0155  -0.0034 624  ALA B CB  
13529 N N   . PRO B 627  ? 0.2768 0.3025 0.2533 0.0153  0.0130  -0.0030 625  PRO B N   
13530 C CA  . PRO B 627  ? 0.2764 0.3027 0.2508 0.0150  0.0109  -0.0020 625  PRO B CA  
13531 C C   . PRO B 627  ? 0.2873 0.3134 0.2594 0.0145  0.0091  -0.0042 625  PRO B C   
13532 O O   . PRO B 627  ? 0.2785 0.3053 0.2514 0.0142  0.0070  -0.0037 625  PRO B O   
13533 C CB  . PRO B 627  ? 0.2945 0.3217 0.2648 0.0151  0.0119  -0.0003 625  PRO B CB  
13534 C CG  . PRO B 627  ? 0.3759 0.4033 0.3478 0.0154  0.0145  0.0004  625  PRO B CG  
13535 C CD  . PRO B 627  ? 0.3027 0.3293 0.2773 0.0156  0.0152  -0.0019 625  PRO B CD  
13536 N N   . ASP B 628  ? 0.2614 0.2864 0.2306 0.0144  0.0098  -0.0065 626  ASP B N   
13537 C CA  . ASP B 628  ? 0.2790 0.3033 0.2456 0.0136  0.0080  -0.0085 626  ASP B CA  
13538 C C   . ASP B 628  ? 0.2889 0.3129 0.2596 0.0132  0.0066  -0.0094 626  ASP B C   
13539 O O   . ASP B 628  ? 0.2998 0.3244 0.2700 0.0123  0.0045  -0.0098 626  ASP B O   
13540 C CB  . ASP B 628  ? 0.3133 0.3358 0.2758 0.0137  0.0091  -0.0109 626  ASP B CB  
13541 C CG  . ASP B 628  ? 0.4292 0.4522 0.3865 0.0141  0.0102  -0.0104 626  ASP B CG  
13542 O OD1 . ASP B 628  ? 0.4513 0.4759 0.4071 0.0138  0.0092  -0.0084 626  ASP B OD1 
13543 O OD2 . ASP B 628  ? 0.4675 0.4892 0.4222 0.0148  0.0120  -0.0119 626  ASP B OD2 
13544 N N   . TRP B 629  ? 0.2254 0.2485 0.2000 0.0137  0.0078  -0.0097 627  TRP B N   
13545 C CA  . TRP B 629  ? 0.2133 0.2359 0.1915 0.0132  0.0066  -0.0105 627  TRP B CA  
13546 C C   . TRP B 629  ? 0.2306 0.2550 0.2120 0.0133  0.0054  -0.0085 627  TRP B C   
13547 O O   . TRP B 629  ? 0.2384 0.2635 0.2210 0.0127  0.0037  -0.0089 627  TRP B O   
13548 C CB  . TRP B 629  ? 0.2172 0.2384 0.1984 0.0138  0.0081  -0.0114 627  TRP B CB  
13549 C CG  . TRP B 629  ? 0.1966 0.2172 0.1812 0.0133  0.0069  -0.0121 627  TRP B CG  
13550 C CD1 . TRP B 629  ? 0.2237 0.2444 0.2128 0.0137  0.0072  -0.0113 627  TRP B CD1 
13551 C CD2 . TRP B 629  ? 0.2136 0.2334 0.1972 0.0123  0.0053  -0.0137 627  TRP B CD2 
13552 N NE1 . TRP B 629  ? 0.2238 0.2439 0.2145 0.0131  0.0060  -0.0124 627  TRP B NE1 
13553 C CE2 . TRP B 629  ? 0.2161 0.2358 0.2037 0.0122  0.0048  -0.0137 627  TRP B CE2 
13554 C CE3 . TRP B 629  ? 0.2327 0.2518 0.2122 0.0113  0.0042  -0.0151 627  TRP B CE3 
13555 C CZ2 . TRP B 629  ? 0.2066 0.2258 0.1944 0.0111  0.0034  -0.0149 627  TRP B CZ2 
13556 C CZ3 . TRP B 629  ? 0.2354 0.2538 0.2153 0.0101  0.0026  -0.0163 627  TRP B CZ3 
13557 C CH2 . TRP B 629  ? 0.2432 0.2618 0.2273 0.0100  0.0023  -0.0161 627  TRP B CH2 
13558 N N   . ALA B 630  ? 0.2321 0.2571 0.2146 0.0140  0.0062  -0.0064 628  ALA B N   
13559 C CA  . ALA B 630  ? 0.2341 0.2603 0.2191 0.0144  0.0051  -0.0045 628  ALA B CA  
13560 C C   . ALA B 630  ? 0.2509 0.2790 0.2336 0.0141  0.0031  -0.0040 628  ALA B C   
13561 O O   . ALA B 630  ? 0.2611 0.2905 0.2461 0.0144  0.0017  -0.0033 628  ALA B O   
13562 C CB  . ALA B 630  ? 0.2637 0.2896 0.2495 0.0151  0.0063  -0.0022 628  ALA B CB  
13563 N N   . ALA B 631  ? 0.2411 0.2695 0.2194 0.0136  0.0029  -0.0046 629  ALA B N   
13564 C CA  . ALA B 631  ? 0.2574 0.2878 0.2332 0.0131  0.0009  -0.0040 629  ALA B CA  
13565 C C   . ALA B 631  ? 0.2740 0.3052 0.2502 0.0119  -0.0008 -0.0058 629  ALA B C   
13566 O O   . ALA B 631  ? 0.2779 0.3114 0.2530 0.0114  -0.0028 -0.0053 629  ALA B O   
13567 C CB  . ALA B 631  ? 0.2823 0.3127 0.2528 0.0128  0.0012  -0.0039 629  ALA B CB  
13568 N N   . VAL B 632  ? 0.2457 0.2750 0.2232 0.0114  -0.0002 -0.0078 630  VAL B N   
13569 C CA  . VAL B 632  ? 0.2473 0.2771 0.2253 0.0101  -0.0018 -0.0093 630  VAL B CA  
13570 C C   . VAL B 632  ? 0.2562 0.2883 0.2388 0.0106  -0.0027 -0.0080 630  VAL B C   
13571 O O   . VAL B 632  ? 0.2535 0.2848 0.2394 0.0117  -0.0016 -0.0074 630  VAL B O   
13572 C CB  . VAL B 632  ? 0.2483 0.2751 0.2264 0.0096  -0.0009 -0.0116 630  VAL B CB  
13573 C CG1 . VAL B 632  ? 0.2448 0.2720 0.2236 0.0080  -0.0027 -0.0128 630  VAL B CG1 
13574 C CG2 . VAL B 632  ? 0.2622 0.2866 0.2356 0.0095  0.0001  -0.0129 630  VAL B CG2 
13575 N N   . PRO B 633  ? 0.2196 0.2547 0.2023 0.0099  -0.0047 -0.0075 631  PRO B N   
13576 C CA  . PRO B 633  ? 0.2330 0.2708 0.2199 0.0107  -0.0054 -0.0061 631  PRO B CA  
13577 C C   . PRO B 633  ? 0.2312 0.2676 0.2215 0.0107  -0.0047 -0.0072 631  PRO B C   
13578 O O   . PRO B 633  ? 0.2126 0.2472 0.2021 0.0094  -0.0046 -0.0091 631  PRO B O   
13579 C CB  . PRO B 633  ? 0.2352 0.2767 0.2215 0.0095  -0.0077 -0.0060 631  PRO B CB  
13580 C CG  . PRO B 633  ? 0.2888 0.3297 0.2700 0.0086  -0.0082 -0.0063 631  PRO B CG  
13581 C CD  . PRO B 633  ? 0.2375 0.2740 0.2164 0.0084  -0.0064 -0.0080 631  PRO B CD  
13582 N N   . PRO B 634  ? 0.2175 0.2545 0.2114 0.0122  -0.0042 -0.0061 632  PRO B N   
13583 C CA  . PRO B 634  ? 0.2279 0.2636 0.2249 0.0122  -0.0035 -0.0071 632  PRO B CA  
13584 C C   . PRO B 634  ? 0.1930 0.2300 0.1903 0.0105  -0.0046 -0.0084 632  PRO B C   
13585 O O   . PRO B 634  ? 0.2116 0.2463 0.2094 0.0098  -0.0040 -0.0098 632  PRO B O   
13586 C CB  . PRO B 634  ? 0.2486 0.2854 0.2487 0.0141  -0.0034 -0.0055 632  PRO B CB  
13587 C CG  . PRO B 634  ? 0.2856 0.3224 0.2841 0.0152  -0.0033 -0.0037 632  PRO B CG  
13588 C CD  . PRO B 634  ? 0.2367 0.2746 0.2315 0.0140  -0.0041 -0.0039 632  PRO B CD  
13589 N N   . SER B 635  ? 0.2250 0.2657 0.2222 0.0098  -0.0062 -0.0078 633  SER B N   
13590 C CA  . SER B 635  ? 0.2493 0.2915 0.2470 0.0079  -0.0073 -0.0089 633  SER B CA  
13591 C C   . SER B 635  ? 0.2004 0.2394 0.1946 0.0059  -0.0074 -0.0107 633  SER B C   
13592 O O   . SER B 635  ? 0.2298 0.2677 0.2244 0.0045  -0.0076 -0.0119 633  SER B O   
13593 C CB  . SER B 635  ? 0.2866 0.3341 0.2851 0.0073  -0.0091 -0.0077 633  SER B CB  
13594 O OG  . SER B 635  ? 0.3950 0.4431 0.3901 0.0068  -0.0101 -0.0073 633  SER B OG  
13595 N N   . GLU B 636  ? 0.2106 0.2480 0.2013 0.0059  -0.0073 -0.0109 634  GLU B N   
13596 C CA  . GLU B 636  ? 0.2223 0.2560 0.2092 0.0044  -0.0072 -0.0129 634  GLU B CA  
13597 C C   . GLU B 636  ? 0.2168 0.2464 0.2043 0.0053  -0.0053 -0.0139 634  GLU B C   
13598 O O   . GLU B 636  ? 0.2208 0.2475 0.2068 0.0042  -0.0053 -0.0156 634  GLU B O   
13599 C CB  . GLU B 636  ? 0.2434 0.2767 0.2259 0.0041  -0.0076 -0.0130 634  GLU B CB  
13600 C CG  . GLU B 636  ? 0.3977 0.4268 0.3758 0.0028  -0.0075 -0.0152 634  GLU B CG  
13601 C CD  . GLU B 636  ? 0.4503 0.4785 0.4283 0.0006  -0.0089 -0.0166 634  GLU B CD  
13602 O OE1 . GLU B 636  ? 0.4392 0.4707 0.4179 -0.0011 -0.0108 -0.0160 634  GLU B OE1 
13603 O OE2 . GLU B 636  ? 0.3678 0.3919 0.3450 0.0004  -0.0080 -0.0182 634  GLU B OE2 
13604 N N   . ARG B 637  ? 0.1901 0.2194 0.1796 0.0073  -0.0038 -0.0129 635  ARG B N   
13605 C CA  . ARG B 637  ? 0.1900 0.2161 0.1807 0.0080  -0.0022 -0.0138 635  ARG B CA  
13606 C C   . ARG B 637  ? 0.2018 0.2277 0.1953 0.0074  -0.0026 -0.0144 635  ARG B C   
13607 O O   . ARG B 637  ? 0.1910 0.2140 0.1841 0.0070  -0.0021 -0.0158 635  ARG B O   
13608 C CB  . ARG B 637  ? 0.2043 0.2305 0.1969 0.0099  -0.0008 -0.0123 635  ARG B CB  
13609 C CG  . ARG B 637  ? 0.2002 0.2266 0.1899 0.0104  -0.0003 -0.0115 635  ARG B CG  
13610 C CD  . ARG B 637  ? 0.2053 0.2310 0.1968 0.0119  0.0013  -0.0102 635  ARG B CD  
13611 N NE  . ARG B 637  ? 0.2130 0.2398 0.2079 0.0128  0.0010  -0.0088 635  ARG B NE  
13612 C CZ  . ARG B 637  ? 0.2315 0.2596 0.2269 0.0138  0.0009  -0.0069 635  ARG B CZ  
13613 N NH1 . ARG B 637  ? 0.2715 0.3003 0.2639 0.0138  0.0008  -0.0060 635  ARG B NH1 
13614 N NH2 . ARG B 637  ? 0.2115 0.2397 0.2099 0.0148  0.0009  -0.0059 635  ARG B NH2 
13615 N N   . ALA B 638  ? 0.1794 0.2085 0.1756 0.0074  -0.0034 -0.0133 636  ALA B N   
13616 C CA  . ALA B 638  ? 0.1805 0.2098 0.1790 0.0067  -0.0037 -0.0137 636  ALA B CA  
13617 C C   . ALA B 638  ? 0.1871 0.2156 0.1836 0.0045  -0.0048 -0.0151 636  ALA B C   
13618 O O   . ALA B 638  ? 0.1838 0.2103 0.1809 0.0038  -0.0047 -0.0160 636  ALA B O   
13619 C CB  . ALA B 638  ? 0.1884 0.2219 0.1899 0.0074  -0.0043 -0.0123 636  ALA B CB  
13620 N N   . ALA B 639  ? 0.2073 0.2369 0.2010 0.0032  -0.0061 -0.0152 637  ALA B N   
13621 C CA  . ALA B 639  ? 0.2094 0.2376 0.2007 0.0007  -0.0073 -0.0165 637  ALA B CA  
13622 C C   . ALA B 639  ? 0.2051 0.2279 0.1938 0.0007  -0.0065 -0.0182 637  ALA B C   
13623 O O   . ALA B 639  ? 0.2107 0.2311 0.1985 -0.0009 -0.0071 -0.0193 637  ALA B O   
13624 C CB  . ALA B 639  ? 0.2059 0.2361 0.1943 -0.0007 -0.0089 -0.0163 637  ALA B CB  
13625 N N   . CYS B 640  ? 0.1934 0.2142 0.1810 0.0024  -0.0050 -0.0185 638  CYS B N   
13626 C CA  . CYS B 640  ? 0.1933 0.2093 0.1790 0.0029  -0.0040 -0.0200 638  CYS B CA  
13627 C C   . CYS B 640  ? 0.1630 0.1778 0.1518 0.0033  -0.0034 -0.0202 638  CYS B C   
13628 O O   . CYS B 640  ? 0.1888 0.2001 0.1764 0.0026  -0.0035 -0.0215 638  CYS B O   
13629 C CB  . CYS B 640  ? 0.1956 0.2109 0.1805 0.0049  -0.0023 -0.0199 638  CYS B CB  
13630 S SG  . CYS B 640  ? 0.2435 0.2592 0.2236 0.0046  -0.0028 -0.0200 638  CYS B SG  
13631 N N   . LEU B 641  ? 0.1767 0.1939 0.1694 0.0045  -0.0028 -0.0188 639  LEU B N   
13632 C CA  . LEU B 641  ? 0.1719 0.1880 0.1673 0.0048  -0.0023 -0.0189 639  LEU B CA  
13633 C C   . LEU B 641  ? 0.1840 0.2002 0.1793 0.0028  -0.0036 -0.0193 639  LEU B C   
13634 O O   . LEU B 641  ? 0.1727 0.1859 0.1680 0.0024  -0.0036 -0.0202 639  LEU B O   
13635 C CB  . LEU B 641  ? 0.1787 0.1975 0.1778 0.0062  -0.0017 -0.0175 639  LEU B CB  
13636 C CG  . LEU B 641  ? 0.1866 0.2044 0.1869 0.0081  -0.0002 -0.0171 639  LEU B CG  
13637 C CD1 . LEU B 641  ? 0.2155 0.2332 0.2135 0.0087  0.0005  -0.0170 639  LEU B CD1 
13638 C CD2 . LEU B 641  ? 0.1761 0.1959 0.1796 0.0091  0.0001  -0.0157 639  LEU B CD2 
13639 N N   . ASP B 642  ? 0.1715 0.1911 0.1670 0.0015  -0.0049 -0.0186 640  ASP B N   
13640 C CA  . ASP B 642  ? 0.1719 0.1921 0.1674 -0.0007 -0.0061 -0.0188 640  ASP B CA  
13641 C C   . ASP B 642  ? 0.1843 0.2002 0.1761 -0.0025 -0.0069 -0.0203 640  ASP B C   
13642 O O   . ASP B 642  ? 0.1862 0.2000 0.1778 -0.0038 -0.0074 -0.0208 640  ASP B O   
13643 C CB  . ASP B 642  ? 0.1883 0.2137 0.1849 -0.0018 -0.0073 -0.0176 640  ASP B CB  
13644 C CG  . ASP B 642  ? 0.2428 0.2721 0.2434 -0.0003 -0.0067 -0.0162 640  ASP B CG  
13645 O OD1 . ASP B 642  ? 0.2426 0.2705 0.2450 0.0008  -0.0057 -0.0163 640  ASP B OD1 
13646 O OD2 . ASP B 642  ? 0.2327 0.2665 0.2344 -0.0002 -0.0073 -0.0150 640  ASP B OD2 
13647 N N   . ARG B 643  ? 0.1911 0.2053 0.1794 -0.0025 -0.0070 -0.0211 641  ARG B N   
13648 C CA  . ARG B 643  ? 0.2202 0.2294 0.2044 -0.0038 -0.0077 -0.0227 641  ARG B CA  
13649 C C   . ARG B 643  ? 0.2136 0.2184 0.1979 -0.0025 -0.0065 -0.0237 641  ARG B C   
13650 O O   . ARG B 643  ? 0.2000 0.2009 0.1824 -0.0037 -0.0072 -0.0247 641  ARG B O   
13651 C CB  . ARG B 643  ? 0.2040 0.2122 0.1842 -0.0038 -0.0079 -0.0235 641  ARG B CB  
13652 C CG  . ARG B 643  ? 0.2473 0.2587 0.2262 -0.0062 -0.0099 -0.0230 641  ARG B CG  
13653 C CD  . ARG B 643  ? 0.2857 0.2951 0.2597 -0.0065 -0.0104 -0.0241 641  ARG B CD  
13654 N NE  . ARG B 643  ? 0.2620 0.2728 0.2362 -0.0039 -0.0089 -0.0236 641  ARG B NE  
13655 C CZ  . ARG B 643  ? 0.2710 0.2863 0.2463 -0.0035 -0.0092 -0.0221 641  ARG B CZ  
13656 N NH1 . ARG B 643  ? 0.2867 0.3063 0.2632 -0.0052 -0.0109 -0.0210 641  ARG B NH1 
13657 N NH2 . ARG B 643  ? 0.3189 0.3347 0.2940 -0.0013 -0.0077 -0.0216 641  ARG B NH2 
13658 N N   . ALA B 644  ? 0.1776 0.1827 0.1639 0.0001  -0.0049 -0.0234 642  ALA B N   
13659 C CA  . ALA B 644  ? 0.1963 0.1978 0.1830 0.0015  -0.0038 -0.0241 642  ALA B CA  
13660 C C   . ALA B 644  ? 0.2026 0.2038 0.1917 0.0006  -0.0043 -0.0237 642  ALA B C   
13661 O O   . ALA B 644  ? 0.1952 0.1923 0.1831 0.0005  -0.0044 -0.0246 642  ALA B O   
13662 C CB  . ALA B 644  ? 0.1954 0.1983 0.1845 0.0040  -0.0020 -0.0235 642  ALA B CB  
13663 N N   . ALA B 645  ? 0.1911 0.1965 0.1831 0.0000  -0.0046 -0.0224 643  ALA B N   
13664 C CA  . ALA B 645  ? 0.1971 0.2025 0.1910 -0.0008 -0.0050 -0.0219 643  ALA B CA  
13665 C C   . ALA B 645  ? 0.2015 0.2045 0.1928 -0.0034 -0.0065 -0.0225 643  ALA B C   
13666 O O   . ALA B 645  ? 0.2094 0.2095 0.2007 -0.0039 -0.0067 -0.0228 643  ALA B O   
13667 C CB  . ALA B 645  ? 0.1743 0.1849 0.1717 -0.0007 -0.0049 -0.0205 643  ALA B CB  
13668 N N   . GLU B 646  ? 0.1894 0.1934 0.1786 -0.0053 -0.0076 -0.0227 644  GLU B N   
13669 C CA  . GLU B 646  ? 0.2407 0.2420 0.2270 -0.0082 -0.0092 -0.0232 644  GLU B CA  
13670 C C   . GLU B 646  ? 0.2207 0.2151 0.2036 -0.0077 -0.0091 -0.0248 644  GLU B C   
13671 O O   . GLU B 646  ? 0.2276 0.2186 0.2092 -0.0093 -0.0099 -0.0251 644  GLU B O   
13672 C CB  . GLU B 646  ? 0.2665 0.2699 0.2507 -0.0101 -0.0105 -0.0232 644  GLU B CB  
13673 C CG  . GLU B 646  ? 0.3096 0.3200 0.2971 -0.0109 -0.0109 -0.0216 644  GLU B CG  
13674 C CD  . GLU B 646  ? 0.3967 0.4091 0.3863 -0.0127 -0.0114 -0.0206 644  GLU B CD  
13675 O OE1 . GLU B 646  ? 0.5234 0.5323 0.5108 -0.0151 -0.0125 -0.0211 644  GLU B OE1 
13676 O OE2 . GLU B 646  ? 0.4662 0.4834 0.4597 -0.0117 -0.0107 -0.0193 644  GLU B OE2 
13677 N N   . LEU B 647  ? 0.2228 0.2153 0.2042 -0.0056 -0.0081 -0.0258 645  LEU B N   
13678 C CA  . LEU B 647  ? 0.2493 0.2354 0.2275 -0.0046 -0.0078 -0.0274 645  LEU B CA  
13679 C C   . LEU B 647  ? 0.2299 0.2143 0.2105 -0.0032 -0.0071 -0.0271 645  LEU B C   
13680 O O   . LEU B 647  ? 0.2475 0.2269 0.2260 -0.0036 -0.0077 -0.0279 645  LEU B O   
13681 C CB  . LEU B 647  ? 0.2177 0.2030 0.1941 -0.0023 -0.0066 -0.0283 645  LEU B CB  
13682 C CG  . LEU B 647  ? 0.2343 0.2205 0.2075 -0.0036 -0.0075 -0.0288 645  LEU B CG  
13683 C CD1 . LEU B 647  ? 0.2455 0.2311 0.2170 -0.0011 -0.0060 -0.0296 645  LEU B CD1 
13684 C CD2 . LEU B 647  ? 0.2918 0.2735 0.2605 -0.0063 -0.0093 -0.0300 645  LEU B CD2 
13685 N N   . MET B 648  ? 0.1718 0.1600 0.1565 -0.0014 -0.0059 -0.0261 646  MET B N   
13686 C CA  . MET B 648  ? 0.1931 0.1798 0.1800 -0.0002 -0.0054 -0.0258 646  MET B CA  
13687 C C   . MET B 648  ? 0.2108 0.1968 0.1978 -0.0024 -0.0066 -0.0252 646  MET B C   
13688 O O   . MET B 648  ? 0.2347 0.2171 0.2214 -0.0021 -0.0068 -0.0254 646  MET B O   
13689 C CB  . MET B 648  ? 0.2317 0.2226 0.2227 0.0017  -0.0041 -0.0247 646  MET B CB  
13690 C CG  . MET B 648  ? 0.2407 0.2316 0.2320 0.0042  -0.0027 -0.0252 646  MET B CG  
13691 S SD  . MET B 648  ? 0.2489 0.2435 0.2451 0.0059  -0.0015 -0.0239 646  MET B SD  
13692 C CE  . MET B 648  ? 0.2775 0.2727 0.2735 0.0081  0.0001  -0.0243 646  MET B CE  
13693 N N   . GLN B 649  ? 0.1957 0.1855 0.1835 -0.0046 -0.0074 -0.0243 647  GLN B N   
13694 C CA  . GLN B 649  ? 0.2127 0.2023 0.2006 -0.0069 -0.0084 -0.0235 647  GLN B CA  
13695 C C   . GLN B 649  ? 0.2042 0.1879 0.1880 -0.0088 -0.0097 -0.0244 647  GLN B C   
13696 O O   . GLN B 649  ? 0.2588 0.2393 0.2420 -0.0095 -0.0102 -0.0242 647  GLN B O   
13697 C CB  . GLN B 649  ? 0.2076 0.2028 0.1971 -0.0089 -0.0089 -0.0224 647  GLN B CB  
13698 C CG  . GLN B 649  ? 0.2326 0.2288 0.2227 -0.0113 -0.0098 -0.0213 647  GLN B CG  
13699 C CD  . GLN B 649  ? 0.2333 0.2310 0.2264 -0.0098 -0.0088 -0.0206 647  GLN B CD  
13700 O OE1 . GLN B 649  ? 0.2275 0.2302 0.2237 -0.0087 -0.0080 -0.0197 647  GLN B OE1 
13701 N NE2 . GLN B 649  ? 0.2448 0.2380 0.2369 -0.0096 -0.0089 -0.0208 647  GLN B NE2 
13702 N N   . ALA B 650  ? 0.2193 0.2012 0.1998 -0.0097 -0.0103 -0.0255 648  ALA B N   
13703 C CA  . ALA B 650  ? 0.2375 0.2132 0.2135 -0.0117 -0.0117 -0.0265 648  ALA B CA  
13704 C C   . ALA B 650  ? 0.2665 0.2359 0.2406 -0.0095 -0.0112 -0.0276 648  ALA B C   
13705 O O   . ALA B 650  ? 0.2997 0.2636 0.2711 -0.0108 -0.0123 -0.0280 648  ALA B O   
13706 C CB  . ALA B 650  ? 0.2687 0.2439 0.2413 -0.0130 -0.0126 -0.0275 648  ALA B CB  
13707 N N   . ARG B 651  ? 0.2361 0.2063 0.2118 -0.0061 -0.0096 -0.0281 649  ARG B N   
13708 C CA  . ARG B 651  ? 0.2397 0.2048 0.2141 -0.0035 -0.0090 -0.0291 649  ARG B CA  
13709 C C   . ARG B 651  ? 0.2450 0.2110 0.2230 -0.0019 -0.0083 -0.0281 649  ARG B C   
13710 O O   . ARG B 651  ? 0.2576 0.2206 0.2356 0.0006  -0.0076 -0.0287 649  ARG B O   
13711 C CB  . ARG B 651  ? 0.2460 0.2114 0.2196 -0.0009 -0.0076 -0.0303 649  ARG B CB  
13712 C CG  . ARG B 651  ? 0.2651 0.2284 0.2342 -0.0026 -0.0085 -0.0314 649  ARG B CG  
13713 C CD  . ARG B 651  ? 0.2894 0.2540 0.2577 -0.0003 -0.0071 -0.0324 649  ARG B CD  
13714 N NE  . ARG B 651  ? 0.3017 0.2656 0.2661 -0.0023 -0.0082 -0.0332 649  ARG B NE  
13715 C CZ  . ARG B 651  ? 0.3167 0.2818 0.2794 -0.0010 -0.0073 -0.0339 649  ARG B CZ  
13716 N NH1 . ARG B 651  ? 0.2816 0.2486 0.2463 0.0021  -0.0053 -0.0339 649  ARG B NH1 
13717 N NH2 . ARG B 651  ? 0.3160 0.2807 0.2750 -0.0032 -0.0086 -0.0346 649  ARG B NH2 
13718 N N   . MET B 652  ? 0.2389 0.2091 0.2199 -0.0033 -0.0085 -0.0266 650  MET B N   
13719 C CA  . MET B 652  ? 0.2313 0.2025 0.2154 -0.0020 -0.0080 -0.0257 650  MET B CA  
13720 C C   . MET B 652  ? 0.2559 0.2211 0.2382 -0.0012 -0.0086 -0.0261 650  MET B C   
13721 O O   . MET B 652  ? 0.2595 0.2246 0.2438 0.0014  -0.0078 -0.0261 650  MET B O   
13722 C CB  . MET B 652  ? 0.2305 0.2063 0.2171 -0.0040 -0.0084 -0.0242 650  MET B CB  
13723 C CG  . MET B 652  ? 0.2270 0.2035 0.2163 -0.0028 -0.0080 -0.0233 650  MET B CG  
13724 S SD  . MET B 652  ? 0.2704 0.2521 0.2621 -0.0048 -0.0083 -0.0217 650  MET B SD  
13725 C CE  . MET B 652  ? 0.2501 0.2380 0.2447 -0.0035 -0.0071 -0.0215 650  MET B CE  
13726 N N   . PRO B 653  ? 0.2478 0.2080 0.2265 -0.0032 -0.0100 -0.0264 651  PRO B N   
13727 C CA  . PRO B 653  ? 0.2783 0.2325 0.2553 -0.0022 -0.0105 -0.0266 651  PRO B CA  
13728 C C   . PRO B 653  ? 0.2650 0.2164 0.2414 0.0015  -0.0095 -0.0279 651  PRO B C   
13729 O O   . PRO B 653  ? 0.2763 0.2266 0.2543 0.0037  -0.0092 -0.0276 651  PRO B O   
13730 C CB  . PRO B 653  ? 0.2834 0.2323 0.2558 -0.0052 -0.0122 -0.0269 651  PRO B CB  
13731 C CG  . PRO B 653  ? 0.2974 0.2515 0.2710 -0.0085 -0.0126 -0.0259 651  PRO B CG  
13732 C CD  . PRO B 653  ? 0.2692 0.2290 0.2454 -0.0069 -0.0113 -0.0262 651  PRO B CD  
13733 N N   . THR B 654  ? 0.2623 0.2130 0.2367 0.0021  -0.0090 -0.0293 652  THR B N   
13734 C CA  . THR B 654  ? 0.2783 0.2271 0.2523 0.0057  -0.0078 -0.0306 652  THR B CA  
13735 C C   . THR B 654  ? 0.2714 0.2261 0.2504 0.0082  -0.0062 -0.0298 652  THR B C   
13736 O O   . THR B 654  ? 0.2679 0.2217 0.2484 0.0110  -0.0054 -0.0300 652  THR B O   
13737 C CB  . THR B 654  ? 0.2964 0.2437 0.2668 0.0057  -0.0075 -0.0322 652  THR B CB  
13738 O OG1 . THR B 654  ? 0.3048 0.2461 0.2702 0.0031  -0.0092 -0.0329 652  THR B OG1 
13739 C CG2 . THR B 654  ? 0.2966 0.2421 0.2663 0.0095  -0.0060 -0.0335 652  THR B CG2 
13740 N N   . LEU B 655  ? 0.2191 0.1797 0.2008 0.0071  -0.0056 -0.0290 653  LEU B N   
13741 C CA  . LEU B 655  ? 0.2416 0.2075 0.2279 0.0091  -0.0043 -0.0282 653  LEU B CA  
13742 C C   . LEU B 655  ? 0.2400 0.2060 0.2290 0.0097  -0.0047 -0.0271 653  LEU B C   
13743 O O   . LEU B 655  ? 0.2465 0.2142 0.2384 0.0121  -0.0038 -0.0269 653  LEU B O   
13744 C CB  . LEU B 655  ? 0.2322 0.2037 0.2206 0.0075  -0.0040 -0.0273 653  LEU B CB  
13745 C CG  . LEU B 655  ? 0.2599 0.2319 0.2457 0.0067  -0.0038 -0.0281 653  LEU B CG  
13746 C CD1 . LEU B 655  ? 0.2576 0.2353 0.2458 0.0055  -0.0036 -0.0271 653  LEU B CD1 
13747 C CD2 . LEU B 655  ? 0.2973 0.2684 0.2821 0.0094  -0.0025 -0.0292 653  LEU B CD2 
13748 N N   . LEU B 656  ? 0.2483 0.2127 0.2365 0.0075  -0.0060 -0.0264 654  LEU B N   
13749 C CA  . LEU B 656  ? 0.2720 0.2363 0.2623 0.0080  -0.0065 -0.0254 654  LEU B CA  
13750 C C   . LEU B 656  ? 0.2431 0.2033 0.2328 0.0106  -0.0065 -0.0260 654  LEU B C   
13751 O O   . LEU B 656  ? 0.2745 0.2365 0.2673 0.0125  -0.0062 -0.0253 654  LEU B O   
13752 C CB  . LEU B 656  ? 0.2930 0.2550 0.2813 0.0051  -0.0080 -0.0246 654  LEU B CB  
13753 C CG  . LEU B 656  ? 0.3087 0.2748 0.2976 0.0024  -0.0082 -0.0239 654  LEU B CG  
13754 C CD1 . LEU B 656  ? 0.3059 0.2701 0.2934 -0.0001 -0.0095 -0.0229 654  LEU B CD1 
13755 C CD2 . LEU B 656  ? 0.2885 0.2606 0.2815 0.0033  -0.0071 -0.0232 654  LEU B CD2 
13756 N N   . GLY B 657  ? 0.2629 0.2175 0.2486 0.0108  -0.0070 -0.0271 655  GLY B N   
13757 C CA  . GLY B 657  ? 0.2867 0.2372 0.2716 0.0136  -0.0069 -0.0277 655  GLY B CA  
13758 C C   . GLY B 657  ? 0.2887 0.2427 0.2767 0.0169  -0.0053 -0.0280 655  GLY B C   
13759 O O   . GLY B 657  ? 0.2815 0.2358 0.2719 0.0192  -0.0051 -0.0275 655  GLY B O   
13760 N N   . LEU B 658  ? 0.2485 0.2058 0.2369 0.0170  -0.0040 -0.0286 656  LEU B N   
13761 C CA  . LEU B 658  ? 0.2291 0.1903 0.2207 0.0198  -0.0023 -0.0287 656  LEU B CA  
13762 C C   . LEU B 658  ? 0.2349 0.2014 0.2316 0.0200  -0.0021 -0.0272 656  LEU B C   
13763 O O   . LEU B 658  ? 0.2314 0.1996 0.2310 0.0224  -0.0015 -0.0269 656  LEU B O   
13764 C CB  . LEU B 658  ? 0.2309 0.1942 0.2212 0.0196  -0.0010 -0.0296 656  LEU B CB  
13765 C CG  . LEU B 658  ? 0.2530 0.2203 0.2461 0.0223  0.0009  -0.0296 656  LEU B CG  
13766 C CD1 . LEU B 658  ? 0.2438 0.2083 0.2363 0.0257  0.0016  -0.0305 656  LEU B CD1 
13767 C CD2 . LEU B 658  ? 0.2530 0.2220 0.2442 0.0218  0.0019  -0.0303 656  LEU B CD2 
13768 N N   . ILE B 659  ? 0.2047 0.1740 0.2025 0.0174  -0.0026 -0.0263 657  ILE B N   
13769 C CA  . ILE B 659  ? 0.1910 0.1650 0.1932 0.0174  -0.0025 -0.0250 657  ILE B CA  
13770 C C   . ILE B 659  ? 0.1985 0.1708 0.2018 0.0182  -0.0036 -0.0243 657  ILE B C   
13771 O O   . ILE B 659  ? 0.2252 0.2005 0.2322 0.0196  -0.0033 -0.0236 657  ILE B O   
13772 C CB  . ILE B 659  ? 0.2093 0.1859 0.2118 0.0147  -0.0029 -0.0243 657  ILE B CB  
13773 C CG1 . ILE B 659  ? 0.2278 0.2068 0.2298 0.0144  -0.0018 -0.0247 657  ILE B CG1 
13774 C CG2 . ILE B 659  ? 0.2221 0.2021 0.2282 0.0146  -0.0031 -0.0231 657  ILE B CG2 
13775 C CD1 . ILE B 659  ? 0.2269 0.2075 0.2281 0.0118  -0.0024 -0.0243 657  ILE B CD1 
13776 N N   . ILE B 660  ? 0.2171 0.1847 0.2174 0.0172  -0.0049 -0.0244 658  ILE B N   
13777 C CA  . ILE B 660  ? 0.1991 0.1647 0.2000 0.0178  -0.0061 -0.0236 658  ILE B CA  
13778 C C   . ILE B 660  ? 0.2266 0.1918 0.2292 0.0212  -0.0056 -0.0239 658  ILE B C   
13779 O O   . ILE B 660  ? 0.2495 0.2168 0.2552 0.0224  -0.0059 -0.0230 658  ILE B O   
13780 C CB  . ILE B 660  ? 0.2330 0.1928 0.2296 0.0161  -0.0075 -0.0236 658  ILE B CB  
13781 C CG1 . ILE B 660  ? 0.2358 0.1973 0.2318 0.0128  -0.0081 -0.0229 658  ILE B CG1 
13782 C CG2 . ILE B 660  ? 0.2511 0.2074 0.2475 0.0176  -0.0087 -0.0231 658  ILE B CG2 
13783 C CD1 . ILE B 660  ? 0.2806 0.2369 0.2724 0.0105  -0.0094 -0.0229 658  ILE B CD1 
13784 N N   . ARG B 661  ? 0.2055 0.1683 0.2060 0.0229  -0.0047 -0.0251 659  ARG B N   
13785 C CA  . ARG B 661  ? 0.2149 0.1770 0.2166 0.0264  -0.0041 -0.0255 659  ARG B CA  
13786 C C   . ARG B 661  ? 0.2506 0.2187 0.2565 0.0281  -0.0024 -0.0253 659  ARG B C   
13787 O O   . ARG B 661  ? 0.2368 0.2068 0.2458 0.0306  -0.0022 -0.0248 659  ARG B O   
13788 C CB  . ARG B 661  ? 0.2273 0.1834 0.2243 0.0277  -0.0039 -0.0271 659  ARG B CB  
13789 C CG  . ARG B 661  ? 0.2558 0.2053 0.2491 0.0267  -0.0058 -0.0270 659  ARG B CG  
13790 C CD  . ARG B 661  ? 0.3092 0.2519 0.2973 0.0277  -0.0057 -0.0286 659  ARG B CD  
13791 N NE  . ARG B 661  ? 0.2799 0.2222 0.2687 0.0319  -0.0045 -0.0296 659  ARG B NE  
13792 C CZ  . ARG B 661  ? 0.3186 0.2604 0.3054 0.0333  -0.0030 -0.0312 659  ARG B CZ  
13793 N NH1 . ARG B 661  ? 0.3454 0.2874 0.3298 0.0309  -0.0026 -0.0319 659  ARG B NH1 
13794 N NH2 . ARG B 661  ? 0.3000 0.2411 0.2872 0.0374  -0.0018 -0.0320 659  ARG B NH2 
13795 N N   . GLU B 662  ? 0.2338 0.2054 0.2403 0.0269  -0.0013 -0.0255 660  GLU B N   
13796 C CA  . GLU B 662  ? 0.2288 0.2060 0.2391 0.0283  0.0004  -0.0252 660  GLU B CA  
13797 C C   . GLU B 662  ? 0.2449 0.2269 0.2597 0.0273  -0.0001 -0.0237 660  GLU B C   
13798 O O   . GLU B 662  ? 0.2418 0.2278 0.2605 0.0288  0.0006  -0.0230 660  GLU B O   
13799 C CB  . GLU B 662  ? 0.2521 0.2306 0.2607 0.0275  0.0017  -0.0259 660  GLU B CB  
13800 C CG  . GLU B 662  ? 0.2595 0.2436 0.2717 0.0289  0.0036  -0.0255 660  GLU B CG  
13801 C CD  . GLU B 662  ? 0.2703 0.2558 0.2807 0.0281  0.0049  -0.0261 660  GLU B CD  
13802 O OE1 . GLU B 662  ? 0.2633 0.2475 0.2712 0.0257  0.0042  -0.0263 660  GLU B OE1 
13803 O OE2 . GLU B 662  ? 0.2586 0.2469 0.2702 0.0299  0.0067  -0.0262 660  GLU B OE2 
13804 N N   . ALA B 663  ? 0.1960 0.1777 0.2102 0.0246  -0.0013 -0.0231 661  ALA B N   
13805 C CA  . ALA B 663  ? 0.2082 0.1942 0.2260 0.0234  -0.0016 -0.0219 661  ALA B CA  
13806 C C   . ALA B 663  ? 0.2261 0.2110 0.2446 0.0228  -0.0033 -0.0211 661  ALA B C   
13807 O O   . ALA B 663  ? 0.3207 0.3083 0.3413 0.0215  -0.0038 -0.0203 661  ALA B O   
13808 C CB  . ALA B 663  ? 0.2371 0.2248 0.2542 0.0212  -0.0011 -0.0219 661  ALA B CB  
13809 N N   . GLY B 664  ? 0.2495 0.2301 0.2657 0.0235  -0.0044 -0.0213 662  GLY B N   
13810 C CA  . GLY B 664  ? 0.2829 0.2625 0.2995 0.0229  -0.0061 -0.0204 662  GLY B CA  
13811 C C   . GLY B 664  ? 0.2689 0.2476 0.2836 0.0200  -0.0070 -0.0200 662  GLY B C   
13812 O O   . GLY B 664  ? 0.2937 0.2731 0.3093 0.0193  -0.0081 -0.0191 662  GLY B O   
13813 N N   . LYS B 665  ? 0.2297 0.2073 0.2417 0.0184  -0.0065 -0.0206 663  LYS B N   
13814 C CA  . LYS B 665  ? 0.2268 0.2044 0.2373 0.0158  -0.0071 -0.0203 663  LYS B CA  
13815 C C   . LYS B 665  ? 0.2091 0.1819 0.2160 0.0147  -0.0083 -0.0201 663  LYS B C   
13816 O O   . LYS B 665  ? 0.2133 0.1822 0.2178 0.0154  -0.0084 -0.0207 663  LYS B O   
13817 C CB  . LYS B 665  ? 0.2304 0.2097 0.2401 0.0146  -0.0060 -0.0208 663  LYS B CB  
13818 C CG  . LYS B 665  ? 0.2934 0.2770 0.3062 0.0154  -0.0047 -0.0209 663  LYS B CG  
13819 C CD  . LYS B 665  ? 0.3357 0.3223 0.3514 0.0151  -0.0051 -0.0200 663  LYS B CD  
13820 C CE  . LYS B 665  ? 0.3444 0.3349 0.3629 0.0157  -0.0039 -0.0199 663  LYS B CE  
13821 N NZ  . LYS B 665  ? 0.3730 0.3660 0.3943 0.0154  -0.0044 -0.0191 663  LYS B NZ  
13822 N N   . SER B 666  ? 0.2372 0.2104 0.2435 0.0129  -0.0092 -0.0193 664  SER B N   
13823 C CA  . SER B 666  ? 0.2379 0.2072 0.2406 0.0111  -0.0102 -0.0190 664  SER B CA  
13824 C C   . SER B 666  ? 0.2658 0.2349 0.2664 0.0091  -0.0097 -0.0196 664  SER B C   
13825 O O   . SER B 666  ? 0.2382 0.2107 0.2401 0.0090  -0.0086 -0.0200 664  SER B O   
13826 C CB  . SER B 666  ? 0.2907 0.2612 0.2935 0.0096  -0.0111 -0.0179 664  SER B CB  
13827 O OG  . SER B 666  ? 0.3086 0.2830 0.3123 0.0082  -0.0103 -0.0180 664  SER B OG  
13828 N N   . ALA B 667  ? 0.2398 0.2048 0.2369 0.0075  -0.0105 -0.0194 665  ALA B N   
13829 C CA  . ALA B 667  ? 0.2473 0.2121 0.2422 0.0053  -0.0103 -0.0198 665  ALA B CA  
13830 C C   . ALA B 667  ? 0.2534 0.2234 0.2500 0.0038  -0.0097 -0.0194 665  ALA B C   
13831 O O   . ALA B 667  ? 0.2239 0.1962 0.2207 0.0033  -0.0089 -0.0199 665  ALA B O   
13832 C CB  . ALA B 667  ? 0.2714 0.2312 0.2625 0.0033  -0.0116 -0.0193 665  ALA B CB  
13833 N N   . LEU B 668  ? 0.2480 0.2199 0.2454 0.0031  -0.0100 -0.0184 666  LEU B N   
13834 C CA  . LEU B 668  ? 0.2839 0.2605 0.2826 0.0019  -0.0094 -0.0181 666  LEU B CA  
13835 C C   . LEU B 668  ? 0.2323 0.2126 0.2340 0.0035  -0.0082 -0.0187 666  LEU B C   
13836 O O   . LEU B 668  ? 0.2463 0.2297 0.2486 0.0028  -0.0075 -0.0188 666  LEU B O   
13837 C CB  . LEU B 668  ? 0.2978 0.2754 0.2966 0.0012  -0.0098 -0.0171 666  LEU B CB  
13838 C CG  . LEU B 668  ? 0.3778 0.3539 0.3738 -0.0013 -0.0105 -0.0162 666  LEU B CG  
13839 C CD1 . LEU B 668  ? 0.4235 0.4009 0.4195 -0.0017 -0.0108 -0.0152 666  LEU B CD1 
13840 C CD2 . LEU B 668  ? 0.3744 0.3532 0.3700 -0.0033 -0.0099 -0.0162 666  LEU B CD2 
13841 N N   . ASN B 669  ? 0.2221 0.2022 0.2257 0.0057  -0.0081 -0.0189 667  ASN B N   
13842 C CA  . ASN B 669  ? 0.2408 0.2244 0.2472 0.0069  -0.0071 -0.0192 667  ASN B CA  
13843 C C   . ASN B 669  ? 0.2625 0.2459 0.2686 0.0075  -0.0063 -0.0200 667  ASN B C   
13844 O O   . ASN B 669  ? 0.2521 0.2386 0.2596 0.0078  -0.0054 -0.0202 667  ASN B O   
13845 C CB  . ASN B 669  ? 0.3142 0.2983 0.3231 0.0086  -0.0073 -0.0190 667  ASN B CB  
13846 C CG  . ASN B 669  ? 0.3519 0.3370 0.3611 0.0079  -0.0080 -0.0183 667  ASN B CG  
13847 O OD1 . ASN B 669  ? 0.4019 0.3889 0.4106 0.0067  -0.0077 -0.0181 667  ASN B OD1 
13848 N ND2 . ASN B 669  ? 0.3688 0.3525 0.3784 0.0087  -0.0089 -0.0179 667  ASN B ND2 
13849 N N   . ALA B 670  ? 0.1994 0.1790 0.2032 0.0077  -0.0066 -0.0205 668  ALA B N   
13850 C CA  . ALA B 670  ? 0.2148 0.1939 0.2174 0.0080  -0.0059 -0.0215 668  ALA B CA  
13851 C C   . ALA B 670  ? 0.2104 0.1910 0.2116 0.0058  -0.0059 -0.0214 668  ALA B C   
13852 O O   . ALA B 670  ? 0.2034 0.1861 0.2049 0.0060  -0.0051 -0.0219 668  ALA B O   
13853 C CB  . ALA B 670  ? 0.2205 0.1946 0.2205 0.0088  -0.0064 -0.0221 668  ALA B CB  
13854 N N   . ILE B 671  ? 0.2162 0.1961 0.2159 0.0037  -0.0068 -0.0208 669  ILE B N   
13855 C CA  . ILE B 671  ? 0.1911 0.1734 0.1901 0.0016  -0.0068 -0.0206 669  ILE B CA  
13856 C C   . ILE B 671  ? 0.1862 0.1737 0.1880 0.0022  -0.0059 -0.0203 669  ILE B C   
13857 O O   . ILE B 671  ? 0.2164 0.2063 0.2183 0.0018  -0.0054 -0.0204 669  ILE B O   
13858 C CB  . ILE B 671  ? 0.1961 0.1775 0.1935 -0.0007 -0.0078 -0.0198 669  ILE B CB  
13859 C CG1 . ILE B 671  ? 0.2282 0.2040 0.2221 -0.0018 -0.0088 -0.0201 669  ILE B CG1 
13860 C CG2 . ILE B 671  ? 0.2306 0.2160 0.2282 -0.0027 -0.0076 -0.0192 669  ILE B CG2 
13861 C CD1 . ILE B 671  ? 0.2630 0.2370 0.2552 -0.0039 -0.0098 -0.0190 669  ILE B CD1 
13862 N N   . ALA B 672  ? 0.2030 0.1919 0.2069 0.0031  -0.0057 -0.0198 670  ALA B N   
13863 C CA  . ALA B 672  ? 0.2306 0.2235 0.2368 0.0038  -0.0049 -0.0195 670  ALA B CA  
13864 C C   . ALA B 672  ? 0.2126 0.2066 0.2200 0.0053  -0.0041 -0.0200 670  ALA B C   
13865 O O   . ALA B 672  ? 0.2154 0.2123 0.2237 0.0053  -0.0035 -0.0198 670  ALA B O   
13866 C CB  . ALA B 672  ? 0.2374 0.2307 0.2452 0.0046  -0.0051 -0.0191 670  ALA B CB  
13867 N N   . GLU B 673  ? 0.1989 0.1906 0.2063 0.0066  -0.0039 -0.0205 671  GLU B N   
13868 C CA  . GLU B 673  ? 0.2184 0.2111 0.2269 0.0080  -0.0030 -0.0209 671  GLU B CA  
13869 C C   . GLU B 673  ? 0.2185 0.2117 0.2251 0.0072  -0.0028 -0.0213 671  GLU B C   
13870 O O   . GLU B 673  ? 0.2086 0.2045 0.2162 0.0075  -0.0020 -0.0211 671  GLU B O   
13871 C CB  . GLU B 673  ? 0.2404 0.2305 0.2489 0.0095  -0.0029 -0.0214 671  GLU B CB  
13872 C CG  . GLU B 673  ? 0.2488 0.2402 0.2585 0.0111  -0.0018 -0.0216 671  GLU B CG  
13873 C CD  . GLU B 673  ? 0.2823 0.2766 0.2954 0.0120  -0.0012 -0.0209 671  GLU B CD  
13874 O OE1 . GLU B 673  ? 0.2847 0.2794 0.2992 0.0117  -0.0019 -0.0204 671  GLU B OE1 
13875 O OE2 . GLU B 673  ? 0.2376 0.2338 0.2518 0.0128  -0.0002 -0.0209 671  GLU B OE2 
13876 N N   . VAL B 674  ? 0.1793 0.1697 0.1830 0.0060  -0.0035 -0.0218 672  VAL B N   
13877 C CA  . VAL B 674  ? 0.1924 0.1831 0.1941 0.0050  -0.0035 -0.0222 672  VAL B CA  
13878 C C   . VAL B 674  ? 0.1790 0.1736 0.1814 0.0036  -0.0036 -0.0215 672  VAL B C   
13879 O O   . VAL B 674  ? 0.1826 0.1795 0.1850 0.0036  -0.0032 -0.0214 672  VAL B O   
13880 C CB  . VAL B 674  ? 0.1892 0.1755 0.1873 0.0038  -0.0044 -0.0229 672  VAL B CB  
13881 C CG1 . VAL B 674  ? 0.1913 0.1779 0.1871 0.0026  -0.0046 -0.0235 672  VAL B CG1 
13882 C CG2 . VAL B 674  ? 0.2216 0.2041 0.2191 0.0056  -0.0042 -0.0237 672  VAL B CG2 
13883 N N   . ARG B 675  ? 0.1743 0.1699 0.1774 0.0025  -0.0041 -0.0208 673  ARG B N   
13884 C CA  . ARG B 675  ? 0.1718 0.1714 0.1759 0.0015  -0.0041 -0.0200 673  ARG B CA  
13885 C C   . ARG B 675  ? 0.1721 0.1749 0.1786 0.0032  -0.0032 -0.0197 673  ARG B C   
13886 O O   . ARG B 675  ? 0.1772 0.1830 0.1840 0.0030  -0.0030 -0.0194 673  ARG B O   
13887 C CB  . ARG B 675  ? 0.1792 0.1796 0.1838 0.0005  -0.0045 -0.0193 673  ARG B CB  
13888 C CG  . ARG B 675  ? 0.1988 0.1968 0.2010 -0.0017 -0.0055 -0.0193 673  ARG B CG  
13889 C CD  . ARG B 675  ? 0.1770 0.1768 0.1798 -0.0027 -0.0056 -0.0184 673  ARG B CD  
13890 N NE  . ARG B 675  ? 0.1929 0.1977 0.1970 -0.0032 -0.0052 -0.0178 673  ARG B NE  
13891 C CZ  . ARG B 675  ? 0.1954 0.2032 0.2007 -0.0033 -0.0048 -0.0171 673  ARG B CZ  
13892 N NH1 . ARG B 675  ? 0.2037 0.2098 0.2087 -0.0031 -0.0049 -0.0169 673  ARG B NH1 
13893 N NH2 . ARG B 675  ? 0.1925 0.2050 0.1990 -0.0034 -0.0044 -0.0166 673  ARG B NH2 
13894 N N   . GLU B 676  ? 0.1581 0.1601 0.1662 0.0048  -0.0027 -0.0197 674  GLU B N   
13895 C CA  . GLU B 676  ? 0.1692 0.1736 0.1794 0.0062  -0.0019 -0.0194 674  GLU B CA  
13896 C C   . GLU B 676  ? 0.1713 0.1762 0.1809 0.0067  -0.0013 -0.0195 674  GLU B C   
13897 O O   . GLU B 676  ? 0.1780 0.1856 0.1885 0.0071  -0.0010 -0.0190 674  GLU B O   
13898 C CB  . GLU B 676  ? 0.2075 0.2107 0.2194 0.0074  -0.0016 -0.0193 674  GLU B CB  
13899 C CG  . GLU B 676  ? 0.2177 0.2228 0.2316 0.0086  -0.0010 -0.0189 674  GLU B CG  
13900 C CD  . GLU B 676  ? 0.3022 0.3086 0.3169 0.0085  -0.0012 -0.0185 674  GLU B CD  
13901 O OE1 . GLU B 676  ? 0.3705 0.3772 0.3843 0.0075  -0.0016 -0.0184 674  GLU B OE1 
13902 O OE2 . GLU B 676  ? 0.2975 0.3046 0.3137 0.0094  -0.0008 -0.0182 674  GLU B OE2 
13903 N N   . ALA B 677  ? 0.1626 0.1651 0.1707 0.0069  -0.0013 -0.0203 675  ALA B N   
13904 C CA  . ALA B 677  ? 0.1763 0.1793 0.1834 0.0074  -0.0007 -0.0205 675  ALA B CA  
13905 C C   . ALA B 677  ? 0.1607 0.1657 0.1664 0.0060  -0.0013 -0.0203 675  ALA B C   
13906 O O   . ALA B 677  ? 0.1719 0.1792 0.1779 0.0065  -0.0009 -0.0199 675  ALA B O   
13907 C CB  . ALA B 677  ? 0.1784 0.1781 0.1836 0.0078  -0.0006 -0.0215 675  ALA B CB  
13908 N N   . ILE B 678  ? 0.1625 0.1667 0.1667 0.0043  -0.0023 -0.0205 676  ILE B N   
13909 C CA  . ILE B 678  ? 0.1637 0.1702 0.1668 0.0027  -0.0030 -0.0202 676  ILE B CA  
13910 C C   . ILE B 678  ? 0.1527 0.1636 0.1583 0.0032  -0.0027 -0.0192 676  ILE B C   
13911 O O   . ILE B 678  ? 0.1689 0.1825 0.1744 0.0032  -0.0028 -0.0187 676  ILE B O   
13912 C CB  . ILE B 678  ? 0.1663 0.1714 0.1679 0.0005  -0.0041 -0.0204 676  ILE B CB  
13913 C CG1 . ILE B 678  ? 0.1861 0.1865 0.1846 0.0000  -0.0045 -0.0215 676  ILE B CG1 
13914 C CG2 . ILE B 678  ? 0.1834 0.1923 0.1849 -0.0013 -0.0048 -0.0197 676  ILE B CG2 
13915 C CD1 . ILE B 678  ? 0.1847 0.1821 0.1818 -0.0018 -0.0055 -0.0216 676  ILE B CD1 
13916 N N   . ASP B 679  ? 0.1597 0.1711 0.1673 0.0038  -0.0024 -0.0187 677  ASP B N   
13917 C CA  . ASP B 679  ? 0.1732 0.1881 0.1827 0.0046  -0.0021 -0.0179 677  ASP B CA  
13918 C C   . ASP B 679  ? 0.1630 0.1788 0.1736 0.0063  -0.0013 -0.0175 677  ASP B C   
13919 O O   . ASP B 679  ? 0.1659 0.1847 0.1772 0.0068  -0.0013 -0.0168 677  ASP B O   
13920 C CB  . ASP B 679  ? 0.1734 0.1881 0.1843 0.0049  -0.0019 -0.0177 677  ASP B CB  
13921 C CG  . ASP B 679  ? 0.2063 0.2213 0.2163 0.0030  -0.0026 -0.0176 677  ASP B CG  
13922 O OD1 . ASP B 679  ? 0.2213 0.2384 0.2305 0.0015  -0.0031 -0.0174 677  ASP B OD1 
13923 O OD2 . ASP B 679  ? 0.2156 0.2288 0.2257 0.0029  -0.0026 -0.0178 677  ASP B OD2 
13924 N N   . PHE B 680  ? 0.1574 0.1707 0.1681 0.0073  -0.0008 -0.0179 678  PHE B N   
13925 C CA  . PHE B 680  ? 0.1578 0.1719 0.1693 0.0087  -0.0001 -0.0174 678  PHE B CA  
13926 C C   . PHE B 680  ? 0.1567 0.1722 0.1665 0.0083  -0.0002 -0.0172 678  PHE B C   
13927 O O   . PHE B 680  ? 0.1605 0.1783 0.1709 0.0090  -0.0001 -0.0164 678  PHE B O   
13928 C CB  . PHE B 680  ? 0.1433 0.1550 0.1551 0.0095  0.0006  -0.0178 678  PHE B CB  
13929 C CG  . PHE B 680  ? 0.1650 0.1758 0.1789 0.0102  0.0009  -0.0175 678  PHE B CG  
13930 C CD1 . PHE B 680  ? 0.1669 0.1790 0.1823 0.0109  0.0010  -0.0168 678  PHE B CD1 
13931 C CD2 . PHE B 680  ? 0.1895 0.1981 0.2037 0.0103  0.0009  -0.0181 678  PHE B CD2 
13932 C CE1 . PHE B 680  ? 0.1819 0.1928 0.1989 0.0114  0.0011  -0.0167 678  PHE B CE1 
13933 C CE2 . PHE B 680  ? 0.2075 0.2155 0.2237 0.0108  0.0009  -0.0179 678  PHE B CE2 
13934 C CZ  . PHE B 680  ? 0.1810 0.1901 0.1984 0.0112  0.0009  -0.0173 678  PHE B CZ  
13935 N N   . LEU B 681  ? 0.1536 0.1676 0.1611 0.0072  -0.0006 -0.0181 679  LEU B N   
13936 C CA  . LEU B 681  ? 0.1316 0.1468 0.1371 0.0067  -0.0010 -0.0180 679  LEU B CA  
13937 C C   . LEU B 681  ? 0.1625 0.1815 0.1687 0.0061  -0.0017 -0.0172 679  LEU B C   
13938 O O   . LEU B 681  ? 0.1753 0.1965 0.1815 0.0067  -0.0017 -0.0164 679  LEU B O   
13939 C CB  . LEU B 681  ? 0.1479 0.1604 0.1505 0.0053  -0.0016 -0.0192 679  LEU B CB  
13940 C CG  . LEU B 681  ? 0.1559 0.1650 0.1576 0.0064  -0.0007 -0.0201 679  LEU B CG  
13941 C CD1 . LEU B 681  ? 0.1699 0.1755 0.1689 0.0053  -0.0013 -0.0214 679  LEU B CD1 
13942 C CD2 . LEU B 681  ? 0.1879 0.1977 0.1885 0.0074  0.0001  -0.0200 679  LEU B CD2 
13943 N N   . ARG B 682  ? 0.1479 0.1679 0.1548 0.0049  -0.0024 -0.0171 680  ARG B N   
13944 C CA  . ARG B 682  ? 0.1283 0.1525 0.1359 0.0042  -0.0031 -0.0163 680  ARG B CA  
13945 C C   . ARG B 682  ? 0.1545 0.1812 0.1646 0.0061  -0.0025 -0.0153 680  ARG B C   
13946 O O   . ARG B 682  ? 0.1660 0.1963 0.1767 0.0064  -0.0028 -0.0144 680  ARG B O   
13947 C CB  . ARG B 682  ? 0.1516 0.1764 0.1592 0.0023  -0.0038 -0.0164 680  ARG B CB  
13948 C CG  . ARG B 682  ? 0.1635 0.1857 0.1682 0.0002  -0.0047 -0.0173 680  ARG B CG  
13949 C CD  . ARG B 682  ? 0.1726 0.1951 0.1773 -0.0018 -0.0054 -0.0173 680  ARG B CD  
13950 N NE  . ARG B 682  ? 0.2029 0.2231 0.2047 -0.0042 -0.0065 -0.0180 680  ARG B NE  
13951 C CZ  . ARG B 682  ? 0.2048 0.2230 0.2056 -0.0062 -0.0072 -0.0182 680  ARG B CZ  
13952 N NH1 . ARG B 682  ? 0.2016 0.2203 0.2041 -0.0061 -0.0068 -0.0177 680  ARG B NH1 
13953 N NH2 . ARG B 682  ? 0.2410 0.2564 0.2388 -0.0083 -0.0083 -0.0189 680  ARG B NH2 
13954 N N   . TYR B 683  ? 0.1498 0.1746 0.1612 0.0073  -0.0017 -0.0154 681  TYR B N   
13955 C CA  . TYR B 683  ? 0.1628 0.1892 0.1761 0.0092  -0.0012 -0.0146 681  TYR B CA  
13956 C C   . TYR B 683  ? 0.1642 0.1907 0.1774 0.0104  -0.0008 -0.0139 681  TYR B C   
13957 O O   . TYR B 683  ? 0.1699 0.1990 0.1838 0.0115  -0.0010 -0.0129 681  TYR B O   
13958 C CB  . TYR B 683  ? 0.1445 0.1684 0.1589 0.0099  -0.0006 -0.0150 681  TYR B CB  
13959 C CG  . TYR B 683  ? 0.1591 0.1835 0.1750 0.0117  -0.0001 -0.0143 681  TYR B CG  
13960 C CD1 . TYR B 683  ? 0.1711 0.1982 0.1880 0.0124  -0.0002 -0.0139 681  TYR B CD1 
13961 C CD2 . TYR B 683  ? 0.1686 0.1907 0.1848 0.0128  0.0004  -0.0141 681  TYR B CD2 
13962 C CE1 . TYR B 683  ? 0.1737 0.2006 0.1915 0.0143  0.0003  -0.0135 681  TYR B CE1 
13963 C CE2 . TYR B 683  ? 0.1699 0.1917 0.1871 0.0144  0.0007  -0.0136 681  TYR B CE2 
13964 C CZ  . TYR B 683  ? 0.1684 0.1924 0.1863 0.0153  0.0006  -0.0134 681  TYR B CZ  
13965 O OH  . TYR B 683  ? 0.1960 0.2192 0.2145 0.0171  0.0009  -0.0129 681  TYR B OH  
13966 N N   . TYR B 684  ? 0.1374 0.1611 0.1495 0.0105  -0.0004 -0.0143 682  TYR B N   
13967 C CA  . TYR B 684  ? 0.1479 0.1717 0.1596 0.0115  0.0000  -0.0135 682  TYR B CA  
13968 C C   . TYR B 684  ? 0.1576 0.1841 0.1679 0.0110  -0.0007 -0.0130 682  TYR B C   
13969 O O   . TYR B 684  ? 0.1716 0.1994 0.1819 0.0121  -0.0007 -0.0119 682  TYR B O   
13970 C CB  . TYR B 684  ? 0.1519 0.1729 0.1630 0.0117  0.0008  -0.0139 682  TYR B CB  
13971 C CG  . TYR B 684  ? 0.1618 0.1806 0.1747 0.0123  0.0014  -0.0141 682  TYR B CG  
13972 C CD1 . TYR B 684  ? 0.1767 0.1958 0.1913 0.0132  0.0014  -0.0135 682  TYR B CD1 
13973 C CD2 . TYR B 684  ? 0.1529 0.1695 0.1657 0.0119  0.0018  -0.0150 682  TYR B CD2 
13974 C CE1 . TYR B 684  ? 0.1725 0.1894 0.1884 0.0135  0.0017  -0.0137 682  TYR B CE1 
13975 C CE2 . TYR B 684  ? 0.1470 0.1620 0.1615 0.0123  0.0021  -0.0151 682  TYR B CE2 
13976 C CZ  . TYR B 684  ? 0.1775 0.1926 0.1934 0.0130  0.0020  -0.0144 682  TYR B CZ  
13977 O OH  . TYR B 684  ? 0.1727 0.1860 0.1901 0.0131  0.0021  -0.0146 682  TYR B OH  
13978 N N   . ALA B 685  ? 0.1676 0.1946 0.1764 0.0093  -0.0015 -0.0137 683  ALA B N   
13979 C CA  . ALA B 685  ? 0.1619 0.1918 0.1694 0.0086  -0.0025 -0.0133 683  ALA B CA  
13980 C C   . ALA B 685  ? 0.1676 0.2015 0.1770 0.0093  -0.0030 -0.0121 683  ALA B C   
13981 O O   . ALA B 685  ? 0.1802 0.2165 0.1895 0.0101  -0.0033 -0.0110 683  ALA B O   
13982 C CB  . ALA B 685  ? 0.1505 0.1798 0.1559 0.0063  -0.0034 -0.0143 683  ALA B CB  
13983 N N   . GLU B 686  ? 0.1702 0.2052 0.1815 0.0092  -0.0029 -0.0122 684  GLU B N   
13984 C CA  . GLU B 686  ? 0.1762 0.2154 0.1896 0.0102  -0.0032 -0.0111 684  GLU B CA  
13985 C C   . GLU B 686  ? 0.1896 0.2284 0.2041 0.0128  -0.0025 -0.0102 684  GLU B C   
13986 O O   . GLU B 686  ? 0.1815 0.2233 0.1967 0.0140  -0.0029 -0.0091 684  GLU B O   
13987 C CB  . GLU B 686  ? 0.2168 0.2573 0.2317 0.0097  -0.0031 -0.0115 684  GLU B CB  
13988 C CG  . GLU B 686  ? 0.2463 0.2912 0.2635 0.0112  -0.0031 -0.0104 684  GLU B CG  
13989 C CD  . GLU B 686  ? 0.3123 0.3625 0.3299 0.0107  -0.0042 -0.0094 684  GLU B CD  
13990 O OE1 . GLU B 686  ? 0.2824 0.3330 0.2984 0.0086  -0.0051 -0.0096 684  GLU B OE1 
13991 O OE2 . GLU B 686  ? 0.3200 0.3740 0.3396 0.0125  -0.0041 -0.0084 684  GLU B OE2 
13992 N N   . GLN B 687  ? 0.1592 0.1940 0.1738 0.0136  -0.0016 -0.0106 685  GLN B N   
13993 C CA  . GLN B 687  ? 0.1811 0.2149 0.1965 0.0158  -0.0011 -0.0097 685  GLN B CA  
13994 C C   . GLN B 687  ? 0.1736 0.2078 0.1877 0.0162  -0.0013 -0.0087 685  GLN B C   
13995 O O   . GLN B 687  ? 0.1836 0.2189 0.1982 0.0180  -0.0014 -0.0075 685  GLN B O   
13996 C CB  . GLN B 687  ? 0.1781 0.2076 0.1938 0.0161  -0.0002 -0.0103 685  GLN B CB  
13997 C CG  . GLN B 687  ? 0.1861 0.2151 0.2029 0.0160  0.0000  -0.0112 685  GLN B CG  
13998 C CD  . GLN B 687  ? 0.2308 0.2621 0.2488 0.0177  -0.0001 -0.0106 685  GLN B CD  
13999 O OE1 . GLN B 687  ? 0.2322 0.2626 0.2506 0.0195  0.0001  -0.0099 685  GLN B OE1 
14000 N NE2 . GLN B 687  ? 0.2447 0.2791 0.2634 0.0171  -0.0003 -0.0109 685  GLN B NE2 
14001 N N   . THR B 688  ? 0.1473 0.1806 0.1595 0.0148  -0.0015 -0.0092 686  THR B N   
14002 C CA  . THR B 688  ? 0.1752 0.2092 0.1857 0.0150  -0.0017 -0.0083 686  THR B CA  
14003 C C   . THR B 688  ? 0.1605 0.1989 0.1711 0.0152  -0.0029 -0.0073 686  THR B C   
14004 O O   . THR B 688  ? 0.1916 0.2311 0.2021 0.0166  -0.0032 -0.0059 686  THR B O   
14005 C CB  . THR B 688  ? 0.1570 0.1893 0.1650 0.0134  -0.0017 -0.0093 686  THR B CB  
14006 O OG1 . THR B 688  ? 0.1819 0.2106 0.1900 0.0136  -0.0005 -0.0098 686  THR B OG1 
14007 C CG2 . THR B 688  ? 0.1890 0.2225 0.1947 0.0134  -0.0021 -0.0084 686  THR B CG2 
14008 N N   . ARG B 689  ? 0.1547 0.1957 0.1656 0.0138  -0.0037 -0.0079 687  ARG B N   
14009 C CA  . ARG B 689  ? 0.1788 0.2248 0.1903 0.0138  -0.0049 -0.0069 687  ARG B CA  
14010 C C   . ARG B 689  ? 0.1843 0.2327 0.1983 0.0162  -0.0048 -0.0057 687  ARG B C   
14011 O O   . ARG B 689  ? 0.2084 0.2605 0.2229 0.0171  -0.0057 -0.0044 687  ARG B O   
14012 C CB  . ARG B 689  ? 0.1873 0.2358 0.1991 0.0115  -0.0058 -0.0077 687  ARG B CB  
14013 C CG  . ARG B 689  ? 0.2198 0.2665 0.2285 0.0091  -0.0064 -0.0088 687  ARG B CG  
14014 C CD  . ARG B 689  ? 0.2249 0.2742 0.2337 0.0066  -0.0075 -0.0093 687  ARG B CD  
14015 N NE  . ARG B 689  ? 0.2392 0.2875 0.2496 0.0061  -0.0069 -0.0100 687  ARG B NE  
14016 C CZ  . ARG B 689  ? 0.2747 0.3190 0.2836 0.0047  -0.0066 -0.0114 687  ARG B CZ  
14017 N NH1 . ARG B 689  ? 0.2253 0.2661 0.2311 0.0037  -0.0068 -0.0123 687  ARG B NH1 
14018 N NH2 . ARG B 689  ? 0.2309 0.2746 0.2413 0.0044  -0.0061 -0.0118 687  ARG B NH2 
14019 N N   . ARG B 690  ? 0.1637 0.2099 0.1792 0.0174  -0.0038 -0.0061 688  ARG B N   
14020 C CA  . ARG B 690  ? 0.1677 0.2152 0.1851 0.0200  -0.0035 -0.0052 688  ARG B CA  
14021 C C   . ARG B 690  ? 0.1892 0.2340 0.2060 0.0221  -0.0032 -0.0041 688  ARG B C   
14022 O O   . ARG B 690  ? 0.1919 0.2380 0.2099 0.0245  -0.0033 -0.0030 688  ARG B O   
14023 C CB  . ARG B 690  ? 0.1828 0.2285 0.2016 0.0205  -0.0026 -0.0062 688  ARG B CB  
14024 C CG  . ARG B 690  ? 0.2061 0.2548 0.2258 0.0188  -0.0028 -0.0070 688  ARG B CG  
14025 C CD  . ARG B 690  ? 0.2381 0.2930 0.2598 0.0198  -0.0033 -0.0060 688  ARG B CD  
14026 N NE  . ARG B 690  ? 0.2802 0.3352 0.3034 0.0228  -0.0026 -0.0055 688  ARG B NE  
14027 C CZ  . ARG B 690  ? 0.3035 0.3602 0.3273 0.0253  -0.0028 -0.0042 688  ARG B CZ  
14028 N NH1 . ARG B 690  ? 0.2985 0.3577 0.3219 0.0251  -0.0039 -0.0031 688  ARG B NH1 
14029 N NH2 . ARG B 690  ? 0.2464 0.3021 0.2711 0.0282  -0.0021 -0.0041 688  ARG B NH2 
14030 N N   . THR B 691  ? 0.1817 0.2227 0.1966 0.0213  -0.0028 -0.0042 689  THR B N   
14031 C CA  . THR B 691  ? 0.2042 0.2418 0.2186 0.0231  -0.0023 -0.0031 689  THR B CA  
14032 C C   . THR B 691  ? 0.2223 0.2592 0.2346 0.0227  -0.0025 -0.0021 689  THR B C   
14033 O O   . THR B 691  ? 0.2456 0.2818 0.2575 0.0244  -0.0027 -0.0005 689  THR B O   
14034 C CB  . THR B 691  ? 0.1955 0.2284 0.2103 0.0229  -0.0013 -0.0041 689  THR B CB  
14035 O OG1 . THR B 691  ? 0.2193 0.2508 0.2330 0.0207  -0.0009 -0.0052 689  THR B OG1 
14036 C CG2 . THR B 691  ? 0.2134 0.2465 0.2299 0.0237  -0.0010 -0.0049 689  THR B CG2 
14037 N N   . LEU B 692  ? 0.1984 0.2347 0.2089 0.0207  -0.0024 -0.0028 690  LEU B N   
14038 C CA  . LEU B 692  ? 0.2002 0.2347 0.2085 0.0205  -0.0021 -0.0020 690  LEU B CA  
14039 C C   . LEU B 692  ? 0.2088 0.2462 0.2154 0.0207  -0.0032 -0.0007 690  LEU B C   
14040 O O   . LEU B 692  ? 0.2517 0.2925 0.2578 0.0197  -0.0042 -0.0011 690  LEU B O   
14041 C CB  . LEU B 692  ? 0.1932 0.2257 0.2000 0.0185  -0.0014 -0.0034 690  LEU B CB  
14042 C CG  . LEU B 692  ? 0.2323 0.2616 0.2406 0.0184  -0.0003 -0.0044 690  LEU B CG  
14043 C CD1 . LEU B 692  ? 0.2463 0.2738 0.2530 0.0170  0.0005  -0.0054 690  LEU B CD1 
14044 C CD2 . LEU B 692  ? 0.2262 0.2529 0.2355 0.0198  0.0003  -0.0032 690  LEU B CD2 
14045 N N   . GLY B 693  ? 0.2305 0.2666 0.2361 0.0220  -0.0031 0.0011  691  GLY B N   
14046 C CA  . GLY B 693  ? 0.2317 0.2702 0.2355 0.0225  -0.0042 0.0026  691  GLY B CA  
14047 C C   . GLY B 693  ? 0.2542 0.2900 0.2553 0.0222  -0.0035 0.0036  691  GLY B C   
14048 O O   . GLY B 693  ? 0.2687 0.3013 0.2696 0.0215  -0.0021 0.0031  691  GLY B O   
14049 N N   . PRO B 694  ? 0.3142 0.3517 0.3134 0.0227  -0.0044 0.0053  692  PRO B N   
14050 C CA  . PRO B 694  ? 0.3054 0.3408 0.3014 0.0222  -0.0037 0.0064  692  PRO B CA  
14051 C C   . PRO B 694  ? 0.3249 0.3561 0.3214 0.0230  -0.0024 0.0075  692  PRO B C   
14052 O O   . PRO B 694  ? 0.3586 0.3878 0.3533 0.0219  -0.0012 0.0076  692  PRO B O   
14053 C CB  . PRO B 694  ? 0.3268 0.3651 0.3209 0.0230  -0.0053 0.0082  692  PRO B CB  
14054 C CG  . PRO B 694  ? 0.3749 0.4161 0.3719 0.0246  -0.0066 0.0086  692  PRO B CG  
14055 C CD  . PRO B 694  ? 0.3132 0.3549 0.3127 0.0237  -0.0061 0.0063  692  PRO B CD  
14056 N N   . GLY B 695  ? 0.3004 0.3303 0.2992 0.0247  -0.0026 0.0082  693  GLY B N   
14057 C CA  . GLY B 695  ? 0.3189 0.3444 0.3181 0.0252  -0.0017 0.0093  693  GLY B CA  
14058 C C   . GLY B 695  ? 0.2962 0.3191 0.2970 0.0241  -0.0004 0.0077  693  GLY B C   
14059 O O   . GLY B 695  ? 0.3561 0.3754 0.3573 0.0242  0.0004  0.0086  693  GLY B O   
14060 N N   . HIS B 696  ? 0.2667 0.2912 0.2686 0.0230  -0.0001 0.0055  694  HIS B N   
14061 C CA  . HIS B 696  ? 0.2388 0.2610 0.2422 0.0219  0.0010  0.0040  694  HIS B CA  
14062 C C   . HIS B 696  ? 0.2378 0.2603 0.2396 0.0203  0.0020  0.0033  694  HIS B C   
14063 O O   . HIS B 696  ? 0.2887 0.3125 0.2904 0.0193  0.0021  0.0015  694  HIS B O   
14064 C CB  . HIS B 696  ? 0.2303 0.2539 0.2360 0.0220  0.0005  0.0021  694  HIS B CB  
14065 C CG  . HIS B 696  ? 0.2313 0.2557 0.2383 0.0239  -0.0004 0.0027  694  HIS B CG  
14066 N ND1 . HIS B 696  ? 0.2372 0.2656 0.2447 0.0244  -0.0014 0.0023  694  HIS B ND1 
14067 C CD2 . HIS B 696  ? 0.2543 0.2761 0.2622 0.0256  -0.0005 0.0037  694  HIS B CD2 
14068 C CE1 . HIS B 696  ? 0.2468 0.2753 0.2556 0.0265  -0.0020 0.0031  694  HIS B CE1 
14069 N NE2 . HIS B 696  ? 0.2700 0.2943 0.2789 0.0273  -0.0014 0.0038  694  HIS B NE2 
14070 N N   . GLY B 697  ? 0.2880 0.3090 0.2883 0.0200  0.0028  0.0048  695  GLY B N   
14071 C CA  . GLY B 697  ? 0.2799 0.3013 0.2784 0.0187  0.0040  0.0044  695  GLY B CA  
14072 C C   . GLY B 697  ? 0.2481 0.2683 0.2485 0.0178  0.0052  0.0029  695  GLY B C   
14073 O O   . GLY B 697  ? 0.2559 0.2742 0.2588 0.0179  0.0053  0.0028  695  GLY B O   
14074 N N   . PRO B 698  ? 0.2688 0.2902 0.2679 0.0169  0.0060  0.0016  696  PRO B N   
14075 C CA  . PRO B 698  ? 0.2429 0.2634 0.2438 0.0162  0.0071  0.0001  696  PRO B CA  
14076 C C   . PRO B 698  ? 0.2251 0.2444 0.2271 0.0159  0.0085  0.0016  696  PRO B C   
14077 O O   . PRO B 698  ? 0.2466 0.2657 0.2471 0.0159  0.0089  0.0036  696  PRO B O   
14078 C CB  . PRO B 698  ? 0.2680 0.2898 0.2664 0.0158  0.0076  -0.0014 696  PRO B CB  
14079 C CG  . PRO B 698  ? 0.3416 0.3645 0.3366 0.0159  0.0075  -0.0001 696  PRO B CG  
14080 C CD  . PRO B 698  ? 0.3111 0.3342 0.3067 0.0166  0.0059  0.0013  696  PRO B CD  
14081 N N   . LEU B 699  ? 0.2172 0.2357 0.2218 0.0154  0.0091  0.0006  697  LEU B N   
14082 C CA  . LEU B 699  ? 0.1941 0.2121 0.2000 0.0147  0.0105  0.0018  697  LEU B CA  
14083 C C   . LEU B 699  ? 0.2166 0.2365 0.2205 0.0144  0.0121  0.0019  697  LEU B C   
14084 O O   . LEU B 699  ? 0.2346 0.2548 0.2381 0.0140  0.0132  0.0037  697  LEU B O   
14085 C CB  . LEU B 699  ? 0.2174 0.2345 0.2266 0.0143  0.0106  0.0007  697  LEU B CB  
14086 C CG  . LEU B 699  ? 0.2412 0.2563 0.2523 0.0146  0.0092  0.0005  697  LEU B CG  
14087 C CD1 . LEU B 699  ? 0.2489 0.2634 0.2629 0.0140  0.0093  -0.0007 697  LEU B CD1 
14088 C CD2 . LEU B 699  ? 0.2989 0.3119 0.3099 0.0146  0.0088  0.0027  697  LEU B CD2 
14089 N N   . GLY B 700  ? 0.2032 0.2241 0.2058 0.0147  0.0123  -0.0001 698  GLY B N   
14090 C CA  . GLY B 700  ? 0.2235 0.2460 0.2245 0.0147  0.0140  -0.0005 698  GLY B CA  
14091 C C   . GLY B 700  ? 0.2011 0.2236 0.2039 0.0148  0.0145  -0.0027 698  GLY B C   
14092 O O   . GLY B 700  ? 0.1887 0.2101 0.1931 0.0148  0.0133  -0.0039 698  GLY B O   
14093 N N   . PRO B 701  ? 0.1981 0.2220 0.2006 0.0150  0.0163  -0.0030 699  PRO B N   
14094 C CA  . PRO B 701  ? 0.1870 0.2108 0.1911 0.0155  0.0168  -0.0050 699  PRO B CA  
14095 C C   . PRO B 701  ? 0.2006 0.2237 0.2091 0.0151  0.0160  -0.0049 699  PRO B C   
14096 O O   . PRO B 701  ? 0.2090 0.2325 0.2201 0.0144  0.0164  -0.0032 699  PRO B O   
14097 C CB  . PRO B 701  ? 0.2014 0.2274 0.2052 0.0159  0.0191  -0.0046 699  PRO B CB  
14098 C CG  . PRO B 701  ? 0.2323 0.2590 0.2324 0.0158  0.0197  -0.0033 699  PRO B CG  
14099 C CD  . PRO B 701  ? 0.2170 0.2425 0.2176 0.0150  0.0181  -0.0015 699  PRO B CD  
14100 N N   . ILE B 702  ? 0.1809 0.2027 0.1900 0.0153  0.0149  -0.0067 700  ILE B N   
14101 C CA  A ILE B 702  ? 0.1628 0.1838 0.1756 0.0149  0.0141  -0.0069 700  ILE B CA  
14102 C CA  B ILE B 702  ? 0.1635 0.1844 0.1763 0.0149  0.0140  -0.0070 700  ILE B CA  
14103 C C   . ILE B 702  ? 0.1871 0.2084 0.2012 0.0155  0.0147  -0.0084 700  ILE B C   
14104 O O   . ILE B 702  ? 0.1830 0.2038 0.1949 0.0162  0.0148  -0.0101 700  ILE B O   
14105 C CB  A ILE B 702  ? 0.1640 0.1832 0.1766 0.0147  0.0121  -0.0076 700  ILE B CB  
14106 C CB  B ILE B 702  ? 0.1643 0.1835 0.1768 0.0148  0.0121  -0.0077 700  ILE B CB  
14107 C CG1 A ILE B 702  ? 0.1881 0.2070 0.2004 0.0144  0.0115  -0.0058 700  ILE B CG1 
14108 C CG1 B ILE B 702  ? 0.1903 0.2093 0.2015 0.0146  0.0114  -0.0062 700  ILE B CG1 
14109 C CG2 A ILE B 702  ? 0.1794 0.1976 0.1951 0.0145  0.0114  -0.0083 700  ILE B CG2 
14110 C CG2 B ILE B 702  ? 0.1801 0.1983 0.1959 0.0144  0.0113  -0.0080 700  ILE B CG2 
14111 C CD1 A ILE B 702  ? 0.2067 0.2243 0.2189 0.0145  0.0098  -0.0062 700  ILE B CD1 
14112 C CD1 B ILE B 702  ? 0.1886 0.2072 0.2017 0.0141  0.0117  -0.0042 700  ILE B CD1 
14113 N N   . VAL B 703  ? 0.1609 0.1832 0.1787 0.0152  0.0151  -0.0077 701  VAL B N   
14114 C CA  . VAL B 703  ? 0.1548 0.1776 0.1745 0.0159  0.0156  -0.0089 701  VAL B CA  
14115 C C   . VAL B 703  ? 0.1665 0.1874 0.1878 0.0156  0.0139  -0.0098 701  VAL B C   
14116 O O   . VAL B 703  ? 0.1701 0.1904 0.1934 0.0147  0.0129  -0.0089 701  VAL B O   
14117 C CB  . VAL B 703  ? 0.1638 0.1894 0.1868 0.0157  0.0170  -0.0075 701  VAL B CB  
14118 C CG1 . VAL B 703  ? 0.1869 0.2133 0.2127 0.0164  0.0171  -0.0085 701  VAL B CG1 
14119 C CG2 . VAL B 703  ? 0.1747 0.2025 0.1959 0.0161  0.0190  -0.0067 701  VAL B CG2 
14120 N N   . CYS B 704  ? 0.1484 0.1681 0.1685 0.0163  0.0134  -0.0116 702  CYS B N   
14121 C CA  . CYS B 704  ? 0.1526 0.1704 0.1737 0.0160  0.0118  -0.0125 702  CYS B CA  
14122 C C   . CYS B 704  ? 0.1711 0.1892 0.1944 0.0167  0.0120  -0.0132 702  CYS B C   
14123 O O   . CYS B 704  ? 0.1533 0.1713 0.1752 0.0178  0.0128  -0.0144 702  CYS B O   
14124 C CB  . CYS B 704  ? 0.1610 0.1768 0.1788 0.0160  0.0108  -0.0139 702  CYS B CB  
14125 S SG  . CYS B 704  ? 0.1858 0.2016 0.2012 0.0153  0.0102  -0.0131 702  CYS B SG  
14126 N N   . ILE B 705  ? 0.1534 0.1719 0.1800 0.0161  0.0113  -0.0126 703  ILE B N   
14127 C CA  . ILE B 705  ? 0.1457 0.1651 0.1750 0.0167  0.0114  -0.0129 703  ILE B CA  
14128 C C   . ILE B 705  ? 0.1625 0.1797 0.1922 0.0163  0.0096  -0.0137 703  ILE B C   
14129 O O   . ILE B 705  ? 0.1619 0.1783 0.1923 0.0152  0.0086  -0.0131 703  ILE B O   
14130 C CB  . ILE B 705  ? 0.1653 0.1876 0.1983 0.0162  0.0121  -0.0113 703  ILE B CB  
14131 C CG1 . ILE B 705  ? 0.1914 0.2162 0.2238 0.0168  0.0142  -0.0105 703  ILE B CG1 
14132 C CG2 . ILE B 705  ? 0.1502 0.1735 0.1863 0.0167  0.0117  -0.0115 703  ILE B CG2 
14133 C CD1 . ILE B 705  ? 0.1964 0.2242 0.2322 0.0158  0.0149  -0.0085 703  ILE B CD1 
14134 N N   . SER B 706  ? 0.1581 0.1741 0.1873 0.0172  0.0093  -0.0149 704  SER B N   
14135 C CA  . SER B 706  ? 0.1899 0.2035 0.2185 0.0167  0.0076  -0.0157 704  SER B CA  
14136 C C   . SER B 706  ? 0.1708 0.1845 0.2017 0.0174  0.0071  -0.0159 704  SER B C   
14137 O O   . SER B 706  ? 0.1814 0.1969 0.2139 0.0186  0.0081  -0.0158 704  SER B O   
14138 C CB  . SER B 706  ? 0.1820 0.1932 0.2067 0.0169  0.0074  -0.0170 704  SER B CB  
14139 O OG  . SER B 706  ? 0.1717 0.1827 0.1950 0.0182  0.0084  -0.0178 704  SER B OG  
14140 N N   . PRO B 707  ? 0.1591 0.1713 0.1904 0.0167  0.0056  -0.0161 705  PRO B N   
14141 C CA  . PRO B 707  ? 0.1932 0.2055 0.2266 0.0172  0.0047  -0.0162 705  PRO B CA  
14142 C C   . PRO B 707  ? 0.1900 0.1998 0.2211 0.0183  0.0044  -0.0174 705  PRO B C   
14143 O O   . PRO B 707  ? 0.2075 0.2153 0.2354 0.0181  0.0045  -0.0182 705  PRO B O   
14144 C CB  . PRO B 707  ? 0.1851 0.1963 0.2190 0.0158  0.0032  -0.0159 705  PRO B CB  
14145 C CG  . PRO B 707  ? 0.1747 0.1840 0.2054 0.0151  0.0030  -0.0164 705  PRO B CG  
14146 C CD  . PRO B 707  ? 0.1836 0.1941 0.2133 0.0155  0.0045  -0.0162 705  PRO B CD  
14147 N N   . TRP B 708  ? 0.1706 0.1806 0.2036 0.0192  0.0039  -0.0174 706  TRP B N   
14148 C CA  . TRP B 708  ? 0.1773 0.1845 0.2081 0.0204  0.0036  -0.0184 706  TRP B CA  
14149 C C   . TRP B 708  ? 0.1992 0.2032 0.2278 0.0192  0.0020  -0.0188 706  TRP B C   
14150 O O   . TRP B 708  ? 0.1978 0.1988 0.2235 0.0195  0.0016  -0.0197 706  TRP B O   
14151 C CB  . TRP B 708  ? 0.1807 0.1891 0.2141 0.0222  0.0036  -0.0182 706  TRP B CB  
14152 C CG  . TRP B 708  ? 0.1969 0.2055 0.2325 0.0215  0.0019  -0.0175 706  TRP B CG  
14153 C CD1 . TRP B 708  ? 0.2101 0.2219 0.2494 0.0207  0.0015  -0.0164 706  TRP B CD1 
14154 C CD2 . TRP B 708  ? 0.1990 0.2044 0.2330 0.0212  0.0002  -0.0179 706  TRP B CD2 
14155 N NE1 . TRP B 708  ? 0.2114 0.2222 0.2513 0.0201  -0.0004 -0.0162 706  TRP B NE1 
14156 C CE2 . TRP B 708  ? 0.1903 0.1972 0.2269 0.0204  -0.0011 -0.0170 706  TRP B CE2 
14157 C CE3 . TRP B 708  ? 0.2031 0.2045 0.2334 0.0214  -0.0003 -0.0188 706  TRP B CE3 
14158 C CZ2 . TRP B 708  ? 0.1925 0.1971 0.2281 0.0200  -0.0028 -0.0170 706  TRP B CZ2 
14159 C CZ3 . TRP B 708  ? 0.2252 0.2243 0.2547 0.0208  -0.0020 -0.0186 706  TRP B CZ3 
14160 C CH2 . TRP B 708  ? 0.2091 0.2099 0.2412 0.0202  -0.0032 -0.0178 706  TRP B CH2 
14161 N N   . ASN B 709  ? 0.1929 0.1973 0.2225 0.0178  0.0009  -0.0182 707  ASN B N   
14162 C CA  . ASN B 709  ? 0.2023 0.2043 0.2305 0.0170  -0.0006 -0.0184 707  ASN B CA  
14163 C C   . ASN B 709  ? 0.2193 0.2192 0.2441 0.0158  -0.0008 -0.0190 707  ASN B C   
14164 O O   . ASN B 709  ? 0.2412 0.2388 0.2641 0.0153  -0.0018 -0.0193 707  ASN B O   
14165 C CB  . ASN B 709  ? 0.2024 0.2055 0.2328 0.0161  -0.0017 -0.0177 707  ASN B CB  
14166 C CG  . ASN B 709  ? 0.1985 0.2025 0.2287 0.0149  -0.0015 -0.0174 707  ASN B CG  
14167 O OD1 . ASN B 709  ? 0.2478 0.2538 0.2793 0.0149  -0.0004 -0.0170 707  ASN B OD1 
14168 N ND2 . ASN B 709  ? 0.2041 0.2067 0.2326 0.0138  -0.0024 -0.0176 707  ASN B ND2 
14169 N N   . PHE B 710  ? 0.1992 0.2003 0.2233 0.0154  0.0001  -0.0190 708  PHE B N   
14170 C CA  . PHE B 710  ? 0.2248 0.2246 0.2459 0.0144  0.0001  -0.0195 708  PHE B CA  
14171 C C   . PHE B 710  ? 0.2094 0.2093 0.2292 0.0152  0.0013  -0.0200 708  PHE B C   
14172 O O   . PHE B 710  ? 0.2080 0.2097 0.2277 0.0149  0.0020  -0.0197 708  PHE B O   
14173 C CB  . PHE B 710  ? 0.1889 0.1900 0.2101 0.0133  -0.0001 -0.0190 708  PHE B CB  
14174 C CG  . PHE B 710  ? 0.2124 0.2132 0.2344 0.0126  -0.0011 -0.0187 708  PHE B CG  
14175 C CD1 . PHE B 710  ? 0.2260 0.2249 0.2469 0.0123  -0.0021 -0.0190 708  PHE B CD1 
14176 C CD2 . PHE B 710  ? 0.2453 0.2475 0.2687 0.0123  -0.0012 -0.0182 708  PHE B CD2 
14177 C CE1 . PHE B 710  ? 0.2660 0.2646 0.2871 0.0117  -0.0031 -0.0187 708  PHE B CE1 
14178 C CE2 . PHE B 710  ? 0.2527 0.2543 0.2763 0.0118  -0.0022 -0.0181 708  PHE B CE2 
14179 C CZ  . PHE B 710  ? 0.2613 0.2612 0.2837 0.0115  -0.0031 -0.0183 708  PHE B CZ  
14180 N N   . PRO B 711  ? 0.2108 0.2087 0.2293 0.0162  0.0014  -0.0207 709  PRO B N   
14181 C CA  . PRO B 711  ? 0.2088 0.2071 0.2265 0.0174  0.0027  -0.0212 709  PRO B CA  
14182 C C   . PRO B 711  ? 0.2139 0.2114 0.2284 0.0166  0.0030  -0.0218 709  PRO B C   
14183 O O   . PRO B 711  ? 0.1956 0.1938 0.2092 0.0175  0.0042  -0.0221 709  PRO B O   
14184 C CB  . PRO B 711  ? 0.2216 0.2174 0.2387 0.0189  0.0025  -0.0219 709  PRO B CB  
14185 C CG  . PRO B 711  ? 0.2170 0.2100 0.2326 0.0178  0.0009  -0.0220 709  PRO B CG  
14186 C CD  . PRO B 711  ? 0.2109 0.2060 0.2286 0.0164  0.0003  -0.0210 709  PRO B CD  
14187 N N   . LEU B 712  ? 0.1969 0.1930 0.2094 0.0150  0.0019  -0.0220 710  LEU B N   
14188 C CA  . LEU B 712  ? 0.1920 0.1881 0.2019 0.0140  0.0020  -0.0223 710  LEU B CA  
14189 C C   . LEU B 712  ? 0.1864 0.1852 0.1973 0.0128  0.0018  -0.0214 710  LEU B C   
14190 O O   . LEU B 712  ? 0.1995 0.1998 0.2096 0.0127  0.0023  -0.0213 710  LEU B O   
14191 C CB  . LEU B 712  ? 0.1940 0.1866 0.2005 0.0129  0.0009  -0.0232 710  LEU B CB  
14192 C CG  . LEU B 712  ? 0.1776 0.1701 0.1812 0.0116  0.0007  -0.0236 710  LEU B CG  
14193 C CD1 . LEU B 712  ? 0.2008 0.1932 0.2027 0.0128  0.0019  -0.0243 710  LEU B CD1 
14194 C CD2 . LEU B 712  ? 0.2287 0.2178 0.2292 0.0100  -0.0006 -0.0242 710  LEU B CD2 
14195 N N   . ALA B 713  ? 0.1778 0.1771 0.1903 0.0122  0.0011  -0.0209 711  ALA B N   
14196 C CA  . ALA B 713  ? 0.1970 0.1984 0.2101 0.0113  0.0008  -0.0202 711  ALA B CA  
14197 C C   . ALA B 713  ? 0.1751 0.1788 0.1901 0.0120  0.0017  -0.0194 711  ALA B C   
14198 O O   . ALA B 713  ? 0.1865 0.1918 0.2009 0.0117  0.0020  -0.0191 711  ALA B O   
14199 C CB  . ALA B 713  ? 0.2135 0.2145 0.2274 0.0106  -0.0001 -0.0199 711  ALA B CB  
14200 N N   . ILE B 714  ? 0.1942 0.1983 0.2116 0.0128  0.0020  -0.0190 712  ILE B N   
14201 C CA  . ILE B 714  ? 0.2019 0.2080 0.2211 0.0132  0.0028  -0.0182 712  ILE B CA  
14202 C C   . ILE B 714  ? 0.1941 0.2010 0.2124 0.0138  0.0039  -0.0182 712  ILE B C   
14203 O O   . ILE B 714  ? 0.1770 0.1853 0.1951 0.0137  0.0044  -0.0175 712  ILE B O   
14204 C CB  . ILE B 714  ? 0.2092 0.2156 0.2313 0.0135  0.0027  -0.0177 712  ILE B CB  
14205 C CG1 . ILE B 714  ? 0.2316 0.2373 0.2539 0.0128  0.0016  -0.0176 712  ILE B CG1 
14206 C CG2 . ILE B 714  ? 0.2127 0.2209 0.2366 0.0137  0.0035  -0.0167 712  ILE B CG2 
14207 C CD1 . ILE B 714  ? 0.2766 0.2826 0.3014 0.0128  0.0012  -0.0171 712  ILE B CD1 
14208 N N   . PHE B 715  ? 0.1778 0.1836 0.1952 0.0145  0.0043  -0.0190 713  PHE B N   
14209 C CA  . PHE B 715  ? 0.1775 0.1837 0.1933 0.0152  0.0055  -0.0192 713  PHE B CA  
14210 C C   . PHE B 715  ? 0.1780 0.1845 0.1912 0.0144  0.0053  -0.0193 713  PHE B C   
14211 O O   . PHE B 715  ? 0.1745 0.1826 0.1874 0.0145  0.0060  -0.0186 713  PHE B O   
14212 C CB  . PHE B 715  ? 0.1739 0.1780 0.1883 0.0161  0.0056  -0.0204 713  PHE B CB  
14213 C CG  . PHE B 715  ? 0.1649 0.1691 0.1771 0.0170  0.0068  -0.0209 713  PHE B CG  
14214 C CD1 . PHE B 715  ? 0.1669 0.1731 0.1806 0.0182  0.0083  -0.0204 713  PHE B CD1 
14215 C CD2 . PHE B 715  ? 0.1884 0.1906 0.1966 0.0165  0.0065  -0.0220 713  PHE B CD2 
14216 C CE1 . PHE B 715  ? 0.1903 0.1966 0.2016 0.0191  0.0096  -0.0210 713  PHE B CE1 
14217 C CE2 . PHE B 715  ? 0.1947 0.1966 0.2003 0.0173  0.0075  -0.0226 713  PHE B CE2 
14218 C CZ  . PHE B 715  ? 0.1874 0.1914 0.1945 0.0187  0.0092  -0.0222 713  PHE B CZ  
14219 N N   . THR B 716  ? 0.1628 0.1677 0.1740 0.0134  0.0041  -0.0200 714  THR B N   
14220 C CA  . THR B 716  ? 0.1653 0.1708 0.1741 0.0125  0.0037  -0.0200 714  THR B CA  
14221 C C   . THR B 716  ? 0.1681 0.1760 0.1784 0.0122  0.0036  -0.0188 714  THR B C   
14222 O O   . THR B 716  ? 0.1946 0.2040 0.2037 0.0121  0.0038  -0.0184 714  THR B O   
14223 C CB  . THR B 716  ? 0.1907 0.1943 0.1976 0.0112  0.0025  -0.0208 714  THR B CB  
14224 O OG1 . THR B 716  ? 0.2051 0.2057 0.2100 0.0116  0.0025  -0.0220 714  THR B OG1 
14225 C CG2 . THR B 716  ? 0.1909 0.1958 0.1957 0.0100  0.0018  -0.0207 714  THR B CG2 
14226 N N   . GLY B 717  ? 0.1753 0.1836 0.1879 0.0121  0.0032  -0.0183 715  GLY B N   
14227 C CA  . GLY B 717  ? 0.1912 0.2013 0.2050 0.0120  0.0030  -0.0173 715  GLY B CA  
14228 C C   . GLY B 717  ? 0.1585 0.1698 0.1729 0.0127  0.0039  -0.0163 715  GLY B C   
14229 O O   . GLY B 717  ? 0.1755 0.1881 0.1892 0.0127  0.0039  -0.0156 715  GLY B O   
14230 N N   . GLN B 718  ? 0.1597 0.1707 0.1756 0.0133  0.0048  -0.0161 716  GLN B N   
14231 C CA  . GLN B 718  ? 0.1585 0.1706 0.1750 0.0137  0.0057  -0.0150 716  GLN B CA  
14232 C C   . GLN B 718  ? 0.1534 0.1663 0.1674 0.0139  0.0062  -0.0150 716  GLN B C   
14233 O O   . GLN B 718  ? 0.1625 0.1764 0.1758 0.0139  0.0064  -0.0140 716  GLN B O   
14234 C CB  . GLN B 718  ? 0.1404 0.1527 0.1592 0.0141  0.0065  -0.0147 716  GLN B CB  
14235 C CG  . GLN B 718  ? 0.1530 0.1645 0.1742 0.0139  0.0057  -0.0146 716  GLN B CG  
14236 C CD  . GLN B 718  ? 0.1715 0.1837 0.1954 0.0140  0.0064  -0.0140 716  GLN B CD  
14237 O OE1 . GLN B 718  ? 0.1951 0.2073 0.2209 0.0136  0.0060  -0.0133 716  GLN B OE1 
14238 N NE2 . GLN B 718  ? 0.1776 0.1906 0.2015 0.0147  0.0073  -0.0144 716  GLN B NE2 
14239 N N   . ILE B 719  ? 0.1542 0.1662 0.1663 0.0140  0.0065  -0.0162 717  ILE B N   
14240 C CA  . ILE B 719  ? 0.1810 0.1934 0.1902 0.0141  0.0070  -0.0164 717  ILE B CA  
14241 C C   . ILE B 719  ? 0.1631 0.1762 0.1704 0.0134  0.0060  -0.0162 717  ILE B C   
14242 O O   . ILE B 719  ? 0.1703 0.1846 0.1760 0.0134  0.0063  -0.0155 717  ILE B O   
14243 C CB  . ILE B 719  ? 0.1627 0.1733 0.1699 0.0145  0.0073  -0.0180 717  ILE B CB  
14244 C CG1 . ILE B 719  ? 0.1711 0.1820 0.1804 0.0156  0.0086  -0.0179 717  ILE B CG1 
14245 C CG2 . ILE B 719  ? 0.2673 0.2777 0.2707 0.0144  0.0075  -0.0186 717  ILE B CG2 
14246 C CD1 . ILE B 719  ? 0.2607 0.2694 0.2688 0.0162  0.0087  -0.0194 717  ILE B CD1 
14247 N N   . ALA B 720  ? 0.1637 0.1762 0.1710 0.0126  0.0048  -0.0168 718  ALA B N   
14248 C CA  . ALA B 720  ? 0.1530 0.1668 0.1589 0.0118  0.0037  -0.0166 718  ALA B CA  
14249 C C   . ALA B 720  ? 0.1647 0.1805 0.1719 0.0122  0.0037  -0.0151 718  ALA B C   
14250 O O   . ALA B 720  ? 0.1696 0.1869 0.1752 0.0121  0.0034  -0.0145 718  ALA B O   
14251 C CB  . ALA B 720  ? 0.1908 0.2041 0.1971 0.0108  0.0026  -0.0173 718  ALA B CB  
14252 N N   . ALA B 721  ? 0.1624 0.1780 0.1723 0.0128  0.0040  -0.0144 719  ALA B N   
14253 C CA  . ALA B 721  ? 0.1642 0.1810 0.1751 0.0134  0.0039  -0.0130 719  ALA B CA  
14254 C C   . ALA B 721  ? 0.1582 0.1755 0.1681 0.0138  0.0047  -0.0120 719  ALA B C   
14255 O O   . ALA B 721  ? 0.1663 0.1848 0.1752 0.0141  0.0044  -0.0109 719  ALA B O   
14256 C CB  . ALA B 721  ? 0.1754 0.1911 0.1889 0.0137  0.0040  -0.0127 719  ALA B CB  
14257 N N   . ALA B 722  ? 0.1509 0.1674 0.1610 0.0139  0.0058  -0.0121 720  ALA B N   
14258 C CA  . ALA B 722  ? 0.1565 0.1736 0.1655 0.0143  0.0069  -0.0110 720  ALA B CA  
14259 C C   . ALA B 722  ? 0.1659 0.1839 0.1715 0.0141  0.0066  -0.0113 720  ALA B C   
14260 O O   . ALA B 722  ? 0.1646 0.1837 0.1690 0.0143  0.0066  -0.0100 720  ALA B O   
14261 C CB  . ALA B 722  ? 0.1585 0.1752 0.1685 0.0145  0.0082  -0.0112 720  ALA B CB  
14262 N N   . LEU B 723  ? 0.1608 0.1782 0.1647 0.0137  0.0063  -0.0129 721  LEU B N   
14263 C CA  . LEU B 723  ? 0.1587 0.1767 0.1590 0.0133  0.0059  -0.0133 721  LEU B CA  
14264 C C   . LEU B 723  ? 0.1786 0.1982 0.1784 0.0129  0.0045  -0.0124 721  LEU B C   
14265 O O   . LEU B 723  ? 0.1926 0.2135 0.1903 0.0130  0.0043  -0.0117 721  LEU B O   
14266 C CB  . LEU B 723  ? 0.1617 0.1780 0.1601 0.0127  0.0054  -0.0153 721  LEU B CB  
14267 C CG  . LEU B 723  ? 0.1831 0.1977 0.1807 0.0133  0.0068  -0.0164 721  LEU B CG  
14268 C CD1 . LEU B 723  ? 0.1867 0.1990 0.1827 0.0127  0.0060  -0.0182 721  LEU B CD1 
14269 C CD2 . LEU B 723  ? 0.2037 0.2187 0.1984 0.0138  0.0079  -0.0162 721  LEU B CD2 
14270 N N   . VAL B 724  ? 0.1605 0.1805 0.1624 0.0126  0.0035  -0.0126 722  VAL B N   
14271 C CA  . VAL B 724  ? 0.1502 0.1724 0.1518 0.0124  0.0022  -0.0119 722  VAL B CA  
14272 C C   . VAL B 724  ? 0.1417 0.1652 0.1444 0.0135  0.0023  -0.0100 722  VAL B C   
14273 O O   . VAL B 724  ? 0.1907 0.2162 0.1924 0.0136  0.0014  -0.0091 722  VAL B O   
14274 C CB  . VAL B 724  ? 0.1555 0.1782 0.1589 0.0118  0.0013  -0.0126 722  VAL B CB  
14275 C CG1 . VAL B 724  ? 0.1938 0.2164 0.2004 0.0127  0.0015  -0.0119 722  VAL B CG1 
14276 C CG2 . VAL B 724  ? 0.1711 0.1966 0.1735 0.0110  -0.0002 -0.0123 722  VAL B CG2 
14277 N N   . ALA B 725  ? 0.1846 0.2067 0.1890 0.0142  0.0034  -0.0093 723  ALA B N   
14278 C CA  . ALA B 725  ? 0.1875 0.2097 0.1923 0.0151  0.0036  -0.0074 723  ALA B CA  
14279 C C   . ALA B 725  ? 0.2013 0.2240 0.2035 0.0151  0.0042  -0.0066 723  ALA B C   
14280 O O   . ALA B 725  ? 0.2182 0.2410 0.2203 0.0158  0.0043  -0.0048 723  ALA B O   
14281 C CB  . ALA B 725  ? 0.1953 0.2156 0.2027 0.0155  0.0044  -0.0070 723  ALA B CB  
14282 N N   . GLY B 726  ? 0.1771 0.1998 0.1769 0.0145  0.0045  -0.0077 724  GLY B N   
14283 C CA  . GLY B 726  ? 0.1831 0.2063 0.1797 0.0145  0.0051  -0.0071 724  GLY B CA  
14284 C C   . GLY B 726  ? 0.2140 0.2361 0.2103 0.0146  0.0069  -0.0070 724  GLY B C   
14285 O O   . GLY B 726  ? 0.2373 0.2600 0.2313 0.0148  0.0076  -0.0060 724  GLY B O   
14286 N N   . ASN B 727  ? 0.1774 0.1984 0.1761 0.0146  0.0077  -0.0079 725  ASN B N   
14287 C CA  . ASN B 727  ? 0.1916 0.2123 0.1910 0.0149  0.0095  -0.0077 725  ASN B CA  
14288 C C   . ASN B 727  ? 0.1843 0.2043 0.1821 0.0149  0.0102  -0.0097 725  ASN B C   
14289 O O   . ASN B 727  ? 0.2167 0.2357 0.2151 0.0147  0.0094  -0.0112 725  ASN B O   
14290 C CB  . ASN B 727  ? 0.1843 0.2041 0.1876 0.0149  0.0098  -0.0072 725  ASN B CB  
14291 C CG  . ASN B 727  ? 0.1941 0.2137 0.1989 0.0150  0.0089  -0.0055 725  ASN B CG  
14292 O OD1 . ASN B 727  ? 0.1994 0.2192 0.2039 0.0151  0.0095  -0.0036 725  ASN B OD1 
14293 N ND2 . ASN B 727  ? 0.1802 0.1993 0.1866 0.0151  0.0077  -0.0060 725  ASN B ND2 
14294 N N   . PRO B 728  ? 0.1740 0.1944 0.1696 0.0153  0.0117  -0.0097 726  PRO B N   
14295 C CA  . PRO B 728  ? 0.1821 0.2017 0.1767 0.0157  0.0126  -0.0116 726  PRO B CA  
14296 C C   . PRO B 728  ? 0.1922 0.2117 0.1911 0.0160  0.0134  -0.0116 726  PRO B C   
14297 O O   . PRO B 728  ? 0.1941 0.2144 0.1959 0.0159  0.0137  -0.0100 726  PRO B O   
14298 C CB  . PRO B 728  ? 0.2063 0.2268 0.1978 0.0163  0.0143  -0.0111 726  PRO B CB  
14299 C CG  . PRO B 728  ? 0.2340 0.2561 0.2270 0.0160  0.0148  -0.0086 726  PRO B CG  
14300 C CD  . PRO B 728  ? 0.1865 0.2083 0.1812 0.0154  0.0128  -0.0077 726  PRO B CD  
14301 N N   . VAL B 729  ? 0.1632 0.1813 0.1621 0.0164  0.0134  -0.0134 727  VAL B N   
14302 C CA  . VAL B 729  ? 0.1653 0.1832 0.1681 0.0167  0.0136  -0.0136 727  VAL B CA  
14303 C C   . VAL B 729  ? 0.1990 0.2172 0.2018 0.0179  0.0153  -0.0146 727  VAL B C   
14304 O O   . VAL B 729  ? 0.1946 0.2115 0.1939 0.0185  0.0156  -0.0161 727  VAL B O   
14305 C CB  . VAL B 729  ? 0.1718 0.1878 0.1752 0.0162  0.0118  -0.0149 727  VAL B CB  
14306 C CG1 . VAL B 729  ? 0.1904 0.2059 0.1970 0.0166  0.0120  -0.0154 727  VAL B CG1 
14307 C CG2 . VAL B 729  ? 0.1798 0.1963 0.1844 0.0153  0.0105  -0.0137 727  VAL B CG2 
14308 N N   . LEU B 730  ? 0.1770 0.1967 0.1836 0.0182  0.0162  -0.0136 728  LEU B N   
14309 C CA  . LEU B 730  ? 0.1779 0.1982 0.1858 0.0194  0.0175  -0.0144 728  LEU B CA  
14310 C C   . LEU B 730  ? 0.1526 0.1717 0.1636 0.0193  0.0163  -0.0150 728  LEU B C   
14311 O O   . LEU B 730  ? 0.1879 0.2078 0.2024 0.0185  0.0157  -0.0138 728  LEU B O   
14312 C CB  . LEU B 730  ? 0.1943 0.2179 0.2048 0.0197  0.0194  -0.0127 728  LEU B CB  
14313 C CG  . LEU B 730  ? 0.1949 0.2203 0.2027 0.0197  0.0209  -0.0116 728  LEU B CG  
14314 C CD1 . LEU B 730  ? 0.2121 0.2362 0.2149 0.0208  0.0215  -0.0134 728  LEU B CD1 
14315 C CD2 . LEU B 730  ? 0.2023 0.2275 0.2096 0.0183  0.0199  -0.0099 728  LEU B CD2 
14316 N N   . ALA B 731  ? 0.1627 0.1795 0.1721 0.0200  0.0158  -0.0169 729  ALA B N   
14317 C CA  . ALA B 731  ? 0.1631 0.1783 0.1747 0.0198  0.0144  -0.0175 729  ALA B CA  
14318 C C   . ALA B 731  ? 0.1809 0.1971 0.1952 0.0213  0.0154  -0.0178 729  ALA B C   
14319 O O   . ALA B 731  ? 0.1848 0.2002 0.1971 0.0228  0.0164  -0.0190 729  ALA B O   
14320 C CB  . ALA B 731  ? 0.2038 0.2156 0.2120 0.0195  0.0130  -0.0192 729  ALA B CB  
14321 N N   . LYS B 732  ? 0.1545 0.1723 0.1731 0.0209  0.0151  -0.0167 730  LYS B N   
14322 C CA  . LYS B 732  ? 0.1851 0.2046 0.2069 0.0222  0.0158  -0.0166 730  LYS B CA  
14323 C C   . LYS B 732  ? 0.1603 0.1778 0.1838 0.0219  0.0140  -0.0171 730  LYS B C   
14324 O O   . LYS B 732  ? 0.1800 0.1982 0.2062 0.0206  0.0130  -0.0161 730  LYS B O   
14325 C CB  . LYS B 732  ? 0.1786 0.2021 0.2042 0.0217  0.0169  -0.0147 730  LYS B CB  
14326 C CG  . LYS B 732  ? 0.1771 0.2038 0.2052 0.0234  0.0187  -0.0144 730  LYS B CG  
14327 C CD  . LYS B 732  ? 0.1826 0.2088 0.2130 0.0245  0.0178  -0.0152 730  LYS B CD  
14328 C CE  . LYS B 732  ? 0.1720 0.1993 0.2066 0.0231  0.0164  -0.0140 730  LYS B CE  
14329 N NZ  . LYS B 732  ? 0.1709 0.1974 0.2073 0.0242  0.0154  -0.0148 730  LYS B NZ  
14330 N N   . PRO B 733  ? 0.1595 0.1743 0.1810 0.0229  0.0136  -0.0187 731  PRO B N   
14331 C CA  . PRO B 733  ? 0.1801 0.1928 0.2027 0.0226  0.0118  -0.0191 731  PRO B CA  
14332 C C   . PRO B 733  ? 0.1529 0.1679 0.1798 0.0236  0.0121  -0.0184 731  PRO B C   
14333 O O   . PRO B 733  ? 0.1711 0.1890 0.1996 0.0250  0.0137  -0.0181 731  PRO B O   
14334 C CB  . PRO B 733  ? 0.1823 0.1911 0.2010 0.0234  0.0114  -0.0209 731  PRO B CB  
14335 C CG  . PRO B 733  ? 0.1872 0.1968 0.2042 0.0253  0.0134  -0.0215 731  PRO B CG  
14336 C CD  . PRO B 733  ? 0.1806 0.1936 0.1983 0.0244  0.0145  -0.0202 731  PRO B CD  
14337 N N   . ALA B 734  ? 0.1785 0.1926 0.2072 0.0229  0.0104  -0.0183 732  ALA B N   
14338 C CA  . ALA B 734  ? 0.1803 0.1964 0.2130 0.0238  0.0102  -0.0176 732  ALA B CA  
14339 C C   . ALA B 734  ? 0.1951 0.2108 0.2273 0.0263  0.0111  -0.0186 732  ALA B C   
14340 O O   . ALA B 734  ? 0.1986 0.2107 0.2270 0.0272  0.0111  -0.0200 732  ALA B O   
14341 C CB  . ALA B 734  ? 0.1971 0.2115 0.2307 0.0227  0.0081  -0.0175 732  ALA B CB  
14342 N N   . GLU B 735  ? 0.1894 0.2090 0.2257 0.0276  0.0119  -0.0177 733  GLU B N   
14343 C CA  . GLU B 735  ? 0.1995 0.2192 0.2356 0.0305  0.0130  -0.0185 733  GLU B CA  
14344 C C   . GLU B 735  ? 0.1994 0.2148 0.2339 0.0315  0.0114  -0.0196 733  GLU B C   
14345 O O   . GLU B 735  ? 0.1950 0.2081 0.2271 0.0338  0.0121  -0.0209 733  GLU B O   
14346 C CB  . GLU B 735  ? 0.2334 0.2589 0.2746 0.0317  0.0142  -0.0172 733  GLU B CB  
14347 C CG  . GLU B 735  ? 0.2546 0.2825 0.3004 0.0305  0.0126  -0.0159 733  GLU B CG  
14348 C CD  . GLU B 735  ? 0.2922 0.3226 0.3401 0.0277  0.0124  -0.0144 733  GLU B CD  
14349 O OE1 . GLU B 735  ? 0.2592 0.2878 0.3042 0.0262  0.0126  -0.0145 733  GLU B OE1 
14350 O OE2 . GLU B 735  ? 0.2978 0.3317 0.3501 0.0269  0.0118  -0.0130 733  GLU B OE2 
14351 N N   . GLU B 736  ? 0.1874 0.2013 0.2226 0.0298  0.0093  -0.0192 734  GLU B N   
14352 C CA  . GLU B 736  ? 0.2116 0.2215 0.2454 0.0306  0.0078  -0.0199 734  GLU B CA  
14353 C C   . GLU B 736  ? 0.1987 0.2031 0.2269 0.0302  0.0073  -0.0214 734  GLU B C   
14354 O O   . GLU B 736  ? 0.2326 0.2331 0.2587 0.0314  0.0066  -0.0223 734  GLU B O   
14355 C CB  . GLU B 736  ? 0.2060 0.2160 0.2419 0.0288  0.0057  -0.0190 734  GLU B CB  
14356 C CG  . GLU B 736  ? 0.2294 0.2444 0.2707 0.0289  0.0056  -0.0175 734  GLU B CG  
14357 C CD  . GLU B 736  ? 0.2380 0.2565 0.2815 0.0268  0.0060  -0.0164 734  GLU B CD  
14358 O OE1 . GLU B 736  ? 0.2118 0.2298 0.2531 0.0259  0.0070  -0.0167 734  GLU B OE1 
14359 O OE2 . GLU B 736  ? 0.2905 0.3122 0.3380 0.0260  0.0052  -0.0152 734  GLU B OE2 
14360 N N   . THR B 737  ? 0.2002 0.2040 0.2260 0.0284  0.0077  -0.0216 735  THR B N   
14361 C CA  . THR B 737  ? 0.2095 0.2086 0.2306 0.0272  0.0068  -0.0228 735  THR B CA  
14362 C C   . THR B 737  ? 0.2000 0.1987 0.2178 0.0270  0.0081  -0.0236 735  THR B C   
14363 O O   . THR B 737  ? 0.2227 0.2207 0.2385 0.0250  0.0076  -0.0236 735  THR B O   
14364 C CB  . THR B 737  ? 0.2099 0.2083 0.2311 0.0246  0.0051  -0.0222 735  THR B CB  
14365 O OG1 . THR B 737  ? 0.2020 0.2042 0.2256 0.0234  0.0056  -0.0211 735  THR B OG1 
14366 C CG2 . THR B 737  ? 0.2170 0.2147 0.2402 0.0248  0.0036  -0.0216 735  THR B CG2 
14367 N N   . PRO B 738  ? 0.1882 0.1875 0.2052 0.0292  0.0098  -0.0242 736  PRO B N   
14368 C CA  . PRO B 738  ? 0.2011 0.2002 0.2148 0.0290  0.0110  -0.0250 736  PRO B CA  
14369 C C   . PRO B 738  ? 0.2024 0.1960 0.2106 0.0285  0.0101  -0.0266 736  PRO B C   
14370 O O   . PRO B 738  ? 0.2006 0.1938 0.2058 0.0274  0.0104  -0.0270 736  PRO B O   
14371 C CB  . PRO B 738  ? 0.2061 0.2076 0.2207 0.0318  0.0131  -0.0252 736  PRO B CB  
14372 C CG  . PRO B 738  ? 0.2167 0.2167 0.2328 0.0339  0.0126  -0.0255 736  PRO B CG  
14373 C CD  . PRO B 738  ? 0.2076 0.2081 0.2268 0.0321  0.0107  -0.0243 736  PRO B CD  
14374 N N   . LEU B 739  ? 0.1932 0.1825 0.1999 0.0290  0.0089  -0.0274 737  LEU B N   
14375 C CA  . LEU B 739  ? 0.2126 0.1963 0.2138 0.0285  0.0081  -0.0290 737  LEU B CA  
14376 C C   . LEU B 739  ? 0.1961 0.1790 0.1955 0.0253  0.0067  -0.0287 737  LEU B C   
14377 O O   . LEU B 739  ? 0.2044 0.1854 0.1998 0.0243  0.0066  -0.0296 737  LEU B O   
14378 C CB  . LEU B 739  ? 0.1924 0.1713 0.1922 0.0299  0.0071  -0.0298 737  LEU B CB  
14379 C CG  . LEU B 739  ? 0.1977 0.1775 0.1992 0.0335  0.0086  -0.0301 737  LEU B CG  
14380 C CD1 . LEU B 739  ? 0.2458 0.2204 0.2459 0.0348  0.0073  -0.0306 737  LEU B CD1 
14381 C CD2 . LEU B 739  ? 0.2212 0.2007 0.2196 0.0354  0.0105  -0.0314 737  LEU B CD2 
14382 N N   . ILE B 740  ? 0.1888 0.1730 0.1909 0.0236  0.0054  -0.0275 738  ILE B N   
14383 C CA  . ILE B 740  ? 0.1819 0.1658 0.1826 0.0208  0.0042  -0.0272 738  ILE B CA  
14384 C C   . ILE B 740  ? 0.1847 0.1725 0.1859 0.0200  0.0052  -0.0267 738  ILE B C   
14385 O O   . ILE B 740  ? 0.1998 0.1872 0.1986 0.0183  0.0046  -0.0269 738  ILE B O   
14386 C CB  . ILE B 740  ? 0.2313 0.2156 0.2343 0.0194  0.0028  -0.0262 738  ILE B CB  
14387 C CG1 . ILE B 740  ? 0.2205 0.2043 0.2217 0.0166  0.0016  -0.0260 738  ILE B CG1 
14388 C CG2 . ILE B 740  ? 0.2362 0.2251 0.2440 0.0198  0.0034  -0.0248 738  ILE B CG2 
14389 C CD1 . ILE B 740  ? 0.2656 0.2445 0.2622 0.0156  0.0006  -0.0271 738  ILE B CD1 
14390 N N   . ALA B 741  ? 0.1862 0.1779 0.1906 0.0213  0.0066  -0.0258 739  ALA B N   
14391 C CA  . ALA B 741  ? 0.2031 0.1983 0.2079 0.0208  0.0075  -0.0252 739  ALA B CA  
14392 C C   . ALA B 741  ? 0.1885 0.1820 0.1889 0.0212  0.0083  -0.0264 739  ALA B C   
14393 O O   . ALA B 741  ? 0.2071 0.2012 0.2055 0.0197  0.0080  -0.0263 739  ALA B O   
14394 C CB  . ALA B 741  ? 0.2045 0.2038 0.2134 0.0220  0.0089  -0.0240 739  ALA B CB  
14395 N N   . ALA B 742  ? 0.1943 0.1856 0.1929 0.0232  0.0092  -0.0276 740  ALA B N   
14396 C CA  . ALA B 742  ? 0.1981 0.1872 0.1919 0.0238  0.0098  -0.0290 740  ALA B CA  
14397 C C   . ALA B 742  ? 0.2186 0.2040 0.2083 0.0215  0.0080  -0.0299 740  ALA B C   
14398 O O   . ALA B 742  ? 0.2016 0.1868 0.1880 0.0206  0.0080  -0.0304 740  ALA B O   
14399 C CB  . ALA B 742  ? 0.1936 0.1801 0.1859 0.0266  0.0109  -0.0304 740  ALA B CB  
14400 N N   . GLU B 743  ? 0.1931 0.1757 0.1830 0.0205  0.0064  -0.0300 741  GLU B N   
14401 C CA  . GLU B 743  ? 0.2087 0.1880 0.1951 0.0181  0.0046  -0.0306 741  GLU B CA  
14402 C C   . GLU B 743  ? 0.2113 0.1944 0.1989 0.0158  0.0040  -0.0294 741  GLU B C   
14403 O O   . GLU B 743  ? 0.2280 0.2103 0.2123 0.0142  0.0032  -0.0299 741  GLU B O   
14404 C CB  . GLU B 743  ? 0.2529 0.2287 0.2395 0.0175  0.0031  -0.0307 741  GLU B CB  
14405 C CG  . GLU B 743  ? 0.2560 0.2286 0.2392 0.0147  0.0012  -0.0311 741  GLU B CG  
14406 C CD  . GLU B 743  ? 0.3172 0.2851 0.2946 0.0145  0.0009  -0.0330 741  GLU B CD  
14407 O OE1 . GLU B 743  ? 0.2761 0.2422 0.2517 0.0169  0.0022  -0.0342 741  GLU B OE1 
14408 O OE2 . GLU B 743  ? 0.3321 0.2981 0.3068 0.0118  -0.0007 -0.0332 741  GLU B OE2 
14409 N N   . GLY B 744  ? 0.2126 0.1998 0.2048 0.0158  0.0043  -0.0278 742  GLY B N   
14410 C CA  . GLY B 744  ? 0.2201 0.2109 0.2135 0.0142  0.0040  -0.0267 742  GLY B CA  
14411 C C   . GLY B 744  ? 0.1906 0.1830 0.1819 0.0144  0.0048  -0.0268 742  GLY B C   
14412 O O   . GLY B 744  ? 0.2042 0.1976 0.1939 0.0128  0.0040  -0.0265 742  GLY B O   
14413 N N   . VAL B 745  ? 0.1859 0.1790 0.1773 0.0165  0.0065  -0.0270 743  VAL B N   
14414 C CA  . VAL B 745  ? 0.1857 0.1804 0.1748 0.0167  0.0075  -0.0270 743  VAL B CA  
14415 C C   . VAL B 745  ? 0.2106 0.2018 0.1941 0.0160  0.0067  -0.0287 743  VAL B C   
14416 O O   . VAL B 745  ? 0.2085 0.2009 0.1898 0.0148  0.0063  -0.0285 743  VAL B O   
14417 C CB  . VAL B 745  ? 0.2118 0.2084 0.2024 0.0190  0.0097  -0.0267 743  VAL B CB  
14418 C CG1 . VAL B 745  ? 0.2165 0.2137 0.2035 0.0195  0.0108  -0.0272 743  VAL B CG1 
14419 C CG2 . VAL B 745  ? 0.2144 0.2150 0.2100 0.0190  0.0102  -0.0248 743  VAL B CG2 
14420 N N   . ARG B 746  ? 0.2049 0.1915 0.1859 0.0165  0.0063  -0.0302 744  ARG B N   
14421 C CA  . ARG B 746  ? 0.2292 0.2117 0.2047 0.0154  0.0053  -0.0319 744  ARG B CA  
14422 C C   . ARG B 746  ? 0.1983 0.1814 0.1732 0.0124  0.0032  -0.0313 744  ARG B C   
14423 O O   . ARG B 746  ? 0.2243 0.2070 0.1955 0.0111  0.0025  -0.0319 744  ARG B O   
14424 C CB  . ARG B 746  ? 0.2290 0.2059 0.2024 0.0161  0.0047  -0.0335 744  ARG B CB  
14425 C CG  . ARG B 746  ? 0.2552 0.2305 0.2281 0.0194  0.0066  -0.0345 744  ARG B CG  
14426 C CD  . ARG B 746  ? 0.2452 0.2142 0.2155 0.0200  0.0057  -0.0360 744  ARG B CD  
14427 N NE  . ARG B 746  ? 0.2714 0.2397 0.2423 0.0234  0.0075  -0.0367 744  ARG B NE  
14428 C CZ  . ARG B 746  ? 0.2462 0.2158 0.2215 0.0250  0.0080  -0.0358 744  ARG B CZ  
14429 N NH1 . ARG B 746  ? 0.2464 0.2163 0.2248 0.0234  0.0065  -0.0347 744  ARG B NH1 
14430 N NH2 . ARG B 746  ? 0.2778 0.2484 0.2543 0.0283  0.0099  -0.0361 744  ARG B NH2 
14431 N N   . ILE B 747  ? 0.1946 0.1791 0.1731 0.0112  0.0023  -0.0302 745  ILE B N   
14432 C CA  . ILE B 747  ? 0.2142 0.1997 0.1924 0.0085  0.0004  -0.0296 745  ILE B CA  
14433 C C   . ILE B 747  ? 0.2195 0.2100 0.1989 0.0080  0.0006  -0.0283 745  ILE B C   
14434 O O   . ILE B 747  ? 0.2014 0.1925 0.1785 0.0061  -0.0007 -0.0283 745  ILE B O   
14435 C CB  . ILE B 747  ? 0.2183 0.2041 0.2000 0.0076  -0.0004 -0.0287 745  ILE B CB  
14436 C CG1 . ILE B 747  ? 0.2381 0.2184 0.2173 0.0074  -0.0011 -0.0300 745  ILE B CG1 
14437 C CG2 . ILE B 747  ? 0.2123 0.2012 0.1950 0.0052  -0.0017 -0.0276 745  ILE B CG2 
14438 C CD1 . ILE B 747  ? 0.2476 0.2277 0.2298 0.0070  -0.0017 -0.0291 745  ILE B CD1 
14439 N N   . LEU B 748  ? 0.1949 0.1888 0.1778 0.0096  0.0020  -0.0271 746  LEU B N   
14440 C CA  . LEU B 748  ? 0.1864 0.1845 0.1703 0.0093  0.0022  -0.0258 746  LEU B CA  
14441 C C   . LEU B 748  ? 0.1863 0.1838 0.1657 0.0094  0.0025  -0.0265 746  LEU B C   
14442 O O   . LEU B 748  ? 0.1983 0.1979 0.1765 0.0082  0.0015  -0.0259 746  LEU B O   
14443 C CB  . LEU B 748  ? 0.1936 0.1945 0.1816 0.0109  0.0037  -0.0244 746  LEU B CB  
14444 C CG  . LEU B 748  ? 0.2389 0.2416 0.2311 0.0103  0.0031  -0.0232 746  LEU B CG  
14445 C CD1 . LEU B 748  ? 0.2535 0.2576 0.2495 0.0119  0.0044  -0.0223 746  LEU B CD1 
14446 C CD2 . LEU B 748  ? 0.2613 0.2672 0.2541 0.0092  0.0021  -0.0220 746  LEU B CD2 
14447 N N   . ARG B 749  ? 0.2008 0.1956 0.1777 0.0110  0.0037  -0.0278 747  ARG B N   
14448 C CA  . ARG B 749  ? 0.2224 0.2163 0.1945 0.0111  0.0040  -0.0288 747  ARG B CA  
14449 C C   . ARG B 749  ? 0.2174 0.2085 0.1852 0.0089  0.0019  -0.0300 747  ARG B C   
14450 O O   . ARG B 749  ? 0.2211 0.2133 0.1860 0.0078  0.0011  -0.0299 747  ARG B O   
14451 C CB  . ARG B 749  ? 0.2088 0.2004 0.1790 0.0135  0.0059  -0.0300 747  ARG B CB  
14452 C CG  . ARG B 749  ? 0.2406 0.2358 0.2143 0.0154  0.0081  -0.0286 747  ARG B CG  
14453 C CD  . ARG B 749  ? 0.2661 0.2596 0.2375 0.0178  0.0101  -0.0299 747  ARG B CD  
14454 N NE  . ARG B 749  ? 0.2239 0.2214 0.1983 0.0193  0.0122  -0.0284 747  ARG B NE  
14455 C CZ  . ARG B 749  ? 0.2859 0.2834 0.2588 0.0215  0.0143  -0.0291 747  ARG B CZ  
14456 N NH1 . ARG B 749  ? 0.3009 0.2945 0.2691 0.0225  0.0146  -0.0313 747  ARG B NH1 
14457 N NH2 . ARG B 749  ? 0.2858 0.2874 0.2619 0.0225  0.0162  -0.0275 747  ARG B NH2 
14458 N N   . GLU B 750  ? 0.2056 0.1931 0.1730 0.0080  0.0008  -0.0310 748  GLU B N   
14459 C CA  . GLU B 750  ? 0.2325 0.2171 0.1958 0.0055  -0.0013 -0.0321 748  GLU B CA  
14460 C C   . GLU B 750  ? 0.1894 0.1784 0.1546 0.0031  -0.0029 -0.0305 748  GLU B C   
14461 O O   . GLU B 750  ? 0.2195 0.2083 0.1812 0.0012  -0.0044 -0.0309 748  GLU B O   
14462 C CB  . GLU B 750  ? 0.2198 0.1998 0.1829 0.0048  -0.0021 -0.0330 748  GLU B CB  
14463 C CG  . GLU B 750  ? 0.2547 0.2311 0.2134 0.0020  -0.0044 -0.0341 748  GLU B CG  
14464 C CD  . GLU B 750  ? 0.2870 0.2581 0.2449 0.0014  -0.0052 -0.0351 748  GLU B CD  
14465 O OE1 . GLU B 750  ? 0.2905 0.2603 0.2506 0.0037  -0.0039 -0.0351 748  GLU B OE1 
14466 O OE2 . GLU B 750  ? 0.3471 0.3153 0.3021 -0.0014 -0.0072 -0.0356 748  GLU B OE2 
14467 N N   . ALA B 751  ? 0.2129 0.2060 0.1833 0.0034  -0.0025 -0.0287 749  ALA B N   
14468 C CA  . ALA B 751  ? 0.2062 0.2038 0.1789 0.0017  -0.0038 -0.0271 749  ALA B CA  
14469 C C   . ALA B 751  ? 0.2169 0.2183 0.1891 0.0022  -0.0036 -0.0261 749  ALA B C   
14470 O O   . ALA B 751  ? 0.2360 0.2412 0.2096 0.0009  -0.0048 -0.0249 749  ALA B O   
14471 C CB  . ALA B 751  ? 0.2032 0.2035 0.1814 0.0023  -0.0033 -0.0257 749  ALA B CB  
14472 N N   . GLY B 752  ? 0.2175 0.2179 0.1876 0.0040  -0.0020 -0.0266 750  GLY B N   
14473 C CA  . GLY B 752  ? 0.2211 0.2247 0.1901 0.0043  -0.0019 -0.0256 750  GLY B CA  
14474 C C   . GLY B 752  ? 0.2274 0.2331 0.1986 0.0066  0.0002  -0.0244 750  GLY B C   
14475 O O   . GLY B 752  ? 0.2499 0.2579 0.2198 0.0070  0.0004  -0.0234 750  GLY B O   
14476 N N   . ILE B 753  ? 0.2126 0.2178 0.1873 0.0080  0.0016  -0.0242 751  ILE B N   
14477 C CA  . ILE B 753  ? 0.2148 0.2220 0.1917 0.0099  0.0035  -0.0229 751  ILE B CA  
14478 C C   . ILE B 753  ? 0.2204 0.2258 0.1934 0.0112  0.0051  -0.0240 751  ILE B C   
14479 O O   . ILE B 753  ? 0.2358 0.2378 0.2071 0.0118  0.0056  -0.0257 751  ILE B O   
14480 C CB  . ILE B 753  ? 0.1942 0.2015 0.1758 0.0109  0.0045  -0.0224 751  ILE B CB  
14481 C CG1 . ILE B 753  ? 0.2107 0.2194 0.1957 0.0097  0.0030  -0.0216 751  ILE B CG1 
14482 C CG2 . ILE B 753  ? 0.2111 0.2206 0.1949 0.0124  0.0063  -0.0210 751  ILE B CG2 
14483 C CD1 . ILE B 753  ? 0.2112 0.2236 0.1978 0.0095  0.0025  -0.0197 751  ILE B CD1 
14484 N N   . PRO B 754  ? 0.2230 0.2305 0.1944 0.0117  0.0058  -0.0230 752  PRO B N   
14485 C CA  . PRO B 754  ? 0.2323 0.2383 0.1995 0.0129  0.0074  -0.0241 752  PRO B CA  
14486 C C   . PRO B 754  ? 0.2294 0.2349 0.1990 0.0149  0.0097  -0.0243 752  PRO B C   
14487 O O   . PRO B 754  ? 0.2289 0.2363 0.2035 0.0154  0.0102  -0.0230 752  PRO B O   
14488 C CB  . PRO B 754  ? 0.2483 0.2576 0.2145 0.0130  0.0078  -0.0223 752  PRO B CB  
14489 C CG  . PRO B 754  ? 0.2885 0.3001 0.2569 0.0115  0.0057  -0.0208 752  PRO B CG  
14490 C CD  . PRO B 754  ? 0.2337 0.2448 0.2064 0.0111  0.0051  -0.0209 752  PRO B CD  
14491 N N   . ALA B 755  ? 0.2450 0.2480 0.2108 0.0161  0.0109  -0.0261 753  ALA B N   
14492 C CA  . ALA B 755  ? 0.2809 0.2839 0.2490 0.0182  0.0131  -0.0263 753  ALA B CA  
14493 C C   . ALA B 755  ? 0.2402 0.2475 0.2117 0.0190  0.0149  -0.0241 753  ALA B C   
14494 O O   . ALA B 755  ? 0.2496 0.2582 0.2256 0.0200  0.0160  -0.0233 753  ALA B O   
14495 C CB  . ALA B 755  ? 0.3131 0.3130 0.2760 0.0197  0.0143  -0.0286 753  ALA B CB  
14496 N N   . SER B 756  ? 0.2250 0.2343 0.1945 0.0185  0.0150  -0.0228 754  SER B N   
14497 C CA  . SER B 756  ? 0.2326 0.2456 0.2051 0.0190  0.0166  -0.0204 754  SER B CA  
14498 C C   . SER B 756  ? 0.2316 0.2464 0.2096 0.0181  0.0155  -0.0185 754  SER B C   
14499 O O   . SER B 756  ? 0.2463 0.2634 0.2278 0.0185  0.0168  -0.0167 754  SER B O   
14500 C CB  . SER B 756  ? 0.2755 0.2899 0.2440 0.0187  0.0169  -0.0195 754  SER B CB  
14501 O OG  . SER B 756  ? 0.3175 0.3315 0.2843 0.0171  0.0145  -0.0192 754  SER B OG  
14502 N N   . ALA B 757  ? 0.1958 0.2094 0.1744 0.0168  0.0133  -0.0189 755  ALA B N   
14503 C CA  . ALA B 757  ? 0.1687 0.1837 0.1521 0.0161  0.0123  -0.0173 755  ALA B CA  
14504 C C   . ALA B 757  ? 0.1895 0.2034 0.1767 0.0164  0.0124  -0.0180 755  ALA B C   
14505 O O   . ALA B 757  ? 0.2001 0.2151 0.1913 0.0161  0.0120  -0.0167 755  ALA B O   
14506 C CB  . ALA B 757  ? 0.1946 0.2097 0.1771 0.0147  0.0100  -0.0171 755  ALA B CB  
14507 N N   . LEU B 758  ? 0.2027 0.2144 0.1886 0.0172  0.0129  -0.0199 756  LEU B N   
14508 C CA  . LEU B 758  ? 0.1950 0.2055 0.1843 0.0176  0.0127  -0.0205 756  LEU B CA  
14509 C C   . LEU B 758  ? 0.1991 0.2085 0.1875 0.0193  0.0144  -0.0218 756  LEU B C   
14510 O O   . LEU B 758  ? 0.2124 0.2187 0.1968 0.0196  0.0141  -0.0238 756  LEU B O   
14511 C CB  . LEU B 758  ? 0.1677 0.1761 0.1567 0.0163  0.0106  -0.0215 756  LEU B CB  
14512 C CG  . LEU B 758  ? 0.1884 0.1952 0.1803 0.0167  0.0104  -0.0221 756  LEU B CG  
14513 C CD1 . LEU B 758  ? 0.1984 0.2076 0.1955 0.0168  0.0108  -0.0204 756  LEU B CD1 
14514 C CD2 . LEU B 758  ? 0.2242 0.2287 0.2150 0.0152  0.0084  -0.0230 756  LEU B CD2 
14515 N N   . GLN B 759  ? 0.1890 0.2006 0.1808 0.0204  0.0160  -0.0208 757  GLN B N   
14516 C CA  . GLN B 759  ? 0.1936 0.2050 0.1854 0.0223  0.0178  -0.0218 757  GLN B CA  
14517 C C   . GLN B 759  ? 0.2126 0.2242 0.2091 0.0228  0.0175  -0.0216 757  GLN B C   
14518 O O   . GLN B 759  ? 0.2132 0.2266 0.2138 0.0218  0.0169  -0.0200 757  GLN B O   
14519 C CB  . GLN B 759  ? 0.1797 0.1946 0.1718 0.0232  0.0201  -0.0205 757  GLN B CB  
14520 C CG  . GLN B 759  ? 0.2061 0.2208 0.1930 0.0229  0.0204  -0.0207 757  GLN B CG  
14521 C CD  . GLN B 759  ? 0.1864 0.2047 0.1737 0.0235  0.0226  -0.0190 757  GLN B CD  
14522 O OE1 . GLN B 759  ? 0.2340 0.2531 0.2194 0.0251  0.0247  -0.0197 757  GLN B OE1 
14523 N NE2 . GLN B 759  ? 0.2110 0.2316 0.2006 0.0222  0.0223  -0.0167 757  GLN B NE2 
14524 N N   . LEU B 760  ? 0.1957 0.2051 0.1915 0.0242  0.0178  -0.0232 758  LEU B N   
14525 C CA  . LEU B 760  ? 0.1726 0.1819 0.1725 0.0249  0.0175  -0.0232 758  LEU B CA  
14526 C C   . LEU B 760  ? 0.2027 0.2150 0.2051 0.0270  0.0197  -0.0227 758  LEU B C   
14527 O O   . LEU B 760  ? 0.2103 0.2221 0.2099 0.0288  0.0212  -0.0239 758  LEU B O   
14528 C CB  . LEU B 760  ? 0.2180 0.2227 0.2154 0.0253  0.0162  -0.0252 758  LEU B CB  
14529 C CG  . LEU B 760  ? 0.1857 0.1900 0.1869 0.0260  0.0157  -0.0251 758  LEU B CG  
14530 C CD1 . LEU B 760  ? 0.2167 0.2213 0.2207 0.0240  0.0138  -0.0240 758  LEU B CD1 
14531 C CD2 . LEU B 760  ? 0.2217 0.2213 0.2198 0.0273  0.0152  -0.0271 758  LEU B CD2 
14532 N N   . LEU B 761  ? 0.1826 0.1980 0.1903 0.0267  0.0198  -0.0211 759  LEU B N   
14533 C CA  . LEU B 761  ? 0.1945 0.2137 0.2056 0.0284  0.0218  -0.0203 759  LEU B CA  
14534 C C   . LEU B 761  ? 0.1897 0.2090 0.2049 0.0290  0.0209  -0.0203 759  LEU B C   
14535 O O   . LEU B 761  ? 0.1948 0.2164 0.2144 0.0277  0.0202  -0.0188 759  LEU B O   
14536 C CB  . LEU B 761  ? 0.1922 0.2159 0.2060 0.0272  0.0229  -0.0181 759  LEU B CB  
14537 C CG  . LEU B 761  ? 0.2144 0.2388 0.2246 0.0267  0.0239  -0.0176 759  LEU B CG  
14538 C CD1 . LEU B 761  ? 0.2352 0.2580 0.2404 0.0286  0.0253  -0.0194 759  LEU B CD1 
14539 C CD2 . LEU B 761  ? 0.2581 0.2803 0.2663 0.0246  0.0220  -0.0173 759  LEU B CD2 
14540 N N   . PRO B 762  ? 0.1857 0.2023 0.1995 0.0308  0.0208  -0.0220 760  PRO B N   
14541 C CA  . PRO B 762  ? 0.1677 0.1845 0.1854 0.0316  0.0199  -0.0219 760  PRO B CA  
14542 C C   . PRO B 762  ? 0.1734 0.1957 0.1961 0.0327  0.0216  -0.0204 760  PRO B C   
14543 O O   . PRO B 762  ? 0.2020 0.2274 0.2246 0.0339  0.0238  -0.0201 760  PRO B O   
14544 C CB  . PRO B 762  ? 0.1794 0.1917 0.1936 0.0337  0.0198  -0.0240 760  PRO B CB  
14545 C CG  . PRO B 762  ? 0.2012 0.2100 0.2094 0.0331  0.0198  -0.0254 760  PRO B CG  
14546 C CD  . PRO B 762  ? 0.1813 0.1941 0.1897 0.0324  0.0213  -0.0241 760  PRO B CD  
14547 N N   . GLY B 763  ? 0.1681 0.1918 0.1953 0.0323  0.0204  -0.0195 761  GLY B N   
14548 C CA  . GLY B 763  ? 0.1903 0.2193 0.2227 0.0334  0.0215  -0.0181 761  GLY B CA  
14549 C C   . GLY B 763  ? 0.1844 0.2152 0.2214 0.0312  0.0198  -0.0165 761  GLY B C   
14550 O O   . GLY B 763  ? 0.2030 0.2306 0.2389 0.0294  0.0178  -0.0167 761  GLY B O   
14551 N N   . ASP B 764  ? 0.2125 0.2486 0.2545 0.0315  0.0207  -0.0149 762  ASP B N   
14552 C CA  . ASP B 764  ? 0.2257 0.2635 0.2721 0.0296  0.0190  -0.0135 762  ASP B CA  
14553 C C   . ASP B 764  ? 0.2466 0.2865 0.2941 0.0269  0.0191  -0.0118 762  ASP B C   
14554 O O   . ASP B 764  ? 0.2067 0.2454 0.2508 0.0262  0.0200  -0.0119 762  ASP B O   
14555 C CB  . ASP B 764  ? 0.2553 0.2974 0.3067 0.0313  0.0192  -0.0128 762  ASP B CB  
14556 C CG  . ASP B 764  ? 0.3133 0.3618 0.3678 0.0321  0.0217  -0.0115 762  ASP B CG  
14557 O OD1 . ASP B 764  ? 0.2501 0.3000 0.3035 0.0308  0.0231  -0.0107 762  ASP B OD1 
14558 O OD2 . ASP B 764  ? 0.3708 0.4231 0.4290 0.0341  0.0224  -0.0111 762  ASP B OD2 
14559 N N   . GLY B 765  ? 0.2151 0.2575 0.2669 0.0251  0.0180  -0.0103 763  GLY B N   
14560 C CA  . GLY B 765  ? 0.1881 0.2314 0.2408 0.0224  0.0178  -0.0087 763  GLY B CA  
14561 C C   . GLY B 765  ? 0.2055 0.2526 0.2586 0.0223  0.0202  -0.0074 763  GLY B C   
14562 O O   . GLY B 765  ? 0.2182 0.2648 0.2702 0.0203  0.0203  -0.0064 763  GLY B O   
14563 N N   . ARG B 766  ? 0.2121 0.2633 0.2667 0.0245  0.0223  -0.0074 764  ARG B N   
14564 C CA  . ARG B 766  ? 0.2286 0.2836 0.2832 0.0245  0.0248  -0.0062 764  ARG B CA  
14565 C C   . ARG B 766  ? 0.1985 0.2499 0.2472 0.0248  0.0256  -0.0072 764  ARG B C   
14566 O O   . ARG B 766  ? 0.2137 0.2666 0.2614 0.0235  0.0268  -0.0058 764  ARG B O   
14567 C CB  . ARG B 766  ? 0.2321 0.2922 0.2892 0.0273  0.0270  -0.0062 764  ARG B CB  
14568 C CG  . ARG B 766  ? 0.2843 0.3491 0.3478 0.0271  0.0263  -0.0049 764  ARG B CG  
14569 C CD  . ARG B 766  ? 0.3378 0.4069 0.4033 0.0305  0.0284  -0.0053 764  ARG B CD  
14570 N NE  . ARG B 766  ? 0.3841 0.4483 0.4459 0.0334  0.0278  -0.0078 764  ARG B NE  
14571 C CZ  . ARG B 766  ? 0.4301 0.4959 0.4919 0.0370  0.0295  -0.0089 764  ARG B CZ  
14572 N NH1 . ARG B 766  ? 0.4350 0.5076 0.5003 0.0385  0.0319  -0.0077 764  ARG B NH1 
14573 N NH2 . ARG B 766  ? 0.4715 0.5318 0.5295 0.0392  0.0287  -0.0112 764  ARG B NH2 
14574 N N   . VAL B 767  ? 0.1928 0.2395 0.2374 0.0262  0.0249  -0.0094 765  VAL B N   
14575 C CA  . VAL B 767  ? 0.1864 0.2296 0.2254 0.0262  0.0253  -0.0104 765  VAL B CA  
14576 C C   . VAL B 767  ? 0.1764 0.2171 0.2143 0.0235  0.0236  -0.0095 765  VAL B C   
14577 O O   . VAL B 767  ? 0.2019 0.2424 0.2372 0.0226  0.0244  -0.0088 765  VAL B O   
14578 C CB  . VAL B 767  ? 0.1821 0.2208 0.2171 0.0282  0.0247  -0.0130 765  VAL B CB  
14579 C CG1 . VAL B 767  ? 0.2082 0.2435 0.2373 0.0279  0.0249  -0.0140 765  VAL B CG1 
14580 C CG2 . VAL B 767  ? 0.2144 0.2553 0.2502 0.0313  0.0265  -0.0138 765  VAL B CG2 
14581 N N   . GLY B 768  ? 0.1746 0.2133 0.2144 0.0223  0.0213  -0.0096 766  GLY B N   
14582 C CA  . GLY B 768  ? 0.1947 0.2312 0.2338 0.0199  0.0199  -0.0087 766  GLY B CA  
14583 C C   . GLY B 768  ? 0.1872 0.2269 0.2285 0.0182  0.0207  -0.0064 766  GLY B C   
14584 O O   . GLY B 768  ? 0.1863 0.2246 0.2253 0.0171  0.0207  -0.0056 766  GLY B O   
14585 N N   . ALA B 769  ? 0.1833 0.2273 0.2291 0.0181  0.0215  -0.0051 767  ALA B N   
14586 C CA  . ALA B 769  ? 0.1988 0.2458 0.2470 0.0161  0.0223  -0.0027 767  ALA B CA  
14587 C C   . ALA B 769  ? 0.2169 0.2654 0.2622 0.0165  0.0245  -0.0020 767  ALA B C   
14588 O O   . ALA B 769  ? 0.2006 0.2488 0.2450 0.0147  0.0247  -0.0003 767  ALA B O   
14589 C CB  . ALA B 769  ? 0.1971 0.2491 0.2509 0.0159  0.0227  -0.0014 767  ALA B CB  
14590 N N   . ALA B 770  ? 0.1825 0.2324 0.2260 0.0190  0.0263  -0.0032 768  ALA B N   
14591 C CA  . ALA B 770  ? 0.1733 0.2246 0.2136 0.0195  0.0286  -0.0027 768  ALA B CA  
14592 C C   . ALA B 770  ? 0.1989 0.2457 0.2341 0.0188  0.0276  -0.0032 768  ALA B C   
14593 O O   . ALA B 770  ? 0.2228 0.2703 0.2560 0.0179  0.0286  -0.0018 768  ALA B O   
14594 C CB  . ALA B 770  ? 0.1896 0.2424 0.2284 0.0226  0.0305  -0.0044 768  ALA B CB  
14595 N N   . LEU B 771  ? 0.1832 0.2255 0.2164 0.0191  0.0256  -0.0050 769  LEU B N   
14596 C CA  . LEU B 771  ? 0.1848 0.2234 0.2137 0.0185  0.0246  -0.0054 769  LEU B CA  
14597 C C   . LEU B 771  ? 0.2027 0.2405 0.2327 0.0162  0.0234  -0.0034 769  LEU B C   
14598 O O   . LEU B 771  ? 0.2237 0.2608 0.2510 0.0155  0.0237  -0.0024 769  LEU B O   
14599 C CB  . LEU B 771  ? 0.1985 0.2331 0.2254 0.0192  0.0227  -0.0077 769  LEU B CB  
14600 C CG  . LEU B 771  ? 0.1779 0.2118 0.2021 0.0214  0.0236  -0.0099 769  LEU B CG  
14601 C CD1 . LEU B 771  ? 0.1957 0.2257 0.2188 0.0216  0.0216  -0.0118 769  LEU B CD1 
14602 C CD2 . LEU B 771  ? 0.1877 0.2212 0.2069 0.0219  0.0249  -0.0102 769  LEU B CD2 
14603 N N   . VAL B 772  ? 0.1836 0.2215 0.2176 0.0150  0.0221  -0.0029 770  VAL B N   
14604 C CA  . VAL B 772  ? 0.1764 0.2127 0.2114 0.0129  0.0209  -0.0011 770  VAL B CA  
14605 C C   . VAL B 772  ? 0.2486 0.2876 0.2841 0.0117  0.0224  0.0013  770  VAL B C   
14606 O O   . VAL B 772  ? 0.2471 0.2842 0.2808 0.0105  0.0219  0.0026  770  VAL B O   
14607 C CB  . VAL B 772  ? 0.1968 0.2329 0.2360 0.0119  0.0193  -0.0011 770  VAL B CB  
14608 C CG1 . VAL B 772  ? 0.2166 0.2515 0.2571 0.0096  0.0183  0.0009  770  VAL B CG1 
14609 C CG2 . VAL B 772  ? 0.2033 0.2361 0.2413 0.0128  0.0175  -0.0033 770  VAL B CG2 
14610 N N   . ALA B 773  ? 0.2259 0.2694 0.2638 0.0121  0.0244  0.0021  771  ALA B N   
14611 C CA  . ALA B 773  ? 0.2205 0.2672 0.2593 0.0107  0.0260  0.0046  771  ALA B CA  
14612 C C   . ALA B 773  ? 0.2732 0.3202 0.3075 0.0116  0.0277  0.0049  771  ALA B C   
14613 O O   . ALA B 773  ? 0.2839 0.3328 0.3181 0.0103  0.0290  0.0073  771  ALA B O   
14614 C CB  . ALA B 773  ? 0.2467 0.2989 0.2901 0.0109  0.0276  0.0054  771  ALA B CB  
14615 N N   . ALA B 774  ? 0.2393 0.2844 0.2697 0.0135  0.0278  0.0027  772  ALA B N   
14616 C CA  . ALA B 774  ? 0.2388 0.2844 0.2646 0.0144  0.0294  0.0028  772  ALA B CA  
14617 C C   . ALA B 774  ? 0.2701 0.3135 0.2934 0.0128  0.0286  0.0046  772  ALA B C   
14618 O O   . ALA B 774  ? 0.2678 0.3077 0.2912 0.0119  0.0264  0.0047  772  ALA B O   
14619 C CB  . ALA B 774  ? 0.2703 0.3135 0.2922 0.0165  0.0290  -0.0001 772  ALA B CB  
14620 N N   . ALA B 775  ? 0.2975 0.3429 0.3183 0.0127  0.0305  0.0061  773  ALA B N   
14621 C CA  . ALA B 775  ? 0.2821 0.3260 0.3010 0.0111  0.0300  0.0085  773  ALA B CA  
14622 C C   . ALA B 775  ? 0.2708 0.3102 0.2861 0.0114  0.0278  0.0076  773  ALA B C   
14623 O O   . ALA B 775  ? 0.2920 0.3288 0.3073 0.0101  0.0264  0.0091  773  ALA B O   
14624 C CB  . ALA B 775  ? 0.3361 0.3831 0.3524 0.0111  0.0325  0.0101  773  ALA B CB  
14625 N N   . GLU B 776  ? 0.2473 0.2855 0.2594 0.0131  0.0276  0.0051  774  GLU B N   
14626 C CA  . GLU B 776  ? 0.2406 0.2754 0.2492 0.0133  0.0257  0.0044  774  GLU B CA  
14627 C C   . GLU B 776  ? 0.2075 0.2395 0.2180 0.0134  0.0234  0.0028  774  GLU B C   
14628 O O   . GLU B 776  ? 0.2231 0.2527 0.2313 0.0136  0.0217  0.0021  774  GLU B O   
14629 C CB  . GLU B 776  ? 0.2155 0.2505 0.2192 0.0147  0.0264  0.0027  774  GLU B CB  
14630 C CG  . GLU B 776  ? 0.3196 0.3574 0.3206 0.0149  0.0288  0.0041  774  GLU B CG  
14631 C CD  . GLU B 776  ? 0.4199 0.4612 0.4226 0.0158  0.0313  0.0035  774  GLU B CD  
14632 O OE1 . GLU B 776  ? 0.3483 0.3899 0.3545 0.0164  0.0311  0.0020  774  GLU B OE1 
14633 O OE2 . GLU B 776  ? 0.4396 0.4835 0.4402 0.0161  0.0335  0.0046  774  GLU B OE2 
14634 N N   . THR B 777  ? 0.2198 0.2524 0.2345 0.0132  0.0232  0.0022  775  THR B N   
14635 C CA  . THR B 777  ? 0.2035 0.2334 0.2199 0.0131  0.0211  0.0008  775  THR B CA  
14636 C C   . THR B 777  ? 0.2043 0.2317 0.2209 0.0121  0.0195  0.0023  775  THR B C   
14637 O O   . THR B 777  ? 0.2252 0.2527 0.2434 0.0108  0.0197  0.0045  775  THR B O   
14638 C CB  . THR B 777  ? 0.2102 0.2414 0.2309 0.0130  0.0213  0.0003  775  THR B CB  
14639 O OG1 . THR B 777  ? 0.2267 0.2597 0.2469 0.0145  0.0225  -0.0014 775  THR B OG1 
14640 C CG2 . THR B 777  ? 0.2037 0.2321 0.2261 0.0128  0.0191  -0.0008 775  THR B CG2 
14641 N N   . ALA B 778  ? 0.1789 0.2038 0.1934 0.0126  0.0178  0.0012  776  ALA B N   
14642 C CA  . ALA B 778  ? 0.1805 0.2030 0.1946 0.0121  0.0163  0.0025  776  ALA B CA  
14643 C C   . ALA B 778  ? 0.1880 0.2083 0.2044 0.0120  0.0146  0.0015  776  ALA B C   
14644 O O   . ALA B 778  ? 0.2139 0.2319 0.2302 0.0118  0.0134  0.0024  776  ALA B O   
14645 C CB  . ALA B 778  ? 0.1974 0.2194 0.2074 0.0129  0.0157  0.0024  776  ALA B CB  
14646 N N   . GLY B 779  ? 0.1621 0.1828 0.1802 0.0123  0.0145  -0.0003 777  GLY B N   
14647 C CA  . GLY B 779  ? 0.1697 0.1885 0.1899 0.0121  0.0129  -0.0013 777  GLY B CA  
14648 C C   . GLY B 779  ? 0.1829 0.2027 0.2048 0.0125  0.0132  -0.0030 777  GLY B C   
14649 O O   . GLY B 779  ? 0.1854 0.2068 0.2062 0.0132  0.0142  -0.0039 777  GLY B O   
14650 N N   . VAL B 780  ? 0.1630 0.1816 0.1875 0.0120  0.0121  -0.0035 778  VAL B N   
14651 C CA  . VAL B 780  ? 0.1568 0.1762 0.1832 0.0123  0.0121  -0.0049 778  VAL B CA  
14652 C C   . VAL B 780  ? 0.1470 0.1641 0.1735 0.0124  0.0104  -0.0062 778  VAL B C   
14653 O O   . VAL B 780  ? 0.1591 0.1743 0.1862 0.0118  0.0094  -0.0057 778  VAL B O   
14654 C CB  . VAL B 780  ? 0.1516 0.1727 0.1814 0.0115  0.0127  -0.0040 778  VAL B CB  
14655 C CG1 . VAL B 780  ? 0.1831 0.2050 0.2149 0.0121  0.0125  -0.0055 778  VAL B CG1 
14656 C CG2 . VAL B 780  ? 0.1861 0.2101 0.2158 0.0115  0.0147  -0.0027 778  VAL B CG2 
14657 N N   . MET B 781  ? 0.1531 0.1701 0.1787 0.0131  0.0102  -0.0079 779  MET B N   
14658 C CA  . MET B 781  ? 0.1559 0.1712 0.1818 0.0131  0.0087  -0.0092 779  MET B CA  
14659 C C   . MET B 781  ? 0.1627 0.1786 0.1908 0.0133  0.0088  -0.0099 779  MET B C   
14660 O O   . MET B 781  ? 0.1697 0.1867 0.1973 0.0140  0.0096  -0.0107 779  MET B O   
14661 C CB  . MET B 781  ? 0.1619 0.1766 0.1850 0.0137  0.0083  -0.0103 779  MET B CB  
14662 C CG  . MET B 781  ? 0.1921 0.2068 0.2131 0.0138  0.0083  -0.0094 779  MET B CG  
14663 S SD  . MET B 781  ? 0.1868 0.2015 0.2046 0.0141  0.0077  -0.0106 779  MET B SD  
14664 C CE  . MET B 781  ? 0.1748 0.1882 0.1937 0.0140  0.0062  -0.0113 779  MET B CE  
14665 N N   . PHE B 782  ? 0.1609 0.1761 0.1913 0.0126  0.0079  -0.0097 780  PHE B N   
14666 C CA  . PHE B 782  ? 0.1568 0.1729 0.1896 0.0126  0.0077  -0.0101 780  PHE B CA  
14667 C C   . PHE B 782  ? 0.1425 0.1566 0.1753 0.0124  0.0061  -0.0111 780  PHE B C   
14668 O O   . PHE B 782  ? 0.1741 0.1864 0.2066 0.0118  0.0052  -0.0109 780  PHE B O   
14669 C CB  . PHE B 782  ? 0.1644 0.1821 0.2003 0.0117  0.0080  -0.0087 780  PHE B CB  
14670 C CG  . PHE B 782  ? 0.1528 0.1716 0.1916 0.0116  0.0075  -0.0090 780  PHE B CG  
14671 C CD1 . PHE B 782  ? 0.1550 0.1763 0.1949 0.0127  0.0085  -0.0093 780  PHE B CD1 
14672 C CD2 . PHE B 782  ? 0.1640 0.1814 0.2041 0.0106  0.0059  -0.0090 780  PHE B CD2 
14673 C CE1 . PHE B 782  ? 0.1871 0.2097 0.2298 0.0129  0.0080  -0.0095 780  PHE B CE1 
14674 C CE2 . PHE B 782  ? 0.1759 0.1946 0.2187 0.0106  0.0052  -0.0092 780  PHE B CE2 
14675 C CZ  . PHE B 782  ? 0.1886 0.2101 0.2329 0.0117  0.0063  -0.0093 780  PHE B CZ  
14676 N N   . THR B 783  ? 0.1586 0.1726 0.1915 0.0130  0.0059  -0.0122 781  THR B N   
14677 C CA  . THR B 783  ? 0.1726 0.1851 0.2059 0.0128  0.0044  -0.0129 781  THR B CA  
14678 C C   . THR B 783  ? 0.1704 0.1843 0.2062 0.0131  0.0044  -0.0130 781  THR B C   
14679 O O   . THR B 783  ? 0.1674 0.1824 0.2031 0.0142  0.0053  -0.0134 781  THR B O   
14680 C CB  . THR B 783  ? 0.1750 0.1858 0.2055 0.0131  0.0039  -0.0141 781  THR B CB  
14681 O OG1 . THR B 783  ? 0.1781 0.1883 0.2067 0.0129  0.0040  -0.0139 781  THR B OG1 
14682 C CG2 . THR B 783  ? 0.1912 0.2004 0.2219 0.0127  0.0025  -0.0147 781  THR B CG2 
14683 N N   . GLY B 784  ? 0.1644 0.1782 0.2023 0.0123  0.0032  -0.0126 782  GLY B N   
14684 C CA  . GLY B 784  ? 0.1599 0.1756 0.2006 0.0126  0.0031  -0.0124 782  GLY B CA  
14685 C C   . GLY B 784  ? 0.1776 0.1934 0.2207 0.0113  0.0018  -0.0116 782  GLY B C   
14686 O O   . GLY B 784  ? 0.1921 0.2056 0.2339 0.0103  0.0008  -0.0118 782  GLY B O   
14687 N N   . SER B 785  ? 0.1887 0.2073 0.2351 0.0112  0.0018  -0.0109 783  SER B N   
14688 C CA  . SER B 785  ? 0.2263 0.2451 0.2750 0.0097  0.0003  -0.0102 783  SER B CA  
14689 C C   . SER B 785  ? 0.2112 0.2299 0.2604 0.0081  0.0005  -0.0091 783  SER B C   
14690 O O   . SER B 785  ? 0.2101 0.2302 0.2594 0.0082  0.0021  -0.0083 783  SER B O   
14691 C CB  . SER B 785  ? 0.2069 0.2295 0.2596 0.0100  0.0002  -0.0096 783  SER B CB  
14692 O OG  . SER B 785  ? 0.2079 0.2341 0.2628 0.0103  0.0019  -0.0085 783  SER B OG  
14693 N N   . THR B 786  ? 0.2149 0.2316 0.2642 0.0065  -0.0011 -0.0090 784  THR B N   
14694 C CA  . THR B 786  ? 0.2103 0.2261 0.2600 0.0049  -0.0012 -0.0079 784  THR B CA  
14695 C C   . THR B 786  ? 0.1959 0.2160 0.2494 0.0040  -0.0003 -0.0062 784  THR B C   
14696 O O   . THR B 786  ? 0.2317 0.2520 0.2851 0.0032  0.0007  -0.0050 784  THR B O   
14697 C CB  . THR B 786  ? 0.2372 0.2500 0.2863 0.0034  -0.0034 -0.0082 784  THR B CB  
14698 O OG1 . THR B 786  ? 0.2621 0.2716 0.3078 0.0044  -0.0040 -0.0097 784  THR B OG1 
14699 C CG2 . THR B 786  ? 0.2904 0.3011 0.3390 0.0017  -0.0036 -0.0072 784  THR B CG2 
14700 N N   . GLU B 787  ? 0.2354 0.2589 0.2921 0.0041  -0.0006 -0.0059 785  GLU B N   
14701 C CA  . GLU B 787  ? 0.2546 0.2830 0.3154 0.0034  0.0003  -0.0042 785  GLU B CA  
14702 C C   . GLU B 787  ? 0.2517 0.2822 0.3121 0.0046  0.0029  -0.0037 785  GLU B C   
14703 O O   . GLU B 787  ? 0.2228 0.2554 0.2846 0.0034  0.0039  -0.0021 785  GLU B O   
14704 C CB  . GLU B 787  ? 0.2633 0.2954 0.3276 0.0040  -0.0003 -0.0042 785  GLU B CB  
14705 N N   . VAL B 788  ? 0.1881 0.2181 0.2463 0.0069  0.0038  -0.0050 786  VAL B N   
14706 C CA  . VAL B 788  ? 0.1841 0.2158 0.2412 0.0082  0.0061  -0.0048 786  VAL B CA  
14707 C C   . VAL B 788  ? 0.1921 0.2209 0.2462 0.0073  0.0066  -0.0044 786  VAL B C   
14708 O O   . VAL B 788  ? 0.2050 0.2357 0.2592 0.0070  0.0082  -0.0032 786  VAL B O   
14709 C CB  . VAL B 788  ? 0.1947 0.2257 0.2496 0.0106  0.0068  -0.0064 786  VAL B CB  
14710 C CG1 . VAL B 788  ? 0.2002 0.2318 0.2529 0.0118  0.0089  -0.0065 786  VAL B CG1 
14711 C CG2 . VAL B 788  ? 0.2055 0.2397 0.2636 0.0118  0.0067  -0.0066 786  VAL B CG2 
14712 N N   . ALA B 789  ? 0.2023 0.2267 0.2536 0.0069  0.0052  -0.0052 787  ALA B N   
14713 C CA  . ALA B 789  ? 0.1777 0.1994 0.2262 0.0064  0.0054  -0.0048 787  ALA B CA  
14714 C C   . ALA B 789  ? 0.1780 0.2005 0.2284 0.0043  0.0056  -0.0028 787  ALA B C   
14715 O O   . ALA B 789  ? 0.1851 0.2073 0.2341 0.0041  0.0066  -0.0018 787  ALA B O   
14716 C CB  . ALA B 789  ? 0.1748 0.1920 0.2206 0.0063  0.0038  -0.0060 787  ALA B CB  
14717 N N   . ARG B 790  ? 0.1895 0.2129 0.2429 0.0027  0.0044  -0.0022 788  ARG B N   
14718 C CA  . ARG B 790  ? 0.2189 0.2428 0.2740 0.0004  0.0043  -0.0002 788  ARG B CA  
14719 C C   . ARG B 790  ? 0.2095 0.2383 0.2667 0.0003  0.0064  0.0014  788  ARG B C   
14720 O O   . ARG B 790  ? 0.2507 0.2794 0.3078 -0.0010 0.0071  0.0031  788  ARG B O   
14721 C CB  . ARG B 790  ? 0.2668 0.2909 0.3248 -0.0015 0.0023  0.0001  788  ARG B CB  
14722 C CG  . ARG B 790  ? 0.4008 0.4232 0.4595 -0.0044 0.0014  0.0017  788  ARG B CG  
14723 C CD  . ARG B 790  ? 0.3563 0.3784 0.4173 -0.0063 -0.0009 0.0017  788  ARG B CD  
14724 N NE  . ARG B 790  ? 0.3773 0.3951 0.4355 -0.0054 -0.0026 -0.0004 788  ARG B NE  
14725 C CZ  . ARG B 790  ? 0.4180 0.4300 0.4726 -0.0058 -0.0037 -0.0011 788  ARG B CZ  
14726 N NH1 . ARG B 790  ? 0.3812 0.3904 0.4343 -0.0069 -0.0034 0.0000  788  ARG B NH1 
14727 N NH2 . ARG B 790  ? 0.4259 0.4348 0.4783 -0.0049 -0.0051 -0.0030 788  ARG B NH2 
14728 N N   . LEU B 791  ? 0.1957 0.2287 0.2548 0.0020  0.0076  0.0009  789  LEU B N   
14729 C CA  . LEU B 791  ? 0.2413 0.2792 0.3021 0.0024  0.0100  0.0022  789  LEU B CA  
14730 C C   . LEU B 791  ? 0.2309 0.2671 0.2877 0.0034  0.0115  0.0022  789  LEU B C   
14731 O O   . LEU B 791  ? 0.2280 0.2663 0.2851 0.0026  0.0130  0.0040  789  LEU B O   
14732 C CB  . LEU B 791  ? 0.2287 0.2706 0.2916 0.0045  0.0108  0.0013  789  LEU B CB  
14733 C CG  . LEU B 791  ? 0.2636 0.3080 0.3308 0.0038  0.0094  0.0015  789  LEU B CG  
14734 C CD1 . LEU B 791  ? 0.2586 0.3068 0.3275 0.0064  0.0104  0.0006  789  LEU B CD1 
14735 C CD2 . LEU B 791  ? 0.2524 0.3003 0.3236 0.0011  0.0093  0.0039  789  LEU B CD2 
14736 N N   . ILE B 792  ? 0.2133 0.2462 0.2665 0.0051  0.0111  0.0004  790  ILE B N   
14737 C CA  . ILE B 792  ? 0.2107 0.2420 0.2601 0.0061  0.0123  0.0003  790  ILE B CA  
14738 C C   . ILE B 792  ? 0.1959 0.2244 0.2438 0.0043  0.0118  0.0018  790  ILE B C   
14739 O O   . ILE B 792  ? 0.2313 0.2604 0.2777 0.0042  0.0131  0.0030  790  ILE B O   
14740 C CB  . ILE B 792  ? 0.1874 0.2158 0.2336 0.0079  0.0117  -0.0019 790  ILE B CB  
14741 C CG1 . ILE B 792  ? 0.1869 0.2178 0.2338 0.0097  0.0125  -0.0032 790  ILE B CG1 
14742 C CG2 . ILE B 792  ? 0.2037 0.2300 0.2459 0.0084  0.0122  -0.0019 790  ILE B CG2 
14743 C CD1 . ILE B 792  ? 0.2072 0.2352 0.2516 0.0111  0.0116  -0.0053 790  ILE B CD1 
14744 N N   . GLN B 793  ? 0.2026 0.2276 0.2507 0.0031  0.0098  0.0016  791  GLN B N   
14745 C CA  . GLN B 793  ? 0.2018 0.2233 0.2484 0.0016  0.0090  0.0029  791  GLN B CA  
14746 C C   . GLN B 793  ? 0.2020 0.2260 0.2507 -0.0004 0.0100  0.0054  791  GLN B C   
14747 O O   . GLN B 793  ? 0.2323 0.2549 0.2791 -0.0010 0.0106  0.0068  791  GLN B O   
14748 C CB  . GLN B 793  ? 0.2292 0.2468 0.2760 0.0006  0.0067  0.0021  791  GLN B CB  
14749 C CG  . GLN B 793  ? 0.2212 0.2344 0.2663 -0.0008 0.0058  0.0032  791  GLN B CG  
14750 C CD  . GLN B 793  ? 0.2849 0.2949 0.3308 -0.0023 0.0036  0.0028  791  GLN B CD  
14751 O OE1 . GLN B 793  ? 0.2880 0.3004 0.3370 -0.0034 0.0030  0.0028  791  GLN B OE1 
14752 N NE2 . GLN B 793  ? 0.3143 0.3190 0.3572 -0.0022 0.0024  0.0023  791  GLN B NE2 
14753 N N   . ALA B 794  ? 0.2448 0.2728 0.2976 -0.0015 0.0102  0.0060  792  ALA B N   
14754 C CA  . ALA B 794  ? 0.2510 0.2822 0.3062 -0.0036 0.0112  0.0086  792  ALA B CA  
14755 C C   . ALA B 794  ? 0.2707 0.3052 0.3248 -0.0025 0.0138  0.0095  792  ALA B C   
14756 O O   . ALA B 794  ? 0.2702 0.3048 0.3237 -0.0040 0.0147  0.0117  792  ALA B O   
14757 C CB  . ALA B 794  ? 0.2920 0.3277 0.3523 -0.0048 0.0109  0.0091  792  ALA B CB  
14758 N N   . GLN B 795  ? 0.2482 0.2852 0.3017 0.0001  0.0151  0.0080  793  GLN B N   
14759 C CA  . GLN B 795  ? 0.2419 0.2816 0.2936 0.0014  0.0175  0.0085  793  GLN B CA  
14760 C C   . GLN B 795  ? 0.2294 0.2651 0.2766 0.0013  0.0175  0.0091  793  GLN B C   
14761 O O   . GLN B 795  ? 0.2522 0.2893 0.2984 0.0006  0.0190  0.0109  793  GLN B O   
14762 C CB  . GLN B 795  ? 0.2626 0.3037 0.3131 0.0043  0.0184  0.0062  793  GLN B CB  
14763 C CG  . GLN B 795  ? 0.3295 0.3755 0.3838 0.0052  0.0193  0.0057  793  GLN B CG  
14764 C CD  . GLN B 795  ? 0.3404 0.3866 0.3926 0.0083  0.0202  0.0034  793  GLN B CD  
14765 O OE1 . GLN B 795  ? 0.3657 0.4089 0.4168 0.0093  0.0187  0.0014  793  GLN B OE1 
14766 N NE2 . GLN B 795  ? 0.3213 0.3708 0.3726 0.0097  0.0226  0.0036  793  GLN B NE2 
14767 N N   . LEU B 796  ? 0.1931 0.2239 0.2377 0.0021  0.0158  0.0075  794  LEU B N   
14768 C CA  . LEU B 796  ? 0.2064 0.2338 0.2468 0.0025  0.0156  0.0079  794  LEU B CA  
14769 C C   . LEU B 796  ? 0.2480 0.2729 0.2881 0.0003  0.0151  0.0102  794  LEU B C   
14770 O O   . LEU B 796  ? 0.2811 0.3048 0.3184 0.0004  0.0157  0.0115  794  LEU B O   
14771 C CB  . LEU B 796  ? 0.2026 0.2260 0.2407 0.0039  0.0140  0.0057  794  LEU B CB  
14772 C CG  . LEU B 796  ? 0.2297 0.2546 0.2667 0.0061  0.0145  0.0035  794  LEU B CG  
14773 C CD1 . LEU B 796  ? 0.2200 0.2412 0.2551 0.0071  0.0128  0.0017  794  LEU B CD1 
14774 C CD2 . LEU B 796  ? 0.2182 0.2449 0.2524 0.0072  0.0163  0.0038  794  LEU B CD2 
14775 N N   . ALA B 797  ? 0.2419 0.2656 0.2848 -0.0017 0.0137  0.0109  795  ALA B N   
14776 C CA  . ALA B 797  ? 0.3047 0.3251 0.3472 -0.0039 0.0129  0.0130  795  ALA B CA  
14777 C C   . ALA B 797  ? 0.2908 0.3145 0.3341 -0.0055 0.0147  0.0158  795  ALA B C   
14778 O O   . ALA B 797  ? 0.3204 0.3410 0.3622 -0.0072 0.0143  0.0179  795  ALA B O   
14779 C CB  . ALA B 797  ? 0.3117 0.3301 0.3568 -0.0058 0.0109  0.0129  795  ALA B CB  
14780 N N   . ASP B 798  ? 0.2900 0.3197 0.3353 -0.0050 0.0167  0.0160  796  ASP B N   
14781 C CA  . ASP B 798  ? 0.3502 0.3836 0.3959 -0.0062 0.0188  0.0185  796  ASP B CA  
14782 C C   . ASP B 798  ? 0.3486 0.3808 0.3896 -0.0048 0.0199  0.0190  796  ASP B C   
14783 O O   . ASP B 798  ? 0.3647 0.3989 0.4050 -0.0059 0.0215  0.0214  796  ASP B O   
14784 C CB  . ASP B 798  ? 0.3390 0.3794 0.3881 -0.0057 0.0208  0.0184  796  ASP B CB  
14785 N N   . ARG B 799  ? 0.3074 0.3366 0.3451 -0.0024 0.0191  0.0168  797  ARG B N   
14786 C CA  A ARG B 799  ? 0.3369 0.3658 0.3704 -0.0008 0.0202  0.0168  797  ARG B CA  
14787 C CA  B ARG B 799  ? 0.3369 0.3659 0.3705 -0.0009 0.0202  0.0170  797  ARG B CA  
14788 C C   . ARG B 799  ? 0.3210 0.3441 0.3511 -0.0004 0.0184  0.0169  797  ARG B C   
14789 O O   . ARG B 799  ? 0.3075 0.3268 0.3383 -0.0007 0.0164  0.0161  797  ARG B O   
14790 C CB  A ARG B 799  ? 0.3482 0.3792 0.3808 0.0019  0.0208  0.0140  797  ARG B CB  
14791 C CB  B ARG B 799  ? 0.3570 0.3888 0.3896 0.0017  0.0213  0.0145  797  ARG B CB  
14792 C CG  A ARG B 799  ? 0.3449 0.3808 0.3812 0.0022  0.0220  0.0131  797  ARG B CG  
14793 C CG  B ARG B 799  ? 0.3560 0.3933 0.3924 0.0018  0.0229  0.0141  797  ARG B CG  
14794 C CD  A ARG B 799  ? 0.3286 0.3650 0.3633 0.0049  0.0223  0.0102  797  ARG B CD  
14795 C CD  B ARG B 799  ? 0.3440 0.3846 0.3781 0.0039  0.0250  0.0130  797  ARG B CD  
14796 N NE  A ARG B 799  ? 0.3656 0.4007 0.3955 0.0061  0.0227  0.0100  797  ARG B NE  
14797 N NE  B ARG B 799  ? 0.3705 0.4077 0.4002 0.0056  0.0241  0.0113  797  ARG B NE  
14798 C CZ  A ARG B 799  ? 0.3290 0.3618 0.3560 0.0078  0.0219  0.0078  797  ARG B CZ  
14799 C CZ  B ARG B 799  ? 0.3370 0.3730 0.3662 0.0073  0.0232  0.0086  797  ARG B CZ  
14800 N NH1 A ARG B 799  ? 0.2659 0.2977 0.2942 0.0086  0.0207  0.0056  797  ARG B NH1 
14801 N NH1 B ARG B 799  ? 0.3022 0.3398 0.3344 0.0079  0.0232  0.0072  797  ARG B NH1 
14802 N NH2 A ARG B 799  ? 0.3150 0.3469 0.3378 0.0085  0.0221  0.0080  797  ARG B NH2 
14803 N NH2 B ARG B 799  ? 0.3453 0.3782 0.3707 0.0084  0.0222  0.0075  797  ARG B NH2 
14804 N N   . LEU B 800  ? 0.2710 0.2937 0.2974 0.0004  0.0191  0.0179  798  LEU B N   
14805 C CA  . LEU B 800  ? 0.3059 0.3240 0.3288 0.0014  0.0176  0.0179  798  LEU B CA  
14806 C C   . LEU B 800  ? 0.3225 0.3423 0.3420 0.0035  0.0184  0.0168  798  LEU B C   
14807 O O   . LEU B 800  ? 0.3209 0.3447 0.3399 0.0037  0.0203  0.0170  798  LEU B O   
14808 C CB  . LEU B 800  ? 0.3382 0.3534 0.3596 -0.0003 0.0173  0.0210  798  LEU B CB  
14809 C CG  . LEU B 800  ? 0.3532 0.3652 0.3770 -0.0026 0.0160  0.0223  798  LEU B CG  
14810 C CD1 . LEU B 800  ? 0.3934 0.4022 0.4148 -0.0040 0.0159  0.0255  798  LEU B CD1 
14811 C CD2 . LEU B 800  ? 0.2904 0.2980 0.3144 -0.0016 0.0138  0.0202  798  LEU B CD2 
14812 N N   . SER B 801  ? 0.3136 0.3304 0.3306 0.0050  0.0169  0.0158  799  SER B N   
14813 C CA  . SER B 801  ? 0.3624 0.3802 0.3758 0.0066  0.0172  0.0151  799  SER B CA  
14814 C C   . SER B 801  ? 0.3878 0.4061 0.3985 0.0060  0.0182  0.0179  799  SER B C   
14815 O O   . SER B 801  ? 0.3771 0.3940 0.3885 0.0043  0.0183  0.0204  799  SER B O   
14816 C CB  . SER B 801  ? 0.3562 0.3710 0.3681 0.0081  0.0152  0.0139  799  SER B CB  
14817 O OG  . SER B 801  ? 0.3966 0.4077 0.4072 0.0078  0.0141  0.0160  799  SER B OG  
14818 N N   . PRO B 802  ? 0.4306 0.4507 0.4378 0.0071  0.0190  0.0177  800  PRO B N   
14819 C CA  . PRO B 802  ? 0.4333 0.4535 0.4373 0.0066  0.0197  0.0204  800  PRO B CA  
14820 C C   . PRO B 802  ? 0.4250 0.4407 0.4277 0.0065  0.0179  0.0223  800  PRO B C   
14821 O O   . PRO B 802  ? 0.4622 0.4770 0.4631 0.0055  0.0183  0.0252  800  PRO B O   
14822 C CB  . PRO B 802  ? 0.4041 0.4265 0.4042 0.0082  0.0202  0.0191  800  PRO B CB  
14823 C CG  . PRO B 802  ? 0.4513 0.4761 0.4534 0.0089  0.0209  0.0161  800  PRO B CG  
14824 C CD  . PRO B 802  ? 0.3722 0.3948 0.3782 0.0086  0.0195  0.0150  800  PRO B CD  
14825 N N   . ALA B 803  ? 0.3997 0.4125 0.4031 0.0076  0.0159  0.0209  801  ALA B N   
14826 C CA  . ALA B 803  ? 0.4369 0.4451 0.4395 0.0078  0.0142  0.0225  801  ALA B CA  
14827 C C   . ALA B 803  ? 0.4506 0.4557 0.4559 0.0060  0.0138  0.0236  801  ALA B C   
14828 O O   . ALA B 803  ? 0.4753 0.4758 0.4798 0.0062  0.0123  0.0248  801  ALA B O   
14829 C CB  . ALA B 803  ? 0.4130 0.4197 0.4152 0.0099  0.0124  0.0204  801  ALA B CB  
14830 N N   . GLY B 804  ? 0.4140 0.4213 0.4224 0.0044  0.0149  0.0232  802  GLY B N   
14831 C CA  . GLY B 804  ? 0.3996 0.4042 0.4105 0.0024  0.0145  0.0244  802  GLY B CA  
14832 C C   . GLY B 804  ? 0.3374 0.3389 0.3504 0.0029  0.0127  0.0223  802  GLY B C   
14833 O O   . GLY B 804  ? 0.3718 0.3688 0.3853 0.0018  0.0115  0.0233  802  GLY B O   
14834 N N   . ARG B 805  ? 0.3474 0.3509 0.3614 0.0044  0.0125  0.0194  803  ARG B N   
14835 C CA  . ARG B 805  ? 0.3292 0.3299 0.3447 0.0050  0.0109  0.0174  803  ARG B CA  
14836 C C   . ARG B 805  ? 0.3031 0.3071 0.3217 0.0047  0.0115  0.0152  803  ARG B C   
14837 O O   . ARG B 805  ? 0.3013 0.3098 0.3203 0.0048  0.0130  0.0147  803  ARG B O   
14838 C CB  . ARG B 805  ? 0.3523 0.3516 0.3655 0.0076  0.0098  0.0161  803  ARG B CB  
14839 C CG  . ARG B 805  ? 0.3965 0.3923 0.4068 0.0083  0.0090  0.0182  803  ARG B CG  
14840 C CD  . ARG B 805  ? 0.4322 0.4226 0.4429 0.0072  0.0079  0.0195  803  ARG B CD  
14841 N NE  . ARG B 805  ? 0.4457 0.4323 0.4534 0.0081  0.0070  0.0216  803  ARG B NE  
14842 C CZ  . ARG B 805  ? 0.4233 0.4087 0.4296 0.0067  0.0075  0.0246  803  ARG B CZ  
14843 N NH1 . ARG B 805  ? 0.4208 0.4086 0.4285 0.0041  0.0089  0.0258  803  ARG B NH1 
14844 N NH2 . ARG B 805  ? 0.4995 0.4813 0.5028 0.0079  0.0066  0.0264  803  ARG B NH2 
14845 N N   . PRO B 806  ? 0.2674 0.2692 0.2880 0.0044  0.0102  0.0138  804  PRO B N   
14846 C CA  . PRO B 806  ? 0.2740 0.2789 0.2976 0.0041  0.0106  0.0120  804  PRO B CA  
14847 C C   . PRO B 806  ? 0.2455 0.2531 0.2682 0.0060  0.0110  0.0098  804  PRO B C   
14848 O O   . PRO B 806  ? 0.2548 0.2612 0.2753 0.0077  0.0103  0.0090  804  PRO B O   
14849 C CB  . PRO B 806  ? 0.2792 0.2802 0.3041 0.0036  0.0088  0.0109  804  PRO B CB  
14850 C CG  . PRO B 806  ? 0.2929 0.2890 0.3162 0.0028  0.0079  0.0129  804  PRO B CG  
14851 C CD  . PRO B 806  ? 0.3390 0.3352 0.3592 0.0043  0.0084  0.0140  804  PRO B CD  
14852 N N   . ILE B 807  ? 0.2251 0.2366 0.2497 0.0058  0.0122  0.0089  805  ILE B N   
14853 C CA  . ILE B 807  ? 0.2212 0.2351 0.2452 0.0074  0.0126  0.0066  805  ILE B CA  
14854 C C   . ILE B 807  ? 0.2129 0.2247 0.2378 0.0080  0.0110  0.0046  805  ILE B C   
14855 O O   . ILE B 807  ? 0.2231 0.2344 0.2507 0.0070  0.0105  0.0043  805  ILE B O   
14856 C CB  . ILE B 807  ? 0.2203 0.2384 0.2461 0.0072  0.0143  0.0063  805  ILE B CB  
14857 C CG1 . ILE B 807  ? 0.2768 0.2973 0.3018 0.0065  0.0160  0.0085  805  ILE B CG1 
14858 C CG2 . ILE B 807  ? 0.2140 0.2336 0.2388 0.0089  0.0145  0.0039  805  ILE B CG2 
14859 C CD1 . ILE B 807  ? 0.3145 0.3351 0.3354 0.0077  0.0165  0.0087  805  ILE B CD1 
14860 N N   . PRO B 808  ? 0.2031 0.2139 0.2260 0.0095  0.0102  0.0032  806  PRO B N   
14861 C CA  . PRO B 808  ? 0.2114 0.2205 0.2351 0.0101  0.0089  0.0014  806  PRO B CA  
14862 C C   . PRO B 808  ? 0.2240 0.2352 0.2498 0.0100  0.0092  -0.0002 806  PRO B C   
14863 O O   . PRO B 808  ? 0.1881 0.2020 0.2136 0.0104  0.0103  -0.0008 806  PRO B O   
14864 C CB  . PRO B 808  ? 0.2302 0.2390 0.2514 0.0116  0.0083  0.0006  806  PRO B CB  
14865 C CG  . PRO B 808  ? 0.2632 0.2723 0.2822 0.0118  0.0089  0.0025  806  PRO B CG  
14866 C CD  . PRO B 808  ? 0.1871 0.1983 0.2069 0.0107  0.0104  0.0036  806  PRO B CD  
14867 N N   . LEU B 809  ? 0.1975 0.2071 0.2251 0.0095  0.0081  -0.0010 807  LEU B N   
14868 C CA  . LEU B 809  ? 0.1806 0.1918 0.2101 0.0095  0.0080  -0.0025 807  LEU B CA  
14869 C C   . LEU B 809  ? 0.1823 0.1912 0.2113 0.0101  0.0066  -0.0041 807  LEU B C   
14870 O O   . LEU B 809  ? 0.2079 0.2139 0.2368 0.0097  0.0056  -0.0038 807  LEU B O   
14871 C CB  . LEU B 809  ? 0.1871 0.1990 0.2197 0.0079  0.0081  -0.0016 807  LEU B CB  
14872 C CG  . LEU B 809  ? 0.2028 0.2158 0.2377 0.0079  0.0076  -0.0030 807  LEU B CG  
14873 C CD1 . LEU B 809  ? 0.1855 0.2013 0.2202 0.0091  0.0087  -0.0040 807  LEU B CD1 
14874 C CD2 . LEU B 809  ? 0.2308 0.2447 0.2689 0.0062  0.0074  -0.0019 807  LEU B CD2 
14875 N N   . ILE B 810  ? 0.1660 0.1759 0.1943 0.0110  0.0066  -0.0056 808  ILE B N   
14876 C CA  . ILE B 810  ? 0.1739 0.1823 0.2020 0.0113  0.0054  -0.0071 808  ILE B CA  
14877 C C   . ILE B 810  ? 0.1941 0.2037 0.2245 0.0108  0.0053  -0.0078 808  ILE B C   
14878 O O   . ILE B 810  ? 0.1981 0.2099 0.2289 0.0112  0.0062  -0.0082 808  ILE B O   
14879 C CB  . ILE B 810  ? 0.1943 0.2032 0.2204 0.0124  0.0053  -0.0083 808  ILE B CB  
14880 C CG1 . ILE B 810  ? 0.2059 0.2145 0.2299 0.0130  0.0054  -0.0074 808  ILE B CG1 
14881 C CG2 . ILE B 810  ? 0.2367 0.2442 0.2627 0.0126  0.0042  -0.0096 808  ILE B CG2 
14882 C CD1 . ILE B 810  ? 0.2304 0.2398 0.2526 0.0139  0.0050  -0.0084 808  ILE B CD1 
14883 N N   . ALA B 811  ? 0.1815 0.1895 0.2133 0.0101  0.0043  -0.0079 809  ALA B N   
14884 C CA  . ALA B 811  ? 0.1707 0.1800 0.2049 0.0096  0.0040  -0.0084 809  ALA B CA  
14885 C C   . ALA B 811  ? 0.2101 0.2175 0.2438 0.0097  0.0026  -0.0097 809  ALA B C   
14886 O O   . ALA B 811  ? 0.2113 0.2163 0.2449 0.0090  0.0016  -0.0096 809  ALA B O   
14887 C CB  . ALA B 811  ? 0.2048 0.2149 0.2416 0.0081  0.0040  -0.0070 809  ALA B CB  
14888 N N   . GLU B 812  ? 0.1669 0.1750 0.2000 0.0104  0.0026  -0.0109 810  GLU B N   
14889 C CA  . GLU B 812  ? 0.2005 0.2070 0.2328 0.0105  0.0014  -0.0120 810  GLU B CA  
14890 C C   . GLU B 812  ? 0.1946 0.2021 0.2290 0.0102  0.0009  -0.0123 810  GLU B C   
14891 O O   . GLU B 812  ? 0.1951 0.2044 0.2301 0.0108  0.0016  -0.0125 810  GLU B O   
14892 C CB  . GLU B 812  ? 0.2117 0.2182 0.2416 0.0114  0.0017  -0.0130 810  GLU B CB  
14893 C CG  . GLU B 812  ? 0.2314 0.2375 0.2597 0.0119  0.0021  -0.0125 810  GLU B CG  
14894 C CD  . GLU B 812  ? 0.2732 0.2770 0.3011 0.0117  0.0013  -0.0123 810  GLU B CD  
14895 O OE1 . GLU B 812  ? 0.2509 0.2535 0.2776 0.0120  0.0006  -0.0132 810  GLU B OE1 
14896 O OE2 . GLU B 812  ? 0.2515 0.2543 0.2799 0.0113  0.0014  -0.0113 810  GLU B OE2 
14897 N N   . THR B 813  ? 0.1937 0.1999 0.2290 0.0093  -0.0003 -0.0123 811  THR B N   
14898 C CA  . THR B 813  ? 0.1724 0.1801 0.2104 0.0088  -0.0009 -0.0121 811  THR B CA  
14899 C C   . THR B 813  ? 0.1746 0.1808 0.2120 0.0086  -0.0024 -0.0130 811  THR B C   
14900 O O   . THR B 813  ? 0.2005 0.2053 0.2355 0.0093  -0.0026 -0.0140 811  THR B O   
14901 C CB  . THR B 813  ? 0.1978 0.2061 0.2380 0.0074  -0.0010 -0.0107 811  THR B CB  
14902 O OG1 . THR B 813  ? 0.2070 0.2122 0.2457 0.0067  -0.0018 -0.0107 811  THR B OG1 
14903 C CG2 . THR B 813  ? 0.2135 0.2241 0.2545 0.0077  0.0008  -0.0097 811  THR B CG2 
14904 N N   . GLY B 814  ? 0.1977 0.2046 0.2373 0.0078  -0.0035 -0.0127 812  GLY B N   
14905 C CA  . GLY B 814  ? 0.2077 0.2139 0.2470 0.0078  -0.0048 -0.0134 812  GLY B CA  
14906 C C   . GLY B 814  ? 0.2087 0.2116 0.2454 0.0073  -0.0060 -0.0142 812  GLY B C   
14907 O O   . GLY B 814  ? 0.2339 0.2349 0.2691 0.0071  -0.0059 -0.0143 812  GLY B O   
14908 N N   . GLY B 815  ? 0.1995 0.2018 0.2357 0.0072  -0.0073 -0.0148 813  GLY B N   
14909 C CA  . GLY B 815  ? 0.2026 0.2020 0.2362 0.0068  -0.0085 -0.0156 813  GLY B CA  
14910 C C   . GLY B 815  ? 0.2072 0.2065 0.2416 0.0060  -0.0103 -0.0157 813  GLY B C   
14911 O O   . GLY B 815  ? 0.2339 0.2356 0.2708 0.0060  -0.0106 -0.0151 813  GLY B O   
14912 N N   . GLN B 816  ? 0.1889 0.1854 0.2210 0.0053  -0.0115 -0.0163 814  GLN B N   
14913 C CA  . GLN B 816  ? 0.2131 0.2090 0.2450 0.0045  -0.0134 -0.0166 814  GLN B CA  
14914 C C   . GLN B 816  ? 0.1830 0.1760 0.2106 0.0049  -0.0137 -0.0178 814  GLN B C   
14915 O O   . GLN B 816  ? 0.2219 0.2122 0.2474 0.0043  -0.0146 -0.0184 814  GLN B O   
14916 C CB  . GLN B 816  ? 0.2238 0.2192 0.2573 0.0028  -0.0149 -0.0161 814  GLN B CB  
14917 C CG  . GLN B 816  ? 0.2079 0.2036 0.2418 0.0018  -0.0170 -0.0161 814  GLN B CG  
14918 C CD  . GLN B 816  ? 0.2301 0.2297 0.2674 0.0024  -0.0171 -0.0152 814  GLN B CD  
14919 O OE1 . GLN B 816  ? 0.2220 0.2220 0.2584 0.0037  -0.0165 -0.0155 814  GLN B OE1 
14920 N NE2 . GLN B 816  ? 0.2234 0.2259 0.2648 0.0014  -0.0177 -0.0141 814  GLN B NE2 
14921 N N   . ASN B 817  ? 0.1730 0.1666 0.1993 0.0060  -0.0129 -0.0181 815  ASN B N   
14922 C CA  . ASN B 817  ? 0.1606 0.1524 0.1832 0.0066  -0.0124 -0.0190 815  ASN B CA  
14923 C C   . ASN B 817  ? 0.1890 0.1792 0.2090 0.0062  -0.0138 -0.0196 815  ASN B C   
14924 O O   . ASN B 817  ? 0.2023 0.1934 0.2230 0.0060  -0.0147 -0.0192 815  ASN B O   
14925 C CB  . ASN B 817  ? 0.1694 0.1628 0.1918 0.0076  -0.0109 -0.0189 815  ASN B CB  
14926 C CG  . ASN B 817  ? 0.1730 0.1681 0.1978 0.0080  -0.0096 -0.0182 815  ASN B CG  
14927 O OD1 . ASN B 817  ? 0.1723 0.1669 0.1974 0.0080  -0.0090 -0.0181 815  ASN B OD1 
14928 N ND2 . ASN B 817  ? 0.1719 0.1689 0.1983 0.0084  -0.0091 -0.0178 815  ASN B ND2 
14929 N N   . ALA B 818  ? 0.1900 0.1777 0.2070 0.0063  -0.0139 -0.0205 816  ALA B N   
14930 C CA  . ALA B 818  ? 0.1843 0.1702 0.1981 0.0059  -0.0152 -0.0213 816  ALA B CA  
14931 C C   . ALA B 818  ? 0.1670 0.1527 0.1776 0.0069  -0.0140 -0.0218 816  ALA B C   
14932 O O   . ALA B 818  ? 0.1897 0.1761 0.2001 0.0078  -0.0124 -0.0220 816  ALA B O   
14933 C CB  . ALA B 818  ? 0.1819 0.1647 0.1940 0.0052  -0.0164 -0.0221 816  ALA B CB  
14934 N N   . MET B 819  ? 0.1634 0.1484 0.1715 0.0066  -0.0150 -0.0221 817  MET B N   
14935 C CA  . MET B 819  ? 0.1892 0.1739 0.1937 0.0073  -0.0141 -0.0227 817  MET B CA  
14936 C C   . MET B 819  ? 0.1912 0.1732 0.1922 0.0069  -0.0154 -0.0237 817  MET B C   
14937 O O   . MET B 819  ? 0.1943 0.1757 0.1953 0.0059  -0.0172 -0.0234 817  MET B O   
14938 C CB  . MET B 819  ? 0.1793 0.1658 0.1837 0.0072  -0.0137 -0.0220 817  MET B CB  
14939 C CG  . MET B 819  ? 0.2096 0.1961 0.2102 0.0076  -0.0128 -0.0224 817  MET B CG  
14940 S SD  . MET B 819  ? 0.2505 0.2384 0.2506 0.0070  -0.0128 -0.0213 817  MET B SD  
14941 C CE  . MET B 819  ? 0.2516 0.2419 0.2548 0.0074  -0.0111 -0.0207 817  MET B CE  
14942 N N   . ILE B 820  ? 0.2028 0.1833 0.2007 0.0077  -0.0146 -0.0248 818  ILE B N   
14943 C CA  . ILE B 820  ? 0.1895 0.1672 0.1832 0.0076  -0.0156 -0.0259 818  ILE B CA  
14944 C C   . ILE B 820  ? 0.2046 0.1832 0.1950 0.0081  -0.0147 -0.0261 818  ILE B C   
14945 O O   . ILE B 820  ? 0.2061 0.1866 0.1964 0.0092  -0.0127 -0.0260 818  ILE B O   
14946 C CB  . ILE B 820  ? 0.2026 0.1773 0.1947 0.0083  -0.0154 -0.0272 818  ILE B CB  
14947 C CG1 . ILE B 820  ? 0.2095 0.1831 0.2047 0.0073  -0.0165 -0.0268 818  ILE B CG1 
14948 C CG2 . ILE B 820  ? 0.2374 0.2088 0.2243 0.0084  -0.0163 -0.0286 818  ILE B CG2 
14949 C CD1 . ILE B 820  ? 0.2511 0.2211 0.2445 0.0079  -0.0165 -0.0279 818  ILE B CD1 
14950 N N   . VAL B 821  ? 0.2087 0.1864 0.1965 0.0073  -0.0161 -0.0261 819  VAL B N   
14951 C CA  . VAL B 821  ? 0.1979 0.1765 0.1823 0.0075  -0.0154 -0.0260 819  VAL B CA  
14952 C C   . VAL B 821  ? 0.2144 0.1901 0.1939 0.0076  -0.0162 -0.0274 819  VAL B C   
14953 O O   . VAL B 821  ? 0.2356 0.2090 0.2143 0.0065  -0.0184 -0.0277 819  VAL B O   
14954 C CB  . VAL B 821  ? 0.2002 0.1803 0.1858 0.0064  -0.0164 -0.0246 819  VAL B CB  
14955 C CG1 . VAL B 821  ? 0.2263 0.2071 0.2082 0.0063  -0.0157 -0.0243 819  VAL B CG1 
14956 C CG2 . VAL B 821  ? 0.2220 0.2044 0.2122 0.0063  -0.0157 -0.0234 819  VAL B CG2 
14957 N N   . ASP B 822  ? 0.2350 0.2107 0.2110 0.0089  -0.0145 -0.0283 820  ASP B N   
14958 C CA  . ASP B 822  ? 0.2548 0.2277 0.2255 0.0091  -0.0152 -0.0297 820  ASP B CA  
14959 C C   . ASP B 822  ? 0.2541 0.2283 0.2214 0.0087  -0.0150 -0.0292 820  ASP B C   
14960 O O   . ASP B 822  ? 0.2525 0.2296 0.2217 0.0081  -0.0144 -0.0276 820  ASP B O   
14961 C CB  . ASP B 822  ? 0.2669 0.2378 0.2353 0.0110  -0.0137 -0.0314 820  ASP B CB  
14962 C CG  . ASP B 822  ? 0.2815 0.2556 0.2490 0.0127  -0.0109 -0.0314 820  ASP B CG  
14963 O OD1 . ASP B 822  ? 0.2658 0.2432 0.2335 0.0122  -0.0101 -0.0302 820  ASP B OD1 
14964 O OD2 . ASP B 822  ? 0.3082 0.2813 0.2746 0.0146  -0.0096 -0.0326 820  ASP B OD2 
14965 N N   . SER B 823  ? 0.2696 0.2413 0.2316 0.0089  -0.0155 -0.0304 821  SER B N   
14966 C CA  . SER B 823  ? 0.2711 0.2439 0.2295 0.0083  -0.0155 -0.0298 821  SER B CA  
14967 C C   . SER B 823  ? 0.3109 0.2872 0.2683 0.0093  -0.0127 -0.0293 821  SER B C   
14968 O O   . SER B 823  ? 0.3361 0.3136 0.2908 0.0086  -0.0124 -0.0284 821  SER B O   
14969 C CB  . SER B 823  ? 0.2867 0.2558 0.2393 0.0081  -0.0170 -0.0313 821  SER B CB  
14970 O OG  . SER B 823  ? 0.3421 0.3094 0.2915 0.0100  -0.0155 -0.0333 821  SER B OG  
14971 N N   . SER B 824  ? 0.2678 0.2457 0.2273 0.0108  -0.0106 -0.0297 822  SER B N   
14972 C CA  . SER B 824  ? 0.2618 0.2438 0.2210 0.0116  -0.0080 -0.0291 822  SER B CA  
14973 C C   . SER B 824  ? 0.2869 0.2724 0.2507 0.0105  -0.0075 -0.0270 822  SER B C   
14974 O O   . SER B 824  ? 0.3081 0.2972 0.2718 0.0105  -0.0057 -0.0261 822  SER B O   
14975 C CB  . SER B 824  ? 0.2891 0.2717 0.2482 0.0140  -0.0059 -0.0304 822  SER B CB  
14976 O OG  . SER B 824  ? 0.2546 0.2379 0.2187 0.0144  -0.0056 -0.0301 822  SER B OG  
14977 N N   . ALA B 825  ? 0.2534 0.2380 0.2211 0.0095  -0.0091 -0.0264 823  ALA B N   
14978 C CA  . ALA B 825  ? 0.2396 0.2269 0.2114 0.0086  -0.0087 -0.0247 823  ALA B CA  
14979 C C   . ALA B 825  ? 0.2686 0.2568 0.2388 0.0070  -0.0092 -0.0232 823  ALA B C   
14980 O O   . ALA B 825  ? 0.2822 0.2684 0.2491 0.0063  -0.0106 -0.0232 823  ALA B O   
14981 C CB  . ALA B 825  ? 0.2420 0.2278 0.2179 0.0081  -0.0103 -0.0245 823  ALA B CB  
14982 N N   . LEU B 826  ? 0.2825 0.2735 0.2551 0.0063  -0.0081 -0.0218 824  LEU B N   
14983 C CA  . LEU B 826  ? 0.2940 0.2855 0.2652 0.0046  -0.0086 -0.0201 824  LEU B CA  
14984 C C   . LEU B 826  ? 0.2952 0.2846 0.2690 0.0036  -0.0107 -0.0192 824  LEU B C   
14985 O O   . LEU B 826  ? 0.2611 0.2512 0.2389 0.0037  -0.0106 -0.0190 824  LEU B O   
14986 C CB  . LEU B 826  ? 0.3590 0.3542 0.3313 0.0040  -0.0066 -0.0190 824  LEU B CB  
14987 C CG  . LEU B 826  ? 0.3635 0.3592 0.3342 0.0021  -0.0069 -0.0171 824  LEU B CG  
14988 C CD1 . LEU B 826  ? 0.4272 0.4223 0.3928 0.0017  -0.0070 -0.0171 824  LEU B CD1 
14989 C CD2 . LEU B 826  ? 0.4585 0.4580 0.4308 0.0013  -0.0051 -0.0161 824  LEU B CD2 
14990 N N   . ALA B 827  ? 0.2677 0.2549 0.2391 0.0028  -0.0126 -0.0187 825  ALA B N   
14991 C CA  . ALA B 827  ? 0.2501 0.2353 0.2239 0.0024  -0.0148 -0.0181 825  ALA B CA  
14992 C C   . ALA B 827  ? 0.2650 0.2511 0.2419 0.0017  -0.0145 -0.0167 825  ALA B C   
14993 O O   . ALA B 827  ? 0.2485 0.2341 0.2291 0.0021  -0.0151 -0.0167 825  ALA B O   
14994 C CB  . ALA B 827  ? 0.2863 0.2693 0.2567 0.0016  -0.0168 -0.0175 825  ALA B CB  
14995 N N   . GLU B 828  ? 0.2789 0.2661 0.2541 0.0007  -0.0134 -0.0156 826  GLU B N   
14996 C CA  . GLU B 828  ? 0.2741 0.2615 0.2516 -0.0001 -0.0133 -0.0143 826  GLU B CA  
14997 C C   . GLU B 828  ? 0.3030 0.2921 0.2845 0.0007  -0.0121 -0.0151 826  GLU B C   
14998 O O   . GLU B 828  ? 0.2628 0.2512 0.2471 0.0006  -0.0126 -0.0147 826  GLU B O   
14999 C CB  . GLU B 828  ? 0.3064 0.2949 0.2812 -0.0016 -0.0123 -0.0130 826  GLU B CB  
15000 C CG  . GLU B 828  ? 0.3935 0.3799 0.3646 -0.0027 -0.0137 -0.0117 826  GLU B CG  
15001 C CD  . GLU B 828  ? 0.4062 0.3927 0.3733 -0.0024 -0.0137 -0.0123 826  GLU B CD  
15002 O OE1 . GLU B 828  ? 0.3716 0.3597 0.3387 -0.0012 -0.0125 -0.0139 826  GLU B OE1 
15003 O OE2 . GLU B 828  ? 0.4164 0.4011 0.3801 -0.0033 -0.0149 -0.0112 826  GLU B OE2 
15004 N N   . GLN B 829  ? 0.2417 0.2331 0.2232 0.0015  -0.0104 -0.0161 827  GLN B N   
15005 C CA  . GLN B 829  ? 0.2597 0.2528 0.2447 0.0023  -0.0093 -0.0167 827  GLN B CA  
15006 C C   . GLN B 829  ? 0.2674 0.2589 0.2552 0.0033  -0.0104 -0.0175 827  GLN B C   
15007 O O   . GLN B 829  ? 0.2454 0.2371 0.2363 0.0034  -0.0104 -0.0174 827  GLN B O   
15008 C CB  . GLN B 829  ? 0.3125 0.3083 0.2967 0.0032  -0.0075 -0.0177 827  GLN B CB  
15009 C CG  . GLN B 829  ? 0.3953 0.3943 0.3784 0.0024  -0.0058 -0.0168 827  GLN B CG  
15010 C CD  . GLN B 829  ? 0.4551 0.4572 0.4387 0.0039  -0.0039 -0.0178 827  GLN B CD  
15011 O OE1 . GLN B 829  ? 0.4147 0.4157 0.3979 0.0055  -0.0039 -0.0192 827  GLN B OE1 
15012 N NE2 . GLN B 829  ? 0.4822 0.4881 0.4667 0.0033  -0.0024 -0.0170 827  GLN B NE2 
15013 N N   . VAL B 830  ? 0.2490 0.2389 0.2355 0.0038  -0.0114 -0.0184 828  VAL B N   
15014 C CA  . VAL B 830  ? 0.2230 0.2114 0.2120 0.0044  -0.0127 -0.0189 828  VAL B CA  
15015 C C   . VAL B 830  ? 0.2437 0.2312 0.2350 0.0039  -0.0140 -0.0179 828  VAL B C   
15016 O O   . VAL B 830  ? 0.2366 0.2244 0.2314 0.0044  -0.0140 -0.0180 828  VAL B O   
15017 C CB  . VAL B 830  ? 0.2381 0.2246 0.2247 0.0046  -0.0140 -0.0198 828  VAL B CB  
15018 C CG1 . VAL B 830  ? 0.2362 0.2214 0.2257 0.0048  -0.0156 -0.0200 828  VAL B CG1 
15019 C CG2 . VAL B 830  ? 0.2424 0.2293 0.2269 0.0055  -0.0126 -0.0211 828  VAL B CG2 
15020 N N   . VAL B 831  ? 0.2305 0.2168 0.2196 0.0031  -0.0151 -0.0169 829  VAL B N   
15021 C CA  . VAL B 831  ? 0.2309 0.2159 0.2219 0.0030  -0.0165 -0.0159 829  VAL B CA  
15022 C C   . VAL B 831  ? 0.2190 0.2047 0.2124 0.0031  -0.0154 -0.0155 829  VAL B C   
15023 O O   . VAL B 831  ? 0.2417 0.2271 0.2382 0.0037  -0.0159 -0.0155 829  VAL B O   
15024 C CB  . VAL B 831  ? 0.2332 0.2165 0.2211 0.0022  -0.0179 -0.0148 829  VAL B CB  
15025 C CG1 . VAL B 831  ? 0.2512 0.2330 0.2407 0.0023  -0.0190 -0.0136 829  VAL B CG1 
15026 C CG2 . VAL B 831  ? 0.2429 0.2252 0.2292 0.0024  -0.0195 -0.0153 829  VAL B CG2 
15027 N N   . GLY B 832  ? 0.2217 0.2084 0.2137 0.0023  -0.0140 -0.0153 830  GLY B N   
15028 C CA  . GLY B 832  ? 0.2412 0.2284 0.2352 0.0022  -0.0131 -0.0150 830  GLY B CA  
15029 C C   . GLY B 832  ? 0.2310 0.2197 0.2283 0.0033  -0.0123 -0.0159 830  GLY B C   
15030 O O   . GLY B 832  ? 0.2385 0.2268 0.2381 0.0036  -0.0124 -0.0159 830  GLY B O   
15031 N N   . ASP B 833  ? 0.1975 0.1876 0.1948 0.0038  -0.0116 -0.0168 831  ASP B N   
15032 C CA  . ASP B 833  ? 0.2176 0.2089 0.2178 0.0048  -0.0108 -0.0176 831  ASP B CA  
15033 C C   . ASP B 833  ? 0.2176 0.2079 0.2203 0.0054  -0.0120 -0.0178 831  ASP B C   
15034 O O   . ASP B 833  ? 0.2251 0.2161 0.2306 0.0060  -0.0116 -0.0179 831  ASP B O   
15035 C CB  . ASP B 833  ? 0.2032 0.1960 0.2025 0.0053  -0.0097 -0.0185 831  ASP B CB  
15036 C CG  . ASP B 833  ? 0.2308 0.2257 0.2286 0.0049  -0.0082 -0.0182 831  ASP B CG  
15037 O OD1 . ASP B 833  ? 0.2730 0.2685 0.2713 0.0040  -0.0080 -0.0174 831  ASP B OD1 
15038 O OD2 . ASP B 833  ? 0.2656 0.2617 0.2620 0.0054  -0.0073 -0.0188 831  ASP B OD2 
15039 N N   . VAL B 834  ? 0.1983 0.1872 0.2000 0.0053  -0.0135 -0.0177 832  VAL B N   
15040 C CA  . VAL B 834  ? 0.1925 0.1808 0.1967 0.0057  -0.0148 -0.0176 832  VAL B CA  
15041 C C   . VAL B 834  ? 0.2004 0.1885 0.2065 0.0060  -0.0152 -0.0168 832  VAL B C   
15042 O O   . VAL B 834  ? 0.2040 0.1929 0.2134 0.0067  -0.0151 -0.0169 832  VAL B O   
15043 C CB  . VAL B 834  ? 0.1968 0.1839 0.1993 0.0054  -0.0166 -0.0176 832  VAL B CB  
15044 C CG1 . VAL B 834  ? 0.2251 0.2121 0.2304 0.0057  -0.0182 -0.0171 832  VAL B CG1 
15045 C CG2 . VAL B 834  ? 0.2324 0.2194 0.2334 0.0054  -0.0164 -0.0187 832  VAL B CG2 
15046 N N   . ILE B 835  ? 0.2028 0.1896 0.2069 0.0055  -0.0155 -0.0161 833  ILE B N   
15047 C CA  . ILE B 835  ? 0.2524 0.2383 0.2579 0.0060  -0.0159 -0.0154 833  ILE B CA  
15048 C C   . ILE B 835  ? 0.2362 0.2231 0.2436 0.0064  -0.0143 -0.0158 833  ILE B C   
15049 O O   . ILE B 835  ? 0.2759 0.2630 0.2859 0.0074  -0.0143 -0.0159 833  ILE B O   
15050 C CB  . ILE B 835  ? 0.2683 0.2520 0.2708 0.0053  -0.0165 -0.0145 833  ILE B CB  
15051 C CG1 . ILE B 835  ? 0.3319 0.3145 0.3329 0.0052  -0.0183 -0.0140 833  ILE B CG1 
15052 C CG2 . ILE B 835  ? 0.2790 0.2610 0.2824 0.0058  -0.0166 -0.0140 833  ILE B CG2 
15053 C CD1 . ILE B 835  ? 0.3181 0.2984 0.3159 0.0044  -0.0191 -0.0128 833  ILE B CD1 
15054 N N   . THR B 836  ? 0.2097 0.1974 0.2157 0.0057  -0.0130 -0.0162 834  THR B N   
15055 C CA  . THR B 836  ? 0.2327 0.2216 0.2403 0.0060  -0.0116 -0.0166 834  THR B CA  
15056 C C   . THR B 836  ? 0.2421 0.2325 0.2527 0.0070  -0.0113 -0.0171 834  THR B C   
15057 O O   . THR B 836  ? 0.2896 0.2803 0.3022 0.0077  -0.0108 -0.0172 834  THR B O   
15058 C CB  . THR B 836  ? 0.2296 0.2198 0.2354 0.0051  -0.0105 -0.0167 834  THR B CB  
15059 O OG1 . THR B 836  ? 0.3140 0.3030 0.3172 0.0039  -0.0107 -0.0160 834  THR B OG1 
15060 C CG2 . THR B 836  ? 0.2892 0.2810 0.2966 0.0054  -0.0092 -0.0171 834  THR B CG2 
15061 N N   . SER B 837  ? 0.2064 0.1976 0.2171 0.0070  -0.0114 -0.0175 835  SER B N   
15062 C CA  . SER B 837  ? 0.2014 0.1939 0.2147 0.0077  -0.0109 -0.0179 835  SER B CA  
15063 C C   . SER B 837  ? 0.1857 0.1782 0.2017 0.0082  -0.0119 -0.0176 835  SER B C   
15064 O O   . SER B 837  ? 0.2051 0.1988 0.2236 0.0087  -0.0113 -0.0176 835  SER B O   
15065 C CB  . SER B 837  ? 0.2049 0.1976 0.2171 0.0075  -0.0109 -0.0185 835  SER B CB  
15066 O OG  . SER B 837  ? 0.1903 0.1835 0.2003 0.0073  -0.0098 -0.0187 835  SER B OG  
15067 N N   . ALA B 838  ? 0.1872 0.1787 0.2027 0.0081  -0.0135 -0.0172 836  ALA B N   
15068 C CA  . ALA B 838  ? 0.1834 0.1755 0.2016 0.0086  -0.0146 -0.0168 836  ALA B CA  
15069 C C   . ALA B 838  ? 0.2070 0.1991 0.2268 0.0095  -0.0147 -0.0162 836  ALA B C   
15070 O O   . ALA B 838  ? 0.2362 0.2298 0.2592 0.0103  -0.0147 -0.0160 836  ALA B O   
15071 C CB  . ALA B 838  ? 0.1892 0.1805 0.2062 0.0080  -0.0164 -0.0166 836  ALA B CB  
15072 N N   . PHE B 839  ? 0.2398 0.2300 0.2572 0.0095  -0.0147 -0.0160 837  PHE B N   
15073 C CA  . PHE B 839  ? 0.2501 0.2393 0.2683 0.0105  -0.0153 -0.0155 837  PHE B CA  
15074 C C   . PHE B 839  ? 0.2837 0.2716 0.3008 0.0109  -0.0141 -0.0157 837  PHE B C   
15075 O O   . PHE B 839  ? 0.2751 0.2623 0.2933 0.0121  -0.0141 -0.0155 837  PHE B O   
15076 C CB  . PHE B 839  ? 0.2296 0.2169 0.2458 0.0103  -0.0170 -0.0147 837  PHE B CB  
15077 C CG  . PHE B 839  ? 0.2394 0.2277 0.2563 0.0099  -0.0185 -0.0145 837  PHE B CG  
15078 C CD1 . PHE B 839  ? 0.2137 0.2043 0.2343 0.0106  -0.0191 -0.0143 837  PHE B CD1 
15079 C CD2 . PHE B 839  ? 0.2592 0.2464 0.2729 0.0087  -0.0193 -0.0145 837  PHE B CD2 
15080 C CE1 . PHE B 839  ? 0.2289 0.2204 0.2501 0.0100  -0.0207 -0.0141 837  PHE B CE1 
15081 C CE2 . PHE B 839  ? 0.2542 0.2421 0.2682 0.0083  -0.0208 -0.0144 837  PHE B CE2 
15082 C CZ  . PHE B 839  ? 0.2658 0.2557 0.2835 0.0088  -0.0216 -0.0142 837  PHE B CZ  
15083 N N   . ASP B 840  ? 0.2854 0.2731 0.3004 0.0098  -0.0130 -0.0161 838  ASP B N   
15084 C CA  . ASP B 840  ? 0.2971 0.2839 0.3114 0.0099  -0.0119 -0.0164 838  ASP B CA  
15085 C C   . ASP B 840  ? 0.3011 0.2896 0.3183 0.0112  -0.0110 -0.0168 838  ASP B C   
15086 O O   . ASP B 840  ? 0.2667 0.2577 0.2863 0.0114  -0.0106 -0.0169 838  ASP B O   
15087 C CB  . ASP B 840  ? 0.3863 0.3738 0.3987 0.0086  -0.0110 -0.0168 838  ASP B CB  
15088 C CG  . ASP B 840  ? 0.4753 0.4620 0.4865 0.0082  -0.0101 -0.0171 838  ASP B CG  
15089 O OD1 . ASP B 840  ? 0.5566 0.5441 0.5694 0.0091  -0.0092 -0.0175 838  ASP B OD1 
15090 O OD2 . ASP B 840  ? 0.5635 0.5487 0.5721 0.0070  -0.0103 -0.0168 838  ASP B OD2 
15091 N N   . SER B 841  ? 0.2697 0.2568 0.2867 0.0121  -0.0105 -0.0170 839  SER B N   
15092 C CA  . SER B 841  ? 0.2577 0.2463 0.2772 0.0136  -0.0095 -0.0174 839  SER B CA  
15093 C C   . SER B 841  ? 0.2206 0.2112 0.2434 0.0147  -0.0101 -0.0169 839  SER B C   
15094 O O   . SER B 841  ? 0.2111 0.2043 0.2367 0.0156  -0.0092 -0.0169 839  SER B O   
15095 C CB  . SER B 841  ? 0.3309 0.3217 0.3510 0.0131  -0.0081 -0.0178 839  SER B CB  
15096 O OG  . SER B 841  ? 0.3483 0.3376 0.3654 0.0120  -0.0076 -0.0182 839  SER B OG  
15097 N N   . ALA B 842  ? 0.2278 0.2175 0.2504 0.0147  -0.0117 -0.0163 840  ALA B N   
15098 C CA  . ALA B 842  ? 0.1945 0.1863 0.2203 0.0156  -0.0127 -0.0156 840  ALA B CA  
15099 C C   . ALA B 842  ? 0.1771 0.1721 0.2053 0.0148  -0.0123 -0.0157 840  ALA B C   
15100 O O   . ALA B 842  ? 0.1990 0.1968 0.2308 0.0155  -0.0123 -0.0153 840  ALA B O   
15101 C CB  . ALA B 842  ? 0.2058 0.1981 0.2338 0.0178  -0.0125 -0.0155 840  ALA B CB  
15102 N N   . GLY B 843  ? 0.1869 0.1816 0.2133 0.0133  -0.0119 -0.0161 841  GLY B N   
15103 C CA  . GLY B 843  ? 0.1989 0.1956 0.2268 0.0125  -0.0117 -0.0161 841  GLY B CA  
15104 C C   . GLY B 843  ? 0.1776 0.1765 0.2078 0.0130  -0.0101 -0.0163 841  GLY B C   
15105 O O   . GLY B 843  ? 0.1833 0.1839 0.2153 0.0124  -0.0099 -0.0161 841  GLY B O   
15106 N N   . GLN B 844  ? 0.1713 0.1697 0.2010 0.0140  -0.0089 -0.0165 842  GLN B N   
15107 C CA  . GLN B 844  ? 0.1756 0.1760 0.2070 0.0146  -0.0073 -0.0166 842  GLN B CA  
15108 C C   . GLN B 844  ? 0.1904 0.1904 0.2198 0.0137  -0.0063 -0.0171 842  GLN B C   
15109 O O   . GLN B 844  ? 0.1995 0.1991 0.2278 0.0142  -0.0051 -0.0175 842  GLN B O   
15110 C CB  . GLN B 844  ? 0.1688 0.1690 0.2008 0.0163  -0.0067 -0.0167 842  GLN B CB  
15111 C CG  . GLN B 844  ? 0.1687 0.1703 0.2035 0.0173  -0.0077 -0.0161 842  GLN B CG  
15112 C CD  . GLN B 844  ? 0.1865 0.1873 0.2213 0.0194  -0.0074 -0.0162 842  GLN B CD  
15113 O OE1 . GLN B 844  ? 0.1892 0.1926 0.2270 0.0209  -0.0067 -0.0159 842  GLN B OE1 
15114 N NE2 . GLN B 844  ? 0.2024 0.1993 0.2337 0.0195  -0.0078 -0.0167 842  GLN B NE2 
15115 N N   . ARG B 845  ? 0.1985 0.1984 0.2272 0.0126  -0.0067 -0.0171 843  ARG B N   
15116 C CA  . ARG B 845  ? 0.1657 0.1657 0.1931 0.0119  -0.0058 -0.0174 843  ARG B CA  
15117 C C   . ARG B 845  ? 0.1708 0.1721 0.2000 0.0114  -0.0059 -0.0171 843  ARG B C   
15118 O O   . ARG B 845  ? 0.1722 0.1733 0.2021 0.0109  -0.0071 -0.0169 843  ARG B O   
15119 C CB  . ARG B 845  ? 0.1949 0.1933 0.2192 0.0111  -0.0062 -0.0178 843  ARG B CB  
15120 C CG  . ARG B 845  ? 0.2273 0.2241 0.2495 0.0112  -0.0063 -0.0180 843  ARG B CG  
15121 C CD  . ARG B 845  ? 0.2932 0.2893 0.3128 0.0101  -0.0063 -0.0182 843  ARG B CD  
15122 N NE  . ARG B 845  ? 0.3571 0.3518 0.3745 0.0097  -0.0063 -0.0183 843  ARG B NE  
15123 C CZ  . ARG B 845  ? 0.3947 0.3876 0.4104 0.0091  -0.0073 -0.0181 843  ARG B CZ  
15124 N NH1 . ARG B 845  ? 0.4168 0.4093 0.4327 0.0091  -0.0083 -0.0178 843  ARG B NH1 
15125 N NH2 . ARG B 845  ? 0.4725 0.4639 0.4860 0.0084  -0.0073 -0.0181 843  ARG B NH2 
15126 N N   . CYS B 846  ? 0.1759 0.1781 0.2054 0.0114  -0.0048 -0.0170 844  CYS B N   
15127 C CA  . CYS B 846  ? 0.1918 0.1945 0.2226 0.0108  -0.0049 -0.0166 844  CYS B CA  
15128 C C   . CYS B 846  ? 0.1614 0.1624 0.1902 0.0101  -0.0059 -0.0170 844  CYS B C   
15129 O O   . CYS B 846  ? 0.1892 0.1896 0.2187 0.0095  -0.0067 -0.0169 844  CYS B O   
15130 C CB  . CYS B 846  ? 0.1936 0.1972 0.2246 0.0109  -0.0036 -0.0163 844  CYS B CB  
15131 S SG  . CYS B 846  ? 0.2075 0.2105 0.2355 0.0112  -0.0028 -0.0169 844  CYS B SG  
15132 N N   . SER B 847  ? 0.1610 0.1610 0.1872 0.0102  -0.0057 -0.0175 845  SER B N   
15133 C CA  . SER B 847  ? 0.1606 0.1593 0.1846 0.0098  -0.0062 -0.0180 845  SER B CA  
15134 C C   . SER B 847  ? 0.1828 0.1803 0.2059 0.0094  -0.0076 -0.0181 845  SER B C   
15135 O O   . SER B 847  ? 0.1751 0.1715 0.1961 0.0091  -0.0081 -0.0185 845  SER B O   
15136 C CB  . SER B 847  ? 0.1746 0.1735 0.1964 0.0100  -0.0054 -0.0183 845  SER B CB  
15137 O OG  . SER B 847  ? 0.1930 0.1920 0.2147 0.0100  -0.0054 -0.0182 845  SER B OG  
15138 N N   . ALA B 848  ? 0.1736 0.1715 0.1984 0.0096  -0.0083 -0.0178 846  ALA B N   
15139 C CA  . ALA B 848  ? 0.1796 0.1765 0.2034 0.0093  -0.0096 -0.0177 846  ALA B CA  
15140 C C   . ALA B 848  ? 0.1860 0.1820 0.2093 0.0086  -0.0109 -0.0179 846  ALA B C   
15141 O O   . ALA B 848  ? 0.1782 0.1746 0.2031 0.0083  -0.0111 -0.0178 846  ALA B O   
15142 C CB  . ALA B 848  ? 0.1701 0.1676 0.1961 0.0099  -0.0102 -0.0172 846  ALA B CB  
15143 N N   . LEU B 849  ? 0.1794 0.1740 0.2002 0.0083  -0.0118 -0.0181 847  LEU B N   
15144 C CA  . LEU B 849  ? 0.1857 0.1792 0.2054 0.0076  -0.0132 -0.0184 847  LEU B CA  
15145 C C   . LEU B 849  ? 0.1777 0.1718 0.1999 0.0073  -0.0147 -0.0178 847  LEU B C   
15146 O O   . LEU B 849  ? 0.2025 0.1970 0.2255 0.0077  -0.0154 -0.0173 847  LEU B O   
15147 C CB  . LEU B 849  ? 0.1977 0.1897 0.2138 0.0074  -0.0137 -0.0186 847  LEU B CB  
15148 C CG  . LEU B 849  ? 0.2007 0.1913 0.2150 0.0067  -0.0152 -0.0190 847  LEU B CG  
15149 C CD1 . LEU B 849  ? 0.2149 0.2045 0.2284 0.0066  -0.0150 -0.0198 847  LEU B CD1 
15150 C CD2 . LEU B 849  ? 0.2048 0.1943 0.2154 0.0065  -0.0155 -0.0191 847  LEU B CD2 
15151 N N   . ARG B 850  ? 0.1757 0.1699 0.1993 0.0067  -0.0153 -0.0179 848  ARG B N   
15152 C CA  . ARG B 850  ? 0.1714 0.1668 0.1978 0.0061  -0.0168 -0.0173 848  ARG B CA  
15153 C C   . ARG B 850  ? 0.1809 0.1747 0.2055 0.0051  -0.0188 -0.0176 848  ARG B C   
15154 O O   . ARG B 850  ? 0.1929 0.1877 0.2191 0.0047  -0.0205 -0.0170 848  ARG B O   
15155 C CB  . ARG B 850  ? 0.1974 0.1944 0.2271 0.0058  -0.0162 -0.0168 848  ARG B CB  
15156 C CG  . ARG B 850  ? 0.2132 0.2117 0.2443 0.0068  -0.0142 -0.0166 848  ARG B CG  
15157 C CD  . ARG B 850  ? 0.2147 0.2147 0.2471 0.0078  -0.0140 -0.0161 848  ARG B CD  
15158 N NE  . ARG B 850  ? 0.2040 0.2054 0.2378 0.0087  -0.0121 -0.0159 848  ARG B NE  
15159 C CZ  . ARG B 850  ? 0.1811 0.1831 0.2153 0.0099  -0.0115 -0.0158 848  ARG B CZ  
15160 N NH1 . ARG B 850  ? 0.1950 0.1964 0.2286 0.0103  -0.0126 -0.0156 848  ARG B NH1 
15161 N NH2 . ARG B 850  ? 0.1948 0.1979 0.2298 0.0106  -0.0098 -0.0157 848  ARG B NH2 
15162 N N   . VAL B 851  ? 0.1927 0.1840 0.2138 0.0047  -0.0187 -0.0186 849  VAL B N   
15163 C CA  . VAL B 851  ? 0.1891 0.1784 0.2079 0.0037  -0.0206 -0.0191 849  VAL B CA  
15164 C C   . VAL B 851  ? 0.2038 0.1908 0.2179 0.0041  -0.0202 -0.0201 849  VAL B C   
15165 O O   . VAL B 851  ? 0.2044 0.1904 0.2167 0.0046  -0.0187 -0.0208 849  VAL B O   
15166 C CB  . VAL B 851  ? 0.2263 0.2143 0.2457 0.0027  -0.0211 -0.0195 849  VAL B CB  
15167 C CG1 . VAL B 851  ? 0.2504 0.2360 0.2671 0.0015  -0.0233 -0.0202 849  VAL B CG1 
15168 C CG2 . VAL B 851  ? 0.2501 0.2408 0.2744 0.0021  -0.0212 -0.0184 849  VAL B CG2 
15169 N N   . LEU B 852  ? 0.1975 0.1840 0.2095 0.0039  -0.0214 -0.0199 850  LEU B N   
15170 C CA  . LEU B 852  ? 0.1773 0.1621 0.1846 0.0041  -0.0210 -0.0207 850  LEU B CA  
15171 C C   . LEU B 852  ? 0.1985 0.1808 0.2028 0.0033  -0.0227 -0.0216 850  LEU B C   
15172 O O   . LEU B 852  ? 0.2075 0.1898 0.2123 0.0024  -0.0248 -0.0212 850  LEU B O   
15173 C CB  . LEU B 852  ? 0.1895 0.1750 0.1959 0.0043  -0.0214 -0.0198 850  LEU B CB  
15174 C CG  . LEU B 852  ? 0.1900 0.1740 0.1916 0.0043  -0.0212 -0.0203 850  LEU B CG  
15175 C CD1 . LEU B 852  ? 0.2042 0.1884 0.2044 0.0050  -0.0188 -0.0209 850  LEU B CD1 
15176 C CD2 . LEU B 852  ? 0.2130 0.1974 0.2139 0.0043  -0.0218 -0.0192 850  LEU B CD2 
15177 N N   . CYS B 853  ? 0.2028 0.1831 0.2041 0.0036  -0.0217 -0.0228 851  CYS B N   
15178 C CA  . CYS B 853  ? 0.1985 0.1757 0.1962 0.0030  -0.0231 -0.0240 851  CYS B CA  
15179 C C   . CYS B 853  ? 0.1916 0.1677 0.1843 0.0035  -0.0227 -0.0247 851  CYS B C   
15180 O O   . CYS B 853  ? 0.2125 0.1887 0.2034 0.0047  -0.0207 -0.0252 851  CYS B O   
15181 C CB  . CYS B 853  ? 0.2143 0.1895 0.2119 0.0032  -0.0224 -0.0250 851  CYS B CB  
15182 S SG  . CYS B 853  ? 0.2568 0.2338 0.2603 0.0026  -0.0224 -0.0239 851  CYS B SG  
15183 N N   . LEU B 854  ? 0.2173 0.1924 0.2075 0.0027  -0.0247 -0.0247 852  LEU B N   
15184 C CA  . LEU B 854  ? 0.2119 0.1862 0.1973 0.0030  -0.0244 -0.0251 852  LEU B CA  
15185 C C   . LEU B 854  ? 0.2253 0.1962 0.2060 0.0026  -0.0257 -0.0266 852  LEU B C   
15186 O O   . LEU B 854  ? 0.2421 0.2117 0.2230 0.0013  -0.0281 -0.0267 852  LEU B O   
15187 C CB  . LEU B 854  ? 0.2249 0.2006 0.2107 0.0024  -0.0258 -0.0237 852  LEU B CB  
15188 C CG  . LEU B 854  ? 0.2100 0.1885 0.2000 0.0028  -0.0248 -0.0222 852  LEU B CG  
15189 C CD1 . LEU B 854  ? 0.2353 0.2144 0.2255 0.0023  -0.0266 -0.0208 852  LEU B CD1 
15190 C CD2 . LEU B 854  ? 0.2436 0.2230 0.2326 0.0037  -0.0222 -0.0222 852  LEU B CD2 
15191 N N   . GLN B 855  ? 0.2251 0.1947 0.2015 0.0036  -0.0241 -0.0278 853  GLN B N   
15192 C CA  . GLN B 855  ? 0.2348 0.2008 0.2057 0.0035  -0.0252 -0.0294 853  GLN B CA  
15193 C C   . GLN B 855  ? 0.2685 0.2342 0.2373 0.0021  -0.0276 -0.0288 853  GLN B C   
15194 O O   . GLN B 855  ? 0.2425 0.2105 0.2117 0.0021  -0.0274 -0.0274 853  GLN B O   
15195 C CB  . GLN B 855  ? 0.2164 0.1818 0.1829 0.0051  -0.0228 -0.0306 853  GLN B CB  
15196 C CG  . GLN B 855  ? 0.2728 0.2340 0.2336 0.0054  -0.0236 -0.0327 853  GLN B CG  
15197 C CD  . GLN B 855  ? 0.3363 0.2971 0.2928 0.0074  -0.0211 -0.0339 853  GLN B CD  
15198 O OE1 . GLN B 855  ? 0.3568 0.3199 0.3154 0.0088  -0.0187 -0.0336 853  GLN B OE1 
15199 N NE2 . GLN B 855  ? 0.3544 0.3127 0.3047 0.0075  -0.0216 -0.0352 853  GLN B NE2 
15200 N N   . GLU B 856  ? 0.2702 0.2330 0.2368 0.0010  -0.0301 -0.0298 854  GLU B N   
15201 C CA  . GLU B 856  ? 0.2599 0.2228 0.2255 -0.0005 -0.0329 -0.0290 854  GLU B CA  
15202 C C   . GLU B 856  ? 0.2968 0.2601 0.2579 -0.0001 -0.0325 -0.0286 854  GLU B C   
15203 O O   . GLU B 856  ? 0.3307 0.2956 0.2927 -0.0009 -0.0341 -0.0270 854  GLU B O   
15204 C CB  . GLU B 856  ? 0.3562 0.3155 0.3193 -0.0019 -0.0356 -0.0303 854  GLU B CB  
15205 N N   . ASP B 857  ? 0.2860 0.2480 0.2423 0.0011  -0.0305 -0.0299 855  ASP B N   
15206 C CA  . ASP B 857  ? 0.3051 0.2674 0.2564 0.0012  -0.0301 -0.0296 855  ASP B CA  
15207 C C   . ASP B 857  ? 0.3241 0.2900 0.2780 0.0015  -0.0286 -0.0275 855  ASP B C   
15208 O O   . ASP B 857  ? 0.3585 0.3248 0.3091 0.0011  -0.0289 -0.0266 855  ASP B O   
15209 C CB  . ASP B 857  ? 0.3660 0.3263 0.3116 0.0026  -0.0280 -0.0315 855  ASP B CB  
15210 N N   . VAL B 858  ? 0.2682 0.2363 0.2274 0.0020  -0.0271 -0.0267 856  VAL B N   
15211 C CA  . VAL B 858  ? 0.2534 0.2245 0.2149 0.0021  -0.0258 -0.0249 856  VAL B CA  
15212 C C   . VAL B 858  ? 0.2303 0.2028 0.1975 0.0015  -0.0271 -0.0234 856  VAL B C   
15213 O O   . VAL B 858  ? 0.2660 0.2404 0.2352 0.0016  -0.0264 -0.0218 856  VAL B O   
15214 C CB  . VAL B 858  ? 0.2589 0.2319 0.2213 0.0033  -0.0225 -0.0252 856  VAL B CB  
15215 C CG1 . VAL B 858  ? 0.3074 0.2796 0.2641 0.0042  -0.0210 -0.0265 856  VAL B CG1 
15216 C CG2 . VAL B 858  ? 0.2765 0.2496 0.2432 0.0040  -0.0219 -0.0259 856  VAL B CG2 
15217 N N   . ALA B 859  ? 0.2456 0.2173 0.2154 0.0010  -0.0291 -0.0237 857  ALA B N   
15218 C CA  . ALA B 859  ? 0.2575 0.2312 0.2333 0.0008  -0.0300 -0.0224 857  ALA B CA  
15219 C C   . ALA B 859  ? 0.2341 0.2087 0.2101 0.0004  -0.0314 -0.0205 857  ALA B C   
15220 O O   . ALA B 859  ? 0.2589 0.2352 0.2385 0.0008  -0.0307 -0.0193 857  ALA B O   
15221 C CB  . ALA B 859  ? 0.2538 0.2266 0.2319 0.0000  -0.0320 -0.0230 857  ALA B CB  
15222 N N   . ASP B 860  ? 0.2494 0.2226 0.2216 -0.0004 -0.0335 -0.0204 858  ASP B N   
15223 C CA  . ASP B 860  ? 0.2789 0.2527 0.2512 -0.0006 -0.0352 -0.0185 858  ASP B CA  
15224 C C   . ASP B 860  ? 0.2689 0.2433 0.2402 -0.0002 -0.0332 -0.0174 858  ASP B C   
15225 O O   . ASP B 860  ? 0.2660 0.2414 0.2402 0.0001  -0.0335 -0.0158 858  ASP B O   
15226 C CB  . ASP B 860  ? 0.2617 0.2338 0.2292 -0.0016 -0.0378 -0.0186 858  ASP B CB  
15227 C CG  . ASP B 860  ? 0.4078 0.3796 0.3769 -0.0024 -0.0404 -0.0192 858  ASP B CG  
15228 O OD1 . ASP B 860  ? 0.4028 0.3764 0.3777 -0.0023 -0.0409 -0.0187 858  ASP B OD1 
15229 O OD2 . ASP B 860  ? 0.4667 0.4364 0.4312 -0.0033 -0.0421 -0.0202 858  ASP B OD2 
15230 N N   . ARG B 861  ? 0.2679 0.2417 0.2349 -0.0001 -0.0312 -0.0181 859  ARG B N   
15231 C CA  . ARG B 861  ? 0.2602 0.2348 0.2261 0.0000  -0.0294 -0.0169 859  ARG B CA  
15232 C C   . ARG B 861  ? 0.2686 0.2448 0.2395 0.0006  -0.0276 -0.0166 859  ARG B C   
15233 O O   . ARG B 861  ? 0.2683 0.2449 0.2404 0.0005  -0.0274 -0.0150 859  ARG B O   
15234 C CB  . ARG B 861  ? 0.3487 0.3230 0.3093 0.0000  -0.0274 -0.0178 859  ARG B CB  
15235 C CG  . ARG B 861  ? 0.4573 0.4329 0.4172 -0.0002 -0.0254 -0.0164 859  ARG B CG  
15236 C CD  . ARG B 861  ? 0.5384 0.5141 0.4925 -0.0005 -0.0240 -0.0167 859  ARG B CD  
15237 N NE  . ARG B 861  ? 0.5950 0.5725 0.5493 -0.0010 -0.0220 -0.0153 859  ARG B NE  
15238 C CZ  . ARG B 861  ? 0.5287 0.5084 0.4848 -0.0005 -0.0194 -0.0159 859  ARG B CZ  
15239 N NH1 . ARG B 861  ? 0.5533 0.5335 0.5108 0.0007  -0.0184 -0.0177 859  ARG B NH1 
15240 N NH2 . ARG B 861  ? 0.5398 0.5210 0.4961 -0.0013 -0.0179 -0.0144 859  ARG B NH2 
15241 N N   . ILE B 862  ? 0.2497 0.2267 0.2233 0.0012  -0.0264 -0.0179 860  ILE B N   
15242 C CA  . ILE B 862  ? 0.2241 0.2027 0.2023 0.0018  -0.0248 -0.0176 860  ILE B CA  
15243 C C   . ILE B 862  ? 0.2117 0.1906 0.1942 0.0019  -0.0264 -0.0164 860  ILE B C   
15244 O O   . ILE B 862  ? 0.2361 0.2157 0.2207 0.0022  -0.0256 -0.0155 860  ILE B O   
15245 C CB  . ILE B 862  ? 0.2284 0.2076 0.2083 0.0024  -0.0233 -0.0192 860  ILE B CB  
15246 C CG1 . ILE B 862  ? 0.3002 0.2796 0.2762 0.0027  -0.0213 -0.0201 860  ILE B CG1 
15247 C CG2 . ILE B 862  ? 0.2391 0.2199 0.2239 0.0030  -0.0222 -0.0188 860  ILE B CG2 
15248 C CD1 . ILE B 862  ? 0.3280 0.3072 0.3045 0.0036  -0.0201 -0.0218 860  ILE B CD1 
15249 N N   . LEU B 863  ? 0.2344 0.2130 0.2182 0.0018  -0.0286 -0.0166 861  LEU B N   
15250 C CA  . LEU B 863  ? 0.2418 0.2214 0.2300 0.0021  -0.0300 -0.0154 861  LEU B CA  
15251 C C   . LEU B 863  ? 0.2567 0.2355 0.2435 0.0022  -0.0310 -0.0137 861  LEU B C   
15252 O O   . LEU B 863  ? 0.2303 0.2096 0.2203 0.0029  -0.0309 -0.0127 861  LEU B O   
15253 C CB  . LEU B 863  ? 0.2531 0.2330 0.2429 0.0017  -0.0324 -0.0157 861  LEU B CB  
15254 C CG  . LEU B 863  ? 0.2905 0.2710 0.2827 0.0017  -0.0316 -0.0171 861  LEU B CG  
15255 C CD1 . LEU B 863  ? 0.3073 0.2877 0.3001 0.0008  -0.0342 -0.0174 861  LEU B CD1 
15256 C CD2 . LEU B 863  ? 0.3123 0.2949 0.3098 0.0025  -0.0301 -0.0167 861  LEU B CD2 
15257 N N   . THR B 864  ? 0.2324 0.2097 0.2143 0.0015  -0.0319 -0.0133 862  THR B N   
15258 C CA  . THR B 864  ? 0.2325 0.2086 0.2126 0.0014  -0.0328 -0.0116 862  THR B CA  
15259 C C   . THR B 864  ? 0.2634 0.2393 0.2437 0.0016  -0.0306 -0.0110 862  THR B C   
15260 O O   . THR B 864  ? 0.2601 0.2353 0.2420 0.0020  -0.0310 -0.0097 862  THR B O   
15261 C CB  . THR B 864  ? 0.3167 0.2913 0.2910 0.0005  -0.0339 -0.0113 862  THR B CB  
15262 O OG1 . THR B 864  ? 0.3350 0.3096 0.3091 0.0003  -0.0364 -0.0116 862  THR B OG1 
15263 C CG2 . THR B 864  ? 0.3420 0.3150 0.3139 0.0003  -0.0345 -0.0093 862  THR B CG2 
15264 N N   . MET B 865  ? 0.2417 0.2182 0.2206 0.0012  -0.0282 -0.0120 863  MET B N   
15265 C CA  . MET B 865  ? 0.2529 0.2296 0.2320 0.0010  -0.0262 -0.0115 863  MET B CA  
15266 C C   . MET B 865  ? 0.2318 0.2093 0.2159 0.0019  -0.0256 -0.0116 863  MET B C   
15267 O O   . MET B 865  ? 0.2330 0.2096 0.2179 0.0020  -0.0253 -0.0107 863  MET B O   
15268 C CB  . MET B 865  ? 0.2504 0.2283 0.2272 0.0006  -0.0240 -0.0126 863  MET B CB  
15269 C CG  . MET B 865  ? 0.2801 0.2587 0.2568 0.0000  -0.0220 -0.0120 863  MET B CG  
15270 S SD  . MET B 865  ? 0.3011 0.2819 0.2754 -0.0003 -0.0193 -0.0130 863  MET B SD  
15271 C CE  . MET B 865  ? 0.3390 0.3188 0.3074 -0.0009 -0.0202 -0.0129 863  MET B CE  
15272 N N   . LEU B 866  ? 0.2245 0.2035 0.2119 0.0026  -0.0254 -0.0128 864  LEU B N   
15273 C CA  . LEU B 866  ? 0.2171 0.1971 0.2092 0.0035  -0.0248 -0.0130 864  LEU B CA  
15274 C C   . LEU B 866  ? 0.2383 0.2175 0.2324 0.0043  -0.0265 -0.0117 864  LEU B C   
15275 O O   . LEU B 866  ? 0.2301 0.2088 0.2258 0.0049  -0.0257 -0.0113 864  LEU B O   
15276 C CB  . LEU B 866  ? 0.2117 0.1933 0.2066 0.0039  -0.0248 -0.0142 864  LEU B CB  
15277 C CG  . LEU B 866  ? 0.2197 0.2027 0.2195 0.0048  -0.0242 -0.0143 864  LEU B CG  
15278 C CD1 . LEU B 866  ? 0.2248 0.2081 0.2249 0.0050  -0.0220 -0.0144 864  LEU B CD1 
15279 C CD2 . LEU B 866  ? 0.2536 0.2380 0.2557 0.0048  -0.0243 -0.0153 864  LEU B CD2 
15280 N N   . LYS B 867  ? 0.2325 0.2113 0.2261 0.0043  -0.0288 -0.0111 865  LYS B N   
15281 C CA  . LYS B 867  ? 0.2378 0.2162 0.2336 0.0054  -0.0304 -0.0099 865  LYS B CA  
15282 C C   . LYS B 867  ? 0.2254 0.2010 0.2183 0.0053  -0.0304 -0.0086 865  LYS B C   
15283 O O   . LYS B 867  ? 0.2343 0.2090 0.2291 0.0064  -0.0305 -0.0079 865  LYS B O   
15284 C CB  . LYS B 867  ? 0.2334 0.2123 0.2294 0.0054  -0.0331 -0.0094 865  LYS B CB  
15285 C CG  . LYS B 867  ? 0.2927 0.2742 0.2924 0.0054  -0.0333 -0.0105 865  LYS B CG  
15286 C CD  . LYS B 867  ? 0.3041 0.2863 0.3034 0.0048  -0.0359 -0.0103 865  LYS B CD  
15287 C CE  . LYS B 867  ? 0.3889 0.3732 0.3913 0.0044  -0.0359 -0.0114 865  LYS B CE  
15288 N NZ  . LYS B 867  ? 0.4430 0.4277 0.4444 0.0034  -0.0386 -0.0115 865  LYS B NZ  
15289 N N   . GLY B 868  ? 0.2280 0.2022 0.2161 0.0039  -0.0302 -0.0083 866  GLY B N   
15290 C CA  . GLY B 868  ? 0.2264 0.1979 0.2117 0.0035  -0.0301 -0.0069 866  GLY B CA  
15291 C C   . GLY B 868  ? 0.2423 0.2134 0.2288 0.0035  -0.0280 -0.0072 866  GLY B C   
15292 O O   . GLY B 868  ? 0.2584 0.2271 0.2448 0.0038  -0.0283 -0.0063 866  GLY B O   
15293 N N   . ALA B 869  ? 0.2312 0.2045 0.2189 0.0031  -0.0260 -0.0086 867  ALA B N   
15294 C CA  . ALA B 869  ? 0.2447 0.2181 0.2338 0.0031  -0.0242 -0.0090 867  ALA B CA  
15295 C C   . ALA B 869  ? 0.2393 0.2126 0.2324 0.0048  -0.0244 -0.0092 867  ALA B C   
15296 O O   . ALA B 869  ? 0.2309 0.2024 0.2242 0.0050  -0.0239 -0.0089 867  ALA B O   
15297 C CB  . ALA B 869  ? 0.2482 0.2243 0.2377 0.0025  -0.0222 -0.0104 867  ALA B CB  
15298 N N   . LEU B 870  ? 0.2261 0.2013 0.2225 0.0059  -0.0253 -0.0097 868  LEU B N   
15299 C CA  . LEU B 870  ? 0.2433 0.2190 0.2437 0.0077  -0.0254 -0.0098 868  LEU B CA  
15300 C C   . LEU B 870  ? 0.2197 0.1926 0.2196 0.0087  -0.0267 -0.0085 868  LEU B C   
15301 O O   . LEU B 870  ? 0.2493 0.2213 0.2511 0.0100  -0.0262 -0.0086 868  LEU B O   
15302 C CB  . LEU B 870  ? 0.2187 0.1974 0.2228 0.0084  -0.0262 -0.0102 868  LEU B CB  
15303 C CG  . LEU B 870  ? 0.2736 0.2547 0.2792 0.0079  -0.0246 -0.0116 868  LEU B CG  
15304 C CD1 . LEU B 870  ? 0.2987 0.2823 0.3073 0.0082  -0.0257 -0.0119 868  LEU B CD1 
15305 C CD2 . LEU B 870  ? 0.2460 0.2277 0.2537 0.0086  -0.0227 -0.0122 868  LEU B CD2 
15306 N N   . HIS B 871  ? 0.2144 0.1854 0.2113 0.0082  -0.0285 -0.0073 869  HIS B N   
15307 C CA  A HIS B 871  ? 0.2573 0.2252 0.2534 0.0093  -0.0299 -0.0059 869  HIS B CA  
15308 C CA  B HIS B 871  ? 0.2575 0.2253 0.2534 0.0093  -0.0300 -0.0059 869  HIS B CA  
15309 C C   . HIS B 871  ? 0.2602 0.2245 0.2538 0.0088  -0.0289 -0.0056 869  HIS B C   
15310 O O   . HIS B 871  ? 0.2871 0.2482 0.2803 0.0100  -0.0298 -0.0048 869  HIS B O   
15311 C CB  A HIS B 871  ? 0.2640 0.2307 0.2571 0.0088  -0.0322 -0.0046 869  HIS B CB  
15312 C CB  B HIS B 871  ? 0.2634 0.2301 0.2561 0.0085  -0.0320 -0.0046 869  HIS B CB  
15313 C CG  A HIS B 871  ? 0.2886 0.2579 0.2848 0.0100  -0.0340 -0.0044 869  HIS B CG  
15314 C CG  B HIS B 871  ? 0.2947 0.2578 0.2860 0.0096  -0.0338 -0.0030 869  HIS B CG  
15315 N ND1 A HIS B 871  ? 0.2981 0.2701 0.2942 0.0090  -0.0346 -0.0050 869  HIS B ND1 
15316 N ND1 B HIS B 871  ? 0.3335 0.2973 0.3280 0.0119  -0.0355 -0.0023 869  HIS B ND1 
15317 C CD2 A HIS B 871  ? 0.3370 0.3068 0.3363 0.0121  -0.0355 -0.0037 869  HIS B CD2 
15318 C CD2 B HIS B 871  ? 0.3444 0.3031 0.3317 0.0089  -0.0342 -0.0017 869  HIS B CD2 
15319 C CE1 A HIS B 871  ? 0.2987 0.2726 0.2978 0.0101  -0.0365 -0.0046 869  HIS B CE1 
15320 C CE1 B HIS B 871  ? 0.3146 0.2744 0.3069 0.0127  -0.0369 -0.0008 869  HIS B CE1 
15321 N NE2 A HIS B 871  ? 0.2773 0.2503 0.2786 0.0121  -0.0370 -0.0037 869  HIS B NE2 
15322 N NE2 B HIS B 871  ? 0.3508 0.3072 0.3385 0.0108  -0.0361 -0.0004 869  HIS B NE2 
15323 N N   . GLU B 872  ? 0.2271 0.1918 0.2191 0.0070  -0.0271 -0.0063 870  GLU B N   
15324 C CA  . GLU B 872  ? 0.2310 0.1924 0.2205 0.0061  -0.0263 -0.0060 870  GLU B CA  
15325 C C   . GLU B 872  ? 0.2237 0.1855 0.2159 0.0070  -0.0248 -0.0072 870  GLU B C   
15326 O O   . GLU B 872  ? 0.2533 0.2124 0.2436 0.0061  -0.0241 -0.0072 870  GLU B O   
15327 C CB  . GLU B 872  ? 0.2570 0.2190 0.2432 0.0035  -0.0253 -0.0058 870  GLU B CB  
15328 C CG  . GLU B 872  ? 0.2586 0.2200 0.2415 0.0025  -0.0266 -0.0046 870  GLU B CG  
15329 C CD  . GLU B 872  ? 0.2809 0.2378 0.2612 0.0026  -0.0284 -0.0029 870  GLU B CD  
15330 O OE1 . GLU B 872  ? 0.3276 0.2811 0.3073 0.0027  -0.0282 -0.0025 870  GLU B OE1 
15331 O OE2 . GLU B 872  ? 0.3030 0.2593 0.2816 0.0027  -0.0301 -0.0018 870  GLU B OE2 
15332 N N   . LEU B 873  ? 0.2340 0.1991 0.2303 0.0085  -0.0243 -0.0083 871  LEU B N   
15333 C CA  . LEU B 873  ? 0.2278 0.1935 0.2263 0.0094  -0.0227 -0.0094 871  LEU B CA  
15334 C C   . LEU B 873  ? 0.2434 0.2062 0.2428 0.0116  -0.0234 -0.0092 871  LEU B C   
15335 O O   . LEU B 873  ? 0.2625 0.2249 0.2630 0.0132  -0.0249 -0.0084 871  LEU B O   
15336 C CB  . LEU B 873  ? 0.2436 0.2140 0.2461 0.0101  -0.0218 -0.0105 871  LEU B CB  
15337 C CG  . LEU B 873  ? 0.2981 0.2712 0.3000 0.0084  -0.0210 -0.0111 871  LEU B CG  
15338 C CD1 . LEU B 873  ? 0.2798 0.2566 0.2855 0.0092  -0.0201 -0.0121 871  LEU B CD1 
15339 C CD2 . LEU B 873  ? 0.2745 0.2467 0.2736 0.0065  -0.0197 -0.0113 871  LEU B CD2 
15340 N N   . HIS B 874  ? 0.2591 0.2202 0.2582 0.0118  -0.0222 -0.0100 872  HIS B N   
15341 C CA  . HIS B 874  ? 0.2544 0.2125 0.2540 0.0141  -0.0224 -0.0101 872  HIS B CA  
15342 C C   . HIS B 874  ? 0.2198 0.1815 0.2235 0.0158  -0.0210 -0.0113 872  HIS B C   
15343 O O   . HIS B 874  ? 0.2474 0.2107 0.2513 0.0148  -0.0194 -0.0124 872  HIS B O   
15344 C CB  . HIS B 874  ? 0.2615 0.2146 0.2572 0.0129  -0.0222 -0.0101 872  HIS B CB  
15345 C CG  . HIS B 874  ? 0.2913 0.2402 0.2866 0.0152  -0.0224 -0.0104 872  HIS B CG  
15346 N ND1 . HIS B 874  ? 0.3563 0.2997 0.3478 0.0144  -0.0224 -0.0105 872  HIS B ND1 
15347 C CD2 . HIS B 874  ? 0.3183 0.2678 0.3165 0.0185  -0.0226 -0.0106 872  HIS B CD2 
15348 C CE1 . HIS B 874  ? 0.3715 0.3117 0.3633 0.0172  -0.0226 -0.0109 872  HIS B CE1 
15349 N NE2 . HIS B 874  ? 0.3736 0.3177 0.3695 0.0198  -0.0226 -0.0110 872  HIS B NE2 
15350 N N   . ILE B 875  ? 0.2231 0.1864 0.2300 0.0183  -0.0215 -0.0111 873  ILE B N   
15351 C CA  . ILE B 875  ? 0.2341 0.2011 0.2451 0.0201  -0.0202 -0.0121 873  ILE B CA  
15352 C C   . ILE B 875  ? 0.2428 0.2066 0.2534 0.0226  -0.0199 -0.0125 873  ILE B C   
15353 O O   . ILE B 875  ? 0.2569 0.2179 0.2669 0.0243  -0.0212 -0.0117 873  ILE B O   
15354 C CB  . ILE B 875  ? 0.2684 0.2400 0.2836 0.0213  -0.0211 -0.0115 873  ILE B CB  
15355 C CG1 . ILE B 875  ? 0.2990 0.2729 0.3139 0.0189  -0.0217 -0.0111 873  ILE B CG1 
15356 C CG2 . ILE B 875  ? 0.2542 0.2299 0.2736 0.0229  -0.0195 -0.0123 873  ILE B CG2 
15357 C CD1 . ILE B 875  ? 0.3559 0.3330 0.3738 0.0197  -0.0233 -0.0103 873  ILE B CD1 
15358 N N   . GLY B 876  ? 0.2196 0.1837 0.2304 0.0230  -0.0181 -0.0138 874  GLY B N   
15359 C CA  . GLY B 876  ? 0.2329 0.1937 0.2431 0.0256  -0.0176 -0.0144 874  GLY B CA  
15360 C C   . GLY B 876  ? 0.2114 0.1724 0.2211 0.0255  -0.0157 -0.0159 874  GLY B C   
15361 O O   . GLY B 876  ? 0.2346 0.1991 0.2453 0.0238  -0.0146 -0.0164 874  GLY B O   
15362 N N   . ARG B 877  ? 0.2643 0.2213 0.2723 0.0277  -0.0153 -0.0166 875  ARG B N   
15363 C CA  . ARG B 877  ? 0.2462 0.2025 0.2528 0.0277  -0.0136 -0.0181 875  ARG B CA  
15364 C C   . ARG B 877  ? 0.2657 0.2196 0.2686 0.0241  -0.0137 -0.0184 875  ARG B C   
15365 O O   . ARG B 877  ? 0.2780 0.2277 0.2777 0.0225  -0.0150 -0.0177 875  ARG B O   
15366 C CB  . ARG B 877  ? 0.2801 0.2315 0.2847 0.0306  -0.0134 -0.0190 875  ARG B CB  
15367 C CG  . ARG B 877  ? 0.3058 0.2576 0.3099 0.0316  -0.0114 -0.0206 875  ARG B CG  
15368 C CD  . ARG B 877  ? 0.3730 0.3199 0.3751 0.0350  -0.0112 -0.0215 875  ARG B CD  
15369 N NE  . ARG B 877  ? 0.3515 0.2904 0.3477 0.0338  -0.0122 -0.0221 875  ARG B NE  
15370 C CZ  . ARG B 877  ? 0.4423 0.3754 0.4354 0.0362  -0.0121 -0.0232 875  ARG B CZ  
15371 N NH1 . ARG B 877  ? 0.4248 0.3592 0.4201 0.0404  -0.0110 -0.0237 875  ARG B NH1 
15372 N NH2 . ARG B 877  ? 0.4459 0.3716 0.4334 0.0344  -0.0130 -0.0237 875  ARG B NH2 
15373 N N   . THR B 878  ? 0.2259 0.1828 0.2293 0.0229  -0.0122 -0.0193 876  THR B N   
15374 C CA  . THR B 878  ? 0.2513 0.2084 0.2528 0.0194  -0.0122 -0.0192 876  THR B CA  
15375 C C   . THR B 878  ? 0.2276 0.1795 0.2244 0.0180  -0.0124 -0.0200 876  THR B C   
15376 O O   . THR B 878  ? 0.2511 0.2036 0.2464 0.0151  -0.0123 -0.0199 876  THR B O   
15377 C CB  . THR B 878  ? 0.2330 0.1960 0.2373 0.0187  -0.0108 -0.0196 876  THR B CB  
15378 O OG1 . THR B 878  ? 0.2814 0.2455 0.2868 0.0207  -0.0094 -0.0206 876  THR B OG1 
15379 C CG2 . THR B 878  ? 0.2576 0.2252 0.2658 0.0189  -0.0112 -0.0186 876  THR B CG2 
15380 N N   . ASP B 879  ? 0.2520 0.1986 0.2464 0.0198  -0.0126 -0.0206 877  ASP B N   
15381 C CA  . ASP B 879  ? 0.2595 0.2005 0.2491 0.0183  -0.0129 -0.0215 877  ASP B CA  
15382 C C   . ASP B 879  ? 0.2804 0.2163 0.2666 0.0162  -0.0147 -0.0203 877  ASP B C   
15383 O O   . ASP B 879  ? 0.2852 0.2147 0.2672 0.0156  -0.0155 -0.0208 877  ASP B O   
15384 C CB  . ASP B 879  ? 0.2803 0.2175 0.2683 0.0212  -0.0123 -0.0229 877  ASP B CB  
15385 C CG  . ASP B 879  ? 0.3284 0.2621 0.3165 0.0244  -0.0131 -0.0225 877  ASP B CG  
15386 O OD1 . ASP B 879  ? 0.3496 0.2863 0.3409 0.0253  -0.0137 -0.0212 877  ASP B OD1 
15387 O OD2 . ASP B 879  ? 0.3357 0.2635 0.3205 0.0261  -0.0132 -0.0236 877  ASP B OD2 
15388 N N   . ARG B 880  ? 0.2815 0.2201 0.2693 0.0150  -0.0155 -0.0188 878  ARG B N   
15389 C CA  . ARG B 880  ? 0.2821 0.2170 0.2669 0.0125  -0.0170 -0.0175 878  ARG B CA  
15390 C C   . ARG B 880  ? 0.2621 0.2023 0.2482 0.0096  -0.0167 -0.0167 878  ARG B C   
15391 O O   . ARG B 880  ? 0.2492 0.1949 0.2390 0.0104  -0.0161 -0.0165 878  ARG B O   
15392 C CB  . ARG B 880  ? 0.3040 0.2371 0.2894 0.0145  -0.0184 -0.0163 878  ARG B CB  
15393 C CG  . ARG B 880  ? 0.3933 0.3198 0.3764 0.0172  -0.0191 -0.0166 878  ARG B CG  
15394 C CD  . ARG B 880  ? 0.4221 0.3472 0.4058 0.0188  -0.0206 -0.0151 878  ARG B CD  
15395 N NE  . ARG B 880  ? 0.6058 0.5260 0.5886 0.0225  -0.0211 -0.0155 878  ARG B NE  
15396 C CZ  . ARG B 880  ? 0.6569 0.5693 0.6354 0.0226  -0.0225 -0.0151 878  ARG B CZ  
15397 N NH1 . ARG B 880  ? 0.6503 0.5587 0.6248 0.0190  -0.0236 -0.0140 878  ARG B NH1 
15398 N NH2 . ARG B 880  ? 0.6541 0.5624 0.6320 0.0264  -0.0227 -0.0156 878  ARG B NH2 
15399 N N   . LEU B 881  ? 0.2510 0.1893 0.2340 0.0063  -0.0172 -0.0162 879  LEU B N   
15400 C CA  . LEU B 881  ? 0.2605 0.2036 0.2445 0.0036  -0.0168 -0.0154 879  LEU B CA  
15401 C C   . LEU B 881  ? 0.2585 0.2039 0.2440 0.0040  -0.0174 -0.0141 879  LEU B C   
15402 O O   . LEU B 881  ? 0.2626 0.2135 0.2504 0.0033  -0.0167 -0.0139 879  LEU B O   
15403 C CB  . LEU B 881  ? 0.2634 0.2038 0.2437 0.0000  -0.0174 -0.0149 879  LEU B CB  
15404 C CG  . LEU B 881  ? 0.2965 0.2422 0.2776 -0.0028 -0.0169 -0.0141 879  LEU B CG  
15405 C CD1 . LEU B 881  ? 0.2993 0.2504 0.2832 -0.0025 -0.0154 -0.0153 879  LEU B CD1 
15406 C CD2 . LEU B 881  ? 0.2822 0.2249 0.2598 -0.0064 -0.0177 -0.0132 879  LEU B CD2 
15407 N N   . SER B 882  ? 0.2374 0.1787 0.2216 0.0052  -0.0188 -0.0133 880  SER B N   
15408 C CA  . SER B 882  ? 0.2530 0.1961 0.2382 0.0055  -0.0196 -0.0120 880  SER B CA  
15409 C C   . SER B 882  ? 0.2745 0.2224 0.2641 0.0080  -0.0191 -0.0124 880  SER B C   
15410 O O   . SER B 882  ? 0.2670 0.2168 0.2575 0.0082  -0.0198 -0.0115 880  SER B O   
15411 C CB  . SER B 882  ? 0.2781 0.2151 0.2606 0.0062  -0.0213 -0.0108 880  SER B CB  
15412 O OG  . SER B 882  ? 0.3159 0.2506 0.2996 0.0097  -0.0215 -0.0115 880  SER B OG  
15413 N N   . VAL B 883  ? 0.2466 0.1965 0.2388 0.0099  -0.0179 -0.0138 881  VAL B N   
15414 C CA  . VAL B 883  ? 0.2392 0.1938 0.2357 0.0121  -0.0175 -0.0140 881  VAL B CA  
15415 C C   . VAL B 883  ? 0.2524 0.2125 0.2509 0.0106  -0.0165 -0.0143 881  VAL B C   
15416 O O   . VAL B 883  ? 0.2840 0.2454 0.2821 0.0093  -0.0153 -0.0150 881  VAL B O   
15417 C CB  . VAL B 883  ? 0.2496 0.2041 0.2481 0.0149  -0.0167 -0.0152 881  VAL B CB  
15418 C CG1 . VAL B 883  ? 0.2618 0.2219 0.2649 0.0165  -0.0160 -0.0154 881  VAL B CG1 
15419 C CG2 . VAL B 883  ? 0.2726 0.2219 0.2695 0.0170  -0.0178 -0.0148 881  VAL B CG2 
15420 N N   . ASP B 884  ? 0.2403 0.2034 0.2408 0.0109  -0.0170 -0.0137 882  ASP B N   
15421 C CA  . ASP B 884  ? 0.2438 0.2115 0.2458 0.0097  -0.0162 -0.0139 882  ASP B CA  
15422 C C   . ASP B 884  ? 0.2706 0.2423 0.2767 0.0114  -0.0154 -0.0146 882  ASP B C   
15423 O O   . ASP B 884  ? 0.3116 0.2862 0.3187 0.0107  -0.0142 -0.0153 882  ASP B O   
15424 C CB  . ASP B 884  ? 0.2531 0.2214 0.2543 0.0089  -0.0174 -0.0129 882  ASP B CB  
15425 C CG  . ASP B 884  ? 0.2570 0.2217 0.2540 0.0070  -0.0182 -0.0119 882  ASP B CG  
15426 O OD1 . ASP B 884  ? 0.2793 0.2439 0.2745 0.0051  -0.0173 -0.0121 882  ASP B OD1 
15427 O OD2 . ASP B 884  ? 0.2605 0.2225 0.2561 0.0073  -0.0197 -0.0109 882  ASP B OD2 
15428 N N   . VAL B 885  ? 0.2442 0.2162 0.2526 0.0135  -0.0161 -0.0144 883  VAL B N   
15429 C CA  . VAL B 885  ? 0.2348 0.2107 0.2473 0.0150  -0.0154 -0.0148 883  VAL B CA  
15430 C C   . VAL B 885  ? 0.2125 0.1875 0.2264 0.0174  -0.0149 -0.0152 883  VAL B C   
15431 O O   . VAL B 885  ? 0.2306 0.2028 0.2438 0.0188  -0.0160 -0.0147 883  VAL B O   
15432 C CB  . VAL B 885  ? 0.2631 0.2412 0.2776 0.0153  -0.0168 -0.0140 883  VAL B CB  
15433 C CG1 . VAL B 885  ? 0.2748 0.2572 0.2938 0.0164  -0.0162 -0.0143 883  VAL B CG1 
15434 C CG2 . VAL B 885  ? 0.3082 0.2868 0.3208 0.0131  -0.0172 -0.0138 883  VAL B CG2 
15435 N N   . GLY B 886  ? 0.2380 0.2152 0.2536 0.0179  -0.0133 -0.0161 884  GLY B N   
15436 C CA  . GLY B 886  ? 0.2304 0.2072 0.2472 0.0203  -0.0125 -0.0166 884  GLY B CA  
15437 C C   . GLY B 886  ? 0.2066 0.1877 0.2280 0.0221  -0.0124 -0.0162 884  GLY B C   
15438 O O   . GLY B 886  ? 0.2090 0.1927 0.2325 0.0215  -0.0133 -0.0155 884  GLY B O   
15439 N N   . PRO B 887  ? 0.2174 0.1994 0.2404 0.0243  -0.0111 -0.0168 885  PRO B N   
15440 C CA  . PRO B 887  ? 0.1976 0.1842 0.2253 0.0261  -0.0108 -0.0163 885  PRO B CA  
15441 C C   . PRO B 887  ? 0.1793 0.1705 0.2097 0.0249  -0.0097 -0.0163 885  PRO B C   
15442 O O   . PRO B 887  ? 0.1928 0.1839 0.2216 0.0232  -0.0088 -0.0169 885  PRO B O   
15443 C CB  . PRO B 887  ? 0.1926 0.1779 0.2201 0.0288  -0.0096 -0.0170 885  PRO B CB  
15444 C CG  . PRO B 887  ? 0.1864 0.1683 0.2098 0.0276  -0.0086 -0.0182 885  PRO B CG  
15445 C CD  . PRO B 887  ? 0.2052 0.1838 0.2254 0.0251  -0.0100 -0.0178 885  PRO B CD  
15446 N N   . VAL B 888  ? 0.1932 0.1889 0.2281 0.0258  -0.0099 -0.0156 886  VAL B N   
15447 C CA  . VAL B 888  ? 0.1911 0.1912 0.2289 0.0252  -0.0085 -0.0155 886  VAL B CA  
15448 C C   . VAL B 888  ? 0.1833 0.1844 0.2218 0.0272  -0.0065 -0.0161 886  VAL B C   
15449 O O   . VAL B 888  ? 0.1930 0.1923 0.2308 0.0295  -0.0063 -0.0165 886  VAL B O   
15450 C CB  . VAL B 888  ? 0.2330 0.2377 0.2753 0.0248  -0.0096 -0.0144 886  VAL B CB  
15451 C CG1 . VAL B 888  ? 0.2009 0.2041 0.2418 0.0227  -0.0116 -0.0140 886  VAL B CG1 
15452 C CG2 . VAL B 888  ? 0.2776 0.2844 0.3231 0.0274  -0.0100 -0.0137 886  VAL B CG2 
15453 N N   . ILE B 889  ? 0.1986 0.2023 0.2380 0.0263  -0.0049 -0.0163 887  ILE B N   
15454 C CA  . ILE B 889  ? 0.1967 0.2002 0.2349 0.0277  -0.0029 -0.0172 887  ILE B CA  
15455 C C   . ILE B 889  ? 0.1890 0.1954 0.2304 0.0306  -0.0019 -0.0170 887  ILE B C   
15456 O O   . ILE B 889  ? 0.1912 0.1958 0.2307 0.0326  -0.0007 -0.0179 887  ILE B O   
15457 C CB  . ILE B 889  ? 0.1933 0.1985 0.2313 0.0260  -0.0016 -0.0173 887  ILE B CB  
15458 C CG1 . ILE B 889  ? 0.1988 0.2033 0.2348 0.0272  0.0003  -0.0183 887  ILE B CG1 
15459 C CG2 . ILE B 889  ? 0.2144 0.2248 0.2570 0.0253  -0.0014 -0.0162 887  ILE B CG2 
15460 C CD1 . ILE B 889  ? 0.2192 0.2183 0.2503 0.0275  0.0001  -0.0195 887  ILE B CD1 
15461 N N   . THR B 890  ? 0.1799 0.1911 0.2260 0.0309  -0.0024 -0.0158 888  THR B N   
15462 C CA  . THR B 890  ? 0.1957 0.2109 0.2454 0.0336  -0.0012 -0.0153 888  THR B CA  
15463 C C   . THR B 890  ? 0.1928 0.2113 0.2468 0.0340  -0.0029 -0.0140 888  THR B C   
15464 O O   . THR B 890  ? 0.1882 0.2065 0.2426 0.0318  -0.0048 -0.0134 888  THR B O   
15465 C CB  . THR B 890  ? 0.2248 0.2451 0.2773 0.0332  0.0008  -0.0149 888  THR B CB  
15466 O OG1 . THR B 890  ? 0.2122 0.2351 0.2671 0.0304  -0.0001 -0.0139 888  THR B OG1 
15467 C CG2 . THR B 890  ? 0.2342 0.2519 0.2827 0.0330  0.0027  -0.0161 888  THR B CG2 
15468 N N   . SER B 891  ? 0.2190 0.2405 0.2761 0.0370  -0.0023 -0.0136 889  SER B N   
15469 C CA  A SER B 891  ? 0.2118 0.2378 0.2738 0.0376  -0.0038 -0.0121 889  SER B CA  
15470 C CA  B SER B 891  ? 0.2117 0.2376 0.2736 0.0375  -0.0038 -0.0121 889  SER B CA  
15471 C C   . SER B 891  ? 0.1812 0.2125 0.2471 0.0349  -0.0040 -0.0109 889  SER B C   
15472 O O   . SER B 891  ? 0.2051 0.2383 0.2734 0.0335  -0.0061 -0.0099 889  SER B O   
15473 C CB  A SER B 891  ? 0.2516 0.2808 0.3166 0.0415  -0.0026 -0.0119 889  SER B CB  
15474 C CB  B SER B 891  ? 0.2520 0.2808 0.3168 0.0415  -0.0029 -0.0119 889  SER B CB  
15475 O OG  A SER B 891  ? 0.2773 0.3010 0.3385 0.0442  -0.0028 -0.0129 889  SER B OG  
15476 O OG  B SER B 891  ? 0.2680 0.3010 0.3347 0.0425  -0.0001 -0.0120 889  SER B OG  
15477 N N   . GLU B 892  ? 0.1774 0.2111 0.2439 0.0340  -0.0019 -0.0110 890  GLU B N   
15478 C CA  . GLU B 892  ? 0.2093 0.2475 0.2792 0.0313  -0.0020 -0.0099 890  GLU B CA  
15479 C C   . GLU B 892  ? 0.1951 0.2297 0.2625 0.0281  -0.0040 -0.0100 890  GLU B C   
15480 O O   . GLU B 892  ? 0.2231 0.2602 0.2932 0.0261  -0.0056 -0.0090 890  GLU B O   
15481 C CB  . GLU B 892  ? 0.2607 0.3009 0.3306 0.0309  0.0007  -0.0100 890  GLU B CB  
15482 N N   . ALA B 893  ? 0.1877 0.2166 0.2499 0.0275  -0.0039 -0.0113 891  ALA B N   
15483 C CA  . ALA B 893  ? 0.1955 0.2211 0.2551 0.0248  -0.0055 -0.0115 891  ALA B CA  
15484 C C   . ALA B 893  ? 0.2074 0.2321 0.2674 0.0247  -0.0081 -0.0110 891  ALA B C   
15485 O O   . ALA B 893  ? 0.2114 0.2366 0.2721 0.0225  -0.0098 -0.0105 891  ALA B O   
15486 C CB  . ALA B 893  ? 0.2090 0.2292 0.2632 0.0245  -0.0049 -0.0129 891  ALA B CB  
15487 N N   . LYS B 894  ? 0.1934 0.2166 0.2528 0.0272  -0.0085 -0.0112 892  LYS B N   
15488 C CA  . LYS B 894  ? 0.1969 0.2192 0.2566 0.0274  -0.0110 -0.0106 892  LYS B CA  
15489 C C   . LYS B 894  ? 0.2111 0.2392 0.2761 0.0267  -0.0122 -0.0092 892  LYS B C   
15490 O O   . LYS B 894  ? 0.2058 0.2335 0.2708 0.0249  -0.0145 -0.0087 892  LYS B O   
15491 C CB  . LYS B 894  ? 0.2061 0.2260 0.2646 0.0305  -0.0110 -0.0109 892  LYS B CB  
15492 C CG  . LYS B 894  ? 0.2127 0.2317 0.2714 0.0310  -0.0136 -0.0101 892  LYS B CG  
15493 C CD  . LYS B 894  ? 0.2619 0.2779 0.3191 0.0343  -0.0135 -0.0103 892  LYS B CD  
15494 C CE  . LYS B 894  ? 0.3375 0.3546 0.3967 0.0355  -0.0159 -0.0091 892  LYS B CE  
15495 N NZ  . LYS B 894  ? 0.4087 0.4194 0.4631 0.0356  -0.0175 -0.0092 892  LYS B NZ  
15496 N N   . ASP B 895  ? 0.1914 0.2249 0.2610 0.0281  -0.0108 -0.0085 893  ASP B N   
15497 C CA  . ASP B 895  ? 0.2154 0.2550 0.2905 0.0272  -0.0121 -0.0069 893  ASP B CA  
15498 C C   . ASP B 895  ? 0.1942 0.2341 0.2693 0.0234  -0.0129 -0.0067 893  ASP B C   
15499 O O   . ASP B 895  ? 0.2151 0.2572 0.2925 0.0217  -0.0151 -0.0058 893  ASP B O   
15500 C CB  . ASP B 895  ? 0.2406 0.2863 0.3205 0.0293  -0.0100 -0.0062 893  ASP B CB  
15501 C CG  . ASP B 895  ? 0.2818 0.3277 0.3623 0.0334  -0.0095 -0.0063 893  ASP B CG  
15502 O OD1 . ASP B 895  ? 0.3112 0.3535 0.3896 0.0344  -0.0113 -0.0065 893  ASP B OD1 
15503 O OD2 . ASP B 895  ? 0.3474 0.3970 0.4303 0.0356  -0.0072 -0.0062 893  ASP B OD2 
15504 N N   . ASN B 896  ? 0.2008 0.2387 0.2735 0.0221  -0.0112 -0.0075 894  ASN B N   
15505 C CA  . ASN B 896  ? 0.1952 0.2328 0.2675 0.0188  -0.0118 -0.0073 894  ASN B CA  
15506 C C   . ASN B 896  ? 0.2351 0.2682 0.3039 0.0171  -0.0142 -0.0078 894  ASN B C   
15507 O O   . ASN B 896  ? 0.2166 0.2507 0.2866 0.0149  -0.0161 -0.0073 894  ASN B O   
15508 C CB  . ASN B 896  ? 0.2247 0.2604 0.2945 0.0184  -0.0094 -0.0081 894  ASN B CB  
15509 C CG  . ASN B 896  ? 0.3234 0.3581 0.3923 0.0153  -0.0098 -0.0080 894  ASN B CG  
15510 O OD1 . ASN B 896  ? 0.3647 0.3956 0.4307 0.0137  -0.0114 -0.0086 894  ASN B OD1 
15511 N ND2 . ASN B 896  ? 0.4000 0.4377 0.4712 0.0145  -0.0081 -0.0073 894  ASN B ND2 
15512 N N   . ILE B 897  ? 0.1860 0.2143 0.2504 0.0182  -0.0142 -0.0089 895  ILE B N   
15513 C CA  . ILE B 897  ? 0.1927 0.2168 0.2534 0.0169  -0.0162 -0.0094 895  ILE B CA  
15514 C C   . ILE B 897  ? 0.1894 0.2155 0.2523 0.0170  -0.0188 -0.0084 895  ILE B C   
15515 O O   . ILE B 897  ? 0.2000 0.2254 0.2622 0.0149  -0.0208 -0.0083 895  ILE B O   
15516 C CB  . ILE B 897  ? 0.2004 0.2195 0.2563 0.0181  -0.0156 -0.0105 895  ILE B CB  
15517 C CG1 . ILE B 897  ? 0.2017 0.2189 0.2551 0.0177  -0.0134 -0.0114 895  ILE B CG1 
15518 C CG2 . ILE B 897  ? 0.2036 0.2190 0.2559 0.0169  -0.0177 -0.0107 895  ILE B CG2 
15519 C CD1 . ILE B 897  ? 0.1830 0.1969 0.2332 0.0194  -0.0122 -0.0123 895  ILE B CD1 
15520 N N   . GLU B 898  ? 0.2022 0.2308 0.2678 0.0195  -0.0188 -0.0077 896  GLU B N   
15521 C CA  . GLU B 898  ? 0.1806 0.2113 0.2485 0.0199  -0.0213 -0.0067 896  GLU B CA  
15522 C C   . GLU B 898  ? 0.2105 0.2464 0.2831 0.0179  -0.0225 -0.0055 896  GLU B C   
15523 O O   . GLU B 898  ? 0.2184 0.2549 0.2914 0.0167  -0.0252 -0.0049 896  GLU B O   
15524 C CB  . GLU B 898  ? 0.2567 0.2886 0.3263 0.0234  -0.0210 -0.0062 896  GLU B CB  
15525 C CG  . GLU B 898  ? 0.2734 0.2990 0.3376 0.0247  -0.0208 -0.0072 896  GLU B CG  
15526 C CD  . GLU B 898  ? 0.3885 0.4140 0.4535 0.0283  -0.0204 -0.0069 896  GLU B CD  
15527 O OE1 . GLU B 898  ? 0.3792 0.4097 0.4489 0.0302  -0.0196 -0.0062 896  GLU B OE1 
15528 O OE2 . GLU B 898  ? 0.4308 0.4509 0.4914 0.0292  -0.0208 -0.0074 896  GLU B OE2 
15529 N N   . LYS B 899  ? 0.1829 0.2226 0.2587 0.0173  -0.0208 -0.0052 897  LYS B N   
15530 C CA  . LYS B 899  ? 0.2064 0.2508 0.2865 0.0149  -0.0220 -0.0040 897  LYS B CA  
15531 C C   . LYS B 899  ? 0.1921 0.2327 0.2689 0.0116  -0.0238 -0.0046 897  LYS B C   
15532 O O   . LYS B 899  ? 0.2074 0.2500 0.2860 0.0097  -0.0263 -0.0038 897  LYS B O   
15533 C CB  . LYS B 899  ? 0.2351 0.2834 0.3185 0.0147  -0.0195 -0.0036 897  LYS B CB  
15534 C CG  . LYS B 899  ? 0.2633 0.3161 0.3508 0.0117  -0.0207 -0.0023 897  LYS B CG  
15535 C CD  . LYS B 899  ? 0.3273 0.3857 0.4194 0.0117  -0.0184 -0.0012 897  LYS B CD  
15536 C CE  . LYS B 899  ? 0.3435 0.3984 0.4324 0.0105  -0.0163 -0.0021 897  LYS B CE  
15537 N NZ  . LYS B 899  ? 0.3799 0.4402 0.4731 0.0091  -0.0148 -0.0007 897  LYS B NZ  
15538 N N   . HIS B 900  ? 0.1796 0.2149 0.2514 0.0110  -0.0227 -0.0060 898  HIS B N   
15539 C CA  . HIS B 900  ? 0.1925 0.2238 0.2606 0.0084  -0.0242 -0.0067 898  HIS B CA  
15540 C C   . HIS B 900  ? 0.2099 0.2389 0.2755 0.0083  -0.0268 -0.0069 898  HIS B C   
15541 O O   . HIS B 900  ? 0.2088 0.2373 0.2738 0.0061  -0.0291 -0.0068 898  HIS B O   
15542 C CB  . HIS B 900  ? 0.1839 0.2104 0.2474 0.0083  -0.0222 -0.0081 898  HIS B CB  
15543 C CG  . HIS B 900  ? 0.1964 0.2183 0.2554 0.0063  -0.0236 -0.0091 898  HIS B CG  
15544 N ND1 . HIS B 900  ? 0.2458 0.2673 0.3049 0.0038  -0.0246 -0.0091 898  HIS B ND1 
15545 C CD2 . HIS B 900  ? 0.2012 0.2186 0.2552 0.0066  -0.0241 -0.0101 898  HIS B CD2 
15546 C CE1 . HIS B 900  ? 0.2303 0.2472 0.2846 0.0028  -0.0256 -0.0102 898  HIS B CE1 
15547 N NE2 . HIS B 900  ? 0.2258 0.2404 0.2771 0.0045  -0.0253 -0.0108 898  HIS B NE2 
15548 N N   . ILE B 901  ? 0.2016 0.2287 0.2652 0.0107  -0.0265 -0.0071 899  ILE B N   
15549 C CA  . ILE B 901  ? 0.1799 0.2046 0.2407 0.0107  -0.0289 -0.0071 899  ILE B CA  
15550 C C   . ILE B 901  ? 0.2156 0.2446 0.2805 0.0102  -0.0315 -0.0057 899  ILE B C   
15551 O O   . ILE B 901  ? 0.2419 0.2698 0.3051 0.0084  -0.0341 -0.0057 899  ILE B O   
15552 C CB  . ILE B 901  ? 0.1738 0.1958 0.2322 0.0134  -0.0281 -0.0074 899  ILE B CB  
15553 C CG1 . ILE B 901  ? 0.1841 0.2016 0.2381 0.0133  -0.0259 -0.0087 899  ILE B CG1 
15554 C CG2 . ILE B 901  ? 0.2309 0.2509 0.2870 0.0136  -0.0306 -0.0069 899  ILE B CG2 
15555 C CD1 . ILE B 901  ? 0.2274 0.2425 0.2793 0.0157  -0.0248 -0.0090 899  ILE B CD1 
15556 N N   . GLU B 902  ? 0.2119 0.2464 0.2824 0.0118  -0.0309 -0.0046 900  GLU B N   
15557 C CA  . GLU B 902  ? 0.2308 0.2705 0.3059 0.0115  -0.0334 -0.0031 900  GLU B CA  
15558 C C   . GLU B 902  ? 0.2256 0.2674 0.3025 0.0080  -0.0348 -0.0028 900  GLU B C   
15559 O O   . GLU B 902  ? 0.2562 0.3000 0.3346 0.0066  -0.0377 -0.0019 900  GLU B O   
15560 C CB  . GLU B 902  ? 0.2397 0.2851 0.3205 0.0143  -0.0321 -0.0019 900  GLU B CB  
15561 C CG  . GLU B 902  ? 0.3442 0.3874 0.4233 0.0179  -0.0315 -0.0020 900  GLU B CG  
15562 C CD  . GLU B 902  ? 0.4301 0.4696 0.5054 0.0180  -0.0342 -0.0019 900  GLU B CD  
15563 O OE1 . GLU B 902  ? 0.4117 0.4542 0.4893 0.0170  -0.0370 -0.0008 900  GLU B OE1 
15564 O OE2 . GLU B 902  ? 0.4149 0.4486 0.4850 0.0188  -0.0336 -0.0029 900  GLU B OE2 
15565 N N   . ARG B 903  ? 0.2245 0.2654 0.3011 0.0064  -0.0329 -0.0034 901  ARG B N   
15566 C CA  . ARG B 903  ? 0.2513 0.2930 0.3288 0.0029  -0.0344 -0.0032 901  ARG B CA  
15567 C C   . ARG B 903  ? 0.2991 0.3353 0.3711 0.0009  -0.0367 -0.0043 901  ARG B C   
15568 O O   . ARG B 903  ? 0.2918 0.3291 0.3646 -0.0015 -0.0395 -0.0038 901  ARG B O   
15569 C CB  . ARG B 903  ? 0.2774 0.3186 0.3552 0.0018  -0.0318 -0.0036 901  ARG B CB  
15570 C CG  . ARG B 903  ? 0.3940 0.4365 0.4735 -0.0018 -0.0332 -0.0030 901  ARG B CG  
15571 C CD  . ARG B 903  ? 0.4426 0.4842 0.5221 -0.0028 -0.0307 -0.0033 901  ARG B CD  
15572 N NE  . ARG B 903  ? 0.5092 0.5438 0.5827 -0.0041 -0.0307 -0.0049 901  ARG B NE  
15573 C CZ  . ARG B 903  ? 0.4651 0.4972 0.5371 -0.0072 -0.0324 -0.0052 901  ARG B CZ  
15574 N NH1 . ARG B 903  ? 0.5280 0.5638 0.6038 -0.0097 -0.0345 -0.0039 901  ARG B NH1 
15575 N NH2 . ARG B 903  ? 0.5831 0.6088 0.6494 -0.0078 -0.0321 -0.0068 901  ARG B NH2 
15576 N N   . MET B 904  ? 0.2519 0.2824 0.3183 0.0019  -0.0356 -0.0057 902  MET B N   
15577 C CA  . MET B 904  ? 0.2497 0.2750 0.3104 0.0004  -0.0375 -0.0068 902  MET B CA  
15578 C C   . MET B 904  ? 0.2633 0.2898 0.3240 0.0007  -0.0404 -0.0060 902  MET B C   
15579 O O   . MET B 904  ? 0.2816 0.3067 0.3403 -0.0015 -0.0431 -0.0063 902  MET B O   
15580 C CB  . MET B 904  ? 0.2476 0.2676 0.3028 0.0017  -0.0355 -0.0083 902  MET B CB  
15581 C CG  . MET B 904  ? 0.2423 0.2610 0.2971 0.0014  -0.0327 -0.0090 902  MET B CG  
15582 S SD  . MET B 904  ? 0.3781 0.3943 0.4311 -0.0019 -0.0338 -0.0098 902  MET B SD  
15583 C CE  . MET B 904  ? 0.3923 0.4142 0.4521 -0.0030 -0.0331 -0.0083 902  MET B CE  
15584 N N   . ARG B 905  ? 0.2555 0.2843 0.3183 0.0034  -0.0401 -0.0051 903  ARG B N   
15585 C CA  . ARG B 905  ? 0.3021 0.3321 0.3651 0.0040  -0.0430 -0.0042 903  ARG B CA  
15586 C C   . ARG B 905  ? 0.3017 0.3370 0.3695 0.0021  -0.0456 -0.0029 903  ARG B C   
15587 O O   . ARG B 905  ? 0.2912 0.3259 0.3573 0.0006  -0.0487 -0.0027 903  ARG B O   
15588 C CB  . ARG B 905  ? 0.3009 0.3323 0.3656 0.0076  -0.0419 -0.0034 903  ARG B CB  
15589 C CG  . ARG B 905  ? 0.4200 0.4500 0.4825 0.0087  -0.0444 -0.0027 903  ARG B CG  
15590 C CD  . ARG B 905  ? 0.4068 0.4389 0.4720 0.0123  -0.0436 -0.0016 903  ARG B CD  
15591 N NE  . ARG B 905  ? 0.3945 0.4236 0.4579 0.0142  -0.0404 -0.0026 903  ARG B NE  
15592 C CZ  . ARG B 905  ? 0.3789 0.4022 0.4367 0.0149  -0.0397 -0.0034 903  ARG B CZ  
15593 N NH1 . ARG B 905  ? 0.3976 0.4174 0.4508 0.0139  -0.0418 -0.0034 903  ARG B NH1 
15594 N NH2 . ARG B 905  ? 0.4156 0.4369 0.4724 0.0166  -0.0369 -0.0041 903  ARG B NH2 
15595 N N   . GLY B 906  ? 0.2808 0.3213 0.3545 0.0019  -0.0444 -0.0020 904  GLY B N   
15596 C CA  . GLY B 906  ? 0.3117 0.3580 0.3906 -0.0001 -0.0468 -0.0006 904  GLY B CA  
15597 C C   . GLY B 906  ? 0.3284 0.3721 0.4048 -0.0041 -0.0488 -0.0013 904  GLY B C   
15598 O O   . GLY B 906  ? 0.3959 0.4426 0.4746 -0.0062 -0.0519 -0.0004 904  GLY B O   
15599 N N   . LEU B 907  ? 0.3429 0.3809 0.4145 -0.0051 -0.0471 -0.0030 905  LEU B N   
15600 C CA  . LEU B 907  ? 0.3517 0.3858 0.4197 -0.0086 -0.0489 -0.0041 905  LEU B CA  
15601 C C   . LEU B 907  ? 0.3280 0.3572 0.3898 -0.0090 -0.0513 -0.0051 905  LEU B C   
15602 O O   . LEU B 907  ? 0.3408 0.3663 0.3990 -0.0117 -0.0530 -0.0061 905  LEU B O   
15603 C CB  . LEU B 907  ? 0.3859 0.4157 0.4511 -0.0092 -0.0461 -0.0054 905  LEU B CB  
15604 C CG  . LEU B 907  ? 0.4506 0.4846 0.5212 -0.0097 -0.0441 -0.0044 905  LEU B CG  
15605 C CD1 . LEU B 907  ? 0.5014 0.5305 0.5685 -0.0103 -0.0417 -0.0058 905  LEU B CD1 
15606 C CD2 . LEU B 907  ? 0.4625 0.5012 0.5378 -0.0128 -0.0466 -0.0030 905  LEU B CD2 
15607 N N   . GLY B 908  ? 0.3102 0.3393 0.3707 -0.0065 -0.0516 -0.0048 906  GLY B N   
15608 C CA  . GLY B 908  ? 0.3372 0.3621 0.3919 -0.0069 -0.0538 -0.0055 906  GLY B CA  
15609 C C   . GLY B 908  ? 0.3696 0.3879 0.4174 -0.0060 -0.0519 -0.0073 906  GLY B C   
15610 O O   . GLY B 908  ? 0.3289 0.3434 0.3712 -0.0063 -0.0535 -0.0079 906  GLY B O   
15611 N N   . ARG B 909  ? 0.2803 0.2972 0.3280 -0.0049 -0.0485 -0.0080 907  ARG B N   
15612 C CA  . ARG B 909  ? 0.2683 0.2796 0.3099 -0.0040 -0.0466 -0.0095 907  ARG B CA  
15613 C C   . ARG B 909  ? 0.2940 0.3047 0.3339 -0.0016 -0.0464 -0.0090 907  ARG B C   
15614 O O   . ARG B 909  ? 0.3344 0.3488 0.3784 0.0003  -0.0463 -0.0076 907  ARG B O   
15615 C CB  . ARG B 909  ? 0.2771 0.2879 0.3198 -0.0033 -0.0431 -0.0101 907  ARG B CB  
15616 C CG  . ARG B 909  ? 0.3253 0.3364 0.3698 -0.0055 -0.0429 -0.0105 907  ARG B CG  
15617 C CD  . ARG B 909  ? 0.4545 0.4604 0.4935 -0.0076 -0.0441 -0.0120 907  ARG B CD  
15618 N NE  . ARG B 909  ? 0.5330 0.5386 0.5734 -0.0097 -0.0440 -0.0123 907  ARG B NE  
15619 C CZ  . ARG B 909  ? 0.5584 0.5650 0.6005 -0.0124 -0.0466 -0.0119 907  ARG B CZ  
15620 N NH1 . ARG B 909  ? 0.5403 0.5488 0.5828 -0.0133 -0.0497 -0.0113 907  ARG B NH1 
15621 N NH2 . ARG B 909  ? 0.5964 0.6022 0.6396 -0.0143 -0.0462 -0.0121 907  ARG B NH2 
15622 N N   . LYS B 910  ? 0.2805 0.2863 0.3140 -0.0016 -0.0463 -0.0100 908  LYS B N   
15623 C CA  . LYS B 910  ? 0.2944 0.2989 0.3255 0.0004  -0.0460 -0.0095 908  LYS B CA  
15624 C C   . LYS B 910  ? 0.3034 0.3079 0.3359 0.0025  -0.0427 -0.0096 908  LYS B C   
15625 O O   . LYS B 910  ? 0.2707 0.2732 0.3016 0.0022  -0.0404 -0.0108 908  LYS B O   
15626 C CB  . LYS B 910  ? 0.3295 0.3291 0.3534 -0.0003 -0.0464 -0.0106 908  LYS B CB  
15627 C CG  . LYS B 910  ? 0.3736 0.3718 0.3948 0.0013  -0.0466 -0.0098 908  LYS B CG  
15628 C CD  . LYS B 910  ? 0.4927 0.4864 0.5067 0.0006  -0.0465 -0.0108 908  LYS B CD  
15629 C CE  . LYS B 910  ? 0.6008 0.5932 0.6120 0.0017  -0.0475 -0.0096 908  LYS B CE  
15630 N NZ  . LYS B 910  ? 0.5771 0.5655 0.5816 0.0013  -0.0465 -0.0104 908  LYS B NZ  
15631 N N   . VAL B 911  ? 0.2713 0.2780 0.3068 0.0046  -0.0426 -0.0083 909  VAL B N   
15632 C CA  . VAL B 911  ? 0.2407 0.2474 0.2775 0.0066  -0.0397 -0.0083 909  VAL B CA  
15633 C C   . VAL B 911  ? 0.2526 0.2569 0.2866 0.0083  -0.0400 -0.0077 909  VAL B C   
15634 O O   . VAL B 911  ? 0.2979 0.3034 0.3329 0.0091  -0.0422 -0.0064 909  VAL B O   
15635 C CB  . VAL B 911  ? 0.2524 0.2641 0.2960 0.0078  -0.0391 -0.0074 909  VAL B CB  
15636 C CG1 . VAL B 911  ? 0.2558 0.2671 0.3002 0.0101  -0.0364 -0.0074 909  VAL B CG1 
15637 C CG2 . VAL B 911  ? 0.2599 0.2740 0.3063 0.0058  -0.0389 -0.0078 909  VAL B CG2 
15638 N N   . GLU B 912  ? 0.2362 0.2371 0.2667 0.0088  -0.0378 -0.0084 910  GLU B N   
15639 C CA  . GLU B 912  ? 0.2491 0.2471 0.2766 0.0102  -0.0379 -0.0078 910  GLU B CA  
15640 C C   . GLU B 912  ? 0.2705 0.2677 0.2987 0.0117  -0.0352 -0.0082 910  GLU B C   
15641 O O   . GLU B 912  ? 0.2587 0.2555 0.2865 0.0110  -0.0330 -0.0093 910  GLU B O   
15642 C CB  . GLU B 912  ? 0.3022 0.2963 0.3234 0.0088  -0.0383 -0.0084 910  GLU B CB  
15643 C CG  . GLU B 912  ? 0.3464 0.3407 0.3658 0.0072  -0.0411 -0.0082 910  GLU B CG  
15644 C CD  . GLU B 912  ? 0.5108 0.5013 0.5237 0.0060  -0.0411 -0.0088 910  GLU B CD  
15645 O OE1 . GLU B 912  ? 0.5512 0.5393 0.5609 0.0066  -0.0411 -0.0081 910  GLU B OE1 
15646 O OE2 . GLU B 912  ? 0.5785 0.5685 0.5894 0.0044  -0.0412 -0.0100 910  GLU B OE2 
15647 N N   . GLN B 913  ? 0.2499 0.2465 0.2788 0.0137  -0.0353 -0.0072 911  GLN B N   
15648 C CA  . GLN B 913  ? 0.2503 0.2454 0.2793 0.0152  -0.0330 -0.0076 911  GLN B CA  
15649 C C   . GLN B 913  ? 0.3287 0.3195 0.3536 0.0160  -0.0334 -0.0070 911  GLN B C   
15650 O O   . GLN B 913  ? 0.3326 0.3225 0.3565 0.0165  -0.0356 -0.0058 911  GLN B O   
15651 C CB  . GLN B 913  ? 0.2810 0.2796 0.3155 0.0174  -0.0325 -0.0071 911  GLN B CB  
15652 C CG  . GLN B 913  ? 0.2850 0.2880 0.3238 0.0166  -0.0318 -0.0075 911  GLN B CG  
15653 C CD  . GLN B 913  ? 0.3104 0.3173 0.3545 0.0188  -0.0309 -0.0070 911  GLN B CD  
15654 O OE1 . GLN B 913  ? 0.3992 0.4081 0.4459 0.0205  -0.0324 -0.0058 911  GLN B OE1 
15655 N NE2 . GLN B 913  ? 0.2710 0.2790 0.3166 0.0190  -0.0284 -0.0078 911  GLN B NE2 
15656 N N   . ILE B 914  ? 0.2973 0.2853 0.3198 0.0159  -0.0313 -0.0077 912  ILE B N   
15657 C CA  . ILE B 914  ? 0.4274 0.4112 0.4468 0.0169  -0.0313 -0.0071 912  ILE B CA  
15658 C C   . ILE B 914  ? 0.5376 0.5220 0.5602 0.0197  -0.0318 -0.0063 912  ILE B C   
15659 O O   . ILE B 914  ? 0.5220 0.5104 0.5495 0.0210  -0.0315 -0.0064 912  ILE B O   
15660 C CB  . ILE B 914  ? 0.3084 0.2900 0.3256 0.0162  -0.0288 -0.0082 912  ILE B CB  
15661 N N   . GLY B 915  ? 0.6521 0.6322 0.6718 0.0207  -0.0325 -0.0055 913  GLY B N   
15662 C CA  . GLY B 915  ? 0.5951 0.5748 0.6170 0.0238  -0.0327 -0.0049 913  GLY B CA  
15663 C C   . GLY B 915  ? 0.5981 0.5757 0.6197 0.0248  -0.0303 -0.0060 913  GLY B C   
15664 O O   . GLY B 915  ? 0.6025 0.5780 0.6212 0.0229  -0.0289 -0.0069 913  GLY B O   
15665 N N   . LEU B 916  ? 0.5952 0.5735 0.6197 0.0278  -0.0300 -0.0059 914  LEU B N   
15666 C CA  . LEU B 916  ? 0.4957 0.4718 0.5197 0.0290  -0.0278 -0.0070 914  LEU B CA  
15667 C C   . LEU B 916  ? 0.5588 0.5303 0.5812 0.0318  -0.0285 -0.0064 914  LEU B C   
15668 O O   . LEU B 916  ? 0.5270 0.4998 0.5517 0.0341  -0.0301 -0.0053 914  LEU B O   
15669 C CB  . LEU B 916  ? 0.5261 0.5076 0.5552 0.0302  -0.0261 -0.0079 914  LEU B CB  
15670 N N   . ALA B 917  ? 0.5445 0.5106 0.5628 0.0315  -0.0275 -0.0072 915  ALA B N   
15671 C CA  . ALA B 917  ? 0.5755 0.5360 0.5915 0.0339  -0.0282 -0.0068 915  ALA B CA  
15672 C C   . ALA B 917  ? 0.5648 0.5274 0.5846 0.0378  -0.0273 -0.0072 915  ALA B C   
15673 O O   . ALA B 917  ? 0.5184 0.4859 0.5418 0.0383  -0.0255 -0.0082 915  ALA B O   
15674 C CB  . ALA B 917  ? 0.5486 0.5029 0.5593 0.0323  -0.0272 -0.0076 915  ALA B CB  
15675 N N   . SER B 918  ? 0.5944 0.5531 0.6132 0.0408  -0.0284 -0.0065 916  SER B N   
15676 C CA  . SER B 918  ? 0.6323 0.5928 0.6546 0.0451  -0.0275 -0.0069 916  SER B CA  
15677 C C   . SER B 918  ? 0.5751 0.5345 0.5966 0.0457  -0.0249 -0.0088 916  SER B C   
15678 O O   . SER B 918  ? 0.5578 0.5216 0.5833 0.0482  -0.0233 -0.0095 916  SER B O   
15679 C CB  . SER B 918  ? 0.5480 0.5032 0.5684 0.0483  -0.0293 -0.0058 916  SER B CB  
15680 N N   . GLU B 919  ? 0.5427 0.4965 0.5591 0.0432  -0.0243 -0.0097 917  GLU B N   
15681 C CA  . GLU B 919  ? 0.5296 0.4818 0.5445 0.0433  -0.0220 -0.0116 917  GLU B CA  
15682 C C   . GLU B 919  ? 0.5020 0.4614 0.5209 0.0423  -0.0200 -0.0125 917  GLU B C   
15683 O O   . GLU B 919  ? 0.4963 0.4556 0.5149 0.0432  -0.0180 -0.0140 917  GLU B O   
15684 C CB  . GLU B 919  ? 0.5035 0.4491 0.5124 0.0402  -0.0221 -0.0122 917  GLU B CB  
15685 N N   . THR B 920  ? 0.4607 0.4259 0.4830 0.0405  -0.0206 -0.0116 918  THR B N   
15686 C CA  . THR B 920  ? 0.4390 0.4106 0.4650 0.0395  -0.0189 -0.0122 918  THR B CA  
15687 C C   . THR B 920  ? 0.4417 0.4186 0.4728 0.0428  -0.0178 -0.0123 918  THR B C   
15688 O O   . THR B 920  ? 0.3940 0.3752 0.4276 0.0424  -0.0159 -0.0130 918  THR B O   
15689 C CB  . THR B 920  ? 0.4405 0.4159 0.4680 0.0363  -0.0200 -0.0114 918  THR B CB  
15690 O OG1 . THR B 920  ? 0.4127 0.3903 0.4427 0.0374  -0.0221 -0.0099 918  THR B OG1 
15691 C CG2 . THR B 920  ? 0.3771 0.3481 0.3996 0.0329  -0.0206 -0.0115 918  THR B CG2 
15692 N N   . GLY B 921  ? 0.4491 0.4257 0.4818 0.0462  -0.0188 -0.0115 919  GLY B N   
15693 C CA  . GLY B 921  ? 0.4349 0.4175 0.4731 0.0495  -0.0178 -0.0113 919  GLY B CA  
15694 C C   . GLY B 921  ? 0.4027 0.3855 0.4408 0.0516  -0.0150 -0.0129 919  GLY B C   
15695 O O   . GLY B 921  ? 0.4523 0.4413 0.4952 0.0535  -0.0136 -0.0128 919  GLY B O   
15696 N N   . VAL B 922  ? 0.3248 0.3008 0.3573 0.0510  -0.0142 -0.0143 920  VAL B N   
15697 C CA  . VAL B 922  ? 0.3066 0.2821 0.3382 0.0527  -0.0116 -0.0160 920  VAL B CA  
15698 C C   . VAL B 922  ? 0.3050 0.2843 0.3373 0.0497  -0.0099 -0.0167 920  VAL B C   
15699 O O   . VAL B 922  ? 0.2685 0.2490 0.3008 0.0509  -0.0076 -0.0179 920  VAL B O   
15700 C CB  . VAL B 922  ? 0.3208 0.2872 0.3459 0.0535  -0.0116 -0.0173 920  VAL B CB  
15701 C CG1 . VAL B 922  ? 0.3601 0.3226 0.3846 0.0573  -0.0130 -0.0167 920  VAL B CG1 
15702 C CG2 . VAL B 922  ? 0.3128 0.2742 0.3333 0.0492  -0.0129 -0.0173 920  VAL B CG2 
15703 N N   . GLY B 923  ? 0.2531 0.2344 0.2860 0.0459  -0.0109 -0.0159 921  GLY B N   
15704 C CA  . GLY B 923  ? 0.2237 0.2083 0.2573 0.0432  -0.0095 -0.0164 921  GLY B CA  
15705 C C   . GLY B 923  ? 0.2726 0.2639 0.3112 0.0416  -0.0102 -0.0151 921  GLY B C   
15706 O O   . GLY B 923  ? 0.2848 0.2787 0.3265 0.0429  -0.0116 -0.0139 921  GLY B O   
15707 N N   . THR B 924  ? 0.2061 0.1999 0.2450 0.0387  -0.0095 -0.0153 922  THR B N   
15708 C CA  . THR B 924  ? 0.2091 0.2088 0.2524 0.0369  -0.0101 -0.0142 922  THR B CA  
15709 C C   . THR B 924  ? 0.2256 0.2229 0.2662 0.0335  -0.0116 -0.0140 922  THR B C   
15710 O O   . THR B 924  ? 0.2323 0.2283 0.2705 0.0313  -0.0107 -0.0148 922  THR B O   
15711 C CB  . THR B 924  ? 0.1977 0.2024 0.2438 0.0365  -0.0079 -0.0144 922  THR B CB  
15712 O OG1 . THR B 924  ? 0.2291 0.2307 0.2714 0.0354  -0.0065 -0.0157 922  THR B OG1 
15713 C CG2 . THR B 924  ? 0.2304 0.2389 0.2802 0.0400  -0.0065 -0.0143 922  THR B CG2 
15714 N N   . PHE B 925  ? 0.2179 0.2148 0.2589 0.0331  -0.0138 -0.0130 923  PHE B N   
15715 C CA  . PHE B 925  ? 0.2065 0.2010 0.2446 0.0301  -0.0153 -0.0128 923  PHE B CA  
15716 C C   . PHE B 925  ? 0.2170 0.2158 0.2584 0.0288  -0.0168 -0.0117 923  PHE B C   
15717 O O   . PHE B 925  ? 0.2243 0.2264 0.2695 0.0304  -0.0177 -0.0108 923  PHE B O   
15718 C CB  . PHE B 925  ? 0.2144 0.2032 0.2484 0.0305  -0.0168 -0.0125 923  PHE B CB  
15719 C CG  . PHE B 925  ? 0.2115 0.1950 0.2412 0.0309  -0.0157 -0.0136 923  PHE B CG  
15720 C CD1 . PHE B 925  ? 0.2371 0.2190 0.2669 0.0339  -0.0149 -0.0141 923  PHE B CD1 
15721 C CD2 . PHE B 925  ? 0.2080 0.1882 0.2336 0.0282  -0.0156 -0.0141 923  PHE B CD2 
15722 C CE1 . PHE B 925  ? 0.2445 0.2210 0.2699 0.0341  -0.0140 -0.0152 923  PHE B CE1 
15723 C CE2 . PHE B 925  ? 0.2275 0.2030 0.2492 0.0282  -0.0148 -0.0151 923  PHE B CE2 
15724 C CZ  . PHE B 925  ? 0.2348 0.2081 0.2562 0.0311  -0.0141 -0.0157 923  PHE B CZ  
15725 N N   . VAL B 926  ? 0.2046 0.2030 0.2443 0.0260  -0.0171 -0.0119 924  VAL B N   
15726 C CA  . VAL B 926  ? 0.1867 0.1875 0.2280 0.0243  -0.0189 -0.0111 924  VAL B CA  
15727 C C   . VAL B 926  ? 0.1915 0.1879 0.2279 0.0224  -0.0200 -0.0113 924  VAL B C   
15728 O O   . VAL B 926  ? 0.2029 0.1969 0.2363 0.0211  -0.0189 -0.0121 924  VAL B O   
15729 C CB  . VAL B 926  ? 0.1847 0.1894 0.2286 0.0226  -0.0180 -0.0113 924  VAL B CB  
15730 C CG1 . VAL B 926  ? 0.2132 0.2193 0.2577 0.0206  -0.0200 -0.0108 924  VAL B CG1 
15731 C CG2 . VAL B 926  ? 0.2201 0.2295 0.2689 0.0244  -0.0167 -0.0110 924  VAL B CG2 
15732 N N   . PRO B 927  ? 0.2286 0.2242 0.2643 0.0221  -0.0223 -0.0104 925  PRO B N   
15733 C CA  . PRO B 927  ? 0.2378 0.2295 0.2687 0.0203  -0.0232 -0.0104 925  PRO B CA  
15734 C C   . PRO B 927  ? 0.2466 0.2396 0.2768 0.0178  -0.0231 -0.0109 925  PRO B C   
15735 O O   . PRO B 927  ? 0.2401 0.2369 0.2737 0.0174  -0.0233 -0.0109 925  PRO B O   
15736 C CB  . PRO B 927  ? 0.2889 0.2798 0.3195 0.0211  -0.0256 -0.0092 925  PRO B CB  
15737 C CG  . PRO B 927  ? 0.2416 0.2376 0.2775 0.0221  -0.0264 -0.0085 925  PRO B CG  
15738 C CD  . PRO B 927  ? 0.2452 0.2438 0.2844 0.0234  -0.0241 -0.0092 925  PRO B CD  
15739 N N   . PRO B 928  ? 0.2166 0.2067 0.2426 0.0162  -0.0229 -0.0114 926  PRO B N   
15740 C CA  . PRO B 928  ? 0.2132 0.2040 0.2380 0.0141  -0.0230 -0.0118 926  PRO B CA  
15741 C C   . PRO B 928  ? 0.2275 0.2203 0.2539 0.0136  -0.0252 -0.0112 926  PRO B C   
15742 O O   . PRO B 928  ? 0.2455 0.2375 0.2713 0.0141  -0.0270 -0.0102 926  PRO B O   
15743 C CB  . PRO B 928  ? 0.2260 0.2132 0.2457 0.0129  -0.0230 -0.0119 926  PRO B CB  
15744 C CG  . PRO B 928  ? 0.2973 0.2823 0.3160 0.0138  -0.0219 -0.0120 926  PRO B CG  
15745 C CD  . PRO B 928  ? 0.2368 0.2227 0.2587 0.0161  -0.0224 -0.0115 926  PRO B CD  
15746 N N   . THR B 929  ? 0.2109 0.2062 0.2393 0.0126  -0.0250 -0.0116 927  THR B N   
15747 C CA  . THR B 929  ? 0.1848 0.1824 0.2154 0.0119  -0.0270 -0.0111 927  THR B CA  
15748 C C   . THR B 929  ? 0.2168 0.2136 0.2450 0.0099  -0.0271 -0.0120 927  THR B C   
15749 O O   . THR B 929  ? 0.2219 0.2184 0.2496 0.0093  -0.0254 -0.0129 927  THR B O   
15750 C CB  . THR B 929  ? 0.2213 0.2231 0.2574 0.0127  -0.0265 -0.0108 927  THR B CB  
15751 O OG1 . THR B 929  ? 0.2175 0.2199 0.2555 0.0151  -0.0261 -0.0101 927  THR B OG1 
15752 C CG2 . THR B 929  ? 0.2190 0.2237 0.2578 0.0117  -0.0287 -0.0101 927  THR B CG2 
15753 N N   . ILE B 930  ? 0.2199 0.2162 0.2464 0.0089  -0.0293 -0.0117 928  ILE B N   
15754 C CA  . ILE B 930  ? 0.2245 0.2196 0.2484 0.0070  -0.0298 -0.0126 928  ILE B CA  
15755 C C   . ILE B 930  ? 0.2318 0.2292 0.2584 0.0061  -0.0320 -0.0122 928  ILE B C   
15756 O O   . ILE B 930  ? 0.2378 0.2362 0.2654 0.0064  -0.0341 -0.0112 928  ILE B O   
15757 C CB  . ILE B 930  ? 0.2166 0.2085 0.2350 0.0064  -0.0305 -0.0128 928  ILE B CB  
15758 C CG1 . ILE B 930  ? 0.2364 0.2263 0.2522 0.0070  -0.0284 -0.0131 928  ILE B CG1 
15759 C CG2 . ILE B 930  ? 0.2341 0.2247 0.2495 0.0048  -0.0310 -0.0139 928  ILE B CG2 
15760 C CD1 . ILE B 930  ? 0.3048 0.2920 0.3155 0.0065  -0.0290 -0.0129 928  ILE B CD1 
15761 N N   . ILE B 931  ? 0.2337 0.2317 0.2614 0.0049  -0.0316 -0.0130 929  ILE B N   
15762 C CA  . ILE B 931  ? 0.2325 0.2327 0.2629 0.0035  -0.0335 -0.0127 929  ILE B CA  
15763 C C   . ILE B 931  ? 0.2285 0.2257 0.2548 0.0017  -0.0342 -0.0139 929  ILE B C   
15764 O O   . ILE B 931  ? 0.2253 0.2207 0.2499 0.0016  -0.0323 -0.0150 929  ILE B O   
15765 C CB  . ILE B 931  ? 0.2060 0.2096 0.2417 0.0037  -0.0324 -0.0122 929  ILE B CB  
15766 C CG1 . ILE B 931  ? 0.2272 0.2334 0.2664 0.0058  -0.0314 -0.0112 929  ILE B CG1 
15767 C CG2 . ILE B 931  ? 0.2136 0.2197 0.2523 0.0019  -0.0346 -0.0117 929  ILE B CG2 
15768 C CD1 . ILE B 931  ? 0.2232 0.2336 0.2679 0.0061  -0.0304 -0.0106 929  ILE B CD1 
15769 N N   . GLU B 932  ? 0.2336 0.2302 0.2583 0.0005  -0.0369 -0.0138 930  GLU B N   
15770 C CA  . GLU B 932  ? 0.2360 0.2295 0.2565 -0.0011 -0.0377 -0.0152 930  GLU B CA  
15771 C C   . GLU B 932  ? 0.2374 0.2320 0.2610 -0.0028 -0.0385 -0.0153 930  GLU B C   
15772 O O   . GLU B 932  ? 0.2614 0.2593 0.2890 -0.0036 -0.0404 -0.0142 930  GLU B O   
15773 C CB  . GLU B 932  ? 0.3180 0.3098 0.3345 -0.0018 -0.0402 -0.0152 930  GLU B CB  
15774 C CG  . GLU B 932  ? 0.3429 0.3332 0.3561 -0.0004 -0.0395 -0.0149 930  GLU B CG  
15775 C CD  . GLU B 932  ? 0.5047 0.4913 0.5112 -0.0011 -0.0399 -0.0160 930  GLU B CD  
15776 O OE1 . GLU B 932  ? 0.5843 0.5688 0.5883 -0.0022 -0.0399 -0.0174 930  GLU B OE1 
15777 O OE2 . GLU B 932  ? 0.4788 0.4644 0.4822 -0.0005 -0.0403 -0.0154 930  GLU B OE2 
15778 N N   . LEU B 933  ? 0.2625 0.2547 0.2844 -0.0034 -0.0371 -0.0165 931  LEU B N   
15779 C CA  . LEU B 933  ? 0.2563 0.2487 0.2804 -0.0052 -0.0379 -0.0166 931  LEU B CA  
15780 C C   . LEU B 933  ? 0.3116 0.3000 0.3309 -0.0069 -0.0398 -0.0180 931  LEU B C   
15781 O O   . LEU B 933  ? 0.3590 0.3439 0.3728 -0.0064 -0.0395 -0.0192 931  LEU B O   
15782 C CB  . LEU B 933  ? 0.2698 0.2617 0.2949 -0.0046 -0.0351 -0.0170 931  LEU B CB  
15783 C CG  . LEU B 933  ? 0.2893 0.2847 0.3185 -0.0029 -0.0329 -0.0160 931  LEU B CG  
15784 C CD1 . LEU B 933  ? 0.3330 0.3275 0.3628 -0.0028 -0.0306 -0.0164 931  LEU B CD1 
15785 C CD2 . LEU B 933  ? 0.3566 0.3569 0.3916 -0.0031 -0.0340 -0.0144 931  LEU B CD2 
15786 N N   . GLU B 934  ? 0.3382 0.3270 0.3594 -0.0091 -0.0418 -0.0178 932  GLU B N   
15787 C CA  . GLU B 934  ? 0.3576 0.3417 0.3741 -0.0109 -0.0435 -0.0193 932  GLU B CA  
15788 C C   . GLU B 934  ? 0.4125 0.3930 0.4271 -0.0108 -0.0415 -0.0205 932  GLU B C   
15789 O O   . GLU B 934  ? 0.4333 0.4088 0.4422 -0.0109 -0.0416 -0.0222 932  GLU B O   
15790 C CB  . GLU B 934  ? 0.4012 0.3869 0.4201 -0.0136 -0.0468 -0.0186 932  GLU B CB  
15791 N N   . LYS B 935  ? 0.3596 0.3425 0.3787 -0.0105 -0.0397 -0.0196 933  LYS B N   
15792 C CA  . LYS B 935  ? 0.3807 0.3605 0.3986 -0.0105 -0.0379 -0.0204 933  LYS B CA  
15793 C C   . LYS B 935  ? 0.3284 0.3115 0.3503 -0.0088 -0.0350 -0.0194 933  LYS B C   
15794 O O   . LYS B 935  ? 0.3412 0.3292 0.3681 -0.0086 -0.0349 -0.0178 933  LYS B O   
15795 C CB  . LYS B 935  ? 0.3956 0.3738 0.4146 -0.0132 -0.0398 -0.0203 933  LYS B CB  
15796 N N   . LEU B 936  ? 0.3128 0.2934 0.3326 -0.0076 -0.0328 -0.0202 934  LEU B N   
15797 C CA  . LEU B 936  ? 0.3516 0.3350 0.3746 -0.0061 -0.0301 -0.0193 934  LEU B CA  
15798 C C   . LEU B 936  ? 0.3229 0.3095 0.3514 -0.0075 -0.0303 -0.0178 934  LEU B C   
15799 O O   . LEU B 936  ? 0.3191 0.3098 0.3515 -0.0065 -0.0287 -0.0166 934  LEU B O   
15800 C CB  . LEU B 936  ? 0.3677 0.3477 0.3874 -0.0047 -0.0280 -0.0204 934  LEU B CB  
15801 C CG  . LEU B 936  ? 0.3900 0.3720 0.4101 -0.0024 -0.0254 -0.0202 934  LEU B CG  
15802 C CD1 . LEU B 936  ? 0.3705 0.3491 0.3861 -0.0010 -0.0239 -0.0216 934  LEU B CD1 
15803 C CD2 . LEU B 936  ? 0.4031 0.3885 0.4279 -0.0023 -0.0239 -0.0189 934  LEU B CD2 
15804 N N   . SER B 937  ? 0.3200 0.3049 0.3487 -0.0099 -0.0322 -0.0177 935  SER B N   
15805 C CA  . SER B 937  ? 0.3328 0.3210 0.3667 -0.0116 -0.0323 -0.0161 935  SER B CA  
15806 C C   . SER B 937  ? 0.3184 0.3128 0.3575 -0.0118 -0.0332 -0.0146 935  SER B C   
15807 O O   . SER B 937  ? 0.3337 0.3321 0.3778 -0.0128 -0.0329 -0.0130 935  SER B O   
15808 C CB  . SER B 937  ? 0.3454 0.3299 0.3780 -0.0145 -0.0343 -0.0164 935  SER B CB  
15809 O OG  . SER B 937  ? 0.4117 0.3946 0.4420 -0.0159 -0.0372 -0.0171 935  SER B OG  
15810 N N   . ASP B 938  ? 0.3356 0.3309 0.3736 -0.0109 -0.0343 -0.0148 936  ASP B N   
15811 C CA  . ASP B 938  ? 0.3424 0.3436 0.3853 -0.0104 -0.0348 -0.0133 936  ASP B CA  
15812 C C   . ASP B 938  ? 0.3281 0.3328 0.3742 -0.0081 -0.0320 -0.0125 936  ASP B C   
15813 O O   . ASP B 938  ? 0.3349 0.3448 0.3858 -0.0076 -0.0319 -0.0111 936  ASP B O   
15814 C CB  . ASP B 938  ? 0.3595 0.3604 0.4000 -0.0093 -0.0363 -0.0138 936  ASP B CB  
15815 C CG  . ASP B 938  ? 0.4450 0.4431 0.4823 -0.0114 -0.0394 -0.0145 936  ASP B CG  
15816 O OD1 . ASP B 938  ? 0.4258 0.4229 0.4638 -0.0140 -0.0409 -0.0145 936  ASP B OD1 
15817 O OD2 . ASP B 938  ? 0.5027 0.4993 0.5366 -0.0106 -0.0405 -0.0151 936  ASP B OD2 
15818 N N   . LEU B 939  ? 0.2965 0.2984 0.3397 -0.0067 -0.0296 -0.0134 937  LEU B N   
15819 C CA  . LEU B 939  ? 0.3428 0.3473 0.3881 -0.0046 -0.0269 -0.0129 937  LEU B CA  
15820 C C   . LEU B 939  ? 0.3305 0.3355 0.3778 -0.0054 -0.0254 -0.0123 937  LEU B C   
15821 O O   . LEU B 939  ? 0.4125 0.4134 0.4568 -0.0061 -0.0251 -0.0131 937  LEU B O   
15822 C CB  . LEU B 939  ? 0.3227 0.3237 0.3633 -0.0027 -0.0254 -0.0142 937  LEU B CB  
15823 C CG  . LEU B 939  ? 0.4185 0.4209 0.4589 -0.0005 -0.0244 -0.0142 937  LEU B CG  
15824 C CD1 . LEU B 939  ? 0.3202 0.3195 0.3566 0.0007  -0.0226 -0.0153 937  LEU B CD1 
15825 C CD2 . LEU B 939  ? 0.3635 0.3705 0.4087 0.0006  -0.0230 -0.0130 937  LEU B CD2 
15826 N N   . GLN B 940  ? 0.2891 0.2992 0.3415 -0.0052 -0.0245 -0.0108 938  GLN B N   
15827 C CA  . GLN B 940  ? 0.3328 0.3440 0.3876 -0.0064 -0.0233 -0.0099 938  GLN B CA  
15828 C C   . GLN B 940  ? 0.3154 0.3285 0.3712 -0.0044 -0.0203 -0.0095 938  GLN B C   
15829 O O   . GLN B 940  ? 0.3241 0.3378 0.3812 -0.0051 -0.0190 -0.0088 938  GLN B O   
15830 C CB  . GLN B 940  ? 0.4348 0.4507 0.4948 -0.0084 -0.0246 -0.0082 938  GLN B CB  
15831 N N   . ARG B 941  ? 0.2558 0.2696 0.3108 -0.0019 -0.0192 -0.0100 939  ARG B N   
15832 C CA  . ARG B 941  ? 0.2758 0.2913 0.3316 -0.0001 -0.0165 -0.0098 939  ARG B CA  
15833 C C   . ARG B 941  ? 0.2298 0.2430 0.2821 0.0020  -0.0158 -0.0110 939  ARG B C   
15834 O O   . ARG B 941  ? 0.2285 0.2404 0.2791 0.0023  -0.0172 -0.0116 939  ARG B O   
15835 C CB  . ARG B 941  ? 0.2875 0.3089 0.3485 0.0005  -0.0158 -0.0084 939  ARG B CB  
15836 C CG  . ARG B 941  ? 0.3066 0.3304 0.3692 0.0019  -0.0169 -0.0083 939  ARG B CG  
15837 C CD  . ARG B 941  ? 0.2958 0.3259 0.3640 0.0025  -0.0162 -0.0068 939  ARG B CD  
15838 N NE  . ARG B 941  ? 0.2715 0.3038 0.3413 0.0043  -0.0171 -0.0066 939  ARG B NE  
15839 C CZ  . ARG B 941  ? 0.2891 0.3216 0.3583 0.0071  -0.0157 -0.0071 939  ARG B CZ  
15840 N NH1 . ARG B 941  ? 0.2875 0.3180 0.3542 0.0082  -0.0134 -0.0078 939  ARG B NH1 
15841 N NH2 . ARG B 941  ? 0.2809 0.3154 0.3518 0.0087  -0.0167 -0.0067 939  ARG B NH2 
15842 N N   . GLU B 942  ? 0.2397 0.2524 0.2908 0.0033  -0.0136 -0.0113 940  GLU B N   
15843 C CA  . GLU B 942  ? 0.2342 0.2453 0.2824 0.0052  -0.0128 -0.0123 940  GLU B CA  
15844 C C   . GLU B 942  ? 0.2351 0.2491 0.2857 0.0067  -0.0128 -0.0119 940  GLU B C   
15845 O O   . GLU B 942  ? 0.2603 0.2778 0.3141 0.0074  -0.0116 -0.0111 940  GLU B O   
15846 C CB  . GLU B 942  ? 0.2430 0.2535 0.2898 0.0060  -0.0105 -0.0125 940  GLU B CB  
15847 C CG  . GLU B 942  ? 0.2257 0.2347 0.2697 0.0076  -0.0097 -0.0134 940  GLU B CG  
15848 C CD  . GLU B 942  ? 0.2422 0.2515 0.2855 0.0084  -0.0076 -0.0135 940  GLU B CD  
15849 O OE1 . GLU B 942  ? 0.2794 0.2913 0.3252 0.0085  -0.0065 -0.0127 940  GLU B OE1 
15850 O OE2 . GLU B 942  ? 0.2301 0.2371 0.2701 0.0089  -0.0070 -0.0143 940  GLU B OE2 
15851 N N   . VAL B 943  ? 0.1835 0.1959 0.2322 0.0072  -0.0140 -0.0124 941  VAL B N   
15852 C CA  . VAL B 943  ? 0.2121 0.2263 0.2623 0.0089  -0.0142 -0.0121 941  VAL B CA  
15853 C C   . VAL B 943  ? 0.2084 0.2201 0.2553 0.0104  -0.0130 -0.0130 941  VAL B C   
15854 O O   . VAL B 943  ? 0.2039 0.2124 0.2472 0.0101  -0.0137 -0.0137 941  VAL B O   
15855 C CB  . VAL B 943  ? 0.2508 0.2651 0.3014 0.0084  -0.0167 -0.0118 941  VAL B CB  
15856 C CG1 . VAL B 943  ? 0.2363 0.2523 0.2885 0.0104  -0.0169 -0.0113 941  VAL B CG1 
15857 C CG2 . VAL B 943  ? 0.2812 0.2980 0.3351 0.0066  -0.0181 -0.0109 941  VAL B CG2 
15858 N N   . PHE B 944  ? 0.1933 0.2065 0.2413 0.0119  -0.0112 -0.0129 942  PHE B N   
15859 C CA  . PHE B 944  ? 0.1901 0.2009 0.2349 0.0129  -0.0099 -0.0137 942  PHE B CA  
15860 C C   . PHE B 944  ? 0.1961 0.2057 0.2399 0.0143  -0.0104 -0.0139 942  PHE B C   
15861 O O   . PHE B 944  ? 0.1980 0.2083 0.2425 0.0160  -0.0094 -0.0139 942  PHE B O   
15862 C CB  . PHE B 944  ? 0.2035 0.2160 0.2493 0.0136  -0.0077 -0.0136 942  PHE B CB  
15863 C CG  . PHE B 944  ? 0.1872 0.1972 0.2295 0.0138  -0.0065 -0.0145 942  PHE B CG  
15864 C CD1 . PHE B 944  ? 0.1948 0.2031 0.2350 0.0125  -0.0064 -0.0149 942  PHE B CD1 
15865 C CD2 . PHE B 944  ? 0.2020 0.2114 0.2431 0.0153  -0.0054 -0.0150 942  PHE B CD2 
15866 C CE1 . PHE B 944  ? 0.1914 0.1981 0.2287 0.0126  -0.0054 -0.0155 942  PHE B CE1 
15867 C CE2 . PHE B 944  ? 0.2038 0.2111 0.2416 0.0152  -0.0044 -0.0158 942  PHE B CE2 
15868 C CZ  . PHE B 944  ? 0.2114 0.2176 0.2475 0.0138  -0.0045 -0.0159 942  PHE B CZ  
15869 N N   . GLY B 945  ? 0.1747 0.1820 0.2164 0.0137  -0.0121 -0.0140 943  GLY B N   
15870 C CA  . GLY B 945  ? 0.1991 0.2051 0.2399 0.0149  -0.0131 -0.0139 943  GLY B CA  
15871 C C   . GLY B 945  ? 0.1991 0.2020 0.2364 0.0137  -0.0146 -0.0142 943  GLY B C   
15872 O O   . GLY B 945  ? 0.2083 0.2103 0.2439 0.0123  -0.0147 -0.0146 943  GLY B O   
15873 N N   . PRO B 946  ? 0.1982 0.1995 0.2343 0.0145  -0.0157 -0.0139 944  PRO B N   
15874 C CA  . PRO B 946  ? 0.2205 0.2188 0.2527 0.0135  -0.0169 -0.0141 944  PRO B CA  
15875 C C   . PRO B 946  ? 0.1928 0.1919 0.2256 0.0125  -0.0190 -0.0136 944  PRO B C   
15876 O O   . PRO B 946  ? 0.2082 0.2064 0.2403 0.0128  -0.0207 -0.0130 944  PRO B O   
15877 C CB  . PRO B 946  ? 0.1893 0.1853 0.2199 0.0148  -0.0172 -0.0138 944  PRO B CB  
15878 C CG  . PRO B 946  ? 0.2411 0.2396 0.2757 0.0167  -0.0173 -0.0132 944  PRO B CG  
15879 C CD  . PRO B 946  ? 0.1992 0.2010 0.2369 0.0166  -0.0157 -0.0134 944  PRO B CD  
15880 N N   . VAL B 947  ? 0.1920 0.1927 0.2262 0.0113  -0.0190 -0.0138 945  VAL B N   
15881 C CA  . VAL B 947  ? 0.1955 0.1971 0.2306 0.0102  -0.0210 -0.0134 945  VAL B CA  
15882 C C   . VAL B 947  ? 0.2407 0.2403 0.2727 0.0086  -0.0210 -0.0143 945  VAL B C   
15883 O O   . VAL B 947  ? 0.2364 0.2364 0.2690 0.0080  -0.0199 -0.0147 945  VAL B O   
15884 C CB  . VAL B 947  ? 0.2169 0.2225 0.2571 0.0102  -0.0213 -0.0127 945  VAL B CB  
15885 C CG1 . VAL B 947  ? 0.2366 0.2429 0.2775 0.0088  -0.0237 -0.0123 945  VAL B CG1 
15886 C CG2 . VAL B 947  ? 0.2171 0.2249 0.2604 0.0122  -0.0208 -0.0120 945  VAL B CG2 
15887 N N   . LEU B 948  ? 0.1921 0.1893 0.2205 0.0080  -0.0223 -0.0145 946  LEU B N   
15888 C CA  . LEU B 948  ? 0.1879 0.1830 0.2128 0.0067  -0.0224 -0.0154 946  LEU B CA  
15889 C C   . LEU B 948  ? 0.2022 0.1976 0.2275 0.0055  -0.0245 -0.0153 946  LEU B C   
15890 O O   . LEU B 948  ? 0.2294 0.2252 0.2550 0.0055  -0.0265 -0.0147 946  LEU B O   
15891 C CB  . LEU B 948  ? 0.1960 0.1887 0.2165 0.0068  -0.0223 -0.0157 946  LEU B CB  
15892 C CG  . LEU B 948  ? 0.1999 0.1907 0.2166 0.0058  -0.0221 -0.0166 946  LEU B CG  
15893 C CD1 . LEU B 948  ? 0.2042 0.1951 0.2211 0.0060  -0.0201 -0.0174 946  LEU B CD1 
15894 C CD2 . LEU B 948  ? 0.2337 0.2227 0.2463 0.0058  -0.0222 -0.0165 946  LEU B CD2 
15895 N N   . HIS B 949  ? 0.1834 0.1783 0.2086 0.0045  -0.0244 -0.0160 947  HIS B N   
15896 C CA  . HIS B 949  ? 0.1900 0.1844 0.2147 0.0030  -0.0265 -0.0162 947  HIS B CA  
15897 C C   . HIS B 949  ? 0.2255 0.2165 0.2449 0.0025  -0.0267 -0.0174 947  HIS B C   
15898 O O   . HIS B 949  ? 0.2594 0.2489 0.2765 0.0030  -0.0249 -0.0181 947  HIS B O   
15899 C CB  . HIS B 949  ? 0.2184 0.2141 0.2463 0.0021  -0.0262 -0.0162 947  HIS B CB  
15900 C CG  . HIS B 949  ? 0.1953 0.1947 0.2284 0.0028  -0.0255 -0.0150 947  HIS B CG  
15901 N ND1 . HIS B 949  ? 0.2153 0.2157 0.2497 0.0040  -0.0231 -0.0149 947  HIS B ND1 
15902 C CD2 . HIS B 949  ? 0.2237 0.2265 0.2610 0.0026  -0.0269 -0.0139 947  HIS B CD2 
15903 C CE1 . HIS B 949  ? 0.2048 0.2087 0.2436 0.0046  -0.0229 -0.0139 947  HIS B CE1 
15904 N NE2 . HIS B 949  ? 0.1961 0.2018 0.2370 0.0038  -0.0251 -0.0132 947  HIS B NE2 
15905 N N   . VAL B 950  ? 0.2082 0.1980 0.2255 0.0015  -0.0290 -0.0175 948  VAL B N   
15906 C CA  . VAL B 950  ? 0.2317 0.2183 0.2435 0.0012  -0.0293 -0.0186 948  VAL B CA  
15907 C C   . VAL B 950  ? 0.2304 0.2152 0.2408 -0.0004 -0.0310 -0.0194 948  VAL B C   
15908 O O   . VAL B 950  ? 0.2592 0.2452 0.2717 -0.0015 -0.0333 -0.0188 948  VAL B O   
15909 C CB  . VAL B 950  ? 0.2406 0.2268 0.2498 0.0014  -0.0305 -0.0180 948  VAL B CB  
15910 C CG1 . VAL B 950  ? 0.2691 0.2522 0.2723 0.0009  -0.0309 -0.0192 948  VAL B CG1 
15911 C CG2 . VAL B 950  ? 0.2628 0.2499 0.2725 0.0027  -0.0287 -0.0173 948  VAL B CG2 
15912 N N   . ILE B 951  ? 0.2138 0.1958 0.2207 -0.0004 -0.0300 -0.0208 949  ILE B N   
15913 C CA  . ILE B 951  ? 0.2259 0.2049 0.2301 -0.0017 -0.0315 -0.0220 949  ILE B CA  
15914 C C   . ILE B 951  ? 0.2138 0.1898 0.2118 -0.0013 -0.0314 -0.0232 949  ILE B C   
15915 O O   . ILE B 951  ? 0.2474 0.2233 0.2436 0.0001  -0.0292 -0.0235 949  ILE B O   
15916 C CB  . ILE B 951  ? 0.2718 0.2497 0.2773 -0.0017 -0.0301 -0.0226 949  ILE B CB  
15917 C CG1 . ILE B 951  ? 0.3406 0.3215 0.3520 -0.0024 -0.0304 -0.0213 949  ILE B CG1 
15918 C CG2 . ILE B 951  ? 0.3887 0.3622 0.3899 -0.0026 -0.0312 -0.0242 949  ILE B CG2 
15919 C CD1 . ILE B 951  ? 0.4098 0.3896 0.4223 -0.0025 -0.0290 -0.0216 949  ILE B CD1 
15920 N N   . ARG B 952  ? 0.2356 0.2094 0.2304 -0.0025 -0.0337 -0.0239 950  ARG B N   
15921 C CA  . ARG B 952  ? 0.2556 0.2261 0.2439 -0.0021 -0.0337 -0.0253 950  ARG B CA  
15922 C C   . ARG B 952  ? 0.2569 0.2235 0.2424 -0.0026 -0.0338 -0.0271 950  ARG B C   
15923 O O   . ARG B 952  ? 0.3145 0.2803 0.3020 -0.0041 -0.0355 -0.0271 950  ARG B O   
15924 C CB  . ARG B 952  ? 0.2692 0.2395 0.2550 -0.0031 -0.0363 -0.0250 950  ARG B CB  
15925 C CG  . ARG B 952  ? 0.2898 0.2633 0.2779 -0.0026 -0.0364 -0.0232 950  ARG B CG  
15926 C CD  . ARG B 952  ? 0.3953 0.3693 0.3829 -0.0037 -0.0396 -0.0224 950  ARG B CD  
15927 N NE  . ARG B 952  ? 0.4476 0.4245 0.4379 -0.0030 -0.0397 -0.0205 950  ARG B NE  
15928 C CZ  . ARG B 952  ? 0.4092 0.3856 0.3961 -0.0026 -0.0401 -0.0199 950  ARG B CZ  
15929 N NH1 . ARG B 952  ? 0.3758 0.3495 0.3565 -0.0029 -0.0401 -0.0210 950  ARG B NH1 
15930 N NH2 . ARG B 952  ? 0.4354 0.4141 0.4250 -0.0020 -0.0404 -0.0182 950  ARG B NH2 
15931 N N   . TYR B 953  ? 0.2400 0.2042 0.2210 -0.0012 -0.0320 -0.0285 951  TYR B N   
15932 C CA  . TYR B 953  ? 0.2722 0.2321 0.2503 -0.0013 -0.0321 -0.0303 951  TYR B CA  
15933 C C   . TYR B 953  ? 0.2632 0.2198 0.2342 -0.0004 -0.0318 -0.0320 951  TYR B C   
15934 O O   . TYR B 953  ? 0.2786 0.2368 0.2474 0.0007  -0.0304 -0.0318 951  TYR B O   
15935 C CB  . TYR B 953  ? 0.2654 0.2255 0.2460 0.0000  -0.0296 -0.0303 951  TYR B CB  
15936 C CG  . TYR B 953  ? 0.2519 0.2131 0.2308 0.0022  -0.0267 -0.0306 951  TYR B CG  
15937 C CD1 . TYR B 953  ? 0.2325 0.1980 0.2146 0.0028  -0.0253 -0.0291 951  TYR B CD1 
15938 C CD2 . TYR B 953  ? 0.2445 0.2027 0.2188 0.0037  -0.0254 -0.0323 951  TYR B CD2 
15939 C CE1 . TYR B 953  ? 0.2407 0.2076 0.2214 0.0045  -0.0228 -0.0293 951  TYR B CE1 
15940 C CE2 . TYR B 953  ? 0.2777 0.2377 0.2508 0.0057  -0.0227 -0.0324 951  TYR B CE2 
15941 C CZ  . TYR B 953  ? 0.2511 0.2156 0.2275 0.0059  -0.0215 -0.0308 951  TYR B CZ  
15942 O OH  . TYR B 953  ? 0.2544 0.2210 0.2299 0.0076  -0.0190 -0.0308 951  TYR B OH  
15943 N N   . ARG B 954  ? 0.3116 0.2634 0.2787 -0.0010 -0.0331 -0.0338 952  ARG B N   
15944 C CA  . ARG B 954  ? 0.3255 0.2736 0.2855 0.0002  -0.0325 -0.0358 952  ARG B CA  
15945 C C   . ARG B 954  ? 0.3132 0.2602 0.2726 0.0025  -0.0295 -0.0367 952  ARG B C   
15946 O O   . ARG B 954  ? 0.2915 0.2378 0.2543 0.0025  -0.0291 -0.0365 952  ARG B O   
15947 C CB  . ARG B 954  ? 0.3567 0.2995 0.3125 -0.0014 -0.0353 -0.0374 952  ARG B CB  
15948 N N   . ARG B 955  ? 0.3241 0.2711 0.2792 0.0045  -0.0274 -0.0376 953  ARG B N   
15949 C CA  . ARG B 955  ? 0.3554 0.3024 0.3104 0.0070  -0.0245 -0.0383 953  ARG B CA  
15950 C C   . ARG B 955  ? 0.3466 0.2882 0.2999 0.0075  -0.0249 -0.0399 953  ARG B C   
15951 O O   . ARG B 955  ? 0.3501 0.2919 0.3059 0.0088  -0.0232 -0.0397 953  ARG B O   
15952 C CB  . ARG B 955  ? 0.3822 0.3301 0.3324 0.0090  -0.0224 -0.0391 953  ARG B CB  
15953 C CG  . ARG B 955  ? 0.4394 0.3882 0.3897 0.0118  -0.0192 -0.0397 953  ARG B CG  
15954 C CD  . ARG B 955  ? 0.4390 0.3919 0.3960 0.0120  -0.0179 -0.0379 953  ARG B CD  
15955 N NE  . ARG B 955  ? 0.4413 0.3953 0.3983 0.0146  -0.0151 -0.0383 953  ARG B NE  
15956 C CZ  . ARG B 955  ? 0.4715 0.4218 0.4272 0.0162  -0.0146 -0.0396 953  ARG B CZ  
15957 N NH1 . ARG B 955  ? 0.4514 0.3961 0.4054 0.0152  -0.0167 -0.0407 953  ARG B NH1 
15958 N NH2 . ARG B 955  ? 0.4562 0.4083 0.4124 0.0188  -0.0120 -0.0398 953  ARG B NH2 
15959 N N   . ASP B 956  ? 0.3303 0.2668 0.2791 0.0063  -0.0272 -0.0415 954  ASP B N   
15960 C CA  . ASP B 956  ? 0.3744 0.3050 0.3212 0.0066  -0.0277 -0.0430 954  ASP B CA  
15961 C C   . ASP B 956  ? 0.3679 0.2987 0.3205 0.0047  -0.0290 -0.0417 954  ASP B C   
15962 O O   . ASP B 956  ? 0.4040 0.3302 0.3557 0.0048  -0.0292 -0.0425 954  ASP B O   
15963 C CB  . ASP B 956  ? 0.4244 0.3487 0.3639 0.0061  -0.0297 -0.0454 954  ASP B CB  
15964 C CG  . ASP B 956  ? 0.5109 0.4348 0.4502 0.0028  -0.0332 -0.0450 954  ASP B CG  
15965 O OD1 . ASP B 956  ? 0.5211 0.4485 0.4665 0.0007  -0.0345 -0.0430 954  ASP B OD1 
15966 O OD2 . ASP B 956  ? 0.6100 0.5304 0.5430 0.0025  -0.0346 -0.0466 954  ASP B OD2 
15967 N N   . ASP B 957  ? 0.3283 0.2642 0.2866 0.0030  -0.0297 -0.0395 955  ASP B N   
15968 C CA  . ASP B 957  ? 0.3376 0.2747 0.3018 0.0014  -0.0304 -0.0379 955  ASP B CA  
15969 C C   . ASP B 957  ? 0.2969 0.2386 0.2661 0.0030  -0.0276 -0.0365 955  ASP B C   
15970 O O   . ASP B 957  ? 0.3269 0.2710 0.3015 0.0017  -0.0279 -0.0349 955  ASP B O   
15971 C CB  . ASP B 957  ? 0.3547 0.2948 0.3225 -0.0015 -0.0330 -0.0365 955  ASP B CB  
15972 C CG  . ASP B 957  ? 0.4869 0.4224 0.4509 -0.0037 -0.0362 -0.0377 955  ASP B CG  
15973 O OD1 . ASP B 957  ? 0.4786 0.4081 0.4389 -0.0038 -0.0368 -0.0393 955  ASP B OD1 
15974 O OD2 . ASP B 957  ? 0.5055 0.4433 0.4700 -0.0053 -0.0382 -0.0370 955  ASP B OD2 
15975 N N   . LEU B 958  ? 0.2631 0.2063 0.2306 0.0056  -0.0250 -0.0369 956  LEU B N   
15976 C CA  . LEU B 958  ? 0.2569 0.2048 0.2290 0.0069  -0.0226 -0.0354 956  LEU B CA  
15977 C C   . LEU B 958  ? 0.2665 0.2129 0.2415 0.0070  -0.0222 -0.0350 956  LEU B C   
15978 O O   . LEU B 958  ? 0.2557 0.2057 0.2359 0.0064  -0.0217 -0.0333 956  LEU B O   
15979 C CB  . LEU B 958  ? 0.2647 0.2139 0.2338 0.0097  -0.0200 -0.0362 956  LEU B CB  
15980 C CG  . LEU B 958  ? 0.2865 0.2404 0.2598 0.0111  -0.0176 -0.0348 956  LEU B CG  
15981 C CD1 . LEU B 958  ? 0.2739 0.2327 0.2520 0.0095  -0.0179 -0.0329 956  LEU B CD1 
15982 C CD2 . LEU B 958  ? 0.3042 0.2595 0.2743 0.0136  -0.0153 -0.0356 956  LEU B CD2 
15983 N N   . ASP B 959  ? 0.2654 0.2062 0.2368 0.0078  -0.0224 -0.0365 957  ASP B N   
15984 C CA  . ASP B 959  ? 0.2693 0.2083 0.2431 0.0079  -0.0220 -0.0359 957  ASP B CA  
15985 C C   . ASP B 959  ? 0.2536 0.1935 0.2319 0.0049  -0.0239 -0.0344 957  ASP B C   
15986 O O   . ASP B 959  ? 0.2516 0.1938 0.2344 0.0047  -0.0231 -0.0328 957  ASP B O   
15987 C CB  . ASP B 959  ? 0.2683 0.2002 0.2369 0.0092  -0.0222 -0.0378 957  ASP B CB  
15988 C CG  . ASP B 959  ? 0.2935 0.2241 0.2640 0.0106  -0.0208 -0.0372 957  ASP B CG  
15989 O OD1 . ASP B 959  ? 0.2743 0.2098 0.2481 0.0121  -0.0187 -0.0361 957  ASP B OD1 
15990 O OD2 . ASP B 959  ? 0.3284 0.2530 0.2970 0.0100  -0.0220 -0.0379 957  ASP B OD2 
15991 N N   . ARG B 960  ? 0.2466 0.1847 0.2237 0.0025  -0.0265 -0.0348 958  ARG B N   
15992 C CA  . ARG B 960  ? 0.2400 0.1798 0.2217 -0.0005 -0.0284 -0.0332 958  ARG B CA  
15993 C C   . ARG B 960  ? 0.2668 0.2138 0.2541 -0.0007 -0.0275 -0.0312 958  ARG B C   
15994 O O   . ARG B 960  ? 0.2484 0.1980 0.2406 -0.0020 -0.0277 -0.0296 958  ARG B O   
15995 C CB  . ARG B 960  ? 0.3001 0.2372 0.2792 -0.0030 -0.0315 -0.0340 958  ARG B CB  
15996 N N   . LEU B 961  ? 0.2301 0.1801 0.2165 0.0006  -0.0266 -0.0313 959  LEU B N   
15997 C CA  . LEU B 961  ? 0.2260 0.1822 0.2171 0.0007  -0.0256 -0.0296 959  LEU B CA  
15998 C C   . LEU B 961  ? 0.2274 0.1858 0.2218 0.0021  -0.0233 -0.0286 959  LEU B C   
15999 O O   . LEU B 961  ? 0.2266 0.1888 0.2259 0.0013  -0.0230 -0.0270 959  LEU B O   
16000 C CB  . LEU B 961  ? 0.2550 0.2132 0.2438 0.0019  -0.0250 -0.0300 959  LEU B CB  
16001 C CG  . LEU B 961  ? 0.2489 0.2127 0.2418 0.0023  -0.0239 -0.0283 959  LEU B CG  
16002 C CD1 . LEU B 961  ? 0.2993 0.2657 0.2965 0.0003  -0.0258 -0.0269 959  LEU B CD1 
16003 C CD2 . LEU B 961  ? 0.2723 0.2374 0.2623 0.0034  -0.0230 -0.0287 959  LEU B CD2 
16004 N N   . VAL B 962  ? 0.2238 0.1800 0.2154 0.0042  -0.0215 -0.0296 960  VAL B N   
16005 C CA  . VAL B 962  ? 0.2248 0.1829 0.2193 0.0054  -0.0195 -0.0286 960  VAL B CA  
16006 C C   . VAL B 962  ? 0.2428 0.1999 0.2405 0.0038  -0.0203 -0.0276 960  VAL B C   
16007 O O   . VAL B 962  ? 0.2343 0.1950 0.2362 0.0036  -0.0193 -0.0261 960  VAL B O   
16008 C CB  . VAL B 962  ? 0.2322 0.1880 0.2232 0.0080  -0.0177 -0.0298 960  VAL B CB  
16009 C CG1 . VAL B 962  ? 0.2742 0.2315 0.2681 0.0091  -0.0161 -0.0288 960  VAL B CG1 
16010 C CG2 . VAL B 962  ? 0.2541 0.2124 0.2429 0.0096  -0.0165 -0.0305 960  VAL B CG2 
16011 N N   . ASP B 963  ? 0.2411 0.1933 0.2366 0.0023  -0.0222 -0.0284 961  ASP B N   
16012 C CA  . ASP B 963  ? 0.2606 0.2119 0.2590 0.0002  -0.0232 -0.0272 961  ASP B CA  
16013 C C   . ASP B 963  ? 0.2691 0.2258 0.2728 -0.0016 -0.0239 -0.0255 961  ASP B C   
16014 O O   . ASP B 963  ? 0.2610 0.2202 0.2688 -0.0023 -0.0233 -0.0239 961  ASP B O   
16015 C CB  . ASP B 963  ? 0.2627 0.2079 0.2578 -0.0016 -0.0256 -0.0283 961  ASP B CB  
16016 C CG  . ASP B 963  ? 0.3198 0.2590 0.3102 0.0002  -0.0250 -0.0298 961  ASP B CG  
16017 O OD1 . ASP B 963  ? 0.3667 0.3066 0.3574 0.0025  -0.0228 -0.0295 961  ASP B OD1 
16018 O OD2 . ASP B 963  ? 0.3701 0.3035 0.3563 -0.0008 -0.0268 -0.0312 961  ASP B OD2 
16019 N N   . ASP B 964  ? 0.2584 0.2168 0.2618 -0.0024 -0.0252 -0.0257 962  ASP B N   
16020 C CA  . ASP B 964  ? 0.2585 0.2221 0.2668 -0.0038 -0.0260 -0.0241 962  ASP B CA  
16021 C C   . ASP B 964  ? 0.2738 0.2423 0.2857 -0.0023 -0.0237 -0.0229 962  ASP B C   
16022 O O   . ASP B 964  ? 0.2368 0.2089 0.2533 -0.0032 -0.0235 -0.0214 962  ASP B O   
16023 C CB  . ASP B 964  ? 0.2561 0.2205 0.2629 -0.0044 -0.0277 -0.0247 962  ASP B CB  
16024 C CG  . ASP B 964  ? 0.3344 0.2946 0.3384 -0.0064 -0.0304 -0.0256 962  ASP B CG  
16025 O OD1 . ASP B 964  ? 0.3350 0.2918 0.3386 -0.0078 -0.0312 -0.0257 962  ASP B OD1 
16026 O OD2 . ASP B 964  ? 0.4159 0.3759 0.4175 -0.0068 -0.0319 -0.0263 962  ASP B OD2 
16027 N N   . VAL B 965  ? 0.2130 0.1817 0.2226 0.0000  -0.0218 -0.0237 963  VAL B N   
16028 C CA  . VAL B 965  ? 0.1848 0.1577 0.1973 0.0014  -0.0198 -0.0227 963  VAL B CA  
16029 C C   . VAL B 965  ? 0.2206 0.1936 0.2354 0.0014  -0.0186 -0.0218 963  VAL B C   
16030 O O   . VAL B 965  ? 0.2388 0.2155 0.2576 0.0012  -0.0178 -0.0204 963  VAL B O   
16031 C CB  . VAL B 965  ? 0.2187 0.1918 0.2283 0.0035  -0.0182 -0.0235 963  VAL B CB  
16032 C CG1 . VAL B 965  ? 0.2101 0.1870 0.2223 0.0047  -0.0162 -0.0226 963  VAL B CG1 
16033 C CG2 . VAL B 965  ? 0.2333 0.2069 0.2410 0.0032  -0.0193 -0.0240 963  VAL B CG2 
16034 N N   . ASN B 966  ? 0.2179 0.1865 0.2299 0.0018  -0.0185 -0.0225 964  ASN B N   
16035 C CA  . ASN B 966  ? 0.2265 0.1947 0.2403 0.0018  -0.0174 -0.0215 964  ASN B CA  
16036 C C   . ASN B 966  ? 0.2410 0.2101 0.2583 -0.0007 -0.0186 -0.0201 964  ASN B C   
16037 O O   . ASN B 966  ? 0.2696 0.2406 0.2897 -0.0009 -0.0176 -0.0188 964  ASN B O   
16038 C CB  . ASN B 966  ? 0.2231 0.1859 0.2329 0.0028  -0.0173 -0.0226 964  ASN B CB  
16039 C CG  . ASN B 966  ? 0.2400 0.2029 0.2471 0.0056  -0.0156 -0.0236 964  ASN B CG  
16040 O OD1 . ASN B 966  ? 0.2433 0.2104 0.2520 0.0067  -0.0142 -0.0231 964  ASN B OD1 
16041 N ND2 . ASN B 966  ? 0.2470 0.2051 0.2499 0.0067  -0.0158 -0.0250 964  ASN B ND2 
16042 N N   . ALA B 967  ? 0.2114 0.1795 0.2286 -0.0027 -0.0208 -0.0204 965  ALA B N   
16043 C CA  . ALA B 967  ? 0.2348 0.2034 0.2551 -0.0053 -0.0222 -0.0191 965  ALA B CA  
16044 C C   . ALA B 967  ? 0.2280 0.2031 0.2538 -0.0058 -0.0214 -0.0174 965  ALA B C   
16045 O O   . ALA B 967  ? 0.2670 0.2435 0.2960 -0.0078 -0.0220 -0.0160 965  ALA B O   
16046 C CB  . ALA B 967  ? 0.2802 0.2467 0.2991 -0.0074 -0.0250 -0.0199 965  ALA B CB  
16047 N N   . THR B 968  ? 0.2056 0.1844 0.2324 -0.0040 -0.0202 -0.0174 966  THR B N   
16048 C CA  . THR B 968  ? 0.2236 0.2080 0.2551 -0.0040 -0.0193 -0.0159 966  THR B CA  
16049 C C   . THR B 968  ? 0.2354 0.2209 0.2688 -0.0038 -0.0174 -0.0147 966  THR B C   
16050 O O   . THR B 968  ? 0.2461 0.2359 0.2836 -0.0043 -0.0168 -0.0133 966  THR B O   
16051 C CB  . THR B 968  ? 0.2124 0.1996 0.2440 -0.0021 -0.0183 -0.0162 966  THR B CB  
16052 O OG1 . THR B 968  ? 0.2316 0.2180 0.2612 -0.0001 -0.0163 -0.0167 966  THR B OG1 
16053 C CG2 . THR B 968  ? 0.2455 0.2314 0.2746 -0.0021 -0.0199 -0.0174 966  THR B CG2 
16054 N N   . GLY B 969  ? 0.2280 0.2099 0.2584 -0.0028 -0.0165 -0.0152 967  GLY B N   
16055 C CA  . GLY B 969  ? 0.2342 0.2169 0.2657 -0.0023 -0.0147 -0.0142 967  GLY B CA  
16056 C C   . GLY B 969  ? 0.2200 0.2053 0.2514 0.0000  -0.0127 -0.0143 967  GLY B C   
16057 O O   . GLY B 969  ? 0.2232 0.2087 0.2546 0.0008  -0.0112 -0.0137 967  GLY B O   
16058 N N   . TYR B 970  ? 0.2106 0.1979 0.2419 0.0010  -0.0127 -0.0150 968  TYR B N   
16059 C CA  . TYR B 970  ? 0.1922 0.1816 0.2231 0.0030  -0.0110 -0.0153 968  TYR B CA  
16060 C C   . TYR B 970  ? 0.2035 0.1898 0.2304 0.0044  -0.0106 -0.0165 968  TYR B C   
16061 O O   . TYR B 970  ? 0.2220 0.2046 0.2463 0.0042  -0.0117 -0.0174 968  TYR B O   
16062 C CB  . TYR B 970  ? 0.1905 0.1828 0.2227 0.0033  -0.0113 -0.0155 968  TYR B CB  
16063 C CG  . TYR B 970  ? 0.2365 0.2328 0.2728 0.0026  -0.0110 -0.0142 968  TYR B CG  
16064 C CD1 . TYR B 970  ? 0.2564 0.2554 0.2943 0.0036  -0.0092 -0.0135 968  TYR B CD1 
16065 C CD2 . TYR B 970  ? 0.2489 0.2464 0.2876 0.0012  -0.0126 -0.0137 968  TYR B CD2 
16066 C CE1 . TYR B 970  ? 0.2859 0.2887 0.3275 0.0033  -0.0088 -0.0124 968  TYR B CE1 
16067 C CE2 . TYR B 970  ? 0.2815 0.2833 0.3244 0.0008  -0.0123 -0.0124 968  TYR B CE2 
16068 C CZ  . TYR B 970  ? 0.3299 0.3342 0.3741 0.0020  -0.0102 -0.0118 968  TYR B CZ  
16069 O OH  . TYR B 970  ? 0.4262 0.4349 0.4743 0.0019  -0.0096 -0.0107 968  TYR B OH  
16070 N N   . GLY B 971  ? 0.1766 0.1646 0.2029 0.0060  -0.0091 -0.0166 969  GLY B N   
16071 C CA  . GLY B 971  ? 0.1837 0.1698 0.2068 0.0075  -0.0086 -0.0177 969  GLY B CA  
16072 C C   . GLY B 971  ? 0.1747 0.1636 0.1978 0.0088  -0.0071 -0.0176 969  GLY B C   
16073 O O   . GLY B 971  ? 0.1899 0.1788 0.2122 0.0099  -0.0061 -0.0174 969  GLY B O   
16074 N N   . LEU B 972  ? 0.1574 0.1486 0.1814 0.0086  -0.0072 -0.0177 970  LEU B N   
16075 C CA  . LEU B 972  ? 0.1523 0.1460 0.1763 0.0095  -0.0060 -0.0176 970  LEU B CA  
16076 C C   . LEU B 972  ? 0.1690 0.1623 0.1904 0.0102  -0.0060 -0.0186 970  LEU B C   
16077 O O   . LEU B 972  ? 0.1901 0.1829 0.2098 0.0112  -0.0053 -0.0189 970  LEU B O   
16078 C CB  . LEU B 972  ? 0.1761 0.1722 0.2025 0.0091  -0.0059 -0.0171 970  LEU B CB  
16079 C CG  . LEU B 972  ? 0.1794 0.1776 0.2058 0.0099  -0.0047 -0.0170 970  LEU B CG  
16080 C CD1 . LEU B 972  ? 0.2029 0.2016 0.2289 0.0105  -0.0036 -0.0166 970  LEU B CD1 
16081 C CD2 . LEU B 972  ? 0.2048 0.2049 0.2334 0.0097  -0.0046 -0.0165 970  LEU B CD2 
16082 N N   . THR B 973  ? 0.1597 0.1534 0.1808 0.0098  -0.0067 -0.0189 971  THR B N   
16083 C CA  . THR B 973  ? 0.1472 0.1406 0.1657 0.0102  -0.0067 -0.0196 971  THR B CA  
16084 C C   . THR B 973  ? 0.1432 0.1342 0.1599 0.0098  -0.0079 -0.0203 971  THR B C   
16085 O O   . THR B 973  ? 0.1703 0.1603 0.1880 0.0089  -0.0092 -0.0202 971  THR B O   
16086 C CB  . THR B 973  ? 0.1649 0.1600 0.1836 0.0100  -0.0065 -0.0194 971  THR B CB  
16087 O OG1 . THR B 973  ? 0.1623 0.1573 0.1824 0.0093  -0.0076 -0.0191 971  THR B OG1 
16088 C CG2 . THR B 973  ? 0.1837 0.1807 0.2035 0.0104  -0.0053 -0.0189 971  THR B CG2 
16089 N N   . PHE B 974  ? 0.1648 0.1553 0.1787 0.0104  -0.0076 -0.0210 972  PHE B N   
16090 C CA  . PHE B 974  ? 0.1643 0.1524 0.1757 0.0102  -0.0087 -0.0219 972  PHE B CA  
16091 C C   . PHE B 974  ? 0.1518 0.1407 0.1605 0.0108  -0.0081 -0.0223 972  PHE B C   
16092 O O   . PHE B 974  ? 0.1632 0.1536 0.1715 0.0117  -0.0067 -0.0224 972  PHE B O   
16093 C CB  . PHE B 974  ? 0.1596 0.1448 0.1697 0.0106  -0.0089 -0.0225 972  PHE B CB  
16094 C CG  . PHE B 974  ? 0.1694 0.1520 0.1762 0.0107  -0.0098 -0.0236 972  PHE B CG  
16095 C CD1 . PHE B 974  ? 0.1987 0.1794 0.2052 0.0093  -0.0116 -0.0238 972  PHE B CD1 
16096 C CD2 . PHE B 974  ? 0.1811 0.1632 0.1848 0.0121  -0.0089 -0.0245 972  PHE B CD2 
16097 C CE1 . PHE B 974  ? 0.1998 0.1780 0.2028 0.0093  -0.0126 -0.0249 972  PHE B CE1 
16098 C CE2 . PHE B 974  ? 0.1905 0.1701 0.1907 0.0122  -0.0096 -0.0256 972  PHE B CE2 
16099 C CZ  . PHE B 974  ? 0.2054 0.1828 0.2050 0.0107  -0.0115 -0.0259 972  PHE B CZ  
16100 N N   . GLY B 975  ? 0.1566 0.1448 0.1637 0.0101  -0.0091 -0.0226 973  GLY B N   
16101 C CA  . GLY B 975  ? 0.1731 0.1621 0.1774 0.0104  -0.0085 -0.0229 973  GLY B CA  
16102 C C   . GLY B 975  ? 0.1752 0.1617 0.1760 0.0106  -0.0092 -0.0240 973  GLY B C   
16103 O O   . GLY B 975  ? 0.1909 0.1750 0.1913 0.0099  -0.0107 -0.0243 973  GLY B O   
16104 N N   . LEU B 976  ? 0.1807 0.1681 0.1790 0.0114  -0.0081 -0.0244 974  LEU B N   
16105 C CA  . LEU B 976  ? 0.1863 0.1715 0.1806 0.0118  -0.0084 -0.0255 974  LEU B CA  
16106 C C   . LEU B 976  ? 0.2021 0.1896 0.1943 0.0117  -0.0076 -0.0252 974  LEU B C   
16107 O O   . LEU B 976  ? 0.2011 0.1916 0.1941 0.0123  -0.0060 -0.0248 974  LEU B O   
16108 C CB  . LEU B 976  ? 0.2045 0.1882 0.1975 0.0135  -0.0075 -0.0266 974  LEU B CB  
16109 C CG  . LEU B 976  ? 0.2329 0.2144 0.2212 0.0144  -0.0075 -0.0280 974  LEU B CG  
16110 C CD1 . LEU B 976  ? 0.2338 0.2115 0.2203 0.0131  -0.0097 -0.0286 974  LEU B CD1 
16111 C CD2 . LEU B 976  ? 0.2293 0.2096 0.2164 0.0166  -0.0063 -0.0289 974  LEU B CD2 
16112 N N   . HIS B 977  ? 0.1967 0.1830 0.1865 0.0108  -0.0087 -0.0253 975  HIS B N   
16113 C CA  . HIS B 977  ? 0.2158 0.2039 0.2030 0.0106  -0.0080 -0.0250 975  HIS B CA  
16114 C C   . HIS B 977  ? 0.1965 0.1825 0.1791 0.0115  -0.0079 -0.0263 975  HIS B C   
16115 O O   . HIS B 977  ? 0.2139 0.1969 0.1946 0.0109  -0.0096 -0.0269 975  HIS B O   
16116 C CB  . HIS B 977  ? 0.2052 0.1934 0.1927 0.0090  -0.0093 -0.0239 975  HIS B CB  
16117 C CG  . HIS B 977  ? 0.2281 0.2187 0.2185 0.0083  -0.0087 -0.0226 975  HIS B CG  
16118 N ND1 . HIS B 977  ? 0.3171 0.3098 0.3064 0.0076  -0.0079 -0.0216 975  HIS B ND1 
16119 C CD2 . HIS B 977  ? 0.2956 0.2868 0.2898 0.0082  -0.0087 -0.0221 975  HIS B CD2 
16120 C CE1 . HIS B 977  ? 0.2761 0.2701 0.2682 0.0070  -0.0077 -0.0207 975  HIS B CE1 
16121 N NE2 . HIS B 977  ? 0.3002 0.2934 0.2952 0.0075  -0.0081 -0.0210 975  HIS B NE2 
16122 N N   . THR B 978  ? 0.1960 0.1839 0.1771 0.0129  -0.0060 -0.0268 976  THR B N   
16123 C CA  . THR B 978  ? 0.2146 0.2010 0.1911 0.0141  -0.0055 -0.0281 976  THR B CA  
16124 C C   . THR B 978  ? 0.2209 0.2114 0.1968 0.0154  -0.0030 -0.0279 976  THR B C   
16125 O O   . THR B 978  ? 0.2510 0.2446 0.2302 0.0158  -0.0019 -0.0272 976  THR B O   
16126 C CB  . THR B 978  ? 0.2573 0.2399 0.2329 0.0155  -0.0059 -0.0297 976  THR B CB  
16127 O OG1 . THR B 978  ? 0.2360 0.2168 0.2066 0.0168  -0.0053 -0.0312 976  THR B OG1 
16128 C CG2 . THR B 978  ? 0.2695 0.2535 0.2481 0.0169  -0.0046 -0.0296 976  THR B CG2 
16129 N N   . ARG B 979  ? 0.2394 0.2300 0.2111 0.0160  -0.0023 -0.0286 977  ARG B N   
16130 C CA  . ARG B 979  ? 0.2367 0.2314 0.2076 0.0175  0.0002  -0.0285 977  ARG B CA  
16131 C C   . ARG B 979  ? 0.2505 0.2436 0.2194 0.0204  0.0013  -0.0303 977  ARG B C   
16132 O O   . ARG B 979  ? 0.2632 0.2599 0.2315 0.0222  0.0035  -0.0304 977  ARG B O   
16133 C CB  . ARG B 979  ? 0.3144 0.3110 0.2819 0.0166  0.0008  -0.0280 977  ARG B CB  
16134 C CG  . ARG B 979  ? 0.3705 0.3692 0.3401 0.0140  0.0001  -0.0260 977  ARG B CG  
16135 C CD  . ARG B 979  ? 0.4525 0.4515 0.4181 0.0128  0.0000  -0.0254 977  ARG B CD  
16136 N NE  . ARG B 979  ? 0.5411 0.5424 0.5086 0.0105  -0.0002 -0.0233 977  ARG B NE  
16137 C CZ  . ARG B 979  ? 0.5771 0.5792 0.5416 0.0090  -0.0002 -0.0223 977  ARG B CZ  
16138 N NH1 . ARG B 979  ? 0.4804 0.4816 0.4401 0.0096  0.0001  -0.0230 977  ARG B NH1 
16139 N NH2 . ARG B 979  ? 0.5491 0.5528 0.5155 0.0069  -0.0005 -0.0204 977  ARG B NH2 
16140 N N   . LEU B 980  ? 0.2321 0.2200 0.2000 0.0209  -0.0002 -0.0317 978  LEU B N   
16141 C CA  . LEU B 980  ? 0.2343 0.2191 0.1988 0.0235  0.0005  -0.0336 978  LEU B CA  
16142 C C   . LEU B 980  ? 0.2357 0.2198 0.2032 0.0252  0.0009  -0.0339 978  LEU B C   
16143 O O   . LEU B 980  ? 0.2361 0.2175 0.2060 0.0241  -0.0007 -0.0336 978  LEU B O   
16144 C CB  . LEU B 980  ? 0.2355 0.2143 0.1960 0.0228  -0.0016 -0.0351 978  LEU B CB  
16145 C CG  . LEU B 980  ? 0.2834 0.2623 0.2406 0.0210  -0.0024 -0.0348 978  LEU B CG  
16146 C CD1 . LEU B 980  ? 0.2906 0.2634 0.2439 0.0203  -0.0048 -0.0364 978  LEU B CD1 
16147 C CD2 . LEU B 980  ? 0.2793 0.2617 0.2333 0.0225  0.0000  -0.0350 978  LEU B CD2 
16148 N N   . ASP B 981  ? 0.2350 0.2217 0.2022 0.0279  0.0031  -0.0343 979  ASP B N   
16149 C CA  . ASP B 981  ? 0.2453 0.2318 0.2154 0.0297  0.0036  -0.0342 979  ASP B CA  
16150 C C   . ASP B 981  ? 0.2375 0.2168 0.2058 0.0303  0.0020  -0.0357 979  ASP B C   
16151 O O   . ASP B 981  ? 0.2346 0.2126 0.2060 0.0302  0.0014  -0.0351 979  ASP B O   
16152 C CB  . ASP B 981  ? 0.2507 0.2409 0.2202 0.0330  0.0062  -0.0346 979  ASP B CB  
16153 C CG  . ASP B 981  ? 0.2895 0.2874 0.2622 0.0323  0.0077  -0.0328 979  ASP B CG  
16154 O OD1 . ASP B 981  ? 0.3113 0.3113 0.2872 0.0296  0.0068  -0.0312 979  ASP B OD1 
16155 O OD2 . ASP B 981  ? 0.3347 0.3366 0.3065 0.0347  0.0099  -0.0330 979  ASP B OD2 
16156 N N   . GLU B 982  ? 0.2443 0.2188 0.2075 0.0307  0.0013  -0.0375 980  GLU B N   
16157 C CA  . GLU B 982  ? 0.2580 0.2254 0.2194 0.0309  -0.0004 -0.0388 980  GLU B CA  
16158 C C   . GLU B 982  ? 0.2526 0.2183 0.2171 0.0277  -0.0028 -0.0378 980  GLU B C   
16159 O O   . GLU B 982  ? 0.2633 0.2255 0.2292 0.0275  -0.0038 -0.0378 980  GLU B O   
16160 C CB  . GLU B 982  ? 0.2891 0.2515 0.2440 0.0317  -0.0009 -0.0410 980  GLU B CB  
16161 C CG  . GLU B 982  ? 0.3195 0.2740 0.2720 0.0316  -0.0029 -0.0425 980  GLU B CG  
16162 C CD  . GLU B 982  ? 0.4097 0.3588 0.3560 0.0312  -0.0042 -0.0445 980  GLU B CD  
16163 O OE1 . GLU B 982  ? 0.4976 0.4486 0.4425 0.0293  -0.0048 -0.0442 980  GLU B OE1 
16164 O OE2 . GLU B 982  ? 0.3822 0.3249 0.3246 0.0327  -0.0048 -0.0464 980  GLU B OE2 
16165 N N   . THR B 983  ? 0.2368 0.2049 0.2021 0.0252  -0.0036 -0.0368 981  THR B N   
16166 C CA  . THR B 983  ? 0.2343 0.2016 0.2029 0.0223  -0.0057 -0.0357 981  THR B CA  
16167 C C   . THR B 983  ? 0.2329 0.2035 0.2070 0.0221  -0.0051 -0.0340 981  THR B C   
16168 O O   . THR B 983  ? 0.2366 0.2051 0.2132 0.0210  -0.0064 -0.0336 981  THR B O   
16169 C CB  . THR B 983  ? 0.2509 0.2201 0.2190 0.0201  -0.0067 -0.0350 981  THR B CB  
16170 O OG1 . THR B 983  ? 0.2733 0.2389 0.2359 0.0202  -0.0075 -0.0366 981  THR B OG1 
16171 C CG2 . THR B 983  ? 0.2425 0.2115 0.2143 0.0175  -0.0087 -0.0337 981  THR B CG2 
16172 N N   . ILE B 984  ? 0.2097 0.1855 0.1856 0.0232  -0.0031 -0.0331 982  ILE B N   
16173 C CA  . ILE B 984  ? 0.2263 0.2053 0.2070 0.0232  -0.0025 -0.0317 982  ILE B CA  
16174 C C   . ILE B 984  ? 0.2309 0.2068 0.2121 0.0248  -0.0024 -0.0322 982  ILE B C   
16175 O O   . ILE B 984  ? 0.2431 0.2183 0.2274 0.0239  -0.0032 -0.0313 982  ILE B O   
16176 C CB  . ILE B 984  ? 0.2218 0.2069 0.2039 0.0240  -0.0004 -0.0308 982  ILE B CB  
16177 C CG1 . ILE B 984  ? 0.2653 0.2532 0.2474 0.0218  -0.0007 -0.0299 982  ILE B CG1 
16178 C CG2 . ILE B 984  ? 0.2439 0.2320 0.2304 0.0242  0.0002  -0.0295 982  ILE B CG2 
16179 C CD1 . ILE B 984  ? 0.2427 0.2362 0.2252 0.0224  0.0012  -0.0291 982  ILE B CD1 
16180 N N   . ALA B 985  ? 0.2298 0.2035 0.2076 0.0275  -0.0015 -0.0336 983  ALA B N   
16181 C CA  . ALA B 985  ? 0.2453 0.2156 0.2231 0.0294  -0.0014 -0.0340 983  ALA B CA  
16182 C C   . ALA B 985  ? 0.2337 0.1979 0.2109 0.0276  -0.0036 -0.0345 983  ALA B C   
16183 O O   . ALA B 985  ? 0.2445 0.2073 0.2242 0.0273  -0.0041 -0.0336 983  ALA B O   
16184 C CB  . ALA B 985  ? 0.2628 0.2315 0.2366 0.0328  0.0000  -0.0356 983  ALA B CB  
16185 N N   . HIS B 986  ? 0.2425 0.2033 0.2164 0.0263  -0.0050 -0.0356 984  HIS B N   
16186 C CA  . HIS B 986  ? 0.2524 0.2076 0.2257 0.0243  -0.0073 -0.0360 984  HIS B CA  
16187 C C   . HIS B 986  ? 0.2397 0.1974 0.2181 0.0217  -0.0083 -0.0341 984  HIS B C   
16188 O O   . HIS B 986  ? 0.2435 0.1991 0.2239 0.0211  -0.0089 -0.0335 984  HIS B O   
16189 C CB  . HIS B 986  ? 0.2595 0.2118 0.2286 0.0231  -0.0087 -0.0374 984  HIS B CB  
16190 C CG  . HIS B 986  ? 0.3144 0.2617 0.2831 0.0206  -0.0114 -0.0377 984  HIS B CG  
16191 N ND1 . HIS B 986  ? 0.3905 0.3342 0.3550 0.0193  -0.0131 -0.0390 984  HIS B ND1 
16192 C CD2 . HIS B 986  ? 0.3161 0.2615 0.2877 0.0189  -0.0127 -0.0367 984  HIS B CD2 
16193 C CE1 . HIS B 986  ? 0.3606 0.3007 0.3259 0.0169  -0.0154 -0.0389 984  HIS B CE1 
16194 N NE2 . HIS B 986  ? 0.3391 0.2803 0.3088 0.0166  -0.0151 -0.0374 984  HIS B NE2 
16195 N N   . VAL B 987  ? 0.2000 0.1623 0.1805 0.0202  -0.0083 -0.0331 985  VAL B N   
16196 C CA  . VAL B 987  ? 0.2389 0.2032 0.2237 0.0178  -0.0093 -0.0315 985  VAL B CA  
16197 C C   . VAL B 987  ? 0.2418 0.2087 0.2306 0.0185  -0.0081 -0.0302 985  VAL B C   
16198 O O   . VAL B 987  ? 0.2442 0.2101 0.2356 0.0172  -0.0090 -0.0294 985  VAL B O   
16199 C CB  . VAL B 987  ? 0.2255 0.1935 0.2113 0.0163  -0.0096 -0.0309 985  VAL B CB  
16200 C CG1 . VAL B 987  ? 0.2542 0.2248 0.2447 0.0144  -0.0102 -0.0292 985  VAL B CG1 
16201 C CG2 . VAL B 987  ? 0.2258 0.1907 0.2079 0.0152  -0.0113 -0.0320 985  VAL B CG2 
16202 N N   . THR B 988  ? 0.2252 0.1956 0.2144 0.0204  -0.0062 -0.0300 986  THR B N   
16203 C CA  . THR B 988  ? 0.2385 0.2115 0.2311 0.0209  -0.0053 -0.0286 986  THR B CA  
16204 C C   . THR B 988  ? 0.2558 0.2247 0.2479 0.0221  -0.0054 -0.0289 986  THR B C   
16205 O O   . THR B 988  ? 0.3232 0.2930 0.3183 0.0218  -0.0053 -0.0276 986  THR B O   
16206 C CB  . THR B 988  ? 0.2709 0.2491 0.2644 0.0225  -0.0034 -0.0282 986  THR B CB  
16207 O OG1 . THR B 988  ? 0.2926 0.2699 0.2830 0.0250  -0.0023 -0.0293 986  THR B OG1 
16208 C CG2 . THR B 988  ? 0.2584 0.2403 0.2525 0.0209  -0.0033 -0.0277 986  THR B CG2 
16209 N N   . SER B 989  ? 0.2542 0.2184 0.2425 0.0235  -0.0057 -0.0304 987  SER B N   
16210 C CA  . SER B 989  ? 0.2801 0.2394 0.2675 0.0244  -0.0061 -0.0306 987  SER B CA  
16211 C C   . SER B 989  ? 0.3209 0.2765 0.3093 0.0217  -0.0081 -0.0301 987  SER B C   
16212 O O   . SER B 989  ? 0.3516 0.3041 0.3405 0.0218  -0.0084 -0.0296 987  SER B O   
16213 C CB  . SER B 989  ? 0.3225 0.2774 0.3050 0.0270  -0.0057 -0.0324 987  SER B CB  
16214 O OG  . SER B 989  ? 0.3756 0.3261 0.3546 0.0257  -0.0073 -0.0339 987  SER B OG  
16215 N N   . ARG B 990  ? 0.2408 0.1968 0.2296 0.0192  -0.0094 -0.0302 988  ARG B N   
16216 C CA  . ARG B 990  ? 0.2287 0.1814 0.2183 0.0166  -0.0114 -0.0299 988  ARG B CA  
16217 C C   . ARG B 990  ? 0.2393 0.1964 0.2337 0.0143  -0.0118 -0.0281 988  ARG B C   
16218 O O   . ARG B 990  ? 0.2458 0.2013 0.2421 0.0125  -0.0129 -0.0273 988  ARG B O   
16219 C CB  . ARG B 990  ? 0.2827 0.2320 0.2687 0.0154  -0.0131 -0.0314 988  ARG B CB  
16220 C CG  . ARG B 990  ? 0.3578 0.3026 0.3385 0.0177  -0.0128 -0.0334 988  ARG B CG  
16221 C CD  . ARG B 990  ? 0.3544 0.2925 0.3329 0.0180  -0.0136 -0.0340 988  ARG B CD  
16222 N NE  . ARG B 990  ? 0.3062 0.2392 0.2823 0.0156  -0.0161 -0.0349 988  ARG B NE  
16223 C CZ  . ARG B 990  ? 0.3106 0.2370 0.2845 0.0151  -0.0174 -0.0354 988  ARG B CZ  
16224 N NH1 . ARG B 990  ? 0.3346 0.2584 0.3084 0.0168  -0.0164 -0.0351 988  ARG B NH1 
16225 N NH2 . ARG B 990  ? 0.3289 0.2508 0.3004 0.0126  -0.0197 -0.0363 988  ARG B NH2 
16226 N N   . ILE B 991  ? 0.2147 0.1771 0.2111 0.0145  -0.0108 -0.0275 989  ILE B N   
16227 C CA  . ILE B 991  ? 0.2084 0.1747 0.2091 0.0127  -0.0109 -0.0260 989  ILE B CA  
16228 C C   . ILE B 991  ? 0.2256 0.1932 0.2290 0.0132  -0.0099 -0.0247 989  ILE B C   
16229 O O   . ILE B 991  ? 0.2384 0.2060 0.2409 0.0152  -0.0086 -0.0247 989  ILE B O   
16230 C CB  . ILE B 991  ? 0.2211 0.1919 0.2224 0.0129  -0.0102 -0.0258 989  ILE B CB  
16231 C CG1 . ILE B 991  ? 0.2723 0.2462 0.2773 0.0111  -0.0108 -0.0246 989  ILE B CG1 
16232 C CG2 . ILE B 991  ? 0.2511 0.2249 0.2526 0.0149  -0.0082 -0.0256 989  ILE B CG2 
16233 C CD1 . ILE B 991  ? 0.2927 0.2648 0.2978 0.0091  -0.0129 -0.0247 989  ILE B CD1 
16234 N N   . LYS B 992  ? 0.2167 0.1857 0.2235 0.0114  -0.0105 -0.0234 990  LYS B N   
16235 C CA  . LYS B 992  ? 0.2174 0.1876 0.2265 0.0115  -0.0096 -0.0220 990  LYS B CA  
16236 C C   . LYS B 992  ? 0.2341 0.2095 0.2467 0.0109  -0.0089 -0.0209 990  LYS B C   
16237 O O   . LYS B 992  ? 0.2751 0.2517 0.2904 0.0092  -0.0095 -0.0200 990  LYS B O   
16238 C CB  . LYS B 992  ? 0.2247 0.1915 0.2345 0.0099  -0.0107 -0.0214 990  LYS B CB  
16239 C CG  . LYS B 992  ? 0.2911 0.2518 0.2971 0.0105  -0.0116 -0.0226 990  LYS B CG  
16240 C CD  . LYS B 992  ? 0.4123 0.3694 0.4189 0.0083  -0.0130 -0.0219 990  LYS B CD  
16241 C CE  . LYS B 992  ? 0.4355 0.3941 0.4449 0.0079  -0.0122 -0.0200 990  LYS B CE  
16242 N NZ  . LYS B 992  ? 0.5432 0.4993 0.5538 0.0052  -0.0136 -0.0190 990  LYS B NZ  
16243 N N   . ALA B 993  ? 0.2210 0.1995 0.2334 0.0122  -0.0077 -0.0211 991  ALA B N   
16244 C CA  . ALA B 993  ? 0.1825 0.1652 0.1974 0.0118  -0.0070 -0.0203 991  ALA B CA  
16245 C C   . ALA B 993  ? 0.1972 0.1824 0.2122 0.0134  -0.0055 -0.0199 991  ALA B C   
16246 O O   . ALA B 993  ? 0.2047 0.1891 0.2176 0.0149  -0.0049 -0.0205 991  ALA B O   
16247 C CB  . ALA B 993  ? 0.2316 0.2159 0.2464 0.0112  -0.0076 -0.0207 991  ALA B CB  
16248 N N   . GLY B 994  ? 0.1779 0.1661 0.1951 0.0130  -0.0048 -0.0190 992  GLY B N   
16249 C CA  . GLY B 994  ? 0.1770 0.1675 0.1943 0.0142  -0.0036 -0.0186 992  GLY B CA  
16250 C C   . GLY B 994  ? 0.1689 0.1620 0.1854 0.0148  -0.0030 -0.0191 992  GLY B C   
16251 O O   . GLY B 994  ? 0.1699 0.1646 0.1858 0.0159  -0.0022 -0.0189 992  GLY B O   
16252 N N   . ASN B 995  ? 0.1692 0.1627 0.1855 0.0139  -0.0036 -0.0195 993  ASN B N   
16253 C CA  . ASN B 995  ? 0.1653 0.1611 0.1807 0.0140  -0.0031 -0.0198 993  ASN B CA  
16254 C C   . ASN B 995  ? 0.1627 0.1569 0.1762 0.0137  -0.0039 -0.0206 993  ASN B C   
16255 O O   . ASN B 995  ? 0.1734 0.1665 0.1873 0.0126  -0.0049 -0.0207 993  ASN B O   
16256 C CB  . ASN B 995  ? 0.1699 0.1678 0.1869 0.0130  -0.0031 -0.0192 993  ASN B CB  
16257 C CG  . ASN B 995  ? 0.1823 0.1822 0.2002 0.0134  -0.0021 -0.0186 993  ASN B CG  
16258 O OD1 . ASN B 995  ? 0.1712 0.1708 0.1904 0.0134  -0.0020 -0.0180 993  ASN B OD1 
16259 N ND2 . ASN B 995  ? 0.1787 0.1809 0.1959 0.0137  -0.0016 -0.0186 993  ASN B ND2 
16260 N N   . LEU B 996  ? 0.1778 0.1723 0.1892 0.0148  -0.0033 -0.0212 994  LEU B N   
16261 C CA  . LEU B 996  ? 0.1624 0.1556 0.1714 0.0148  -0.0038 -0.0221 994  LEU B CA  
16262 C C   . LEU B 996  ? 0.1652 0.1613 0.1735 0.0145  -0.0032 -0.0220 994  LEU B C   
16263 O O   . LEU B 996  ? 0.1628 0.1618 0.1718 0.0149  -0.0022 -0.0215 994  LEU B O   
16264 C CB  . LEU B 996  ? 0.1663 0.1574 0.1730 0.0164  -0.0035 -0.0229 994  LEU B CB  
16265 C CG  . LEU B 996  ? 0.1929 0.1811 0.2002 0.0168  -0.0039 -0.0229 994  LEU B CG  
16266 C CD1 . LEU B 996  ? 0.2281 0.2136 0.2326 0.0187  -0.0035 -0.0239 994  LEU B CD1 
16267 C CD2 . LEU B 996  ? 0.1913 0.1769 0.1994 0.0151  -0.0053 -0.0229 994  LEU B CD2 
16268 N N   . TYR B 997  ? 0.1523 0.1476 0.1591 0.0137  -0.0039 -0.0223 995  TYR B N   
16269 C CA  . TYR B 997  ? 0.1721 0.1697 0.1780 0.0130  -0.0035 -0.0220 995  TYR B CA  
16270 C C   . TYR B 997  ? 0.1577 0.1540 0.1605 0.0132  -0.0038 -0.0227 995  TYR B C   
16271 O O   . TYR B 997  ? 0.1932 0.1866 0.1950 0.0127  -0.0050 -0.0232 995  TYR B O   
16272 C CB  . TYR B 997  ? 0.1845 0.1823 0.1917 0.0115  -0.0043 -0.0213 995  TYR B CB  
16273 C CG  . TYR B 997  ? 0.1643 0.1629 0.1743 0.0114  -0.0041 -0.0207 995  TYR B CG  
16274 C CD1 . TYR B 997  ? 0.1700 0.1669 0.1815 0.0114  -0.0047 -0.0207 995  TYR B CD1 
16275 C CD2 . TYR B 997  ? 0.1929 0.1940 0.2036 0.0112  -0.0033 -0.0202 995  TYR B CD2 
16276 C CE1 . TYR B 997  ? 0.2046 0.2024 0.2184 0.0114  -0.0044 -0.0201 995  TYR B CE1 
16277 C CE2 . TYR B 997  ? 0.1847 0.1864 0.1974 0.0111  -0.0031 -0.0197 995  TYR B CE2 
16278 C CZ  . TYR B 997  ? 0.2045 0.2046 0.2188 0.0113  -0.0036 -0.0197 995  TYR B CZ  
16279 O OH  . TYR B 997  ? 0.2365 0.2373 0.2526 0.0113  -0.0032 -0.0192 995  TYR B OH  
16280 N N   . ILE B 998  ? 0.1770 0.1756 0.1782 0.0138  -0.0027 -0.0228 996  ILE B N   
16281 C CA  A ILE B 998  ? 0.1827 0.1804 0.1806 0.0142  -0.0026 -0.0236 996  ILE B CA  
16282 C CA  B ILE B 998  ? 0.1829 0.1806 0.1808 0.0141  -0.0026 -0.0236 996  ILE B CA  
16283 C C   . ILE B 998  ? 0.1770 0.1770 0.1739 0.0128  -0.0024 -0.0228 996  ILE B C   
16284 O O   . ILE B 998  ? 0.1859 0.1894 0.1838 0.0127  -0.0013 -0.0221 996  ILE B O   
16285 C CB  A ILE B 998  ? 0.2075 0.2061 0.2040 0.0163  -0.0012 -0.0243 996  ILE B CB  
16286 C CB  B ILE B 998  ? 0.2075 0.2058 0.2039 0.0163  -0.0013 -0.0244 996  ILE B CB  
16287 C CG1 A ILE B 998  ? 0.2201 0.2164 0.2177 0.0176  -0.0014 -0.0248 996  ILE B CG1 
16288 C CG1 B ILE B 998  ? 0.2173 0.2121 0.2139 0.0174  -0.0018 -0.0251 996  ILE B CG1 
16289 C CG2 A ILE B 998  ? 0.2105 0.2076 0.2030 0.0169  -0.0011 -0.0253 996  ILE B CG2 
16290 C CG2 B ILE B 998  ? 0.2086 0.2070 0.2014 0.0167  -0.0008 -0.0250 996  ILE B CG2 
16291 C CD1 A ILE B 998  ? 0.2254 0.2168 0.2217 0.0173  -0.0029 -0.0256 996  ILE B CD1 
16292 C CD1 B ILE B 998  ? 0.2390 0.2342 0.2349 0.0198  -0.0006 -0.0257 996  ILE B CD1 
16293 N N   . ASN B 999  ? 0.1701 0.1681 0.1652 0.0117  -0.0035 -0.0229 997  ASN B N   
16294 C CA  . ASN B 999  ? 0.1882 0.1875 0.1817 0.0104  -0.0035 -0.0221 997  ASN B CA  
16295 C C   . ASN B 999  ? 0.1903 0.1912 0.1861 0.0090  -0.0036 -0.0209 997  ASN B C   
16296 O O   . ASN B 999  ? 0.1976 0.2008 0.1927 0.0081  -0.0030 -0.0200 997  ASN B O   
16297 C CB  . ASN B 999  ? 0.1940 0.1959 0.1851 0.0112  -0.0019 -0.0223 997  ASN B CB  
16298 C CG  . ASN B 999  ? 0.1989 0.1983 0.1867 0.0124  -0.0021 -0.0236 997  ASN B CG  
16299 O OD1 . ASN B 999  ? 0.2254 0.2214 0.2119 0.0119  -0.0036 -0.0241 997  ASN B OD1 
16300 N ND2 . ASN B 999  ? 0.2172 0.2184 0.2036 0.0142  -0.0005 -0.0243 997  ASN B ND2 
16301 N N   . ARG B 1000 ? 0.1819 0.1814 0.1802 0.0088  -0.0044 -0.0207 998  ARG B N   
16302 C CA  . ARG B 1000 ? 0.1641 0.1645 0.1644 0.0077  -0.0047 -0.0198 998  ARG B CA  
16303 C C   . ARG B 1000 ? 0.1980 0.1959 0.2002 0.0076  -0.0059 -0.0198 998  ARG B C   
16304 O O   . ARG B 1000 ? 0.2104 0.2065 0.2126 0.0082  -0.0067 -0.0204 998  ARG B O   
16305 C CB  . ARG B 1000 ? 0.1872 0.1904 0.1892 0.0081  -0.0034 -0.0195 998  ARG B CB  
16306 C CG  . ARG B 1000 ? 0.1854 0.1887 0.1889 0.0097  -0.0029 -0.0202 998  ARG B CG  
16307 C CD  . ARG B 1000 ? 0.1730 0.1784 0.1787 0.0098  -0.0022 -0.0198 998  ARG B CD  
16308 N NE  . ARG B 1000 ? 0.1691 0.1734 0.1764 0.0088  -0.0030 -0.0193 998  ARG B NE  
16309 C CZ  . ARG B 1000 ? 0.1941 0.1997 0.2028 0.0085  -0.0027 -0.0189 998  ARG B CZ  
16310 N NH1 . ARG B 1000 ? 0.1954 0.2040 0.2046 0.0089  -0.0017 -0.0187 998  ARG B NH1 
16311 N NH2 . ARG B 1000 ? 0.2212 0.2253 0.2308 0.0078  -0.0033 -0.0187 998  ARG B NH2 
16312 N N   . ASN B 1001 ? 0.1714 0.1694 0.1751 0.0069  -0.0062 -0.0192 999  ASN B N   
16313 C CA  . ASN B 1001 ? 0.1693 0.1657 0.1751 0.0071  -0.0071 -0.0192 999  ASN B CA  
16314 C C   . ASN B 1001 ? 0.1755 0.1726 0.1835 0.0081  -0.0065 -0.0196 999  ASN B C   
16315 O O   . ASN B 1001 ? 0.1937 0.1924 0.2015 0.0087  -0.0054 -0.0198 999  ASN B O   
16316 C CB  . ASN B 1001 ? 0.1728 0.1689 0.1794 0.0064  -0.0074 -0.0185 999  ASN B CB  
16317 C CG  . ASN B 1001 ? 0.2116 0.2095 0.2192 0.0063  -0.0063 -0.0183 999  ASN B CG  
16318 O OD1 . ASN B 1001 ? 0.2192 0.2182 0.2284 0.0070  -0.0056 -0.0186 999  ASN B OD1 
16319 N ND2 . ASN B 1001 ? 0.3135 0.3115 0.3199 0.0051  -0.0062 -0.0178 999  ASN B ND2 
16320 N N   . ILE B 1002 ? 0.1748 0.1708 0.1848 0.0083  -0.0071 -0.0196 1000 ILE B N   
16321 C CA  . ILE B 1002 ? 0.1723 0.1685 0.1841 0.0090  -0.0067 -0.0198 1000 ILE B CA  
16322 C C   . ILE B 1002 ? 0.1952 0.1925 0.2093 0.0091  -0.0062 -0.0194 1000 ILE B C   
16323 O O   . ILE B 1002 ? 0.2026 0.1999 0.2186 0.0095  -0.0060 -0.0193 1000 ILE B O   
16324 C CB  . ILE B 1002 ? 0.1881 0.1826 0.2004 0.0091  -0.0077 -0.0202 1000 ILE B CB  
16325 C CG1 . ILE B 1002 ? 0.1675 0.1614 0.1815 0.0086  -0.0089 -0.0197 1000 ILE B CG1 
16326 C CG2 . ILE B 1002 ? 0.2093 0.2025 0.2188 0.0092  -0.0081 -0.0208 1000 ILE B CG2 
16327 C CD1 . ILE B 1002 ? 0.1932 0.1860 0.2084 0.0084  -0.0099 -0.0198 1000 ILE B CD1 
16328 N N   . ILE B 1003 ? 0.1979 0.1958 0.2117 0.0087  -0.0059 -0.0190 1001 ILE B N   
16329 C CA  . ILE B 1003 ? 0.2053 0.2037 0.2207 0.0088  -0.0055 -0.0188 1001 ILE B CA  
16330 C C   . ILE B 1003 ? 0.2399 0.2401 0.2550 0.0088  -0.0044 -0.0187 1001 ILE B C   
16331 O O   . ILE B 1003 ? 0.2509 0.2515 0.2667 0.0088  -0.0041 -0.0186 1001 ILE B O   
16332 C CB  . ILE B 1003 ? 0.2127 0.2100 0.2283 0.0085  -0.0062 -0.0185 1001 ILE B CB  
16333 C CG1 . ILE B 1003 ? 0.3112 0.3078 0.3243 0.0076  -0.0065 -0.0184 1001 ILE B CG1 
16334 C CG2 . ILE B 1003 ? 0.2223 0.2184 0.2389 0.0087  -0.0074 -0.0185 1001 ILE B CG2 
16335 C CD1 . ILE B 1003 ? 0.3873 0.3822 0.4002 0.0074  -0.0072 -0.0181 1001 ILE B CD1 
16336 N N   . GLY B 1004 ? 0.2293 0.2307 0.2433 0.0089  -0.0039 -0.0189 1002 GLY B N   
16337 C CA  . GLY B 1004 ? 0.2316 0.2352 0.2455 0.0089  -0.0031 -0.0187 1002 GLY B CA  
16338 C C   . GLY B 1004 ? 0.2359 0.2403 0.2513 0.0098  -0.0025 -0.0186 1002 GLY B C   
16339 O O   . GLY B 1004 ? 0.2429 0.2469 0.2590 0.0106  -0.0024 -0.0187 1002 GLY B O   
16340 N N   . ALA B 1005 ? 0.2089 0.2142 0.2246 0.0094  -0.0022 -0.0184 1003 ALA B N   
16341 C CA  . ALA B 1005 ? 0.2222 0.2284 0.2390 0.0101  -0.0016 -0.0182 1003 ALA B CA  
16342 C C   . ALA B 1005 ? 0.2329 0.2413 0.2490 0.0097  -0.0012 -0.0180 1003 ALA B C   
16343 O O   . ALA B 1005 ? 0.2449 0.2537 0.2613 0.0097  -0.0010 -0.0179 1003 ALA B O   
16344 C CB  . ALA B 1005 ? 0.2475 0.2524 0.2654 0.0103  -0.0016 -0.0182 1003 ALA B CB  
16345 N N   . VAL B 1006 ? 0.1928 0.2028 0.2080 0.0091  -0.0012 -0.0179 1004 VAL B N   
16346 C CA  . VAL B 1006 ? 0.1892 0.2017 0.2040 0.0084  -0.0011 -0.0176 1004 VAL B CA  
16347 C C   . VAL B 1006 ? 0.1723 0.1866 0.1880 0.0095  -0.0006 -0.0173 1004 VAL B C   
16348 O O   . VAL B 1006 ? 0.1800 0.1951 0.1963 0.0107  -0.0002 -0.0171 1004 VAL B O   
16349 C CB  . VAL B 1006 ? 0.1940 0.2085 0.2079 0.0076  -0.0011 -0.0174 1004 VAL B CB  
16350 C CG1 . VAL B 1006 ? 0.2117 0.2294 0.2256 0.0066  -0.0010 -0.0169 1004 VAL B CG1 
16351 C CG2 . VAL B 1006 ? 0.2173 0.2297 0.2301 0.0063  -0.0017 -0.0175 1004 VAL B CG2 
16352 N N   . VAL B 1007 ? 0.1982 0.2128 0.2136 0.0090  -0.0006 -0.0172 1005 VAL B N   
16353 C CA  . VAL B 1007 ? 0.1924 0.2085 0.2085 0.0100  -0.0003 -0.0167 1005 VAL B CA  
16354 C C   . VAL B 1007 ? 0.2019 0.2214 0.2184 0.0106  -0.0001 -0.0162 1005 VAL B C   
16355 O O   . VAL B 1007 ? 0.1880 0.2098 0.2041 0.0096  -0.0003 -0.0161 1005 VAL B O   
16356 C CB  . VAL B 1007 ? 0.1764 0.1924 0.1916 0.0092  -0.0004 -0.0168 1005 VAL B CB  
16357 C CG1 . VAL B 1007 ? 0.2072 0.2250 0.2228 0.0101  -0.0001 -0.0162 1005 VAL B CG1 
16358 C CG2 . VAL B 1007 ? 0.2046 0.2175 0.2196 0.0092  -0.0004 -0.0173 1005 VAL B CG2 
16359 N N   . GLY B 1008 ? 0.1718 0.1916 0.1891 0.0122  0.0003  -0.0159 1006 GLY B N   
16360 C CA  . GLY B 1008 ? 0.2099 0.2329 0.2276 0.0132  0.0005  -0.0153 1006 GLY B CA  
16361 C C   . GLY B 1008 ? 0.2019 0.2257 0.2196 0.0136  0.0007  -0.0156 1006 GLY B C   
16362 O O   . GLY B 1008 ? 0.2216 0.2485 0.2399 0.0146  0.0011  -0.0152 1006 GLY B O   
16363 N N   . VAL B 1009 ? 0.1752 0.1966 0.1923 0.0128  0.0006  -0.0162 1007 VAL B N   
16364 C CA  . VAL B 1009 ? 0.1847 0.2067 0.2014 0.0130  0.0008  -0.0165 1007 VAL B CA  
16365 C C   . VAL B 1009 ? 0.1991 0.2173 0.2153 0.0139  0.0008  -0.0171 1007 VAL B C   
16366 O O   . VAL B 1009 ? 0.1964 0.2145 0.2123 0.0154  0.0012  -0.0174 1007 VAL B O   
16367 C CB  . VAL B 1009 ? 0.1815 0.2043 0.1974 0.0110  0.0005  -0.0165 1007 VAL B CB  
16368 C CG1 . VAL B 1009 ? 0.1995 0.2231 0.2146 0.0112  0.0009  -0.0167 1007 VAL B CG1 
16369 C CG2 . VAL B 1009 ? 0.1946 0.2210 0.2108 0.0098  0.0004  -0.0159 1007 VAL B CG2 
16370 N N   . GLN B 1010 ? 0.1853 0.2005 0.2015 0.0131  0.0003  -0.0174 1008 GLN B N   
16371 C CA  . GLN B 1010 ? 0.2017 0.2134 0.2179 0.0137  0.0001  -0.0178 1008 GLN B CA  
16372 C C   . GLN B 1010 ? 0.1957 0.2064 0.2129 0.0138  0.0000  -0.0174 1008 GLN B C   
16373 O O   . GLN B 1010 ? 0.2235 0.2328 0.2412 0.0129  -0.0003 -0.0175 1008 GLN B O   
16374 C CB  . GLN B 1010 ? 0.2046 0.2142 0.2202 0.0127  -0.0005 -0.0183 1008 GLN B CB  
16375 C CG  . GLN B 1010 ? 0.2407 0.2511 0.2549 0.0124  -0.0005 -0.0185 1008 GLN B CG  
16376 C CD  . GLN B 1010 ? 0.2074 0.2191 0.2211 0.0108  -0.0007 -0.0183 1008 GLN B CD  
16377 O OE1 . GLN B 1010 ? 0.2107 0.2211 0.2246 0.0098  -0.0012 -0.0182 1008 GLN B OE1 
16378 N NE2 . GLN B 1010 ? 0.2131 0.2273 0.2260 0.0105  -0.0003 -0.0181 1008 GLN B NE2 
16379 N N   . PRO B 1011 ? 0.1742 0.1858 0.1919 0.0149  0.0004  -0.0170 1009 PRO B N   
16380 C CA  . PRO B 1011 ? 0.2023 0.2125 0.2208 0.0151  0.0004  -0.0165 1009 PRO B CA  
16381 C C   . PRO B 1011 ? 0.1714 0.1786 0.1903 0.0147  0.0001  -0.0168 1009 PRO B C   
16382 O O   . PRO B 1011 ? 0.1699 0.1754 0.1884 0.0151  -0.0002 -0.0172 1009 PRO B O   
16383 C CB  . PRO B 1011 ? 0.1937 0.2044 0.2122 0.0166  0.0008  -0.0159 1009 PRO B CB  
16384 C CG  . PRO B 1011 ? 0.1950 0.2088 0.2132 0.0172  0.0010  -0.0160 1009 PRO B CG  
16385 C CD  . PRO B 1011 ? 0.1934 0.2069 0.2109 0.0163  0.0008  -0.0167 1009 PRO B CD  
16386 N N   . PHE B 1012 ? 0.1612 0.1679 0.1810 0.0139  0.0000  -0.0166 1010 PHE B N   
16387 C CA  . PHE B 1012 ? 0.1662 0.1709 0.1866 0.0133  -0.0005 -0.0169 1010 PHE B CA  
16388 C C   . PHE B 1012 ? 0.1931 0.1966 0.2147 0.0133  -0.0004 -0.0163 1010 PHE B C   
16389 O O   . PHE B 1012 ? 0.1901 0.1947 0.2123 0.0134  0.0002  -0.0157 1010 PHE B O   
16390 C CB  . PHE B 1012 ? 0.1780 0.1831 0.1985 0.0124  -0.0007 -0.0172 1010 PHE B CB  
16391 C CG  . PHE B 1012 ? 0.1559 0.1594 0.1772 0.0119  -0.0013 -0.0174 1010 PHE B CG  
16392 C CD1 . PHE B 1012 ? 0.1918 0.1943 0.2122 0.0117  -0.0020 -0.0179 1010 PHE B CD1 
16393 C CD2 . PHE B 1012 ? 0.2042 0.2075 0.2272 0.0118  -0.0013 -0.0170 1010 PHE B CD2 
16394 C CE1 . PHE B 1012 ? 0.1760 0.1772 0.1971 0.0112  -0.0028 -0.0181 1010 PHE B CE1 
16395 C CE2 . PHE B 1012 ? 0.2016 0.2039 0.2256 0.0114  -0.0020 -0.0171 1010 PHE B CE2 
16396 C CZ  . PHE B 1012 ? 0.1906 0.1918 0.2137 0.0111  -0.0029 -0.0176 1010 PHE B CZ  
16397 N N   . GLY B 1013 ? 0.1617 0.1631 0.1837 0.0132  -0.0010 -0.0164 1011 GLY B N   
16398 C CA  . GLY B 1013 ? 0.1674 0.1678 0.1908 0.0128  -0.0010 -0.0157 1011 GLY B CA  
16399 C C   . GLY B 1013 ? 0.1760 0.1738 0.1991 0.0127  -0.0018 -0.0159 1011 GLY B C   
16400 O O   . GLY B 1013 ? 0.1866 0.1832 0.2080 0.0135  -0.0019 -0.0165 1011 GLY B O   
16401 N N   . GLY B 1014 ? 0.1978 0.1946 0.2224 0.0117  -0.0023 -0.0155 1012 GLY B N   
16402 C CA  . GLY B 1014 ? 0.2006 0.1944 0.2246 0.0113  -0.0033 -0.0158 1012 GLY B CA  
16403 C C   . GLY B 1014 ? 0.2201 0.2121 0.2447 0.0108  -0.0033 -0.0148 1012 GLY B C   
16404 O O   . GLY B 1014 ? 0.2368 0.2300 0.2621 0.0110  -0.0025 -0.0138 1012 GLY B O   
16405 N N   . ARG B 1015 ? 0.2137 0.2028 0.2380 0.0100  -0.0045 -0.0150 1013 ARG B N   
16406 C CA  . ARG B 1015 ? 0.2224 0.2089 0.2468 0.0092  -0.0048 -0.0142 1013 ARG B CA  
16407 C C   . ARG B 1015 ? 0.2148 0.2011 0.2412 0.0072  -0.0059 -0.0138 1013 ARG B C   
16408 O O   . ARG B 1015 ? 0.1996 0.1879 0.2273 0.0067  -0.0064 -0.0142 1013 ARG B O   
16409 C CB  . ARG B 1015 ? 0.2223 0.2045 0.2438 0.0102  -0.0054 -0.0150 1013 ARG B CB  
16410 C CG  . ARG B 1015 ? 0.2630 0.2434 0.2828 0.0100  -0.0065 -0.0165 1013 ARG B CG  
16411 C CD  . ARG B 1015 ? 0.2965 0.2716 0.3138 0.0101  -0.0075 -0.0171 1013 ARG B CD  
16412 N NE  . ARG B 1015 ? 0.3457 0.3187 0.3642 0.0078  -0.0087 -0.0164 1013 ARG B NE  
16413 C CZ  . ARG B 1015 ? 0.3567 0.3300 0.3762 0.0061  -0.0100 -0.0167 1013 ARG B CZ  
16414 N NH1 . ARG B 1015 ? 0.3070 0.2822 0.3263 0.0063  -0.0103 -0.0176 1013 ARG B NH1 
16415 N NH2 . ARG B 1015 ? 0.4109 0.3827 0.4318 0.0039  -0.0111 -0.0158 1013 ARG B NH2 
16416 N N   . GLY B 1016 ? 0.2119 0.1958 0.2386 0.0060  -0.0065 -0.0129 1014 GLY B N   
16417 C CA  . GLY B 1016 ? 0.2012 0.1854 0.2302 0.0038  -0.0076 -0.0124 1014 GLY B CA  
16418 C C   . GLY B 1016 ? 0.2143 0.2035 0.2468 0.0033  -0.0067 -0.0113 1014 GLY B C   
16419 O O   . GLY B 1016 ? 0.2255 0.2168 0.2586 0.0039  -0.0053 -0.0104 1014 GLY B O   
16420 N N   . LEU B 1017 ? 0.2000 0.1910 0.2344 0.0023  -0.0076 -0.0115 1015 LEU B N   
16421 C CA  . LEU B 1017 ? 0.2183 0.2142 0.2561 0.0021  -0.0069 -0.0107 1015 LEU B CA  
16422 C C   . LEU B 1017 ? 0.2015 0.1995 0.2385 0.0041  -0.0056 -0.0114 1015 LEU B C   
16423 O O   . LEU B 1017 ? 0.1929 0.1945 0.2322 0.0044  -0.0048 -0.0109 1015 LEU B O   
16424 C CB  . LEU B 1017 ? 0.2042 0.2015 0.2442 0.0008  -0.0084 -0.0108 1015 LEU B CB  
16425 C CG  . LEU B 1017 ? 0.2354 0.2310 0.2764 -0.0016 -0.0099 -0.0100 1015 LEU B CG  
16426 C CD1 . LEU B 1017 ? 0.2454 0.2426 0.2884 -0.0027 -0.0116 -0.0101 1015 LEU B CD1 
16427 C CD2 . LEU B 1017 ? 0.2624 0.2603 0.3060 -0.0026 -0.0088 -0.0081 1015 LEU B CD2 
16428 N N   . SER B 1018 ? 0.1759 0.1718 0.2099 0.0054  -0.0055 -0.0125 1016 SER B N   
16429 C CA  . SER B 1018 ? 0.1797 0.1775 0.2129 0.0069  -0.0046 -0.0132 1016 SER B CA  
16430 C C   . SER B 1018 ? 0.1644 0.1631 0.1968 0.0079  -0.0030 -0.0128 1016 SER B C   
16431 O O   . SER B 1018 ? 0.2054 0.2058 0.2374 0.0088  -0.0022 -0.0132 1016 SER B O   
16432 C CB  . SER B 1018 ? 0.1780 0.1737 0.2085 0.0076  -0.0053 -0.0146 1016 SER B CB  
16433 O OG  . SER B 1018 ? 0.1805 0.1757 0.2115 0.0067  -0.0067 -0.0150 1016 SER B OG  
16434 N N   . GLY B 1019 ? 0.1699 0.1672 0.2019 0.0077  -0.0027 -0.0119 1017 GLY B N   
16435 C CA  . GLY B 1019 ? 0.1811 0.1794 0.2121 0.0087  -0.0014 -0.0114 1017 GLY B CA  
16436 C C   . GLY B 1019 ? 0.1804 0.1767 0.2107 0.0085  -0.0012 -0.0104 1017 GLY B C   
16437 O O   . GLY B 1019 ? 0.2182 0.2112 0.2477 0.0080  -0.0022 -0.0104 1017 GLY B O   
16438 N N   . THR B 1020 ? 0.1906 0.1886 0.2209 0.0090  0.0000  -0.0094 1018 THR B N   
16439 C CA  . THR B 1020 ? 0.1948 0.1910 0.2238 0.0093  0.0003  -0.0084 1018 THR B CA  
16440 C C   . THR B 1020 ? 0.2200 0.2153 0.2465 0.0110  0.0003  -0.0091 1018 THR B C   
16441 O O   . THR B 1020 ? 0.2189 0.2117 0.2440 0.0116  0.0001  -0.0085 1018 THR B O   
16442 C CB  . THR B 1020 ? 0.2149 0.2136 0.2447 0.0090  0.0015  -0.0070 1018 THR B CB  
16443 O OG1 . THR B 1020 ? 0.1852 0.1868 0.2145 0.0100  0.0024  -0.0076 1018 THR B OG1 
16444 C CG2 . THR B 1020 ? 0.1953 0.1956 0.2279 0.0073  0.0017  -0.0060 1018 THR B CG2 
16445 N N   . GLY B 1021 ? 0.1899 0.1874 0.2161 0.0118  0.0006  -0.0102 1019 GLY B N   
16446 C CA  . GLY B 1021 ? 0.2040 0.2020 0.2284 0.0133  0.0009  -0.0105 1019 GLY B CA  
16447 C C   . GLY B 1021 ? 0.1939 0.1937 0.2180 0.0136  0.0018  -0.0093 1019 GLY B C   
16448 O O   . GLY B 1021 ? 0.1966 0.1970 0.2217 0.0127  0.0023  -0.0082 1019 GLY B O   
16449 N N   . PRO B 1022 ? 0.1866 0.1876 0.2093 0.0148  0.0020  -0.0094 1020 PRO B N   
16450 C CA  . PRO B 1022 ? 0.1746 0.1758 0.1962 0.0159  0.0016  -0.0105 1020 PRO B CA  
16451 C C   . PRO B 1022 ? 0.1977 0.2009 0.2198 0.0154  0.0016  -0.0117 1020 PRO B C   
16452 O O   . PRO B 1022 ? 0.2074 0.2118 0.2303 0.0145  0.0020  -0.0117 1020 PRO B O   
16453 C CB  . PRO B 1022 ? 0.2124 0.2153 0.2330 0.0171  0.0019  -0.0097 1020 PRO B CB  
16454 C CG  . PRO B 1022 ? 0.1993 0.2039 0.2201 0.0163  0.0026  -0.0089 1020 PRO B CG  
16455 C CD  . PRO B 1022 ? 0.1959 0.1986 0.2179 0.0152  0.0027  -0.0083 1020 PRO B CD  
16456 N N   . LYS B 1023 ? 0.1720 0.1753 0.1934 0.0159  0.0012  -0.0126 1021 LYS B N   
16457 C CA  . LYS B 1023 ? 0.1809 0.1855 0.2024 0.0153  0.0011  -0.0137 1021 LYS B CA  
16458 C C   . LYS B 1023 ? 0.1802 0.1874 0.2013 0.0151  0.0015  -0.0136 1021 LYS B C   
16459 O O   . LYS B 1023 ? 0.1774 0.1862 0.1977 0.0157  0.0017  -0.0132 1021 LYS B O   
16460 C CB  . LYS B 1023 ? 0.1672 0.1718 0.1878 0.0159  0.0007  -0.0145 1021 LYS B CB  
16461 C CG  . LYS B 1023 ? 0.1730 0.1747 0.1934 0.0160  0.0001  -0.0150 1021 LYS B CG  
16462 C CD  . LYS B 1023 ? 0.1598 0.1620 0.1790 0.0169  0.0001  -0.0158 1021 LYS B CD  
16463 C CE  . LYS B 1023 ? 0.1983 0.1977 0.2166 0.0169  -0.0005 -0.0166 1021 LYS B CE  
16464 N NZ  . LYS B 1023 ? 0.1909 0.1903 0.2096 0.0156  -0.0010 -0.0172 1021 LYS B NZ  
16465 N N   . ALA B 1024 ? 0.1910 0.1987 0.2126 0.0142  0.0016  -0.0141 1022 ALA B N   
16466 C CA  . ALA B 1024 ? 0.1831 0.1925 0.2038 0.0139  0.0018  -0.0145 1022 ALA B CA  
16467 C C   . ALA B 1024 ? 0.1702 0.1807 0.1901 0.0139  0.0013  -0.0150 1022 ALA B C   
16468 O O   . ALA B 1024 ? 0.1796 0.1893 0.1995 0.0140  0.0009  -0.0154 1022 ALA B O   
16469 C CB  . ALA B 1024 ? 0.2029 0.2118 0.2241 0.0132  0.0018  -0.0150 1022 ALA B CB  
16470 N N   . GLY B 1025 ? 0.1477 0.1601 0.1665 0.0137  0.0014  -0.0150 1023 GLY B N   
16471 C CA  . GLY B 1025 ? 0.1814 0.1954 0.1996 0.0134  0.0010  -0.0153 1023 GLY B CA  
16472 C C   . GLY B 1025 ? 0.1639 0.1790 0.1824 0.0146  0.0010  -0.0149 1023 GLY B C   
16473 O O   . GLY B 1025 ? 0.1813 0.1977 0.1996 0.0145  0.0008  -0.0152 1023 GLY B O   
16474 N N   . GLY B 1026 ? 0.1914 0.2058 0.2103 0.0156  0.0012  -0.0142 1024 GLY B N   
16475 C CA  . GLY B 1026 ? 0.1635 0.1782 0.1824 0.0171  0.0013  -0.0138 1024 GLY B CA  
16476 C C   . GLY B 1026 ? 0.1688 0.1848 0.1876 0.0180  0.0014  -0.0127 1024 GLY B C   
16477 O O   . GLY B 1026 ? 0.1689 0.1852 0.1874 0.0174  0.0015  -0.0123 1024 GLY B O   
16478 N N   . PRO B 1027 ? 0.1800 0.1968 0.1988 0.0196  0.0013  -0.0122 1025 PRO B N   
16479 C CA  . PRO B 1027 ? 0.1652 0.1840 0.1838 0.0206  0.0013  -0.0111 1025 PRO B CA  
16480 C C   . PRO B 1027 ? 0.1648 0.1810 0.1831 0.0212  0.0014  -0.0101 1025 PRO B C   
16481 O O   . PRO B 1027 ? 0.1699 0.1874 0.1878 0.0218  0.0013  -0.0090 1025 PRO B O   
16482 C CB  . PRO B 1027 ? 0.1950 0.2157 0.2140 0.0224  0.0013  -0.0110 1025 PRO B CB  
16483 C CG  . PRO B 1027 ? 0.2122 0.2298 0.2310 0.0228  0.0014  -0.0120 1025 PRO B CG  
16484 C CD  . PRO B 1027 ? 0.2011 0.2177 0.2199 0.0207  0.0014  -0.0128 1025 PRO B CD  
16485 N N   . LEU B 1028 ? 0.1737 0.1862 0.1921 0.0208  0.0015  -0.0103 1026 LEU B N   
16486 C CA  . LEU B 1028 ? 0.1875 0.1975 0.2057 0.0210  0.0017  -0.0092 1026 LEU B CA  
16487 C C   . LEU B 1028 ? 0.1862 0.1966 0.2045 0.0194  0.0020  -0.0089 1026 LEU B C   
16488 O O   . LEU B 1028 ? 0.2023 0.2113 0.2203 0.0193  0.0023  -0.0078 1026 LEU B O   
16489 C CB  . LEU B 1028 ? 0.1850 0.1909 0.2034 0.0212  0.0015  -0.0094 1026 LEU B CB  
16490 C CG  . LEU B 1028 ? 0.2401 0.2448 0.2579 0.0230  0.0013  -0.0098 1026 LEU B CG  
16491 C CD1 . LEU B 1028 ? 0.2427 0.2428 0.2602 0.0230  0.0010  -0.0101 1026 LEU B CD1 
16492 C CD2 . LEU B 1028 ? 0.2905 0.2963 0.3078 0.0249  0.0012  -0.0086 1026 LEU B CD2 
16493 N N   . TYR B 1029 ? 0.1709 0.1828 0.1893 0.0182  0.0021  -0.0099 1027 TYR B N   
16494 C CA  . TYR B 1029 ? 0.1560 0.1677 0.1746 0.0170  0.0026  -0.0099 1027 TYR B CA  
16495 C C   . TYR B 1029 ? 0.1588 0.1719 0.1763 0.0170  0.0030  -0.0089 1027 TYR B C   
16496 O O   . TYR B 1029 ? 0.1655 0.1776 0.1830 0.0166  0.0035  -0.0082 1027 TYR B O   
16497 C CB  . TYR B 1029 ? 0.1795 0.1922 0.1980 0.0161  0.0025  -0.0113 1027 TYR B CB  
16498 C CG  . TYR B 1029 ? 0.1791 0.1911 0.1981 0.0151  0.0029  -0.0117 1027 TYR B CG  
16499 C CD1 . TYR B 1029 ? 0.1675 0.1777 0.1879 0.0148  0.0030  -0.0118 1027 TYR B CD1 
16500 C CD2 . TYR B 1029 ? 0.1846 0.1979 0.2026 0.0145  0.0032  -0.0122 1027 TYR B CD2 
16501 C CE1 . TYR B 1029 ? 0.1778 0.1879 0.1990 0.0141  0.0034  -0.0122 1027 TYR B CE1 
16502 C CE2 . TYR B 1029 ? 0.1724 0.1851 0.1908 0.0140  0.0036  -0.0127 1027 TYR B CE2 
16503 C CZ  . TYR B 1029 ? 0.1917 0.2030 0.2118 0.0139  0.0038  -0.0127 1027 TYR B CZ  
16504 O OH  . TYR B 1029 ? 0.2102 0.2214 0.2310 0.0136  0.0042  -0.0131 1027 TYR B OH  
16505 N N   . LEU B 1030 ? 0.1649 0.1804 0.1813 0.0173  0.0026  -0.0089 1028 LEU B N   
16506 C CA  . LEU B 1030 ? 0.1574 0.1743 0.1723 0.0172  0.0028  -0.0081 1028 LEU B CA  
16507 C C   . LEU B 1030 ? 0.1634 0.1792 0.1781 0.0180  0.0030  -0.0064 1028 LEU B C   
16508 O O   . LEU B 1030 ? 0.1759 0.1918 0.1896 0.0176  0.0035  -0.0056 1028 LEU B O   
16509 C CB  . LEU B 1030 ? 0.1786 0.1985 0.1925 0.0172  0.0021  -0.0082 1028 LEU B CB  
16510 C CG  . LEU B 1030 ? 0.2079 0.2289 0.2216 0.0160  0.0019  -0.0097 1028 LEU B CG  
16511 C CD1 . LEU B 1030 ? 0.2410 0.2652 0.2537 0.0158  0.0010  -0.0096 1028 LEU B CD1 
16512 C CD2 . LEU B 1030 ? 0.2279 0.2475 0.2407 0.0150  0.0025  -0.0104 1028 LEU B CD2 
16513 N N   . GLY B 1031 ? 0.1753 0.1897 0.1907 0.0191  0.0026  -0.0059 1029 GLY B N   
16514 C CA  . GLY B 1031 ? 0.1907 0.2034 0.2056 0.0200  0.0027  -0.0042 1029 GLY B CA  
16515 C C   . GLY B 1031 ? 0.1683 0.1786 0.1834 0.0190  0.0033  -0.0035 1029 GLY B C   
16516 O O   . GLY B 1031 ? 0.2112 0.2203 0.2255 0.0192  0.0035  -0.0018 1029 GLY B O   
16517 N N   . ARG B 1032 ? 0.1602 0.1699 0.1766 0.0179  0.0037  -0.0045 1030 ARG B N   
16518 C CA  . ARG B 1032 ? 0.1692 0.1774 0.1862 0.0168  0.0044  -0.0039 1030 ARG B CA  
16519 C C   . ARG B 1032 ? 0.1835 0.1939 0.1997 0.0161  0.0053  -0.0034 1030 ARG B C   
16520 O O   . ARG B 1032 ? 0.2153 0.2252 0.2319 0.0153  0.0061  -0.0024 1030 ARG B O   
16521 C CB  . ARG B 1032 ? 0.1823 0.1896 0.2011 0.0159  0.0043  -0.0052 1030 ARG B CB  
16522 C CG  . ARG B 1032 ? 0.1871 0.1930 0.2073 0.0148  0.0048  -0.0044 1030 ARG B CG  
16523 C CD  . ARG B 1032 ? 0.2047 0.2074 0.2248 0.0149  0.0043  -0.0031 1030 ARG B CD  
16524 N NE  . ARG B 1032 ? 0.2308 0.2321 0.2525 0.0134  0.0045  -0.0025 1030 ARG B NE  
16525 C CZ  . ARG B 1032 ? 0.2584 0.2585 0.2801 0.0125  0.0048  -0.0007 1030 ARG B CZ  
16526 N NH1 . ARG B 1032 ? 0.2765 0.2763 0.2964 0.0132  0.0050  0.0008  1030 ARG B NH1 
16527 N NH2 . ARG B 1032 ? 0.2815 0.2810 0.3050 0.0109  0.0049  -0.0002 1030 ARG B NH2 
16528 N N   . LEU B 1033 ? 0.1831 0.1957 0.1979 0.0163  0.0053  -0.0041 1031 LEU B N   
16529 C CA  . LEU B 1033 ? 0.1783 0.1926 0.1917 0.0158  0.0061  -0.0042 1031 LEU B CA  
16530 C C   . LEU B 1033 ? 0.1762 0.1917 0.1874 0.0163  0.0061  -0.0028 1031 LEU B C   
16531 O O   . LEU B 1033 ? 0.1959 0.2130 0.2052 0.0160  0.0066  -0.0031 1031 LEU B O   
16532 C CB  . LEU B 1033 ? 0.1893 0.2050 0.2025 0.0155  0.0060  -0.0061 1031 LEU B CB  
16533 C CG  . LEU B 1033 ? 0.1847 0.1992 0.2000 0.0152  0.0058  -0.0073 1031 LEU B CG  
16534 C CD1 . LEU B 1033 ? 0.1878 0.2031 0.2025 0.0149  0.0055  -0.0090 1031 LEU B CD1 
16535 C CD2 . LEU B 1033 ? 0.2142 0.2279 0.2312 0.0146  0.0067  -0.0069 1031 LEU B CD2 
16536 N N   . VAL B 1034 ? 0.1889 0.2035 0.1999 0.0171  0.0054  -0.0015 1032 VAL B N   
16537 C CA  . VAL B 1034 ? 0.2113 0.2266 0.2201 0.0177  0.0052  0.0001  1032 VAL B CA  
16538 C C   . VAL B 1034 ? 0.2210 0.2336 0.2301 0.0179  0.0053  0.0021  1032 VAL B C   
16539 O O   . VAL B 1034 ? 0.2348 0.2451 0.2457 0.0177  0.0052  0.0020  1032 VAL B O   
16540 C CB  . VAL B 1034 ? 0.2066 0.2236 0.2147 0.0187  0.0039  -0.0001 1032 VAL B CB  
16541 C CG1 . VAL B 1034 ? 0.2004 0.2200 0.2077 0.0180  0.0037  -0.0018 1032 VAL B CG1 
16542 C CG2 . VAL B 1034 ? 0.1907 0.2065 0.2007 0.0197  0.0032  -0.0005 1032 VAL B CG2 
16543 N N   . THR B 1035 ? 0.2384 0.2513 0.2455 0.0181  0.0054  0.0039  1033 THR B N   
16544 C CA  . THR B 1035 ? 0.2761 0.2861 0.2832 0.0181  0.0055  0.0060  1033 THR B CA  
16545 C C   . THR B 1035 ? 0.2753 0.2831 0.2826 0.0196  0.0043  0.0067  1033 THR B C   
16546 O O   . THR B 1035 ? 0.3210 0.3252 0.3285 0.0196  0.0042  0.0079  1033 THR B O   
16547 C CB  . THR B 1035 ? 0.3243 0.3351 0.3290 0.0176  0.0063  0.0080  1033 THR B CB  
16548 O OG1 . THR B 1035 ? 0.3966 0.4098 0.3990 0.0184  0.0056  0.0080  1033 THR B OG1 
16549 C CG2 . THR B 1035 ? 0.3720 0.3842 0.3769 0.0161  0.0079  0.0075  1033 THR B CG2 
16550 N N   . THR B 1036 ? 0.2393 0.2490 0.2464 0.0210  0.0034  0.0059  1034 THR B N   
16551 C CA  . THR B 1036 ? 0.2806 0.2886 0.2881 0.0228  0.0023  0.0063  1034 THR B CA  
16552 C C   . THR B 1036 ? 0.2815 0.2915 0.2905 0.0233  0.0019  0.0041  1034 THR B C   
16553 O O   . THR B 1036 ? 0.2515 0.2651 0.2602 0.0231  0.0017  0.0032  1034 THR B O   
16554 C CB  . THR B 1036 ? 0.3333 0.3427 0.3389 0.0243  0.0015  0.0080  1034 THR B CB  
16555 O OG1 . THR B 1036 ? 0.4031 0.4110 0.4068 0.0237  0.0019  0.0101  1034 THR B OG1 
16556 C CG2 . THR B 1036 ? 0.3490 0.3564 0.3551 0.0267  0.0005  0.0084  1034 THR B CG2 
16557 N N   . ALA B 1037 ? 0.2644 0.2719 0.2749 0.0237  0.0018  0.0032  1035 ALA B N   
16558 C CA  . ALA B 1037 ? 0.2458 0.2551 0.2576 0.0240  0.0016  0.0012  1035 ALA B CA  
16559 C C   . ALA B 1037 ? 0.2398 0.2517 0.2516 0.0259  0.0008  0.0013  1035 ALA B C   
16560 O O   . ALA B 1037 ? 0.2590 0.2695 0.2703 0.0278  0.0003  0.0026  1035 ALA B O   
16561 C CB  . ALA B 1037 ? 0.2718 0.2777 0.2849 0.0239  0.0016  0.0002  1035 ALA B CB  
16562 N N   . PRO B 1038 ? 0.1950 0.2108 0.2074 0.0256  0.0006  0.0001  1036 PRO B N   
16563 C CA  . PRO B 1038 ? 0.2025 0.2215 0.2155 0.0274  -0.0002 0.0002  1036 PRO B CA  
16564 C C   . PRO B 1038 ? 0.2120 0.2295 0.2262 0.0287  -0.0001 -0.0008 1036 PRO B C   
16565 O O   . PRO B 1038 ? 0.2139 0.2282 0.2285 0.0280  0.0003  -0.0018 1036 PRO B O   
16566 C CB  . PRO B 1038 ? 0.2291 0.2524 0.2422 0.0259  -0.0003 -0.0009 1036 PRO B CB  
16567 C CG  . PRO B 1038 ? 0.2571 0.2785 0.2704 0.0239  0.0004  -0.0024 1036 PRO B CG  
16568 C CD  . PRO B 1038 ? 0.2278 0.2453 0.2404 0.0236  0.0010  -0.0014 1036 PRO B CD  
16569 N N   . VAL B 1039 ? 0.2095 0.2297 0.2244 0.0307  -0.0006 -0.0006 1037 VAL B N   
16570 C CA  . VAL B 1039 ? 0.2015 0.2214 0.2175 0.0322  -0.0005 -0.0017 1037 VAL B CA  
16571 C C   . VAL B 1039 ? 0.1982 0.2218 0.2153 0.0307  -0.0003 -0.0032 1037 VAL B C   
16572 O O   . VAL B 1039 ? 0.2041 0.2326 0.2218 0.0304  -0.0007 -0.0030 1037 VAL B O   
16573 C CB  . VAL B 1039 ? 0.2299 0.2515 0.2462 0.0353  -0.0009 -0.0007 1037 VAL B CB  
16574 C CG1 . VAL B 1039 ? 0.2435 0.2650 0.2608 0.0369  -0.0005 -0.0020 1037 VAL B CG1 
16575 C CG2 . VAL B 1039 ? 0.2592 0.2766 0.2741 0.0368  -0.0012 0.0010  1037 VAL B CG2 
16576 N N   . PRO B 1040 ? 0.2034 0.2247 0.2208 0.0295  0.0002  -0.0047 1038 PRO B N   
16577 C CA  . PRO B 1040 ? 0.2023 0.2267 0.2205 0.0279  0.0003  -0.0060 1038 PRO B CA  
16578 C C   . PRO B 1040 ? 0.2078 0.2362 0.2271 0.0294  0.0003  -0.0062 1038 PRO B C   
16579 O O   . PRO B 1040 ? 0.1938 0.2216 0.2133 0.0319  0.0003  -0.0058 1038 PRO B O   
16580 C CB  . PRO B 1040 ? 0.2317 0.2520 0.2498 0.0268  0.0008  -0.0073 1038 PRO B CB  
16581 C CG  . PRO B 1040 ? 0.2574 0.2732 0.2747 0.0270  0.0009  -0.0065 1038 PRO B CG  
16582 C CD  . PRO B 1040 ? 0.2240 0.2398 0.2409 0.0293  0.0006  -0.0051 1038 PRO B CD  
16583 N N   . PRO B 1041 ? 0.1927 0.2252 0.2128 0.0278  0.0001  -0.0068 1039 PRO B N   
16584 C CA  . PRO B 1041 ? 0.1949 0.2316 0.2163 0.0289  0.0003  -0.0071 1039 PRO B CA  
16585 C C   . PRO B 1041 ? 0.2080 0.2421 0.2294 0.0304  0.0010  -0.0080 1039 PRO B C   
16586 O O   . PRO B 1041 ? 0.2260 0.2558 0.2466 0.0294  0.0013  -0.0090 1039 PRO B O   
16587 C CB  . PRO B 1041 ? 0.2222 0.2619 0.2439 0.0261  0.0000  -0.0078 1039 PRO B CB  
16588 C CG  . PRO B 1041 ? 0.2507 0.2889 0.2712 0.0242  -0.0004 -0.0075 1039 PRO B CG  
16589 C CD  . PRO B 1041 ? 0.2496 0.2826 0.2692 0.0250  0.0000  -0.0074 1039 PRO B CD  
16590 N N   . GLN B 1042 ? 0.2128 0.2493 0.2349 0.0330  0.0012  -0.0077 1040 GLN B N   
16591 C CA  . GLN B 1042 ? 0.2250 0.2596 0.2469 0.0348  0.0019  -0.0086 1040 GLN B CA  
16592 C C   . GLN B 1042 ? 0.2104 0.2380 0.2306 0.0359  0.0020  -0.0090 1040 GLN B C   
16593 O O   . GLN B 1042 ? 0.2191 0.2439 0.2385 0.0369  0.0025  -0.0101 1040 GLN B O   
16594 C CB  . GLN B 1042 ? 0.2511 0.2868 0.2732 0.0329  0.0024  -0.0099 1040 GLN B CB  
16595 C CG  . GLN B 1042 ? 0.2953 0.3377 0.3189 0.0315  0.0023  -0.0096 1040 GLN B CG  
16596 C CD  . GLN B 1042 ? 0.3960 0.4387 0.4193 0.0294  0.0027  -0.0107 1040 GLN B CD  
16597 O OE1 . GLN B 1042 ? 0.4900 0.5294 0.5124 0.0271  0.0024  -0.0113 1040 GLN B OE1 
16598 N NE2 . GLN B 1042 ? 0.4987 0.5452 0.5228 0.0302  0.0033  -0.0109 1040 GLN B NE2 
16599 N N   . HIS B 1043 ? 0.1964 0.2210 0.2160 0.0355  0.0015  -0.0081 1041 HIS B N   
16600 C CA  . HIS B 1043 ? 0.1960 0.2138 0.2141 0.0357  0.0015  -0.0083 1041 HIS B CA  
16601 C C   . HIS B 1043 ? 0.2072 0.2227 0.2245 0.0391  0.0014  -0.0075 1041 HIS B C   
16602 O O   . HIS B 1043 ? 0.2370 0.2520 0.2540 0.0399  0.0009  -0.0060 1041 HIS B O   
16603 C CB  . HIS B 1043 ? 0.2116 0.2275 0.2293 0.0334  0.0011  -0.0076 1041 HIS B CB  
16604 C CG  . HIS B 1043 ? 0.1983 0.2078 0.2148 0.0331  0.0010  -0.0076 1041 HIS B CG  
16605 N ND1 . HIS B 1043 ? 0.2033 0.2096 0.2195 0.0313  0.0011  -0.0087 1041 HIS B ND1 
16606 C CD2 . HIS B 1043 ? 0.2326 0.2383 0.2481 0.0342  0.0007  -0.0064 1041 HIS B CD2 
16607 C CE1 . HIS B 1043 ? 0.2348 0.2360 0.2501 0.0312  0.0009  -0.0083 1041 HIS B CE1 
16608 N NE2 . HIS B 1043 ? 0.2190 0.2195 0.2337 0.0329  0.0006  -0.0068 1041 HIS B NE2 
16609 N N   . SER B 1044 ? 0.1864 0.2001 0.2031 0.0411  0.0018  -0.0086 1042 SER B N   
16610 C CA  . SER B 1044 ? 0.2159 0.2263 0.2314 0.0445  0.0018  -0.0082 1042 SER B CA  
16611 C C   . SER B 1044 ? 0.2021 0.2094 0.2162 0.0458  0.0024  -0.0100 1042 SER B C   
16612 O O   . SER B 1044 ? 0.2129 0.2219 0.2273 0.0442  0.0028  -0.0113 1042 SER B O   
16613 C CB  . SER B 1044 ? 0.1999 0.2160 0.2168 0.0473  0.0019  -0.0070 1042 SER B CB  
16614 O OG  . SER B 1044 ? 0.2328 0.2542 0.2510 0.0481  0.0026  -0.0079 1042 SER B OG  
16615 N N   . SER B 1045 ? 0.1973 0.1998 0.2097 0.0487  0.0023  -0.0101 1043 SER B N   
16616 C CA  . SER B 1045 ? 0.1899 0.1890 0.2004 0.0505  0.0028  -0.0119 1043 SER B CA  
16617 C C   . SER B 1045 ? 0.2059 0.2030 0.2153 0.0549  0.0030  -0.0116 1043 SER B C   
16618 O O   . SER B 1045 ? 0.2261 0.2203 0.2349 0.0560  0.0024  -0.0101 1043 SER B O   
16619 C CB  . SER B 1045 ? 0.2017 0.1933 0.2102 0.0482  0.0023  -0.0128 1043 SER B CB  
16620 O OG  . SER B 1045 ? 0.2348 0.2222 0.2408 0.0500  0.0026  -0.0146 1043 SER B OG  
16621 N N   . VAL B 1046 ? 0.2068 0.2052 0.2156 0.0576  0.0040  -0.0129 1044 VAL B N   
16622 C CA  . VAL B 1046 ? 0.2204 0.2163 0.2277 0.0623  0.0042  -0.0128 1044 VAL B CA  
16623 C C   . VAL B 1046 ? 0.2357 0.2215 0.2391 0.0631  0.0038  -0.0141 1044 VAL B C   
16624 O O   . VAL B 1046 ? 0.2534 0.2353 0.2550 0.0670  0.0038  -0.0142 1044 VAL B O   
16625 C CB  . VAL B 1046 ? 0.2784 0.2806 0.2867 0.0654  0.0056  -0.0136 1044 VAL B CB  
16626 C CG1 . VAL B 1046 ? 0.3010 0.3131 0.3133 0.0645  0.0058  -0.0121 1044 VAL B CG1 
16627 C CG2 . VAL B 1046 ? 0.2457 0.2469 0.2525 0.0643  0.0064  -0.0158 1044 VAL B CG2 
16628 N N   . HIS B 1047 ? 0.2409 0.2225 0.2431 0.0595  0.0032  -0.0151 1045 HIS B N   
16629 C CA  A HIS B 1047 ? 0.2592 0.2314 0.2577 0.0597  0.0026  -0.0164 1045 HIS B CA  
16630 C CA  B HIS B 1047 ? 0.2592 0.2314 0.2578 0.0595  0.0026  -0.0164 1045 HIS B CA  
16631 C C   . HIS B 1047 ? 0.2280 0.1941 0.2256 0.0586  0.0014  -0.0148 1045 HIS B C   
16632 O O   . HIS B 1047 ? 0.2555 0.2241 0.2552 0.0559  0.0009  -0.0132 1045 HIS B O   
16633 C CB  A HIS B 1047 ? 0.2634 0.2345 0.2611 0.0565  0.0026  -0.0181 1045 HIS B CB  
16634 C CB  B HIS B 1047 ? 0.2556 0.2268 0.2537 0.0557  0.0024  -0.0178 1045 HIS B CB  
16635 C CG  A HIS B 1047 ? 0.2788 0.2560 0.2772 0.0574  0.0039  -0.0193 1045 HIS B CG  
16636 C CG  B HIS B 1047 ? 0.2628 0.2247 0.2577 0.0542  0.0013  -0.0187 1045 HIS B CG  
16637 N ND1 A HIS B 1047 ? 0.3180 0.2944 0.3143 0.0611  0.0048  -0.0208 1045 HIS B ND1 
16638 N ND1 B HIS B 1047 ? 0.2867 0.2420 0.2777 0.0567  0.0012  -0.0204 1045 HIS B ND1 
16639 C CD2 A HIS B 1047 ? 0.2874 0.2716 0.2883 0.0550  0.0044  -0.0193 1045 HIS B CD2 
16640 C CD2 B HIS B 1047 ? 0.2675 0.2257 0.2624 0.0504  0.0002  -0.0181 1045 HIS B CD2 
16641 C CE1 A HIS B 1047 ? 0.3065 0.2894 0.3040 0.0609  0.0060  -0.0215 1045 HIS B CE1 
16642 C CE1 B HIS B 1047 ? 0.3114 0.2592 0.3002 0.0543  0.0000  -0.0209 1045 HIS B CE1 
16643 N NE2 A HIS B 1047 ? 0.3470 0.3346 0.3474 0.0571  0.0056  -0.0205 1045 HIS B NE2 
16644 N NE2 B HIS B 1047 ? 0.2989 0.2486 0.2903 0.0505  -0.0007 -0.0194 1045 HIS B NE2 
16645 N N   . THR B 1048 ? 0.2294 0.1873 0.2237 0.0608  0.0009  -0.0153 1046 THR B N   
16646 C CA  . THR B 1048 ? 0.2386 0.1896 0.2314 0.0596  -0.0004 -0.0139 1046 THR B CA  
16647 C C   . THR B 1048 ? 0.2721 0.2145 0.2617 0.0577  -0.0013 -0.0155 1046 THR B C   
16648 O O   . THR B 1048 ? 0.2680 0.2062 0.2546 0.0599  -0.0011 -0.0175 1046 THR B O   
16649 C CB  . THR B 1048 ? 0.3155 0.2635 0.3070 0.0640  -0.0005 -0.0128 1046 THR B CB  
16650 O OG1 . THR B 1048 ? 0.2641 0.2209 0.2587 0.0662  0.0003  -0.0116 1046 THR B OG1 
16651 C CG2 . THR B 1048 ? 0.3298 0.2716 0.3202 0.0623  -0.0018 -0.0108 1046 THR B CG2 
16652 N N   . ASP B 1049 ? 0.2496 0.1898 0.2397 0.0535  -0.0022 -0.0146 1047 ASP B N   
16653 C CA  . ASP B 1049 ? 0.2487 0.1813 0.2361 0.0511  -0.0033 -0.0159 1047 ASP B CA  
16654 C C   . ASP B 1049 ? 0.2438 0.1668 0.2270 0.0539  -0.0040 -0.0163 1047 ASP B C   
16655 O O   . ASP B 1049 ? 0.2629 0.1837 0.2458 0.0555  -0.0043 -0.0144 1047 ASP B O   
16656 C CB  . ASP B 1049 ? 0.2351 0.1673 0.2243 0.0464  -0.0042 -0.0143 1047 ASP B CB  
16657 C CG  . ASP B 1049 ? 0.2477 0.1730 0.2346 0.0435  -0.0054 -0.0155 1047 ASP B CG  
16658 O OD1 . ASP B 1049 ? 0.2806 0.1976 0.2645 0.0438  -0.0064 -0.0152 1047 ASP B OD1 
16659 O OD2 . ASP B 1049 ? 0.2749 0.2028 0.2628 0.0411  -0.0054 -0.0168 1047 ASP B OD2 
16660 N N   . PRO B 1050 ? 0.2652 0.1825 0.2448 0.0547  -0.0043 -0.0187 1048 PRO B N   
16661 C CA  . PRO B 1050 ? 0.2970 0.2049 0.2722 0.0578  -0.0050 -0.0193 1048 PRO B CA  
16662 C C   . PRO B 1050 ? 0.2984 0.1978 0.2717 0.0550  -0.0067 -0.0180 1048 PRO B C   
16663 O O   . PRO B 1050 ? 0.3193 0.2118 0.2898 0.0575  -0.0073 -0.0173 1048 PRO B O   
16664 C CB  . PRO B 1050 ? 0.3573 0.2619 0.3290 0.0591  -0.0047 -0.0225 1048 PRO B CB  
16665 C CG  . PRO B 1050 ? 0.3435 0.2529 0.3174 0.0548  -0.0048 -0.0231 1048 PRO B CG  
16666 C CD  . PRO B 1050 ? 0.2917 0.2109 0.2709 0.0534  -0.0040 -0.0210 1048 PRO B CD  
16667 N N   . VAL B 1051 ? 0.3115 0.2114 0.2864 0.0499  -0.0075 -0.0175 1049 VAL B N   
16668 C CA  . VAL B 1051 ? 0.3057 0.1984 0.2794 0.0467  -0.0091 -0.0160 1049 VAL B CA  
16669 C C   . VAL B 1051 ? 0.2781 0.1733 0.2541 0.0468  -0.0089 -0.0128 1049 VAL B C   
16670 O O   . VAL B 1051 ? 0.2905 0.1785 0.2642 0.0470  -0.0099 -0.0114 1049 VAL B O   
16671 C CB  . VAL B 1051 ? 0.3035 0.1966 0.2784 0.0414  -0.0100 -0.0163 1049 VAL B CB  
16672 C CG1 . VAL B 1051 ? 0.3323 0.2189 0.3065 0.0378  -0.0116 -0.0144 1049 VAL B CG1 
16673 C CG2 . VAL B 1051 ? 0.3396 0.2290 0.3114 0.0414  -0.0105 -0.0194 1049 VAL B CG2 
16674 N N   . LEU B 1052 ? 0.2598 0.1648 0.2399 0.0469  -0.0077 -0.0118 1050 LEU B N   
16675 C CA  . LEU B 1052 ? 0.2592 0.1671 0.2410 0.0478  -0.0074 -0.0090 1050 LEU B CA  
16676 C C   . LEU B 1052 ? 0.3073 0.2102 0.2863 0.0527  -0.0075 -0.0086 1050 LEU B C   
16677 O O   . LEU B 1052 ? 0.3001 0.1986 0.2779 0.0529  -0.0082 -0.0064 1050 LEU B O   
16678 C CB  . LEU B 1052 ? 0.2542 0.1733 0.2403 0.0479  -0.0061 -0.0085 1050 LEU B CB  
16679 C CG  . LEU B 1052 ? 0.2345 0.1583 0.2227 0.0487  -0.0057 -0.0058 1050 LEU B CG  
16680 C CD1 . LEU B 1052 ? 0.2551 0.1792 0.2423 0.0539  -0.0054 -0.0054 1050 LEU B CD1 
16681 C CD2 . LEU B 1052 ? 0.2492 0.1682 0.2367 0.0456  -0.0067 -0.0034 1050 LEU B CD2 
16682 N N   . LEU B 1053 ? 0.2856 0.1891 0.2632 0.0568  -0.0067 -0.0107 1051 LEU B N   
16683 C CA  . LEU B 1053 ? 0.3260 0.2253 0.3011 0.0620  -0.0067 -0.0105 1051 LEU B CA  
16684 C C   . LEU B 1053 ? 0.3040 0.1907 0.2743 0.0619  -0.0082 -0.0105 1051 LEU B C   
16685 O O   . LEU B 1053 ? 0.3249 0.2071 0.2936 0.0642  -0.0088 -0.0087 1051 LEU B O   
16686 C CB  . LEU B 1053 ? 0.3592 0.2616 0.3337 0.0664  -0.0054 -0.0130 1051 LEU B CB  
16687 C CG  . LEU B 1053 ? 0.3753 0.2900 0.3543 0.0675  -0.0040 -0.0125 1051 LEU B CG  
16688 C CD1 . LEU B 1053 ? 0.3630 0.2809 0.3415 0.0709  -0.0026 -0.0151 1051 LEU B CD1 
16689 C CD2 . LEU B 1053 ? 0.3817 0.2998 0.3625 0.0701  -0.0039 -0.0099 1051 LEU B CD2 
16690 N N   . ASP B 1054 ? 0.3364 0.2173 0.3043 0.0592  -0.0091 -0.0124 1052 ASP B N   
16691 C CA  . ASP B 1054 ? 0.3496 0.2181 0.3127 0.0585  -0.0107 -0.0124 1052 ASP B CA  
16692 C C   . ASP B 1054 ? 0.3118 0.1780 0.2759 0.0548  -0.0118 -0.0092 1052 ASP B C   
16693 O O   . ASP B 1054 ? 0.3388 0.1961 0.2996 0.0556  -0.0129 -0.0080 1052 ASP B O   
16694 C CB  . ASP B 1054 ? 0.3477 0.2115 0.3085 0.0556  -0.0115 -0.0151 1052 ASP B CB  
16695 C CG  . ASP B 1054 ? 0.4589 0.3225 0.4172 0.0597  -0.0106 -0.0184 1052 ASP B CG  
16696 O OD1 . ASP B 1054 ? 0.4267 0.2915 0.3844 0.0650  -0.0096 -0.0186 1052 ASP B OD1 
16697 O OD2 . ASP B 1054 ? 0.5096 0.3721 0.4667 0.0575  -0.0110 -0.0207 1052 ASP B OD2 
16698 N N   . PHE B 1055 ? 0.3139 0.1880 0.2824 0.0508  -0.0114 -0.0078 1053 PHE B N   
16699 C CA  . PHE B 1055 ? 0.3152 0.1884 0.2849 0.0473  -0.0121 -0.0046 1053 PHE B CA  
16700 C C   . PHE B 1055 ? 0.3167 0.1907 0.2865 0.0507  -0.0118 -0.0021 1053 PHE B C   
16701 O O   . PHE B 1055 ? 0.3250 0.1923 0.2926 0.0500  -0.0128 0.0001  1053 PHE B O   
16702 C CB  . PHE B 1055 ? 0.2998 0.1821 0.2742 0.0429  -0.0115 -0.0039 1053 PHE B CB  
16703 C CG  . PHE B 1055 ? 0.2878 0.1698 0.2636 0.0390  -0.0120 -0.0008 1053 PHE B CG  
16704 C CD1 . PHE B 1055 ? 0.3201 0.1931 0.2933 0.0359  -0.0135 0.0001  1053 PHE B CD1 
16705 C CD2 . PHE B 1055 ? 0.3202 0.2110 0.2997 0.0381  -0.0109 0.0012  1053 PHE B CD2 
16706 C CE1 . PHE B 1055 ? 0.3284 0.2016 0.3029 0.0322  -0.0138 0.0031  1053 PHE B CE1 
16707 C CE2 . PHE B 1055 ? 0.3232 0.2140 0.3037 0.0346  -0.0112 0.0040  1053 PHE B CE2 
16708 C CZ  . PHE B 1055 ? 0.3270 0.2091 0.3051 0.0316  -0.0126 0.0051  1053 PHE B CZ  
16709 N N   . ALA B 1056 ? 0.2988 0.1810 0.2709 0.0544  -0.0105 -0.0024 1054 ALA B N   
16710 C CA  . ALA B 1056 ? 0.3148 0.1985 0.2871 0.0578  -0.0103 0.0000  1054 ALA B CA  
16711 C C   . ALA B 1056 ? 0.3143 0.1875 0.2820 0.0617  -0.0112 0.0001  1054 ALA B C   
16712 O O   . ALA B 1056 ? 0.3585 0.2279 0.3249 0.0624  -0.0120 0.0028  1054 ALA B O   
16713 C CB  . ALA B 1056 ? 0.3484 0.2427 0.3240 0.0611  -0.0088 -0.0006 1054 ALA B CB  
16714 N N   . LYS B 1057 ? 0.3470 0.2149 0.3117 0.0643  -0.0113 -0.0028 1055 LYS B N   
16715 C CA  . LYS B 1057 ? 0.3765 0.2335 0.3362 0.0682  -0.0122 -0.0031 1055 LYS B CA  
16716 C C   . LYS B 1057 ? 0.4151 0.2613 0.3714 0.0644  -0.0140 -0.0016 1055 LYS B C   
16717 O O   . LYS B 1057 ? 0.4060 0.2445 0.3592 0.0666  -0.0150 0.0002  1055 LYS B O   
16718 C CB  . LYS B 1057 ? 0.3849 0.2386 0.3417 0.0714  -0.0117 -0.0068 1055 LYS B CB  
16719 C CG  . LYS B 1057 ? 0.4481 0.3101 0.4070 0.0768  -0.0100 -0.0079 1055 LYS B CG  
16720 C CD  . LYS B 1057 ? 0.4109 0.2688 0.3665 0.0799  -0.0095 -0.0116 1055 LYS B CD  
16721 C CE  . LYS B 1057 ? 0.4459 0.3031 0.4011 0.0751  -0.0098 -0.0138 1055 LYS B CE  
16722 N NZ  . LYS B 1057 ? 0.4603 0.3167 0.4130 0.0783  -0.0089 -0.0174 1055 LYS B NZ  
16723 N N   . TRP B 1058 ? 0.4025 0.2479 0.3594 0.0588  -0.0146 -0.0022 1056 TRP B N   
16724 C CA  . TRP B 1058 ? 0.4130 0.2492 0.3674 0.0545  -0.0163 -0.0005 1056 TRP B CA  
16725 C C   . TRP B 1058 ? 0.3944 0.2326 0.3505 0.0530  -0.0165 0.0035  1056 TRP B C   
16726 O O   . TRP B 1058 ? 0.4235 0.2527 0.3763 0.0530  -0.0177 0.0055  1056 TRP B O   
16727 C CB  . TRP B 1058 ? 0.4165 0.2536 0.3721 0.0487  -0.0168 -0.0018 1056 TRP B CB  
16728 C CG  . TRP B 1058 ? 0.4260 0.2551 0.3798 0.0436  -0.0185 0.0000  1056 TRP B CG  
16729 C CD1 . TRP B 1058 ? 0.5089 0.3252 0.4574 0.0429  -0.0203 -0.0007 1056 TRP B CD1 
16730 C CD2 . TRP B 1058 ? 0.4237 0.2571 0.3808 0.0383  -0.0186 0.0028  1056 TRP B CD2 
16731 N NE1 . TRP B 1058 ? 0.4758 0.2885 0.4245 0.0373  -0.0216 0.0017  1056 TRP B NE1 
16732 C CE2 . TRP B 1058 ? 0.4693 0.2926 0.4233 0.0344  -0.0205 0.0039  1056 TRP B CE2 
16733 C CE3 . TRP B 1058 ? 0.3919 0.2368 0.3542 0.0364  -0.0172 0.0045  1056 TRP B CE3 
16734 C CZ2 . TRP B 1058 ? 0.4468 0.2717 0.4030 0.0288  -0.0209 0.0068  1056 TRP B CZ2 
16735 C CZ3 . TRP B 1058 ? 0.4731 0.3192 0.4374 0.0312  -0.0176 0.0072  1056 TRP B CZ3 
16736 C CH2 . TRP B 1058 ? 0.4399 0.2764 0.4013 0.0274  -0.0193 0.0083  1056 TRP B CH2 
16737 N N   . LEU B 1059 ? 0.3449 0.1948 0.3059 0.0519  -0.0152 0.0048  1057 LEU B N   
16738 C CA  . LEU B 1059 ? 0.3970 0.2497 0.3596 0.0507  -0.0152 0.0085  1057 LEU B CA  
16739 C C   . LEU B 1059 ? 0.4531 0.3018 0.4132 0.0560  -0.0155 0.0101  1057 LEU B C   
16740 O O   . LEU B 1059 ? 0.4418 0.2852 0.4000 0.0551  -0.0164 0.0132  1057 LEU B O   
16741 C CB  . LEU B 1059 ? 0.3659 0.2320 0.3338 0.0496  -0.0136 0.0090  1057 LEU B CB  
16742 C CG  . LEU B 1059 ? 0.3640 0.2346 0.3348 0.0440  -0.0133 0.0084  1057 LEU B CG  
16743 C CD1 . LEU B 1059 ? 0.3758 0.2590 0.3512 0.0436  -0.0118 0.0086  1057 LEU B CD1 
16744 C CD2 . LEU B 1059 ? 0.3786 0.2439 0.3483 0.0391  -0.0143 0.0111  1057 LEU B CD2 
16745 N N   . ASP B 1060 ? 0.4313 0.2827 0.3914 0.0615  -0.0147 0.0083  1058 ASP B N   
16746 C CA  . ASP B 1060 ? 0.4258 0.2737 0.3837 0.0669  -0.0151 0.0097  1058 ASP B CA  
16747 C C   . ASP B 1060 ? 0.4723 0.3056 0.4244 0.0679  -0.0167 0.0098  1058 ASP B C   
16748 O O   . ASP B 1060 ? 0.5183 0.3461 0.4681 0.0700  -0.0176 0.0124  1058 ASP B O   
16749 C CB  . ASP B 1060 ? 0.4543 0.3087 0.4138 0.0727  -0.0139 0.0076  1058 ASP B CB  
16750 C CG  . ASP B 1060 ? 0.5095 0.3763 0.4735 0.0736  -0.0128 0.0093  1058 ASP B CG  
16751 O OD1 . ASP B 1060 ? 0.6027 0.4701 0.5671 0.0731  -0.0134 0.0126  1058 ASP B OD1 
16752 O OD2 . ASP B 1060 ? 0.5327 0.4087 0.5000 0.0746  -0.0115 0.0074  1058 ASP B OD2 
16753 N N   . GLY B 1061 ? 0.4730 0.2995 0.4225 0.0662  -0.0173 0.0071  1059 GLY B N   
16754 C CA  . GLY B 1061 ? 0.4932 0.3050 0.4368 0.0666  -0.0190 0.0069  1059 GLY B CA  
16755 C C   . GLY B 1061 ? 0.5253 0.3312 0.4676 0.0621  -0.0204 0.0106  1059 GLY B C   
16756 O O   . GLY B 1061 ? 0.5218 0.3173 0.4598 0.0640  -0.0217 0.0121  1059 GLY B O   
16757 N N   . LYS B 1062 ? 0.4954 0.3076 0.4412 0.0563  -0.0201 0.0120  1060 LYS B N   
16758 C CA  . LYS B 1062 ? 0.5314 0.3391 0.4764 0.0516  -0.0212 0.0156  1060 LYS B CA  
16759 C C   . LYS B 1062 ? 0.5554 0.3695 0.5026 0.0527  -0.0206 0.0193  1060 LYS B C   
16760 O O   . LYS B 1062 ? 0.5909 0.4035 0.5380 0.0486  -0.0211 0.0225  1060 LYS B O   
16761 C CB  . LYS B 1062 ? 0.5394 0.3494 0.4866 0.0446  -0.0213 0.0154  1060 LYS B CB  
16762 C CG  . LYS B 1062 ? 0.5387 0.3627 0.4918 0.0427  -0.0196 0.0148  1060 LYS B CG  
16763 C CD  . LYS B 1062 ? 0.5274 0.3525 0.4823 0.0363  -0.0199 0.0141  1060 LYS B CD  
16764 C CE  . LYS B 1062 ? 0.4950 0.3153 0.4490 0.0312  -0.0210 0.0176  1060 LYS B CE  
16765 N NZ  . LYS B 1062 ? 0.5532 0.3724 0.5083 0.0253  -0.0217 0.0168  1060 LYS B NZ  
16766 N N   . GLY B 1063 ? 0.5143 0.3355 0.4633 0.0579  -0.0195 0.0189  1061 GLY B N   
16767 C CA  . GLY B 1063 ? 0.5112 0.3379 0.4618 0.0594  -0.0192 0.0223  1061 GLY B CA  
16768 C C   . GLY B 1063 ? 0.5571 0.3956 0.5125 0.0553  -0.0180 0.0237  1061 GLY B C   
16769 O O   . GLY B 1063 ? 0.5367 0.3786 0.4928 0.0553  -0.0180 0.0269  1061 GLY B O   
16770 N N   . ALA B 1064 ? 0.4707 0.3151 0.4291 0.0520  -0.0171 0.0214  1062 ALA B N   
16771 C CA  . ALA B 1064 ? 0.4387 0.2944 0.4017 0.0485  -0.0159 0.0223  1062 ALA B CA  
16772 C C   . ALA B 1064 ? 0.4574 0.3236 0.4235 0.0526  -0.0146 0.0213  1062 ALA B C   
16773 O O   . ALA B 1064 ? 0.4054 0.2788 0.3745 0.0524  -0.0136 0.0186  1062 ALA B O   
16774 C CB  . ALA B 1064 ? 0.4572 0.3148 0.4222 0.0435  -0.0155 0.0203  1062 ALA B CB  
16775 N N   . ARG B 1065 ? 0.4686 0.3355 0.4338 0.0563  -0.0149 0.0236  1063 ARG B N   
16776 C CA  . ARG B 1065 ? 0.4326 0.3080 0.4002 0.0609  -0.0141 0.0227  1063 ARG B CA  
16777 C C   . ARG B 1065 ? 0.4191 0.3068 0.3912 0.0585  -0.0128 0.0224  1063 ARG B C   
16778 O O   . ARG B 1065 ? 0.4220 0.3170 0.3968 0.0603  -0.0119 0.0201  1063 ARG B O   
16779 C CB  . ARG B 1065 ? 0.5062 0.3796 0.4720 0.0651  -0.0149 0.0256  1063 ARG B CB  
16780 N N   . ALA B 1066 ? 0.4006 0.2908 0.3735 0.0543  -0.0127 0.0248  1064 ALA B N   
16781 C CA  . ALA B 1066 ? 0.4037 0.3050 0.3805 0.0519  -0.0115 0.0245  1064 ALA B CA  
16782 C C   . ALA B 1066 ? 0.3907 0.2946 0.3697 0.0494  -0.0106 0.0212  1064 ALA B C   
16783 O O   . ALA B 1066 ? 0.3624 0.2749 0.3444 0.0499  -0.0097 0.0194  1064 ALA B O   
16784 C CB  . ALA B 1066 ? 0.4224 0.3250 0.3991 0.0478  -0.0114 0.0276  1064 ALA B CB  
16785 N N   . GLU B 1067 ? 0.3540 0.2505 0.3314 0.0466  -0.0111 0.0204  1065 GLU B N   
16786 C CA  . GLU B 1067 ? 0.3738 0.2726 0.3532 0.0440  -0.0105 0.0175  1065 GLU B CA  
16787 C C   . GLU B 1067 ? 0.3325 0.2322 0.3121 0.0479  -0.0103 0.0143  1065 GLU B C   
16788 O O   . GLU B 1067 ? 0.3277 0.2340 0.3100 0.0471  -0.0094 0.0121  1065 GLU B O   
16789 C CB  . GLU B 1067 ? 0.3564 0.2470 0.3340 0.0401  -0.0114 0.0177  1065 GLU B CB  
16790 C CG  . GLU B 1067 ? 0.3639 0.2556 0.3422 0.0354  -0.0113 0.0207  1065 GLU B CG  
16791 C CD  . GLU B 1067 ? 0.4458 0.3325 0.4213 0.0363  -0.0120 0.0242  1065 GLU B CD  
16792 O OE1 . GLU B 1067 ? 0.4220 0.3032 0.3948 0.0405  -0.0129 0.0244  1065 GLU B OE1 
16793 O OE2 . GLU B 1067 ? 0.4712 0.3596 0.4472 0.0329  -0.0117 0.0269  1065 GLU B OE2 
16794 N N   . ALA B 1068 ? 0.3468 0.2396 0.3234 0.0520  -0.0110 0.0140  1066 ALA B N   
16795 C CA  . ALA B 1068 ? 0.3992 0.2931 0.3758 0.0561  -0.0106 0.0111  1066 ALA B CA  
16796 C C   . ALA B 1068 ? 0.3605 0.2656 0.3406 0.0584  -0.0095 0.0108  1066 ALA B C   
16797 O O   . ALA B 1068 ? 0.3188 0.2290 0.3008 0.0591  -0.0086 0.0082  1066 ALA B O   
16798 C CB  . ALA B 1068 ? 0.3685 0.2531 0.3410 0.0606  -0.0115 0.0112  1066 ALA B CB  
16799 N N   . GLU B 1069 ? 0.3213 0.2306 0.3023 0.0592  -0.0096 0.0135  1067 GLU B N   
16800 C CA  . GLU B 1069 ? 0.3932 0.3134 0.3776 0.0609  -0.0087 0.0134  1067 GLU B CA  
16801 C C   . GLU B 1069 ? 0.3808 0.3083 0.3683 0.0567  -0.0078 0.0123  1067 GLU B C   
16802 O O   . GLU B 1069 ? 0.3406 0.2753 0.3306 0.0576  -0.0069 0.0104  1067 GLU B O   
16803 C CB  . GLU B 1069 ? 0.3983 0.3206 0.3824 0.0623  -0.0093 0.0167  1067 GLU B CB  
16804 C CG  . GLU B 1069 ? 0.4105 0.3439 0.3979 0.0634  -0.0087 0.0170  1067 GLU B CG  
16805 C CD  . GLU B 1069 ? 0.5210 0.4580 0.5095 0.0685  -0.0084 0.0155  1067 GLU B CD  
16806 O OE1 . GLU B 1069 ? 0.5485 0.4790 0.5349 0.0717  -0.0086 0.0145  1067 GLU B OE1 
16807 O OE2 . GLU B 1069 ? 0.5749 0.5214 0.5664 0.0693  -0.0079 0.0155  1067 GLU B OE2 
16808 N N   . ALA B 1070 ? 0.3236 0.2497 0.3111 0.0521  -0.0078 0.0134  1068 ALA B N   
16809 C CA  . ALA B 1070 ? 0.3448 0.2772 0.3351 0.0483  -0.0069 0.0122  1068 ALA B CA  
16810 C C   . ALA B 1070 ? 0.2772 0.2088 0.2680 0.0481  -0.0066 0.0090  1068 ALA B C   
16811 O O   . ALA B 1070 ? 0.3233 0.2617 0.3166 0.0471  -0.0058 0.0073  1068 ALA B O   
16812 C CB  . ALA B 1070 ? 0.3750 0.3053 0.3650 0.0437  -0.0070 0.0140  1068 ALA B CB  
16813 N N   . ALA B 1071 ? 0.2966 0.2195 0.2846 0.0489  -0.0073 0.0080  1069 ALA B N   
16814 C CA  . ALA B 1071 ? 0.2950 0.2167 0.2830 0.0487  -0.0071 0.0049  1069 ALA B CA  
16815 C C   . ALA B 1071 ? 0.2819 0.2093 0.2711 0.0526  -0.0063 0.0031  1069 ALA B C   
16816 O O   . ALA B 1071 ? 0.2857 0.2182 0.2769 0.0516  -0.0055 0.0011  1069 ALA B O   
16817 C CB  . ALA B 1071 ? 0.2955 0.2063 0.2797 0.0489  -0.0081 0.0042  1069 ALA B CB  
16818 N N   . ARG B 1072 ? 0.2837 0.2102 0.2718 0.0572  -0.0064 0.0039  1070 ARG B N   
16819 C CA  . ARG B 1072 ? 0.2848 0.2175 0.2744 0.0610  -0.0056 0.0024  1070 ARG B CA  
16820 C C   . ARG B 1072 ? 0.2949 0.2386 0.2884 0.0594  -0.0048 0.0027  1070 ARG B C   
16821 O O   . ARG B 1072 ? 0.2868 0.2361 0.2821 0.0599  -0.0039 0.0008  1070 ARG B O   
16822 C CB  . ARG B 1072 ? 0.3008 0.2314 0.2889 0.0662  -0.0059 0.0037  1070 ARG B CB  
16823 C CG  . ARG B 1072 ? 0.3839 0.3038 0.3679 0.0687  -0.0066 0.0027  1070 ARG B CG  
16824 C CD  . ARG B 1072 ? 0.3761 0.2947 0.3589 0.0745  -0.0068 0.0036  1070 ARG B CD  
16825 N NE  . ARG B 1072 ? 0.4570 0.3749 0.4396 0.0745  -0.0077 0.0070  1070 ARG B NE  
16826 C CZ  . ARG B 1072 ? 0.4595 0.3677 0.4386 0.0743  -0.0088 0.0086  1070 ARG B CZ  
16827 N NH1 . ARG B 1072 ? 0.4408 0.3388 0.4163 0.0743  -0.0094 0.0071  1070 ARG B NH1 
16828 N NH2 . ARG B 1072 ? 0.3896 0.2980 0.3687 0.0739  -0.0096 0.0118  1070 ARG B NH2 
16829 N N   . ASN B 1073 ? 0.2794 0.2258 0.2739 0.0575  -0.0050 0.0051  1071 ASN B N   
16830 C CA  . ASN B 1073 ? 0.2814 0.2375 0.2791 0.0558  -0.0044 0.0054  1071 ASN B CA  
16831 C C   . ASN B 1073 ? 0.3097 0.2682 0.3089 0.0521  -0.0038 0.0035  1071 ASN B C   
16832 O O   . ASN B 1073 ? 0.3121 0.2778 0.3137 0.0517  -0.0031 0.0024  1071 ASN B O   
16833 C CB  . ASN B 1073 ? 0.3119 0.2697 0.3097 0.0544  -0.0049 0.0082  1071 ASN B CB  
16834 C CG  . ASN B 1073 ? 0.3713 0.3291 0.3683 0.0585  -0.0055 0.0102  1071 ASN B CG  
16835 O OD1 . ASN B 1073 ? 0.3924 0.3526 0.3900 0.0623  -0.0053 0.0093  1071 ASN B OD1 
16836 N ND2 . ASN B 1073 ? 0.4315 0.3867 0.4270 0.0577  -0.0062 0.0128  1071 ASN B ND2 
16837 N N   . ALA B 1074 ? 0.2854 0.2379 0.2833 0.0491  -0.0041 0.0032  1072 ALA B N   
16838 C CA  . ALA B 1074 ? 0.2626 0.2170 0.2619 0.0457  -0.0036 0.0014  1072 ALA B CA  
16839 C C   . ALA B 1074 ? 0.2141 0.1690 0.2134 0.0475  -0.0032 -0.0012 1072 ALA B C   
16840 O O   . ALA B 1074 ? 0.2410 0.2014 0.2423 0.0462  -0.0026 -0.0026 1072 ALA B O   
16841 C CB  . ALA B 1074 ? 0.3030 0.2509 0.3010 0.0424  -0.0042 0.0019  1072 ALA B CB  
16842 N N   . GLY B 1075 ? 0.2294 0.1783 0.2261 0.0505  -0.0036 -0.0020 1073 GLY B N   
16843 C CA  . GLY B 1075 ? 0.2635 0.2128 0.2598 0.0526  -0.0030 -0.0045 1073 GLY B CA  
16844 C C   . GLY B 1075 ? 0.2929 0.2514 0.2918 0.0544  -0.0021 -0.0049 1073 GLY B C   
16845 O O   . GLY B 1075 ? 0.2809 0.2430 0.2808 0.0538  -0.0014 -0.0068 1073 GLY B O   
16846 N N   . SER B 1076 ? 0.2964 0.2590 0.2965 0.0564  -0.0021 -0.0031 1074 SER B N   
16847 C CA  . SER B 1076 ? 0.2603 0.2319 0.2630 0.0580  -0.0013 -0.0033 1074 SER B CA  
16848 C C   . SER B 1076 ? 0.2804 0.2587 0.2858 0.0542  -0.0010 -0.0032 1074 SER B C   
16849 O O   . SER B 1076 ? 0.2919 0.2759 0.2990 0.0540  -0.0003 -0.0044 1074 SER B O   
16850 C CB  . SER B 1076 ? 0.3256 0.2995 0.3287 0.0615  -0.0016 -0.0013 1074 SER B CB  
16851 O OG  . SER B 1076 ? 0.3538 0.3227 0.3548 0.0658  -0.0017 -0.0017 1074 SER B OG  
16852 N N   . SER B 1077 ? 0.2477 0.2251 0.2532 0.0513  -0.0015 -0.0017 1075 SER B N   
16853 C CA  . SER B 1077 ? 0.2885 0.2722 0.2962 0.0481  -0.0012 -0.0016 1075 SER B CA  
16854 C C   . SER B 1077 ? 0.2573 0.2401 0.2654 0.0450  -0.0009 -0.0033 1075 SER B C   
16855 O O   . SER B 1077 ? 0.3065 0.2945 0.3163 0.0428  -0.0005 -0.0037 1075 SER B O   
16856 C CB  . SER B 1077 ? 0.3685 0.3525 0.3761 0.0465  -0.0017 0.0007  1075 SER B CB  
16857 O OG  . SER B 1077 ? 0.3796 0.3576 0.3860 0.0440  -0.0019 0.0011  1075 SER B OG  
16858 N N   . SER B 1078 ? 0.2245 0.2007 0.2308 0.0447  -0.0011 -0.0044 1076 SER B N   
16859 C CA  . SER B 1078 ? 0.2363 0.2118 0.2428 0.0421  -0.0009 -0.0061 1076 SER B CA  
16860 C C   . SER B 1078 ? 0.2164 0.1976 0.2243 0.0429  -0.0002 -0.0077 1076 SER B C   
16861 O O   . SER B 1078 ? 0.2384 0.2212 0.2460 0.0461  0.0002  -0.0082 1076 SER B O   
16862 C CB  . SER B 1078 ? 0.2366 0.2042 0.2406 0.0423  -0.0014 -0.0072 1076 SER B CB  
16863 O OG  . SER B 1078 ? 0.2099 0.1772 0.2141 0.0402  -0.0014 -0.0090 1076 SER B OG  
16864 N N   . ALA B 1079 ? 0.1909 0.1752 0.2002 0.0400  0.0001  -0.0085 1077 ALA B N   
16865 C CA  . ALA B 1079 ? 0.1916 0.1806 0.2019 0.0402  0.0007  -0.0100 1077 ALA B CA  
16866 C C   . ALA B 1079 ? 0.2100 0.1955 0.2190 0.0393  0.0007  -0.0119 1077 ALA B C   
16867 O O   . ALA B 1079 ? 0.2081 0.1970 0.2177 0.0387  0.0011  -0.0130 1077 ALA B O   
16868 C CB  . ALA B 1079 ? 0.2271 0.2221 0.2395 0.0377  0.0009  -0.0096 1077 ALA B CB  
16869 N N   . LEU B 1080 ? 0.2067 0.1852 0.2138 0.0391  0.0000  -0.0121 1078 LEU B N   
16870 C CA  . LEU B 1080 ? 0.1909 0.1655 0.1963 0.0386  -0.0002 -0.0140 1078 LEU B CA  
16871 C C   . LEU B 1080 ? 0.1910 0.1676 0.1955 0.0415  0.0006  -0.0154 1078 LEU B C   
16872 O O   . LEU B 1080 ? 0.2287 0.2052 0.2324 0.0448  0.0009  -0.0152 1078 LEU B O   
16873 C CB  . LEU B 1080 ? 0.1988 0.1652 0.2016 0.0388  -0.0011 -0.0139 1078 LEU B CB  
16874 C CG  . LEU B 1080 ? 0.2227 0.1841 0.2231 0.0387  -0.0015 -0.0160 1078 LEU B CG  
16875 C CD1 . LEU B 1080 ? 0.2279 0.1900 0.2293 0.0350  -0.0020 -0.0165 1078 LEU B CD1 
16876 C CD2 . LEU B 1080 ? 0.2255 0.1785 0.2229 0.0397  -0.0024 -0.0159 1078 LEU B CD2 
16877 N N   . GLY B 1081 ? 0.1981 0.1765 0.2026 0.0402  0.0008  -0.0169 1079 GLY B N   
16878 C CA  . GLY B 1081 ? 0.2100 0.1908 0.2136 0.0426  0.0017  -0.0182 1079 GLY B CA  
16879 C C   . GLY B 1081 ? 0.2344 0.2236 0.2406 0.0426  0.0026  -0.0177 1079 GLY B C   
16880 O O   . GLY B 1081 ? 0.2335 0.2257 0.2393 0.0442  0.0035  -0.0187 1079 GLY B O   
16881 N N   . LEU B 1082 ? 0.2105 0.2033 0.2190 0.0408  0.0024  -0.0163 1080 LEU B N   
16882 C CA  A LEU B 1082 ? 0.2242 0.2245 0.2350 0.0400  0.0030  -0.0159 1080 LEU B CA  
16883 C CA  B LEU B 1082 ? 0.2241 0.2244 0.2349 0.0400  0.0030  -0.0159 1080 LEU B CA  
16884 C C   . LEU B 1082 ? 0.2208 0.2221 0.2312 0.0383  0.0033  -0.0173 1080 LEU B C   
16885 O O   . LEU B 1082 ? 0.2190 0.2164 0.2284 0.0363  0.0027  -0.0180 1080 LEU B O   
16886 C CB  A LEU B 1082 ? 0.1981 0.2005 0.2108 0.0376  0.0025  -0.0145 1080 LEU B CB  
16887 C CB  B LEU B 1082 ? 0.1984 0.2008 0.2111 0.0376  0.0025  -0.0145 1080 LEU B CB  
16888 C CG  A LEU B 1082 ? 0.2098 0.2191 0.2245 0.0361  0.0028  -0.0141 1080 LEU B CG  
16889 C CG  B LEU B 1082 ? 0.2101 0.2193 0.2248 0.0361  0.0028  -0.0140 1080 LEU B CG  
16890 C CD1 A LEU B 1082 ? 0.2454 0.2597 0.2609 0.0387  0.0035  -0.0137 1080 LEU B CD1 
16891 C CD1 B LEU B 1082 ? 0.2156 0.2265 0.2316 0.0352  0.0024  -0.0124 1080 LEU B CD1 
16892 C CD2 A LEU B 1082 ? 0.2204 0.2308 0.2363 0.0343  0.0023  -0.0127 1080 LEU B CD2 
16893 C CD2 B LEU B 1082 ? 0.2121 0.2217 0.2270 0.0332  0.0027  -0.0149 1080 LEU B CD2 
16894 N N   . ASP B 1083 ? 0.2018 0.2086 0.2129 0.0391  0.0041  -0.0175 1081 ASP B N   
16895 C CA  . ASP B 1083 ? 0.2456 0.2534 0.2560 0.0378  0.0045  -0.0187 1081 ASP B CA  
16896 C C   . ASP B 1083 ? 0.2498 0.2652 0.2623 0.0373  0.0052  -0.0180 1081 ASP B C   
16897 O O   . ASP B 1083 ? 0.2946 0.3138 0.3074 0.0398  0.0061  -0.0179 1081 ASP B O   
16898 C CB  . ASP B 1083 ? 0.2821 0.2865 0.2897 0.0402  0.0050  -0.0202 1081 ASP B CB  
16899 C CG  . ASP B 1083 ? 0.3806 0.3858 0.3869 0.0390  0.0054  -0.0214 1081 ASP B CG  
16900 O OD1 . ASP B 1083 ? 0.4359 0.4423 0.4431 0.0359  0.0049  -0.0212 1081 ASP B OD1 
16901 O OD2 . ASP B 1083 ? 0.4761 0.4806 0.4804 0.0412  0.0062  -0.0225 1081 ASP B OD2 
16902 N N   . LEU B 1084 ? 0.2403 0.2579 0.2541 0.0343  0.0047  -0.0175 1082 LEU B N   
16903 C CA  . LEU B 1084 ? 0.2214 0.2457 0.2372 0.0333  0.0051  -0.0167 1082 LEU B CA  
16904 C C   . LEU B 1084 ? 0.2262 0.2515 0.2416 0.0308  0.0051  -0.0173 1082 LEU B C   
16905 O O   . LEU B 1084 ? 0.2191 0.2401 0.2333 0.0292  0.0046  -0.0180 1082 LEU B O   
16906 C CB  . LEU B 1084 ? 0.2653 0.2908 0.2826 0.0316  0.0043  -0.0155 1082 LEU B CB  
16907 C CG  . LEU B 1084 ? 0.3075 0.3328 0.3254 0.0336  0.0041  -0.0145 1082 LEU B CG  
16908 C CD1 . LEU B 1084 ? 0.3135 0.3396 0.3325 0.0315  0.0034  -0.0135 1082 LEU B CD1 
16909 C CD2 . LEU B 1084 ? 0.3453 0.3760 0.3644 0.0362  0.0048  -0.0139 1082 LEU B CD2 
16910 N N   . GLU B 1085 ? 0.2160 0.2470 0.2324 0.0304  0.0057  -0.0169 1083 GLU B N   
16911 C CA  . GLU B 1085 ? 0.1950 0.2276 0.2113 0.0275  0.0056  -0.0170 1083 GLU B CA  
16912 C C   . GLU B 1085 ? 0.2098 0.2455 0.2279 0.0253  0.0050  -0.0159 1083 GLU B C   
16913 O O   . GLU B 1085 ? 0.2468 0.2872 0.2665 0.0260  0.0051  -0.0149 1083 GLU B O   
16914 C CB  . GLU B 1085 ? 0.2220 0.2588 0.2380 0.0280  0.0067  -0.0171 1083 GLU B CB  
16915 C CG  . GLU B 1085 ? 0.2561 0.2940 0.2718 0.0248  0.0064  -0.0170 1083 GLU B CG  
16916 C CD  . GLU B 1085 ? 0.3261 0.3673 0.3409 0.0248  0.0075  -0.0172 1083 GLU B CD  
16917 O OE1 . GLU B 1085 ? 0.3567 0.3990 0.3708 0.0276  0.0086  -0.0176 1083 GLU B OE1 
16918 O OE2 . GLU B 1085 ? 0.3340 0.3763 0.3485 0.0221  0.0072  -0.0168 1083 GLU B OE2 
16919 N N   . LEU B 1086 ? 0.2056 0.2388 0.2233 0.0228  0.0042  -0.0160 1084 LEU B N   
16920 C CA  . LEU B 1086 ? 0.2049 0.2398 0.2236 0.0206  0.0035  -0.0153 1084 LEU B CA  
16921 C C   . LEU B 1086 ? 0.2754 0.3140 0.2944 0.0184  0.0036  -0.0150 1084 LEU B C   
16922 O O   . LEU B 1086 ? 0.2585 0.2963 0.2764 0.0177  0.0038  -0.0155 1084 LEU B O   
16923 C CB  . LEU B 1086 ? 0.2129 0.2428 0.2310 0.0193  0.0028  -0.0157 1084 LEU B CB  
16924 C CG  . LEU B 1086 ? 0.2428 0.2689 0.2608 0.0209  0.0026  -0.0158 1084 LEU B CG  
16925 C CD1 . LEU B 1086 ? 0.2214 0.2437 0.2391 0.0194  0.0020  -0.0160 1084 LEU B CD1 
16926 C CD2 . LEU B 1086 ? 0.2747 0.3035 0.2937 0.0225  0.0027  -0.0149 1084 LEU B CD2 
16927 N N   . PRO B 1087 ? 0.2492 0.2919 0.2694 0.0171  0.0032  -0.0141 1085 PRO B N   
16928 C CA  . PRO B 1087 ? 0.2924 0.3382 0.3126 0.0146  0.0030  -0.0137 1085 PRO B CA  
16929 C C   . PRO B 1087 ? 0.2486 0.2900 0.2673 0.0122  0.0024  -0.0142 1085 PRO B C   
16930 O O   . PRO B 1087 ? 0.2658 0.3032 0.2840 0.0119  0.0018  -0.0146 1085 PRO B O   
16931 C CB  . PRO B 1087 ? 0.2707 0.3205 0.2924 0.0136  0.0024  -0.0127 1085 PRO B CB  
16932 C CG  . PRO B 1087 ? 0.3077 0.3583 0.3304 0.0164  0.0026  -0.0124 1085 PRO B CG  
16933 C CD  . PRO B 1087 ? 0.2679 0.3127 0.2894 0.0181  0.0029  -0.0133 1085 PRO B CD  
16934 N N   . GLY B 1088 ? 0.2388 0.2811 0.2567 0.0107  0.0026  -0.0142 1086 GLY B N   
16935 C CA  . GLY B 1088 ? 0.2402 0.2783 0.2565 0.0087  0.0019  -0.0146 1086 GLY B CA  
16936 C C   . GLY B 1088 ? 0.2085 0.2488 0.2241 0.0066  0.0021  -0.0141 1086 GLY B C   
16937 O O   . GLY B 1088 ? 0.2335 0.2792 0.2502 0.0063  0.0026  -0.0133 1086 GLY B O   
16938 N N   . PRO B 1089 ? 0.2209 0.2572 0.2347 0.0053  0.0017  -0.0144 1087 PRO B N   
16939 C CA  . PRO B 1089 ? 0.2318 0.2697 0.2446 0.0032  0.0017  -0.0138 1087 PRO B CA  
16940 C C   . PRO B 1089 ? 0.2116 0.2523 0.2241 0.0046  0.0030  -0.0137 1087 PRO B C   
16941 O O   . PRO B 1089 ? 0.2328 0.2725 0.2453 0.0072  0.0036  -0.0145 1087 PRO B O   
16942 C CB  . PRO B 1089 ? 0.2533 0.2853 0.2642 0.0021  0.0009  -0.0143 1087 PRO B CB  
16943 C CG  . PRO B 1089 ? 0.2904 0.3188 0.3015 0.0044  0.0008  -0.0153 1087 PRO B CG  
16944 C CD  . PRO B 1089 ? 0.2574 0.2880 0.2703 0.0057  0.0010  -0.0153 1087 PRO B CD  
16945 N N   . VAL B 1090 ? 0.2025 0.2469 0.2147 0.0027  0.0034  -0.0128 1088 VAL B N   
16946 C CA  . VAL B 1090 ? 0.1919 0.2388 0.2033 0.0038  0.0047  -0.0127 1088 VAL B CA  
16947 C C   . VAL B 1090 ? 0.2002 0.2417 0.2091 0.0043  0.0044  -0.0136 1088 VAL B C   
16948 O O   . VAL B 1090 ? 0.2103 0.2468 0.2182 0.0031  0.0032  -0.0139 1088 VAL B O   
16949 C CB  . VAL B 1090 ? 0.2082 0.2601 0.2197 0.0013  0.0051  -0.0113 1088 VAL B CB  
16950 C CG1 . VAL B 1090 ? 0.2106 0.2685 0.2250 0.0007  0.0052  -0.0104 1088 VAL B CG1 
16951 C CG2 . VAL B 1090 ? 0.2172 0.2653 0.2267 -0.0020 0.0040  -0.0108 1088 VAL B CG2 
16952 N N   . GLY B 1091 ? 0.2047 0.2472 0.2125 0.0061  0.0056  -0.0140 1089 GLY B N   
16953 C CA  . GLY B 1091 ? 0.2153 0.2530 0.2204 0.0065  0.0053  -0.0148 1089 GLY B CA  
16954 C C   . GLY B 1091 ? 0.2174 0.2499 0.2224 0.0082  0.0045  -0.0161 1089 GLY B C   
16955 O O   . GLY B 1091 ? 0.2062 0.2343 0.2093 0.0081  0.0038  -0.0167 1089 GLY B O   
16956 N N   . GLU B 1092 ? 0.2065 0.2396 0.2136 0.0097  0.0045  -0.0164 1090 GLU B N   
16957 C CA  . GLU B 1092 ? 0.2140 0.2426 0.2212 0.0113  0.0038  -0.0174 1090 GLU B CA  
16958 C C   . GLU B 1092 ? 0.2251 0.2559 0.2337 0.0139  0.0047  -0.0176 1090 GLU B C   
16959 O O   . GLU B 1092 ? 0.2500 0.2856 0.2603 0.0139  0.0053  -0.0169 1090 GLU B O   
16960 C CB  . GLU B 1092 ? 0.2372 0.2633 0.2455 0.0097  0.0026  -0.0171 1090 GLU B CB  
16961 C CG  . GLU B 1092 ? 0.3365 0.3572 0.3439 0.0097  0.0016  -0.0178 1090 GLU B CG  
16962 C CD  . GLU B 1092 ? 0.3516 0.3704 0.3601 0.0083  0.0006  -0.0175 1090 GLU B CD  
16963 O OE1 . GLU B 1092 ? 0.3068 0.3268 0.3170 0.0087  0.0007  -0.0174 1090 GLU B OE1 
16964 O OE2 . GLU B 1092 ? 0.3491 0.3653 0.3565 0.0069  -0.0003 -0.0174 1090 GLU B OE2 
16965 N N   . ARG B 1093 ? 0.2080 0.2353 0.2158 0.0159  0.0046  -0.0187 1091 ARG B N   
16966 C CA  . ARG B 1093 ? 0.2015 0.2295 0.2105 0.0184  0.0051  -0.0189 1091 ARG B CA  
16967 C C   . ARG B 1093 ? 0.2030 0.2265 0.2126 0.0184  0.0040  -0.0192 1091 ARG B C   
16968 O O   . ARG B 1093 ? 0.2093 0.2283 0.2176 0.0182  0.0033  -0.0199 1091 ARG B O   
16969 C CB  . ARG B 1093 ? 0.2244 0.2519 0.2317 0.0211  0.0061  -0.0198 1091 ARG B CB  
16970 C CG  . ARG B 1093 ? 0.3599 0.3932 0.3673 0.0220  0.0076  -0.0194 1091 ARG B CG  
16971 C CD  . ARG B 1093 ? 0.4619 0.4950 0.4681 0.0255  0.0087  -0.0203 1091 ARG B CD  
16972 N NE  . ARG B 1093 ? 0.5499 0.5775 0.5528 0.0262  0.0084  -0.0217 1091 ARG B NE  
16973 C CZ  . ARG B 1093 ? 0.6037 0.6315 0.6040 0.0261  0.0091  -0.0223 1091 ARG B CZ  
16974 N NH1 . ARG B 1093 ? 0.5410 0.5744 0.5415 0.0255  0.0102  -0.0215 1091 ARG B NH1 
16975 N NH2 . ARG B 1093 ? 0.5694 0.5917 0.5666 0.0265  0.0085  -0.0236 1091 ARG B NH2 
16976 N N   . ASN B 1094 ? 0.1792 0.2042 0.1908 0.0185  0.0039  -0.0186 1092 ASN B N   
16977 C CA  . ASN B 1094 ? 0.1766 0.1980 0.1890 0.0183  0.0030  -0.0186 1092 ASN B CA  
16978 C C   . ASN B 1094 ? 0.2008 0.2220 0.2138 0.0207  0.0034  -0.0186 1092 ASN B C   
16979 O O   . ASN B 1094 ? 0.2158 0.2408 0.2302 0.0216  0.0039  -0.0179 1092 ASN B O   
16980 C CB  . ASN B 1094 ? 0.1992 0.2220 0.2129 0.0162  0.0025  -0.0179 1092 ASN B CB  
16981 C CG  . ASN B 1094 ? 0.2067 0.2279 0.2194 0.0140  0.0019  -0.0180 1092 ASN B CG  
16982 O OD1 . ASN B 1094 ? 0.2001 0.2174 0.2121 0.0136  0.0012  -0.0185 1092 ASN B OD1 
16983 N ND2 . ASN B 1094 ? 0.2113 0.2357 0.2238 0.0125  0.0021  -0.0174 1092 ASN B ND2 
16984 N N   . LEU B 1095 ? 0.1743 0.1909 0.1862 0.0218  0.0031  -0.0194 1093 LEU B N   
16985 C CA  . LEU B 1095 ? 0.1712 0.1863 0.1830 0.0242  0.0033  -0.0195 1093 LEU B CA  
16986 C C   . LEU B 1095 ? 0.1737 0.1857 0.1864 0.0238  0.0026  -0.0191 1093 LEU B C   
16987 O O   . LEU B 1095 ? 0.1972 0.2068 0.2100 0.0220  0.0018  -0.0192 1093 LEU B O   
16988 C CB  . LEU B 1095 ? 0.2167 0.2284 0.2261 0.0258  0.0035  -0.0207 1093 LEU B CB  
16989 C CG  . LEU B 1095 ? 0.2378 0.2525 0.2459 0.0261  0.0044  -0.0211 1093 LEU B CG  
16990 C CD1 . LEU B 1095 ? 0.2613 0.2720 0.2665 0.0276  0.0045  -0.0225 1093 LEU B CD1 
16991 C CD2 . LEU B 1095 ? 0.2600 0.2806 0.2696 0.0275  0.0055  -0.0204 1093 LEU B CD2 
16992 N N   . TYR B 1096 ? 0.1618 0.1739 0.1751 0.0255  0.0028  -0.0186 1094 TYR B N   
16993 C CA  . TYR B 1096 ? 0.1654 0.1749 0.1794 0.0252  0.0022  -0.0180 1094 TYR B CA  
16994 C C   . TYR B 1096 ? 0.1896 0.1963 0.2027 0.0277  0.0023  -0.0181 1094 TYR B C   
16995 O O   . TYR B 1096 ? 0.1878 0.1969 0.2009 0.0298  0.0030  -0.0178 1094 TYR B O   
16996 C CB  . TYR B 1096 ? 0.1695 0.1827 0.1853 0.0244  0.0022  -0.0169 1094 TYR B CB  
16997 C CG  . TYR B 1096 ? 0.1882 0.1995 0.2046 0.0243  0.0019  -0.0161 1094 TYR B CG  
16998 C CD1 . TYR B 1096 ? 0.1879 0.1971 0.2047 0.0224  0.0014  -0.0160 1094 TYR B CD1 
16999 C CD2 . TYR B 1096 ? 0.2174 0.2293 0.2340 0.0262  0.0021  -0.0152 1094 TYR B CD2 
17000 C CE1 . TYR B 1096 ? 0.1999 0.2078 0.2173 0.0223  0.0013  -0.0151 1094 TYR B CE1 
17001 C CE2 . TYR B 1096 ? 0.2123 0.2226 0.2293 0.0261  0.0018  -0.0143 1094 TYR B CE2 
17002 C CZ  . TYR B 1096 ? 0.2166 0.2249 0.2339 0.0240  0.0014  -0.0142 1094 TYR B CZ  
17003 O OH  . TYR B 1096 ? 0.2135 0.2205 0.2311 0.0238  0.0013  -0.0132 1094 TYR B OH  
17004 N N   . THR B 1097 ? 0.1787 0.1801 0.1909 0.0274  0.0017  -0.0184 1095 THR B N   
17005 C CA  . THR B 1097 ? 0.1882 0.1857 0.1989 0.0295  0.0016  -0.0186 1095 THR B CA  
17006 C C   . THR B 1097 ? 0.1679 0.1616 0.1789 0.0286  0.0009  -0.0178 1095 THR B C   
17007 O O   . THR B 1097 ? 0.1983 0.1913 0.2103 0.0263  0.0004  -0.0176 1095 THR B O   
17008 C CB  . THR B 1097 ? 0.2437 0.2376 0.2519 0.0301  0.0015  -0.0202 1095 THR B CB  
17009 O OG1 . THR B 1097 ? 0.2821 0.2735 0.2903 0.0275  0.0006  -0.0206 1095 THR B OG1 
17010 C CG2 . THR B 1097 ? 0.2440 0.2418 0.2517 0.0309  0.0024  -0.0208 1095 THR B CG2 
17011 N N   . LEU B 1098 ? 0.1873 0.1786 0.1976 0.0306  0.0009  -0.0173 1096 LEU B N   
17012 C CA  . LEU B 1098 ? 0.1754 0.1628 0.1858 0.0297  0.0003  -0.0164 1096 LEU B CA  
17013 C C   . LEU B 1098 ? 0.1911 0.1721 0.1991 0.0306  -0.0003 -0.0172 1096 LEU B C   
17014 O O   . LEU B 1098 ? 0.2032 0.1825 0.2095 0.0333  -0.0001 -0.0177 1096 LEU B O   
17015 C CB  . LEU B 1098 ? 0.1750 0.1642 0.1863 0.0310  0.0005  -0.0148 1096 LEU B CB  
17016 C CG  . LEU B 1098 ? 0.1897 0.1848 0.2031 0.0299  0.0009  -0.0140 1096 LEU B CG  
17017 C CD1 . LEU B 1098 ? 0.2003 0.1968 0.2141 0.0312  0.0010  -0.0124 1096 LEU B CD1 
17018 C CD2 . LEU B 1098 ? 0.1974 0.1926 0.2118 0.0270  0.0006  -0.0139 1096 LEU B CD2 
17019 N N   . HIS B 1099 ? 0.1851 0.1626 0.1930 0.0283  -0.0012 -0.0173 1097 HIS B N   
17020 C CA  . HIS B 1099 ? 0.2053 0.1762 0.2108 0.0283  -0.0021 -0.0181 1097 HIS B CA  
17021 C C   . HIS B 1099 ? 0.1885 0.1561 0.1945 0.0270  -0.0028 -0.0166 1097 HIS B C   
17022 O O   . HIS B 1099 ? 0.2054 0.1761 0.2137 0.0259  -0.0024 -0.0151 1097 HIS B O   
17023 C CB  . HIS B 1099 ? 0.2174 0.1873 0.2225 0.0262  -0.0028 -0.0193 1097 HIS B CB  
17024 C CG  . HIS B 1099 ? 0.2544 0.2276 0.2589 0.0271  -0.0022 -0.0206 1097 HIS B CG  
17025 N ND1 . HIS B 1099 ? 0.2829 0.2532 0.2844 0.0286  -0.0022 -0.0222 1097 HIS B ND1 
17026 C CD2 . HIS B 1099 ? 0.2850 0.2639 0.2913 0.0265  -0.0015 -0.0204 1097 HIS B CD2 
17027 C CE1 . HIS B 1099 ? 0.2885 0.2630 0.2901 0.0289  -0.0015 -0.0229 1097 HIS B CE1 
17028 N NE2 . HIS B 1099 ? 0.2810 0.2606 0.2855 0.0276  -0.0011 -0.0218 1097 HIS B NE2 
17029 N N   . ALA B 1100 ? 0.2139 0.1750 0.2177 0.0269  -0.0037 -0.0170 1098 ALA B N   
17030 C CA  . ALA B 1100 ? 0.2289 0.1866 0.2332 0.0250  -0.0045 -0.0156 1098 ALA B CA  
17031 C C   . ALA B 1100 ? 0.2318 0.1921 0.2386 0.0216  -0.0048 -0.0152 1098 ALA B C   
17032 O O   . ALA B 1100 ? 0.2574 0.2194 0.2646 0.0207  -0.0050 -0.0164 1098 ALA B O   
17033 C CB  . ALA B 1100 ? 0.2527 0.2025 0.2538 0.0252  -0.0056 -0.0163 1098 ALA B CB  
17034 N N   . ARG B 1101 ? 0.2237 0.1843 0.2323 0.0199  -0.0049 -0.0134 1099 ARG B N   
17035 C CA  . ARG B 1101 ? 0.2341 0.1970 0.2452 0.0169  -0.0052 -0.0128 1099 ARG B CA  
17036 C C   . ARG B 1101 ? 0.2494 0.2078 0.2597 0.0148  -0.0067 -0.0135 1099 ARG B C   
17037 O O   . ARG B 1101 ? 0.2611 0.2215 0.2729 0.0130  -0.0071 -0.0140 1099 ARG B O   
17038 C CB  . ARG B 1101 ? 0.2704 0.2350 0.2834 0.0157  -0.0047 -0.0107 1099 ARG B CB  
17039 C CG  . ARG B 1101 ? 0.2746 0.2451 0.2891 0.0167  -0.0034 -0.0100 1099 ARG B CG  
17040 C CD  . ARG B 1101 ? 0.3309 0.3060 0.3482 0.0147  -0.0030 -0.0099 1099 ARG B CD  
17041 N NE  . ARG B 1101 ? 0.2790 0.2591 0.2973 0.0156  -0.0019 -0.0095 1099 ARG B NE  
17042 C CZ  . ARG B 1101 ? 0.2809 0.2648 0.3013 0.0142  -0.0013 -0.0090 1099 ARG B CZ  
17043 N NH1 . ARG B 1101 ? 0.2805 0.2644 0.3026 0.0121  -0.0016 -0.0086 1099 ARG B NH1 
17044 N NH2 . ARG B 1101 ? 0.3358 0.3236 0.3565 0.0151  -0.0004 -0.0088 1099 ARG B NH2 
17045 N N   . GLY B 1102 ? 0.2381 0.1901 0.2458 0.0151  -0.0075 -0.0135 1100 GLY B N   
17046 C CA  . GLY B 1102 ? 0.2565 0.2038 0.2632 0.0127  -0.0091 -0.0140 1100 GLY B CA  
17047 C C   . GLY B 1102 ? 0.2679 0.2099 0.2736 0.0116  -0.0098 -0.0125 1100 GLY B C   
17048 O O   . GLY B 1102 ? 0.2817 0.2198 0.2850 0.0138  -0.0097 -0.0123 1100 GLY B O   
17049 N N   . ARG B 1103 ? 0.2419 0.1837 0.2496 0.0083  -0.0107 -0.0112 1101 ARG B N   
17050 C CA  . ARG B 1103 ? 0.2663 0.2034 0.2733 0.0067  -0.0113 -0.0095 1101 ARG B CA  
17051 C C   . ARG B 1103 ? 0.2477 0.1897 0.2578 0.0058  -0.0101 -0.0071 1101 ARG B C   
17052 O O   . ARG B 1103 ? 0.2572 0.2052 0.2708 0.0042  -0.0096 -0.0066 1101 ARG B O   
17053 C CB  . ARG B 1103 ? 0.2563 0.1894 0.2631 0.0033  -0.0133 -0.0096 1101 ARG B CB  
17054 C CG  . ARG B 1103 ? 0.2917 0.2190 0.2971 0.0016  -0.0141 -0.0078 1101 ARG B CG  
17055 C CD  . ARG B 1103 ? 0.3636 0.2854 0.3679 -0.0017 -0.0163 -0.0082 1101 ARG B CD  
17056 N NE  . ARG B 1103 ? 0.4393 0.3536 0.4387 0.0001  -0.0175 -0.0104 1101 ARG B NE  
17057 C CZ  . ARG B 1103 ? 0.4617 0.3746 0.4595 -0.0001 -0.0186 -0.0127 1101 ARG B CZ  
17058 N NH1 . ARG B 1103 ? 0.5571 0.4757 0.5580 -0.0020 -0.0189 -0.0130 1101 ARG B NH1 
17059 N NH2 . ARG B 1103 ? 0.4502 0.3558 0.4430 0.0018  -0.0194 -0.0147 1101 ARG B NH2 
17060 N N   . ILE B 1104 ? 0.2111 0.1509 0.2199 0.0070  -0.0096 -0.0056 1102 ILE B N   
17061 C CA  . ILE B 1104 ? 0.2277 0.1718 0.2388 0.0065  -0.0083 -0.0033 1102 ILE B CA  
17062 C C   . ILE B 1104 ? 0.2398 0.1805 0.2511 0.0034  -0.0091 -0.0011 1102 ILE B C   
17063 O O   . ILE B 1104 ? 0.2384 0.1718 0.2468 0.0033  -0.0103 -0.0009 1102 ILE B O   
17064 C CB  . ILE B 1104 ? 0.2326 0.1770 0.2420 0.0099  -0.0073 -0.0029 1102 ILE B CB  
17065 C CG1 . ILE B 1104 ? 0.2310 0.1784 0.2400 0.0128  -0.0067 -0.0051 1102 ILE B CG1 
17066 C CG2 . ILE B 1104 ? 0.2367 0.1862 0.2483 0.0093  -0.0060 -0.0006 1102 ILE B CG2 
17067 C CD1 . ILE B 1104 ? 0.2276 0.1824 0.2397 0.0121  -0.0058 -0.0056 1102 ILE B CD1 
17068 N N   . LEU B 1105 ? 0.2168 0.1626 0.2315 0.0010  -0.0084 0.0005  1103 LEU B N   
17069 C CA  . LEU B 1105 ? 0.2387 0.1824 0.2540 -0.0021 -0.0088 0.0030  1103 LEU B CA  
17070 C C   . LEU B 1105 ? 0.2199 0.1625 0.2336 -0.0007 -0.0078 0.0050  1103 LEU B C   
17071 O O   . LEU B 1105 ? 0.2340 0.1819 0.2488 0.0011  -0.0063 0.0054  1103 LEU B O   
17072 C CB  . LEU B 1105 ? 0.2313 0.1818 0.2510 -0.0048 -0.0081 0.0040  1103 LEU B CB  
17073 C CG  . LEU B 1105 ? 0.2583 0.2088 0.2795 -0.0082 -0.0081 0.0069  1103 LEU B CG  
17074 C CD1 . LEU B 1105 ? 0.2476 0.1911 0.2673 -0.0110 -0.0102 0.0071  1103 LEU B CD1 
17075 C CD2 . LEU B 1105 ? 0.2326 0.1913 0.2584 -0.0100 -0.0070 0.0077  1103 LEU B CD2 
17076 N N   . LEU B 1106 ? 0.2165 0.1519 0.2275 -0.0013 -0.0089 0.0062  1104 LEU B N   
17077 C CA  . LEU B 1106 ? 0.2363 0.1698 0.2454 -0.0001 -0.0083 0.0084  1104 LEU B CA  
17078 C C   . LEU B 1106 ? 0.2472 0.1805 0.2577 -0.0039 -0.0083 0.0113  1104 LEU B C   
17079 O O   . LEU B 1106 ? 0.2642 0.1929 0.2743 -0.0069 -0.0097 0.0118  1104 LEU B O   
17080 C CB  . LEU B 1106 ? 0.2352 0.1601 0.2399 0.0023  -0.0094 0.0078  1104 LEU B CB  
17081 C CG  . LEU B 1106 ? 0.3177 0.2437 0.3209 0.0070  -0.0088 0.0061  1104 LEU B CG  
17082 C CD1 . LEU B 1106 ? 0.3063 0.2384 0.3116 0.0080  -0.0081 0.0037  1104 LEU B CD1 
17083 C CD2 . LEU B 1106 ? 0.2670 0.1842 0.2659 0.0093  -0.0100 0.0052  1104 LEU B CD2 
17084 N N   . VAL B 1107 ? 0.2323 0.1706 0.2441 -0.0039 -0.0067 0.0134  1105 VAL B N   
17085 C CA  . VAL B 1107 ? 0.2415 0.1803 0.2544 -0.0073 -0.0063 0.0165  1105 VAL B CA  
17086 C C   . VAL B 1107 ? 0.2280 0.1641 0.2380 -0.0057 -0.0058 0.0186  1105 VAL B C   
17087 O O   . VAL B 1107 ? 0.2549 0.1965 0.2657 -0.0048 -0.0042 0.0198  1105 VAL B O   
17088 C CB  . VAL B 1107 ? 0.2273 0.1754 0.2446 -0.0090 -0.0047 0.0170  1105 VAL B CB  
17089 C CG1 . VAL B 1107 ? 0.2503 0.1991 0.2690 -0.0129 -0.0044 0.0202  1105 VAL B CG1 
17090 C CG2 . VAL B 1107 ? 0.2390 0.1901 0.2589 -0.0095 -0.0052 0.0145  1105 VAL B CG2 
17091 N N   . PRO B 1108 ? 0.2471 0.1746 0.2535 -0.0052 -0.0073 0.0192  1106 PRO B N   
17092 C CA  . PRO B 1108 ? 0.2762 0.2005 0.2797 -0.0035 -0.0070 0.0214  1106 PRO B CA  
17093 C C   . PRO B 1108 ? 0.2985 0.2221 0.3021 -0.0072 -0.0068 0.0250  1106 PRO B C   
17094 O O   . PRO B 1108 ? 0.3319 0.2555 0.3375 -0.0112 -0.0072 0.0258  1106 PRO B O   
17095 C CB  . PRO B 1108 ? 0.2722 0.1868 0.2717 -0.0016 -0.0089 0.0203  1106 PRO B CB  
17096 C CG  . PRO B 1108 ? 0.2853 0.1964 0.2855 -0.0048 -0.0103 0.0191  1106 PRO B CG  
17097 C CD  . PRO B 1108 ? 0.2790 0.1988 0.2835 -0.0057 -0.0093 0.0175  1106 PRO B CD  
17098 N N   . ALA B 1109 ? 0.3092 0.2324 0.3108 -0.0058 -0.0061 0.0273  1107 ALA B N   
17099 C CA  . ALA B 1109 ? 0.3083 0.2292 0.3089 -0.0087 -0.0060 0.0310  1107 ALA B CA  
17100 C C   . ALA B 1109 ? 0.3213 0.2323 0.3174 -0.0076 -0.0075 0.0324  1107 ALA B C   
17101 O O   . ALA B 1109 ? 0.3518 0.2572 0.3466 -0.0108 -0.0084 0.0348  1107 ALA B O   
17102 C CB  . ALA B 1109 ? 0.3138 0.2423 0.3154 -0.0083 -0.0039 0.0329  1107 ALA B CB  
17103 N N   . THR B 1110 ? 0.2967 0.2054 0.2903 -0.0030 -0.0079 0.0311  1108 THR B N   
17104 C CA  . THR B 1110 ? 0.3132 0.2128 0.3024 -0.0011 -0.0092 0.0325  1108 THR B CA  
17105 C C   . THR B 1110 ? 0.3271 0.2211 0.3143 0.0023  -0.0105 0.0294  1108 THR B C   
17106 O O   . THR B 1110 ? 0.2986 0.1969 0.2878 0.0040  -0.0101 0.0263  1108 THR B O   
17107 C CB  . THR B 1110 ? 0.3432 0.2453 0.3308 0.0019  -0.0083 0.0344  1108 THR B CB  
17108 O OG1 . THR B 1110 ? 0.3344 0.2424 0.3232 0.0058  -0.0075 0.0318  1108 THR B OG1 
17109 C CG2 . THR B 1110 ? 0.3542 0.2623 0.3433 -0.0012 -0.0068 0.0375  1108 THR B CG2 
17110 N N   . GLU B 1111 ? 0.3084 0.1923 0.2914 0.0035  -0.0121 0.0303  1109 GLU B N   
17111 C CA  . GLU B 1111 ? 0.3382 0.2161 0.3188 0.0071  -0.0133 0.0274  1109 GLU B CA  
17112 C C   . GLU B 1111 ? 0.3165 0.2000 0.2977 0.0122  -0.0123 0.0255  1109 GLU B C   
17113 O O   . GLU B 1111 ? 0.3226 0.2077 0.3046 0.0143  -0.0123 0.0223  1109 GLU B O   
17114 C CB  . GLU B 1111 ? 0.3354 0.2014 0.3111 0.0078  -0.0150 0.0289  1109 GLU B CB  
17115 C CG  . GLU B 1111 ? 0.3720 0.2318 0.3447 0.0126  -0.0160 0.0262  1109 GLU B CG  
17116 C CD  . GLU B 1111 ? 0.4056 0.2528 0.3731 0.0134  -0.0178 0.0277  1109 GLU B CD  
17117 O OE1 . GLU B 1111 ? 0.4369 0.2765 0.4026 0.0101  -0.0192 0.0273  1109 GLU B OE1 
17118 O OE2 . GLU B 1111 ? 0.4646 0.3095 0.4298 0.0171  -0.0178 0.0292  1109 GLU B OE2 
17119 N N   . SER B 1112 ? 0.2994 0.1862 0.2803 0.0142  -0.0115 0.0277  1110 SER B N   
17120 C CA  . SER B 1112 ? 0.3304 0.2233 0.3121 0.0188  -0.0107 0.0262  1110 SER B CA  
17121 C C   . SER B 1112 ? 0.3255 0.2281 0.3114 0.0178  -0.0093 0.0239  1110 SER B C   
17122 O O   . SER B 1112 ? 0.3151 0.2208 0.3019 0.0208  -0.0090 0.0212  1110 SER B O   
17123 C CB  . SER B 1112 ? 0.3807 0.2758 0.3613 0.0205  -0.0102 0.0291  1110 SER B CB  
17124 O OG  . SER B 1112 ? 0.3888 0.2904 0.3706 0.0245  -0.0095 0.0277  1110 SER B OG  
17125 N N   . GLY B 1113 ? 0.3000 0.2074 0.2884 0.0138  -0.0084 0.0251  1111 GLY B N   
17126 C CA  . GLY B 1113 ? 0.2907 0.2066 0.2829 0.0128  -0.0072 0.0230  1111 GLY B CA  
17127 C C   . GLY B 1113 ? 0.2753 0.1892 0.2682 0.0128  -0.0079 0.0197  1111 GLY B C   
17128 O O   . GLY B 1113 ? 0.2775 0.1966 0.2721 0.0146  -0.0073 0.0172  1111 GLY B O   
17129 N N   . LEU B 1114 ? 0.2736 0.1799 0.2649 0.0106  -0.0093 0.0198  1112 LEU B N   
17130 C CA  . LEU B 1114 ? 0.2666 0.1701 0.2579 0.0106  -0.0102 0.0167  1112 LEU B CA  
17131 C C   . LEU B 1114 ? 0.2791 0.1807 0.2684 0.0155  -0.0104 0.0143  1112 LEU B C   
17132 O O   . LEU B 1114 ? 0.2588 0.1636 0.2494 0.0166  -0.0101 0.0115  1112 LEU B O   
17133 C CB  . LEU B 1114 ? 0.2784 0.1730 0.2676 0.0075  -0.0119 0.0173  1112 LEU B CB  
17134 C CG  . LEU B 1114 ? 0.2979 0.1878 0.2860 0.0075  -0.0131 0.0142  1112 LEU B CG  
17135 C CD1 . LEU B 1114 ? 0.2839 0.1816 0.2758 0.0062  -0.0124 0.0121  1112 LEU B CD1 
17136 C CD2 . LEU B 1114 ? 0.3540 0.2346 0.3396 0.0041  -0.0150 0.0151  1112 LEU B CD2 
17137 N N   . TYR B 1115 ? 0.2892 0.1858 0.2754 0.0186  -0.0109 0.0155  1113 TYR B N   
17138 C CA  . TYR B 1115 ? 0.2959 0.1913 0.2805 0.0236  -0.0110 0.0134  1113 TYR B CA  
17139 C C   . TYR B 1115 ? 0.2798 0.1852 0.2673 0.0258  -0.0095 0.0123  1113 TYR B C   
17140 O O   . TYR B 1115 ? 0.2877 0.1948 0.2755 0.0282  -0.0093 0.0096  1113 TYR B O   
17141 C CB  . TYR B 1115 ? 0.3102 0.1990 0.2911 0.0267  -0.0117 0.0153  1113 TYR B CB  
17142 C CG  . TYR B 1115 ? 0.3181 0.1954 0.2953 0.0254  -0.0133 0.0161  1113 TYR B CG  
17143 C CD1 . TYR B 1115 ? 0.3047 0.1774 0.2813 0.0222  -0.0143 0.0145  1113 TYR B CD1 
17144 C CD2 . TYR B 1115 ? 0.3415 0.2123 0.3154 0.0272  -0.0141 0.0185  1113 TYR B CD2 
17145 C CE1 . TYR B 1115 ? 0.3505 0.2122 0.3233 0.0208  -0.0160 0.0152  1113 TYR B CE1 
17146 C CE2 . TYR B 1115 ? 0.3768 0.2363 0.3468 0.0260  -0.0157 0.0192  1113 TYR B CE2 
17147 C CZ  . TYR B 1115 ? 0.3899 0.2449 0.3595 0.0227  -0.0167 0.0175  1113 TYR B CZ  
17148 O OH  . TYR B 1115 ? 0.4430 0.2863 0.4084 0.0212  -0.0184 0.0183  1113 TYR B OH  
17149 N N   . HIS B 1116 ? 0.2662 0.1781 0.2557 0.0248  -0.0085 0.0143  1114 HIS B N   
17150 C CA  . HIS B 1116 ? 0.2755 0.1968 0.2677 0.0264  -0.0072 0.0132  1114 HIS B CA  
17151 C C   . HIS B 1116 ? 0.2857 0.2115 0.2806 0.0242  -0.0067 0.0108  1114 HIS B C   
17152 O O   . HIS B 1116 ? 0.2795 0.2102 0.2758 0.0262  -0.0062 0.0087  1114 HIS B O   
17153 C CB  . HIS B 1116 ? 0.2557 0.1824 0.2489 0.0255  -0.0064 0.0158  1114 HIS B CB  
17154 C CG  . HIS B 1116 ? 0.3093 0.2345 0.3004 0.0287  -0.0067 0.0177  1114 HIS B CG  
17155 N ND1 . HIS B 1116 ? 0.3428 0.2609 0.3310 0.0284  -0.0076 0.0203  1114 HIS B ND1 
17156 C CD2 . HIS B 1116 ? 0.3260 0.2558 0.3173 0.0322  -0.0064 0.0176  1114 HIS B CD2 
17157 C CE1 . HIS B 1116 ? 0.3517 0.2701 0.3385 0.0318  -0.0078 0.0217  1114 HIS B CE1 
17158 N NE2 . HIS B 1116 ? 0.3690 0.2948 0.3578 0.0341  -0.0071 0.0201  1114 HIS B NE2 
17159 N N   . GLN B 1117 ? 0.2367 0.1615 0.2327 0.0201  -0.0069 0.0112  1115 GLN B N   
17160 C CA  . GLN B 1117 ? 0.2234 0.1523 0.2220 0.0182  -0.0066 0.0091  1115 GLN B CA  
17161 C C   . GLN B 1117 ? 0.2362 0.1612 0.2334 0.0199  -0.0074 0.0062  1115 GLN B C   
17162 O O   . GLN B 1117 ? 0.2295 0.1592 0.2283 0.0207  -0.0068 0.0041  1115 GLN B O   
17163 C CB  . GLN B 1117 ? 0.2319 0.1602 0.2320 0.0136  -0.0068 0.0103  1115 GLN B CB  
17164 C CG  . GLN B 1117 ? 0.2367 0.1704 0.2387 0.0116  -0.0056 0.0127  1115 GLN B CG  
17165 C CD  . GLN B 1117 ? 0.2485 0.1819 0.2521 0.0071  -0.0058 0.0141  1115 GLN B CD  
17166 O OE1 . GLN B 1117 ? 0.2558 0.1838 0.2588 0.0053  -0.0070 0.0135  1115 GLN B OE1 
17167 N NE2 . GLN B 1117 ? 0.2520 0.1914 0.2579 0.0053  -0.0044 0.0157  1115 GLN B NE2 
17168 N N   . LEU B 1118 ? 0.2348 0.1511 0.2289 0.0203  -0.0087 0.0063  1116 LEU B N   
17169 C CA  . LEU B 1118 ? 0.2316 0.1434 0.2237 0.0222  -0.0094 0.0035  1116 LEU B CA  
17170 C C   . LEU B 1118 ? 0.2498 0.1652 0.2416 0.0268  -0.0086 0.0020  1116 LEU B C   
17171 O O   . LEU B 1118 ? 0.2571 0.1745 0.2493 0.0279  -0.0084 -0.0005 1116 LEU B O   
17172 C CB  . LEU B 1118 ? 0.2751 0.1762 0.2631 0.0224  -0.0109 0.0039  1116 LEU B CB  
17173 C CG  . LEU B 1118 ? 0.3318 0.2280 0.3195 0.0177  -0.0122 0.0045  1116 LEU B CG  
17174 C CD1 . LEU B 1118 ? 0.3459 0.2314 0.3294 0.0180  -0.0136 0.0056  1116 LEU B CD1 
17175 C CD2 . LEU B 1118 ? 0.3281 0.2243 0.3161 0.0167  -0.0127 0.0015  1116 LEU B CD2 
17176 N N   . ALA B 1119 ? 0.2704 0.1868 0.2616 0.0294  -0.0082 0.0037  1117 ALA B N   
17177 C CA  . ALA B 1119 ? 0.2661 0.1866 0.2575 0.0338  -0.0074 0.0026  1117 ALA B CA  
17178 C C   . ALA B 1119 ? 0.2616 0.1913 0.2564 0.0331  -0.0063 0.0013  1117 ALA B C   
17179 O O   . ALA B 1119 ? 0.2497 0.1815 0.2446 0.0351  -0.0059 -0.0010 1117 ALA B O   
17180 C CB  . ALA B 1119 ? 0.2644 0.1856 0.2552 0.0362  -0.0073 0.0050  1117 ALA B CB  
17181 N N   . ALA B 1120 ? 0.2213 0.1562 0.2186 0.0302  -0.0057 0.0026  1118 ALA B N   
17182 C CA  . ALA B 1120 ? 0.2099 0.1530 0.2102 0.0294  -0.0048 0.0014  1118 ALA B CA  
17183 C C   . ALA B 1120 ? 0.2370 0.1796 0.2378 0.0281  -0.0050 -0.0010 1118 ALA B C   
17184 O O   . ALA B 1120 ? 0.2370 0.1838 0.2387 0.0295  -0.0044 -0.0029 1118 ALA B O   
17185 C CB  . ALA B 1120 ? 0.2361 0.1838 0.2385 0.0265  -0.0041 0.0033  1118 ALA B CB  
17186 N N   . ALA B 1121 ? 0.2092 0.1469 0.2094 0.0252  -0.0058 -0.0010 1119 ALA B N   
17187 C CA  . ALA B 1121 ? 0.2359 0.1732 0.2365 0.0237  -0.0062 -0.0032 1119 ALA B CA  
17188 C C   . ALA B 1121 ? 0.2031 0.1365 0.2011 0.0266  -0.0066 -0.0055 1119 ALA B C   
17189 O O   . ALA B 1121 ? 0.2116 0.1478 0.2102 0.0269  -0.0063 -0.0075 1119 ALA B O   
17190 C CB  . ALA B 1121 ? 0.2459 0.1791 0.2466 0.0199  -0.0072 -0.0025 1119 ALA B CB  
17191 N N   . LEU B 1122 ? 0.2233 0.1500 0.2182 0.0288  -0.0073 -0.0052 1120 LEU B N   
17192 C CA  . LEU B 1122 ? 0.2315 0.1541 0.2235 0.0318  -0.0075 -0.0074 1120 LEU B CA  
17193 C C   . LEU B 1122 ? 0.2154 0.1442 0.2084 0.0354  -0.0063 -0.0083 1120 LEU B C   
17194 O O   . LEU B 1122 ? 0.2342 0.1638 0.2265 0.0369  -0.0060 -0.0106 1120 LEU B O   
17195 C CB  . LEU B 1122 ? 0.2340 0.1474 0.2222 0.0337  -0.0085 -0.0069 1120 LEU B CB  
17196 C CG  . LEU B 1122 ? 0.2820 0.1878 0.2685 0.0301  -0.0100 -0.0063 1120 LEU B CG  
17197 C CD1 . LEU B 1122 ? 0.2808 0.1777 0.2634 0.0321  -0.0109 -0.0053 1120 LEU B CD1 
17198 C CD2 . LEU B 1122 ? 0.2988 0.2022 0.2843 0.0283  -0.0108 -0.0088 1120 LEU B CD2 
17199 N N   . ALA B 1123 ? 0.2246 0.1583 0.2193 0.0366  -0.0055 -0.0065 1121 ALA B N   
17200 C CA  . ALA B 1123 ? 0.2234 0.1634 0.2193 0.0398  -0.0045 -0.0071 1121 ALA B CA  
17201 C C   . ALA B 1123 ? 0.2350 0.1816 0.2332 0.0384  -0.0038 -0.0086 1121 ALA B C   
17202 O O   . ALA B 1123 ? 0.2241 0.1750 0.2228 0.0408  -0.0030 -0.0097 1121 ALA B O   
17203 C CB  . ALA B 1123 ? 0.2301 0.1744 0.2275 0.0406  -0.0041 -0.0047 1121 ALA B CB  
17204 N N   . THR B 1124 ? 0.2104 0.1582 0.2102 0.0346  -0.0040 -0.0084 1122 THR B N   
17205 C CA  . THR B 1124 ? 0.1878 0.1412 0.1897 0.0330  -0.0035 -0.0097 1122 THR B CA  
17206 C C   . THR B 1124 ? 0.1773 0.1269 0.1779 0.0317  -0.0041 -0.0117 1122 THR B C   
17207 O O   . THR B 1124 ? 0.2168 0.1699 0.2190 0.0296  -0.0040 -0.0126 1122 THR B O   
17208 C CB  . THR B 1124 ? 0.2161 0.1740 0.2208 0.0300  -0.0032 -0.0083 1122 THR B CB  
17209 O OG1 . THR B 1124 ? 0.2111 0.1645 0.2154 0.0277  -0.0039 -0.0068 1122 THR B OG1 
17210 C CG2 . THR B 1124 ? 0.2062 0.1695 0.2122 0.0315  -0.0024 -0.0068 1122 THR B CG2 
17211 N N   . GLY B 1125 ? 0.2062 0.1485 0.2036 0.0328  -0.0049 -0.0125 1123 GLY B N   
17212 C CA  . GLY B 1125 ? 0.2257 0.1641 0.2210 0.0323  -0.0056 -0.0147 1123 GLY B CA  
17213 C C   . GLY B 1125 ? 0.2216 0.1565 0.2170 0.0283  -0.0068 -0.0145 1123 GLY B C   
17214 O O   . GLY B 1125 ? 0.2285 0.1608 0.2225 0.0274  -0.0076 -0.0163 1123 GLY B O   
17215 N N   . ASN B 1126 ? 0.2134 0.1486 0.2107 0.0259  -0.0071 -0.0124 1124 ASN B N   
17216 C CA  . ASN B 1126 ? 0.1962 0.1299 0.1945 0.0219  -0.0081 -0.0120 1124 ASN B CA  
17217 C C   . ASN B 1126 ? 0.2187 0.1435 0.2141 0.0209  -0.0096 -0.0119 1124 ASN B C   
17218 O O   . ASN B 1126 ? 0.2437 0.1634 0.2364 0.0231  -0.0098 -0.0115 1124 ASN B O   
17219 C CB  . ASN B 1126 ? 0.2078 0.1464 0.2096 0.0197  -0.0075 -0.0098 1124 ASN B CB  
17220 C CG  . ASN B 1126 ? 0.2032 0.1501 0.2077 0.0204  -0.0062 -0.0099 1124 ASN B CG  
17221 O OD1 . ASN B 1126 ? 0.2387 0.1888 0.2446 0.0193  -0.0062 -0.0111 1124 ASN B OD1 
17222 N ND2 . ASN B 1126 ? 0.1982 0.1483 0.2033 0.0222  -0.0052 -0.0087 1124 ASN B ND2 
17223 N N   . SER B 1127 ? 0.2321 0.1550 0.2279 0.0174  -0.0109 -0.0123 1125 SER B N   
17224 C CA  . SER B 1127 ? 0.2328 0.1484 0.2268 0.0151  -0.0124 -0.0114 1125 SER B CA  
17225 C C   . SER B 1127 ? 0.2354 0.1542 0.2327 0.0121  -0.0122 -0.0086 1125 SER B C   
17226 O O   . SER B 1127 ? 0.2392 0.1655 0.2399 0.0118  -0.0109 -0.0078 1125 SER B O   
17227 C CB  . SER B 1127 ? 0.2838 0.1959 0.2764 0.0127  -0.0140 -0.0132 1125 SER B CB  
17228 O OG  . SER B 1127 ? 0.3205 0.2392 0.3169 0.0101  -0.0139 -0.0131 1125 SER B OG  
17229 N N   . VAL B 1128 ? 0.2590 0.1718 0.2550 0.0098  -0.0133 -0.0072 1126 VAL B N   
17230 C CA  . VAL B 1128 ? 0.2421 0.1578 0.2410 0.0070  -0.0130 -0.0044 1126 VAL B CA  
17231 C C   . VAL B 1128 ? 0.2742 0.1861 0.2734 0.0026  -0.0147 -0.0036 1126 VAL B C   
17232 O O   . VAL B 1128 ? 0.2954 0.1998 0.2913 0.0019  -0.0164 -0.0049 1126 VAL B O   
17233 C CB  . VAL B 1128 ? 0.2541 0.1677 0.2518 0.0087  -0.0123 -0.0022 1126 VAL B CB  
17234 C CG1 . VAL B 1128 ? 0.2424 0.1607 0.2403 0.0128  -0.0108 -0.0027 1126 VAL B CG1 
17235 C CG2 . VAL B 1128 ? 0.2732 0.1764 0.2664 0.0091  -0.0138 -0.0022 1126 VAL B CG2 
17236 N N   . ALA B 1129 ? 0.2492 0.1664 0.2523 -0.0005 -0.0142 -0.0016 1127 ALA B N   
17237 C CA  . ALA B 1129 ? 0.2800 0.1943 0.2839 -0.0049 -0.0156 0.0001  1127 ALA B CA  
17238 C C   . ALA B 1129 ? 0.2439 0.1596 0.2489 -0.0058 -0.0145 0.0033  1127 ALA B C   
17239 O O   . ALA B 1129 ? 0.2490 0.1722 0.2570 -0.0051 -0.0127 0.0043  1127 ALA B O   
17240 C CB  . ALA B 1129 ? 0.2826 0.2029 0.2905 -0.0080 -0.0159 -0.0002 1127 ALA B CB  
17241 N N   . ILE B 1130 ? 0.2379 0.1460 0.2401 -0.0069 -0.0156 0.0048  1128 ILE B N   
17242 C CA  . ILE B 1130 ? 0.2471 0.1554 0.2496 -0.0076 -0.0147 0.0079  1128 ILE B CA  
17243 C C   . ILE B 1130 ? 0.2605 0.1702 0.2657 -0.0127 -0.0152 0.0102  1128 ILE B C   
17244 O O   . ILE B 1130 ? 0.2577 0.1626 0.2622 -0.0158 -0.0172 0.0099  1128 ILE B O   
17245 C CB  . ILE B 1130 ? 0.2691 0.1680 0.2667 -0.0056 -0.0155 0.0085  1128 ILE B CB  
17246 C CG1 . ILE B 1130 ? 0.2874 0.1848 0.2823 -0.0004 -0.0151 0.0059  1128 ILE B CG1 
17247 C CG2 . ILE B 1130 ? 0.2545 0.1545 0.2524 -0.0059 -0.0145 0.0118  1128 ILE B CG2 
17248 C CD1 . ILE B 1130 ? 0.3040 0.1910 0.2937 0.0017  -0.0163 0.0058  1128 ILE B CD1 
17249 N N   . ASP B 1131 ? 0.2412 0.1575 0.2495 -0.0137 -0.0136 0.0127  1129 ASP B N   
17250 C CA  . ASP B 1131 ? 0.2357 0.1546 0.2470 -0.0184 -0.0137 0.0152  1129 ASP B CA  
17251 C C   . ASP B 1131 ? 0.2445 0.1543 0.2528 -0.0211 -0.0154 0.0171  1129 ASP B C   
17252 O O   . ASP B 1131 ? 0.2850 0.1907 0.2905 -0.0199 -0.0150 0.0189  1129 ASP B O   
17253 C CB  . ASP B 1131 ? 0.2511 0.1779 0.2652 -0.0182 -0.0113 0.0174  1129 ASP B CB  
17254 C CG  . ASP B 1131 ? 0.2744 0.2047 0.2917 -0.0227 -0.0110 0.0203  1129 ASP B CG  
17255 O OD1 . ASP B 1131 ? 0.2746 0.2048 0.2939 -0.0261 -0.0124 0.0201  1129 ASP B OD1 
17256 O OD2 . ASP B 1131 ? 0.2905 0.2239 0.3083 -0.0229 -0.0094 0.0229  1129 ASP B OD2 
17257 N N   . ALA B 1132 ? 0.2716 0.1781 0.2802 -0.0249 -0.0174 0.0169  1130 ALA B N   
17258 C CA  . ALA B 1132 ? 0.2993 0.1966 0.3048 -0.0280 -0.0192 0.0187  1130 ALA B CA  
17259 C C   . ALA B 1132 ? 0.3140 0.2137 0.3213 -0.0309 -0.0182 0.0227  1130 ALA B C   
17260 O O   . ALA B 1132 ? 0.3380 0.2299 0.3419 -0.0321 -0.0191 0.0247  1130 ALA B O   
17261 C CB  . ALA B 1132 ? 0.3153 0.2096 0.3214 -0.0320 -0.0216 0.0176  1130 ALA B CB  
17262 N N   . ALA B 1133 ? 0.3074 0.2176 0.3196 -0.0319 -0.0162 0.0241  1131 ALA B N   
17263 C CA  . ALA B 1133 ? 0.3336 0.2468 0.3473 -0.0345 -0.0149 0.0280  1131 ALA B CA  
17264 C C   . ALA B 1133 ? 0.3458 0.2562 0.3561 -0.0313 -0.0137 0.0294  1131 ALA B C   
17265 O O   . ALA B 1133 ? 0.3528 0.2636 0.3631 -0.0334 -0.0129 0.0328  1131 ALA B O   
17266 C CB  . ALA B 1133 ? 0.3341 0.2595 0.3537 -0.0358 -0.0128 0.0288  1131 ALA B CB  
17267 N N   . SER B 1134 ? 0.2982 0.2061 0.3056 -0.0263 -0.0136 0.0270  1132 SER B N   
17268 C CA  . SER B 1134 ? 0.3093 0.2139 0.3132 -0.0232 -0.0128 0.0284  1132 SER B CA  
17269 C C   . SER B 1134 ? 0.2958 0.1895 0.2954 -0.0248 -0.0146 0.0303  1132 SER B C   
17270 O O   . SER B 1134 ? 0.3247 0.2159 0.3218 -0.0235 -0.0140 0.0326  1132 SER B O   
17271 C CB  . SER B 1134 ? 0.3068 0.2113 0.3089 -0.0177 -0.0125 0.0253  1132 SER B CB  
17272 O OG  . SER B 1134 ? 0.3112 0.2072 0.3101 -0.0167 -0.0145 0.0229  1132 SER B OG  
17273 N N   . GLY B 1135 ? 0.3225 0.2091 0.3207 -0.0273 -0.0169 0.0293  1133 GLY B N   
17274 C CA  . GLY B 1135 ? 0.3190 0.1941 0.3126 -0.0288 -0.0188 0.0310  1133 GLY B CA  
17275 C C   . GLY B 1135 ? 0.3392 0.2061 0.3275 -0.0238 -0.0194 0.0296  1133 GLY B C   
17276 O O   . GLY B 1135 ? 0.3798 0.2374 0.3639 -0.0241 -0.0206 0.0315  1133 GLY B O   
17277 N N   . LEU B 1136 ? 0.3513 0.2214 0.3397 -0.0190 -0.0186 0.0265  1134 LEU B N   
17278 C CA  . LEU B 1136 ? 0.3500 0.2145 0.3342 -0.0136 -0.0187 0.0253  1134 LEU B CA  
17279 C C   . LEU B 1136 ? 0.3858 0.2415 0.3662 -0.0118 -0.0206 0.0220  1134 LEU B C   
17280 O O   . LEU B 1136 ? 0.3679 0.2208 0.3456 -0.0068 -0.0205 0.0201  1134 LEU B O   
17281 C CB  . LEU B 1136 ? 0.3226 0.1963 0.3090 -0.0093 -0.0165 0.0242  1134 LEU B CB  
17282 C CG  . LEU B 1136 ? 0.3395 0.2211 0.3285 -0.0101 -0.0146 0.0273  1134 LEU B CG  
17283 C CD1 . LEU B 1136 ? 0.3543 0.2452 0.3456 -0.0063 -0.0127 0.0257  1134 LEU B CD1 
17284 C CD2 . LEU B 1136 ? 0.3618 0.2369 0.3470 -0.0094 -0.0149 0.0304  1134 LEU B CD2 
17285 N N   . GLN B 1137 ? 0.3521 0.2036 0.3324 -0.0159 -0.0224 0.0212  1135 GLN B N   
17286 C CA  . GLN B 1137 ? 0.3743 0.2180 0.3510 -0.0144 -0.0242 0.0178  1135 GLN B CA  
17287 C C   . GLN B 1137 ? 0.4276 0.2597 0.3982 -0.0108 -0.0253 0.0176  1135 GLN B C   
17288 O O   . GLN B 1137 ? 0.4307 0.2590 0.3983 -0.0066 -0.0256 0.0145  1135 GLN B O   
17289 C CB  . GLN B 1137 ? 0.4245 0.2649 0.4016 -0.0200 -0.0263 0.0175  1135 GLN B CB  
17290 C CG  . GLN B 1137 ? 0.3927 0.2441 0.3756 -0.0226 -0.0255 0.0167  1135 GLN B CG  
17291 C CD  . GLN B 1137 ? 0.3850 0.2446 0.3728 -0.0266 -0.0243 0.0203  1135 GLN B CD  
17292 O OE1 . GLN B 1137 ? 0.3783 0.2371 0.3655 -0.0267 -0.0234 0.0234  1135 GLN B OE1 
17293 N NE2 . GLN B 1137 ? 0.4065 0.2743 0.3992 -0.0296 -0.0240 0.0200  1135 GLN B NE2 
17294 N N   . ALA B 1138 ? 0.3958 0.2224 0.3642 -0.0123 -0.0257 0.0210  1136 ALA B N   
17295 C CA  . ALA B 1138 ? 0.4216 0.2366 0.3840 -0.0088 -0.0269 0.0210  1136 ALA B CA  
17296 C C   . ALA B 1138 ? 0.4540 0.2722 0.4158 -0.0020 -0.0252 0.0201  1136 ALA B C   
17297 O O   . ALA B 1138 ? 0.4686 0.2781 0.4256 0.0021  -0.0260 0.0191  1136 ALA B O   
17298 C CB  . ALA B 1138 ? 0.4434 0.2519 0.4037 -0.0120 -0.0277 0.0252  1136 ALA B CB  
17299 N N   . SER B 1139 ? 0.4006 0.2310 0.3671 -0.0008 -0.0230 0.0203  1137 SER B N   
17300 C CA  . SER B 1139 ? 0.3975 0.2319 0.3639 0.0052  -0.0216 0.0196  1137 SER B CA  
17301 C C   . SER B 1139 ? 0.4285 0.2621 0.3936 0.0095  -0.0216 0.0154  1137 SER B C   
17302 O O   . SER B 1139 ? 0.4006 0.2350 0.3645 0.0148  -0.0208 0.0146  1137 SER B O   
17303 C CB  . SER B 1139 ? 0.3803 0.2279 0.3519 0.0048  -0.0193 0.0208  1137 SER B CB  
17304 O OG  . SER B 1139 ? 0.4377 0.2863 0.4099 0.0021  -0.0190 0.0248  1137 SER B OG  
17305 N N   . LEU B 1140 ? 0.4111 0.2435 0.3764 0.0072  -0.0225 0.0128  1138 LEU B N   
17306 C CA  . LEU B 1140 ? 0.4563 0.2878 0.4200 0.0108  -0.0226 0.0088  1138 LEU B CA  
17307 C C   . LEU B 1140 ? 0.4681 0.2864 0.4261 0.0109  -0.0247 0.0070  1138 LEU B C   
17308 O O   . LEU B 1140 ? 0.5162 0.3327 0.4727 0.0116  -0.0253 0.0037  1138 LEU B O   
17309 C CB  . LEU B 1140 ? 0.4323 0.2730 0.4004 0.0088  -0.0218 0.0068  1138 LEU B CB  
17310 C CG  . LEU B 1140 ? 0.4425 0.2959 0.4158 0.0092  -0.0196 0.0079  1138 LEU B CG  
17311 C CD1 . LEU B 1140 ? 0.4046 0.2663 0.3817 0.0079  -0.0190 0.0057  1138 LEU B CD1 
17312 C CD2 . LEU B 1140 ? 0.4376 0.2934 0.4102 0.0149  -0.0183 0.0080  1138 LEU B CD2 
17313 N N   . LYS B 1141 ? 0.5284 0.3370 0.4826 0.0102  -0.0260 0.0093  1139 LYS B N   
17314 C CA  . LYS B 1141 ? 0.5082 0.3032 0.4563 0.0107  -0.0282 0.0077  1139 LYS B CA  
17315 C C   . LYS B 1141 ? 0.5513 0.3431 0.4960 0.0176  -0.0276 0.0048  1139 LYS B C   
17316 O O   . LYS B 1141 ? 0.5619 0.3577 0.5074 0.0223  -0.0261 0.0056  1139 LYS B O   
17317 C CB  . LYS B 1141 ? 0.5303 0.3156 0.4751 0.0086  -0.0296 0.0111  1139 LYS B CB  
17318 N N   . ASN B 1142 ? 0.5670 0.3520 0.5079 0.0184  -0.0288 0.0013  1140 ASN B N   
17319 C CA  . ASN B 1142 ? 0.5706 0.3515 0.5076 0.0249  -0.0283 -0.0018 1140 ASN B CA  
17320 C C   . ASN B 1142 ? 0.5676 0.3609 0.5087 0.0288  -0.0259 -0.0034 1140 ASN B C   
17321 O O   . ASN B 1142 ? 0.5265 0.3197 0.4660 0.0348  -0.0249 -0.0047 1140 ASN B O   
17322 C CB  . ASN B 1142 ? 0.6176 0.3891 0.5500 0.0291  -0.0288 -0.0003 1140 ASN B CB  
17323 C CG  . ASN B 1142 ? 0.7111 0.4688 0.6386 0.0254  -0.0314 0.0010  1140 ASN B CG  
17324 O OD1 . ASN B 1142 ? 0.7823 0.5323 0.7063 0.0230  -0.0331 -0.0013 1140 ASN B OD1 
17325 N ND2 . ASN B 1142 ? 0.7494 0.5038 0.6764 0.0247  -0.0317 0.0048  1140 ASN B ND2 
17326 N N   . LEU B 1143 ? 0.5749 0.3790 0.5215 0.0253  -0.0251 -0.0032 1141 LEU B N   
17327 C CA  . LEU B 1143 ? 0.5081 0.3235 0.4584 0.0283  -0.0230 -0.0047 1141 LEU B CA  
17328 C C   . LEU B 1143 ? 0.4981 0.3104 0.4451 0.0315  -0.0230 -0.0089 1141 LEU B C   
17329 O O   . LEU B 1143 ? 0.5612 0.3665 0.5051 0.0289  -0.0247 -0.0107 1141 LEU B O   
17330 C CB  . LEU B 1143 ? 0.4515 0.2772 0.4075 0.0234  -0.0224 -0.0040 1141 LEU B CB  
17331 C CG  . LEU B 1143 ? 0.4511 0.2899 0.4121 0.0253  -0.0202 -0.0044 1141 LEU B CG  
17332 C CD1 . LEU B 1143 ? 0.4134 0.2570 0.3765 0.0275  -0.0189 -0.0016 1141 LEU B CD1 
17333 C CD2 . LEU B 1143 ? 0.3946 0.2409 0.3601 0.0203  -0.0201 -0.0043 1141 LEU B CD2 
17334 N N   . PRO B 1144 ? 0.4827 0.3000 0.4301 0.0370  -0.0213 -0.0103 1142 PRO B N   
17335 C CA  . PRO B 1144 ? 0.5133 0.3287 0.4577 0.0401  -0.0210 -0.0142 1142 PRO B CA  
17336 C C   . PRO B 1144 ? 0.4933 0.3137 0.4399 0.0360  -0.0213 -0.0160 1142 PRO B C   
17337 O O   . PRO B 1144 ? 0.4450 0.2749 0.3969 0.0328  -0.0206 -0.0145 1142 PRO B O   
17338 C CB  . PRO B 1144 ? 0.5699 0.3935 0.5165 0.0459  -0.0188 -0.0146 1142 PRO B CB  
17339 C CG  . PRO B 1144 ? 0.5457 0.3709 0.4942 0.0469  -0.0184 -0.0110 1142 PRO B CG  
17340 C CD  . PRO B 1144 ? 0.4717 0.2968 0.4223 0.0406  -0.0195 -0.0084 1142 PRO B CD  
17341 N N   . GLN B 1145 ? 0.5090 0.3228 0.4512 0.0363  -0.0223 -0.0192 1143 GLN B N   
17342 C CA  . GLN B 1145 ? 0.4755 0.2931 0.4190 0.0326  -0.0228 -0.0210 1143 GLN B CA  
17343 C C   . GLN B 1145 ? 0.4482 0.2789 0.3968 0.0338  -0.0207 -0.0214 1143 GLN B C   
17344 O O   . GLN B 1145 ? 0.4132 0.2502 0.3653 0.0298  -0.0208 -0.0212 1143 GLN B O   
17345 C CB  . GLN B 1145 ? 0.4991 0.3073 0.4362 0.0337  -0.0241 -0.0246 1143 GLN B CB  
17346 N N   . THR B 1146 ? 0.4482 0.2833 0.3972 0.0392  -0.0187 -0.0218 1144 THR B N   
17347 C CA  . THR B 1146 ? 0.4593 0.3067 0.4131 0.0401  -0.0167 -0.0220 1144 THR B CA  
17348 C C   . THR B 1146 ? 0.4077 0.2634 0.3675 0.0364  -0.0164 -0.0190 1144 THR B C   
17349 O O   . THR B 1146 ? 0.4598 0.3237 0.4233 0.0341  -0.0158 -0.0192 1144 THR B O   
17350 C CB  . THR B 1146 ? 0.4787 0.3294 0.4323 0.0463  -0.0148 -0.0224 1144 THR B CB  
17351 O OG1 . THR B 1146 ? 0.5309 0.3772 0.4836 0.0483  -0.0150 -0.0201 1144 THR B OG1 
17352 C CG2 . THR B 1146 ? 0.5423 0.3880 0.4909 0.0502  -0.0146 -0.0258 1144 THR B CG2 
17353 N N   . VAL B 1147 ? 0.3996 0.2529 0.3600 0.0358  -0.0167 -0.0162 1145 VAL B N   
17354 C CA  . VAL B 1147 ? 0.3783 0.2389 0.3438 0.0322  -0.0163 -0.0133 1145 VAL B CA  
17355 C C   . VAL B 1147 ? 0.3916 0.2501 0.3579 0.0263  -0.0179 -0.0129 1145 VAL B C   
17356 O O   . VAL B 1147 ? 0.3646 0.2310 0.3354 0.0231  -0.0175 -0.0120 1145 VAL B O   
17357 C CB  . VAL B 1147 ? 0.3512 0.2105 0.3169 0.0337  -0.0160 -0.0103 1145 VAL B CB  
17358 C CG1 . VAL B 1147 ? 0.3640 0.2319 0.3350 0.0304  -0.0153 -0.0076 1145 VAL B CG1 
17359 C CG2 . VAL B 1147 ? 0.3632 0.2241 0.3279 0.0398  -0.0147 -0.0109 1145 VAL B CG2 
17360 N N   . GLY B 1148 ? 0.3897 0.2375 0.3516 0.0247  -0.0199 -0.0134 1146 GLY B N   
17361 C CA  . GLY B 1148 ? 0.4025 0.2480 0.3651 0.0189  -0.0216 -0.0127 1146 GLY B CA  
17362 C C   . GLY B 1148 ? 0.3919 0.2430 0.3566 0.0166  -0.0218 -0.0146 1146 GLY B C   
17363 O O   . GLY B 1148 ? 0.4044 0.2595 0.3726 0.0119  -0.0224 -0.0134 1146 GLY B O   
17364 N N   . LEU B 1149 ? 0.3807 0.2324 0.3434 0.0199  -0.0212 -0.0176 1147 LEU B N   
17365 C CA  . LEU B 1149 ? 0.3960 0.2532 0.3604 0.0180  -0.0213 -0.0194 1147 LEU B CA  
17366 C C   . LEU B 1149 ? 0.3883 0.2574 0.3591 0.0166  -0.0198 -0.0178 1147 LEU B C   
17367 O O   . LEU B 1149 ? 0.4075 0.2812 0.3807 0.0137  -0.0202 -0.0184 1147 LEU B O   
17368 C CB  . LEU B 1149 ? 0.4524 0.3088 0.4135 0.0224  -0.0205 -0.0227 1147 LEU B CB  
17369 N N   . ARG B 1150 ? 0.3357 0.2097 0.3092 0.0186  -0.0181 -0.0158 1148 ARG B N   
17370 C CA  . ARG B 1150 ? 0.3446 0.2292 0.3236 0.0174  -0.0167 -0.0143 1148 ARG B CA  
17371 C C   . ARG B 1150 ? 0.3088 0.1948 0.2909 0.0133  -0.0172 -0.0113 1148 ARG B C   
17372 O O   . ARG B 1150 ? 0.2811 0.1756 0.2677 0.0120  -0.0160 -0.0100 1148 ARG B O   
17373 C CB  . ARG B 1150 ? 0.3215 0.2113 0.3017 0.0217  -0.0147 -0.0137 1148 ARG B CB  
17374 C CG  . ARG B 1150 ? 0.3507 0.2428 0.3295 0.0257  -0.0137 -0.0162 1148 ARG B CG  
17375 C CD  . ARG B 1150 ? 0.3859 0.2888 0.3691 0.0258  -0.0121 -0.0161 1148 ARG B CD  
17376 N NE  . ARG B 1150 ? 0.3388 0.2443 0.3208 0.0300  -0.0108 -0.0179 1148 ARG B NE  
17377 C CZ  . ARG B 1150 ? 0.3329 0.2440 0.3166 0.0330  -0.0093 -0.0171 1148 ARG B CZ  
17378 N NH1 . ARG B 1150 ? 0.2806 0.1959 0.2674 0.0322  -0.0088 -0.0146 1148 ARG B NH1 
17379 N NH2 . ARG B 1150 ? 0.2981 0.2112 0.2806 0.0367  -0.0082 -0.0188 1148 ARG B NH2 
17380 N N   . VAL B 1151 ? 0.3568 0.2347 0.3364 0.0113  -0.0187 -0.0102 1149 VAL B N   
17381 C CA  . VAL B 1151 ? 0.3026 0.1814 0.2848 0.0077  -0.0189 -0.0070 1149 VAL B CA  
17382 C C   . VAL B 1151 ? 0.3547 0.2309 0.3374 0.0026  -0.0208 -0.0069 1149 VAL B C   
17383 O O   . VAL B 1151 ? 0.3674 0.2352 0.3461 0.0018  -0.0227 -0.0084 1149 VAL B O   
17384 C CB  . VAL B 1151 ? 0.3497 0.2216 0.3290 0.0092  -0.0191 -0.0051 1149 VAL B CB  
17385 C CG1 . VAL B 1151 ? 0.3791 0.2509 0.3604 0.0049  -0.0196 -0.0018 1149 VAL B CG1 
17386 C CG2 . VAL B 1151 ? 0.3482 0.2242 0.3279 0.0140  -0.0173 -0.0048 1149 VAL B CG2 
17387 N N   . SER B 1152 ? 0.3216 0.2049 0.3091 -0.0009 -0.0205 -0.0050 1150 SER B N   
17388 C CA  . SER B 1152 ? 0.3423 0.2237 0.3310 -0.0062 -0.0222 -0.0040 1150 SER B CA  
17389 C C   . SER B 1152 ? 0.3050 0.1902 0.2971 -0.0088 -0.0214 -0.0004 1150 SER B C   
17390 O O   . SER B 1152 ? 0.3101 0.2010 0.3043 -0.0067 -0.0195 0.0009  1150 SER B O   
17391 C CB  . SER B 1152 ? 0.3326 0.2197 0.3241 -0.0082 -0.0227 -0.0056 1150 SER B CB  
17392 O OG  . SER B 1152 ? 0.3960 0.2936 0.3923 -0.0075 -0.0208 -0.0049 1150 SER B OG  
17393 N N   . TRP B 1153 ? 0.3183 0.2002 0.3109 -0.0135 -0.0231 0.0012  1151 TRP B N   
17394 C CA  . TRP B 1153 ? 0.2734 0.1592 0.2694 -0.0167 -0.0224 0.0047  1151 TRP B CA  
17395 C C   . TRP B 1153 ? 0.3037 0.1968 0.3047 -0.0207 -0.0227 0.0051  1151 TRP B C   
17396 O O   . TRP B 1153 ? 0.3496 0.2400 0.3500 -0.0230 -0.0247 0.0036  1151 TRP B O   
17397 C CB  . TRP B 1153 ? 0.3309 0.2070 0.3236 -0.0191 -0.0240 0.0066  1151 TRP B CB  
17398 C CG  . TRP B 1153 ? 0.3473 0.2170 0.3356 -0.0150 -0.0235 0.0068  1151 TRP B CG  
17399 C CD1 . TRP B 1153 ? 0.3670 0.2283 0.3500 -0.0116 -0.0244 0.0044  1151 TRP B CD1 
17400 C CD2 . TRP B 1153 ? 0.3649 0.2365 0.3536 -0.0136 -0.0219 0.0095  1151 TRP B CD2 
17401 N NE1 . TRP B 1153 ? 0.3618 0.2197 0.3423 -0.0081 -0.0235 0.0055  1151 TRP B NE1 
17402 C CE2 . TRP B 1153 ? 0.3521 0.2162 0.3360 -0.0094 -0.0220 0.0087  1151 TRP B CE2 
17403 C CE3 . TRP B 1153 ? 0.3032 0.1822 0.2960 -0.0155 -0.0203 0.0126  1151 TRP B CE3 
17404 C CZ2 . TRP B 1153 ? 0.3613 0.2251 0.3443 -0.0070 -0.0209 0.0110  1151 TRP B CZ2 
17405 C CZ3 . TRP B 1153 ? 0.3064 0.1849 0.2980 -0.0133 -0.0191 0.0147  1151 TRP B CZ3 
17406 C CH2 . TRP B 1153 ? 0.3474 0.2184 0.3342 -0.0092 -0.0195 0.0140  1151 TRP B CH2 
17407 N N   . SER B 1154 ? 0.2813 0.1836 0.2870 -0.0214 -0.0208 0.0071  1152 SER B N   
17408 C CA  . SER B 1154 ? 0.2960 0.2063 0.3069 -0.0246 -0.0208 0.0076  1152 SER B CA  
17409 C C   . SER B 1154 ? 0.2745 0.1876 0.2885 -0.0286 -0.0204 0.0112  1152 SER B C   
17410 O O   . SER B 1154 ? 0.2869 0.2027 0.3016 -0.0276 -0.0186 0.0133  1152 SER B O   
17411 C CB  . SER B 1154 ? 0.3236 0.2433 0.3378 -0.0217 -0.0188 0.0064  1152 SER B CB  
17412 O OG  . SER B 1154 ? 0.2907 0.2178 0.3099 -0.0247 -0.0188 0.0071  1152 SER B OG  
17413 N N   . LYS B 1155 ? 0.2738 0.1864 0.2896 -0.0333 -0.0223 0.0119  1153 LYS B N   
17414 C CA  . LYS B 1155 ? 0.3233 0.2409 0.3434 -0.0376 -0.0219 0.0153  1153 LYS B CA  
17415 C C   . LYS B 1155 ? 0.3346 0.2631 0.3607 -0.0387 -0.0210 0.0152  1153 LYS B C   
17416 O O   . LYS B 1155 ? 0.3367 0.2704 0.3669 -0.0425 -0.0209 0.0177  1153 LYS B O   
17417 C CB  . LYS B 1155 ? 0.3585 0.2686 0.3769 -0.0425 -0.0246 0.0165  1153 LYS B CB  
17418 N N   . ASP B 1156 ? 0.2596 0.1917 0.2861 -0.0354 -0.0205 0.0125  1154 ASP B N   
17419 C CA  . ASP B 1156 ? 0.2407 0.1826 0.2727 -0.0360 -0.0199 0.0122  1154 ASP B CA  
17420 C C   . ASP B 1156 ? 0.2551 0.2001 0.2864 -0.0311 -0.0184 0.0097  1154 ASP B C   
17421 O O   . ASP B 1156 ? 0.2570 0.1996 0.2865 -0.0297 -0.0196 0.0070  1154 ASP B O   
17422 C CB  . ASP B 1156 ? 0.2361 0.1766 0.2690 -0.0394 -0.0227 0.0113  1154 ASP B CB  
17423 C CG  . ASP B 1156 ? 0.2789 0.2297 0.3179 -0.0406 -0.0222 0.0116  1154 ASP B CG  
17424 O OD1 . ASP B 1156 ? 0.2534 0.2112 0.2948 -0.0376 -0.0199 0.0113  1154 ASP B OD1 
17425 O OD2 . ASP B 1156 ? 0.2840 0.2357 0.3253 -0.0445 -0.0243 0.0122  1154 ASP B OD2 
17426 N N   . TRP B 1157 ? 0.2150 0.1654 0.2478 -0.0288 -0.0158 0.0107  1155 TRP B N   
17427 C CA  . TRP B 1157 ? 0.2110 0.1636 0.2427 -0.0243 -0.0144 0.0085  1155 TRP B CA  
17428 C C   . TRP B 1157 ? 0.2515 0.2095 0.2859 -0.0238 -0.0147 0.0066  1155 TRP B C   
17429 O O   . TRP B 1157 ? 0.2493 0.2058 0.2816 -0.0211 -0.0150 0.0040  1155 TRP B O   
17430 C CB  . TRP B 1157 ? 0.2429 0.2008 0.2758 -0.0222 -0.0117 0.0099  1155 TRP B CB  
17431 C CG  . TRP B 1157 ? 0.2197 0.1731 0.2499 -0.0223 -0.0111 0.0120  1155 TRP B CG  
17432 C CD1 . TRP B 1157 ? 0.2295 0.1741 0.2560 -0.0235 -0.0127 0.0124  1155 TRP B CD1 
17433 C CD2 . TRP B 1157 ? 0.2023 0.1597 0.2331 -0.0212 -0.0088 0.0138  1155 TRP B CD2 
17434 N NE1 . TRP B 1157 ? 0.2478 0.1908 0.2727 -0.0231 -0.0116 0.0147  1155 TRP B NE1 
17435 C CE2 . TRP B 1157 ? 0.2346 0.1855 0.2621 -0.0217 -0.0092 0.0156  1155 TRP B CE2 
17436 C CE3 . TRP B 1157 ? 0.2271 0.1927 0.2607 -0.0197 -0.0066 0.0142  1155 TRP B CE3 
17437 C CZ2 . TRP B 1157 ? 0.2494 0.2021 0.2764 -0.0209 -0.0074 0.0178  1155 TRP B CZ2 
17438 C CZ3 . TRP B 1157 ? 0.2555 0.2228 0.2885 -0.0190 -0.0048 0.0162  1155 TRP B CZ3 
17439 C CH2 . TRP B 1157 ? 0.2541 0.2150 0.2838 -0.0196 -0.0052 0.0181  1155 TRP B CH2 
17440 N N   . ALA B 1158 ? 0.2282 0.1926 0.2675 -0.0265 -0.0147 0.0079  1156 ALA B N   
17441 C CA  . ALA B 1158 ? 0.2385 0.2084 0.2806 -0.0259 -0.0150 0.0064  1156 ALA B CA  
17442 C C   . ALA B 1158 ? 0.2766 0.2417 0.3167 -0.0268 -0.0177 0.0043  1156 ALA B C   
17443 O O   . ALA B 1158 ? 0.2996 0.2664 0.3395 -0.0249 -0.0179 0.0022  1156 ALA B O   
17444 C CB  . ALA B 1158 ? 0.2239 0.2023 0.2719 -0.0283 -0.0143 0.0085  1156 ALA B CB  
17445 N N   . ALA B 1159 ? 0.2359 0.1947 0.2740 -0.0299 -0.0198 0.0049  1157 ALA B N   
17446 C CA  . ALA B 1159 ? 0.2609 0.2144 0.2965 -0.0310 -0.0225 0.0028  1157 ALA B CA  
17447 C C   . ALA B 1159 ? 0.2827 0.2290 0.3125 -0.0275 -0.0227 0.0002  1157 ALA B C   
17448 O O   . ALA B 1159 ? 0.3067 0.2506 0.3343 -0.0269 -0.0242 -0.0021 1157 ALA B O   
17449 C CB  . ALA B 1159 ? 0.2965 0.2456 0.3319 -0.0357 -0.0248 0.0043  1157 ALA B CB  
17450 N N   . ASP B 1160 ? 0.2918 0.2351 0.3190 -0.0252 -0.0211 0.0007  1158 ASP B N   
17451 C CA  . ASP B 1160 ? 0.3057 0.2417 0.3273 -0.0220 -0.0213 -0.0014 1158 ASP B CA  
17452 C C   . ASP B 1160 ? 0.3041 0.2439 0.3253 -0.0176 -0.0194 -0.0030 1158 ASP B C   
17453 O O   . ASP B 1160 ? 0.3345 0.2694 0.3515 -0.0147 -0.0193 -0.0049 1158 ASP B O   
17454 C CB  . ASP B 1160 ? 0.3022 0.2320 0.3210 -0.0221 -0.0211 0.0001  1158 ASP B CB  
17455 C CG  . ASP B 1160 ? 0.3221 0.2460 0.3399 -0.0264 -0.0234 0.0013  1158 ASP B CG  
17456 O OD1 . ASP B 1160 ? 0.3631 0.2867 0.3816 -0.0291 -0.0254 0.0005  1158 ASP B OD1 
17457 O OD2 . ASP B 1160 ? 0.3409 0.2603 0.3571 -0.0274 -0.0233 0.0032  1158 ASP B OD2 
17458 N N   . GLY B 1161 ? 0.2622 0.2104 0.2877 -0.0171 -0.0178 -0.0024 1159 GLY B N   
17459 C CA  . GLY B 1161 ? 0.2989 0.2508 0.3242 -0.0135 -0.0163 -0.0040 1159 GLY B CA  
17460 C C   . GLY B 1161 ? 0.3176 0.2698 0.3423 -0.0130 -0.0175 -0.0063 1159 GLY B C   
17461 O O   . GLY B 1161 ? 0.3778 0.3262 0.4012 -0.0152 -0.0197 -0.0070 1159 GLY B O   
17462 N N   . PRO B 1162 ? 0.3533 0.3100 0.3786 -0.0104 -0.0163 -0.0075 1160 PRO B N   
17463 C CA  . PRO B 1162 ? 0.2970 0.2586 0.3238 -0.0081 -0.0139 -0.0068 1160 PRO B CA  
17464 C C   . PRO B 1162 ? 0.3057 0.2634 0.3290 -0.0054 -0.0129 -0.0071 1160 PRO B C   
17465 O O   . PRO B 1162 ? 0.3228 0.2752 0.3422 -0.0039 -0.0136 -0.0087 1160 PRO B O   
17466 C CB  . PRO B 1162 ? 0.3424 0.3084 0.3702 -0.0066 -0.0135 -0.0083 1160 PRO B CB  
17467 C CG  . PRO B 1162 ? 0.3826 0.3437 0.4071 -0.0064 -0.0153 -0.0104 1160 PRO B CG  
17468 C CD  . PRO B 1162 ? 0.3856 0.3423 0.4097 -0.0096 -0.0173 -0.0097 1160 PRO B CD  
17469 N N   . PHE B 1163 ? 0.2266 0.1869 0.2511 -0.0047 -0.0112 -0.0055 1161 PHE B N   
17470 C CA  . PHE B 1163 ? 0.2487 0.2069 0.2705 -0.0019 -0.0101 -0.0055 1161 PHE B CA  
17471 C C   . PHE B 1163 ? 0.2198 0.1831 0.2422 0.0007  -0.0086 -0.0065 1161 PHE B C   
17472 O O   . PHE B 1163 ? 0.2399 0.2081 0.2648 0.0003  -0.0083 -0.0069 1161 PHE B O   
17473 C CB  . PHE B 1163 ? 0.2217 0.1793 0.2439 -0.0029 -0.0094 -0.0030 1161 PHE B CB  
17474 C CG  . PHE B 1163 ? 0.2371 0.1895 0.2587 -0.0059 -0.0110 -0.0019 1161 PHE B CG  
17475 C CD1 . PHE B 1163 ? 0.2986 0.2433 0.3163 -0.0056 -0.0125 -0.0030 1161 PHE B CD1 
17476 C CD2 . PHE B 1163 ? 0.2711 0.2265 0.2960 -0.0091 -0.0109 0.0002  1161 PHE B CD2 
17477 C CE1 . PHE B 1163 ? 0.3151 0.2545 0.3320 -0.0086 -0.0141 -0.0020 1161 PHE B CE1 
17478 C CE2 . PHE B 1163 ? 0.2693 0.2201 0.2938 -0.0122 -0.0125 0.0014  1161 PHE B CE2 
17479 C CZ  . PHE B 1163 ? 0.2885 0.2310 0.3088 -0.0121 -0.0142 0.0003  1161 PHE B CZ  
17480 N N   . ALA B 1164 ? 0.2215 0.1834 0.2415 0.0034  -0.0078 -0.0068 1162 ALA B N   
17481 C CA  . ALA B 1164 ? 0.2430 0.2095 0.2634 0.0058  -0.0064 -0.0076 1162 ALA B CA  
17482 C C   . ALA B 1164 ? 0.2609 0.2297 0.2816 0.0069  -0.0050 -0.0061 1162 ALA B C   
17483 O O   . ALA B 1164 ? 0.2816 0.2535 0.3020 0.0089  -0.0040 -0.0067 1162 ALA B O   
17484 C CB  . ALA B 1164 ? 0.2692 0.2333 0.2868 0.0081  -0.0068 -0.0097 1162 ALA B CB  
17485 N N   . GLY B 1165 ? 0.2086 0.1758 0.2295 0.0055  -0.0049 -0.0041 1163 GLY B N   
17486 C CA  . GLY B 1165 ? 0.2265 0.1958 0.2474 0.0063  -0.0037 -0.0024 1163 GLY B CA  
17487 C C   . GLY B 1165 ? 0.2318 0.1972 0.2521 0.0047  -0.0041 -0.0004 1163 GLY B C   
17488 O O   . GLY B 1165 ? 0.2191 0.1801 0.2389 0.0029  -0.0054 -0.0004 1163 GLY B O   
17489 N N   . ALA B 1166 ? 0.2251 0.1923 0.2454 0.0050  -0.0030 0.0015  1164 ALA B N   
17490 C CA  . ALA B 1166 ? 0.2027 0.1663 0.2223 0.0033  -0.0033 0.0038  1164 ALA B CA  
17491 C C   . ALA B 1166 ? 0.2149 0.1784 0.2326 0.0052  -0.0024 0.0053  1164 ALA B C   
17492 O O   . ALA B 1166 ? 0.2358 0.2043 0.2541 0.0065  -0.0012 0.0052  1164 ALA B O   
17493 C CB  . ALA B 1166 ? 0.2236 0.1905 0.2462 0.0001  -0.0029 0.0054  1164 ALA B CB  
17494 N N   . LEU B 1167 ? 0.1961 0.1539 0.2115 0.0051  -0.0032 0.0066  1165 LEU B N   
17495 C CA  . LEU B 1167 ? 0.2235 0.1806 0.2370 0.0066  -0.0026 0.0085  1165 LEU B CA  
17496 C C   . LEU B 1167 ? 0.2522 0.2075 0.2659 0.0036  -0.0026 0.0113  1165 LEU B C   
17497 O O   . LEU B 1167 ? 0.2400 0.1903 0.2533 0.0016  -0.0038 0.0117  1165 LEU B O   
17498 C CB  . LEU B 1167 ? 0.2190 0.1703 0.2293 0.0094  -0.0036 0.0079  1165 LEU B CB  
17499 C CG  . LEU B 1167 ? 0.2234 0.1765 0.2335 0.0122  -0.0036 0.0052  1165 LEU B CG  
17500 C CD1 . LEU B 1167 ? 0.2485 0.1959 0.2553 0.0152  -0.0044 0.0048  1165 LEU B CD1 
17501 C CD2 . LEU B 1167 ? 0.2457 0.2061 0.2572 0.0135  -0.0022 0.0050  1165 LEU B CD2 
17502 N N   . VAL B 1168 ? 0.2249 0.1842 0.2391 0.0033  -0.0013 0.0132  1166 VAL B N   
17503 C CA  . VAL B 1168 ? 0.2308 0.1896 0.2455 0.0004  -0.0009 0.0161  1166 VAL B CA  
17504 C C   . VAL B 1168 ? 0.2303 0.1876 0.2423 0.0017  -0.0005 0.0183  1166 VAL B C   
17505 O O   . VAL B 1168 ? 0.2392 0.1999 0.2504 0.0042  0.0003  0.0179  1166 VAL B O   
17506 C CB  . VAL B 1168 ? 0.2486 0.2147 0.2667 -0.0016 0.0006  0.0164  1166 VAL B CB  
17507 C CG1 . VAL B 1168 ? 0.2381 0.2043 0.2570 -0.0048 0.0011  0.0195  1166 VAL B CG1 
17508 C CG2 . VAL B 1168 ? 0.2374 0.2056 0.2584 -0.0025 0.0001  0.0141  1166 VAL B CG2 
17509 N N   . GLU B 1169 ? 0.2456 0.1976 0.2559 -0.0001 -0.0012 0.0207  1167 GLU B N   
17510 C CA  . GLU B 1169 ? 0.2360 0.1863 0.2438 0.0007  -0.0008 0.0233  1167 GLU B CA  
17511 C C   . GLU B 1169 ? 0.2551 0.2072 0.2640 -0.0030 0.0001  0.0263  1167 GLU B C   
17512 O O   . GLU B 1169 ? 0.2972 0.2472 0.3075 -0.0062 -0.0006 0.0268  1167 GLU B O   
17513 C CB  . GLU B 1169 ? 0.2555 0.1969 0.2598 0.0019  -0.0025 0.0238  1167 GLU B CB  
17514 C CG  . GLU B 1169 ? 0.2765 0.2154 0.2779 0.0027  -0.0024 0.0268  1167 GLU B CG  
17515 C CD  . GLU B 1169 ? 0.3087 0.2379 0.3067 0.0034  -0.0042 0.0278  1167 GLU B CD  
17516 O OE1 . GLU B 1169 ? 0.2838 0.2080 0.2817 0.0026  -0.0055 0.0262  1167 GLU B OE1 
17517 O OE2 . GLU B 1169 ? 0.3288 0.2553 0.3241 0.0047  -0.0044 0.0300  1167 GLU B OE2 
17518 N N   . GLY B 1170 ? 0.2738 0.2298 0.2820 -0.0027 0.0015  0.0281  1168 GLY B N   
17519 C CA  . GLY B 1170 ? 0.2950 0.2525 0.3037 -0.0059 0.0025  0.0313  1168 GLY B CA  
17520 C C   . GLY B 1170 ? 0.3229 0.2870 0.3314 -0.0052 0.0044  0.0323  1168 GLY B C   
17521 O O   . GLY B 1170 ? 0.2846 0.2520 0.2926 -0.0023 0.0049  0.0306  1168 GLY B O   
17522 N N   . ASP B 1171 ? 0.3276 0.2936 0.3364 -0.0079 0.0056  0.0353  1169 ASP B N   
17523 C CA  . ASP B 1171 ? 0.3290 0.3015 0.3375 -0.0075 0.0077  0.0363  1169 ASP B CA  
17524 C C   . ASP B 1171 ? 0.2971 0.2771 0.3093 -0.0077 0.0091  0.0341  1169 ASP B C   
17525 O O   . ASP B 1171 ? 0.3055 0.2856 0.3205 -0.0085 0.0085  0.0322  1169 ASP B O   
17526 C CB  . ASP B 1171 ? 0.3496 0.3216 0.3565 -0.0100 0.0086  0.0403  1169 ASP B CB  
17527 C CG  . ASP B 1171 ? 0.3829 0.3561 0.3929 -0.0142 0.0091  0.0418  1169 ASP B CG  
17528 O OD1 . ASP B 1171 ? 0.3500 0.3252 0.3636 -0.0152 0.0088  0.0399  1169 ASP B OD1 
17529 O OD2 . ASP B 1171 ? 0.4568 0.4290 0.4656 -0.0166 0.0096  0.0453  1169 ASP B OD2 
17530 N N   . ALA B 1172 ? 0.3179 0.3038 0.3296 -0.0071 0.0111  0.0345  1170 ALA B N   
17531 C CA  . ALA B 1172 ? 0.3425 0.3351 0.3571 -0.0066 0.0125  0.0323  1170 ALA B CA  
17532 C C   . ALA B 1172 ? 0.3042 0.2992 0.3231 -0.0096 0.0130  0.0325  1170 ALA B C   
17533 O O   . ALA B 1172 ? 0.2928 0.2899 0.3146 -0.0092 0.0127  0.0300  1170 ALA B O   
17534 C CB  . ALA B 1172 ? 0.3419 0.3399 0.3548 -0.0057 0.0146  0.0330  1170 ALA B CB  
17535 N N   . GLU B 1173 ? 0.3092 0.3040 0.3286 -0.0126 0.0135  0.0357  1171 GLU B N   
17536 C CA  . GLU B 1173 ? 0.3097 0.3076 0.3334 -0.0155 0.0140  0.0361  1171 GLU B CA  
17537 C C   . GLU B 1173 ? 0.2772 0.2700 0.3025 -0.0166 0.0116  0.0348  1171 GLU B C   
17538 O O   . GLU B 1173 ? 0.2978 0.2938 0.3271 -0.0177 0.0115  0.0334  1171 GLU B O   
17539 C CB  . GLU B 1173 ? 0.4150 0.4151 0.4392 -0.0188 0.0154  0.0399  1171 GLU B CB  
17540 C CG  . GLU B 1173 ? 0.4731 0.4801 0.4967 -0.0178 0.0182  0.0407  1171 GLU B CG  
17541 C CD  . GLU B 1173 ? 0.4956 0.5092 0.5219 -0.0158 0.0196  0.0377  1171 GLU B CD  
17542 O OE1 . GLU B 1173 ? 0.4565 0.4725 0.4870 -0.0170 0.0194  0.0366  1171 GLU B OE1 
17543 O OE2 . GLU B 1173 ? 0.5456 0.5617 0.5695 -0.0131 0.0208  0.0365  1171 GLU B OE2 
17544 N N   . ARG B 1174 ? 0.2718 0.2569 0.2941 -0.0161 0.0096  0.0350  1172 ARG B N   
17545 C CA  . ARG B 1174 ? 0.2891 0.2688 0.3121 -0.0166 0.0073  0.0333  1172 ARG B CA  
17546 C C   . ARG B 1174 ? 0.2515 0.2334 0.2758 -0.0138 0.0070  0.0295  1172 ARG B C   
17547 O O   . ARG B 1174 ? 0.2572 0.2395 0.2842 -0.0149 0.0061  0.0279  1172 ARG B O   
17548 C CB  . ARG B 1174 ? 0.3225 0.2933 0.3414 -0.0159 0.0054  0.0341  1172 ARG B CB  
17549 C CG  . ARG B 1174 ? 0.2802 0.2446 0.2988 -0.0157 0.0031  0.0320  1172 ARG B CG  
17550 C CD  . ARG B 1174 ? 0.2991 0.2629 0.3206 -0.0198 0.0022  0.0327  1172 ARG B CD  
17551 N NE  . ARG B 1174 ? 0.3118 0.2692 0.3326 -0.0197 -0.0002 0.0306  1172 ARG B NE  
17552 C CZ  . ARG B 1174 ? 0.3283 0.2855 0.3517 -0.0225 -0.0013 0.0300  1172 ARG B CZ  
17553 N NH1 . ARG B 1174 ? 0.3200 0.2833 0.3474 -0.0256 -0.0003 0.0314  1172 ARG B NH1 
17554 N NH2 . ARG B 1174 ? 0.3231 0.2738 0.3450 -0.0221 -0.0035 0.0279  1172 ARG B NH2 
17555 N N   . ILE B 1175 ? 0.2433 0.2266 0.2654 -0.0105 0.0076  0.0282  1173 ILE B N   
17556 C CA  . ILE B 1175 ? 0.2476 0.2331 0.2707 -0.0079 0.0074  0.0248  1173 ILE B CA  
17557 C C   . ILE B 1175 ? 0.2635 0.2556 0.2907 -0.0089 0.0086  0.0238  1173 ILE B C   
17558 O O   . ILE B 1175 ? 0.2509 0.2433 0.2801 -0.0087 0.0077  0.0215  1173 ILE B O   
17559 C CB  . ILE B 1175 ? 0.2536 0.2402 0.2738 -0.0046 0.0080  0.0240  1173 ILE B CB  
17560 C CG1 . ILE B 1175 ? 0.2719 0.2518 0.2886 -0.0030 0.0064  0.0243  1173 ILE B CG1 
17561 C CG2 . ILE B 1175 ? 0.2579 0.2483 0.2794 -0.0025 0.0083  0.0208  1173 ILE B CG2 
17562 C CD1 . ILE B 1175 ? 0.2707 0.2517 0.2845 -0.0003 0.0069  0.0245  1173 ILE B CD1 
17563 N N   . ARG B 1176 ? 0.2612 0.2588 0.2895 -0.0099 0.0107  0.0255  1174 ARG B N   
17564 C CA  . ARG B 1176 ? 0.2545 0.2587 0.2868 -0.0105 0.0120  0.0246  1174 ARG B CA  
17565 C C   . ARG B 1176 ? 0.2398 0.2436 0.2757 -0.0134 0.0108  0.0249  1174 ARG B C   
17566 O O   . ARG B 1176 ? 0.2384 0.2448 0.2770 -0.0130 0.0105  0.0229  1174 ARG B O   
17567 C CB  . ARG B 1176 ? 0.2604 0.2704 0.2929 -0.0111 0.0145  0.0266  1174 ARG B CB  
17568 C CG  . ARG B 1176 ? 0.3091 0.3263 0.3454 -0.0109 0.0161  0.0255  1174 ARG B CG  
17569 C CD  . ARG B 1176 ? 0.3586 0.3815 0.3959 -0.0121 0.0187  0.0280  1174 ARG B CD  
17570 N NE  . ARG B 1176 ? 0.3903 0.4125 0.4233 -0.0111 0.0198  0.0293  1174 ARG B NE  
17571 C CZ  . ARG B 1176 ? 0.4052 0.4302 0.4360 -0.0085 0.0213  0.0280  1174 ARG B CZ  
17572 N NH1 . ARG B 1176 ? 0.3819 0.4101 0.4141 -0.0066 0.0218  0.0253  1174 ARG B NH1 
17573 N NH2 . ARG B 1176 ? 0.4310 0.4552 0.4578 -0.0080 0.0221  0.0295  1174 ARG B NH2 
17574 N N   . ALA B 1177 ? 0.2395 0.2397 0.2751 -0.0163 0.0100  0.0274  1175 ALA B N   
17575 C CA  . ALA B 1177 ? 0.2553 0.2549 0.2942 -0.0194 0.0087  0.0278  1175 ALA B CA  
17576 C C   . ALA B 1177 ? 0.2100 0.2048 0.2485 -0.0185 0.0063  0.0251  1175 ALA B C   
17577 O O   . ALA B 1177 ? 0.2382 0.2351 0.2800 -0.0196 0.0055  0.0239  1175 ALA B O   
17578 C CB  . ALA B 1177 ? 0.2615 0.2574 0.2996 -0.0228 0.0081  0.0311  1175 ALA B CB  
17579 N N   . VAL B 1178 ? 0.2478 0.2364 0.2822 -0.0163 0.0052  0.0240  1176 VAL B N   
17580 C CA  . VAL B 1178 ? 0.2123 0.1964 0.2460 -0.0152 0.0032  0.0214  1176 VAL B CA  
17581 C C   . VAL B 1178 ? 0.2201 0.2088 0.2554 -0.0129 0.0037  0.0186  1176 VAL B C   
17582 O O   . VAL B 1178 ? 0.2349 0.2233 0.2719 -0.0132 0.0025  0.0168  1176 VAL B O   
17583 C CB  . VAL B 1178 ? 0.2493 0.2261 0.2783 -0.0132 0.0021  0.0211  1176 VAL B CB  
17584 C CG1 . VAL B 1178 ? 0.2619 0.2350 0.2899 -0.0114 0.0004  0.0181  1176 VAL B CG1 
17585 C CG2 . VAL B 1178 ? 0.2639 0.2348 0.2912 -0.0158 0.0011  0.0237  1176 VAL B CG2 
17586 N N   . ASN B 1179 ? 0.2261 0.2190 0.2609 -0.0106 0.0055  0.0182  1177 ASN B N   
17587 C CA  . ASN B 1179 ? 0.2312 0.2281 0.2672 -0.0084 0.0060  0.0157  1177 ASN B CA  
17588 C C   . ASN B 1179 ? 0.2422 0.2444 0.2826 -0.0100 0.0064  0.0155  1177 ASN B C   
17589 O O   . ASN B 1179 ? 0.2440 0.2471 0.2858 -0.0092 0.0056  0.0133  1177 ASN B O   
17590 C CB  . ASN B 1179 ? 0.2339 0.2340 0.2681 -0.0060 0.0079  0.0156  1177 ASN B CB  
17591 C CG  . ASN B 1179 ? 0.2959 0.2978 0.3298 -0.0033 0.0079  0.0128  1177 ASN B CG  
17592 O OD1 . ASN B 1179 ? 0.2983 0.2976 0.3321 -0.0027 0.0064  0.0108  1177 ASN B OD1 
17593 N ND2 . ASN B 1179 ? 0.2835 0.2898 0.3170 -0.0019 0.0096  0.0125  1177 ASN B ND2 
17594 N N   . LYS B 1180 ? 0.2321 0.2381 0.2749 -0.0122 0.0076  0.0179  1178 LYS B N   
17595 C CA  . LYS B 1180 ? 0.2339 0.2452 0.2813 -0.0139 0.0079  0.0181  1178 LYS B CA  
17596 C C   . LYS B 1180 ? 0.2108 0.2188 0.2597 -0.0159 0.0055  0.0174  1178 LYS B C   
17597 O O   . LYS B 1180 ? 0.2482 0.2590 0.2998 -0.0157 0.0049  0.0160  1178 LYS B O   
17598 C CB  . LYS B 1180 ? 0.2676 0.2833 0.3171 -0.0162 0.0096  0.0211  1178 LYS B CB  
17599 C CG  . LYS B 1180 ? 0.3208 0.3422 0.3702 -0.0143 0.0124  0.0214  1178 LYS B CG  
17600 C CD  . LYS B 1180 ? 0.3514 0.3779 0.4034 -0.0168 0.0141  0.0245  1178 LYS B CD  
17601 C CE  . LYS B 1180 ? 0.4831 0.5166 0.5361 -0.0148 0.0169  0.0243  1178 LYS B CE  
17602 N NZ  . LYS B 1180 ? 0.4777 0.5147 0.5334 -0.0129 0.0168  0.0217  1178 LYS B NZ  
17603 N N   . ALA B 1181 ? 0.2221 0.2239 0.2690 -0.0178 0.0039  0.0185  1179 ALA B N   
17604 C CA  . ALA B 1181 ? 0.2134 0.2113 0.2610 -0.0198 0.0014  0.0178  1179 ALA B CA  
17605 C C   . ALA B 1181 ? 0.2161 0.2114 0.2622 -0.0173 0.0002  0.0146  1179 ALA B C   
17606 O O   . ALA B 1181 ? 0.2383 0.2343 0.2865 -0.0182 -0.0012 0.0134  1179 ALA B O   
17607 C CB  . ALA B 1181 ? 0.2318 0.2225 0.2767 -0.0220 0.0000  0.0195  1179 ALA B CB  
17608 N N   . ILE B 1182 ? 0.2220 0.2146 0.2645 -0.0143 0.0006  0.0133  1180 ILE B N   
17609 C CA  . ILE B 1182 ? 0.2286 0.2190 0.2695 -0.0119 -0.0004 0.0104  1180 ILE B CA  
17610 C C   . ILE B 1182 ? 0.2463 0.2428 0.2901 -0.0107 0.0004  0.0090  1180 ILE B C   
17611 O O   . ILE B 1182 ? 0.2306 0.2266 0.2750 -0.0104 -0.0009 0.0071  1180 ILE B O   
17612 C CB  . ILE B 1182 ? 0.2324 0.2194 0.2693 -0.0089 0.0000  0.0097  1180 ILE B CB  
17613 C CG1 . ILE B 1182 ? 0.2045 0.1842 0.2382 -0.0097 -0.0012 0.0107  1180 ILE B CG1 
17614 C CG2 . ILE B 1182 ? 0.2709 0.2577 0.3067 -0.0063 -0.0005 0.0068  1180 ILE B CG2 
17615 C CD1 . ILE B 1182 ? 0.2453 0.2220 0.2752 -0.0069 -0.0008 0.0105  1180 ILE B CD1 
17616 N N   . ALA B 1183 ? 0.2518 0.2542 0.2974 -0.0101 0.0025  0.0099  1181 ALA B N   
17617 C CA  . ALA B 1183 ? 0.2500 0.2579 0.2982 -0.0088 0.0032  0.0085  1181 ALA B CA  
17618 C C   . ALA B 1183 ? 0.2801 0.2905 0.3323 -0.0110 0.0021  0.0087  1181 ALA B C   
17619 O O   . ALA B 1183 ? 0.3045 0.3175 0.3583 -0.0098 0.0018  0.0072  1181 ALA B O   
17620 C CB  . ALA B 1183 ? 0.2578 0.2712 0.3068 -0.0077 0.0058  0.0095  1181 ALA B CB  
17621 N N   . ALA B 1184 ? 0.2559 0.2655 0.3096 -0.0141 0.0013  0.0107  1182 ALA B N   
17622 C CA  . ALA B 1184 ? 0.2551 0.2672 0.3127 -0.0166 0.0000  0.0111  1182 ALA B CA  
17623 C C   . ALA B 1184 ? 0.2511 0.2576 0.3072 -0.0175 -0.0028 0.0096  1182 ALA B C   
17624 O O   . ALA B 1184 ? 0.2709 0.2791 0.3299 -0.0196 -0.0042 0.0098  1182 ALA B O   
17625 C CB  . ALA B 1184 ? 0.2533 0.2679 0.3136 -0.0199 0.0005  0.0142  1182 ALA B CB  
17626 N N   . LEU B 1185 ? 0.2234 0.2235 0.2751 -0.0160 -0.0036 0.0082  1183 LEU B N   
17627 C CA  . LEU B 1185 ? 0.2364 0.2310 0.2862 -0.0167 -0.0061 0.0066  1183 LEU B CA  
17628 C C   . LEU B 1185 ? 0.2711 0.2686 0.3223 -0.0153 -0.0066 0.0045  1183 LEU B C   
17629 O O   . LEU B 1185 ? 0.2612 0.2620 0.3125 -0.0126 -0.0051 0.0036  1183 LEU B O   
17630 C CB  . LEU B 1185 ? 0.2290 0.2166 0.2737 -0.0149 -0.0065 0.0054  1183 LEU B CB  
17631 C CG  . LEU B 1185 ? 0.2273 0.2109 0.2700 -0.0160 -0.0062 0.0074  1183 LEU B CG  
17632 C CD1 . LEU B 1185 ? 0.2340 0.2116 0.2719 -0.0134 -0.0063 0.0061  1183 LEU B CD1 
17633 C CD2 . LEU B 1185 ? 0.2228 0.2032 0.2662 -0.0199 -0.0080 0.0088  1183 LEU B CD2 
17634 N N   . PRO B 1186 ? 0.2681 0.2642 0.3201 -0.0171 -0.0088 0.0038  1184 PRO B N   
17635 C CA  . PRO B 1186 ? 0.2655 0.2637 0.3183 -0.0157 -0.0096 0.0019  1184 PRO B CA  
17636 C C   . PRO B 1186 ? 0.2560 0.2495 0.3042 -0.0129 -0.0097 -0.0004 1184 PRO B C   
17637 O O   . PRO B 1186 ? 0.2985 0.2867 0.3431 -0.0123 -0.0098 -0.0007 1184 PRO B O   
17638 C CB  . PRO B 1186 ? 0.2998 0.2966 0.3539 -0.0187 -0.0122 0.0020  1184 PRO B CB  
17639 C CG  . PRO B 1186 ? 0.3553 0.3458 0.4067 -0.0208 -0.0133 0.0028  1184 PRO B CG  
17640 C CD  . PRO B 1186 ? 0.2939 0.2856 0.3454 -0.0204 -0.0110 0.0047  1184 PRO B CD  
17641 N N   . GLY B 1187 ? 0.2550 0.2509 0.3036 -0.0111 -0.0098 -0.0020 1185 GLY B N   
17642 C CA  . GLY B 1187 ? 0.2585 0.2508 0.3033 -0.0087 -0.0100 -0.0041 1185 GLY B CA  
17643 C C   . GLY B 1187 ? 0.2538 0.2475 0.2973 -0.0060 -0.0078 -0.0044 1185 GLY B C   
17644 O O   . GLY B 1187 ? 0.2990 0.2977 0.3449 -0.0052 -0.0063 -0.0037 1185 GLY B O   
17645 N N   . PRO B 1188 ? 0.2469 0.2362 0.2865 -0.0043 -0.0078 -0.0055 1186 PRO B N   
17646 C CA  . PRO B 1188 ? 0.2400 0.2308 0.2782 -0.0017 -0.0060 -0.0060 1186 PRO B CA  
17647 C C   . PRO B 1188 ? 0.2268 0.2196 0.2659 -0.0018 -0.0044 -0.0042 1186 PRO B C   
17648 O O   . PRO B 1188 ? 0.2550 0.2462 0.2944 -0.0035 -0.0045 -0.0027 1186 PRO B O   
17649 C CB  . PRO B 1188 ? 0.2600 0.2457 0.2941 -0.0003 -0.0066 -0.0074 1186 PRO B CB  
17650 C CG  . PRO B 1188 ? 0.3191 0.2999 0.3521 -0.0021 -0.0082 -0.0070 1186 PRO B CG  
17651 C CD  . PRO B 1188 ? 0.2471 0.2301 0.2832 -0.0046 -0.0093 -0.0065 1186 PRO B CD  
17652 N N   . LEU B 1189 ? 0.2334 0.2296 0.2726 0.0001  -0.0028 -0.0045 1187 LEU B N   
17653 C CA  . LEU B 1189 ? 0.2244 0.2222 0.2635 0.0005  -0.0011 -0.0030 1187 LEU B CA  
17654 C C   . LEU B 1189 ? 0.2428 0.2363 0.2784 0.0016  -0.0012 -0.0031 1187 LEU B C   
17655 O O   . LEU B 1189 ? 0.2787 0.2709 0.3121 0.0034  -0.0013 -0.0046 1187 LEU B O   
17656 C CB  . LEU B 1189 ? 0.1941 0.1962 0.2338 0.0021  0.0004  -0.0035 1187 LEU B CB  
17657 C CG  . LEU B 1189 ? 0.2608 0.2678 0.3041 0.0015  0.0011  -0.0030 1187 LEU B CG  
17658 C CD1 . LEU B 1189 ? 0.3155 0.3229 0.3602 0.0012  -0.0002 -0.0042 1187 LEU B CD1 
17659 C CD2 . LEU B 1189 ? 0.2693 0.2796 0.3122 0.0032  0.0030  -0.0032 1187 LEU B CD2 
17660 N N   . LEU B 1190 ? 0.2229 0.2143 0.2579 0.0005  -0.0011 -0.0014 1188 LEU B N   
17661 C CA  . LEU B 1190 ? 0.2411 0.2279 0.2727 0.0017  -0.0013 -0.0014 1188 LEU B CA  
17662 C C   . LEU B 1190 ? 0.2345 0.2235 0.2650 0.0035  0.0002  -0.0008 1188 LEU B C   
17663 O O   . LEU B 1190 ? 0.2367 0.2290 0.2685 0.0029  0.0014  0.0005  1188 LEU B O   
17664 C CB  . LEU B 1190 ? 0.2198 0.2025 0.2509 -0.0002 -0.0021 0.0003  1188 LEU B CB  
17665 C CG  . LEU B 1190 ? 0.2147 0.1944 0.2465 -0.0024 -0.0039 -0.0001 1188 LEU B CG  
17666 C CD1 . LEU B 1190 ? 0.2431 0.2174 0.2732 -0.0038 -0.0048 0.0014  1188 LEU B CD1 
17667 C CD2 . LEU B 1190 ? 0.2480 0.2255 0.2782 -0.0010 -0.0051 -0.0026 1188 LEU B CD2 
17668 N N   . LEU B 1191 ? 0.2227 0.2098 0.2506 0.0056  0.0000  -0.0019 1189 LEU B N   
17669 C CA  . LEU B 1191 ? 0.2120 0.2004 0.2384 0.0073  0.0010  -0.0013 1189 LEU B CA  
17670 C C   . LEU B 1191 ? 0.2464 0.2314 0.2713 0.0069  0.0009  0.0006  1189 LEU B C   
17671 O O   . LEU B 1191 ? 0.2510 0.2311 0.2740 0.0074  -0.0001 0.0004  1189 LEU B O   
17672 C CB  . LEU B 1191 ? 0.2504 0.2384 0.2749 0.0096  0.0008  -0.0030 1189 LEU B CB  
17673 C CG  . LEU B 1191 ? 0.2228 0.2137 0.2462 0.0112  0.0018  -0.0028 1189 LEU B CG  
17674 C CD1 . LEU B 1191 ? 0.2278 0.2192 0.2503 0.0130  0.0014  -0.0046 1189 LEU B CD1 
17675 C CD2 . LEU B 1191 ? 0.2221 0.2112 0.2439 0.0118  0.0019  -0.0010 1189 LEU B CD2 
17676 N N   . VAL B 1192 ? 0.2209 0.2081 0.2465 0.0059  0.0020  0.0025  1190 VAL B N   
17677 C CA  . VAL B 1192 ? 0.2295 0.2136 0.2539 0.0050  0.0019  0.0047  1190 VAL B CA  
17678 C C   . VAL B 1192 ? 0.2268 0.2113 0.2488 0.0070  0.0025  0.0055  1190 VAL B C   
17679 O O   . VAL B 1192 ? 0.2500 0.2387 0.2721 0.0079  0.0036  0.0053  1190 VAL B O   
17680 C CB  . VAL B 1192 ? 0.2668 0.2536 0.2935 0.0025  0.0028  0.0066  1190 VAL B CB  
17681 C CG1 . VAL B 1192 ? 0.2479 0.2316 0.2731 0.0014  0.0028  0.0092  1190 VAL B CG1 
17682 C CG2 . VAL B 1192 ? 0.2488 0.2358 0.2782 0.0004  0.0020  0.0060  1190 VAL B CG2 
17683 N N   . GLN B 1193 ? 0.2164 0.1961 0.2362 0.0077  0.0018  0.0065  1191 GLN B N   
17684 C CA  . GLN B 1193 ? 0.2164 0.1961 0.2339 0.0094  0.0022  0.0077  1191 GLN B CA  
17685 C C   . GLN B 1193 ? 0.2351 0.2114 0.2515 0.0079  0.0021  0.0104  1191 GLN B C   
17686 O O   . GLN B 1193 ? 0.2358 0.2069 0.2517 0.0069  0.0010  0.0108  1191 GLN B O   
17687 C CB  . GLN B 1193 ? 0.2256 0.2024 0.2411 0.0121  0.0012  0.0066  1191 GLN B CB  
17688 C CG  . GLN B 1193 ? 0.2525 0.2321 0.2689 0.0134  0.0012  0.0040  1191 GLN B CG  
17689 C CD  . GLN B 1193 ? 0.2598 0.2384 0.2744 0.0162  0.0007  0.0033  1191 GLN B CD  
17690 O OE1 . GLN B 1193 ? 0.2520 0.2326 0.2656 0.0176  0.0011  0.0042  1191 GLN B OE1 
17691 N NE2 . GLN B 1193 ? 0.2404 0.2162 0.2545 0.0172  -0.0001 0.0017  1191 GLN B NE2 
17692 N N   . ALA B 1194 ? 0.2156 0.1945 0.2313 0.0078  0.0031  0.0122  1192 ALA B N   
17693 C CA  . ALA B 1194 ? 0.2474 0.2236 0.2620 0.0062  0.0032  0.0151  1192 ALA B CA  
17694 C C   . ALA B 1194 ? 0.2466 0.2223 0.2584 0.0081  0.0033  0.0166  1192 ALA B C   
17695 O O   . ALA B 1194 ? 0.3079 0.2874 0.3191 0.0100  0.0038  0.0157  1192 ALA B O   
17696 C CB  . ALA B 1194 ? 0.2583 0.2385 0.2750 0.0035  0.0046  0.0165  1192 ALA B CB  
17697 N N   . ALA B 1195 ? 0.2437 0.2146 0.2536 0.0075  0.0027  0.0189  1193 ALA B N   
17698 C CA  . ALA B 1195 ? 0.2754 0.2453 0.2824 0.0092  0.0027  0.0208  1193 ALA B CA  
17699 C C   . ALA B 1195 ? 0.3039 0.2695 0.3095 0.0071  0.0025  0.0239  1193 ALA B C   
17700 O O   . ALA B 1195 ? 0.2861 0.2478 0.2926 0.0050  0.0019  0.0242  1193 ALA B O   
17701 C CB  . ALA B 1195 ? 0.2722 0.2386 0.2774 0.0124  0.0014  0.0197  1193 ALA B CB  
17702 N N   . SER B 1196 ? 0.2737 0.2402 0.2772 0.0074  0.0031  0.0262  1194 SER B N   
17703 C CA  . SER B 1196 ? 0.2996 0.2614 0.3013 0.0057  0.0027  0.0294  1194 SER B CA  
17704 C C   . SER B 1196 ? 0.3299 0.2844 0.3289 0.0079  0.0010  0.0298  1194 SER B C   
17705 O O   . SER B 1196 ? 0.3167 0.2710 0.3151 0.0111  0.0002  0.0280  1194 SER B O   
17706 C CB  . SER B 1196 ? 0.3320 0.2972 0.3318 0.0055  0.0039  0.0319  1194 SER B CB  
17707 O OG  . SER B 1196 ? 0.3474 0.3137 0.3452 0.0088  0.0035  0.0314  1194 SER B OG  
17708 N N   . SER B 1197 ? 0.3207 0.2692 0.3180 0.0062  0.0003  0.0324  1195 SER B N   
17709 C CA  . SER B 1197 ? 0.3199 0.2607 0.3141 0.0084  -0.0014 0.0331  1195 SER B CA  
17710 C C   . SER B 1197 ? 0.3201 0.2624 0.3121 0.0119  -0.0015 0.0339  1195 SER B C   
17711 O O   . SER B 1197 ? 0.3342 0.2734 0.3249 0.0152  -0.0027 0.0328  1195 SER B O   
17712 C CB  . SER B 1197 ? 0.3462 0.2804 0.3386 0.0056  -0.0021 0.0361  1195 SER B CB  
17713 O OG  . SER B 1197 ? 0.3604 0.2935 0.3551 0.0021  -0.0021 0.0355  1195 SER B OG  
17714 N N   . GLY B 1198 ? 0.3396 0.2869 0.3310 0.0112  -0.0004 0.0357  1196 GLY B N   
17715 C CA  . GLY B 1198 ? 0.3843 0.3335 0.3735 0.0143  -0.0006 0.0365  1196 GLY B CA  
17716 C C   . GLY B 1198 ? 0.4207 0.3750 0.4115 0.0171  -0.0006 0.0334  1196 GLY B C   
17717 O O   . GLY B 1198 ? 0.3864 0.3404 0.3760 0.0204  -0.0015 0.0332  1196 GLY B O   
17718 N N   . GLU B 1199 ? 0.3545 0.3138 0.3482 0.0157  0.0005  0.0310  1197 GLU B N   
17719 C CA  . GLU B 1199 ? 0.3846 0.3484 0.3799 0.0179  0.0005  0.0280  1197 GLU B CA  
17720 C C   . GLU B 1199 ? 0.3829 0.3425 0.3784 0.0203  -0.0008 0.0262  1197 GLU B C   
17721 O O   . GLU B 1199 ? 0.3821 0.3435 0.3775 0.0234  -0.0014 0.0251  1197 GLU B O   
17722 C CB  . GLU B 1199 ? 0.3696 0.3385 0.3678 0.0157  0.0018  0.0261  1197 GLU B CB  
17723 C CG  . GLU B 1199 ? 0.4793 0.4537 0.4791 0.0173  0.0021  0.0232  1197 GLU B CG  
17724 C CD  . GLU B 1199 ? 0.4898 0.4684 0.4921 0.0151  0.0034  0.0216  1197 GLU B CD  
17725 O OE1 . GLU B 1199 ? 0.4950 0.4734 0.4980 0.0124  0.0042  0.0230  1197 GLU B OE1 
17726 O OE2 . GLU B 1199 ? 0.5886 0.5710 0.5923 0.0160  0.0035  0.0192  1197 GLU B OE2 
17727 N N   . ILE B 1200 ? 0.3249 0.2787 0.3207 0.0190  -0.0014 0.0260  1198 ILE B N   
17728 C CA  . ILE B 1200 ? 0.3511 0.2999 0.3464 0.0214  -0.0026 0.0244  1198 ILE B CA  
17729 C C   . ILE B 1200 ? 0.3844 0.3297 0.3769 0.0248  -0.0037 0.0259  1198 ILE B C   
17730 O O   . ILE B 1200 ? 0.3760 0.3215 0.3684 0.0281  -0.0043 0.0243  1198 ILE B O   
17731 C CB  . ILE B 1200 ? 0.3211 0.2636 0.3165 0.0190  -0.0032 0.0241  1198 ILE B CB  
17732 C CG1 . ILE B 1200 ? 0.3215 0.2681 0.3199 0.0162  -0.0024 0.0222  1198 ILE B CG1 
17733 C CG2 . ILE B 1200 ? 0.3203 0.2563 0.3141 0.0216  -0.0046 0.0228  1198 ILE B CG2 
17734 C CD1 . ILE B 1200 ? 0.3185 0.2598 0.3173 0.0133  -0.0030 0.0223  1198 ILE B CD1 
17735 N N   . ALA B 1201 ? 0.3787 0.3210 0.3689 0.0240  -0.0039 0.0291  1199 ALA B N   
17736 C CA  . ALA B 1201 ? 0.4143 0.3527 0.4017 0.0272  -0.0050 0.0309  1199 ALA B CA  
17737 C C   . ALA B 1201 ? 0.4427 0.3878 0.4304 0.0301  -0.0049 0.0307  1199 ALA B C   
17738 O O   . ALA B 1201 ? 0.4526 0.3962 0.4393 0.0338  -0.0059 0.0307  1199 ALA B O   
17739 C CB  . ALA B 1201 ? 0.3965 0.3300 0.3812 0.0254  -0.0054 0.0346  1199 ALA B CB  
17740 N N   . ARG B 1202 ? 0.4515 0.4038 0.4405 0.0285  -0.0038 0.0305  1200 ARG B N   
17741 C CA  . ARG B 1202 ? 0.4186 0.3770 0.4074 0.0306  -0.0039 0.0308  1200 ARG B CA  
17742 C C   . ARG B 1202 ? 0.4514 0.4157 0.4427 0.0320  -0.0036 0.0276  1200 ARG B C   
17743 O O   . ARG B 1202 ? 0.4713 0.4394 0.4626 0.0346  -0.0042 0.0275  1200 ARG B O   
17744 C CB  . ARG B 1202 ? 0.4903 0.4528 0.4781 0.0283  -0.0030 0.0327  1200 ARG B CB  
17745 C CG  . ARG B 1202 ? 0.5078 0.4770 0.4977 0.0262  -0.0016 0.0307  1200 ARG B CG  
17746 C CD  . ARG B 1202 ? 0.5825 0.5553 0.5708 0.0243  -0.0006 0.0326  1200 ARG B CD  
17747 N NE  . ARG B 1202 ? 0.5757 0.5450 0.5632 0.0214  0.0002  0.0347  1200 ARG B NE  
17748 C CZ  . ARG B 1202 ? 0.5553 0.5266 0.5447 0.0184  0.0016  0.0339  1200 ARG B CZ  
17749 N NH1 . ARG B 1202 ? 0.5334 0.5096 0.5252 0.0181  0.0024  0.0311  1200 ARG B NH1 
17750 N NH2 . ARG B 1202 ? 0.5743 0.5427 0.5631 0.0157  0.0022  0.0361  1200 ARG B NH2 
17751 N N   . ASN B 1203 ? 0.3946 0.3598 0.3883 0.0302  -0.0029 0.0252  1201 ASN B N   
17752 C CA  . ASN B 1203 ? 0.3992 0.3702 0.3952 0.0309  -0.0025 0.0223  1201 ASN B CA  
17753 C C   . ASN B 1203 ? 0.3894 0.3574 0.3866 0.0322  -0.0029 0.0200  1201 ASN B C   
17754 O O   . ASN B 1203 ? 0.3611 0.3259 0.3591 0.0302  -0.0026 0.0190  1201 ASN B O   
17755 C CB  . ASN B 1203 ? 0.4101 0.3854 0.4076 0.0277  -0.0012 0.0214  1201 ASN B CB  
17756 C CG  . ASN B 1203 ? 0.4285 0.4095 0.4283 0.0281  -0.0008 0.0185  1201 ASN B CG  
17757 O OD1 . ASN B 1203 ? 0.4407 0.4231 0.4409 0.0306  -0.0015 0.0174  1201 ASN B OD1 
17758 N ND2 . ASN B 1203 ? 0.4417 0.4258 0.4427 0.0256  0.0003  0.0175  1201 ASN B ND2 
17759 N N   . PRO B 1204 ? 0.3981 0.3673 0.3957 0.0356  -0.0035 0.0190  1202 PRO B N   
17760 C CA  . PRO B 1204 ? 0.4337 0.4005 0.4322 0.0370  -0.0037 0.0167  1202 PRO B CA  
17761 C C   . PRO B 1204 ? 0.3803 0.3501 0.3810 0.0348  -0.0029 0.0141  1202 PRO B C   
17762 O O   . PRO B 1204 ? 0.3922 0.3586 0.3933 0.0349  -0.0030 0.0123  1202 PRO B O   
17763 C CB  . PRO B 1204 ? 0.4584 0.4283 0.4572 0.0410  -0.0043 0.0163  1202 PRO B CB  
17764 C CG  . PRO B 1204 ? 0.5016 0.4732 0.4989 0.0419  -0.0048 0.0190  1202 PRO B CG  
17765 C CD  . PRO B 1204 ? 0.4542 0.4276 0.4513 0.0382  -0.0041 0.0201  1202 PRO B CD  
17766 N N   . ASP B 1205 ? 0.3924 0.3682 0.3945 0.0330  -0.0022 0.0138  1203 ASP B N   
17767 C CA  . ASP B 1205 ? 0.4205 0.3993 0.4246 0.0310  -0.0014 0.0115  1203 ASP B CA  
17768 C C   . ASP B 1205 ? 0.4061 0.3840 0.4105 0.0275  -0.0007 0.0121  1203 ASP B C   
17769 O O   . ASP B 1205 ? 0.3573 0.3392 0.3633 0.0257  0.0001  0.0108  1203 ASP B O   
17770 C CB  . ASP B 1205 ? 0.4077 0.3936 0.4130 0.0314  -0.0011 0.0105  1203 ASP B CB  
17771 C CG  . ASP B 1205 ? 0.4732 0.4610 0.4790 0.0346  -0.0017 0.0096  1203 ASP B CG  
17772 O OD1 . ASP B 1205 ? 0.4329 0.4165 0.4383 0.0364  -0.0021 0.0091  1203 ASP B OD1 
17773 O OD2 . ASP B 1205 ? 0.5556 0.5490 0.5620 0.0353  -0.0018 0.0094  1203 ASP B OD2 
17774 N N   . ALA B 1206 ? 0.3589 0.3318 0.3619 0.0265  -0.0009 0.0141  1204 ALA B N   
17775 C CA  . ALA B 1206 ? 0.3792 0.3515 0.3829 0.0231  -0.0002 0.0148  1204 ALA B CA  
17776 C C   . ALA B 1206 ? 0.3120 0.2847 0.3179 0.0216  0.0001  0.0125  1204 ALA B C   
17777 O O   . ALA B 1206 ? 0.3518 0.3279 0.3592 0.0193  0.0010  0.0121  1204 ALA B O   
17778 C CB  . ALA B 1206 ? 0.3651 0.3310 0.3670 0.0222  -0.0007 0.0172  1204 ALA B CB  
17779 N N   . TYR B 1207 ? 0.2796 0.2489 0.2855 0.0228  -0.0007 0.0109  1205 TYR B N   
17780 C CA  . TYR B 1207 ? 0.2909 0.2608 0.2986 0.0218  -0.0006 0.0085  1205 TYR B CA  
17781 C C   . TYR B 1207 ? 0.2819 0.2554 0.2902 0.0242  -0.0006 0.0064  1205 TYR B C   
17782 O O   . TYR B 1207 ? 0.3503 0.3225 0.3574 0.0269  -0.0011 0.0064  1205 TYR B O   
17783 C CB  . TYR B 1207 ? 0.2640 0.2272 0.2709 0.0212  -0.0015 0.0081  1205 TYR B CB  
17784 C CG  . TYR B 1207 ? 0.2538 0.2136 0.2604 0.0184  -0.0016 0.0102  1205 TYR B CG  
17785 C CD1 . TYR B 1207 ? 0.2714 0.2346 0.2801 0.0154  -0.0008 0.0107  1205 TYR B CD1 
17786 C CD2 . TYR B 1207 ? 0.2698 0.2228 0.2740 0.0187  -0.0025 0.0118  1205 TYR B CD2 
17787 C CE1 . TYR B 1207 ? 0.2415 0.2022 0.2501 0.0126  -0.0008 0.0128  1205 TYR B CE1 
17788 C CE2 . TYR B 1207 ? 0.2697 0.2195 0.2735 0.0158  -0.0026 0.0140  1205 TYR B CE2 
17789 C CZ  . TYR B 1207 ? 0.2723 0.2263 0.2785 0.0127  -0.0017 0.0145  1205 TYR B CZ  
17790 O OH  . TYR B 1207 ? 0.2670 0.2185 0.2731 0.0097  -0.0018 0.0168  1205 TYR B OH  
17791 N N   . CYS B 1208 ? 0.2380 0.2159 0.2481 0.0231  0.0000  0.0048  1206 CYS B N   
17792 C CA  . CYS B 1208 ? 0.2404 0.2223 0.2512 0.0247  0.0001  0.0030  1206 CYS B CA  
17793 C C   . CYS B 1208 ? 0.2434 0.2228 0.2545 0.0251  -0.0003 0.0010  1206 CYS B C   
17794 O O   . CYS B 1208 ? 0.2438 0.2221 0.2559 0.0230  -0.0003 0.0001  1206 CYS B O   
17795 C CB  . CYS B 1208 ? 0.2899 0.2774 0.3021 0.0232  0.0009  0.0025  1206 CYS B CB  
17796 S SG  . CYS B 1208 ? 0.2984 0.2909 0.3114 0.0247  0.0009  0.0005  1206 CYS B SG  
17797 N N   . LEU B 1209 ? 0.2210 0.1999 0.2313 0.0278  -0.0007 0.0001  1207 LEU B N   
17798 C CA  . LEU B 1209 ? 0.2330 0.2098 0.2433 0.0285  -0.0010 -0.0019 1207 LEU B CA  
17799 C C   . LEU B 1209 ? 0.2213 0.2027 0.2333 0.0274  -0.0005 -0.0036 1207 LEU B C   
17800 O O   . LEU B 1209 ? 0.2168 0.1964 0.2287 0.0272  -0.0007 -0.0053 1207 LEU B O   
17801 C CB  . LEU B 1209 ? 0.2099 0.1851 0.2187 0.0319  -0.0013 -0.0022 1207 LEU B CB  
17802 C CG  . LEU B 1209 ? 0.2456 0.2159 0.2525 0.0334  -0.0018 -0.0004 1207 LEU B CG  
17803 C CD1 . LEU B 1209 ? 0.2865 0.2554 0.2921 0.0373  -0.0020 -0.0010 1207 LEU B CD1 
17804 C CD2 . LEU B 1209 ? 0.2622 0.2259 0.2679 0.0314  -0.0024 0.0001  1207 LEU B CD2 
17805 N N   . ASN B 1210 ? 0.2235 0.2103 0.2367 0.0267  0.0000  -0.0034 1208 ASN B N   
17806 C CA  . ASN B 1210 ? 0.2468 0.2372 0.2613 0.0256  0.0004  -0.0050 1208 ASN B CA  
17807 C C   . ASN B 1210 ? 0.2323 0.2207 0.2476 0.0233  0.0003  -0.0057 1208 ASN B C   
17808 O O   . ASN B 1210 ? 0.2491 0.2384 0.2650 0.0228  0.0003  -0.0072 1208 ASN B O   
17809 C CB  . ASN B 1210 ? 0.2890 0.2845 0.3042 0.0249  0.0009  -0.0045 1208 ASN B CB  
17810 C CG  . ASN B 1210 ? 0.2967 0.2955 0.3115 0.0269  0.0008  -0.0038 1208 ASN B CG  
17811 O OD1 . ASN B 1210 ? 0.3487 0.3458 0.3627 0.0291  0.0005  -0.0034 1208 ASN B OD1 
17812 N ND2 . ASN B 1210 ? 0.3690 0.3722 0.3842 0.0262  0.0010  -0.0038 1208 ASN B ND2 
17813 N N   . TRP B 1211 ? 0.1979 0.1838 0.2132 0.0218  0.0003  -0.0044 1209 TRP B N   
17814 C CA  . TRP B 1211 ? 0.2156 0.2006 0.2322 0.0194  0.0002  -0.0048 1209 TRP B CA  
17815 C C   . TRP B 1211 ? 0.2440 0.2236 0.2598 0.0191  -0.0007 -0.0053 1209 TRP B C   
17816 O O   . TRP B 1211 ? 0.2551 0.2338 0.2720 0.0170  -0.0010 -0.0056 1209 TRP B O   
17817 C CB  . TRP B 1211 ? 0.2464 0.2323 0.2638 0.0176  0.0007  -0.0031 1209 TRP B CB  
17818 C CG  . TRP B 1211 ? 0.2530 0.2431 0.2702 0.0182  0.0015  -0.0023 1209 TRP B CG  
17819 C CD1 . TRP B 1211 ? 0.2805 0.2707 0.2968 0.0183  0.0018  -0.0004 1209 TRP B CD1 
17820 C CD2 . TRP B 1211 ? 0.2234 0.2178 0.2410 0.0187  0.0018  -0.0034 1209 TRP B CD2 
17821 N NE1 . TRP B 1211 ? 0.2565 0.2509 0.2725 0.0189  0.0023  -0.0004 1209 TRP B NE1 
17822 C CE2 . TRP B 1211 ? 0.2491 0.2460 0.2660 0.0191  0.0023  -0.0023 1209 TRP B CE2 
17823 C CE3 . TRP B 1211 ? 0.2450 0.2412 0.2633 0.0188  0.0018  -0.0053 1209 TRP B CE3 
17824 C CZ2 . TRP B 1211 ? 0.2511 0.2522 0.2679 0.0194  0.0026  -0.0029 1209 TRP B CZ2 
17825 C CZ3 . TRP B 1211 ? 0.2432 0.2434 0.2615 0.0191  0.0021  -0.0058 1209 TRP B CZ3 
17826 C CH2 . TRP B 1211 ? 0.2408 0.2434 0.2584 0.0193  0.0025  -0.0047 1209 TRP B CH2 
17827 N N   . LEU B 1212 ? 0.2163 0.1925 0.2302 0.0211  -0.0012 -0.0055 1210 LEU B N   
17828 C CA  . LEU B 1212 ? 0.1896 0.1599 0.2020 0.0210  -0.0021 -0.0061 1210 LEU B CA  
17829 C C   . LEU B 1212 ? 0.2110 0.1808 0.2225 0.0224  -0.0023 -0.0083 1210 LEU B C   
17830 O O   . LEU B 1212 ? 0.1985 0.1632 0.2082 0.0227  -0.0031 -0.0091 1210 LEU B O   
17831 C CB  . LEU B 1212 ? 0.1893 0.1549 0.1997 0.0223  -0.0025 -0.0047 1210 LEU B CB  
17832 C CG  . LEU B 1212 ? 0.1920 0.1565 0.2028 0.0202  -0.0025 -0.0025 1210 LEU B CG  
17833 C CD1 . LEU B 1212 ? 0.2250 0.1858 0.2338 0.0219  -0.0028 -0.0009 1210 LEU B CD1 
17834 C CD2 . LEU B 1212 ? 0.2167 0.1779 0.2281 0.0173  -0.0032 -0.0025 1210 LEU B CD2 
17835 N N   . VAL B 1213 ? 0.2004 0.1752 0.2128 0.0232  -0.0017 -0.0092 1211 VAL B N   
17836 C CA  . VAL B 1213 ? 0.2027 0.1780 0.2146 0.0241  -0.0018 -0.0111 1211 VAL B CA  
17837 C C   . VAL B 1213 ? 0.2302 0.2089 0.2439 0.0219  -0.0017 -0.0118 1211 VAL B C   
17838 O O   . VAL B 1213 ? 0.2272 0.2088 0.2426 0.0205  -0.0013 -0.0109 1211 VAL B O   
17839 C CB  . VAL B 1213 ? 0.1973 0.1757 0.2086 0.0269  -0.0011 -0.0115 1211 VAL B CB  
17840 C CG1 . VAL B 1213 ? 0.2188 0.1932 0.2282 0.0294  -0.0013 -0.0110 1211 VAL B CG1 
17841 C CG2 . VAL B 1213 ? 0.2095 0.1936 0.2226 0.0266  -0.0004 -0.0104 1211 VAL B CG2 
17842 N N   . GLU B 1214 ? 0.2117 0.1896 0.2247 0.0218  -0.0020 -0.0134 1212 GLU B N   
17843 C CA  . GLU B 1214 ? 0.2182 0.1990 0.2326 0.0201  -0.0020 -0.0142 1212 GLU B CA  
17844 C C   . GLU B 1214 ? 0.1843 0.1687 0.1984 0.0215  -0.0014 -0.0151 1212 GLU B C   
17845 O O   . GLU B 1214 ? 0.2013 0.1845 0.2137 0.0233  -0.0014 -0.0160 1212 GLU B O   
17846 C CB  . GLU B 1214 ? 0.2571 0.2344 0.2709 0.0187  -0.0031 -0.0151 1212 GLU B CB  
17847 C CG  . GLU B 1214 ? 0.2893 0.2697 0.3047 0.0170  -0.0032 -0.0157 1212 GLU B CG  
17848 C CD  . GLU B 1214 ? 0.3589 0.3364 0.3736 0.0158  -0.0044 -0.0167 1212 GLU B CD  
17849 O OE1 . GLU B 1214 ? 0.3742 0.3471 0.3876 0.0153  -0.0052 -0.0168 1212 GLU B OE1 
17850 O OE2 . GLU B 1214 ? 0.4140 0.3936 0.4290 0.0152  -0.0045 -0.0175 1212 GLU B OE2 
17851 N N   . GLU B 1215 ? 0.1920 0.1807 0.2077 0.0206  -0.0010 -0.0149 1213 GLU B N   
17852 C CA  . GLU B 1215 ? 0.1931 0.1855 0.2087 0.0212  -0.0005 -0.0157 1213 GLU B CA  
17853 C C   . GLU B 1215 ? 0.1627 0.1543 0.1778 0.0202  -0.0010 -0.0169 1213 GLU B C   
17854 O O   . GLU B 1215 ? 0.1830 0.1737 0.1990 0.0185  -0.0015 -0.0169 1213 GLU B O   
17855 C CB  . GLU B 1215 ? 0.1942 0.1907 0.2113 0.0204  0.0000  -0.0150 1213 GLU B CB  
17856 C CG  . GLU B 1215 ? 0.1954 0.1934 0.2128 0.0212  0.0004  -0.0137 1213 GLU B CG  
17857 C CD  . GLU B 1215 ? 0.1692 0.1704 0.1878 0.0199  0.0007  -0.0132 1213 GLU B CD  
17858 O OE1 . GLU B 1215 ? 0.1929 0.1932 0.2124 0.0186  0.0007  -0.0127 1213 GLU B OE1 
17859 O OE2 . GLU B 1215 ? 0.2090 0.2136 0.2276 0.0203  0.0010  -0.0132 1213 GLU B OE2 
17860 N N   . VAL B 1216 ? 0.1885 0.1810 0.2023 0.0214  -0.0007 -0.0179 1214 VAL B N   
17861 C CA  . VAL B 1216 ? 0.1997 0.1920 0.2128 0.0205  -0.0011 -0.0189 1214 VAL B CA  
17862 C C   . VAL B 1216 ? 0.1809 0.1774 0.1940 0.0208  -0.0004 -0.0191 1214 VAL B C   
17863 O O   . VAL B 1216 ? 0.1964 0.1948 0.2090 0.0226  0.0003  -0.0191 1214 VAL B O   
17864 C CB  . VAL B 1216 ? 0.2033 0.1914 0.2140 0.0213  -0.0016 -0.0201 1214 VAL B CB  
17865 C CG1 . VAL B 1216 ? 0.2271 0.2156 0.2367 0.0204  -0.0019 -0.0211 1214 VAL B CG1 
17866 C CG2 . VAL B 1216 ? 0.2229 0.2066 0.2336 0.0203  -0.0026 -0.0198 1214 VAL B CG2 
17867 N N   . SER B 1217 ? 0.1665 0.1647 0.1803 0.0192  -0.0006 -0.0192 1215 SER B N   
17868 C CA  . SER B 1217 ? 0.1623 0.1640 0.1760 0.0189  -0.0001 -0.0193 1215 SER B CA  
17869 C C   . SER B 1217 ? 0.1645 0.1650 0.1765 0.0185  -0.0005 -0.0203 1215 SER B C   
17870 O O   . SER B 1217 ? 0.1865 0.1844 0.1983 0.0175  -0.0014 -0.0206 1215 SER B O   
17871 C CB  . SER B 1217 ? 0.1999 0.2037 0.2151 0.0173  -0.0002 -0.0187 1215 SER B CB  
17872 O OG  . SER B 1217 ? 0.2331 0.2390 0.2479 0.0165  -0.0001 -0.0189 1215 SER B OG  
17873 N N   . ALA B 1218 ? 0.1724 0.1751 0.1833 0.0194  0.0002  -0.0206 1216 ALA B N   
17874 C CA  . ALA B 1218 ? 0.1985 0.2005 0.2074 0.0189  0.0000  -0.0214 1216 ALA B CA  
17875 C C   . ALA B 1218 ? 0.2091 0.2152 0.2181 0.0182  0.0006  -0.0210 1216 ALA B C   
17876 O O   . ALA B 1218 ? 0.2136 0.2232 0.2232 0.0192  0.0015  -0.0206 1216 ALA B O   
17877 C CB  . ALA B 1218 ? 0.2038 0.2037 0.2105 0.0208  0.0003  -0.0224 1216 ALA B CB  
17878 N N   . SER B 1219 ? 0.1849 0.1907 0.1935 0.0165  0.0000  -0.0210 1217 SER B N   
17879 C CA  . SER B 1219 ? 0.1799 0.1890 0.1884 0.0154  0.0004  -0.0205 1217 SER B CA  
17880 C C   . SER B 1219 ? 0.1672 0.1756 0.1732 0.0153  0.0004  -0.0211 1217 SER B C   
17881 O O   . SER B 1219 ? 0.1665 0.1718 0.1715 0.0144  -0.0006 -0.0214 1217 SER B O   
17882 C CB  . SER B 1219 ? 0.1904 0.1994 0.2001 0.0135  -0.0003 -0.0199 1217 SER B CB  
17883 O OG  . SER B 1219 ? 0.2139 0.2256 0.2231 0.0123  0.0000  -0.0194 1217 SER B OG  
17884 N N   . ILE B 1220 ? 0.1886 0.2000 0.1936 0.0161  0.0015  -0.0211 1218 ILE B N   
17885 C CA  . ILE B 1220 ? 0.2034 0.2145 0.2057 0.0161  0.0018  -0.0216 1218 ILE B CA  
17886 C C   . ILE B 1220 ? 0.2112 0.2258 0.2134 0.0144  0.0021  -0.0206 1218 ILE B C   
17887 O O   . ILE B 1220 ? 0.2138 0.2327 0.2173 0.0144  0.0031  -0.0199 1218 ILE B O   
17888 C CB  . ILE B 1220 ? 0.2445 0.2564 0.2454 0.0186  0.0029  -0.0223 1218 ILE B CB  
17889 C CG1 . ILE B 1220 ? 0.2865 0.2947 0.2877 0.0202  0.0025  -0.0231 1218 ILE B CG1 
17890 C CG2 . ILE B 1220 ? 0.2590 0.2705 0.2567 0.0188  0.0033  -0.0230 1218 ILE B CG2 
17891 C CD1 . ILE B 1220 ? 0.3887 0.3981 0.3896 0.0230  0.0037  -0.0235 1218 ILE B CD1 
17892 N N   . ASN B 1221 ? 0.1908 0.2035 0.1913 0.0128  0.0014  -0.0205 1219 ASN B N   
17893 C CA  . ASN B 1221 ? 0.2096 0.2250 0.2094 0.0110  0.0017  -0.0196 1219 ASN B CA  
17894 C C   . ASN B 1221 ? 0.2459 0.2640 0.2437 0.0120  0.0030  -0.0198 1219 ASN B C   
17895 O O   . ASN B 1221 ? 0.2405 0.2562 0.2355 0.0126  0.0029  -0.0205 1219 ASN B O   
17896 C CB  . ASN B 1221 ? 0.2062 0.2182 0.2047 0.0092  0.0003  -0.0193 1219 ASN B CB  
17897 C CG  . ASN B 1221 ? 0.2381 0.2520 0.2353 0.0073  0.0004  -0.0183 1219 ASN B CG  
17898 O OD1 . ASN B 1221 ? 0.2261 0.2441 0.2237 0.0069  0.0016  -0.0176 1219 ASN B OD1 
17899 N ND2 . ASN B 1221 ? 0.2562 0.2670 0.2517 0.0060  -0.0007 -0.0180 1219 ASN B ND2 
17900 N N   . THR B 1222 ? 0.1982 0.2214 0.1973 0.0123  0.0043  -0.0191 1220 THR B N   
17901 C CA  . THR B 1222 ? 0.2153 0.2419 0.2128 0.0135  0.0059  -0.0192 1220 THR B CA  
17902 C C   . THR B 1222 ? 0.2846 0.3137 0.2807 0.0112  0.0062  -0.0181 1220 THR B C   
17903 O O   . THR B 1222 ? 0.3282 0.3609 0.3230 0.0118  0.0077  -0.0179 1220 THR B O   
17904 C CB  . THR B 1222 ? 0.2331 0.2644 0.2329 0.0153  0.0072  -0.0190 1220 THR B CB  
17905 O OG1 . THR B 1222 ? 0.2557 0.2904 0.2581 0.0134  0.0070  -0.0177 1220 THR B OG1 
17906 C CG2 . THR B 1222 ? 0.2730 0.3014 0.2736 0.0177  0.0069  -0.0201 1220 THR B CG2 
17907 N N   . ALA B 1223 ? 0.2480 0.2752 0.2443 0.0086  0.0050  -0.0172 1221 ALA B N   
17908 C CA  . ALA B 1223 ? 0.3244 0.3524 0.3187 0.0062  0.0049  -0.0161 1221 ALA B CA  
17909 C C   . ALA B 1223 ? 0.4390 0.4624 0.4302 0.0059  0.0039  -0.0166 1221 ALA B C   
17910 O O   . ALA B 1223 ? 0.5108 0.5338 0.5001 0.0038  0.0036  -0.0155 1221 ALA B O   
17911 C CB  . ALA B 1223 ? 0.3191 0.3475 0.3152 0.0035  0.0040  -0.0148 1221 ALA B CB  
17912 N N   . ALA B 1224 ? 0.4261 0.4457 0.4165 0.0077  0.0033  -0.0180 1222 ALA B N   
17913 C CA  . ALA B 1224 ? 0.4432 0.4580 0.4310 0.0072  0.0019  -0.0184 1222 ALA B CA  
17914 C C   . ALA B 1224 ? 0.5553 0.5707 0.5392 0.0070  0.0025  -0.0183 1222 ALA B C   
17915 O O   . ALA B 1224 ? 0.5158 0.5283 0.4974 0.0057  0.0013  -0.0180 1222 ALA B O   
17916 C CB  . ALA B 1224 ? 0.3846 0.3955 0.3727 0.0089  0.0009  -0.0199 1222 ALA B CB  
17917 N N   . ALA B 1225 ? 0.6088 0.6281 0.5919 0.0084  0.0044  -0.0186 1223 ALA B N   
17918 C CA  . ALA B 1225 ? 0.5507 0.5710 0.5298 0.0084  0.0054  -0.0185 1223 ALA B CA  
17919 C C   . ALA B 1225 ? 0.6158 0.6390 0.5943 0.0057  0.0057  -0.0166 1223 ALA B C   
17920 O O   . ALA B 1225 ? 0.6380 0.6622 0.6131 0.0053  0.0064  -0.0162 1223 ALA B O   
17921 C CB  . ALA B 1225 ? 0.5488 0.5723 0.5271 0.0111  0.0075  -0.0196 1223 ALA B CB  
17922 N N   . GLY B 1226 ? 0.5782 0.6026 0.5596 0.0037  0.0052  -0.0153 1224 GLY B N   
17923 C CA  . GLY B 1226 ? 0.5811 0.6076 0.5619 0.0008  0.0053  -0.0133 1224 GLY B CA  
17924 C C   . GLY B 1226 ? 0.6085 0.6409 0.5921 -0.0002 0.0066  -0.0121 1224 GLY B C   
17925 O O   . GLY B 1226 ? 0.5275 0.5616 0.5108 -0.0030 0.0066  -0.0104 1224 GLY B O   
17926 N N   . GLY B 1227 ? 0.5225 0.5581 0.5090 0.0018  0.0076  -0.0129 1225 GLY B N   
17927 C CA  . GLY B 1227 ? 0.5525 0.5941 0.5420 0.0009  0.0087  -0.0117 1225 GLY B CA  
17928 C C   . GLY B 1227 ? 0.5931 0.6365 0.5857 0.0035  0.0092  -0.0128 1225 GLY B C   
17929 O O   . GLY B 1227 ? 0.5439 0.5837 0.5362 0.0059  0.0088  -0.0144 1225 GLY B O   
17930 N N   . ASN B 1228 ? 0.5277 0.5770 0.5233 0.0029  0.0100  -0.0118 1226 ASN B N   
17931 C CA  . ASN B 1228 ? 0.5955 0.6472 0.5942 0.0051  0.0105  -0.0124 1226 ASN B CA  
17932 C C   . ASN B 1228 ? 0.6174 0.6757 0.6168 0.0074  0.0127  -0.0124 1226 ASN B C   
17933 O O   . ASN B 1228 ? 0.6799 0.7440 0.6798 0.0058  0.0138  -0.0109 1226 ASN B O   
17934 C CB  . ASN B 1228 ? 0.5677 0.6212 0.5695 0.0028  0.0095  -0.0113 1226 ASN B CB  
17935 C CG  . ASN B 1228 ? 0.5804 0.6349 0.5852 0.0050  0.0094  -0.0120 1226 ASN B CG  
17936 O OD1 . ASN B 1228 ? 0.5648 0.6220 0.5704 0.0081  0.0106  -0.0127 1226 ASN B OD1 
17937 N ND2 . ASN B 1228 ? 0.4670 0.5192 0.4732 0.0036  0.0079  -0.0119 1226 ASN B ND2 
17938 N N   . ALA B 1229 ? 0.6289 0.6863 0.6283 0.0111  0.0134  -0.0139 1227 ALA B N   
17939 C CA  . ALA B 1229 ? 0.6662 0.7292 0.6660 0.0139  0.0156  -0.0141 1227 ALA B CA  
17940 C C   . ALA B 1229 ? 0.7020 0.7722 0.7062 0.0139  0.0162  -0.0129 1227 ALA B C   
17941 O O   . ALA B 1229 ? 0.6636 0.7410 0.6689 0.0139  0.0178  -0.0118 1227 ALA B O   
17942 C CB  . ALA B 1229 ? 0.6043 0.6633 0.6025 0.0179  0.0159  -0.0162 1227 ALA B CB  
17943 N N   . SER B 1230 ? 0.7042 0.7727 0.7108 0.0139  0.0148  -0.0130 1228 SER B N   
17944 C CA  . SER B 1230 ? 0.7136 0.7886 0.7242 0.0142  0.0152  -0.0119 1228 SER B CA  
17945 C C   . SER B 1230 ? 0.7445 0.8246 0.7568 0.0102  0.0149  -0.0099 1228 SER B C   
17946 O O   . SER B 1230 ? 0.7578 0.8458 0.7728 0.0102  0.0160  -0.0087 1228 SER B O   
17947 C CB  . SER B 1230 ? 0.7010 0.7724 0.7134 0.0152  0.0137  -0.0125 1228 SER B CB  
17948 N N   . LEU B 1231 ? 0.6979 0.7736 0.7086 0.0067  0.0135  -0.0095 1229 LEU B N   
17949 C CA  . LEU B 1231 ? 0.6921 0.7716 0.7038 0.0026  0.0130  -0.0076 1229 LEU B CA  
17950 C C   . LEU B 1231 ? 0.7231 0.8077 0.7337 0.0015  0.0148  -0.0064 1229 LEU B C   
17951 O O   . LEU B 1231 ? 0.7244 0.8133 0.7361 -0.0019 0.0146  -0.0046 1229 LEU B O   
17952 C CB  . LEU B 1231 ? 0.6371 0.7097 0.6470 -0.0007 0.0110  -0.0075 1229 LEU B CB  
17953 C CG  . LEU B 1231 ? 0.5286 0.5973 0.5399 -0.0010 0.0091  -0.0081 1229 LEU B CG  
17954 C CD1 . LEU B 1231 ? 0.4459 0.5085 0.4551 -0.0042 0.0074  -0.0079 1229 LEU B CD1 
17955 C CD2 . LEU B 1231 ? 0.5332 0.6079 0.5480 -0.0018 0.0090  -0.0071 1229 LEU B CD2 
17956 N N   . MET B 1232 ? 0.7058 0.7900 0.7141 0.0044  0.0163  -0.0074 1230 MET B N   
17957 C CA  . MET B 1232 ? 0.6991 0.7890 0.7064 0.0038  0.0183  -0.0063 1230 MET B CA  
17958 C C   . MET B 1232 ? 0.7082 0.8082 0.7194 0.0043  0.0198  -0.0050 1230 MET B C   
17959 O O   . MET B 1232 ? 0.6160 0.7222 0.6279 0.0018  0.0208  -0.0031 1230 MET B O   
17960 C CB  . MET B 1232 ? 0.6489 0.7360 0.6526 0.0072  0.0196  -0.0080 1230 MET B CB  
17961 N N   . ALA B 1233 ? 0.7872 0.8893 0.8013 0.0075  0.0199  -0.0058 1231 ALA B N   
17962 C CA  . ALA B 1233 ? 0.8395 0.9514 0.8579 0.0082  0.0211  -0.0044 1231 ALA B CA  
17963 C C   . ALA B 1233 ? 0.8440 0.9589 0.8656 0.0044  0.0194  -0.0028 1231 ALA B C   
17964 O O   . ALA B 1233 ? 0.8754 0.9992 0.9006 0.0038  0.0202  -0.0012 1231 ALA B O   
17965 C CB  . ALA B 1233 ? 0.8033 0.9161 0.8232 0.0135  0.0219  -0.0058 1231 ALA B CB  
17966 N N   . ILE B 1234 ? 0.7785 0.8861 0.7988 0.0018  0.0171  -0.0031 1232 ILE B N   
17967 C CA  . ILE B 1234 ? 0.7426 0.8517 0.7654 -0.0018 0.0153  -0.0019 1232 ILE B CA  
17968 C C   . ILE B 1234 ? 0.7076 0.8185 0.7295 -0.0068 0.0150  0.0000  1232 ILE B C   
17969 O O   . ILE B 1234 ? 0.6798 0.7840 0.6983 -0.0089 0.0141  -0.0002 1232 ILE B O   
17970 C CB  . ILE B 1234 ? 0.6750 0.7755 0.6967 -0.0019 0.0131  -0.0032 1232 ILE B CB  
17971 C CG1 . ILE B 1234 ? 0.7057 0.8061 0.7291 0.0025  0.0133  -0.0045 1232 ILE B CG1 
17972 C CG2 . ILE B 1234 ? 0.5546 0.6551 0.5774 -0.0063 0.0111  -0.0021 1232 ILE B CG2 
17973 C CD1 . ILE B 1234 ? 0.5485 0.6424 0.5717 0.0022  0.0112  -0.0054 1232 ILE B CD1 
17974 N N   . GLY B 1235 ? 0.6451 0.7652 0.6701 -0.0087 0.0156  0.0019  1233 GLY B N   
17975 C CA  . GLY B 1235 ? 0.4698 0.5924 0.4944 -0.0138 0.0153  0.0040  1233 GLY B CA  
17976 C C   . GLY B 1235 ? 0.4628 0.5912 0.4910 -0.0172 0.0140  0.0057  1233 GLY B C   
17977 O O   . GLY B 1235 ? 0.5919 0.7270 0.6240 -0.0151 0.0144  0.0059  1233 GLY B O   
17978 O OXT . GLY B 1235 ? 0.2695 0.3960 0.2970 -0.0220 0.0124  0.0068  1233 GLY B OXT 
# 
