data_9E5W
# 
_entry.id   9E5W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9E5W         pdb_00009e5w 10.2210/pdb9e5w/pdb 
WWPDB D_1000289409 ?            ?                   
# 
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 2025-02-05 
2 'Structure model' 1 1 2025-02-19 
# 
_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 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9E5W 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tannerjj@missouri.edu 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Tanner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8314-113X 
# 
_audit_author.name               'Tanner, J.J.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            765 
_citation.language                  ? 
_citation.page_first                110319 
_citation.page_last                 110319 
_citation.title                     
;Biochemical, structural, and cellular characterization of S-but-3-yn-2-ylglycine as a mechanism-based covalent inactivator of the flavoenzyme proline dehydrogenase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2025.110319 
_citation.pdbx_database_id_PubMed   39870289 
_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 'Ji, J.'         2 ? 
primary 'Scott, G.K.'    3 ? 
primary 'Campbell, A.C.' 4 ? 
primary 'Nix, J.C.'      5 ? 
primary 'Tadeo, A.'      6 ? 
primary 'Ellerby, L.M.'  7 ? 
primary 'Benz, C.C.'     8 ? 
primary 'Tanner, J.J.'   9 ? 
# 
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 'N-propargylglycine-modified flavin adenine dinucleotide' 898.664    2    ?                ? ? ? 
3  non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE                         663.425    2    ?                ? ? ? 
4  non-polymer syn 'SULFATE ION'                                             96.063     7    ?                ? ? ? 
5  non-polymer syn 'MAGNESIUM ION'                                           24.305     2    ?                ? ? ? 
6  non-polymer syn 'FORMIC ACID'                                             46.025     2    ?                ? ? ? 
7  non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                   106.120    3    ?                ? ? ? 
8  non-polymer syn 'TETRAETHYLENE GLYCOL'                                    194.226    1    ?                ? ? ? 
9  non-polymer syn 'TRIETHYLENE GLYCOL'                                      150.173    1    ?                ? ? ? 
10 water       nat water                                                     18.015     1444 ?                ? ? ? 
# 
_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  'N-propargylglycine-modified flavin adenine dinucleotide' P5F 
3  NICOTINAMIDE-ADENINE-DINUCLEOTIDE                         NAD 
4  'SULFATE ION'                                             SO4 
5  'MAGNESIUM ION'                                           MG  
6  'FORMIC ACID'                                             FMT 
7  'DI(HYDROXYETHYL)ETHER'                                   PEG 
8  'TETRAETHYLENE GLYCOL'                                    PG4 
9  'TRIETHYLENE GLYCOL'                                      PGE 
10 water                                                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    SER n 
1 2    MET n 
1 3    MET n 
1 4    SER n 
1 5    PRO n 
1 6    ASN n 
1 7    PRO n 
1 8    LEU n 
1 9    GLN n 
1 10   LYS n 
1 11   PRO n 
1 12   ALA n 
1 13   ILE n 
1 14   ASP n 
1 15   ALA n 
1 16   ALA n 
1 17   PRO n 
1 18   ALA n 
1 19   PRO n 
1 20   PHE n 
1 21   ALA n 
1 22   ASP n 
1 23   PHE n 
1 24   ALA n 
1 25   PRO n 
1 26   PRO n 
1 27   VAL n 
1 28   ARG n 
1 29   PRO n 
1 30   GLN n 
1 31   SER n 
1 32   THR n 
1 33   LEU n 
1 34   ARG n 
1 35   ARG n 
1 36   ALA n 
1 37   ILE n 
1 38   THR n 
1 39   ALA n 
1 40   ALA n 
1 41   TYR n 
1 42   ARG n 
1 43   ARG n 
1 44   PRO n 
1 45   GLU n 
1 46   THR n 
1 47   GLU n 
1 48   CYS n 
1 49   LEU n 
1 50   PRO n 
1 51   PRO n 
1 52   LEU n 
1 53   VAL n 
1 54   GLU n 
1 55   ALA n 
1 56   ALA n 
1 57   THR n 
1 58   GLN n 
1 59   SER n 
1 60   LYS n 
1 61   GLU n 
1 62   ILE n 
1 63   ARG n 
1 64   ASP n 
1 65   ALA n 
1 66   ALA n 
1 67   ALA n 
1 68   SER n 
1 69   THR n 
1 70   ALA n 
1 71   ARG n 
1 72   LYS n 
1 73   LEU n 
1 74   ILE n 
1 75   GLU n 
1 76   ALA n 
1 77   LEU n 
1 78   ARG n 
1 79   GLY n 
1 80   LYS n 
1 81   HIS n 
1 82   SER n 
1 83   GLY n 
1 84   SER n 
1 85   GLY n 
1 86   VAL n 
1 87   GLU n 
1 88   GLY n 
1 89   LEU n 
1 90   VAL n 
1 91   GLN n 
1 92   GLU n 
1 93   TYR n 
1 94   SER n 
1 95   LEU n 
1 96   SER n 
1 97   SER n 
1 98   GLN n 
1 99   GLU n 
1 100  GLY n 
1 101  VAL n 
1 102  ALA n 
1 103  LEU n 
1 104  MET n 
1 105  CYS n 
1 106  LEU n 
1 107  ALA n 
1 108  GLU n 
1 109  ALA n 
1 110  LEU n 
1 111  LEU n 
1 112  ARG n 
1 113  ILE n 
1 114  PRO n 
1 115  ASP n 
1 116  THR n 
1 117  ALA n 
1 118  THR n 
1 119  ARG n 
1 120  ASP n 
1 121  ALA n 
1 122  LEU n 
1 123  ILE n 
1 124  ARG n 
1 125  ASP n 
1 126  LYS n 
1 127  ILE n 
1 128  ALA n 
1 129  ASP n 
1 130  GLY n 
1 131  ASN n 
1 132  TRP n 
1 133  LYS n 
1 134  SER n 
1 135  HIS n 
1 136  LEU n 
1 137  GLY n 
1 138  GLY n 
1 139  SER n 
1 140  ARG n 
1 141  SER n 
1 142  LEU n 
1 143  PHE n 
1 144  VAL n 
1 145  ASN n 
1 146  ALA n 
1 147  ALA n 
1 148  THR n 
1 149  TRP n 
1 150  GLY n 
1 151  LEU n 
1 152  VAL n 
1 153  VAL n 
1 154  THR n 
1 155  GLY n 
1 156  LYS n 
1 157  LEU n 
1 158  THR n 
1 159  SER n 
1 160  THR n 
1 161  VAL n 
1 162  ASN n 
1 163  ASP n 
1 164  ARG n 
1 165  SER n 
1 166  LEU n 
1 167  ALA n 
1 168  ALA n 
1 169  ALA n 
1 170  LEU n 
1 171  THR n 
1 172  ARG n 
1 173  LEU n 
1 174  ILE n 
1 175  SER n 
1 176  ARG n 
1 177  CYS n 
1 178  GLY n 
1 179  GLU n 
1 180  PRO n 
1 181  VAL n 
1 182  ILE n 
1 183  ARG n 
1 184  ARG n 
1 185  GLY n 
1 186  VAL n 
1 187  ASP n 
1 188  MET n 
1 189  ALA n 
1 190  MET n 
1 191  ARG n 
1 192  MET n 
1 193  MET n 
1 194  GLY n 
1 195  GLU n 
1 196  GLN n 
1 197  PHE n 
1 198  VAL n 
1 199  THR n 
1 200  GLY n 
1 201  GLU n 
1 202  THR n 
1 203  ILE n 
1 204  ARG n 
1 205  GLU n 
1 206  ALA n 
1 207  LEU n 
1 208  LYS n 
1 209  ARG n 
1 210  SER n 
1 211  LYS n 
1 212  GLU n 
1 213  LEU n 
1 214  GLU n 
1 215  GLU n 
1 216  LYS n 
1 217  GLY n 
1 218  PHE n 
1 219  SER n 
1 220  TYR n 
1 221  SER n 
1 222  TYR n 
1 223  ASP n 
1 224  MET n 
1 225  LEU n 
1 226  GLY n 
1 227  GLU n 
1 228  ALA n 
1 229  ALA n 
1 230  THR n 
1 231  THR n 
1 232  ALA n 
1 233  ALA n 
1 234  ASP n 
1 235  ALA n 
1 236  GLU n 
1 237  ARG n 
1 238  TYR n 
1 239  TYR n 
1 240  ARG n 
1 241  ASP n 
1 242  TYR n 
1 243  GLU n 
1 244  SER n 
1 245  ALA n 
1 246  ILE n 
1 247  HIS n 
1 248  ALA n 
1 249  ILE n 
1 250  GLY n 
1 251  LYS n 
1 252  ALA n 
1 253  SER n 
1 254  ALA n 
1 255  GLY n 
1 256  ARG n 
1 257  GLY n 
1 258  ILE n 
1 259  TYR n 
1 260  GLU n 
1 261  GLY n 
1 262  PRO n 
1 263  GLY n 
1 264  ILE n 
1 265  SER n 
1 266  ILE n 
1 267  LYS n 
1 268  LEU n 
1 269  SER n 
1 270  ALA n 
1 271  LEU n 
1 272  HIS n 
1 273  PRO n 
1 274  ARG n 
1 275  TYR n 
1 276  SER n 
1 277  ARG n 
1 278  ALA n 
1 279  GLN n 
1 280  ALA n 
1 281  ALA n 
1 282  ARG n 
1 283  VAL n 
1 284  MET n 
1 285  GLY n 
1 286  GLU n 
1 287  LEU n 
1 288  LEU n 
1 289  PRO n 
1 290  ARG n 
1 291  VAL n 
1 292  LYS n 
1 293  ALA n 
1 294  LEU n 
1 295  ALA n 
1 296  LEU n 
1 297  LEU n 
1 298  ALA n 
1 299  LYS n 
1 300  ASN n 
1 301  TYR n 
1 302  ASP n 
1 303  ILE n 
1 304  GLY n 
1 305  LEU n 
1 306  ASN n 
1 307  ILE n 
1 308  ASP n 
1 309  ALA n 
1 310  GLU n 
1 311  GLU n 
1 312  ALA n 
1 313  ASP n 
1 314  ARG n 
1 315  LEU n 
1 316  GLU n 
1 317  LEU n 
1 318  SER n 
1 319  LEU n 
1 320  ASP n 
1 321  LEU n 
1 322  LEU n 
1 323  GLU n 
1 324  VAL n 
1 325  LEU n 
1 326  CYS n 
1 327  LEU n 
1 328  ASP n 
1 329  GLY n 
1 330  ASP n 
1 331  LEU n 
1 332  SER n 
1 333  GLY n 
1 334  TRP n 
1 335  ASN n 
1 336  GLY n 
1 337  MET n 
1 338  GLY n 
1 339  PHE n 
1 340  VAL n 
1 341  VAL n 
1 342  GLN n 
1 343  ALA n 
1 344  TYR n 
1 345  GLY n 
1 346  LYS n 
1 347  ARG n 
1 348  CYS n 
1 349  PRO n 
1 350  PHE n 
1 351  VAL n 
1 352  LEU n 
1 353  ASP n 
1 354  PHE n 
1 355  ILE n 
1 356  ILE n 
1 357  ASP n 
1 358  LEU n 
1 359  ALA n 
1 360  ARG n 
1 361  ARG n 
1 362  SER n 
1 363  GLY n 
1 364  ARG n 
1 365  ARG n 
1 366  ILE n 
1 367  MET n 
1 368  VAL n 
1 369  ARG n 
1 370  LEU n 
1 371  VAL n 
1 372  LYS n 
1 373  GLY n 
1 374  ALA n 
1 375  TYR n 
1 376  TRP n 
1 377  ASP n 
1 378  ALA n 
1 379  GLU n 
1 380  ILE n 
1 381  LYS n 
1 382  ARG n 
1 383  ALA n 
1 384  GLN n 
1 385  LEU n 
1 386  ASP n 
1 387  GLY n 
1 388  LEU n 
1 389  ALA n 
1 390  ASP n 
1 391  PHE n 
1 392  PRO n 
1 393  VAL n 
1 394  PHE n 
1 395  THR n 
1 396  ARG n 
1 397  LYS n 
1 398  ILE n 
1 399  HIS n 
1 400  THR n 
1 401  ASP n 
1 402  VAL n 
1 403  SER n 
1 404  TYR n 
1 405  ILE n 
1 406  ALA n 
1 407  CYS n 
1 408  ALA n 
1 409  ALA n 
1 410  LYS n 
1 411  LEU n 
1 412  LEU n 
1 413  ALA n 
1 414  ALA n 
1 415  THR n 
1 416  ASP n 
1 417  VAL n 
1 418  VAL n 
1 419  PHE n 
1 420  PRO n 
1 421  GLN n 
1 422  PHE n 
1 423  ALA n 
1 424  THR n 
1 425  HIS n 
1 426  ASN n 
1 427  ALA n 
1 428  GLN n 
1 429  THR n 
1 430  LEU n 
1 431  ALA n 
1 432  ALA n 
1 433  ILE n 
1 434  TYR n 
1 435  HIS n 
1 436  MET n 
1 437  ALA n 
1 438  GLY n 
1 439  LYS n 
1 440  ASP n 
1 441  PHE n 
1 442  HIS n 
1 443  VAL n 
1 444  GLY n 
1 445  LYS n 
1 446  TYR n 
1 447  GLU n 
1 448  PHE n 
1 449  GLN n 
1 450  CYS n 
1 451  LEU n 
1 452  HIS n 
1 453  GLY n 
1 454  MET n 
1 455  GLY n 
1 456  GLU n 
1 457  PRO n 
1 458  LEU n 
1 459  TYR n 
1 460  GLU n 
1 461  GLU n 
1 462  VAL n 
1 463  VAL n 
1 464  GLY n 
1 465  ARG n 
1 466  GLY n 
1 467  LYS n 
1 468  LEU n 
1 469  ASP n 
1 470  ARG n 
1 471  PRO n 
1 472  CYS n 
1 473  ARG n 
1 474  ILE n 
1 475  TYR n 
1 476  ALA n 
1 477  PRO n 
1 478  VAL n 
1 479  GLY n 
1 480  THR n 
1 481  HIS n 
1 482  GLU n 
1 483  THR n 
1 484  LEU n 
1 485  LEU n 
1 486  ALA n 
1 487  TYR n 
1 488  LEU n 
1 489  VAL n 
1 490  ARG n 
1 491  ARG n 
1 492  LEU n 
1 493  LEU n 
1 494  GLU n 
1 495  ASN n 
1 496  GLY n 
1 497  ALA n 
1 498  ASN n 
1 499  SER n 
1 500  SER n 
1 501  PHE n 
1 502  VAL n 
1 503  HIS n 
1 504  ARG n 
1 505  ILE n 
1 506  ASN n 
1 507  ASP n 
1 508  PRO n 
1 509  LYS n 
1 510  VAL n 
1 511  SER n 
1 512  ILE n 
1 513  ASP n 
1 514  GLU n 
1 515  LEU n 
1 516  ILE n 
1 517  ALA n 
1 518  ASP n 
1 519  PRO n 
1 520  VAL n 
1 521  GLU n 
1 522  VAL n 
1 523  VAL n 
1 524  ARG n 
1 525  ALA n 
1 526  MET n 
1 527  PRO n 
1 528  VAL n 
1 529  VAL n 
1 530  GLY n 
1 531  ALA n 
1 532  LYS n 
1 533  HIS n 
1 534  ASP n 
1 535  ARG n 
1 536  ILE n 
1 537  ALA n 
1 538  LEU n 
1 539  PRO n 
1 540  ALA n 
1 541  GLU n 
1 542  LEU n 
1 543  PHE n 
1 544  GLY n 
1 545  ASP n 
1 546  ALA n 
1 547  ARG n 
1 548  THR n 
1 549  ASN n 
1 550  SER n 
1 551  ALA n 
1 552  GLY n 
1 553  LEU n 
1 554  ASP n 
1 555  LEU n 
1 556  SER n 
1 557  ASN n 
1 558  GLU n 
1 559  GLU n 
1 560  THR n 
1 561  LEU n 
1 562  ALA n 
1 563  SER n 
1 564  LEU n 
1 565  THR n 
1 566  GLU n 
1 567  ALA n 
1 568  LEU n 
1 569  ARG n 
1 570  GLU n 
1 571  SER n 
1 572  ALA n 
1 573  ALA n 
1 574  MET n 
1 575  LYS n 
1 576  TRP n 
1 577  THR n 
1 578  ALA n 
1 579  LEU n 
1 580  PRO n 
1 581  GLN n 
1 582  LEU n 
1 583  ALA n 
1 584  THR n 
1 585  GLY n 
1 586  PRO n 
1 587  ALA n 
1 588  ALA n 
1 589  GLY n 
1 590  GLU n 
1 591  THR n 
1 592  ARG n 
1 593  THR n 
1 594  VAL n 
1 595  LEU n 
1 596  ASN n 
1 597  PRO n 
1 598  GLY n 
1 599  ASP n 
1 600  HIS n 
1 601  ARG n 
1 602  ASP n 
1 603  VAL n 
1 604  VAL n 
1 605  GLY n 
1 606  SER n 
1 607  VAL n 
1 608  THR n 
1 609  GLU n 
1 610  THR n 
1 611  SER n 
1 612  GLU n 
1 613  GLU n 
1 614  ASP n 
1 615  ALA n 
1 616  ARG n 
1 617  ARG n 
1 618  ALA n 
1 619  VAL n 
1 620  ARG n 
1 621  LEU n 
1 622  ALA n 
1 623  ALA n 
1 624  ASP n 
1 625  ALA n 
1 626  ALA n 
1 627  PRO n 
1 628  ASP n 
1 629  TRP n 
1 630  ALA n 
1 631  ALA n 
1 632  VAL n 
1 633  PRO n 
1 634  PRO n 
1 635  SER n 
1 636  GLU n 
1 637  ARG n 
1 638  ALA n 
1 639  ALA n 
1 640  CYS n 
1 641  LEU n 
1 642  ASP n 
1 643  ARG n 
1 644  ALA n 
1 645  ALA n 
1 646  GLU n 
1 647  LEU n 
1 648  MET n 
1 649  GLN n 
1 650  ALA n 
1 651  ARG n 
1 652  MET n 
1 653  PRO n 
1 654  THR n 
1 655  LEU n 
1 656  LEU n 
1 657  GLY n 
1 658  LEU n 
1 659  ILE n 
1 660  ILE n 
1 661  ARG n 
1 662  GLU n 
1 663  ALA n 
1 664  GLY n 
1 665  LYS n 
1 666  SER n 
1 667  ALA n 
1 668  LEU n 
1 669  ASN n 
1 670  ALA n 
1 671  ILE n 
1 672  ALA n 
1 673  GLU n 
1 674  VAL n 
1 675  ARG n 
1 676  GLU n 
1 677  ALA n 
1 678  ILE n 
1 679  ASP n 
1 680  PHE n 
1 681  LEU n 
1 682  ARG n 
1 683  TYR n 
1 684  TYR n 
1 685  ALA n 
1 686  GLU n 
1 687  GLN n 
1 688  THR n 
1 689  ARG n 
1 690  ARG n 
1 691  THR n 
1 692  LEU n 
1 693  GLY n 
1 694  PRO n 
1 695  GLY n 
1 696  HIS n 
1 697  GLY n 
1 698  PRO n 
1 699  LEU n 
1 700  GLY n 
1 701  PRO n 
1 702  ILE n 
1 703  VAL n 
1 704  CYS n 
1 705  ILE n 
1 706  SER n 
1 707  PRO n 
1 708  TRP n 
1 709  ASN n 
1 710  PHE n 
1 711  PRO n 
1 712  LEU n 
1 713  ALA n 
1 714  ILE n 
1 715  PHE n 
1 716  THR n 
1 717  GLY n 
1 718  GLN n 
1 719  ILE n 
1 720  ALA n 
1 721  ALA n 
1 722  ALA n 
1 723  LEU n 
1 724  VAL n 
1 725  ALA n 
1 726  GLY n 
1 727  ASN n 
1 728  PRO n 
1 729  VAL n 
1 730  LEU n 
1 731  ALA n 
1 732  LYS n 
1 733  PRO n 
1 734  ALA n 
1 735  GLU n 
1 736  GLU n 
1 737  THR n 
1 738  PRO n 
1 739  LEU n 
1 740  ILE n 
1 741  ALA n 
1 742  ALA n 
1 743  GLU n 
1 744  GLY n 
1 745  VAL n 
1 746  ARG n 
1 747  ILE n 
1 748  LEU n 
1 749  ARG n 
1 750  GLU n 
1 751  ALA n 
1 752  GLY n 
1 753  ILE n 
1 754  PRO n 
1 755  ALA n 
1 756  SER n 
1 757  ALA n 
1 758  LEU n 
1 759  GLN n 
1 760  LEU n 
1 761  LEU n 
1 762  PRO n 
1 763  GLY n 
1 764  ASP n 
1 765  GLY n 
1 766  ARG n 
1 767  VAL n 
1 768  GLY n 
1 769  ALA n 
1 770  ALA n 
1 771  LEU n 
1 772  VAL n 
1 773  ALA n 
1 774  ALA n 
1 775  ALA n 
1 776  GLU n 
1 777  THR n 
1 778  ALA n 
1 779  GLY n 
1 780  VAL n 
1 781  MET n 
1 782  PHE n 
1 783  THR n 
1 784  GLY n 
1 785  SER n 
1 786  THR n 
1 787  GLU n 
1 788  VAL n 
1 789  ALA n 
1 790  ARG n 
1 791  LEU n 
1 792  ILE n 
1 793  GLN n 
1 794  ALA n 
1 795  GLN n 
1 796  LEU n 
1 797  ALA n 
1 798  ASP n 
1 799  ARG n 
1 800  LEU n 
1 801  SER n 
1 802  PRO n 
1 803  ALA n 
1 804  GLY n 
1 805  ARG n 
1 806  PRO n 
1 807  ILE n 
1 808  PRO n 
1 809  LEU n 
1 810  ILE n 
1 811  ALA n 
1 812  GLU n 
1 813  THR n 
1 814  GLY n 
1 815  GLY n 
1 816  GLN n 
1 817  ASN n 
1 818  ALA n 
1 819  MET n 
1 820  ILE n 
1 821  VAL n 
1 822  ASP n 
1 823  SER n 
1 824  SER n 
1 825  ALA n 
1 826  LEU n 
1 827  ALA n 
1 828  GLU n 
1 829  GLN n 
1 830  VAL n 
1 831  VAL n 
1 832  GLY n 
1 833  ASP n 
1 834  VAL n 
1 835  ILE n 
1 836  THR n 
1 837  SER n 
1 838  ALA n 
1 839  PHE n 
1 840  ASP n 
1 841  SER n 
1 842  ALA n 
1 843  GLY n 
1 844  GLN n 
1 845  ARG n 
1 846  CYS n 
1 847  SER n 
1 848  ALA n 
1 849  LEU n 
1 850  ARG n 
1 851  VAL n 
1 852  LEU n 
1 853  CYS n 
1 854  LEU n 
1 855  GLN n 
1 856  GLU n 
1 857  ASP n 
1 858  VAL n 
1 859  ALA n 
1 860  ASP n 
1 861  ARG n 
1 862  ILE n 
1 863  LEU n 
1 864  THR n 
1 865  MET n 
1 866  LEU n 
1 867  LYS n 
1 868  GLY n 
1 869  ALA n 
1 870  LEU n 
1 871  HIS n 
1 872  GLU n 
1 873  LEU n 
1 874  HIS n 
1 875  ILE n 
1 876  GLY n 
1 877  ARG n 
1 878  THR n 
1 879  ASP n 
1 880  ARG n 
1 881  LEU n 
1 882  SER n 
1 883  VAL n 
1 884  ASP n 
1 885  VAL n 
1 886  GLY n 
1 887  PRO n 
1 888  VAL n 
1 889  ILE n 
1 890  THR n 
1 891  SER n 
1 892  GLU n 
1 893  ALA n 
1 894  LYS n 
1 895  ASP n 
1 896  ASN n 
1 897  ILE n 
1 898  GLU n 
1 899  LYS n 
1 900  HIS n 
1 901  ILE n 
1 902  GLU n 
1 903  ARG n 
1 904  MET n 
1 905  ARG n 
1 906  GLY n 
1 907  LEU n 
1 908  GLY n 
1 909  ARG n 
1 910  LYS n 
1 911  VAL n 
1 912  GLU n 
1 913  GLN n 
1 914  ILE n 
1 915  GLY n 
1 916  LEU n 
1 917  ALA n 
1 918  SER n 
1 919  GLU n 
1 920  THR n 
1 921  GLY n 
1 922  VAL n 
1 923  GLY n 
1 924  THR n 
1 925  PHE n 
1 926  VAL n 
1 927  PRO n 
1 928  PRO n 
1 929  THR n 
1 930  ILE n 
1 931  ILE n 
1 932  GLU n 
1 933  LEU n 
1 934  GLU n 
1 935  LYS n 
1 936  LEU n 
1 937  SER n 
1 938  ASP n 
1 939  LEU n 
1 940  GLN n 
1 941  ARG n 
1 942  GLU n 
1 943  VAL n 
1 944  PHE n 
1 945  GLY n 
1 946  PRO n 
1 947  VAL n 
1 948  LEU n 
1 949  HIS n 
1 950  VAL n 
1 951  ILE n 
1 952  ARG n 
1 953  TYR n 
1 954  ARG n 
1 955  ARG n 
1 956  ASP n 
1 957  ASP n 
1 958  LEU n 
1 959  ASP n 
1 960  ARG n 
1 961  LEU n 
1 962  VAL n 
1 963  ASP n 
1 964  ASP n 
1 965  VAL n 
1 966  ASN n 
1 967  ALA n 
1 968  THR n 
1 969  GLY n 
1 970  TYR n 
1 971  GLY n 
1 972  LEU n 
1 973  THR n 
1 974  PHE n 
1 975  GLY n 
1 976  LEU n 
1 977  HIS n 
1 978  THR n 
1 979  ARG n 
1 980  LEU n 
1 981  ASP n 
1 982  GLU n 
1 983  THR n 
1 984  ILE n 
1 985  ALA n 
1 986  HIS n 
1 987  VAL n 
1 988  THR n 
1 989  SER n 
1 990  ARG n 
1 991  ILE n 
1 992  LYS n 
1 993  ALA n 
1 994  GLY n 
1 995  ASN n 
1 996  LEU n 
1 997  TYR n 
1 998  ILE n 
1 999  ASN n 
1 1000 ARG n 
1 1001 ASN n 
1 1002 ILE n 
1 1003 ILE n 
1 1004 GLY n 
1 1005 ALA n 
1 1006 VAL n 
1 1007 VAL n 
1 1008 GLY n 
1 1009 VAL n 
1 1010 GLN n 
1 1011 PRO n 
1 1012 PHE n 
1 1013 GLY n 
1 1014 GLY n 
1 1015 ARG n 
1 1016 GLY n 
1 1017 LEU n 
1 1018 SER n 
1 1019 GLY n 
1 1020 THR n 
1 1021 GLY n 
1 1022 PRO n 
1 1023 LYS n 
1 1024 ALA n 
1 1025 GLY n 
1 1026 GLY n 
1 1027 PRO n 
1 1028 LEU n 
1 1029 TYR n 
1 1030 LEU n 
1 1031 GLY n 
1 1032 ARG n 
1 1033 LEU n 
1 1034 VAL n 
1 1035 THR n 
1 1036 THR n 
1 1037 ALA n 
1 1038 PRO n 
1 1039 VAL n 
1 1040 PRO n 
1 1041 PRO n 
1 1042 GLN n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
1 1046 VAL n 
1 1047 HIS n 
1 1048 THR n 
1 1049 ASP n 
1 1050 PRO n 
1 1051 VAL n 
1 1052 LEU n 
1 1053 LEU n 
1 1054 ASP n 
1 1055 PHE n 
1 1056 ALA n 
1 1057 LYS n 
1 1058 TRP n 
1 1059 LEU n 
1 1060 ASP n 
1 1061 GLY n 
1 1062 LYS n 
1 1063 GLY n 
1 1064 ALA n 
1 1065 ARG n 
1 1066 ALA n 
1 1067 GLU n 
1 1068 ALA n 
1 1069 GLU n 
1 1070 ALA n 
1 1071 ALA n 
1 1072 ARG n 
1 1073 ASN n 
1 1074 ALA n 
1 1075 GLY n 
1 1076 SER n 
1 1077 SER n 
1 1078 SER n 
1 1079 ALA n 
1 1080 LEU n 
1 1081 GLY n 
1 1082 LEU n 
1 1083 ASP n 
1 1084 LEU n 
1 1085 GLU n 
1 1086 LEU n 
1 1087 PRO n 
1 1088 GLY n 
1 1089 PRO n 
1 1090 VAL n 
1 1091 GLY n 
1 1092 GLU n 
1 1093 ARG n 
1 1094 ASN n 
1 1095 LEU n 
1 1096 TYR n 
1 1097 THR n 
1 1098 LEU n 
1 1099 HIS n 
1 1100 ALA n 
1 1101 ARG n 
1 1102 GLY n 
1 1103 ARG n 
1 1104 ILE n 
1 1105 LEU n 
1 1106 LEU n 
1 1107 VAL n 
1 1108 PRO n 
1 1109 ALA n 
1 1110 THR n 
1 1111 GLU n 
1 1112 SER n 
1 1113 GLY n 
1 1114 LEU n 
1 1115 TYR n 
1 1116 HIS n 
1 1117 GLN n 
1 1118 LEU n 
1 1119 ALA n 
1 1120 ALA n 
1 1121 ALA n 
1 1122 LEU n 
1 1123 ALA n 
1 1124 THR n 
1 1125 GLY n 
1 1126 ASN n 
1 1127 SER n 
1 1128 VAL n 
1 1129 ALA n 
1 1130 ILE n 
1 1131 ASP n 
1 1132 ALA n 
1 1133 ALA n 
1 1134 SER n 
1 1135 GLY n 
1 1136 LEU n 
1 1137 GLN n 
1 1138 ALA n 
1 1139 SER n 
1 1140 LEU n 
1 1141 LYS n 
1 1142 ASN n 
1 1143 LEU n 
1 1144 PRO n 
1 1145 GLN n 
1 1146 THR n 
1 1147 VAL n 
1 1148 GLY n 
1 1149 LEU n 
1 1150 ARG n 
1 1151 VAL n 
1 1152 SER n 
1 1153 TRP n 
1 1154 SER n 
1 1155 LYS n 
1 1156 ASP n 
1 1157 TRP n 
1 1158 ALA n 
1 1159 ALA n 
1 1160 ASP n 
1 1161 GLY n 
1 1162 PRO n 
1 1163 PHE n 
1 1164 ALA n 
1 1165 GLY n 
1 1166 ALA n 
1 1167 LEU n 
1 1168 VAL n 
1 1169 GLU n 
1 1170 GLY n 
1 1171 ASP n 
1 1172 ALA n 
1 1173 GLU n 
1 1174 ARG n 
1 1175 ILE n 
1 1176 ARG n 
1 1177 ALA n 
1 1178 VAL n 
1 1179 ASN n 
1 1180 LYS n 
1 1181 ALA n 
1 1182 ILE n 
1 1183 ALA n 
1 1184 ALA n 
1 1185 LEU n 
1 1186 PRO n 
1 1187 GLY n 
1 1188 PRO n 
1 1189 LEU n 
1 1190 LEU n 
1 1191 LEU n 
1 1192 VAL n 
1 1193 GLN n 
1 1194 ALA n 
1 1195 ALA n 
1 1196 SER n 
1 1197 SER n 
1 1198 GLY n 
1 1199 GLU n 
1 1200 ILE n 
1 1201 ALA n 
1 1202 ARG n 
1 1203 ASN n 
1 1204 PRO n 
1 1205 ASP n 
1 1206 ALA n 
1 1207 TYR n 
1 1208 CYS n 
1 1209 LEU n 
1 1210 ASN n 
1 1211 TRP n 
1 1212 LEU n 
1 1213 VAL n 
1 1214 GLU n 
1 1215 GLU n 
1 1216 VAL n 
1 1217 SER n 
1 1218 ALA n 
1 1219 SER n 
1 1220 ILE n 
1 1221 ASN n 
1 1222 THR n 
1 1223 ALA n 
1 1224 ALA n 
1 1225 ALA n 
1 1226 GLY n 
1 1227 GLY n 
1 1228 ASN n 
1 1229 ALA n 
1 1230 SER n 
1 1231 LEU n 
1 1232 MET n 
1 1233 ALA n 
1 1234 ILE n 
1 1235 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1235 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'putA, SMc02181' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Sinorhizobium meliloti' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     382 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                   ? 'C3 H7 N O2'         89.093  
ARG 'L-peptide linking' y ARGININE                                                  ? 'C6 H15 N4 O2 1'     175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                ? 'C4 H8 N2 O3'        132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                           ? 'C4 H7 N O4'         133.103 
CYS 'L-peptide linking' y CYSTEINE                                                  ? 'C3 H7 N O2 S'       121.158 
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 
P5F non-polymer         . 'N-propargylglycine-modified flavin adenine dinucleotide' ? 'C32 H40 N10 O17 P2' 898.664 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                   ? 'C4 H10 O3'          106.120 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'                                    ? 'C8 H18 O5'          194.226 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'                                      ? 'C6 H14 O4'          150.173 
PHE 'L-peptide linking' y PHENYLALANINE                                             ? 'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                   ? 'C5 H9 N O2'         115.130 
SER 'L-peptide linking' y SERINE                                                    ? 'C3 H7 N O3'         105.093 
SO4 non-polymer         . 'SULFATE ION'                                             ? 'O4 S -2'            96.063  
THR 'L-peptide linking' y THREONINE                                                 ? 'C4 H9 N O3'         119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                ? 'C11 H12 N2 O2'      204.225 
TYR 'L-peptide linking' y TYROSINE                                                  ? 'C9 H11 N O3'        181.189 
VAL 'L-peptide linking' y VALINE                                                    ? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    SER 1    -1   ?    ?   ?   A . n 
A 1 2    MET 2    0    ?    ?   ?   A . n 
A 1 3    MET 3    1    ?    ?   ?   A . n 
A 1 4    SER 4    2    ?    ?   ?   A . n 
A 1 5    PRO 5    3    ?    ?   ?   A . n 
A 1 6    ASN 6    4    ?    ?   ?   A . n 
A 1 7    PRO 7    5    ?    ?   ?   A . n 
A 1 8    LEU 8    6    ?    ?   ?   A . n 
A 1 9    GLN 9    7    ?    ?   ?   A . n 
A 1 10   LYS 10   8    ?    ?   ?   A . n 
A 1 11   PRO 11   9    ?    ?   ?   A . n 
A 1 12   ALA 12   10   ?    ?   ?   A . n 
A 1 13   ILE 13   11   ?    ?   ?   A . n 
A 1 14   ASP 14   12   ?    ?   ?   A . n 
A 1 15   ALA 15   13   ?    ?   ?   A . n 
A 1 16   ALA 16   14   14   ALA ALA A . n 
A 1 17   PRO 17   15   15   PRO PRO A . n 
A 1 18   ALA 18   16   16   ALA ALA A . n 
A 1 19   PRO 19   17   17   PRO PRO A . n 
A 1 20   PHE 20   18   18   PHE PHE A . n 
A 1 21   ALA 21   19   19   ALA ALA A . n 
A 1 22   ASP 22   20   20   ASP ASP A . n 
A 1 23   PHE 23   21   21   PHE PHE A . n 
A 1 24   ALA 24   22   22   ALA ALA A . n 
A 1 25   PRO 25   23   23   PRO PRO A . n 
A 1 26   PRO 26   24   24   PRO PRO A . n 
A 1 27   VAL 27   25   25   VAL VAL A . n 
A 1 28   ARG 28   26   26   ARG ARG A . n 
A 1 29   PRO 29   27   27   PRO PRO A . n 
A 1 30   GLN 30   28   28   GLN GLN A . n 
A 1 31   SER 31   29   29   SER SER A . n 
A 1 32   THR 32   30   30   THR THR A . n 
A 1 33   LEU 33   31   31   LEU LEU A . n 
A 1 34   ARG 34   32   32   ARG ARG A . n 
A 1 35   ARG 35   33   33   ARG ARG A . n 
A 1 36   ALA 36   34   34   ALA ALA A . n 
A 1 37   ILE 37   35   35   ILE ILE A . n 
A 1 38   THR 38   36   36   THR THR A . n 
A 1 39   ALA 39   37   37   ALA ALA A . n 
A 1 40   ALA 40   38   38   ALA ALA A . n 
A 1 41   TYR 41   39   39   TYR TYR A . n 
A 1 42   ARG 42   40   40   ARG ARG A . n 
A 1 43   ARG 43   41   41   ARG ARG A . n 
A 1 44   PRO 44   42   42   PRO PRO A . n 
A 1 45   GLU 45   43   43   GLU GLU A . n 
A 1 46   THR 46   44   44   THR THR A . n 
A 1 47   GLU 47   45   45   GLU GLU A . n 
A 1 48   CYS 48   46   46   CYS CYS A . n 
A 1 49   LEU 49   47   47   LEU LEU A . n 
A 1 50   PRO 50   48   48   PRO PRO A . n 
A 1 51   PRO 51   49   49   PRO PRO A . n 
A 1 52   LEU 52   50   50   LEU LEU A . n 
A 1 53   VAL 53   51   51   VAL VAL A . n 
A 1 54   GLU 54   52   52   GLU GLU A . n 
A 1 55   ALA 55   53   53   ALA ALA A . n 
A 1 56   ALA 56   54   54   ALA ALA A . n 
A 1 57   THR 57   55   55   THR THR A . n 
A 1 58   GLN 58   56   56   GLN GLN A . n 
A 1 59   SER 59   57   57   SER SER A . n 
A 1 60   LYS 60   58   58   LYS LYS A . n 
A 1 61   GLU 61   59   59   GLU GLU A . n 
A 1 62   ILE 62   60   60   ILE ILE A . n 
A 1 63   ARG 63   61   61   ARG ARG A . n 
A 1 64   ASP 64   62   62   ASP ASP A . n 
A 1 65   ALA 65   63   63   ALA ALA A . n 
A 1 66   ALA 66   64   64   ALA ALA A . n 
A 1 67   ALA 67   65   65   ALA ALA A . n 
A 1 68   SER 68   66   66   SER SER A . n 
A 1 69   THR 69   67   67   THR THR A . n 
A 1 70   ALA 70   68   68   ALA ALA A . n 
A 1 71   ARG 71   69   69   ARG ARG A . n 
A 1 72   LYS 72   70   70   LYS LYS A . n 
A 1 73   LEU 73   71   71   LEU LEU A . n 
A 1 74   ILE 74   72   72   ILE ILE A . n 
A 1 75   GLU 75   73   73   GLU GLU A . n 
A 1 76   ALA 76   74   74   ALA ALA A . n 
A 1 77   LEU 77   75   75   LEU LEU A . n 
A 1 78   ARG 78   76   76   ARG ARG A . n 
A 1 79   GLY 79   77   77   GLY GLY A . n 
A 1 80   LYS 80   78   78   LYS LYS A . n 
A 1 81   HIS 81   79   ?    ?   ?   A . n 
A 1 82   SER 82   80   ?    ?   ?   A . n 
A 1 83   GLY 83   81   ?    ?   ?   A . n 
A 1 84   SER 84   82   ?    ?   ?   A . n 
A 1 85   GLY 85   83   83   GLY GLY A . n 
A 1 86   VAL 86   84   84   VAL VAL A . n 
A 1 87   GLU 87   85   85   GLU GLU A . n 
A 1 88   GLY 88   86   86   GLY GLY A . n 
A 1 89   LEU 89   87   87   LEU LEU A . n 
A 1 90   VAL 90   88   88   VAL VAL A . n 
A 1 91   GLN 91   89   89   GLN GLN A . n 
A 1 92   GLU 92   90   90   GLU GLU A . n 
A 1 93   TYR 93   91   91   TYR TYR A . n 
A 1 94   SER 94   92   92   SER SER A . n 
A 1 95   LEU 95   93   93   LEU LEU A . n 
A 1 96   SER 96   94   94   SER SER A . n 
A 1 97   SER 97   95   95   SER SER A . n 
A 1 98   GLN 98   96   96   GLN GLN A . n 
A 1 99   GLU 99   97   97   GLU GLU A . n 
A 1 100  GLY 100  98   98   GLY GLY A . n 
A 1 101  VAL 101  99   99   VAL VAL A . n 
A 1 102  ALA 102  100  100  ALA ALA A . n 
A 1 103  LEU 103  101  101  LEU LEU A . n 
A 1 104  MET 104  102  102  MET MET A . n 
A 1 105  CYS 105  103  103  CYS CYS A . n 
A 1 106  LEU 106  104  104  LEU LEU A . n 
A 1 107  ALA 107  105  105  ALA ALA A . n 
A 1 108  GLU 108  106  106  GLU GLU A . n 
A 1 109  ALA 109  107  107  ALA ALA A . n 
A 1 110  LEU 110  108  108  LEU LEU A . n 
A 1 111  LEU 111  109  109  LEU LEU A . n 
A 1 112  ARG 112  110  110  ARG ARG A . n 
A 1 113  ILE 113  111  111  ILE ILE A . n 
A 1 114  PRO 114  112  112  PRO PRO A . n 
A 1 115  ASP 115  113  113  ASP ASP A . n 
A 1 116  THR 116  114  114  THR THR A . n 
A 1 117  ALA 117  115  115  ALA ALA A . n 
A 1 118  THR 118  116  116  THR THR A . n 
A 1 119  ARG 119  117  117  ARG ARG A . n 
A 1 120  ASP 120  118  118  ASP ASP A . n 
A 1 121  ALA 121  119  119  ALA ALA A . n 
A 1 122  LEU 122  120  120  LEU LEU A . n 
A 1 123  ILE 123  121  121  ILE ILE A . n 
A 1 124  ARG 124  122  122  ARG ARG A . n 
A 1 125  ASP 125  123  123  ASP ASP A . n 
A 1 126  LYS 126  124  124  LYS LYS A . n 
A 1 127  ILE 127  125  125  ILE ILE A . n 
A 1 128  ALA 128  126  126  ALA ALA A . n 
A 1 129  ASP 129  127  127  ASP ASP A . n 
A 1 130  GLY 130  128  128  GLY GLY A . n 
A 1 131  ASN 131  129  129  ASN ASN A . n 
A 1 132  TRP 132  130  130  TRP TRP A . n 
A 1 133  LYS 133  131  131  LYS LYS A . n 
A 1 134  SER 134  132  132  SER SER A . n 
A 1 135  HIS 135  133  133  HIS HIS A . n 
A 1 136  LEU 136  134  134  LEU LEU A . n 
A 1 137  GLY 137  135  ?    ?   ?   A . n 
A 1 138  GLY 138  136  ?    ?   ?   A . n 
A 1 139  SER 139  137  137  SER SER A . n 
A 1 140  ARG 140  138  138  ARG ARG A . n 
A 1 141  SER 141  139  139  SER SER A . n 
A 1 142  LEU 142  140  140  LEU LEU A . n 
A 1 143  PHE 143  141  141  PHE PHE A . n 
A 1 144  VAL 144  142  142  VAL VAL A . n 
A 1 145  ASN 145  143  143  ASN ASN A . n 
A 1 146  ALA 146  144  144  ALA ALA A . n 
A 1 147  ALA 147  145  145  ALA ALA A . n 
A 1 148  THR 148  146  146  THR THR A . n 
A 1 149  TRP 149  147  147  TRP TRP A . n 
A 1 150  GLY 150  148  148  GLY GLY A . n 
A 1 151  LEU 151  149  149  LEU LEU A . n 
A 1 152  VAL 152  150  150  VAL VAL A . n 
A 1 153  VAL 153  151  151  VAL VAL A . n 
A 1 154  THR 154  152  152  THR THR A . n 
A 1 155  GLY 155  153  153  GLY GLY A . n 
A 1 156  LYS 156  154  154  LYS LYS A . n 
A 1 157  LEU 157  155  155  LEU LEU A . n 
A 1 158  THR 158  156  156  THR THR A . n 
A 1 159  SER 159  157  157  SER SER A . n 
A 1 160  THR 160  158  158  THR THR A . n 
A 1 161  VAL 161  159  159  VAL VAL A . n 
A 1 162  ASN 162  160  160  ASN ASN A . n 
A 1 163  ASP 163  161  161  ASP ASP A . n 
A 1 164  ARG 164  162  162  ARG ARG A . n 
A 1 165  SER 165  163  163  SER SER A . n 
A 1 166  LEU 166  164  164  LEU LEU A . n 
A 1 167  ALA 167  165  165  ALA ALA A . n 
A 1 168  ALA 168  166  166  ALA ALA A . n 
A 1 169  ALA 169  167  167  ALA ALA A . n 
A 1 170  LEU 170  168  168  LEU LEU A . n 
A 1 171  THR 171  169  169  THR THR A . n 
A 1 172  ARG 172  170  170  ARG ARG A . n 
A 1 173  LEU 173  171  171  LEU LEU A . n 
A 1 174  ILE 174  172  172  ILE ILE A . n 
A 1 175  SER 175  173  173  SER SER A . n 
A 1 176  ARG 176  174  174  ARG ARG A . n 
A 1 177  CYS 177  175  175  CYS CYS A . n 
A 1 178  GLY 178  176  176  GLY GLY A . n 
A 1 179  GLU 179  177  177  GLU GLU A . n 
A 1 180  PRO 180  178  178  PRO PRO A . n 
A 1 181  VAL 181  179  179  VAL VAL A . n 
A 1 182  ILE 182  180  180  ILE ILE A . n 
A 1 183  ARG 183  181  181  ARG ARG A . n 
A 1 184  ARG 184  182  182  ARG ARG A . n 
A 1 185  GLY 185  183  183  GLY GLY A . n 
A 1 186  VAL 186  184  184  VAL VAL A . n 
A 1 187  ASP 187  185  185  ASP ASP A . n 
A 1 188  MET 188  186  186  MET MET A . n 
A 1 189  ALA 189  187  187  ALA ALA A . n 
A 1 190  MET 190  188  188  MET MET A . n 
A 1 191  ARG 191  189  189  ARG ARG A . n 
A 1 192  MET 192  190  190  MET MET A . n 
A 1 193  MET 193  191  191  MET MET A . n 
A 1 194  GLY 194  192  192  GLY GLY A . n 
A 1 195  GLU 195  193  193  GLU GLU A . n 
A 1 196  GLN 196  194  194  GLN GLN A . n 
A 1 197  PHE 197  195  195  PHE PHE A . n 
A 1 198  VAL 198  196  196  VAL VAL A . n 
A 1 199  THR 199  197  197  THR THR A . n 
A 1 200  GLY 200  198  198  GLY GLY A . n 
A 1 201  GLU 201  199  199  GLU GLU A . n 
A 1 202  THR 202  200  200  THR THR A . n 
A 1 203  ILE 203  201  201  ILE ILE A . n 
A 1 204  ARG 204  202  202  ARG ARG A . n 
A 1 205  GLU 205  203  203  GLU GLU A . n 
A 1 206  ALA 206  204  204  ALA ALA A . n 
A 1 207  LEU 207  205  205  LEU LEU A . n 
A 1 208  LYS 208  206  206  LYS LYS A . n 
A 1 209  ARG 209  207  207  ARG ARG A . n 
A 1 210  SER 210  208  208  SER SER A . n 
A 1 211  LYS 211  209  209  LYS LYS A . n 
A 1 212  GLU 212  210  210  GLU GLU A . n 
A 1 213  LEU 213  211  211  LEU LEU A . n 
A 1 214  GLU 214  212  212  GLU GLU A . n 
A 1 215  GLU 215  213  213  GLU GLU A . n 
A 1 216  LYS 216  214  214  LYS LYS A . n 
A 1 217  GLY 217  215  215  GLY GLY A . n 
A 1 218  PHE 218  216  216  PHE PHE A . n 
A 1 219  SER 219  217  217  SER SER A . n 
A 1 220  TYR 220  218  218  TYR TYR A . n 
A 1 221  SER 221  219  219  SER SER A . n 
A 1 222  TYR 222  220  220  TYR TYR A . n 
A 1 223  ASP 223  221  221  ASP ASP A . n 
A 1 224  MET 224  222  222  MET MET A . n 
A 1 225  LEU 225  223  223  LEU LEU A . n 
A 1 226  GLY 226  224  224  GLY GLY A . n 
A 1 227  GLU 227  225  225  GLU GLU A . n 
A 1 228  ALA 228  226  226  ALA ALA A . n 
A 1 229  ALA 229  227  227  ALA ALA A . n 
A 1 230  THR 230  228  228  THR THR A . n 
A 1 231  THR 231  229  229  THR THR A . n 
A 1 232  ALA 232  230  230  ALA ALA A . n 
A 1 233  ALA 233  231  231  ALA ALA A . n 
A 1 234  ASP 234  232  232  ASP ASP A . n 
A 1 235  ALA 235  233  233  ALA ALA A . n 
A 1 236  GLU 236  234  234  GLU GLU A . n 
A 1 237  ARG 237  235  235  ARG ARG A . n 
A 1 238  TYR 238  236  236  TYR TYR A . n 
A 1 239  TYR 239  237  237  TYR TYR A . n 
A 1 240  ARG 240  238  238  ARG ARG A . n 
A 1 241  ASP 241  239  239  ASP ASP A . n 
A 1 242  TYR 242  240  240  TYR TYR A . n 
A 1 243  GLU 243  241  241  GLU GLU A . n 
A 1 244  SER 244  242  242  SER SER A . n 
A 1 245  ALA 245  243  243  ALA ALA A . n 
A 1 246  ILE 246  244  244  ILE ILE A . n 
A 1 247  HIS 247  245  245  HIS HIS A . n 
A 1 248  ALA 248  246  246  ALA ALA A . n 
A 1 249  ILE 249  247  247  ILE ILE A . n 
A 1 250  GLY 250  248  248  GLY GLY A . n 
A 1 251  LYS 251  249  249  LYS LYS A . n 
A 1 252  ALA 252  250  250  ALA ALA A . n 
A 1 253  SER 253  251  251  SER SER A . n 
A 1 254  ALA 254  252  252  ALA ALA A . n 
A 1 255  GLY 255  253  253  GLY GLY A . n 
A 1 256  ARG 256  254  254  ARG ARG A . n 
A 1 257  GLY 257  255  255  GLY GLY A . n 
A 1 258  ILE 258  256  256  ILE ILE A . n 
A 1 259  TYR 259  257  257  TYR TYR A . n 
A 1 260  GLU 260  258  258  GLU GLU A . n 
A 1 261  GLY 261  259  259  GLY GLY A . n 
A 1 262  PRO 262  260  260  PRO PRO A . n 
A 1 263  GLY 263  261  261  GLY GLY A . n 
A 1 264  ILE 264  262  262  ILE ILE A . n 
A 1 265  SER 265  263  263  SER SER A . n 
A 1 266  ILE 266  264  264  ILE ILE A . n 
A 1 267  LYS 267  265  265  LYS LYS A . n 
A 1 268  LEU 268  266  266  LEU LEU A . n 
A 1 269  SER 269  267  267  SER SER A . n 
A 1 270  ALA 270  268  268  ALA ALA A . n 
A 1 271  LEU 271  269  269  LEU LEU A . n 
A 1 272  HIS 272  270  270  HIS HIS A . n 
A 1 273  PRO 273  271  271  PRO PRO A . n 
A 1 274  ARG 274  272  272  ARG ARG A . n 
A 1 275  TYR 275  273  273  TYR TYR A . n 
A 1 276  SER 276  274  274  SER SER A . n 
A 1 277  ARG 277  275  275  ARG ARG A . n 
A 1 278  ALA 278  276  276  ALA ALA A . n 
A 1 279  GLN 279  277  277  GLN GLN A . n 
A 1 280  ALA 280  278  278  ALA ALA A . n 
A 1 281  ALA 281  279  279  ALA ALA A . n 
A 1 282  ARG 282  280  280  ARG ARG A . n 
A 1 283  VAL 283  281  281  VAL VAL A . n 
A 1 284  MET 284  282  282  MET MET A . n 
A 1 285  GLY 285  283  283  GLY GLY A . n 
A 1 286  GLU 286  284  284  GLU GLU A . n 
A 1 287  LEU 287  285  285  LEU LEU A . n 
A 1 288  LEU 288  286  286  LEU LEU A . n 
A 1 289  PRO 289  287  287  PRO PRO A . n 
A 1 290  ARG 290  288  288  ARG ARG A . n 
A 1 291  VAL 291  289  289  VAL VAL A . n 
A 1 292  LYS 292  290  290  LYS LYS A . n 
A 1 293  ALA 293  291  291  ALA ALA A . n 
A 1 294  LEU 294  292  292  LEU LEU A . n 
A 1 295  ALA 295  293  293  ALA ALA A . n 
A 1 296  LEU 296  294  294  LEU LEU A . n 
A 1 297  LEU 297  295  295  LEU LEU A . n 
A 1 298  ALA 298  296  296  ALA ALA A . n 
A 1 299  LYS 299  297  297  LYS LYS A . n 
A 1 300  ASN 300  298  298  ASN ASN A . n 
A 1 301  TYR 301  299  299  TYR TYR A . n 
A 1 302  ASP 302  300  300  ASP ASP A . n 
A 1 303  ILE 303  301  301  ILE ILE A . n 
A 1 304  GLY 304  302  302  GLY GLY A . n 
A 1 305  LEU 305  303  303  LEU LEU A . n 
A 1 306  ASN 306  304  304  ASN ASN A . n 
A 1 307  ILE 307  305  305  ILE ILE A . n 
A 1 308  ASP 308  306  306  ASP ASP A . n 
A 1 309  ALA 309  307  307  ALA ALA A . n 
A 1 310  GLU 310  308  308  GLU GLU A . n 
A 1 311  GLU 311  309  309  GLU GLU A . n 
A 1 312  ALA 312  310  310  ALA ALA A . n 
A 1 313  ASP 313  311  311  ASP ASP A . n 
A 1 314  ARG 314  312  312  ARG ARG A . n 
A 1 315  LEU 315  313  313  LEU LEU A . n 
A 1 316  GLU 316  314  314  GLU GLU A . n 
A 1 317  LEU 317  315  315  LEU LEU A . n 
A 1 318  SER 318  316  316  SER SER A . n 
A 1 319  LEU 319  317  317  LEU LEU A . n 
A 1 320  ASP 320  318  318  ASP ASP A . n 
A 1 321  LEU 321  319  319  LEU LEU A . n 
A 1 322  LEU 322  320  320  LEU LEU A . n 
A 1 323  GLU 323  321  321  GLU GLU A . n 
A 1 324  VAL 324  322  322  VAL VAL A . n 
A 1 325  LEU 325  323  323  LEU LEU A . n 
A 1 326  CYS 326  324  324  CYS CYS A . n 
A 1 327  LEU 327  325  325  LEU LEU A . n 
A 1 328  ASP 328  326  326  ASP ASP A . n 
A 1 329  GLY 329  327  327  GLY GLY A . n 
A 1 330  ASP 330  328  328  ASP ASP A . n 
A 1 331  LEU 331  329  329  LEU LEU A . n 
A 1 332  SER 332  330  330  SER SER A . n 
A 1 333  GLY 333  331  331  GLY GLY A . n 
A 1 334  TRP 334  332  332  TRP TRP A . n 
A 1 335  ASN 335  333  333  ASN ASN A . n 
A 1 336  GLY 336  334  334  GLY GLY A . n 
A 1 337  MET 337  335  335  MET MET A . n 
A 1 338  GLY 338  336  336  GLY GLY A . n 
A 1 339  PHE 339  337  337  PHE PHE A . n 
A 1 340  VAL 340  338  338  VAL VAL A . n 
A 1 341  VAL 341  339  339  VAL VAL A . n 
A 1 342  GLN 342  340  340  GLN GLN A . n 
A 1 343  ALA 343  341  341  ALA ALA A . n 
A 1 344  TYR 344  342  342  TYR TYR A . n 
A 1 345  GLY 345  343  343  GLY GLY A . n 
A 1 346  LYS 346  344  344  LYS LYS A . n 
A 1 347  ARG 347  345  345  ARG ARG A . n 
A 1 348  CYS 348  346  346  CYS CYS A . n 
A 1 349  PRO 349  347  347  PRO PRO A . n 
A 1 350  PHE 350  348  348  PHE PHE A . n 
A 1 351  VAL 351  349  349  VAL VAL A . n 
A 1 352  LEU 352  350  350  LEU LEU A . n 
A 1 353  ASP 353  351  351  ASP ASP A . n 
A 1 354  PHE 354  352  352  PHE PHE A . n 
A 1 355  ILE 355  353  353  ILE ILE A . n 
A 1 356  ILE 356  354  354  ILE ILE A . n 
A 1 357  ASP 357  355  355  ASP ASP A . n 
A 1 358  LEU 358  356  356  LEU LEU A . n 
A 1 359  ALA 359  357  357  ALA ALA A . n 
A 1 360  ARG 360  358  358  ARG ARG A . n 
A 1 361  ARG 361  359  359  ARG ARG A . n 
A 1 362  SER 362  360  360  SER SER A . n 
A 1 363  GLY 363  361  361  GLY GLY A . n 
A 1 364  ARG 364  362  362  ARG ARG A . n 
A 1 365  ARG 365  363  363  ARG ARG A . n 
A 1 366  ILE 366  364  364  ILE ILE A . n 
A 1 367  MET 367  365  365  MET MET A . n 
A 1 368  VAL 368  366  366  VAL VAL A . n 
A 1 369  ARG 369  367  367  ARG ARG A . n 
A 1 370  LEU 370  368  368  LEU LEU A . n 
A 1 371  VAL 371  369  369  VAL VAL A . n 
A 1 372  LYS 372  370  370  LYS LYS A . n 
A 1 373  GLY 373  371  371  GLY GLY A . n 
A 1 374  ALA 374  372  372  ALA ALA A . n 
A 1 375  TYR 375  373  373  TYR TYR A . n 
A 1 376  TRP 376  374  374  TRP TRP A . n 
A 1 377  ASP 377  375  375  ASP ASP A . n 
A 1 378  ALA 378  376  376  ALA ALA A . n 
A 1 379  GLU 379  377  377  GLU GLU A . n 
A 1 380  ILE 380  378  378  ILE ILE A . n 
A 1 381  LYS 381  379  379  LYS LYS A . n 
A 1 382  ARG 382  380  380  ARG ARG A . n 
A 1 383  ALA 383  381  381  ALA ALA A . n 
A 1 384  GLN 384  382  382  GLN GLN A . n 
A 1 385  LEU 385  383  383  LEU LEU A . n 
A 1 386  ASP 386  384  384  ASP ASP A . n 
A 1 387  GLY 387  385  385  GLY GLY A . n 
A 1 388  LEU 388  386  386  LEU LEU A . n 
A 1 389  ALA 389  387  387  ALA ALA A . n 
A 1 390  ASP 390  388  388  ASP ASP A . n 
A 1 391  PHE 391  389  389  PHE PHE A . n 
A 1 392  PRO 392  390  390  PRO PRO A . n 
A 1 393  VAL 393  391  391  VAL VAL A . n 
A 1 394  PHE 394  392  392  PHE PHE A . n 
A 1 395  THR 395  393  393  THR THR A . n 
A 1 396  ARG 396  394  394  ARG ARG A . n 
A 1 397  LYS 397  395  395  LYS LYS A . n 
A 1 398  ILE 398  396  396  ILE ILE A . n 
A 1 399  HIS 399  397  397  HIS HIS A . n 
A 1 400  THR 400  398  398  THR THR A . n 
A 1 401  ASP 401  399  399  ASP ASP A . n 
A 1 402  VAL 402  400  400  VAL VAL A . n 
A 1 403  SER 403  401  401  SER SER A . n 
A 1 404  TYR 404  402  402  TYR TYR A . n 
A 1 405  ILE 405  403  403  ILE ILE A . n 
A 1 406  ALA 406  404  404  ALA ALA A . n 
A 1 407  CYS 407  405  405  CYS CYS A . n 
A 1 408  ALA 408  406  406  ALA ALA A . n 
A 1 409  ALA 409  407  407  ALA ALA A . n 
A 1 410  LYS 410  408  408  LYS LYS A . n 
A 1 411  LEU 411  409  409  LEU LEU A . n 
A 1 412  LEU 412  410  410  LEU LEU A . n 
A 1 413  ALA 413  411  411  ALA ALA A . n 
A 1 414  ALA 414  412  412  ALA ALA A . n 
A 1 415  THR 415  413  413  THR THR A . n 
A 1 416  ASP 416  414  414  ASP ASP A . n 
A 1 417  VAL 417  415  415  VAL VAL A . n 
A 1 418  VAL 418  416  416  VAL VAL A . n 
A 1 419  PHE 419  417  417  PHE PHE A . n 
A 1 420  PRO 420  418  418  PRO PRO A . n 
A 1 421  GLN 421  419  419  GLN GLN A . n 
A 1 422  PHE 422  420  420  PHE PHE A . n 
A 1 423  ALA 423  421  421  ALA ALA A . n 
A 1 424  THR 424  422  422  THR THR A . n 
A 1 425  HIS 425  423  423  HIS HIS A . n 
A 1 426  ASN 426  424  424  ASN ASN A . n 
A 1 427  ALA 427  425  425  ALA ALA A . n 
A 1 428  GLN 428  426  426  GLN GLN A . n 
A 1 429  THR 429  427  427  THR THR A . n 
A 1 430  LEU 430  428  428  LEU LEU A . n 
A 1 431  ALA 431  429  429  ALA ALA A . n 
A 1 432  ALA 432  430  430  ALA ALA A . n 
A 1 433  ILE 433  431  431  ILE ILE A . n 
A 1 434  TYR 434  432  432  TYR TYR A . n 
A 1 435  HIS 435  433  433  HIS HIS A . n 
A 1 436  MET 436  434  434  MET MET A . n 
A 1 437  ALA 437  435  435  ALA ALA A . n 
A 1 438  GLY 438  436  436  GLY GLY A . n 
A 1 439  LYS 439  437  437  LYS LYS A . n 
A 1 440  ASP 440  438  438  ASP ASP A . n 
A 1 441  PHE 441  439  439  PHE PHE A . n 
A 1 442  HIS 442  440  440  HIS HIS A . n 
A 1 443  VAL 443  441  441  VAL VAL A . n 
A 1 444  GLY 444  442  442  GLY GLY A . n 
A 1 445  LYS 445  443  443  LYS LYS A . n 
A 1 446  TYR 446  444  444  TYR TYR A . n 
A 1 447  GLU 447  445  445  GLU GLU A . n 
A 1 448  PHE 448  446  446  PHE PHE A . n 
A 1 449  GLN 449  447  447  GLN GLN A . n 
A 1 450  CYS 450  448  448  CYS CYS A . n 
A 1 451  LEU 451  449  449  LEU LEU A . n 
A 1 452  HIS 452  450  450  HIS HIS A . n 
A 1 453  GLY 453  451  451  GLY GLY A . n 
A 1 454  MET 454  452  452  MET MET A . n 
A 1 455  GLY 455  453  453  GLY GLY A . n 
A 1 456  GLU 456  454  454  GLU GLU A . n 
A 1 457  PRO 457  455  455  PRO PRO A . n 
A 1 458  LEU 458  456  456  LEU LEU A . n 
A 1 459  TYR 459  457  457  TYR TYR A . n 
A 1 460  GLU 460  458  458  GLU GLU A . n 
A 1 461  GLU 461  459  459  GLU GLU A . n 
A 1 462  VAL 462  460  460  VAL VAL A . n 
A 1 463  VAL 463  461  461  VAL VAL A . n 
A 1 464  GLY 464  462  462  GLY GLY A . n 
A 1 465  ARG 465  463  463  ARG ARG A . n 
A 1 466  GLY 466  464  464  GLY GLY A . n 
A 1 467  LYS 467  465  465  LYS LYS A . n 
A 1 468  LEU 468  466  466  LEU LEU A . n 
A 1 469  ASP 469  467  467  ASP ASP A . n 
A 1 470  ARG 470  468  468  ARG ARG A . n 
A 1 471  PRO 471  469  469  PRO PRO A . n 
A 1 472  CYS 472  470  470  CYS CYS A . n 
A 1 473  ARG 473  471  471  ARG ARG A . n 
A 1 474  ILE 474  472  472  ILE ILE A . n 
A 1 475  TYR 475  473  473  TYR TYR A . n 
A 1 476  ALA 476  474  474  ALA ALA A . n 
A 1 477  PRO 477  475  475  PRO PRO A . n 
A 1 478  VAL 478  476  476  VAL VAL A . n 
A 1 479  GLY 479  477  477  GLY GLY A . n 
A 1 480  THR 480  478  478  THR THR A . n 
A 1 481  HIS 481  479  479  HIS HIS A . n 
A 1 482  GLU 482  480  480  GLU GLU A . n 
A 1 483  THR 483  481  481  THR THR A . n 
A 1 484  LEU 484  482  482  LEU LEU A . n 
A 1 485  LEU 485  483  483  LEU LEU A . n 
A 1 486  ALA 486  484  484  ALA ALA A . n 
A 1 487  TYR 487  485  485  TYR TYR A . n 
A 1 488  LEU 488  486  486  LEU LEU A . n 
A 1 489  VAL 489  487  487  VAL VAL A . n 
A 1 490  ARG 490  488  488  ARG ARG A . n 
A 1 491  ARG 491  489  489  ARG ARG A . n 
A 1 492  LEU 492  490  490  LEU LEU A . n 
A 1 493  LEU 493  491  491  LEU LEU A . n 
A 1 494  GLU 494  492  492  GLU GLU A . n 
A 1 495  ASN 495  493  493  ASN ASN A . n 
A 1 496  GLY 496  494  494  GLY GLY A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 1224 GLY GLY A . n 
A 1 1227 GLY 1227 1225 1225 GLY GLY A . n 
A 1 1228 ASN 1228 1226 1226 ASN ASN A . n 
A 1 1229 ALA 1229 1227 1227 ALA ALA A . n 
A 1 1230 SER 1230 1228 1228 SER SER A . n 
A 1 1231 LEU 1231 1229 1229 LEU LEU A . n 
A 1 1232 MET 1232 1230 1230 MET MET A . n 
A 1 1233 ALA 1233 1231 1231 ALA ALA A . n 
A 1 1234 ILE 1234 1232 ?    ?   ?   A . n 
A 1 1235 GLY 1235 1233 ?    ?   ?   A . n 
B 1 1    SER 1    -1   ?    ?   ?   B . n 
B 1 2    MET 2    0    ?    ?   ?   B . n 
B 1 3    MET 3    1    ?    ?   ?   B . n 
B 1 4    SER 4    2    ?    ?   ?   B . n 
B 1 5    PRO 5    3    ?    ?   ?   B . n 
B 1 6    ASN 6    4    ?    ?   ?   B . n 
B 1 7    PRO 7    5    ?    ?   ?   B . n 
B 1 8    LEU 8    6    ?    ?   ?   B . n 
B 1 9    GLN 9    7    ?    ?   ?   B . n 
B 1 10   LYS 10   8    ?    ?   ?   B . n 
B 1 11   PRO 11   9    ?    ?   ?   B . n 
B 1 12   ALA 12   10   ?    ?   ?   B . n 
B 1 13   ILE 13   11   ?    ?   ?   B . n 
B 1 14   ASP 14   12   ?    ?   ?   B . n 
B 1 15   ALA 15   13   ?    ?   ?   B . n 
B 1 16   ALA 16   14   14   ALA ALA B . n 
B 1 17   PRO 17   15   15   PRO PRO B . n 
B 1 18   ALA 18   16   16   ALA ALA B . n 
B 1 19   PRO 19   17   17   PRO PRO B . n 
B 1 20   PHE 20   18   18   PHE PHE B . n 
B 1 21   ALA 21   19   19   ALA ALA B . n 
B 1 22   ASP 22   20   20   ASP ASP B . n 
B 1 23   PHE 23   21   21   PHE PHE B . n 
B 1 24   ALA 24   22   22   ALA ALA B . n 
B 1 25   PRO 25   23   23   PRO PRO B . n 
B 1 26   PRO 26   24   24   PRO PRO B . n 
B 1 27   VAL 27   25   25   VAL VAL B . n 
B 1 28   ARG 28   26   26   ARG ARG B . n 
B 1 29   PRO 29   27   27   PRO PRO B . n 
B 1 30   GLN 30   28   28   GLN GLN B . n 
B 1 31   SER 31   29   29   SER SER B . n 
B 1 32   THR 32   30   30   THR THR B . n 
B 1 33   LEU 33   31   31   LEU LEU B . n 
B 1 34   ARG 34   32   32   ARG ARG B . n 
B 1 35   ARG 35   33   33   ARG ARG B . n 
B 1 36   ALA 36   34   34   ALA ALA B . n 
B 1 37   ILE 37   35   35   ILE ILE B . n 
B 1 38   THR 38   36   36   THR THR B . n 
B 1 39   ALA 39   37   37   ALA ALA B . n 
B 1 40   ALA 40   38   38   ALA ALA B . n 
B 1 41   TYR 41   39   39   TYR TYR B . n 
B 1 42   ARG 42   40   40   ARG ARG B . n 
B 1 43   ARG 43   41   41   ARG ARG B . n 
B 1 44   PRO 44   42   42   PRO PRO B . n 
B 1 45   GLU 45   43   43   GLU GLU B . n 
B 1 46   THR 46   44   44   THR THR B . n 
B 1 47   GLU 47   45   45   GLU GLU B . n 
B 1 48   CYS 48   46   46   CYS CYS B . n 
B 1 49   LEU 49   47   47   LEU LEU B . n 
B 1 50   PRO 50   48   48   PRO PRO B . n 
B 1 51   PRO 51   49   49   PRO PRO B . n 
B 1 52   LEU 52   50   50   LEU LEU B . n 
B 1 53   VAL 53   51   51   VAL VAL B . n 
B 1 54   GLU 54   52   52   GLU GLU B . n 
B 1 55   ALA 55   53   53   ALA ALA B . n 
B 1 56   ALA 56   54   54   ALA ALA B . n 
B 1 57   THR 57   55   55   THR THR B . n 
B 1 58   GLN 58   56   56   GLN GLN B . n 
B 1 59   SER 59   57   57   SER SER B . n 
B 1 60   LYS 60   58   58   LYS LYS B . n 
B 1 61   GLU 61   59   59   GLU GLU B . n 
B 1 62   ILE 62   60   60   ILE ILE B . n 
B 1 63   ARG 63   61   61   ARG ARG B . n 
B 1 64   ASP 64   62   62   ASP ASP B . n 
B 1 65   ALA 65   63   63   ALA ALA B . n 
B 1 66   ALA 66   64   64   ALA ALA B . n 
B 1 67   ALA 67   65   65   ALA ALA B . n 
B 1 68   SER 68   66   66   SER SER B . n 
B 1 69   THR 69   67   67   THR THR B . n 
B 1 70   ALA 70   68   68   ALA ALA B . n 
B 1 71   ARG 71   69   69   ARG ARG B . n 
B 1 72   LYS 72   70   70   LYS LYS B . n 
B 1 73   LEU 73   71   71   LEU LEU B . n 
B 1 74   ILE 74   72   72   ILE ILE B . n 
B 1 75   GLU 75   73   73   GLU GLU B . n 
B 1 76   ALA 76   74   74   ALA ALA B . n 
B 1 77   LEU 77   75   75   LEU LEU B . n 
B 1 78   ARG 78   76   76   ARG ARG B . n 
B 1 79   GLY 79   77   77   GLY GLY B . n 
B 1 80   LYS 80   78   78   LYS LYS B . n 
B 1 81   HIS 81   79   ?    ?   ?   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  135  GLY GLY B . n 
B 1 138  GLY 138  136  136  GLY GLY B . n 
B 1 139  SER 139  137  137  SER SER B . n 
B 1 140  ARG 140  138  138  ARG ARG B . n 
B 1 141  SER 141  139  139  SER SER B . n 
B 1 142  LEU 142  140  140  LEU LEU B . n 
B 1 143  PHE 143  141  141  PHE PHE B . n 
B 1 144  VAL 144  142  142  VAL VAL B . n 
B 1 145  ASN 145  143  143  ASN ASN B . n 
B 1 146  ALA 146  144  144  ALA ALA B . n 
B 1 147  ALA 147  145  145  ALA ALA B . n 
B 1 148  THR 148  146  146  THR THR B . n 
B 1 149  TRP 149  147  147  TRP TRP B . n 
B 1 150  GLY 150  148  148  GLY GLY B . n 
B 1 151  LEU 151  149  149  LEU LEU B . n 
B 1 152  VAL 152  150  150  VAL VAL B . n 
B 1 153  VAL 153  151  151  VAL VAL B . n 
B 1 154  THR 154  152  152  THR THR B . n 
B 1 155  GLY 155  153  153  GLY GLY B . n 
B 1 156  LYS 156  154  154  LYS LYS B . n 
B 1 157  LEU 157  155  155  LEU LEU B . n 
B 1 158  THR 158  156  156  THR THR B . n 
B 1 159  SER 159  157  157  SER SER B . n 
B 1 160  THR 160  158  158  THR THR B . n 
B 1 161  VAL 161  159  159  VAL VAL B . n 
B 1 162  ASN 162  160  160  ASN ASN B . n 
B 1 163  ASP 163  161  161  ASP ASP B . n 
B 1 164  ARG 164  162  162  ARG ARG B . n 
B 1 165  SER 165  163  163  SER SER B . n 
B 1 166  LEU 166  164  164  LEU LEU B . n 
B 1 167  ALA 167  165  165  ALA ALA B . n 
B 1 168  ALA 168  166  166  ALA ALA B . n 
B 1 169  ALA 169  167  167  ALA ALA B . n 
B 1 170  LEU 170  168  168  LEU LEU B . n 
B 1 171  THR 171  169  169  THR THR B . n 
B 1 172  ARG 172  170  170  ARG ARG B . n 
B 1 173  LEU 173  171  171  LEU LEU B . n 
B 1 174  ILE 174  172  172  ILE ILE B . n 
B 1 175  SER 175  173  173  SER SER B . n 
B 1 176  ARG 176  174  174  ARG ARG B . n 
B 1 177  CYS 177  175  175  CYS CYS B . n 
B 1 178  GLY 178  176  176  GLY GLY B . n 
B 1 179  GLU 179  177  177  GLU GLU B . n 
B 1 180  PRO 180  178  178  PRO PRO B . n 
B 1 181  VAL 181  179  179  VAL VAL B . n 
B 1 182  ILE 182  180  180  ILE ILE B . n 
B 1 183  ARG 183  181  181  ARG ARG B . n 
B 1 184  ARG 184  182  182  ARG ARG B . n 
B 1 185  GLY 185  183  183  GLY GLY B . n 
B 1 186  VAL 186  184  184  VAL VAL B . n 
B 1 187  ASP 187  185  185  ASP ASP B . n 
B 1 188  MET 188  186  186  MET MET B . n 
B 1 189  ALA 189  187  187  ALA ALA B . n 
B 1 190  MET 190  188  188  MET MET B . n 
B 1 191  ARG 191  189  189  ARG ARG B . n 
B 1 192  MET 192  190  190  MET MET B . n 
B 1 193  MET 193  191  191  MET MET B . n 
B 1 194  GLY 194  192  192  GLY GLY B . n 
B 1 195  GLU 195  193  193  GLU GLU B . n 
B 1 196  GLN 196  194  194  GLN GLN B . n 
B 1 197  PHE 197  195  195  PHE PHE B . n 
B 1 198  VAL 198  196  196  VAL VAL B . n 
B 1 199  THR 199  197  197  THR THR B . n 
B 1 200  GLY 200  198  198  GLY GLY B . n 
B 1 201  GLU 201  199  199  GLU GLU B . n 
B 1 202  THR 202  200  200  THR THR B . n 
B 1 203  ILE 203  201  201  ILE ILE B . n 
B 1 204  ARG 204  202  202  ARG ARG B . n 
B 1 205  GLU 205  203  203  GLU GLU B . n 
B 1 206  ALA 206  204  204  ALA ALA B . n 
B 1 207  LEU 207  205  205  LEU LEU B . n 
B 1 208  LYS 208  206  206  LYS LYS B . n 
B 1 209  ARG 209  207  207  ARG ARG B . n 
B 1 210  SER 210  208  208  SER SER B . n 
B 1 211  LYS 211  209  209  LYS LYS B . n 
B 1 212  GLU 212  210  210  GLU GLU B . n 
B 1 213  LEU 213  211  211  LEU LEU B . n 
B 1 214  GLU 214  212  212  GLU GLU B . n 
B 1 215  GLU 215  213  213  GLU GLU B . n 
B 1 216  LYS 216  214  214  LYS LYS B . n 
B 1 217  GLY 217  215  215  GLY GLY B . n 
B 1 218  PHE 218  216  216  PHE PHE B . n 
B 1 219  SER 219  217  217  SER SER B . n 
B 1 220  TYR 220  218  218  TYR TYR B . n 
B 1 221  SER 221  219  219  SER SER B . n 
B 1 222  TYR 222  220  220  TYR TYR B . n 
B 1 223  ASP 223  221  221  ASP ASP B . n 
B 1 224  MET 224  222  222  MET MET B . n 
B 1 225  LEU 225  223  223  LEU LEU B . n 
B 1 226  GLY 226  224  224  GLY GLY B . n 
B 1 227  GLU 227  225  225  GLU GLU B . n 
B 1 228  ALA 228  226  226  ALA ALA B . n 
B 1 229  ALA 229  227  227  ALA ALA B . n 
B 1 230  THR 230  228  228  THR THR B . n 
B 1 231  THR 231  229  229  THR THR B . n 
B 1 232  ALA 232  230  230  ALA ALA B . n 
B 1 233  ALA 233  231  231  ALA ALA B . n 
B 1 234  ASP 234  232  232  ASP ASP B . n 
B 1 235  ALA 235  233  233  ALA ALA B . n 
B 1 236  GLU 236  234  234  GLU GLU B . n 
B 1 237  ARG 237  235  235  ARG ARG B . n 
B 1 238  TYR 238  236  236  TYR TYR B . n 
B 1 239  TYR 239  237  237  TYR TYR B . n 
B 1 240  ARG 240  238  238  ARG ARG B . n 
B 1 241  ASP 241  239  239  ASP ASP B . n 
B 1 242  TYR 242  240  240  TYR TYR B . n 
B 1 243  GLU 243  241  241  GLU GLU B . n 
B 1 244  SER 244  242  242  SER SER B . n 
B 1 245  ALA 245  243  243  ALA ALA B . n 
B 1 246  ILE 246  244  244  ILE ILE B . n 
B 1 247  HIS 247  245  245  HIS HIS B . n 
B 1 248  ALA 248  246  246  ALA ALA B . n 
B 1 249  ILE 249  247  247  ILE ILE B . n 
B 1 250  GLY 250  248  248  GLY GLY B . n 
B 1 251  LYS 251  249  249  LYS LYS B . n 
B 1 252  ALA 252  250  250  ALA ALA B . n 
B 1 253  SER 253  251  251  SER SER B . n 
B 1 254  ALA 254  252  252  ALA ALA B . n 
B 1 255  GLY 255  253  253  GLY GLY B . n 
B 1 256  ARG 256  254  254  ARG ARG B . n 
B 1 257  GLY 257  255  255  GLY GLY B . n 
B 1 258  ILE 258  256  256  ILE ILE B . n 
B 1 259  TYR 259  257  257  TYR TYR B . n 
B 1 260  GLU 260  258  258  GLU GLU B . n 
B 1 261  GLY 261  259  259  GLY GLY B . n 
B 1 262  PRO 262  260  260  PRO PRO B . n 
B 1 263  GLY 263  261  261  GLY GLY B . n 
B 1 264  ILE 264  262  262  ILE ILE B . n 
B 1 265  SER 265  263  263  SER SER B . n 
B 1 266  ILE 266  264  264  ILE ILE B . n 
B 1 267  LYS 267  265  265  LYS LYS B . n 
B 1 268  LEU 268  266  266  LEU LEU B . n 
B 1 269  SER 269  267  267  SER SER B . n 
B 1 270  ALA 270  268  268  ALA ALA B . n 
B 1 271  LEU 271  269  269  LEU LEU B . n 
B 1 272  HIS 272  270  270  HIS HIS B . n 
B 1 273  PRO 273  271  271  PRO PRO B . n 
B 1 274  ARG 274  272  272  ARG ARG B . n 
B 1 275  TYR 275  273  273  TYR TYR B . n 
B 1 276  SER 276  274  274  SER SER B . n 
B 1 277  ARG 277  275  275  ARG ARG B . n 
B 1 278  ALA 278  276  276  ALA ALA B . n 
B 1 279  GLN 279  277  277  GLN GLN B . n 
B 1 280  ALA 280  278  278  ALA ALA B . n 
B 1 281  ALA 281  279  279  ALA ALA B . n 
B 1 282  ARG 282  280  280  ARG ARG B . n 
B 1 283  VAL 283  281  281  VAL VAL B . n 
B 1 284  MET 284  282  282  MET MET B . n 
B 1 285  GLY 285  283  283  GLY GLY B . n 
B 1 286  GLU 286  284  284  GLU GLU B . n 
B 1 287  LEU 287  285  285  LEU LEU B . n 
B 1 288  LEU 288  286  286  LEU LEU B . n 
B 1 289  PRO 289  287  287  PRO PRO B . n 
B 1 290  ARG 290  288  288  ARG ARG B . n 
B 1 291  VAL 291  289  289  VAL VAL B . n 
B 1 292  LYS 292  290  290  LYS LYS B . n 
B 1 293  ALA 293  291  291  ALA ALA B . n 
B 1 294  LEU 294  292  292  LEU LEU B . n 
B 1 295  ALA 295  293  293  ALA ALA B . n 
B 1 296  LEU 296  294  294  LEU LEU B . n 
B 1 297  LEU 297  295  295  LEU LEU B . n 
B 1 298  ALA 298  296  296  ALA ALA B . n 
B 1 299  LYS 299  297  297  LYS LYS B . n 
B 1 300  ASN 300  298  298  ASN ASN B . n 
B 1 301  TYR 301  299  299  TYR TYR B . n 
B 1 302  ASP 302  300  300  ASP ASP B . n 
B 1 303  ILE 303  301  301  ILE ILE B . n 
B 1 304  GLY 304  302  302  GLY GLY B . n 
B 1 305  LEU 305  303  303  LEU LEU B . n 
B 1 306  ASN 306  304  304  ASN ASN B . n 
B 1 307  ILE 307  305  305  ILE ILE B . n 
B 1 308  ASP 308  306  306  ASP ASP B . n 
B 1 309  ALA 309  307  307  ALA ALA B . n 
B 1 310  GLU 310  308  308  GLU GLU B . n 
B 1 311  GLU 311  309  309  GLU GLU B . n 
B 1 312  ALA 312  310  310  ALA ALA B . n 
B 1 313  ASP 313  311  311  ASP ASP B . n 
B 1 314  ARG 314  312  312  ARG ARG B . n 
B 1 315  LEU 315  313  313  LEU LEU B . n 
B 1 316  GLU 316  314  314  GLU GLU B . n 
B 1 317  LEU 317  315  315  LEU LEU B . n 
B 1 318  SER 318  316  316  SER SER B . n 
B 1 319  LEU 319  317  317  LEU LEU B . n 
B 1 320  ASP 320  318  318  ASP ASP B . n 
B 1 321  LEU 321  319  319  LEU LEU B . n 
B 1 322  LEU 322  320  320  LEU LEU B . n 
B 1 323  GLU 323  321  321  GLU GLU B . n 
B 1 324  VAL 324  322  322  VAL VAL B . n 
B 1 325  LEU 325  323  323  LEU LEU B . n 
B 1 326  CYS 326  324  324  CYS CYS B . n 
B 1 327  LEU 327  325  325  LEU LEU B . n 
B 1 328  ASP 328  326  326  ASP ASP B . n 
B 1 329  GLY 329  327  327  GLY GLY B . n 
B 1 330  ASP 330  328  328  ASP ASP B . n 
B 1 331  LEU 331  329  329  LEU LEU B . n 
B 1 332  SER 332  330  330  SER SER B . n 
B 1 333  GLY 333  331  331  GLY GLY B . n 
B 1 334  TRP 334  332  332  TRP TRP B . n 
B 1 335  ASN 335  333  333  ASN ASN B . n 
B 1 336  GLY 336  334  334  GLY GLY B . n 
B 1 337  MET 337  335  335  MET MET B . n 
B 1 338  GLY 338  336  336  GLY GLY B . n 
B 1 339  PHE 339  337  337  PHE PHE B . n 
B 1 340  VAL 340  338  338  VAL VAL B . n 
B 1 341  VAL 341  339  339  VAL VAL B . n 
B 1 342  GLN 342  340  340  GLN GLN B . n 
B 1 343  ALA 343  341  341  ALA ALA B . n 
B 1 344  TYR 344  342  342  TYR TYR B . n 
B 1 345  GLY 345  343  343  GLY GLY B . n 
B 1 346  LYS 346  344  344  LYS LYS B . n 
B 1 347  ARG 347  345  345  ARG ARG B . n 
B 1 348  CYS 348  346  346  CYS CYS B . n 
B 1 349  PRO 349  347  347  PRO PRO B . n 
B 1 350  PHE 350  348  348  PHE PHE B . n 
B 1 351  VAL 351  349  349  VAL VAL B . n 
B 1 352  LEU 352  350  350  LEU LEU B . n 
B 1 353  ASP 353  351  351  ASP ASP B . n 
B 1 354  PHE 354  352  352  PHE PHE B . n 
B 1 355  ILE 355  353  353  ILE ILE B . n 
B 1 356  ILE 356  354  354  ILE ILE B . n 
B 1 357  ASP 357  355  355  ASP ASP B . n 
B 1 358  LEU 358  356  356  LEU LEU B . n 
B 1 359  ALA 359  357  357  ALA ALA B . n 
B 1 360  ARG 360  358  358  ARG ARG B . n 
B 1 361  ARG 361  359  359  ARG ARG B . n 
B 1 362  SER 362  360  360  SER SER B . n 
B 1 363  GLY 363  361  361  GLY GLY B . n 
B 1 364  ARG 364  362  362  ARG ARG B . n 
B 1 365  ARG 365  363  363  ARG ARG B . n 
B 1 366  ILE 366  364  364  ILE ILE B . n 
B 1 367  MET 367  365  365  MET MET B . n 
B 1 368  VAL 368  366  366  VAL VAL B . n 
B 1 369  ARG 369  367  367  ARG ARG B . n 
B 1 370  LEU 370  368  368  LEU LEU B . n 
B 1 371  VAL 371  369  369  VAL VAL B . n 
B 1 372  LYS 372  370  370  LYS LYS B . n 
B 1 373  GLY 373  371  371  GLY GLY B . n 
B 1 374  ALA 374  372  372  ALA ALA B . n 
B 1 375  TYR 375  373  373  TYR TYR B . n 
B 1 376  TRP 376  374  374  TRP TRP B . n 
B 1 377  ASP 377  375  375  ASP ASP B . n 
B 1 378  ALA 378  376  376  ALA ALA B . n 
B 1 379  GLU 379  377  377  GLU GLU B . n 
B 1 380  ILE 380  378  378  ILE ILE B . n 
B 1 381  LYS 381  379  379  LYS LYS B . n 
B 1 382  ARG 382  380  380  ARG ARG B . n 
B 1 383  ALA 383  381  381  ALA ALA B . n 
B 1 384  GLN 384  382  382  GLN GLN B . n 
B 1 385  LEU 385  383  383  LEU LEU B . n 
B 1 386  ASP 386  384  384  ASP ASP B . n 
B 1 387  GLY 387  385  385  GLY GLY B . n 
B 1 388  LEU 388  386  386  LEU LEU B . n 
B 1 389  ALA 389  387  387  ALA ALA B . n 
B 1 390  ASP 390  388  388  ASP ASP B . n 
B 1 391  PHE 391  389  389  PHE PHE B . n 
B 1 392  PRO 392  390  390  PRO PRO B . n 
B 1 393  VAL 393  391  391  VAL VAL B . n 
B 1 394  PHE 394  392  392  PHE PHE B . n 
B 1 395  THR 395  393  393  THR THR B . n 
B 1 396  ARG 396  394  394  ARG ARG B . n 
B 1 397  LYS 397  395  395  LYS LYS B . n 
B 1 398  ILE 398  396  396  ILE ILE B . n 
B 1 399  HIS 399  397  397  HIS HIS B . n 
B 1 400  THR 400  398  398  THR THR B . n 
B 1 401  ASP 401  399  399  ASP ASP B . n 
B 1 402  VAL 402  400  400  VAL VAL B . n 
B 1 403  SER 403  401  401  SER SER B . n 
B 1 404  TYR 404  402  402  TYR TYR B . n 
B 1 405  ILE 405  403  403  ILE ILE B . n 
B 1 406  ALA 406  404  404  ALA ALA B . n 
B 1 407  CYS 407  405  405  CYS CYS B . n 
B 1 408  ALA 408  406  406  ALA ALA B . n 
B 1 409  ALA 409  407  407  ALA ALA B . n 
B 1 410  LYS 410  408  408  LYS LYS B . n 
B 1 411  LEU 411  409  409  LEU LEU B . n 
B 1 412  LEU 412  410  410  LEU LEU B . n 
B 1 413  ALA 413  411  411  ALA ALA B . n 
B 1 414  ALA 414  412  412  ALA ALA B . n 
B 1 415  THR 415  413  413  THR THR B . n 
B 1 416  ASP 416  414  414  ASP ASP B . n 
B 1 417  VAL 417  415  415  VAL VAL B . n 
B 1 418  VAL 418  416  416  VAL VAL B . n 
B 1 419  PHE 419  417  417  PHE PHE B . n 
B 1 420  PRO 420  418  418  PRO PRO B . n 
B 1 421  GLN 421  419  419  GLN GLN B . n 
B 1 422  PHE 422  420  420  PHE PHE B . n 
B 1 423  ALA 423  421  421  ALA ALA B . n 
B 1 424  THR 424  422  422  THR THR B . n 
B 1 425  HIS 425  423  423  HIS HIS B . n 
B 1 426  ASN 426  424  424  ASN ASN B . n 
B 1 427  ALA 427  425  425  ALA ALA B . n 
B 1 428  GLN 428  426  426  GLN GLN B . n 
B 1 429  THR 429  427  427  THR THR B . n 
B 1 430  LEU 430  428  428  LEU LEU B . n 
B 1 431  ALA 431  429  429  ALA ALA B . n 
B 1 432  ALA 432  430  430  ALA ALA B . n 
B 1 433  ILE 433  431  431  ILE ILE B . n 
B 1 434  TYR 434  432  432  TYR TYR B . n 
B 1 435  HIS 435  433  433  HIS HIS B . n 
B 1 436  MET 436  434  434  MET MET B . n 
B 1 437  ALA 437  435  435  ALA ALA B . n 
B 1 438  GLY 438  436  ?    ?   ?   B . n 
B 1 439  LYS 439  437  ?    ?   ?   B . n 
B 1 440  ASP 440  438  ?    ?   ?   B . n 
B 1 441  PHE 441  439  439  PHE PHE B . n 
B 1 442  HIS 442  440  440  HIS HIS B . n 
B 1 443  VAL 443  441  441  VAL VAL B . n 
B 1 444  GLY 444  442  442  GLY GLY B . n 
B 1 445  LYS 445  443  443  LYS LYS B . n 
B 1 446  TYR 446  444  444  TYR TYR B . n 
B 1 447  GLU 447  445  445  GLU GLU B . n 
B 1 448  PHE 448  446  446  PHE PHE B . n 
B 1 449  GLN 449  447  447  GLN GLN B . n 
B 1 450  CYS 450  448  448  CYS CYS B . n 
B 1 451  LEU 451  449  449  LEU LEU B . n 
B 1 452  HIS 452  450  450  HIS HIS B . n 
B 1 453  GLY 453  451  451  GLY GLY B . n 
B 1 454  MET 454  452  452  MET MET B . n 
B 1 455  GLY 455  453  453  GLY GLY B . n 
B 1 456  GLU 456  454  454  GLU GLU B . n 
B 1 457  PRO 457  455  455  PRO PRO B . n 
B 1 458  LEU 458  456  456  LEU LEU B . n 
B 1 459  TYR 459  457  457  TYR TYR B . n 
B 1 460  GLU 460  458  458  GLU GLU B . n 
B 1 461  GLU 461  459  459  GLU GLU B . n 
B 1 462  VAL 462  460  460  VAL VAL B . n 
B 1 463  VAL 463  461  461  VAL VAL B . n 
B 1 464  GLY 464  462  462  GLY GLY B . n 
B 1 465  ARG 465  463  463  ARG ARG B . n 
B 1 466  GLY 466  464  464  GLY GLY B . n 
B 1 467  LYS 467  465  465  LYS LYS B . n 
B 1 468  LEU 468  466  466  LEU LEU B . n 
B 1 469  ASP 469  467  467  ASP ASP B . n 
B 1 470  ARG 470  468  468  ARG ARG B . n 
B 1 471  PRO 471  469  469  PRO PRO B . n 
B 1 472  CYS 472  470  470  CYS CYS B . n 
B 1 473  ARG 473  471  471  ARG ARG B . n 
B 1 474  ILE 474  472  472  ILE ILE B . n 
B 1 475  TYR 475  473  473  TYR TYR B . n 
B 1 476  ALA 476  474  474  ALA ALA B . n 
B 1 477  PRO 477  475  475  PRO PRO B . n 
B 1 478  VAL 478  476  476  VAL VAL B . n 
B 1 479  GLY 479  477  477  GLY GLY B . n 
B 1 480  THR 480  478  478  THR THR B . n 
B 1 481  HIS 481  479  479  HIS HIS B . n 
B 1 482  GLU 482  480  480  GLU GLU B . n 
B 1 483  THR 483  481  481  THR THR B . n 
B 1 484  LEU 484  482  482  LEU LEU B . n 
B 1 485  LEU 485  483  483  LEU LEU B . n 
B 1 486  ALA 486  484  484  ALA ALA B . n 
B 1 487  TYR 487  485  485  TYR TYR B . n 
B 1 488  LEU 488  486  486  LEU LEU B . n 
B 1 489  VAL 489  487  487  VAL VAL B . n 
B 1 490  ARG 490  488  488  ARG ARG B . n 
B 1 491  ARG 491  489  489  ARG ARG B . n 
B 1 492  LEU 492  490  490  LEU LEU B . n 
B 1 493  LEU 493  491  491  LEU LEU B . n 
B 1 494  GLU 494  492  492  GLU GLU B . n 
B 1 495  ASN 495  493  493  ASN ASN B . n 
B 1 496  GLY 496  494  494  GLY GLY B . n 
B 1 497  ALA 497  495  495  ALA ALA B . n 
B 1 498  ASN 498  496  496  ASN ASN B . n 
B 1 499  SER 499  497  497  SER SER B . n 
B 1 500  SER 500  498  498  SER SER B . n 
B 1 501  PHE 501  499  499  PHE PHE B . n 
B 1 502  VAL 502  500  500  VAL VAL B . n 
B 1 503  HIS 503  501  501  HIS HIS B . n 
B 1 504  ARG 504  502  502  ARG ARG B . n 
B 1 505  ILE 505  503  503  ILE ILE B . n 
B 1 506  ASN 506  504  504  ASN ASN B . n 
B 1 507  ASP 507  505  505  ASP ASP B . n 
B 1 508  PRO 508  506  506  PRO PRO B . n 
B 1 509  LYS 509  507  507  LYS LYS B . n 
B 1 510  VAL 510  508  508  VAL VAL B . n 
B 1 511  SER 511  509  509  SER SER B . n 
B 1 512  ILE 512  510  510  ILE ILE B . n 
B 1 513  ASP 513  511  511  ASP ASP B . n 
B 1 514  GLU 514  512  512  GLU GLU B . n 
B 1 515  LEU 515  513  513  LEU LEU B . n 
B 1 516  ILE 516  514  514  ILE ILE B . n 
B 1 517  ALA 517  515  515  ALA ALA B . n 
B 1 518  ASP 518  516  516  ASP ASP B . n 
B 1 519  PRO 519  517  517  PRO PRO B . n 
B 1 520  VAL 520  518  518  VAL VAL B . n 
B 1 521  GLU 521  519  519  GLU GLU B . n 
B 1 522  VAL 522  520  520  VAL VAL B . n 
B 1 523  VAL 523  521  521  VAL VAL B . n 
B 1 524  ARG 524  522  522  ARG ARG B . n 
B 1 525  ALA 525  523  523  ALA ALA B . n 
B 1 526  MET 526  524  524  MET MET B . n 
B 1 527  PRO 527  525  525  PRO PRO B . n 
B 1 528  VAL 528  526  526  VAL VAL B . n 
B 1 529  VAL 529  527  527  VAL VAL B . n 
B 1 530  GLY 530  528  528  GLY GLY B . n 
B 1 531  ALA 531  529  529  ALA ALA B . n 
B 1 532  LYS 532  530  530  LYS LYS B . n 
B 1 533  HIS 533  531  531  HIS HIS B . n 
B 1 534  ASP 534  532  532  ASP ASP B . n 
B 1 535  ARG 535  533  533  ARG ARG B . n 
B 1 536  ILE 536  534  534  ILE ILE B . n 
B 1 537  ALA 537  535  535  ALA ALA B . n 
B 1 538  LEU 538  536  536  LEU LEU B . n 
B 1 539  PRO 539  537  537  PRO PRO B . n 
B 1 540  ALA 540  538  538  ALA ALA B . n 
B 1 541  GLU 541  539  539  GLU GLU B . n 
B 1 542  LEU 542  540  540  LEU LEU B . n 
B 1 543  PHE 543  541  541  PHE PHE B . n 
B 1 544  GLY 544  542  542  GLY GLY B . n 
B 1 545  ASP 545  543  543  ASP ASP B . n 
B 1 546  ALA 546  544  544  ALA ALA B . n 
B 1 547  ARG 547  545  545  ARG ARG B . n 
B 1 548  THR 548  546  546  THR THR B . n 
B 1 549  ASN 549  547  547  ASN ASN B . n 
B 1 550  SER 550  548  548  SER SER B . n 
B 1 551  ALA 551  549  549  ALA ALA B . n 
B 1 552  GLY 552  550  550  GLY GLY B . n 
B 1 553  LEU 553  551  551  LEU LEU B . n 
B 1 554  ASP 554  552  552  ASP ASP B . n 
B 1 555  LEU 555  553  553  LEU LEU B . n 
B 1 556  SER 556  554  554  SER SER B . n 
B 1 557  ASN 557  555  555  ASN ASN B . n 
B 1 558  GLU 558  556  556  GLU GLU B . n 
B 1 559  GLU 559  557  557  GLU GLU B . n 
B 1 560  THR 560  558  558  THR THR B . n 
B 1 561  LEU 561  559  559  LEU LEU B . n 
B 1 562  ALA 562  560  560  ALA ALA B . n 
B 1 563  SER 563  561  561  SER SER B . n 
B 1 564  LEU 564  562  562  LEU LEU B . n 
B 1 565  THR 565  563  563  THR THR B . n 
B 1 566  GLU 566  564  564  GLU GLU B . n 
B 1 567  ALA 567  565  565  ALA ALA B . n 
B 1 568  LEU 568  566  566  LEU LEU B . n 
B 1 569  ARG 569  567  567  ARG ARG B . n 
B 1 570  GLU 570  568  568  GLU GLU B . n 
B 1 571  SER 571  569  569  SER SER B . n 
B 1 572  ALA 572  570  570  ALA ALA B . n 
B 1 573  ALA 573  571  571  ALA ALA B . n 
B 1 574  MET 574  572  572  MET MET B . n 
B 1 575  LYS 575  573  573  LYS LYS B . n 
B 1 576  TRP 576  574  574  TRP TRP B . n 
B 1 577  THR 577  575  575  THR THR B . n 
B 1 578  ALA 578  576  576  ALA ALA B . n 
B 1 579  LEU 579  577  577  LEU LEU B . n 
B 1 580  PRO 580  578  578  PRO PRO B . n 
B 1 581  GLN 581  579  579  GLN GLN B . n 
B 1 582  LEU 582  580  580  LEU LEU B . n 
B 1 583  ALA 583  581  581  ALA ALA B . n 
B 1 584  THR 584  582  582  THR THR B . n 
B 1 585  GLY 585  583  583  GLY GLY B . n 
B 1 586  PRO 586  584  584  PRO PRO B . n 
B 1 587  ALA 587  585  585  ALA ALA B . n 
B 1 588  ALA 588  586  586  ALA ALA B . n 
B 1 589  GLY 589  587  587  GLY GLY B . n 
B 1 590  GLU 590  588  588  GLU GLU B . n 
B 1 591  THR 591  589  589  THR THR B . n 
B 1 592  ARG 592  590  590  ARG ARG B . n 
B 1 593  THR 593  591  591  THR THR B . n 
B 1 594  VAL 594  592  592  VAL VAL B . n 
B 1 595  LEU 595  593  593  LEU LEU B . n 
B 1 596  ASN 596  594  594  ASN ASN B . n 
B 1 597  PRO 597  595  595  PRO PRO B . n 
B 1 598  GLY 598  596  596  GLY GLY B . n 
B 1 599  ASP 599  597  597  ASP ASP B . n 
B 1 600  HIS 600  598  598  HIS HIS B . n 
B 1 601  ARG 601  599  599  ARG ARG B . n 
B 1 602  ASP 602  600  600  ASP ASP B . n 
B 1 603  VAL 603  601  601  VAL VAL B . n 
B 1 604  VAL 604  602  602  VAL VAL B . n 
B 1 605  GLY 605  603  603  GLY GLY B . n 
B 1 606  SER 606  604  604  SER SER B . n 
B 1 607  VAL 607  605  605  VAL VAL B . n 
B 1 608  THR 608  606  606  THR THR B . n 
B 1 609  GLU 609  607  607  GLU GLU B . n 
B 1 610  THR 610  608  608  THR THR B . n 
B 1 611  SER 611  609  609  SER SER B . n 
B 1 612  GLU 612  610  610  GLU GLU B . n 
B 1 613  GLU 613  611  611  GLU GLU B . n 
B 1 614  ASP 614  612  612  ASP ASP B . n 
B 1 615  ALA 615  613  613  ALA ALA B . n 
B 1 616  ARG 616  614  614  ARG ARG B . n 
B 1 617  ARG 617  615  615  ARG ARG B . n 
B 1 618  ALA 618  616  616  ALA ALA B . n 
B 1 619  VAL 619  617  617  VAL VAL B . n 
B 1 620  ARG 620  618  618  ARG ARG B . n 
B 1 621  LEU 621  619  619  LEU LEU B . n 
B 1 622  ALA 622  620  620  ALA ALA B . n 
B 1 623  ALA 623  621  621  ALA ALA B . n 
B 1 624  ASP 624  622  622  ASP ASP B . n 
B 1 625  ALA 625  623  623  ALA ALA B . n 
B 1 626  ALA 626  624  624  ALA ALA B . n 
B 1 627  PRO 627  625  625  PRO PRO B . n 
B 1 628  ASP 628  626  626  ASP ASP B . n 
B 1 629  TRP 629  627  627  TRP TRP B . n 
B 1 630  ALA 630  628  628  ALA ALA B . n 
B 1 631  ALA 631  629  629  ALA ALA B . n 
B 1 632  VAL 632  630  630  VAL VAL B . n 
B 1 633  PRO 633  631  631  PRO PRO B . n 
B 1 634  PRO 634  632  632  PRO PRO B . n 
B 1 635  SER 635  633  633  SER SER B . n 
B 1 636  GLU 636  634  634  GLU GLU B . n 
B 1 637  ARG 637  635  635  ARG ARG B . n 
B 1 638  ALA 638  636  636  ALA ALA B . n 
B 1 639  ALA 639  637  637  ALA ALA B . n 
B 1 640  CYS 640  638  638  CYS CYS B . n 
B 1 641  LEU 641  639  639  LEU LEU B . n 
B 1 642  ASP 642  640  640  ASP ASP B . n 
B 1 643  ARG 643  641  641  ARG ARG B . n 
B 1 644  ALA 644  642  642  ALA ALA B . n 
B 1 645  ALA 645  643  643  ALA ALA B . n 
B 1 646  GLU 646  644  644  GLU GLU B . n 
B 1 647  LEU 647  645  645  LEU LEU B . n 
B 1 648  MET 648  646  646  MET MET B . n 
B 1 649  GLN 649  647  647  GLN GLN B . n 
B 1 650  ALA 650  648  648  ALA ALA B . n 
B 1 651  ARG 651  649  649  ARG ARG B . n 
B 1 652  MET 652  650  650  MET MET B . n 
B 1 653  PRO 653  651  651  PRO PRO B . n 
B 1 654  THR 654  652  652  THR THR B . n 
B 1 655  LEU 655  653  653  LEU LEU B . n 
B 1 656  LEU 656  654  654  LEU LEU B . n 
B 1 657  GLY 657  655  655  GLY GLY B . n 
B 1 658  LEU 658  656  656  LEU LEU B . n 
B 1 659  ILE 659  657  657  ILE ILE B . n 
B 1 660  ILE 660  658  658  ILE ILE B . n 
B 1 661  ARG 661  659  659  ARG ARG B . n 
B 1 662  GLU 662  660  660  GLU GLU B . n 
B 1 663  ALA 663  661  661  ALA ALA B . n 
B 1 664  GLY 664  662  662  GLY GLY B . n 
B 1 665  LYS 665  663  663  LYS LYS B . n 
B 1 666  SER 666  664  664  SER SER B . n 
B 1 667  ALA 667  665  665  ALA ALA B . n 
B 1 668  LEU 668  666  666  LEU LEU B . n 
B 1 669  ASN 669  667  667  ASN ASN B . n 
B 1 670  ALA 670  668  668  ALA ALA B . n 
B 1 671  ILE 671  669  669  ILE ILE B . n 
B 1 672  ALA 672  670  670  ALA ALA B . n 
B 1 673  GLU 673  671  671  GLU GLU B . n 
B 1 674  VAL 674  672  672  VAL VAL B . n 
B 1 675  ARG 675  673  673  ARG ARG B . n 
B 1 676  GLU 676  674  674  GLU GLU B . n 
B 1 677  ALA 677  675  675  ALA ALA B . n 
B 1 678  ILE 678  676  676  ILE ILE B . n 
B 1 679  ASP 679  677  677  ASP ASP B . n 
B 1 680  PHE 680  678  678  PHE PHE B . n 
B 1 681  LEU 681  679  679  LEU LEU B . n 
B 1 682  ARG 682  680  680  ARG ARG B . n 
B 1 683  TYR 683  681  681  TYR TYR B . n 
B 1 684  TYR 684  682  682  TYR TYR B . n 
B 1 685  ALA 685  683  683  ALA ALA B . n 
B 1 686  GLU 686  684  684  GLU GLU B . n 
B 1 687  GLN 687  685  685  GLN GLN B . n 
B 1 688  THR 688  686  686  THR THR B . n 
B 1 689  ARG 689  687  687  ARG ARG B . n 
B 1 690  ARG 690  688  688  ARG ARG B . n 
B 1 691  THR 691  689  689  THR THR B . n 
B 1 692  LEU 692  690  690  LEU LEU B . n 
B 1 693  GLY 693  691  691  GLY GLY B . n 
B 1 694  PRO 694  692  692  PRO PRO B . n 
B 1 695  GLY 695  693  693  GLY GLY B . n 
B 1 696  HIS 696  694  694  HIS HIS B . n 
B 1 697  GLY 697  695  695  GLY GLY B . n 
B 1 698  PRO 698  696  696  PRO PRO B . n 
B 1 699  LEU 699  697  697  LEU LEU B . n 
B 1 700  GLY 700  698  698  GLY GLY B . n 
B 1 701  PRO 701  699  699  PRO PRO B . n 
B 1 702  ILE 702  700  700  ILE ILE B . n 
B 1 703  VAL 703  701  701  VAL VAL B . n 
B 1 704  CYS 704  702  702  CYS CYS B . n 
B 1 705  ILE 705  703  703  ILE ILE B . n 
B 1 706  SER 706  704  704  SER SER B . n 
B 1 707  PRO 707  705  705  PRO PRO B . n 
B 1 708  TRP 708  706  706  TRP TRP B . n 
B 1 709  ASN 709  707  707  ASN ASN B . n 
B 1 710  PHE 710  708  708  PHE PHE B . n 
B 1 711  PRO 711  709  709  PRO PRO B . n 
B 1 712  LEU 712  710  710  LEU LEU B . n 
B 1 713  ALA 713  711  711  ALA ALA B . n 
B 1 714  ILE 714  712  712  ILE ILE B . n 
B 1 715  PHE 715  713  713  PHE PHE B . n 
B 1 716  THR 716  714  714  THR THR B . n 
B 1 717  GLY 717  715  715  GLY GLY B . n 
B 1 718  GLN 718  716  716  GLN GLN B . n 
B 1 719  ILE 719  717  717  ILE ILE B . n 
B 1 720  ALA 720  718  718  ALA ALA B . n 
B 1 721  ALA 721  719  719  ALA ALA B . n 
B 1 722  ALA 722  720  720  ALA ALA B . n 
B 1 723  LEU 723  721  721  LEU LEU B . n 
B 1 724  VAL 724  722  722  VAL VAL B . n 
B 1 725  ALA 725  723  723  ALA ALA B . n 
B 1 726  GLY 726  724  724  GLY GLY B . n 
B 1 727  ASN 727  725  725  ASN ASN B . n 
B 1 728  PRO 728  726  726  PRO PRO B . n 
B 1 729  VAL 729  727  727  VAL VAL B . n 
B 1 730  LEU 730  728  728  LEU LEU B . n 
B 1 731  ALA 731  729  729  ALA ALA B . n 
B 1 732  LYS 732  730  730  LYS LYS B . n 
B 1 733  PRO 733  731  731  PRO PRO B . n 
B 1 734  ALA 734  732  732  ALA ALA B . n 
B 1 735  GLU 735  733  733  GLU GLU B . n 
B 1 736  GLU 736  734  734  GLU GLU B . n 
B 1 737  THR 737  735  735  THR THR B . n 
B 1 738  PRO 738  736  736  PRO PRO B . n 
B 1 739  LEU 739  737  737  LEU LEU B . n 
B 1 740  ILE 740  738  738  ILE ILE B . n 
B 1 741  ALA 741  739  739  ALA ALA B . n 
B 1 742  ALA 742  740  740  ALA ALA B . n 
B 1 743  GLU 743  741  741  GLU GLU B . n 
B 1 744  GLY 744  742  742  GLY GLY B . n 
B 1 745  VAL 745  743  743  VAL VAL B . n 
B 1 746  ARG 746  744  744  ARG ARG B . n 
B 1 747  ILE 747  745  745  ILE ILE B . n 
B 1 748  LEU 748  746  746  LEU LEU B . n 
B 1 749  ARG 749  747  747  ARG ARG B . n 
B 1 750  GLU 750  748  748  GLU GLU B . n 
B 1 751  ALA 751  749  749  ALA ALA B . n 
B 1 752  GLY 752  750  750  GLY GLY B . n 
B 1 753  ILE 753  751  751  ILE ILE B . n 
B 1 754  PRO 754  752  752  PRO PRO B . n 
B 1 755  ALA 755  753  753  ALA ALA B . n 
B 1 756  SER 756  754  754  SER SER B . n 
B 1 757  ALA 757  755  755  ALA ALA B . n 
B 1 758  LEU 758  756  756  LEU LEU B . n 
B 1 759  GLN 759  757  757  GLN GLN B . n 
B 1 760  LEU 760  758  758  LEU LEU B . n 
B 1 761  LEU 761  759  759  LEU LEU B . n 
B 1 762  PRO 762  760  760  PRO PRO B . n 
B 1 763  GLY 763  761  761  GLY GLY B . n 
B 1 764  ASP 764  762  762  ASP ASP B . n 
B 1 765  GLY 765  763  763  GLY GLY B . n 
B 1 766  ARG 766  764  764  ARG ARG B . n 
B 1 767  VAL 767  765  765  VAL VAL B . n 
B 1 768  GLY 768  766  766  GLY GLY B . n 
B 1 769  ALA 769  767  767  ALA ALA B . n 
B 1 770  ALA 770  768  768  ALA ALA B . n 
B 1 771  LEU 771  769  769  LEU LEU B . n 
B 1 772  VAL 772  770  770  VAL VAL B . n 
B 1 773  ALA 773  771  771  ALA ALA B . n 
B 1 774  ALA 774  772  772  ALA ALA B . n 
B 1 775  ALA 775  773  773  ALA ALA B . n 
B 1 776  GLU 776  774  774  GLU GLU B . n 
B 1 777  THR 777  775  775  THR THR B . n 
B 1 778  ALA 778  776  776  ALA ALA B . n 
B 1 779  GLY 779  777  777  GLY GLY B . n 
B 1 780  VAL 780  778  778  VAL VAL B . n 
B 1 781  MET 781  779  779  MET MET B . n 
B 1 782  PHE 782  780  780  PHE PHE B . n 
B 1 783  THR 783  781  781  THR THR B . n 
B 1 784  GLY 784  782  782  GLY GLY B . n 
B 1 785  SER 785  783  783  SER SER B . n 
B 1 786  THR 786  784  784  THR THR B . n 
B 1 787  GLU 787  785  785  GLU GLU B . n 
B 1 788  VAL 788  786  786  VAL VAL B . n 
B 1 789  ALA 789  787  787  ALA ALA B . n 
B 1 790  ARG 790  788  788  ARG ARG B . n 
B 1 791  LEU 791  789  789  LEU LEU B . n 
B 1 792  ILE 792  790  790  ILE ILE B . n 
B 1 793  GLN 793  791  791  GLN GLN B . n 
B 1 794  ALA 794  792  792  ALA ALA B . n 
B 1 795  GLN 795  793  793  GLN GLN B . n 
B 1 796  LEU 796  794  794  LEU LEU B . n 
B 1 797  ALA 797  795  795  ALA ALA B . n 
B 1 798  ASP 798  796  796  ASP ASP B . n 
B 1 799  ARG 799  797  797  ARG ARG B . n 
B 1 800  LEU 800  798  798  LEU LEU B . n 
B 1 801  SER 801  799  799  SER SER B . n 
B 1 802  PRO 802  800  800  PRO PRO B . n 
B 1 803  ALA 803  801  801  ALA ALA B . n 
B 1 804  GLY 804  802  802  GLY GLY B . n 
B 1 805  ARG 805  803  803  ARG ARG B . n 
B 1 806  PRO 806  804  804  PRO PRO B . n 
B 1 807  ILE 807  805  805  ILE ILE B . n 
B 1 808  PRO 808  806  806  PRO PRO B . n 
B 1 809  LEU 809  807  807  LEU LEU B . n 
B 1 810  ILE 810  808  808  ILE ILE B . n 
B 1 811  ALA 811  809  809  ALA ALA B . n 
B 1 812  GLU 812  810  810  GLU GLU B . n 
B 1 813  THR 813  811  811  THR THR B . n 
B 1 814  GLY 814  812  812  GLY GLY B . n 
B 1 815  GLY 815  813  813  GLY GLY B . n 
B 1 816  GLN 816  814  814  GLN GLN B . n 
B 1 817  ASN 817  815  815  ASN ASN B . n 
B 1 818  ALA 818  816  816  ALA ALA B . n 
B 1 819  MET 819  817  817  MET MET B . n 
B 1 820  ILE 820  818  818  ILE ILE B . n 
B 1 821  VAL 821  819  819  VAL VAL B . n 
B 1 822  ASP 822  820  820  ASP ASP B . n 
B 1 823  SER 823  821  821  SER SER B . n 
B 1 824  SER 824  822  822  SER SER B . n 
B 1 825  ALA 825  823  823  ALA ALA B . n 
B 1 826  LEU 826  824  824  LEU LEU B . n 
B 1 827  ALA 827  825  825  ALA ALA B . n 
B 1 828  GLU 828  826  826  GLU GLU B . n 
B 1 829  GLN 829  827  827  GLN GLN B . n 
B 1 830  VAL 830  828  828  VAL VAL B . n 
B 1 831  VAL 831  829  829  VAL VAL B . n 
B 1 832  GLY 832  830  830  GLY GLY B . n 
B 1 833  ASP 833  831  831  ASP ASP B . n 
B 1 834  VAL 834  832  832  VAL VAL B . n 
B 1 835  ILE 835  833  833  ILE ILE B . n 
B 1 836  THR 836  834  834  THR THR B . n 
B 1 837  SER 837  835  835  SER SER B . n 
B 1 838  ALA 838  836  836  ALA ALA B . n 
B 1 839  PHE 839  837  837  PHE PHE B . n 
B 1 840  ASP 840  838  838  ASP ASP B . n 
B 1 841  SER 841  839  839  SER SER B . n 
B 1 842  ALA 842  840  840  ALA ALA B . n 
B 1 843  GLY 843  841  841  GLY GLY B . n 
B 1 844  GLN 844  842  842  GLN GLN B . n 
B 1 845  ARG 845  843  843  ARG ARG B . n 
B 1 846  CYS 846  844  844  CYS CYS B . n 
B 1 847  SER 847  845  845  SER SER B . n 
B 1 848  ALA 848  846  846  ALA ALA B . n 
B 1 849  LEU 849  847  847  LEU LEU B . n 
B 1 850  ARG 850  848  848  ARG ARG B . n 
B 1 851  VAL 851  849  849  VAL VAL B . n 
B 1 852  LEU 852  850  850  LEU LEU B . n 
B 1 853  CYS 853  851  851  CYS CYS B . n 
B 1 854  LEU 854  852  852  LEU LEU B . n 
B 1 855  GLN 855  853  853  GLN GLN B . n 
B 1 856  GLU 856  854  854  GLU GLU B . n 
B 1 857  ASP 857  855  855  ASP ASP B . n 
B 1 858  VAL 858  856  856  VAL VAL B . n 
B 1 859  ALA 859  857  857  ALA ALA B . n 
B 1 860  ASP 860  858  858  ASP ASP B . n 
B 1 861  ARG 861  859  859  ARG ARG B . n 
B 1 862  ILE 862  860  860  ILE ILE B . n 
B 1 863  LEU 863  861  861  LEU LEU B . n 
B 1 864  THR 864  862  862  THR THR B . n 
B 1 865  MET 865  863  863  MET MET B . n 
B 1 866  LEU 866  864  864  LEU LEU B . n 
B 1 867  LYS 867  865  865  LYS LYS B . n 
B 1 868  GLY 868  866  866  GLY GLY B . n 
B 1 869  ALA 869  867  867  ALA ALA B . n 
B 1 870  LEU 870  868  868  LEU LEU B . n 
B 1 871  HIS 871  869  869  HIS HIS B . n 
B 1 872  GLU 872  870  870  GLU GLU B . n 
B 1 873  LEU 873  871  871  LEU LEU B . n 
B 1 874  HIS 874  872  872  HIS HIS B . n 
B 1 875  ILE 875  873  873  ILE ILE B . n 
B 1 876  GLY 876  874  874  GLY GLY B . n 
B 1 877  ARG 877  875  875  ARG ARG B . n 
B 1 878  THR 878  876  876  THR THR B . n 
B 1 879  ASP 879  877  877  ASP ASP B . n 
B 1 880  ARG 880  878  878  ARG ARG B . n 
B 1 881  LEU 881  879  879  LEU LEU B . n 
B 1 882  SER 882  880  880  SER SER B . n 
B 1 883  VAL 883  881  881  VAL VAL B . n 
B 1 884  ASP 884  882  882  ASP ASP B . n 
B 1 885  VAL 885  883  883  VAL VAL B . n 
B 1 886  GLY 886  884  884  GLY GLY B . n 
B 1 887  PRO 887  885  885  PRO PRO B . n 
B 1 888  VAL 888  886  886  VAL VAL B . n 
B 1 889  ILE 889  887  887  ILE ILE B . n 
B 1 890  THR 890  888  888  THR THR B . n 
B 1 891  SER 891  889  889  SER SER B . n 
B 1 892  GLU 892  890  890  GLU GLU B . n 
B 1 893  ALA 893  891  891  ALA ALA B . n 
B 1 894  LYS 894  892  892  LYS LYS B . n 
B 1 895  ASP 895  893  893  ASP ASP B . n 
B 1 896  ASN 896  894  894  ASN ASN B . n 
B 1 897  ILE 897  895  895  ILE ILE B . n 
B 1 898  GLU 898  896  896  GLU GLU B . n 
B 1 899  LYS 899  897  897  LYS LYS B . n 
B 1 900  HIS 900  898  898  HIS HIS B . n 
B 1 901  ILE 901  899  899  ILE ILE B . n 
B 1 902  GLU 902  900  900  GLU GLU B . n 
B 1 903  ARG 903  901  901  ARG ARG B . n 
B 1 904  MET 904  902  902  MET MET B . n 
B 1 905  ARG 905  903  903  ARG ARG B . n 
B 1 906  GLY 906  904  904  GLY GLY B . n 
B 1 907  LEU 907  905  905  LEU LEU B . n 
B 1 908  GLY 908  906  906  GLY GLY B . n 
B 1 909  ARG 909  907  907  ARG ARG B . n 
B 1 910  LYS 910  908  908  LYS LYS B . n 
B 1 911  VAL 911  909  909  VAL VAL B . n 
B 1 912  GLU 912  910  910  GLU GLU B . n 
B 1 913  GLN 913  911  911  GLN GLN B . n 
B 1 914  ILE 914  912  912  ILE ILE B . n 
B 1 915  GLY 915  913  913  GLY GLY B . n 
B 1 916  LEU 916  914  914  LEU LEU B . n 
B 1 917  ALA 917  915  915  ALA ALA B . n 
B 1 918  SER 918  916  916  SER SER B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 1222 ALA ALA B . n 
B 1 1225 ALA 1225 1223 ?    ?   ?   B . n 
B 1 1226 GLY 1226 1224 ?    ?   ?   B . n 
B 1 1227 GLY 1227 1225 ?    ?   ?   B . n 
B 1 1228 ASN 1228 1226 ?    ?   ?   B . n 
B 1 1229 ALA 1229 1227 ?    ?   ?   B . n 
B 1 1230 SER 1230 1228 ?    ?   ?   B . n 
B 1 1231 LEU 1231 1229 ?    ?   ?   B . n 
B 1 1232 MET 1232 1230 ?    ?   ?   B . n 
B 1 1233 ALA 1233 1231 ?    ?   ?   B . n 
B 1 1234 ILE 1234 1232 ?    ?   ?   B . n 
B 1 1235 GLY 1235 1233 ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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  P5F 1   1301 1301 P5F FDA A . 
D 3  NAD 1   1302 1302 NAD NAD A . 
E 4  SO4 1   1303 2    SO4 SO4 A . 
F 4  SO4 1   1304 3    SO4 SO4 A . 
G 4  SO4 1   1305 4    SO4 SO4 A . 
H 4  SO4 1   1306 6    SO4 SO4 A . 
I 4  SO4 1   1307 7    SO4 SO4 A . 
J 5  MG  1   1308 1    MG  MG  A . 
K 6  FMT 1   1309 2002 FMT FMT A . 
L 7  PEG 1   1310 2    PEG PEG A . 
M 7  PEG 1   1311 4    PEG PEG A . 
N 2  P5F 1   1301 1301 P5F FDA B . 
O 3  NAD 1   1302 1302 NAD NAD B . 
P 4  SO4 1   1303 1    SO4 SO4 B . 
Q 4  SO4 1   1304 5    SO4 SO4 B . 
R 5  MG  1   1305 2    MG  MG  B . 
S 6  FMT 1   1306 2003 FMT FMT B . 
T 7  PEG 1   1307 3    PEG PEG B . 
U 8  PG4 1   1308 5    PG4 PG4 B . 
V 9  PGE 1   1309 6    PGE PGE B . 
W 10 HOH 1   1401 237  HOH HOH A . 
W 10 HOH 2   1402 1381 HOH HOH A . 
W 10 HOH 3   1403 851  HOH HOH A . 
W 10 HOH 4   1404 975  HOH HOH A . 
W 10 HOH 5   1405 595  HOH HOH A . 
W 10 HOH 6   1406 648  HOH HOH A . 
W 10 HOH 7   1407 1295 HOH HOH A . 
W 10 HOH 8   1408 1068 HOH HOH A . 
W 10 HOH 9   1409 791  HOH HOH A . 
W 10 HOH 10  1410 982  HOH HOH A . 
W 10 HOH 11  1411 492  HOH HOH A . 
W 10 HOH 12  1412 450  HOH HOH A . 
W 10 HOH 13  1413 779  HOH HOH A . 
W 10 HOH 14  1414 559  HOH HOH A . 
W 10 HOH 15  1415 1064 HOH HOH A . 
W 10 HOH 16  1416 888  HOH HOH A . 
W 10 HOH 17  1417 1172 HOH HOH A . 
W 10 HOH 18  1418 873  HOH HOH A . 
W 10 HOH 19  1419 1161 HOH HOH A . 
W 10 HOH 20  1420 898  HOH HOH A . 
W 10 HOH 21  1421 1219 HOH HOH A . 
W 10 HOH 22  1422 1347 HOH HOH A . 
W 10 HOH 23  1423 141  HOH HOH A . 
W 10 HOH 24  1424 767  HOH HOH A . 
W 10 HOH 25  1425 252  HOH HOH A . 
W 10 HOH 26  1426 404  HOH HOH A . 
W 10 HOH 27  1427 1392 HOH HOH A . 
W 10 HOH 28  1428 1317 HOH HOH A . 
W 10 HOH 29  1429 905  HOH HOH A . 
W 10 HOH 30  1430 1145 HOH HOH A . 
W 10 HOH 31  1431 1131 HOH HOH A . 
W 10 HOH 32  1432 321  HOH HOH A . 
W 10 HOH 33  1433 1185 HOH HOH A . 
W 10 HOH 34  1434 765  HOH HOH A . 
W 10 HOH 35  1435 1081 HOH HOH A . 
W 10 HOH 36  1436 832  HOH HOH A . 
W 10 HOH 37  1437 980  HOH HOH A . 
W 10 HOH 38  1438 385  HOH HOH A . 
W 10 HOH 39  1439 323  HOH HOH A . 
W 10 HOH 40  1440 152  HOH HOH A . 
W 10 HOH 41  1441 406  HOH HOH A . 
W 10 HOH 42  1442 516  HOH HOH A . 
W 10 HOH 43  1443 35   HOH HOH A . 
W 10 HOH 44  1444 1071 HOH HOH A . 
W 10 HOH 45  1445 673  HOH HOH A . 
W 10 HOH 46  1446 608  HOH HOH A . 
W 10 HOH 47  1447 49   HOH HOH A . 
W 10 HOH 48  1448 452  HOH HOH A . 
W 10 HOH 49  1449 159  HOH HOH A . 
W 10 HOH 50  1450 1339 HOH HOH A . 
W 10 HOH 51  1451 332  HOH HOH A . 
W 10 HOH 52  1452 1105 HOH HOH A . 
W 10 HOH 53  1453 485  HOH HOH A . 
W 10 HOH 54  1454 555  HOH HOH A . 
W 10 HOH 55  1455 1085 HOH HOH A . 
W 10 HOH 56  1456 285  HOH HOH A . 
W 10 HOH 57  1457 1168 HOH HOH A . 
W 10 HOH 58  1458 136  HOH HOH A . 
W 10 HOH 59  1459 122  HOH HOH A . 
W 10 HOH 60  1460 507  HOH HOH A . 
W 10 HOH 61  1461 1045 HOH HOH A . 
W 10 HOH 62  1462 433  HOH HOH A . 
W 10 HOH 63  1463 91   HOH HOH A . 
W 10 HOH 64  1464 315  HOH HOH A . 
W 10 HOH 65  1465 1108 HOH HOH A . 
W 10 HOH 66  1466 371  HOH HOH A . 
W 10 HOH 67  1467 941  HOH HOH A . 
W 10 HOH 68  1468 124  HOH HOH A . 
W 10 HOH 69  1469 384  HOH HOH A . 
W 10 HOH 70  1470 283  HOH HOH A . 
W 10 HOH 71  1471 924  HOH HOH A . 
W 10 HOH 72  1472 967  HOH HOH A . 
W 10 HOH 73  1473 973  HOH HOH A . 
W 10 HOH 74  1474 1008 HOH HOH A . 
W 10 HOH 75  1475 1333 HOH HOH A . 
W 10 HOH 76  1476 637  HOH HOH A . 
W 10 HOH 77  1477 487  HOH HOH A . 
W 10 HOH 78  1478 996  HOH HOH A . 
W 10 HOH 79  1479 373  HOH HOH A . 
W 10 HOH 80  1480 100  HOH HOH A . 
W 10 HOH 81  1481 1078 HOH HOH A . 
W 10 HOH 82  1482 585  HOH HOH A . 
W 10 HOH 83  1483 502  HOH HOH A . 
W 10 HOH 84  1484 137  HOH HOH A . 
W 10 HOH 85  1485 1312 HOH HOH A . 
W 10 HOH 86  1486 1047 HOH HOH A . 
W 10 HOH 87  1487 1379 HOH HOH A . 
W 10 HOH 88  1488 952  HOH HOH A . 
W 10 HOH 89  1489 961  HOH HOH A . 
W 10 HOH 90  1490 144  HOH HOH A . 
W 10 HOH 91  1491 488  HOH HOH A . 
W 10 HOH 92  1492 444  HOH HOH A . 
W 10 HOH 93  1493 177  HOH HOH A . 
W 10 HOH 94  1494 687  HOH HOH A . 
W 10 HOH 95  1495 1135 HOH HOH A . 
W 10 HOH 96  1496 303  HOH HOH A . 
W 10 HOH 97  1497 972  HOH HOH A . 
W 10 HOH 98  1498 130  HOH HOH A . 
W 10 HOH 99  1499 1444 HOH HOH A . 
W 10 HOH 100 1500 721  HOH HOH A . 
W 10 HOH 101 1501 782  HOH HOH A . 
W 10 HOH 102 1502 509  HOH HOH A . 
W 10 HOH 103 1503 1241 HOH HOH A . 
W 10 HOH 104 1504 45   HOH HOH A . 
W 10 HOH 105 1505 614  HOH HOH A . 
W 10 HOH 106 1506 1393 HOH HOH A . 
W 10 HOH 107 1507 72   HOH HOH A . 
W 10 HOH 108 1508 1060 HOH HOH A . 
W 10 HOH 109 1509 31   HOH HOH A . 
W 10 HOH 110 1510 279  HOH HOH A . 
W 10 HOH 111 1511 659  HOH HOH A . 
W 10 HOH 112 1512 804  HOH HOH A . 
W 10 HOH 113 1513 263  HOH HOH A . 
W 10 HOH 114 1514 189  HOH HOH A . 
W 10 HOH 115 1515 1116 HOH HOH A . 
W 10 HOH 116 1516 232  HOH HOH A . 
W 10 HOH 117 1517 1189 HOH HOH A . 
W 10 HOH 118 1518 361  HOH HOH A . 
W 10 HOH 119 1519 1036 HOH HOH A . 
W 10 HOH 120 1520 57   HOH HOH A . 
W 10 HOH 121 1521 500  HOH HOH A . 
W 10 HOH 122 1522 129  HOH HOH A . 
W 10 HOH 123 1523 170  HOH HOH A . 
W 10 HOH 124 1524 671  HOH HOH A . 
W 10 HOH 125 1525 840  HOH HOH A . 
W 10 HOH 126 1526 272  HOH HOH A . 
W 10 HOH 127 1527 612  HOH HOH A . 
W 10 HOH 128 1528 402  HOH HOH A . 
W 10 HOH 129 1529 684  HOH HOH A . 
W 10 HOH 130 1530 939  HOH HOH A . 
W 10 HOH 131 1531 1025 HOH HOH A . 
W 10 HOH 132 1532 153  HOH HOH A . 
W 10 HOH 133 1533 236  HOH HOH A . 
W 10 HOH 134 1534 13   HOH HOH A . 
W 10 HOH 135 1535 154  HOH HOH A . 
W 10 HOH 136 1536 850  HOH HOH A . 
W 10 HOH 137 1537 443  HOH HOH A . 
W 10 HOH 138 1538 328  HOH HOH A . 
W 10 HOH 139 1539 11   HOH HOH A . 
W 10 HOH 140 1540 1417 HOH HOH A . 
W 10 HOH 141 1541 772  HOH HOH A . 
W 10 HOH 142 1542 460  HOH HOH A . 
W 10 HOH 143 1543 654  HOH HOH A . 
W 10 HOH 144 1544 174  HOH HOH A . 
W 10 HOH 145 1545 698  HOH HOH A . 
W 10 HOH 146 1546 592  HOH HOH A . 
W 10 HOH 147 1547 838  HOH HOH A . 
W 10 HOH 148 1548 1152 HOH HOH A . 
W 10 HOH 149 1549 222  HOH HOH A . 
W 10 HOH 150 1550 860  HOH HOH A . 
W 10 HOH 151 1551 250  HOH HOH A . 
W 10 HOH 152 1552 51   HOH HOH A . 
W 10 HOH 153 1553 1352 HOH HOH A . 
W 10 HOH 154 1554 863  HOH HOH A . 
W 10 HOH 155 1555 1209 HOH HOH A . 
W 10 HOH 156 1556 269  HOH HOH A . 
W 10 HOH 157 1557 113  HOH HOH A . 
W 10 HOH 158 1558 976  HOH HOH A . 
W 10 HOH 159 1559 546  HOH HOH A . 
W 10 HOH 160 1560 1118 HOH HOH A . 
W 10 HOH 161 1561 486  HOH HOH A . 
W 10 HOH 162 1562 1093 HOH HOH A . 
W 10 HOH 163 1563 1443 HOH HOH A . 
W 10 HOH 164 1564 225  HOH HOH A . 
W 10 HOH 165 1565 1186 HOH HOH A . 
W 10 HOH 166 1566 1357 HOH HOH A . 
W 10 HOH 167 1567 375  HOH HOH A . 
W 10 HOH 168 1568 138  HOH HOH A . 
W 10 HOH 169 1569 214  HOH HOH A . 
W 10 HOH 170 1570 547  HOH HOH A . 
W 10 HOH 171 1571 501  HOH HOH A . 
W 10 HOH 172 1572 405  HOH HOH A . 
W 10 HOH 173 1573 212  HOH HOH A . 
W 10 HOH 174 1574 422  HOH HOH A . 
W 10 HOH 175 1575 205  HOH HOH A . 
W 10 HOH 176 1576 1170 HOH HOH A . 
W 10 HOH 177 1577 319  HOH HOH A . 
W 10 HOH 178 1578 796  HOH HOH A . 
W 10 HOH 179 1579 1039 HOH HOH A . 
W 10 HOH 180 1580 1433 HOH HOH A . 
W 10 HOH 181 1581 179  HOH HOH A . 
W 10 HOH 182 1582 101  HOH HOH A . 
W 10 HOH 183 1583 149  HOH HOH A . 
W 10 HOH 184 1584 588  HOH HOH A . 
W 10 HOH 185 1585 169  HOH HOH A . 
W 10 HOH 186 1586 1290 HOH HOH A . 
W 10 HOH 187 1587 968  HOH HOH A . 
W 10 HOH 188 1588 278  HOH HOH A . 
W 10 HOH 189 1589 453  HOH HOH A . 
W 10 HOH 190 1590 676  HOH HOH A . 
W 10 HOH 191 1591 917  HOH HOH A . 
W 10 HOH 192 1592 110  HOH HOH A . 
W 10 HOH 193 1593 204  HOH HOH A . 
W 10 HOH 194 1594 1259 HOH HOH A . 
W 10 HOH 195 1595 392  HOH HOH A . 
W 10 HOH 196 1596 401  HOH HOH A . 
W 10 HOH 197 1597 1038 HOH HOH A . 
W 10 HOH 198 1598 123  HOH HOH A . 
W 10 HOH 199 1599 723  HOH HOH A . 
W 10 HOH 200 1600 1059 HOH HOH A . 
W 10 HOH 201 1601 577  HOH HOH A . 
W 10 HOH 202 1602 192  HOH HOH A . 
W 10 HOH 203 1603 210  HOH HOH A . 
W 10 HOH 204 1604 864  HOH HOH A . 
W 10 HOH 205 1605 246  HOH HOH A . 
W 10 HOH 206 1606 131  HOH HOH A . 
W 10 HOH 207 1607 21   HOH HOH A . 
W 10 HOH 208 1608 1373 HOH HOH A . 
W 10 HOH 209 1609 64   HOH HOH A . 
W 10 HOH 210 1610 510  HOH HOH A . 
W 10 HOH 211 1611 289  HOH HOH A . 
W 10 HOH 212 1612 712  HOH HOH A . 
W 10 HOH 213 1613 627  HOH HOH A . 
W 10 HOH 214 1614 639  HOH HOH A . 
W 10 HOH 215 1615 825  HOH HOH A . 
W 10 HOH 216 1616 29   HOH HOH A . 
W 10 HOH 217 1617 1454 HOH HOH A . 
W 10 HOH 218 1618 645  HOH HOH A . 
W 10 HOH 219 1619 420  HOH HOH A . 
W 10 HOH 220 1620 150  HOH HOH A . 
W 10 HOH 221 1621 664  HOH HOH A . 
W 10 HOH 222 1622 1361 HOH HOH A . 
W 10 HOH 223 1623 897  HOH HOH A . 
W 10 HOH 224 1624 1104 HOH HOH A . 
W 10 HOH 225 1625 88   HOH HOH A . 
W 10 HOH 226 1626 590  HOH HOH A . 
W 10 HOH 227 1627 1097 HOH HOH A . 
W 10 HOH 228 1628 1176 HOH HOH A . 
W 10 HOH 229 1629 1327 HOH HOH A . 
W 10 HOH 230 1630 1220 HOH HOH A . 
W 10 HOH 231 1631 468  HOH HOH A . 
W 10 HOH 232 1632 692  HOH HOH A . 
W 10 HOH 233 1633 1001 HOH HOH A . 
W 10 HOH 234 1634 142  HOH HOH A . 
W 10 HOH 235 1635 643  HOH HOH A . 
W 10 HOH 236 1636 383  HOH HOH A . 
W 10 HOH 237 1637 1095 HOH HOH A . 
W 10 HOH 238 1638 1210 HOH HOH A . 
W 10 HOH 239 1639 467  HOH HOH A . 
W 10 HOH 240 1640 1431 HOH HOH A . 
W 10 HOH 241 1641 1079 HOH HOH A . 
W 10 HOH 242 1642 1234 HOH HOH A . 
W 10 HOH 243 1643 525  HOH HOH A . 
W 10 HOH 244 1644 477  HOH HOH A . 
W 10 HOH 245 1645 363  HOH HOH A . 
W 10 HOH 246 1646 1032 HOH HOH A . 
W 10 HOH 247 1647 97   HOH HOH A . 
W 10 HOH 248 1648 181  HOH HOH A . 
W 10 HOH 249 1649 681  HOH HOH A . 
W 10 HOH 250 1650 1371 HOH HOH A . 
W 10 HOH 251 1651 440  HOH HOH A . 
W 10 HOH 252 1652 380  HOH HOH A . 
W 10 HOH 253 1653 1115 HOH HOH A . 
W 10 HOH 254 1654 175  HOH HOH A . 
W 10 HOH 255 1655 824  HOH HOH A . 
W 10 HOH 256 1656 462  HOH HOH A . 
W 10 HOH 257 1657 1041 HOH HOH A . 
W 10 HOH 258 1658 1274 HOH HOH A . 
W 10 HOH 259 1659 251  HOH HOH A . 
W 10 HOH 260 1660 160  HOH HOH A . 
W 10 HOH 261 1661 1034 HOH HOH A . 
W 10 HOH 262 1662 425  HOH HOH A . 
W 10 HOH 263 1663 32   HOH HOH A . 
W 10 HOH 264 1664 98   HOH HOH A . 
W 10 HOH 265 1665 358  HOH HOH A . 
W 10 HOH 266 1666 143  HOH HOH A . 
W 10 HOH 267 1667 62   HOH HOH A . 
W 10 HOH 268 1668 10   HOH HOH A . 
W 10 HOH 269 1669 856  HOH HOH A . 
W 10 HOH 270 1670 370  HOH HOH A . 
W 10 HOH 271 1671 349  HOH HOH A . 
W 10 HOH 272 1672 693  HOH HOH A . 
W 10 HOH 273 1673 600  HOH HOH A . 
W 10 HOH 274 1674 1106 HOH HOH A . 
W 10 HOH 275 1675 542  HOH HOH A . 
W 10 HOH 276 1676 259  HOH HOH A . 
W 10 HOH 277 1677 763  HOH HOH A . 
W 10 HOH 278 1678 650  HOH HOH A . 
W 10 HOH 279 1679 879  HOH HOH A . 
W 10 HOH 280 1680 921  HOH HOH A . 
W 10 HOH 281 1681 435  HOH HOH A . 
W 10 HOH 282 1682 50   HOH HOH A . 
W 10 HOH 283 1683 644  HOH HOH A . 
W 10 HOH 284 1684 1042 HOH HOH A . 
W 10 HOH 285 1685 877  HOH HOH A . 
W 10 HOH 286 1686 301  HOH HOH A . 
W 10 HOH 287 1687 1307 HOH HOH A . 
W 10 HOH 288 1688 306  HOH HOH A . 
W 10 HOH 289 1689 1308 HOH HOH A . 
W 10 HOH 290 1690 93   HOH HOH A . 
W 10 HOH 291 1691 906  HOH HOH A . 
W 10 HOH 292 1692 42   HOH HOH A . 
W 10 HOH 293 1693 889  HOH HOH A . 
W 10 HOH 294 1694 7    HOH HOH A . 
W 10 HOH 295 1695 845  HOH HOH A . 
W 10 HOH 296 1696 708  HOH HOH A . 
W 10 HOH 297 1697 1217 HOH HOH A . 
W 10 HOH 298 1698 167  HOH HOH A . 
W 10 HOH 299 1699 423  HOH HOH A . 
W 10 HOH 300 1700 621  HOH HOH A . 
W 10 HOH 301 1701 431  HOH HOH A . 
W 10 HOH 302 1702 247  HOH HOH A . 
W 10 HOH 303 1703 722  HOH HOH A . 
W 10 HOH 304 1704 75   HOH HOH A . 
W 10 HOH 305 1705 680  HOH HOH A . 
W 10 HOH 306 1706 193  HOH HOH A . 
W 10 HOH 307 1707 145  HOH HOH A . 
W 10 HOH 308 1708 711  HOH HOH A . 
W 10 HOH 309 1709 346  HOH HOH A . 
W 10 HOH 310 1710 17   HOH HOH A . 
W 10 HOH 311 1711 276  HOH HOH A . 
W 10 HOH 312 1712 135  HOH HOH A . 
W 10 HOH 313 1713 71   HOH HOH A . 
W 10 HOH 314 1714 1066 HOH HOH A . 
W 10 HOH 315 1715 1458 HOH HOH A . 
W 10 HOH 316 1716 228  HOH HOH A . 
W 10 HOH 317 1717 890  HOH HOH A . 
W 10 HOH 318 1718 44   HOH HOH A . 
W 10 HOH 319 1719 217  HOH HOH A . 
W 10 HOH 320 1720 1296 HOH HOH A . 
W 10 HOH 321 1721 445  HOH HOH A . 
W 10 HOH 322 1722 883  HOH HOH A . 
W 10 HOH 323 1723 79   HOH HOH A . 
W 10 HOH 324 1724 1122 HOH HOH A . 
W 10 HOH 325 1725 398  HOH HOH A . 
W 10 HOH 326 1726 439  HOH HOH A . 
W 10 HOH 327 1727 752  HOH HOH A . 
W 10 HOH 328 1728 331  HOH HOH A . 
W 10 HOH 329 1729 1412 HOH HOH A . 
W 10 HOH 330 1730 622  HOH HOH A . 
W 10 HOH 331 1731 1020 HOH HOH A . 
W 10 HOH 332 1732 24   HOH HOH A . 
W 10 HOH 333 1733 867  HOH HOH A . 
W 10 HOH 334 1734 764  HOH HOH A . 
W 10 HOH 335 1735 458  HOH HOH A . 
W 10 HOH 336 1736 28   HOH HOH A . 
W 10 HOH 337 1737 377  HOH HOH A . 
W 10 HOH 338 1738 393  HOH HOH A . 
W 10 HOH 339 1739 294  HOH HOH A . 
W 10 HOH 340 1740 1086 HOH HOH A . 
W 10 HOH 341 1741 962  HOH HOH A . 
W 10 HOH 342 1742 158  HOH HOH A . 
W 10 HOH 343 1743 128  HOH HOH A . 
W 10 HOH 344 1744 1270 HOH HOH A . 
W 10 HOH 345 1745 180  HOH HOH A . 
W 10 HOH 346 1746 823  HOH HOH A . 
W 10 HOH 347 1747 1414 HOH HOH A . 
W 10 HOH 348 1748 1340 HOH HOH A . 
W 10 HOH 349 1749 382  HOH HOH A . 
W 10 HOH 350 1750 1367 HOH HOH A . 
W 10 HOH 351 1751 1354 HOH HOH A . 
W 10 HOH 352 1752 268  HOH HOH A . 
W 10 HOH 353 1753 1460 HOH HOH A . 
W 10 HOH 354 1754 1229 HOH HOH A . 
W 10 HOH 355 1755 844  HOH HOH A . 
W 10 HOH 356 1756 977  HOH HOH A . 
W 10 HOH 357 1757 430  HOH HOH A . 
W 10 HOH 358 1758 493  HOH HOH A . 
W 10 HOH 359 1759 808  HOH HOH A . 
W 10 HOH 360 1760 820  HOH HOH A . 
W 10 HOH 361 1761 310  HOH HOH A . 
W 10 HOH 362 1762 830  HOH HOH A . 
W 10 HOH 363 1763 734  HOH HOH A . 
W 10 HOH 364 1764 846  HOH HOH A . 
W 10 HOH 365 1765 280  HOH HOH A . 
W 10 HOH 366 1766 352  HOH HOH A . 
W 10 HOH 367 1767 544  HOH HOH A . 
W 10 HOH 368 1768 216  HOH HOH A . 
W 10 HOH 369 1769 699  HOH HOH A . 
W 10 HOH 370 1770 915  HOH HOH A . 
W 10 HOH 371 1771 1033 HOH HOH A . 
W 10 HOH 372 1772 527  HOH HOH A . 
W 10 HOH 373 1773 647  HOH HOH A . 
W 10 HOH 374 1774 532  HOH HOH A . 
W 10 HOH 375 1775 560  HOH HOH A . 
W 10 HOH 376 1776 518  HOH HOH A . 
W 10 HOH 377 1777 121  HOH HOH A . 
W 10 HOH 378 1778 508  HOH HOH A . 
W 10 HOH 379 1779 271  HOH HOH A . 
W 10 HOH 380 1780 327  HOH HOH A . 
W 10 HOH 381 1781 894  HOH HOH A . 
W 10 HOH 382 1782 781  HOH HOH A . 
W 10 HOH 383 1783 221  HOH HOH A . 
W 10 HOH 384 1784 1405 HOH HOH A . 
W 10 HOH 385 1785 1236 HOH HOH A . 
W 10 HOH 386 1786 562  HOH HOH A . 
W 10 HOH 387 1787 1440 HOH HOH A . 
W 10 HOH 388 1788 646  HOH HOH A . 
W 10 HOH 389 1789 1365 HOH HOH A . 
W 10 HOH 390 1790 735  HOH HOH A . 
W 10 HOH 391 1791 674  HOH HOH A . 
W 10 HOH 392 1792 753  HOH HOH A . 
W 10 HOH 393 1793 367  HOH HOH A . 
W 10 HOH 394 1794 397  HOH HOH A . 
W 10 HOH 395 1795 464  HOH HOH A . 
W 10 HOH 396 1796 574  HOH HOH A . 
W 10 HOH 397 1797 1320 HOH HOH A . 
W 10 HOH 398 1798 489  HOH HOH A . 
W 10 HOH 399 1799 1344 HOH HOH A . 
W 10 HOH 400 1800 1325 HOH HOH A . 
W 10 HOH 401 1801 1298 HOH HOH A . 
W 10 HOH 402 1802 930  HOH HOH A . 
W 10 HOH 403 1803 580  HOH HOH A . 
W 10 HOH 404 1804 1332 HOH HOH A . 
W 10 HOH 405 1805 495  HOH HOH A . 
W 10 HOH 406 1806 461  HOH HOH A . 
W 10 HOH 407 1807 1232 HOH HOH A . 
W 10 HOH 408 1808 480  HOH HOH A . 
W 10 HOH 409 1809 211  HOH HOH A . 
W 10 HOH 410 1810 652  HOH HOH A . 
W 10 HOH 411 1811 318  HOH HOH A . 
W 10 HOH 412 1812 933  HOH HOH A . 
W 10 HOH 413 1813 520  HOH HOH A . 
W 10 HOH 414 1814 418  HOH HOH A . 
W 10 HOH 415 1815 87   HOH HOH A . 
W 10 HOH 416 1816 1187 HOH HOH A . 
W 10 HOH 417 1817 208  HOH HOH A . 
W 10 HOH 418 1818 584  HOH HOH A . 
W 10 HOH 419 1819 866  HOH HOH A . 
W 10 HOH 420 1820 244  HOH HOH A . 
W 10 HOH 421 1821 536  HOH HOH A . 
W 10 HOH 422 1822 134  HOH HOH A . 
W 10 HOH 423 1823 1370 HOH HOH A . 
W 10 HOH 424 1824 865  HOH HOH A . 
W 10 HOH 425 1825 286  HOH HOH A . 
W 10 HOH 426 1826 1451 HOH HOH A . 
W 10 HOH 427 1827 1102 HOH HOH A . 
W 10 HOH 428 1828 426  HOH HOH A . 
W 10 HOH 429 1829 451  HOH HOH A . 
W 10 HOH 430 1830 1199 HOH HOH A . 
W 10 HOH 431 1831 320  HOH HOH A . 
W 10 HOH 432 1832 1271 HOH HOH A . 
W 10 HOH 433 1833 806  HOH HOH A . 
W 10 HOH 434 1834 1463 HOH HOH A . 
W 10 HOH 435 1835 59   HOH HOH A . 
W 10 HOH 436 1836 852  HOH HOH A . 
W 10 HOH 437 1837 869  HOH HOH A . 
W 10 HOH 438 1838 322  HOH HOH A . 
W 10 HOH 439 1839 1465 HOH HOH A . 
W 10 HOH 440 1840 568  HOH HOH A . 
W 10 HOH 441 1841 718  HOH HOH A . 
W 10 HOH 442 1842 282  HOH HOH A . 
W 10 HOH 443 1843 342  HOH HOH A . 
W 10 HOH 444 1844 103  HOH HOH A . 
W 10 HOH 445 1845 1012 HOH HOH A . 
W 10 HOH 446 1846 974  HOH HOH A . 
W 10 HOH 447 1847 882  HOH HOH A . 
W 10 HOH 448 1848 437  HOH HOH A . 
W 10 HOH 449 1849 260  HOH HOH A . 
W 10 HOH 450 1850 364  HOH HOH A . 
W 10 HOH 451 1851 1057 HOH HOH A . 
W 10 HOH 452 1852 986  HOH HOH A . 
W 10 HOH 453 1853 235  HOH HOH A . 
W 10 HOH 454 1854 1139 HOH HOH A . 
W 10 HOH 455 1855 348  HOH HOH A . 
W 10 HOH 456 1856 979  HOH HOH A . 
W 10 HOH 457 1857 355  HOH HOH A . 
W 10 HOH 458 1858 566  HOH HOH A . 
W 10 HOH 459 1859 601  HOH HOH A . 
W 10 HOH 460 1860 245  HOH HOH A . 
W 10 HOH 461 1861 730  HOH HOH A . 
W 10 HOH 462 1862 412  HOH HOH A . 
W 10 HOH 463 1863 629  HOH HOH A . 
W 10 HOH 464 1864 847  HOH HOH A . 
W 10 HOH 465 1865 89   HOH HOH A . 
W 10 HOH 466 1866 958  HOH HOH A . 
W 10 HOH 467 1867 478  HOH HOH A . 
W 10 HOH 468 1868 1300 HOH HOH A . 
W 10 HOH 469 1869 90   HOH HOH A . 
W 10 HOH 470 1870 531  HOH HOH A . 
W 10 HOH 471 1871 292  HOH HOH A . 
W 10 HOH 472 1872 550  HOH HOH A . 
W 10 HOH 473 1873 839  HOH HOH A . 
W 10 HOH 474 1874 951  HOH HOH A . 
W 10 HOH 475 1875 1181 HOH HOH A . 
W 10 HOH 476 1876 669  HOH HOH A . 
W 10 HOH 477 1877 469  HOH HOH A . 
W 10 HOH 478 1878 802  HOH HOH A . 
W 10 HOH 479 1879 199  HOH HOH A . 
W 10 HOH 480 1880 1006 HOH HOH A . 
W 10 HOH 481 1881 201  HOH HOH A . 
W 10 HOH 482 1882 511  HOH HOH A . 
W 10 HOH 483 1883 234  HOH HOH A . 
W 10 HOH 484 1884 814  HOH HOH A . 
W 10 HOH 485 1885 374  HOH HOH A . 
W 10 HOH 486 1886 317  HOH HOH A . 
W 10 HOH 487 1887 207  HOH HOH A . 
W 10 HOH 488 1888 1331 HOH HOH A . 
W 10 HOH 489 1889 105  HOH HOH A . 
W 10 HOH 490 1890 389  HOH HOH A . 
W 10 HOH 491 1891 902  HOH HOH A . 
W 10 HOH 492 1892 1362 HOH HOH A . 
W 10 HOH 493 1893 971  HOH HOH A . 
W 10 HOH 494 1894 819  HOH HOH A . 
W 10 HOH 495 1895 506  HOH HOH A . 
W 10 HOH 496 1896 459  HOH HOH A . 
W 10 HOH 497 1897 333  HOH HOH A . 
W 10 HOH 498 1898 1426 HOH HOH A . 
W 10 HOH 499 1899 316  HOH HOH A . 
W 10 HOH 500 1900 1046 HOH HOH A . 
W 10 HOH 501 1901 611  HOH HOH A . 
W 10 HOH 502 1902 172  HOH HOH A . 
W 10 HOH 503 1903 596  HOH HOH A . 
W 10 HOH 504 1904 429  HOH HOH A . 
W 10 HOH 505 1905 1103 HOH HOH A . 
W 10 HOH 506 1906 413  HOH HOH A . 
W 10 HOH 507 1907 762  HOH HOH A . 
W 10 HOH 508 1908 603  HOH HOH A . 
W 10 HOH 509 1909 1404 HOH HOH A . 
W 10 HOH 510 1910 1282 HOH HOH A . 
W 10 HOH 511 1911 442  HOH HOH A . 
W 10 HOH 512 1912 182  HOH HOH A . 
W 10 HOH 513 1913 689  HOH HOH A . 
W 10 HOH 514 1914 1180 HOH HOH A . 
W 10 HOH 515 1915 1416 HOH HOH A . 
W 10 HOH 516 1916 876  HOH HOH A . 
W 10 HOH 517 1917 1098 HOH HOH A . 
W 10 HOH 518 1918 1094 HOH HOH A . 
W 10 HOH 519 1919 1204 HOH HOH A . 
W 10 HOH 520 1920 1353 HOH HOH A . 
W 10 HOH 521 1921 927  HOH HOH A . 
W 10 HOH 522 1922 758  HOH HOH A . 
W 10 HOH 523 1923 350  HOH HOH A . 
W 10 HOH 524 1924 771  HOH HOH A . 
W 10 HOH 525 1925 1146 HOH HOH A . 
W 10 HOH 526 1926 934  HOH HOH A . 
W 10 HOH 527 1927 966  HOH HOH A . 
W 10 HOH 528 1928 1398 HOH HOH A . 
W 10 HOH 529 1929 257  HOH HOH A . 
W 10 HOH 530 1930 26   HOH HOH A . 
W 10 HOH 531 1931 931  HOH HOH A . 
W 10 HOH 532 1932 120  HOH HOH A . 
W 10 HOH 533 1933 387  HOH HOH A . 
W 10 HOH 534 1934 784  HOH HOH A . 
W 10 HOH 535 1935 1377 HOH HOH A . 
W 10 HOH 536 1936 799  HOH HOH A . 
W 10 HOH 537 1937 1265 HOH HOH A . 
W 10 HOH 538 1938 1080 HOH HOH A . 
W 10 HOH 539 1939 399  HOH HOH A . 
W 10 HOH 540 1940 602  HOH HOH A . 
W 10 HOH 541 1941 330  HOH HOH A . 
W 10 HOH 542 1942 1435 HOH HOH A . 
W 10 HOH 543 1943 616  HOH HOH A . 
W 10 HOH 544 1944 959  HOH HOH A . 
W 10 HOH 545 1945 81   HOH HOH A . 
W 10 HOH 546 1946 790  HOH HOH A . 
W 10 HOH 547 1947 1268 HOH HOH A . 
W 10 HOH 548 1948 116  HOH HOH A . 
W 10 HOH 549 1949 1413 HOH HOH A . 
W 10 HOH 550 1950 1403 HOH HOH A . 
W 10 HOH 551 1951 575  HOH HOH A . 
W 10 HOH 552 1952 519  HOH HOH A . 
W 10 HOH 553 1953 224  HOH HOH A . 
W 10 HOH 554 1954 1002 HOH HOH A . 
W 10 HOH 555 1955 1215 HOH HOH A . 
W 10 HOH 556 1956 1342 HOH HOH A . 
W 10 HOH 557 1957 1208 HOH HOH A . 
W 10 HOH 558 1958 223  HOH HOH A . 
W 10 HOH 559 1959 1315 HOH HOH A . 
W 10 HOH 560 1960 778  HOH HOH A . 
W 10 HOH 561 1961 940  HOH HOH A . 
W 10 HOH 562 1962 1246 HOH HOH A . 
W 10 HOH 563 1963 886  HOH HOH A . 
W 10 HOH 564 1964 1143 HOH HOH A . 
W 10 HOH 565 1965 102  HOH HOH A . 
W 10 HOH 566 1966 688  HOH HOH A . 
W 10 HOH 567 1967 868  HOH HOH A . 
W 10 HOH 568 1968 572  HOH HOH A . 
W 10 HOH 569 1969 1053 HOH HOH A . 
W 10 HOH 570 1970 993  HOH HOH A . 
W 10 HOH 571 1971 1158 HOH HOH A . 
W 10 HOH 572 1972 1299 HOH HOH A . 
W 10 HOH 573 1973 1127 HOH HOH A . 
W 10 HOH 574 1974 416  HOH HOH A . 
W 10 HOH 575 1975 797  HOH HOH A . 
W 10 HOH 576 1976 1013 HOH HOH A . 
W 10 HOH 577 1977 925  HOH HOH A . 
W 10 HOH 578 1978 241  HOH HOH A . 
W 10 HOH 579 1979 702  HOH HOH A . 
W 10 HOH 580 1980 1126 HOH HOH A . 
W 10 HOH 581 1981 732  HOH HOH A . 
W 10 HOH 582 1982 1162 HOH HOH A . 
W 10 HOH 583 1983 1015 HOH HOH A . 
W 10 HOH 584 1984 761  HOH HOH A . 
W 10 HOH 585 1985 1448 HOH HOH A . 
W 10 HOH 586 1986 821  HOH HOH A . 
W 10 HOH 587 1987 978  HOH HOH A . 
W 10 HOH 588 1988 1114 HOH HOH A . 
W 10 HOH 589 1989 773  HOH HOH A . 
W 10 HOH 590 1990 1406 HOH HOH A . 
W 10 HOH 591 1991 625  HOH HOH A . 
W 10 HOH 592 1992 1058 HOH HOH A . 
W 10 HOH 593 1993 1159 HOH HOH A . 
W 10 HOH 594 1994 1309 HOH HOH A . 
W 10 HOH 595 1995 1167 HOH HOH A . 
W 10 HOH 596 1996 878  HOH HOH A . 
W 10 HOH 597 1997 706  HOH HOH A . 
W 10 HOH 598 1998 849  HOH HOH A . 
W 10 HOH 599 1999 1206 HOH HOH A . 
W 10 HOH 600 2000 313  HOH HOH A . 
W 10 HOH 601 2001 1140 HOH HOH A . 
W 10 HOH 602 2002 1455 HOH HOH A . 
W 10 HOH 603 2003 1153 HOH HOH A . 
W 10 HOH 604 2004 1400 HOH HOH A . 
W 10 HOH 605 2005 785  HOH HOH A . 
W 10 HOH 606 2006 1166 HOH HOH A . 
W 10 HOH 607 2007 1035 HOH HOH A . 
W 10 HOH 608 2008 943  HOH HOH A . 
W 10 HOH 609 2009 472  HOH HOH A . 
W 10 HOH 610 2010 1349 HOH HOH A . 
W 10 HOH 611 2011 1147 HOH HOH A . 
W 10 HOH 612 2012 1356 HOH HOH A . 
W 10 HOH 613 2013 1101 HOH HOH A . 
W 10 HOH 614 2014 1244 HOH HOH A . 
W 10 HOH 615 2015 463  HOH HOH A . 
W 10 HOH 616 2016 892  HOH HOH A . 
W 10 HOH 617 2017 1090 HOH HOH A . 
W 10 HOH 618 2018 1065 HOH HOH A . 
W 10 HOH 619 2019 1144 HOH HOH A . 
W 10 HOH 620 2020 997  HOH HOH A . 
W 10 HOH 621 2021 1182 HOH HOH A . 
W 10 HOH 622 2022 1011 HOH HOH A . 
W 10 HOH 623 2023 1129 HOH HOH A . 
W 10 HOH 624 2024 1148 HOH HOH A . 
W 10 HOH 625 2025 672  HOH HOH A . 
W 10 HOH 626 2026 533  HOH HOH A . 
W 10 HOH 627 2027 610  HOH HOH A . 
W 10 HOH 628 2028 1437 HOH HOH A . 
W 10 HOH 629 2029 1235 HOH HOH A . 
W 10 HOH 630 2030 1286 HOH HOH A . 
W 10 HOH 631 2031 1284 HOH HOH A . 
W 10 HOH 632 2032 1149 HOH HOH A . 
W 10 HOH 633 2033 1450 HOH HOH A . 
W 10 HOH 634 2034 548  HOH HOH A . 
W 10 HOH 635 2035 522  HOH HOH A . 
W 10 HOH 636 2036 1388 HOH HOH A . 
W 10 HOH 637 2037 1031 HOH HOH A . 
W 10 HOH 638 2038 549  HOH HOH A . 
W 10 HOH 639 2039 1192 HOH HOH A . 
W 10 HOH 640 2040 336  HOH HOH A . 
W 10 HOH 641 2041 1007 HOH HOH A . 
W 10 HOH 642 2042 1306 HOH HOH A . 
W 10 HOH 643 2043 165  HOH HOH A . 
W 10 HOH 644 2044 1151 HOH HOH A . 
W 10 HOH 645 2045 1184 HOH HOH A . 
W 10 HOH 646 2046 1009 HOH HOH A . 
W 10 HOH 647 2047 1125 HOH HOH A . 
W 10 HOH 648 2048 1117 HOH HOH A . 
W 10 HOH 649 2049 696  HOH HOH A . 
W 10 HOH 650 2050 1423 HOH HOH A . 
W 10 HOH 651 2051 983  HOH HOH A . 
W 10 HOH 652 2052 563  HOH HOH A . 
W 10 HOH 653 2053 1334 HOH HOH A . 
W 10 HOH 654 2054 1087 HOH HOH A . 
W 10 HOH 655 2055 1407 HOH HOH A . 
W 10 HOH 656 2056 1383 HOH HOH A . 
W 10 HOH 657 2057 1326 HOH HOH A . 
W 10 HOH 658 2058 1355 HOH HOH A . 
W 10 HOH 659 2059 1088 HOH HOH A . 
W 10 HOH 660 2060 1258 HOH HOH A . 
W 10 HOH 661 2061 843  HOH HOH A . 
W 10 HOH 662 2062 1269 HOH HOH A . 
W 10 HOH 663 2063 1194 HOH HOH A . 
W 10 HOH 664 2064 308  HOH HOH A . 
W 10 HOH 665 2065 1089 HOH HOH A . 
W 10 HOH 666 2066 928  HOH HOH A . 
W 10 HOH 667 2067 1277 HOH HOH A . 
W 10 HOH 668 2068 1436 HOH HOH A . 
W 10 HOH 669 2069 1289 HOH HOH A . 
W 10 HOH 670 2070 1207 HOH HOH A . 
W 10 HOH 671 2071 1233 HOH HOH A . 
W 10 HOH 672 2072 1375 HOH HOH A . 
W 10 HOH 673 2073 470  HOH HOH A . 
W 10 HOH 674 2074 1297 HOH HOH A . 
W 10 HOH 675 2075 935  HOH HOH A . 
W 10 HOH 676 2076 1250 HOH HOH A . 
W 10 HOH 677 2077 833  HOH HOH A . 
W 10 HOH 678 2078 1255 HOH HOH A . 
W 10 HOH 679 2079 989  HOH HOH A . 
W 10 HOH 680 2080 857  HOH HOH A . 
W 10 HOH 681 2081 932  HOH HOH A . 
W 10 HOH 682 2082 581  HOH HOH A . 
W 10 HOH 683 2083 909  HOH HOH A . 
W 10 HOH 684 2084 1453 HOH HOH A . 
W 10 HOH 685 2085 1024 HOH HOH A . 
W 10 HOH 686 2086 1382 HOH HOH A . 
W 10 HOH 687 2087 655  HOH HOH A . 
W 10 HOH 688 2088 1113 HOH HOH A . 
W 10 HOH 689 2089 543  HOH HOH A . 
W 10 HOH 690 2090 1422 HOH HOH A . 
W 10 HOH 691 2091 275  HOH HOH A . 
W 10 HOH 692 2092 1091 HOH HOH A . 
W 10 HOH 693 2093 1049 HOH HOH A . 
W 10 HOH 694 2094 1294 HOH HOH A . 
W 10 HOH 695 2095 1221 HOH HOH A . 
W 10 HOH 696 2096 1421 HOH HOH A . 
W 10 HOH 697 2097 949  HOH HOH A . 
W 10 HOH 698 2098 1227 HOH HOH A . 
W 10 HOH 699 2099 1179 HOH HOH A . 
W 10 HOH 700 2100 901  HOH HOH A . 
W 10 HOH 701 2101 1337 HOH HOH A . 
W 10 HOH 702 2102 1280 HOH HOH A . 
W 10 HOH 703 2103 1171 HOH HOH A . 
W 10 HOH 704 2104 998  HOH HOH A . 
W 10 HOH 705 2105 1212 HOH HOH A . 
W 10 HOH 706 2106 1003 HOH HOH A . 
W 10 HOH 707 2107 1056 HOH HOH A . 
W 10 HOH 708 2108 957  HOH HOH A . 
W 10 HOH 709 2109 965  HOH HOH A . 
W 10 HOH 710 2110 1418 HOH HOH A . 
W 10 HOH 711 2111 1293 HOH HOH A . 
W 10 HOH 712 2112 1004 HOH HOH A . 
W 10 HOH 713 2113 1128 HOH HOH A . 
W 10 HOH 714 2114 716  HOH HOH A . 
W 10 HOH 715 2115 1216 HOH HOH A . 
W 10 HOH 716 2116 1360 HOH HOH A . 
W 10 HOH 717 2117 1249 HOH HOH A . 
W 10 HOH 718 2118 1359 HOH HOH A . 
W 10 HOH 719 2119 1419 HOH HOH A . 
X 10 HOH 1   1401 1380 HOH HOH B . 
X 10 HOH 2   1402 1281 HOH HOH B . 
X 10 HOH 3   1403 769  HOH HOH B . 
X 10 HOH 4   1404 1096 HOH HOH B . 
X 10 HOH 5   1405 871  HOH HOH B . 
X 10 HOH 6   1406 1023 HOH HOH B . 
X 10 HOH 7   1407 390  HOH HOH B . 
X 10 HOH 8   1408 528  HOH HOH B . 
X 10 HOH 9   1409 1336 HOH HOH B . 
X 10 HOH 10  1410 893  HOH HOH B . 
X 10 HOH 11  1411 1285 HOH HOH B . 
X 10 HOH 12  1412 302  HOH HOH B . 
X 10 HOH 13  1413 1138 HOH HOH B . 
X 10 HOH 14  1414 1111 HOH HOH B . 
X 10 HOH 15  1415 1420 HOH HOH B . 
X 10 HOH 16  1416 1415 HOH HOH B . 
X 10 HOH 17  1417 599  HOH HOH B . 
X 10 HOH 18  1418 1029 HOH HOH B . 
X 10 HOH 19  1419 970  HOH HOH B . 
X 10 HOH 20  1420 1439 HOH HOH B . 
X 10 HOH 21  1421 1021 HOH HOH B . 
X 10 HOH 22  1422 660  HOH HOH B . 
X 10 HOH 23  1423 456  HOH HOH B . 
X 10 HOH 24  1424 1446 HOH HOH B . 
X 10 HOH 25  1425 1218 HOH HOH B . 
X 10 HOH 26  1426 923  HOH HOH B . 
X 10 HOH 27  1427 1173 HOH HOH B . 
X 10 HOH 28  1428 573  HOH HOH B . 
X 10 HOH 29  1429 76   HOH HOH B . 
X 10 HOH 30  1430 1390 HOH HOH B . 
X 10 HOH 31  1431 1272 HOH HOH B . 
X 10 HOH 32  1432 746  HOH HOH B . 
X 10 HOH 33  1433 1287 HOH HOH B . 
X 10 HOH 34  1434 277  HOH HOH B . 
X 10 HOH 35  1435 1374 HOH HOH B . 
X 10 HOH 36  1436 341  HOH HOH B . 
X 10 HOH 37  1437 569  HOH HOH B . 
X 10 HOH 38  1438 606  HOH HOH B . 
X 10 HOH 39  1439 1261 HOH HOH B . 
X 10 HOH 40  1440 936  HOH HOH B . 
X 10 HOH 41  1441 329  HOH HOH B . 
X 10 HOH 42  1442 579  HOH HOH B . 
X 10 HOH 43  1443 604  HOH HOH B . 
X 10 HOH 44  1444 576  HOH HOH B . 
X 10 HOH 45  1445 1291 HOH HOH B . 
X 10 HOH 46  1446 913  HOH HOH B . 
X 10 HOH 47  1447 338  HOH HOH B . 
X 10 HOH 48  1448 281  HOH HOH B . 
X 10 HOH 49  1449 919  HOH HOH B . 
X 10 HOH 50  1450 884  HOH HOH B . 
X 10 HOH 51  1451 43   HOH HOH B . 
X 10 HOH 52  1452 1196 HOH HOH B . 
X 10 HOH 53  1453 52   HOH HOH B . 
X 10 HOH 54  1454 1044 HOH HOH B . 
X 10 HOH 55  1455 661  HOH HOH B . 
X 10 HOH 56  1456 540  HOH HOH B . 
X 10 HOH 57  1457 80   HOH HOH B . 
X 10 HOH 58  1458 920  HOH HOH B . 
X 10 HOH 59  1459 707  HOH HOH B . 
X 10 HOH 60  1460 953  HOH HOH B . 
X 10 HOH 61  1461 54   HOH HOH B . 
X 10 HOH 62  1462 162  HOH HOH B . 
X 10 HOH 63  1463 887  HOH HOH B . 
X 10 HOH 64  1464 1253 HOH HOH B . 
X 10 HOH 65  1465 291  HOH HOH B . 
X 10 HOH 66  1466 37   HOH HOH B . 
X 10 HOH 67  1467 1351 HOH HOH B . 
X 10 HOH 68  1468 20   HOH HOH B . 
X 10 HOH 69  1469 748  HOH HOH B . 
X 10 HOH 70  1470 754  HOH HOH B . 
X 10 HOH 71  1471 388  HOH HOH B . 
X 10 HOH 72  1472 1054 HOH HOH B . 
X 10 HOH 73  1473 619  HOH HOH B . 
X 10 HOH 74  1474 1201 HOH HOH B . 
X 10 HOH 75  1475 391  HOH HOH B . 
X 10 HOH 76  1476 607  HOH HOH B . 
X 10 HOH 77  1477 133  HOH HOH B . 
X 10 HOH 78  1478 438  HOH HOH B . 
X 10 HOH 79  1479 816  HOH HOH B . 
X 10 HOH 80  1480 126  HOH HOH B . 
X 10 HOH 81  1481 552  HOH HOH B . 
X 10 HOH 82  1482 5    HOH HOH B . 
X 10 HOH 83  1483 3    HOH HOH B . 
X 10 HOH 84  1484 777  HOH HOH B . 
X 10 HOH 85  1485 16   HOH HOH B . 
X 10 HOH 86  1486 1301 HOH HOH B . 
X 10 HOH 87  1487 83   HOH HOH B . 
X 10 HOH 88  1488 151  HOH HOH B . 
X 10 HOH 89  1489 56   HOH HOH B . 
X 10 HOH 90  1490 739  HOH HOH B . 
X 10 HOH 91  1491 786  HOH HOH B . 
X 10 HOH 92  1492 984  HOH HOH B . 
X 10 HOH 93  1493 1074 HOH HOH B . 
X 10 HOH 94  1494 233  HOH HOH B . 
X 10 HOH 95  1495 1328 HOH HOH B . 
X 10 HOH 96  1496 1449 HOH HOH B . 
X 10 HOH 97  1497 147  HOH HOH B . 
X 10 HOH 98  1498 1137 HOH HOH B . 
X 10 HOH 99  1499 1240 HOH HOH B . 
X 10 HOH 100 1500 801  HOH HOH B . 
X 10 HOH 101 1501 187  HOH HOH B . 
X 10 HOH 102 1502 994  HOH HOH B . 
X 10 HOH 103 1503 526  HOH HOH B . 
X 10 HOH 104 1504 822  HOH HOH B . 
X 10 HOH 105 1505 1084 HOH HOH B . 
X 10 HOH 106 1506 697  HOH HOH B . 
X 10 HOH 107 1507 1224 HOH HOH B . 
X 10 HOH 108 1508 161  HOH HOH B . 
X 10 HOH 109 1509 378  HOH HOH B . 
X 10 HOH 110 1510 68   HOH HOH B . 
X 10 HOH 111 1511 1378 HOH HOH B . 
X 10 HOH 112 1512 1178 HOH HOH B . 
X 10 HOH 113 1513 944  HOH HOH B . 
X 10 HOH 114 1514 293  HOH HOH B . 
X 10 HOH 115 1515 18   HOH HOH B . 
X 10 HOH 116 1516 1107 HOH HOH B . 
X 10 HOH 117 1517 1052 HOH HOH B . 
X 10 HOH 118 1518 410  HOH HOH B . 
X 10 HOH 119 1519 1429 HOH HOH B . 
X 10 HOH 120 1520 668  HOH HOH B . 
X 10 HOH 121 1521 191  HOH HOH B . 
X 10 HOH 122 1522 1397 HOH HOH B . 
X 10 HOH 123 1523 258  HOH HOH B . 
X 10 HOH 124 1524 490  HOH HOH B . 
X 10 HOH 125 1525 798  HOH HOH B . 
X 10 HOH 126 1526 34   HOH HOH B . 
X 10 HOH 127 1527 366  HOH HOH B . 
X 10 HOH 128 1528 565  HOH HOH B . 
X 10 HOH 129 1529 39   HOH HOH B . 
X 10 HOH 130 1530 715  HOH HOH B . 
X 10 HOH 131 1531 1076 HOH HOH B . 
X 10 HOH 132 1532 362  HOH HOH B . 
X 10 HOH 133 1533 194  HOH HOH B . 
X 10 HOH 134 1534 369  HOH HOH B . 
X 10 HOH 135 1535 396  HOH HOH B . 
X 10 HOH 136 1536 1311 HOH HOH B . 
X 10 HOH 137 1537 541  HOH HOH B . 
X 10 HOH 138 1538 678  HOH HOH B . 
X 10 HOH 139 1539 598  HOH HOH B . 
X 10 HOH 140 1540 907  HOH HOH B . 
X 10 HOH 141 1541 242  HOH HOH B . 
X 10 HOH 142 1542 807  HOH HOH B . 
X 10 HOH 143 1543 737  HOH HOH B . 
X 10 HOH 144 1544 704  HOH HOH B . 
X 10 HOH 145 1545 353  HOH HOH B . 
X 10 HOH 146 1546 69   HOH HOH B . 
X 10 HOH 147 1547 407  HOH HOH B . 
X 10 HOH 148 1548 60   HOH HOH B . 
X 10 HOH 149 1549 417  HOH HOH B . 
X 10 HOH 150 1550 63   HOH HOH B . 
X 10 HOH 151 1551 419  HOH HOH B . 
X 10 HOH 152 1552 597  HOH HOH B . 
X 10 HOH 153 1553 628  HOH HOH B . 
X 10 HOH 154 1554 1391 HOH HOH B . 
X 10 HOH 155 1555 139  HOH HOH B . 
X 10 HOH 156 1556 125  HOH HOH B . 
X 10 HOH 157 1557 1112 HOH HOH B . 
X 10 HOH 158 1558 694  HOH HOH B . 
X 10 HOH 159 1559 768  HOH HOH B . 
X 10 HOH 160 1560 848  HOH HOH B . 
X 10 HOH 161 1561 1314 HOH HOH B . 
X 10 HOH 162 1562 127  HOH HOH B . 
X 10 HOH 163 1563 106  HOH HOH B . 
X 10 HOH 164 1564 1313 HOH HOH B . 
X 10 HOH 165 1565 415  HOH HOH B . 
X 10 HOH 166 1566 58   HOH HOH B . 
X 10 HOH 167 1567 517  HOH HOH B . 
X 10 HOH 168 1568 1055 HOH HOH B . 
X 10 HOH 169 1569 682  HOH HOH B . 
X 10 HOH 170 1570 770  HOH HOH B . 
X 10 HOH 171 1571 609  HOH HOH B . 
X 10 HOH 172 1572 789  HOH HOH B . 
X 10 HOH 173 1573 870  HOH HOH B . 
X 10 HOH 174 1574 719  HOH HOH B . 
X 10 HOH 175 1575 70   HOH HOH B . 
X 10 HOH 176 1576 496  HOH HOH B . 
X 10 HOH 177 1577 1364 HOH HOH B . 
X 10 HOH 178 1578 104  HOH HOH B . 
X 10 HOH 179 1579 1191 HOH HOH B . 
X 10 HOH 180 1580 14   HOH HOH B . 
X 10 HOH 181 1581 264  HOH HOH B . 
X 10 HOH 182 1582 491  HOH HOH B . 
X 10 HOH 183 1583 1    HOH HOH B . 
X 10 HOH 184 1584 215  HOH HOH B . 
X 10 HOH 185 1585 267  HOH HOH B . 
X 10 HOH 186 1586 1457 HOH HOH B . 
X 10 HOH 187 1587 262  HOH HOH B . 
X 10 HOH 188 1588 745  HOH HOH B . 
X 10 HOH 189 1589 1434 HOH HOH B . 
X 10 HOH 190 1590 561  HOH HOH B . 
X 10 HOH 191 1591 424  HOH HOH B . 
X 10 HOH 192 1592 827  HOH HOH B . 
X 10 HOH 193 1593 85   HOH HOH B . 
X 10 HOH 194 1594 701  HOH HOH B . 
X 10 HOH 195 1595 705  HOH HOH B . 
X 10 HOH 196 1596 690  HOH HOH B . 
X 10 HOH 197 1597 1062 HOH HOH B . 
X 10 HOH 198 1598 307  HOH HOH B . 
X 10 HOH 199 1599 503  HOH HOH B . 
X 10 HOH 200 1600 118  HOH HOH B . 
X 10 HOH 201 1601 48   HOH HOH B . 
X 10 HOH 202 1602 229  HOH HOH B . 
X 10 HOH 203 1603 1319 HOH HOH B . 
X 10 HOH 204 1604 1427 HOH HOH B . 
X 10 HOH 205 1605 248  HOH HOH B . 
X 10 HOH 206 1606 8    HOH HOH B . 
X 10 HOH 207 1607 1223 HOH HOH B . 
X 10 HOH 208 1608 685  HOH HOH B . 
X 10 HOH 209 1609 434  HOH HOH B . 
X 10 HOH 210 1610 96   HOH HOH B . 
X 10 HOH 211 1611 812  HOH HOH B . 
X 10 HOH 212 1612 826  HOH HOH B . 
X 10 HOH 213 1613 749  HOH HOH B . 
X 10 HOH 214 1614 805  HOH HOH B . 
X 10 HOH 215 1615 339  HOH HOH B . 
X 10 HOH 216 1616 132  HOH HOH B . 
X 10 HOH 217 1617 15   HOH HOH B . 
X 10 HOH 218 1618 1040 HOH HOH B . 
X 10 HOH 219 1619 432  HOH HOH B . 
X 10 HOH 220 1620 238  HOH HOH B . 
X 10 HOH 221 1621 910  HOH HOH B . 
X 10 HOH 222 1622 815  HOH HOH B . 
X 10 HOH 223 1623 365  HOH HOH B . 
X 10 HOH 224 1624 955  HOH HOH B . 
X 10 HOH 225 1625 351  HOH HOH B . 
X 10 HOH 226 1626 1461 HOH HOH B . 
X 10 HOH 227 1627 117  HOH HOH B . 
X 10 HOH 228 1628 23   HOH HOH B . 
X 10 HOH 229 1629 817  HOH HOH B . 
X 10 HOH 230 1630 1222 HOH HOH B . 
X 10 HOH 231 1631 937  HOH HOH B . 
X 10 HOH 232 1632 755  HOH HOH B . 
X 10 HOH 233 1633 178  HOH HOH B . 
X 10 HOH 234 1634 964  HOH HOH B . 
X 10 HOH 235 1635 587  HOH HOH B . 
X 10 HOH 236 1636 186  HOH HOH B . 
X 10 HOH 237 1637 641  HOH HOH B . 
X 10 HOH 238 1638 109  HOH HOH B . 
X 10 HOH 239 1639 466  HOH HOH B . 
X 10 HOH 240 1640 457  HOH HOH B . 
X 10 HOH 241 1641 240  HOH HOH B . 
X 10 HOH 242 1642 372  HOH HOH B . 
X 10 HOH 243 1643 38   HOH HOH B . 
X 10 HOH 244 1644 476  HOH HOH B . 
X 10 HOH 245 1645 530  HOH HOH B . 
X 10 HOH 246 1646 811  HOH HOH B . 
X 10 HOH 247 1647 662  HOH HOH B . 
X 10 HOH 248 1648 33   HOH HOH B . 
X 10 HOH 249 1649 334  HOH HOH B . 
X 10 HOH 250 1650 479  HOH HOH B . 
X 10 HOH 251 1651 521  HOH HOH B . 
X 10 HOH 252 1652 912  HOH HOH B . 
X 10 HOH 253 1653 926  HOH HOH B . 
X 10 HOH 254 1654 200  HOH HOH B . 
X 10 HOH 255 1655 2    HOH HOH B . 
X 10 HOH 256 1656 354  HOH HOH B . 
X 10 HOH 257 1657 1464 HOH HOH B . 
X 10 HOH 258 1658 766  HOH HOH B . 
X 10 HOH 259 1659 686  HOH HOH B . 
X 10 HOH 260 1660 61   HOH HOH B . 
X 10 HOH 261 1661 297  HOH HOH B . 
X 10 HOH 262 1662 95   HOH HOH B . 
X 10 HOH 263 1663 274  HOH HOH B . 
X 10 HOH 264 1664 1345 HOH HOH B . 
X 10 HOH 265 1665 41   HOH HOH B . 
X 10 HOH 266 1666 695  HOH HOH B . 
X 10 HOH 267 1667 40   HOH HOH B . 
X 10 HOH 268 1668 899  HOH HOH B . 
X 10 HOH 269 1669 368  HOH HOH B . 
X 10 HOH 270 1670 556  HOH HOH B . 
X 10 HOH 271 1671 624  HOH HOH B . 
X 10 HOH 272 1672 862  HOH HOH B . 
X 10 HOH 273 1673 226  HOH HOH B . 
X 10 HOH 274 1674 115  HOH HOH B . 
X 10 HOH 275 1675 209  HOH HOH B . 
X 10 HOH 276 1676 1389 HOH HOH B . 
X 10 HOH 277 1677 46   HOH HOH B . 
X 10 HOH 278 1678 582  HOH HOH B . 
X 10 HOH 279 1679 740  HOH HOH B . 
X 10 HOH 280 1680 635  HOH HOH B . 
X 10 HOH 281 1681 985  HOH HOH B . 
X 10 HOH 282 1682 649  HOH HOH B . 
X 10 HOH 283 1683 157  HOH HOH B . 
X 10 HOH 284 1684 534  HOH HOH B . 
X 10 HOH 285 1685 376  HOH HOH B . 
X 10 HOH 286 1686 27   HOH HOH B . 
X 10 HOH 287 1687 312  HOH HOH B . 
X 10 HOH 288 1688 394  HOH HOH B . 
X 10 HOH 289 1689 25   HOH HOH B . 
X 10 HOH 290 1690 545  HOH HOH B . 
X 10 HOH 291 1691 1017 HOH HOH B . 
X 10 HOH 292 1692 190  HOH HOH B . 
X 10 HOH 293 1693 111  HOH HOH B . 
X 10 HOH 294 1694 300  HOH HOH B . 
X 10 HOH 295 1695 78   HOH HOH B . 
X 10 HOH 296 1696 400  HOH HOH B . 
X 10 HOH 297 1697 66   HOH HOH B . 
X 10 HOH 298 1698 818  HOH HOH B . 
X 10 HOH 299 1699 324  HOH HOH B . 
X 10 HOH 300 1700 1386 HOH HOH B . 
X 10 HOH 301 1701 908  HOH HOH B . 
X 10 HOH 302 1702 9    HOH HOH B . 
X 10 HOH 303 1703 73   HOH HOH B . 
X 10 HOH 304 1704 185  HOH HOH B . 
X 10 HOH 305 1705 203  HOH HOH B . 
X 10 HOH 306 1706 449  HOH HOH B . 
X 10 HOH 307 1707 1369 HOH HOH B . 
X 10 HOH 308 1708 538  HOH HOH B . 
X 10 HOH 309 1709 666  HOH HOH B . 
X 10 HOH 310 1710 1257 HOH HOH B . 
X 10 HOH 311 1711 309  HOH HOH B . 
X 10 HOH 312 1712 1028 HOH HOH B . 
X 10 HOH 313 1713 171  HOH HOH B . 
X 10 HOH 314 1714 841  HOH HOH B . 
X 10 HOH 315 1715 1254 HOH HOH B . 
X 10 HOH 316 1716 903  HOH HOH B . 
X 10 HOH 317 1717 670  HOH HOH B . 
X 10 HOH 318 1718 1155 HOH HOH B . 
X 10 HOH 319 1719 198  HOH HOH B . 
X 10 HOH 320 1720 94   HOH HOH B . 
X 10 HOH 321 1721 1283 HOH HOH B . 
X 10 HOH 322 1722 578  HOH HOH B . 
X 10 HOH 323 1723 197  HOH HOH B . 
X 10 HOH 324 1724 859  HOH HOH B . 
X 10 HOH 325 1725 1230 HOH HOH B . 
X 10 HOH 326 1726 499  HOH HOH B . 
X 10 HOH 327 1727 218  HOH HOH B . 
X 10 HOH 328 1728 954  HOH HOH B . 
X 10 HOH 329 1729 1016 HOH HOH B . 
X 10 HOH 330 1730 22   HOH HOH B . 
X 10 HOH 331 1731 731  HOH HOH B . 
X 10 HOH 332 1732 900  HOH HOH B . 
X 10 HOH 333 1733 67   HOH HOH B . 
X 10 HOH 334 1734 284  HOH HOH B . 
X 10 HOH 335 1735 12   HOH HOH B . 
X 10 HOH 336 1736 557  HOH HOH B . 
X 10 HOH 337 1737 1019 HOH HOH B . 
X 10 HOH 338 1738 1130 HOH HOH B . 
X 10 HOH 339 1739 326  HOH HOH B . 
X 10 HOH 340 1740 107  HOH HOH B . 
X 10 HOH 341 1741 1304 HOH HOH B . 
X 10 HOH 342 1742 793  HOH HOH B . 
X 10 HOH 343 1743 299  HOH HOH B . 
X 10 HOH 344 1744 836  HOH HOH B . 
X 10 HOH 345 1745 231  HOH HOH B . 
X 10 HOH 346 1746 634  HOH HOH B . 
X 10 HOH 347 1747 108  HOH HOH B . 
X 10 HOH 348 1748 938  HOH HOH B . 
X 10 HOH 349 1749 950  HOH HOH B . 
X 10 HOH 350 1750 347  HOH HOH B . 
X 10 HOH 351 1751 1302 HOH HOH B . 
X 10 HOH 352 1752 230  HOH HOH B . 
X 10 HOH 353 1753 220  HOH HOH B . 
X 10 HOH 354 1754 168  HOH HOH B . 
X 10 HOH 355 1755 1243 HOH HOH B . 
X 10 HOH 356 1756 613  HOH HOH B . 
X 10 HOH 357 1757 675  HOH HOH B . 
X 10 HOH 358 1758 834  HOH HOH B . 
X 10 HOH 359 1759 296  HOH HOH B . 
X 10 HOH 360 1760 617  HOH HOH B . 
X 10 HOH 361 1761 337  HOH HOH B . 
X 10 HOH 362 1762 414  HOH HOH B . 
X 10 HOH 363 1763 1163 HOH HOH B . 
X 10 HOH 364 1764 403  HOH HOH B . 
X 10 HOH 365 1765 945  HOH HOH B . 
X 10 HOH 366 1766 554  HOH HOH B . 
X 10 HOH 367 1767 455  HOH HOH B . 
X 10 HOH 368 1768 164  HOH HOH B . 
X 10 HOH 369 1769 411  HOH HOH B . 
X 10 HOH 370 1770 408  HOH HOH B . 
X 10 HOH 371 1771 436  HOH HOH B . 
X 10 HOH 372 1772 632  HOH HOH B . 
X 10 HOH 373 1773 184  HOH HOH B . 
X 10 HOH 374 1774 703  HOH HOH B . 
X 10 HOH 375 1775 553  HOH HOH B . 
X 10 HOH 376 1776 956  HOH HOH B . 
X 10 HOH 377 1777 386  HOH HOH B . 
X 10 HOH 378 1778 1266 HOH HOH B . 
X 10 HOH 379 1779 713  HOH HOH B . 
X 10 HOH 380 1780 270  HOH HOH B . 
X 10 HOH 381 1781 1010 HOH HOH B . 
X 10 HOH 382 1782 960  HOH HOH B . 
X 10 HOH 383 1783 290  HOH HOH B . 
X 10 HOH 384 1784 854  HOH HOH B . 
X 10 HOH 385 1785 254  HOH HOH B . 
X 10 HOH 386 1786 176  HOH HOH B . 
X 10 HOH 387 1787 593  HOH HOH B . 
X 10 HOH 388 1788 663  HOH HOH B . 
X 10 HOH 389 1789 273  HOH HOH B . 
X 10 HOH 390 1790 1211 HOH HOH B . 
X 10 HOH 391 1791 1213 HOH HOH B . 
X 10 HOH 392 1792 196  HOH HOH B . 
X 10 HOH 393 1793 30   HOH HOH B . 
X 10 HOH 394 1794 1177 HOH HOH B . 
X 10 HOH 395 1795 356  HOH HOH B . 
X 10 HOH 396 1796 202  HOH HOH B . 
X 10 HOH 397 1797 359  HOH HOH B . 
X 10 HOH 398 1798 1154 HOH HOH B . 
X 10 HOH 399 1799 148  HOH HOH B . 
X 10 HOH 400 1800 483  HOH HOH B . 
X 10 HOH 401 1801 441  HOH HOH B . 
X 10 HOH 402 1802 788  HOH HOH B . 
X 10 HOH 403 1803 895  HOH HOH B . 
X 10 HOH 404 1804 1156 HOH HOH B . 
X 10 HOH 405 1805 1264 HOH HOH B . 
X 10 HOH 406 1806 539  HOH HOH B . 
X 10 HOH 407 1807 65   HOH HOH B . 
X 10 HOH 408 1808 904  HOH HOH B . 
X 10 HOH 409 1809 720  HOH HOH B . 
X 10 HOH 410 1810 1248 HOH HOH B . 
X 10 HOH 411 1811 482  HOH HOH B . 
X 10 HOH 412 1812 1027 HOH HOH B . 
X 10 HOH 413 1813 1395 HOH HOH B . 
X 10 HOH 414 1814 1256 HOH HOH B . 
X 10 HOH 415 1815 421  HOH HOH B . 
X 10 HOH 416 1816 1075 HOH HOH B . 
X 10 HOH 417 1817 343  HOH HOH B . 
X 10 HOH 418 1818 379  HOH HOH B . 
X 10 HOH 419 1819 1430 HOH HOH B . 
X 10 HOH 420 1820 114  HOH HOH B . 
X 10 HOH 421 1821 219  HOH HOH B . 
X 10 HOH 422 1822 99   HOH HOH B . 
X 10 HOH 423 1823 311  HOH HOH B . 
X 10 HOH 424 1824 618  HOH HOH B . 
X 10 HOH 425 1825 1459 HOH HOH B . 
X 10 HOH 426 1826 947  HOH HOH B . 
X 10 HOH 427 1827 340  HOH HOH B . 
X 10 HOH 428 1828 911  HOH HOH B . 
X 10 HOH 429 1829 53   HOH HOH B . 
X 10 HOH 430 1830 1174 HOH HOH B . 
X 10 HOH 431 1831 792  HOH HOH B . 
X 10 HOH 432 1832 395  HOH HOH B . 
X 10 HOH 433 1833 448  HOH HOH B . 
X 10 HOH 434 1834 809  HOH HOH B . 
X 10 HOH 435 1835 249  HOH HOH B . 
X 10 HOH 436 1836 658  HOH HOH B . 
X 10 HOH 437 1837 1447 HOH HOH B . 
X 10 HOH 438 1838 1276 HOH HOH B . 
X 10 HOH 439 1839 828  HOH HOH B . 
X 10 HOH 440 1840 1082 HOH HOH B . 
X 10 HOH 441 1841 795  HOH HOH B . 
X 10 HOH 442 1842 475  HOH HOH B . 
X 10 HOH 443 1843 195  HOH HOH B . 
X 10 HOH 444 1844 1305 HOH HOH B . 
X 10 HOH 445 1845 213  HOH HOH B . 
X 10 HOH 446 1846 474  HOH HOH B . 
X 10 HOH 447 1847 729  HOH HOH B . 
X 10 HOH 448 1848 163  HOH HOH B . 
X 10 HOH 449 1849 1136 HOH HOH B . 
X 10 HOH 450 1850 991  HOH HOH B . 
X 10 HOH 451 1851 775  HOH HOH B . 
X 10 HOH 452 1852 1321 HOH HOH B . 
X 10 HOH 453 1853 447  HOH HOH B . 
X 10 HOH 454 1854 656  HOH HOH B . 
X 10 HOH 455 1855 253  HOH HOH B . 
X 10 HOH 456 1856 255  HOH HOH B . 
X 10 HOH 457 1857 1202 HOH HOH B . 
X 10 HOH 458 1858 4    HOH HOH B . 
X 10 HOH 459 1859 1228 HOH HOH B . 
X 10 HOH 460 1860 166  HOH HOH B . 
X 10 HOH 461 1861 173  HOH HOH B . 
X 10 HOH 462 1862 630  HOH HOH B . 
X 10 HOH 463 1863 633  HOH HOH B . 
X 10 HOH 464 1864 896  HOH HOH B . 
X 10 HOH 465 1865 1005 HOH HOH B . 
X 10 HOH 466 1866 183  HOH HOH B . 
X 10 HOH 467 1867 564  HOH HOH B . 
X 10 HOH 468 1868 305  HOH HOH B . 
X 10 HOH 469 1869 1073 HOH HOH B . 
X 10 HOH 470 1870 19   HOH HOH B . 
X 10 HOH 471 1871 1262 HOH HOH B . 
X 10 HOH 472 1872 636  HOH HOH B . 
X 10 HOH 473 1873 256  HOH HOH B . 
X 10 HOH 474 1874 1110 HOH HOH B . 
X 10 HOH 475 1875 428  HOH HOH B . 
X 10 HOH 476 1876 742  HOH HOH B . 
X 10 HOH 477 1877 261  HOH HOH B . 
X 10 HOH 478 1878 623  HOH HOH B . 
X 10 HOH 479 1879 74   HOH HOH B . 
X 10 HOH 480 1880 1048 HOH HOH B . 
X 10 HOH 481 1881 743  HOH HOH B . 
X 10 HOH 482 1882 92   HOH HOH B . 
X 10 HOH 483 1883 1119 HOH HOH B . 
X 10 HOH 484 1884 471  HOH HOH B . 
X 10 HOH 485 1885 589  HOH HOH B . 
X 10 HOH 486 1886 1384 HOH HOH B . 
X 10 HOH 487 1887 446  HOH HOH B . 
X 10 HOH 488 1888 615  HOH HOH B . 
X 10 HOH 489 1889 266  HOH HOH B . 
X 10 HOH 490 1890 112  HOH HOH B . 
X 10 HOH 491 1891 119  HOH HOH B . 
X 10 HOH 492 1892 535  HOH HOH B . 
X 10 HOH 493 1893 885  HOH HOH B . 
X 10 HOH 494 1894 497  HOH HOH B . 
X 10 HOH 495 1895 1132 HOH HOH B . 
X 10 HOH 496 1896 239  HOH HOH B . 
X 10 HOH 497 1897 55   HOH HOH B . 
X 10 HOH 498 1898 1401 HOH HOH B . 
X 10 HOH 499 1899 1247 HOH HOH B . 
X 10 HOH 500 1900 524  HOH HOH B . 
X 10 HOH 501 1901 6    HOH HOH B . 
X 10 HOH 502 1902 835  HOH HOH B . 
X 10 HOH 503 1903 551  HOH HOH B . 
X 10 HOH 504 1904 1346 HOH HOH B . 
X 10 HOH 505 1905 494  HOH HOH B . 
X 10 HOH 506 1906 780  HOH HOH B . 
X 10 HOH 507 1907 344  HOH HOH B . 
X 10 HOH 508 1908 156  HOH HOH B . 
X 10 HOH 509 1909 523  HOH HOH B . 
X 10 HOH 510 1910 140  HOH HOH B . 
X 10 HOH 511 1911 243  HOH HOH B . 
X 10 HOH 512 1912 861  HOH HOH B . 
X 10 HOH 513 1913 714  HOH HOH B . 
X 10 HOH 514 1914 1329 HOH HOH B . 
X 10 HOH 515 1915 529  HOH HOH B . 
X 10 HOH 516 1916 813  HOH HOH B . 
X 10 HOH 517 1917 314  HOH HOH B . 
X 10 HOH 518 1918 1188 HOH HOH B . 
X 10 HOH 519 1919 594  HOH HOH B . 
X 10 HOH 520 1920 1330 HOH HOH B . 
X 10 HOH 521 1921 1077 HOH HOH B . 
X 10 HOH 522 1922 47   HOH HOH B . 
X 10 HOH 523 1923 1456 HOH HOH B . 
X 10 HOH 524 1924 287  HOH HOH B . 
X 10 HOH 525 1925 381  HOH HOH B . 
X 10 HOH 526 1926 642  HOH HOH B . 
X 10 HOH 527 1927 227  HOH HOH B . 
X 10 HOH 528 1928 1462 HOH HOH B . 
X 10 HOH 529 1929 1350 HOH HOH B . 
X 10 HOH 530 1930 357  HOH HOH B . 
X 10 HOH 531 1931 691  HOH HOH B . 
X 10 HOH 532 1932 638  HOH HOH B . 
X 10 HOH 533 1933 514  HOH HOH B . 
X 10 HOH 534 1934 880  HOH HOH B . 
X 10 HOH 535 1935 155  HOH HOH B . 
X 10 HOH 536 1936 206  HOH HOH B . 
X 10 HOH 537 1937 427  HOH HOH B . 
X 10 HOH 538 1938 586  HOH HOH B . 
X 10 HOH 539 1939 288  HOH HOH B . 
X 10 HOH 540 1940 1100 HOH HOH B . 
X 10 HOH 541 1941 571  HOH HOH B . 
X 10 HOH 542 1942 1134 HOH HOH B . 
X 10 HOH 543 1943 481  HOH HOH B . 
X 10 HOH 544 1944 605  HOH HOH B . 
X 10 HOH 545 1945 872  HOH HOH B . 
X 10 HOH 546 1946 84   HOH HOH B . 
X 10 HOH 547 1947 1123 HOH HOH B . 
X 10 HOH 548 1948 1387 HOH HOH B . 
X 10 HOH 549 1949 1018 HOH HOH B . 
X 10 HOH 550 1950 325  HOH HOH B . 
X 10 HOH 551 1951 86   HOH HOH B . 
X 10 HOH 552 1952 728  HOH HOH B . 
X 10 HOH 553 1953 842  HOH HOH B . 
X 10 HOH 554 1954 783  HOH HOH B . 
X 10 HOH 555 1955 537  HOH HOH B . 
X 10 HOH 556 1956 999  HOH HOH B . 
X 10 HOH 557 1957 1394 HOH HOH B . 
X 10 HOH 558 1958 188  HOH HOH B . 
X 10 HOH 559 1959 1067 HOH HOH B . 
X 10 HOH 560 1960 298  HOH HOH B . 
X 10 HOH 561 1961 969  HOH HOH B . 
X 10 HOH 562 1962 800  HOH HOH B . 
X 10 HOH 563 1963 776  HOH HOH B . 
X 10 HOH 564 1964 82   HOH HOH B . 
X 10 HOH 565 1965 1292 HOH HOH B . 
X 10 HOH 566 1966 747  HOH HOH B . 
X 10 HOH 567 1967 1323 HOH HOH B . 
X 10 HOH 568 1968 465  HOH HOH B . 
X 10 HOH 569 1969 1109 HOH HOH B . 
X 10 HOH 570 1970 1022 HOH HOH B . 
X 10 HOH 571 1971 265  HOH HOH B . 
X 10 HOH 572 1972 1120 HOH HOH B . 
X 10 HOH 573 1973 874  HOH HOH B . 
X 10 HOH 574 1974 665  HOH HOH B . 
X 10 HOH 575 1975 473  HOH HOH B . 
X 10 HOH 576 1976 992  HOH HOH B . 
X 10 HOH 577 1977 295  HOH HOH B . 
X 10 HOH 578 1978 744  HOH HOH B . 
X 10 HOH 579 1979 505  HOH HOH B . 
X 10 HOH 580 1980 1442 HOH HOH B . 
X 10 HOH 581 1981 626  HOH HOH B . 
X 10 HOH 582 1982 700  HOH HOH B . 
X 10 HOH 583 1983 1099 HOH HOH B . 
X 10 HOH 584 1984 567  HOH HOH B . 
X 10 HOH 585 1985 1424 HOH HOH B . 
X 10 HOH 586 1986 837  HOH HOH B . 
X 10 HOH 587 1987 1245 HOH HOH B . 
X 10 HOH 588 1988 1376 HOH HOH B . 
X 10 HOH 589 1989 757  HOH HOH B . 
X 10 HOH 590 1990 1368 HOH HOH B . 
X 10 HOH 591 1991 677  HOH HOH B . 
X 10 HOH 592 1992 504  HOH HOH B . 
X 10 HOH 593 1993 1316 HOH HOH B . 
X 10 HOH 594 1994 990  HOH HOH B . 
X 10 HOH 595 1995 916  HOH HOH B . 
X 10 HOH 596 1996 454  HOH HOH B . 
X 10 HOH 597 1997 717  HOH HOH B . 
X 10 HOH 598 1998 1252 HOH HOH B . 
X 10 HOH 599 1999 1358 HOH HOH B . 
X 10 HOH 600 2000 1014 HOH HOH B . 
X 10 HOH 601 2001 1083 HOH HOH B . 
X 10 HOH 602 2002 1275 HOH HOH B . 
X 10 HOH 603 2003 1072 HOH HOH B . 
X 10 HOH 604 2004 1237 HOH HOH B . 
X 10 HOH 605 2005 36   HOH HOH B . 
X 10 HOH 606 2006 1061 HOH HOH B . 
X 10 HOH 607 2007 981  HOH HOH B . 
X 10 HOH 608 2008 1133 HOH HOH B . 
X 10 HOH 609 2009 1000 HOH HOH B . 
X 10 HOH 610 2010 1267 HOH HOH B . 
X 10 HOH 611 2011 1198 HOH HOH B . 
X 10 HOH 612 2012 515  HOH HOH B . 
X 10 HOH 613 2013 1288 HOH HOH B . 
X 10 HOH 614 2014 787  HOH HOH B . 
X 10 HOH 615 2015 726  HOH HOH B . 
X 10 HOH 616 2016 1203 HOH HOH B . 
X 10 HOH 617 2017 583  HOH HOH B . 
X 10 HOH 618 2018 948  HOH HOH B . 
X 10 HOH 619 2019 1348 HOH HOH B . 
X 10 HOH 620 2020 683  HOH HOH B . 
X 10 HOH 621 2021 1226 HOH HOH B . 
X 10 HOH 622 2022 1160 HOH HOH B . 
X 10 HOH 623 2023 750  HOH HOH B . 
X 10 HOH 624 2024 667  HOH HOH B . 
X 10 HOH 625 2025 1124 HOH HOH B . 
X 10 HOH 626 2026 498  HOH HOH B . 
X 10 HOH 627 2027 304  HOH HOH B . 
X 10 HOH 628 2028 881  HOH HOH B . 
X 10 HOH 629 2029 591  HOH HOH B . 
X 10 HOH 630 2030 512  HOH HOH B . 
X 10 HOH 631 2031 146  HOH HOH B . 
X 10 HOH 632 2032 1063 HOH HOH B . 
X 10 HOH 633 2033 640  HOH HOH B . 
X 10 HOH 634 2034 631  HOH HOH B . 
X 10 HOH 635 2035 1372 HOH HOH B . 
X 10 HOH 636 2036 1278 HOH HOH B . 
X 10 HOH 637 2037 918  HOH HOH B . 
X 10 HOH 638 2038 1409 HOH HOH B . 
X 10 HOH 639 2039 736  HOH HOH B . 
X 10 HOH 640 2040 710  HOH HOH B . 
X 10 HOH 641 2041 657  HOH HOH B . 
X 10 HOH 642 2042 1366 HOH HOH B . 
X 10 HOH 643 2043 409  HOH HOH B . 
X 10 HOH 644 2044 738  HOH HOH B . 
X 10 HOH 645 2045 1445 HOH HOH B . 
X 10 HOH 646 2046 1335 HOH HOH B . 
X 10 HOH 647 2047 1239 HOH HOH B . 
X 10 HOH 648 2048 759  HOH HOH B . 
X 10 HOH 649 2049 1205 HOH HOH B . 
X 10 HOH 650 2050 1432 HOH HOH B . 
X 10 HOH 651 2051 1183 HOH HOH B . 
X 10 HOH 652 2052 1169 HOH HOH B . 
X 10 HOH 653 2053 756  HOH HOH B . 
X 10 HOH 654 2054 1026 HOH HOH B . 
X 10 HOH 655 2055 1238 HOH HOH B . 
X 10 HOH 656 2056 1231 HOH HOH B . 
X 10 HOH 657 2057 1260 HOH HOH B . 
X 10 HOH 658 2058 653  HOH HOH B . 
X 10 HOH 659 2059 1037 HOH HOH B . 
X 10 HOH 660 2060 1310 HOH HOH B . 
X 10 HOH 661 2061 725  HOH HOH B . 
X 10 HOH 662 2062 1343 HOH HOH B . 
X 10 HOH 663 2063 1273 HOH HOH B . 
X 10 HOH 664 2064 875  HOH HOH B . 
X 10 HOH 665 2065 1069 HOH HOH B . 
X 10 HOH 666 2066 858  HOH HOH B . 
X 10 HOH 667 2067 1303 HOH HOH B . 
X 10 HOH 668 2068 922  HOH HOH B . 
X 10 HOH 669 2069 1121 HOH HOH B . 
X 10 HOH 670 2070 1385 HOH HOH B . 
X 10 HOH 671 2071 570  HOH HOH B . 
X 10 HOH 672 2072 1030 HOH HOH B . 
X 10 HOH 673 2073 774  HOH HOH B . 
X 10 HOH 674 2074 929  HOH HOH B . 
X 10 HOH 675 2075 1399 HOH HOH B . 
X 10 HOH 676 2076 77   HOH HOH B . 
X 10 HOH 677 2077 1263 HOH HOH B . 
X 10 HOH 678 2078 1338 HOH HOH B . 
X 10 HOH 679 2079 751  HOH HOH B . 
X 10 HOH 680 2080 335  HOH HOH B . 
X 10 HOH 681 2081 513  HOH HOH B . 
X 10 HOH 682 2082 829  HOH HOH B . 
X 10 HOH 683 2083 946  HOH HOH B . 
X 10 HOH 684 2084 891  HOH HOH B . 
X 10 HOH 685 2085 1070 HOH HOH B . 
X 10 HOH 686 2086 1425 HOH HOH B . 
X 10 HOH 687 2087 360  HOH HOH B . 
X 10 HOH 688 2088 1410 HOH HOH B . 
X 10 HOH 689 2089 1318 HOH HOH B . 
X 10 HOH 690 2090 942  HOH HOH B . 
X 10 HOH 691 2091 620  HOH HOH B . 
X 10 HOH 692 2092 760  HOH HOH B . 
X 10 HOH 693 2093 724  HOH HOH B . 
X 10 HOH 694 2094 679  HOH HOH B . 
X 10 HOH 695 2095 853  HOH HOH B . 
X 10 HOH 696 2096 1408 HOH HOH B . 
X 10 HOH 697 2097 1157 HOH HOH B . 
X 10 HOH 698 2098 1092 HOH HOH B . 
X 10 HOH 699 2099 1428 HOH HOH B . 
X 10 HOH 700 2100 1396 HOH HOH B . 
X 10 HOH 701 2101 1150 HOH HOH B . 
X 10 HOH 702 2102 1452 HOH HOH B . 
X 10 HOH 703 2103 1242 HOH HOH B . 
X 10 HOH 704 2104 963  HOH HOH B . 
X 10 HOH 705 2105 1200 HOH HOH B . 
X 10 HOH 706 2106 1175 HOH HOH B . 
X 10 HOH 707 2107 558  HOH HOH B . 
X 10 HOH 708 2108 831  HOH HOH B . 
X 10 HOH 709 2109 709  HOH HOH B . 
X 10 HOH 710 2110 1322 HOH HOH B . 
X 10 HOH 711 2111 1438 HOH HOH B . 
X 10 HOH 712 2112 1363 HOH HOH B . 
X 10 HOH 713 2113 1214 HOH HOH B . 
X 10 HOH 714 2114 1411 HOH HOH B . 
X 10 HOH 715 2115 1164 HOH HOH B . 
X 10 HOH 716 2116 987  HOH HOH B . 
X 10 HOH 717 2117 1193 HOH HOH B . 
X 10 HOH 718 2118 1225 HOH HOH B . 
X 10 HOH 719 2119 1341 HOH HOH B . 
X 10 HOH 720 2120 1195 HOH HOH B . 
X 10 HOH 721 2121 1402 HOH HOH B . 
X 10 HOH 722 2122 727  HOH HOH B . 
X 10 HOH 723 2123 914  HOH HOH B . 
X 10 HOH 724 2124 1251 HOH HOH B . 
X 10 HOH 725 2125 1279 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 LYS 58   ? CG  ? A LYS 60   CG  
2   1 Y 1 A LYS 58   ? CD  ? A LYS 60   CD  
3   1 Y 1 A LYS 58   ? CE  ? A LYS 60   CE  
4   1 Y 1 A LYS 58   ? NZ  ? A LYS 60   NZ  
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 GLU 85   ? CG  ? A GLU 87   CG  
10  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
11  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
12  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
13  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
14  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
15  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
16  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
17  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
18  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
19  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
20  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
21  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
22  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
23  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
24  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
25  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
26  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
27  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
28  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
29  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
30  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
31  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
32  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
33  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
34  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
35  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
36  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
37  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
38  1 Y 1 A ARG 138  ? CG  ? A ARG 140  CG  
39  1 Y 1 A ARG 138  ? CD  ? A ARG 140  CD  
40  1 Y 1 A ARG 138  ? NE  ? A ARG 140  NE  
41  1 Y 1 A ARG 138  ? CZ  ? A ARG 140  CZ  
42  1 Y 1 A ARG 138  ? NH1 ? A ARG 140  NH1 
43  1 Y 1 A ARG 138  ? NH2 ? A ARG 140  NH2 
44  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
45  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
46  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
47  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
48  1 Y 1 A GLU 177  ? CG  ? A GLU 179  CG  
49  1 Y 1 A GLU 177  ? CD  ? A GLU 179  CD  
50  1 Y 1 A GLU 177  ? OE1 ? A GLU 179  OE1 
51  1 Y 1 A GLU 177  ? OE2 ? A GLU 179  OE2 
52  1 Y 1 A ARG 189  ? CG  ? A ARG 191  CG  
53  1 Y 1 A ARG 189  ? CD  ? A ARG 191  CD  
54  1 Y 1 A ARG 189  ? NE  ? A ARG 191  NE  
55  1 Y 1 A ARG 189  ? CZ  ? A ARG 191  CZ  
56  1 Y 1 A ARG 189  ? NH1 ? A ARG 191  NH1 
57  1 Y 1 A ARG 189  ? NH2 ? A ARG 191  NH2 
58  1 Y 1 A GLN 194  ? CG  ? A GLN 196  CG  
59  1 Y 1 A GLN 194  ? CD  ? A GLN 196  CD  
60  1 Y 1 A GLN 194  ? OE1 ? A GLN 196  OE1 
61  1 Y 1 A GLN 194  ? NE2 ? A GLN 196  NE2 
62  1 Y 1 A GLU 199  ? CG  ? A GLU 201  CG  
63  1 Y 1 A GLU 199  ? CD  ? A GLU 201  CD  
64  1 Y 1 A GLU 199  ? OE1 ? A GLU 201  OE1 
65  1 Y 1 A GLU 199  ? OE2 ? A GLU 201  OE2 
66  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
67  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
68  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
69  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
70  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
71  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
72  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
73  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
74  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
75  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
76  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
77  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
78  1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
79  1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
80  1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
81  1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
82  1 Y 1 A GLU 234  ? CG  ? A GLU 236  CG  
83  1 Y 1 A GLU 234  ? CD  ? A GLU 236  CD  
84  1 Y 1 A GLU 234  ? OE1 ? A GLU 236  OE1 
85  1 Y 1 A GLU 234  ? OE2 ? A GLU 236  OE2 
86  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
87  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
88  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
89  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
90  1 Y 1 A MET 452  ? CG  ? A MET 454  CG  
91  1 Y 1 A MET 452  ? SD  ? A MET 454  SD  
92  1 Y 1 A MET 452  ? CE  ? A MET 454  CE  
93  1 Y 1 A GLU 458  ? CG  ? A GLU 460  CG  
94  1 Y 1 A GLU 458  ? CD  ? A GLU 460  CD  
95  1 Y 1 A GLU 458  ? OE1 ? A GLU 460  OE1 
96  1 Y 1 A GLU 458  ? OE2 ? A GLU 460  OE2 
97  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
98  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
99  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
100 1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
101 1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
102 1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
103 1 Y 1 A HIS 479  ? CG  ? A HIS 481  CG  
104 1 Y 1 A HIS 479  ? ND1 ? A HIS 481  ND1 
105 1 Y 1 A HIS 479  ? CD2 ? A HIS 481  CD2 
106 1 Y 1 A HIS 479  ? CE1 ? A HIS 481  CE1 
107 1 Y 1 A HIS 479  ? NE2 ? A HIS 481  NE2 
108 1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
109 1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
110 1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
111 1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
112 1 Y 1 A THR 481  ? OG1 ? A THR 483  OG1 
113 1 Y 1 A THR 481  ? CG2 ? A THR 483  CG2 
114 1 Y 1 A LEU 482  ? CG  ? A LEU 484  CG  
115 1 Y 1 A LEU 482  ? CD1 ? A LEU 484  CD1 
116 1 Y 1 A LEU 482  ? CD2 ? A LEU 484  CD2 
117 1 Y 1 A LEU 483  ? CG  ? A LEU 485  CG  
118 1 Y 1 A LEU 483  ? CD1 ? A LEU 485  CD1 
119 1 Y 1 A LEU 483  ? CD2 ? A LEU 485  CD2 
120 1 Y 1 A TYR 485  ? CG  ? A TYR 487  CG  
121 1 Y 1 A TYR 485  ? CD1 ? A TYR 487  CD1 
122 1 Y 1 A TYR 485  ? CD2 ? A TYR 487  CD2 
123 1 Y 1 A TYR 485  ? CE1 ? A TYR 487  CE1 
124 1 Y 1 A TYR 485  ? CE2 ? A TYR 487  CE2 
125 1 Y 1 A TYR 485  ? CZ  ? A TYR 487  CZ  
126 1 Y 1 A TYR 485  ? OH  ? A TYR 487  OH  
127 1 Y 1 A LEU 486  ? CG  ? A LEU 488  CG  
128 1 Y 1 A LEU 486  ? CD1 ? A LEU 488  CD1 
129 1 Y 1 A LEU 486  ? CD2 ? A LEU 488  CD2 
130 1 Y 1 A VAL 487  ? CG1 ? A VAL 489  CG1 
131 1 Y 1 A VAL 487  ? CG2 ? A VAL 489  CG2 
132 1 Y 1 A ARG 488  ? CG  ? A ARG 490  CG  
133 1 Y 1 A ARG 488  ? CD  ? A ARG 490  CD  
134 1 Y 1 A ARG 488  ? NE  ? A ARG 490  NE  
135 1 Y 1 A ARG 488  ? CZ  ? A ARG 490  CZ  
136 1 Y 1 A ARG 488  ? NH1 ? A ARG 490  NH1 
137 1 Y 1 A ARG 488  ? NH2 ? A ARG 490  NH2 
138 1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
139 1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
140 1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
141 1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
142 1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
143 1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
144 1 Y 1 A LEU 490  ? CG  ? A LEU 492  CG  
145 1 Y 1 A LEU 490  ? CD1 ? A LEU 492  CD1 
146 1 Y 1 A LEU 490  ? CD2 ? A LEU 492  CD2 
147 1 Y 1 A LEU 491  ? CG  ? A LEU 493  CG  
148 1 Y 1 A LEU 491  ? CD1 ? A LEU 493  CD1 
149 1 Y 1 A LEU 491  ? CD2 ? A LEU 493  CD2 
150 1 Y 1 A GLU 492  ? CG  ? A GLU 494  CG  
151 1 Y 1 A GLU 492  ? CD  ? A GLU 494  CD  
152 1 Y 1 A GLU 492  ? OE1 ? A GLU 494  OE1 
153 1 Y 1 A GLU 492  ? OE2 ? A GLU 494  OE2 
154 1 Y 1 A ASN 493  ? CG  ? A ASN 495  CG  
155 1 Y 1 A ASN 493  ? OD1 ? A ASN 495  OD1 
156 1 Y 1 A ASN 493  ? ND2 ? A ASN 495  ND2 
157 1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
158 1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
159 1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
160 1 Y 1 A VAL 500  ? CG1 ? A VAL 502  CG1 
161 1 Y 1 A VAL 500  ? CG2 ? A VAL 502  CG2 
162 1 Y 1 A ILE 503  ? CG1 ? A ILE 505  CG1 
163 1 Y 1 A ILE 503  ? CG2 ? A ILE 505  CG2 
164 1 Y 1 A ILE 503  ? CD1 ? A ILE 505  CD1 
165 1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
166 1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
167 1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
168 1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
169 1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
170 1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
171 1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
172 1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
173 1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
174 1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
175 1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
176 1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
177 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
178 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
179 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
180 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
181 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
182 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
183 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
184 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
185 1 Y 1 A ARG 614  ? CG  ? A ARG 616  CG  
186 1 Y 1 A ARG 614  ? CD  ? A ARG 616  CD  
187 1 Y 1 A ARG 614  ? NE  ? A ARG 616  NE  
188 1 Y 1 A ARG 614  ? CZ  ? A ARG 616  CZ  
189 1 Y 1 A ARG 614  ? NH1 ? A ARG 616  NH1 
190 1 Y 1 A ARG 614  ? NH2 ? A ARG 616  NH2 
191 1 Y 1 A GLN 793  ? CG  ? A GLN 795  CG  
192 1 Y 1 A GLN 793  ? CD  ? A GLN 795  CD  
193 1 Y 1 A GLN 793  ? OE1 ? A GLN 795  OE1 
194 1 Y 1 A GLN 793  ? NE2 ? A GLN 795  NE2 
195 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
196 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
197 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
198 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
199 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
200 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
201 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
202 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
203 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
204 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
205 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
206 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
207 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
208 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
209 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
210 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
211 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
212 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
213 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
214 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
215 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
216 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
217 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
218 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
219 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
220 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
221 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
222 1 Y 1 A ARG 958  ? CG  ? A ARG 960  CG  
223 1 Y 1 A ARG 958  ? CD  ? A ARG 960  CD  
224 1 Y 1 A ARG 958  ? NE  ? A ARG 960  NE  
225 1 Y 1 A ARG 958  ? CZ  ? A ARG 960  CZ  
226 1 Y 1 A ARG 958  ? NH1 ? A ARG 960  NH1 
227 1 Y 1 A ARG 958  ? NH2 ? A ARG 960  NH2 
228 1 Y 1 A LYS 990  ? CG  ? A LYS 992  CG  
229 1 Y 1 A LYS 990  ? CD  ? A LYS 992  CD  
230 1 Y 1 A LYS 990  ? CE  ? A LYS 992  CE  
231 1 Y 1 A LYS 990  ? NZ  ? A LYS 992  NZ  
232 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
233 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
234 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
235 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
236 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
237 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
238 1 Y 1 A ARG 1091 ? CG  ? A ARG 1093 CG  
239 1 Y 1 A ARG 1091 ? CD  ? A ARG 1093 CD  
240 1 Y 1 A ARG 1091 ? NE  ? A ARG 1093 NE  
241 1 Y 1 A ARG 1091 ? CZ  ? A ARG 1093 CZ  
242 1 Y 1 A ARG 1091 ? NH1 ? A ARG 1093 NH1 
243 1 Y 1 A ARG 1091 ? NH2 ? A ARG 1093 NH2 
244 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
245 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
246 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
247 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
248 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
249 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
250 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
251 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
252 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
253 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
254 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
255 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
256 1 Y 1 A MET 1230 ? CG  ? A MET 1232 CG  
257 1 Y 1 A MET 1230 ? SD  ? A MET 1232 SD  
258 1 Y 1 A MET 1230 ? CE  ? A MET 1232 CE  
259 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
260 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
261 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
262 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
263 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
264 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
265 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
266 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
267 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
268 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
269 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
270 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
271 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
272 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
273 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
274 1 Y 1 B ARG 69   ? CG  ? B ARG 71   CG  
275 1 Y 1 B ARG 69   ? CD  ? B ARG 71   CD  
276 1 Y 1 B ARG 69   ? NE  ? B ARG 71   NE  
277 1 Y 1 B ARG 69   ? CZ  ? B ARG 71   CZ  
278 1 Y 1 B ARG 69   ? NH1 ? B ARG 71   NH1 
279 1 Y 1 B ARG 69   ? NH2 ? B ARG 71   NH2 
280 1 Y 1 B LYS 70   ? CG  ? B LYS 72   CG  
281 1 Y 1 B LYS 70   ? CD  ? B LYS 72   CD  
282 1 Y 1 B LYS 70   ? CE  ? B LYS 72   CE  
283 1 Y 1 B LYS 70   ? NZ  ? B LYS 72   NZ  
284 1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
285 1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
286 1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
287 1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
288 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
289 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
290 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
291 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
292 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
293 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
294 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
295 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
296 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
297 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
298 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
299 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
300 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
301 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
302 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
303 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
304 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
305 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
306 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
307 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
308 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
309 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
310 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
311 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
312 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
313 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
314 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
315 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
316 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
317 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
318 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
319 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
320 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
321 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
322 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
323 1 Y 1 B GLU 199  ? CG  ? B GLU 201  CG  
324 1 Y 1 B GLU 199  ? CD  ? B GLU 201  CD  
325 1 Y 1 B GLU 199  ? OE1 ? B GLU 201  OE1 
326 1 Y 1 B GLU 199  ? OE2 ? B GLU 201  OE2 
327 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
328 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
329 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
330 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
331 1 Y 1 B LYS 209  ? CG  ? B LYS 211  CG  
332 1 Y 1 B LYS 209  ? CD  ? B LYS 211  CD  
333 1 Y 1 B LYS 209  ? CE  ? B LYS 211  CE  
334 1 Y 1 B LYS 209  ? NZ  ? B LYS 211  NZ  
335 1 Y 1 B LYS 214  ? CG  ? B LYS 216  CG  
336 1 Y 1 B LYS 214  ? CD  ? B LYS 216  CD  
337 1 Y 1 B LYS 214  ? CE  ? B LYS 216  CE  
338 1 Y 1 B LYS 214  ? NZ  ? B LYS 216  NZ  
339 1 Y 1 B GLU 225  ? CG  ? B GLU 227  CG  
340 1 Y 1 B GLU 225  ? CD  ? B GLU 227  CD  
341 1 Y 1 B GLU 225  ? OE1 ? B GLU 227  OE1 
342 1 Y 1 B GLU 225  ? OE2 ? B GLU 227  OE2 
343 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
344 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
345 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
346 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
347 1 Y 1 B ASP 414  ? CG  ? B ASP 416  CG  
348 1 Y 1 B ASP 414  ? OD1 ? B ASP 416  OD1 
349 1 Y 1 B ASP 414  ? OD2 ? B ASP 416  OD2 
350 1 Y 1 B VAL 415  ? CG1 ? B VAL 417  CG1 
351 1 Y 1 B VAL 415  ? CG2 ? B VAL 417  CG2 
352 1 Y 1 B LYS 443  ? CG  ? B LYS 445  CG  
353 1 Y 1 B LYS 443  ? CD  ? B LYS 445  CD  
354 1 Y 1 B LYS 443  ? CE  ? B LYS 445  CE  
355 1 Y 1 B LYS 443  ? NZ  ? B LYS 445  NZ  
356 1 Y 1 B GLU 458  ? CG  ? B GLU 460  CG  
357 1 Y 1 B GLU 458  ? CD  ? B GLU 460  CD  
358 1 Y 1 B GLU 458  ? OE1 ? B GLU 460  OE1 
359 1 Y 1 B GLU 458  ? OE2 ? B GLU 460  OE2 
360 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
361 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
362 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
363 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
364 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
365 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
366 1 Y 1 B HIS 479  ? CG  ? B HIS 481  CG  
367 1 Y 1 B HIS 479  ? ND1 ? B HIS 481  ND1 
368 1 Y 1 B HIS 479  ? CD2 ? B HIS 481  CD2 
369 1 Y 1 B HIS 479  ? CE1 ? B HIS 481  CE1 
370 1 Y 1 B HIS 479  ? NE2 ? B HIS 481  NE2 
371 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
372 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
373 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
374 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
375 1 Y 1 B LEU 483  ? CG  ? B LEU 485  CG  
376 1 Y 1 B LEU 483  ? CD1 ? B LEU 485  CD1 
377 1 Y 1 B LEU 483  ? CD2 ? B LEU 485  CD2 
378 1 Y 1 B TYR 485  ? CG  ? B TYR 487  CG  
379 1 Y 1 B TYR 485  ? CD1 ? B TYR 487  CD1 
380 1 Y 1 B TYR 485  ? CD2 ? B TYR 487  CD2 
381 1 Y 1 B TYR 485  ? CE1 ? B TYR 487  CE1 
382 1 Y 1 B TYR 485  ? CE2 ? B TYR 487  CE2 
383 1 Y 1 B TYR 485  ? CZ  ? B TYR 487  CZ  
384 1 Y 1 B TYR 485  ? OH  ? B TYR 487  OH  
385 1 Y 1 B LEU 486  ? CG  ? B LEU 488  CG  
386 1 Y 1 B LEU 486  ? CD1 ? B LEU 488  CD1 
387 1 Y 1 B LEU 486  ? CD2 ? B LEU 488  CD2 
388 1 Y 1 B ARG 488  ? CG  ? B ARG 490  CG  
389 1 Y 1 B ARG 488  ? CD  ? B ARG 490  CD  
390 1 Y 1 B ARG 488  ? NE  ? B ARG 490  NE  
391 1 Y 1 B ARG 488  ? CZ  ? B ARG 490  CZ  
392 1 Y 1 B ARG 488  ? NH1 ? B ARG 490  NH1 
393 1 Y 1 B ARG 488  ? NH2 ? B ARG 490  NH2 
394 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
395 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
396 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
397 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
398 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
399 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
400 1 Y 1 B LEU 490  ? CG  ? B LEU 492  CG  
401 1 Y 1 B LEU 490  ? CD1 ? B LEU 492  CD1 
402 1 Y 1 B LEU 490  ? CD2 ? B LEU 492  CD2 
403 1 Y 1 B LEU 491  ? CG  ? B LEU 493  CG  
404 1 Y 1 B LEU 491  ? CD1 ? B LEU 493  CD1 
405 1 Y 1 B LEU 491  ? CD2 ? B LEU 493  CD2 
406 1 Y 1 B GLU 492  ? CG  ? B GLU 494  CG  
407 1 Y 1 B GLU 492  ? CD  ? B GLU 494  CD  
408 1 Y 1 B GLU 492  ? OE1 ? B GLU 494  OE1 
409 1 Y 1 B GLU 492  ? OE2 ? B GLU 494  OE2 
410 1 Y 1 B ASN 493  ? CG  ? B ASN 495  CG  
411 1 Y 1 B ASN 493  ? OD1 ? B ASN 495  OD1 
412 1 Y 1 B ASN 493  ? ND2 ? B ASN 495  ND2 
413 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
414 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
415 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
416 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
417 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
418 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
419 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
420 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
421 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
422 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
423 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
424 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
425 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
426 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
427 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
428 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
429 1 Y 1 B GLU 588  ? CG  ? B GLU 590  CG  
430 1 Y 1 B GLU 588  ? CD  ? B GLU 590  CD  
431 1 Y 1 B GLU 588  ? OE1 ? B GLU 590  OE1 
432 1 Y 1 B GLU 588  ? OE2 ? B GLU 590  OE2 
433 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
434 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
435 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
436 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
437 1 Y 1 B GLN 793  ? CG  ? B GLN 795  CG  
438 1 Y 1 B GLN 793  ? CD  ? B GLN 795  CD  
439 1 Y 1 B GLN 793  ? OE1 ? B GLN 795  OE1 
440 1 Y 1 B GLN 793  ? NE2 ? B GLN 795  NE2 
441 1 Y 1 B GLU 854  ? CG  ? B GLU 856  CG  
442 1 Y 1 B GLU 854  ? CD  ? B GLU 856  CD  
443 1 Y 1 B GLU 854  ? OE1 ? B GLU 856  OE1 
444 1 Y 1 B GLU 854  ? OE2 ? B GLU 856  OE2 
445 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
446 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
447 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
448 1 Y 1 B GLU 917  ? CG  ? B GLU 919  CG  
449 1 Y 1 B GLU 917  ? CD  ? B GLU 919  CD  
450 1 Y 1 B GLU 917  ? OE1 ? B GLU 919  OE1 
451 1 Y 1 B GLU 917  ? OE2 ? B GLU 919  OE2 
452 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
453 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
454 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
455 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
456 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
457 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
458 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
459 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
460 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
461 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
462 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
463 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
464 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
465 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
466 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
467 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
468 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
469 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
470 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
471 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
472 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
473 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
474 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
475 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
476 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
477 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
478 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
479 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
480 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
481 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
482 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
483 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
484 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
485 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
486 1 Y 1 B ASN 1140 ? CG  ? B ASN 1142 CG  
487 1 Y 1 B ASN 1140 ? OD1 ? B ASN 1142 OD1 
488 1 Y 1 B ASN 1140 ? ND2 ? B ASN 1142 ND2 
489 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
490 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
491 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
492 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
493 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
494 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
495 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
496 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21rc1_5156 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .            2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .            4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.50 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9E5W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.848 
_cell.length_a_esd                 ? 
_cell.length_b                     101.967 
_cell.length_b_esd                 ? 
_cell.length_c                     126.567 
_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                         9E5W 
_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                   9E5W 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.97 
_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              8 
_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    
;19% PEG-3350, 0.2 M ammonium sulfate, 0.1 M magnesium chloride, 0.1 M HEPES (pH 8.0), and 0.1 M sodium formate; Cryobuffer: reservoir supplemented with 15 % PEG-200
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            286 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CMOS 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RDI CMOS_8M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-02-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97625 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 4.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   4.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9E5W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               47.00 
_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                                     686872 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.95 
_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                                0.086 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.073 
_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                                    1.52 
_reflns_shell.d_res_low                                     1.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           52980 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             17429 
_reflns_shell.percent_possible_obs                          93.6 
_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                               3.0 
_reflns_shell.pdbx_chi_squared                              0.69 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.7 
_reflns_shell.pdbx_Rrim_I_all                               1.525 
_reflns_shell.pdbx_Rpim_I_all                               0.849 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.377 
_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                                  1.256 
_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                                 9E5W 
_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                            1.52 
_refine.ls_d_res_low                             47.00 
_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                     686872 
_refine.ls_number_reflns_R_free                  33980 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.29 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1916 
_refine.ls_R_factor_R_free                       0.2108 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1906 
_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                          0.85 
_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                 23.10 
_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                            0.20 
_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        17664 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         287 
_refine_hist.number_atoms_solvent             1444 
_refine_hist.number_atoms_total               19395 
_refine_hist.d_res_high                       1.52 
_refine_hist.d_res_low                        47.00 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 18409 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.842  ? 25127 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.448 ? 6644  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 2956  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3272  ? 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' 1.52 1.54  . . 939  18393 78.00 . . . . 0.3276 . . . . . . . . . . . 0.3413 
'X-RAY DIFFRACTION' 1.54 1.56  . . 1068 20279 86.00 . . . . 0.3202 . . . . . . . . . . . 0.3241 
'X-RAY DIFFRACTION' 1.56 1.57  . . 1185 22999 97.00 . . . . 0.3088 . . . . . . . . . . . 0.3310 
'X-RAY DIFFRACTION' 1.57 1.59  . . 1214 22833 97.00 . . . . 0.2978 . . . . . . . . . . . 0.3121 
'X-RAY DIFFRACTION' 1.59 1.62  . . 1124 22661 96.00 . . . . 0.2904 . . . . . . . . . . . 0.3178 
'X-RAY DIFFRACTION' 1.62 1.64  . . 1283 22288 95.00 . . . . 0.2835 . . . . . . . . . . . 0.3161 
'X-RAY DIFFRACTION' 1.64 1.66  . . 1158 22256 94.00 . . . . 0.2768 . . . . . . . . . . . 0.3066 
'X-RAY DIFFRACTION' 1.66 1.69  . . 1039 21924 93.00 . . . . 0.2657 . . . . . . . . . . . 0.2851 
'X-RAY DIFFRACTION' 1.69 1.71  . . 1096 21429 91.00 . . . . 0.2631 . . . . . . . . . . . 0.2860 
'X-RAY DIFFRACTION' 1.71 1.74  . . 1089 20552 88.00 . . . . 0.2715 . . . . . . . . . . . 0.3041 
'X-RAY DIFFRACTION' 1.74 1.77  . . 1096 20775 88.00 . . . . 0.2595 . . . . . . . . . . . 0.2958 
'X-RAY DIFFRACTION' 1.77 1.80  . . 1081 20921 89.00 . . . . 0.2427 . . . . . . . . . . . 0.2832 
'X-RAY DIFFRACTION' 1.80 1.84  . . 1036 21230 90.00 . . . . 0.2296 . . . . . . . . . . . 0.2575 
'X-RAY DIFFRACTION' 1.84 1.87  . . 1088 21287 91.00 . . . . 0.2192 . . . . . . . . . . . 0.2392 
'X-RAY DIFFRACTION' 1.87 1.92  . . 1127 21806 92.00 . . . . 0.2122 . . . . . . . . . . . 0.2305 
'X-RAY DIFFRACTION' 1.92 1.96  . . 1120 22428 95.00 . . . . 0.2131 . . . . . . . . . . . 0.2360 
'X-RAY DIFFRACTION' 1.96 2.01  . . 1123 23154 98.00 . . . . 0.2098 . . . . . . . . . . . 0.2438 
'X-RAY DIFFRACTION' 2.01 2.06  . . 1242 23022 98.00 . . . . 0.2053 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 2.06 2.12  . . 1264 22953 97.00 . . . . 0.1931 . . . . . . . . . . . 0.2111 
'X-RAY DIFFRACTION' 2.12 2.19  . . 1208 22730 97.00 . . . . 0.1877 . . . . . . . . . . . 0.2162 
'X-RAY DIFFRACTION' 2.19 2.27  . . 1118 22484 95.00 . . . . 0.1811 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 2.27 2.36  . . 1157 22413 95.00 . . . . 0.1842 . . . . . . . . . . . 0.2123 
'X-RAY DIFFRACTION' 2.36 2.47  . . 1097 22302 94.00 . . . . 0.1820 . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 2.47 2.60  . . 1111 22015 93.00 . . . . 0.1828 . . . . . . . . . . . 0.2051 
'X-RAY DIFFRACTION' 2.60 2.76  . . 1135 21605 92.00 . . . . 0.1822 . . . . . . . . . . . 0.2051 
'X-RAY DIFFRACTION' 2.76 2.98  . . 1171 21203 90.00 . . . . 0.1858 . . . . . . . . . . . 0.1972 
'X-RAY DIFFRACTION' 2.98 3.27  . . 1093 20907 89.00 . . . . 0.1823 . . . . . . . . . . . 0.1964 
'X-RAY DIFFRACTION' 3.27 3.75  . . 1080 20713 88.00 . . . . 0.1646 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 3.75 4.72  . . 1183 21258 90.00 . . . . 0.1359 . . . . . . . . . . . 0.1584 
'X-RAY DIFFRACTION' 4.72 47.00 . . 1255 22072 94.00 . . . . 0.1495 . . . . . . . . . . . 0.1608 
# 
_struct.entry_id                     9E5W 
_struct.title                        'Proline utilization A (PutA) from Sinorhizobium meliloti inactivated by N-propargylglycine' 
_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        9E5W 
_struct_keywords.text            
'BETA/ALPHA BARREL, FLAVOENZYME, PROLINE CATABOLISM, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1  ? 
B N N 1  ? 
C N N 2  ? 
D N N 3  ? 
E N N 4  ? 
F N N 4  ? 
G N N 4  ? 
H N N 4  ? 
I N N 4  ? 
J N N 5  ? 
K N N 6  ? 
L N N 7  ? 
M N N 7  ? 
N N N 2  ? 
O N N 3  ? 
P N N 4  ? 
Q N N 4  ? 
R N N 5  ? 
S N N 6  ? 
T N N 7  ? 
U N N 8  ? 
V N N 9  ? 
W N N 10 ? 
X N N 10 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q92SD7_RHIME 
_struct_ref.pdbx_db_accession          Q92SD7 
_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 9E5W A 3 ? 1235 ? Q92SD7 1 ? 1233 ? 1 1233 
2 1 9E5W B 3 ? 1235 ? Q92SD7 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 9E5W SER A 1 ? UNP Q92SD7 ? ? 'expression tag' -1 1 
1 9E5W MET A 2 ? UNP Q92SD7 ? ? 'expression tag' 0  2 
2 9E5W SER B 1 ? UNP Q92SD7 ? ? 'expression tag' -1 3 
2 9E5W MET B 2 ? UNP Q92SD7 ? ? '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)' 8990  ? 
1 MORE         -133  ? 
1 'SSA (A^2)'  78650 ? 
# 
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 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,W                       
3 1 B,N,O,P,Q,R,S,T,U,V,X                           
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 SER A 31   ? ALA A 40   ? SER A 29   ALA A 38   1 ? 10 
HELX_P HELX_P2   AA2 PRO A 44   ? ALA A 56   ? PRO A 42   ALA A 54   1 ? 13 
HELX_P HELX_P3   AA3 SER A 59   ? GLY A 79   ? SER A 57   GLY A 77   1 ? 21 
HELX_P HELX_P4   AA4 VAL A 86   ? TYR A 93   ? VAL A 84   TYR A 91   1 ? 8  
HELX_P HELX_P5   AA5 SER A 96   ? ARG A 112  ? SER A 94   ARG A 110  1 ? 17 
HELX_P HELX_P6   AA6 ASP A 115  ? LYS A 126  ? ASP A 113  LYS A 124  1 ? 12 
HELX_P HELX_P7   AA7 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  ? GLU A 215  ? THR A 200  GLU A 213  1 ? 14 
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  ? LEU A 485  ? THR A 478  LEU A 483  1 ? 6  
HELX_P HELX_P24  AC6 LEU A 488  ? ASN A 495  ? LEU A 486  ASN A 493  1 ? 8  
HELX_P HELX_P25  AC7 SER A 500  ? ASP A 507  ? SER A 498  ASP A 505  1 ? 8  
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 ASN A 557  ? ALA A 573  ? ASN A 555  ALA A 571  1 ? 17 
HELX_P HELX_P30  AD3 SER A 611  ? ALA A 631  ? SER A 609  ALA A 629  1 ? 21 
HELX_P HELX_P31  AD4 PRO A 633  ? ARG A 651  ? PRO A 631  ARG A 649  1 ? 19 
HELX_P HELX_P32  AD5 ARG A 651  ? GLY A 664  ? ARG A 649  GLY A 662  1 ? 14 
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 ? GLY A 1063 ? ASP A 1047 GLY A 1061 1 ? 15 
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 ASN B 131  ? LEU B 136  ? ASN B 129  LEU B 134  1 ? 6  
HELX_P HELX_P67  AH4 GLY B 137  ? PHE B 143  ? GLY B 135  PHE B 141  1 ? 7  
HELX_P HELX_P68  AH5 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P69  AH6 ASN B 162  ? GLN B 196  ? ASN B 160  GLN B 194  1 ? 35 
HELX_P HELX_P70  AH7 THR B 202  ? GLY B 217  ? THR B 200  GLY B 215  1 ? 16 
HELX_P HELX_P71  AH8 THR B 231  ? ALA B 254  ? THR B 229  ALA B 252  1 ? 24 
HELX_P HELX_P72  AH9 ARG B 256  ? GLY B 261  ? ARG B 254  GLY B 259  1 ? 6  
HELX_P HELX_P73  AI1 LYS B 267  ? LEU B 271  ? LYS B 265  LEU B 269  5 ? 5  
HELX_P HELX_P74  AI2 SER B 276  ? ALA B 278  ? SER B 274  ALA B 276  5 ? 3  
HELX_P HELX_P75  AI3 GLN B 279  ? ASP B 302  ? GLN B 277  ASP B 300  1 ? 24 
HELX_P HELX_P76  AI4 GLU B 311  ? ASP B 313  ? GLU B 309  ASP B 311  5 ? 3  
HELX_P HELX_P77  AI5 ARG B 314  ? 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  ? ASP B 386  ? TYR B 373  ASP B 384  1 ? 12 
HELX_P HELX_P81  AI9 ARG B 396  ? ALA B 413  ? ARG B 394  ALA B 411  1 ? 18 
HELX_P HELX_P82  AJ1 ASN B 426  ? 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  ? LEU B 485  ? THR B 478  LEU B 483  1 ? 6  
HELX_P HELX_P85  AJ4 TYR B 487  ? ALA B 497  ? TYR B 485  ALA B 495  1 ? 11 
HELX_P HELX_P86  AJ5 SER B 500  ? ILE B 505  ? SER B 498  ILE B 503  1 ? 6  
HELX_P HELX_P87  AJ6 SER B 511  ? ILE B 516  ? SER B 509  ILE B 514  1 ? 6  
HELX_P HELX_P88  AJ7 ASP B 518  ? ALA B 525  ? ASP B 516  ALA B 523  1 ? 8  
HELX_P HELX_P89  AJ8 LEU B 538  ? LEU B 542  ? LEU B 536  LEU B 540  5 ? 5  
HELX_P HELX_P90  AJ9 PHE B 543  ? ARG B 547  ? PHE B 541  ARG B 545  5 ? 5  
HELX_P HELX_P91  AK1 ASN B 557  ? ALA B 573  ? ASN B 555  ALA B 571  1 ? 17 
HELX_P HELX_P92  AK2 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P93  AK3 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P94  AK4 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P95  AK5 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P96  AK6 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P97  AK7 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P98  AK8 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P99  AK9 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P100 AL1 SER B 785  ? ASP B 798  ? SER B 783  ASP B 796  1 ? 14 
HELX_P HELX_P101 AL2 LEU B 826  ? ASP B 840  ? LEU B 824  ASP B 838  1 ? 15 
HELX_P HELX_P102 AL3 SER B 841  ? GLN B 844  ? SER B 839  GLN B 842  5 ? 4  
HELX_P HELX_P103 AL4 GLU B 856  ? HIS B 871  ? GLU B 854  HIS B 869  1 ? 16 
HELX_P HELX_P104 AL5 THR B 890  ? LEU B 907  ? THR B 888  LEU B 905  1 ? 18 
HELX_P HELX_P105 AL6 ALA B 917  ? GLY B 923  ? ALA B 915  GLY B 921  5 ? 7  
HELX_P HELX_P106 AL7 LYS B 935  ? LEU B 939  ? LYS B 933  LEU B 937  5 ? 5  
HELX_P HELX_P107 AL8 ARG B 954  ? ASP B 956  ? ARG B 952  ASP B 954  5 ? 3  
HELX_P HELX_P108 AL9 ASP B 957  ? ALA B 967  ? ASP B 955  ALA B 965  1 ? 11 
HELX_P HELX_P109 AM1 LEU B 980  ? ILE B 991  ? LEU B 978  ILE B 989  1 ? 12 
HELX_P HELX_P110 AM2 ARG B 1015 ? GLY B 1019 ? ARG B 1013 GLY B 1017 5 ? 5  
HELX_P HELX_P111 AM3 TYR B 1029 ? VAL B 1034 ? TYR B 1027 VAL B 1032 5 ? 6  
HELX_P HELX_P112 AM4 ASP B 1049 ? LYS B 1062 ? ASP B 1047 LYS B 1060 1 ? 14 
HELX_P HELX_P113 AM5 ALA B 1064 ? SER B 1078 ? ALA B 1062 SER B 1076 1 ? 15 
HELX_P HELX_P114 AM6 THR B 1110 ? THR B 1124 ? THR B 1108 THR B 1122 1 ? 15 
HELX_P HELX_P115 AM7 ALA B 1133 ? GLY B 1135 ? ALA B 1131 GLY B 1133 5 ? 3  
HELX_P HELX_P116 AM8 LEU B 1136 ? LYS B 1141 ? LEU B 1134 LYS B 1139 5 ? 6  
HELX_P HELX_P117 AM9 PRO B 1144 ? LEU B 1149 ? PRO B 1142 LEU B 1147 1 ? 6  
HELX_P HELX_P118 AN1 ASP B 1156 ? GLY B 1161 ? ASP B 1154 GLY B 1159 1 ? 6  
HELX_P HELX_P119 AN2 ASP B 1171 ? ALA B 1184 ? ASP B 1169 ALA B 1182 1 ? 14 
HELX_P HELX_P120 AN3 SER B 1196 ? ASN B 1203 ? SER B 1194 ASN B 1201 1 ? 8  
HELX_P HELX_P121 AN4 CYS B 1208 ? TRP B 1211 ? CYS B 1206 TRP B 1209 5 ? 4  
# 
_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 
covale1  covale one ? A LYS 267 NZ  ? ? ? 1_555 C P5F . C23 ? ? A LYS 265  A P5F 1301 1_555 ? ? ? ? ? ? ? 1.358 doub ? 
covale2  covale one ? B LYS 267 NZ  ? ? ? 1_555 N P5F . C23 ? ? B LYS 265  B P5F 1301 1_555 ? ? ? ? ? ? ? 1.325 doub ? 
metalc1  metalc ?   ? D NAD .   O2A ? ? ? 1_555 J MG  . MG  ? ? A NAD 1302 A MG  1308 1_555 ? ? ? ? ? ? ? 2.046 ?    ? 
metalc2  metalc ?   ? J MG  .   MG  ? ? ? 1_555 W HOH . O   ? ? A MG  1308 A HOH 1432 1_555 ? ? ? ? ? ? ? 1.900 ?    ? 
metalc3  metalc ?   ? J MG  .   MG  ? ? ? 1_555 W HOH . O   ? ? A MG  1308 A HOH 1439 1_555 ? ? ? ? ? ? ? 2.054 ?    ? 
metalc4  metalc ?   ? J MG  .   MG  ? ? ? 1_555 W HOH . O   ? ? A MG  1308 A HOH 1831 1_555 ? ? ? ? ? ? ? 2.038 ?    ? 
metalc5  metalc ?   ? J MG  .   MG  ? ? ? 1_555 W HOH . O   ? ? A MG  1308 A HOH 1838 1_555 ? ? ? ? ? ? ? 2.117 ?    ? 
metalc6  metalc ?   ? J MG  .   MG  ? ? ? 1_555 W HOH . O   ? ? A MG  1308 A HOH 2034 1_555 ? ? ? ? ? ? ? 2.128 ?    ? 
metalc7  metalc ?   ? O NAD .   O2A ? ? ? 1_555 R MG  . MG  ? ? B NAD 1302 B MG  1305 1_555 ? ? ? ? ? ? ? 2.096 ?    ? 
metalc8  metalc ?   ? R MG  .   MG  ? ? ? 1_555 X HOH . O   ? ? B MG  1305 B HOH 1481 1_555 ? ? ? ? ? ? ? 1.823 ?    ? 
metalc9  metalc ?   ? R MG  .   MG  ? ? ? 1_555 X HOH . O   ? ? B MG  1305 B HOH 1766 1_555 ? ? ? ? ? ? ? 2.363 ?    ? 
metalc10 metalc ?   ? R MG  .   MG  ? ? ? 1_555 X HOH . O   ? ? B MG  1305 B HOH 1775 1_555 ? ? ? ? ? ? ? 2.018 ?    ? 
metalc11 metalc ?   ? R MG  .   MG  ? ? ? 1_555 X HOH . O   ? ? B MG  1305 B HOH 1903 1_555 ? ? ? ? ? ? ? 2.385 ?    ? 
metalc12 metalc ?   ? R MG  .   MG  ? ? ? 1_555 X HOH . O   ? ? B MG  1305 B HOH 2035 1_555 ? ? ? ? ? ? ? 2.000 ?    ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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 ? D NAD . ? A NAD 1302 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1432 ? 1_555 80.5  ? 
2  O2A ? D NAD . ? A NAD 1302 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1439 ? 1_555 88.4  ? 
3  O   ? W HOH . ? A HOH 1432 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1439 ? 1_555 92.2  ? 
4  O2A ? D NAD . ? A NAD 1302 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1831 ? 1_555 88.6  ? 
5  O   ? W HOH . ? A HOH 1432 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1831 ? 1_555 92.1  ? 
6  O   ? W HOH . ? A HOH 1439 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1831 ? 1_555 174.3 ? 
7  O2A ? D NAD . ? A NAD 1302 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1838 ? 1_555 95.6  ? 
8  O   ? W HOH . ? A HOH 1432 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1838 ? 1_555 170.8 ? 
9  O   ? W HOH . ? A HOH 1439 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1838 ? 1_555 96.1  ? 
10 O   ? W HOH . ? A HOH 1831 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 1838 ? 1_555 79.4  ? 
11 O2A ? D NAD . ? A NAD 1302 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 2034 ? 1_555 172.1 ? 
12 O   ? W HOH . ? A HOH 1432 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 2034 ? 1_555 93.2  ? 
13 O   ? W HOH . ? A HOH 1439 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 2034 ? 1_555 87.0  ? 
14 O   ? W HOH . ? A HOH 1831 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 2034 ? 1_555 96.5  ? 
15 O   ? W HOH . ? A HOH 1838 ? 1_555 MG ? J MG . ? A MG 1308 ? 1_555 O ? W HOH . ? A HOH 2034 ? 1_555 91.3  ? 
16 O2A ? O NAD . ? B NAD 1302 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1481 ? 1_555 100.2 ? 
17 O2A ? O NAD . ? B NAD 1302 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1766 ? 1_555 77.5  ? 
18 O   ? X HOH . ? B HOH 1481 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1766 ? 1_555 154.5 ? 
19 O2A ? O NAD . ? B NAD 1302 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1775 ? 1_555 94.2  ? 
20 O   ? X HOH . ? B HOH 1481 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1775 ? 1_555 129.4 ? 
21 O   ? X HOH . ? B HOH 1766 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1775 ? 1_555 76.0  ? 
22 O2A ? O NAD . ? B NAD 1302 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1903 ? 1_555 80.9  ? 
23 O   ? X HOH . ? B HOH 1481 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1903 ? 1_555 87.4  ? 
24 O   ? X HOH . ? B HOH 1766 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1903 ? 1_555 67.1  ? 
25 O   ? X HOH . ? B HOH 1775 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 1903 ? 1_555 143.0 ? 
26 O2A ? O NAD . ? B NAD 1302 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 2035 ? 1_555 152.5 ? 
27 O   ? X HOH . ? B HOH 1481 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 2035 ? 1_555 97.7  ? 
28 O   ? X HOH . ? B HOH 1766 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 2035 ? 1_555 77.3  ? 
29 O   ? X HOH . ? B HOH 1775 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 2035 ? 1_555 90.2  ? 
30 O   ? X HOH . ? B HOH 1903 ? 1_555 MG ? R MG . ? B MG 1305 ? 1_555 O ? X HOH . ? B HOH 2035 ? 1_555 79.3  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 P5F C . ? LYS A 267 ? P5F A 1301 ? 1_555 LYS A 265 ? 1_555 C23 NZ LYS 1 P5F None 'Covalent chemical modification' 
2 P5F N . ? LYS B 267 ? P5F B 1301 ? 1_555 LYS B 265 ? 1_555 C23 NZ LYS 1 P5F None 'Covalent chemical modification' 
# 
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 -1.33 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 3.73  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -4.55 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 6.07  
# 
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  ? MET A 224  ? PHE A 216  MET A 222  
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  ? VAL A 478  ? CYS A 470  VAL A 476  
AA1 9  PHE A 218  ? MET A 224  ? PHE A 216  MET A 222  
AA2 1  TRP A 576  ? ALA A 578  ? TRP A 574  ALA A 576  
AA2 2  ASP A 599  ? GLU A 609  ? ASP A 597  GLU A 607  
AA2 3  GLU A 590  ? ASN A 596  ? GLU A 588  ASN A 594  
AA3 1  GLN A 581  ? LEU A 582  ? GLN A 579  LEU A 580  
AA3 2  GLY A 585  ? PRO A 586  ? GLY A 583  PRO A 584  
AA4 1  LEU A 758  ? LEU A 760  ? LEU A 756  LEU A 758  
AA4 2  VAL A 729  ? LYS A 732  ? VAL A 727  LYS A 730  
AA4 3  ILE A 702  ? ILE A 705  ? ILE A 700  ILE A 703  
AA4 4  GLY A 779  ? THR A 783  ? GLY A 777  THR A 781  
AA4 5  LEU A 809  ? GLU A 812  ? LEU A 807  GLU A 810  
AA5 1  VAL A 911  ? GLN A 913  ? VAL A 909  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  GLY A 1165 ? GLU A 1169 ? GLY A 1163 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  SER B 219  ? MET B 224  ? SER B 217  MET B 222  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  LEU B 305  ? ILE B 307  ? LEU B 303  ILE B 305  
AA7 4  MET B 337  ? GLN B 342  ? MET B 335  GLN B 340  
AA7 5  ILE B 366  ? VAL B 371  ? ILE B 364  VAL B 369  
AA7 6  VAL B 418  ? ALA B 423  ? VAL B 416  ALA B 421  
AA7 7  GLU B 447  ? LEU B 451  ? GLU B 445  LEU B 449  
AA7 8  CYS B 472  ? VAL B 478  ? CYS B 470  VAL B 476  
AA7 9  SER B 219  ? MET B 224  ? SER B 217  MET B 222  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? GLU B 609  ? ASP B 597  GLU B 607  
AA8 3  GLU B 590  ? ASN B 596  ? GLU B 588  ASN B 594  
AA9 1  GLN B 581  ? LEU B 582  ? GLN B 579  LEU B 580  
AA9 2  GLY B 585  ? PRO B 586  ? GLY B 583  PRO B 584  
AB1 1  LEU B 758  ? LEU B 760  ? LEU B 756  LEU B 758  
AB1 2  VAL B 729  ? LYS B 732  ? VAL B 727  LYS B 730  
AB1 3  ILE B 702  ? ILE B 705  ? ILE B 700  ILE B 703  
AB1 4  GLY B 779  ? THR B 783  ? GLY B 777  THR B 781  
AB1 5  LEU B 809  ? GLU B 812  ? LEU B 807  GLU B 810  
AB2 1  VAL B 911  ? GLN B 913  ? VAL B 909  GLN B 911  
AB2 2  THR B 929  ? GLU B 932  ? THR B 927  GLU B 930  
AB2 3  VAL B 947  ? TYR B 953  ? VAL B 945  TYR B 951  
AB2 4  LEU B 849  ? GLN B 855  ? LEU B 847  GLN B 853  
AB2 5  ASN B 817  ? VAL B 821  ? ASN B 815  VAL B 819  
AB2 6  THR B 973  ? HIS B 977  ? THR B 971  HIS B 975  
AB2 7  ASN B 995  ? ILE B 998  ? ASN B 993  ILE B 996  
AB2 8  VAL B 1213 ? ASN B 1221 ? VAL B 1211 ASN B 1219 
AB2 9  GLU B 1092 ? ALA B 1100 ? GLU B 1090 ALA B 1098 
AB2 10 ASP B 1083 ? LEU B 1086 ? ASP B 1081 LEU B 1084 
AB3 1  VAL B 1151 ? SER B 1154 ? VAL B 1149 SER B 1152 
AB3 2  SER B 1127 ? ASP B 1131 ? SER B 1125 ASP B 1129 
AB3 3  ARG B 1103 ? VAL B 1107 ? ARG B 1101 VAL B 1105 
AB3 4  ALA B 1166 ? GLU B 1169 ? ALA B 1164 GLU B 1167 
AB3 5  VAL B 1192 ? ALA B 1195 ? VAL B 1190 ALA B 1193 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N TYR A 222  ? N TYR A 220  O SER A 265  ? O SER A 263  
AA1 2 3  N ILE A 266  ? N ILE A 264  O ASN A 306  ? O ASN A 304  
AA1 3 4  N LEU A 305  ? N LEU A 303  O GLY A 338  ? O GLY A 336  
AA1 4 5  N PHE A 339  ? N PHE A 337  O MET A 367  ? O MET A 365  
AA1 5 6  N ILE A 366  ? N ILE A 364  O PHE A 419  ? O PHE A 417  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O GLU A 609  ? O GLU A 607  N GLU A 590  ? N GLU A 588  
AA3 1 2  N LEU A 582  ? N LEU A 580  O GLY A 585  ? O GLY A 583  
AA4 1 2  O GLN A 759  ? O GLN A 757  N ALA A 731  ? N ALA A 729  
AA4 2 3  O LYS A 732  ? O LYS A 730  N CYS A 704  ? N CYS A 702  
AA4 3 4  N ILE A 705  ? N ILE A 703  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O ALA A 1218 ? O ALA A 1216 N LEU A 1095 ? N LEU A 1093 
AA5 9 10 O TYR A 1096 ? O TYR A 1094 N LEU A 1084 ? N LEU A 1082 
AA6 1 2  O SER A 1152 ? O SER A 1150 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O 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                   9E5W 
_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   Y 
# 
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 GLU 539  ? ? O B HOH 1401 ? ? 2.10 
2 1 O   A LEU 1183 ? ? O A HOH 1401 ? ? 2.13 
# 
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   ? ? -162.14 56.09   
2  1 LYS A 124  ? ? -120.48 -54.59  
3  1 GLU A 308  ? ? -120.91 -134.10 
4  1 VAL A 460  ? ? -120.20 -53.25  
5  1 LYS A 465  ? ? -121.44 -123.20 
6  1 TYR A 485  ? ? -146.75 48.57   
7  1 ASP A 597  ? ? -172.93 96.25   
8  1 THR A 689  ? ? -130.18 -44.97  
9  1 THR A 811  ? ? -126.56 -153.60 
10 1 GLN A 842  ? ? -94.19  51.76   
11 1 LEU A 970  ? ? -98.11  -87.16  
12 1 ALA A 1003 ? A -142.31 36.14   
13 1 GLN A 1008 ? ? -117.54 78.24   
14 1 ALA B 22   ? ? -156.89 61.07   
15 1 LYS B 124  ? ? -134.77 -40.17  
16 1 ASP B 127  ? ? -87.31  30.35   
17 1 ASN B 129  ? ? -67.51  55.96   
18 1 GLU B 308  ? ? -120.06 -134.58 
19 1 VAL B 460  ? ? -125.89 -55.87  
20 1 LYS B 465  ? ? -118.30 -129.44 
21 1 LEU B 483  ? ? -62.95  3.85    
22 1 ALA B 484  ? ? -69.20  -116.16 
23 1 TYR B 485  ? ? -70.80  39.32   
24 1 GLU B 492  ? ? -79.63  38.64   
25 1 ASN B 493  ? ? -152.55 -40.55  
26 1 PRO B 578  ? ? -68.26  98.91   
27 1 ASP B 597  ? ? -170.56 97.17   
28 1 THR B 689  ? ? -130.52 -46.07  
29 1 HIS B 694  ? ? -101.15 77.14   
30 1 THR B 811  ? ? -125.85 -151.49 
31 1 GLN B 842  ? ? -94.06  53.34   
32 1 LEU B 970  ? ? -98.56  -87.00  
33 1 GLN B 1008 ? ? -115.67 79.53   
34 1 VAL B 1105 ? ? -119.68 79.70   
35 1 ASP B 1154 ? ? -157.73 88.33   
# 
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 -26.0230 66.6059 93.2357 0.1547 ? 0.0172 ? 0.0145 ? 0.1197 ? 0.0031  ? 0.1263 ? 0.7250 ? -0.0222 ? 
0.2198 ? 0.1080 ? -0.0272 ? 0.1933 ? -0.0426 ? -0.1033 ? 0.0187  ? 0.0289 ? 0.0369 ? 0.0146  ? -0.0252 ? -0.0284 ? 0.0029  ? 
2 'X-RAY DIFFRACTION' ? refined 5.7267   31.9757 91.4602 0.1123 ? 0.0013 ? 0.0051 ? 0.1332 ? -0.0180 ? 0.1173 ? 0.1996 ? -0.0012 ? 
0.1017 ? 0.2451 ? -0.0825 ? 0.4613 ? 0.0132  ? -0.0363 ? -0.0047 ? 0.0492 ? 0.0108 ? -0.0019 ? 0.0376  ? -0.1001 ? -0.0273 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'chain A and peptide' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain B and peptide' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER -1   ? A SER 1    
2  1 Y 1 A MET 0    ? A MET 2    
3  1 Y 1 A MET 1    ? A MET 3    
4  1 Y 1 A SER 2    ? A SER 4    
5  1 Y 1 A PRO 3    ? A PRO 5    
6  1 Y 1 A ASN 4    ? A ASN 6    
7  1 Y 1 A PRO 5    ? A PRO 7    
8  1 Y 1 A LEU 6    ? A LEU 8    
9  1 Y 1 A GLN 7    ? A GLN 9    
10 1 Y 1 A LYS 8    ? A LYS 10   
11 1 Y 1 A PRO 9    ? A PRO 11   
12 1 Y 1 A ALA 10   ? A ALA 12   
13 1 Y 1 A ILE 11   ? A ILE 13   
14 1 Y 1 A ASP 12   ? A ASP 14   
15 1 Y 1 A ALA 13   ? A ALA 15   
16 1 Y 1 A HIS 79   ? A HIS 81   
17 1 Y 1 A SER 80   ? A SER 82   
18 1 Y 1 A GLY 81   ? A GLY 83   
19 1 Y 1 A SER 82   ? A SER 84   
20 1 Y 1 A GLY 135  ? A GLY 137  
21 1 Y 1 A GLY 136  ? A GLY 138  
22 1 Y 1 A ILE 1232 ? A ILE 1234 
23 1 Y 1 A GLY 1233 ? A GLY 1235 
24 1 Y 1 B SER -1   ? B SER 1    
25 1 Y 1 B MET 0    ? B MET 2    
26 1 Y 1 B MET 1    ? B MET 3    
27 1 Y 1 B SER 2    ? B SER 4    
28 1 Y 1 B PRO 3    ? B PRO 5    
29 1 Y 1 B ASN 4    ? B ASN 6    
30 1 Y 1 B PRO 5    ? B PRO 7    
31 1 Y 1 B LEU 6    ? B LEU 8    
32 1 Y 1 B GLN 7    ? B GLN 9    
33 1 Y 1 B LYS 8    ? B LYS 10   
34 1 Y 1 B PRO 9    ? B PRO 11   
35 1 Y 1 B ALA 10   ? B ALA 12   
36 1 Y 1 B ILE 11   ? B ILE 13   
37 1 Y 1 B ASP 12   ? B ASP 14   
38 1 Y 1 B ALA 13   ? B ALA 15   
39 1 Y 1 B HIS 79   ? B HIS 81   
40 1 Y 1 B SER 80   ? B SER 82   
41 1 Y 1 B GLY 81   ? B GLY 83   
42 1 Y 1 B SER 82   ? B SER 84   
43 1 Y 1 B GLY 436  ? B GLY 438  
44 1 Y 1 B LYS 437  ? B LYS 439  
45 1 Y 1 B ASP 438  ? B ASP 440  
46 1 Y 1 B ALA 1223 ? B ALA 1225 
47 1 Y 1 B GLY 1224 ? B GLY 1226 
48 1 Y 1 B GLY 1225 ? B GLY 1227 
49 1 Y 1 B ASN 1226 ? B ASN 1228 
50 1 Y 1 B ALA 1227 ? B ALA 1229 
51 1 Y 1 B SER 1228 ? B SER 1230 
52 1 Y 1 B LEU 1229 ? B LEU 1231 
53 1 Y 1 B MET 1230 ? B MET 1232 
54 1 Y 1 B ALA 1231 ? B ALA 1233 
55 1 Y 1 B ILE 1232 ? B ILE 1234 
56 1 Y 1 B GLY 1233 ? B GLY 1235 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N     N  N N 1   
ALA CA    C  N S 2   
ALA C     C  N N 3   
ALA O     O  N N 4   
ALA CB    C  N N 5   
ALA OXT   O  N N 6   
ALA H     H  N N 7   
ALA H2    H  N N 8   
ALA HA    H  N N 9   
ALA HB1   H  N N 10  
ALA HB2   H  N N 11  
ALA HB3   H  N N 12  
ALA HXT   H  N N 13  
ARG N     N  N N 14  
ARG CA    C  N S 15  
ARG C     C  N N 16  
ARG O     O  N N 17  
ARG CB    C  N N 18  
ARG CG    C  N N 19  
ARG CD    C  N N 20  
ARG NE    N  N N 21  
ARG CZ    C  N N 22  
ARG NH1   N  N N 23  
ARG NH2   N  N N 24  
ARG OXT   O  N N 25  
ARG H     H  N N 26  
ARG H2    H  N N 27  
ARG HA    H  N N 28  
ARG HB2   H  N N 29  
ARG HB3   H  N N 30  
ARG HG2   H  N N 31  
ARG HG3   H  N N 32  
ARG HD2   H  N N 33  
ARG HD3   H  N N 34  
ARG HE    H  N N 35  
ARG HH11  H  N N 36  
ARG HH12  H  N N 37  
ARG HH21  H  N N 38  
ARG HH22  H  N N 39  
ARG HXT   H  N N 40  
ASN N     N  N N 41  
ASN CA    C  N S 42  
ASN C     C  N N 43  
ASN O     O  N N 44  
ASN CB    C  N N 45  
ASN CG    C  N N 46  
ASN OD1   O  N N 47  
ASN ND2   N  N N 48  
ASN OXT   O  N N 49  
ASN H     H  N N 50  
ASN H2    H  N N 51  
ASN HA    H  N N 52  
ASN HB2   H  N N 53  
ASN HB3   H  N N 54  
ASN HD21  H  N N 55  
ASN HD22  H  N N 56  
ASN HXT   H  N N 57  
ASP N     N  N N 58  
ASP CA    C  N S 59  
ASP C     C  N N 60  
ASP O     O  N N 61  
ASP CB    C  N N 62  
ASP CG    C  N N 63  
ASP OD1   O  N N 64  
ASP OD2   O  N N 65  
ASP OXT   O  N N 66  
ASP H     H  N N 67  
ASP H2    H  N N 68  
ASP HA    H  N N 69  
ASP HB2   H  N N 70  
ASP HB3   H  N N 71  
ASP HD2   H  N N 72  
ASP HXT   H  N N 73  
CYS N     N  N N 74  
CYS CA    C  N R 75  
CYS C     C  N N 76  
CYS O     O  N N 77  
CYS CB    C  N N 78  
CYS SG    S  N N 79  
CYS OXT   O  N N 80  
CYS H     H  N N 81  
CYS H2    H  N N 82  
CYS HA    H  N N 83  
CYS HB2   H  N N 84  
CYS HB3   H  N N 85  
CYS HG    H  N N 86  
CYS HXT   H  N N 87  
FMT C     C  N N 88  
FMT O1    O  N N 89  
FMT O2    O  N N 90  
FMT H     H  N N 91  
FMT HO2   H  N N 92  
GLN N     N  N N 93  
GLN CA    C  N S 94  
GLN C     C  N N 95  
GLN O     O  N N 96  
GLN CB    C  N N 97  
GLN CG    C  N N 98  
GLN CD    C  N N 99  
GLN OE1   O  N N 100 
GLN NE2   N  N N 101 
GLN OXT   O  N N 102 
GLN H     H  N N 103 
GLN H2    H  N N 104 
GLN HA    H  N N 105 
GLN HB2   H  N N 106 
GLN HB3   H  N N 107 
GLN HG2   H  N N 108 
GLN HG3   H  N N 109 
GLN HE21  H  N N 110 
GLN HE22  H  N N 111 
GLN HXT   H  N N 112 
GLU N     N  N N 113 
GLU CA    C  N S 114 
GLU C     C  N N 115 
GLU O     O  N N 116 
GLU CB    C  N N 117 
GLU CG    C  N N 118 
GLU CD    C  N N 119 
GLU OE1   O  N N 120 
GLU OE2   O  N N 121 
GLU OXT   O  N N 122 
GLU H     H  N N 123 
GLU H2    H  N N 124 
GLU HA    H  N N 125 
GLU HB2   H  N N 126 
GLU HB3   H  N N 127 
GLU HG2   H  N N 128 
GLU HG3   H  N N 129 
GLU HE2   H  N N 130 
GLU HXT   H  N N 131 
GLY N     N  N N 132 
GLY CA    C  N N 133 
GLY C     C  N N 134 
GLY O     O  N N 135 
GLY OXT   O  N N 136 
GLY H     H  N N 137 
GLY H2    H  N N 138 
GLY HA2   H  N N 139 
GLY HA3   H  N N 140 
GLY HXT   H  N N 141 
HIS N     N  N N 142 
HIS CA    C  N S 143 
HIS C     C  N N 144 
HIS O     O  N N 145 
HIS CB    C  N N 146 
HIS CG    C  Y N 147 
HIS ND1   N  Y N 148 
HIS CD2   C  Y N 149 
HIS CE1   C  Y N 150 
HIS NE2   N  Y N 151 
HIS OXT   O  N N 152 
HIS H     H  N N 153 
HIS H2    H  N N 154 
HIS HA    H  N N 155 
HIS HB2   H  N N 156 
HIS HB3   H  N N 157 
HIS HD1   H  N N 158 
HIS HD2   H  N N 159 
HIS HE1   H  N N 160 
HIS HE2   H  N N 161 
HIS HXT   H  N N 162 
HOH O     O  N N 163 
HOH H1    H  N N 164 
HOH H2    H  N N 165 
ILE N     N  N N 166 
ILE CA    C  N S 167 
ILE C     C  N N 168 
ILE O     O  N N 169 
ILE CB    C  N S 170 
ILE CG1   C  N N 171 
ILE CG2   C  N N 172 
ILE CD1   C  N N 173 
ILE OXT   O  N N 174 
ILE H     H  N N 175 
ILE H2    H  N N 176 
ILE HA    H  N N 177 
ILE HB    H  N N 178 
ILE HG12  H  N N 179 
ILE HG13  H  N N 180 
ILE HG21  H  N N 181 
ILE HG22  H  N N 182 
ILE HG23  H  N N 183 
ILE HD11  H  N N 184 
ILE HD12  H  N N 185 
ILE HD13  H  N N 186 
ILE HXT   H  N N 187 
LEU N     N  N N 188 
LEU CA    C  N S 189 
LEU C     C  N N 190 
LEU O     O  N N 191 
LEU CB    C  N N 192 
LEU CG    C  N N 193 
LEU CD1   C  N N 194 
LEU CD2   C  N N 195 
LEU OXT   O  N N 196 
LEU H     H  N N 197 
LEU H2    H  N N 198 
LEU HA    H  N N 199 
LEU HB2   H  N N 200 
LEU HB3   H  N N 201 
LEU HG    H  N N 202 
LEU HD11  H  N N 203 
LEU HD12  H  N N 204 
LEU HD13  H  N N 205 
LEU HD21  H  N N 206 
LEU HD22  H  N N 207 
LEU HD23  H  N N 208 
LEU HXT   H  N N 209 
LYS N     N  N N 210 
LYS CA    C  N S 211 
LYS C     C  N N 212 
LYS O     O  N N 213 
LYS CB    C  N N 214 
LYS CG    C  N N 215 
LYS CD    C  N N 216 
LYS CE    C  N N 217 
LYS NZ    N  N N 218 
LYS OXT   O  N N 219 
LYS H     H  N N 220 
LYS H2    H  N N 221 
LYS HA    H  N N 222 
LYS HB2   H  N N 223 
LYS HB3   H  N N 224 
LYS HG2   H  N N 225 
LYS HG3   H  N N 226 
LYS HD2   H  N N 227 
LYS HD3   H  N N 228 
LYS HE2   H  N N 229 
LYS HE3   H  N N 230 
LYS HZ1   H  N N 231 
LYS HZ2   H  N N 232 
LYS HZ3   H  N N 233 
LYS HXT   H  N N 234 
MET N     N  N N 235 
MET CA    C  N S 236 
MET C     C  N N 237 
MET O     O  N N 238 
MET CB    C  N N 239 
MET CG    C  N N 240 
MET SD    S  N N 241 
MET CE    C  N N 242 
MET OXT   O  N N 243 
MET H     H  N N 244 
MET H2    H  N N 245 
MET HA    H  N N 246 
MET HB2   H  N N 247 
MET HB3   H  N N 248 
MET HG2   H  N N 249 
MET HG3   H  N N 250 
MET HE1   H  N N 251 
MET HE2   H  N N 252 
MET HE3   H  N N 253 
MET HXT   H  N N 254 
MG  MG    MG N N 255 
NAD PA    P  N S 256 
NAD O1A   O  N N 257 
NAD O2A   O  N N 258 
NAD O5B   O  N N 259 
NAD C5B   C  N N 260 
NAD C4B   C  N R 261 
NAD O4B   O  N N 262 
NAD C3B   C  N S 263 
NAD O3B   O  N N 264 
NAD C2B   C  N R 265 
NAD O2B   O  N N 266 
NAD C1B   C  N R 267 
NAD N9A   N  Y N 268 
NAD C8A   C  Y N 269 
NAD N7A   N  Y N 270 
NAD C5A   C  Y N 271 
NAD C6A   C  Y N 272 
NAD N6A   N  N N 273 
NAD N1A   N  Y N 274 
NAD C2A   C  Y N 275 
NAD N3A   N  Y N 276 
NAD C4A   C  Y N 277 
NAD O3    O  N N 278 
NAD PN    P  N N 279 
NAD O1N   O  N N 280 
NAD O2N   O  N N 281 
NAD O5D   O  N N 282 
NAD C5D   C  N N 283 
NAD C4D   C  N R 284 
NAD O4D   O  N N 285 
NAD C3D   C  N S 286 
NAD O3D   O  N N 287 
NAD C2D   C  N R 288 
NAD O2D   O  N N 289 
NAD C1D   C  N R 290 
NAD N1N   N  Y N 291 
NAD C2N   C  Y N 292 
NAD C3N   C  Y N 293 
NAD C7N   C  N N 294 
NAD O7N   O  N N 295 
NAD N7N   N  N N 296 
NAD C4N   C  Y N 297 
NAD C5N   C  Y N 298 
NAD C6N   C  Y N 299 
NAD HOA2  H  N N 300 
NAD H51A  H  N N 301 
NAD H52A  H  N N 302 
NAD H4B   H  N N 303 
NAD H3B   H  N N 304 
NAD HO3A  H  N N 305 
NAD H2B   H  N N 306 
NAD HO2A  H  N N 307 
NAD H1B   H  N N 308 
NAD H8A   H  N N 309 
NAD H61A  H  N N 310 
NAD H62A  H  N N 311 
NAD H2A   H  N N 312 
NAD H51N  H  N N 313 
NAD H52N  H  N N 314 
NAD H4D   H  N N 315 
NAD H3D   H  N N 316 
NAD HO3N  H  N N 317 
NAD H2D   H  N N 318 
NAD HO2N  H  N N 319 
NAD H1D   H  N N 320 
NAD H2N   H  N N 321 
NAD H71N  H  N N 322 
NAD H72N  H  N N 323 
NAD H4N   H  N N 324 
NAD H5N   H  N N 325 
NAD H6N   H  N N 326 
P5F PA    P  N N 327 
P5F O1A   O  N N 328 
P5F O2A   O  N N 329 
P5F O5B   O  N N 330 
P5F C5B   C  N N 331 
P5F C4B   C  N R 332 
P5F O4B   O  N N 333 
P5F C3B   C  N S 334 
P5F O3B   O  N N 335 
P5F C2B   C  N R 336 
P5F O2B   O  N N 337 
P5F C1B   C  N R 338 
P5F N9A   N  Y N 339 
P5F C8A   C  Y N 340 
P5F N7A   N  Y N 341 
P5F C5A   C  Y N 342 
P5F C6A   C  Y N 343 
P5F N6A   N  N N 344 
P5F N1A   N  Y N 345 
P5F C2A   C  Y N 346 
P5F N3A   N  Y N 347 
P5F C4A   C  Y N 348 
P5F N1    N  N N 349 
P5F C2    C  N N 350 
P5F O2    O  N N 351 
P5F N3    N  N N 352 
P5F C4    C  N N 353 
P5F O4    O  N N 354 
P5F C4X   C  Y N 355 
P5F N5    N  Y N 356 
P5F C5X   C  Y N 357 
P5F C6    C  Y N 358 
P5F C7    C  Y N 359 
P5F C7M   C  N N 360 
P5F C8    C  Y N 361 
P5F C8M   C  N N 362 
P5F C9    C  Y N 363 
P5F C9A   C  Y N 364 
P5F N10   N  Y N 365 
P5F C10   C  Y N 366 
P5F "C1'" C  N N 367 
P5F "C2'" C  N S 368 
P5F "O2'" O  N N 369 
P5F "C3'" C  N S 370 
P5F "O3'" O  N N 371 
P5F "C4'" C  N R 372 
P5F "O4'" O  N N 373 
P5F "C5'" C  N N 374 
P5F "O5'" O  N N 375 
P5F P     P  N N 376 
P5F O1P   O  N N 377 
P5F O2P   O  N N 378 
P5F O3P   O  N N 379 
P5F C21   C  N N 380 
P5F C22   C  N N 381 
P5F C23   C  N N 382 
P5F H1    H  N N 383 
P5F H2    H  N N 384 
P5F H3    H  N N 385 
P5F H4    H  N N 386 
P5F H5    H  N N 387 
P5F H6    H  N N 388 
P5F H7    H  N N 389 
P5F H8    H  N N 390 
P5F H9    H  N N 391 
P5F H10   H  N N 392 
P5F H11   H  N N 393 
P5F H12   H  N N 394 
P5F H13   H  N N 395 
P5F H14   H  N N 396 
P5F H15   H  N N 397 
P5F H16   H  N N 398 
P5F H17   H  N N 399 
P5F H18   H  N N 400 
P5F H19   H  N N 401 
P5F H20   H  N N 402 
P5F H21   H  N N 403 
P5F H22   H  N N 404 
P5F H23   H  N N 405 
P5F H24   H  N N 406 
P5F H25   H  N N 407 
P5F H26   H  N N 408 
P5F H27   H  N N 409 
P5F H28   H  N N 410 
P5F H29   H  N N 411 
P5F H30   H  N N 412 
P5F H31   H  N N 413 
P5F H32   H  N N 414 
P5F H33   H  N N 415 
P5F H34   H  N N 416 
P5F H35   H  N N 417 
P5F H37   H  N N 418 
P5F H39   H  N N 419 
P5F N2    N  N N 420 
P5F C1    C  N N 421 
P5F C3    C  N N 422 
P5F O1    O  N N 423 
P5F O3    O  N N 424 
P5F H36   H  N N 425 
P5F H38   H  N N 426 
P5F H40   H  N N 427 
PEG C1    C  N N 428 
PEG O1    O  N N 429 
PEG C2    C  N N 430 
PEG O2    O  N N 431 
PEG C3    C  N N 432 
PEG C4    C  N N 433 
PEG O4    O  N N 434 
PEG H11   H  N N 435 
PEG H12   H  N N 436 
PEG HO1   H  N N 437 
PEG H21   H  N N 438 
PEG H22   H  N N 439 
PEG H31   H  N N 440 
PEG H32   H  N N 441 
PEG H41   H  N N 442 
PEG H42   H  N N 443 
PEG HO4   H  N N 444 
PG4 O1    O  N N 445 
PG4 C1    C  N N 446 
PG4 C2    C  N N 447 
PG4 O2    O  N N 448 
PG4 C3    C  N N 449 
PG4 C4    C  N N 450 
PG4 O3    O  N N 451 
PG4 C5    C  N N 452 
PG4 C6    C  N N 453 
PG4 O4    O  N N 454 
PG4 C7    C  N N 455 
PG4 C8    C  N N 456 
PG4 O5    O  N N 457 
PG4 HO1   H  N N 458 
PG4 H11   H  N N 459 
PG4 H12   H  N N 460 
PG4 H21   H  N N 461 
PG4 H22   H  N N 462 
PG4 H31   H  N N 463 
PG4 H32   H  N N 464 
PG4 H41   H  N N 465 
PG4 H42   H  N N 466 
PG4 H51   H  N N 467 
PG4 H52   H  N N 468 
PG4 H61   H  N N 469 
PG4 H62   H  N N 470 
PG4 H71   H  N N 471 
PG4 H72   H  N N 472 
PG4 H81   H  N N 473 
PG4 H82   H  N N 474 
PG4 HO5   H  N N 475 
PGE C1    C  N N 476 
PGE O1    O  N N 477 
PGE C2    C  N N 478 
PGE O2    O  N N 479 
PGE C3    C  N N 480 
PGE C4    C  N N 481 
PGE O4    O  N N 482 
PGE C6    C  N N 483 
PGE C5    C  N N 484 
PGE O3    O  N N 485 
PGE H1    H  N N 486 
PGE H12   H  N N 487 
PGE HO1   H  N N 488 
PGE H2    H  N N 489 
PGE H22   H  N N 490 
PGE H3    H  N N 491 
PGE H32   H  N N 492 
PGE H4    H  N N 493 
PGE H42   H  N N 494 
PGE HO4   H  N N 495 
PGE H6    H  N N 496 
PGE H62   H  N N 497 
PGE H5    H  N N 498 
PGE H52   H  N N 499 
PHE N     N  N N 500 
PHE CA    C  N S 501 
PHE C     C  N N 502 
PHE O     O  N N 503 
PHE CB    C  N N 504 
PHE CG    C  Y N 505 
PHE CD1   C  Y N 506 
PHE CD2   C  Y N 507 
PHE CE1   C  Y N 508 
PHE CE2   C  Y N 509 
PHE CZ    C  Y N 510 
PHE OXT   O  N N 511 
PHE H     H  N N 512 
PHE H2    H  N N 513 
PHE HA    H  N N 514 
PHE HB2   H  N N 515 
PHE HB3   H  N N 516 
PHE HD1   H  N N 517 
PHE HD2   H  N N 518 
PHE HE1   H  N N 519 
PHE HE2   H  N N 520 
PHE HZ    H  N N 521 
PHE HXT   H  N N 522 
PRO N     N  N N 523 
PRO CA    C  N S 524 
PRO C     C  N N 525 
PRO O     O  N N 526 
PRO CB    C  N N 527 
PRO CG    C  N N 528 
PRO CD    C  N N 529 
PRO OXT   O  N N 530 
PRO H     H  N N 531 
PRO HA    H  N N 532 
PRO HB2   H  N N 533 
PRO HB3   H  N N 534 
PRO HG2   H  N N 535 
PRO HG3   H  N N 536 
PRO HD2   H  N N 537 
PRO HD3   H  N N 538 
PRO HXT   H  N N 539 
SER N     N  N N 540 
SER CA    C  N S 541 
SER C     C  N N 542 
SER O     O  N N 543 
SER CB    C  N N 544 
SER OG    O  N N 545 
SER OXT   O  N N 546 
SER H     H  N N 547 
SER H2    H  N N 548 
SER HA    H  N N 549 
SER HB2   H  N N 550 
SER HB3   H  N N 551 
SER HG    H  N N 552 
SER HXT   H  N N 553 
SO4 S     S  N N 554 
SO4 O1    O  N N 555 
SO4 O2    O  N N 556 
SO4 O3    O  N N 557 
SO4 O4    O  N N 558 
THR N     N  N N 559 
THR CA    C  N S 560 
THR C     C  N N 561 
THR O     O  N N 562 
THR CB    C  N R 563 
THR OG1   O  N N 564 
THR CG2   C  N N 565 
THR OXT   O  N N 566 
THR H     H  N N 567 
THR H2    H  N N 568 
THR HA    H  N N 569 
THR HB    H  N N 570 
THR HG1   H  N N 571 
THR HG21  H  N N 572 
THR HG22  H  N N 573 
THR HG23  H  N N 574 
THR HXT   H  N N 575 
TRP N     N  N N 576 
TRP CA    C  N S 577 
TRP C     C  N N 578 
TRP O     O  N N 579 
TRP CB    C  N N 580 
TRP CG    C  Y N 581 
TRP CD1   C  Y N 582 
TRP CD2   C  Y N 583 
TRP NE1   N  Y N 584 
TRP CE2   C  Y N 585 
TRP CE3   C  Y N 586 
TRP CZ2   C  Y N 587 
TRP CZ3   C  Y N 588 
TRP CH2   C  Y N 589 
TRP OXT   O  N N 590 
TRP H     H  N N 591 
TRP H2    H  N N 592 
TRP HA    H  N N 593 
TRP HB2   H  N N 594 
TRP HB3   H  N N 595 
TRP HD1   H  N N 596 
TRP HE1   H  N N 597 
TRP HE3   H  N N 598 
TRP HZ2   H  N N 599 
TRP HZ3   H  N N 600 
TRP HH2   H  N N 601 
TRP HXT   H  N N 602 
TYR N     N  N N 603 
TYR CA    C  N S 604 
TYR C     C  N N 605 
TYR O     O  N N 606 
TYR CB    C  N N 607 
TYR CG    C  Y N 608 
TYR CD1   C  Y N 609 
TYR CD2   C  Y N 610 
TYR CE1   C  Y N 611 
TYR CE2   C  Y N 612 
TYR CZ    C  Y N 613 
TYR OH    O  N N 614 
TYR OXT   O  N N 615 
TYR H     H  N N 616 
TYR H2    H  N N 617 
TYR HA    H  N N 618 
TYR HB2   H  N N 619 
TYR HB3   H  N N 620 
TYR HD1   H  N N 621 
TYR HD2   H  N N 622 
TYR HE1   H  N N 623 
TYR HE2   H  N N 624 
TYR HH    H  N N 625 
TYR HXT   H  N N 626 
VAL N     N  N N 627 
VAL CA    C  N S 628 
VAL C     C  N N 629 
VAL O     O  N N 630 
VAL CB    C  N N 631 
VAL CG1   C  N N 632 
VAL CG2   C  N N 633 
VAL OXT   O  N N 634 
VAL H     H  N N 635 
VAL H2    H  N N 636 
VAL HA    H  N N 637 
VAL HB    H  N N 638 
VAL HG11  H  N N 639 
VAL HG12  H  N N 640 
VAL HG13  H  N N 641 
VAL HG21  H  N N 642 
VAL HG22  H  N N 643 
VAL HG23  H  N N 644 
VAL HXT   H  N N 645 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA    sing N N 1   
ALA N     H     sing N N 2   
ALA N     H2    sing N N 3   
ALA CA    C     sing N N 4   
ALA CA    CB    sing N N 5   
ALA CA    HA    sing N N 6   
ALA C     O     doub N N 7   
ALA C     OXT   sing N N 8   
ALA CB    HB1   sing N N 9   
ALA CB    HB2   sing N N 10  
ALA CB    HB3   sing N N 11  
ALA OXT   HXT   sing N N 12  
ARG N     CA    sing N N 13  
ARG N     H     sing N N 14  
ARG N     H2    sing N N 15  
ARG CA    C     sing N N 16  
ARG CA    CB    sing N N 17  
ARG CA    HA    sing N N 18  
ARG C     O     doub N N 19  
ARG C     OXT   sing N N 20  
ARG CB    CG    sing N N 21  
ARG CB    HB2   sing N N 22  
ARG CB    HB3   sing N N 23  
ARG CG    CD    sing N N 24  
ARG CG    HG2   sing N N 25  
ARG CG    HG3   sing N N 26  
ARG CD    NE    sing N N 27  
ARG CD    HD2   sing N N 28  
ARG CD    HD3   sing N N 29  
ARG NE    CZ    sing N N 30  
ARG NE    HE    sing N N 31  
ARG CZ    NH1   sing N N 32  
ARG CZ    NH2   doub N N 33  
ARG NH1   HH11  sing N N 34  
ARG NH1   HH12  sing N N 35  
ARG NH2   HH21  sing N N 36  
ARG NH2   HH22  sing N N 37  
ARG OXT   HXT   sing N N 38  
ASN N     CA    sing N N 39  
ASN N     H     sing N N 40  
ASN N     H2    sing N N 41  
ASN CA    C     sing N N 42  
ASN CA    CB    sing N N 43  
ASN CA    HA    sing N N 44  
ASN C     O     doub N N 45  
ASN C     OXT   sing N N 46  
ASN CB    CG    sing N N 47  
ASN CB    HB2   sing N N 48  
ASN CB    HB3   sing N N 49  
ASN CG    OD1   doub N N 50  
ASN CG    ND2   sing N N 51  
ASN ND2   HD21  sing N N 52  
ASN ND2   HD22  sing N N 53  
ASN OXT   HXT   sing N N 54  
ASP N     CA    sing N N 55  
ASP N     H     sing N N 56  
ASP N     H2    sing N N 57  
ASP CA    C     sing N N 58  
ASP CA    CB    sing N N 59  
ASP CA    HA    sing N N 60  
ASP C     O     doub N N 61  
ASP C     OXT   sing N N 62  
ASP CB    CG    sing N N 63  
ASP CB    HB2   sing N N 64  
ASP CB    HB3   sing N N 65  
ASP CG    OD1   doub N N 66  
ASP CG    OD2   sing N N 67  
ASP OD2   HD2   sing N N 68  
ASP OXT   HXT   sing N N 69  
CYS N     CA    sing N N 70  
CYS N     H     sing N N 71  
CYS N     H2    sing N N 72  
CYS CA    C     sing N N 73  
CYS CA    CB    sing N N 74  
CYS CA    HA    sing N N 75  
CYS C     O     doub N N 76  
CYS C     OXT   sing N N 77  
CYS CB    SG    sing N N 78  
CYS CB    HB2   sing N N 79  
CYS CB    HB3   sing N N 80  
CYS SG    HG    sing N N 81  
CYS OXT   HXT   sing N N 82  
FMT C     O1    doub N N 83  
FMT C     O2    sing N N 84  
FMT C     H     sing N N 85  
FMT O2    HO2   sing N N 86  
GLN N     CA    sing N N 87  
GLN N     H     sing N N 88  
GLN N     H2    sing N N 89  
GLN CA    C     sing N N 90  
GLN CA    CB    sing N N 91  
GLN CA    HA    sing N N 92  
GLN C     O     doub N N 93  
GLN C     OXT   sing N N 94  
GLN CB    CG    sing N N 95  
GLN CB    HB2   sing N N 96  
GLN CB    HB3   sing N N 97  
GLN CG    CD    sing N N 98  
GLN CG    HG2   sing N N 99  
GLN CG    HG3   sing N N 100 
GLN CD    OE1   doub N N 101 
GLN CD    NE2   sing N N 102 
GLN NE2   HE21  sing N N 103 
GLN NE2   HE22  sing N N 104 
GLN OXT   HXT   sing N N 105 
GLU N     CA    sing N N 106 
GLU N     H     sing N N 107 
GLU N     H2    sing N N 108 
GLU CA    C     sing N N 109 
GLU CA    CB    sing N N 110 
GLU CA    HA    sing N N 111 
GLU C     O     doub N N 112 
GLU C     OXT   sing N N 113 
GLU CB    CG    sing N N 114 
GLU CB    HB2   sing N N 115 
GLU CB    HB3   sing N N 116 
GLU CG    CD    sing N N 117 
GLU CG    HG2   sing N N 118 
GLU CG    HG3   sing N N 119 
GLU CD    OE1   doub N N 120 
GLU CD    OE2   sing N N 121 
GLU OE2   HE2   sing N N 122 
GLU OXT   HXT   sing N N 123 
GLY N     CA    sing N N 124 
GLY N     H     sing N N 125 
GLY N     H2    sing N N 126 
GLY CA    C     sing N N 127 
GLY CA    HA2   sing N N 128 
GLY CA    HA3   sing N N 129 
GLY C     O     doub N N 130 
GLY C     OXT   sing N N 131 
GLY OXT   HXT   sing N N 132 
HIS N     CA    sing N N 133 
HIS N     H     sing N N 134 
HIS N     H2    sing N N 135 
HIS CA    C     sing N N 136 
HIS CA    CB    sing N N 137 
HIS CA    HA    sing N N 138 
HIS C     O     doub N N 139 
HIS C     OXT   sing N N 140 
HIS CB    CG    sing N N 141 
HIS CB    HB2   sing N N 142 
HIS CB    HB3   sing N N 143 
HIS CG    ND1   sing Y N 144 
HIS CG    CD2   doub Y N 145 
HIS ND1   CE1   doub Y N 146 
HIS ND1   HD1   sing N N 147 
HIS CD2   NE2   sing Y N 148 
HIS CD2   HD2   sing N N 149 
HIS CE1   NE2   sing Y N 150 
HIS CE1   HE1   sing N N 151 
HIS NE2   HE2   sing N N 152 
HIS OXT   HXT   sing N N 153 
HOH O     H1    sing N N 154 
HOH O     H2    sing N N 155 
ILE N     CA    sing N N 156 
ILE N     H     sing N N 157 
ILE N     H2    sing N N 158 
ILE CA    C     sing N N 159 
ILE CA    CB    sing N N 160 
ILE CA    HA    sing N N 161 
ILE C     O     doub N N 162 
ILE C     OXT   sing N N 163 
ILE CB    CG1   sing N N 164 
ILE CB    CG2   sing N N 165 
ILE CB    HB    sing N N 166 
ILE CG1   CD1   sing N N 167 
ILE CG1   HG12  sing N N 168 
ILE CG1   HG13  sing N N 169 
ILE CG2   HG21  sing N N 170 
ILE CG2   HG22  sing N N 171 
ILE CG2   HG23  sing N N 172 
ILE CD1   HD11  sing N N 173 
ILE CD1   HD12  sing N N 174 
ILE CD1   HD13  sing N N 175 
ILE OXT   HXT   sing N N 176 
LEU N     CA    sing N N 177 
LEU N     H     sing N N 178 
LEU N     H2    sing N N 179 
LEU CA    C     sing N N 180 
LEU CA    CB    sing N N 181 
LEU CA    HA    sing N N 182 
LEU C     O     doub N N 183 
LEU C     OXT   sing N N 184 
LEU CB    CG    sing N N 185 
LEU CB    HB2   sing N N 186 
LEU CB    HB3   sing N N 187 
LEU CG    CD1   sing N N 188 
LEU CG    CD2   sing N N 189 
LEU CG    HG    sing N N 190 
LEU CD1   HD11  sing N N 191 
LEU CD1   HD12  sing N N 192 
LEU CD1   HD13  sing N N 193 
LEU CD2   HD21  sing N N 194 
LEU CD2   HD22  sing N N 195 
LEU CD2   HD23  sing N N 196 
LEU OXT   HXT   sing N N 197 
LYS N     CA    sing N N 198 
LYS N     H     sing N N 199 
LYS N     H2    sing N N 200 
LYS CA    C     sing N N 201 
LYS CA    CB    sing N N 202 
LYS CA    HA    sing N N 203 
LYS C     O     doub N N 204 
LYS C     OXT   sing N N 205 
LYS CB    CG    sing N N 206 
LYS CB    HB2   sing N N 207 
LYS CB    HB3   sing N N 208 
LYS CG    CD    sing N N 209 
LYS CG    HG2   sing N N 210 
LYS CG    HG3   sing N N 211 
LYS CD    CE    sing N N 212 
LYS CD    HD2   sing N N 213 
LYS CD    HD3   sing N N 214 
LYS CE    NZ    sing N N 215 
LYS CE    HE2   sing N N 216 
LYS CE    HE3   sing N N 217 
LYS NZ    HZ1   sing N N 218 
LYS NZ    HZ2   sing N N 219 
LYS NZ    HZ3   sing N N 220 
LYS OXT   HXT   sing N N 221 
MET N     CA    sing N N 222 
MET N     H     sing N N 223 
MET N     H2    sing N N 224 
MET CA    C     sing N N 225 
MET CA    CB    sing N N 226 
MET CA    HA    sing N N 227 
MET C     O     doub N N 228 
MET C     OXT   sing N N 229 
MET CB    CG    sing N N 230 
MET CB    HB2   sing N N 231 
MET CB    HB3   sing N N 232 
MET CG    SD    sing N N 233 
MET CG    HG2   sing N N 234 
MET CG    HG3   sing N N 235 
MET SD    CE    sing N N 236 
MET CE    HE1   sing N N 237 
MET CE    HE2   sing N N 238 
MET CE    HE3   sing N N 239 
MET OXT   HXT   sing N N 240 
NAD PA    O1A   doub N N 241 
NAD PA    O2A   sing N N 242 
NAD PA    O5B   sing N N 243 
NAD PA    O3    sing N N 244 
NAD O2A   HOA2  sing N N 245 
NAD O5B   C5B   sing N N 246 
NAD C5B   C4B   sing N N 247 
NAD C5B   H51A  sing N N 248 
NAD C5B   H52A  sing N N 249 
NAD C4B   O4B   sing N N 250 
NAD C4B   C3B   sing N N 251 
NAD C4B   H4B   sing N N 252 
NAD O4B   C1B   sing N N 253 
NAD C3B   O3B   sing N N 254 
NAD C3B   C2B   sing N N 255 
NAD C3B   H3B   sing N N 256 
NAD O3B   HO3A  sing N N 257 
NAD C2B   O2B   sing N N 258 
NAD C2B   C1B   sing N N 259 
NAD C2B   H2B   sing N N 260 
NAD O2B   HO2A  sing N N 261 
NAD C1B   N9A   sing N N 262 
NAD C1B   H1B   sing N N 263 
NAD N9A   C8A   sing Y N 264 
NAD N9A   C4A   sing Y N 265 
NAD C8A   N7A   doub Y N 266 
NAD C8A   H8A   sing N N 267 
NAD N7A   C5A   sing Y N 268 
NAD C5A   C6A   sing Y N 269 
NAD C5A   C4A   doub Y N 270 
NAD C6A   N6A   sing N N 271 
NAD C6A   N1A   doub Y N 272 
NAD N6A   H61A  sing N N 273 
NAD N6A   H62A  sing N N 274 
NAD N1A   C2A   sing Y N 275 
NAD C2A   N3A   doub Y N 276 
NAD C2A   H2A   sing N N 277 
NAD N3A   C4A   sing Y N 278 
NAD O3    PN    sing N N 279 
NAD PN    O1N   doub N N 280 
NAD PN    O2N   sing N N 281 
NAD PN    O5D   sing N N 282 
NAD O5D   C5D   sing N N 283 
NAD C5D   C4D   sing N N 284 
NAD C5D   H51N  sing N N 285 
NAD C5D   H52N  sing N N 286 
NAD C4D   O4D   sing N N 287 
NAD C4D   C3D   sing N N 288 
NAD C4D   H4D   sing N N 289 
NAD O4D   C1D   sing N N 290 
NAD C3D   O3D   sing N N 291 
NAD C3D   C2D   sing N N 292 
NAD C3D   H3D   sing N N 293 
NAD O3D   HO3N  sing N N 294 
NAD C2D   O2D   sing N N 295 
NAD C2D   C1D   sing N N 296 
NAD C2D   H2D   sing N N 297 
NAD O2D   HO2N  sing N N 298 
NAD C1D   N1N   sing N N 299 
NAD C1D   H1D   sing N N 300 
NAD N1N   C2N   sing Y N 301 
NAD N1N   C6N   doub Y N 302 
NAD C2N   C3N   doub Y N 303 
NAD C2N   H2N   sing N N 304 
NAD C3N   C7N   sing N N 305 
NAD C3N   C4N   sing Y N 306 
NAD C7N   O7N   doub N N 307 
NAD C7N   N7N   sing N N 308 
NAD N7N   H71N  sing N N 309 
NAD N7N   H72N  sing N N 310 
NAD C4N   C5N   doub Y N 311 
NAD C4N   H4N   sing N N 312 
NAD C5N   C6N   sing Y N 313 
NAD C5N   H5N   sing N N 314 
NAD C6N   H6N   sing N N 315 
P5F C7M   C7    sing N N 316 
P5F C7    C6    doub Y N 317 
P5F C7    C8    sing Y N 318 
P5F C8M   C8    sing N N 319 
P5F C6    C5X   sing Y N 320 
P5F C8    C9    doub Y N 321 
P5F C23   C21   sing N N 322 
P5F C22   C21   doub N E 323 
P5F C22   N5    sing N N 324 
P5F C5X   N5    doub Y N 325 
P5F C5X   C9A   sing Y N 326 
P5F C9    C9A   sing Y N 327 
P5F N5    C4X   sing Y N 328 
P5F C9A   N10   doub Y N 329 
P5F "O4'" "C4'" sing N N 330 
P5F N10   "C1'" sing N N 331 
P5F N10   C10   sing Y N 332 
P5F O2P   P     doub N N 333 
P5F C4X   C10   doub Y N 334 
P5F C4X   C4    sing N N 335 
P5F "C1'" "C2'" sing N N 336 
P5F O4    C4    doub N N 337 
P5F C10   N1    sing N N 338 
P5F "C4'" "C5'" sing N N 339 
P5F "C4'" "C3'" sing N N 340 
P5F C4    N3    sing N N 341 
P5F "C5'" "O5'" sing N N 342 
P5F "C2'" "C3'" sing N N 343 
P5F "C2'" "O2'" sing N N 344 
P5F P     "O5'" sing N N 345 
P5F P     O3P   sing N N 346 
P5F P     O1P   sing N N 347 
P5F "C3'" "O3'" sing N N 348 
P5F O3P   PA    sing N N 349 
P5F N1    C2    sing N N 350 
P5F N3    C2    sing N N 351 
P5F C2    O2    doub N N 352 
P5F O2A   PA    doub N N 353 
P5F PA    O1A   sing N N 354 
P5F PA    O5B   sing N N 355 
P5F C5B   O5B   sing N N 356 
P5F C5B   C4B   sing N N 357 
P5F O3B   C3B   sing N N 358 
P5F C4B   C3B   sing N N 359 
P5F C4B   O4B   sing N N 360 
P5F C3B   C2B   sing N N 361 
P5F O2B   C2B   sing N N 362 
P5F O4B   C1B   sing N N 363 
P5F C2B   C1B   sing N N 364 
P5F C1B   N9A   sing N N 365 
P5F C8A   N9A   sing Y N 366 
P5F C8A   N7A   doub Y N 367 
P5F N9A   C4A   sing Y N 368 
P5F N7A   C5A   sing Y N 369 
P5F C4A   C5A   doub Y N 370 
P5F C4A   N3A   sing Y N 371 
P5F C5A   C6A   sing Y N 372 
P5F N3A   C2A   doub Y N 373 
P5F C6A   N6A   sing N N 374 
P5F C6A   N1A   doub Y N 375 
P5F C2A   N1A   sing Y N 376 
P5F O1A   H1    sing N N 377 
P5F C5B   H2    sing N N 378 
P5F C5B   H3    sing N N 379 
P5F C4B   H4    sing N N 380 
P5F C3B   H5    sing N N 381 
P5F O3B   H6    sing N N 382 
P5F C2B   H7    sing N N 383 
P5F O2B   H8    sing N N 384 
P5F C1B   H9    sing N N 385 
P5F C8A   H10   sing N N 386 
P5F N6A   H11   sing N N 387 
P5F N6A   H12   sing N N 388 
P5F C2A   H13   sing N N 389 
P5F N1    H14   sing N N 390 
P5F N3    H15   sing N N 391 
P5F C6    H16   sing N N 392 
P5F C7M   H17   sing N N 393 
P5F C7M   H18   sing N N 394 
P5F C7M   H19   sing N N 395 
P5F C8M   H20   sing N N 396 
P5F C8M   H21   sing N N 397 
P5F C8M   H22   sing N N 398 
P5F C9    H23   sing N N 399 
P5F "C1'" H24   sing N N 400 
P5F "C1'" H25   sing N N 401 
P5F "C2'" H26   sing N N 402 
P5F "O2'" H27   sing N N 403 
P5F "C3'" H28   sing N N 404 
P5F "O3'" H29   sing N N 405 
P5F "C4'" H30   sing N N 406 
P5F "O4'" H31   sing N N 407 
P5F "C5'" H32   sing N N 408 
P5F "C5'" H33   sing N N 409 
P5F O1P   H34   sing N N 410 
P5F C21   H35   sing N N 411 
P5F C22   H37   sing N N 412 
P5F C23   H39   sing N N 413 
P5F C23   N2    doub N N 414 
P5F N2    C1    sing N N 415 
P5F C1    C3    sing N N 416 
P5F C3    O1    sing N N 417 
P5F C3    O3    doub N N 418 
P5F C1    H36   sing N N 419 
P5F C1    H38   sing N N 420 
P5F O1    H40   sing N N 421 
PEG C1    O1    sing N N 422 
PEG C1    C2    sing N N 423 
PEG C1    H11   sing N N 424 
PEG C1    H12   sing N N 425 
PEG O1    HO1   sing N N 426 
PEG C2    O2    sing N N 427 
PEG C2    H21   sing N N 428 
PEG C2    H22   sing N N 429 
PEG O2    C3    sing N N 430 
PEG C3    C4    sing N N 431 
PEG C3    H31   sing N N 432 
PEG C3    H32   sing N N 433 
PEG C4    O4    sing N N 434 
PEG C4    H41   sing N N 435 
PEG C4    H42   sing N N 436 
PEG O4    HO4   sing N N 437 
PG4 O1    C1    sing N N 438 
PG4 O1    HO1   sing N N 439 
PG4 C1    C2    sing N N 440 
PG4 C1    H11   sing N N 441 
PG4 C1    H12   sing N N 442 
PG4 C2    O2    sing N N 443 
PG4 C2    H21   sing N N 444 
PG4 C2    H22   sing N N 445 
PG4 O2    C3    sing N N 446 
PG4 C3    C4    sing N N 447 
PG4 C3    H31   sing N N 448 
PG4 C3    H32   sing N N 449 
PG4 C4    O3    sing N N 450 
PG4 C4    H41   sing N N 451 
PG4 C4    H42   sing N N 452 
PG4 O3    C5    sing N N 453 
PG4 C5    C6    sing N N 454 
PG4 C5    H51   sing N N 455 
PG4 C5    H52   sing N N 456 
PG4 C6    O4    sing N N 457 
PG4 C6    H61   sing N N 458 
PG4 C6    H62   sing N N 459 
PG4 O4    C7    sing N N 460 
PG4 C7    C8    sing N N 461 
PG4 C7    H71   sing N N 462 
PG4 C7    H72   sing N N 463 
PG4 C8    O5    sing N N 464 
PG4 C8    H81   sing N N 465 
PG4 C8    H82   sing N N 466 
PG4 O5    HO5   sing N N 467 
PGE C1    O1    sing N N 468 
PGE C1    C2    sing N N 469 
PGE C1    H1    sing N N 470 
PGE C1    H12   sing N N 471 
PGE O1    HO1   sing N N 472 
PGE C2    O2    sing N N 473 
PGE C2    H2    sing N N 474 
PGE C2    H22   sing N N 475 
PGE O2    C3    sing N N 476 
PGE C3    C4    sing N N 477 
PGE C3    H3    sing N N 478 
PGE C3    H32   sing N N 479 
PGE C4    O3    sing N N 480 
PGE C4    H4    sing N N 481 
PGE C4    H42   sing N N 482 
PGE O4    C6    sing N N 483 
PGE O4    HO4   sing N N 484 
PGE C6    C5    sing N N 485 
PGE C6    H6    sing N N 486 
PGE C6    H62   sing N N 487 
PGE C5    O3    sing N N 488 
PGE C5    H5    sing N N 489 
PGE C5    H52   sing N N 490 
PHE N     CA    sing N N 491 
PHE N     H     sing N N 492 
PHE N     H2    sing N N 493 
PHE CA    C     sing N N 494 
PHE CA    CB    sing N N 495 
PHE CA    HA    sing N N 496 
PHE C     O     doub N N 497 
PHE C     OXT   sing N N 498 
PHE CB    CG    sing N N 499 
PHE CB    HB2   sing N N 500 
PHE CB    HB3   sing N N 501 
PHE CG    CD1   doub Y N 502 
PHE CG    CD2   sing Y N 503 
PHE CD1   CE1   sing Y N 504 
PHE CD1   HD1   sing N N 505 
PHE CD2   CE2   doub Y N 506 
PHE CD2   HD2   sing N N 507 
PHE CE1   CZ    doub Y N 508 
PHE CE1   HE1   sing N N 509 
PHE CE2   CZ    sing Y N 510 
PHE CE2   HE2   sing N N 511 
PHE CZ    HZ    sing N N 512 
PHE OXT   HXT   sing N N 513 
PRO N     CA    sing N N 514 
PRO N     CD    sing N N 515 
PRO N     H     sing N N 516 
PRO CA    C     sing N N 517 
PRO CA    CB    sing N N 518 
PRO CA    HA    sing N N 519 
PRO C     O     doub N N 520 
PRO C     OXT   sing N N 521 
PRO CB    CG    sing N N 522 
PRO CB    HB2   sing N N 523 
PRO CB    HB3   sing N N 524 
PRO CG    CD    sing N N 525 
PRO CG    HG2   sing N N 526 
PRO CG    HG3   sing N N 527 
PRO CD    HD2   sing N N 528 
PRO CD    HD3   sing N N 529 
PRO OXT   HXT   sing N N 530 
SER N     CA    sing N N 531 
SER N     H     sing N N 532 
SER N     H2    sing N N 533 
SER CA    C     sing N N 534 
SER CA    CB    sing N N 535 
SER CA    HA    sing N N 536 
SER C     O     doub N N 537 
SER C     OXT   sing N N 538 
SER CB    OG    sing N N 539 
SER CB    HB2   sing N N 540 
SER CB    HB3   sing N N 541 
SER OG    HG    sing N N 542 
SER OXT   HXT   sing N N 543 
SO4 S     O1    doub N N 544 
SO4 S     O2    doub N N 545 
SO4 S     O3    sing N N 546 
SO4 S     O4    sing N N 547 
THR N     CA    sing N N 548 
THR N     H     sing N N 549 
THR N     H2    sing N N 550 
THR CA    C     sing N N 551 
THR CA    CB    sing N N 552 
THR CA    HA    sing N N 553 
THR C     O     doub N N 554 
THR C     OXT   sing N N 555 
THR CB    OG1   sing N N 556 
THR CB    CG2   sing N N 557 
THR CB    HB    sing N N 558 
THR OG1   HG1   sing N N 559 
THR CG2   HG21  sing N N 560 
THR CG2   HG22  sing N N 561 
THR CG2   HG23  sing N N 562 
THR OXT   HXT   sing N N 563 
TRP N     CA    sing N N 564 
TRP N     H     sing N N 565 
TRP N     H2    sing N N 566 
TRP CA    C     sing N N 567 
TRP CA    CB    sing N N 568 
TRP CA    HA    sing N N 569 
TRP C     O     doub N N 570 
TRP C     OXT   sing N N 571 
TRP CB    CG    sing N N 572 
TRP CB    HB2   sing N N 573 
TRP CB    HB3   sing N N 574 
TRP CG    CD1   doub Y N 575 
TRP CG    CD2   sing Y N 576 
TRP CD1   NE1   sing Y N 577 
TRP CD1   HD1   sing N N 578 
TRP CD2   CE2   doub Y N 579 
TRP CD2   CE3   sing Y N 580 
TRP NE1   CE2   sing Y N 581 
TRP NE1   HE1   sing N N 582 
TRP CE2   CZ2   sing Y N 583 
TRP CE3   CZ3   doub Y N 584 
TRP CE3   HE3   sing N N 585 
TRP CZ2   CH2   doub Y N 586 
TRP CZ2   HZ2   sing N N 587 
TRP CZ3   CH2   sing Y N 588 
TRP CZ3   HZ3   sing N N 589 
TRP CH2   HH2   sing N N 590 
TRP OXT   HXT   sing N N 591 
TYR N     CA    sing N N 592 
TYR N     H     sing N N 593 
TYR N     H2    sing N N 594 
TYR CA    C     sing N N 595 
TYR CA    CB    sing N N 596 
TYR CA    HA    sing N N 597 
TYR C     O     doub N N 598 
TYR C     OXT   sing N N 599 
TYR CB    CG    sing N N 600 
TYR CB    HB2   sing N N 601 
TYR CB    HB3   sing N N 602 
TYR CG    CD1   doub Y N 603 
TYR CG    CD2   sing Y N 604 
TYR CD1   CE1   sing Y N 605 
TYR CD1   HD1   sing N N 606 
TYR CD2   CE2   doub Y N 607 
TYR CD2   HD2   sing N N 608 
TYR CE1   CZ    doub Y N 609 
TYR CE1   HE1   sing N N 610 
TYR CE2   CZ    sing Y N 611 
TYR CE2   HE2   sing N N 612 
TYR CZ    OH    sing N N 613 
TYR OH    HH    sing N N 614 
TYR OXT   HXT   sing N N 615 
VAL N     CA    sing N N 616 
VAL N     H     sing N N 617 
VAL N     H2    sing N N 618 
VAL CA    C     sing N N 619 
VAL CA    CB    sing N N 620 
VAL CA    HA    sing N N 621 
VAL C     O     doub N N 622 
VAL C     OXT   sing N N 623 
VAL CB    CG1   sing N N 624 
VAL CB    CG2   sing N N 625 
VAL CB    HB    sing N N 626 
VAL CG1   HG11  sing N N 627 
VAL CG1   HG12  sing N N 628 
VAL CG1   HG13  sing N N 629 
VAL CG2   HG21  sing N N 630 
VAL CG2   HG22  sing N N 631 
VAL CG2   HG23  sing N N 632 
VAL OXT   HXT   sing N N 633 
# 
_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           R01GM132640 
_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                    9E5W 
_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]   0.009916 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002937 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009807 
_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]   0.008240 
_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   ? -49.815 94.085  103.761 1.00 46.83 ? 14   ALA A N     1 
ATOM   2     C  CA    . ALA A 1  16   ? -48.719 93.210  104.174 1.00 46.28 ? 14   ALA A CA    1 
ATOM   3     C  C     . ALA A 1  16   ? -49.206 91.770  104.322 1.00 45.81 ? 14   ALA A C     1 
ATOM   4     O  O     . ALA A 1  16   ? -49.966 91.459  105.238 1.00 48.01 ? 14   ALA A O     1 
ATOM   5     C  CB    . ALA A 1  16   ? -48.110 93.706  105.478 1.00 48.78 ? 14   ALA A CB    1 
ATOM   6     N  N     . PRO A 1  17   ? -48.770 90.892  103.418 1.00 42.84 ? 15   PRO A N     1 
ATOM   7     C  CA    . PRO A 1  17   ? -49.278 89.513  103.429 1.00 37.63 ? 15   PRO A CA    1 
ATOM   8     C  C     . PRO A 1  17   ? -48.869 88.773  104.694 1.00 40.39 ? 15   PRO A C     1 
ATOM   9     O  O     . PRO A 1  17   ? -47.748 88.918  105.187 1.00 39.88 ? 15   PRO A O     1 
ATOM   10    C  CB    . PRO A 1  17   ? -48.640 88.887  102.181 1.00 43.40 ? 15   PRO A CB    1 
ATOM   11    C  CG    . PRO A 1  17   ? -48.238 90.054  101.323 1.00 42.86 ? 15   PRO A CG    1 
ATOM   12    C  CD    . PRO A 1  17   ? -47.872 91.146  102.282 1.00 39.36 ? 15   PRO A CD    1 
ATOM   13    N  N     . ALA A 1  18   ? -49.801 87.988  105.229 1.00 38.47 ? 16   ALA A N     1 
ATOM   14    C  CA    . ALA A 1  18   ? -49.496 87.193  106.408 1.00 33.28 ? 16   ALA A CA    1 
ATOM   15    C  C     . ALA A 1  18   ? -48.469 86.118  106.054 1.00 32.82 ? 16   ALA A C     1 
ATOM   16    O  O     . ALA A 1  18   ? -48.545 85.513  104.976 1.00 29.65 ? 16   ALA A O     1 
ATOM   17    C  CB    . ALA A 1  18   ? -50.762 86.552  106.971 1.00 34.60 ? 16   ALA A CB    1 
ATOM   18    N  N     . PRO A 1  19   ? -47.488 85.877  106.921 1.00 31.32 ? 17   PRO A N     1 
ATOM   19    C  CA    . PRO A 1  19   ? -46.423 84.922  106.590 1.00 28.24 ? 17   PRO A CA    1 
ATOM   20    C  C     . PRO A 1  19   ? -46.980 83.522  106.384 1.00 27.54 ? 17   PRO A C     1 
ATOM   21    O  O     . PRO A 1  19   ? -47.763 83.019  107.197 1.00 27.22 ? 17   PRO A O     1 
ATOM   22    C  CB    . PRO A 1  19   ? -45.494 84.993  107.810 1.00 30.55 ? 17   PRO A CB    1 
ATOM   23    C  CG    . PRO A 1  19   ? -45.784 86.336  108.425 1.00 30.31 ? 17   PRO A CG    1 
ATOM   24    C  CD    . PRO A 1  19   ? -47.243 86.574  108.195 1.00 29.52 ? 17   PRO A CD    1 
ATOM   25    N  N     . PHE A 1  20   ? -46.596 82.912  105.262 1.00 25.77 ? 18   PHE A N     1 
ATOM   26    C  CA    . PHE A 1  20   ? -46.909 81.533  104.903 1.00 26.95 ? 18   PHE A CA    1 
ATOM   27    C  C     . PHE A 1  20   ? -48.389 81.310  104.635 1.00 26.47 ? 18   PHE A C     1 
ATOM   28    O  O     . PHE A 1  20   ? -48.818 80.158  104.516 1.00 28.56 ? 18   PHE A O     1 
ATOM   29    C  CB    . PHE A 1  20   ? -46.438 80.553  105.981 1.00 25.21 ? 18   PHE A CB    1 
ATOM   30    C  CG    . PHE A 1  20   ? -44.960 80.602  106.233 1.00 24.58 ? 18   PHE A CG    1 
ATOM   31    C  CD1   . PHE A 1  20   ? -44.082 80.062  105.314 1.00 23.22 ? 18   PHE A CD1   1 
ATOM   32    C  CD2   . PHE A 1  20   ? -44.453 81.178  107.384 1.00 26.64 ? 18   PHE A CD2   1 
ATOM   33    C  CE1   . PHE A 1  20   ? -42.708 80.098  105.538 1.00 25.50 ? 18   PHE A CE1   1 
ATOM   34    C  CE2   . PHE A 1  20   ? -43.087 81.215  107.614 1.00 24.34 ? 18   PHE A CE2   1 
ATOM   35    C  CZ    . PHE A 1  20   ? -42.218 80.680  106.691 1.00 26.98 ? 18   PHE A CZ    1 
ATOM   36    N  N     . ALA A 1  21   ? -49.180 82.376  104.534 1.00 29.17 ? 19   ALA A N     1 
ATOM   37    C  CA    . ALA A 1  21   ? -50.604 82.226  104.261 1.00 28.81 ? 19   ALA A CA    1 
ATOM   38    C  C     . ALA A 1  21   ? -50.875 81.644  102.880 1.00 30.87 ? 19   ALA A C     1 
ATOM   39    O  O     . ALA A 1  21   ? -51.988 81.171  102.627 1.00 32.11 ? 19   ALA A O     1 
ATOM   40    C  CB    . ALA A 1  21   ? -51.309 83.573  104.404 1.00 31.93 ? 19   ALA A CB    1 
ATOM   41    N  N     . ASP A 1  22   ? -49.892 81.666  101.986 1.00 25.97 ? 20   ASP A N     1 
ATOM   42    C  CA    . ASP A 1  22   ? -50.034 81.124  100.640 1.00 29.56 ? 20   ASP A CA    1 
ATOM   43    C  C     . ASP A 1  22   ? -48.838 80.249  100.304 1.00 23.82 ? 20   ASP A C     1 
ATOM   44    O  O     . ASP A 1  22   ? -48.322 80.257  99.181  1.00 24.96 ? 20   ASP A O     1 
ATOM   45    C  CB    . ASP A 1  22   ? -50.198 82.245  99.618  1.00 33.14 ? 20   ASP A CB    1 
ATOM   46    C  CG    . ASP A 1  22   ? -50.560 81.728  98.236  1.00 39.21 ? 20   ASP A CG    1 
ATOM   47    O  OD1   . ASP A 1  22   ? -51.581 81.013  98.108  1.00 43.35 ? 20   ASP A OD1   1 
ATOM   48    O  OD2   . ASP A 1  22   ? -49.817 82.030  97.278  1.00 43.17 ? 20   ASP A OD2   1 
ATOM   49    N  N     . PHE A 1  23   ? -48.371 79.478  101.285 1.00 21.55 ? 21   PHE A N     1 
ATOM   50    C  CA    . PHE A 1  23   ? -47.092 78.798  101.123 1.00 20.27 ? 21   PHE A CA    1 
ATOM   51    C  C     . PHE A 1  23   ? -47.142 77.782  99.987  1.00 19.63 ? 21   PHE A C     1 
ATOM   52    O  O     . PHE A 1  23   ? -46.265 77.767  99.111  1.00 20.34 ? 21   PHE A O     1 
ATOM   53    C  CB    . PHE A 1  23   ? -46.683 78.122  102.430 1.00 21.23 ? 21   PHE A CB    1 
ATOM   54    C  CG    . PHE A 1  23   ? -45.488 77.239  102.283 1.00 20.41 ? 21   PHE A CG    1 
ATOM   55    C  CD1   . PHE A 1  23   ? -44.248 77.779  101.987 1.00 22.16 ? 21   PHE A CD1   1 
ATOM   56    C  CD2   . PHE A 1  23   ? -45.606 75.864  102.404 1.00 21.14 ? 21   PHE A CD2   1 
ATOM   57    C  CE1   . PHE A 1  23   ? -43.134 76.960  101.815 1.00 19.87 ? 21   PHE A CE1   1 
ATOM   58    C  CE2   . PHE A 1  23   ? -44.496 75.040  102.246 1.00 22.73 ? 21   PHE A CE2   1 
ATOM   59    C  CZ    . PHE A 1  23   ? -43.258 75.594  101.951 1.00 20.64 ? 21   PHE A CZ    1 
ATOM   60    N  N     . ALA A 1  24   ? -48.141 76.903  100.000 1.00 20.00 ? 22   ALA A N     1 
ATOM   61    C  CA    . ALA A 1  24   ? -48.186 75.830  99.010  1.00 21.41 ? 22   ALA A CA    1 
ATOM   62    C  C     . ALA A 1  24   ? -49.580 75.228  98.918  1.00 19.71 ? 22   ALA A C     1 
ATOM   63    O  O     . ALA A 1  24   ? -49.732 74.008  99.072  1.00 20.03 ? 22   ALA A O     1 
ATOM   64    C  CB    . ALA A 1  24   ? -47.182 74.724  99.345  1.00 22.48 ? 22   ALA A CB    1 
ATOM   65    N  N     . PRO A 1  25   ? -50.610 76.028  98.651  1.00 21.98 ? 23   PRO A N     1 
ATOM   66    C  CA    . PRO A 1  25   ? -51.957 75.469  98.532  1.00 22.70 ? 23   PRO A CA    1 
ATOM   67    C  C     . PRO A 1  25   ? -52.021 74.495  97.373  1.00 20.67 ? 23   PRO A C     1 
ATOM   68    O  O     . PRO A 1  25   ? -51.464 74.761  96.299  1.00 20.64 ? 23   PRO A O     1 
ATOM   69    C  CB    . PRO A 1  25   ? -52.834 76.702  98.271  1.00 25.39 ? 23   PRO A CB    1 
ATOM   70    C  CG    . PRO A 1  25   ? -51.924 77.631  97.555  1.00 25.04 ? 23   PRO A CG    1 
ATOM   71    C  CD    . PRO A 1  25   ? -50.575 77.440  98.233  1.00 24.29 ? 23   PRO A CD    1 
ATOM   72    N  N     . PRO A 1  26   ? -52.672 73.352  97.551  1.00 21.79 ? 24   PRO A N     1 
ATOM   73    C  CA    . PRO A 1  26   ? -52.795 72.400  96.445  1.00 19.75 ? 24   PRO A CA    1 
ATOM   74    C  C     . PRO A 1  26   ? -53.650 72.959  95.319  1.00 21.06 ? 24   PRO A C     1 
ATOM   75    O  O     . PRO A 1  26   ? -54.481 73.858  95.504  1.00 21.24 ? 24   PRO A O     1 
ATOM   76    C  CB    . PRO A 1  26   ? -53.459 71.181  97.094  1.00 21.00 ? 24   PRO A CB    1 
ATOM   77    C  CG    . PRO A 1  26   ? -54.218 71.758  98.265  1.00 25.00 ? 24   PRO A CG    1 
ATOM   78    C  CD    . PRO A 1  26   ? -53.388 72.911  98.761  1.00 22.76 ? 24   PRO A CD    1 
ATOM   79    N  N     . VAL A 1  27   ? -53.413 72.401  94.125  1.00 22.00 ? 25   VAL A N     1 
ATOM   80    C  CA    . VAL A 1  27   ? -54.187 72.755  92.937  1.00 22.28 ? 25   VAL A CA    1 
ATOM   81    C  C     . VAL A 1  27   ? -55.678 72.652  93.218  1.00 23.20 ? 25   VAL A C     1 
ATOM   82    O  O     . VAL A 1  27   ? -56.462 73.513  92.804  1.00 23.68 ? 25   VAL A O     1 
ATOM   83    C  CB    . VAL A 1  27   ? -53.782 71.854  91.751  1.00 21.94 ? 25   VAL A CB    1 
ATOM   84    C  CG1   . VAL A 1  27   ? -54.758 72.013  90.593  1.00 22.25 ? 25   VAL A CG1   1 
ATOM   85    C  CG2   . VAL A 1  27   ? -52.351 72.161  91.291  1.00 19.93 ? 25   VAL A CG2   1 
ATOM   86    N  N     . ARG A 1  28   ? -56.093 71.599  93.913  1.00 24.48 ? 26   ARG A N     1 
ATOM   87    C  CA    . ARG A 1  28   ? -57.495 71.370  94.228  1.00 24.60 ? 26   ARG A CA    1 
ATOM   88    C  C     . ARG A 1  28   ? -57.575 70.650  95.564  1.00 28.53 ? 26   ARG A C     1 
ATOM   89    O  O     . ARG A 1  28   ? -56.588 70.049  96.010  1.00 23.62 ? 26   ARG A O     1 
ATOM   90    C  CB    . ARG A 1  28   ? -58.178 70.538  93.134  1.00 28.60 ? 26   ARG A CB    1 
ATOM   91    C  CG    . ARG A 1  28   ? -57.794 69.060  93.165  1.00 28.67 ? 26   ARG A CG    1 
ATOM   92    C  CD    . ARG A 1  28   ? -58.448 68.269  92.032  1.00 30.04 ? 26   ARG A CD    1 
ATOM   93    N  NE    . ARG A 1  28   ? -57.710 68.427  90.783  1.00 32.92 ? 26   ARG A NE    1 
ATOM   94    C  CZ    . ARG A 1  28   ? -58.029 69.296  89.834  1.00 32.46 ? 26   ARG A CZ    1 
ATOM   95    N  NH1   . ARG A 1  28   ? -59.095 70.075  89.939  1.00 33.20 ? 26   ARG A NH1   1 
ATOM   96    N  NH2   . ARG A 1  28   ? -57.255 69.396  88.761  1.00 31.20 ? 26   ARG A NH2   1 
ATOM   97    N  N     . PRO A 1  29   ? -58.730 70.686  96.231  1.00 24.68 ? 27   PRO A N     1 
ATOM   98    C  CA    . PRO A 1  29   ? -58.877 69.886  97.448  1.00 27.01 ? 27   PRO A CA    1 
ATOM   99    C  C     . PRO A 1  29   ? -58.669 68.416  97.128  1.00 23.00 ? 27   PRO A C     1 
ATOM   100   O  O     . PRO A 1  29   ? -59.108 67.923  96.088  1.00 26.85 ? 27   PRO A O     1 
ATOM   101   C  CB    . PRO A 1  29   ? -60.315 70.179  97.899  1.00 27.89 ? 27   PRO A CB    1 
ATOM   102   C  CG    . PRO A 1  29   ? -60.616 71.529  97.326  1.00 28.21 ? 27   PRO A CG    1 
ATOM   103   C  CD    . PRO A 1  29   ? -59.918 71.531  95.989  1.00 27.99 ? 27   PRO A CD    1 
ATOM   104   N  N     . GLN A 1  30   ? -57.976 67.722  98.024  1.00 25.12 ? 28   GLN A N     1 
ATOM   105   C  CA    . GLN A 1  30   ? -57.605 66.338  97.772  1.00 26.22 ? 28   GLN A CA    1 
ATOM   106   C  C     . GLN A 1  30   ? -58.790 65.433  98.089  1.00 25.78 ? 28   GLN A C     1 
ATOM   107   O  O     . GLN A 1  30   ? -59.254 65.384  99.231  1.00 27.49 ? 28   GLN A O     1 
ATOM   108   C  CB    . GLN A 1  30   ? -56.382 65.954  98.602  1.00 24.72 ? 28   GLN A CB    1 
ATOM   109   C  CG    . GLN A 1  30   ? -55.178 66.867  98.365  1.00 21.80 ? 28   GLN A CG    1 
ATOM   110   C  CD    . GLN A 1  30   ? -54.652 66.785  96.942  1.00 23.32 ? 28   GLN A CD    1 
ATOM   111   O  OE1   . GLN A 1  30   ? -53.934 65.850  96.598  1.00 23.17 ? 28   GLN A OE1   1 
ATOM   112   N  NE2   . GLN A 1  30   ? -55.011 67.761  96.108  1.00 22.24 ? 28   GLN A NE2   1 
ATOM   113   N  N     . SER A 1  31   ? -59.278 64.726  97.077  1.00 26.57 ? 29   SER A N     1 
ATOM   114   C  CA    . SER A 1  31   ? -60.354 63.768  97.279  1.00 25.38 ? 29   SER A CA    1 
ATOM   115   C  C     . SER A 1  31   ? -59.865 62.585  98.111  1.00 26.64 ? 29   SER A C     1 
ATOM   116   O  O     . SER A 1  31   ? -58.665 62.400  98.343  1.00 23.76 ? 29   SER A O     1 
ATOM   117   C  CB    . SER A 1  31   ? -60.887 63.274  95.934  1.00 24.97 ? 29   SER A CB    1 
ATOM   118   O  OG    . SER A 1  31   ? -59.905 62.492  95.265  1.00 21.79 ? 29   SER A OG    1 
ATOM   119   N  N     . THR A 1  32   ? -60.822 61.769  98.564  1.00 23.19 ? 30   THR A N     1 
ATOM   120   C  CA    . THR A 1  32   ? -60.474 60.527  99.248  1.00 23.06 ? 30   THR A CA    1 
ATOM   121   C  C     . THR A 1  32   ? -59.536 59.677  98.401  1.00 21.20 ? 30   THR A C     1 
ATOM   122   O  O     . THR A 1  32   ? -58.547 59.131  98.909  1.00 23.85 ? 30   THR A O     1 
ATOM   123   C  CB    . THR A 1  32   ? -61.740 59.733  99.575  1.00 27.23 ? 30   THR A CB    1 
ATOM   124   O  OG1   . THR A 1  32   ? -62.563 60.496  100.463 1.00 33.02 ? 30   THR A OG1   1 
ATOM   125   C  CG2   . THR A 1  32   ? -61.386 58.407  100.216 1.00 26.80 ? 30   THR A CG2   1 
ATOM   126   N  N     . LEU A 1  33   ? -59.828 59.558  97.105  1.00 24.23 ? 31   LEU A N     1 
ATOM   127   C  CA    . LEU A 1  33   ? -58.977 58.761  96.227  1.00 21.66 ? 31   LEU A CA    1 
ATOM   128   C  C     . LEU A 1  33   ? -57.603 59.394  96.055  1.00 23.23 ? 31   LEU A C     1 
ATOM   129   O  O     . LEU A 1  33   ? -56.591 58.685  96.009  1.00 20.24 ? 31   LEU A O     1 
ATOM   130   C  CB    . LEU A 1  33   ? -59.655 58.571  94.873  1.00 22.36 ? 31   LEU A CB    1 
ATOM   131   C  CG    . LEU A 1  33   ? -60.818 57.575  94.904  1.00 22.37 ? 31   LEU A CG    1 
ATOM   132   C  CD1   . LEU A 1  33   ? -61.579 57.613  93.603  1.00 21.11 ? 31   LEU A CD1   1 
ATOM   133   C  CD2   . LEU A 1  33   ? -60.286 56.170  95.166  1.00 25.77 ? 31   LEU A CD2   1 
ATOM   134   N  N     . ARG A 1  34   ? -57.545 60.724  95.936  1.00 20.18 ? 32   ARG A N     1 
ATOM   135   C  CA    . ARG A 1  34   ? -56.245 61.385  95.836  1.00 21.70 ? 32   ARG A CA    1 
ATOM   136   C  C     . ARG A 1  34   ? -55.451 61.213  97.119  1.00 19.80 ? 32   ARG A C     1 
ATOM   137   O  O     . ARG A 1  34   ? -54.238 60.984  97.081  1.00 19.99 ? 32   ARG A O     1 
ATOM   138   C  CB    . ARG A 1  34   ? -56.433 62.871  95.528  1.00 22.03 ? 32   ARG A CB    1 
ATOM   139   C  CG    . ARG A 1  34   ? -56.796 63.168  94.087  1.00 23.03 ? 32   ARG A CG    1 
ATOM   140   C  CD    . ARG A 1  34   ? -55.631 62.887  93.121  1.00 21.84 ? 32   ARG A CD    1 
ATOM   141   N  NE    . ARG A 1  34   ? -54.504 63.812  93.241  1.00 21.11 ? 32   ARG A NE    1 
ATOM   142   C  CZ    . ARG A 1  34   ? -54.425 64.983  92.618  1.00 22.53 ? 32   ARG A CZ    1 
ATOM   143   N  NH1   . ARG A 1  34   ? -55.412 65.431  91.853  1.00 23.24 ? 32   ARG A NH1   1 
ATOM   144   N  NH2   . ARG A 1  34   ? -53.330 65.729  92.766  1.00 20.83 ? 32   ARG A NH2   1 
ATOM   145   N  N     . ARG A 1  35   ? -56.120 61.317  98.270  1.00 21.40 ? 33   ARG A N     1 
ATOM   146   C  CA    . ARG A 1  35   ? -55.426 61.176  99.544  1.00 21.51 ? 33   ARG A CA    1 
ATOM   147   C  C     . ARG A 1  35   ? -54.868 59.775  99.734  1.00 23.39 ? 33   ARG A C     1 
ATOM   148   O  O     . ARG A 1  35   ? -53.811 59.615  100.353 1.00 21.28 ? 33   ARG A O     1 
ATOM   149   C  CB    . ARG A 1  35   ? -56.369 61.538  100.696 1.00 23.46 ? 33   ARG A CB    1 
ATOM   150   C  CG    . ARG A 1  35   ? -56.647 63.024  100.760 1.00 25.10 ? 33   ARG A CG    1 
ATOM   151   C  CD    . ARG A 1  35   ? -57.664 63.401  101.837 1.00 32.97 ? 33   ARG A CD    1 
ATOM   152   N  NE    . ARG A 1  35   ? -57.713 64.854  101.939 1.00 38.27 ? 33   ARG A NE    1 
ATOM   153   C  CZ    . ARG A 1  35   ? -56.865 65.578  102.658 1.00 42.58 ? 33   ARG A CZ    1 
ATOM   154   N  NH1   . ARG A 1  35   ? -55.953 65.009  103.430 1.00 43.15 ? 33   ARG A NH1   1 
ATOM   155   N  NH2   . ARG A 1  35   ? -56.928 66.907  102.594 1.00 45.45 ? 33   ARG A NH2   1 
ATOM   156   N  N     . ALA A 1  36   ? -55.552 58.753  99.213  1.00 20.65 ? 34   ALA A N     1 
ATOM   157   C  CA    . ALA A 1  36   ? -55.029 57.396  99.347  1.00 21.92 ? 34   ALA A CA    1 
ATOM   158   C  C     . ALA A 1  36   ? -53.779 57.194  98.501  1.00 22.23 ? 34   ALA A C     1 
ATOM   159   O  O     . ALA A 1  36   ? -52.906 56.402  98.872  1.00 23.23 ? 34   ALA A O     1 
ATOM   160   C  CB    . ALA A 1  36   ? -56.097 56.368  98.978  1.00 21.43 ? 34   ALA A CB    1 
ATOM   161   N  N     . ILE A 1  37   ? -53.669 57.904  97.377  1.00 19.46 ? 35   ILE A N     1 
ATOM   162   C  CA    . ILE A 1  37   ? -52.414 57.921  96.620  1.00 17.18 ? 35   ILE A CA    1 
ATOM   163   C  C     . ILE A 1  37   ? -51.293 58.504  97.469  1.00 17.79 ? 35   ILE A C     1 
ATOM   164   O  O     . ILE A 1  37   ? -50.234 57.893  97.650  1.00 17.59 ? 35   ILE A O     1 
ATOM   165   C  CB    . ILE A 1  37   ? -52.590 58.727  95.324  1.00 16.70 ? 35   ILE A CB    1 
ATOM   166   C  CG1   . ILE A 1  37   ? -53.621 58.045  94.436  1.00 19.40 ? 35   ILE A CG1   1 
ATOM   167   C  CG2   . ILE A 1  37   ? -51.236 58.899  94.609  1.00 16.49 ? 35   ILE A CG2   1 
ATOM   168   C  CD1   . ILE A 1  37   ? -54.039 58.910  93.263  1.00 16.28 ? 35   ILE A CD1   1 
ATOM   169   N  N     . THR A 1  38   ? -51.505 59.718  97.980  1.00 19.13 ? 36   THR A N     1 
ATOM   170   C  CA    . THR A 1  38   ? -50.459 60.391  98.738  1.00 19.48 ? 36   THR A CA    1 
ATOM   171   C  C     . THR A 1  38   ? -50.032 59.562  99.945  1.00 20.19 ? 36   THR A C     1 
ATOM   172   O  O     . THR A 1  38   ? -48.842 59.505  100.286 1.00 19.82 ? 36   THR A O     1 
ATOM   173   C  CB    . THR A 1  38   ? -50.960 61.763  99.165  1.00 20.52 ? 36   THR A CB    1 
ATOM   174   O  OG1   . THR A 1  38   ? -51.482 62.444  98.019  1.00 19.27 ? 36   THR A OG1   1 
ATOM   175   C  CG2   . THR A 1  38   ? -49.834 62.579  99.731  1.00 19.90 ? 36   THR A CG2   1 
ATOM   176   N  N     . ALA A 1  39   ? -50.988 58.891  100.588 1.00 19.36 ? 37   ALA A N     1 
ATOM   177   C  CA    . ALA A 1  39   ? -50.663 58.092  101.761 1.00 23.20 ? 37   ALA A CA    1 
ATOM   178   C  C     . ALA A 1  39   ? -49.705 56.943  101.455 1.00 22.15 ? 37   ALA A C     1 
ATOM   179   O  O     . ALA A 1  39   ? -48.979 56.508  102.355 1.00 22.59 ? 37   ALA A O     1 
ATOM   180   C  CB    . ALA A 1  39   ? -51.950 57.556  102.391 1.00 22.30 ? 37   ALA A CB    1 
ATOM   181   N  N     . ALA A 1  40   ? -49.663 56.459  100.213 1.00 20.09 ? 38   ALA A N     1 
ATOM   182   C  CA    . ALA A 1  40   ? -48.834 55.316  99.855  1.00 20.21 ? 38   ALA A CA    1 
ATOM   183   C  C     . ALA A 1  40   ? -47.469 55.715  99.323  1.00 20.28 ? 38   ALA A C     1 
ATOM   184   O  O     . ALA A 1  40   ? -46.672 54.828  99.003  1.00 21.31 ? 38   ALA A O     1 
ATOM   185   C  CB    . ALA A 1  40   ? -49.535 54.458  98.802  1.00 20.39 ? 38   ALA A CB    1 
ATOM   186   N  N     . TYR A 1  41   ? -47.189 57.019  99.241  1.00 20.56 ? 39   TYR A N     1 
ATOM   187   C  CA    . TYR A 1  41   ? -46.014 57.535  98.533  1.00 20.30 ? 39   TYR A CA    1 
ATOM   188   C  C     . TYR A 1  41   ? -44.732 56.802  98.926  1.00 19.88 ? 39   TYR A C     1 
ATOM   189   O  O     . TYR A 1  41   ? -43.976 56.338  98.062  1.00 20.18 ? 39   TYR A O     1 
ATOM   190   C  CB    . TYR A 1  41   ? -45.899 59.036  98.820  1.00 20.73 ? 39   TYR A CB    1 
ATOM   191   C  CG    . TYR A 1  41   ? -45.115 59.901  97.832  1.00 18.35 ? 39   TYR A CG    1 
ATOM   192   C  CD1   . TYR A 1  41   ? -44.006 59.419  97.150  1.00 16.52 ? 39   TYR A CD1   1 
ATOM   193   C  CD2   . TYR A 1  41   ? -45.486 61.225  97.627  1.00 18.27 ? 39   TYR A CD2   1 
ATOM   194   C  CE1   . TYR A 1  41   ? -43.296 60.241  96.278  1.00 15.62 ? 39   TYR A CE1   1 
ATOM   195   C  CE2   . TYR A 1  41   ? -44.796 62.047  96.766  1.00 17.81 ? 39   TYR A CE2   1 
ATOM   196   C  CZ    . TYR A 1  41   ? -43.692 61.553  96.094  1.00 14.88 ? 39   TYR A CZ    1 
ATOM   197   O  OH    . TYR A 1  41   ? -43.000 62.392  95.238  1.00 16.10 ? 39   TYR A OH    1 
ATOM   198   N  N     . ARG A 1  42   ? -44.459 56.708  100.226 1.00 21.90 ? 40   ARG A N     1 
ATOM   199   C  CA    . ARG A 1  42   ? -43.249 56.049  100.710 1.00 21.72 ? 40   ARG A CA    1 
ATOM   200   C  C     . ARG A 1  42   ? -43.581 54.945  101.708 1.00 22.30 ? 40   ARG A C     1 
ATOM   201   O  O     . ARG A 1  42   ? -42.820 54.680  102.650 1.00 22.74 ? 40   ARG A O     1 
ATOM   202   C  CB    . ARG A 1  42   ? -42.283 57.079  101.290 1.00 23.43 ? 40   ARG A CB    1 
ATOM   203   C  CG    . ARG A 1  42   ? -41.654 57.917  100.175 1.00 22.13 ? 40   ARG A CG    1 
ATOM   204   C  CD    . ARG A 1  42   ? -40.937 59.152  100.656 1.00 23.19 ? 40   ARG A CD    1 
ATOM   205   N  NE    . ARG A 1  42   ? -40.964 60.162  99.607  1.00 22.18 ? 40   ARG A NE    1 
ATOM   206   C  CZ    . ARG A 1  42   ? -40.118 60.217  98.589  1.00 19.81 ? 40   ARG A CZ    1 
ATOM   207   N  NH1   . ARG A 1  42   ? -39.086 59.384  98.496  1.00 18.65 ? 40   ARG A NH1   1 
ATOM   208   N  NH2   . ARG A 1  42   ? -40.317 61.121  97.635  1.00 19.33 ? 40   ARG A NH2   1 
ATOM   209   N  N     . ARG A 1  43   ? -44.689 54.252  101.466 1.00 22.03 ? 41   ARG A N     1 
ATOM   210   C  CA    . ARG A 1  43   ? -45.142 53.184  102.350 1.00 20.29 ? 41   ARG A CA    1 
ATOM   211   C  C     . ARG A 1  43   ? -44.078 52.092  102.444 1.00 22.81 ? 41   ARG A C     1 
ATOM   212   O  O     . ARG A 1  43   ? -43.451 51.751  101.436 1.00 22.17 ? 41   ARG A O     1 
ATOM   213   C  CB    . ARG A 1  43   ? -46.453 52.600  101.824 1.00 21.15 ? 41   ARG A CB    1 
ATOM   214   C  CG    . ARG A 1  43   ? -46.976 51.397  102.592 1.00 24.18 ? 41   ARG A CG    1 
ATOM   215   C  CD    . ARG A 1  43   ? -48.390 51.136  102.195 1.00 27.08 ? 41   ARG A CD    1 
ATOM   216   N  NE    . ARG A 1  43   ? -49.231 52.269  102.556 1.00 24.82 ? 41   ARG A NE    1 
ATOM   217   C  CZ    . ARG A 1  43   ? -50.350 52.596  101.930 1.00 22.43 ? 41   ARG A CZ    1 
ATOM   218   N  NH1   . ARG A 1  43   ? -50.760 51.933  100.864 1.00 25.83 ? 41   ARG A NH1   1 
ATOM   219   N  NH2   . ARG A 1  43   ? -51.081 53.606  102.394 1.00 25.68 ? 41   ARG A NH2   1 
ATOM   220   N  N     . PRO A 1  44   ? -43.843 51.529  103.628 1.00 24.41 ? 42   PRO A N     1 
ATOM   221   C  CA    . PRO A 1  44   ? -42.839 50.468  103.751 1.00 25.87 ? 42   PRO A CA    1 
ATOM   222   C  C     . PRO A 1  44   ? -43.102 49.334  102.770 1.00 22.25 ? 42   PRO A C     1 
ATOM   223   O  O     . PRO A 1  44   ? -44.244 48.952  102.516 1.00 23.54 ? 42   PRO A O     1 
ATOM   224   C  CB    . PRO A 1  44   ? -42.991 50.005  105.206 1.00 27.36 ? 42   PRO A CB    1 
ATOM   225   C  CG    . PRO A 1  44   ? -43.501 51.215  105.923 1.00 28.52 ? 42   PRO A CG    1 
ATOM   226   C  CD    . PRO A 1  44   ? -44.428 51.895  104.933 1.00 27.82 ? 42   PRO A CD    1 
ATOM   227   N  N     . GLU A 1  45   ? -42.014 48.805  102.206 1.00 25.34 ? 43   GLU A N     1 
ATOM   228   C  CA    . GLU A 1  45   ? -42.133 47.798  101.158 1.00 23.59 ? 43   GLU A CA    1 
ATOM   229   C  C     . GLU A 1  45   ? -42.848 46.546  101.664 1.00 25.02 ? 43   GLU A C     1 
ATOM   230   O  O     . GLU A 1  45   ? -43.632 45.930  100.934 1.00 27.03 ? 43   GLU A O     1 
ATOM   231   C  CB    . GLU A 1  45   ? -40.734 47.475  100.618 1.00 25.91 ? 43   GLU A CB    1 
ATOM   232   C  CG    . GLU A 1  45   ? -40.725 46.929  99.217  1.00 27.26 ? 43   GLU A CG    1 
ATOM   233   C  CD    . GLU A 1  45   ? -39.430 47.210  98.455  1.00 23.45 ? 43   GLU A CD    1 
ATOM   234   O  OE1   . GLU A 1  45   ? -38.513 47.914  98.961  1.00 22.92 ? 43   GLU A OE1   1 
ATOM   235   O  OE2   . GLU A 1  45   ? -39.342 46.705  97.324  1.00 21.78 ? 43   GLU A OE2   1 
ATOM   236   N  N     . THR A 1  46   ? -42.611 46.166  102.919 1.00 26.74 ? 44   THR A N     1 
ATOM   237   C  CA    . THR A 1  46   ? -43.304 45.013  103.490 1.00 27.07 ? 44   THR A CA    1 
ATOM   238   C  C     . THR A 1  46   ? -44.807 45.233  103.605 1.00 28.52 ? 44   THR A C     1 
ATOM   239   O  O     . THR A 1  46   ? -45.568 44.257  103.645 1.00 28.36 ? 44   THR A O     1 
ATOM   240   C  CB    . THR A 1  46   ? -42.723 44.683  104.863 1.00 25.37 ? 44   THR A CB    1 
ATOM   241   O  OG1   . THR A 1  46   ? -42.699 45.870  105.669 1.00 27.73 ? 44   THR A OG1   1 
ATOM   242   C  CG2   . THR A 1  46   ? -41.310 44.127  104.728 1.00 29.00 ? 44   THR A CG2   1 
ATOM   243   N  N     . GLU A 1  47   ? -45.260 46.485  103.654 1.00 27.93 ? 45   GLU A N     1 
ATOM   244   C  CA    . GLU A 1  47   ? -46.694 46.745  103.698 1.00 28.43 ? 45   GLU A CA    1 
ATOM   245   C  C     . GLU A 1  47   ? -47.319 46.789  102.315 1.00 24.40 ? 45   GLU A C     1 
ATOM   246   O  O     . GLU A 1  47   ? -48.502 46.466  102.167 1.00 25.99 ? 45   GLU A O     1 
ATOM   247   C  CB    . GLU A 1  47   ? -46.976 48.061  104.422 1.00 30.50 ? 45   GLU A CB    1 
ATOM   248   C  CG    . GLU A 1  47   ? -46.432 48.078  105.832 1.00 36.36 ? 45   GLU A CG    1 
ATOM   249   C  CD    . GLU A 1  47   ? -46.764 49.353  106.562 1.00 38.43 ? 45   GLU A CD    1 
ATOM   250   O  OE1   . GLU A 1  47   ? -47.606 50.124  106.050 1.00 36.56 ? 45   GLU A OE1   1 
ATOM   251   O  OE2   . GLU A 1  47   ? -46.181 49.572  107.647 1.00 44.24 ? 45   GLU A OE2   1 
ATOM   252   N  N     . CYS A 1  48   ? -46.538 47.151  101.298 1.00 24.89 ? 46   CYS A N     1 
ATOM   253   C  CA    . CYS A 1  48   ? -47.086 47.236  99.952  1.00 24.74 ? 46   CYS A CA    1 
ATOM   254   C  C     . CYS A 1  48   ? -47.374 45.861  99.371  1.00 24.44 ? 46   CYS A C     1 
ATOM   255   O  O     . CYS A 1  48   ? -48.345 45.690  98.629  1.00 22.76 ? 46   CYS A O     1 
ATOM   256   C  CB    . CYS A 1  48   ? -46.117 47.984  99.034  1.00 22.71 ? 46   CYS A CB    1 
ATOM   257   S  SG    . CYS A 1  48   ? -45.858 49.698  99.492  1.00 24.44 ? 46   CYS A SG    1 
ATOM   258   N  N     . LEU A 1  49   ? -46.519 44.872  99.660  1.00 24.50 ? 47   LEU A N     1 
ATOM   259   C  CA    . LEU A 1  49   ? -46.541 43.662  98.840  1.00 25.28 ? 47   LEU A CA    1 
ATOM   260   C  C     . LEU A 1  49   ? -47.729 42.728  99.086  1.00 25.04 ? 47   LEU A C     1 
ATOM   261   O  O     . LEU A 1  49   ? -48.297 42.225  98.108  1.00 25.70 ? 47   LEU A O     1 
ATOM   262   C  CB    . LEU A 1  49   ? -45.226 42.888  99.005  1.00 26.86 ? 47   LEU A CB    1 
ATOM   263   C  CG    . LEU A 1  49   ? -44.190 43.183  97.919  1.00 27.15 ? 47   LEU A CG    1 
ATOM   264   C  CD1   . LEU A 1  49   ? -44.631 42.619  96.575  1.00 26.48 ? 47   LEU A CD1   1 
ATOM   265   C  CD2   . LEU A 1  49   ? -43.941 44.681  97.787  1.00 23.75 ? 47   LEU A CD2   1 
ATOM   266   N  N     . PRO A 1  50   ? -48.147 42.463  100.325 1.00 27.50 ? 48   PRO A N     1 
ATOM   267   C  CA    . PRO A 1  50   ? -49.187 41.431  100.548 1.00 26.53 ? 48   PRO A CA    1 
ATOM   268   C  C     . PRO A 1  50   ? -50.465 41.683  99.759  1.00 26.05 ? 48   PRO A C     1 
ATOM   269   O  O     . PRO A 1  50   ? -50.985 40.742  99.139  1.00 28.89 ? 48   PRO A O     1 
ATOM   270   C  CB    . PRO A 1  50   ? -49.422 41.492  102.066 1.00 29.00 ? 48   PRO A CB    1 
ATOM   271   C  CG    . PRO A 1  50   ? -48.086 41.852  102.602 1.00 29.36 ? 48   PRO A CG    1 
ATOM   272   C  CD    . PRO A 1  50   ? -47.538 42.881  101.604 1.00 28.10 ? 48   PRO A CD    1 
ATOM   273   N  N     . PRO A 1  51   ? -51.018 42.910  99.727  1.00 25.78 ? 49   PRO A N     1 
ATOM   274   C  CA    . PRO A 1  51   ? -52.208 43.104  98.876  1.00 28.33 ? 49   PRO A CA    1 
ATOM   275   C  C     . PRO A 1  51   ? -51.926 42.897  97.397  1.00 26.16 ? 49   PRO A C     1 
ATOM   276   O  O     . PRO A 1  51   ? -52.824 42.454  96.665  1.00 25.44 ? 49   PRO A O     1 
ATOM   277   C  CB    . PRO A 1  51   ? -52.645 44.547  99.179  1.00 27.18 ? 49   PRO A CB    1 
ATOM   278   C  CG    . PRO A 1  51   ? -51.471 45.198  99.747  1.00 27.91 ? 49   PRO A CG    1 
ATOM   279   C  CD    . PRO A 1  51   ? -50.713 44.132  100.491 1.00 26.77 ? 49   PRO A CD    1 
ATOM   280   N  N     . LEU A 1  52   ? -50.705 43.196  96.936  1.00 26.30 ? 50   LEU A N     1 
ATOM   281   C  CA    . LEU A 1  52   ? -50.365 42.968  95.534  1.00 25.37 ? 50   LEU A CA    1 
ATOM   282   C  C     . LEU A 1  52   ? -50.248 41.477  95.243  1.00 23.85 ? 50   LEU A C     1 
ATOM   283   O  O     . LEU A 1  52   ? -50.703 41.001  94.197  1.00 25.31 ? 50   LEU A O     1 
ATOM   284   C  CB    . LEU A 1  52   ? -49.060 43.690  95.181  1.00 24.45 ? 50   LEU A CB    1 
ATOM   285   C  CG    . LEU A 1  52   ? -49.034 45.204  95.408  1.00 25.22 ? 50   LEU A CG    1 
ATOM   286   C  CD1   . LEU A 1  52   ? -47.643 45.773  95.128  1.00 26.66 ? 50   LEU A CD1   1 
ATOM   287   C  CD2   . LEU A 1  52   ? -50.086 45.898  94.551  1.00 28.28 ? 50   LEU A CD2   1 
ATOM   288   N  N     . VAL A 1  53   ? -49.640 40.726  96.161  1.00 24.82 ? 51   VAL A N     1 
ATOM   289   C  CA    . VAL A 1  53   ? -49.591 39.273  96.026  1.00 26.65 ? 51   VAL A CA    1 
ATOM   290   C  C     . VAL A 1  53   ? -50.998 38.699  95.912  1.00 27.31 ? 51   VAL A C     1 
ATOM   291   O  O     . VAL A 1  53   ? -51.274 37.859  95.044  1.00 26.68 ? 51   VAL A O     1 
ATOM   292   C  CB    . VAL A 1  53   ? -48.817 38.659  97.206  1.00 24.41 ? 51   VAL A CB    1 
ATOM   293   C  CG1   . VAL A 1  53   ? -48.942 37.148  97.199  1.00 29.75 ? 51   VAL A CG1   1 
ATOM   294   C  CG2   . VAL A 1  53   ? -47.351 39.076  97.150  1.00 25.70 ? 51   VAL A CG2   1 
ATOM   295   N  N     . GLU A 1  54   ? -51.923 39.167  96.752  1.00 25.66 ? 52   GLU A N     1 
ATOM   296   C  CA    . GLU A 1  54   ? -53.279 38.625  96.694  1.00 28.65 ? 52   GLU A CA    1 
ATOM   297   C  C     . GLU A 1  54   ? -53.955 38.976  95.375  1.00 25.95 ? 52   GLU A C     1 
ATOM   298   O  O     . GLU A 1  54   ? -54.548 38.106  94.724  1.00 28.39 ? 52   GLU A O     1 
ATOM   299   C  CB    . GLU A 1  54   ? -54.110 39.117  97.878  1.00 30.81 ? 52   GLU A CB    1 
ATOM   300   C  CG    . GLU A 1  54   ? -55.560 38.614  97.849  1.00 31.40 ? 52   GLU A CG    1 
ATOM   301   C  CD    . GLU A 1  54   ? -55.685 37.084  97.847  1.00 34.93 ? 52   GLU A CD    1 
ATOM   302   O  OE1   . GLU A 1  54   ? -54.857 36.389  98.480  1.00 37.42 ? 52   GLU A OE1   1 
ATOM   303   O  OE2   . GLU A 1  54   ? -56.630 36.570  97.212  1.00 35.57 ? 52   GLU A OE2   1 
ATOM   304   N  N     . ALA A 1  55   ? -53.854 40.242  94.947  1.00 24.92 ? 53   ALA A N     1 
ATOM   305   C  CA    . ALA A 1  55   ? -54.534 40.662  93.725  1.00 26.94 ? 53   ALA A CA    1 
ATOM   306   C  C     . ALA A 1  55   ? -53.955 39.978  92.495  1.00 26.88 ? 53   ALA A C     1 
ATOM   307   O  O     . ALA A 1  55   ? -54.665 39.788  91.500  1.00 26.30 ? 53   ALA A O     1 
ATOM   308   C  CB    . ALA A 1  55   ? -54.449 42.179  93.574  1.00 29.13 ? 53   ALA A CB    1 
ATOM   309   N  N     . ALA A 1  56   ? -52.683 39.596  92.551  1.00 25.44 ? 54   ALA A N     1 
ATOM   310   C  CA    . ALA A 1  56   ? -51.981 38.988  91.430  1.00 25.17 ? 54   ALA A CA    1 
ATOM   311   C  C     . ALA A 1  56   ? -52.093 37.470  91.408  1.00 29.46 ? 54   ALA A C     1 
ATOM   312   O  O     . ALA A 1  56   ? -51.546 36.833  90.500  1.00 28.70 ? 54   ALA A O     1 
ATOM   313   C  CB    . ALA A 1  56   ? -50.503 39.380  91.465  1.00 26.34 ? 54   ALA A CB    1 
ATOM   314   N  N     . THR A 1  57   ? -52.767 36.878  92.385  1.00 27.65 ? 55   THR A N     1 
ATOM   315   C  CA    . THR A 1  57   ? -52.835 35.428  92.474  1.00 27.64 ? 55   THR A CA    1 
ATOM   316   C  C     . THR A 1  57   ? -53.784 34.879  91.417  1.00 31.12 ? 55   THR A C     1 
ATOM   317   O  O     . THR A 1  57   ? -54.863 35.429  91.184  1.00 30.41 ? 55   THR A O     1 
ATOM   318   C  CB    . THR A 1  57   ? -53.292 35.016  93.871  1.00 29.84 ? 55   THR A CB    1 
ATOM   319   O  OG1   . THR A 1  57   ? -52.278 35.375  94.820  1.00 31.35 ? 55   THR A OG1   1 
ATOM   320   C  CG2   . THR A 1  57   ? -53.551 33.512  93.943  1.00 33.31 ? 55   THR A CG2   1 
ATOM   321   N  N     . GLN A 1  58   ? -53.361 33.802  90.752  1.00 30.25 ? 56   GLN A N     1 
ATOM   322   C  CA    . GLN A 1  58   ? -54.194 33.125  89.771  1.00 30.26 ? 56   GLN A CA    1 
ATOM   323   C  C     . GLN A 1  58   ? -54.229 31.637  90.091  1.00 31.73 ? 56   GLN A C     1 
ATOM   324   O  O     . GLN A 1  58   ? -53.419 31.129  90.869  1.00 32.93 ? 56   GLN A O     1 
ATOM   325   C  CB    . GLN A 1  58   ? -53.687 33.360  88.337  1.00 30.46 ? 56   GLN A CB    1 
ATOM   326   C  CG    . GLN A 1  58   ? -53.612 34.834  87.954  1.00 27.20 ? 56   GLN A CG    1 
ATOM   327   C  CD    . GLN A 1  58   ? -53.471 35.053  86.459  1.00 29.33 ? 56   GLN A CD    1 
ATOM   328   O  OE1   . GLN A 1  58   ? -54.456 35.015  85.716  1.00 28.28 ? 56   GLN A OE1   1 
ATOM   329   N  NE2   . GLN A 1  58   ? -52.240 35.278  86.007  1.00 28.23 ? 56   GLN A NE2   1 
ATOM   330   N  N     . SER A 1  59   ? -55.181 30.944  89.477  1.00 32.96 ? 57   SER A N     1 
ATOM   331   C  CA    . SER A 1  59   ? -55.355 29.525  89.741  1.00 32.09 ? 57   SER A CA    1 
ATOM   332   C  C     . SER A 1  59   ? -54.128 28.742  89.286  1.00 37.37 ? 57   SER A C     1 
ATOM   333   O  O     . SER A 1  59   ? -53.365 29.178  88.415  1.00 33.66 ? 57   SER A O     1 
ATOM   334   C  CB    . SER A 1  59   ? -56.589 29.002  89.018  1.00 32.47 ? 57   SER A CB    1 
ATOM   335   O  OG    . SER A 1  59   ? -56.371 29.031  87.618  1.00 34.62 ? 57   SER A OG    1 
ATOM   336   N  N     . LYS A 1  60   ? -53.943 27.564  89.890  1.00 34.27 ? 58   LYS A N     1 
ATOM   337   C  CA    . LYS A 1  60   ? -52.854 26.692  89.465  1.00 35.36 ? 58   LYS A CA    1 
ATOM   338   C  C     . LYS A 1  60   ? -52.969 26.368  87.982  1.00 35.33 ? 58   LYS A C     1 
ATOM   339   O  O     . LYS A 1  60   ? -51.961 26.334  87.268  1.00 37.45 ? 58   LYS A O     1 
ATOM   340   C  CB    . LYS A 1  60   ? -52.841 25.408  90.301  1.00 40.38 ? 58   LYS A CB    1 
ATOM   341   N  N     . GLU A 1  61   ? -54.193 26.143  87.500  1.00 35.09 ? 59   GLU A N     1 
ATOM   342   C  CA    . GLU A 1  61   ? -54.399 25.892  86.075  1.00 35.65 ? 59   GLU A CA    1 
ATOM   343   C  C     . GLU A 1  61   ? -53.871 27.052  85.238  1.00 36.19 ? 59   GLU A C     1 
ATOM   344   O  O     . GLU A 1  61   ? -53.171 26.848  84.239  1.00 36.77 ? 59   GLU A O     1 
ATOM   345   C  CB    . GLU A 1  61   ? -55.883 25.651  85.790  1.00 35.28 ? 59   GLU A CB    1 
ATOM   346   N  N     . ILE A 1  62   ? -54.180 28.283  85.642  1.00 34.50 ? 60   ILE A N     1 
ATOM   347   C  CA    . ILE A 1  62   ? -53.720 29.439  84.879  1.00 33.18 ? 60   ILE A CA    1 
ATOM   348   C  C     . ILE A 1  62   ? -52.206 29.584  84.973  1.00 34.57 ? 60   ILE A C     1 
ATOM   349   O  O     . ILE A 1  62   ? -51.539 29.874  83.972  1.00 34.36 ? 60   ILE A O     1 
ATOM   350   C  CB    . ILE A 1  62   ? -54.447 30.710  85.346  1.00 31.32 ? 60   ILE A CB    1 
ATOM   351   C  CG1   . ILE A 1  62   ? -55.871 30.706  84.794  1.00 33.64 ? 60   ILE A CG1   1 
ATOM   352   C  CG2   . ILE A 1  62   ? -53.685 31.956  84.904  1.00 31.53 ? 60   ILE A CG2   1 
ATOM   353   C  CD1   . ILE A 1  62   ? -56.615 31.954  85.060  1.00 33.83 ? 60   ILE A CD1   1 
ATOM   354   N  N     . ARG A 1  63   ? -51.636 29.389  86.167  1.00 33.74 ? 61   ARG A N     1 
ATOM   355   C  CA    . ARG A 1  63   ? -50.186 29.504  86.308  1.00 32.52 ? 61   ARG A CA    1 
ATOM   356   C  C     . ARG A 1  63   ? -49.466 28.489  85.426  1.00 33.37 ? 61   ARG A C     1 
ATOM   357   O  O     . ARG A 1  63   ? -48.467 28.818  84.777  1.00 31.04 ? 61   ARG A O     1 
ATOM   358   C  CB    . ARG A 1  63   ? -49.770 29.333  87.771  1.00 34.20 ? 61   ARG A CB    1 
ATOM   359   C  CG    . ARG A 1  63   ? -50.409 30.316  88.734  1.00 36.84 ? 61   ARG A CG    1 
ATOM   360   C  CD    . ARG A 1  63   ? -49.697 30.333  90.082  1.00 42.79 ? 61   ARG A CD    1 
ATOM   361   N  NE    . ARG A 1  63   ? -49.678 29.032  90.738  1.00 42.34 ? 61   ARG A NE    1 
ATOM   362   C  CZ    . ARG A 1  63   ? -50.577 28.634  91.628  1.00 46.73 ? 61   ARG A CZ    1 
ATOM   363   N  NH1   . ARG A 1  63   ? -51.585 29.413  91.988  1.00 47.61 ? 61   ARG A NH1   1 
ATOM   364   N  NH2   . ARG A 1  63   ? -50.465 27.425  92.170  1.00 49.99 ? 61   ARG A NH2   1 
ATOM   365   N  N     . ASP A 1  64   ? -49.958 27.247  85.395  1.00 33.88 ? 62   ASP A N     1 
ATOM   366   C  CA    . ASP A 1  64   ? -49.371 26.241  84.517  1.00 34.90 ? 62   ASP A CA    1 
ATOM   367   C  C     . ASP A 1  64   ? -49.507 26.637  83.052  1.00 34.72 ? 62   ASP A C     1 
ATOM   368   O  O     . ASP A 1  64   ? -48.552 26.513  82.277  1.00 32.11 ? 62   ASP A O     1 
ATOM   369   C  CB    . ASP A 1  64   ? -50.028 24.881  84.768  1.00 35.90 ? 62   ASP A CB    1 
ATOM   370   C  CG    . ASP A 1  64   ? -49.622 24.272  86.102  1.00 37.11 ? 62   ASP A CG    1 
ATOM   371   O  OD1   . ASP A 1  64   ? -48.705 24.810  86.755  1.00 37.37 ? 62   ASP A OD1   1 
ATOM   372   O  OD2   . ASP A 1  64   ? -50.224 23.247  86.488  1.00 42.26 ? 62   ASP A OD2   1 
ATOM   373   N  N     . ALA A 1  65   ? -50.688 27.113  82.651  1.00 32.39 ? 63   ALA A N     1 
ATOM   374   C  CA    . ALA A 1  65   ? -50.883 27.519  81.261  1.00 32.84 ? 63   ALA A CA    1 
ATOM   375   C  C     . ALA A 1  65   ? -50.007 28.711  80.908  1.00 33.61 ? 63   ALA A C     1 
ATOM   376   O  O     . ALA A 1  65   ? -49.439 28.769  79.810  1.00 34.80 ? 63   ALA A O     1 
ATOM   377   C  CB    . ALA A 1  65   ? -52.355 27.844  81.002  1.00 33.22 ? 63   ALA A CB    1 
ATOM   378   N  N     . ALA A 1  66   ? -49.878 29.668  81.830  1.00 31.08 ? 64   ALA A N     1 
ATOM   379   C  CA    . ALA A 1  66   ? -49.029 30.829  81.583  1.00 33.60 ? 64   ALA A CA    1 
ATOM   380   C  C     . ALA A 1  66   ? -47.565 30.429  81.446  1.00 34.31 ? 64   ALA A C     1 
ATOM   381   O  O     . ALA A 1  66   ? -46.852 30.950  80.579  1.00 30.68 ? 64   ALA A O     1 
ATOM   382   C  CB    . ALA A 1  66   ? -49.196 31.852  82.705  1.00 31.35 ? 64   ALA A CB    1 
ATOM   383   N  N     . ALA A 1  67   ? -47.097 29.509  82.297  1.00 29.98 ? 65   ALA A N     1 
ATOM   384   C  CA    . ALA A 1  67   ? -45.715 29.054  82.200  1.00 34.82 ? 65   ALA A CA    1 
ATOM   385   C  C     . ALA A 1  67   ? -45.455 28.379  80.859  1.00 32.70 ? 65   ALA A C     1 
ATOM   386   O  O     . ALA A 1  67   ? -44.397 28.576  80.252  1.00 36.21 ? 65   ALA A O     1 
ATOM   387   C  CB    . ALA A 1  67   ? -45.390 28.102  83.353  1.00 35.14 ? 65   ALA A CB    1 
ATOM   388   N  N     . SER A 1  68   ? -46.409 27.582  80.378  1.00 33.97 ? 66   SER A N     1 
ATOM   389   C  CA    . SER A 1  68   ? -46.231 26.927  79.087  1.00 36.27 ? 66   SER A CA    1 
ATOM   390   C  C     . SER A 1  68   ? -46.210 27.943  77.952  1.00 36.33 ? 66   SER A C     1 
ATOM   391   O  O     . SER A 1  68   ? -45.389 27.839  77.033  1.00 34.37 ? 66   SER A O     1 
ATOM   392   C  CB    . SER A 1  68   ? -47.330 25.889  78.866  1.00 36.66 ? 66   SER A CB    1 
ATOM   393   O  OG    . SER A 1  68   ? -47.335 25.441  77.524  1.00 41.06 ? 66   SER A OG    1 
ATOM   394   N  N     . THR A 1  69   ? -47.098 28.938  78.005  1.00 32.67 ? 67   THR A N     1 
ATOM   395   C  CA    . THR A 1  69   ? -47.078 30.006  77.014  1.00 32.09 ? 67   THR A CA    1 
ATOM   396   C  C     . THR A 1  69   ? -45.772 30.790  77.078  1.00 32.51 ? 67   THR A C     1 
ATOM   397   O  O     . THR A 1  69   ? -45.163 31.094  76.046  1.00 32.31 ? 67   THR A O     1 
ATOM   398   C  CB    . THR A 1  69   ? -48.270 30.936  77.228  1.00 31.04 ? 67   THR A CB    1 
ATOM   399   O  OG1   . THR A 1  69   ? -49.487 30.212  77.009  1.00 31.66 ? 67   THR A OG1   1 
ATOM   400   C  CG2   . THR A 1  69   ? -48.197 32.133  76.271  1.00 30.65 ? 67   THR A CG2   1 
ATOM   401   N  N     . ALA A 1  70   ? -45.337 31.145  78.286  1.00 31.66 ? 68   ALA A N     1 
ATOM   402   C  CA    . ALA A 1  70   ? -44.076 31.863  78.425  1.00 32.05 ? 68   ALA A CA    1 
ATOM   403   C  C     . ALA A 1  70   ? -42.917 31.036  77.882  1.00 35.67 ? 68   ALA A C     1 
ATOM   404   O  O     . ALA A 1  70   ? -42.062 31.551  77.149  1.00 33.00 ? 68   ALA A O     1 
ATOM   405   C  CB    . ALA A 1  70   ? -43.841 32.240  79.889  1.00 31.81 ? 68   ALA A CB    1 
ATOM   406   N  N     . ARG A 1  71   ? -42.877 29.743  78.226  1.00 35.98 ? 69   ARG A N     1 
ATOM   407   C  CA    . ARG A 1  71   ? -41.817 28.872  77.723  1.00 34.48 ? 69   ARG A CA    1 
ATOM   408   C  C     . ARG A 1  71   ? -41.832 28.812  76.201  1.00 37.19 ? 69   ARG A C     1 
ATOM   409   O  O     . ARG A 1  71   ? -40.773 28.803  75.562  1.00 37.55 ? 69   ARG A O     1 
ATOM   410   C  CB    . ARG A 1  71   ? -41.959 27.467  78.312  1.00 36.38 ? 69   ARG A CB    1 
ATOM   411   C  CG    . ARG A 1  71   ? -41.209 26.390  77.520  1.00 41.18 ? 69   ARG A CG    1 
ATOM   412   C  CD    . ARG A 1  71   ? -41.205 25.032  78.222  1.00 38.69 ? 69   ARG A CD    1 
ATOM   413   N  NE    . ARG A 1  71   ? -40.457 25.079  79.472  1.00 37.50 ? 69   ARG A NE    1 
ATOM   414   C  CZ    . ARG A 1  71   ? -39.133 25.099  79.554  1.00 42.82 ? 69   ARG A CZ    1 
ATOM   415   N  NH1   . ARG A 1  71   ? -38.370 25.056  78.472  1.00 40.71 ? 69   ARG A NH1   1 
ATOM   416   N  NH2   . ARG A 1  71   ? -38.559 25.173  80.752  1.00 41.33 ? 69   ARG A NH2   1 
ATOM   417   N  N     . LYS A 1  72   ? -43.026 28.774  75.605  1.00 34.48 ? 70   LYS A N     1 
ATOM   418   C  CA    . LYS A 1  72   ? -43.136 28.718  74.151  1.00 35.89 ? 70   LYS A CA    1 
ATOM   419   C  C     . LYS A 1  72   ? -42.627 30.001  73.504  1.00 37.74 ? 70   LYS A C     1 
ATOM   420   O  O     . LYS A 1  72   ? -41.903 29.950  72.501  1.00 34.88 ? 70   LYS A O     1 
ATOM   421   C  CB    . LYS A 1  72   ? -44.582 28.448  73.743  1.00 34.09 ? 70   LYS A CB    1 
ATOM   422   C  CG    . LYS A 1  72   ? -44.855 28.697  72.268  1.00 37.11 ? 70   LYS A CG    1 
ATOM   423   C  CD    . LYS A 1  72   ? -46.163 28.077  71.820  1.00 40.18 ? 70   LYS A CD    1 
ATOM   424   C  CE    . LYS A 1  72   ? -46.291 28.128  70.304  1.00 45.08 ? 70   LYS A CE    1 
ATOM   425   N  NZ    . LYS A 1  72   ? -47.364 27.227  69.789  1.00 54.35 ? 70   LYS A NZ    1 
ATOM   426   N  N     . LEU A 1  73   ? -42.994 31.159  74.060  1.00 35.24 ? 71   LEU A N     1 
ATOM   427   C  CA    . LEU A 1  73   ? -42.483 32.425  73.539  1.00 35.43 ? 71   LEU A CA    1 
ATOM   428   C  C     . LEU A 1  73   ? -40.967 32.513  73.671  1.00 34.54 ? 71   LEU A C     1 
ATOM   429   O  O     . LEU A 1  73   ? -40.281 32.942  72.737  1.00 34.94 ? 71   LEU A O     1 
ATOM   430   C  CB    . LEU A 1  73   ? -43.137 33.600  74.267  1.00 33.15 ? 71   LEU A CB    1 
ATOM   431   C  CG    . LEU A 1  73   ? -44.649 33.771  74.161  1.00 31.49 ? 71   LEU A CG    1 
ATOM   432   C  CD1   . LEU A 1  73   ? -45.096 34.876  75.111  1.00 32.78 ? 71   LEU A CD1   1 
ATOM   433   C  CD2   . LEU A 1  73   ? -45.064 34.091  72.739  1.00 31.84 ? 71   LEU A CD2   1 
ATOM   434   N  N     . ILE A 1  74   ? -40.428 32.114  74.826  1.00 31.64 ? 72   ILE A N     1 
ATOM   435   C  CA    . ILE A 1  74   ? -38.990 32.222  75.062  1.00 36.94 ? 72   ILE A CA    1 
ATOM   436   C  C     . ILE A 1  74   ? -38.221 31.253  74.172  1.00 36.85 ? 72   ILE A C     1 
ATOM   437   O  O     . ILE A 1  74   ? -37.129 31.572  73.687  1.00 37.55 ? 72   ILE A O     1 
ATOM   438   C  CB    . ILE A 1  74   ? -38.682 31.998  76.553  1.00 33.37 ? 72   ILE A CB    1 
ATOM   439   C  CG1   . ILE A 1  74   ? -39.220 33.173  77.370  1.00 34.17 ? 72   ILE A CG1   1 
ATOM   440   C  CG2   . ILE A 1  74   ? -37.184 31.828  76.788  1.00 35.64 ? 72   ILE A CG2   1 
ATOM   441   C  CD1   . ILE A 1  74   ? -39.170 32.959  78.856  1.00 36.37 ? 72   ILE A CD1   1 
ATOM   442   N  N     . GLU A 1  75   ? -38.769 30.059  73.943  1.00 36.95 ? 73   GLU A N     1 
ATOM   443   C  CA    . GLU A 1  75   ? -38.120 29.131  73.024  1.00 38.60 ? 73   GLU A CA    1 
ATOM   444   C  C     . GLU A 1  75   ? -38.085 29.700  71.613  1.00 39.36 ? 73   GLU A C     1 
ATOM   445   O  O     . GLU A 1  75   ? -37.074 29.579  70.911  1.00 39.39 ? 73   GLU A O     1 
ATOM   446   C  CB    . GLU A 1  75   ? -38.825 27.774  73.057  1.00 36.99 ? 73   GLU A CB    1 
ATOM   447   C  CG    . GLU A 1  75   ? -38.381 26.924  74.224  1.00 36.71 ? 73   GLU A CG    1 
ATOM   448   C  CD    . GLU A 1  75   ? -39.292 25.752  74.509  1.00 42.38 ? 73   GLU A CD    1 
ATOM   449   O  OE1   . GLU A 1  75   ? -40.316 25.598  73.810  1.00 41.66 ? 73   GLU A OE1   1 
ATOM   450   O  OE2   . GLU A 1  75   ? -38.974 24.986  75.445  1.00 46.23 ? 73   GLU A OE2   1 
ATOM   451   N  N     . ALA A 1  76   ? -39.173 30.346  71.185  1.00 39.91 ? 74   ALA A N     1 
ATOM   452   C  CA    . ALA A 1  76   ? -39.166 31.012  69.888  1.00 38.17 ? 74   ALA A CA    1 
ATOM   453   C  C     . ALA A 1  76   ? -38.137 32.135  69.853  1.00 39.74 ? 74   ALA A C     1 
ATOM   454   O  O     . ALA A 1  76   ? -37.424 32.300  68.857  1.00 43.55 ? 74   ALA A O     1 
ATOM   455   C  CB    . ALA A 1  76   ? -40.560 31.545  69.561  1.00 37.69 ? 74   ALA A CB    1 
ATOM   456   N  N     . LEU A 1  77   ? -38.044 32.916  70.933  1.00 38.86 ? 75   LEU A N     1 
ATOM   457   C  CA    . LEU A 1  77   ? -37.072 34.007  70.989  1.00 38.40 ? 75   LEU A CA    1 
ATOM   458   C  C     . LEU A 1  77   ? -35.647 33.484  70.866  1.00 41.64 ? 75   LEU A C     1 
ATOM   459   O  O     . LEU A 1  77   ? -34.844 34.008  70.086  1.00 44.17 ? 75   LEU A O     1 
ATOM   460   C  CB    . LEU A 1  77   ? -37.226 34.793  72.292  1.00 35.42 ? 75   LEU A CB    1 
ATOM   461   C  CG    . LEU A 1  77   ? -38.318 35.856  72.378  1.00 36.89 ? 75   LEU A CG    1 
ATOM   462   C  CD1   . LEU A 1  77   ? -38.256 36.538  73.736  1.00 36.68 ? 75   LEU A CD1   1 
ATOM   463   C  CD2   . LEU A 1  77   ? -38.151 36.868  71.262  1.00 36.77 ? 75   LEU A CD2   1 
ATOM   464   N  N     . ARG A 1  78   ? -35.308 32.459  71.648  1.00 41.75 ? 76   ARG A N     1 
ATOM   465   C  CA    . ARG A 1  78   ? -33.952 31.933  71.621  1.00 41.86 ? 76   ARG A CA    1 
ATOM   466   C  C     . ARG A 1  78   ? -33.657 31.172  70.336  1.00 41.23 ? 76   ARG A C     1 
ATOM   467   O  O     . ARG A 1  78   ? -32.492 31.083  69.939  1.00 48.44 ? 76   ARG A O     1 
ATOM   468   C  CB    . ARG A 1  78   ? -33.710 31.054  72.849  1.00 40.37 ? 76   ARG A CB    1 
ATOM   469   C  CG    . ARG A 1  78   ? -33.603 31.858  74.130  1.00 39.96 ? 76   ARG A CG    1 
ATOM   470   C  CD    . ARG A 1  78   ? -33.241 31.008  75.330  1.00 38.71 ? 76   ARG A CD    1 
ATOM   471   N  NE    . ARG A 1  78   ? -32.672 31.827  76.395  1.00 39.56 ? 76   ARG A NE    1 
ATOM   472   C  CZ    . ARG A 1  78   ? -32.250 31.359  77.562  1.00 39.85 ? 76   ARG A CZ    1 
ATOM   473   N  NH1   . ARG A 1  78   ? -32.341 30.075  77.864  1.00 40.50 ? 76   ARG A NH1   1 
ATOM   474   N  NH2   . ARG A 1  78   ? -31.720 32.200  78.447  1.00 44.48 ? 76   ARG A NH2   1 
ATOM   475   N  N     . GLY A 1  79   ? -34.676 30.643  69.670  1.00 42.61 ? 77   GLY A N     1 
ATOM   476   C  CA    . GLY A 1  79   ? -34.473 29.971  68.405  1.00 47.73 ? 77   GLY A CA    1 
ATOM   477   C  C     . GLY A 1  79   ? -34.263 30.878  67.215  1.00 50.42 ? 77   GLY A C     1 
ATOM   478   O  O     . GLY A 1  79   ? -34.060 30.390  66.100  1.00 48.64 ? 77   GLY A O     1 
ATOM   479   N  N     . LYS A 1  80   ? -34.305 32.191  67.422  1.00 49.67 ? 78   LYS A N     1 
ATOM   480   C  CA    . LYS A 1  80   ? -34.126 33.152  66.343  1.00 50.51 ? 78   LYS A CA    1 
ATOM   481   C  C     . LYS A 1  80   ? -33.366 34.364  66.861  1.00 50.04 ? 78   LYS A C     1 
ATOM   482   O  O     . LYS A 1  80   ? -32.223 34.600  66.488  1.00 55.22 ? 78   LYS A O     1 
ATOM   483   C  CB    . LYS A 1  80   ? -35.481 33.576  65.767  1.00 51.88 ? 78   LYS A CB    1 
ATOM   484   C  CG    . LYS A 1  80   ? -36.292 34.453  66.717  1.00 48.20 ? 78   LYS A CG    1 
ATOM   485   C  CD    . LYS A 1  80   ? -37.716 34.702  66.231  1.00 43.89 ? 78   LYS A CD    1 
ATOM   486   C  CE    . LYS A 1  80   ? -38.451 35.633  67.196  1.00 43.67 ? 78   LYS A CE    1 
ATOM   487   N  NZ    . LYS A 1  80   ? -39.863 35.919  66.789  1.00 34.50 ? 78   LYS A NZ    1 
ATOM   488   N  N     . GLY A 1  85   ? -25.331 42.193  64.782  1.00 42.60 ? 83   GLY A N     1 
ATOM   489   C  CA    . GLY A 1  85   ? -24.951 43.328  63.962  1.00 36.91 ? 83   GLY A CA    1 
ATOM   490   C  C     . GLY A 1  85   ? -23.575 43.871  64.324  1.00 34.62 ? 83   GLY A C     1 
ATOM   491   O  O     . GLY A 1  85   ? -22.595 43.644  63.610  1.00 34.43 ? 83   GLY A O     1 
ATOM   492   N  N     . VAL A 1  86   ? -23.510 44.602  65.438  1.00 36.24 ? 84   VAL A N     1 
ATOM   493   C  CA    . VAL A 1  86   ? -22.222 45.054  65.961  1.00 34.72 ? 84   VAL A CA    1 
ATOM   494   C  C     . VAL A 1  86   ? -21.344 43.859  66.300  1.00 35.27 ? 84   VAL A C     1 
ATOM   495   O  O     . VAL A 1  86   ? -20.130 43.870  66.054  1.00 33.05 ? 84   VAL A O     1 
ATOM   496   C  CB    . VAL A 1  86   ? -22.441 45.966  67.181  1.00 37.35 ? 84   VAL A CB    1 
ATOM   497   C  CG1   . VAL A 1  86   ? -21.128 46.230  67.910  1.00 33.69 ? 84   VAL A CG1   1 
ATOM   498   C  CG2   . VAL A 1  86   ? -23.081 47.272  66.746  1.00 36.83 ? 84   VAL A CG2   1 
ATOM   499   N  N     . GLU A 1  87   ? -21.944 42.806  66.864  1.00 36.48 ? 85   GLU A N     1 
ATOM   500   C  CA    . GLU A 1  87   ? -21.181 41.610  67.210  1.00 38.52 ? 85   GLU A CA    1 
ATOM   501   C  C     . GLU A 1  87   ? -20.520 40.996  65.982  1.00 36.22 ? 85   GLU A C     1 
ATOM   502   O  O     . GLU A 1  87   ? -19.360 40.567  66.043  1.00 37.85 ? 85   GLU A O     1 
ATOM   503   C  CB    . GLU A 1  87   ? -22.088 40.588  67.898  1.00 44.27 ? 85   GLU A CB    1 
ATOM   504   N  N     . GLY A 1  88   ? -21.233 40.949  64.854  1.00 34.32 ? 86   GLY A N     1 
ATOM   505   C  CA    . GLY A 1  88   ? -20.648 40.380  63.651  1.00 32.80 ? 86   GLY A CA    1 
ATOM   506   C  C     . GLY A 1  88   ? -19.532 41.228  63.078  1.00 33.86 ? 86   GLY A C     1 
ATOM   507   O  O     . GLY A 1  88   ? -18.576 40.700  62.504  1.00 31.75 ? 86   GLY A O     1 
ATOM   508   N  N     . LEU A 1  89   ? -19.638 42.549  63.227  1.00 32.27 ? 87   LEU A N     1 
ATOM   509   C  CA    . LEU A 1  89   ? -18.576 43.454  62.802  1.00 31.03 ? 87   LEU A CA    1 
ATOM   510   C  C     . LEU A 1  89   ? -17.328 43.273  63.663  1.00 29.71 ? 87   LEU A C     1 
ATOM   511   O  O     . LEU A 1  89   ? -16.213 43.129  63.144  1.00 28.69 ? 87   LEU A O     1 
ATOM   512   C  CB    . LEU A 1  89   ? -19.096 44.892  62.873  1.00 31.66 ? 87   LEU A CB    1 
ATOM   513   C  CG    . LEU A 1  89   ? -18.174 46.069  62.577  1.00 34.61 ? 87   LEU A CG    1 
ATOM   514   C  CD1   . LEU A 1  89   ? -17.835 46.093  61.120  1.00 34.90 ? 87   LEU A CD1   1 
ATOM   515   C  CD2   . LEU A 1  89   ? -18.852 47.370  62.998  1.00 35.96 ? 87   LEU A CD2   1 
ATOM   516   N  N     . VAL A 1  90   ? -17.505 43.269  64.986  1.00 32.63 ? 88   VAL A N     1 
ATOM   517   C  CA    . VAL A 1  90   ? -16.397 42.998  65.897  1.00 28.73 ? 88   VAL A CA    1 
ATOM   518   C  C     . VAL A 1  90   ? -15.719 41.679  65.547  1.00 31.05 ? 88   VAL A C     1 
ATOM   519   O  O     . VAL A 1  90   ? -14.484 41.574  65.548  1.00 30.71 ? 88   VAL A O     1 
ATOM   520   C  CB    . VAL A 1  90   ? -16.906 43.012  67.350  1.00 25.94 ? 88   VAL A CB    1 
ATOM   521   C  CG1   . VAL A 1  90   ? -15.846 42.473  68.296  1.00 29.45 ? 88   VAL A CG1   1 
ATOM   522   C  CG2   . VAL A 1  90   ? -17.309 44.423  67.737  1.00 28.79 ? 88   VAL A CG2   1 
ATOM   523   N  N     . GLN A 1  91   ? -16.513 40.654  65.227  1.00 32.30 ? 89   GLN A N     1 
ATOM   524   C  CA    . GLN A 1  91   ? -15.946 39.349  64.903  1.00 32.57 ? 89   GLN A CA    1 
ATOM   525   C  C     . GLN A 1  91   ? -15.178 39.391  63.589  1.00 31.82 ? 89   GLN A C     1 
ATOM   526   O  O     . GLN A 1  91   ? -14.055 38.883  63.500  1.00 33.51 ? 89   GLN A O     1 
ATOM   527   C  CB    . GLN A 1  91   ? -17.055 38.294  64.848  1.00 32.44 ? 89   GLN A CB    1 
ATOM   528   N  N     . GLU A 1  92   ? -15.762 40.009  62.557  1.00 32.07 ? 90   GLU A N     1 
ATOM   529   C  CA    . GLU A 1  92   ? -15.148 39.973  61.231  1.00 33.52 ? 90   GLU A CA    1 
ATOM   530   C  C     . GLU A 1  92   ? -13.778 40.641  61.227  1.00 31.40 ? 90   GLU A C     1 
ATOM   531   O  O     . GLU A 1  92   ? -12.843 40.158  60.572  1.00 30.95 ? 90   GLU A O     1 
ATOM   532   C  CB    . GLU A 1  92   ? -16.073 40.635  60.209  1.00 32.06 ? 90   GLU A CB    1 
ATOM   533   C  CG    . GLU A 1  92   ? -15.420 40.864  58.855  1.00 32.39 ? 90   GLU A CG    1 
ATOM   534   C  CD    . GLU A 1  92   ? -16.406 41.343  57.803  1.00 38.59 ? 90   GLU A CD    1 
ATOM   535   O  OE1   . GLU A 1  92   ? -17.547 41.691  58.174  1.00 36.91 ? 90   GLU A OE1   1 
ATOM   536   O  OE2   . GLU A 1  92   ? -16.038 41.370  56.610  1.00 37.48 ? 90   GLU A OE2   1 
ATOM   537   N  N     . TYR A 1  93   ? -13.631 41.745  61.956  1.00 29.36 ? 91   TYR A N     1 
ATOM   538   C  CA    . TYR A 1  93   ? -12.382 42.494  61.959  1.00 29.70 ? 91   TYR A CA    1 
ATOM   539   C  C     . TYR A 1  93   ? -11.569 42.289  63.228  1.00 30.06 ? 91   TYR A C     1 
ATOM   540   O  O     . TYR A 1  93   ? -10.596 43.020  63.451  1.00 27.61 ? 91   TYR A O     1 
ATOM   541   C  CB    . TYR A 1  93   ? -12.665 43.979  61.731  1.00 26.56 ? 91   TYR A CB    1 
ATOM   542   C  CG    . TYR A 1  93   ? -13.111 44.244  60.314  1.00 27.84 ? 91   TYR A CG    1 
ATOM   543   C  CD1   . TYR A 1  93   ? -12.176 44.411  59.293  1.00 26.16 ? 91   TYR A CD1   1 
ATOM   544   C  CD2   . TYR A 1  93   ? -14.457 44.286  59.985  1.00 31.08 ? 91   TYR A CD2   1 
ATOM   545   C  CE1   . TYR A 1  93   ? -12.573 44.627  57.990  1.00 28.91 ? 91   TYR A CE1   1 
ATOM   546   C  CE2   . TYR A 1  93   ? -14.863 44.504  58.679  1.00 30.95 ? 91   TYR A CE2   1 
ATOM   547   C  CZ    . TYR A 1  93   ? -13.915 44.677  57.692  1.00 30.28 ? 91   TYR A CZ    1 
ATOM   548   O  OH    . TYR A 1  93   ? -14.307 44.892  56.395  1.00 32.57 ? 91   TYR A OH    1 
ATOM   549   N  N     . SER A 1  94   ? -11.937 41.307  64.051  1.00 28.55 ? 92   SER A N     1 
ATOM   550   C  CA    . SER A 1  94   ? -11.186 40.955  65.259  1.00 28.21 ? 92   SER A CA    1 
ATOM   551   C  C     . SER A 1  94   ? -10.990 42.161  66.180  1.00 25.02 ? 92   SER A C     1 
ATOM   552   O  O     . SER A 1  94   ? -9.910  42.373  66.733  1.00 26.26 ? 92   SER A O     1 
ATOM   553   C  CB    . SER A 1  94   ? -9.836  40.323  64.898  1.00 28.97 ? 92   SER A CB    1 
ATOM   554   O  OG    . SER A 1  94   ? -10.005 39.275  63.954  1.00 33.25 ? 92   SER A OG    1 
ATOM   555   N  N     . LEU A 1  95   ? -12.046 42.950  66.362  1.00 24.34 ? 93   LEU A N     1 
ATOM   556   C  CA    . LEU A 1  95   ? -11.952 44.181  67.132  1.00 24.73 ? 93   LEU A CA    1 
ATOM   557   C  C     . LEU A 1  95   ? -11.983 43.898  68.628  1.00 23.88 ? 93   LEU A C     1 
ATOM   558   O  O     . LEU A 1  95   ? -12.736 43.045  69.103  1.00 25.35 ? 93   LEU A O     1 
ATOM   559   C  CB    . LEU A 1  95   ? -13.101 45.130  66.777  1.00 22.55 ? 93   LEU A CB    1 
ATOM   560   C  CG    . LEU A 1  95   ? -13.197 45.546  65.305  1.00 22.40 ? 93   LEU A CG    1 
ATOM   561   C  CD1   . LEU A 1  95   ? -14.305 46.575  65.135  1.00 26.04 ? 93   LEU A CD1   1 
ATOM   562   C  CD2   . LEU A 1  95   ? -11.857 46.097  64.811  1.00 23.38 ? 93   LEU A CD2   1 
ATOM   563   N  N     . SER A 1  96   ? -11.152 44.615  69.370  1.00 19.59 ? 94   SER A N     1 
ATOM   564   C  CA    . SER A 1  96   ? -11.355 44.683  70.805  1.00 22.07 ? 94   SER A CA    1 
ATOM   565   C  C     . SER A 1  96   ? -12.611 45.507  71.106  1.00 20.55 ? 94   SER A C     1 
ATOM   566   O  O     . SER A 1  96   ? -13.168 46.176  70.233  1.00 20.87 ? 94   SER A O     1 
ATOM   567   C  CB    . SER A 1  96   ? -10.145 45.320  71.470  1.00 22.90 ? 94   SER A CB    1 
ATOM   568   O  OG    . SER A 1  96   ? -10.096 46.693  71.120  1.00 21.09 ? 94   SER A OG    1 
ATOM   569   N  N     . SER A 1  97   ? -13.043 45.482  72.369  1.00 20.52 ? 95   SER A N     1 
ATOM   570   C  CA    . SER A 1  97   ? -14.195 46.287  72.765  1.00 22.95 ? 95   SER A CA    1 
ATOM   571   C  C     . SER A 1  97   ? -13.936 47.770  72.532  1.00 20.28 ? 95   SER A C     1 
ATOM   572   O  O     . SER A 1  97   ? -14.773 48.478  71.960  1.00 19.50 ? 95   SER A O     1 
ATOM   573   C  CB    . SER A 1  97   ? -14.543 46.024  74.231  1.00 24.94 ? 95   SER A CB    1 
ATOM   574   O  OG    . SER A 1  97   ? -15.177 44.768  74.366  1.00 28.62 ? 95   SER A OG    1 
ATOM   575   N  N     . GLN A 1  98   ? -12.769 48.256  72.949  1.00 18.34 ? 96   GLN A N     1 
ATOM   576   C  CA    . GLN A 1  98   ? -12.472 49.667  72.744  1.00 18.54 ? 96   GLN A CA    1 
ATOM   577   C  C     . GLN A 1  98   ? -12.424 50.015  71.257  1.00 18.05 ? 96   GLN A C     1 
ATOM   578   O  O     . GLN A 1  98   ? -12.863 51.100  70.860  1.00 18.03 ? 96   GLN A O     1 
ATOM   579   C  CB    . GLN A 1  98   ? -11.161 50.031  73.449  1.00 17.98 ? 96   GLN A CB    1 
ATOM   580   C  CG    . GLN A 1  98   ? -11.317 50.151  74.972  1.00 19.46 ? 96   GLN A CG    1 
ATOM   581   C  CD    . GLN A 1  98   ? -12.269 51.269  75.381  1.00 18.51 ? 96   GLN A CD    1 
ATOM   582   O  OE1   . GLN A 1  98   ? -13.492 51.104  75.360  1.00 20.55 ? 96   GLN A OE1   1 
ATOM   583   N  NE2   . GLN A 1  98   ? -11.715 52.413  75.760  1.00 19.89 ? 96   GLN A NE2   1 
ATOM   584   N  N     . GLU A 1  99   ? -11.900 49.111  70.420  1.00 17.43 ? 97   GLU A N     1 
ATOM   585   C  CA    . GLU A 1  99   ? -11.906 49.363  68.975  1.00 15.42 ? 97   GLU A CA    1 
ATOM   586   C  C     . GLU A 1  99   ? -13.323 49.428  68.427  1.00 18.35 ? 97   GLU A C     1 
ATOM   587   O  O     . GLU A 1  99   ? -13.645 50.310  67.621  1.00 18.63 ? 97   GLU A O     1 
ATOM   588   C  CB    . GLU A 1  99   ? -11.098 48.291  68.249  1.00 16.93 ? 97   GLU A CB    1 
ATOM   589   C  CG    . GLU A 1  99   ? -9.599  48.410  68.543  1.00 18.07 ? 97   GLU A CG    1 
ATOM   590   C  CD    . GLU A 1  99   ? -8.794  47.235  68.022  1.00 19.94 ? 97   GLU A CD    1 
ATOM   591   O  OE1   . GLU A 1  99   ? -9.407  46.234  67.560  1.00 19.24 ? 97   GLU A OE1   1 
ATOM   592   O  OE2   . GLU A 1  99   ? -7.548  47.306  68.088  1.00 18.79 ? 97   GLU A OE2   1 
ATOM   593   N  N     . GLY A 1  100  ? -14.188 48.507  68.849  1.00 18.38 ? 98   GLY A N     1 
ATOM   594   C  CA    . GLY A 1  100  ? -15.573 48.582  68.411  1.00 17.22 ? 98   GLY A CA    1 
ATOM   595   C  C     . GLY A 1  100  ? -16.223 49.904  68.788  1.00 18.97 ? 98   GLY A C     1 
ATOM   596   O  O     . GLY A 1  100  ? -16.905 50.528  67.969  1.00 18.28 ? 98   GLY A O     1 
ATOM   597   N  N     . VAL A 1  101  ? -16.015 50.350  70.032  1.00 18.18 ? 99   VAL A N     1 
ATOM   598   C  CA    . VAL A 1  101  ? -16.594 51.615  70.474  1.00 17.85 ? 99   VAL A CA    1 
ATOM   599   C  C     . VAL A 1  101  ? -16.022 52.769  69.662  1.00 20.66 ? 99   VAL A C     1 
ATOM   600   O  O     . VAL A 1  101  ? -16.760 53.636  69.176  1.00 17.99 ? 99   VAL A O     1 
ATOM   601   C  CB    . VAL A 1  101  ? -16.349 51.821  71.976  1.00 17.31 ? 99   VAL A CB    1 
ATOM   602   C  CG1   . VAL A 1  101  ? -16.834 53.194  72.381  1.00 17.40 ? 99   VAL A CG1   1 
ATOM   603   C  CG2   . VAL A 1  101  ? -17.044 50.722  72.782  1.00 20.13 ? 99   VAL A CG2   1 
ATOM   604   N  N     . ALA A 1  102  ? -14.691 52.799  69.512  1.00 18.27 ? 100  ALA A N     1 
ATOM   605   C  CA    . ALA A 1  102  ? -14.057 53.871  68.754  1.00 16.22 ? 100  ALA A CA    1 
ATOM   606   C  C     . ALA A 1  102  ? -14.553 53.892  67.317  1.00 16.56 ? 100  ALA A C     1 
ATOM   607   O  O     . ALA A 1  102  ? -14.767 54.963  66.746  1.00 18.11 ? 100  ALA A O     1 
ATOM   608   C  CB    . ALA A 1  102  ? -12.529 53.716  68.779  1.00 18.43 ? 100  ALA A CB    1 
ATOM   609   N  N     . LEU A 1  103  ? -14.686 52.717  66.706  1.00 17.08 ? 101  LEU A N     1 
ATOM   610   C  CA    . LEU A 1  103  ? -15.198 52.636  65.341  1.00 16.22 ? 101  LEU A CA    1 
ATOM   611   C  C     . LEU A 1  103  ? -16.589 53.242  65.239  1.00 19.34 ? 101  LEU A C     1 
ATOM   612   O  O     . LEU A 1  103  ? -16.875 54.008  64.312  1.00 21.18 ? 101  LEU A O     1 
ATOM   613   C  CB    . LEU A 1  103  ? -15.208 51.184  64.874  1.00 18.26 ? 101  LEU A CB    1 
ATOM   614   C  CG    . LEU A 1  103  ? -15.794 50.951  63.475  1.00 20.06 ? 101  LEU A CG    1 
ATOM   615   C  CD1   . LEU A 1  103  ? -14.978 51.681  62.411  1.00 18.74 ? 101  LEU A CD1   1 
ATOM   616   C  CD2   . LEU A 1  103  ? -15.870 49.474  63.165  1.00 20.26 ? 101  LEU A CD2   1 
ATOM   617   N  N     . MET A 1  104  ? -17.466 52.926  66.186  1.00 19.90 ? 102  MET A N     1 
ATOM   618   C  CA    . MET A 1  104  ? -18.817 53.472  66.113  1.00 18.64 ? 102  MET A CA    1 
ATOM   619   C  C     . MET A 1  104  ? -18.826 54.973  66.362  1.00 19.35 ? 102  MET A C     1 
ATOM   620   O  O     . MET A 1  104  ? -19.633 55.693  65.763  1.00 22.29 ? 102  MET A O     1 
ATOM   621   C  CB    . MET A 1  104  ? -19.727 52.741  67.094  1.00 21.21 ? 102  MET A CB    1 
ATOM   622   C  CG    . MET A 1  104  ? -19.821 51.244  66.820  1.00 19.72 ? 102  MET A CG    1 
ATOM   623   S  SD    . MET A 1  104  ? -20.293 50.848  65.122  1.00 30.16 ? 102  MET A SD    1 
ATOM   624   C  CE    . MET A 1  104  ? -21.991 51.396  65.138  1.00 30.53 ? 102  MET A CE    1 
ATOM   625   N  N     . CYS A 1  105  ? -17.929 55.471  67.215  1.00 18.81 ? 103  CYS A N     1 
ATOM   626   C  CA    . CYS A 1  105  ? -17.815 56.917  67.389  1.00 19.53 ? 103  CYS A CA    1 
ATOM   627   C  C     . CYS A 1  105  ? -17.358 57.582  66.098  1.00 23.66 ? 103  CYS A C     1 
ATOM   628   O  O     . CYS A 1  105  ? -17.853 58.656  65.735  1.00 23.55 ? 103  CYS A O     1 
ATOM   629   C  CB    . CYS A 1  105  ? -16.839 57.247  68.515  1.00 20.16 ? 103  CYS A CB    1 
ATOM   630   S  SG    . CYS A 1  105  ? -17.388 56.784  70.147  1.00 20.07 ? 103  CYS A SG    1 
ATOM   631   N  N     . LEU A 1  106  ? -16.391 56.978  65.407  1.00 21.74 ? 104  LEU A N     1 
ATOM   632   C  CA    . LEU A 1  106  ? -15.971 57.508  64.116  1.00 21.69 ? 104  LEU A CA    1 
ATOM   633   C  C     . LEU A 1  106  ? -17.118 57.483  63.119  1.00 25.67 ? 104  LEU A C     1 
ATOM   634   O  O     . LEU A 1  106  ? -17.338 58.453  62.384  1.00 25.48 ? 104  LEU A O     1 
ATOM   635   C  CB    . LEU A 1  106  ? -14.790 56.709  63.566  1.00 23.47 ? 104  LEU A CB    1 
ATOM   636   C  CG    . LEU A 1  106  ? -14.442 57.061  62.109  1.00 24.71 ? 104  LEU A CG    1 
ATOM   637   C  CD1   . LEU A 1  106  ? -13.884 58.468  62.006  1.00 29.30 ? 104  LEU A CD1   1 
ATOM   638   C  CD2   . LEU A 1  106  ? -13.465 56.058  61.531  1.00 25.74 ? 104  LEU A CD2   1 
ATOM   639   N  N     . ALA A 1  107  ? -17.838 56.361  63.051  1.00 21.18 ? 105  ALA A N     1 
ATOM   640   C  CA    . ALA A 1  107  ? -18.956 56.270  62.120  1.00 24.14 ? 105  ALA A CA    1 
ATOM   641   C  C     . ALA A 1  107  ? -19.992 57.346  62.412  1.00 29.80 ? 105  ALA A C     1 
ATOM   642   O  O     . ALA A 1  107  ? -20.507 57.986  61.487  1.00 28.58 ? 105  ALA A O     1 
ATOM   643   C  CB    . ALA A 1  107  ? -19.582 54.881  62.188  1.00 22.44 ? 105  ALA A CB    1 
ATOM   644   N  N     . GLU A 1  108  ? -20.309 57.551  63.695  1.00 25.89 ? 106  GLU A N     1 
ATOM   645   C  CA    . GLU A 1  108  ? -21.202 58.633  64.103  1.00 27.59 ? 106  GLU A CA    1 
ATOM   646   C  C     . GLU A 1  108  ? -20.727 59.978  63.556  1.00 33.08 ? 106  GLU A C     1 
ATOM   647   O  O     . GLU A 1  108  ? -21.516 60.757  63.007  1.00 32.78 ? 106  GLU A O     1 
ATOM   648   C  CB    . GLU A 1  108  ? -21.287 58.667  65.634  1.00 27.74 ? 106  GLU A CB    1 
ATOM   649   C  CG    . GLU A 1  108  ? -22.121 59.802  66.216  1.00 27.79 ? 106  GLU A CG    1 
ATOM   650   C  CD    . GLU A 1  108  ? -21.779 60.101  67.670  1.00 31.19 ? 106  GLU A CD    1 
ATOM   651   O  OE1   . GLU A 1  108  ? -21.249 59.208  68.372  1.00 27.67 ? 106  GLU A OE1   1 
ATOM   652   O  OE2   . GLU A 1  108  ? -22.026 61.244  68.112  1.00 31.69 ? 106  GLU A OE2   1 
ATOM   653   N  N     . ALA A 1  109  ? -19.426 60.257  63.685  1.00 27.42 ? 107  ALA A N     1 
ATOM   654   C  CA    . ALA A 1  109  ? -18.878 61.526  63.217  1.00 33.21 ? 107  ALA A CA    1 
ATOM   655   C  C     . ALA A 1  109  ? -18.959 61.641  61.701  1.00 36.92 ? 107  ALA A C     1 
ATOM   656   O  O     . ALA A 1  109  ? -19.325 62.697  61.172  1.00 38.68 ? 107  ALA A O     1 
ATOM   657   C  CB    . ALA A 1  109  ? -17.432 61.674  63.684  1.00 31.96 ? 107  ALA A CB    1 
ATOM   658   N  N     . LEU A 1  110  ? -18.622 60.565  60.988  1.00 33.57 ? 108  LEU A N     1 
ATOM   659   C  CA    . LEU A 1  110  ? -18.710 60.576  59.533  1.00 34.59 ? 108  LEU A CA    1 
ATOM   660   C  C     . LEU A 1  110  ? -20.143 60.770  59.056  1.00 39.72 ? 108  LEU A C     1 
ATOM   661   O  O     . LEU A 1  110  ? -20.371 61.401  58.017  1.00 40.83 ? 108  LEU A O     1 
ATOM   662   C  CB    . LEU A 1  110  ? -18.132 59.278  58.971  1.00 30.86 ? 108  LEU A CB    1 
ATOM   663   C  CG    . LEU A 1  110  ? -16.619 59.172  59.117  1.00 32.94 ? 108  LEU A CG    1 
ATOM   664   C  CD1   . LEU A 1  110  ? -16.155 57.763  58.790  1.00 28.17 ? 108  LEU A CD1   1 
ATOM   665   C  CD2   . LEU A 1  110  ? -15.931 60.201  58.216  1.00 34.92 ? 108  LEU A CD2   1 
ATOM   666   N  N     . LEU A 1  111  ? -21.120 60.236  59.789  1.00 36.11 ? 109  LEU A N     1 
ATOM   667   C  CA    . LEU A 1  111  ? -22.512 60.439  59.405  1.00 38.84 ? 109  LEU A CA    1 
ATOM   668   C  C     . LEU A 1  111  ? -22.985 61.867  59.654  1.00 42.42 ? 109  LEU A C     1 
ATOM   669   O  O     . LEU A 1  111  ? -24.010 62.273  59.096  1.00 46.23 ? 109  LEU A O     1 
ATOM   670   C  CB    . LEU A 1  111  ? -23.397 59.438  60.142  1.00 34.49 ? 109  LEU A CB    1 
ATOM   671   C  CG    . LEU A 1  111  ? -23.157 58.018  59.624  1.00 34.91 ? 109  LEU A CG    1 
ATOM   672   C  CD1   . LEU A 1  111  ? -23.902 56.987  60.447  1.00 32.34 ? 109  LEU A CD1   1 
ATOM   673   C  CD2   . LEU A 1  111  ? -23.535 57.924  58.153  1.00 36.67 ? 109  LEU A CD2   1 
ATOM   674   N  N     . ARG A 1  112  ? -22.267 62.640  60.473  1.00 41.48 ? 110  ARG A N     1 
ATOM   675   C  CA    . ARG A 1  112  ? -22.561 64.063  60.589  1.00 44.60 ? 110  ARG A CA    1 
ATOM   676   C  C     . ARG A 1  112  ? -22.164 64.842  59.346  1.00 48.70 ? 110  ARG A C     1 
ATOM   677   O  O     . ARG A 1  112  ? -22.508 66.026  59.241  1.00 49.63 ? 110  ARG A O     1 
ATOM   678   C  CB    . ARG A 1  112  ? -21.868 64.658  61.811  1.00 43.63 ? 110  ARG A CB    1 
ATOM   679   C  CG    . ARG A 1  112  ? -22.534 64.298  63.118  1.00 42.02 ? 110  ARG A CG    1 
ATOM   680   C  CD    . ARG A 1  112  ? -22.122 65.247  64.223  1.00 47.30 ? 110  ARG A CD    1 
ATOM   681   N  NE    . ARG A 1  112  ? -20.720 65.096  64.587  1.00 46.74 ? 110  ARG A NE    1 
ATOM   682   C  CZ    . ARG A 1  112  ? -20.269 64.187  65.442  1.00 51.53 ? 110  ARG A CZ    1 
ATOM   683   N  NH1   . ARG A 1  112  ? -21.083 63.315  66.016  1.00 51.26 ? 110  ARG A NH1   1 
ATOM   684   N  NH2   . ARG A 1  112  ? -18.969 64.151  65.728  1.00 48.40 ? 110  ARG A NH2   1 
ATOM   685   N  N     . ILE A 1  113  ? -21.444 64.218  58.419  1.00 49.67 ? 111  ILE A N     1 
ATOM   686   C  CA    . ILE A 1  113  ? -21.191 64.795  57.103  1.00 49.45 ? 111  ILE A CA    1 
ATOM   687   C  C     . ILE A 1  113  ? -22.432 64.559  56.250  1.00 53.59 ? 111  ILE A C     1 
ATOM   688   O  O     . ILE A 1  113  ? -22.759 63.406  55.932  1.00 51.71 ? 111  ILE A O     1 
ATOM   689   C  CB    . ILE A 1  113  ? -19.934 64.193  56.459  1.00 47.00 ? 111  ILE A CB    1 
ATOM   690   C  CG1   . ILE A 1  113  ? -18.690 64.651  57.222  1.00 46.87 ? 111  ILE A CG1   1 
ATOM   691   C  CG2   . ILE A 1  113  ? -19.851 64.571  54.985  1.00 50.72 ? 111  ILE A CG2   1 
ATOM   692   C  CD1   . ILE A 1  113  ? -17.418 64.052  56.710  1.00 39.56 ? 111  ILE A CD1   1 
ATOM   693   N  N     . PRO A 1  114  ? -23.152 65.612  55.868  1.00 56.79 ? 112  PRO A N     1 
ATOM   694   C  CA    . PRO A 1  114  ? -24.446 65.422  55.198  1.00 56.45 ? 112  PRO A CA    1 
ATOM   695   C  C     . PRO A 1  114  ? -24.331 64.787  53.820  1.00 56.79 ? 112  PRO A C     1 
ATOM   696   O  O     . PRO A 1  114  ? -25.046 63.826  53.518  1.00 59.47 ? 112  PRO A O     1 
ATOM   697   C  CB    . PRO A 1  114  ? -25.007 66.849  55.112  1.00 59.08 ? 112  PRO A CB    1 
ATOM   698   C  CG    . PRO A 1  114  ? -24.252 67.627  56.150  1.00 58.03 ? 112  PRO A CG    1 
ATOM   699   C  CD    . PRO A 1  114  ? -22.881 67.029  56.156  1.00 56.10 ? 112  PRO A CD    1 
ATOM   700   N  N     . ASP A 1  115  ? -23.448 65.308  52.973  1.00 57.02 ? 113  ASP A N     1 
ATOM   701   C  CA    . ASP A 1  115  ? -23.329 64.783  51.619  1.00 57.84 ? 113  ASP A CA    1 
ATOM   702   C  C     . ASP A 1  115  ? -22.659 63.416  51.638  1.00 54.45 ? 113  ASP A C     1 
ATOM   703   O  O     . ASP A 1  115  ? -21.551 63.266  52.164  1.00 54.94 ? 113  ASP A O     1 
ATOM   704   C  CB    . ASP A 1  115  ? -22.544 65.738  50.728  1.00 55.28 ? 113  ASP A CB    1 
ATOM   705   C  CG    . ASP A 1  115  ? -22.292 65.155  49.353  1.00 57.65 ? 113  ASP A CG    1 
ATOM   706   O  OD1   . ASP A 1  115  ? -23.279 64.756  48.694  1.00 57.08 ? 113  ASP A OD1   1 
ATOM   707   O  OD2   . ASP A 1  115  ? -21.116 65.083  48.933  1.00 55.36 ? 113  ASP A OD2   1 
ATOM   708   N  N     . THR A 1  116  ? -23.326 62.425  51.042  1.00 55.27 ? 114  THR A N     1 
ATOM   709   C  CA    . THR A 1  116  ? -22.787 61.069  51.018  1.00 53.49 ? 114  THR A CA    1 
ATOM   710   C  C     . THR A 1  116  ? -21.482 61.000  50.231  1.00 54.19 ? 114  THR A C     1 
ATOM   711   O  O     . THR A 1  116  ? -20.529 60.337  50.656  1.00 54.93 ? 114  THR A O     1 
ATOM   712   C  CB    . THR A 1  116  ? -23.824 60.109  50.435  1.00 52.48 ? 114  THR A CB    1 
ATOM   713   O  OG1   . THR A 1  116  ? -24.987 60.097  51.274  1.00 56.85 ? 114  THR A OG1   1 
ATOM   714   C  CG2   . THR A 1  116  ? -23.260 58.698  50.337  1.00 54.83 ? 114  THR A CG2   1 
ATOM   715   N  N     . ALA A 1  117  ? -21.413 61.682  49.086  1.00 52.32 ? 115  ALA A N     1 
ATOM   716   C  CA    . ALA A 1  117  ? -20.192 61.633  48.287  1.00 52.86 ? 115  ALA A CA    1 
ATOM   717   C  C     . ALA A 1  117  ? -19.028 62.304  49.008  1.00 50.66 ? 115  ALA A C     1 
ATOM   718   O  O     . ALA A 1  117  ? -17.894 61.813  48.952  1.00 49.88 ? 115  ALA A O     1 
ATOM   719   C  CB    . ALA A 1  117  ? -20.427 62.276  46.919  1.00 53.00 ? 115  ALA A CB    1 
ATOM   720   N  N     . THR A 1  118  ? -19.283 63.426  49.688  1.00 50.62 ? 116  THR A N     1 
ATOM   721   C  CA    . THR A 1  118  ? -18.227 64.073  50.463  1.00 51.95 ? 116  THR A CA    1 
ATOM   722   C  C     . THR A 1  118  ? -17.704 63.141  51.547  1.00 47.60 ? 116  THR A C     1 
ATOM   723   O  O     . THR A 1  118  ? -16.492 63.055  51.778  1.00 48.50 ? 116  THR A O     1 
ATOM   724   C  CB    . THR A 1  118  ? -18.742 65.372  51.089  1.00 52.62 ? 116  THR A CB    1 
ATOM   725   O  OG1   . THR A 1  118  ? -19.313 66.208  50.075  1.00 58.26 ? 116  THR A OG1   1 
ATOM   726   C  CG2   . THR A 1  118  ? -17.612 66.122  51.776  1.00 45.71 ? 116  THR A CG2   1 
ATOM   727   N  N     . ARG A 1  119  ? -18.611 62.426  52.211  1.00 49.81 ? 117  ARG A N     1 
ATOM   728   C  CA    . ARG A 1  119  ? -18.220 61.488  53.257  1.00 48.80 ? 117  ARG A CA    1 
ATOM   729   C  C     . ARG A 1  119  ? -17.335 60.379  52.698  1.00 47.86 ? 117  ARG A C     1 
ATOM   730   O  O     . ARG A 1  119  ? -16.284 60.058  53.267  1.00 45.06 ? 117  ARG A O     1 
ATOM   731   C  CB    . ARG A 1  119  ? -19.472 60.901  53.907  1.00 43.98 ? 117  ARG A CB    1 
ATOM   732   C  CG    . ARG A 1  119  ? -19.209 60.087  55.155  1.00 41.45 ? 117  ARG A CG    1 
ATOM   733   C  CD    . ARG A 1  119  ? -20.456 59.330  55.576  1.00 41.62 ? 117  ARG A CD    1 
ATOM   734   N  NE    . ARG A 1  119  ? -21.613 60.211  55.682  1.00 45.60 ? 117  ARG A NE    1 
ATOM   735   C  CZ    . ARG A 1  119  ? -22.761 60.023  55.046  1.00 46.90 ? 117  ARG A CZ    1 
ATOM   736   N  NH1   . ARG A 1  119  ? -22.963 58.963  54.280  1.00 43.90 ? 117  ARG A NH1   1 
ATOM   737   N  NH2   . ARG A 1  119  ? -23.735 60.917  55.188  1.00 52.08 ? 117  ARG A NH2   1 
ATOM   738   N  N     . ASP A 1  120  ? -17.747 59.783  51.576  1.00 46.80 ? 118  ASP A N     1 
ATOM   739   C  CA    . ASP A 1  120  ? -16.991 58.671  51.012  1.00 45.90 ? 118  ASP A CA    1 
ATOM   740   C  C     . ASP A 1  120  ? -15.613 59.125  50.554  1.00 46.55 ? 118  ASP A C     1 
ATOM   741   O  O     . ASP A 1  120  ? -14.633 58.381  50.679  1.00 46.04 ? 118  ASP A O     1 
ATOM   742   C  CB    . ASP A 1  120  ? -17.773 58.034  49.863  1.00 45.99 ? 118  ASP A CB    1 
ATOM   743   C  CG    . ASP A 1  120  ? -19.109 57.478  50.315  1.00 48.87 ? 118  ASP A CG    1 
ATOM   744   O  OD1   . ASP A 1  120  ? -19.387 57.541  51.527  1.00 44.71 ? 118  ASP A OD1   1 
ATOM   745   O  OD2   . ASP A 1  120  ? -19.881 56.983  49.468  1.00 48.68 ? 118  ASP A OD2   1 
ATOM   746   N  N     . ALA A 1  121  ? -15.514 60.353  50.038  1.00 46.99 ? 119  ALA A N     1 
ATOM   747   C  CA    . ALA A 1  121  ? -14.210 60.880  49.650  1.00 49.66 ? 119  ALA A CA    1 
ATOM   748   C  C     . ALA A 1  121  ? -13.317 61.082  50.866  1.00 47.66 ? 119  ALA A C     1 
ATOM   749   O  O     . ALA A 1  121  ? -12.128 60.744  50.834  1.00 48.33 ? 119  ALA A O     1 
ATOM   750   C  CB    . ALA A 1  121  ? -14.376 62.191  48.883  1.00 51.52 ? 119  ALA A CB    1 
ATOM   751   N  N     . LEU A 1  122  ? -13.871 61.629  51.948  1.00 48.18 ? 120  LEU A N     1 
ATOM   752   C  CA    . LEU A 1  122  ? -13.083 61.804  53.161  1.00 46.09 ? 120  LEU A CA    1 
ATOM   753   C  C     . LEU A 1  122  ? -12.603 60.462  53.697  1.00 44.99 ? 120  LEU A C     1 
ATOM   754   O  O     . LEU A 1  122  ? -11.444 60.326  54.106  1.00 47.10 ? 120  LEU A O     1 
ATOM   755   C  CB    . LEU A 1  122  ? -13.897 62.543  54.219  1.00 47.63 ? 120  LEU A CB    1 
ATOM   756   C  CG    . LEU A 1  122  ? -13.051 63.020  55.397  1.00 45.03 ? 120  LEU A CG    1 
ATOM   757   C  CD1   . LEU A 1  122  ? -12.050 64.043  54.912  1.00 50.99 ? 120  LEU A CD1   1 
ATOM   758   C  CD2   . LEU A 1  122  ? -13.913 63.597  56.497  1.00 44.26 ? 120  LEU A CD2   1 
ATOM   759   N  N     . ILE A 1  123  ? -13.479 59.457  53.691  1.00 44.87 ? 121  ILE A N     1 
ATOM   760   C  CA    . ILE A 1  123  ? -13.084 58.120  54.130  1.00 44.77 ? 121  ILE A CA    1 
ATOM   761   C  C     . ILE A 1  123  ? -11.948 57.593  53.261  1.00 46.18 ? 121  ILE A C     1 
ATOM   762   O  O     . ILE A 1  123  ? -10.898 57.178  53.766  1.00 41.26 ? 121  ILE A O     1 
ATOM   763   C  CB    . ILE A 1  123  ? -14.295 57.170  54.108  1.00 42.85 ? 121  ILE A CB    1 
ATOM   764   C  CG1   . ILE A 1  123  ? -15.328 57.595  55.156  1.00 40.87 ? 121  ILE A CG1   1 
ATOM   765   C  CG2   . ILE A 1  123  ? -13.846 55.727  54.319  1.00 36.72 ? 121  ILE A CG2   1 
ATOM   766   C  CD1   . ILE A 1  123  ? -16.654 56.886  55.022  1.00 36.54 ? 121  ILE A CD1   1 
ATOM   767   N  N     . ARG A 1  124  ? -12.135 57.622  51.939  1.00 46.34 ? 122  ARG A N     1 
ATOM   768   C  CA    . ARG A 1  124  ? -11.183 56.973  51.040  1.00 45.17 ? 122  ARG A CA    1 
ATOM   769   C  C     . ARG A 1  124  ? -9.846  57.701  51.013  1.00 49.61 ? 122  ARG A C     1 
ATOM   770   O  O     . ARG A 1  124  ? -8.788  57.064  51.069  1.00 50.52 ? 122  ARG A O     1 
ATOM   771   C  CB    . ARG A 1  124  ? -11.766 56.886  49.631  1.00 44.76 ? 122  ARG A CB    1 
ATOM   772   N  N     . ASP A 1  125  ? -9.868  59.030  50.939  1.00 50.98 ? 123  ASP A N     1 
ATOM   773   C  CA    . ASP A 1  125  ? -8.651  59.786  50.676  1.00 51.78 ? 123  ASP A CA    1 
ATOM   774   C  C     . ASP A 1  125  ? -7.955  60.271  51.938  1.00 52.42 ? 123  ASP A C     1 
ATOM   775   O  O     . ASP A 1  125  ? -6.738  60.488  51.914  1.00 57.72 ? 123  ASP A O     1 
ATOM   776   C  CB    . ASP A 1  125  ? -8.963  60.990  49.781  1.00 55.39 ? 123  ASP A CB    1 
ATOM   777   C  CG    . ASP A 1  125  ? -9.775  60.613  48.557  1.00 59.16 ? 123  ASP A CG    1 
ATOM   778   O  OD1   . ASP A 1  125  ? -9.577  59.498  48.028  1.00 57.13 ? 123  ASP A OD1   1 
ATOM   779   O  OD2   . ASP A 1  125  ? -10.617 61.432  48.129  1.00 62.87 ? 123  ASP A OD2   1 
ATOM   780   N  N     . LYS A 1  126  ? -8.684  60.443  53.038  1.00 52.21 ? 124  LYS A N     1 
ATOM   781   C  CA    . LYS A 1  126  ? -8.125  61.066  54.231  1.00 51.73 ? 124  LYS A CA    1 
ATOM   782   C  C     . LYS A 1  126  ? -8.166  60.165  55.456  1.00 51.24 ? 124  LYS A C     1 
ATOM   783   O  O     . LYS A 1  126  ? -7.125  59.941  56.084  1.00 53.48 ? 124  LYS A O     1 
ATOM   784   C  CB    . LYS A 1  126  ? -8.860  62.385  54.521  1.00 52.73 ? 124  LYS A CB    1 
ATOM   785   N  N     . ILE A 1  127  ? -9.338  59.642  55.824  1.00 48.73 ? 125  ILE A N     1 
ATOM   786   C  CA    . ILE A 1  127  ? -9.447  58.851  57.050  1.00 45.57 ? 125  ILE A CA    1 
ATOM   787   C  C     . ILE A 1  127  ? -8.652  57.556  56.921  1.00 47.95 ? 125  ILE A C     1 
ATOM   788   O  O     . ILE A 1  127  ? -7.788  57.252  57.751  1.00 47.90 ? 125  ILE A O     1 
ATOM   789   C  CB    . ILE A 1  127  ? -10.921 58.561  57.384  1.00 40.35 ? 125  ILE A CB    1 
ATOM   790   C  CG1   . ILE A 1  127  ? -11.758 59.842  57.341  1.00 46.41 ? 125  ILE A CG1   1 
ATOM   791   C  CG2   . ILE A 1  127  ? -11.032 57.899  58.754  1.00 40.34 ? 125  ILE A CG2   1 
ATOM   792   C  CD1   . ILE A 1  127  ? -11.310 60.903  58.313  1.00 45.97 ? 125  ILE A CD1   1 
ATOM   793   N  N     . ALA A 1  128  ? -8.934  56.776  55.873  1.00 48.46 ? 126  ALA A N     1 
ATOM   794   C  CA    . ALA A 1  128  ? -8.333  55.453  55.755  1.00 47.15 ? 126  ALA A CA    1 
ATOM   795   C  C     . ALA A 1  128  ? -6.824  55.539  55.580  1.00 55.27 ? 126  ALA A C     1 
ATOM   796   O  O     . ALA A 1  128  ? -6.086  54.691  56.093  1.00 49.32 ? 126  ALA A O     1 
ATOM   797   C  CB    . ALA A 1  128  ? -8.957  54.690  54.589  1.00 42.53 ? 126  ALA A CB    1 
ATOM   798   N  N     . ASP A 1  129  ? -6.349  56.559  54.861  1.00 77.15 ? 127  ASP A N     1 
ATOM   799   C  CA    . ASP A 1  129  ? -4.938  56.633  54.501  1.00 80.60 ? 127  ASP A CA    1 
ATOM   800   C  C     . ASP A 1  129  ? -4.047  56.984  55.686  1.00 80.69 ? 127  ASP A C     1 
ATOM   801   O  O     . ASP A 1  129  ? -2.858  56.646  55.670  1.00 84.50 ? 127  ASP A O     1 
ATOM   802   C  CB    . ASP A 1  129  ? -4.737  57.651  53.375  1.00 76.70 ? 127  ASP A CB    1 
ATOM   803   N  N     . GLY A 1  130  ? -4.582  57.643  56.709  1.00 66.64 ? 128  GLY A N     1 
ATOM   804   C  CA    . GLY A 1  130  ? -3.755  57.979  57.848  1.00 68.94 ? 128  GLY A CA    1 
ATOM   805   C  C     . GLY A 1  130  ? -4.477  58.658  58.991  1.00 66.58 ? 128  GLY A C     1 
ATOM   806   O  O     . GLY A 1  130  ? -5.372  58.075  59.609  1.00 60.70 ? 128  GLY A O     1 
ATOM   807   N  N     . ASN A 1  131  ? -4.087  59.899  59.275  1.00 70.95 ? 129  ASN A N     1 
ATOM   808   C  CA    . ASN A 1  131  ? -4.549  60.609  60.463  1.00 69.94 ? 129  ASN A CA    1 
ATOM   809   C  C     . ASN A 1  131  ? -6.040  60.902  60.355  1.00 62.95 ? 129  ASN A C     1 
ATOM   810   O  O     . ASN A 1  131  ? -6.462  61.736  59.547  1.00 65.90 ? 129  ASN A O     1 
ATOM   811   C  CB    . ASN A 1  131  ? -3.752  61.898  60.642  1.00 69.78 ? 129  ASN A CB    1 
ATOM   812   N  N     . TRP A 1  132  ? -6.840  60.208  61.166  1.00 53.95 ? 130  TRP A N     1 
ATOM   813   C  CA    . TRP A 1  132  ? -8.240  60.588  61.326  1.00 50.46 ? 130  TRP A CA    1 
ATOM   814   C  C     . TRP A 1  132  ? -8.376  61.852  62.159  1.00 48.77 ? 130  TRP A C     1 
ATOM   815   O  O     . TRP A 1  132  ? -9.358  62.589  62.012  1.00 50.54 ? 130  TRP A O     1 
ATOM   816   C  CB    . TRP A 1  132  ? -9.024  59.456  61.987  1.00 42.45 ? 130  TRP A CB    1 
ATOM   817   C  CG    . TRP A 1  132  ? -8.459  59.062  63.322  1.00 38.30 ? 130  TRP A CG    1 
ATOM   818   C  CD1   . TRP A 1  132  ? -7.538  58.084  63.559  1.00 33.79 ? 130  TRP A CD1   1 
ATOM   819   C  CD2   . TRP A 1  132  ? -8.767  59.641  64.600  1.00 31.74 ? 130  TRP A CD2   1 
ATOM   820   N  NE1   . TRP A 1  132  ? -7.260  58.010  64.903  1.00 32.15 ? 130  TRP A NE1   1 
ATOM   821   C  CE2   . TRP A 1  132  ? -7.998  58.956  65.565  1.00 31.02 ? 130  TRP A CE2   1 
ATOM   822   C  CE3   . TRP A 1  132  ? -9.617  60.667  65.021  1.00 34.70 ? 130  TRP A CE3   1 
ATOM   823   C  CZ2   . TRP A 1  132  ? -8.054  59.262  66.920  1.00 28.32 ? 130  TRP A CZ2   1 
ATOM   824   C  CZ3   . TRP A 1  132  ? -9.673  60.972  66.371  1.00 27.60 ? 130  TRP A CZ3   1 
ATOM   825   C  CH2   . TRP A 1  132  ? -8.897  60.273  67.305  1.00 28.45 ? 130  TRP A CH2   1 
ATOM   826   N  N     . LYS A 1  133  ? -7.410  62.107  63.045  1.00 48.42 ? 131  LYS A N     1 
ATOM   827   C  CA    . LYS A 1  133  ? -7.503  63.255  63.939  1.00 52.29 ? 131  LYS A CA    1 
ATOM   828   C  C     . LYS A 1  133  ? -7.429  64.564  63.165  1.00 59.96 ? 131  LYS A C     1 
ATOM   829   O  O     . LYS A 1  133  ? -8.146  65.520  63.483  1.00 61.60 ? 131  LYS A O     1 
ATOM   830   C  CB    . LYS A 1  133  ? -6.398  63.184  64.995  1.00 45.46 ? 131  LYS A CB    1 
ATOM   831   N  N     . SER A 1  134  ? -6.587  64.617  62.129  1.00 62.73 ? 132  SER A N     1 
ATOM   832   C  CA    . SER A 1  134  ? -6.393  65.850  61.375  1.00 64.90 ? 132  SER A CA    1 
ATOM   833   C  C     . SER A 1  134  ? -7.660  66.316  60.666  1.00 66.81 ? 132  SER A C     1 
ATOM   834   O  O     . SER A 1  134  ? -7.741  67.486  60.276  1.00 69.63 ? 132  SER A O     1 
ATOM   835   C  CB    . SER A 1  134  ? -5.266  65.663  60.356  1.00 65.35 ? 132  SER A CB    1 
ATOM   836   N  N     . HIS A 1  135  ? -8.655  65.442  60.498  1.00 65.45 ? 133  HIS A N     1 
ATOM   837   C  CA    . HIS A 1  135  ? -9.849  65.778  59.736  1.00 66.69 ? 133  HIS A CA    1 
ATOM   838   C  C     . HIS A 1  135  ? -11.139 65.768  60.541  1.00 67.44 ? 133  HIS A C     1 
ATOM   839   O  O     . HIS A 1  135  ? -12.138 66.322  60.069  1.00 69.00 ? 133  HIS A O     1 
ATOM   840   C  CB    . HIS A 1  135  ? -10.015 64.819  58.546  1.00 64.75 ? 133  HIS A CB    1 
ATOM   841   C  CG    . HIS A 1  135  ? -8.800  64.717  57.678  1.00 68.37 ? 133  HIS A CG    1 
ATOM   842   N  ND1   . HIS A 1  135  ? -7.744  63.880  57.970  1.00 65.64 ? 133  HIS A ND1   1 
ATOM   843   C  CD2   . HIS A 1  135  ? -8.473  65.347  56.525  1.00 68.53 ? 133  HIS A CD2   1 
ATOM   844   C  CE1   . HIS A 1  135  ? -6.819  63.999  57.035  1.00 68.58 ? 133  HIS A CE1   1 
ATOM   845   N  NE2   . HIS A 1  135  ? -7.237  64.883  56.146  1.00 70.58 ? 133  HIS A NE2   1 
ATOM   846   N  N     . LEU A 1  136  ? -11.158 65.159  61.722  1.00 66.93 ? 134  LEU A N     1 
ATOM   847   C  CA    . LEU A 1  136  ? -12.379 65.090  62.519  1.00 67.63 ? 134  LEU A CA    1 
ATOM   848   C  C     . LEU A 1  136  ? -12.099 65.341  63.999  1.00 68.94 ? 134  LEU A C     1 
ATOM   849   O  O     . LEU A 1  136  ? -13.012 65.637  64.773  1.00 69.15 ? 134  LEU A O     1 
ATOM   850   C  CB    . LEU A 1  136  ? -13.060 63.730  62.337  1.00 64.55 ? 134  LEU A CB    1 
ATOM   851   C  CG    . LEU A 1  136  ? -13.767 63.464  61.006  1.00 61.32 ? 134  LEU A CG    1 
ATOM   852   C  CD1   . LEU A 1  136  ? -14.202 62.012  60.918  1.00 52.62 ? 134  LEU A CD1   1 
ATOM   853   C  CD2   . LEU A 1  136  ? -14.961 64.391  60.839  1.00 58.66 ? 134  LEU A CD2   1 
ATOM   854   N  N     . SER A 1  139  ? -13.260 70.600  67.467  1.00 51.62 ? 137  SER A N     1 
ATOM   855   C  CA    . SER A 1  139  ? -13.876 71.342  68.564  1.00 46.27 ? 137  SER A CA    1 
ATOM   856   C  C     . SER A 1  139  ? -14.696 70.430  69.466  1.00 46.08 ? 137  SER A C     1 
ATOM   857   O  O     . SER A 1  139  ? -15.099 70.824  70.564  1.00 43.46 ? 137  SER A O     1 
ATOM   858   C  CB    . SER A 1  139  ? -14.764 72.465  68.024  1.00 47.74 ? 137  SER A CB    1 
ATOM   859   O  OG    . SER A 1  139  ? -13.987 73.501  67.449  1.00 60.59 ? 137  SER A OG    1 
ATOM   860   N  N     . ARG A 1  140  ? -14.957 69.213  68.991  1.00 38.48 ? 138  ARG A N     1 
ATOM   861   C  CA    . ARG A 1  140  ? -15.688 68.221  69.769  1.00 33.39 ? 138  ARG A CA    1 
ATOM   862   C  C     . ARG A 1  140  ? -14.983 66.884  69.624  1.00 33.29 ? 138  ARG A C     1 
ATOM   863   O  O     . ARG A 1  140  ? -14.720 66.433  68.505  1.00 34.19 ? 138  ARG A O     1 
ATOM   864   C  CB    . ARG A 1  140  ? -17.148 68.110  69.317  1.00 33.38 ? 138  ARG A CB    1 
ATOM   865   N  N     . SER A 1  141  ? -14.655 66.274  70.759  1.00 31.52 ? 139  SER A N     1 
ATOM   866   C  CA    . SER A 1  141  ? -14.086 64.937  70.756  1.00 26.25 ? 139  SER A CA    1 
ATOM   867   C  C     . SER A 1  141  ? -14.922 64.009  69.883  1.00 27.42 ? 139  SER A C     1 
ATOM   868   O  O     . SER A 1  141  ? -16.154 64.061  69.887  1.00 25.21 ? 139  SER A O     1 
ATOM   869   C  CB    . SER A 1  141  ? -14.019 64.401  72.188  1.00 26.61 ? 139  SER A CB    1 
ATOM   870   O  OG    . SER A 1  141  ? -13.529 63.071  72.218  1.00 23.96 ? 139  SER A OG    1 
ATOM   871   N  N     . LEU A 1  142  ? -14.240 63.171  69.104  1.00 26.20 ? 140  LEU A N     1 
ATOM   872   C  CA    . LEU A 1  142  ? -14.936 62.099  68.409  1.00 22.58 ? 140  LEU A CA    1 
ATOM   873   C  C     . LEU A 1  142  ? -15.748 61.229  69.360  1.00 21.13 ? 140  LEU A C     1 
ATOM   874   O  O     . LEU A 1  142  ? -16.736 60.606  68.949  1.00 21.43 ? 140  LEU A O     1 
ATOM   875   C  CB    . LEU A 1  142  ? -13.910 61.240  67.676  1.00 21.57 ? 140  LEU A CB    1 
ATOM   876   C  CG    . LEU A 1  142  ? -14.321 60.879  66.262  1.00 25.53 ? 140  LEU A CG    1 
ATOM   877   C  CD1   . LEU A 1  142  ? -14.253 62.118  65.387  1.00 33.78 ? 140  LEU A CD1   1 
ATOM   878   C  CD2   . LEU A 1  142  ? -13.435 59.769  65.726  1.00 27.48 ? 140  LEU A CD2   1 
ATOM   879   N  N     . PHE A 1  143  ? -15.368 61.196  70.632  1.00 18.59 ? 141  PHE A N     1 
ATOM   880   C  CA    . PHE A 1  143  ? -15.834 60.184  71.561  1.00 20.44 ? 141  PHE A CA    1 
ATOM   881   C  C     . PHE A 1  143  ? -16.836 60.737  72.571  1.00 22.44 ? 141  PHE A C     1 
ATOM   882   O  O     . PHE A 1  143  ? -17.050 60.123  73.618  1.00 22.56 ? 141  PHE A O     1 
ATOM   883   C  CB    . PHE A 1  143  ? -14.615 59.560  72.246  1.00 19.25 ? 141  PHE A CB    1 
ATOM   884   C  CG    . PHE A 1  143  ? -13.555 59.122  71.264  1.00 19.12 ? 141  PHE A CG    1 
ATOM   885   C  CD1   . PHE A 1  143  ? -13.838 58.127  70.334  1.00 18.32 ? 141  PHE A CD1   1 
ATOM   886   C  CD2   . PHE A 1  143  ? -12.308 59.716  71.244  1.00 20.62 ? 141  PHE A CD2   1 
ATOM   887   C  CE1   . PHE A 1  143  ? -12.891 57.723  69.410  1.00 19.51 ? 141  PHE A CE1   1 
ATOM   888   C  CE2   . PHE A 1  143  ? -11.352 59.309  70.317  1.00 20.40 ? 141  PHE A CE2   1 
ATOM   889   C  CZ    . PHE A 1  143  ? -11.647 58.311  69.403  1.00 18.01 ? 141  PHE A CZ    1 
ATOM   890   N  N     . VAL A 1  144  ? -17.463 61.878  72.263  1.00 20.77 ? 142  VAL A N     1 
ATOM   891   C  CA    A VAL A 1  144  ? -18.400 62.485  73.209  0.48 23.19 ? 142  VAL A CA    1 
ATOM   892   C  CA    B VAL A 1  144  ? -18.416 62.499  73.185  0.52 23.18 ? 142  VAL A CA    1 
ATOM   893   C  C     . VAL A 1  144  ? -19.518 61.520  73.578  1.00 22.24 ? 142  VAL A C     1 
ATOM   894   O  O     . VAL A 1  144  ? -19.978 61.501  74.725  1.00 23.16 ? 142  VAL A O     1 
ATOM   895   C  CB    A VAL A 1  144  ? -18.965 63.809  72.650  0.48 22.79 ? 142  VAL A CB    1 
ATOM   896   C  CB    B VAL A 1  144  ? -18.985 63.787  72.555  0.52 22.79 ? 142  VAL A CB    1 
ATOM   897   C  CG1   A VAL A 1  144  ? -17.883 64.881  72.619  0.48 24.96 ? 142  VAL A CG1   1 
ATOM   898   C  CG1   B VAL A 1  144  ? -20.186 64.277  73.311  0.52 23.63 ? 142  VAL A CG1   1 
ATOM   899   C  CG2   A VAL A 1  144  ? -19.553 63.601  71.265  0.48 22.16 ? 142  VAL A CG2   1 
ATOM   900   C  CG2   B VAL A 1  144  ? -17.916 64.875  72.513  0.52 24.98 ? 142  VAL A CG2   1 
ATOM   901   N  N     . ASN A 1  145  ? -19.958 60.686  72.643  1.00 22.46 ? 143  ASN A N     1 
ATOM   902   C  CA    . ASN A 1  145  ? -21.042 59.751  72.912  1.00 22.27 ? 143  ASN A CA    1 
ATOM   903   C  C     . ASN A 1  145  ? -20.552 58.318  73.116  1.00 24.79 ? 143  ASN A C     1 
ATOM   904   O  O     . ASN A 1  145  ? -21.335 57.376  72.970  1.00 22.10 ? 143  ASN A O     1 
ATOM   905   C  CB    . ASN A 1  145  ? -22.066 59.811  71.778  1.00 24.79 ? 143  ASN A CB    1 
ATOM   906   C  CG    . ASN A 1  145  ? -22.858 61.112  71.779  1.00 26.15 ? 143  ASN A CG    1 
ATOM   907   O  OD1   . ASN A 1  145  ? -23.345 61.549  72.821  1.00 30.97 ? 143  ASN A OD1   1 
ATOM   908   N  ND2   . ASN A 1  145  ? -22.975 61.739  70.619  1.00 27.16 ? 143  ASN A ND2   1 
ATOM   909   N  N     . ALA A 1  146  ? -19.277 58.134  73.470  1.00 20.61 ? 144  ALA A N     1 
ATOM   910   C  CA    . ALA A 1  146  ? -18.742 56.783  73.593  1.00 21.59 ? 144  ALA A CA    1 
ATOM   911   C  C     . ALA A 1  146  ? -19.398 55.970  74.704  1.00 21.27 ? 144  ALA A C     1 
ATOM   912   O  O     . ALA A 1  146  ? -19.398 54.737  74.623  1.00 24.63 ? 144  ALA A O     1 
ATOM   913   C  CB    . ALA A 1  146  ? -17.229 56.847  73.820  1.00 20.49 ? 144  ALA A CB    1 
ATOM   914   N  N     . ALA A 1  147  ? -19.964 56.613  75.732  1.00 23.91 ? 145  ALA A N     1 
ATOM   915   C  CA    . ALA A 1  147  ? -20.659 55.846  76.764  1.00 25.24 ? 145  ALA A CA    1 
ATOM   916   C  C     . ALA A 1  147  ? -21.842 55.099  76.170  1.00 25.75 ? 145  ALA A C     1 
ATOM   917   O  O     . ALA A 1  147  ? -22.116 53.949  76.537  1.00 24.55 ? 145  ALA A O     1 
ATOM   918   C  CB    . ALA A 1  147  ? -21.117 56.769  77.895  1.00 28.84 ? 145  ALA A CB    1 
ATOM   919   N  N     . THR A 1  148  ? -22.548 55.737  75.236  1.00 24.60 ? 146  THR A N     1 
ATOM   920   C  CA    . THR A 1  148  ? -23.644 55.076  74.538  1.00 24.75 ? 146  THR A CA    1 
ATOM   921   C  C     . THR A 1  148  ? -23.140 53.931  73.667  1.00 24.46 ? 146  THR A C     1 
ATOM   922   O  O     . THR A 1  148  ? -23.662 52.811  73.726  1.00 24.58 ? 146  THR A O     1 
ATOM   923   C  CB    . THR A 1  148  ? -24.403 56.097  73.694  1.00 27.12 ? 146  THR A CB    1 
ATOM   924   O  OG1   . THR A 1  148  ? -24.907 57.129  74.551  1.00 26.68 ? 146  THR A OG1   1 
ATOM   925   C  CG2   . THR A 1  148  ? -25.557 55.439  72.952  1.00 29.22 ? 146  THR A CG2   1 
ATOM   926   N  N     . TRP A 1  149  ? -22.130 54.192  72.835  1.00 22.44 ? 147  TRP A N     1 
ATOM   927   C  CA    . TRP A 1  149  ? -21.595 53.124  72.005  1.00 23.36 ? 147  TRP A CA    1 
ATOM   928   C  C     . TRP A 1  149  ? -20.960 52.025  72.843  1.00 21.41 ? 147  TRP A C     1 
ATOM   929   O  O     . TRP A 1  149  ? -21.005 50.853  72.454  1.00 24.42 ? 147  TRP A O     1 
ATOM   930   C  CB    . TRP A 1  149  ? -20.593 53.691  70.999  1.00 21.51 ? 147  TRP A CB    1 
ATOM   931   C  CG    . TRP A 1  149  ? -21.244 54.590  69.995  1.00 20.18 ? 147  TRP A CG    1 
ATOM   932   C  CD1   . TRP A 1  149  ? -20.988 55.915  69.788  1.00 24.45 ? 147  TRP A CD1   1 
ATOM   933   C  CD2   . TRP A 1  149  ? -22.268 54.228  69.059  1.00 22.81 ? 147  TRP A CD2   1 
ATOM   934   N  NE1   . TRP A 1  149  ? -21.783 56.398  68.770  1.00 25.35 ? 147  TRP A NE1   1 
ATOM   935   C  CE2   . TRP A 1  149  ? -22.576 55.379  68.309  1.00 24.58 ? 147  TRP A CE2   1 
ATOM   936   C  CE3   . TRP A 1  149  ? -22.939 53.034  68.769  1.00 22.11 ? 147  TRP A CE3   1 
ATOM   937   C  CZ2   . TRP A 1  149  ? -23.536 55.377  67.299  1.00 27.03 ? 147  TRP A CZ2   1 
ATOM   938   C  CZ3   . TRP A 1  149  ? -23.891 53.033  67.764  1.00 28.77 ? 147  TRP A CZ3   1 
ATOM   939   C  CH2   . TRP A 1  149  ? -24.179 54.197  67.040  1.00 29.95 ? 147  TRP A CH2   1 
ATOM   940   N  N     . GLY A 1  150  ? -20.382 52.373  73.999  1.00 21.71 ? 148  GLY A N     1 
ATOM   941   C  CA    . GLY A 1  150  ? -19.891 51.344  74.898  1.00 22.23 ? 148  GLY A CA    1 
ATOM   942   C  C     . GLY A 1  150  ? -20.990 50.402  75.354  1.00 24.29 ? 148  GLY A C     1 
ATOM   943   O  O     . GLY A 1  150  ? -20.780 49.191  75.471  1.00 25.85 ? 148  GLY A O     1 
ATOM   944   N  N     . LEU A 1  151  ? -22.179 50.947  75.622  1.00 23.59 ? 149  LEU A N     1 
ATOM   945   C  CA    . LEU A 1  151  ? -23.319 50.096  75.948  1.00 27.35 ? 149  LEU A CA    1 
ATOM   946   C  C     . LEU A 1  151  ? -23.692 49.209  74.768  1.00 26.53 ? 149  LEU A C     1 
ATOM   947   O  O     . LEU A 1  151  ? -23.979 48.019  74.942  1.00 27.29 ? 149  LEU A O     1 
ATOM   948   C  CB    . LEU A 1  151  ? -24.508 50.957  76.380  1.00 27.44 ? 149  LEU A CB    1 
ATOM   949   C  CG    . LEU A 1  151  ? -24.641 51.206  77.879  1.00 32.18 ? 149  LEU A CG    1 
ATOM   950   C  CD1   . LEU A 1  151  ? -25.656 52.306  78.153  1.00 37.53 ? 149  LEU A CD1   1 
ATOM   951   C  CD2   . LEU A 1  151  ? -25.047 49.912  78.577  1.00 32.41 ? 149  LEU A CD2   1 
ATOM   952   N  N     . VAL A 1  152  ? -23.675 49.766  73.555  1.00 28.15 ? 150  VAL A N     1 
ATOM   953   C  CA    . VAL A 1  152  ? -24.003 48.979  72.364  1.00 23.74 ? 150  VAL A CA    1 
ATOM   954   C  C     . VAL A 1  152  ? -23.010 47.840  72.177  1.00 27.57 ? 150  VAL A C     1 
ATOM   955   O  O     . VAL A 1  152  ? -23.394 46.708  71.858  1.00 28.19 ? 150  VAL A O     1 
ATOM   956   C  CB    . VAL A 1  152  ? -24.051 49.888  71.123  1.00 26.63 ? 150  VAL A CB    1 
ATOM   957   C  CG1   . VAL A 1  152  ? -24.202 49.058  69.865  1.00 28.80 ? 150  VAL A CG1   1 
ATOM   958   C  CG2   . VAL A 1  152  ? -25.183 50.902  71.242  1.00 27.90 ? 150  VAL A CG2   1 
ATOM   959   N  N     . VAL A 1  153  ? -21.719 48.120  72.364  1.00 26.02 ? 151  VAL A N     1 
ATOM   960   C  CA    . VAL A 1  153  ? -20.687 47.136  72.058  1.00 26.97 ? 151  VAL A CA    1 
ATOM   961   C  C     . VAL A 1  153  ? -20.513 46.137  73.197  1.00 24.80 ? 151  VAL A C     1 
ATOM   962   O  O     . VAL A 1  153  ? -20.378 44.928  72.959  1.00 28.16 ? 151  VAL A O     1 
ATOM   963   C  CB    . VAL A 1  153  ? -19.360 47.846  71.728  1.00 24.06 ? 151  VAL A CB    1 
ATOM   964   C  CG1   . VAL A 1  153  ? -18.239 46.826  71.639  1.00 25.57 ? 151  VAL A CG1   1 
ATOM   965   C  CG2   . VAL A 1  153  ? -19.475 48.626  70.424  1.00 23.26 ? 151  VAL A CG2   1 
ATOM   966   N  N     . THR A 1  154  ? -20.485 46.614  74.443  1.00 25.09 ? 152  THR A N     1 
ATOM   967   C  CA    . THR A 1  154  ? -20.150 45.776  75.586  1.00 26.47 ? 152  THR A CA    1 
ATOM   968   C  C     . THR A 1  154  ? -21.336 45.438  76.482  1.00 28.83 ? 152  THR A C     1 
ATOM   969   O  O     . THR A 1  154  ? -21.213 44.545  77.325  1.00 29.34 ? 152  THR A O     1 
ATOM   970   C  CB    . THR A 1  154  ? -19.074 46.453  76.448  1.00 28.29 ? 152  THR A CB    1 
ATOM   971   O  OG1   . THR A 1  154  ? -19.644 47.583  77.122  1.00 28.86 ? 152  THR A OG1   1 
ATOM   972   C  CG2   . THR A 1  154  ? -17.917 46.926  75.583  1.00 26.63 ? 152  THR A CG2   1 
ATOM   973   N  N     . GLY A 1  155  ? -22.465 46.126  76.344  1.00 28.29 ? 153  GLY A N     1 
ATOM   974   C  CA    . GLY A 1  155  ? -23.562 45.945  77.272  1.00 29.07 ? 153  GLY A CA    1 
ATOM   975   C  C     . GLY A 1  155  ? -23.340 46.539  78.644  1.00 33.03 ? 153  GLY A C     1 
ATOM   976   O  O     . GLY A 1  155  ? -24.181 46.342  79.530  1.00 34.00 ? 153  GLY A O     1 
ATOM   977   N  N     . LYS A 1  156  ? -22.247 47.265  78.847  1.00 28.64 ? 154  LYS A N     1 
ATOM   978   C  CA    . LYS A 1  156  ? -21.906 47.852  80.130  1.00 30.97 ? 154  LYS A CA    1 
ATOM   979   C  C     . LYS A 1  156  ? -21.804 49.363  79.984  1.00 30.66 ? 154  LYS A C     1 
ATOM   980   O  O     . LYS A 1  156  ? -21.389 49.879  78.938  1.00 28.30 ? 154  LYS A O     1 
ATOM   981   C  CB    . LYS A 1  156  ? -20.585 47.287  80.663  1.00 34.68 ? 154  LYS A CB    1 
ATOM   982   N  N     . LEU A 1  157  ? -22.198 50.067  81.041  1.00 28.04 ? 155  LEU A N     1 
ATOM   983   C  CA    . LEU A 1  157  ? -22.149 51.522  81.086  1.00 29.75 ? 155  LEU A CA    1 
ATOM   984   C  C     . LEU A 1  157  ? -20.920 51.984  81.861  1.00 34.27 ? 155  LEU A C     1 
ATOM   985   O  O     . LEU A 1  157  ? -20.690 51.545  82.993  1.00 32.18 ? 155  LEU A O     1 
ATOM   986   C  CB    . LEU A 1  157  ? -23.415 52.084  81.734  1.00 30.94 ? 155  LEU A CB    1 
ATOM   987   C  CG    . LEU A 1  157  ? -23.451 53.605  81.889  1.00 36.41 ? 155  LEU A CG    1 
ATOM   988   C  CD1   . LEU A 1  157  ? -23.486 54.289  80.532  1.00 31.34 ? 155  LEU A CD1   1 
ATOM   989   C  CD2   . LEU A 1  157  ? -24.641 54.021  82.736  1.00 35.24 ? 155  LEU A CD2   1 
ATOM   990   N  N     . THR A 1  158  ? -20.131 52.860  81.241  1.00 33.41 ? 156  THR A N     1 
ATOM   991   C  CA    . THR A 1  158  ? -19.064 53.601  81.903  1.00 31.68 ? 156  THR A CA    1 
ATOM   992   C  C     . THR A 1  158  ? -19.436 55.077  81.862  1.00 33.86 ? 156  THR A C     1 
ATOM   993   O  O     . THR A 1  158  ? -19.709 55.615  80.785  1.00 37.27 ? 156  THR A O     1 
ATOM   994   C  CB    . THR A 1  158  ? -17.710 53.370  81.215  1.00 35.45 ? 156  THR A CB    1 
ATOM   995   O  OG1   . THR A 1  158  ? -17.516 51.968  80.981  1.00 38.85 ? 156  THR A OG1   1 
ATOM   996   C  CG2   . THR A 1  158  ? -16.572 53.891  82.081  1.00 36.96 ? 156  THR A CG2   1 
ATOM   997   N  N     . SER A 1  159  ? -19.446 55.732  83.029  1.00 28.60 ? 157  SER A N     1 
ATOM   998   C  CA    . SER A 1  159  ? -20.024 57.070  83.119  1.00 27.81 ? 157  SER A CA    1 
ATOM   999   C  C     . SER A 1  159  ? -19.206 58.114  82.363  1.00 25.97 ? 157  SER A C     1 
ATOM   1000  O  O     . SER A 1  159  ? -19.764 59.098  81.871  1.00 29.53 ? 157  SER A O     1 
ATOM   1001  C  CB    . SER A 1  159  ? -20.176 57.470  84.584  1.00 32.51 ? 157  SER A CB    1 
ATOM   1002  O  OG    . SER A 1  159  ? -18.975 57.222  85.293  1.00 35.84 ? 157  SER A OG    1 
ATOM   1003  N  N     . THR A 1  160  ? -17.899 57.928  82.267  1.00 26.42 ? 158  THR A N     1 
ATOM   1004  C  CA    . THR A 1  160  ? -17.039 58.824  81.511  1.00 21.93 ? 158  THR A CA    1 
ATOM   1005  C  C     . THR A 1  160  ? -16.263 58.014  80.485  1.00 22.23 ? 158  THR A C     1 
ATOM   1006  O  O     . THR A 1  160  ? -16.191 56.783  80.552  1.00 24.33 ? 158  THR A O     1 
ATOM   1007  C  CB    . THR A 1  160  ? -16.069 59.585  82.423  1.00 22.61 ? 158  THR A CB    1 
ATOM   1008  O  OG1   . THR A 1  160  ? -15.288 58.639  83.151  1.00 23.65 ? 158  THR A OG1   1 
ATOM   1009  C  CG2   . THR A 1  160  ? -16.823 60.481  83.380  1.00 25.96 ? 158  THR A CG2   1 
ATOM   1010  N  N     . VAL A 1  161  ? -15.667 58.736  79.537  1.00 16.51 ? 159  VAL A N     1 
ATOM   1011  C  CA    . VAL A 1  161  ? -15.062 58.158  78.341  1.00 18.08 ? 159  VAL A CA    1 
ATOM   1012  C  C     . VAL A 1  161  ? -13.548 58.172  78.504  1.00 16.96 ? 159  VAL A C     1 
ATOM   1013  O  O     . VAL A 1  161  ? -12.961 59.227  78.760  1.00 18.02 ? 159  VAL A O     1 
ATOM   1014  C  CB    . VAL A 1  161  ? -15.467 58.966  77.095  1.00 18.72 ? 159  VAL A CB    1 
ATOM   1015  C  CG1   . VAL A 1  161  ? -14.744 58.480  75.886  1.00 21.81 ? 159  VAL A CG1   1 
ATOM   1016  C  CG2   . VAL A 1  161  ? -16.984 58.953  76.898  1.00 22.15 ? 159  VAL A CG2   1 
ATOM   1017  N  N     . ASN A 1  162  ? -12.903 57.021  78.337  1.00 15.82 ? 160  ASN A N     1 
ATOM   1018  C  CA    . ASN A 1  162  ? -11.441 57.043  78.298  1.00 16.36 ? 160  ASN A CA    1 
ATOM   1019  C  C     . ASN A 1  162  ? -11.065 57.401  76.872  1.00 16.08 ? 160  ASN A C     1 
ATOM   1020  O  O     . ASN A 1  162  ? -10.854 56.537  76.017  1.00 16.68 ? 160  ASN A O     1 
ATOM   1021  C  CB    . ASN A 1  162  ? -10.831 55.721  78.745  1.00 16.14 ? 160  ASN A CB    1 
ATOM   1022  C  CG    . ASN A 1  162  ? -9.304  55.785  78.787  1.00 20.09 ? 160  ASN A CG    1 
ATOM   1023  O  OD1   . ASN A 1  162  ? -8.693  56.643  78.131  1.00 18.04 ? 160  ASN A OD1   1 
ATOM   1024  N  ND2   . ASN A 1  162  ? -8.688  54.905  79.568  1.00 20.84 ? 160  ASN A ND2   1 
ATOM   1025  N  N     . ASP A 1  163  ? -10.995 58.707  76.608  1.00 14.92 ? 161  ASP A N     1 
ATOM   1026  C  CA    . ASP A 1  163  ? -10.816 59.157  75.241  1.00 15.34 ? 161  ASP A CA    1 
ATOM   1027  C  C     . ASP A 1  163  ? -9.412  58.897  74.725  1.00 17.00 ? 161  ASP A C     1 
ATOM   1028  O  O     . ASP A 1  163  ? -9.234  58.766  73.518  1.00 16.57 ? 161  ASP A O     1 
ATOM   1029  C  CB    . ASP A 1  163  ? -11.180 60.648  75.092  1.00 16.33 ? 161  ASP A CB    1 
ATOM   1030  C  CG    . ASP A 1  163  ? -10.532 61.559  76.139  1.00 20.42 ? 161  ASP A CG    1 
ATOM   1031  O  OD1   . ASP A 1  163  ? -10.392 61.181  77.325  1.00 18.41 ? 161  ASP A OD1   1 
ATOM   1032  O  OD2   . ASP A 1  163  ? -10.211 62.707  75.751  1.00 20.51 ? 161  ASP A OD2   1 
ATOM   1033  N  N     . ARG A 1  164  ? -8.409  58.780  75.593  1.00 16.54 ? 162  ARG A N     1 
ATOM   1034  C  CA    A ARG A 1  164  ? -7.093  58.415  75.085  0.60 15.99 ? 162  ARG A CA    1 
ATOM   1035  C  CA    B ARG A 1  164  ? -7.083  58.411  75.107  0.40 16.04 ? 162  ARG A CA    1 
ATOM   1036  C  C     . ARG A 1  164  ? -7.026  56.938  74.709  1.00 15.89 ? 162  ARG A C     1 
ATOM   1037  O  O     . ARG A 1  164  ? -6.339  56.577  73.744  1.00 17.57 ? 162  ARG A O     1 
ATOM   1038  C  CB    A ARG A 1  164  ? -6.009  58.765  76.109  0.60 17.73 ? 162  ARG A CB    1 
ATOM   1039  C  CB    B ARG A 1  164  ? -6.029  58.735  76.167  0.40 17.75 ? 162  ARG A CB    1 
ATOM   1040  C  CG    A ARG A 1  164  ? -5.901  60.249  76.430  0.60 18.76 ? 162  ARG A CG    1 
ATOM   1041  C  CG    B ARG A 1  164  ? -5.900  60.217  76.488  0.40 18.78 ? 162  ARG A CG    1 
ATOM   1042  C  CD    A ARG A 1  164  ? -5.923  61.124  75.177  0.60 21.73 ? 162  ARG A CD    1 
ATOM   1043  C  CD    B ARG A 1  164  ? -5.228  61.005  75.363  0.40 19.40 ? 162  ARG A CD    1 
ATOM   1044  N  NE    A ARG A 1  164  ? -5.002  60.689  74.134  0.60 20.48 ? 162  ARG A NE    1 
ATOM   1045  N  NE    B ARG A 1  164  ? -6.196  61.503  74.391  0.40 23.28 ? 162  ARG A NE    1 
ATOM   1046  C  CZ    A ARG A 1  164  ? -5.099  61.029  72.851  0.60 24.21 ? 162  ARG A CZ    1 
ATOM   1047  C  CZ    B ARG A 1  164  ? -6.237  61.152  73.113  0.40 23.03 ? 162  ARG A CZ    1 
ATOM   1048  N  NH1   A ARG A 1  164  ? -6.085  61.796  72.410  0.60 24.63 ? 162  ARG A NH1   1 
ATOM   1049  N  NH1   B ARG A 1  164  ? -5.340  60.331  72.591  0.40 24.17 ? 162  ARG A NH1   1 
ATOM   1050  N  NH2   A ARG A 1  164  ? -4.193  60.575  71.984  0.60 20.83 ? 162  ARG A NH2   1 
ATOM   1051  N  NH2   B ARG A 1  164  ? -7.192  61.649  72.335  0.40 24.08 ? 162  ARG A NH2   1 
ATOM   1052  N  N     . SER A 1  165  ? -7.733  56.072  75.444  1.00 15.37 ? 163  SER A N     1 
ATOM   1053  C  CA    . SER A 1  165  ? -7.819  54.666  75.048  1.00 14.93 ? 163  SER A CA    1 
ATOM   1054  C  C     . SER A 1  165  ? -8.541  54.515  73.715  1.00 15.08 ? 163  SER A C     1 
ATOM   1055  O  O     . SER A 1  165  ? -8.130  53.719  72.861  1.00 14.16 ? 163  SER A O     1 
ATOM   1056  C  CB    . SER A 1  165  ? -8.547  53.863  76.128  1.00 15.34 ? 163  SER A CB    1 
ATOM   1057  O  OG    . SER A 1  165  ? -8.841  52.550  75.675  1.00 17.45 ? 163  SER A OG    1 
ATOM   1058  N  N     . LEU A 1  166  ? -9.644  55.256  73.537  1.00 14.68 ? 164  LEU A N     1 
ATOM   1059  C  CA    . LEU A 1  166  ? -10.401 55.187  72.290  1.00 16.33 ? 164  LEU A CA    1 
ATOM   1060  C  C     . LEU A 1  166  ? -9.600  55.737  71.119  1.00 15.85 ? 164  LEU A C     1 
ATOM   1061  O  O     . LEU A 1  166  ? -9.688  55.215  70.004  1.00 15.81 ? 164  LEU A O     1 
ATOM   1062  C  CB    . LEU A 1  166  ? -11.712 55.948  72.445  1.00 16.54 ? 164  LEU A CB    1 
ATOM   1063  C  CG    . LEU A 1  166  ? -12.686 55.242  73.383  1.00 16.79 ? 164  LEU A CG    1 
ATOM   1064  C  CD1   . LEU A 1  166  ? -13.933 56.074  73.533  1.00 17.43 ? 164  LEU A CD1   1 
ATOM   1065  C  CD2   . LEU A 1  166  ? -13.043 53.863  72.826  1.00 16.61 ? 164  LEU A CD2   1 
ATOM   1066  N  N     . ALA A 1  167  ? -8.847  56.816  71.342  1.00 16.57 ? 165  ALA A N     1 
ATOM   1067  C  CA    . ALA A 1  167  ? -8.026  57.363  70.269  1.00 15.81 ? 165  ALA A CA    1 
ATOM   1068  C  C     . ALA A 1  167  ? -6.977  56.353  69.843  1.00 16.52 ? 165  ALA A C     1 
ATOM   1069  O  O     . ALA A 1  167  ? -6.751  56.145  68.653  1.00 16.48 ? 165  ALA A O     1 
ATOM   1070  C  CB    . ALA A 1  167  ? -7.362  58.660  70.721  1.00 17.59 ? 165  ALA A CB    1 
ATOM   1071  N  N     . ALA A 1  168  ? -6.310  55.723  70.814  1.00 15.68 ? 166  ALA A N     1 
ATOM   1072  C  CA    . ALA A 1  168  ? -5.332  54.695  70.467  1.00 16.63 ? 166  ALA A CA    1 
ATOM   1073  C  C     . ALA A 1  168  ? -5.991  53.554  69.706  1.00 15.75 ? 166  ALA A C     1 
ATOM   1074  O  O     . ALA A 1  168  ? -5.463  53.084  68.694  1.00 16.40 ? 166  ALA A O     1 
ATOM   1075  C  CB    . ALA A 1  168  ? -4.642  54.183  71.733  1.00 16.39 ? 166  ALA A CB    1 
ATOM   1076  N  N     . ALA A 1  169  ? -7.170  53.122  70.156  1.00 16.27 ? 167  ALA A N     1 
ATOM   1077  C  CA    . ALA A 1  169  ? -7.850  52.006  69.513  1.00 15.37 ? 167  ALA A CA    1 
ATOM   1078  C  C     . ALA A 1  169  ? -8.281  52.355  68.094  1.00 15.58 ? 167  ALA A C     1 
ATOM   1079  O  O     . ALA A 1  169  ? -8.251  51.504  67.202  1.00 16.18 ? 167  ALA A O     1 
ATOM   1080  C  CB    . ALA A 1  169  ? -9.064  51.592  70.343  1.00 15.57 ? 167  ALA A CB    1 
ATOM   1081  N  N     . LEU A 1  170  ? -8.705  53.596  67.874  1.00 15.16 ? 168  LEU A N     1 
ATOM   1082  C  CA    . LEU A 1  170  ? -9.138  54.003  66.539  1.00 15.58 ? 168  LEU A CA    1 
ATOM   1083  C  C     . LEU A 1  170  ? -7.962  54.043  65.579  1.00 17.59 ? 168  LEU A C     1 
ATOM   1084  O  O     . LEU A 1  170  ? -8.038  53.529  64.455  1.00 18.19 ? 168  LEU A O     1 
ATOM   1085  C  CB    . LEU A 1  170  ? -9.821  55.365  66.619  1.00 18.76 ? 168  LEU A CB    1 
ATOM   1086  C  CG    . LEU A 1  170  ? -10.441 55.830  65.304  1.00 21.44 ? 168  LEU A CG    1 
ATOM   1087  C  CD1   . LEU A 1  170  ? -11.424 54.776  64.789  1.00 20.49 ? 168  LEU A CD1   1 
ATOM   1088  C  CD2   . LEU A 1  170  ? -11.121 57.171  65.510  1.00 22.02 ? 168  LEU A CD2   1 
ATOM   1089  N  N     . THR A 1  171  ? -6.845  54.631  66.017  1.00 17.80 ? 169  THR A N     1 
ATOM   1090  C  CA    . THR A 1  171  ? -5.644  54.607  65.195  1.00 17.01 ? 169  THR A CA    1 
ATOM   1091  C  C     . THR A 1  171  ? -5.245  53.174  64.873  1.00 17.70 ? 169  THR A C     1 
ATOM   1092  O  O     . THR A 1  171  ? -4.941  52.845  63.726  1.00 18.98 ? 169  THR A O     1 
ATOM   1093  C  CB    . THR A 1  171  ? -4.502  55.321  65.914  1.00 18.69 ? 169  THR A CB    1 
ATOM   1094  O  OG1   . THR A 1  171  ? -4.869  56.681  66.147  1.00 21.39 ? 169  THR A OG1   1 
ATOM   1095  C  CG2   . THR A 1  171  ? -3.217  55.262  65.081  1.00 21.85 ? 169  THR A CG2   1 
ATOM   1096  N  N     . ARG A 1  172  ? -5.258  52.304  65.884  1.00 16.20 ? 170  ARG A N     1 
ATOM   1097  C  CA    . ARG A 1  172  ? -4.834  50.922  65.682  1.00 17.08 ? 170  ARG A CA    1 
ATOM   1098  C  C     . ARG A 1  172  ? -5.724  50.218  64.671  1.00 18.10 ? 170  ARG A C     1 
ATOM   1099  O  O     . ARG A 1  172  ? -5.233  49.534  63.765  1.00 19.56 ? 170  ARG A O     1 
ATOM   1100  C  CB    . ARG A 1  172  ? -4.836  50.175  67.021  1.00 18.46 ? 170  ARG A CB    1 
ATOM   1101  C  CG    . ARG A 1  172  ? -4.096  48.827  66.998  1.00 18.22 ? 170  ARG A CG    1 
ATOM   1102  C  CD    . ARG A 1  172  ? -4.357  48.024  68.288  1.00 19.01 ? 170  ARG A CD    1 
ATOM   1103  N  NE    . ARG A 1  172  ? -4.111  48.809  69.489  1.00 17.63 ? 170  ARG A NE    1 
ATOM   1104  C  CZ    . ARG A 1  172  ? -5.055  49.301  70.286  1.00 16.74 ? 170  ARG A CZ    1 
ATOM   1105  N  NH1   . ARG A 1  172  ? -6.338  49.079  70.061  1.00 16.54 ? 170  ARG A NH1   1 
ATOM   1106  N  NH2   . ARG A 1  172  ? -4.700  50.031  71.340  1.00 17.95 ? 170  ARG A NH2   1 
ATOM   1107  N  N     . LEU A 1  173  ? -7.046  50.387  64.794  1.00 17.32 ? 171  LEU A N     1 
ATOM   1108  C  CA    . LEU A 1  173  ? -7.936  49.613  63.939  1.00 17.18 ? 171  LEU A CA    1 
ATOM   1109  C  C     . LEU A 1  173  ? -7.904  50.132  62.508  1.00 18.15 ? 171  LEU A C     1 
ATOM   1110  O  O     . LEU A 1  173  ? -7.987  49.351  61.561  1.00 19.59 ? 171  LEU A O     1 
ATOM   1111  C  CB    . LEU A 1  173  ? -9.359  49.621  64.509  1.00 19.15 ? 171  LEU A CB    1 
ATOM   1112  C  CG    . LEU A 1  173  ? -10.274 50.851  64.430  1.00 19.48 ? 171  LEU A CG    1 
ATOM   1113  C  CD1   . LEU A 1  173  ? -11.040 50.918  63.105  1.00 22.00 ? 171  LEU A CD1   1 
ATOM   1114  C  CD2   . LEU A 1  173  ? -11.252 50.883  65.595  1.00 19.93 ? 171  LEU A CD2   1 
ATOM   1115  N  N     . ILE A 1  174  ? -7.777  51.449  62.331  1.00 20.05 ? 172  ILE A N     1 
ATOM   1116  C  CA    . ILE A 1  174  ? -7.688  51.999  60.982  1.00 18.22 ? 172  ILE A CA    1 
ATOM   1117  C  C     . ILE A 1  174  ? -6.383  51.572  60.323  1.00 19.52 ? 172  ILE A C     1 
ATOM   1118  O  O     . ILE A 1  174  ? -6.361  51.167  59.156  1.00 20.52 ? 172  ILE A O     1 
ATOM   1119  C  CB    . ILE A 1  174  ? -7.830  53.532  61.021  1.00 20.06 ? 172  ILE A CB    1 
ATOM   1120  C  CG1   . ILE A 1  174  ? -9.274  53.915  61.360  1.00 23.64 ? 172  ILE A CG1   1 
ATOM   1121  C  CG2   . ILE A 1  174  ? -7.411  54.140  59.683  1.00 24.10 ? 172  ILE A CG2   1 
ATOM   1122  C  CD1   . ILE A 1  174  ? -9.463  55.395  61.635  1.00 23.37 ? 172  ILE A CD1   1 
ATOM   1123  N  N     . SER A 1  175  ? -5.274  51.655  61.059  1.00 19.48 ? 173  SER A N     1 
ATOM   1124  C  CA    . SER A 1  175  ? -3.991  51.264  60.485  1.00 18.56 ? 173  SER A CA    1 
ATOM   1125  C  C     . SER A 1  175  ? -3.947  49.773  60.193  1.00 21.08 ? 173  SER A C     1 
ATOM   1126  O  O     . SER A 1  175  ? -3.259  49.350  59.257  1.00 22.59 ? 173  SER A O     1 
ATOM   1127  C  CB    . SER A 1  175  ? -2.840  51.644  61.411  1.00 19.99 ? 173  SER A CB    1 
ATOM   1128  O  OG    . SER A 1  175  ? -2.738  53.044  61.561  1.00 24.01 ? 173  SER A OG    1 
ATOM   1129  N  N     . ARG A 1  176  ? -4.689  48.971  60.958  1.00 20.26 ? 174  ARG A N     1 
ATOM   1130  C  CA    . ARG A 1  176  ? -4.698  47.531  60.719  1.00 20.68 ? 174  ARG A CA    1 
ATOM   1131  C  C     . ARG A 1  176  ? -5.649  47.151  59.593  1.00 22.79 ? 174  ARG A C     1 
ATOM   1132  O  O     . ARG A 1  176  ? -5.298  46.330  58.740  1.00 23.86 ? 174  ARG A O     1 
ATOM   1133  C  CB    . ARG A 1  176  ? -5.074  46.792  62.011  1.00 24.60 ? 174  ARG A CB    1 
ATOM   1134  C  CG    . ARG A 1  176  ? -4.920  45.267  61.947  1.00 22.87 ? 174  ARG A CG    1 
ATOM   1135  C  CD    . ARG A 1  176  ? -5.174  44.620  63.316  1.00 21.73 ? 174  ARG A CD    1 
ATOM   1136  N  NE    . ARG A 1  176  ? -6.586  44.636  63.684  1.00 21.89 ? 174  ARG A NE    1 
ATOM   1137  C  CZ    . ARG A 1  176  ? -7.135  45.355  64.660  1.00 24.14 ? 174  ARG A CZ    1 
ATOM   1138  N  NH1   . ARG A 1  176  ? -6.411  46.125  65.475  1.00 20.54 ? 174  ARG A NH1   1 
ATOM   1139  N  NH2   . ARG A 1  176  ? -8.452  45.294  64.838  1.00 25.73 ? 174  ARG A NH2   1 
ATOM   1140  N  N     . CYS A 1  177  ? -6.847  47.752  59.556  1.00 22.26 ? 175  CYS A N     1 
ATOM   1141  C  CA    . CYS A 1  177  ? -7.911  47.274  58.684  1.00 24.86 ? 175  CYS A CA    1 
ATOM   1142  C  C     . CYS A 1  177  ? -8.366  48.268  57.623  1.00 26.40 ? 175  CYS A C     1 
ATOM   1143  O  O     . CYS A 1  177  ? -9.073  47.863  56.698  1.00 28.31 ? 175  CYS A O     1 
ATOM   1144  C  CB    . CYS A 1  177  ? -9.130  46.860  59.516  1.00 24.13 ? 175  CYS A CB    1 
ATOM   1145  S  SG    . CYS A 1  177  ? -8.750  45.631  60.773  1.00 26.74 ? 175  CYS A SG    1 
ATOM   1146  N  N     . GLY A 1  178  ? -8.019  49.544  57.745  1.00 25.33 ? 176  GLY A N     1 
ATOM   1147  C  CA    . GLY A 1  178  ? -8.202  50.440  56.620  1.00 24.62 ? 176  GLY A CA    1 
ATOM   1148  C  C     . GLY A 1  178  ? -9.646  50.768  56.286  1.00 23.48 ? 176  GLY A C     1 
ATOM   1149  O  O     . GLY A 1  178  ? -10.565 50.638  57.093  1.00 25.17 ? 176  GLY A O     1 
ATOM   1150  N  N     . GLU A 1  179  ? -9.825  51.195  55.041  1.00 27.14 ? 177  GLU A N     1 
ATOM   1151  C  CA    . GLU A 1  179  ? -11.143 51.608  54.567  1.00 24.76 ? 177  GLU A CA    1 
ATOM   1152  C  C     . GLU A 1  179  ? -12.238 50.559  54.755  1.00 22.82 ? 177  GLU A C     1 
ATOM   1153  O  O     . GLU A 1  179  ? -13.357 50.945  55.137  1.00 26.77 ? 177  GLU A O     1 
ATOM   1154  C  CB    . GLU A 1  179  ? -11.025 52.024  53.094  1.00 24.93 ? 177  GLU A CB    1 
ATOM   1155  N  N     . PRO A 1  180  ? -12.018 49.259  54.515  1.00 25.18 ? 178  PRO A N     1 
ATOM   1156  C  CA    . PRO A 1  180  ? -13.136 48.311  54.667  1.00 24.71 ? 178  PRO A CA    1 
ATOM   1157  C  C     . PRO A 1  180  ? -13.797 48.331  56.038  1.00 24.47 ? 178  PRO A C     1 
ATOM   1158  O  O     . PRO A 1  180  ? -15.029 48.267  56.119  1.00 25.86 ? 178  PRO A O     1 
ATOM   1159  C  CB    . PRO A 1  180  ? -12.481 46.957  54.363  1.00 26.26 ? 178  PRO A CB    1 
ATOM   1160  C  CG    . PRO A 1  180  ? -11.380 47.293  53.418  1.00 27.80 ? 178  PRO A CG    1 
ATOM   1161  C  CD    . PRO A 1  180  ? -10.840 48.608  53.910  1.00 28.60 ? 178  PRO A CD    1 
ATOM   1162  N  N     . VAL A 1  181  ? -13.028 48.419  57.127  1.00 22.38 ? 179  VAL A N     1 
ATOM   1163  C  CA    . VAL A 1  181  ? -13.677 48.433  58.436  1.00 23.26 ? 179  VAL A CA    1 
ATOM   1164  C  C     . VAL A 1  181  ? -14.409 49.752  58.667  1.00 22.96 ? 179  VAL A C     1 
ATOM   1165  O  O     . VAL A 1  181  ? -15.437 49.780  59.353  1.00 23.27 ? 179  VAL A O     1 
ATOM   1166  C  CB    . VAL A 1  181  ? -12.661 48.140  59.562  1.00 24.09 ? 179  VAL A CB    1 
ATOM   1167  C  CG1   . VAL A 1  181  ? -11.720 49.328  59.800  1.00 21.90 ? 179  VAL A CG1   1 
ATOM   1168  C  CG2   . VAL A 1  181  ? -13.396 47.765  60.840  1.00 25.53 ? 179  VAL A CG2   1 
ATOM   1169  N  N     . ILE A 1  182  ? -13.909 50.857  58.109  1.00 23.45 ? 180  ILE A N     1 
ATOM   1170  C  CA    . ILE A 1  182  ? -14.600 52.132  58.263  1.00 20.62 ? 180  ILE A CA    1 
ATOM   1171  C  C     . ILE A 1  182  ? -15.930 52.091  57.528  1.00 26.74 ? 180  ILE A C     1 
ATOM   1172  O  O     . ILE A 1  182  ? -16.962 52.526  58.050  1.00 24.34 ? 180  ILE A O     1 
ATOM   1173  C  CB    . ILE A 1  182  ? -13.735 53.297  57.759  1.00 22.79 ? 180  ILE A CB    1 
ATOM   1174  C  CG1   . ILE A 1  182  ? -12.423 53.375  58.536  1.00 23.55 ? 180  ILE A CG1   1 
ATOM   1175  C  CG2   . ILE A 1  182  ? -14.498 54.607  57.897  1.00 25.23 ? 180  ILE A CG2   1 
ATOM   1176  C  CD1   . ILE A 1  182  ? -11.405 54.289  57.895  1.00 26.74 ? 180  ILE A CD1   1 
ATOM   1177  N  N     . ARG A 1  183  ? -15.912 51.574  56.303  1.00 23.68 ? 181  ARG A N     1 
ATOM   1178  C  CA    . ARG A 1  183  ? -17.139 51.438  55.519  1.00 26.93 ? 181  ARG A CA    1 
ATOM   1179  C  C     . ARG A 1  183  ? -18.177 50.606  56.267  1.00 30.35 ? 181  ARG A C     1 
ATOM   1180  O  O     . ARG A 1  183  ? -19.355 50.983  56.354  1.00 29.17 ? 181  ARG A O     1 
ATOM   1181  C  CB    . ARG A 1  183  ? -16.796 50.825  54.156  1.00 29.67 ? 181  ARG A CB    1 
ATOM   1182  C  CG    . ARG A 1  183  ? -17.975 50.366  53.287  1.00 34.48 ? 181  ARG A CG    1 
ATOM   1183  C  CD    . ARG A 1  183  ? -19.057 51.437  53.153  1.00 39.72 ? 181  ARG A CD    1 
ATOM   1184  N  NE    . ARG A 1  183  ? -18.528 52.712  52.690  1.00 40.99 ? 181  ARG A NE    1 
ATOM   1185  C  CZ    . ARG A 1  183  ? -19.071 53.888  52.971  1.00 38.79 ? 181  ARG A CZ    1 
ATOM   1186  N  NH1   . ARG A 1  183  ? -20.148 53.987  53.734  1.00 35.86 ? 181  ARG A NH1   1 
ATOM   1187  N  NH2   . ARG A 1  183  ? -18.509 54.993  52.484  1.00 43.47 ? 181  ARG A NH2   1 
ATOM   1188  N  N     . ARG A 1  184  ? -17.750 49.476  56.835  1.00 26.72 ? 182  ARG A N     1 
ATOM   1189  C  CA    . ARG A 1  184  ? -18.676 48.609  57.551  1.00 27.97 ? 182  ARG A CA    1 
ATOM   1190  C  C     . ARG A 1  184  ? -19.201 49.279  58.815  1.00 27.70 ? 182  ARG A C     1 
ATOM   1191  O  O     . ARG A 1  184  ? -20.372 49.102  59.181  1.00 27.16 ? 182  ARG A O     1 
ATOM   1192  C  CB    . ARG A 1  184  ? -17.989 47.286  57.875  1.00 27.55 ? 182  ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1  184  ? -17.927 46.331  56.696  1.00 32.50 ? 182  ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1  184  ? -19.152 45.415  56.676  1.00 31.99 ? 182  ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1  184  ? -18.991 44.270  57.569  1.00 37.10 ? 182  ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1  184  ? -19.754 44.009  58.623  1.00 35.95 ? 182  ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1  184  ? -20.770 44.791  58.955  1.00 38.19 ? 182  ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1  184  ? -19.502 42.927  59.355  1.00 33.59 ? 182  ARG A NH2   1 
ATOM   1199  N  N     . GLY A 1  185  ? -18.349 50.042  59.502  1.00 24.65 ? 183  GLY A N     1 
ATOM   1200  C  CA    . GLY A 1  185  ? -18.805 50.760  60.681  1.00 24.51 ? 183  GLY A CA    1 
ATOM   1201  C  C     . GLY A 1  185  ? -19.797 51.854  60.336  1.00 27.08 ? 183  GLY A C     1 
ATOM   1202  O  O     . GLY A 1  185  ? -20.783 52.057  61.048  1.00 26.62 ? 183  GLY A O     1 
ATOM   1203  N  N     . VAL A 1  186  ? -19.544 52.578  59.245  1.00 24.97 ? 184  VAL A N     1 
ATOM   1204  C  CA    . VAL A 1  186  ? -20.462 53.629  58.810  1.00 30.40 ? 184  VAL A CA    1 
ATOM   1205  C  C     . VAL A 1  186  ? -21.829 53.041  58.480  1.00 28.85 ? 184  VAL A C     1 
ATOM   1206  O  O     . VAL A 1  186  ? -22.868 53.537  58.940  1.00 28.65 ? 184  VAL A O     1 
ATOM   1207  C  CB    . VAL A 1  186  ? -19.866 54.397  57.616  1.00 28.05 ? 184  VAL A CB    1 
ATOM   1208  C  CG1   . VAL A 1  186  ? -20.952 55.161  56.867  1.00 30.28 ? 184  VAL A CG1   1 
ATOM   1209  C  CG2   . VAL A 1  186  ? -18.782 55.353  58.101  1.00 29.08 ? 184  VAL A CG2   1 
ATOM   1210  N  N     . ASP A 1  187  ? -21.853 51.964  57.698  1.00 28.37 ? 185  ASP A N     1 
ATOM   1211  C  CA    . ASP A 1  187  ? -23.132 51.373  57.311  1.00 31.51 ? 185  ASP A CA    1 
ATOM   1212  C  C     . ASP A 1  187  ? -23.862 50.799  58.520  1.00 33.77 ? 185  ASP A C     1 
ATOM   1213  O  O     . ASP A 1  187  ? -25.095 50.890  58.609  1.00 33.13 ? 185  ASP A O     1 
ATOM   1214  C  CB    . ASP A 1  187  ? -22.920 50.298  56.246  1.00 32.55 ? 185  ASP A CB    1 
ATOM   1215  C  CG    . ASP A 1  187  ? -22.362 50.865  54.949  1.00 33.66 ? 185  ASP A CG    1 
ATOM   1216  O  OD1   . ASP A 1  187  ? -22.535 52.078  54.701  1.00 37.60 ? 185  ASP A OD1   1 
ATOM   1217  O  OD2   . ASP A 1  187  ? -21.743 50.104  54.181  1.00 33.17 ? 185  ASP A OD2   1 
ATOM   1218  N  N     . MET A 1  188  ? -23.119 50.219  59.466  1.00 30.59 ? 186  MET A N     1 
ATOM   1219  C  CA    . MET A 1  188  ? -23.730 49.717  60.695  1.00 30.94 ? 186  MET A CA    1 
ATOM   1220  C  C     . MET A 1  188  ? -24.342 50.847  61.516  1.00 32.15 ? 186  MET A C     1 
ATOM   1221  O  O     . MET A 1  188  ? -25.498 50.759  61.953  1.00 33.21 ? 186  MET A O     1 
ATOM   1222  C  CB    . MET A 1  188  ? -22.686 48.968  61.521  1.00 34.38 ? 186  MET A CB    1 
ATOM   1223  C  CG    . MET A 1  188  ? -23.233 48.360  62.797  1.00 37.93 ? 186  MET A CG    1 
ATOM   1224  S  SD    . MET A 1  188  ? -24.363 47.010  62.413  1.00 47.51 ? 186  MET A SD    1 
ATOM   1225  C  CE    . MET A 1  188  ? -23.298 45.978  61.404  1.00 35.54 ? 186  MET A CE    1 
ATOM   1226  N  N     . ALA A 1  189  ? -23.572 51.913  61.758  1.00 31.28 ? 187  ALA A N     1 
ATOM   1227  C  CA    . ALA A 1  189  ? -24.096 53.041  62.525  1.00 30.34 ? 187  ALA A CA    1 
ATOM   1228  C  C     . ALA A 1  189  ? -25.300 53.670  61.836  1.00 33.23 ? 187  ALA A C     1 
ATOM   1229  O  O     . ALA A 1  189  ? -26.269 54.055  62.500  1.00 30.65 ? 187  ALA A O     1 
ATOM   1230  C  CB    . ALA A 1  189  ? -23.008 54.089  62.741  1.00 32.22 ? 187  ALA A CB    1 
ATOM   1231  N  N     . MET A 1  190  ? -25.253 53.788  60.505  1.00 29.64 ? 188  MET A N     1 
ATOM   1232  C  CA    . MET A 1  190  ? -26.373 54.371  59.766  1.00 33.46 ? 188  MET A CA    1 
ATOM   1233  C  C     . MET A 1  190  ? -27.648 53.563  59.969  1.00 31.31 ? 188  MET A C     1 
ATOM   1234  O  O     . MET A 1  190  ? -28.730 54.133  60.172  1.00 34.11 ? 188  MET A O     1 
ATOM   1235  C  CB    . MET A 1  190  ? -26.035 54.465  58.277  1.00 32.47 ? 188  MET A CB    1 
ATOM   1236  C  CG    . MET A 1  190  ? -27.037 55.270  57.455  1.00 36.86 ? 188  MET A CG    1 
ATOM   1237  S  SD    . MET A 1  190  ? -26.677 55.232  55.677  1.00 46.89 ? 188  MET A SD    1 
ATOM   1238  C  CE    . MET A 1  190  ? -24.910 55.534  55.670  1.00 38.39 ? 188  MET A CE    1 
ATOM   1239  N  N     . ARG A 1  191  ? -27.534 52.232  59.935  1.00 32.49 ? 189  ARG A N     1 
ATOM   1240  C  CA    . ARG A 1  191  ? -28.694 51.374  60.155  1.00 34.40 ? 189  ARG A CA    1 
ATOM   1241  C  C     . ARG A 1  191  ? -29.205 51.485  61.585  1.00 36.16 ? 189  ARG A C     1 
ATOM   1242  O  O     . ARG A 1  191  ? -30.417 51.576  61.812  1.00 35.49 ? 189  ARG A O     1 
ATOM   1243  C  CB    . ARG A 1  191  ? -28.344 49.925  59.831  1.00 33.62 ? 189  ARG A CB    1 
ATOM   1244  N  N     . MET A 1  192  ? -28.301 51.476  62.566  1.00 35.17 ? 190  MET A N     1 
ATOM   1245  C  CA    . MET A 1  192  ? -28.731 51.555  63.959  1.00 32.88 ? 190  MET A CA    1 
ATOM   1246  C  C     . MET A 1  192  ? -29.368 52.901  64.268  1.00 34.68 ? 190  MET A C     1 
ATOM   1247  O  O     . MET A 1  192  ? -30.420 52.968  64.912  1.00 36.97 ? 190  MET A O     1 
ATOM   1248  C  CB    . MET A 1  192  ? -27.546 51.302  64.889  1.00 34.22 ? 190  MET A CB    1 
ATOM   1249  C  CG    . MET A 1  192  ? -26.864 49.983  64.652  1.00 33.39 ? 190  MET A CG    1 
ATOM   1250  S  SD    . MET A 1  192  ? -25.590 49.685  65.885  1.00 43.77 ? 190  MET A SD    1 
ATOM   1251  C  CE    . MET A 1  192  ? -26.592 49.742  67.365  1.00 31.19 ? 190  MET A CE    1 
ATOM   1252  N  N     . MET A 1  193  ? -28.735 53.991  63.835  1.00 34.48 ? 191  MET A N     1 
ATOM   1253  C  CA    . MET A 1  193  ? -29.223 55.317  64.189  1.00 33.32 ? 191  MET A CA    1 
ATOM   1254  C  C     . MET A 1  193  ? -30.415 55.755  63.352  1.00 34.90 ? 191  MET A C     1 
ATOM   1255  O  O     . MET A 1  193  ? -31.184 56.615  63.798  1.00 37.11 ? 191  MET A O     1 
ATOM   1256  C  CB    . MET A 1  193  ? -28.105 56.349  64.056  1.00 32.80 ? 191  MET A CB    1 
ATOM   1257  C  CG    . MET A 1  193  ? -27.009 56.173  65.073  1.00 29.69 ? 191  MET A CG    1 
ATOM   1258  S  SD    . MET A 1  193  ? -26.004 57.660  65.224  1.00 40.55 ? 191  MET A SD    1 
ATOM   1259  C  CE    . MET A 1  193  ? -25.274 57.778  63.604  1.00 33.39 ? 191  MET A CE    1 
ATOM   1260  N  N     . GLY A 1  194  ? -30.585 55.189  62.162  1.00 33.64 ? 192  GLY A N     1 
ATOM   1261  C  CA    . GLY A 1  194  ? -31.663 55.588  61.282  1.00 34.67 ? 192  GLY A CA    1 
ATOM   1262  C  C     . GLY A 1  194  ? -32.858 54.658  61.322  1.00 35.17 ? 192  GLY A C     1 
ATOM   1263  O  O     . GLY A 1  194  ? -33.971 55.071  60.978  1.00 37.35 ? 192  GLY A O     1 
ATOM   1264  N  N     . GLU A 1  195  ? -32.653 53.407  61.751  1.00 33.79 ? 193  GLU A N     1 
ATOM   1265  C  CA    . GLU A 1  195  ? -33.690 52.384  61.648  1.00 34.58 ? 193  GLU A CA    1 
ATOM   1266  C  C     . GLU A 1  195  ? -33.933 51.573  62.913  1.00 32.74 ? 193  GLU A C     1 
ATOM   1267  O  O     . GLU A 1  195  ? -35.027 51.014  63.048  1.00 28.01 ? 193  GLU A O     1 
ATOM   1268  C  CB    . GLU A 1  195  ? -33.366 51.400  60.514  1.00 37.81 ? 193  GLU A CB    1 
ATOM   1269  C  CG    . GLU A 1  195  ? -33.149 52.043  59.161  1.00 43.88 ? 193  GLU A CG    1 
ATOM   1270  C  CD    . GLU A 1  195  ? -32.703 51.037  58.122  1.00 48.67 ? 193  GLU A CD    1 
ATOM   1271  O  OE1   . GLU A 1  195  ? -32.857 49.821  58.371  1.00 48.52 ? 193  GLU A OE1   1 
ATOM   1272  O  OE2   . GLU A 1  195  ? -32.198 51.460  57.060  1.00 55.36 ? 193  GLU A OE2   1 
ATOM   1273  N  N     . GLN A 1  196  ? -32.968 51.472  63.827  1.00 34.76 ? 194  GLN A N     1 
ATOM   1274  C  CA    . GLN A 1  196  ? -33.097 50.641  65.021  1.00 34.00 ? 194  GLN A CA    1 
ATOM   1275  C  C     . GLN A 1  196  ? -33.332 51.457  66.290  1.00 36.42 ? 194  GLN A C     1 
ATOM   1276  O  O     . GLN A 1  196  ? -34.200 51.114  67.098  1.00 37.35 ? 194  GLN A O     1 
ATOM   1277  C  CB    . GLN A 1  196  ? -31.845 49.766  65.183  1.00 38.60 ? 194  GLN A CB    1 
ATOM   1278  N  N     . PHE A 1  197  ? -32.563 52.524  66.499  1.00 34.44 ? 195  PHE A N     1 
ATOM   1279  C  CA    . PHE A 1  197  ? -32.798 53.373  67.660  1.00 34.70 ? 195  PHE A CA    1 
ATOM   1280  C  C     . PHE A 1  197  ? -34.018 54.256  67.469  1.00 31.75 ? 195  PHE A C     1 
ATOM   1281  O  O     . PHE A 1  197  ? -34.650 54.651  68.453  1.00 34.32 ? 195  PHE A O     1 
ATOM   1282  C  CB    . PHE A 1  197  ? -31.582 54.246  67.937  1.00 36.11 ? 195  PHE A CB    1 
ATOM   1283  C  CG    . PHE A 1  197  ? -30.388 53.480  68.403  1.00 39.49 ? 195  PHE A CG    1 
ATOM   1284  C  CD1   . PHE A 1  197  ? -30.542 52.330  69.158  1.00 39.59 ? 195  PHE A CD1   1 
ATOM   1285  C  CD2   . PHE A 1  197  ? -29.111 53.908  68.088  1.00 37.57 ? 195  PHE A CD2   1 
ATOM   1286  C  CE1   . PHE A 1  197  ? -29.442 51.622  69.595  1.00 41.11 ? 195  PHE A CE1   1 
ATOM   1287  C  CE2   . PHE A 1  197  ? -28.007 53.201  68.519  1.00 40.36 ? 195  PHE A CE2   1 
ATOM   1288  C  CZ    . PHE A 1  197  ? -28.178 52.058  69.277  1.00 38.50 ? 195  PHE A CZ    1 
ATOM   1289  N  N     . VAL A 1  198  ? -34.347 54.583  66.225  1.00 29.67 ? 196  VAL A N     1 
ATOM   1290  C  CA    . VAL A 1  198  ? -35.534 55.361  65.908  1.00 28.28 ? 196  VAL A CA    1 
ATOM   1291  C  C     . VAL A 1  198  ? -36.294 54.636  64.812  1.00 28.22 ? 196  VAL A C     1 
ATOM   1292  O  O     . VAL A 1  198  ? -35.714 53.913  63.996  1.00 30.50 ? 196  VAL A O     1 
ATOM   1293  C  CB    . VAL A 1  198  ? -35.206 56.810  65.469  1.00 25.96 ? 196  VAL A CB    1 
ATOM   1294  C  CG1   . VAL A 1  198  ? -34.522 57.566  66.600  1.00 30.52 ? 196  VAL A CG1   1 
ATOM   1295  C  CG2   . VAL A 1  198  ? -34.353 56.811  64.207  1.00 27.09 ? 196  VAL A CG2   1 
ATOM   1296  N  N     . THR A 1  199  ? -37.613 54.810  64.818  1.00 23.93 ? 197  THR A N     1 
ATOM   1297  C  CA    . THR A 1  199  ? -38.407 54.333  63.697  1.00 25.90 ? 197  THR A CA    1 
ATOM   1298  C  C     . THR A 1  199  ? -38.139 55.168  62.455  1.00 27.52 ? 197  THR A C     1 
ATOM   1299  O  O     . THR A 1  199  ? -38.140 54.634  61.343  1.00 29.63 ? 197  THR A O     1 
ATOM   1300  C  CB    . THR A 1  199  ? -39.885 54.347  64.078  1.00 24.72 ? 197  THR A CB    1 
ATOM   1301  O  OG1   . THR A 1  199  ? -40.042 53.584  65.280  1.00 25.15 ? 197  THR A OG1   1 
ATOM   1302  C  CG2   . THR A 1  199  ? -40.732 53.743  62.983  1.00 26.15 ? 197  THR A CG2   1 
ATOM   1303  N  N     . GLY A 1  200  ? -37.879 56.460  62.627  1.00 24.37 ? 198  GLY A N     1 
ATOM   1304  C  CA    . GLY A 1  200  ? -37.445 57.300  61.524  1.00 25.74 ? 198  GLY A CA    1 
ATOM   1305  C  C     . GLY A 1  200  ? -36.864 58.594  62.043  1.00 25.35 ? 198  GLY A C     1 
ATOM   1306  O  O     . GLY A 1  200  ? -37.059 58.961  63.205  1.00 23.32 ? 198  GLY A O     1 
ATOM   1307  N  N     . GLU A 1  201  ? -36.131 59.288  61.166  1.00 26.49 ? 199  GLU A N     1 
ATOM   1308  C  CA    . GLU A 1  201  ? -35.549 60.566  61.569  1.00 25.33 ? 199  GLU A CA    1 
ATOM   1309  C  C     . GLU A 1  201  ? -36.609 61.656  61.656  1.00 26.07 ? 199  GLU A C     1 
ATOM   1310  O  O     . GLU A 1  201  ? -36.479 62.590  62.454  1.00 25.72 ? 199  GLU A O     1 
ATOM   1311  C  CB    . GLU A 1  201  ? -34.439 60.980  60.595  1.00 29.04 ? 199  GLU A CB    1 
ATOM   1312  N  N     . THR A 1  202  ? -37.654 61.552  60.849  1.00 23.98 ? 200  THR A N     1 
ATOM   1313  C  CA    . THR A 1  202  ? -38.754 62.502  60.846  1.00 24.30 ? 200  THR A CA    1 
ATOM   1314  C  C     . THR A 1  202  ? -40.058 61.736  61.011  1.00 21.81 ? 200  THR A C     1 
ATOM   1315  O  O     . THR A 1  202  ? -40.116 60.526  60.782  1.00 21.76 ? 200  THR A O     1 
ATOM   1316  C  CB    . THR A 1  202  ? -38.808 63.272  59.543  1.00 23.70 ? 200  THR A CB    1 
ATOM   1317  O  OG1   . THR A 1  202  ? -39.016 62.321  58.493  1.00 25.71 ? 200  THR A OG1   1 
ATOM   1318  C  CG2   . THR A 1  202  ? -37.489 64.022  59.294  1.00 25.02 ? 200  THR A CG2   1 
ATOM   1319  N  N     . ILE A 1  203  ? -41.127 62.448  61.382  1.00 21.23 ? 201  ILE A N     1 
ATOM   1320  C  CA    . ILE A 1  203  ? -42.407 61.752  61.531  1.00 21.54 ? 201  ILE A CA    1 
ATOM   1321  C  C     . ILE A 1  203  ? -42.847 61.149  60.200  1.00 23.21 ? 201  ILE A C     1 
ATOM   1322  O  O     . ILE A 1  203  ? -43.376 60.034  60.158  1.00 22.41 ? 201  ILE A O     1 
ATOM   1323  C  CB    . ILE A 1  203  ? -43.478 62.685  62.134  1.00 20.01 ? 201  ILE A CB    1 
ATOM   1324  C  CG1   . ILE A 1  203  ? -44.747 61.891  62.483  1.00 19.28 ? 201  ILE A CG1   1 
ATOM   1325  C  CG2   . ILE A 1  203  ? -43.820 63.845  61.190  1.00 22.47 ? 201  ILE A CG2   1 
ATOM   1326  C  CD1   . ILE A 1  203  ? -44.525 60.777  63.488  1.00 20.29 ? 201  ILE A CD1   1 
ATOM   1327  N  N     . ARG A 1  204  ? -42.596 61.848  59.088  1.00 21.64 ? 202  ARG A N     1 
ATOM   1328  C  CA    . ARG A 1  204  ? -42.955 61.306  57.780  1.00 24.46 ? 202  ARG A CA    1 
ATOM   1329  C  C     . ARG A 1  204  ? -42.224 60.005  57.485  1.00 23.02 ? 202  ARG A C     1 
ATOM   1330  O  O     . ARG A 1  204  ? -42.827 59.046  56.990  1.00 25.37 ? 202  ARG A O     1 
ATOM   1331  C  CB    . ARG A 1  204  ? -42.663 62.335  56.697  1.00 28.33 ? 202  ARG A CB    1 
ATOM   1332  C  CG    . ARG A 1  204  ? -43.811 63.278  56.503  1.00 31.26 ? 202  ARG A CG    1 
ATOM   1333  C  CD    . ARG A 1  204  ? -43.384 64.577  55.850  1.00 34.95 ? 202  ARG A CD    1 
ATOM   1334  N  NE    . ARG A 1  204  ? -44.525 65.476  55.758  1.00 33.55 ? 202  ARG A NE    1 
ATOM   1335  C  CZ    . ARG A 1  204  ? -45.049 66.125  56.789  1.00 34.04 ? 202  ARG A CZ    1 
ATOM   1336  N  NH1   . ARG A 1  204  ? -44.534 66.026  58.011  1.00 28.60 ? 202  ARG A NH1   1 
ATOM   1337  N  NH2   . ARG A 1  204  ? -46.118 66.893  56.592  1.00 31.21 ? 202  ARG A NH2   1 
ATOM   1338  N  N     . GLU A 1  205  ? -40.922 59.958  57.770  1.00 23.12 ? 203  GLU A N     1 
ATOM   1339  C  CA    . GLU A 1  205  ? -40.169 58.726  57.568  1.00 25.15 ? 203  GLU A CA    1 
ATOM   1340  C  C     . GLU A 1  205  ? -40.645 57.624  58.508  1.00 25.30 ? 203  GLU A C     1 
ATOM   1341  O  O     . GLU A 1  205  ? -40.779 56.467  58.096  1.00 25.84 ? 203  GLU A O     1 
ATOM   1342  C  CB    . GLU A 1  205  ? -38.684 58.990  57.770  1.00 25.94 ? 203  GLU A CB    1 
ATOM   1343  C  CG    . GLU A 1  205  ? -37.814 57.815  57.401  1.00 28.19 ? 203  GLU A CG    1 
ATOM   1344  C  CD    . GLU A 1  205  ? -36.345 58.163  57.457  1.00 35.37 ? 203  GLU A CD    1 
ATOM   1345  O  OE1   . GLU A 1  205  ? -35.819 58.344  58.576  1.00 33.11 ? 203  GLU A OE1   1 
ATOM   1346  O  OE2   . GLU A 1  205  ? -35.719 58.266  56.379  1.00 38.08 ? 203  GLU A OE2   1 
ATOM   1347  N  N     . ALA A 1  206  ? -40.917 57.963  59.770  1.00 22.84 ? 204  ALA A N     1 
ATOM   1348  C  CA    . ALA A 1  206  ? -41.396 56.956  60.715  1.00 24.23 ? 204  ALA A CA    1 
ATOM   1349  C  C     . ALA A 1  206  ? -42.737 56.385  60.278  1.00 23.76 ? 204  ALA A C     1 
ATOM   1350  O  O     . ALA A 1  206  ? -42.950 55.167  60.335  1.00 24.75 ? 204  ALA A O     1 
ATOM   1351  C  CB    . ALA A 1  206  ? -41.492 57.555  62.120  1.00 21.02 ? 204  ALA A CB    1 
ATOM   1352  N  N     . LEU A 1  207  ? -43.647 57.249  59.820  1.00 22.15 ? 205  LEU A N     1 
ATOM   1353  C  CA    . LEU A 1  207  ? -44.939 56.782  59.323  1.00 23.47 ? 205  LEU A CA    1 
ATOM   1354  C  C     . LEU A 1  207  ? -44.779 55.879  58.110  1.00 26.53 ? 205  LEU A C     1 
ATOM   1355  O  O     . LEU A 1  207  ? -45.537 54.915  57.943  1.00 27.26 ? 205  LEU A O     1 
ATOM   1356  C  CB    . LEU A 1  207  ? -45.832 57.973  58.980  1.00 25.59 ? 205  LEU A CB    1 
ATOM   1357  C  CG    . LEU A 1  207  ? -46.384 58.725  60.187  1.00 24.79 ? 205  LEU A CG    1 
ATOM   1358  C  CD1   . LEU A 1  207  ? -47.067 60.016  59.745  1.00 22.49 ? 205  LEU A CD1   1 
ATOM   1359  C  CD2   . LEU A 1  207  ? -47.359 57.840  60.966  1.00 21.46 ? 205  LEU A CD2   1 
ATOM   1360  N  N     . LYS A 1  208  ? -43.814 56.187  57.236  1.00 24.53 ? 206  LYS A N     1 
ATOM   1361  C  CA    . LYS A 1  208  ? -43.595 55.343  56.067  1.00 29.83 ? 206  LYS A CA    1 
ATOM   1362  C  C     . LYS A 1  208  ? -43.160 53.949  56.485  1.00 25.72 ? 206  LYS A C     1 
ATOM   1363  O  O     . LYS A 1  208  ? -43.674 52.949  55.971  1.00 32.77 ? 206  LYS A O     1 
ATOM   1364  C  CB    . LYS A 1  208  ? -42.552 55.975  55.141  1.00 27.29 ? 206  LYS A CB    1 
ATOM   1365  N  N     . ARG A 1  209  ? -42.237 53.865  57.440  1.00 28.00 ? 207  ARG A N     1 
ATOM   1366  C  CA    . ARG A 1  209  ? -41.713 52.584  57.885  1.00 27.81 ? 207  ARG A CA    1 
ATOM   1367  C  C     . ARG A 1  209  ? -42.668 51.821  58.792  1.00 29.41 ? 207  ARG A C     1 
ATOM   1368  O  O     . ARG A 1  209  ? -42.409 50.650  59.085  1.00 33.20 ? 207  ARG A O     1 
ATOM   1369  C  CB    . ARG A 1  209  ? -40.385 52.811  58.588  1.00 27.75 ? 207  ARG A CB    1 
ATOM   1370  C  CG    . ARG A 1  209  ? -39.357 53.369  57.630  1.00 32.00 ? 207  ARG A CG    1 
ATOM   1371  C  CD    . ARG A 1  209  ? -38.176 53.892  58.365  1.00 33.50 ? 207  ARG A CD    1 
ATOM   1372  N  NE    . ARG A 1  209  ? -37.090 54.234  57.461  1.00 39.35 ? 207  ARG A NE    1 
ATOM   1373  C  CZ    . ARG A 1  209  ? -35.878 54.586  57.869  1.00 43.06 ? 207  ARG A CZ    1 
ATOM   1374  N  NH1   . ARG A 1  209  ? -35.582 54.670  59.157  1.00 37.23 ? 207  ARG A NH1   1 
ATOM   1375  N  NH2   . ARG A 1  209  ? -34.942 54.858  56.963  1.00 46.73 ? 207  ARG A NH2   1 
ATOM   1376  N  N     . SER A 1  210  ? -43.768 52.440  59.221  1.00 30.04 ? 208  SER A N     1 
ATOM   1377  C  CA    . SER A 1  210  ? -44.721 51.752  60.085  1.00 28.34 ? 208  SER A CA    1 
ATOM   1378  C  C     . SER A 1  210  ? -45.705 50.879  59.313  1.00 29.80 ? 208  SER A C     1 
ATOM   1379  O  O     . SER A 1  210  ? -46.338 50.004  59.913  1.00 26.88 ? 208  SER A O     1 
ATOM   1380  C  CB    . SER A 1  210  ? -45.486 52.775  60.927  1.00 26.40 ? 208  SER A CB    1 
ATOM   1381  O  OG    . SER A 1  210  ? -44.587 53.502  61.750  1.00 27.65 ? 208  SER A OG    1 
ATOM   1382  N  N     . LYS A 1  211  ? -45.829 51.075  57.998  1.00 30.49 ? 209  LYS A N     1 
ATOM   1383  C  CA    . LYS A 1  211  ? -46.860 50.370  57.241  1.00 29.77 ? 209  LYS A CA    1 
ATOM   1384  C  C     . LYS A 1  211  ? -46.658 48.860  57.289  1.00 30.68 ? 209  LYS A C     1 
ATOM   1385  O  O     . LYS A 1  211  ? -47.631 48.102  57.386  1.00 30.72 ? 209  LYS A O     1 
ATOM   1386  C  CB    . LYS A 1  211  ? -46.877 50.866  55.795  1.00 32.29 ? 209  LYS A CB    1 
ATOM   1387  N  N     . GLU A 1  212  ? -45.401 48.407  57.251  1.00 32.46 ? 210  GLU A N     1 
ATOM   1388  C  CA    . GLU A 1  212  ? -45.131 46.975  57.155  1.00 32.61 ? 210  GLU A CA    1 
ATOM   1389  C  C     . GLU A 1  212  ? -45.719 46.212  58.339  1.00 31.73 ? 210  GLU A C     1 
ATOM   1390  O  O     . GLU A 1  212  ? -46.445 45.227  58.154  1.00 30.99 ? 210  GLU A O     1 
ATOM   1391  C  CB    . GLU A 1  212  ? -43.628 46.730  57.048  1.00 35.03 ? 210  GLU A CB    1 
ATOM   1392  C  CG    . GLU A 1  212  ? -43.263 45.264  56.954  1.00 40.03 ? 210  GLU A CG    1 
ATOM   1393  C  CD    . GLU A 1  212  ? -41.770 45.043  56.864  1.00 47.10 ? 210  GLU A CD    1 
ATOM   1394  O  OE1   . GLU A 1  212  ? -41.020 46.041  56.886  1.00 49.47 ? 210  GLU A OE1   1 
ATOM   1395  O  OE2   . GLU A 1  212  ? -41.346 43.872  56.774  1.00 54.09 ? 210  GLU A OE2   1 
ATOM   1396  N  N     . LEU A 1  213  ? -45.434 46.665  59.563  1.00 30.77 ? 211  LEU A N     1 
ATOM   1397  C  CA    . LEU A 1  213  ? -45.926 45.960  60.741  1.00 30.24 ? 211  LEU A CA    1 
ATOM   1398  C  C     . LEU A 1  213  ? -47.384 46.278  61.048  1.00 30.43 ? 211  LEU A C     1 
ATOM   1399  O  O     . LEU A 1  213  ? -48.070 45.457  61.662  1.00 29.36 ? 211  LEU A O     1 
ATOM   1400  C  CB    . LEU A 1  213  ? -45.042 46.272  61.951  1.00 28.76 ? 211  LEU A CB    1 
ATOM   1401  C  CG    . LEU A 1  213  ? -43.648 45.632  61.866  1.00 31.49 ? 211  LEU A CG    1 
ATOM   1402  C  CD1   . LEU A 1  213  ? -42.805 45.930  63.090  1.00 29.42 ? 211  LEU A CD1   1 
ATOM   1403  C  CD2   . LEU A 1  213  ? -43.777 44.134  61.666  1.00 32.74 ? 211  LEU A CD2   1 
ATOM   1404  N  N     . GLU A 1  214  ? -47.891 47.437  60.618  1.00 28.56 ? 212  GLU A N     1 
ATOM   1405  C  CA    . GLU A 1  214  ? -49.323 47.685  60.760  1.00 30.27 ? 212  GLU A CA    1 
ATOM   1406  C  C     . GLU A 1  214  ? -50.135 46.691  59.941  1.00 31.14 ? 212  GLU A C     1 
ATOM   1407  O  O     . GLU A 1  214  ? -51.216 46.259  60.365  1.00 30.46 ? 212  GLU A O     1 
ATOM   1408  C  CB    . GLU A 1  214  ? -49.661 49.114  60.348  1.00 30.05 ? 212  GLU A CB    1 
ATOM   1409  C  CG    . GLU A 1  214  ? -49.293 50.142  61.398  1.00 25.34 ? 212  GLU A CG    1 
ATOM   1410  C  CD    . GLU A 1  214  ? -49.722 51.534  61.010  1.00 28.71 ? 212  GLU A CD    1 
ATOM   1411  O  OE1   . GLU A 1  214  ? -50.064 51.741  59.826  1.00 30.63 ? 212  GLU A OE1   1 
ATOM   1412  O  OE2   . GLU A 1  214  ? -49.714 52.424  61.888  1.00 27.98 ? 212  GLU A OE2   1 
ATOM   1413  N  N     . GLU A 1  215  ? -49.636 46.328  58.755  1.00 30.70 ? 213  GLU A N     1 
ATOM   1414  C  CA    . GLU A 1  215  ? -50.311 45.338  57.924  1.00 32.06 ? 213  GLU A CA    1 
ATOM   1415  C  C     . GLU A 1  215  ? -50.328 43.962  58.575  1.00 36.59 ? 213  GLU A C     1 
ATOM   1416  O  O     . GLU A 1  215  ? -51.148 43.117  58.195  1.00 35.52 ? 213  GLU A O     1 
ATOM   1417  C  CB    . GLU A 1  215  ? -49.641 45.257  56.551  1.00 34.79 ? 213  GLU A CB    1 
ATOM   1418  N  N     . LYS A 1  216  ? -49.451 43.723  59.550  1.00 33.16 ? 214  LYS A N     1 
ATOM   1419  C  CA    . LYS A 1  216  ? -49.402 42.466  60.283  1.00 32.70 ? 214  LYS A CA    1 
ATOM   1420  C  C     . LYS A 1  216  ? -50.242 42.485  61.555  1.00 35.51 ? 214  LYS A C     1 
ATOM   1421  O  O     . LYS A 1  216  ? -50.378 41.444  62.205  1.00 37.69 ? 214  LYS A O     1 
ATOM   1422  C  CB    . LYS A 1  216  ? -47.947 42.116  60.637  1.00 31.48 ? 214  LYS A CB    1 
ATOM   1423  N  N     . GLY A 1  217  ? -50.814 43.632  61.922  1.00 32.98 ? 215  GLY A N     1 
ATOM   1424  C  CA    . GLY A 1  217  ? -51.644 43.738  63.104  1.00 29.11 ? 215  GLY A CA    1 
ATOM   1425  C  C     . GLY A 1  217  ? -51.062 44.578  64.221  1.00 30.27 ? 215  GLY A C     1 
ATOM   1426  O  O     . GLY A 1  217  ? -51.725 44.746  65.250  1.00 29.60 ? 215  GLY A O     1 
ATOM   1427  N  N     . PHE A 1  218  ? -49.855 45.111  64.065  1.00 28.28 ? 216  PHE A N     1 
ATOM   1428  C  CA    . PHE A 1  218  ? -49.326 46.038  65.055  1.00 24.88 ? 216  PHE A CA    1 
ATOM   1429  C  C     . PHE A 1  218  ? -49.930 47.423  64.860  1.00 25.73 ? 216  PHE A C     1 
ATOM   1430  O  O     . PHE A 1  218  ? -50.456 47.759  63.797  1.00 24.64 ? 216  PHE A O     1 
ATOM   1431  C  CB    . PHE A 1  218  ? -47.800 46.158  64.954  1.00 24.58 ? 216  PHE A CB    1 
ATOM   1432  C  CG    . PHE A 1  218  ? -47.043 44.929  65.388  1.00 27.50 ? 216  PHE A CG    1 
ATOM   1433  C  CD1   . PHE A 1  218  ? -46.906 43.842  64.538  1.00 28.73 ? 216  PHE A CD1   1 
ATOM   1434  C  CD2   . PHE A 1  218  ? -46.423 44.885  66.628  1.00 26.67 ? 216  PHE A CD2   1 
ATOM   1435  C  CE1   . PHE A 1  218  ? -46.199 42.725  64.930  1.00 28.40 ? 216  PHE A CE1   1 
ATOM   1436  C  CE2   . PHE A 1  218  ? -45.703 43.766  67.019  1.00 27.96 ? 216  PHE A CE2   1 
ATOM   1437  C  CZ    . PHE A 1  218  ? -45.594 42.691  66.172  1.00 24.37 ? 216  PHE A CZ    1 
ATOM   1438  N  N     . SER A 1  219  ? -49.817 48.243  65.899  1.00 21.39 ? 217  SER A N     1 
ATOM   1439  C  CA    . SER A 1  219  ? -50.119 49.665  65.826  1.00 21.83 ? 217  SER A CA    1 
ATOM   1440  C  C     . SER A 1  219  ? -48.922 50.434  66.365  1.00 20.67 ? 217  SER A C     1 
ATOM   1441  O  O     . SER A 1  219  ? -47.939 49.841  66.825  1.00 19.94 ? 217  SER A O     1 
ATOM   1442  C  CB    . SER A 1  219  ? -51.383 50.010  66.618  1.00 21.98 ? 217  SER A CB    1 
ATOM   1443  O  OG    . SER A 1  219  ? -51.222 49.631  67.969  1.00 23.81 ? 217  SER A OG    1 
ATOM   1444  N  N     . TYR A 1  220  ? -49.016 51.770  66.338  1.00 19.54 ? 218  TYR A N     1 
ATOM   1445  C  CA    . TYR A 1  220  ? -47.897 52.634  66.698  1.00 20.39 ? 218  TYR A CA    1 
ATOM   1446  C  C     . TYR A 1  220  ? -48.319 53.765  67.629  1.00 20.54 ? 218  TYR A C     1 
ATOM   1447  O  O     . TYR A 1  220  ? -49.452 54.250  67.582  1.00 19.71 ? 218  TYR A O     1 
ATOM   1448  C  CB    . TYR A 1  220  ? -47.238 53.225  65.433  1.00 20.74 ? 218  TYR A CB    1 
ATOM   1449  C  CG    . TYR A 1  220  ? -46.295 52.246  64.778  1.00 21.17 ? 218  TYR A CG    1 
ATOM   1450  C  CD1   . TYR A 1  220  ? -46.771 51.272  63.906  1.00 23.61 ? 218  TYR A CD1   1 
ATOM   1451  C  CD2   . TYR A 1  220  ? -44.929 52.284  65.047  1.00 22.36 ? 218  TYR A CD2   1 
ATOM   1452  C  CE1   . TYR A 1  220  ? -45.906 50.361  63.311  1.00 24.21 ? 218  TYR A CE1   1 
ATOM   1453  C  CE2   . TYR A 1  220  ? -44.065 51.393  64.461  1.00 23.87 ? 218  TYR A CE2   1 
ATOM   1454  C  CZ    . TYR A 1  220  ? -44.553 50.434  63.597  1.00 25.22 ? 218  TYR A CZ    1 
ATOM   1455  O  OH    . TYR A 1  220  ? -43.672 49.541  63.026  1.00 24.88 ? 218  TYR A OH    1 
ATOM   1456  N  N     . SER A 1  221  ? -47.381 54.171  68.488  1.00 19.21 ? 219  SER A N     1 
ATOM   1457  C  CA    . SER A 1  221  ? -47.457 55.427  69.228  1.00 18.61 ? 219  SER A CA    1 
ATOM   1458  C  C     . SER A 1  221  ? -46.120 56.129  69.050  1.00 18.84 ? 219  SER A C     1 
ATOM   1459  O  O     . SER A 1  221  ? -45.079 55.567  69.400  1.00 21.32 ? 219  SER A O     1 
ATOM   1460  C  CB    . SER A 1  221  ? -47.748 55.204  70.713  1.00 20.02 ? 219  SER A CB    1 
ATOM   1461  O  OG    . SER A 1  221  ? -47.909 56.454  71.383  1.00 20.06 ? 219  SER A OG    1 
ATOM   1462  N  N     . TYR A 1  222  ? -46.139 57.350  68.535  1.00 15.53 ? 220  TYR A N     1 
ATOM   1463  C  CA    . TYR A 1  222  ? -44.898 58.028  68.167  1.00 18.28 ? 220  TYR A CA    1 
ATOM   1464  C  C     . TYR A 1  222  ? -44.429 58.961  69.271  1.00 17.80 ? 220  TYR A C     1 
ATOM   1465  O  O     . TYR A 1  222  ? -45.224 59.699  69.857  1.00 19.03 ? 220  TYR A O     1 
ATOM   1466  C  CB    . TYR A 1  222  ? -45.070 58.801  66.860  1.00 18.18 ? 220  TYR A CB    1 
ATOM   1467  C  CG    . TYR A 1  222  ? -45.398 57.872  65.745  1.00 17.19 ? 220  TYR A CG    1 
ATOM   1468  C  CD1   . TYR A 1  222  ? -44.394 57.188  65.074  1.00 18.58 ? 220  TYR A CD1   1 
ATOM   1469  C  CD2   . TYR A 1  222  ? -46.712 57.625  65.393  1.00 18.51 ? 220  TYR A CD2   1 
ATOM   1470  C  CE1   . TYR A 1  222  ? -44.697 56.303  64.067  1.00 18.95 ? 220  TYR A CE1   1 
ATOM   1471  C  CE2   . TYR A 1  222  ? -47.018 56.745  64.377  1.00 20.07 ? 220  TYR A CE2   1 
ATOM   1472  C  CZ    . TYR A 1  222  ? -46.007 56.090  63.725  1.00 19.62 ? 220  TYR A CZ    1 
ATOM   1473  O  OH    . TYR A 1  222  ? -46.306 55.213  62.726  1.00 22.23 ? 220  TYR A OH    1 
ATOM   1474  N  N     . ASP A 1  223  ? -43.118 58.932  69.519  1.00 18.66 ? 221  ASP A N     1 
ATOM   1475  C  CA    . ASP A 1  223  ? -42.436 59.713  70.547  1.00 20.30 ? 221  ASP A CA    1 
ATOM   1476  C  C     . ASP A 1  223  ? -41.457 60.646  69.844  1.00 21.59 ? 221  ASP A C     1 
ATOM   1477  O  O     . ASP A 1  223  ? -40.434 60.193  69.312  1.00 23.19 ? 221  ASP A O     1 
ATOM   1478  C  CB    . ASP A 1  223  ? -41.706 58.775  71.507  1.00 20.92 ? 221  ASP A CB    1 
ATOM   1479  C  CG    . ASP A 1  223  ? -40.759 59.499  72.471  1.00 26.74 ? 221  ASP A CG    1 
ATOM   1480  O  OD1   . ASP A 1  223  ? -40.889 60.723  72.680  1.00 28.47 ? 221  ASP A OD1   1 
ATOM   1481  O  OD2   . ASP A 1  223  ? -39.876 58.810  73.033  1.00 30.93 ? 221  ASP A OD2   1 
ATOM   1482  N  N     . MET A 1  224  ? -41.776 61.934  69.816  1.00 23.10 ? 222  MET A N     1 
ATOM   1483  C  CA    . MET A 1  224  ? -40.856 62.926  69.266  1.00 22.41 ? 222  MET A CA    1 
ATOM   1484  C  C     . MET A 1  224  ? -39.737 63.118  70.286  1.00 25.13 ? 222  MET A C     1 
ATOM   1485  O  O     . MET A 1  224  ? -39.904 63.812  71.290  1.00 29.18 ? 222  MET A O     1 
ATOM   1486  C  CB    . MET A 1  224  ? -41.587 64.223  68.951  1.00 23.77 ? 222  MET A CB    1 
ATOM   1487  C  CG    . MET A 1  224  ? -42.789 64.028  68.022  1.00 26.88 ? 222  MET A CG    1 
ATOM   1488  S  SD    . MET A 1  224  ? -42.371 63.197  66.467  1.00 27.85 ? 222  MET A SD    1 
ATOM   1489  C  CE    . MET A 1  224  ? -41.476 64.501  65.638  1.00 30.21 ? 222  MET A CE    1 
ATOM   1490  N  N     . LEU A 1  225  ? -38.602 62.471  70.037  1.00 26.08 ? 223  LEU A N     1 
ATOM   1491  C  CA    . LEU A 1  225  ? -37.500 62.470  70.995  1.00 28.02 ? 223  LEU A CA    1 
ATOM   1492  C  C     . LEU A 1  225  ? -37.015 63.884  71.289  1.00 31.03 ? 223  LEU A C     1 
ATOM   1493  O  O     . LEU A 1  225  ? -36.921 64.725  70.392  1.00 33.04 ? 223  LEU A O     1 
ATOM   1494  C  CB    . LEU A 1  225  ? -36.335 61.649  70.451  1.00 29.07 ? 223  LEU A CB    1 
ATOM   1495  C  CG    . LEU A 1  225  ? -36.468 60.131  70.433  1.00 30.22 ? 223  LEU A CG    1 
ATOM   1496  C  CD1   . LEU A 1  225  ? -35.242 59.542  69.746  1.00 32.22 ? 223  LEU A CD1   1 
ATOM   1497  C  CD2   . LEU A 1  225  ? -36.633 59.580  71.854  1.00 27.59 ? 223  LEU A CD2   1 
ATOM   1498  N  N     . GLY A 1  226  ? -36.683 64.134  72.550  1.00 32.62 ? 224  GLY A N     1 
ATOM   1499  C  CA    . GLY A 1  226  ? -36.060 65.397  72.910  1.00 35.46 ? 224  GLY A CA    1 
ATOM   1500  C  C     . GLY A 1  226  ? -35.727 65.410  74.384  1.00 35.88 ? 224  GLY A C     1 
ATOM   1501  O  O     . GLY A 1  226  ? -36.070 64.489  75.133  1.00 38.03 ? 224  GLY A O     1 
ATOM   1502  N  N     . GLU A 1  227  ? -35.045 66.477  74.791  1.00 36.68 ? 225  GLU A N     1 
ATOM   1503  C  CA    . GLU A 1  227  ? -34.777 66.700  76.204  1.00 38.94 ? 225  GLU A CA    1 
ATOM   1504  C  C     . GLU A 1  227  ? -35.958 67.402  76.873  1.00 31.29 ? 225  GLU A C     1 
ATOM   1505  O  O     . GLU A 1  227  ? -36.827 67.970  76.212  1.00 33.12 ? 225  GLU A O     1 
ATOM   1506  C  CB    . GLU A 1  227  ? -33.511 67.540  76.386  1.00 36.04 ? 225  GLU A CB    1 
ATOM   1507  C  CG    . GLU A 1  227  ? -32.226 66.793  76.077  1.00 41.65 ? 225  GLU A CG    1 
ATOM   1508  C  CD    . GLU A 1  227  ? -32.005 65.625  77.014  1.00 48.50 ? 225  GLU A CD    1 
ATOM   1509  O  OE1   . GLU A 1  227  ? -32.086 65.822  78.246  1.00 47.43 ? 225  GLU A OE1   1 
ATOM   1510  O  OE2   . GLU A 1  227  ? -31.767 64.507  76.517  1.00 61.95 ? 225  GLU A OE2   1 
ATOM   1511  N  N     . ALA A 1  228  ? -35.979 67.360  78.203  1.00 29.21 ? 226  ALA A N     1 
ATOM   1512  C  CA    . ALA A 1  228  ? -36.934 68.163  78.955  1.00 29.40 ? 226  ALA A CA    1 
ATOM   1513  C  C     . ALA A 1  228  ? -36.611 69.636  78.762  1.00 25.78 ? 226  ALA A C     1 
ATOM   1514  O  O     . ALA A 1  228  ? -35.456 70.018  78.584  1.00 26.01 ? 226  ALA A O     1 
ATOM   1515  C  CB    . ALA A 1  228  ? -36.896 67.817  80.441  1.00 23.09 ? 226  ALA A CB    1 
ATOM   1516  N  N     . ALA A 1  229  ? -37.642 70.469  78.778  1.00 20.34 ? 227  ALA A N     1 
ATOM   1517  C  CA    . ALA A 1  229  ? -37.440 71.861  78.403  1.00 19.36 ? 227  ALA A CA    1 
ATOM   1518  C  C     . ALA A 1  229  ? -36.696 72.606  79.507  1.00 20.62 ? 227  ALA A C     1 
ATOM   1519  O  O     . ALA A 1  229  ? -37.018 72.480  80.692  1.00 19.22 ? 227  ALA A O     1 
ATOM   1520  C  CB    . ALA A 1  229  ? -38.776 72.533  78.107  1.00 21.28 ? 227  ALA A CB    1 
ATOM   1521  N  N     . THR A 1  230  ? -35.685 73.372  79.108  1.00 19.22 ? 228  THR A N     1 
ATOM   1522  C  CA    . THR A 1  230  ? -34.957 74.246  80.014  1.00 19.66 ? 228  THR A CA    1 
ATOM   1523  C  C     . THR A 1  230  ? -35.379 75.696  79.869  1.00 17.58 ? 228  THR A C     1 
ATOM   1524  O  O     . THR A 1  230  ? -35.210 76.479  80.805  1.00 17.34 ? 228  THR A O     1 
ATOM   1525  C  CB    . THR A 1  230  ? -33.445 74.104  79.750  1.00 23.41 ? 228  THR A CB    1 
ATOM   1526  O  OG1   . THR A 1  230  ? -33.066 72.724  79.910  1.00 28.52 ? 228  THR A OG1   1 
ATOM   1527  C  CG2   . THR A 1  230  ? -32.632 74.945  80.693  1.00 29.26 ? 228  THR A CG2   1 
ATOM   1528  N  N     . THR A 1  231  ? -35.951 76.066  78.726  1.00 19.54 ? 229  THR A N     1 
ATOM   1529  C  CA    . THR A 1  231  ? -36.317 77.442  78.461  1.00 15.99 ? 229  THR A CA    1 
ATOM   1530  C  C     . THR A 1  231  ? -37.716 77.470  77.879  1.00 16.40 ? 229  THR A C     1 
ATOM   1531  O  O     . THR A 1  231  ? -38.229 76.450  77.417  1.00 17.49 ? 229  THR A O     1 
ATOM   1532  C  CB    . THR A 1  231  ? -35.359 78.105  77.473  1.00 19.29 ? 229  THR A CB    1 
ATOM   1533  O  OG1   . THR A 1  231  ? -35.550 77.515  76.183  1.00 20.01 ? 229  THR A OG1   1 
ATOM   1534  C  CG2   . THR A 1  231  ? -33.892 77.890  77.909  1.00 18.49 ? 229  THR A CG2   1 
ATOM   1535  N  N     . ALA A 1  232  ? -38.324 78.652  77.932  1.00 17.42 ? 230  ALA A N     1 
ATOM   1536  C  CA    . ALA A 1  232  ? -39.598 78.867  77.253  1.00 18.38 ? 230  ALA A CA    1 
ATOM   1537  C  C     . ALA A 1  232  ? -39.488 78.556  75.765  1.00 20.70 ? 230  ALA A C     1 
ATOM   1538  O  O     . ALA A 1  232  ? -40.372 77.908  75.187  1.00 20.92 ? 230  ALA A O     1 
ATOM   1539  C  CB    . ALA A 1  232  ? -40.056 80.308  77.467  1.00 22.21 ? 230  ALA A CB    1 
ATOM   1540  N  N     . ALA A 1  233  ? -38.412 79.011  75.123  1.00 21.99 ? 231  ALA A N     1 
ATOM   1541  C  CA    . ALA A 1  233  ? -38.275 78.798  73.686  1.00 20.93 ? 231  ALA A CA    1 
ATOM   1542  C  C     . ALA A 1  233  ? -38.190 77.317  73.357  1.00 21.69 ? 231  ALA A C     1 
ATOM   1543  O  O     . ALA A 1  233  ? -38.757 76.862  72.361  1.00 22.48 ? 231  ALA A O     1 
ATOM   1544  C  CB    . ALA A 1  233  ? -37.047 79.539  73.153  1.00 25.43 ? 231  ALA A CB    1 
ATOM   1545  N  N     . ASP A 1  234  ? -37.514 76.537  74.198  1.00 19.03 ? 232  ASP A N     1 
ATOM   1546  C  CA    . ASP A 1  234  ? -37.402 75.117  73.912  1.00 20.35 ? 232  ASP A CA    1 
ATOM   1547  C  C     . ASP A 1  234  ? -38.724 74.404  74.169  1.00 20.99 ? 232  ASP A C     1 
ATOM   1548  O  O     . ASP A 1  234  ? -39.079 73.466  73.447  1.00 20.73 ? 232  ASP A O     1 
ATOM   1549  C  CB    . ASP A 1  234  ? -36.270 74.503  74.732  1.00 26.33 ? 232  ASP A CB    1 
ATOM   1550  C  CG    . ASP A 1  234  ? -34.893 74.936  74.237  1.00 27.61 ? 232  ASP A CG    1 
ATOM   1551  O  OD1   . ASP A 1  234  ? -34.808 75.552  73.150  1.00 30.65 ? 232  ASP A OD1   1 
ATOM   1552  O  OD2   . ASP A 1  234  ? -33.900 74.685  74.943  1.00 32.76 ? 232  ASP A OD2   1 
ATOM   1553  N  N     . ALA A 1  235  ? -39.477 74.837  75.183  1.00 18.75 ? 233  ALA A N     1 
ATOM   1554  C  CA    . ALA A 1  235  ? -40.800 74.258  75.387  1.00 17.20 ? 233  ALA A CA    1 
ATOM   1555  C  C     . ALA A 1  235  ? -41.708 74.567  74.207  1.00 18.89 ? 233  ALA A C     1 
ATOM   1556  O  O     . ALA A 1  235  ? -42.503 73.718  73.778  1.00 19.62 ? 233  ALA A O     1 
ATOM   1557  C  CB    . ALA A 1  235  ? -41.417 74.778  76.683  1.00 18.02 ? 233  ALA A CB    1 
ATOM   1558  N  N     . GLU A 1  236  ? -41.612 75.788  73.677  1.00 19.33 ? 234  GLU A N     1 
ATOM   1559  C  CA    . GLU A 1  236  ? -42.414 76.136  72.511  1.00 19.95 ? 234  GLU A CA    1 
ATOM   1560  C  C     . GLU A 1  236  ? -41.992 75.326  71.291  1.00 19.82 ? 234  GLU A C     1 
ATOM   1561  O  O     . GLU A 1  236  ? -42.840 74.938  70.479  1.00 20.88 ? 234  GLU A O     1 
ATOM   1562  C  CB    . GLU A 1  236  ? -42.318 77.644  72.245  1.00 22.75 ? 234  GLU A CB    1 
ATOM   1563  N  N     . ARG A 1  237  ? -40.692 75.057  71.142  1.00 19.88 ? 235  ARG A N     1 
ATOM   1564  C  CA    . ARG A 1  237  ? -40.233 74.195  70.055  1.00 22.25 ? 235  ARG A CA    1 
ATOM   1565  C  C     . ARG A 1  237  ? -40.798 72.785  70.192  1.00 22.03 ? 235  ARG A C     1 
ATOM   1566  O  O     . ARG A 1  237  ? -41.247 72.186  69.208  1.00 21.70 ? 235  ARG A O     1 
ATOM   1567  C  CB    . ARG A 1  237  ? -38.701 74.148  70.010  1.00 23.53 ? 235  ARG A CB    1 
ATOM   1568  C  CG    . ARG A 1  237  ? -38.169 73.207  68.927  1.00 29.15 ? 235  ARG A CG    1 
ATOM   1569  C  CD    . ARG A 1  237  ? -36.662 73.384  68.671  1.00 35.98 ? 235  ARG A CD    1 
ATOM   1570  N  NE    . ARG A 1  237  ? -35.852 72.642  69.630  1.00 37.77 ? 235  ARG A NE    1 
ATOM   1571  C  CZ    . ARG A 1  237  ? -35.257 73.186  70.682  1.00 38.68 ? 235  ARG A CZ    1 
ATOM   1572  N  NH1   . ARG A 1  237  ? -35.329 74.487  70.920  1.00 39.18 ? 235  ARG A NH1   1 
ATOM   1573  N  NH2   . ARG A 1  237  ? -34.571 72.407  71.513  1.00 36.19 ? 235  ARG A NH2   1 
ATOM   1574  N  N     . TYR A 1  238  ? -40.762 72.219  71.401  1.00 18.10 ? 236  TYR A N     1 
ATOM   1575  C  CA    . TYR A 1  238  ? -41.331 70.889  71.574  1.00 18.35 ? 236  TYR A CA    1 
ATOM   1576  C  C     . TYR A 1  238  ? -42.824 70.912  71.294  1.00 17.97 ? 236  TYR A C     1 
ATOM   1577  O  O     . TYR A 1  238  ? -43.369 69.971  70.708  1.00 20.16 ? 236  TYR A O     1 
ATOM   1578  C  CB    . TYR A 1  238  ? -41.047 70.355  72.983  1.00 19.67 ? 236  TYR A CB    1 
ATOM   1579  C  CG    . TYR A 1  238  ? -39.589 69.993  73.181  1.00 22.55 ? 236  TYR A CG    1 
ATOM   1580  C  CD1   . TYR A 1  238  ? -38.931 69.177  72.272  1.00 30.29 ? 236  TYR A CD1   1 
ATOM   1581  C  CD2   . TYR A 1  238  ? -38.869 70.495  74.251  1.00 22.38 ? 236  TYR A CD2   1 
ATOM   1582  C  CE1   . TYR A 1  238  ? -37.590 68.854  72.437  1.00 34.84 ? 236  TYR A CE1   1 
ATOM   1583  C  CE2   . TYR A 1  238  ? -37.533 70.195  74.422  1.00 30.36 ? 236  TYR A CE2   1 
ATOM   1584  C  CZ    . TYR A 1  238  ? -36.896 69.365  73.516  1.00 36.51 ? 236  TYR A CZ    1 
ATOM   1585  O  OH    . TYR A 1  238  ? -35.563 69.049  73.686  1.00 42.82 ? 236  TYR A OH    1 
ATOM   1586  N  N     . TYR A 1  239  ? -43.500 71.992  71.680  1.00 15.99 ? 237  TYR A N     1 
ATOM   1587  C  CA    . TYR A 1  239  ? -44.918 72.086  71.374  1.00 15.65 ? 237  TYR A CA    1 
ATOM   1588  C  C     . TYR A 1  239  ? -45.150 72.014  69.872  1.00 18.33 ? 237  TYR A C     1 
ATOM   1589  O  O     . TYR A 1  239  ? -46.002 71.250  69.408  1.00 15.81 ? 237  TYR A O     1 
ATOM   1590  C  CB    . TYR A 1  239  ? -45.522 73.365  71.938  1.00 18.31 ? 237  TYR A CB    1 
ATOM   1591  C  CG    . TYR A 1  239  ? -46.980 73.459  71.571  1.00 19.63 ? 237  TYR A CG    1 
ATOM   1592  C  CD1   . TYR A 1  239  ? -47.376 73.956  70.332  1.00 19.92 ? 237  TYR A CD1   1 
ATOM   1593  C  CD2   . TYR A 1  239  ? -47.961 73.009  72.443  1.00 19.62 ? 237  TYR A CD2   1 
ATOM   1594  C  CE1   . TYR A 1  239  ? -48.696 74.017  69.985  1.00 22.36 ? 237  TYR A CE1   1 
ATOM   1595  C  CE2   . TYR A 1  239  ? -49.290 73.082  72.104  1.00 20.60 ? 237  TYR A CE2   1 
ATOM   1596  C  CZ    . TYR A 1  239  ? -49.649 73.577  70.879  1.00 20.73 ? 237  TYR A CZ    1 
ATOM   1597  O  OH    . TYR A 1  239  ? -50.972 73.647  70.513  1.00 24.04 ? 237  TYR A OH    1 
ATOM   1598  N  N     . ARG A 1  240  ? -44.432 72.832  69.087  1.00 16.97 ? 238  ARG A N     1 
ATOM   1599  C  CA    A ARG A 1  240  ? -44.695 72.822  67.653  0.53 18.09 ? 238  ARG A CA    1 
ATOM   1600  C  CA    B ARG A 1  240  ? -44.690 72.823  67.651  0.47 18.10 ? 238  ARG A CA    1 
ATOM   1601  C  C     . ARG A 1  240  ? -44.285 71.497  67.023  1.00 17.69 ? 238  ARG A C     1 
ATOM   1602  O  O     . ARG A 1  240  ? -44.907 71.063  66.049  1.00 16.92 ? 238  ARG A O     1 
ATOM   1603  C  CB    A ARG A 1  240  ? -44.014 74.009  66.959  0.53 20.29 ? 238  ARG A CB    1 
ATOM   1604  C  CB    B ARG A 1  240  ? -44.001 74.009  66.961  0.47 20.29 ? 238  ARG A CB    1 
ATOM   1605  C  CG    A ARG A 1  240  ? -42.503 74.023  66.995  0.53 21.96 ? 238  ARG A CG    1 
ATOM   1606  C  CG    B ARG A 1  240  ? -42.481 74.003  66.924  0.47 21.96 ? 238  ARG A CG    1 
ATOM   1607  C  CD    A ARG A 1  240  ? -41.957 75.135  66.097  0.53 21.96 ? 238  ARG A CD    1 
ATOM   1608  C  CD    B ARG A 1  240  ? -41.985 75.317  66.307  0.47 21.97 ? 238  ARG A CD    1 
ATOM   1609  N  NE    A ARG A 1  240  ? -40.523 75.327  66.268  0.53 19.30 ? 238  ARG A NE    1 
ATOM   1610  N  NE    B ARG A 1  240  ? -42.752 76.431  66.853  0.47 21.42 ? 238  ARG A NE    1 
ATOM   1611  C  CZ    A ARG A 1  240  ? -39.974 76.189  67.117  0.53 21.03 ? 238  ARG A CZ    1 
ATOM   1612  C  CZ    B ARG A 1  240  ? -42.299 77.305  67.741  0.47 20.72 ? 238  ARG A CZ    1 
ATOM   1613  N  NH1   A ARG A 1  240  ? -40.713 76.981  67.879  0.53 22.13 ? 238  ARG A NH1   1 
ATOM   1614  N  NH1   B ARG A 1  240  ? -41.016 77.365  68.067  0.47 21.76 ? 238  ARG A NH1   1 
ATOM   1615  N  NH2   A ARG A 1  240  ? -38.651 76.272  67.193  0.53 22.90 ? 238  ARG A NH2   1 
ATOM   1616  N  NH2   B ARG A 1  240  ? -43.158 78.134  68.322  0.47 19.53 ? 238  ARG A NH2   1 
ATOM   1617  N  N     . ASP A 1  241  ? -43.280 70.818  67.582  1.00 17.70 ? 239  ASP A N     1 
ATOM   1618  C  CA    . ASP A 1  241  ? -42.928 69.486  67.091  1.00 18.03 ? 239  ASP A CA    1 
ATOM   1619  C  C     . ASP A 1  241  ? -44.070 68.498  67.318  1.00 18.77 ? 239  ASP A C     1 
ATOM   1620  O  O     . ASP A 1  241  ? -44.406 67.714  66.430  1.00 18.64 ? 239  ASP A O     1 
ATOM   1621  C  CB    . ASP A 1  241  ? -41.658 68.976  67.772  1.00 20.92 ? 239  ASP A CB    1 
ATOM   1622  C  CG    . ASP A 1  241  ? -40.417 69.745  67.362  1.00 26.21 ? 239  ASP A CG    1 
ATOM   1623  O  OD1   . ASP A 1  241  ? -40.453 70.448  66.330  1.00 28.22 ? 239  ASP A OD1   1 
ATOM   1624  O  OD2   . ASP A 1  241  ? -39.404 69.645  68.091  1.00 31.85 ? 239  ASP A OD2   1 
ATOM   1625  N  N     . TYR A 1  242  ? -44.656 68.499  68.523  1.00 17.43 ? 240  TYR A N     1 
ATOM   1626  C  CA    . TYR A 1  242  ? -45.794 67.621  68.798  1.00 15.84 ? 240  TYR A CA    1 
ATOM   1627  C  C     . TYR A 1  242  ? -46.983 67.959  67.908  1.00 15.35 ? 240  TYR A C     1 
ATOM   1628  O  O     . TYR A 1  242  ? -47.668 67.065  67.398  1.00 16.67 ? 240  TYR A O     1 
ATOM   1629  C  CB    . TYR A 1  242  ? -46.218 67.740  70.262  1.00 16.21 ? 240  TYR A CB    1 
ATOM   1630  C  CG    . TYR A 1  242  ? -45.345 67.012  71.269  1.00 15.24 ? 240  TYR A CG    1 
ATOM   1631  C  CD1   . TYR A 1  242  ? -44.772 65.780  70.977  1.00 18.86 ? 240  TYR A CD1   1 
ATOM   1632  C  CD2   . TYR A 1  242  ? -45.141 67.547  72.534  1.00 20.46 ? 240  TYR A CD2   1 
ATOM   1633  C  CE1   . TYR A 1  242  ? -43.976 65.110  71.934  1.00 20.97 ? 240  TYR A CE1   1 
ATOM   1634  C  CE2   . TYR A 1  242  ? -44.352 66.897  73.480  1.00 17.27 ? 240  TYR A CE2   1 
ATOM   1635  C  CZ    . TYR A 1  242  ? -43.782 65.683  73.173  1.00 18.12 ? 240  TYR A CZ    1 
ATOM   1636  O  OH    . TYR A 1  242  ? -43.003 65.045  74.133  1.00 18.75 ? 240  TYR A OH    1 
ATOM   1637  N  N     . GLU A 1  243  ? -47.284 69.247  67.779  1.00 15.61 ? 241  GLU A N     1 
ATOM   1638  C  CA    . GLU A 1  243  ? -48.410 69.659  66.955  1.00 15.93 ? 241  GLU A CA    1 
ATOM   1639  C  C     . GLU A 1  243  ? -48.223 69.202  65.516  1.00 17.33 ? 241  GLU A C     1 
ATOM   1640  O  O     . GLU A 1  243  ? -49.139 68.636  64.911  1.00 16.80 ? 241  GLU A O     1 
ATOM   1641  C  CB    . GLU A 1  243  ? -48.566 71.172  67.044  1.00 16.98 ? 241  GLU A CB    1 
ATOM   1642  C  CG    . GLU A 1  243  ? -49.638 71.743  66.149  1.00 20.01 ? 241  GLU A CG    1 
ATOM   1643  C  CD    . GLU A 1  243  ? -49.511 73.256  66.032  1.00 23.44 ? 241  GLU A CD    1 
ATOM   1644  O  OE1   . GLU A 1  243  ? -48.364 73.785  66.047  1.00 30.14 ? 241  GLU A OE1   1 
ATOM   1645  O  OE2   . GLU A 1  243  ? -50.552 73.901  65.924  1.00 21.92 ? 241  GLU A OE2   1 
ATOM   1646  N  N     . SER A 1  244  ? -47.016 69.398  64.963  1.00 16.94 ? 242  SER A N     1 
ATOM   1647  C  CA    . SER A 1  244  ? -46.797 68.957  63.591  1.00 17.03 ? 242  SER A CA    1 
ATOM   1648  C  C     . SER A 1  244  ? -46.851 67.434  63.479  1.00 18.09 ? 242  SER A C     1 
ATOM   1649  O  O     . SER A 1  244  ? -47.346 66.909  62.476  1.00 18.45 ? 242  SER A O     1 
ATOM   1650  C  CB    . SER A 1  244  ? -45.472 69.520  63.050  1.00 17.27 ? 242  SER A CB    1 
ATOM   1651  O  OG    . SER A 1  244  ? -44.359 68.932  63.682  1.00 23.22 ? 242  SER A OG    1 
ATOM   1652  N  N     . ALA A 1  245  ? -46.387 66.708  64.500  1.00 16.98 ? 243  ALA A N     1 
ATOM   1653  C  CA    . ALA A 1  245  ? -46.496 65.253  64.466  1.00 15.78 ? 243  ALA A CA    1 
ATOM   1654  C  C     . ALA A 1  245  ? -47.956 64.794  64.534  1.00 17.48 ? 243  ALA A C     1 
ATOM   1655  O  O     . ALA A 1  245  ? -48.350 63.851  63.837  1.00 17.70 ? 243  ALA A O     1 
ATOM   1656  C  CB    . ALA A 1  245  ? -45.684 64.643  65.610  1.00 16.97 ? 243  ALA A CB    1 
ATOM   1657  N  N     . ILE A 1  246  ? -48.774 65.430  65.374  1.00 16.54 ? 244  ILE A N     1 
ATOM   1658  C  CA    . ILE A 1  246  ? -50.186 65.053  65.434  1.00 15.52 ? 244  ILE A CA    1 
ATOM   1659  C  C     . ILE A 1  246  ? -50.836 65.188  64.064  1.00 18.15 ? 244  ILE A C     1 
ATOM   1660  O  O     . ILE A 1  246  ? -51.573 64.300  63.627  1.00 18.12 ? 244  ILE A O     1 
ATOM   1661  C  CB    . ILE A 1  246  ? -50.921 65.884  66.494  1.00 16.29 ? 244  ILE A CB    1 
ATOM   1662  C  CG1   . ILE A 1  246  ? -50.460 65.471  67.893  1.00 17.48 ? 244  ILE A CG1   1 
ATOM   1663  C  CG2   . ILE A 1  246  ? -52.437 65.682  66.354  1.00 18.24 ? 244  ILE A CG2   1 
ATOM   1664  C  CD1   . ILE A 1  246  ? -50.938 66.416  68.977  1.00 18.72 ? 244  ILE A CD1   1 
ATOM   1665  N  N     . HIS A 1  247  ? -50.551 66.283  63.348  1.00 16.17 ? 245  HIS A N     1 
ATOM   1666  C  CA    . HIS A 1  247  ? -51.107 66.431  62.004  1.00 17.28 ? 245  HIS A CA    1 
ATOM   1667  C  C     . HIS A 1  247  ? -50.668 65.287  61.096  1.00 18.41 ? 245  HIS A C     1 
ATOM   1668  O  O     . HIS A 1  247  ? -51.487 64.690  60.392  1.00 18.94 ? 245  HIS A O     1 
ATOM   1669  C  CB    . HIS A 1  247  ? -50.695 67.770  61.390  1.00 18.23 ? 245  HIS A CB    1 
ATOM   1670  C  CG    . HIS A 1  247  ? -51.424 68.953  61.950  1.00 20.02 ? 245  HIS A CG    1 
ATOM   1671  N  ND1   . HIS A 1  247  ? -52.781 69.141  61.804  1.00 19.12 ? 245  HIS A ND1   1 
ATOM   1672  C  CD2   . HIS A 1  247  ? -50.968 70.031  62.633  1.00 20.53 ? 245  HIS A CD2   1 
ATOM   1673  C  CE1   . HIS A 1  247  ? -53.132 70.279  62.379  1.00 21.13 ? 245  HIS A CE1   1 
ATOM   1674  N  NE2   . HIS A 1  247  ? -52.049 70.833  62.895  1.00 19.85 ? 245  HIS A NE2   1 
ATOM   1675  N  N     . ALA A 1  248  ? -49.374 64.975  61.083  1.00 17.84 ? 246  ALA A N     1 
ATOM   1676  C  CA    . ALA A 1  248  ? -48.910 63.916  60.195  1.00 17.69 ? 246  ALA A CA    1 
ATOM   1677  C  C     . ALA A 1  248  ? -49.491 62.565  60.594  1.00 19.60 ? 246  ALA A C     1 
ATOM   1678  O  O     . ALA A 1  248  ? -49.914 61.790  59.730  1.00 18.18 ? 246  ALA A O     1 
ATOM   1679  C  CB    . ALA A 1  248  ? -47.378 63.877  60.170  1.00 19.11 ? 246  ALA A CB    1 
ATOM   1680  N  N     . ILE A 1  249  ? -49.561 62.284  61.900  1.00 18.29 ? 247  ILE A N     1 
ATOM   1681  C  CA    . ILE A 1  249  ? -50.120 61.013  62.360  1.00 17.29 ? 247  ILE A CA    1 
ATOM   1682  C  C     . ILE A 1  249  ? -51.616 60.946  62.073  1.00 17.81 ? 247  ILE A C     1 
ATOM   1683  O  O     . ILE A 1  249  ? -52.138 59.911  61.637  1.00 18.50 ? 247  ILE A O     1 
ATOM   1684  C  CB    . ILE A 1  249  ? -49.826 60.819  63.858  1.00 17.74 ? 247  ILE A CB    1 
ATOM   1685  C  CG1   . ILE A 1  249  ? -48.323 60.671  64.099  1.00 16.76 ? 247  ILE A CG1   1 
ATOM   1686  C  CG2   . ILE A 1  249  ? -50.617 59.627  64.414  1.00 18.31 ? 247  ILE A CG2   1 
ATOM   1687  C  CD1   . ILE A 1  249  ? -47.912 60.954  65.548  1.00 16.57 ? 247  ILE A CD1   1 
ATOM   1688  N  N     . GLY A 1  250  ? -52.332 62.037  62.339  1.00 17.63 ? 248  GLY A N     1 
ATOM   1689  C  CA    . GLY A 1  250  ? -53.759 62.055  62.079  1.00 18.19 ? 248  GLY A CA    1 
ATOM   1690  C  C     . GLY A 1  250  ? -54.087 61.938  60.604  1.00 18.90 ? 248  GLY A C     1 
ATOM   1691  O  O     . GLY A 1  250  ? -55.071 61.295  60.232  1.00 19.19 ? 248  GLY A O     1 
ATOM   1692  N  N     . LYS A 1  251  ? -53.284 62.579  59.742  1.00 18.15 ? 249  LYS A N     1 
ATOM   1693  C  CA    . LYS A 1  251  ? -53.491 62.426  58.301  1.00 19.40 ? 249  LYS A CA    1 
ATOM   1694  C  C     . LYS A 1  251  ? -53.304 60.980  57.878  1.00 21.79 ? 249  LYS A C     1 
ATOM   1695  O  O     . LYS A 1  251  ? -54.067 60.462  57.051  1.00 21.22 ? 249  LYS A O     1 
ATOM   1696  C  CB    . LYS A 1  251  ? -52.519 63.295  57.512  1.00 20.38 ? 249  LYS A CB    1 
ATOM   1697  C  CG    . LYS A 1  251  ? -52.754 64.787  57.566  1.00 20.78 ? 249  LYS A CG    1 
ATOM   1698  C  CD    . LYS A 1  251  ? -51.539 65.444  56.939  1.00 20.25 ? 249  LYS A CD    1 
ATOM   1699  C  CE    . LYS A 1  251  ? -51.635 66.950  56.904  1.00 20.02 ? 249  LYS A CE    1 
ATOM   1700  N  NZ    . LYS A 1  251  ? -50.302 67.499  56.492  1.00 19.86 ? 249  LYS A NZ    1 
ATOM   1701  N  N     . ALA A 1  252  ? -52.273 60.327  58.430  1.00 19.59 ? 250  ALA A N     1 
ATOM   1702  C  CA    . ALA A 1  252  ? -51.970 58.941  58.095  1.00 19.96 ? 250  ALA A CA    1 
ATOM   1703  C  C     . ALA A 1  252  ? -52.987 57.997  58.706  1.00 22.92 ? 250  ALA A C     1 
ATOM   1704  O  O     . ALA A 1  252  ? -53.369 56.999  58.079  1.00 21.47 ? 250  ALA A O     1 
ATOM   1705  C  CB    . ALA A 1  252  ? -50.562 58.583  58.573  1.00 23.06 ? 250  ALA A CB    1 
ATOM   1706  N  N     . SER A 1  253  ? -53.434 58.294  59.929  1.00 21.15 ? 251  SER A N     1 
ATOM   1707  C  CA    . SER A 1  253  ? -54.456 57.467  60.560  1.00 21.35 ? 251  SER A CA    1 
ATOM   1708  C  C     . SER A 1  253  ? -55.677 57.347  59.672  1.00 21.38 ? 251  SER A C     1 
ATOM   1709  O  O     . SER A 1  253  ? -56.229 56.254  59.507  1.00 21.87 ? 251  SER A O     1 
ATOM   1710  C  CB    . SER A 1  253  ? -54.853 58.046  61.912  1.00 19.90 ? 251  SER A CB    1 
ATOM   1711  O  OG    . SER A 1  253  ? -55.930 57.296  62.442  1.00 21.26 ? 251  SER A OG    1 
ATOM   1712  N  N     . ALA A 1  254  ? -56.099 58.462  59.084  1.00 20.58 ? 252  ALA A N     1 
ATOM   1713  C  CA    . ALA A 1  254  ? -57.162 58.487  58.084  1.00 21.62 ? 252  ALA A CA    1 
ATOM   1714  C  C     . ALA A 1  254  ? -58.421 57.774  58.578  1.00 24.49 ? 252  ALA A C     1 
ATOM   1715  O  O     . ALA A 1  254  ? -59.010 56.937  57.887  1.00 23.44 ? 252  ALA A O     1 
ATOM   1716  C  CB    . ALA A 1  254  ? -56.673 57.895  56.761  1.00 26.27 ? 252  ALA A CB    1 
ATOM   1717  N  N     . GLY A 1  255  ? -58.838 58.110  59.795  1.00 20.00 ? 253  GLY A N     1 
ATOM   1718  C  CA    . GLY A 1  255  ? -60.071 57.571  60.331  1.00 21.97 ? 253  GLY A CA    1 
ATOM   1719  C  C     . GLY A 1  255  ? -60.009 56.159  60.867  1.00 23.47 ? 253  GLY A C     1 
ATOM   1720  O  O     . GLY A 1  255  ? -61.063 55.585  61.138  1.00 25.65 ? 253  GLY A O     1 
ATOM   1721  N  N     . ARG A 1  256  ? -58.817 55.578  61.049  1.00 22.21 ? 254  ARG A N     1 
ATOM   1722  C  CA    . ARG A 1  256  ? -58.746 54.242  61.636  1.00 22.38 ? 254  ARG A CA    1 
ATOM   1723  C  C     . ARG A 1  256  ? -59.123 54.227  63.111  1.00 22.79 ? 254  ARG A C     1 
ATOM   1724  O  O     . ARG A 1  256  ? -59.403 53.152  63.650  1.00 22.57 ? 254  ARG A O     1 
ATOM   1725  C  CB    . ARG A 1  256  ? -57.351 53.642  61.466  1.00 21.68 ? 254  ARG A CB    1 
ATOM   1726  C  CG    . ARG A 1  256  ? -57.134 52.964  60.124  1.00 24.89 ? 254  ARG A CG    1 
ATOM   1727  C  CD    . ARG A 1  256  ? -55.691 52.500  59.973  1.00 27.26 ? 254  ARG A CD    1 
ATOM   1728  N  NE    . ARG A 1  256  ? -54.777 53.617  59.761  1.00 26.41 ? 254  ARG A NE    1 
ATOM   1729  C  CZ    . ARG A 1  256  ? -53.455 53.509  59.739  1.00 27.46 ? 254  ARG A CZ    1 
ATOM   1730  N  NH1   . ARG A 1  256  ? -52.849 52.355  59.987  1.00 26.59 ? 254  ARG A NH1   1 
ATOM   1731  N  NH2   . ARG A 1  256  ? -52.722 54.578  59.444  1.00 24.78 ? 254  ARG A NH2   1 
ATOM   1732  N  N     . GLY A 1  257  ? -59.136 55.379  63.776  1.00 20.62 ? 255  GLY A N     1 
ATOM   1733  C  CA    . GLY A 1  257  ? -59.558 55.423  65.164  1.00 19.50 ? 255  GLY A CA    1 
ATOM   1734  C  C     . GLY A 1  257  ? -58.421 55.198  66.145  1.00 19.45 ? 255  GLY A C     1 
ATOM   1735  O  O     . GLY A 1  257  ? -57.259 54.998  65.787  1.00 19.89 ? 255  GLY A O     1 
ATOM   1736  N  N     . ILE A 1  258  ? -58.774 55.221  67.427  1.00 17.42 ? 256  ILE A N     1 
ATOM   1737  C  CA    . ILE A 1  258  ? -57.742 55.259  68.457  1.00 17.11 ? 256  ILE A CA    1 
ATOM   1738  C  C     . ILE A 1  258  ? -57.166 53.887  68.777  1.00 17.97 ? 256  ILE A C     1 
ATOM   1739  O  O     . ILE A 1  258  ? -56.092 53.806  69.387  1.00 17.82 ? 256  ILE A O     1 
ATOM   1740  C  CB    . ILE A 1  258  ? -58.278 55.903  69.745  1.00 16.62 ? 256  ILE A CB    1 
ATOM   1741  C  CG1   . ILE A 1  258  ? -59.384 55.042  70.356  1.00 17.18 ? 256  ILE A CG1   1 
ATOM   1742  C  CG2   . ILE A 1  258  ? -58.738 57.350  69.483  1.00 18.53 ? 256  ILE A CG2   1 
ATOM   1743  C  CD1   . ILE A 1  258  ? -59.944 55.638  71.626  1.00 20.66 ? 256  ILE A CD1   1 
ATOM   1744  N  N     . TYR A 1  259  ? -57.831 52.800  68.396  1.00 19.55 ? 257  TYR A N     1 
ATOM   1745  C  CA    . TYR A 1  259  ? -57.298 51.475  68.705  1.00 19.75 ? 257  TYR A CA    1 
ATOM   1746  C  C     . TYR A 1  259  ? -56.519 50.877  67.542  1.00 20.77 ? 257  TYR A C     1 
ATOM   1747  O  O     . TYR A 1  259  ? -55.377 50.444  67.725  1.00 24.30 ? 257  TYR A O     1 
ATOM   1748  C  CB    . TYR A 1  259  ? -58.438 50.541  69.134  1.00 22.42 ? 257  TYR A CB    1 
ATOM   1749  C  CG    . TYR A 1  259  ? -59.253 51.121  70.268  1.00 21.60 ? 257  TYR A CG    1 
ATOM   1750  C  CD1   . TYR A 1  259  ? -58.663 51.403  71.494  1.00 20.50 ? 257  TYR A CD1   1 
ATOM   1751  C  CD2   . TYR A 1  259  ? -60.595 51.425  70.099  1.00 22.55 ? 257  TYR A CD2   1 
ATOM   1752  C  CE1   . TYR A 1  259  ? -59.393 51.942  72.521  1.00 21.81 ? 257  TYR A CE1   1 
ATOM   1753  C  CE2   . TYR A 1  259  ? -61.343 51.961  71.128  1.00 23.67 ? 257  TYR A CE2   1 
ATOM   1754  C  CZ    . TYR A 1  259  ? -60.733 52.222  72.337  1.00 20.28 ? 257  TYR A CZ    1 
ATOM   1755  O  OH    . TYR A 1  259  ? -61.461 52.777  73.360  1.00 21.73 ? 257  TYR A OH    1 
ATOM   1756  N  N     . GLU A 1  260  ? -57.094 50.888  66.333  1.00 20.22 ? 258  GLU A N     1 
ATOM   1757  C  CA    . GLU A 1  260  ? -56.384 50.362  65.171  1.00 25.37 ? 258  GLU A CA    1 
ATOM   1758  C  C     . GLU A 1  260  ? -55.333 51.332  64.657  1.00 25.65 ? 258  GLU A C     1 
ATOM   1759  O  O     . GLU A 1  260  ? -54.268 50.903  64.196  1.00 27.73 ? 258  GLU A O     1 
ATOM   1760  C  CB    . GLU A 1  260  ? -57.362 50.035  64.033  1.00 26.16 ? 258  GLU A CB    1 
ATOM   1761  C  CG    . GLU A 1  260  ? -56.630 49.656  62.733  1.00 32.60 ? 258  GLU A CG    1 
ATOM   1762  C  CD    . GLU A 1  260  ? -57.537 49.344  61.550  1.00 38.45 ? 258  GLU A CD    1 
ATOM   1763  O  OE1   . GLU A 1  260  ? -58.762 49.166  61.737  1.00 43.12 ? 258  GLU A OE1   1 
ATOM   1764  O  OE2   . GLU A 1  260  ? -57.003 49.270  60.420  1.00 41.75 ? 258  GLU A OE2   1 
ATOM   1765  N  N     . GLY A 1  261  ? -55.595 52.632  64.756  1.00 21.66 ? 259  GLY A N     1 
ATOM   1766  C  CA    . GLY A 1  261  ? -54.749 53.626  64.151  1.00 19.15 ? 259  GLY A CA    1 
ATOM   1767  C  C     . GLY A 1  261  ? -53.684 54.131  65.097  1.00 20.14 ? 259  GLY A C     1 
ATOM   1768  O  O     . GLY A 1  261  ? -53.716 53.882  66.305  1.00 19.28 ? 259  GLY A O     1 
ATOM   1769  N  N     . PRO A 1  262  ? -52.726 54.870  64.548  1.00 19.56 ? 260  PRO A N     1 
ATOM   1770  C  CA    . PRO A 1  262  ? -51.581 55.322  65.338  1.00 17.36 ? 260  PRO A CA    1 
ATOM   1771  C  C     . PRO A 1  262  ? -51.967 56.444  66.286  1.00 17.95 ? 260  PRO A C     1 
ATOM   1772  O  O     . PRO A 1  262  ? -52.988 57.112  66.125  1.00 19.22 ? 260  PRO A O     1 
ATOM   1773  C  CB    . PRO A 1  262  ? -50.601 55.818  64.273  1.00 19.99 ? 260  PRO A CB    1 
ATOM   1774  C  CG    . PRO A 1  262  ? -51.505 56.265  63.157  1.00 20.04 ? 260  PRO A CG    1 
ATOM   1775  C  CD    . PRO A 1  262  ? -52.631 55.284  63.141  1.00 22.88 ? 260  PRO A CD    1 
ATOM   1776  N  N     . GLY A 1  263  ? -51.136 56.624  67.307  1.00 18.28 ? 261  GLY A N     1 
ATOM   1777  C  CA    . GLY A 1  263  ? -51.309 57.730  68.227  1.00 18.53 ? 261  GLY A CA    1 
ATOM   1778  C  C     . GLY A 1  263  ? -49.997 58.417  68.531  1.00 18.72 ? 261  GLY A C     1 
ATOM   1779  O  O     . GLY A 1  263  ? -48.967 58.089  67.927  1.00 16.72 ? 261  GLY A O     1 
ATOM   1780  N  N     . ILE A 1  264  ? -50.019 59.378  69.456  1.00 16.92 ? 262  ILE A N     1 
ATOM   1781  C  CA    . ILE A 1  264  ? -48.814 60.089  69.864  1.00 17.26 ? 262  ILE A CA    1 
ATOM   1782  C  C     . ILE A 1  264  ? -48.679 59.963  71.375  1.00 17.18 ? 262  ILE A C     1 
ATOM   1783  O  O     . ILE A 1  264  ? -49.663 59.771  72.095  1.00 17.02 ? 262  ILE A O     1 
ATOM   1784  C  CB    . ILE A 1  264  ? -48.850 61.573  69.423  1.00 17.15 ? 262  ILE A CB    1 
ATOM   1785  C  CG1   . ILE A 1  264  ? -47.451 62.203  69.500  1.00 16.35 ? 262  ILE A CG1   1 
ATOM   1786  C  CG2   . ILE A 1  264  ? -49.883 62.343  70.243  1.00 17.89 ? 262  ILE A CG2   1 
ATOM   1787  C  CD1   . ILE A 1  264  ? -47.354 63.597  68.866  1.00 18.64 ? 262  ILE A CD1   1 
ATOM   1788  N  N     . SER A 1  265  ? -47.440 60.027  71.850  1.00 14.35 ? 263  SER A N     1 
ATOM   1789  C  CA    . SER A 1  265  ? -47.137 60.088  73.271  1.00 16.92 ? 263  SER A CA    1 
ATOM   1790  C  C     . SER A 1  265  ? -46.352 61.358  73.529  1.00 17.72 ? 263  SER A C     1 
ATOM   1791  O  O     . SER A 1  265  ? -45.485 61.735  72.728  1.00 20.43 ? 263  SER A O     1 
ATOM   1792  C  CB    . SER A 1  265  ? -46.322 58.886  73.745  1.00 17.71 ? 263  SER A CB    1 
ATOM   1793  O  OG    . SER A 1  265  ? -47.057 57.684  73.679  1.00 19.12 ? 263  SER A OG    1 
ATOM   1794  N  N     . ILE A 1  266  ? -46.642 62.004  74.655  1.00 16.36 ? 264  ILE A N     1 
ATOM   1795  C  CA    . ILE A 1  266  ? -45.970 63.247  75.010  1.00 16.15 ? 264  ILE A CA    1 
ATOM   1796  C  C     . ILE A 1  266  ? -45.404 63.148  76.417  1.00 16.66 ? 264  ILE A C     1 
ATOM   1797  O  O     . ILE A 1  266  ? -45.913 62.419  77.272  1.00 16.77 ? 264  ILE A O     1 
ATOM   1798  C  CB    . ILE A 1  266  ? -46.906 64.466  74.902  1.00 15.63 ? 264  ILE A CB    1 
ATOM   1799  C  CG1   . ILE A 1  266  ? -48.048 64.373  75.920  1.00 18.28 ? 264  ILE A CG1   1 
ATOM   1800  C  CG2   . ILE A 1  266  ? -47.458 64.599  73.483  1.00 19.16 ? 264  ILE A CG2   1 
ATOM   1801  C  CD1   . ILE A 1  266  ? -48.865 65.656  75.991  1.00 21.44 ? 264  ILE A CD1   1 
ATOM   1802  N  N     . LYS A 1  267  ? -44.330 63.887  76.654  1.00 16.73 ? 265  LYS A N     1 
ATOM   1803  C  CA    . LYS A 1  267  ? -43.781 64.014  77.994  1.00 15.84 ? 265  LYS A CA    1 
ATOM   1804  C  C     . LYS A 1  267  ? -44.030 65.439  78.451  1.00 15.02 ? 265  LYS A C     1 
ATOM   1805  O  O     . LYS A 1  267  ? -43.656 66.396  77.759  1.00 17.42 ? 265  LYS A O     1 
ATOM   1806  C  CB    . LYS A 1  267  ? -42.297 63.648  78.022  1.00 18.91 ? 265  LYS A CB    1 
ATOM   1807  C  CG    . LYS A 1  267  ? -42.098 62.138  77.814  1.00 20.83 ? 265  LYS A CG    1 
ATOM   1808  C  CD    . LYS A 1  267  ? -40.655 61.726  77.733  1.00 21.82 ? 265  LYS A CD    1 
ATOM   1809  C  CE    . LYS A 1  267  ? -40.530 60.382  77.036  1.00 22.29 ? 265  LYS A CE    1 
ATOM   1810  N  NZ    . LYS A 1  267  ? -41.044 59.263  77.858  1.00 20.47 ? 265  LYS A NZ    1 
ATOM   1811  N  N     . LEU A 1  268  ? -44.724 65.581  79.584  1.00 13.96 ? 266  LEU A N     1 
ATOM   1812  C  CA    . LEU A 1  268  ? -45.103 66.912  80.041  1.00 15.05 ? 266  LEU A CA    1 
ATOM   1813  C  C     . LEU A 1  268  ? -43.894 67.796  80.298  1.00 14.57 ? 266  LEU A C     1 
ATOM   1814  O  O     . LEU A 1  268  ? -43.970 69.012  80.093  1.00 14.71 ? 266  LEU A O     1 
ATOM   1815  C  CB    . LEU A 1  268  ? -45.968 66.816  81.295  1.00 15.86 ? 266  LEU A CB    1 
ATOM   1816  C  CG    . LEU A 1  268  ? -47.332 66.162  81.066  1.00 17.90 ? 266  LEU A CG    1 
ATOM   1817  C  CD1   . LEU A 1  268  ? -48.140 66.147  82.334  1.00 18.18 ? 266  LEU A CD1   1 
ATOM   1818  C  CD2   . LEU A 1  268  ? -48.083 66.924  79.953  1.00 20.21 ? 266  LEU A CD2   1 
ATOM   1819  N  N     . SER A 1  269  ? -42.771 67.217  80.735  1.00 16.81 ? 267  SER A N     1 
ATOM   1820  C  CA    . SER A 1  269  ? -41.587 68.030  80.987  1.00 18.01 ? 267  SER A CA    1 
ATOM   1821  C  C     . SER A 1  269  ? -41.021 68.640  79.712  1.00 19.52 ? 267  SER A C     1 
ATOM   1822  O  O     . SER A 1  269  ? -40.227 69.580  79.798  1.00 19.06 ? 267  SER A O     1 
ATOM   1823  C  CB    . SER A 1  269  ? -40.499 67.204  81.672  1.00 16.01 ? 267  SER A CB    1 
ATOM   1824  O  OG    . SER A 1  269  ? -40.025 66.208  80.784  1.00 16.98 ? 267  SER A OG    1 
ATOM   1825  N  N     . ALA A 1  270  ? -41.395 68.118  78.533  1.00 15.26 ? 268  ALA A N     1 
ATOM   1826  C  CA    . ALA A 1  270  ? -40.988 68.761  77.292  1.00 17.34 ? 268  ALA A CA    1 
ATOM   1827  C  C     . ALA A 1  270  ? -41.731 70.063  77.055  1.00 17.88 ? 268  ALA A C     1 
ATOM   1828  O  O     . ALA A 1  270  ? -41.249 70.909  76.302  1.00 16.97 ? 268  ALA A O     1 
ATOM   1829  C  CB    . ALA A 1  270  ? -41.222 67.820  76.105  1.00 19.21 ? 268  ALA A CB    1 
ATOM   1830  N  N     . LEU A 1  271  ? -42.894 70.240  77.671  1.00 16.41 ? 269  LEU A N     1 
ATOM   1831  C  CA    . LEU A 1  271  ? -43.803 71.312  77.297  1.00 17.02 ? 269  LEU A CA    1 
ATOM   1832  C  C     . LEU A 1  271  ? -43.809 72.474  78.279  1.00 16.44 ? 269  LEU A C     1 
ATOM   1833  O  O     . LEU A 1  271  ? -44.534 73.444  78.060  1.00 17.64 ? 269  LEU A O     1 
ATOM   1834  C  CB    . LEU A 1  271  ? -45.213 70.753  77.141  1.00 16.92 ? 269  LEU A CB    1 
ATOM   1835  C  CG    . LEU A 1  271  ? -45.349 69.808  75.960  1.00 16.33 ? 269  LEU A CG    1 
ATOM   1836  C  CD1   . LEU A 1  271  ? -46.725 69.145  76.004  1.00 19.56 ? 269  LEU A CD1   1 
ATOM   1837  C  CD2   . LEU A 1  271  ? -45.218 70.652  74.731  1.00 19.63 ? 269  LEU A CD2   1 
ATOM   1838  N  N     . HIS A 1  272  ? -42.995 72.418  79.339  1.00 16.67 ? 270  HIS A N     1 
ATOM   1839  C  CA    . HIS A 1  272  ? -42.896 73.583  80.205  1.00 15.33 ? 270  HIS A CA    1 
ATOM   1840  C  C     . HIS A 1  272  ? -41.557 73.510  80.911  1.00 17.04 ? 270  HIS A C     1 
ATOM   1841  O  O     . HIS A 1  272  ? -41.184 72.430  81.375  1.00 17.18 ? 270  HIS A O     1 
ATOM   1842  C  CB    . HIS A 1  272  ? -44.027 73.630  81.238  1.00 15.66 ? 270  HIS A CB    1 
ATOM   1843  C  CG    . HIS A 1  272  ? -44.168 74.972  81.880  1.00 16.34 ? 270  HIS A CG    1 
ATOM   1844  N  ND1   . HIS A 1  272  ? -43.280 75.439  82.825  1.00 18.86 ? 270  HIS A ND1   1 
ATOM   1845  C  CD2   . HIS A 1  272  ? -45.072 75.960  81.687  1.00 19.66 ? 270  HIS A CD2   1 
ATOM   1846  C  CE1   . HIS A 1  272  ? -43.637 76.658  83.193  1.00 19.56 ? 270  HIS A CE1   1 
ATOM   1847  N  NE2   . HIS A 1  272  ? -44.721 76.997  82.516  1.00 20.37 ? 270  HIS A NE2   1 
ATOM   1848  N  N     . PRO A 1  273  ? -40.813 74.614  81.015  1.00 15.93 ? 271  PRO A N     1 
ATOM   1849  C  CA    . PRO A 1  273  ? -39.491 74.551  81.654  1.00 16.97 ? 271  PRO A CA    1 
ATOM   1850  C  C     . PRO A 1  273  ? -39.527 74.473  83.172  1.00 18.34 ? 271  PRO A C     1 
ATOM   1851  O  O     . PRO A 1  273  ? -38.483 74.208  83.778  1.00 18.72 ? 271  PRO A O     1 
ATOM   1852  C  CB    . PRO A 1  273  ? -38.823 75.854  81.190  1.00 18.69 ? 271  PRO A CB    1 
ATOM   1853  C  CG    . PRO A 1  273  ? -39.959 76.803  81.049  1.00 18.85 ? 271  PRO A CG    1 
ATOM   1854  C  CD    . PRO A 1  273  ? -41.126 75.967  80.517  1.00 16.69 ? 271  PRO A CD    1 
ATOM   1855  N  N     . ARG A 1  274  ? -40.676 74.671  83.811  1.00 16.86 ? 272  ARG A N     1 
ATOM   1856  C  CA    . ARG A 1  274  ? -40.785 74.575  85.264  1.00 16.77 ? 272  ARG A CA    1 
ATOM   1857  C  C     . ARG A 1  274  ? -41.910 73.625  85.642  1.00 16.22 ? 272  ARG A C     1 
ATOM   1858  O  O     . ARG A 1  274  ? -42.827 73.966  86.395  1.00 16.31 ? 272  ARG A O     1 
ATOM   1859  C  CB    . ARG A 1  274  ? -41.008 75.946  85.894  1.00 17.12 ? 272  ARG A CB    1 
ATOM   1860  C  CG    . ARG A 1  274  ? -39.882 76.945  85.646  1.00 18.93 ? 272  ARG A CG    1 
ATOM   1861  C  CD    . ARG A 1  274  ? -38.542 76.428  86.194  1.00 17.66 ? 272  ARG A CD    1 
ATOM   1862  N  NE    . ARG A 1  274  ? -38.622 76.014  87.591  1.00 18.80 ? 272  ARG A NE    1 
ATOM   1863  C  CZ    . ARG A 1  274  ? -38.577 76.847  88.623  1.00 17.84 ? 272  ARG A CZ    1 
ATOM   1864  N  NH1   . ARG A 1  274  ? -38.496 78.155  88.455  1.00 18.63 ? 272  ARG A NH1   1 
ATOM   1865  N  NH2   . ARG A 1  274  ? -38.629 76.354  89.859  1.00 20.20 ? 272  ARG A NH2   1 
ATOM   1866  N  N     . TYR A 1  275  ? -41.848 72.410  85.106  1.00 15.69 ? 273  TYR A N     1 
ATOM   1867  C  CA    . TYR A 1  275  ? -42.852 71.379  85.377  1.00 14.28 ? 273  TYR A CA    1 
ATOM   1868  C  C     . TYR A 1  275  ? -42.504 70.716  86.709  1.00 17.12 ? 273  TYR A C     1 
ATOM   1869  O  O     . TYR A 1  275  ? -41.741 69.750  86.776  1.00 16.29 ? 273  TYR A O     1 
ATOM   1870  C  CB    . TYR A 1  275  ? -42.905 70.376  84.228  1.00 16.18 ? 273  TYR A CB    1 
ATOM   1871  C  CG    . TYR A 1  275  ? -43.857 69.238  84.478  1.00 13.93 ? 273  TYR A CG    1 
ATOM   1872  C  CD1   . TYR A 1  275  ? -45.164 69.485  84.882  1.00 15.30 ? 273  TYR A CD1   1 
ATOM   1873  C  CD2   . TYR A 1  275  ? -43.448 67.913  84.310  1.00 14.73 ? 273  TYR A CD2   1 
ATOM   1874  C  CE1   . TYR A 1  275  ? -46.033 68.444  85.135  1.00 17.42 ? 273  TYR A CE1   1 
ATOM   1875  C  CE2   . TYR A 1  275  ? -44.319 66.860  84.564  1.00 15.89 ? 273  TYR A CE2   1 
ATOM   1876  C  CZ    . TYR A 1  275  ? -45.610 67.146  84.977  1.00 17.36 ? 273  TYR A CZ    1 
ATOM   1877  O  OH    . TYR A 1  275  ? -46.496 66.139  85.233  1.00 17.40 ? 273  TYR A OH    1 
ATOM   1878  N  N     . SER A 1  276  ? -43.075 71.251  87.785  1.00 16.06 ? 274  SER A N     1 
ATOM   1879  C  CA    . SER A 1  276  ? -42.800 70.736  89.122  1.00 15.61 ? 274  SER A CA    1 
ATOM   1880  C  C     . SER A 1  276  ? -43.920 71.166  90.051  1.00 16.57 ? 274  SER A C     1 
ATOM   1881  O  O     . SER A 1  276  ? -44.627 72.149  89.794  1.00 15.90 ? 274  SER A O     1 
ATOM   1882  C  CB    . SER A 1  276  ? -41.466 71.242  89.672  1.00 18.87 ? 274  SER A CB    1 
ATOM   1883  O  OG    . SER A 1  276  ? -41.585 72.607  90.015  1.00 23.08 ? 274  SER A OG    1 
ATOM   1884  N  N     . ARG A 1  277  ? -44.054 70.418  91.152  1.00 16.97 ? 275  ARG A N     1 
ATOM   1885  C  CA    . ARG A 1  277  ? -45.045 70.761  92.162  1.00 16.08 ? 275  ARG A CA    1 
ATOM   1886  C  C     . ARG A 1  277  ? -44.798 72.152  92.726  1.00 16.80 ? 275  ARG A C     1 
ATOM   1887  O  O     . ARG A 1  277  ? -45.749 72.868  93.049  1.00 16.98 ? 275  ARG A O     1 
ATOM   1888  C  CB    . ARG A 1  277  ? -45.048 69.713  93.285  1.00 15.99 ? 275  ARG A CB    1 
ATOM   1889  C  CG    . ARG A 1  277  ? -45.938 70.075  94.485  1.00 16.42 ? 275  ARG A CG    1 
ATOM   1890  C  CD    . ARG A 1  277  ? -47.409 70.283  94.111  1.00 16.40 ? 275  ARG A CD    1 
ATOM   1891  N  NE    . ARG A 1  277  ? -48.205 70.604  95.289  1.00 17.23 ? 275  ARG A NE    1 
ATOM   1892  C  CZ    . ARG A 1  277  ? -48.371 71.828  95.777  1.00 16.97 ? 275  ARG A CZ    1 
ATOM   1893  N  NH1   . ARG A 1  277  ? -47.757 72.877  95.246  1.00 15.96 ? 275  ARG A NH1   1 
ATOM   1894  N  NH2   . ARG A 1  277  ? -49.192 72.012  96.812  1.00 16.68 ? 275  ARG A NH2   1 
ATOM   1895  N  N     . ALA A 1  278  ? -43.525 72.551  92.868  1.00 17.47 ? 276  ALA A N     1 
ATOM   1896  C  CA    . ALA A 1  278  ? -43.244 73.876  93.416  1.00 18.69 ? 276  ALA A CA    1 
ATOM   1897  C  C     . ALA A 1  278  ? -43.810 74.977  92.534  1.00 18.73 ? 276  ALA A C     1 
ATOM   1898  O  O     . ALA A 1  278  ? -44.111 76.075  93.022  1.00 19.38 ? 276  ALA A O     1 
ATOM   1899  C  CB    . ALA A 1  278  ? -41.733 74.066  93.596  1.00 19.27 ? 276  ALA A CB    1 
ATOM   1900  N  N     . GLN A 1  279  ? -43.967 74.705  91.240  1.00 16.66 ? 277  GLN A N     1 
ATOM   1901  C  CA    . GLN A 1  279  ? -44.511 75.660  90.282  1.00 16.83 ? 277  GLN A CA    1 
ATOM   1902  C  C     . GLN A 1  279  ? -45.891 75.228  89.803  1.00 18.46 ? 277  GLN A C     1 
ATOM   1903  O  O     . GLN A 1  279  ? -46.252 75.452  88.645  1.00 17.80 ? 277  GLN A O     1 
ATOM   1904  C  CB    . GLN A 1  279  ? -43.567 75.817  89.091  1.00 17.93 ? 277  GLN A CB    1 
ATOM   1905  C  CG    . GLN A 1  279  ? -42.171 76.264  89.494  1.00 17.75 ? 277  GLN A CG    1 
ATOM   1906  C  CD    . GLN A 1  279  ? -42.176 77.667  90.075  1.00 21.52 ? 277  GLN A CD    1 
ATOM   1907  O  OE1   . GLN A 1  279  ? -42.802 78.573  89.532  1.00 27.00 ? 277  GLN A OE1   1 
ATOM   1908  N  NE2   . GLN A 1  279  ? -41.497 77.844  91.195  1.00 18.80 ? 277  GLN A NE2   1 
ATOM   1909  N  N     . ALA A 1  280  ? -46.663 74.596  90.687  1.00 16.66 ? 278  ALA A N     1 
ATOM   1910  C  CA    . ALA A 1  280  ? -47.938 74.010  90.270  1.00 19.38 ? 278  ALA A CA    1 
ATOM   1911  C  C     . ALA A 1  280  ? -48.852 75.038  89.614  1.00 17.71 ? 278  ALA A C     1 
ATOM   1912  O  O     . ALA A 1  280  ? -49.528 74.727  88.624  1.00 17.89 ? 278  ALA A O     1 
ATOM   1913  C  CB    . ALA A 1  280  ? -48.636 73.373  91.468  1.00 18.51 ? 278  ALA A CB    1 
ATOM   1914  N  N     . ALA A 1  281  ? -48.911 76.257  90.158  1.00 16.78 ? 279  ALA A N     1 
ATOM   1915  C  CA    . ALA A 1  281  ? -49.799 77.266  89.591  1.00 17.96 ? 279  ALA A CA    1 
ATOM   1916  C  C     . ALA A 1  281  ? -49.399 77.614  88.162  1.00 18.95 ? 279  ALA A C     1 
ATOM   1917  O  O     . ALA A 1  281  ? -50.266 77.794  87.296  1.00 18.19 ? 279  ALA A O     1 
ATOM   1918  C  CB    . ALA A 1  281  ? -49.809 78.526  90.459  1.00 20.46 ? 279  ALA A CB    1 
ATOM   1919  N  N     . ARG A 1  282  ? -48.094 77.731  87.895  1.00 16.76 ? 280  ARG A N     1 
ATOM   1920  C  CA    . ARG A 1  282  ? -47.670 77.969  86.516  1.00 17.27 ? 280  ARG A CA    1 
ATOM   1921  C  C     . ARG A 1  282  ? -47.983 76.771  85.635  1.00 16.34 ? 280  ARG A C     1 
ATOM   1922  O  O     . ARG A 1  282  ? -48.329 76.930  84.460  1.00 16.98 ? 280  ARG A O     1 
ATOM   1923  C  CB    . ARG A 1  282  ? -46.169 78.274  86.448  1.00 17.33 ? 280  ARG A CB    1 
ATOM   1924  C  CG    . ARG A 1  282  ? -45.789 79.632  86.983  1.00 19.23 ? 280  ARG A CG    1 
ATOM   1925  C  CD    . ARG A 1  282  ? -44.342 79.915  86.609  1.00 20.02 ? 280  ARG A CD    1 
ATOM   1926  N  NE    . ARG A 1  282  ? -44.214 80.032  85.163  1.00 20.17 ? 280  ARG A NE    1 
ATOM   1927  C  CZ    . ARG A 1  282  ? -43.066 79.983  84.506  1.00 19.82 ? 280  ARG A CZ    1 
ATOM   1928  N  NH1   . ARG A 1  282  ? -41.906 79.847  85.143  1.00 17.81 ? 280  ARG A NH1   1 
ATOM   1929  N  NH2   . ARG A 1  282  ? -43.080 80.074  83.179  1.00 20.91 ? 280  ARG A NH2   1 
ATOM   1930  N  N     . VAL A 1  283  ? -47.843 75.561  86.176  1.00 15.20 ? 281  VAL A N     1 
ATOM   1931  C  CA    . VAL A 1  283  ? -48.144 74.367  85.392  1.00 16.01 ? 281  VAL A CA    1 
ATOM   1932  C  C     . VAL A 1  283  ? -49.609 74.368  84.972  1.00 17.60 ? 281  VAL A C     1 
ATOM   1933  O  O     . VAL A 1  283  ? -49.942 74.142  83.804  1.00 16.28 ? 281  VAL A O     1 
ATOM   1934  C  CB    . VAL A 1  283  ? -47.789 73.101  86.187  1.00 15.85 ? 281  VAL A CB    1 
ATOM   1935  C  CG1   . VAL A 1  283  ? -48.357 71.864  85.481  1.00 18.37 ? 281  VAL A CG1   1 
ATOM   1936  C  CG2   . VAL A 1  283  ? -46.282 72.981  86.321  1.00 16.73 ? 281  VAL A CG2   1 
ATOM   1937  N  N     . MET A 1  284  ? -50.511 74.626  85.916  1.00 16.17 ? 282  MET A N     1 
ATOM   1938  C  CA    . MET A 1  284  ? -51.926 74.611  85.547  1.00 15.88 ? 282  MET A CA    1 
ATOM   1939  C  C     . MET A 1  284  ? -52.293 75.791  84.661  1.00 17.67 ? 282  MET A C     1 
ATOM   1940  O  O     . MET A 1  284  ? -53.183 75.672  83.809  1.00 19.15 ? 282  MET A O     1 
ATOM   1941  C  CB    . MET A 1  284  ? -52.795 74.604  86.799  1.00 17.32 ? 282  MET A CB    1 
ATOM   1942  C  CG    . MET A 1  284  ? -52.492 73.433  87.732  1.00 18.78 ? 282  MET A CG    1 
ATOM   1943  S  SD    . MET A 1  284  ? -52.704 71.820  86.971  1.00 20.05 ? 282  MET A SD    1 
ATOM   1944  C  CE    . MET A 1  284  ? -54.461 71.852  86.554  1.00 18.71 ? 282  MET A CE    1 
ATOM   1945  N  N     . GLY A 1  285  ? -51.641 76.937  84.853  1.00 17.20 ? 283  GLY A N     1 
ATOM   1946  C  CA    . GLY A 1  285  ? -51.968 78.098  84.049  1.00 16.57 ? 283  GLY A CA    1 
ATOM   1947  C  C     . GLY A 1  285  ? -51.365 78.086  82.665  1.00 18.44 ? 283  GLY A C     1 
ATOM   1948  O  O     . GLY A 1  285  ? -51.966 78.619  81.724  1.00 19.70 ? 283  GLY A O     1 
ATOM   1949  N  N     . GLU A 1  286  ? -50.188 77.486  82.508  1.00 17.76 ? 284  GLU A N     1 
ATOM   1950  C  CA    . GLU A 1  286  ? -49.426 77.611  81.271  1.00 16.30 ? 284  GLU A CA    1 
ATOM   1951  C  C     . GLU A 1  286  ? -49.244 76.298  80.535  1.00 18.16 ? 284  GLU A C     1 
ATOM   1952  O  O     . GLU A 1  286  ? -49.338 76.269  79.303  1.00 21.18 ? 284  GLU A O     1 
ATOM   1953  C  CB    . GLU A 1  286  ? -48.050 78.212  81.569  1.00 17.65 ? 284  GLU A CB    1 
ATOM   1954  C  CG    . GLU A 1  286  ? -48.123 79.527  82.322  1.00 20.15 ? 284  GLU A CG    1 
ATOM   1955  C  CD    . GLU A 1  286  ? -46.776 79.954  82.873  1.00 21.39 ? 284  GLU A CD    1 
ATOM   1956  O  OE1   . GLU A 1  286  ? -45.754 79.489  82.341  1.00 22.45 ? 284  GLU A OE1   1 
ATOM   1957  O  OE2   . GLU A 1  286  ? -46.741 80.755  83.835  1.00 22.49 ? 284  GLU A OE2   1 
ATOM   1958  N  N     . LEU A 1  287  ? -48.975 75.209  81.252  1.00 16.22 ? 285  LEU A N     1 
ATOM   1959  C  CA    . LEU A 1  287  ? -48.806 73.918  80.608  1.00 15.93 ? 285  LEU A CA    1 
ATOM   1960  C  C     . LEU A 1  287  ? -50.148 73.304  80.222  1.00 17.27 ? 285  LEU A C     1 
ATOM   1961  O  O     . LEU A 1  287  ? -50.297 72.783  79.113  1.00 17.74 ? 285  LEU A O     1 
ATOM   1962  C  CB    . LEU A 1  287  ? -48.021 72.984  81.528  1.00 15.98 ? 285  LEU A CB    1 
ATOM   1963  C  CG    . LEU A 1  287  ? -47.903 71.541  81.047  1.00 19.27 ? 285  LEU A CG    1 
ATOM   1964  C  CD1   . LEU A 1  287  ? -47.340 71.508  79.660  1.00 22.25 ? 285  LEU A CD1   1 
ATOM   1965  C  CD2   . LEU A 1  287  ? -47.012 70.766  82.003  1.00 21.54 ? 285  LEU A CD2   1 
ATOM   1966  N  N     . LEU A 1  288  ? -51.125 73.339  81.126  1.00 15.82 ? 286  LEU A N     1 
ATOM   1967  C  CA    . LEU A 1  288  ? -52.429 72.733  80.850  1.00 16.80 ? 286  LEU A CA    1 
ATOM   1968  C  C     . LEU A 1  288  ? -53.054 73.210  79.542  1.00 17.08 ? 286  LEU A C     1 
ATOM   1969  O  O     . LEU A 1  288  ? -53.453 72.356  78.736  1.00 17.96 ? 286  LEU A O     1 
ATOM   1970  C  CB    . LEU A 1  288  ? -53.379 72.965  82.033  1.00 18.24 ? 286  LEU A CB    1 
ATOM   1971  C  CG    . LEU A 1  288  ? -54.816 72.469  81.857  1.00 22.64 ? 286  LEU A CG    1 
ATOM   1972  C  CD1   . LEU A 1  288  ? -54.849 70.981  81.548  1.00 21.75 ? 286  LEU A CD1   1 
ATOM   1973  C  CD2   . LEU A 1  288  ? -55.609 72.773  83.121  1.00 27.07 ? 286  LEU A CD2   1 
ATOM   1974  N  N     . PRO A 1  289  ? -53.136 74.513  79.246  1.00 17.77 ? 287  PRO A N     1 
ATOM   1975  C  CA    . PRO A 1  289  ? -53.712 74.916  77.951  1.00 16.00 ? 287  PRO A CA    1 
ATOM   1976  C  C     . PRO A 1  289  ? -52.956 74.371  76.765  1.00 16.97 ? 287  PRO A C     1 
ATOM   1977  O  O     . PRO A 1  289  ? -53.558 74.167  75.700  1.00 16.24 ? 287  PRO A O     1 
ATOM   1978  C  CB    . PRO A 1  289  ? -53.641 76.446  77.992  1.00 19.07 ? 287  PRO A CB    1 
ATOM   1979  C  CG    . PRO A 1  289  ? -53.573 76.793  79.435  1.00 22.34 ? 287  PRO A CG    1 
ATOM   1980  C  CD    . PRO A 1  289  ? -52.823 75.681  80.091  1.00 18.82 ? 287  PRO A CD    1 
ATOM   1981  N  N     . ARG A 1  290  ? -51.645 74.160  76.898  1.00 15.52 ? 288  ARG A N     1 
ATOM   1982  C  CA    . ARG A 1  290  ? -50.889 73.622  75.777  1.00 15.40 ? 288  ARG A CA    1 
ATOM   1983  C  C     . ARG A 1  290  ? -51.246 72.173  75.534  1.00 15.55 ? 288  ARG A C     1 
ATOM   1984  O  O     . ARG A 1  290  ? -51.428 71.764  74.384  1.00 16.62 ? 288  ARG A O     1 
ATOM   1985  C  CB    . ARG A 1  290  ? -49.388 73.765  76.023  1.00 18.11 ? 288  ARG A CB    1 
ATOM   1986  C  CG    . ARG A 1  290  ? -48.969 75.202  76.146  1.00 19.33 ? 288  ARG A CG    1 
ATOM   1987  C  CD    . ARG A 1  290  ? -47.484 75.306  76.470  1.00 22.29 ? 288  ARG A CD    1 
ATOM   1988  N  NE    . ARG A 1  290  ? -47.119 76.704  76.673  1.00 26.29 ? 288  ARG A NE    1 
ATOM   1989  C  CZ    . ARG A 1  290  ? -46.121 77.115  77.445  1.00 25.84 ? 288  ARG A CZ    1 
ATOM   1990  N  NH1   . ARG A 1  290  ? -45.325 76.259  78.068  1.00 23.41 ? 288  ARG A NH1   1 
ATOM   1991  N  NH2   . ARG A 1  290  ? -45.918 78.420  77.598  1.00 29.07 ? 288  ARG A NH2   1 
ATOM   1992  N  N     . VAL A 1  291  ? -51.336 71.380  76.603  1.00 14.98 ? 289  VAL A N     1 
ATOM   1993  C  CA    . VAL A 1  291  ? -51.758 69.990  76.452  1.00 15.43 ? 289  VAL A CA    1 
ATOM   1994  C  C     . VAL A 1  291  ? -53.170 69.941  75.895  1.00 15.88 ? 289  VAL A C     1 
ATOM   1995  O  O     . VAL A 1  291  ? -53.481 69.118  75.025  1.00 15.62 ? 289  VAL A O     1 
ATOM   1996  C  CB    . VAL A 1  291  ? -51.656 69.243  77.793  1.00 14.01 ? 289  VAL A CB    1 
ATOM   1997  C  CG1   . VAL A 1  291  ? -52.038 67.786  77.627  1.00 16.28 ? 289  VAL A CG1   1 
ATOM   1998  C  CG2   . VAL A 1  291  ? -50.248 69.350  78.329  1.00 16.14 ? 289  VAL A CG2   1 
ATOM   1999  N  N     . LYS A 1  292  ? -54.037 70.832  76.372  1.00 14.95 ? 290  LYS A N     1 
ATOM   2000  C  CA    . LYS A 1  292  ? -55.399 70.873  75.850  1.00 13.80 ? 290  LYS A CA    1 
ATOM   2001  C  C     . LYS A 1  292  ? -55.409 71.143  74.355  1.00 16.53 ? 290  LYS A C     1 
ATOM   2002  O  O     . LYS A 1  292  ? -56.144 70.484  73.606  1.00 15.21 ? 290  LYS A O     1 
ATOM   2003  C  CB    . LYS A 1  292  ? -56.222 71.920  76.588  1.00 13.86 ? 290  LYS A CB    1 
ATOM   2004  C  CG    . LYS A 1  292  ? -57.623 72.055  75.979  1.00 15.28 ? 290  LYS A CG    1 
ATOM   2005  C  CD    . LYS A 1  292  ? -58.468 73.081  76.679  1.00 16.36 ? 290  LYS A CD    1 
ATOM   2006  C  CE    . LYS A 1  292  ? -59.836 73.141  76.002  1.00 18.82 ? 290  LYS A CE    1 
ATOM   2007  N  NZ    . LYS A 1  292  ? -60.797 73.907  76.845  1.00 18.93 ? 290  LYS A NZ    1 
ATOM   2008  N  N     . ALA A 1  293  ? -54.590 72.095  73.892  1.00 14.41 ? 291  ALA A N     1 
ATOM   2009  C  CA    . ALA A 1  293  ? -54.582 72.399  72.464  1.00 15.73 ? 291  ALA A CA    1 
ATOM   2010  C  C     . ALA A 1  293  ? -54.116 71.195  71.651  1.00 15.82 ? 291  ALA A C     1 
ATOM   2011  O  O     . ALA A 1  293  ? -54.668 70.907  70.583  1.00 17.01 ? 291  ALA A O     1 
ATOM   2012  C  CB    . ALA A 1  293  ? -53.710 73.626  72.196  1.00 16.34 ? 291  ALA A CB    1 
ATOM   2013  N  N     . LEU A 1  294  ? -53.106 70.470  72.142  1.00 14.75 ? 292  LEU A N     1 
ATOM   2014  C  CA    . LEU A 1  294  ? -52.674 69.262  71.444  1.00 14.55 ? 292  LEU A CA    1 
ATOM   2015  C  C     . LEU A 1  294  ? -53.763 68.205  71.485  1.00 15.42 ? 292  LEU A C     1 
ATOM   2016  O  O     . LEU A 1  294  ? -54.019 67.530  70.482  1.00 14.60 ? 292  LEU A O     1 
ATOM   2017  C  CB    . LEU A 1  294  ? -51.383 68.724  72.060  1.00 15.91 ? 292  LEU A CB    1 
ATOM   2018  C  CG    . LEU A 1  294  ? -50.177 69.654  71.920  1.00 16.06 ? 292  LEU A CG    1 
ATOM   2019  C  CD1   . LEU A 1  294  ? -49.025 69.095  72.733  1.00 15.27 ? 292  LEU A CD1   1 
ATOM   2020  C  CD2   . LEU A 1  294  ? -49.736 69.822  70.464  1.00 18.19 ? 292  LEU A CD2   1 
ATOM   2021  N  N     . ALA A 1  295  ? -54.439 68.076  72.629  1.00 13.31 ? 293  ALA A N     1 
ATOM   2022  C  CA    . ALA A 1  295  ? -55.512 67.088  72.756  1.00 15.01 ? 293  ALA A CA    1 
ATOM   2023  C  C     . ALA A 1  295  ? -56.689 67.402  71.835  1.00 15.83 ? 293  ALA A C     1 
ATOM   2024  O  O     . ALA A 1  295  ? -57.314 66.489  71.286  1.00 16.36 ? 293  ALA A O     1 
ATOM   2025  C  CB    . ALA A 1  295  ? -55.981 67.011  74.210  1.00 15.83 ? 293  ALA A CB    1 
ATOM   2026  N  N     . LEU A 1  296  ? -57.029 68.684  71.680  1.00 14.96 ? 294  LEU A N     1 
ATOM   2027  C  CA    . LEU A 1  296  ? -58.098 69.052  70.752  1.00 15.03 ? 294  LEU A CA    1 
ATOM   2028  C  C     . LEU A 1  296  ? -57.763 68.619  69.334  1.00 16.41 ? 294  LEU A C     1 
ATOM   2029  O  O     . LEU A 1  296  ? -58.647 68.213  68.572  1.00 15.40 ? 294  LEU A O     1 
ATOM   2030  C  CB    . LEU A 1  296  ? -58.347 70.564  70.795  1.00 15.10 ? 294  LEU A CB    1 
ATOM   2031  C  CG    . LEU A 1  296  ? -59.047 71.091  72.051  1.00 18.08 ? 294  LEU A CG    1 
ATOM   2032  C  CD1   . LEU A 1  296  ? -58.937 72.597  72.132  1.00 18.70 ? 294  LEU A CD1   1 
ATOM   2033  C  CD2   . LEU A 1  296  ? -60.524 70.694  72.068  1.00 20.87 ? 294  LEU A CD2   1 
ATOM   2034  N  N     . LEU A 1  297  ? -56.486 68.718  68.950  1.00 16.59 ? 295  LEU A N     1 
ATOM   2035  C  CA    . LEU A 1  297  ? -56.108 68.297  67.607  1.00 17.72 ? 295  LEU A CA    1 
ATOM   2036  C  C     . LEU A 1  297  ? -56.155 66.777  67.485  1.00 16.14 ? 295  LEU A C     1 
ATOM   2037  O  O     . LEU A 1  297  ? -56.646 66.243  66.486  1.00 16.93 ? 295  LEU A O     1 
ATOM   2038  C  CB    . LEU A 1  297  ? -54.719 68.843  67.266  1.00 19.79 ? 295  LEU A CB    1 
ATOM   2039  C  CG    . LEU A 1  297  ? -54.329 68.767  65.790  1.00 21.18 ? 295  LEU A CG    1 
ATOM   2040  C  CD1   . LEU A 1  297  ? -55.281 69.599  64.949  1.00 23.66 ? 295  LEU A CD1   1 
ATOM   2041  C  CD2   . LEU A 1  297  ? -52.886 69.259  65.645  1.00 23.68 ? 295  LEU A CD2   1 
ATOM   2042  N  N     . ALA A 1  298  ? -55.663 66.060  68.499  1.00 15.64 ? 296  ALA A N     1 
ATOM   2043  C  CA    . ALA A 1  298  ? -55.776 64.605  68.479  1.00 15.50 ? 296  ALA A CA    1 
ATOM   2044  C  C     . ALA A 1  298  ? -57.239 64.167  68.416  1.00 15.87 ? 296  ALA A C     1 
ATOM   2045  O  O     . ALA A 1  298  ? -57.574 63.212  67.707  1.00 15.86 ? 296  ALA A O     1 
ATOM   2046  C  CB    . ALA A 1  298  ? -55.060 64.012  69.698  1.00 16.52 ? 296  ALA A CB    1 
ATOM   2047  N  N     . LYS A 1  299  ? -58.123 64.872  69.136  1.00 14.49 ? 297  LYS A N     1 
ATOM   2048  C  CA    A LYS A 1  299  ? -59.553 64.587  69.062  0.57 15.63 ? 297  LYS A CA    1 
ATOM   2049  C  CA    B LYS A 1  299  ? -59.552 64.590  69.064  0.43 15.65 ? 297  LYS A CA    1 
ATOM   2050  C  C     . LYS A 1  299  ? -60.083 64.758  67.643  1.00 17.60 ? 297  LYS A C     1 
ATOM   2051  O  O     . LYS A 1  299  ? -60.847 63.919  67.156  1.00 18.24 ? 297  LYS A O     1 
ATOM   2052  C  CB    A LYS A 1  299  ? -60.323 65.492  70.029  0.57 16.08 ? 297  LYS A CB    1 
ATOM   2053  C  CB    B LYS A 1  299  ? -60.294 65.505  70.042  0.43 16.10 ? 297  LYS A CB    1 
ATOM   2054  C  CG    A LYS A 1  299  ? -61.802 65.651  69.681  0.57 18.13 ? 297  LYS A CG    1 
ATOM   2055  C  CG    B LYS A 1  299  ? -61.793 65.595  69.849  0.43 18.16 ? 297  LYS A CG    1 
ATOM   2056  C  CD    A LYS A 1  299  ? -62.554 66.483  70.713  0.57 18.31 ? 297  LYS A CD    1 
ATOM   2057  C  CD    B LYS A 1  299  ? -62.421 66.342  71.017  0.43 18.01 ? 297  LYS A CD    1 
ATOM   2058  C  CE    A LYS A 1  299  ? -63.940 66.865  70.192  0.57 20.19 ? 297  LYS A CE    1 
ATOM   2059  C  CE    B LYS A 1  299  ? -63.868 66.691  70.736  0.43 20.54 ? 297  LYS A CE    1 
ATOM   2060  N  NZ    A LYS A 1  299  ? -64.726 67.611  71.202  0.57 19.90 ? 297  LYS A NZ    1 
ATOM   2061  N  NZ    B LYS A 1  299  ? -64.012 67.608  69.585  0.43 20.26 ? 297  LYS A NZ    1 
ATOM   2062  N  N     . ASN A 1  300  ? -59.697 65.838  66.958  1.00 16.80 ? 298  ASN A N     1 
ATOM   2063  C  CA    . ASN A 1  300  ? -60.252 66.045  65.624  1.00 16.87 ? 298  ASN A CA    1 
ATOM   2064  C  C     . ASN A 1  300  ? -59.834 64.937  64.661  1.00 17.25 ? 298  ASN A C     1 
ATOM   2065  O  O     . ASN A 1  300  ? -60.626 64.521  63.804  1.00 19.16 ? 298  ASN A O     1 
ATOM   2066  C  CB    . ASN A 1  300  ? -59.849 67.400  65.052  1.00 19.77 ? 298  ASN A CB    1 
ATOM   2067  C  CG    . ASN A 1  300  ? -60.577 67.694  63.744  1.00 20.81 ? 298  ASN A CG    1 
ATOM   2068  O  OD1   . ASN A 1  300  ? -60.030 67.478  62.661  1.00 25.09 ? 298  ASN A OD1   1 
ATOM   2069  N  ND2   . ASN A 1  300  ? -61.830 68.157  63.844  1.00 25.59 ? 298  ASN A ND2   1 
ATOM   2070  N  N     . TYR A 1  301  ? -58.586 64.470  64.758  1.00 17.20 ? 299  TYR A N     1 
ATOM   2071  C  CA    . TYR A 1  301  ? -58.153 63.350  63.936  1.00 17.97 ? 299  TYR A CA    1 
ATOM   2072  C  C     . TYR A 1  301  ? -58.572 61.996  64.503  1.00 18.26 ? 299  TYR A C     1 
ATOM   2073  O  O     . TYR A 1  301  ? -58.417 60.980  63.813  1.00 18.48 ? 299  TYR A O     1 
ATOM   2074  C  CB    . TYR A 1  301  ? -56.633 63.364  63.774  1.00 16.16 ? 299  TYR A CB    1 
ATOM   2075  C  CG    . TYR A 1  301  ? -56.080 64.445  62.878  1.00 17.24 ? 299  TYR A CG    1 
ATOM   2076  C  CD1   . TYR A 1  301  ? -56.251 64.393  61.498  1.00 17.99 ? 299  TYR A CD1   1 
ATOM   2077  C  CD2   . TYR A 1  301  ? -55.352 65.494  63.407  1.00 15.97 ? 299  TYR A CD2   1 
ATOM   2078  C  CE1   . TYR A 1  301  ? -55.709 65.364  60.672  1.00 18.17 ? 299  TYR A CE1   1 
ATOM   2079  C  CE2   . TYR A 1  301  ? -54.798 66.466  62.590  1.00 17.24 ? 299  TYR A CE2   1 
ATOM   2080  C  CZ    . TYR A 1  301  ? -54.988 66.401  61.219  1.00 19.56 ? 299  TYR A CZ    1 
ATOM   2081  O  OH    . TYR A 1  301  ? -54.437 67.367  60.408  1.00 19.15 ? 299  TYR A OH    1 
ATOM   2082  N  N     . ASP A 1  302  ? -59.086 61.960  65.733  1.00 17.27 ? 300  ASP A N     1 
ATOM   2083  C  CA    . ASP A 1  302  ? -59.432 60.722  66.438  1.00 16.95 ? 300  ASP A CA    1 
ATOM   2084  C  C     . ASP A 1  302  ? -58.232 59.775  66.537  1.00 18.31 ? 300  ASP A C     1 
ATOM   2085  O  O     . ASP A 1  302  ? -58.291 58.605  66.148  1.00 17.24 ? 300  ASP A O     1 
ATOM   2086  C  CB    . ASP A 1  302  ? -60.635 60.018  65.789  1.00 18.19 ? 300  ASP A CB    1 
ATOM   2087  C  CG    . ASP A 1  302  ? -61.346 59.075  66.760  1.00 20.70 ? 300  ASP A CG    1 
ATOM   2088  O  OD1   . ASP A 1  302  ? -61.304 59.349  67.984  1.00 18.19 ? 300  ASP A OD1   1 
ATOM   2089  O  OD2   . ASP A 1  302  ? -61.923 58.054  66.316  1.00 23.61 ? 300  ASP A OD2   1 
ATOM   2090  N  N     . ILE A 1  303  ? -57.145 60.288  67.114  1.00 16.92 ? 301  ILE A N     1 
ATOM   2091  C  CA    . ILE A 1  303  ? -55.972 59.475  67.411  1.00 17.06 ? 301  ILE A CA    1 
ATOM   2092  C  C     . ILE A 1  303  ? -55.752 59.478  68.915  1.00 17.92 ? 301  ILE A C     1 
ATOM   2093  O  O     . ILE A 1  303  ? -56.260 60.332  69.640  1.00 16.57 ? 301  ILE A O     1 
ATOM   2094  C  CB    . ILE A 1  303  ? -54.693 59.964  66.693  1.00 15.82 ? 301  ILE A CB    1 
ATOM   2095  C  CG1   . ILE A 1  303  ? -54.198 61.290  67.300  1.00 15.18 ? 301  ILE A CG1   1 
ATOM   2096  C  CG2   . ILE A 1  303  ? -54.949 60.094  65.189  1.00 17.48 ? 301  ILE A CG2   1 
ATOM   2097  C  CD1   . ILE A 1  303  ? -52.791 61.708  66.811  1.00 18.27 ? 301  ILE A CD1   1 
ATOM   2098  N  N     . GLY A 1  304  ? -54.963 58.515  69.383  1.00 17.18 ? 302  GLY A N     1 
ATOM   2099  C  CA    . GLY A 1  304  ? -54.587 58.507  70.782  1.00 16.08 ? 302  GLY A CA    1 
ATOM   2100  C  C     . GLY A 1  304  ? -53.568 59.591  71.092  1.00 15.90 ? 302  GLY A C     1 
ATOM   2101  O  O     . GLY A 1  304  ? -52.714 59.936  70.272  1.00 16.89 ? 302  GLY A O     1 
ATOM   2102  N  N     . LEU A 1  305  ? -53.664 60.140  72.297  1.00 14.91 ? 303  LEU A N     1 
ATOM   2103  C  CA    . LEU A 1  305  ? -52.656 61.056  72.825  1.00 15.88 ? 303  LEU A CA    1 
ATOM   2104  C  C     . LEU A 1  305  ? -52.372 60.605  74.248  1.00 17.19 ? 303  LEU A C     1 
ATOM   2105  O  O     . LEU A 1  305  ? -53.245 60.715  75.114  1.00 15.83 ? 303  LEU A O     1 
ATOM   2106  C  CB    . LEU A 1  305  ? -53.128 62.514  72.791  1.00 17.12 ? 303  LEU A CB    1 
ATOM   2107  C  CG    . LEU A 1  305  ? -52.085 63.554  73.239  1.00 17.51 ? 303  LEU A CG    1 
ATOM   2108  C  CD1   . LEU A 1  305  ? -52.231 64.884  72.497  1.00 18.91 ? 303  LEU A CD1   1 
ATOM   2109  C  CD2   . LEU A 1  305  ? -52.167 63.814  74.744  1.00 21.13 ? 303  LEU A CD2   1 
ATOM   2110  N  N     . ASN A 1  306  ? -51.161 60.106  74.495  1.00 16.80 ? 304  ASN A N     1 
ATOM   2111  C  CA    . ASN A 1  306  ? -50.797 59.505  75.772  1.00 18.24 ? 304  ASN A CA    1 
ATOM   2112  C  C     . ASN A 1  306  ? -49.851 60.429  76.527  1.00 15.47 ? 304  ASN A C     1 
ATOM   2113  O  O     . ASN A 1  306  ? -48.882 60.929  75.948  1.00 16.55 ? 304  ASN A O     1 
ATOM   2114  C  CB    . ASN A 1  306  ? -50.129 58.145  75.561  1.00 17.22 ? 304  ASN A CB    1 
ATOM   2115  C  CG    . ASN A 1  306  ? -49.513 57.611  76.824  1.00 17.17 ? 304  ASN A CG    1 
ATOM   2116  O  OD1   . ASN A 1  306  ? -48.333 57.859  77.110  1.00 20.91 ? 304  ASN A OD1   1 
ATOM   2117  N  ND2   . ASN A 1  306  ? -50.311 56.911  77.622  1.00 16.51 ? 304  ASN A ND2   1 
ATOM   2118  N  N     . ILE A 1  307  ? -50.120 60.631  77.813  1.00 15.21 ? 305  ILE A N     1 
ATOM   2119  C  CA    . ILE A 1  307  ? -49.207 61.348  78.698  1.00 15.37 ? 305  ILE A CA    1 
ATOM   2120  C  C     . ILE A 1  307  ? -48.258 60.340  79.341  1.00 14.04 ? 305  ILE A C     1 
ATOM   2121  O  O     . ILE A 1  307  ? -48.674 59.496  80.149  1.00 16.03 ? 305  ILE A O     1 
ATOM   2122  C  CB    . ILE A 1  307  ? -49.971 62.151  79.759  1.00 16.10 ? 305  ILE A CB    1 
ATOM   2123  C  CG1   . ILE A 1  307  ? -50.824 63.238  79.087  1.00 16.23 ? 305  ILE A CG1   1 
ATOM   2124  C  CG2   . ILE A 1  307  ? -49.003 62.756  80.779  1.00 16.14 ? 305  ILE A CG2   1 
ATOM   2125  C  CD1   . ILE A 1  307  ? -51.782 63.917  80.048  1.00 18.75 ? 305  ILE A CD1   1 
ATOM   2126  N  N     . ASP A 1  308  ? -46.970 60.440  78.990  1.00 14.84 ? 306  ASP A N     1 
ATOM   2127  C  CA    . ASP A 1  308  ? -45.962 59.548  79.537  1.00 14.26 ? 306  ASP A CA    1 
ATOM   2128  C  C     . ASP A 1  308  ? -45.676 59.899  81.000  1.00 14.52 ? 306  ASP A C     1 
ATOM   2129  O  O     . ASP A 1  308  ? -45.890 61.027  81.447  1.00 15.80 ? 306  ASP A O     1 
ATOM   2130  C  CB    . ASP A 1  308  ? -44.672 59.641  78.712  1.00 15.17 ? 306  ASP A CB    1 
ATOM   2131  C  CG    . ASP A 1  308  ? -44.818 59.057  77.305  1.00 18.84 ? 306  ASP A CG    1 
ATOM   2132  O  OD1   . ASP A 1  308  ? -45.681 58.180  77.100  1.00 18.22 ? 306  ASP A OD1   1 
ATOM   2133  O  OD2   . ASP A 1  308  ? -44.058 59.471  76.395  1.00 21.60 ? 306  ASP A OD2   1 
ATOM   2134  N  N     . ALA A 1  309  ? -45.201 58.907  81.758  1.00 14.74 ? 307  ALA A N     1 
ATOM   2135  C  CA    . ALA A 1  309  ? -44.931 59.095  83.179  1.00 13.84 ? 307  ALA A CA    1 
ATOM   2136  C  C     . ALA A 1  309  ? -43.444 59.322  83.420  1.00 15.86 ? 307  ALA A C     1 
ATOM   2137  O  O     . ALA A 1  309  ? -42.594 58.661  82.811  1.00 16.74 ? 307  ALA A O     1 
ATOM   2138  C  CB    . ALA A 1  309  ? -45.410 57.896  83.993  1.00 14.23 ? 307  ALA A CB    1 
ATOM   2139  N  N     . GLU A 1  310  ? -43.136 60.257  84.320  1.00 15.11 ? 308  GLU A N     1 
ATOM   2140  C  CA    . GLU A 1  310  ? -41.739 60.628  84.524  1.00 16.27 ? 308  GLU A CA    1 
ATOM   2141  C  C     . GLU A 1  310  ? -41.334 60.383  85.972  1.00 13.91 ? 308  GLU A C     1 
ATOM   2142  O  O     . GLU A 1  310  ? -41.631 59.308  86.514  1.00 15.50 ? 308  GLU A O     1 
ATOM   2143  C  CB    . GLU A 1  310  ? -41.529 62.075  84.069  1.00 15.13 ? 308  GLU A CB    1 
ATOM   2144  C  CG    . GLU A 1  310  ? -41.984 62.251  82.609  1.00 14.45 ? 308  GLU A CG    1 
ATOM   2145  C  CD    . GLU A 1  310  ? -41.662 63.628  82.045  1.00 18.45 ? 308  GLU A CD    1 
ATOM   2146  O  OE1   . GLU A 1  310  ? -40.453 63.952  81.925  1.00 18.32 ? 308  GLU A OE1   1 
ATOM   2147  O  OE2   . GLU A 1  310  ? -42.612 64.373  81.725  1.00 17.05 ? 308  GLU A OE2   1 
ATOM   2148  N  N     . GLU A 1  311  ? -40.650 61.336  86.606  1.00 15.46 ? 309  GLU A N     1 
ATOM   2149  C  CA    . GLU A 1  311  ? -40.120 61.077  87.939  1.00 17.27 ? 309  GLU A CA    1 
ATOM   2150  C  C     . GLU A 1  311  ? -41.245 60.985  88.958  1.00 14.59 ? 309  GLU A C     1 
ATOM   2151  O  O     . GLU A 1  311  ? -42.361 61.460  88.746  1.00 14.89 ? 309  GLU A O     1 
ATOM   2152  C  CB    . GLU A 1  311  ? -39.144 62.167  88.374  1.00 17.39 ? 309  GLU A CB    1 
ATOM   2153  C  CG    . GLU A 1  311  ? -37.878 62.221  87.531  1.00 18.02 ? 309  GLU A CG    1 
ATOM   2154  C  CD    . GLU A 1  311  ? -37.993 63.084  86.285  1.00 21.41 ? 309  GLU A CD    1 
ATOM   2155  O  OE1   . GLU A 1  311  ? -39.121 63.440  85.870  1.00 18.06 ? 309  GLU A OE1   1 
ATOM   2156  O  OE2   . GLU A 1  311  ? -36.937 63.414  85.700  1.00 22.68 ? 309  GLU A OE2   1 
ATOM   2157  N  N     . ALA A 1  312  ? -40.934 60.366  90.092  1.00 15.30 ? 310  ALA A N     1 
ATOM   2158  C  CA    . ALA A 1  312  ? -41.980 60.129  91.079  1.00 14.00 ? 310  ALA A CA    1 
ATOM   2159  C  C     . ALA A 1  312  ? -42.570 61.427  91.607  1.00 15.25 ? 310  ALA A C     1 
ATOM   2160  O  O     . ALA A 1  312  ? -43.754 61.464  91.951  1.00 16.54 ? 310  ALA A O     1 
ATOM   2161  C  CB    . ALA A 1  312  ? -41.428 59.284  92.232  1.00 15.19 ? 310  ALA A CB    1 
ATOM   2162  N  N     . ASP A 1  313  ? -41.776 62.500  91.688  1.00 16.15 ? 311  ASP A N     1 
ATOM   2163  C  CA    . ASP A 1  313  ? -42.300 63.752  92.223  1.00 16.61 ? 311  ASP A CA    1 
ATOM   2164  C  C     . ASP A 1  313  ? -43.134 64.530  91.197  1.00 14.27 ? 311  ASP A C     1 
ATOM   2165  O  O     . ASP A 1  313  ? -43.577 65.643  91.496  1.00 15.52 ? 311  ASP A O     1 
ATOM   2166  C  CB    . ASP A 1  313  ? -41.169 64.630  92.791  1.00 18.14 ? 311  ASP A CB    1 
ATOM   2167  C  CG    . ASP A 1  313  ? -40.163 65.092  91.734  1.00 21.18 ? 311  ASP A CG    1 
ATOM   2168  O  OD1   . ASP A 1  313  ? -40.352 64.823  90.521  1.00 18.54 ? 311  ASP A OD1   1 
ATOM   2169  O  OD2   . ASP A 1  313  ? -39.171 65.740  92.134  1.00 20.57 ? 311  ASP A OD2   1 
ATOM   2170  N  N     . ARG A 1  314  ? -43.374 63.951  90.021  1.00 14.18 ? 312  ARG A N     1 
ATOM   2171  C  CA    . ARG A 1  314  ? -44.287 64.539  89.051  1.00 14.66 ? 312  ARG A CA    1 
ATOM   2172  C  C     . ARG A 1  314  ? -45.582 63.758  88.913  1.00 16.94 ? 312  ARG A C     1 
ATOM   2173  O  O     . ARG A 1  314  ? -46.502 64.239  88.243  1.00 15.28 ? 312  ARG A O     1 
ATOM   2174  C  CB    . ARG A 1  314  ? -43.612 64.660  87.676  1.00 16.07 ? 312  ARG A CB    1 
ATOM   2175  C  CG    . ARG A 1  314  ? -42.597 65.793  87.661  1.00 16.87 ? 312  ARG A CG    1 
ATOM   2176  C  CD    . ARG A 1  314  ? -41.557 65.639  86.580  1.00 17.26 ? 312  ARG A CD    1 
ATOM   2177  N  NE    . ARG A 1  314  ? -40.962 66.936  86.279  1.00 19.03 ? 312  ARG A NE    1 
ATOM   2178  C  CZ    . ARG A 1  314  ? -39.970 67.126  85.417  1.00 17.80 ? 312  ARG A CZ    1 
ATOM   2179  N  NH1   . ARG A 1  314  ? -39.368 66.107  84.820  1.00 19.40 ? 312  ARG A NH1   1 
ATOM   2180  N  NH2   . ARG A 1  314  ? -39.575 68.369  85.150  1.00 19.73 ? 312  ARG A NH2   1 
ATOM   2181  N  N     . LEU A 1  315  ? -45.688 62.595  89.555  1.00 15.52 ? 313  LEU A N     1 
ATOM   2182  C  CA    . LEU A 1  315  ? -46.869 61.747  89.390  1.00 16.30 ? 313  LEU A CA    1 
ATOM   2183  C  C     . LEU A 1  315  ? -48.143 62.484  89.785  1.00 16.03 ? 313  LEU A C     1 
ATOM   2184  O  O     . LEU A 1  315  ? -49.066 62.642  88.975  1.00 16.00 ? 313  LEU A O     1 
ATOM   2185  C  CB    . LEU A 1  315  ? -46.716 60.468  90.221  1.00 16.43 ? 313  LEU A CB    1 
ATOM   2186  C  CG    . LEU A 1  315  ? -47.509 59.228  89.777  1.00 14.46 ? 313  LEU A CG    1 
ATOM   2187  C  CD1   . LEU A 1  315  ? -47.161 58.044  90.672  1.00 16.33 ? 313  LEU A CD1   1 
ATOM   2188  C  CD2   . LEU A 1  315  ? -49.010 59.442  89.785  1.00 16.95 ? 313  LEU A CD2   1 
ATOM   2189  N  N     . GLU A 1  316  ? -48.232 62.919  91.039  1.00 16.04 ? 314  GLU A N     1 
ATOM   2190  C  CA    . GLU A 1  316  ? -49.511 63.452  91.496  1.00 17.24 ? 314  GLU A CA    1 
ATOM   2191  C  C     . GLU A 1  316  ? -49.823 64.785  90.823  1.00 15.97 ? 314  GLU A C     1 
ATOM   2192  O  O     . GLU A 1  316  ? -50.986 65.056  90.496  1.00 16.63 ? 314  GLU A O     1 
ATOM   2193  C  CB    . GLU A 1  316  ? -49.525 63.553  93.019  1.00 15.97 ? 314  GLU A CB    1 
ATOM   2194  C  CG    . GLU A 1  316  ? -49.488 62.168  93.634  1.00 15.93 ? 314  GLU A CG    1 
ATOM   2195  C  CD    . GLU A 1  316  ? -49.518 62.173  95.127  1.00 16.46 ? 314  GLU A CD    1 
ATOM   2196  O  OE1   . GLU A 1  316  ? -50.270 62.982  95.707  1.00 18.53 ? 314  GLU A OE1   1 
ATOM   2197  O  OE2   . GLU A 1  316  ? -48.790 61.345  95.716  1.00 17.43 ? 314  GLU A OE2   1 
ATOM   2198  N  N     . LEU A 1  317  ? -48.795 65.593  90.538  1.00 15.93 ? 315  LEU A N     1 
ATOM   2199  C  CA    . LEU A 1  317  ? -49.003 66.803  89.744  1.00 16.62 ? 315  LEU A CA    1 
ATOM   2200  C  C     . LEU A 1  317  ? -49.666 66.479  88.404  1.00 15.99 ? 315  LEU A C     1 
ATOM   2201  O  O     . LEU A 1  317  ? -50.624 67.145  87.995  1.00 16.24 ? 315  LEU A O     1 
ATOM   2202  C  CB    . LEU A 1  317  ? -47.668 67.523  89.526  1.00 17.94 ? 315  LEU A CB    1 
ATOM   2203  C  CG    . LEU A 1  317  ? -47.729 68.772  88.643  1.00 17.50 ? 315  LEU A CG    1 
ATOM   2204  C  CD1   . LEU A 1  317  ? -48.645 69.834  89.264  1.00 20.68 ? 315  LEU A CD1   1 
ATOM   2205  C  CD2   . LEU A 1  317  ? -46.308 69.313  88.474  1.00 20.94 ? 315  LEU A CD2   1 
ATOM   2206  N  N     . SER A 1  318  ? -49.184 65.434  87.716  1.00 14.16 ? 316  SER A N     1 
ATOM   2207  C  CA    . SER A 1  318  ? -49.752 65.086  86.415  1.00 14.60 ? 316  SER A CA    1 
ATOM   2208  C  C     . SER A 1  318  ? -51.214 64.666  86.527  1.00 16.30 ? 316  SER A C     1 
ATOM   2209  O  O     . SER A 1  318  ? -51.970 64.806  85.557  1.00 15.91 ? 316  SER A O     1 
ATOM   2210  C  CB    . SER A 1  318  ? -48.932 63.972  85.746  1.00 15.31 ? 316  SER A CB    1 
ATOM   2211  O  OG    . SER A 1  318  ? -49.157 62.709  86.360  1.00 15.69 ? 316  SER A OG    1 
ATOM   2212  N  N     . LEU A 1  319  ? -51.629 64.151  87.691  1.00 15.18 ? 317  LEU A N     1 
ATOM   2213  C  CA    . LEU A 1  319  ? -53.034 63.783  87.878  1.00 16.80 ? 317  LEU A CA    1 
ATOM   2214  C  C     . LEU A 1  319  ? -53.938 64.997  87.837  1.00 16.13 ? 317  LEU A C     1 
ATOM   2215  O  O     . LEU A 1  319  ? -55.096 64.892  87.411  1.00 15.65 ? 317  LEU A O     1 
ATOM   2216  C  CB    . LEU A 1  319  ? -53.236 63.046  89.203  1.00 15.31 ? 317  LEU A CB    1 
ATOM   2217  C  CG    . LEU A 1  319  ? -52.502 61.712  89.347  1.00 19.53 ? 317  LEU A CG    1 
ATOM   2218  C  CD1   . LEU A 1  319  ? -52.737 61.140  90.737  1.00 17.49 ? 317  LEU A CD1   1 
ATOM   2219  C  CD2   . LEU A 1  319  ? -52.935 60.732  88.284  1.00 16.27 ? 317  LEU A CD2   1 
ATOM   2220  N  N     . ASP A 1  320  ? -53.449 66.159  88.264  1.00 15.83 ? 318  ASP A N     1 
ATOM   2221  C  CA    . ASP A 1  320  ? -54.295 67.338  88.180  1.00 17.90 ? 318  ASP A CA    1 
ATOM   2222  C  C     . ASP A 1  320  ? -54.513 67.754  86.732  1.00 18.51 ? 318  ASP A C     1 
ATOM   2223  O  O     . ASP A 1  320  ? -55.610 68.194  86.369  1.00 18.66 ? 318  ASP A O     1 
ATOM   2224  C  CB    . ASP A 1  320  ? -53.708 68.465  89.020  1.00 18.08 ? 318  ASP A CB    1 
ATOM   2225  C  CG    . ASP A 1  320  ? -53.911 68.228  90.501  1.00 20.81 ? 318  ASP A CG    1 
ATOM   2226  O  OD1   . ASP A 1  320  ? -55.079 68.087  90.904  1.00 21.57 ? 318  ASP A OD1   1 
ATOM   2227  O  OD2   . ASP A 1  320  ? -52.910 68.129  91.251  1.00 23.87 ? 318  ASP A OD2   1 
ATOM   2228  N  N     . LEU A 1  321  ? -53.501 67.596  85.875  1.00 15.46 ? 319  LEU A N     1 
ATOM   2229  C  CA    . LEU A 1  321  ? -53.720 67.858  84.458  1.00 15.46 ? 319  LEU A CA    1 
ATOM   2230  C  C     . LEU A 1  321  ? -54.674 66.839  83.860  1.00 16.57 ? 319  LEU A C     1 
ATOM   2231  O  O     . LEU A 1  321  ? -55.583 67.206  83.105  1.00 16.91 ? 319  LEU A O     1 
ATOM   2232  C  CB    . LEU A 1  321  ? -52.397 67.856  83.698  1.00 16.09 ? 319  LEU A CB    1 
ATOM   2233  C  CG    . LEU A 1  321  ? -51.570 69.120  83.926  1.00 21.24 ? 319  LEU A CG    1 
ATOM   2234  C  CD1   . LEU A 1  321  ? -50.658 68.939  85.122  1.00 24.34 ? 319  LEU A CD1   1 
ATOM   2235  C  CD2   . LEU A 1  321  ? -50.758 69.451  82.679  1.00 25.77 ? 319  LEU A CD2   1 
ATOM   2236  N  N     . LEU A 1  322  ? -54.492 65.558  84.195  1.00 15.56 ? 320  LEU A N     1 
ATOM   2237  C  CA    . LEU A 1  322  ? -55.389 64.529  83.665  1.00 17.26 ? 320  LEU A CA    1 
ATOM   2238  C  C     . LEU A 1  322  ? -56.829 64.801  84.087  1.00 16.89 ? 320  LEU A C     1 
ATOM   2239  O  O     . LEU A 1  322  ? -57.757 64.674  83.276  1.00 18.39 ? 320  LEU A O     1 
ATOM   2240  C  CB    . LEU A 1  322  ? -54.943 63.138  84.141  1.00 15.28 ? 320  LEU A CB    1 
ATOM   2241  C  CG    . LEU A 1  322  ? -55.798 61.983  83.603  1.00 16.45 ? 320  LEU A CG    1 
ATOM   2242  C  CD1   . LEU A 1  322  ? -55.547 61.780  82.102  1.00 16.58 ? 320  LEU A CD1   1 
ATOM   2243  C  CD2   . LEU A 1  322  ? -55.501 60.718  84.388  1.00 14.59 ? 320  LEU A CD2   1 
ATOM   2244  N  N     . GLU A 1  323  ? -57.029 65.198  85.343  1.00 16.15 ? 321  GLU A N     1 
ATOM   2245  C  CA    . GLU A 1  323  ? -58.376 65.477  85.844  1.00 19.85 ? 321  GLU A CA    1 
ATOM   2246  C  C     . GLU A 1  323  ? -59.040 66.589  85.042  1.00 19.30 ? 321  GLU A C     1 
ATOM   2247  O  O     . GLU A 1  323  ? -60.161 66.429  84.543  1.00 16.91 ? 321  GLU A O     1 
ATOM   2248  C  CB    . GLU A 1  323  ? -58.310 65.846  87.330  1.00 18.80 ? 321  GLU A CB    1 
ATOM   2249  C  CG    . GLU A 1  323  ? -59.616 66.432  87.920  1.00 23.42 ? 321  GLU A CG    1 
ATOM   2250  C  CD    . GLU A 1  323  ? -60.376 65.445  88.777  1.00 25.80 ? 321  GLU A CD    1 
ATOM   2251  O  OE1   . GLU A 1  323  ? -59.823 64.386  89.096  1.00 27.29 ? 321  GLU A OE1   1 
ATOM   2252  O  OE2   . GLU A 1  323  ? -61.545 65.722  89.123  1.00 27.46 ? 321  GLU A OE2   1 
ATOM   2253  N  N     . VAL A 1  324  ? -58.361 67.731  84.898  1.00 18.39 ? 322  VAL A N     1 
ATOM   2254  C  CA    . VAL A 1  324  ? -58.979 68.855  84.202  1.00 18.27 ? 322  VAL A CA    1 
ATOM   2255  C  C     . VAL A 1  324  ? -59.269 68.492  82.752  1.00 17.76 ? 322  VAL A C     1 
ATOM   2256  O  O     . VAL A 1  324  ? -60.335 68.818  82.220  1.00 18.17 ? 322  VAL A O     1 
ATOM   2257  C  CB    . VAL A 1  324  ? -58.104 70.118  84.301  1.00 20.14 ? 322  VAL A CB    1 
ATOM   2258  C  CG1   . VAL A 1  324  ? -58.778 71.257  83.537  1.00 19.68 ? 322  VAL A CG1   1 
ATOM   2259  C  CG2   . VAL A 1  324  ? -57.932 70.507  85.740  1.00 20.58 ? 322  VAL A CG2   1 
ATOM   2260  N  N     . LEU A 1  325  ? -58.332 67.806  82.089  1.00 15.32 ? 323  LEU A N     1 
ATOM   2261  C  CA    . LEU A 1  325  ? -58.543 67.474  80.682  1.00 16.01 ? 323  LEU A CA    1 
ATOM   2262  C  C     . LEU A 1  325  ? -59.731 66.540  80.511  1.00 16.76 ? 323  LEU A C     1 
ATOM   2263  O  O     . LEU A 1  325  ? -60.550 66.722  79.600  1.00 15.29 ? 323  LEU A O     1 
ATOM   2264  C  CB    . LEU A 1  325  ? -57.282 66.845  80.100  1.00 16.51 ? 323  LEU A CB    1 
ATOM   2265  C  CG    . LEU A 1  325  ? -56.102 67.801  80.024  1.00 17.38 ? 323  LEU A CG    1 
ATOM   2266  C  CD1   . LEU A 1  325  ? -54.828 66.974  79.876  1.00 15.75 ? 323  LEU A CD1   1 
ATOM   2267  C  CD2   . LEU A 1  325  ? -56.315 68.739  78.859  1.00 18.39 ? 323  LEU A CD2   1 
ATOM   2268  N  N     . CYS A 1  326  ? -59.843 65.532  81.380  1.00 17.54 ? 324  CYS A N     1 
ATOM   2269  C  CA    . CYS A 1  326  ? -60.937 64.583  81.229  1.00 14.49 ? 324  CYS A CA    1 
ATOM   2270  C  C     . CYS A 1  326  ? -62.284 65.190  81.580  1.00 17.41 ? 324  CYS A C     1 
ATOM   2271  O  O     . CYS A 1  326  ? -63.311 64.652  81.148  1.00 17.30 ? 324  CYS A O     1 
ATOM   2272  C  CB    . CYS A 1  326  ? -60.694 63.337  82.081  1.00 16.94 ? 324  CYS A CB    1 
ATOM   2273  S  SG    . CYS A 1  326  ? -59.349 62.319  81.423  1.00 17.86 ? 324  CYS A SG    1 
ATOM   2274  N  N     . LEU A 1  327  ? -62.302 66.278  82.353  1.00 17.53 ? 325  LEU A N     1 
ATOM   2275  C  CA    . LEU A 1  327  ? -63.525 66.986  82.716  1.00 16.97 ? 325  LEU A CA    1 
ATOM   2276  C  C     . LEU A 1  327  ? -63.846 68.140  81.770  1.00 16.99 ? 325  LEU A C     1 
ATOM   2277  O  O     . LEU A 1  327  ? -64.922 68.737  81.877  1.00 18.46 ? 325  LEU A O     1 
ATOM   2278  C  CB    . LEU A 1  327  ? -63.414 67.526  84.149  1.00 17.67 ? 325  LEU A CB    1 
ATOM   2279  C  CG    . LEU A 1  327  ? -63.302 66.452  85.239  1.00 23.48 ? 325  LEU A CG    1 
ATOM   2280  C  CD1   . LEU A 1  327  ? -63.262 67.083  86.631  1.00 25.23 ? 325  LEU A CD1   1 
ATOM   2281  C  CD2   . LEU A 1  327  ? -64.431 65.455  85.129  1.00 20.55 ? 325  LEU A CD2   1 
ATOM   2282  N  N     . ASP A 1  328  ? -62.958 68.453  80.843  1.00 17.74 ? 326  ASP A N     1 
ATOM   2283  C  CA    . ASP A 1  328  ? -63.138 69.591  79.948  1.00 15.72 ? 326  ASP A CA    1 
ATOM   2284  C  C     . ASP A 1  328  ? -64.087 69.200  78.818  1.00 17.34 ? 326  ASP A C     1 
ATOM   2285  O  O     . ASP A 1  328  ? -63.760 68.348  77.990  1.00 16.59 ? 326  ASP A O     1 
ATOM   2286  C  CB    . ASP A 1  328  ? -61.777 70.028  79.414  1.00 17.80 ? 326  ASP A CB    1 
ATOM   2287  C  CG    . ASP A 1  328  ? -61.839 71.328  78.653  1.00 17.96 ? 326  ASP A CG    1 
ATOM   2288  O  OD1   . ASP A 1  328  ? -62.845 71.565  77.953  1.00 18.24 ? 326  ASP A OD1   1 
ATOM   2289  O  OD2   . ASP A 1  328  ? -60.878 72.118  78.763  1.00 23.34 ? 326  ASP A OD2   1 
ATOM   2290  N  N     . GLY A 1  329  ? -65.263 69.821  78.785  1.00 17.19 ? 327  GLY A N     1 
ATOM   2291  C  CA    . GLY A 1  329  ? -66.251 69.458  77.784  1.00 17.98 ? 327  GLY A CA    1 
ATOM   2292  C  C     . GLY A 1  329  ? -65.789 69.654  76.355  1.00 19.29 ? 327  GLY A C     1 
ATOM   2293  O  O     . GLY A 1  329  ? -66.325 69.009  75.452  1.00 18.12 ? 327  GLY A O     1 
ATOM   2294  N  N     . ASP A 1  330  ? -64.803 70.526  76.123  1.00 16.13 ? 328  ASP A N     1 
ATOM   2295  C  CA    . ASP A 1  330  ? -64.311 70.735  74.761  1.00 17.51 ? 328  ASP A CA    1 
ATOM   2296  C  C     . ASP A 1  330  ? -63.662 69.481  74.194  1.00 17.86 ? 328  ASP A C     1 
ATOM   2297  O  O     . ASP A 1  330  ? -63.531 69.368  72.971  1.00 18.23 ? 328  ASP A O     1 
ATOM   2298  C  CB    . ASP A 1  330  ? -63.274 71.873  74.693  1.00 17.35 ? 328  ASP A CB    1 
ATOM   2299  C  CG    . ASP A 1  330  ? -63.872 73.249  74.919  1.00 21.12 ? 328  ASP A CG    1 
ATOM   2300  O  OD1   . ASP A 1  330  ? -65.088 73.447  74.705  1.00 22.60 ? 328  ASP A OD1   1 
ATOM   2301  O  OD2   . ASP A 1  330  ? -63.110 74.151  75.312  1.00 20.13 ? 328  ASP A OD2   1 
ATOM   2302  N  N     . LEU A 1  331  ? -63.229 68.552  75.053  1.00 15.98 ? 329  LEU A N     1 
ATOM   2303  C  CA    . LEU A 1  331  ? -62.610 67.311  74.604  1.00 16.67 ? 329  LEU A CA    1 
ATOM   2304  C  C     . LEU A 1  331  ? -63.582 66.137  74.587  1.00 18.34 ? 329  LEU A C     1 
ATOM   2305  O  O     . LEU A 1  331  ? -63.177 65.008  74.279  1.00 17.55 ? 329  LEU A O     1 
ATOM   2306  C  CB    . LEU A 1  331  ? -61.391 66.983  75.485  1.00 15.39 ? 329  LEU A CB    1 
ATOM   2307  C  CG    . LEU A 1  331  ? -60.193 67.932  75.279  1.00 17.02 ? 329  LEU A CG    1 
ATOM   2308  C  CD1   . LEU A 1  331  ? -59.130 67.792  76.380  1.00 15.52 ? 329  LEU A CD1   1 
ATOM   2309  C  CD2   . LEU A 1  331  ? -59.536 67.717  73.926  1.00 18.09 ? 329  LEU A CD2   1 
ATOM   2310  N  N     . SER A 1  332  ? -64.856 66.373  74.891  1.00 18.66 ? 330  SER A N     1 
ATOM   2311  C  CA    . SER A 1  332  ? -65.793 65.268  74.972  1.00 20.15 ? 330  SER A CA    1 
ATOM   2312  C  C     . SER A 1  332  ? -66.016 64.652  73.595  1.00 18.49 ? 330  SER A C     1 
ATOM   2313  O  O     . SER A 1  332  ? -65.827 65.289  72.549  1.00 19.57 ? 330  SER A O     1 
ATOM   2314  C  CB    . SER A 1  332  ? -67.118 65.732  75.569  1.00 19.73 ? 330  SER A CB    1 
ATOM   2315  O  OG    . SER A 1  332  ? -67.843 66.508  74.634  1.00 20.71 ? 330  SER A OG    1 
ATOM   2316  N  N     . GLY A 1  333  ? -66.412 63.381  73.604  1.00 15.64 ? 331  GLY A N     1 
ATOM   2317  C  CA    . GLY A 1  333  ? -66.622 62.633  72.383  1.00 18.85 ? 331  GLY A CA    1 
ATOM   2318  C  C     . GLY A 1  333  ? -65.406 61.875  71.905  1.00 18.65 ? 331  GLY A C     1 
ATOM   2319  O  O     . GLY A 1  333  ? -65.509 61.082  70.963  1.00 20.95 ? 331  GLY A O     1 
ATOM   2320  N  N     . TRP A 1  334  ? -64.266 62.071  72.544  1.00 16.55 ? 332  TRP A N     1 
ATOM   2321  C  CA    . TRP A 1  334  ? -63.011 61.464  72.135  1.00 17.65 ? 332  TRP A CA    1 
ATOM   2322  C  C     . TRP A 1  334  ? -62.485 60.627  73.290  1.00 17.26 ? 332  TRP A C     1 
ATOM   2323  O  O     . TRP A 1  334  ? -62.400 61.120  74.419  1.00 18.19 ? 332  TRP A O     1 
ATOM   2324  C  CB    . TRP A 1  334  ? -62.024 62.568  71.744  1.00 18.68 ? 332  TRP A CB    1 
ATOM   2325  C  CG    . TRP A 1  334  ? -60.583 62.199  71.589  1.00 16.60 ? 332  TRP A CG    1 
ATOM   2326  C  CD1   . TRP A 1  334  ? -60.032 61.446  70.605  1.00 16.20 ? 332  TRP A CD1   1 
ATOM   2327  C  CD2   . TRP A 1  334  ? -59.502 62.670  72.399  1.00 17.27 ? 332  TRP A CD2   1 
ATOM   2328  N  NE1   . TRP A 1  334  ? -58.665 61.379  70.769  1.00 16.62 ? 332  TRP A NE1   1 
ATOM   2329  C  CE2   . TRP A 1  334  ? -58.314 62.129  71.866  1.00 16.28 ? 332  TRP A CE2   1 
ATOM   2330  C  CE3   . TRP A 1  334  ? -59.425 63.481  73.539  1.00 17.45 ? 332  TRP A CE3   1 
ATOM   2331  C  CZ2   . TRP A 1  334  ? -57.065 62.377  72.430  1.00 16.00 ? 332  TRP A CZ2   1 
ATOM   2332  C  CZ3   . TRP A 1  334  ? -58.184 63.732  74.100  1.00 17.51 ? 332  TRP A CZ3   1 
ATOM   2333  C  CH2   . TRP A 1  334  ? -57.014 63.177  73.548  1.00 16.55 ? 332  TRP A CH2   1 
ATOM   2334  N  N     . ASN A 1  335  ? -62.128 59.368  73.009  1.00 16.78 ? 333  ASN A N     1 
ATOM   2335  C  CA    . ASN A 1  335  ? -61.613 58.454  74.024  1.00 16.39 ? 333  ASN A CA    1 
ATOM   2336  C  C     . ASN A 1  335  ? -60.113 58.225  73.892  1.00 16.99 ? 333  ASN A C     1 
ATOM   2337  O  O     . ASN A 1  335  ? -59.579 57.265  74.469  1.00 16.50 ? 333  ASN A O     1 
ATOM   2338  C  CB    . ASN A 1  335  ? -62.342 57.110  73.964  1.00 18.49 ? 333  ASN A CB    1 
ATOM   2339  C  CG    . ASN A 1  335  ? -63.672 57.120  74.708  1.00 20.23 ? 333  ASN A CG    1 
ATOM   2340  O  OD1   . ASN A 1  335  ? -63.912 57.946  75.590  1.00 19.02 ? 333  ASN A OD1   1 
ATOM   2341  N  ND2   . ASN A 1  335  ? -64.540 56.172  74.360  1.00 21.74 ? 333  ASN A ND2   1 
ATOM   2342  N  N     . GLY A 1  336  ? -59.423 59.094  73.155  1.00 16.18 ? 334  GLY A N     1 
ATOM   2343  C  CA    . GLY A 1  336  ? -58.007 58.915  72.885  1.00 15.18 ? 334  GLY A CA    1 
ATOM   2344  C  C     . GLY A 1  336  ? -57.050 59.379  73.973  1.00 15.35 ? 334  GLY A C     1 
ATOM   2345  O  O     . GLY A 1  336  ? -55.852 59.104  73.863  1.00 15.59 ? 334  GLY A O     1 
ATOM   2346  N  N     . MET A 1  337  ? -57.516 60.071  75.013  1.00 16.32 ? 335  MET A N     1 
ATOM   2347  C  CA    A MET A 1  337  ? -56.603 60.517  76.060  0.48 15.79 ? 335  MET A CA    1 
ATOM   2348  C  CA    B MET A 1  337  ? -56.595 60.514  76.054  0.52 15.79 ? 335  MET A CA    1 
ATOM   2349  C  C     . MET A 1  337  ? -56.032 59.314  76.809  1.00 15.39 ? 335  MET A C     1 
ATOM   2350  O  O     . MET A 1  337  ? -56.779 58.447  77.284  1.00 15.94 ? 335  MET A O     1 
ATOM   2351  C  CB    A MET A 1  337  ? -57.311 61.466  77.024  0.48 15.81 ? 335  MET A CB    1 
ATOM   2352  C  CB    B MET A 1  337  ? -57.283 61.478  77.013  0.52 15.80 ? 335  MET A CB    1 
ATOM   2353  C  CG    A MET A 1  337  ? -56.403 62.021  78.104  0.48 16.79 ? 335  MET A CG    1 
ATOM   2354  C  CG    B MET A 1  337  ? -56.439 61.815  78.228  0.52 16.84 ? 335  MET A CG    1 
ATOM   2355  S  SD    A MET A 1  337  ? -55.235 63.193  77.412  0.48 21.22 ? 335  MET A SD    1 
ATOM   2356  S  SD    B MET A 1  337  ? -56.458 63.579  78.511  0.52 20.20 ? 335  MET A SD    1 
ATOM   2357  C  CE    A MET A 1  337  ? -56.255 64.656  77.260  0.48 17.81 ? 335  MET A CE    1 
ATOM   2358  C  CE    B MET A 1  337  ? -55.689 64.114  76.981  0.52 14.75 ? 335  MET A CE    1 
ATOM   2359  N  N     . GLY A 1  338  ? -54.703 59.262  76.911  1.00 15.50 ? 336  GLY A N     1 
ATOM   2360  C  CA    . GLY A 1  338  ? -54.033 58.153  77.549  1.00 17.55 ? 336  GLY A CA    1 
ATOM   2361  C  C     . GLY A 1  338  ? -53.083 58.641  78.628  1.00 16.18 ? 336  GLY A C     1 
ATOM   2362  O  O     . GLY A 1  338  ? -52.726 59.816  78.693  1.00 15.86 ? 336  GLY A O     1 
ATOM   2363  N  N     . PHE A 1  339  ? -52.715 57.713  79.507  1.00 14.93 ? 337  PHE A N     1 
ATOM   2364  C  CA    . PHE A 1  339  ? -51.948 58.045  80.705  1.00 15.63 ? 337  PHE A CA    1 
ATOM   2365  C  C     . PHE A 1  339  ? -51.160 56.825  81.160  1.00 17.59 ? 337  PHE A C     1 
ATOM   2366  O  O     . PHE A 1  339  ? -51.724 55.738  81.305  1.00 17.11 ? 337  PHE A O     1 
ATOM   2367  C  CB    . PHE A 1  339  ? -52.908 58.489  81.817  1.00 15.52 ? 337  PHE A CB    1 
ATOM   2368  C  CG    . PHE A 1  339  ? -52.255 59.194  82.958  1.00 15.37 ? 337  PHE A CG    1 
ATOM   2369  C  CD1   . PHE A 1  339  ? -51.960 60.549  82.872  1.00 15.62 ? 337  PHE A CD1   1 
ATOM   2370  C  CD2   . PHE A 1  339  ? -51.975 58.516  84.138  1.00 16.00 ? 337  PHE A CD2   1 
ATOM   2371  C  CE1   . PHE A 1  339  ? -51.379 61.214  83.940  1.00 16.37 ? 337  PHE A CE1   1 
ATOM   2372  C  CE2   . PHE A 1  339  ? -51.395 59.184  85.214  1.00 17.18 ? 337  PHE A CE2   1 
ATOM   2373  C  CZ    . PHE A 1  339  ? -51.104 60.539  85.101  1.00 16.90 ? 337  PHE A CZ    1 
ATOM   2374  N  N     . VAL A 1  340  ? -49.878 57.020  81.440  1.00 15.62 ? 338  VAL A N     1 
ATOM   2375  C  CA    . VAL A 1  340  ? -49.005 55.952  81.920  1.00 14.76 ? 338  VAL A CA    1 
ATOM   2376  C  C     . VAL A 1  340  ? -49.025 55.894  83.438  1.00 14.15 ? 338  VAL A C     1 
ATOM   2377  O  O     . VAL A 1  340  ? -48.988 56.935  84.114  1.00 17.38 ? 338  VAL A O     1 
ATOM   2378  C  CB    . VAL A 1  340  ? -47.566 56.176  81.420  1.00 15.71 ? 338  VAL A CB    1 
ATOM   2379  C  CG1   . VAL A 1  340  ? -46.637 55.111  82.001  1.00 15.34 ? 338  VAL A CG1   1 
ATOM   2380  C  CG2   . VAL A 1  340  ? -47.524 56.150  79.917  1.00 17.45 ? 338  VAL A CG2   1 
ATOM   2381  N  N     . VAL A 1  341  ? -49.050 54.679  83.987  1.00 14.19 ? 339  VAL A N     1 
ATOM   2382  C  CA    . VAL A 1  341  ? -48.760 54.458  85.401  1.00 13.87 ? 339  VAL A CA    1 
ATOM   2383  C  C     . VAL A 1  341  ? -47.632 53.439  85.519  1.00 15.25 ? 339  VAL A C     1 
ATOM   2384  O  O     . VAL A 1  341  ? -47.535 52.501  84.719  1.00 16.18 ? 339  VAL A O     1 
ATOM   2385  C  CB    . VAL A 1  341  ? -49.996 54.007  86.206  1.00 18.10 ? 339  VAL A CB    1 
ATOM   2386  C  CG1   . VAL A 1  341  ? -51.108 55.035  86.057  1.00 18.71 ? 339  VAL A CG1   1 
ATOM   2387  C  CG2   . VAL A 1  341  ? -50.486 52.644  85.753  1.00 21.80 ? 339  VAL A CG2   1 
ATOM   2388  N  N     . GLN A 1  342  ? -46.766 53.650  86.507  1.00 15.06 ? 340  GLN A N     1 
ATOM   2389  C  CA    . GLN A 1  342  ? -45.513 52.912  86.663  1.00 16.86 ? 340  GLN A CA    1 
ATOM   2390  C  C     . GLN A 1  342  ? -45.654 51.902  87.796  1.00 15.75 ? 340  GLN A C     1 
ATOM   2391  O  O     . GLN A 1  342  ? -45.768 52.283  88.969  1.00 18.08 ? 340  GLN A O     1 
ATOM   2392  C  CB    . GLN A 1  342  ? -44.363 53.873  86.937  1.00 14.28 ? 340  GLN A CB    1 
ATOM   2393  C  CG    . GLN A 1  342  ? -44.143 54.904  85.837  1.00 14.15 ? 340  GLN A CG    1 
ATOM   2394  C  CD    . GLN A 1  342  ? -43.581 56.212  86.373  1.00 14.82 ? 340  GLN A CD    1 
ATOM   2395  O  OE1   . GLN A 1  342  ? -44.100 56.786  87.337  1.00 16.60 ? 340  GLN A OE1   1 
ATOM   2396  N  NE2   . GLN A 1  342  ? -42.534 56.709  85.724  1.00 14.96 ? 340  GLN A NE2   1 
ATOM   2397  N  N     . ALA A 1  343  ? -45.629 50.616  87.441  1.00 14.01 ? 341  ALA A N     1 
ATOM   2398  C  CA    . ALA A 1  343  ? -45.837 49.558  88.423  1.00 15.60 ? 341  ALA A CA    1 
ATOM   2399  C  C     . ALA A 1  343  ? -44.706 49.456  89.438  1.00 19.96 ? 341  ALA A C     1 
ATOM   2400  O  O     . ALA A 1  343  ? -44.892 48.841  90.496  1.00 18.74 ? 341  ALA A O     1 
ATOM   2401  C  CB    . ALA A 1  343  ? -46.024 48.219  87.712  1.00 19.77 ? 341  ALA A CB    1 
ATOM   2402  N  N     . TYR A 1  344  ? -43.536 50.026  89.161  1.00 16.54 ? 342  TYR A N     1 
ATOM   2403  C  CA    . TYR A 1  344  ? -42.530 50.013  90.212  1.00 17.07 ? 342  TYR A CA    1 
ATOM   2404  C  C     . TYR A 1  344  ? -42.825 51.017  91.309  1.00 17.86 ? 342  TYR A C     1 
ATOM   2405  O  O     . TYR A 1  344  ? -42.104 51.042  92.304  1.00 17.71 ? 342  TYR A O     1 
ATOM   2406  C  CB    . TYR A 1  344  ? -41.118 50.228  89.636  1.00 16.93 ? 342  TYR A CB    1 
ATOM   2407  C  CG    . TYR A 1  344  ? -40.684 51.610  89.123  1.00 16.29 ? 342  TYR A CG    1 
ATOM   2408  C  CD1   . TYR A 1  344  ? -41.544 52.701  89.041  1.00 16.64 ? 342  TYR A CD1   1 
ATOM   2409  C  CD2   . TYR A 1  344  ? -39.359 51.789  88.700  1.00 16.05 ? 342  TYR A CD2   1 
ATOM   2410  C  CE1   . TYR A 1  344  ? -41.092 53.938  88.550  1.00 15.10 ? 342  TYR A CE1   1 
ATOM   2411  C  CE2   . TYR A 1  344  ? -38.911 52.984  88.213  1.00 18.13 ? 342  TYR A CE2   1 
ATOM   2412  C  CZ    . TYR A 1  344  ? -39.763 54.061  88.141  1.00 16.62 ? 342  TYR A CZ    1 
ATOM   2413  O  OH    . TYR A 1  344  ? -39.275 55.243  87.657  1.00 16.40 ? 342  TYR A OH    1 
ATOM   2414  N  N     . GLY A 1  345  ? -43.878 51.818  91.164  1.00 18.38 ? 343  GLY A N     1 
ATOM   2415  C  CA    . GLY A 1  345  ? -44.206 52.828  92.151  1.00 18.21 ? 343  GLY A CA    1 
ATOM   2416  C  C     . GLY A 1  345  ? -45.193 52.306  93.183  1.00 17.39 ? 343  GLY A C     1 
ATOM   2417  O  O     . GLY A 1  345  ? -46.144 51.591  92.858  1.00 18.64 ? 343  GLY A O     1 
ATOM   2418  N  N     . LYS A 1  346  ? -44.944 52.670  94.441  1.00 16.52 ? 344  LYS A N     1 
ATOM   2419  C  CA    . LYS A 1  346  ? -45.779 52.199  95.541  1.00 18.71 ? 344  LYS A CA    1 
ATOM   2420  C  C     . LYS A 1  346  ? -47.194 52.737  95.470  1.00 20.50 ? 344  LYS A C     1 
ATOM   2421  O  O     . LYS A 1  346  ? -48.099 52.166  96.089  1.00 19.49 ? 344  LYS A O     1 
ATOM   2422  C  CB    . LYS A 1  346  ? -45.156 52.596  96.873  1.00 18.87 ? 344  LYS A CB    1 
ATOM   2423  C  CG    . LYS A 1  346  ? -43.784 51.986  97.078  1.00 18.41 ? 344  LYS A CG    1 
ATOM   2424  C  CD    . LYS A 1  346  ? -43.147 52.501  98.349  1.00 19.66 ? 344  LYS A CD    1 
ATOM   2425  C  CE    . LYS A 1  346  ? -41.918 51.658  98.696  1.00 19.03 ? 344  LYS A CE    1 
ATOM   2426  N  NZ    . LYS A 1  346  ? -41.233 52.204  99.909  1.00 21.23 ? 344  LYS A NZ    1 
ATOM   2427  N  N     . ARG A 1  347  ? -47.408 53.834  94.756  1.00 17.14 ? 345  ARG A N     1 
ATOM   2428  C  CA    . ARG A 1  347  ? -48.752 54.391  94.629  1.00 17.05 ? 345  ARG A CA    1 
ATOM   2429  C  C     . ARG A 1  347  ? -49.553 53.796  93.474  1.00 18.45 ? 345  ARG A C     1 
ATOM   2430  O  O     . ARG A 1  347  ? -50.745 54.095  93.367  1.00 19.27 ? 345  ARG A O     1 
ATOM   2431  C  CB    . ARG A 1  347  ? -48.672 55.914  94.458  1.00 17.63 ? 345  ARG A CB    1 
ATOM   2432  C  CG    . ARG A 1  347  ? -48.177 56.624  95.721  1.00 17.51 ? 345  ARG A CG    1 
ATOM   2433  C  CD    . ARG A 1  347  ? -47.747 58.045  95.431  1.00 16.00 ? 345  ARG A CD    1 
ATOM   2434  N  NE    . ARG A 1  347  ? -46.510 58.093  94.654  1.00 17.91 ? 345  ARG A NE    1 
ATOM   2435  C  CZ    . ARG A 1  347  ? -46.025 59.203  94.108  1.00 16.01 ? 345  ARG A CZ    1 
ATOM   2436  N  NH1   . ARG A 1  347  ? -46.626 60.373  94.272  1.00 15.92 ? 345  ARG A NH1   1 
ATOM   2437  N  NH2   . ARG A 1  347  ? -44.911 59.137  93.374  1.00 15.29 ? 345  ARG A NH2   1 
ATOM   2438  N  N     . CYS A 1  348  ? -48.954 52.939  92.641  1.00 16.94 ? 346  CYS A N     1 
ATOM   2439  C  CA    . CYS A 1  348  ? -49.586 52.519  91.384  1.00 18.00 ? 346  CYS A CA    1 
ATOM   2440  C  C     . CYS A 1  348  ? -51.027 52.023  91.529  1.00 17.98 ? 346  CYS A C     1 
ATOM   2441  O  O     . CYS A 1  348  ? -51.899 52.515  90.793  1.00 16.81 ? 346  CYS A O     1 
ATOM   2442  C  CB    . CYS A 1  348  ? -48.722 51.443  90.703  1.00 19.40 ? 346  CYS A CB    1 
ATOM   2443  S  SG    . CYS A 1  348  ? -49.163 51.186  88.976  1.00 20.65 ? 346  CYS A SG    1 
ATOM   2444  N  N     . PRO A 1  349  ? -51.352 51.060  92.398  1.00 18.45 ? 347  PRO A N     1 
ATOM   2445  C  CA    . PRO A 1  349  ? -52.757 50.608  92.449  1.00 18.07 ? 347  PRO A CA    1 
ATOM   2446  C  C     . PRO A 1  349  ? -53.712 51.707  92.872  1.00 18.04 ? 347  PRO A C     1 
ATOM   2447  O  O     . PRO A 1  349  ? -54.856 51.733  92.404  1.00 19.12 ? 347  PRO A O     1 
ATOM   2448  C  CB    . PRO A 1  349  ? -52.727 49.449  93.459  1.00 19.79 ? 347  PRO A CB    1 
ATOM   2449  C  CG    . PRO A 1  349  ? -51.512 49.666  94.264  1.00 20.64 ? 347  PRO A CG    1 
ATOM   2450  C  CD    . PRO A 1  349  ? -50.515 50.354  93.387  1.00 19.88 ? 347  PRO A CD    1 
ATOM   2451  N  N     . PHE A 1  350  ? -53.271 52.623  93.735  1.00 19.77 ? 348  PHE A N     1 
ATOM   2452  C  CA    . PHE A 1  350  ? -54.135 53.716  94.173  1.00 20.64 ? 348  PHE A CA    1 
ATOM   2453  C  C     . PHE A 1  350  ? -54.287 54.762  93.085  1.00 17.66 ? 348  PHE A C     1 
ATOM   2454  O  O     . PHE A 1  350  ? -55.349 55.386  92.959  1.00 18.96 ? 348  PHE A O     1 
ATOM   2455  C  CB    . PHE A 1  350  ? -53.563 54.321  95.454  1.00 17.24 ? 348  PHE A CB    1 
ATOM   2456  C  CG    . PHE A 1  350  ? -53.238 53.292  96.481  1.00 22.36 ? 348  PHE A CG    1 
ATOM   2457  C  CD1   . PHE A 1  350  ? -54.233 52.779  97.290  1.00 21.37 ? 348  PHE A CD1   1 
ATOM   2458  C  CD2   . PHE A 1  350  ? -51.953 52.805  96.608  1.00 21.96 ? 348  PHE A CD2   1 
ATOM   2459  C  CE1   . PHE A 1  350  ? -53.945 51.801  98.225  1.00 25.62 ? 348  PHE A CE1   1 
ATOM   2460  C  CE2   . PHE A 1  350  ? -51.657 51.814  97.538  1.00 20.70 ? 348  PHE A CE2   1 
ATOM   2461  C  CZ    . PHE A 1  350  ? -52.654 51.321  98.350  1.00 26.11 ? 348  PHE A CZ    1 
ATOM   2462  N  N     . VAL A 1  351  ? -53.242 54.950  92.280  1.00 17.26 ? 349  VAL A N     1 
ATOM   2463  C  CA    . VAL A 1  351  ? -53.356 55.807  91.107  1.00 16.71 ? 349  VAL A CA    1 
ATOM   2464  C  C     . VAL A 1  351  ? -54.369 55.222  90.135  1.00 17.95 ? 349  VAL A C     1 
ATOM   2465  O  O     . VAL A 1  351  ? -55.193 55.945  89.564  1.00 18.00 ? 349  VAL A O     1 
ATOM   2466  C  CB    . VAL A 1  351  ? -51.975 55.989  90.449  1.00 16.01 ? 349  VAL A CB    1 
ATOM   2467  C  CG1   . VAL A 1  351  ? -52.117 56.805  89.169  1.00 16.18 ? 349  VAL A CG1   1 
ATOM   2468  C  CG2   . VAL A 1  351  ? -51.025 56.680  91.402  1.00 18.33 ? 349  VAL A CG2   1 
ATOM   2469  N  N     . LEU A 1  352  ? -54.336 53.896  89.946  1.00 18.21 ? 350  LEU A N     1 
ATOM   2470  C  CA    . LEU A 1  352  ? -55.294 53.263  89.055  1.00 15.97 ? 350  LEU A CA    1 
ATOM   2471  C  C     . LEU A 1  352  ? -56.713 53.410  89.579  1.00 17.93 ? 350  LEU A C     1 
ATOM   2472  O  O     . LEU A 1  352  ? -57.643 53.633  88.796  1.00 18.67 ? 350  LEU A O     1 
ATOM   2473  C  CB    . LEU A 1  352  ? -54.941 51.793  88.857  1.00 19.22 ? 350  LEU A CB    1 
ATOM   2474  C  CG    . LEU A 1  352  ? -53.688 51.600  88.002  1.00 18.89 ? 350  LEU A CG    1 
ATOM   2475  C  CD1   . LEU A 1  352  ? -53.225 50.146  88.028  1.00 20.62 ? 350  LEU A CD1   1 
ATOM   2476  C  CD2   . LEU A 1  352  ? -53.959 52.051  86.571  1.00 19.76 ? 350  LEU A CD2   1 
ATOM   2477  N  N     . ASP A 1  353  ? -56.908 53.275  90.898  1.00 19.93 ? 351  ASP A N     1 
ATOM   2478  C  CA    . ASP A 1  353  ? -58.241 53.504  91.456  1.00 18.67 ? 351  ASP A CA    1 
ATOM   2479  C  C     . ASP A 1  353  ? -58.724 54.907  91.131  1.00 18.31 ? 351  ASP A C     1 
ATOM   2480  O  O     . ASP A 1  353  ? -59.898 55.104  90.791  1.00 18.69 ? 351  ASP A O     1 
ATOM   2481  C  CB    . ASP A 1  353  ? -58.247 53.304  92.970  1.00 20.92 ? 351  ASP A CB    1 
ATOM   2482  C  CG    . ASP A 1  353  ? -58.081 51.856  93.375  1.00 21.43 ? 351  ASP A CG    1 
ATOM   2483  O  OD1   . ASP A 1  353  ? -58.380 50.953  92.576  1.00 24.71 ? 351  ASP A OD1   1 
ATOM   2484  O  OD2   . ASP A 1  353  ? -57.656 51.633  94.511  1.00 23.55 ? 351  ASP A OD2   1 
ATOM   2485  N  N     . PHE A 1  354  ? -57.829 55.893  91.238  1.00 17.78 ? 352  PHE A N     1 
ATOM   2486  C  CA    . PHE A 1  354  ? -58.192 57.272  90.925  1.00 16.87 ? 352  PHE A CA    1 
ATOM   2487  C  C     . PHE A 1  354  ? -58.557 57.419  89.454  1.00 17.15 ? 352  PHE A C     1 
ATOM   2488  O  O     . PHE A 1  354  ? -59.563 58.047  89.112  1.00 19.12 ? 352  PHE A O     1 
ATOM   2489  C  CB    . PHE A 1  354  ? -57.040 58.217  91.293  1.00 17.61 ? 352  PHE A CB    1 
ATOM   2490  C  CG    . PHE A 1  354  ? -57.221 59.600  90.762  1.00 20.04 ? 352  PHE A CG    1 
ATOM   2491  C  CD1   . PHE A 1  354  ? -57.953 60.542  91.474  1.00 21.39 ? 352  PHE A CD1   1 
ATOM   2492  C  CD2   . PHE A 1  354  ? -56.699 59.955  89.528  1.00 19.22 ? 352  PHE A CD2   1 
ATOM   2493  C  CE1   . PHE A 1  354  ? -58.143 61.824  90.958  1.00 23.24 ? 352  PHE A CE1   1 
ATOM   2494  C  CE2   . PHE A 1  354  ? -56.895 61.224  89.009  1.00 20.44 ? 352  PHE A CE2   1 
ATOM   2495  C  CZ    . PHE A 1  354  ? -57.612 62.155  89.724  1.00 19.81 ? 352  PHE A CZ    1 
ATOM   2496  N  N     . ILE A 1  355  ? -57.729 56.863  88.568  1.00 16.27 ? 353  ILE A N     1 
ATOM   2497  C  CA    . ILE A 1  355  ? -57.968 56.986  87.132  1.00 15.34 ? 353  ILE A CA    1 
ATOM   2498  C  C     . ILE A 1  355  ? -59.249 56.274  86.727  1.00 18.37 ? 353  ILE A C     1 
ATOM   2499  O  O     . ILE A 1  355  ? -60.020 56.782  85.905  1.00 17.34 ? 353  ILE A O     1 
ATOM   2500  C  CB    . ILE A 1  355  ? -56.768 56.436  86.348  1.00 15.02 ? 353  ILE A CB    1 
ATOM   2501  C  CG1   . ILE A 1  355  ? -55.543 57.318  86.584  1.00 15.88 ? 353  ILE A CG1   1 
ATOM   2502  C  CG2   . ILE A 1  355  ? -57.120 56.348  84.866  1.00 16.20 ? 353  ILE A CG2   1 
ATOM   2503  C  CD1   . ILE A 1  355  ? -54.266 56.671  86.068  1.00 17.26 ? 353  ILE A CD1   1 
ATOM   2504  N  N     . ILE A 1  356  ? -59.473 55.064  87.249  1.00 18.14 ? 354  ILE A N     1 
ATOM   2505  C  CA    . ILE A 1  356  ? -60.690 54.336  86.898  1.00 18.14 ? 354  ILE A CA    1 
ATOM   2506  C  C     . ILE A 1  356  ? -61.911 55.125  87.340  1.00 17.50 ? 354  ILE A C     1 
ATOM   2507  O  O     . ILE A 1  356  ? -62.905 55.226  86.614  1.00 17.67 ? 354  ILE A O     1 
ATOM   2508  C  CB    . ILE A 1  356  ? -60.662 52.920  87.515  1.00 16.60 ? 354  ILE A CB    1 
ATOM   2509  C  CG1   . ILE A 1  356  ? -59.617 52.073  86.791  1.00 19.87 ? 354  ILE A CG1   1 
ATOM   2510  C  CG2   . ILE A 1  356  ? -62.061 52.260  87.487  1.00 20.80 ? 354  ILE A CG2   1 
ATOM   2511  C  CD1   . ILE A 1  356  ? -59.121 50.863  87.583  1.00 20.81 ? 354  ILE A CD1   1 
ATOM   2512  N  N     . ASP A 1  357  ? -61.838 55.731  88.522  1.00 17.11 ? 355  ASP A N     1 
ATOM   2513  C  CA    . ASP A 1  357  ? -62.958 56.540  88.985  1.00 19.43 ? 355  ASP A CA    1 
ATOM   2514  C  C     . ASP A 1  357  ? -63.127 57.785  88.122  1.00 19.80 ? 355  ASP A C     1 
ATOM   2515  O  O     . ASP A 1  357  ? -64.259 58.180  87.806  1.00 18.32 ? 355  ASP A O     1 
ATOM   2516  C  CB    . ASP A 1  357  ? -62.755 56.922  90.448  1.00 19.46 ? 355  ASP A CB    1 
ATOM   2517  C  CG    . ASP A 1  357  ? -63.785 57.912  90.931  1.00 20.85 ? 355  ASP A CG    1 
ATOM   2518  O  OD1   . ASP A 1  357  ? -64.912 57.473  91.239  1.00 23.81 ? 355  ASP A OD1   1 
ATOM   2519  O  OD2   . ASP A 1  357  ? -63.484 59.123  90.985  1.00 19.85 ? 355  ASP A OD2   1 
ATOM   2520  N  N     . LEU A 1  358  ? -62.013 58.408  87.727  1.00 17.48 ? 356  LEU A N     1 
ATOM   2521  C  CA    . LEU A 1  358  ? -62.089 59.571  86.847  1.00 16.71 ? 356  LEU A CA    1 
ATOM   2522  C  C     . LEU A 1  358  ? -62.705 59.193  85.512  1.00 17.18 ? 356  LEU A C     1 
ATOM   2523  O  O     . LEU A 1  358  ? -63.490 59.956  84.937  1.00 17.60 ? 356  LEU A O     1 
ATOM   2524  C  CB    . LEU A 1  358  ? -60.691 60.165  86.643  1.00 15.65 ? 356  LEU A CB    1 
ATOM   2525  C  CG    . LEU A 1  358  ? -60.578 61.304  85.627  1.00 16.35 ? 356  LEU A CG    1 
ATOM   2526  C  CD1   . LEU A 1  358  ? -61.453 62.485  86.037  1.00 19.16 ? 356  LEU A CD1   1 
ATOM   2527  C  CD2   . LEU A 1  358  ? -59.083 61.734  85.471  1.00 17.30 ? 356  LEU A CD2   1 
ATOM   2528  N  N     . ALA A 1  359  ? -62.374 58.003  85.011  1.00 17.06 ? 357  ALA A N     1 
ATOM   2529  C  CA    . ALA A 1  359  ? -62.974 57.546  83.770  1.00 16.77 ? 357  ALA A CA    1 
ATOM   2530  C  C     . ALA A 1  359  ? -64.479 57.380  83.938  1.00 17.82 ? 357  ALA A C     1 
ATOM   2531  O  O     . ALA A 1  359  ? -65.253 57.734  83.047  1.00 18.92 ? 357  ALA A O     1 
ATOM   2532  C  CB    . ALA A 1  359  ? -62.325 56.235  83.327  1.00 18.89 ? 357  ALA A CB    1 
ATOM   2533  N  N     . ARG A 1  360  ? -64.911 56.850  85.082  1.00 17.61 ? 358  ARG A N     1 
ATOM   2534  C  CA    . ARG A 1  360  ? -66.346 56.700  85.326  1.00 18.74 ? 358  ARG A CA    1 
ATOM   2535  C  C     . ARG A 1  360  ? -67.036 58.056  85.411  1.00 21.70 ? 358  ARG A C     1 
ATOM   2536  O  O     . ARG A 1  360  ? -68.082 58.275  84.781  1.00 21.37 ? 358  ARG A O     1 
ATOM   2537  C  CB    . ARG A 1  360  ? -66.584 55.903  86.607  1.00 20.07 ? 358  ARG A CB    1 
ATOM   2538  C  CG    . ARG A 1  360  ? -66.190 54.437  86.531  1.00 24.66 ? 358  ARG A CG    1 
ATOM   2539  C  CD    . ARG A 1  360  ? -66.775 53.656  87.712  1.00 26.42 ? 358  ARG A CD    1 
ATOM   2540  N  NE    . ARG A 1  360  ? -66.050 52.405  87.906  1.00 30.25 ? 358  ARG A NE    1 
ATOM   2541  C  CZ    . ARG A 1  360  ? -66.269 51.304  87.199  1.00 34.24 ? 358  ARG A CZ    1 
ATOM   2542  N  NH1   . ARG A 1  360  ? -67.237 51.244  86.295  1.00 34.52 ? 358  ARG A NH1   1 
ATOM   2543  N  NH2   . ARG A 1  360  ? -65.502 50.238  87.405  1.00 32.61 ? 358  ARG A NH2   1 
ATOM   2544  N  N     . ARG A 1  361  ? -66.463 58.979  86.186  1.00 18.95 ? 359  ARG A N     1 
ATOM   2545  C  CA    . ARG A 1  361  ? -67.055 60.308  86.353  1.00 19.77 ? 359  ARG A CA    1 
ATOM   2546  C  C     . ARG A 1  361  ? -67.121 61.061  85.033  1.00 19.47 ? 359  ARG A C     1 
ATOM   2547  O  O     . ARG A 1  361  ? -68.121 61.719  84.725  1.00 20.68 ? 359  ARG A O     1 
ATOM   2548  C  CB    . ARG A 1  361  ? -66.231 61.124  87.353  1.00 21.99 ? 359  ARG A CB    1 
ATOM   2549  C  CG    . ARG A 1  361  ? -66.325 60.679  88.788  1.00 25.06 ? 359  ARG A CG    1 
ATOM   2550  C  CD    . ARG A 1  361  ? -65.617 61.684  89.668  1.00 24.16 ? 359  ARG A CD    1 
ATOM   2551  N  NE    . ARG A 1  361  ? -64.162 61.554  89.629  1.00 22.20 ? 359  ARG A NE    1 
ATOM   2552  C  CZ    . ARG A 1  361  ? -63.320 62.549  89.386  1.00 22.96 ? 359  ARG A CZ    1 
ATOM   2553  N  NH1   . ARG A 1  361  ? -63.751 63.754  89.051  1.00 21.72 ? 359  ARG A NH1   1 
ATOM   2554  N  NH2   . ARG A 1  361  ? -62.011 62.331  89.491  1.00 20.18 ? 359  ARG A NH2   1 
ATOM   2555  N  N     . SER A 1  362  ? -66.033 61.028  84.263  1.00 18.31 ? 360  SER A N     1 
ATOM   2556  C  CA    . SER A 1  362  ? -65.975 61.772  83.013  1.00 17.92 ? 360  SER A CA    1 
ATOM   2557  C  C     . SER A 1  362  ? -66.657 61.050  81.862  1.00 19.58 ? 360  SER A C     1 
ATOM   2558  O  O     . SER A 1  362  ? -66.959 61.680  80.846  1.00 20.66 ? 360  SER A O     1 
ATOM   2559  C  CB    . SER A 1  362  ? -64.516 62.035  82.634  1.00 18.02 ? 360  SER A CB    1 
ATOM   2560  O  OG    . SER A 1  362  ? -63.858 60.806  82.344  1.00 17.89 ? 360  SER A OG    1 
ATOM   2561  N  N     . GLY A 1  363  ? -66.898 59.750  81.993  1.00 20.09 ? 361  GLY A N     1 
ATOM   2562  C  CA    . GLY A 1  363  ? -67.388 58.993  80.863  1.00 21.32 ? 361  GLY A CA    1 
ATOM   2563  C  C     . GLY A 1  363  ? -66.402 58.805  79.738  1.00 22.38 ? 361  GLY A C     1 
ATOM   2564  O  O     . GLY A 1  363  ? -66.819 58.435  78.632  1.00 22.33 ? 361  GLY A O     1 
ATOM   2565  N  N     . ARG A 1  364  ? -65.117 59.062  79.984  1.00 18.44 ? 362  ARG A N     1 
ATOM   2566  C  CA    . ARG A 1  364  ? -64.046 58.896  79.004  1.00 20.21 ? 362  ARG A CA    1 
ATOM   2567  C  C     . ARG A 1  364  ? -63.334 57.578  79.268  1.00 19.78 ? 362  ARG A C     1 
ATOM   2568  O  O     . ARG A 1  364  ? -62.916 57.312  80.401  1.00 20.61 ? 362  ARG A O     1 
ATOM   2569  C  CB    . ARG A 1  364  ? -63.018 60.027  79.084  1.00 20.39 ? 362  ARG A CB    1 
ATOM   2570  C  CG    . ARG A 1  364  ? -63.586 61.425  79.189  1.00 25.56 ? 362  ARG A CG    1 
ATOM   2571  C  CD    . ARG A 1  364  ? -63.380 62.236  77.939  1.00 19.16 ? 362  ARG A CD    1 
ATOM   2572  N  NE    . ARG A 1  364  ? -64.176 63.458  78.009  1.00 17.48 ? 362  ARG A NE    1 
ATOM   2573  C  CZ    . ARG A 1  364  ? -63.686 64.687  78.125  1.00 17.02 ? 362  ARG A CZ    1 
ATOM   2574  N  NH1   . ARG A 1  364  ? -62.376 64.935  78.054  1.00 15.87 ? 362  ARG A NH1   1 
ATOM   2575  N  NH2   . ARG A 1  364  ? -64.530 65.698  78.295  1.00 17.09 ? 362  ARG A NH2   1 
ATOM   2576  N  N     . ARG A 1  365  ? -63.172 56.771  78.225  1.00 17.42 ? 363  ARG A N     1 
ATOM   2577  C  CA    . ARG A 1  365  ? -62.483 55.490  78.361  1.00 17.98 ? 363  ARG A CA    1 
ATOM   2578  C  C     . ARG A 1  365  ? -60.983 55.756  78.304  1.00 18.43 ? 363  ARG A C     1 
ATOM   2579  O  O     . ARG A 1  365  ? -60.344 55.692  77.250  1.00 19.23 ? 363  ARG A O     1 
ATOM   2580  C  CB    . ARG A 1  365  ? -62.928 54.516  77.283  1.00 19.23 ? 363  ARG A CB    1 
ATOM   2581  C  CG    . ARG A 1  365  ? -62.383 53.121  77.504  1.00 18.46 ? 363  ARG A CG    1 
ATOM   2582  C  CD    . ARG A 1  365  ? -63.238 52.075  76.835  1.00 21.68 ? 363  ARG A CD    1 
ATOM   2583  N  NE    . ARG A 1  365  ? -62.737 50.745  77.162  1.00 20.95 ? 363  ARG A NE    1 
ATOM   2584  C  CZ    . ARG A 1  365  ? -62.007 50.006  76.340  1.00 20.69 ? 363  ARG A CZ    1 
ATOM   2585  N  NH1   . ARG A 1  365  ? -61.725 50.411  75.111  1.00 19.47 ? 363  ARG A NH1   1 
ATOM   2586  N  NH2   . ARG A 1  365  ? -61.558 48.830  76.757  1.00 20.50 ? 363  ARG A NH2   1 
ATOM   2587  N  N     . ILE A 1  366  ? -60.407 56.050  79.466  1.00 16.91 ? 364  ILE A N     1 
ATOM   2588  C  CA    . ILE A 1  366  ? -59.009 56.455  79.517  1.00 16.62 ? 364  ILE A CA    1 
ATOM   2589  C  C     . ILE A 1  366  ? -58.121 55.293  79.097  1.00 16.44 ? 364  ILE A C     1 
ATOM   2590  O  O     . ILE A 1  366  ? -58.288 54.159  79.556  1.00 17.51 ? 364  ILE A O     1 
ATOM   2591  C  CB    . ILE A 1  366  ? -58.661 56.969  80.919  1.00 15.05 ? 364  ILE A CB    1 
ATOM   2592  C  CG1   . ILE A 1  366  ? -59.491 58.230  81.218  1.00 17.31 ? 364  ILE A CG1   1 
ATOM   2593  C  CG2   . ILE A 1  366  ? -57.162 57.253  81.034  1.00 17.72 ? 364  ILE A CG2   1 
ATOM   2594  C  CD1   . ILE A 1  366  ? -59.380 58.707  82.645  1.00 17.10 ? 364  ILE A CD1   1 
ATOM   2595  N  N     . MET A 1  367  ? -57.184 55.569  78.195  1.00 16.85 ? 365  MET A N     1 
ATOM   2596  C  CA    . MET A 1  367  ? -56.204 54.572  77.787  1.00 17.21 ? 365  MET A CA    1 
ATOM   2597  C  C     . MET A 1  367  ? -55.096 54.567  78.828  1.00 18.39 ? 365  MET A C     1 
ATOM   2598  O  O     . MET A 1  367  ? -54.433 55.584  79.028  1.00 19.54 ? 365  MET A O     1 
ATOM   2599  C  CB    . MET A 1  367  ? -55.653 54.896  76.398  1.00 15.78 ? 365  MET A CB    1 
ATOM   2600  C  CG    . MET A 1  367  ? -56.759 55.226  75.361  1.00 16.82 ? 365  MET A CG    1 
ATOM   2601  S  SD    . MET A 1  367  ? -56.146 55.585  73.682  1.00 20.74 ? 365  MET A SD    1 
ATOM   2602  C  CE    . MET A 1  367  ? -56.005 53.951  72.954  1.00 21.90 ? 365  MET A CE    1 
ATOM   2603  N  N     . VAL A 1  368  ? -54.912 53.452  79.516  1.00 16.00 ? 366  VAL A N     1 
ATOM   2604  C  CA    . VAL A 1  368  ? -53.979 53.394  80.634  1.00 14.98 ? 366  VAL A CA    1 
ATOM   2605  C  C     . VAL A 1  368  ? -52.844 52.470  80.233  1.00 16.00 ? 366  VAL A C     1 
ATOM   2606  O  O     . VAL A 1  368  ? -53.049 51.261  80.063  1.00 16.93 ? 366  VAL A O     1 
ATOM   2607  C  CB    . VAL A 1  368  ? -54.653 52.919  81.926  1.00 17.37 ? 366  VAL A CB    1 
ATOM   2608  C  CG1   . VAL A 1  368  ? -53.629 52.910  83.062  1.00 18.57 ? 366  VAL A CG1   1 
ATOM   2609  C  CG2   . VAL A 1  368  ? -55.844 53.806  82.255  1.00 18.92 ? 366  VAL A CG2   1 
ATOM   2610  N  N     . ARG A 1  369  ? -51.655 53.044  80.041  1.00 15.30 ? 367  ARG A N     1 
ATOM   2611  C  CA    . ARG A 1  369  ? -50.472 52.258  79.723  1.00 16.60 ? 367  ARG A CA    1 
ATOM   2612  C  C     . ARG A 1  369  ? -49.772 51.898  81.021  1.00 16.69 ? 367  ARG A C     1 
ATOM   2613  O  O     . ARG A 1  369  ? -49.263 52.776  81.727  1.00 16.48 ? 367  ARG A O     1 
ATOM   2614  C  CB    . ARG A 1  369  ? -49.520 53.014  78.795  1.00 16.48 ? 367  ARG A CB    1 
ATOM   2615  C  CG    . ARG A 1  369  ? -48.281 52.183  78.461  1.00 18.21 ? 367  ARG A CG    1 
ATOM   2616  C  CD    . ARG A 1  369  ? -47.139 53.052  77.972  1.00 17.51 ? 367  ARG A CD    1 
ATOM   2617  N  NE    . ARG A 1  369  ? -47.505 53.717  76.732  1.00 17.41 ? 367  ARG A NE    1 
ATOM   2618  C  CZ    . ARG A 1  369  ? -46.995 54.871  76.334  1.00 20.11 ? 367  ARG A CZ    1 
ATOM   2619  N  NH1   . ARG A 1  369  ? -46.100 55.516  77.061  1.00 19.25 ? 367  ARG A NH1   1 
ATOM   2620  N  NH2   . ARG A 1  369  ? -47.399 55.392  75.183  1.00 19.75 ? 367  ARG A NH2   1 
ATOM   2621  N  N     . LEU A 1  370  ? -49.732 50.608  81.318  1.00 16.05 ? 368  LEU A N     1 
ATOM   2622  C  CA    . LEU A 1  370  ? -49.036 50.106  82.490  1.00 16.16 ? 368  LEU A CA    1 
ATOM   2623  C  C     . LEU A 1  370  ? -47.605 49.775  82.080  1.00 15.88 ? 368  LEU A C     1 
ATOM   2624  O  O     . LEU A 1  370  ? -47.385 48.944  81.197  1.00 16.51 ? 368  LEU A O     1 
ATOM   2625  C  CB    . LEU A 1  370  ? -49.774 48.887  83.043  1.00 17.47 ? 368  LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1  370  ? -49.253 48.308  84.352  1.00 16.65 ? 368  LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1  370  ? -49.422 49.306  85.492  1.00 18.97 ? 368  LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1  370  ? -49.939 46.980  84.676  1.00 20.46 ? 368  LEU A CD2   1 
ATOM   2629  N  N     . VAL A 1  371  ? -46.639 50.439  82.705  1.00 15.56 ? 369  VAL A N     1 
ATOM   2630  C  CA    . VAL A 1  371  ? -45.224 50.164  82.491  1.00 16.40 ? 369  VAL A CA    1 
ATOM   2631  C  C     . VAL A 1  371  ? -44.648 49.778  83.838  1.00 16.22 ? 369  VAL A C     1 
ATOM   2632  O  O     . VAL A 1  371  ? -45.272 49.972  84.882  1.00 17.03 ? 369  VAL A O     1 
ATOM   2633  C  CB    . VAL A 1  371  ? -44.457 51.367  81.907  1.00 16.02 ? 369  VAL A CB    1 
ATOM   2634  C  CG1   . VAL A 1  371  ? -45.108 51.874  80.639  1.00 15.67 ? 369  VAL A CG1   1 
ATOM   2635  C  CG2   . VAL A 1  371  ? -44.384 52.483  82.939  1.00 15.42 ? 369  VAL A CG2   1 
ATOM   2636  N  N     . LYS A 1  372  ? -43.431 49.254  83.821  1.00 17.20 ? 370  LYS A N     1 
ATOM   2637  C  CA    . LYS A 1  372  ? -42.823 48.996  85.119  1.00 16.75 ? 370  LYS A CA    1 
ATOM   2638  C  C     . LYS A 1  372  ? -42.172 50.262  85.679  1.00 16.94 ? 370  LYS A C     1 
ATOM   2639  O  O     . LYS A 1  372  ? -42.488 50.677  86.798  1.00 18.45 ? 370  LYS A O     1 
ATOM   2640  C  CB    . LYS A 1  372  ? -41.869 47.806  85.014  1.00 19.34 ? 370  LYS A CB    1 
ATOM   2641  C  CG    . LYS A 1  372  ? -42.689 46.498  84.889  1.00 18.49 ? 370  LYS A CG    1 
ATOM   2642  C  CD    . LYS A 1  372  ? -41.849 45.244  84.807  1.00 19.98 ? 370  LYS A CD    1 
ATOM   2643  C  CE    . LYS A 1  372  ? -42.751 44.050  84.482  1.00 20.05 ? 370  LYS A CE    1 
ATOM   2644  N  NZ    . LYS A 1  372  ? -41.980 42.792  84.313  1.00 19.51 ? 370  LYS A NZ    1 
ATOM   2645  N  N     . GLY A 1  373  ? -41.321 50.931  84.898  1.00 15.86 ? 371  GLY A N     1 
ATOM   2646  C  CA    . GLY A 1  373  ? -40.796 52.231  85.296  1.00 15.46 ? 371  GLY A CA    1 
ATOM   2647  C  C     . GLY A 1  373  ? -39.369 52.449  84.823  1.00 17.65 ? 371  GLY A C     1 
ATOM   2648  O  O     . GLY A 1  373  ? -38.542 51.540  84.916  1.00 18.73 ? 371  GLY A O     1 
ATOM   2649  N  N     . ALA A 1  374  ? -39.044 53.659  84.364  1.00 17.33 ? 372  ALA A N     1 
ATOM   2650  C  CA    . ALA A 1  374  ? -37.789 53.894  83.659  1.00 15.95 ? 372  ALA A CA    1 
ATOM   2651  C  C     . ALA A 1  374  ? -36.749 54.645  84.473  1.00 17.71 ? 372  ALA A C     1 
ATOM   2652  O  O     . ALA A 1  374  ? -35.629 54.828  83.983  1.00 18.25 ? 372  ALA A O     1 
ATOM   2653  C  CB    . ALA A 1  374  ? -38.036 54.672  82.366  1.00 19.07 ? 372  ALA A CB    1 
ATOM   2654  N  N     . TYR A 1  375  ? -37.072 55.089  85.688  1.00 15.89 ? 373  TYR A N     1 
ATOM   2655  C  CA    . TYR A 1  375  ? -36.190 55.985  86.435  1.00 16.29 ? 373  TYR A CA    1 
ATOM   2656  C  C     . TYR A 1  375  ? -35.661 55.359  87.719  1.00 14.51 ? 373  TYR A C     1 
ATOM   2657  O  O     . TYR A 1  375  ? -35.348 56.080  88.670  1.00 16.90 ? 373  TYR A O     1 
ATOM   2658  C  CB    . TYR A 1  375  ? -36.904 57.289  86.786  1.00 15.00 ? 373  TYR A CB    1 
ATOM   2659  C  CG    . TYR A 1  375  ? -37.454 58.038  85.589  1.00 15.61 ? 373  TYR A CG    1 
ATOM   2660  C  CD1   . TYR A 1  375  ? -38.656 57.649  84.993  1.00 15.14 ? 373  TYR A CD1   1 
ATOM   2661  C  CD2   . TYR A 1  375  ? -36.792 59.134  85.074  1.00 18.23 ? 373  TYR A CD2   1 
ATOM   2662  C  CE1   . TYR A 1  375  ? -39.171 58.347  83.905  1.00 16.35 ? 373  TYR A CE1   1 
ATOM   2663  C  CE2   . TYR A 1  375  ? -37.294 59.838  83.995  1.00 17.51 ? 373  TYR A CE2   1 
ATOM   2664  C  CZ    . TYR A 1  375  ? -38.477 59.439  83.414  1.00 19.13 ? 373  TYR A CZ    1 
ATOM   2665  O  OH    . TYR A 1  375  ? -38.975 60.150  82.343  1.00 19.51 ? 373  TYR A OH    1 
ATOM   2666  N  N     . TRP A 1  376  ? -35.552 54.032  87.763  1.00 16.31 ? 374  TRP A N     1 
ATOM   2667  C  CA    . TRP A 1  376  ? -35.350 53.361  89.043  1.00 16.45 ? 374  TRP A CA    1 
ATOM   2668  C  C     . TRP A 1  376  ? -34.093 53.855  89.745  1.00 16.23 ? 374  TRP A C     1 
ATOM   2669  O  O     . TRP A 1  376  ? -34.148 54.266  90.913  1.00 16.30 ? 374  TRP A O     1 
ATOM   2670  C  CB    . TRP A 1  376  ? -35.296 51.841  88.866  1.00 18.68 ? 374  TRP A CB    1 
ATOM   2671  C  CG    . TRP A 1  376  ? -35.144 51.143  90.182  1.00 17.99 ? 374  TRP A CG    1 
ATOM   2672  C  CD1   . TRP A 1  376  ? -36.133 50.877  91.089  1.00 17.68 ? 374  TRP A CD1   1 
ATOM   2673  C  CD2   . TRP A 1  376  ? -33.932 50.651  90.760  1.00 20.60 ? 374  TRP A CD2   1 
ATOM   2674  N  NE1   . TRP A 1  376  ? -35.609 50.245  92.194  1.00 17.87 ? 374  TRP A NE1   1 
ATOM   2675  C  CE2   . TRP A 1  376  ? -34.261 50.087  92.012  1.00 18.60 ? 374  TRP A CE2   1 
ATOM   2676  C  CE3   . TRP A 1  376  ? -32.603 50.609  90.332  1.00 22.09 ? 374  TRP A CE3   1 
ATOM   2677  C  CZ2   . TRP A 1  376  ? -33.305 49.496  92.844  1.00 18.15 ? 374  TRP A CZ2   1 
ATOM   2678  C  CZ3   . TRP A 1  376  ? -31.655 50.021  91.165  1.00 22.93 ? 374  TRP A CZ3   1 
ATOM   2679  C  CH2   . TRP A 1  376  ? -32.012 49.477  92.400  1.00 22.26 ? 374  TRP A CH2   1 
ATOM   2680  N  N     . ASP A 1  377  ? -32.942 53.827  89.057  1.00 18.60 ? 375  ASP A N     1 
ATOM   2681  C  CA    A ASP A 1  377  ? -31.688 54.228  89.694  0.53 20.13 ? 375  ASP A CA    1 
ATOM   2682  C  CA    B ASP A 1  377  ? -31.728 54.204  89.771  0.47 20.14 ? 375  ASP A CA    1 
ATOM   2683  C  C     . ASP A 1  377  ? -31.748 55.675  90.158  1.00 17.29 ? 375  ASP A C     1 
ATOM   2684  O  O     . ASP A 1  377  ? -31.229 56.025  91.222  1.00 17.91 ? 375  ASP A O     1 
ATOM   2685  C  CB    A ASP A 1  377  ? -30.524 54.032  88.721  0.53 23.57 ? 375  ASP A CB    1 
ATOM   2686  C  CB    B ASP A 1  377  ? -30.459 53.845  88.978  0.47 23.75 ? 375  ASP A CB    1 
ATOM   2687  C  CG    A ASP A 1  377  ? -30.319 52.581  88.345  0.53 25.21 ? 375  ASP A CG    1 
ATOM   2688  C  CG    B ASP A 1  377  ? -30.405 54.465  87.595  0.47 24.15 ? 375  ASP A CG    1 
ATOM   2689  O  OD1   A ASP A 1  377  ? -30.037 51.774  89.243  0.53 30.45 ? 375  ASP A OD1   1 
ATOM   2690  O  OD1   B ASP A 1  377  ? -30.858 55.610  87.418  0.47 26.84 ? 375  ASP A OD1   1 
ATOM   2691  O  OD2   A ASP A 1  377  ? -30.452 52.241  87.155  0.53 30.03 ? 375  ASP A OD2   1 
ATOM   2692  O  OD2   B ASP A 1  377  ? -29.852 53.808  86.687  0.47 26.39 ? 375  ASP A OD2   1 
ATOM   2693  N  N     . ALA A 1  378  ? -32.371 56.534  89.349  1.00 16.93 ? 376  ALA A N     1 
ATOM   2694  C  CA    . ALA A 1  378  ? -32.471 57.941  89.711  1.00 18.47 ? 376  ALA A CA    1 
ATOM   2695  C  C     . ALA A 1  378  ? -33.340 58.133  90.943  1.00 16.60 ? 376  ALA A C     1 
ATOM   2696  O  O     . ALA A 1  378  ? -33.057 59.004  91.775  1.00 16.15 ? 376  ALA A O     1 
ATOM   2697  C  CB    . ALA A 1  378  ? -33.025 58.746  88.538  1.00 16.36 ? 376  ALA A CB    1 
ATOM   2698  N  N     . GLU A 1  379  ? -34.407 57.340  91.073  1.00 16.22 ? 377  GLU A N     1 
ATOM   2699  C  CA    . GLU A 1  379  ? -35.273 57.478  92.242  1.00 14.61 ? 377  GLU A CA    1 
ATOM   2700  C  C     . GLU A 1  379  ? -34.556 57.049  93.510  1.00 15.46 ? 377  GLU A C     1 
ATOM   2701  O  O     . GLU A 1  379  ? -34.763 57.651  94.570  1.00 16.25 ? 377  GLU A O     1 
ATOM   2702  C  CB    . GLU A 1  379  ? -36.552 56.660  92.088  1.00 16.38 ? 377  GLU A CB    1 
ATOM   2703  C  CG    . GLU A 1  379  ? -37.439 57.031  90.895  1.00 17.40 ? 377  GLU A CG    1 
ATOM   2704  C  CD    . GLU A 1  379  ? -38.060 58.417  90.971  1.00 18.48 ? 377  GLU A CD    1 
ATOM   2705  O  OE1   . GLU A 1  379  ? -37.909 59.122  92.003  1.00 17.31 ? 377  GLU A OE1   1 
ATOM   2706  O  OE2   . GLU A 1  379  ? -38.715 58.794  89.971  1.00 17.49 ? 377  GLU A OE2   1 
ATOM   2707  N  N     . ILE A 1  380  ? -33.739 55.988  93.433  1.00 16.64 ? 378  ILE A N     1 
ATOM   2708  C  CA    . ILE A 1  380  ? -32.978 55.559  94.612  1.00 17.02 ? 378  ILE A CA    1 
ATOM   2709  C  C     . ILE A 1  380  ? -32.018 56.666  95.045  1.00 18.04 ? 378  ILE A C     1 
ATOM   2710  O  O     . ILE A 1  380  ? -31.972 57.054  96.221  1.00 17.30 ? 378  ILE A O     1 
ATOM   2711  C  CB    . ILE A 1  380  ? -32.229 54.241  94.330  1.00 16.39 ? 378  ILE A CB    1 
ATOM   2712  C  CG1   . ILE A 1  380  ? -33.169 53.114  93.883  1.00 17.99 ? 378  ILE A CG1   1 
ATOM   2713  C  CG2   . ILE A 1  380  ? -31.459 53.781  95.570  1.00 16.70 ? 378  ILE A CG2   1 
ATOM   2714  C  CD1   . ILE A 1  380  ? -34.292 52.792  94.858  1.00 18.09 ? 378  ILE A CD1   1 
ATOM   2715  N  N     . LYS A 1  381  ? -31.252 57.208  94.093  1.00 15.48 ? 379  LYS A N     1 
ATOM   2716  C  CA    . LYS A 1  381  ? -30.317 58.278  94.426  1.00 16.41 ? 379  LYS A CA    1 
ATOM   2717  C  C     . LYS A 1  381  ? -31.037 59.487  95.009  1.00 16.88 ? 379  LYS A C     1 
ATOM   2718  O  O     . LYS A 1  381  ? -30.595 60.056  96.010  1.00 15.96 ? 379  LYS A O     1 
ATOM   2719  C  CB    . LYS A 1  381  ? -29.503 58.682  93.193  1.00 17.88 ? 379  LYS A CB    1 
ATOM   2720  C  CG    . LYS A 1  381  ? -28.560 59.858  93.447  1.00 17.02 ? 379  LYS A CG    1 
ATOM   2721  C  CD    . LYS A 1  381  ? -27.690 60.133  92.219  1.00 17.28 ? 379  LYS A CD    1 
ATOM   2722  C  CE    . LYS A 1  381  ? -26.674 61.242  92.500  1.00 17.30 ? 379  LYS A CE    1 
ATOM   2723  N  NZ    . LYS A 1  381  ? -25.741 61.446  91.330  1.00 15.22 ? 379  LYS A NZ    1 
ATOM   2724  N  N     . ARG A 1  382  ? -32.162 59.879  94.407  1.00 15.78 ? 380  ARG A N     1 
ATOM   2725  C  CA    . ARG A 1  382  ? -32.855 61.085  94.836  1.00 15.69 ? 380  ARG A CA    1 
ATOM   2726  C  C     . ARG A 1  382  ? -33.371 60.962  96.265  1.00 16.34 ? 380  ARG A C     1 
ATOM   2727  O  O     . ARG A 1  382  ? -33.267 61.908  97.051  1.00 17.04 ? 380  ARG A O     1 
ATOM   2728  C  CB    . ARG A 1  382  ? -34.009 61.373  93.872  1.00 18.42 ? 380  ARG A CB    1 
ATOM   2729  C  CG    . ARG A 1  382  ? -34.744 62.667  94.134  1.00 24.53 ? 380  ARG A CG    1 
ATOM   2730  C  CD    . ARG A 1  382  ? -33.977 63.835  93.556  1.00 31.34 ? 380  ARG A CD    1 
ATOM   2731  N  NE    . ARG A 1  382  ? -33.157 64.493  94.562  1.00 33.03 ? 380  ARG A NE    1 
ATOM   2732  C  CZ    . ARG A 1  382  ? -32.176 65.347  94.298  1.00 32.98 ? 380  ARG A CZ    1 
ATOM   2733  N  NH1   . ARG A 1  382  ? -31.810 65.617  93.055  1.00 37.72 ? 380  ARG A NH1   1 
ATOM   2734  N  NH2   . ARG A 1  382  ? -31.560 65.959  95.308  1.00 28.21 ? 380  ARG A NH2   1 
ATOM   2735  N  N     . ALA A 1  383  ? -33.943 59.808  96.622  1.00 17.61 ? 381  ALA A N     1 
ATOM   2736  C  CA    . ALA A 1  383  ? -34.455 59.646  97.981  1.00 16.57 ? 381  ALA A CA    1 
ATOM   2737  C  C     . ALA A 1  383  ? -33.317 59.666  98.990  1.00 18.76 ? 381  ALA A C     1 
ATOM   2738  O  O     . ALA A 1  383  ? -33.451 60.226  100.090 1.00 18.08 ? 381  ALA A O     1 
ATOM   2739  C  CB    . ALA A 1  383  ? -35.247 58.343  98.103  1.00 16.46 ? 381  ALA A CB    1 
ATOM   2740  N  N     . GLN A 1  384  ? -32.183 59.064  98.628  1.00 17.85 ? 382  GLN A N     1 
ATOM   2741  C  CA    . GLN A 1  384  ? -31.041 59.082  99.532  1.00 16.91 ? 382  GLN A CA    1 
ATOM   2742  C  C     . GLN A 1  384  ? -30.513 60.498  99.700  1.00 16.75 ? 382  GLN A C     1 
ATOM   2743  O  O     . GLN A 1  384  ? -30.244 60.932  100.826 1.00 19.00 ? 382  GLN A O     1 
ATOM   2744  C  CB    . GLN A 1  384  ? -29.953 58.140  99.015  1.00 17.87 ? 382  GLN A CB    1 
ATOM   2745  C  CG    . GLN A 1  384  ? -30.343 56.672  99.093  1.00 16.97 ? 382  GLN A CG    1 
ATOM   2746  C  CD    . GLN A 1  384  ? -29.198 55.758  98.717  1.00 20.01 ? 382  GLN A CD    1 
ATOM   2747  O  OE1   . GLN A 1  384  ? -28.251 56.179  98.054  1.00 20.28 ? 382  GLN A OE1   1 
ATOM   2748  N  NE2   . GLN A 1  384  ? -29.271 54.509  99.152  1.00 20.23 ? 382  GLN A NE2   1 
ATOM   2749  N  N     . LEU A 1  385  ? -30.366 61.240  98.596  1.00 17.28 ? 383  LEU A N     1 
ATOM   2750  C  CA    . LEU A 1  385  ? -29.866 62.605  98.695  1.00 16.78 ? 383  LEU A CA    1 
ATOM   2751  C  C     . LEU A 1  385  ? -30.777 63.457  99.563  1.00 19.60 ? 383  LEU A C     1 
ATOM   2752  O  O     . LEU A 1  385  ? -30.306 64.308  100.326 1.00 18.65 ? 383  LEU A O     1 
ATOM   2753  C  CB    . LEU A 1  385  ? -29.745 63.243  97.308  1.00 15.89 ? 383  LEU A CB    1 
ATOM   2754  C  CG    . LEU A 1  385  ? -28.650 62.810  96.336  1.00 18.00 ? 383  LEU A CG    1 
ATOM   2755  C  CD1   . LEU A 1  385  ? -28.856 63.525  95.010  1.00 20.86 ? 383  LEU A CD1   1 
ATOM   2756  C  CD2   . LEU A 1  385  ? -27.299 63.133  96.897  1.00 20.58 ? 383  LEU A CD2   1 
ATOM   2757  N  N     . ASP A 1  386  ? -32.086 63.261  99.443  1.00 17.45 ? 384  ASP A N     1 
ATOM   2758  C  CA    . ASP A 1  386  ? -33.037 64.110  100.135 1.00 18.32 ? 384  ASP A CA    1 
ATOM   2759  C  C     . ASP A 1  386  ? -33.318 63.629  101.549 1.00 19.85 ? 384  ASP A C     1 
ATOM   2760  O  O     . ASP A 1  386  ? -34.101 64.268  102.260 1.00 20.63 ? 384  ASP A O     1 
ATOM   2761  C  CB    . ASP A 1  386  ? -34.339 64.203  99.326  1.00 20.11 ? 384  ASP A CB    1 
ATOM   2762  C  CG    . ASP A 1  386  ? -34.189 65.044  98.070  1.00 25.35 ? 384  ASP A CG    1 
ATOM   2763  O  OD1   . ASP A 1  386  ? -33.139 65.704  97.896  1.00 23.23 ? 384  ASP A OD1   1 
ATOM   2764  O  OD2   . ASP A 1  386  ? -35.116 65.027  97.228  1.00 23.07 ? 384  ASP A OD2   1 
ATOM   2765  N  N     . GLY A 1  387  ? -32.684 62.540  101.976 1.00 19.96 ? 385  GLY A N     1 
ATOM   2766  C  CA    . GLY A 1  387  ? -32.871 62.031  103.329 1.00 19.78 ? 385  GLY A CA    1 
ATOM   2767  C  C     . GLY A 1  387  ? -34.309 61.707  103.666 1.00 21.21 ? 385  GLY A C     1 
ATOM   2768  O  O     . GLY A 1  387  ? -34.772 62.019  104.771 1.00 21.12 ? 385  GLY A O     1 
ATOM   2769  N  N     . LEU A 1  388  ? -35.030 61.084  102.742 1.00 20.20 ? 386  LEU A N     1 
ATOM   2770  C  CA    . LEU A 1  388  ? -36.447 60.843  102.966 1.00 21.40 ? 386  LEU A CA    1 
ATOM   2771  C  C     . LEU A 1  388  ? -36.672 59.489  103.632 1.00 20.92 ? 386  LEU A C     1 
ATOM   2772  O  O     . LEU A 1  388  ? -35.771 58.654  103.744 1.00 20.80 ? 386  LEU A O     1 
ATOM   2773  C  CB    . LEU A 1  388  ? -37.220 60.973  101.648 1.00 18.55 ? 386  LEU A CB    1 
ATOM   2774  C  CG    . LEU A 1  388  ? -37.109 62.399  101.094 1.00 19.89 ? 386  LEU A CG    1 
ATOM   2775  C  CD1   . LEU A 1  388  ? -37.821 62.587  99.752  1.00 20.72 ? 386  LEU A CD1   1 
ATOM   2776  C  CD2   . LEU A 1  388  ? -37.611 63.416  102.093 1.00 22.84 ? 386  LEU A CD2   1 
ATOM   2777  N  N     . ALA A 1  389  ? -37.902 59.289  104.120 1.00 20.75 ? 387  ALA A N     1 
ATOM   2778  C  CA    . ALA A 1  389  ? -38.169 58.142  104.974 1.00 23.60 ? 387  ALA A CA    1 
ATOM   2779  C  C     . ALA A 1  389  ? -38.010 56.824  104.231 1.00 20.70 ? 387  ALA A C     1 
ATOM   2780  O  O     . ALA A 1  389  ? -37.629 55.817  104.833 1.00 22.19 ? 387  ALA A O     1 
ATOM   2781  C  CB    . ALA A 1  389  ? -39.577 58.251  105.554 1.00 24.64 ? 387  ALA A CB    1 
ATOM   2782  N  N     . ASP A 1  390  ? -38.312 56.797  102.940 1.00 19.36 ? 388  ASP A N     1 
ATOM   2783  C  CA    . ASP A 1  390  ? -38.279 55.548  102.192 1.00 22.60 ? 388  ASP A CA    1 
ATOM   2784  C  C     . ASP A 1  390  ? -38.276 55.901  100.713 1.00 19.23 ? 388  ASP A C     1 
ATOM   2785  O  O     . ASP A 1  390  ? -38.296 57.076  100.337 1.00 18.23 ? 388  ASP A O     1 
ATOM   2786  C  CB    . ASP A 1  390  ? -39.464 54.648  102.579 1.00 21.96 ? 388  ASP A CB    1 
ATOM   2787  C  CG    . ASP A 1  390  ? -39.177 53.168  102.376 1.00 20.72 ? 388  ASP A CG    1 
ATOM   2788  O  OD1   . ASP A 1  390  ? -38.471 52.810  101.412 1.00 21.21 ? 388  ASP A OD1   1 
ATOM   2789  O  OD2   . ASP A 1  390  ? -39.656 52.349  103.191 1.00 24.91 ? 388  ASP A OD2   1 
ATOM   2790  N  N     . PHE A 1  391  ? -38.235 54.879  99.878  1.00 19.02 ? 389  PHE A N     1 
ATOM   2791  C  CA    . PHE A 1  391  ? -38.242 55.107  98.446  1.00 18.12 ? 389  PHE A CA    1 
ATOM   2792  C  C     . PHE A 1  391  ? -39.671 55.158  97.928  1.00 18.56 ? 389  PHE A C     1 
ATOM   2793  O  O     . PHE A 1  391  ? -40.579 54.587  98.546  1.00 18.04 ? 389  PHE A O     1 
ATOM   2794  C  CB    . PHE A 1  391  ? -37.457 54.004  97.740  1.00 19.19 ? 389  PHE A CB    1 
ATOM   2795  C  CG    . PHE A 1  391  ? -36.034 53.932  98.205  1.00 17.29 ? 389  PHE A CG    1 
ATOM   2796  C  CD1   . PHE A 1  391  ? -35.128 54.875  97.778  1.00 16.33 ? 389  PHE A CD1   1 
ATOM   2797  C  CD2   . PHE A 1  391  ? -35.635 52.985  99.135  1.00 18.67 ? 389  PHE A CD2   1 
ATOM   2798  C  CE1   . PHE A 1  391  ? -33.813 54.849  98.226  1.00 19.68 ? 389  PHE A CE1   1 
ATOM   2799  C  CE2   . PHE A 1  391  ? -34.316 52.959  99.597  1.00 19.38 ? 389  PHE A CE2   1 
ATOM   2800  C  CZ    . PHE A 1  391  ? -33.417 53.891  99.143  1.00 19.74 ? 389  PHE A CZ    1 
ATOM   2801  N  N     . PRO A 1  392  ? -39.897 55.879  96.827  1.00 17.70 ? 390  PRO A N     1 
ATOM   2802  C  CA    . PRO A 1  392  ? -41.219 55.878  96.176  1.00 16.58 ? 390  PRO A CA    1 
ATOM   2803  C  C     . PRO A 1  392  ? -41.408 54.755  95.165  1.00 16.59 ? 390  PRO A C     1 
ATOM   2804  O  O     . PRO A 1  392  ? -42.461 54.690  94.502  1.00 18.16 ? 390  PRO A O     1 
ATOM   2805  C  CB    . PRO A 1  392  ? -41.235 57.242  95.477  1.00 15.80 ? 390  PRO A CB    1 
ATOM   2806  C  CG    . PRO A 1  392  ? -39.795 57.400  95.028  1.00 15.71 ? 390  PRO A CG    1 
ATOM   2807  C  CD    . PRO A 1  392  ? -38.973 56.846  96.197  1.00 15.50 ? 390  PRO A CD    1 
ATOM   2808  N  N     . VAL A 1  393  ? -40.400 53.895  95.043  1.00 18.24 ? 391  VAL A N     1 
ATOM   2809  C  CA    . VAL A 1  393  ? -40.385 52.751  94.153  1.00 17.81 ? 391  VAL A CA    1 
ATOM   2810  C  C     . VAL A 1  393  ? -39.967 51.539  94.968  1.00 17.51 ? 391  VAL A C     1 
ATOM   2811  O  O     . VAL A 1  393  ? -39.386 51.661  96.045  1.00 19.31 ? 391  VAL A O     1 
ATOM   2812  C  CB    . VAL A 1  393  ? -39.415 52.953  92.971  1.00 17.71 ? 391  VAL A CB    1 
ATOM   2813  C  CG1   . VAL A 1  393  ? -39.908 54.074  92.075  1.00 19.47 ? 391  VAL A CG1   1 
ATOM   2814  C  CG2   . VAL A 1  393  ? -38.023 53.282  93.500  1.00 15.82 ? 391  VAL A CG2   1 
ATOM   2815  N  N     . PHE A 1  394  ? -40.270 50.360  94.438  1.00 17.99 ? 392  PHE A N     1 
ATOM   2816  C  CA    . PHE A 1  394  ? -39.790 49.140  95.070  1.00 18.68 ? 392  PHE A CA    1 
ATOM   2817  C  C     . PHE A 1  394  ? -38.280 49.027  94.896  1.00 18.98 ? 392  PHE A C     1 
ATOM   2818  O  O     . PHE A 1  394  ? -37.674 49.707  94.067  1.00 19.03 ? 392  PHE A O     1 
ATOM   2819  C  CB    . PHE A 1  394  ? -40.512 47.932  94.490  1.00 19.88 ? 392  PHE A CB    1 
ATOM   2820  C  CG    . PHE A 1  394  ? -41.983 47.981  94.719  1.00 19.09 ? 392  PHE A CG    1 
ATOM   2821  C  CD1   . PHE A 1  394  ? -42.480 47.880  96.008  1.00 21.77 ? 392  PHE A CD1   1 
ATOM   2822  C  CD2   . PHE A 1  394  ? -42.860 48.154  93.672  1.00 19.19 ? 392  PHE A CD2   1 
ATOM   2823  C  CE1   . PHE A 1  394  ? -43.835 47.947  96.252  1.00 20.04 ? 392  PHE A CE1   1 
ATOM   2824  C  CE2   . PHE A 1  394  ? -44.223 48.219  93.900  1.00 18.10 ? 392  PHE A CE2   1 
ATOM   2825  C  CZ    . PHE A 1  394  ? -44.707 48.107  95.197  1.00 21.14 ? 392  PHE A CZ    1 
ATOM   2826  N  N     . THR A 1  395  ? -37.659 48.182  95.725  1.00 19.56 ? 393  THR A N     1 
ATOM   2827  C  CA    . THR A 1  395  ? -36.217 47.995  95.646  1.00 21.40 ? 393  THR A CA    1 
ATOM   2828  C  C     . THR A 1  395  ? -35.804 46.597  95.222  1.00 21.03 ? 393  THR A C     1 
ATOM   2829  O  O     . THR A 1  395  ? -34.615 46.385  94.949  1.00 20.36 ? 393  THR A O     1 
ATOM   2830  C  CB    . THR A 1  395  ? -35.524 48.323  96.979  1.00 21.18 ? 393  THR A CB    1 
ATOM   2831  O  OG1   . THR A 1  395  ? -36.038 47.479  98.014  1.00 21.01 ? 393  THR A OG1   1 
ATOM   2832  C  CG2   . THR A 1  395  ? -35.724 49.782  97.357  1.00 22.57 ? 393  THR A CG2   1 
ATOM   2833  N  N     . ARG A 1  396  ? -36.728 45.646  95.154  1.00 20.34 ? 394  ARG A N     1 
ATOM   2834  C  CA    . ARG A 1  396  ? -36.468 44.356  94.529  1.00 21.54 ? 394  ARG A CA    1 
ATOM   2835  C  C     . ARG A 1  396  ? -37.258 44.274  93.235  1.00 21.67 ? 394  ARG A C     1 
ATOM   2836  O  O     . ARG A 1  396  ? -38.448 44.606  93.207  1.00 22.04 ? 394  ARG A O     1 
ATOM   2837  C  CB    . ARG A 1  396  ? -36.832 43.195  95.450  1.00 23.24 ? 394  ARG A CB    1 
ATOM   2838  C  CG    . ARG A 1  396  ? -36.012 43.174  96.702  1.00 23.57 ? 394  ARG A CG    1 
ATOM   2839  C  CD    . ARG A 1  396  ? -36.239 41.899  97.500  1.00 26.21 ? 394  ARG A CD    1 
ATOM   2840  N  NE    . ARG A 1  396  ? -35.642 42.044  98.821  1.00 29.50 ? 394  ARG A NE    1 
ATOM   2841  C  CZ    . ARG A 1  396  ? -35.008 41.080  99.471  1.00 31.55 ? 394  ARG A CZ    1 
ATOM   2842  N  NH1   . ARG A 1  396  ? -34.915 39.857  98.972  1.00 34.72 ? 394  ARG A NH1   1 
ATOM   2843  N  NH2   . ARG A 1  396  ? -34.438 41.357  100.642 1.00 30.51 ? 394  ARG A NH2   1 
ATOM   2844  N  N     . LYS A 1  397  ? -36.577 43.871  92.162  1.00 20.89 ? 395  LYS A N     1 
ATOM   2845  C  CA    . LYS A 1  397  ? -37.215 43.822  90.850  1.00 20.27 ? 395  LYS A CA    1 
ATOM   2846  C  C     . LYS A 1  397  ? -38.444 42.927  90.863  1.00 23.74 ? 395  LYS A C     1 
ATOM   2847  O  O     . LYS A 1  397  ? -39.438 43.222  90.194  1.00 21.73 ? 395  LYS A O     1 
ATOM   2848  C  CB    . LYS A 1  397  ? -36.198 43.351  89.809  1.00 24.71 ? 395  LYS A CB    1 
ATOM   2849  C  CG    . LYS A 1  397  ? -36.590 43.629  88.375  1.00 24.25 ? 395  LYS A CG    1 
ATOM   2850  C  CD    . LYS A 1  397  ? -37.201 42.394  87.738  1.00 23.38 ? 395  LYS A CD    1 
ATOM   2851  C  CE    . LYS A 1  397  ? -37.815 42.740  86.390  1.00 23.31 ? 395  LYS A CE    1 
ATOM   2852  N  NZ    . LYS A 1  397  ? -38.409 41.544  85.739  1.00 23.11 ? 395  LYS A NZ    1 
ATOM   2853  N  N     . ILE A 1  398  ? -38.405 41.842  91.635  1.00 21.20 ? 396  ILE A N     1 
ATOM   2854  C  CA    . ILE A 1  398  ? -39.534 40.929  91.656  1.00 23.39 ? 396  ILE A CA    1 
ATOM   2855  C  C     . ILE A 1  398  ? -40.773 41.592  92.252  1.00 21.05 ? 396  ILE A C     1 
ATOM   2856  O  O     . ILE A 1  398  ? -41.905 41.226  91.916  1.00 22.03 ? 396  ILE A O     1 
ATOM   2857  C  CB    . ILE A 1  398  ? -39.125 39.647  92.408  1.00 27.38 ? 396  ILE A CB    1 
ATOM   2858  C  CG1   . ILE A 1  398  ? -40.162 38.560  92.192  1.00 27.37 ? 396  ILE A CG1   1 
ATOM   2859  C  CG2   . ILE A 1  398  ? -38.922 39.924  93.888  1.00 23.60 ? 396  ILE A CG2   1 
ATOM   2860  C  CD1   . ILE A 1  398  ? -39.625 37.187  92.514  1.00 31.32 ? 396  ILE A CD1   1 
ATOM   2861  N  N     . HIS A 1  399  ? -40.593 42.580  93.126  1.00 22.17 ? 397  HIS A N     1 
ATOM   2862  C  CA    . HIS A 1  399  ? -41.740 43.296  93.680  1.00 22.45 ? 397  HIS A CA    1 
ATOM   2863  C  C     . HIS A 1  399  ? -42.450 44.100  92.602  1.00 19.31 ? 397  HIS A C     1 
ATOM   2864  O  O     . HIS A 1  399  ? -43.686 44.111  92.532  1.00 20.36 ? 397  HIS A O     1 
ATOM   2865  C  CB    . HIS A 1  399  ? -41.284 44.214  94.813  1.00 21.25 ? 397  HIS A CB    1 
ATOM   2866  C  CG    . HIS A 1  399  ? -40.733 43.477  95.994  1.00 22.76 ? 397  HIS A CG    1 
ATOM   2867  N  ND1   . HIS A 1  399  ? -40.028 44.101  96.998  1.00 22.11 ? 397  HIS A ND1   1 
ATOM   2868  C  CD2   . HIS A 1  399  ? -40.777 42.164  96.324  1.00 24.30 ? 397  HIS A CD2   1 
ATOM   2869  C  CE1   . HIS A 1  399  ? -39.662 43.205  97.900  1.00 23.14 ? 397  HIS A CE1   1 
ATOM   2870  N  NE2   . HIS A 1  399  ? -40.102 42.021  97.513  1.00 23.87 ? 397  HIS A NE2   1 
ATOM   2871  N  N     . THR A 1  400  ? -41.676 44.771  91.748  1.00 19.87 ? 398  THR A N     1 
ATOM   2872  C  CA    . THR A 1  400  ? -42.262 45.462  90.604  1.00 18.58 ? 398  THR A CA    1 
ATOM   2873  C  C     . THR A 1  400  ? -43.041 44.503  89.711  1.00 19.54 ? 398  THR A C     1 
ATOM   2874  O  O     . THR A 1  400  ? -44.110 44.850  89.204  1.00 18.71 ? 398  THR A O     1 
ATOM   2875  C  CB    . THR A 1  400  ? -41.156 46.165  89.820  1.00 19.63 ? 398  THR A CB    1 
ATOM   2876  O  OG1   . THR A 1  400  ? -40.622 47.218  90.629  1.00 18.22 ? 398  THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1  400  ? -41.704 46.744  88.490  1.00 18.58 ? 398  THR A CG2   1 
ATOM   2878  N  N     . ASP A 1  401  ? -42.523 43.289  89.503  1.00 18.61 ? 399  ASP A N     1 
ATOM   2879  C  CA    . ASP A 1  401  ? -43.244 42.322  88.680  1.00 21.22 ? 399  ASP A CA    1 
ATOM   2880  C  C     . ASP A 1  401  ? -44.575 41.948  89.314  1.00 20.31 ? 399  ASP A C     1 
ATOM   2881  O  O     . ASP A 1  401  ? -45.597 41.874  88.623  1.00 19.68 ? 399  ASP A O     1 
ATOM   2882  C  CB    . ASP A 1  401  ? -42.401 41.066  88.448  1.00 20.67 ? 399  ASP A CB    1 
ATOM   2883  C  CG    . ASP A 1  401  ? -41.212 41.320  87.547  1.00 23.07 ? 399  ASP A CG    1 
ATOM   2884  O  OD1   . ASP A 1  401  ? -41.246 42.310  86.779  1.00 24.76 ? 399  ASP A OD1   1 
ATOM   2885  O  OD2   . ASP A 1  401  ? -40.242 40.528  87.613  1.00 25.41 ? 399  ASP A OD2   1 
ATOM   2886  N  N     . VAL A 1  402  ? -44.581 41.700  90.627  1.00 19.86 ? 400  VAL A N     1 
ATOM   2887  C  CA    . VAL A 1  402  ? -45.830 41.375  91.314  1.00 20.95 ? 400  VAL A CA    1 
ATOM   2888  C  C     . VAL A 1  402  ? -46.784 42.560  91.257  1.00 21.89 ? 400  VAL A C     1 
ATOM   2889  O  O     . VAL A 1  402  ? -47.983 42.401  90.995  1.00 22.56 ? 400  VAL A O     1 
ATOM   2890  C  CB    . VAL A 1  402  ? -45.546 40.949  92.765  1.00 22.28 ? 400  VAL A CB    1 
ATOM   2891  C  CG1   . VAL A 1  402  ? -46.857 40.777  93.541  1.00 22.77 ? 400  VAL A CG1   1 
ATOM   2892  C  CG2   . VAL A 1  402  ? -44.741 39.651  92.786  1.00 25.51 ? 400  VAL A CG2   1 
ATOM   2893  N  N     . SER A 1  403  ? -46.263 43.764  91.504  1.00 20.71 ? 401  SER A N     1 
ATOM   2894  C  CA    . SER A 1  403  ? -47.072 44.973  91.387  1.00 21.09 ? 401  SER A CA    1 
ATOM   2895  C  C     . SER A 1  403  ? -47.690 45.085  90.002  1.00 21.02 ? 401  SER A C     1 
ATOM   2896  O  O     . SER A 1  403  ? -48.879 45.403  89.863  1.00 19.30 ? 401  SER A O     1 
ATOM   2897  C  CB    . SER A 1  403  ? -46.210 46.199  91.691  1.00 18.75 ? 401  SER A CB    1 
ATOM   2898  O  OG    . SER A 1  403  ? -46.927 47.398  91.478  1.00 20.56 ? 401  SER A OG    1 
ATOM   2899  N  N     . TYR A 1  404  ? -46.895 44.817  88.961  1.00 20.33 ? 402  TYR A N     1 
ATOM   2900  C  CA    . TYR A 1  404  ? -47.406 44.916  87.601  1.00 20.08 ? 402  TYR A CA    1 
ATOM   2901  C  C     . TYR A 1  404  ? -48.575 43.956  87.390  1.00 20.90 ? 402  TYR A C     1 
ATOM   2902  O  O     . TYR A 1  404  ? -49.618 44.336  86.848  1.00 18.77 ? 402  TYR A O     1 
ATOM   2903  C  CB    . TYR A 1  404  ? -46.269 44.649  86.610  1.00 19.82 ? 402  TYR A CB    1 
ATOM   2904  C  CG    . TYR A 1  404  ? -46.584 45.008  85.168  1.00 19.36 ? 402  TYR A CG    1 
ATOM   2905  C  CD1   . TYR A 1  404  ? -47.331 44.153  84.370  1.00 20.19 ? 402  TYR A CD1   1 
ATOM   2906  C  CD2   . TYR A 1  404  ? -46.104 46.185  84.605  1.00 18.87 ? 402  TYR A CD2   1 
ATOM   2907  C  CE1   . TYR A 1  404  ? -47.611 44.465  83.063  1.00 18.64 ? 402  TYR A CE1   1 
ATOM   2908  C  CE2   . TYR A 1  404  ? -46.380 46.506  83.275  1.00 19.42 ? 402  TYR A CE2   1 
ATOM   2909  C  CZ    . TYR A 1  404  ? -47.124 45.635  82.517  1.00 18.25 ? 402  TYR A CZ    1 
ATOM   2910  O  OH    . TYR A 1  404  ? -47.422 45.916  81.209  1.00 19.02 ? 402  TYR A OH    1 
ATOM   2911  N  N     . ILE A 1  405  ? -48.425 42.707  87.837  1.00 20.79 ? 403  ILE A N     1 
ATOM   2912  C  CA    . ILE A 1  405  ? -49.469 41.716  87.612  1.00 22.42 ? 403  ILE A CA    1 
ATOM   2913  C  C     . ILE A 1  405  ? -50.709 42.038  88.444  1.00 20.66 ? 403  ILE A C     1 
ATOM   2914  O  O     . ILE A 1  405  ? -51.841 41.902  87.965  1.00 21.87 ? 403  ILE A O     1 
ATOM   2915  C  CB    . ILE A 1  405  ? -48.916 40.306  87.893  1.00 22.82 ? 403  ILE A CB    1 
ATOM   2916  C  CG1   . ILE A 1  405  ? -47.877 39.959  86.822  1.00 22.50 ? 403  ILE A CG1   1 
ATOM   2917  C  CG2   . ILE A 1  405  ? -50.028 39.274  87.884  1.00 26.84 ? 403  ILE A CG2   1 
ATOM   2918  C  CD1   . ILE A 1  405  ? -47.070 38.715  87.127  1.00 28.05 ? 403  ILE A CD1   1 
ATOM   2919  N  N     . ALA A 1  406  ? -50.521 42.500  89.684  1.00 20.97 ? 404  ALA A N     1 
ATOM   2920  C  CA    . ALA A 1  406  ? -51.665 42.911  90.499  1.00 20.96 ? 404  ALA A CA    1 
ATOM   2921  C  C     . ALA A 1  406  ? -52.416 44.064  89.855  1.00 22.35 ? 404  ALA A C     1 
ATOM   2922  O  O     . ALA A 1  406  ? -53.653 44.080  89.842  1.00 22.62 ? 404  ALA A O     1 
ATOM   2923  C  CB    . ALA A 1  406  ? -51.204 43.319  91.896  1.00 25.10 ? 404  ALA A CB    1 
ATOM   2924  N  N     . CYS A 1  407  ? -51.684 45.049  89.335  1.00 21.70 ? 405  CYS A N     1 
ATOM   2925  C  CA    . CYS A 1  407  ? -52.317 46.197  88.701  1.00 18.75 ? 405  CYS A CA    1 
ATOM   2926  C  C     . CYS A 1  407  ? -52.980 45.816  87.388  1.00 20.78 ? 405  CYS A C     1 
ATOM   2927  O  O     . CYS A 1  407  ? -53.983 46.429  86.997  1.00 19.58 ? 405  CYS A O     1 
ATOM   2928  C  CB    . CYS A 1  407  ? -51.279 47.303  88.499  1.00 19.89 ? 405  CYS A CB    1 
ATOM   2929  S  SG    . CYS A 1  407  ? -50.803 48.068  90.056  1.00 22.39 ? 405  CYS A SG    1 
ATOM   2930  N  N     . ALA A 1  408  ? -52.447 44.804  86.700  1.00 19.49 ? 406  ALA A N     1 
ATOM   2931  C  CA    . ALA A 1  408  ? -53.109 44.301  85.503  1.00 20.12 ? 406  ALA A CA    1 
ATOM   2932  C  C     . ALA A 1  408  ? -54.439 43.643  85.848  1.00 17.71 ? 406  ALA A C     1 
ATOM   2933  O  O     . ALA A 1  408  ? -55.404 43.750  85.088  1.00 21.59 ? 406  ALA A O     1 
ATOM   2934  C  CB    . ALA A 1  408  ? -52.193 43.315  84.773  1.00 24.14 ? 406  ALA A CB    1 
ATOM   2935  N  N     . ALA A 1  409  ? -54.502 42.937  86.980  1.00 20.94 ? 407  ALA A N     1 
ATOM   2936  C  CA    . ALA A 1  409  ? -55.774 42.361  87.407  1.00 21.68 ? 407  ALA A CA    1 
ATOM   2937  C  C     . ALA A 1  409  ? -56.806 43.451  87.675  1.00 21.22 ? 407  ALA A C     1 
ATOM   2938  O  O     . ALA A 1  409  ? -57.987 43.302  87.323  1.00 20.98 ? 407  ALA A O     1 
ATOM   2939  C  CB    . ALA A 1  409  ? -55.567 41.489  88.649  1.00 23.05 ? 407  ALA A CB    1 
ATOM   2940  N  N     . LYS A 1  410  ? -56.375 44.566  88.278  1.00 21.41 ? 408  LYS A N     1 
ATOM   2941  C  CA    . LYS A 1  410  ? -57.286 45.684  88.515  1.00 21.78 ? 408  LYS A CA    1 
ATOM   2942  C  C     . LYS A 1  410  ? -57.768 46.287  87.199  1.00 20.08 ? 408  LYS A C     1 
ATOM   2943  O  O     . LYS A 1  410  ? -58.964 46.546  87.020  1.00 20.49 ? 408  LYS A O     1 
ATOM   2944  C  CB    . LYS A 1  410  ? -56.600 46.750  89.373  1.00 20.43 ? 408  LYS A CB    1 
ATOM   2945  C  CG    . LYS A 1  410  ? -57.488 47.959  89.682  1.00 22.81 ? 408  LYS A CG    1 
ATOM   2946  C  CD    . LYS A 1  410  ? -56.724 49.019  90.455  1.00 21.78 ? 408  LYS A CD    1 
ATOM   2947  C  CE    . LYS A 1  410  ? -56.238 48.524  91.815  1.00 22.74 ? 408  LYS A CE    1 
ATOM   2948  N  NZ    . LYS A 1  410  ? -57.364 48.322  92.773  1.00 22.99 ? 408  LYS A NZ    1 
ATOM   2949  N  N     . LEU A 1  411  ? -56.846 46.510  86.261  1.00 18.46 ? 409  LEU A N     1 
ATOM   2950  C  CA    . LEU A 1  411  ? -57.225 47.054  84.963  1.00 18.96 ? 409  LEU A CA    1 
ATOM   2951  C  C     . LEU A 1  411  ? -58.154 46.112  84.205  1.00 18.84 ? 409  LEU A C     1 
ATOM   2952  O  O     . LEU A 1  411  ? -59.129 46.554  83.588  1.00 19.39 ? 409  LEU A O     1 
ATOM   2953  C  CB    . LEU A 1  411  ? -55.971 47.341  84.136  1.00 18.85 ? 409  LEU A CB    1 
ATOM   2954  C  CG    . LEU A 1  411  ? -55.207 48.611  84.514  1.00 18.23 ? 409  LEU A CG    1 
ATOM   2955  C  CD1   . LEU A 1  411  ? -53.820 48.605  83.884  1.00 19.98 ? 409  LEU A CD1   1 
ATOM   2956  C  CD2   . LEU A 1  411  ? -55.961 49.868  84.096  1.00 18.56 ? 409  LEU A CD2   1 
ATOM   2957  N  N     . LEU A 1  412  ? -57.862 44.808  84.224  1.00 20.28 ? 410  LEU A N     1 
ATOM   2958  C  CA    . LEU A 1  412  ? -58.678 43.884  83.446  1.00 20.03 ? 410  LEU A CA    1 
ATOM   2959  C  C     . LEU A 1  412  ? -60.079 43.733  84.013  1.00 20.38 ? 410  LEU A C     1 
ATOM   2960  O  O     . LEU A 1  412  ? -60.964 43.257  83.298  1.00 23.68 ? 410  LEU A O     1 
ATOM   2961  C  CB    . LEU A 1  412  ? -57.992 42.523  83.347  1.00 22.75 ? 410  LEU A CB    1 
ATOM   2962  C  CG    . LEU A 1  412  ? -56.848 42.503  82.315  1.00 20.58 ? 410  LEU A CG    1 
ATOM   2963  C  CD1   . LEU A 1  412  ? -56.061 41.215  82.422  1.00 23.76 ? 410  LEU A CD1   1 
ATOM   2964  C  CD2   . LEU A 1  412  ? -57.407 42.678  80.909  1.00 22.60 ? 410  LEU A CD2   1 
ATOM   2965  N  N     . ALA A 1  413  ? -60.308 44.146  85.264  1.00 21.10 ? 411  ALA A N     1 
ATOM   2966  C  CA    . ALA A 1  413  ? -61.659 44.164  85.826  1.00 21.57 ? 411  ALA A CA    1 
ATOM   2967  C  C     . ALA A 1  413  ? -62.440 45.417  85.451  1.00 24.50 ? 411  ALA A C     1 
ATOM   2968  O  O     . ALA A 1  413  ? -63.630 45.521  85.786  1.00 23.73 ? 411  ALA A O     1 
ATOM   2969  C  CB    . ALA A 1  413  ? -61.592 44.049  87.352  1.00 22.71 ? 411  ALA A CB    1 
ATOM   2970  N  N     . ALA A 1  414  ? -61.806 46.376  84.772  1.00 22.93 ? 412  ALA A N     1 
ATOM   2971  C  CA    . ALA A 1  414  ? -62.446 47.646  84.452  1.00 23.54 ? 412  ALA A CA    1 
ATOM   2972  C  C     . ALA A 1  414  ? -62.341 47.979  82.966  1.00 23.75 ? 412  ALA A C     1 
ATOM   2973  O  O     . ALA A 1  414  ? -62.326 49.153  82.600  1.00 20.00 ? 412  ALA A O     1 
ATOM   2974  C  CB    . ALA A 1  414  ? -61.844 48.777  85.290  1.00 24.51 ? 412  ALA A CB    1 
ATOM   2975  N  N     . THR A 1  415  ? -62.292 46.967  82.088  1.00 23.08 ? 413  THR A N     1 
ATOM   2976  C  CA    . THR A 1  415  ? -62.168 47.251  80.660  1.00 23.24 ? 413  THR A CA    1 
ATOM   2977  C  C     . THR A 1  415  ? -63.391 47.954  80.089  1.00 22.02 ? 413  THR A C     1 
ATOM   2978  O  O     . THR A 1  415  ? -63.313 48.491  78.979  1.00 23.43 ? 413  THR A O     1 
ATOM   2979  C  CB    . THR A 1  415  ? -61.900 45.972  79.849  1.00 24.99 ? 413  THR A CB    1 
ATOM   2980  O  OG1   . THR A 1  415  ? -62.951 45.025  80.061  1.00 25.74 ? 413  THR A OG1   1 
ATOM   2981  C  CG2   . THR A 1  415  ? -60.574 45.344  80.251  1.00 23.40 ? 413  THR A CG2   1 
ATOM   2982  N  N     . ASP A 1  416  ? -64.520 47.972  80.803  1.00 22.24 ? 414  ASP A N     1 
ATOM   2983  C  CA    . ASP A 1  416  ? -65.648 48.752  80.305  1.00 21.62 ? 414  ASP A CA    1 
ATOM   2984  C  C     . ASP A 1  416  ? -65.392 50.249  80.416  1.00 23.40 ? 414  ASP A C     1 
ATOM   2985  O  O     . ASP A 1  416  ? -65.928 51.021  79.617  1.00 25.56 ? 414  ASP A O     1 
ATOM   2986  C  CB    . ASP A 1  416  ? -66.937 48.365  81.036  1.00 27.40 ? 414  ASP A CB    1 
ATOM   2987  C  CG    . ASP A 1  416  ? -66.846 48.559  82.537  1.00 30.24 ? 414  ASP A CG    1 
ATOM   2988  O  OD1   . ASP A 1  416  ? -65.739 48.410  83.094  1.00 28.24 ? 414  ASP A OD1   1 
ATOM   2989  O  OD2   . ASP A 1  416  ? -67.892 48.847  83.168  1.00 35.65 ? 414  ASP A OD2   1 
ATOM   2990  N  N     . VAL A 1  417  ? -64.546 50.685  81.350  1.00 21.82 ? 415  VAL A N     1 
ATOM   2991  C  CA    . VAL A 1  417  ? -64.348 52.110  81.572  1.00 22.21 ? 415  VAL A CA    1 
ATOM   2992  C  C     . VAL A 1  417  ? -62.936 52.602  81.252  1.00 19.11 ? 415  VAL A C     1 
ATOM   2993  O  O     . VAL A 1  417  ? -62.757 53.817  81.078  1.00 21.19 ? 415  VAL A O     1 
ATOM   2994  C  CB    . VAL A 1  417  ? -64.733 52.505  83.009  1.00 24.84 ? 415  VAL A CB    1 
ATOM   2995  C  CG1   . VAL A 1  417  ? -66.207 52.229  83.231  1.00 28.54 ? 415  VAL A CG1   1 
ATOM   2996  C  CG2   . VAL A 1  417  ? -63.889 51.760  83.999  1.00 22.82 ? 415  VAL A CG2   1 
ATOM   2997  N  N     . VAL A 1  418  ? -61.940 51.718  81.155  1.00 18.50 ? 416  VAL A N     1 
ATOM   2998  C  CA    . VAL A 1  418  ? -60.606 52.104  80.704  1.00 17.98 ? 416  VAL A CA    1 
ATOM   2999  C  C     . VAL A 1  418  ? -60.121 51.092  79.679  1.00 18.00 ? 416  VAL A C     1 
ATOM   3000  O  O     . VAL A 1  418  ? -60.631 49.975  79.579  1.00 19.40 ? 416  VAL A O     1 
ATOM   3001  C  CB    . VAL A 1  418  ? -59.579 52.218  81.852  1.00 17.17 ? 416  VAL A CB    1 
ATOM   3002  C  CG1   . VAL A 1  418  ? -59.992 53.307  82.842  1.00 20.96 ? 416  VAL A CG1   1 
ATOM   3003  C  CG2   . VAL A 1  418  ? -59.390 50.893  82.553  1.00 17.94 ? 416  VAL A CG2   1 
ATOM   3004  N  N     . PHE A 1  419  ? -59.112 51.501  78.918  1.00 16.25 ? 417  PHE A N     1 
ATOM   3005  C  CA    . PHE A 1  419  ? -58.480 50.660  77.908  1.00 18.77 ? 417  PHE A CA    1 
ATOM   3006  C  C     . PHE A 1  419  ? -57.078 50.297  78.384  1.00 15.87 ? 417  PHE A C     1 
ATOM   3007  O  O     . PHE A 1  419  ? -56.157 51.125  78.288  1.00 16.95 ? 417  PHE A O     1 
ATOM   3008  C  CB    . PHE A 1  419  ? -58.423 51.392  76.563  1.00 18.67 ? 417  PHE A CB    1 
ATOM   3009  C  CG    . PHE A 1  419  ? -57.714 50.623  75.480  1.00 18.77 ? 417  PHE A CG    1 
ATOM   3010  C  CD1   . PHE A 1  419  ? -58.172 49.370  75.083  1.00 18.88 ? 417  PHE A CD1   1 
ATOM   3011  C  CD2   . PHE A 1  419  ? -56.609 51.159  74.847  1.00 19.21 ? 417  PHE A CD2   1 
ATOM   3012  C  CE1   . PHE A 1  419  ? -57.524 48.672  74.081  1.00 20.24 ? 417  PHE A CE1   1 
ATOM   3013  C  CE2   . PHE A 1  419  ? -55.957 50.460  73.852  1.00 17.46 ? 417  PHE A CE2   1 
ATOM   3014  C  CZ    . PHE A 1  419  ? -56.424 49.222  73.458  1.00 17.43 ? 417  PHE A CZ    1 
ATOM   3015  N  N     . PRO A 1  420  ? -56.863 49.093  78.916  1.00 16.27 ? 418  PRO A N     1 
ATOM   3016  C  CA    . PRO A 1  420  ? -55.529 48.736  79.423  1.00 17.34 ? 418  PRO A CA    1 
ATOM   3017  C  C     . PRO A 1  420  ? -54.547 48.484  78.295  1.00 17.74 ? 418  PRO A C     1 
ATOM   3018  O  O     . PRO A 1  420  ? -54.881 47.881  77.271  1.00 19.08 ? 418  PRO A O     1 
ATOM   3019  C  CB    . PRO A 1  420  ? -55.775 47.453  80.231  1.00 15.55 ? 418  PRO A CB    1 
ATOM   3020  C  CG    . PRO A 1  420  ? -57.277 47.456  80.506  1.00 17.17 ? 418  PRO A CG    1 
ATOM   3021  C  CD    . PRO A 1  420  ? -57.879 48.088  79.277  1.00 16.93 ? 418  PRO A CD    1 
ATOM   3022  N  N     . GLN A 1  421  ? -53.317 48.935  78.510  1.00 16.34 ? 419  GLN A N     1 
ATOM   3023  C  CA    . GLN A 1  421  ? -52.246 48.806  77.532  1.00 15.93 ? 419  GLN A CA    1 
ATOM   3024  C  C     . GLN A 1  421  ? -51.034 48.296  78.288  1.00 17.18 ? 419  GLN A C     1 
ATOM   3025  O  O     . GLN A 1  421  ? -50.438 49.043  79.065  1.00 17.42 ? 419  GLN A O     1 
ATOM   3026  C  CB    . GLN A 1  421  ? -51.959 50.147  76.863  1.00 15.23 ? 419  GLN A CB    1 
ATOM   3027  C  CG    . GLN A 1  421  ? -53.182 50.740  76.153  1.00 15.42 ? 419  GLN A CG    1 
ATOM   3028  C  CD    . GLN A 1  421  ? -52.997 52.207  75.833  1.00 18.43 ? 419  GLN A CD    1 
ATOM   3029  O  OE1   . GLN A 1  421  ? -52.763 53.020  76.730  1.00 18.27 ? 419  GLN A OE1   1 
ATOM   3030  N  NE2   . GLN A 1  421  ? -53.102 52.557  74.554  1.00 16.42 ? 419  GLN A NE2   1 
ATOM   3031  N  N     . PHE A 1  422  ? -50.682 47.028  78.082  1.00 16.65 ? 420  PHE A N     1 
ATOM   3032  C  CA    . PHE A 1  422  ? -49.677 46.376  78.914  1.00 15.93 ? 420  PHE A CA    1 
ATOM   3033  C  C     . PHE A 1  422  ? -48.340 46.449  78.192  1.00 16.60 ? 420  PHE A C     1 
ATOM   3034  O  O     . PHE A 1  422  ? -48.048 45.643  77.304  1.00 19.57 ? 420  PHE A O     1 
ATOM   3035  C  CB    . PHE A 1  422  ? -50.090 44.948  79.242  1.00 17.42 ? 420  PHE A CB    1 
ATOM   3036  C  CG    . PHE A 1  422  ? -51.404 44.878  79.970  1.00 19.32 ? 420  PHE A CG    1 
ATOM   3037  C  CD1   . PHE A 1  422  ? -51.516 45.364  81.261  1.00 20.14 ? 420  PHE A CD1   1 
ATOM   3038  C  CD2   . PHE A 1  422  ? -52.529 44.352  79.352  1.00 18.95 ? 420  PHE A CD2   1 
ATOM   3039  C  CE1   . PHE A 1  422  ? -52.720 45.308  81.941  1.00 20.72 ? 420  PHE A CE1   1 
ATOM   3040  C  CE2   . PHE A 1  422  ? -53.732 44.293  80.020  1.00 21.39 ? 420  PHE A CE2   1 
ATOM   3041  C  CZ    . PHE A 1  422  ? -53.826 44.781  81.317  1.00 19.70 ? 420  PHE A CZ    1 
ATOM   3042  N  N     . ALA A 1  423  ? -47.537 47.422  78.600  1.00 17.43 ? 421  ALA A N     1 
ATOM   3043  C  CA    . ALA A 1  423  ? -46.244 47.697  77.996  1.00 15.63 ? 421  ALA A CA    1 
ATOM   3044  C  C     . ALA A 1  423  ? -45.213 46.834  78.710  1.00 19.90 ? 421  ALA A C     1 
ATOM   3045  O  O     . ALA A 1  423  ? -44.898 47.068  79.883  1.00 22.12 ? 421  ALA A O     1 
ATOM   3046  C  CB    . ALA A 1  423  ? -45.929 49.185  78.113  1.00 17.41 ? 421  ALA A CB    1 
ATOM   3047  N  N     . THR A 1  424  ? -44.705 45.822  78.018  1.00 18.02 ? 422  THR A N     1 
ATOM   3048  C  CA    . THR A 1  424  ? -43.680 44.980  78.616  1.00 19.14 ? 422  THR A CA    1 
ATOM   3049  C  C     . THR A 1  424  ? -43.009 44.165  77.523  1.00 19.89 ? 422  THR A C     1 
ATOM   3050  O  O     . THR A 1  424  ? -43.641 43.795  76.527  1.00 20.25 ? 422  THR A O     1 
ATOM   3051  C  CB    . THR A 1  424  ? -44.262 44.046  79.692  1.00 20.66 ? 422  THR A CB    1 
ATOM   3052  O  OG1   . THR A 1  424  ? -43.190 43.343  80.334  1.00 20.88 ? 422  THR A OG1   1 
ATOM   3053  C  CG2   . THR A 1  424  ? -45.228 43.038  79.079  1.00 21.95 ? 422  THR A CG2   1 
ATOM   3054  N  N     . HIS A 1  425  ? -41.718 43.890  77.729  1.00 20.33 ? 423  HIS A N     1 
ATOM   3055  C  CA    . HIS A 1  425  ? -40.968 42.943  76.914  1.00 19.10 ? 423  HIS A CA    1 
ATOM   3056  C  C     . HIS A 1  425  ? -40.699 41.636  77.638  1.00 23.59 ? 423  HIS A C     1 
ATOM   3057  O  O     . HIS A 1  425  ? -39.944 40.802  77.130  1.00 24.99 ? 423  HIS A O     1 
ATOM   3058  C  CB    . HIS A 1  425  ? -39.638 43.549  76.480  1.00 20.99 ? 423  HIS A CB    1 
ATOM   3059  C  CG    . HIS A 1  425  ? -39.790 44.847  75.765  1.00 24.66 ? 423  HIS A CG    1 
ATOM   3060  N  ND1   . HIS A 1  425  ? -39.348 46.042  76.287  1.00 33.44 ? 423  HIS A ND1   1 
ATOM   3061  C  CD2   . HIS A 1  425  ? -40.369 45.143  74.581  1.00 24.48 ? 423  HIS A CD2   1 
ATOM   3062  C  CE1   . HIS A 1  425  ? -39.635 47.018  75.444  1.00 30.86 ? 423  HIS A CE1   1 
ATOM   3063  N  NE2   . HIS A 1  425  ? -40.247 46.496  74.398  1.00 23.57 ? 423  HIS A NE2   1 
ATOM   3064  N  N     . ASN A 1  426  ? -41.285 41.452  78.814  1.00 22.56 ? 424  ASN A N     1 
ATOM   3065  C  CA    . ASN A 1  426  ? -41.050 40.276  79.644  1.00 22.23 ? 424  ASN A CA    1 
ATOM   3066  C  C     . ASN A 1  426  ? -42.064 39.206  79.253  1.00 24.20 ? 424  ASN A C     1 
ATOM   3067  O  O     . ASN A 1  426  ? -43.270 39.370  79.473  1.00 22.79 ? 424  ASN A O     1 
ATOM   3068  C  CB    . ASN A 1  426  ? -41.154 40.671  81.116  1.00 23.62 ? 424  ASN A CB    1 
ATOM   3069  C  CG    . ASN A 1  426  ? -40.833 39.532  82.062  1.00 22.32 ? 424  ASN A CG    1 
ATOM   3070  O  OD1   . ASN A 1  426  ? -41.253 38.402  81.852  1.00 24.09 ? 424  ASN A OD1   1 
ATOM   3071  N  ND2   . ASN A 1  426  ? -40.090 39.837  83.126  1.00 21.96 ? 424  ASN A ND2   1 
ATOM   3072  N  N     . ALA A 1  427  ? -41.579 38.105  78.669  1.00 20.55 ? 425  ALA A N     1 
ATOM   3073  C  CA    . ALA A 1  427  ? -42.490 37.067  78.186  1.00 25.25 ? 425  ALA A CA    1 
ATOM   3074  C  C     . ALA A 1  427  ? -43.281 36.419  79.319  1.00 22.61 ? 425  ALA A C     1 
ATOM   3075  O  O     . ALA A 1  427  ? -44.393 35.935  79.095  1.00 23.18 ? 425  ALA A O     1 
ATOM   3076  C  CB    . ALA A 1  427  ? -41.713 35.995  77.416  1.00 27.31 ? 425  ALA A CB    1 
ATOM   3077  N  N     . GLN A 1  428  ? -42.724 36.384  80.527  1.00 23.96 ? 426  GLN A N     1 
ATOM   3078  C  CA    . GLN A 1  428  ? -43.452 35.828  81.664  1.00 25.96 ? 426  GLN A CA    1 
ATOM   3079  C  C     . GLN A 1  428  ? -44.586 36.752  82.075  1.00 24.01 ? 426  GLN A C     1 
ATOM   3080  O  O     . GLN A 1  428  ? -45.710 36.299  82.326  1.00 23.77 ? 426  GLN A O     1 
ATOM   3081  C  CB    . GLN A 1  428  ? -42.491 35.594  82.834  1.00 23.77 ? 426  GLN A CB    1 
ATOM   3082  C  CG    . GLN A 1  428  ? -43.021 34.680  83.945  1.00 26.76 ? 426  GLN A CG    1 
ATOM   3083  C  CD    . GLN A 1  428  ? -44.088 35.340  84.804  1.00 29.58 ? 426  GLN A CD    1 
ATOM   3084  O  OE1   . GLN A 1  428  ? -44.012 36.538  85.103  1.00 31.05 ? 426  GLN A OE1   1 
ATOM   3085  N  NE2   . GLN A 1  428  ? -45.090 34.567  85.197  1.00 27.47 ? 426  GLN A NE2   1 
ATOM   3086  N  N     . THR A 1  429  ? -44.294 38.054  82.164  1.00 24.64 ? 427  THR A N     1 
ATOM   3087  C  CA    . THR A 1  429  ? -45.327 39.045  82.436  1.00 21.74 ? 427  THR A CA    1 
ATOM   3088  C  C     . THR A 1  429  ? -46.426 38.973  81.390  1.00 21.62 ? 427  THR A C     1 
ATOM   3089  O  O     . THR A 1  429  ? -47.619 38.937  81.722  1.00 21.84 ? 427  THR A O     1 
ATOM   3090  C  CB    . THR A 1  429  ? -44.712 40.445  82.453  1.00 21.86 ? 427  THR A CB    1 
ATOM   3091  O  OG1   . THR A 1  429  ? -43.551 40.452  83.289  1.00 23.25 ? 427  THR A OG1   1 
ATOM   3092  C  CG2   . THR A 1  429  ? -45.723 41.462  82.981  1.00 22.66 ? 427  THR A CG2   1 
ATOM   3093  N  N     . LEU A 1  430  ? -46.031 38.943  80.115  1.00 19.20 ? 428  LEU A N     1 
ATOM   3094  C  CA    . LEU A 1  430  ? -46.994 38.882  79.019  1.00 20.63 ? 428  LEU A CA    1 
ATOM   3095  C  C     . LEU A 1  430  ? -47.898 37.665  79.146  1.00 22.96 ? 428  LEU A C     1 
ATOM   3096  O  O     . LEU A 1  430  ? -49.129 37.777  79.077  1.00 23.36 ? 428  LEU A O     1 
ATOM   3097  C  CB    . LEU A 1  430  ? -46.244 38.860  77.684  1.00 21.24 ? 428  LEU A CB    1 
ATOM   3098  C  CG    . LEU A 1  430  ? -46.988 39.064  76.358  1.00 23.57 ? 428  LEU A CG    1 
ATOM   3099  C  CD1   . LEU A 1  430  ? -45.944 39.328  75.293  1.00 27.74 ? 428  LEU A CD1   1 
ATOM   3100  C  CD2   . LEU A 1  430  ? -47.843 37.872  75.935  1.00 25.53 ? 428  LEU A CD2   1 
ATOM   3101  N  N     . ALA A 1  431  ? -47.296 36.483  79.323  1.00 22.28 ? 429  ALA A N     1 
ATOM   3102  C  CA    . ALA A 1  431  ? -48.070 35.250  79.399  1.00 25.06 ? 429  ALA A CA    1 
ATOM   3103  C  C     . ALA A 1  431  ? -49.051 35.284  80.565  1.00 24.06 ? 429  ALA A C     1 
ATOM   3104  O  O     . ALA A 1  431  ? -50.202 34.849  80.431  1.00 24.12 ? 429  ALA A O     1 
ATOM   3105  C  CB    . ALA A 1  431  ? -47.124 34.054  79.526  1.00 23.74 ? 429  ALA A CB    1 
ATOM   3106  N  N     . ALA A 1  432  ? -48.617 35.813  81.711  1.00 24.51 ? 430  ALA A N     1 
ATOM   3107  C  CA    . ALA A 1  432  ? -49.487 35.856  82.883  1.00 23.97 ? 430  ALA A CA    1 
ATOM   3108  C  C     . ALA A 1  432  ? -50.721 36.706  82.621  1.00 24.44 ? 430  ALA A C     1 
ATOM   3109  O  O     . ALA A 1  432  ? -51.832 36.342  83.026  1.00 25.73 ? 430  ALA A O     1 
ATOM   3110  C  CB    . ALA A 1  432  ? -48.712 36.385  84.091  1.00 23.74 ? 430  ALA A CB    1 
ATOM   3111  N  N     . ILE A 1  433  ? -50.554 37.822  81.913  1.00 23.86 ? 431  ILE A N     1 
ATOM   3112  C  CA    . ILE A 1  433  ? -51.676 38.704  81.627  1.00 22.30 ? 431  ILE A CA    1 
ATOM   3113  C  C     . ILE A 1  433  ? -52.531 38.147  80.504  1.00 24.16 ? 431  ILE A C     1 
ATOM   3114  O  O     . ILE A 1  433  ? -53.761 38.244  80.541  1.00 24.74 ? 431  ILE A O     1 
ATOM   3115  C  CB    . ILE A 1  433  ? -51.147 40.111  81.304  1.00 22.62 ? 431  ILE A CB    1 
ATOM   3116  C  CG1   . ILE A 1  433  ? -50.557 40.720  82.574  1.00 22.89 ? 431  ILE A CG1   1 
ATOM   3117  C  CG2   . ILE A 1  433  ? -52.238 40.979  80.710  1.00 24.57 ? 431  ILE A CG2   1 
ATOM   3118  C  CD1   . ILE A 1  433  ? -49.779 41.958  82.347  1.00 25.56 ? 431  ILE A CD1   1 
ATOM   3119  N  N     . TYR A 1  434  ? -51.892 37.559  79.489  1.00 23.77 ? 432  TYR A N     1 
ATOM   3120  C  CA    . TYR A 1  434  ? -52.628 36.917  78.405  1.00 26.00 ? 432  TYR A CA    1 
ATOM   3121  C  C     . TYR A 1  434  ? -53.621 35.888  78.937  1.00 26.08 ? 432  TYR A C     1 
ATOM   3122  O  O     . TYR A 1  434  ? -54.777 35.845  78.501  1.00 26.91 ? 432  TYR A O     1 
ATOM   3123  C  CB    . TYR A 1  434  ? -51.635 36.273  77.437  1.00 25.06 ? 432  TYR A CB    1 
ATOM   3124  C  CG    . TYR A 1  434  ? -52.249 35.334  76.435  1.00 26.22 ? 432  TYR A CG    1 
ATOM   3125  C  CD1   . TYR A 1  434  ? -53.067 35.809  75.419  1.00 26.01 ? 432  TYR A CD1   1 
ATOM   3126  C  CD2   . TYR A 1  434  ? -51.996 33.967  76.497  1.00 29.26 ? 432  TYR A CD2   1 
ATOM   3127  C  CE1   . TYR A 1  434  ? -53.625 34.953  74.498  1.00 28.35 ? 432  TYR A CE1   1 
ATOM   3128  C  CE2   . TYR A 1  434  ? -52.548 33.102  75.579  1.00 27.99 ? 432  TYR A CE2   1 
ATOM   3129  C  CZ    . TYR A 1  434  ? -53.360 33.600  74.583  1.00 31.66 ? 432  TYR A CZ    1 
ATOM   3130  O  OH    . TYR A 1  434  ? -53.912 32.741  73.669  1.00 33.03 ? 432  TYR A OH    1 
ATOM   3131  N  N     . HIS A 1  435  ? -53.197 35.060  79.890  1.00 25.77 ? 433  HIS A N     1 
ATOM   3132  C  CA    . HIS A 1  435  ? -54.125 34.081  80.451  1.00 27.76 ? 433  HIS A CA    1 
ATOM   3133  C  C     . HIS A 1  435  ? -55.065 34.702  81.470  1.00 27.91 ? 433  HIS A C     1 
ATOM   3134  O  O     . HIS A 1  435  ? -56.205 34.244  81.615  1.00 27.61 ? 433  HIS A O     1 
ATOM   3135  C  CB    . HIS A 1  435  ? -53.353 32.921  81.069  1.00 26.88 ? 433  HIS A CB    1 
ATOM   3136  C  CG    . HIS A 1  435  ? -52.728 32.033  80.046  1.00 31.45 ? 433  HIS A CG    1 
ATOM   3137  N  ND1   . HIS A 1  435  ? -53.426 31.022  79.425  1.00 31.06 ? 433  HIS A ND1   1 
ATOM   3138  C  CD2   . HIS A 1  435  ? -51.496 32.042  79.487  1.00 30.20 ? 433  HIS A CD2   1 
ATOM   3139  C  CE1   . HIS A 1  435  ? -52.640 30.426  78.546  1.00 33.47 ? 433  HIS A CE1   1 
ATOM   3140  N  NE2   . HIS A 1  435  ? -51.463 31.021  78.567  1.00 31.59 ? 433  HIS A NE2   1 
ATOM   3141  N  N     . MET A 1  436  ? -54.615 35.750  82.164  1.00 28.43 ? 434  MET A N     1 
ATOM   3142  C  CA    . MET A 1  436  ? -55.495 36.447  83.093  1.00 26.89 ? 434  MET A CA    1 
ATOM   3143  C  C     . MET A 1  436  ? -56.679 37.069  82.366  1.00 24.37 ? 434  MET A C     1 
ATOM   3144  O  O     . MET A 1  436  ? -57.798 37.083  82.887  1.00 28.60 ? 434  MET A O     1 
ATOM   3145  C  CB    . MET A 1  436  ? -54.710 37.518  83.843  1.00 24.96 ? 434  MET A CB    1 
ATOM   3146  C  CG    . MET A 1  436  ? -55.546 38.294  84.834  1.00 25.57 ? 434  MET A CG    1 
ATOM   3147  S  SD    . MET A 1  436  ? -54.609 39.649  85.548  1.00 27.65 ? 434  MET A SD    1 
ATOM   3148  C  CE    . MET A 1  436  ? -53.411 38.771  86.537  1.00 24.98 ? 434  MET A CE    1 
ATOM   3149  N  N     . ALA A 1  437  ? -56.443 37.601  81.163  1.00 24.52 ? 435  ALA A N     1 
ATOM   3150  C  CA    . ALA A 1  437  ? -57.490 38.280  80.412  1.00 26.67 ? 435  ALA A CA    1 
ATOM   3151  C  C     . ALA A 1  437  ? -58.513 37.311  79.836  1.00 31.65 ? 435  ALA A C     1 
ATOM   3152  O  O     . ALA A 1  437  ? -59.624 37.732  79.495  1.00 28.71 ? 435  ALA A O     1 
ATOM   3153  C  CB    . ALA A 1  437  ? -56.869 39.110  79.292  1.00 25.53 ? 435  ALA A CB    1 
ATOM   3154  N  N     . GLY A 1  438  ? -58.166 36.035  79.712  1.00 31.20 ? 436  GLY A N     1 
ATOM   3155  C  CA    . GLY A 1  438  ? -59.135 35.034  79.328  1.00 34.53 ? 436  GLY A CA    1 
ATOM   3156  C  C     . GLY A 1  438  ? -59.391 34.982  77.835  1.00 36.80 ? 436  GLY A C     1 
ATOM   3157  O  O     . GLY A 1  438  ? -58.738 35.644  77.024  1.00 36.60 ? 436  GLY A O     1 
ATOM   3158  N  N     . LYS A 1  439  ? -60.410 34.189  77.483  1.00 40.91 ? 437  LYS A N     1 
ATOM   3159  C  CA    . LYS A 1  439  ? -60.643 33.808  76.094  1.00 41.01 ? 437  LYS A CA    1 
ATOM   3160  C  C     . LYS A 1  439  ? -61.437 34.851  75.318  1.00 39.32 ? 437  LYS A C     1 
ATOM   3161  O  O     . LYS A 1  439  ? -61.267 34.967  74.100  1.00 44.30 ? 437  LYS A O     1 
ATOM   3162  C  CB    . LYS A 1  439  ? -61.366 32.459  76.040  1.00 47.95 ? 437  LYS A CB    1 
ATOM   3163  N  N     . ASP A 1  440  ? -62.301 35.611  75.982  1.00 39.45 ? 438  ASP A N     1 
ATOM   3164  C  CA    . ASP A 1  440  ? -63.062 36.641  75.287  1.00 40.59 ? 438  ASP A CA    1 
ATOM   3165  C  C     . ASP A 1  440  ? -62.143 37.798  74.931  1.00 40.16 ? 438  ASP A C     1 
ATOM   3166  O  O     . ASP A 1  440  ? -61.595 38.463  75.819  1.00 38.20 ? 438  ASP A O     1 
ATOM   3167  C  CB    . ASP A 1  440  ? -64.222 37.129  76.148  1.00 41.64 ? 438  ASP A CB    1 
ATOM   3168  C  CG    . ASP A 1  440  ? -65.231 36.041  76.433  1.00 45.02 ? 438  ASP A CG    1 
ATOM   3169  O  OD1   . ASP A 1  440  ? -65.054 34.917  75.915  1.00 43.34 ? 438  ASP A OD1   1 
ATOM   3170  O  OD2   . ASP A 1  440  ? -66.194 36.310  77.182  1.00 41.84 ? 438  ASP A OD2   1 
ATOM   3171  N  N     . PHE A 1  441  ? -61.960 38.035  73.636  1.00 36.46 ? 439  PHE A N     1 
ATOM   3172  C  CA    . PHE A 1  441  ? -61.191 39.192  73.216  1.00 32.90 ? 439  PHE A CA    1 
ATOM   3173  C  C     . PHE A 1  441  ? -61.832 39.841  72.005  1.00 34.08 ? 439  PHE A C     1 
ATOM   3174  O  O     . PHE A 1  441  ? -62.371 39.164  71.127  1.00 31.30 ? 439  PHE A O     1 
ATOM   3175  C  CB    . PHE A 1  441  ? -59.734 38.852  72.877  1.00 29.99 ? 439  PHE A CB    1 
ATOM   3176  C  CG    . PHE A 1  441  ? -58.917 40.068  72.547  1.00 31.82 ? 439  PHE A CG    1 
ATOM   3177  C  CD1   . PHE A 1  441  ? -58.417 40.874  73.560  1.00 29.69 ? 439  PHE A CD1   1 
ATOM   3178  C  CD2   . PHE A 1  441  ? -58.693 40.437  71.229  1.00 28.02 ? 439  PHE A CD2   1 
ATOM   3179  C  CE1   . PHE A 1  441  ? -57.685 42.013  73.264  1.00 25.12 ? 439  PHE A CE1   1 
ATOM   3180  C  CE2   . PHE A 1  441  ? -57.971 41.584  70.929  1.00 29.28 ? 439  PHE A CE2   1 
ATOM   3181  C  CZ    . PHE A 1  441  ? -57.471 42.367  71.953  1.00 26.72 ? 439  PHE A CZ    1 
ATOM   3182  N  N     . HIS A 1  442  ? -61.754 41.163  71.976  1.00 30.24 ? 440  HIS A N     1 
ATOM   3183  C  CA    . HIS A 1  442  ? -62.064 41.958  70.806  1.00 30.11 ? 440  HIS A CA    1 
ATOM   3184  C  C     . HIS A 1  442  ? -61.077 43.108  70.775  1.00 30.36 ? 440  HIS A C     1 
ATOM   3185  O  O     . HIS A 1  442  ? -60.613 43.564  71.824  1.00 25.42 ? 440  HIS A O     1 
ATOM   3186  C  CB    . HIS A 1  442  ? -63.501 42.477  70.849  1.00 30.67 ? 440  HIS A CB    1 
ATOM   3187  C  CG    . HIS A 1  442  ? -63.836 43.216  72.106  1.00 29.54 ? 440  HIS A CG    1 
ATOM   3188  N  ND1   . HIS A 1  442  ? -63.740 44.588  72.210  1.00 28.96 ? 440  HIS A ND1   1 
ATOM   3189  C  CD2   . HIS A 1  442  ? -64.271 42.776  73.311  1.00 28.35 ? 440  HIS A CD2   1 
ATOM   3190  C  CE1   . HIS A 1  442  ? -64.100 44.961  73.425  1.00 28.12 ? 440  HIS A CE1   1 
ATOM   3191  N  NE2   . HIS A 1  442  ? -64.429 43.882  74.113  1.00 31.52 ? 440  HIS A NE2   1 
ATOM   3192  N  N     . VAL A 1  443  ? -60.734 43.562  69.568  1.00 29.38 ? 441  VAL A N     1 
ATOM   3193  C  CA    . VAL A 1  443  ? -59.856 44.719  69.465  1.00 31.91 ? 441  VAL A CA    1 
ATOM   3194  C  C     . VAL A 1  443  ? -60.550 45.906  70.114  1.00 26.08 ? 441  VAL A C     1 
ATOM   3195  O  O     . VAL A 1  443  ? -61.719 46.195  69.831  1.00 29.02 ? 441  VAL A O     1 
ATOM   3196  C  CB    . VAL A 1  443  ? -59.482 44.997  68.001  1.00 33.86 ? 441  VAL A CB    1 
ATOM   3197  C  CG1   . VAL A 1  443  ? -58.898 46.395  67.867  1.00 33.21 ? 441  VAL A CG1   1 
ATOM   3198  C  CG2   . VAL A 1  443  ? -58.478 43.962  67.513  1.00 35.50 ? 441  VAL A CG2   1 
ATOM   3199  N  N     . GLY A 1  444  ? -59.836 46.586  71.009  1.00 24.19 ? 442  GLY A N     1 
ATOM   3200  C  CA    . GLY A 1  444  ? -60.407 47.599  71.866  1.00 22.52 ? 442  GLY A CA    1 
ATOM   3201  C  C     . GLY A 1  444  ? -60.587 47.162  73.304  1.00 20.69 ? 442  GLY A C     1 
ATOM   3202  O  O     . GLY A 1  444  ? -60.779 48.014  74.176  1.00 20.74 ? 442  GLY A O     1 
ATOM   3203  N  N     . LYS A 1  445  ? -60.519 45.863  73.586  1.00 21.70 ? 443  LYS A N     1 
ATOM   3204  C  CA    . LYS A 1  445  ? -60.651 45.433  74.971  1.00 21.15 ? 443  LYS A CA    1 
ATOM   3205  C  C     . LYS A 1  445  ? -59.403 45.783  75.758  1.00 21.28 ? 443  LYS A C     1 
ATOM   3206  O  O     . LYS A 1  445  ? -59.479 46.400  76.828  1.00 21.73 ? 443  LYS A O     1 
ATOM   3207  C  CB    . LYS A 1  445  ? -60.924 43.936  75.052  1.00 22.81 ? 443  LYS A CB    1 
ATOM   3208  C  CG    . LYS A 1  445  ? -61.289 43.509  76.465  1.00 26.51 ? 443  LYS A CG    1 
ATOM   3209  C  CD    . LYS A 1  445  ? -61.737 42.069  76.545  1.00 34.58 ? 443  LYS A CD    1 
ATOM   3210  C  CE    . LYS A 1  445  ? -62.502 41.832  77.844  1.00 36.61 ? 443  LYS A CE    1 
ATOM   3211  N  NZ    . LYS A 1  445  ? -63.032 40.441  77.944  1.00 39.51 ? 443  LYS A NZ    1 
ATOM   3212  N  N     . TYR A 1  446  ? -58.247 45.380  75.245  1.00 19.41 ? 444  TYR A N     1 
ATOM   3213  C  CA    . TYR A 1  446  ? -56.959 45.751  75.812  1.00 19.42 ? 444  TYR A CA    1 
ATOM   3214  C  C     . TYR A 1  446  ? -55.911 45.511  74.738  1.00 20.30 ? 444  TYR A C     1 
ATOM   3215  O  O     . TYR A 1  446  ? -56.191 44.923  73.694  1.00 19.54 ? 444  TYR A O     1 
ATOM   3216  C  CB    . TYR A 1  446  ? -56.655 44.960  77.090  1.00 19.86 ? 444  TYR A CB    1 
ATOM   3217  C  CG    . TYR A 1  446  ? -56.239 43.523  76.852  1.00 22.09 ? 444  TYR A CG    1 
ATOM   3218  C  CD1   . TYR A 1  446  ? -57.179 42.490  76.806  1.00 28.42 ? 444  TYR A CD1   1 
ATOM   3219  C  CD2   . TYR A 1  446  ? -54.904 43.200  76.687  1.00 23.04 ? 444  TYR A CD2   1 
ATOM   3220  C  CE1   . TYR A 1  446  ? -56.774 41.179  76.590  1.00 24.32 ? 444  TYR A CE1   1 
ATOM   3221  C  CE2   . TYR A 1  446  ? -54.501 41.912  76.471  1.00 28.74 ? 444  TYR A CE2   1 
ATOM   3222  C  CZ    . TYR A 1  446  ? -55.431 40.908  76.424  1.00 26.35 ? 444  TYR A CZ    1 
ATOM   3223  O  OH    . TYR A 1  446  ? -54.978 39.619  76.212  1.00 36.81 ? 444  TYR A OH    1 
ATOM   3224  N  N     . GLU A 1  447  ? -54.692 45.970  74.994  1.00 17.49 ? 445  GLU A N     1 
ATOM   3225  C  CA    . GLU A 1  447  ? -53.613 45.661  74.066  1.00 18.35 ? 445  GLU A CA    1 
ATOM   3226  C  C     . GLU A 1  447  ? -52.329 45.511  74.854  1.00 19.28 ? 445  GLU A C     1 
ATOM   3227  O  O     . GLU A 1  447  ? -52.254 45.858  76.031  1.00 19.05 ? 445  GLU A O     1 
ATOM   3228  C  CB    . GLU A 1  447  ? -53.445 46.737  72.984  1.00 16.44 ? 445  GLU A CB    1 
ATOM   3229  C  CG    . GLU A 1  447  ? -53.046 48.095  73.550  1.00 18.46 ? 445  GLU A CG    1 
ATOM   3230  C  CD    . GLU A 1  447  ? -52.949 49.197  72.517  1.00 18.01 ? 445  GLU A CD    1 
ATOM   3231  O  OE1   . GLU A 1  447  ? -53.469 49.037  71.390  1.00 20.27 ? 445  GLU A OE1   1 
ATOM   3232  O  OE2   . GLU A 1  447  ? -52.336 50.237  72.840  1.00 17.41 ? 445  GLU A OE2   1 
ATOM   3233  N  N     . PHE A 1  448  ? -51.319 44.968  74.186  1.00 19.69 ? 446  PHE A N     1 
ATOM   3234  C  CA    . PHE A 1  448  ? -49.945 44.997  74.654  1.00 18.54 ? 446  PHE A CA    1 
ATOM   3235  C  C     . PHE A 1  448  ? -49.209 46.150  73.982  1.00 17.24 ? 446  PHE A C     1 
ATOM   3236  O  O     . PHE A 1  448  ? -49.676 46.701  72.981  1.00 18.01 ? 446  PHE A O     1 
ATOM   3237  C  CB    . PHE A 1  448  ? -49.250 43.674  74.342  1.00 19.94 ? 446  PHE A CB    1 
ATOM   3238  C  CG    . PHE A 1  448  ? -49.807 42.511  75.095  1.00 18.74 ? 446  PHE A CG    1 
ATOM   3239  C  CD1   . PHE A 1  448  ? -49.465 42.302  76.422  1.00 20.98 ? 446  PHE A CD1   1 
ATOM   3240  C  CD2   . PHE A 1  448  ? -50.667 41.620  74.474  1.00 20.83 ? 446  PHE A CD2   1 
ATOM   3241  C  CE1   . PHE A 1  448  ? -49.988 41.229  77.121  1.00 21.74 ? 446  PHE A CE1   1 
ATOM   3242  C  CE2   . PHE A 1  448  ? -51.192 40.539  75.169  1.00 22.78 ? 446  PHE A CE2   1 
ATOM   3243  C  CZ    . PHE A 1  448  ? -50.852 40.352  76.495  1.00 20.93 ? 446  PHE A CZ    1 
ATOM   3244  N  N     . GLN A 1  449  ? -48.052 46.518  74.541  1.00 17.43 ? 447  GLN A N     1 
ATOM   3245  C  CA    . GLN A 1  449  ? -47.202 47.538  73.929  1.00 16.92 ? 447  GLN A CA    1 
ATOM   3246  C  C     . GLN A 1  449  ? -45.737 47.163  74.102  1.00 18.44 ? 447  GLN A C     1 
ATOM   3247  O  O     . GLN A 1  449  ? -45.358 46.421  75.015  1.00 19.41 ? 447  GLN A O     1 
ATOM   3248  C  CB    . GLN A 1  449  ? -47.419 48.939  74.517  1.00 17.73 ? 447  GLN A CB    1 
ATOM   3249  C  CG    . GLN A 1  449  ? -48.844 49.412  74.445  1.00 16.55 ? 447  GLN A CG    1 
ATOM   3250  C  CD    . GLN A 1  449  ? -48.974 50.909  74.630  1.00 18.36 ? 447  GLN A CD    1 
ATOM   3251  O  OE1   . GLN A 1  449  ? -48.040 51.576  75.089  1.00 18.55 ? 447  GLN A OE1   1 
ATOM   3252  N  NE2   . GLN A 1  449  ? -50.131 51.448  74.273  1.00 17.40 ? 447  GLN A NE2   1 
ATOM   3253  N  N     . CYS A 1  450  ? -44.911 47.692  73.206  1.00 18.48 ? 448  CYS A N     1 
ATOM   3254  C  CA    . CYS A 1  450  ? -43.479 47.416  73.249  1.00 18.79 ? 448  CYS A CA    1 
ATOM   3255  C  C     . CYS A 1  450  ? -42.740 48.598  72.644  1.00 21.39 ? 448  CYS A C     1 
ATOM   3256  O  O     . CYS A 1  450  ? -43.344 49.512  72.076  1.00 19.38 ? 448  CYS A O     1 
ATOM   3257  C  CB    . CYS A 1  450  ? -43.133 46.111  72.516  1.00 20.99 ? 448  CYS A CB    1 
ATOM   3258  S  SG    . CYS A 1  450  ? -43.259 46.203  70.709  1.00 22.08 ? 448  CYS A SG    1 
ATOM   3259  N  N     . LEU A 1  451  ? -41.418 48.571  72.773  1.00 19.17 ? 449  LEU A N     1 
ATOM   3260  C  CA    . LEU A 1  451  ? -40.568 49.606  72.196  1.00 22.50 ? 449  LEU A CA    1 
ATOM   3261  C  C     . LEU A 1  451  ? -40.095 49.159  70.820  1.00 22.00 ? 449  LEU A C     1 
ATOM   3262  O  O     . LEU A 1  451  ? -39.814 47.976  70.598  1.00 23.78 ? 449  LEU A O     1 
ATOM   3263  C  CB    . LEU A 1  451  ? -39.360 49.902  73.097  1.00 21.57 ? 449  LEU A CB    1 
ATOM   3264  C  CG    . LEU A 1  451  ? -39.601 50.418  74.523  1.00 23.89 ? 449  LEU A CG    1 
ATOM   3265  C  CD1   . LEU A 1  451  ? -38.271 50.591  75.254  1.00 26.11 ? 449  LEU A CD1   1 
ATOM   3266  C  CD2   . LEU A 1  451  ? -40.381 51.719  74.546  1.00 24.72 ? 449  LEU A CD2   1 
ATOM   3267  N  N     . HIS A 1  452  ? -40.039 50.112  69.892  1.00 20.63 ? 450  HIS A N     1 
ATOM   3268  C  CA    . HIS A 1  452  ? -39.484 49.850  68.572  1.00 24.78 ? 450  HIS A CA    1 
ATOM   3269  C  C     . HIS A 1  452  ? -38.091 49.242  68.686  1.00 25.86 ? 450  HIS A C     1 
ATOM   3270  O  O     . HIS A 1  452  ? -37.297 49.635  69.541  1.00 24.74 ? 450  HIS A O     1 
ATOM   3271  C  CB    . HIS A 1  452  ? -39.417 51.152  67.769  1.00 24.12 ? 450  HIS A CB    1 
ATOM   3272  C  CG    . HIS A 1  452  ? -38.653 51.028  66.484  1.00 23.81 ? 450  HIS A CG    1 
ATOM   3273  N  ND1   . HIS A 1  452  ? -39.237 50.608  65.308  1.00 24.74 ? 450  HIS A ND1   1 
ATOM   3274  C  CD2   . HIS A 1  452  ? -37.353 51.272  66.194  1.00 26.88 ? 450  HIS A CD2   1 
ATOM   3275  C  CE1   . HIS A 1  452  ? -38.329 50.598  64.347  1.00 28.16 ? 450  HIS A CE1   1 
ATOM   3276  N  NE2   . HIS A 1  452  ? -37.176 50.994  64.860  1.00 24.53 ? 450  HIS A NE2   1 
ATOM   3277  N  N     . GLY A 1  453  ? -37.810 48.261  67.825  1.00 32.63 ? 451  GLY A N     1 
ATOM   3278  C  CA    . GLY A 1  453  ? -36.491 47.658  67.754  1.00 32.25 ? 451  GLY A CA    1 
ATOM   3279  C  C     . GLY A 1  453  ? -36.090 46.808  68.938  1.00 33.58 ? 451  GLY A C     1 
ATOM   3280  O  O     . GLY A 1  453  ? -34.958 46.306  68.961  1.00 41.71 ? 451  GLY A O     1 
ATOM   3281  N  N     . MET A 1  454  ? -36.949 46.643  69.919  1.00 32.40 ? 452  MET A N     1 
ATOM   3282  C  CA    . MET A 1  454  ? -36.651 45.803  71.072  1.00 29.06 ? 452  MET A CA    1 
ATOM   3283  C  C     . MET A 1  454  ? -37.708 44.737  71.285  1.00 31.13 ? 452  MET A C     1 
ATOM   3284  O  O     . MET A 1  454  ? -37.372 43.601  71.629  1.00 29.17 ? 452  MET A O     1 
ATOM   3285  C  CB    . MET A 1  454  ? -36.511 46.658  72.347  1.00 27.63 ? 452  MET A CB    1 
ATOM   3286  N  N     . GLY A 1  455  ? -38.974 45.059  71.052  1.00 27.59 ? 453  GLY A N     1 
ATOM   3287  C  CA    . GLY A 1  455  ? -40.031 44.116  71.353  1.00 29.48 ? 453  GLY A CA    1 
ATOM   3288  C  C     . GLY A 1  455  ? -40.590 43.360  70.168  1.00 28.25 ? 453  GLY A C     1 
ATOM   3289  O  O     . GLY A 1  455  ? -41.397 42.448  70.353  1.00 25.75 ? 453  GLY A O     1 
ATOM   3290  N  N     . GLU A 1  456  ? -40.191 43.726  68.949  1.00 29.44 ? 454  GLU A N     1 
ATOM   3291  C  CA    . GLU A 1  456  ? -40.715 43.032  67.775  1.00 29.39 ? 454  GLU A CA    1 
ATOM   3292  C  C     . GLU A 1  456  ? -40.454 41.532  67.787  1.00 29.01 ? 454  GLU A C     1 
ATOM   3293  O  O     . GLU A 1  456  ? -41.378 40.781  67.433  1.00 30.30 ? 454  GLU A O     1 
ATOM   3294  C  CB    . GLU A 1  456  ? -40.155 43.644  66.487  1.00 34.06 ? 454  GLU A CB    1 
ATOM   3295  C  CG    . GLU A 1  456  ? -40.693 45.018  66.176  1.00 37.01 ? 454  GLU A CG    1 
ATOM   3296  C  CD    . GLU A 1  456  ? -39.831 46.106  66.745  1.00 32.64 ? 454  GLU A CD    1 
ATOM   3297  O  OE1   . GLU A 1  456  ? -39.022 45.807  67.649  1.00 35.58 ? 454  GLU A OE1   1 
ATOM   3298  O  OE2   . GLU A 1  456  ? -39.944 47.259  66.281  1.00 30.78 ? 454  GLU A OE2   1 
ATOM   3299  N  N     . PRO A 1  457  ? -39.267 41.028  68.153  1.00 30.76 ? 455  PRO A N     1 
ATOM   3300  C  CA    . PRO A 1  457  ? -39.103 39.564  68.206  1.00 32.86 ? 455  PRO A CA    1 
ATOM   3301  C  C     . PRO A 1  457  ? -40.133 38.881  69.090  1.00 32.24 ? 455  PRO A C     1 
ATOM   3302  O  O     . PRO A 1  457  ? -40.746 37.888  68.676  1.00 31.86 ? 455  PRO A O     1 
ATOM   3303  C  CB    . PRO A 1  457  ? -37.679 39.394  68.746  1.00 30.99 ? 455  PRO A CB    1 
ATOM   3304  C  CG    . PRO A 1  457  ? -36.978 40.645  68.369  1.00 35.51 ? 455  PRO A CG    1 
ATOM   3305  C  CD    . PRO A 1  457  ? -38.013 41.725  68.492  1.00 30.95 ? 455  PRO A CD    1 
ATOM   3306  N  N     . LEU A 1  458  ? -40.342 39.398  70.302  1.00 31.34 ? 456  LEU A N     1 
ATOM   3307  C  CA    . LEU A 1  458  ? -41.349 38.822  71.190  1.00 28.09 ? 456  LEU A CA    1 
ATOM   3308  C  C     . LEU A 1  458  ? -42.741 38.939  70.589  1.00 28.37 ? 456  LEU A C     1 
ATOM   3309  O  O     . LEU A 1  458  ? -43.483 37.956  70.512  1.00 26.28 ? 456  LEU A O     1 
ATOM   3310  C  CB    . LEU A 1  458  ? -41.306 39.512  72.553  1.00 25.56 ? 456  LEU A CB    1 
ATOM   3311  C  CG    . LEU A 1  458  ? -42.409 39.097  73.534  1.00 25.27 ? 456  LEU A CG    1 
ATOM   3312  C  CD1   . LEU A 1  458  ? -42.426 37.577  73.753  1.00 26.06 ? 456  LEU A CD1   1 
ATOM   3313  C  CD2   . LEU A 1  458  ? -42.210 39.825  74.851  1.00 26.25 ? 456  LEU A CD2   1 
ATOM   3314  N  N     . TYR A 1  459  ? -43.119 40.136  70.157  1.00 26.79 ? 457  TYR A N     1 
ATOM   3315  C  CA    . TYR A 1  459  ? -44.507 40.306  69.764  1.00 26.67 ? 457  TYR A CA    1 
ATOM   3316  C  C     . TYR A 1  459  ? -44.817 39.772  68.373  1.00 27.71 ? 457  TYR A C     1 
ATOM   3317  O  O     . TYR A 1  459  ? -45.998 39.611  68.046  1.00 27.68 ? 457  TYR A O     1 
ATOM   3318  C  CB    . TYR A 1  459  ? -44.897 41.771  69.918  1.00 24.83 ? 457  TYR A CB    1 
ATOM   3319  C  CG    . TYR A 1  459  ? -45.141 42.070  71.374  1.00 24.32 ? 457  TYR A CG    1 
ATOM   3320  C  CD1   . TYR A 1  459  ? -46.352 41.727  71.962  1.00 23.74 ? 457  TYR A CD1   1 
ATOM   3321  C  CD2   . TYR A 1  459  ? -44.157 42.641  72.173  1.00 22.72 ? 457  TYR A CD2   1 
ATOM   3322  C  CE1   . TYR A 1  459  ? -46.586 41.965  73.287  1.00 21.25 ? 457  TYR A CE1   1 
ATOM   3323  C  CE2   . TYR A 1  459  ? -44.395 42.890  73.523  1.00 20.66 ? 457  TYR A CE2   1 
ATOM   3324  C  CZ    . TYR A 1  459  ? -45.616 42.547  74.068  1.00 22.61 ? 457  TYR A CZ    1 
ATOM   3325  O  OH    . TYR A 1  459  ? -45.889 42.775  75.402  1.00 22.88 ? 457  TYR A OH    1 
ATOM   3326  N  N     . GLU A 1  460  ? -43.806 39.450  67.564  1.00 27.92 ? 458  GLU A N     1 
ATOM   3327  C  CA    . GLU A 1  460  ? -44.061 38.664  66.362  1.00 30.55 ? 458  GLU A CA    1 
ATOM   3328  C  C     . GLU A 1  460  ? -44.562 37.265  66.699  1.00 32.24 ? 458  GLU A C     1 
ATOM   3329  O  O     . GLU A 1  460  ? -45.135 36.592  65.833  1.00 31.15 ? 458  GLU A O     1 
ATOM   3330  C  CB    . GLU A 1  460  ? -42.794 38.581  65.507  1.00 34.55 ? 458  GLU A CB    1 
ATOM   3331  N  N     . GLU A 1  461  ? -44.371 36.821  67.939  1.00 28.77 ? 459  GLU A N     1 
ATOM   3332  C  CA    . GLU A 1  461  ? -44.930 35.572  68.437  1.00 31.73 ? 459  GLU A CA    1 
ATOM   3333  C  C     . GLU A 1  461  ? -46.270 35.766  69.138  1.00 31.31 ? 459  GLU A C     1 
ATOM   3334  O  O     . GLU A 1  461  ? -46.810 34.804  69.695  1.00 31.28 ? 459  GLU A O     1 
ATOM   3335  C  CB    . GLU A 1  461  ? -43.946 34.901  69.395  1.00 30.76 ? 459  GLU A CB    1 
ATOM   3336  C  CG    . GLU A 1  461  ? -42.561 34.726  68.825  1.00 33.78 ? 459  GLU A CG    1 
ATOM   3337  C  CD    . GLU A 1  461  ? -42.518 33.775  67.636  1.00 38.35 ? 459  GLU A CD    1 
ATOM   3338  O  OE1   . GLU A 1  461  ? -43.475 32.990  67.447  1.00 37.99 ? 459  GLU A OE1   1 
ATOM   3339  O  OE2   . GLU A 1  461  ? -41.512 33.816  66.892  1.00 40.75 ? 459  GLU A OE2   1 
ATOM   3340  N  N     . VAL A 1  462  ? -46.813 36.983  69.122  1.00 30.40 ? 460  VAL A N     1 
ATOM   3341  C  CA    . VAL A 1  462  ? -48.051 37.320  69.814  1.00 27.18 ? 460  VAL A CA    1 
ATOM   3342  C  C     . VAL A 1  462  ? -49.111 37.821  68.841  1.00 30.16 ? 460  VAL A C     1 
ATOM   3343  O  O     . VAL A 1  462  ? -50.235 37.307  68.807  1.00 30.06 ? 460  VAL A O     1 
ATOM   3344  C  CB    . VAL A 1  462  ? -47.801 38.362  70.929  1.00 27.88 ? 460  VAL A CB    1 
ATOM   3345  C  CG1   . VAL A 1  462  ? -49.121 38.783  71.571  1.00 26.21 ? 460  VAL A CG1   1 
ATOM   3346  C  CG2   . VAL A 1  462  ? -46.842 37.812  71.968  1.00 27.25 ? 460  VAL A CG2   1 
ATOM   3347  N  N     . VAL A 1  463  ? -48.766 38.826  68.037  1.00 29.12 ? 461  VAL A N     1 
ATOM   3348  C  CA    . VAL A 1  463  ? -49.721 39.432  67.117  1.00 28.80 ? 461  VAL A CA    1 
ATOM   3349  C  C     . VAL A 1  463  ? -50.095 38.445  66.020  1.00 32.78 ? 461  VAL A C     1 
ATOM   3350  O  O     . VAL A 1  463  ? -49.243 37.711  65.501  1.00 36.04 ? 461  VAL A O     1 
ATOM   3351  C  CB    . VAL A 1  463  ? -49.123 40.715  66.519  1.00 26.95 ? 461  VAL A CB    1 
ATOM   3352  C  CG1   . VAL A 1  463  ? -50.068 41.315  65.489  1.00 29.80 ? 461  VAL A CG1   1 
ATOM   3353  C  CG2   . VAL A 1  463  ? -48.811 41.719  67.618  1.00 28.24 ? 461  VAL A CG2   1 
ATOM   3354  N  N     . GLY A 1  464  ? -51.367 38.428  65.657  1.00 32.04 ? 462  GLY A N     1 
ATOM   3355  C  CA    . GLY A 1  464  ? -51.776 37.650  64.509  1.00 35.86 ? 462  GLY A CA    1 
ATOM   3356  C  C     . GLY A 1  464  ? -52.524 36.390  64.907  1.00 36.56 ? 462  GLY A C     1 
ATOM   3357  O  O     . GLY A 1  464  ? -52.259 35.775  65.950  1.00 36.18 ? 462  GLY A O     1 
ATOM   3358  N  N     . ARG A 1  465  ? -53.472 35.990  64.050  1.00 36.74 ? 463  ARG A N     1 
ATOM   3359  C  CA    . ARG A 1  465  ? -54.271 34.798  64.318  1.00 34.42 ? 463  ARG A CA    1 
ATOM   3360  C  C     . ARG A 1  465  ? -53.409 33.548  64.414  1.00 38.56 ? 463  ARG A C     1 
ATOM   3361  O  O     . ARG A 1  465  ? -53.777 32.591  65.101  1.00 41.28 ? 463  ARG A O     1 
ATOM   3362  C  CB    . ARG A 1  465  ? -55.340 34.626  63.238  1.00 39.64 ? 463  ARG A CB    1 
ATOM   3363  N  N     . GLY A 1  466  ? -52.264 33.534  63.738  1.00 36.00 ? 464  GLY A N     1 
ATOM   3364  C  CA    . GLY A 1  466  ? -51.361 32.400  63.827  1.00 37.25 ? 464  GLY A CA    1 
ATOM   3365  C  C     . GLY A 1  466  ? -50.570 32.331  65.116  1.00 40.00 ? 464  GLY A C     1 
ATOM   3366  O  O     . GLY A 1  466  ? -49.836 31.358  65.317  1.00 38.57 ? 464  GLY A O     1 
ATOM   3367  N  N     . LYS A 1  467  ? -50.700 33.336  65.991  1.00 37.36 ? 465  LYS A N     1 
ATOM   3368  C  CA    . LYS A 1  467  ? -49.974 33.347  67.260  1.00 32.15 ? 465  LYS A CA    1 
ATOM   3369  C  C     . LYS A 1  467  ? -51.019 33.420  68.365  1.00 33.96 ? 465  LYS A C     1 
ATOM   3370  O  O     . LYS A 1  467  ? -51.891 32.559  68.430  1.00 37.36 ? 465  LYS A O     1 
ATOM   3371  C  CB    . LYS A 1  467  ? -48.949 34.461  67.291  1.00 33.44 ? 465  LYS A CB    1 
ATOM   3372  C  CG    . LYS A 1  467  ? -47.911 34.397  66.182  1.00 36.12 ? 465  LYS A CG    1 
ATOM   3373  C  CD    . LYS A 1  467  ? -47.059 33.147  66.287  1.00 37.03 ? 465  LYS A CD    1 
ATOM   3374  C  CE    . LYS A 1  467  ? -45.918 33.183  65.283  1.00 36.52 ? 465  LYS A CE    1 
ATOM   3375  N  NZ    . LYS A 1  467  ? -44.991 32.036  65.484  1.00 37.96 ? 465  LYS A NZ    1 
ATOM   3376  N  N     . LEU A 1  468  ? -50.950 34.426  69.236  1.00 34.18 ? 466  LEU A N     1 
ATOM   3377  C  CA    . LEU A 1  468  ? -51.922 34.605  70.305  1.00 31.69 ? 466  LEU A CA    1 
ATOM   3378  C  C     . LEU A 1  468  ? -53.080 35.507  69.903  1.00 31.46 ? 466  LEU A C     1 
ATOM   3379  O  O     . LEU A 1  468  ? -54.059 35.602  70.650  1.00 31.38 ? 466  LEU A O     1 
ATOM   3380  C  CB    . LEU A 1  468  ? -51.231 35.174  71.549  1.00 31.77 ? 466  LEU A CB    1 
ATOM   3381  C  CG    . LEU A 1  468  ? -50.022 34.370  72.033  1.00 32.46 ? 466  LEU A CG    1 
ATOM   3382  C  CD1   . LEU A 1  468  ? -49.501 34.891  73.369  1.00 31.57 ? 466  LEU A CD1   1 
ATOM   3383  C  CD2   . LEU A 1  468  ? -50.376 32.894  72.127  1.00 32.51 ? 466  LEU A CD2   1 
ATOM   3384  N  N     . ASP A 1  469  ? -52.987 36.161  68.745  1.00 32.60 ? 467  ASP A N     1 
ATOM   3385  C  CA    . ASP A 1  469  ? -54.053 37.013  68.218  1.00 30.68 ? 467  ASP A CA    1 
ATOM   3386  C  C     . ASP A 1  469  ? -54.405 38.118  69.209  1.00 28.61 ? 467  ASP A C     1 
ATOM   3387  O  O     . ASP A 1  469  ? -55.573 38.388  69.495  1.00 29.34 ? 467  ASP A O     1 
ATOM   3388  C  CB    . ASP A 1  469  ? -55.289 36.192  67.848  1.00 33.81 ? 467  ASP A CB    1 
ATOM   3389  C  CG    . ASP A 1  469  ? -56.207 36.927  66.895  1.00 35.22 ? 467  ASP A CG    1 
ATOM   3390  O  OD1   . ASP A 1  469  ? -55.731 37.848  66.204  1.00 36.38 ? 467  ASP A OD1   1 
ATOM   3391  O  OD2   . ASP A 1  469  ? -57.408 36.590  66.842  1.00 40.49 ? 467  ASP A OD2   1 
ATOM   3392  N  N     . ARG A 1  470  ? -53.371 38.747  69.751  1.00 30.32 ? 468  ARG A N     1 
ATOM   3393  C  CA    . ARG A 1  470  ? -53.499 39.930  70.572  1.00 26.46 ? 468  ARG A CA    1 
ATOM   3394  C  C     . ARG A 1  470  ? -52.688 41.060  69.956  1.00 27.02 ? 468  ARG A C     1 
ATOM   3395  O  O     . ARG A 1  470  ? -51.569 40.835  69.481  1.00 26.35 ? 468  ARG A O     1 
ATOM   3396  C  CB    . ARG A 1  470  ? -53.017 39.674  72.009  1.00 26.55 ? 468  ARG A CB    1 
ATOM   3397  C  CG    . ARG A 1  470  ? -53.789 38.570  72.730  1.00 25.54 ? 468  ARG A CG    1 
ATOM   3398  C  CD    . ARG A 1  470  ? -55.231 38.954  72.978  1.00 26.87 ? 468  ARG A CD    1 
ATOM   3399  N  NE    . ARG A 1  470  ? -55.966 37.883  73.646  1.00 29.25 ? 468  ARG A NE    1 
ATOM   3400  C  CZ    . ARG A 1  470  ? -56.747 37.006  73.029  1.00 29.55 ? 468  ARG A CZ    1 
ATOM   3401  N  NH1   . ARG A 1  470  ? -56.915 37.032  71.717  1.00 29.48 ? 468  ARG A NH1   1 
ATOM   3402  N  NH2   . ARG A 1  470  ? -57.384 36.084  73.748  1.00 30.64 ? 468  ARG A NH2   1 
ATOM   3403  N  N     . PRO A 1  471  ? -53.224 42.272  69.937  1.00 24.73 ? 469  PRO A N     1 
ATOM   3404  C  CA    . PRO A 1  471  ? -52.531 43.381  69.281  1.00 22.54 ? 469  PRO A CA    1 
ATOM   3405  C  C     . PRO A 1  471  ? -51.428 43.953  70.152  1.00 23.40 ? 469  PRO A C     1 
ATOM   3406  O  O     . PRO A 1  471  ? -51.418 43.818  71.376  1.00 22.11 ? 469  PRO A O     1 
ATOM   3407  C  CB    . PRO A 1  471  ? -53.645 44.408  69.073  1.00 23.62 ? 469  PRO A CB    1 
ATOM   3408  C  CG    . PRO A 1  471  ? -54.554 44.169  70.252  1.00 23.17 ? 469  PRO A CG    1 
ATOM   3409  C  CD    . PRO A 1  471  ? -54.542 42.670  70.455  1.00 25.19 ? 469  PRO A CD    1 
ATOM   3410  N  N     . CYS A 1  472  ? -50.483 44.604  69.483  1.00 23.19 ? 470  CYS A N     1 
ATOM   3411  C  CA    . CYS A 1  472  ? -49.373 45.258  70.154  1.00 20.43 ? 470  CYS A CA    1 
ATOM   3412  C  C     . CYS A 1  472  ? -49.160 46.614  69.517  1.00 21.00 ? 470  CYS A C     1 
ATOM   3413  O  O     . CYS A 1  472  ? -49.131 46.723  68.288  1.00 23.77 ? 470  CYS A O     1 
ATOM   3414  C  CB    . CYS A 1  472  ? -48.082 44.434  70.063  1.00 20.22 ? 470  CYS A CB    1 
ATOM   3415  S  SG    . CYS A 1  472  ? -46.691 45.167  70.944  1.00 22.94 ? 470  CYS A SG    1 
ATOM   3416  N  N     . ARG A 1  473  ? -49.024 47.640  70.349  1.00 18.03 ? 471  ARG A N     1 
ATOM   3417  C  CA    . ARG A 1  473  ? -48.716 48.988  69.890  1.00 17.69 ? 471  ARG A CA    1 
ATOM   3418  C  C     . ARG A 1  473  ? -47.227 49.225  70.097  1.00 17.01 ? 471  ARG A C     1 
ATOM   3419  O  O     . ARG A 1  473  ? -46.727 49.128  71.223  1.00 18.83 ? 471  ARG A O     1 
ATOM   3420  C  CB    . ARG A 1  473  ? -49.541 50.037  70.633  1.00 17.22 ? 471  ARG A CB    1 
ATOM   3421  C  CG    . ARG A 1  473  ? -49.377 51.457  70.065  1.00 18.71 ? 471  ARG A CG    1 
ATOM   3422  C  CD    . ARG A 1  473  ? -50.299 52.429  70.768  1.00 18.59 ? 471  ARG A CD    1 
ATOM   3423  N  NE    . ARG A 1  473  ? -51.666 51.928  70.711  1.00 17.61 ? 471  ARG A NE    1 
ATOM   3424  C  CZ    . ARG A 1  473  ? -52.481 52.081  69.675  1.00 20.87 ? 471  ARG A CZ    1 
ATOM   3425  N  NH1   . ARG A 1  473  ? -52.160 52.851  68.642  1.00 19.83 ? 471  ARG A NH1   1 
ATOM   3426  N  NH2   . ARG A 1  473  ? -53.643 51.435  69.667  1.00 17.43 ? 471  ARG A NH2   1 
ATOM   3427  N  N     . ILE A 1  474  ? -46.530 49.548  69.016  1.00 19.68 ? 472  ILE A N     1 
ATOM   3428  C  CA    . ILE A 1  474  ? -45.095 49.803  69.063  1.00 18.56 ? 472  ILE A CA    1 
ATOM   3429  C  C     . ILE A 1  474  ? -44.859 51.262  69.411  1.00 18.42 ? 472  ILE A C     1 
ATOM   3430  O  O     . ILE A 1  474  ? -45.377 52.162  68.736  1.00 20.69 ? 472  ILE A O     1 
ATOM   3431  C  CB    . ILE A 1  474  ? -44.437 49.448  67.724  1.00 17.93 ? 472  ILE A CB    1 
ATOM   3432  C  CG1   . ILE A 1  474  ? -44.660 47.963  67.429  1.00 22.97 ? 472  ILE A CG1   1 
ATOM   3433  C  CG2   . ILE A 1  474  ? -42.956 49.858  67.736  1.00 19.48 ? 472  ILE A CG2   1 
ATOM   3434  C  CD1   . ILE A 1  474  ? -44.249 47.549  66.020  1.00 26.23 ? 472  ILE A CD1   1 
ATOM   3435  N  N     . TYR A 1  475  ? -44.063 51.498  70.455  1.00 17.64 ? 473  TYR A N     1 
ATOM   3436  C  CA    . TYR A 1  475  ? -43.673 52.851  70.845  1.00 18.30 ? 473  TYR A CA    1 
ATOM   3437  C  C     . TYR A 1  475  ? -42.496 53.262  69.972  1.00 19.12 ? 473  TYR A C     1 
ATOM   3438  O  O     . TYR A 1  475  ? -41.407 52.694  70.089  1.00 19.00 ? 473  TYR A O     1 
ATOM   3439  C  CB    . TYR A 1  475  ? -43.305 52.896  72.325  1.00 21.05 ? 473  TYR A CB    1 
ATOM   3440  C  CG    . TYR A 1  475  ? -43.136 54.286  72.917  1.00 19.93 ? 473  TYR A CG    1 
ATOM   3441  C  CD1   . TYR A 1  475  ? -44.242 55.014  73.354  1.00 21.53 ? 473  TYR A CD1   1 
ATOM   3442  C  CD2   . TYR A 1  475  ? -41.877 54.862  73.056  1.00 20.14 ? 473  TYR A CD2   1 
ATOM   3443  C  CE1   . TYR A 1  475  ? -44.105 56.280  73.900  1.00 19.96 ? 473  TYR A CE1   1 
ATOM   3444  C  CE2   . TYR A 1  475  ? -41.724 56.139  73.602  1.00 20.31 ? 473  TYR A CE2   1 
ATOM   3445  C  CZ    . TYR A 1  475  ? -42.849 56.840  74.016  1.00 21.36 ? 473  TYR A CZ    1 
ATOM   3446  O  OH    . TYR A 1  475  ? -42.716 58.105  74.546  1.00 22.72 ? 473  TYR A OH    1 
ATOM   3447  N  N     . ALA A 1  476  ? -42.707 54.257  69.117  1.00 19.83 ? 474  ALA A N     1 
ATOM   3448  C  CA    . ALA A 1  476  ? -41.767 54.563  68.042  1.00 19.21 ? 474  ALA A CA    1 
ATOM   3449  C  C     . ALA A 1  476  ? -41.065 55.890  68.281  1.00 18.92 ? 474  ALA A C     1 
ATOM   3450  O  O     . ALA A 1  476  ? -41.681 56.950  68.097  1.00 19.13 ? 474  ALA A O     1 
ATOM   3451  C  CB    . ALA A 1  476  ? -42.511 54.586  66.704  1.00 22.24 ? 474  ALA A CB    1 
ATOM   3452  N  N     . PRO A 1  477  ? -39.784 55.895  68.650  1.00 19.96 ? 475  PRO A N     1 
ATOM   3453  C  CA    . PRO A 1  477  ? -39.068 57.165  68.780  1.00 20.15 ? 475  PRO A CA    1 
ATOM   3454  C  C     . PRO A 1  477  ? -38.808 57.761  67.407  1.00 19.06 ? 475  PRO A C     1 
ATOM   3455  O  O     . PRO A 1  477  ? -38.548 57.047  66.437  1.00 21.40 ? 475  PRO A O     1 
ATOM   3456  C  CB    . PRO A 1  477  ? -37.755 56.771  69.473  1.00 24.45 ? 475  PRO A CB    1 
ATOM   3457  C  CG    . PRO A 1  477  ? -37.909 55.312  69.849  1.00 25.76 ? 475  PRO A CG    1 
ATOM   3458  C  CD    . PRO A 1  477  ? -38.900 54.744  68.882  1.00 21.56 ? 475  PRO A CD    1 
ATOM   3459  N  N     . VAL A 1  478  ? -38.890 59.081  67.330  1.00 19.05 ? 476  VAL A N     1 
ATOM   3460  C  CA    . VAL A 1  478  ? -38.697 59.808  66.085  1.00 21.86 ? 476  VAL A CA    1 
ATOM   3461  C  C     . VAL A 1  478  ? -37.714 60.936  66.347  1.00 24.30 ? 476  VAL A C     1 
ATOM   3462  O  O     . VAL A 1  478  ? -37.903 61.723  67.281  1.00 25.24 ? 476  VAL A O     1 
ATOM   3463  C  CB    . VAL A 1  478  ? -40.028 60.364  65.550  1.00 21.23 ? 476  VAL A CB    1 
ATOM   3464  C  CG1   . VAL A 1  478  ? -39.815 61.131  64.246  1.00 22.19 ? 476  VAL A CG1   1 
ATOM   3465  C  CG2   . VAL A 1  478  ? -41.025 59.223  65.347  1.00 22.61 ? 476  VAL A CG2   1 
ATOM   3466  N  N     . GLY A 1  479  ? -36.666 61.010  65.543  1.00 23.32 ? 477  GLY A N     1 
ATOM   3467  C  CA    . GLY A 1  479  ? -35.738 62.107  65.707  1.00 26.18 ? 477  GLY A CA    1 
ATOM   3468  C  C     . GLY A 1  479  ? -34.448 61.862  64.967  1.00 27.99 ? 477  GLY A C     1 
ATOM   3469  O  O     . GLY A 1  479  ? -34.136 60.745  64.548  1.00 24.05 ? 477  GLY A O     1 
ATOM   3470  N  N     . THR A 1  480  ? -33.690 62.943  64.805  1.00 33.29 ? 478  THR A N     1 
ATOM   3471  C  CA    . THR A 1  480  ? -32.411 62.885  64.113  1.00 34.94 ? 478  THR A CA    1 
ATOM   3472  C  C     . THR A 1  480  ? -31.369 62.184  64.982  1.00 39.08 ? 478  THR A C     1 
ATOM   3473  O  O     . THR A 1  480  ? -31.595 61.884  66.159  1.00 41.40 ? 478  THR A O     1 
ATOM   3474  C  CB    . THR A 1  480  ? -31.929 64.291  63.763  1.00 36.54 ? 478  THR A CB    1 
ATOM   3475  O  OG1   . THR A 1  480  ? -31.647 64.999  64.976  1.00 41.35 ? 478  THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1  480  ? -32.993 65.039  62.977  1.00 37.74 ? 478  THR A CG2   1 
ATOM   3477  N  N     . HIS A 1  481  ? -30.201 61.932  64.382  1.00 42.60 ? 479  HIS A N     1 
ATOM   3478  C  CA    . HIS A 1  481  ? -29.108 61.293  65.110  1.00 43.95 ? 479  HIS A CA    1 
ATOM   3479  C  C     . HIS A 1  481  ? -28.698 62.111  66.329  1.00 49.56 ? 479  HIS A C     1 
ATOM   3480  O  O     . HIS A 1  481  ? -28.452 61.555  67.406  1.00 53.17 ? 479  HIS A O     1 
ATOM   3481  C  CB    . HIS A 1  481  ? -27.912 61.082  64.179  1.00 43.27 ? 479  HIS A CB    1 
ATOM   3482  N  N     . GLU A 1  482  ? -28.617 63.436  66.178  1.00 52.10 ? 480  GLU A N     1 
ATOM   3483  C  CA    . GLU A 1  482  ? -28.262 64.290  67.308  1.00 54.50 ? 480  GLU A CA    1 
ATOM   3484  C  C     . GLU A 1  482  ? -29.277 64.160  68.438  1.00 56.56 ? 480  GLU A C     1 
ATOM   3485  O  O     . GLU A 1  482  ? -28.901 64.033  69.610  1.00 58.75 ? 480  GLU A O     1 
ATOM   3486  C  CB    . GLU A 1  482  ? -28.145 65.743  66.848  1.00 54.11 ? 480  GLU A CB    1 
ATOM   3487  N  N     . THR A 1  483  ? -30.572 64.166  68.104  1.00 53.83 ? 481  THR A N     1 
ATOM   3488  C  CA    . THR A 1  483  ? -31.603 64.078  69.131  1.00 54.79 ? 481  THR A CA    1 
ATOM   3489  C  C     . THR A 1  483  ? -31.648 62.697  69.774  1.00 58.33 ? 481  THR A C     1 
ATOM   3490  O  O     . THR A 1  483  ? -31.957 62.581  70.966  1.00 60.34 ? 481  THR A O     1 
ATOM   3491  C  CB    . THR A 1  483  ? -32.969 64.431  68.538  1.00 43.66 ? 481  THR A CB    1 
ATOM   3492  N  N     . LEU A 1  484  ? -31.340 61.643  69.010  1.00 56.51 ? 482  LEU A N     1 
ATOM   3493  C  CA    . LEU A 1  484  ? -31.419 60.287  69.548  1.00 58.00 ? 482  LEU A CA    1 
ATOM   3494  C  C     . LEU A 1  484  ? -30.334 60.033  70.589  1.00 65.64 ? 482  LEU A C     1 
ATOM   3495  O  O     . LEU A 1  484  ? -30.601 59.437  71.639  1.00 67.98 ? 482  LEU A O     1 
ATOM   3496  C  CB    . LEU A 1  484  ? -31.324 59.264  68.414  1.00 52.30 ? 482  LEU A CB    1 
ATOM   3497  N  N     . LEU A 1  485  ? -29.106 60.480  70.318  1.00 71.44 ? 483  LEU A N     1 
ATOM   3498  C  CA    . LEU A 1  485  ? -27.996 60.240  71.234  1.00 71.60 ? 483  LEU A CA    1 
ATOM   3499  C  C     . LEU A 1  485  ? -28.182 60.921  72.584  1.00 78.25 ? 483  LEU A C     1 
ATOM   3500  O  O     . LEU A 1  485  ? -27.464 60.578  73.530  1.00 76.45 ? 483  LEU A O     1 
ATOM   3501  C  CB    . LEU A 1  485  ? -26.686 60.708  70.595  1.00 66.46 ? 483  LEU A CB    1 
ATOM   3502  N  N     . ALA A 1  486  ? -29.138 61.849  72.700  1.00 90.28 ? 484  ALA A N     1 
ATOM   3503  C  CA    . ALA A 1  486  ? -29.278 62.641  73.919  1.00 86.92 ? 484  ALA A CA    1 
ATOM   3504  C  C     . ALA A 1  486  ? -29.543 61.765  75.138  1.00 90.91 ? 484  ALA A C     1 
ATOM   3505  O  O     . ALA A 1  486  ? -28.953 61.983  76.203  1.00 93.28 ? 484  ALA A O     1 
ATOM   3506  C  CB    . ALA A 1  486  ? -30.395 63.669  73.745  1.00 86.71 ? 484  ALA A CB    1 
ATOM   3507  N  N     . TYR A 1  487  ? -30.422 60.776  75.009  1.00 75.85 ? 485  TYR A N     1 
ATOM   3508  C  CA    . TYR A 1  487  ? -30.778 59.941  76.151  1.00 71.75 ? 485  TYR A CA    1 
ATOM   3509  C  C     . TYR A 1  487  ? -31.073 58.512  75.696  1.00 69.82 ? 485  TYR A C     1 
ATOM   3510  O  O     . TYR A 1  487  ? -32.083 57.911  76.068  1.00 64.08 ? 485  TYR A O     1 
ATOM   3511  C  CB    . TYR A 1  487  ? -31.960 60.540  76.914  1.00 76.29 ? 485  TYR A CB    1 
ATOM   3512  N  N     . LEU A 1  488  ? -30.180 57.946  74.884  1.00 65.76 ? 486  LEU A N     1 
ATOM   3513  C  CA    . LEU A 1  488  ? -30.284 56.537  74.521  1.00 60.34 ? 486  LEU A CA    1 
ATOM   3514  C  C     . LEU A 1  488  ? -29.725 55.608  75.594  1.00 57.18 ? 486  LEU A C     1 
ATOM   3515  O  O     . LEU A 1  488  ? -29.939 54.391  75.513  1.00 53.61 ? 486  LEU A O     1 
ATOM   3516  C  CB    . LEU A 1  488  ? -29.566 56.283  73.192  1.00 54.36 ? 486  LEU A CB    1 
ATOM   3517  N  N     . VAL A 1  489  ? -29.024 56.150  76.597  1.00 55.30 ? 487  VAL A N     1 
ATOM   3518  C  CA    . VAL A 1  489  ? -28.406 55.314  77.619  1.00 51.34 ? 487  VAL A CA    1 
ATOM   3519  C  C     . VAL A 1  489  ? -29.459 54.605  78.464  1.00 54.28 ? 487  VAL A C     1 
ATOM   3520  O  O     . VAL A 1  489  ? -29.205 53.513  78.983  1.00 51.93 ? 487  VAL A O     1 
ATOM   3521  C  CB    . VAL A 1  489  ? -27.460 56.153  78.498  1.00 45.77 ? 487  VAL A CB    1 
ATOM   3522  N  N     . ARG A 1  490  ? -30.650 55.195  78.610  1.00 55.53 ? 488  ARG A N     1 
ATOM   3523  C  CA    . ARG A 1  490  ? -31.664 54.626  79.499  1.00 58.65 ? 488  ARG A CA    1 
ATOM   3524  C  C     . ARG A 1  490  ? -32.101 53.239  79.035  1.00 54.71 ? 488  ARG A C     1 
ATOM   3525  O  O     . ARG A 1  490  ? -32.044 52.269  79.803  1.00 51.95 ? 488  ARG A O     1 
ATOM   3526  C  CB    . ARG A 1  490  ? -32.864 55.568  79.595  1.00 56.86 ? 488  ARG A CB    1 
ATOM   3527  N  N     . ARG A 1  491  ? -32.535 53.122  77.775  1.00 57.10 ? 489  ARG A N     1 
ATOM   3528  C  CA    . ARG A 1  491  ? -32.990 51.827  77.271  1.00 53.45 ? 489  ARG A CA    1 
ATOM   3529  C  C     . ARG A 1  491  ? -31.847 50.818  77.225  1.00 54.50 ? 489  ARG A C     1 
ATOM   3530  O  O     . ARG A 1  491  ? -32.025 49.649  77.593  1.00 51.78 ? 489  ARG A O     1 
ATOM   3531  C  CB    . ARG A 1  491  ? -33.619 51.992  75.887  1.00 51.67 ? 489  ARG A CB    1 
ATOM   3532  N  N     . LEU A 1  492  ? -30.659 51.253  76.789  1.00 52.13 ? 490  LEU A N     1 
ATOM   3533  C  CA    . LEU A 1  492  ? -29.531 50.331  76.680  1.00 51.29 ? 490  LEU A CA    1 
ATOM   3534  C  C     . LEU A 1  492  ? -29.068 49.849  78.054  1.00 52.80 ? 490  LEU A C     1 
ATOM   3535  O  O     . LEU A 1  492  ? -28.755 48.663  78.226  1.00 49.34 ? 490  LEU A O     1 
ATOM   3536  C  CB    . LEU A 1  492  ? -28.384 50.995  75.914  1.00 44.40 ? 490  LEU A CB    1 
ATOM   3537  N  N     . LEU A 1  493  ? -29.021 50.750  79.044  1.00 50.90 ? 491  LEU A N     1 
ATOM   3538  C  CA    . LEU A 1  493  ? -28.657 50.344  80.399  1.00 49.22 ? 491  LEU A CA    1 
ATOM   3539  C  C     . LEU A 1  493  ? -29.696 49.399  80.986  1.00 54.87 ? 491  LEU A C     1 
ATOM   3540  O  O     . LEU A 1  493  ? -29.349 48.468  81.724  1.00 57.03 ? 491  LEU A O     1 
ATOM   3541  C  CB    . LEU A 1  493  ? -28.486 51.571  81.297  1.00 47.39 ? 491  LEU A CB    1 
ATOM   3542  N  N     . GLU A 1  494  ? -30.974 49.626  80.675  1.00 53.31 ? 492  GLU A N     1 
ATOM   3543  C  CA    . GLU A 1  494  ? -32.024 48.725  81.135  1.00 54.83 ? 492  GLU A CA    1 
ATOM   3544  C  C     . GLU A 1  494  ? -31.808 47.318  80.588  1.00 57.61 ? 492  GLU A C     1 
ATOM   3545  O  O     . GLU A 1  494  ? -31.638 46.363  81.351  1.00 58.95 ? 492  GLU A O     1 
ATOM   3546  C  CB    . GLU A 1  494  ? -33.394 49.269  80.729  1.00 54.54 ? 492  GLU A CB    1 
ATOM   3547  N  N     . ASN A 1  495  ? -31.764 47.180  79.260  1.00 58.77 ? 493  ASN A N     1 
ATOM   3548  C  CA    . ASN A 1  495  ? -31.594 45.882  78.612  1.00 58.85 ? 493  ASN A CA    1 
ATOM   3549  C  C     . ASN A 1  495  ? -30.255 45.215  78.928  1.00 61.22 ? 493  ASN A C     1 
ATOM   3550  O  O     . ASN A 1  495  ? -30.039 44.082  78.483  1.00 63.75 ? 493  ASN A O     1 
ATOM   3551  C  CB    . ASN A 1  495  ? -31.741 46.033  77.094  1.00 60.35 ? 493  ASN A CB    1 
ATOM   3552  N  N     . GLY A 1  496  ? -29.366 45.866  79.680  1.00 63.07 ? 494  GLY A N     1 
ATOM   3553  C  CA    . GLY A 1  496  ? -28.100 45.259  80.048  1.00 62.85 ? 494  GLY A CA    1 
ATOM   3554  C  C     . GLY A 1  496  ? -28.006 44.881  81.512  1.00 66.34 ? 494  GLY A C     1 
ATOM   3555  O  O     . GLY A 1  496  ? -27.070 44.185  81.919  1.00 68.91 ? 494  GLY A O     1 
ATOM   3556  N  N     . ALA A 1  497  ? -28.963 45.342  82.313  1.00 62.46 ? 495  ALA A N     1 
ATOM   3557  C  CA    . ALA A 1  497  ? -28.984 44.997  83.726  1.00 58.27 ? 495  ALA A CA    1 
ATOM   3558  C  C     . ALA A 1  497  ? -29.334 43.526  83.905  1.00 61.00 ? 495  ALA A C     1 
ATOM   3559  O  O     . ALA A 1  497  ? -30.247 43.005  83.257  1.00 56.94 ? 495  ALA A O     1 
ATOM   3560  C  CB    . ALA A 1  497  ? -29.986 45.875  84.472  1.00 56.80 ? 495  ALA A CB    1 
ATOM   3561  N  N     . ASN A 1  498  ? -28.599 42.854  84.798  1.00 70.89 ? 496  ASN A N     1 
ATOM   3562  C  CA    . ASN A 1  498  ? -28.810 41.426  85.018  1.00 68.43 ? 496  ASN A CA    1 
ATOM   3563  C  C     . ASN A 1  498  ? -30.227 41.116  85.477  1.00 64.06 ? 496  ASN A C     1 
ATOM   3564  O  O     . ASN A 1  498  ? -30.665 39.967  85.362  1.00 67.29 ? 496  ASN A O     1 
ATOM   3565  C  CB    . ASN A 1  498  ? -27.802 40.891  86.037  1.00 68.55 ? 496  ASN A CB    1 
ATOM   3566  N  N     . SER A 1  499  ? -30.953 42.111  85.992  1.00 54.69 ? 497  SER A N     1 
ATOM   3567  C  CA    . SER A 1  499  ? -32.350 41.907  86.349  1.00 52.85 ? 497  SER A CA    1 
ATOM   3568  C  C     . SER A 1  499  ? -33.283 41.980  85.145  1.00 44.51 ? 497  SER A C     1 
ATOM   3569  O  O     . SER A 1  499  ? -34.415 41.494  85.234  1.00 42.07 ? 497  SER A O     1 
ATOM   3570  C  CB    . SER A 1  499  ? -32.784 42.931  87.404  1.00 46.59 ? 497  SER A CB    1 
ATOM   3571  O  OG    . SER A 1  499  ? -32.479 44.255  87.000  1.00 49.79 ? 497  SER A OG    1 
ATOM   3572  N  N     . SER A 1  500  ? -32.833 42.546  84.026  1.00 45.68 ? 498  SER A N     1 
ATOM   3573  C  CA    . SER A 1  500  ? -33.699 42.766  82.872  1.00 43.27 ? 498  SER A CA    1 
ATOM   3574  C  C     . SER A 1  500  ? -33.963 41.471  82.115  1.00 46.09 ? 498  SER A C     1 
ATOM   3575  O  O     . SER A 1  500  ? -33.035 40.705  81.830  1.00 44.98 ? 498  SER A O     1 
ATOM   3576  C  CB    . SER A 1  500  ? -33.080 43.786  81.924  1.00 47.17 ? 498  SER A CB    1 
ATOM   3577  O  OG    . SER A 1  500  ? -33.050 45.071  82.515  1.00 51.49 ? 498  SER A OG    1 
ATOM   3578  N  N     . PHE A 1  501  ? -35.234 41.253  81.761  1.00 36.80 ? 499  PHE A N     1 
ATOM   3579  C  CA    . PHE A 1  501  ? -35.600 40.099  80.947  1.00 36.92 ? 499  PHE A CA    1 
ATOM   3580  C  C     . PHE A 1  501  ? -34.809 40.056  79.642  1.00 41.04 ? 499  PHE A C     1 
ATOM   3581  O  O     . PHE A 1  501  ? -34.386 38.980  79.202  1.00 40.73 ? 499  PHE A O     1 
ATOM   3582  C  CB    . PHE A 1  501  ? -37.102 40.123  80.654  1.00 30.98 ? 499  PHE A CB    1 
ATOM   3583  C  CG    . PHE A 1  501  ? -37.564 38.987  79.795  1.00 31.23 ? 499  PHE A CG    1 
ATOM   3584  C  CD1   . PHE A 1  501  ? -37.565 39.099  78.412  1.00 32.74 ? 499  PHE A CD1   1 
ATOM   3585  C  CD2   . PHE A 1  501  ? -37.998 37.810  80.368  1.00 30.40 ? 499  PHE A CD2   1 
ATOM   3586  C  CE1   . PHE A 1  501  ? -37.982 38.048  77.617  1.00 32.42 ? 499  PHE A CE1   1 
ATOM   3587  C  CE2   . PHE A 1  501  ? -38.419 36.761  79.586  1.00 31.62 ? 499  PHE A CE2   1 
ATOM   3588  C  CZ    . PHE A 1  501  ? -38.407 36.874  78.207  1.00 32.57 ? 499  PHE A CZ    1 
ATOM   3589  N  N     . VAL A 1  502  ? -34.617 41.210  78.999  1.00 40.62 ? 500  VAL A N     1 
ATOM   3590  C  CA    . VAL A 1  502  ? -33.937 41.231  77.707  1.00 42.97 ? 500  VAL A CA    1 
ATOM   3591  C  C     . VAL A 1  502  ? -32.499 40.751  77.857  1.00 47.52 ? 500  VAL A C     1 
ATOM   3592  O  O     . VAL A 1  502  ? -31.993 39.983  77.028  1.00 48.10 ? 500  VAL A O     1 
ATOM   3593  C  CB    . VAL A 1  502  ? -34.009 42.638  77.088  1.00 43.81 ? 500  VAL A CB    1 
ATOM   3594  N  N     . HIS A 1  503  ? -31.822 41.181  78.924  1.00 47.78 ? 501  HIS A N     1 
ATOM   3595  C  CA    . HIS A 1  503  ? -30.471 40.694  79.186  1.00 49.73 ? 501  HIS A CA    1 
ATOM   3596  C  C     . HIS A 1  503  ? -30.474 39.206  79.510  1.00 50.22 ? 501  HIS A C     1 
ATOM   3597  O  O     . HIS A 1  503  ? -29.630 38.453  79.010  1.00 48.56 ? 501  HIS A O     1 
ATOM   3598  C  CB    . HIS A 1  503  ? -29.836 41.484  80.333  1.00 55.75 ? 501  HIS A CB    1 
ATOM   3599  C  CG    . HIS A 1  503  ? -28.404 41.127  80.592  1.00 60.80 ? 501  HIS A CG    1 
ATOM   3600  N  ND1   . HIS A 1  503  ? -28.013 40.328  81.646  1.00 60.56 ? 501  HIS A ND1   1 
ATOM   3601  C  CD2   . HIS A 1  503  ? -27.270 41.456  79.928  1.00 59.84 ? 501  HIS A CD2   1 
ATOM   3602  C  CE1   . HIS A 1  503  ? -26.699 40.184  81.622  1.00 60.42 ? 501  HIS A CE1   1 
ATOM   3603  N  NE2   . HIS A 1  503  ? -26.224 40.857  80.589  1.00 59.27 ? 501  HIS A NE2   1 
ATOM   3604  N  N     . ARG A 1  504  ? -31.417 38.764  80.342  1.00 46.29 ? 502  ARG A N     1 
ATOM   3605  C  CA    . ARG A 1  504  ? -31.433 37.366  80.756  1.00 46.66 ? 502  ARG A CA    1 
ATOM   3606  C  C     . ARG A 1  504  ? -31.801 36.444  79.599  1.00 47.22 ? 502  ARG A C     1 
ATOM   3607  O  O     . ARG A 1  504  ? -31.241 35.349  79.474  1.00 45.29 ? 502  ARG A O     1 
ATOM   3608  C  CB    . ARG A 1  504  ? -32.388 37.186  81.934  1.00 46.38 ? 502  ARG A CB    1 
ATOM   3609  C  CG    . ARG A 1  504  ? -31.883 37.819  83.217  1.00 44.77 ? 502  ARG A CG    1 
ATOM   3610  C  CD    . ARG A 1  504  ? -33.014 38.047  84.206  1.00 47.93 ? 502  ARG A CD    1 
ATOM   3611  N  NE    . ARG A 1  504  ? -33.747 36.822  84.495  1.00 48.09 ? 502  ARG A NE    1 
ATOM   3612  C  CZ    . ARG A 1  504  ? -33.334 35.882  85.335  1.00 47.43 ? 502  ARG A CZ    1 
ATOM   3613  N  NH1   . ARG A 1  504  ? -32.176 35.981  85.969  1.00 48.13 ? 502  ARG A NH1   1 
ATOM   3614  N  NH2   . ARG A 1  504  ? -34.102 34.816  85.543  1.00 45.85 ? 502  ARG A NH2   1 
ATOM   3615  N  N     . ILE A 1  505  ? -32.723 36.873  78.730  1.00 46.68 ? 503  ILE A N     1 
ATOM   3616  C  CA    . ILE A 1  505  ? -33.110 36.042  77.591  1.00 45.52 ? 503  ILE A CA    1 
ATOM   3617  C  C     . ILE A 1  505  ? -31.895 35.699  76.735  1.00 49.88 ? 503  ILE A C     1 
ATOM   3618  O  O     . ILE A 1  505  ? -31.831 34.618  76.133  1.00 48.30 ? 503  ILE A O     1 
ATOM   3619  C  CB    . ILE A 1  505  ? -34.205 36.741  76.762  1.00 40.16 ? 503  ILE A CB    1 
ATOM   3620  N  N     . ASN A 1  506  ? -30.908 36.598  76.680  1.00 49.06 ? 504  ASN A N     1 
ATOM   3621  C  CA    . ASN A 1  506  ? -29.679 36.367  75.931  1.00 52.65 ? 504  ASN A CA    1 
ATOM   3622  C  C     . ASN A 1  506  ? -28.608 35.644  76.737  1.00 53.40 ? 504  ASN A C     1 
ATOM   3623  O  O     . ASN A 1  506  ? -27.716 35.028  76.143  1.00 56.71 ? 504  ASN A O     1 
ATOM   3624  C  CB    . ASN A 1  506  ? -29.106 37.697  75.431  1.00 52.25 ? 504  ASN A CB    1 
ATOM   3625  C  CG    . ASN A 1  506  ? -30.068 38.442  74.526  1.00 53.24 ? 504  ASN A CG    1 
ATOM   3626  O  OD1   . ASN A 1  506  ? -30.875 37.833  73.825  1.00 56.34 ? 504  ASN A OD1   1 
ATOM   3627  N  ND2   . ASN A 1  506  ? -29.983 39.767  74.535  1.00 57.10 ? 504  ASN A ND2   1 
ATOM   3628  N  N     . ASP A 1  507  ? -28.665 35.709  78.057  1.00 53.19 ? 505  ASP A N     1 
ATOM   3629  C  CA    . ASP A 1  507  ? -27.669 35.071  78.904  1.00 55.68 ? 505  ASP A CA    1 
ATOM   3630  C  C     . ASP A 1  507  ? -27.831 33.559  78.853  1.00 58.00 ? 505  ASP A C     1 
ATOM   3631  O  O     . ASP A 1  507  ? -28.839 33.041  79.354  1.00 54.28 ? 505  ASP A O     1 
ATOM   3632  C  CB    . ASP A 1  507  ? -27.805 35.579  80.341  1.00 56.43 ? 505  ASP A CB    1 
ATOM   3633  C  CG    . ASP A 1  507  ? -26.701 35.072  81.259  1.00 58.43 ? 505  ASP A CG    1 
ATOM   3634  O  OD1   . ASP A 1  507  ? -25.909 34.198  80.844  1.00 61.23 ? 505  ASP A OD1   1 
ATOM   3635  O  OD2   . ASP A 1  507  ? -26.627 35.558  82.408  1.00 56.52 ? 505  ASP A OD2   1 
ATOM   3636  N  N     . PRO A 1  508  ? -26.881 32.815  78.282  1.00 68.37 ? 506  PRO A N     1 
ATOM   3637  C  CA    . PRO A 1  508  ? -27.025 31.351  78.245  1.00 63.88 ? 506  PRO A CA    1 
ATOM   3638  C  C     . PRO A 1  508  ? -27.014 30.719  79.622  1.00 62.66 ? 506  PRO A C     1 
ATOM   3639  O  O     . PRO A 1  508  ? -27.533 29.608  79.782  1.00 66.99 ? 506  PRO A O     1 
ATOM   3640  C  CB    . PRO A 1  508  ? -25.818 30.894  77.411  1.00 66.22 ? 506  PRO A CB    1 
ATOM   3641  C  CG    . PRO A 1  508  ? -25.292 32.142  76.743  1.00 68.53 ? 506  PRO A CG    1 
ATOM   3642  C  CD    . PRO A 1  508  ? -25.617 33.262  77.674  1.00 64.28 ? 506  PRO A CD    1 
ATOM   3643  N  N     . LYS A 1  509  ? -26.451 31.397  80.624  1.00 57.12 ? 507  LYS A N     1 
ATOM   3644  C  CA    . LYS A 1  509  ? -26.366 30.840  81.967  1.00 56.66 ? 507  LYS A CA    1 
ATOM   3645  C  C     . LYS A 1  509  ? -27.705 30.811  82.691  1.00 55.11 ? 507  LYS A C     1 
ATOM   3646  O  O     . LYS A 1  509  ? -27.778 30.238  83.783  1.00 59.37 ? 507  LYS A O     1 
ATOM   3647  C  CB    . LYS A 1  509  ? -25.350 31.627  82.797  1.00 57.58 ? 507  LYS A CB    1 
ATOM   3648  N  N     . VAL A 1  510  ? -28.757 31.407  82.134  1.00 54.50 ? 508  VAL A N     1 
ATOM   3649  C  CA    . VAL A 1  510  ? -30.078 31.394  82.755  1.00 51.66 ? 508  VAL A CA    1 
ATOM   3650  C  C     . VAL A 1  510  ? -30.995 30.502  81.925  1.00 45.42 ? 508  VAL A C     1 
ATOM   3651  O  O     . VAL A 1  510  ? -31.042 30.605  80.692  1.00 44.96 ? 508  VAL A O     1 
ATOM   3652  C  CB    . VAL A 1  510  ? -30.645 32.818  82.937  1.00 50.04 ? 508  VAL A CB    1 
ATOM   3653  C  CG1   . VAL A 1  510  ? -29.532 33.802  83.290  1.00 50.99 ? 508  VAL A CG1   1 
ATOM   3654  C  CG2   . VAL A 1  510  ? -31.415 33.295  81.725  1.00 49.08 ? 508  VAL A CG2   1 
ATOM   3655  N  N     . SER A 1  511  ? -31.686 29.591  82.600  1.00 46.09 ? 509  SER A N     1 
ATOM   3656  C  CA    . SER A 1  511  ? -32.533 28.621  81.932  1.00 43.04 ? 509  SER A CA    1 
ATOM   3657  C  C     . SER A 1  511  ? -33.897 29.230  81.627  1.00 42.89 ? 509  SER A C     1 
ATOM   3658  O  O     . SER A 1  511  ? -34.276 30.282  82.154  1.00 42.28 ? 509  SER A O     1 
ATOM   3659  C  CB    . SER A 1  511  ? -32.694 27.372  82.795  1.00 44.93 ? 509  SER A CB    1 
ATOM   3660  O  OG    . SER A 1  511  ? -33.229 27.713  84.063  1.00 45.01 ? 509  SER A OG    1 
ATOM   3661  N  N     . ILE A 1  512  ? -34.644 28.550  80.755  1.00 40.29 ? 510  ILE A N     1 
ATOM   3662  C  CA    . ILE A 1  512  ? -36.017 28.965  80.503  1.00 41.30 ? 510  ILE A CA    1 
ATOM   3663  C  C     . ILE A 1  512  ? -36.855 28.788  81.760  1.00 42.27 ? 510  ILE A C     1 
ATOM   3664  O  O     . ILE A 1  512  ? -37.748 29.599  82.040  1.00 41.69 ? 510  ILE A O     1 
ATOM   3665  C  CB    . ILE A 1  512  ? -36.591 28.191  79.303  1.00 39.78 ? 510  ILE A CB    1 
ATOM   3666  C  CG1   . ILE A 1  512  ? -35.742 28.477  78.063  1.00 38.03 ? 510  ILE A CG1   1 
ATOM   3667  C  CG2   . ILE A 1  512  ? -38.052 28.561  79.063  1.00 40.10 ? 510  ILE A CG2   1 
ATOM   3668  C  CD1   . ILE A 1  512  ? -36.341 27.991  76.780  1.00 39.44 ? 510  ILE A CD1   1 
ATOM   3669  N  N     . ASP A 1  513  ? -36.558 27.752  82.553  1.00 39.46 ? 511  ASP A N     1 
ATOM   3670  C  CA    . ASP A 1  513  ? -37.221 27.560  83.841  1.00 42.77 ? 511  ASP A CA    1 
ATOM   3671  C  C     . ASP A 1  513  ? -37.074 28.788  84.730  1.00 41.63 ? 511  ASP A C     1 
ATOM   3672  O  O     . ASP A 1  513  ? -38.039 29.227  85.367  1.00 40.64 ? 511  ASP A O     1 
ATOM   3673  C  CB    . ASP A 1  513  ? -36.652 26.328  84.546  1.00 45.47 ? 511  ASP A CB    1 
ATOM   3674  C  CG    . ASP A 1  513  ? -37.415 25.064  84.220  1.00 50.58 ? 511  ASP A CG    1 
ATOM   3675  O  OD1   . ASP A 1  513  ? -38.398 25.133  83.453  1.00 48.28 ? 511  ASP A OD1   1 
ATOM   3676  O  OD2   . ASP A 1  513  ? -37.032 23.994  84.738  1.00 58.68 ? 511  ASP A OD2   1 
ATOM   3677  N  N     . GLU A 1  514  ? -35.864 29.350  84.801  1.00 39.80 ? 512  GLU A N     1 
ATOM   3678  C  CA    . GLU A 1  514  ? -35.658 30.550  85.604  1.00 39.71 ? 512  GLU A CA    1 
ATOM   3679  C  C     . GLU A 1  514  ? -36.376 31.757  85.012  1.00 39.70 ? 512  GLU A C     1 
ATOM   3680  O  O     . GLU A 1  514  ? -36.776 32.661  85.753  1.00 40.30 ? 512  GLU A O     1 
ATOM   3681  C  CB    . GLU A 1  514  ? -34.162 30.838  85.745  1.00 44.96 ? 512  GLU A CB    1 
ATOM   3682  C  CG    . GLU A 1  514  ? -33.412 29.799  86.563  1.00 46.64 ? 512  GLU A CG    1 
ATOM   3683  C  CD    . GLU A 1  514  ? -31.911 30.030  86.572  1.00 51.55 ? 512  GLU A CD    1 
ATOM   3684  O  OE1   . GLU A 1  514  ? -31.362 30.448  85.531  1.00 50.57 ? 512  GLU A OE1   1 
ATOM   3685  O  OE2   . GLU A 1  514  ? -31.278 29.798  87.623  1.00 55.56 ? 512  GLU A OE2   1 
ATOM   3686  N  N     . LEU A 1  515  ? -36.543 31.794  83.689  1.00 40.34 ? 513  LEU A N     1 
ATOM   3687  C  CA    . LEU A 1  515  ? -37.205 32.930  83.054  1.00 39.36 ? 513  LEU A CA    1 
ATOM   3688  C  C     . LEU A 1  515  ? -38.719 32.854  83.177  1.00 37.54 ? 513  LEU A C     1 
ATOM   3689  O  O     . LEU A 1  515  ? -39.389 33.892  83.154  1.00 34.03 ? 513  LEU A O     1 
ATOM   3690  C  CB    . LEU A 1  515  ? -36.818 33.017  81.578  1.00 37.43 ? 513  LEU A CB    1 
ATOM   3691  C  CG    . LEU A 1  515  ? -35.378 33.399  81.242  1.00 40.49 ? 513  LEU A CG    1 
ATOM   3692  C  CD1   . LEU A 1  515  ? -35.147 33.272  79.747  1.00 38.95 ? 513  LEU A CD1   1 
ATOM   3693  C  CD2   . LEU A 1  515  ? -35.090 34.816  81.719  1.00 37.76 ? 513  LEU A CD2   1 
ATOM   3694  N  N     . ILE A 1  516  ? -39.275 31.649  83.294  1.00 35.86 ? 514  ILE A N     1 
ATOM   3695  C  CA    . ILE A 1  516  ? -40.712 31.479  83.445  1.00 36.00 ? 514  ILE A CA    1 
ATOM   3696  C  C     . ILE A 1  516  ? -41.110 31.322  84.908  1.00 34.90 ? 514  ILE A C     1 
ATOM   3697  O  O     . ILE A 1  516  ? -42.275 31.033  85.204  1.00 34.58 ? 514  ILE A O     1 
ATOM   3698  C  CB    . ILE A 1  516  ? -41.219 30.298  82.607  1.00 36.11 ? 514  ILE A CB    1 
ATOM   3699  C  CG1   . ILE A 1  516  ? -40.680 28.981  83.165  1.00 39.99 ? 514  ILE A CG1   1 
ATOM   3700  C  CG2   . ILE A 1  516  ? -40.827 30.490  81.144  1.00 36.65 ? 514  ILE A CG2   1 
ATOM   3701  C  CD1   . ILE A 1  516  ? -41.244 27.752  82.482  1.00 38.43 ? 514  ILE A CD1   1 
ATOM   3702  N  N     . ALA A 1  517  ? -40.169 31.509  85.830  1.00 33.76 ? 515  ALA A N     1 
ATOM   3703  C  CA    . ALA A 1  517  ? -40.495 31.510  87.247  1.00 33.03 ? 515  ALA A CA    1 
ATOM   3704  C  C     . ALA A 1  517  ? -41.543 32.576  87.543  1.00 34.13 ? 515  ALA A C     1 
ATOM   3705  O  O     . ALA A 1  517  ? -41.428 33.721  87.098  1.00 31.03 ? 515  ALA A O     1 
ATOM   3706  C  CB    . ALA A 1  517  ? -39.238 31.755  88.082  1.00 35.36 ? 515  ALA A CB    1 
ATOM   3707  N  N     . ASP A 1  518  ? -42.569 32.186  88.285  1.00 30.82 ? 516  ASP A N     1 
ATOM   3708  C  CA    . ASP A 1  518  ? -43.674 33.059  88.647  1.00 31.20 ? 516  ASP A CA    1 
ATOM   3709  C  C     . ASP A 1  518  ? -43.270 33.995  89.778  1.00 29.72 ? 516  ASP A C     1 
ATOM   3710  O  O     . ASP A 1  518  ? -43.047 33.543  90.907  1.00 32.18 ? 516  ASP A O     1 
ATOM   3711  C  CB    . ASP A 1  518  ? -44.880 32.214  89.053  1.00 32.36 ? 516  ASP A CB    1 
ATOM   3712  C  CG    . ASP A 1  518  ? -46.064 33.051  89.469  1.00 34.03 ? 516  ASP A CG    1 
ATOM   3713  O  OD1   . ASP A 1  518  ? -46.034 34.286  89.288  1.00 32.16 ? 516  ASP A OD1   1 
ATOM   3714  O  OD2   . ASP A 1  518  ? -47.040 32.463  89.967  1.00 38.61 ? 516  ASP A OD2   1 
ATOM   3715  N  N     . PRO A 1  519  ? -43.187 35.305  89.532  1.00 31.58 ? 517  PRO A N     1 
ATOM   3716  C  CA    . PRO A 1  519  ? -42.767 36.207  90.614  1.00 31.58 ? 517  PRO A CA    1 
ATOM   3717  C  C     . PRO A 1  519  ? -43.767 36.273  91.758  1.00 26.38 ? 517  PRO A C     1 
ATOM   3718  O  O     . PRO A 1  519  ? -43.361 36.523  92.900  1.00 29.35 ? 517  PRO A O     1 
ATOM   3719  C  CB    . PRO A 1  519  ? -42.615 37.563  89.902  1.00 27.49 ? 517  PRO A CB    1 
ATOM   3720  C  CG    . PRO A 1  519  ? -43.546 37.466  88.730  1.00 30.30 ? 517  PRO A CG    1 
ATOM   3721  C  CD    . PRO A 1  519  ? -43.509 36.032  88.290  1.00 28.36 ? 517  PRO A CD    1 
ATOM   3722  N  N     . VAL A 1  520  ? -45.053 36.041  91.486  1.00 28.42 ? 518  VAL A N     1 
ATOM   3723  C  CA    . VAL A 1  520  ? -46.065 36.094  92.537  1.00 28.89 ? 518  VAL A CA    1 
ATOM   3724  C  C     . VAL A 1  520  ? -45.809 35.007  93.572  1.00 30.94 ? 518  VAL A C     1 
ATOM   3725  O  O     . VAL A 1  520  ? -45.775 35.268  94.779  1.00 31.14 ? 518  VAL A O     1 
ATOM   3726  C  CB    . VAL A 1  520  ? -47.474 35.976  91.927  1.00 28.41 ? 518  VAL A CB    1 
ATOM   3727  C  CG1   . VAL A 1  520  ? -48.538 35.976  93.021  1.00 29.46 ? 518  VAL A CG1   1 
ATOM   3728  C  CG2   . VAL A 1  520  ? -47.719 37.117  90.949  1.00 29.77 ? 518  VAL A CG2   1 
ATOM   3729  N  N     . GLU A 1  521  ? -45.592 33.775  93.110  1.00 30.73 ? 519  GLU A N     1 
ATOM   3730  C  CA    . GLU A 1  521  ? -45.367 32.677  94.044  1.00 31.76 ? 519  GLU A CA    1 
ATOM   3731  C  C     . GLU A 1  521  ? -44.001 32.767  94.705  1.00 33.83 ? 519  GLU A C     1 
ATOM   3732  O  O     . GLU A 1  521  ? -43.849 32.353  95.860  1.00 34.51 ? 519  GLU A O     1 
ATOM   3733  C  CB    . GLU A 1  521  ? -45.536 31.339  93.327  1.00 36.52 ? 519  GLU A CB    1 
ATOM   3734  C  CG    . GLU A 1  521  ? -46.956 31.103  92.829  1.00 37.74 ? 519  GLU A CG    1 
ATOM   3735  C  CD    . GLU A 1  521  ? -47.993 31.235  93.931  1.00 42.56 ? 519  GLU A CD    1 
ATOM   3736  O  OE1   . GLU A 1  521  ? -47.711 30.805  95.072  1.00 45.39 ? 519  GLU A OE1   1 
ATOM   3737  O  OE2   . GLU A 1  521  ? -49.091 31.767  93.662  1.00 43.60 ? 519  GLU A OE2   1 
ATOM   3738  N  N     . VAL A 1  522  ? -42.998 33.304  94.003  1.00 32.90 ? 520  VAL A N     1 
ATOM   3739  C  CA    . VAL A 1  522  ? -41.686 33.461  94.616  1.00 29.58 ? 520  VAL A CA    1 
ATOM   3740  C  C     . VAL A 1  522  ? -41.752 34.470  95.755  1.00 36.12 ? 520  VAL A C     1 
ATOM   3741  O  O     . VAL A 1  522  ? -41.176 34.257  96.830  1.00 33.74 ? 520  VAL A O     1 
ATOM   3742  C  CB    . VAL A 1  522  ? -40.634 33.859  93.564  1.00 33.64 ? 520  VAL A CB    1 
ATOM   3743  C  CG1   . VAL A 1  522  ? -39.296 34.137  94.236  1.00 34.99 ? 520  VAL A CG1   1 
ATOM   3744  C  CG2   . VAL A 1  522  ? -40.477 32.763  92.517  1.00 35.94 ? 520  VAL A CG2   1 
ATOM   3745  N  N     . VAL A 1  523  ? -42.458 35.583  95.546  1.00 29.33 ? 521  VAL A N     1 
ATOM   3746  C  CA    . VAL A 1  523  ? -42.599 36.563  96.616  1.00 29.91 ? 521  VAL A CA    1 
ATOM   3747  C  C     . VAL A 1  523  ? -43.424 35.989  97.763  1.00 33.99 ? 521  VAL A C     1 
ATOM   3748  O  O     . VAL A 1  523  ? -43.092 36.185  98.938  1.00 31.11 ? 521  VAL A O     1 
ATOM   3749  C  CB    . VAL A 1  523  ? -43.210 37.865  96.071  1.00 28.02 ? 521  VAL A CB    1 
ATOM   3750  C  CG1   . VAL A 1  523  ? -43.666 38.750  97.211  1.00 31.21 ? 521  VAL A CG1   1 
ATOM   3751  C  CG2   . VAL A 1  523  ? -42.191 38.593  95.206  1.00 30.16 ? 521  VAL A CG2   1 
ATOM   3752  N  N     . ARG A 1  524  ? -44.502 35.261  97.442  1.00 32.06 ? 522  ARG A N     1 
ATOM   3753  C  CA    . ARG A 1  524  ? -45.380 34.735  98.486  1.00 33.95 ? 522  ARG A CA    1 
ATOM   3754  C  C     . ARG A 1  524  ? -44.638 33.812  99.439  1.00 36.53 ? 522  ARG A C     1 
ATOM   3755  O  O     . ARG A 1  524  ? -44.962 33.763  100.631 1.00 39.08 ? 522  ARG A O     1 
ATOM   3756  C  CB    . ARG A 1  524  ? -46.555 33.982  97.874  1.00 38.12 ? 522  ARG A CB    1 
ATOM   3757  C  CG    . ARG A 1  524  ? -47.497 33.399  98.923  1.00 36.21 ? 522  ARG A CG    1 
ATOM   3758  C  CD    . ARG A 1  524  ? -48.297 32.260  98.357  1.00 38.75 ? 522  ARG A CD    1 
ATOM   3759  N  NE    . ARG A 1  524  ? -48.879 32.629  97.075  1.00 39.15 ? 522  ARG A NE    1 
ATOM   3760  C  CZ    . ARG A 1  524  ? -49.928 33.427  96.936  1.00 36.90 ? 522  ARG A CZ    1 
ATOM   3761  N  NH1   . ARG A 1  524  ? -50.524 33.974  97.982  1.00 37.75 ? 522  ARG A NH1   1 
ATOM   3762  N  NH2   . ARG A 1  524  ? -50.392 33.680  95.716  1.00 37.61 ? 522  ARG A NH2   1 
ATOM   3763  N  N     . ALA A 1  525  ? -43.642 33.084  98.937  1.00 37.47 ? 523  ALA A N     1 
ATOM   3764  C  CA    . ALA A 1  525  ? -42.901 32.103  99.716  1.00 38.08 ? 523  ALA A CA    1 
ATOM   3765  C  C     . ALA A 1  525  ? -41.683 32.687  100.419 1.00 37.89 ? 523  ALA A C     1 
ATOM   3766  O  O     . ALA A 1  525  ? -41.024 31.969  101.180 1.00 39.80 ? 523  ALA A O     1 
ATOM   3767  C  CB    . ALA A 1  525  ? -42.470 30.943  98.813  1.00 35.50 ? 523  ALA A CB    1 
ATOM   3768  N  N     . MET A 1  526  ? -41.359 33.956  100.179 1.00 37.00 ? 524  MET A N     1 
ATOM   3769  C  CA    A MET A 1  526  ? -40.243 34.572  100.872 0.48 38.80 ? 524  MET A CA    1 
ATOM   3770  C  CA    B MET A 1  526  ? -40.250 34.590  100.871 0.52 38.80 ? 524  MET A CA    1 
ATOM   3771  C  C     . MET A 1  526  ? -40.512 34.599  102.376 1.00 40.74 ? 524  MET A C     1 
ATOM   3772  O  O     . MET A 1  526  ? -41.665 34.684  102.810 1.00 37.22 ? 524  MET A O     1 
ATOM   3773  C  CB    A MET A 1  526  ? -40.000 35.986  100.347 0.48 39.45 ? 524  MET A CB    1 
ATOM   3774  C  CB    B MET A 1  526  ? -40.055 36.016  100.360 0.52 39.46 ? 524  MET A CB    1 
ATOM   3775  C  CG    A MET A 1  526  ? -39.471 36.026  98.925  0.48 37.25 ? 524  MET A CG    1 
ATOM   3776  C  CG    B MET A 1  526  ? -38.760 36.240  99.605  0.52 38.42 ? 524  MET A CG    1 
ATOM   3777  S  SD    A MET A 1  526  ? -37.956 35.067  98.746  0.48 43.14 ? 524  MET A SD    1 
ATOM   3778  S  SD    B MET A 1  526  ? -38.946 37.379  98.221  0.52 38.90 ? 524  MET A SD    1 
ATOM   3779  C  CE    A MET A 1  526  ? -36.829 36.034  99.754  0.48 39.68 ? 524  MET A CE    1 
ATOM   3780  C  CE    B MET A 1  526  ? -39.691 38.807  99.019  0.52 36.53 ? 524  MET A CE    1 
ATOM   3781  N  N     . PRO A 1  527  ? -39.460 34.513  103.200 1.00 44.40 ? 525  PRO A N     1 
ATOM   3782  C  CA    . PRO A 1  527  ? -39.687 34.482  104.657 1.00 42.65 ? 525  PRO A CA    1 
ATOM   3783  C  C     . PRO A 1  527  ? -40.309 35.761  105.183 1.00 39.01 ? 525  PRO A C     1 
ATOM   3784  O  O     . PRO A 1  527  ? -41.211 35.717  106.030 1.00 38.38 ? 525  PRO A O     1 
ATOM   3785  C  CB    . PRO A 1  527  ? -38.279 34.251  105.221 1.00 40.97 ? 525  PRO A CB    1 
ATOM   3786  C  CG    . PRO A 1  527  ? -37.366 34.786  104.172 1.00 42.73 ? 525  PRO A CG    1 
ATOM   3787  C  CD    . PRO A 1  527  ? -38.027 34.462  102.865 1.00 40.98 ? 525  PRO A CD    1 
ATOM   3788  N  N     . VAL A 1  528  ? -39.848 36.904  104.694 1.00 40.80 ? 526  VAL A N     1 
ATOM   3789  C  CA    . VAL A 1  528  ? -40.479 38.189  104.949 1.00 35.17 ? 526  VAL A CA    1 
ATOM   3790  C  C     . VAL A 1  528  ? -40.984 38.687  103.604 1.00 36.52 ? 526  VAL A C     1 
ATOM   3791  O  O     . VAL A 1  528  ? -40.189 38.964  102.695 1.00 36.43 ? 526  VAL A O     1 
ATOM   3792  C  CB    . VAL A 1  528  ? -39.507 39.186  105.590 1.00 35.86 ? 526  VAL A CB    1 
ATOM   3793  C  CG1   . VAL A 1  528  ? -40.211 40.507  105.877 1.00 34.29 ? 526  VAL A CG1   1 
ATOM   3794  C  CG2   . VAL A 1  528  ? -38.895 38.593  106.856 1.00 40.01 ? 526  VAL A CG2   1 
ATOM   3795  N  N     . VAL A 1  529  ? -42.303 38.768  103.455 1.00 31.00 ? 527  VAL A N     1 
ATOM   3796  C  CA    . VAL A 1  529  ? -42.872 39.213  102.191 1.00 29.79 ? 527  VAL A CA    1 
ATOM   3797  C  C     . VAL A 1  529  ? -42.605 40.704  102.030 1.00 33.48 ? 527  VAL A C     1 
ATOM   3798  O  O     . VAL A 1  529  ? -42.949 41.508  102.904 1.00 31.57 ? 527  VAL A O     1 
ATOM   3799  C  CB    . VAL A 1  529  ? -44.370 38.899  102.117 1.00 30.17 ? 527  VAL A CB    1 
ATOM   3800  C  CG1   . VAL A 1  529  ? -44.975 39.565  100.903 1.00 30.58 ? 527  VAL A CG1   1 
ATOM   3801  C  CG2   . VAL A 1  529  ? -44.586 37.392  102.051 1.00 32.37 ? 527  VAL A CG2   1 
ATOM   3802  N  N     . GLY A 1  530  ? -41.950 41.071  100.929 1.00 28.47 ? 528  GLY A N     1 
ATOM   3803  C  CA    . GLY A 1  530  ? -41.744 42.468  100.607 1.00 26.17 ? 528  GLY A CA    1 
ATOM   3804  C  C     . GLY A 1  530  ? -40.582 43.153  101.288 1.00 27.66 ? 528  GLY A C     1 
ATOM   3805  O  O     . GLY A 1  530  ? -40.558 44.387  101.338 1.00 27.25 ? 528  GLY A O     1 
ATOM   3806  N  N     . ALA A 1  531  ? -39.614 42.401  101.817 1.00 29.63 ? 529  ALA A N     1 
ATOM   3807  C  CA    . ALA A 1  531  ? -38.455 43.024  102.448 1.00 26.88 ? 529  ALA A CA    1 
ATOM   3808  C  C     . ALA A 1  531  ? -37.684 43.898  101.459 1.00 26.25 ? 529  ALA A C     1 
ATOM   3809  O  O     . ALA A 1  531  ? -37.564 43.575  100.275 1.00 27.24 ? 529  ALA A O     1 
ATOM   3810  C  CB    . ALA A 1  531  ? -37.528 41.954  103.030 1.00 28.99 ? 529  ALA A CB    1 
ATOM   3811  N  N     . LYS A 1  532  ? -37.168 45.017  101.959 1.00 24.69 ? 530  LYS A N     1 
ATOM   3812  C  CA    . LYS A 1  532  ? -36.278 45.873  101.184 1.00 27.52 ? 530  LYS A CA    1 
ATOM   3813  C  C     . LYS A 1  532  ? -35.084 45.071  100.677 1.00 28.04 ? 530  LYS A C     1 
ATOM   3814  O  O     . LYS A 1  532  ? -34.624 44.125  101.322 1.00 26.61 ? 530  LYS A O     1 
ATOM   3815  C  CB    . LYS A 1  532  ? -35.793 47.044  102.048 1.00 28.56 ? 530  LYS A CB    1 
ATOM   3816  C  CG    . LYS A 1  532  ? -34.807 48.000  101.368 1.00 29.50 ? 530  LYS A CG    1 
ATOM   3817  C  CD    . LYS A 1  532  ? -34.310 49.095  102.319 1.00 25.95 ? 530  LYS A CD    1 
ATOM   3818  C  CE    . LYS A 1  532  ? -33.538 48.514  103.505 1.00 24.59 ? 530  LYS A CE    1 
ATOM   3819  N  NZ    . LYS A 1  532  ? -32.223 47.941  103.089 1.00 26.99 ? 530  LYS A NZ    1 
ATOM   3820  N  N     . HIS A 1  533  ? -34.600 45.442  99.494  1.00 24.64 ? 531  HIS A N     1 
ATOM   3821  C  CA    . HIS A 1  533  ? -33.342 44.903  98.992  1.00 25.02 ? 531  HIS A CA    1 
ATOM   3822  C  C     . HIS A 1  533  ? -32.250 45.028  100.047 1.00 26.19 ? 531  HIS A C     1 
ATOM   3823  O  O     . HIS A 1  533  ? -32.075 46.091  100.648 1.00 24.79 ? 531  HIS A O     1 
ATOM   3824  C  CB    . HIS A 1  533  ? -32.927 45.649  97.725  1.00 25.13 ? 531  HIS A CB    1 
ATOM   3825  C  CG    . HIS A 1  533  ? -31.910 44.920  96.907  1.00 25.63 ? 531  HIS A CG    1 
ATOM   3826  N  ND1   . HIS A 1  533  ? -30.632 44.663  97.361  1.00 26.20 ? 531  HIS A ND1   1 
ATOM   3827  C  CD2   . HIS A 1  533  ? -31.986 44.380  95.668  1.00 29.63 ? 531  HIS A CD2   1 
ATOM   3828  C  CE1   . HIS A 1  533  ? -29.961 44.008  96.432  1.00 30.29 ? 531  HIS A CE1   1 
ATOM   3829  N  NE2   . HIS A 1  533  ? -30.760 43.819  95.396  1.00 31.64 ? 531  HIS A NE2   1 
ATOM   3830  N  N     . ASP A 1  534  ? -31.512 43.930  100.263 1.00 25.18 ? 532  ASP A N     1 
ATOM   3831  C  CA    . ASP A 1  534  ? -30.471 43.913  101.290 1.00 29.37 ? 532  ASP A CA    1 
ATOM   3832  C  C     . ASP A 1  534  ? -29.335 44.885  101.001 1.00 30.18 ? 532  ASP A C     1 
ATOM   3833  O  O     . ASP A 1  534  ? -28.661 45.337  101.937 1.00 33.04 ? 532  ASP A O     1 
ATOM   3834  C  CB    . ASP A 1  534  ? -29.889 42.505  101.434 1.00 32.57 ? 532  ASP A CB    1 
ATOM   3835  C  CG    . ASP A 1  534  ? -30.803 41.569  102.190 1.00 41.88 ? 532  ASP A CG    1 
ATOM   3836  O  OD1   . ASP A 1  534  ? -31.621 42.056  103.004 1.00 45.05 ? 532  ASP A OD1   1 
ATOM   3837  O  OD2   . ASP A 1  534  ? -30.693 40.341  101.978 1.00 51.27 ? 532  ASP A OD2   1 
ATOM   3838  N  N     . ARG A 1  535  ? -29.073 45.189  99.734  1.00 25.73 ? 533  ARG A N     1 
ATOM   3839  C  CA    . ARG A 1  535  ? -27.903 45.970  99.368  1.00 28.39 ? 533  ARG A CA    1 
ATOM   3840  C  C     . ARG A 1  535  ? -28.233 47.418  99.033  1.00 26.02 ? 533  ARG A C     1 
ATOM   3841  O  O     . ARG A 1  535  ? -27.387 48.124  98.477  1.00 26.68 ? 533  ARG A O     1 
ATOM   3842  C  CB    . ARG A 1  535  ? -27.172 45.307  98.196  1.00 28.90 ? 533  ARG A CB    1 
ATOM   3843  C  CG    . ARG A 1  535  ? -26.559 43.946  98.539  1.00 37.12 ? 533  ARG A CG    1 
ATOM   3844  C  CD    . ARG A 1  535  ? -25.800 43.360  97.354  1.00 41.51 ? 533  ARG A CD    1 
ATOM   3845  N  N     . ILE A 1  536  ? -29.425 47.888  99.377  1.00 24.06 ? 534  ILE A N     1 
ATOM   3846  C  CA    . ILE A 1  536  ? -29.796 49.278  99.163  1.00 23.88 ? 534  ILE A CA    1 
ATOM   3847  C  C     . ILE A 1  536  ? -30.093 49.895  100.521 1.00 24.15 ? 534  ILE A C     1 
ATOM   3848  O  O     . ILE A 1  536  ? -30.961 49.408  101.252 1.00 25.03 ? 534  ILE A O     1 
ATOM   3849  C  CB    . ILE A 1  536  ? -30.999 49.400  98.219  1.00 24.14 ? 534  ILE A CB    1 
ATOM   3850  C  CG1   . ILE A 1  536  ? -30.624 48.824  96.855  1.00 26.33 ? 534  ILE A CG1   1 
ATOM   3851  C  CG2   . ILE A 1  536  ? -31.475 50.861  98.126  1.00 24.32 ? 534  ILE A CG2   1 
ATOM   3852  C  CD1   . ILE A 1  536  ? -31.784 48.808  95.901  1.00 22.92 ? 534  ILE A CD1   1 
ATOM   3853  N  N     . ALA A 1  537  ? -29.384 50.964  100.854 1.00 20.80 ? 535  ALA A N     1 
ATOM   3854  C  CA    . ALA A 1  537  ? -29.555 51.601  102.152 1.00 23.01 ? 535  ALA A CA    1 
ATOM   3855  C  C     . ALA A 1  537  ? -30.747 52.552  102.137 1.00 22.94 ? 535  ALA A C     1 
ATOM   3856  O  O     . ALA A 1  537  ? -30.894 53.363  101.219 1.00 21.18 ? 535  ALA A O     1 
ATOM   3857  C  CB    . ALA A 1  537  ? -28.285 52.357  102.531 1.00 24.00 ? 535  ALA A CB    1 
ATOM   3858  N  N     . LEU A 1  538  ? -31.594 52.467  103.160 1.00 22.40 ? 536  LEU A N     1 
ATOM   3859  C  CA    . LEU A 1  538  ? -32.553 53.541  103.363 1.00 23.45 ? 536  LEU A CA    1 
ATOM   3860  C  C     . LEU A 1  538  ? -31.777 54.842  103.569 1.00 21.14 ? 536  LEU A C     1 
ATOM   3861  O  O     . LEU A 1  538  ? -30.620 54.816  104.003 1.00 21.46 ? 536  LEU A O     1 
ATOM   3862  C  CB    . LEU A 1  538  ? -33.451 53.258  104.571 1.00 22.36 ? 536  LEU A CB    1 
ATOM   3863  C  CG    . LEU A 1  538  ? -34.499 52.144  104.448 1.00 23.05 ? 536  LEU A CG    1 
ATOM   3864  C  CD1   . LEU A 1  538  ? -35.098 51.805  105.804 1.00 29.70 ? 536  LEU A CD1   1 
ATOM   3865  C  CD2   . LEU A 1  538  ? -35.605 52.562  103.484 1.00 22.44 ? 536  LEU A CD2   1 
ATOM   3866  N  N     . PRO A 1  539  ? -32.369 55.995  103.247 1.00 19.72 ? 537  PRO A N     1 
ATOM   3867  C  CA    . PRO A 1  539  ? -31.599 57.242  103.372 1.00 19.65 ? 537  PRO A CA    1 
ATOM   3868  C  C     . PRO A 1  539  ? -31.052 57.471  104.767 1.00 19.79 ? 537  PRO A C     1 
ATOM   3869  O  O     . PRO A 1  539  ? -29.911 57.927  104.899 1.00 20.66 ? 537  PRO A O     1 
ATOM   3870  C  CB    . PRO A 1  539  ? -32.605 58.312  102.943 1.00 19.97 ? 537  PRO A CB    1 
ATOM   3871  C  CG    . PRO A 1  539  ? -33.458 57.597  101.934 1.00 20.91 ? 537  PRO A CG    1 
ATOM   3872  C  CD    . PRO A 1  539  ? -33.638 56.210  102.519 1.00 19.06 ? 537  PRO A CD    1 
ATOM   3873  N  N     . ALA A 1  540  ? -31.816 57.120  105.804 1.00 19.77 ? 538  ALA A N     1 
ATOM   3874  C  CA    . ALA A 1  540  ? -31.353 57.283  107.180 1.00 22.91 ? 538  ALA A CA    1 
ATOM   3875  C  C     . ALA A 1  540  ? -30.111 56.454  107.479 1.00 23.63 ? 538  ALA A C     1 
ATOM   3876  O  O     . ALA A 1  540  ? -29.371 56.781  108.414 1.00 24.07 ? 538  ALA A O     1 
ATOM   3877  C  CB    . ALA A 1  540  ? -32.465 56.907  108.164 1.00 25.53 ? 538  ALA A CB    1 
ATOM   3878  N  N     . GLU A 1  541  ? -29.854 55.402  106.703 1.00 22.69 ? 539  GLU A N     1 
ATOM   3879  C  CA    . GLU A 1  541  ? -28.801 54.452  107.027 1.00 25.03 ? 539  GLU A CA    1 
ATOM   3880  C  C     . GLU A 1  541  ? -27.600 54.591  106.102 1.00 23.10 ? 539  GLU A C     1 
ATOM   3881  O  O     . GLU A 1  541  ? -26.759 53.690  106.047 1.00 23.84 ? 539  GLU A O     1 
ATOM   3882  C  CB    . GLU A 1  541  ? -29.373 53.030  107.014 1.00 26.02 ? 539  GLU A CB    1 
ATOM   3883  C  CG    . GLU A 1  541  ? -30.560 52.905  107.969 1.00 29.87 ? 539  GLU A CG    1 
ATOM   3884  C  CD    . GLU A 1  541  ? -31.167 51.514  108.035 1.00 34.79 ? 539  GLU A CD    1 
ATOM   3885  O  OE1   . GLU A 1  541  ? -30.414 50.521  108.033 1.00 43.81 ? 539  GLU A OE1   1 
ATOM   3886  O  OE2   . GLU A 1  541  ? -32.407 51.413  108.095 1.00 39.82 ? 539  GLU A OE2   1 
ATOM   3887  N  N     . LEU A 1  542  ? -27.486 55.731  105.405 1.00 20.49 ? 540  LEU A N     1 
ATOM   3888  C  CA    . LEU A 1  542  ? -26.391 55.936  104.459 1.00 23.19 ? 540  LEU A CA    1 
ATOM   3889  C  C     . LEU A 1  542  ? -25.026 55.741  105.100 1.00 24.13 ? 540  LEU A C     1 
ATOM   3890  O  O     . LEU A 1  542  ? -24.084 55.300  104.435 1.00 23.86 ? 540  LEU A O     1 
ATOM   3891  C  CB    . LEU A 1  542  ? -26.450 57.343  103.867 1.00 23.96 ? 540  LEU A CB    1 
ATOM   3892  C  CG    . LEU A 1  542  ? -27.256 57.624  102.610 1.00 23.57 ? 540  LEU A CG    1 
ATOM   3893  C  CD1   . LEU A 1  542  ? -26.761 58.952  102.014 1.00 18.64 ? 540  LEU A CD1   1 
ATOM   3894  C  CD2   . LEU A 1  542  ? -27.163 56.486  101.596 1.00 24.53 ? 540  LEU A CD2   1 
ATOM   3895  N  N     . PHE A 1  543  ? -24.891 56.076  106.377 1.00 20.49 ? 541  PHE A N     1 
ATOM   3896  C  CA    . PHE A 1  543  ? -23.604 55.992  107.049 1.00 22.88 ? 541  PHE A CA    1 
ATOM   3897  C  C     . PHE A 1  543  ? -23.515 54.796  107.979 1.00 23.91 ? 541  PHE A C     1 
ATOM   3898  O  O     . PHE A 1  543  ? -22.540 54.677  108.728 1.00 24.07 ? 541  PHE A O     1 
ATOM   3899  C  CB    . PHE A 1  543  ? -23.338 57.298  107.792 1.00 22.78 ? 541  PHE A CB    1 
ATOM   3900  C  CG    . PHE A 1  543  ? -23.576 58.506  106.937 1.00 22.97 ? 541  PHE A CG    1 
ATOM   3901  C  CD1   . PHE A 1  543  ? -22.905 58.637  105.729 1.00 24.18 ? 541  PHE A CD1   1 
ATOM   3902  C  CD2   . PHE A 1  543  ? -24.496 59.482  107.303 1.00 20.58 ? 541  PHE A CD2   1 
ATOM   3903  C  CE1   . PHE A 1  543  ? -23.133 59.717  104.909 1.00 23.81 ? 541  PHE A CE1   1 
ATOM   3904  C  CE2   . PHE A 1  543  ? -24.717 60.574  106.485 1.00 20.75 ? 541  PHE A CE2   1 
ATOM   3905  C  CZ    . PHE A 1  543  ? -24.036 60.688  105.282 1.00 21.59 ? 541  PHE A CZ    1 
ATOM   3906  N  N     . GLY A 1  544  ? -24.501 53.906  107.935 1.00 23.12 ? 542  GLY A N     1 
ATOM   3907  C  CA    . GLY A 1  544  ? -24.424 52.671  108.701 1.00 26.84 ? 542  GLY A CA    1 
ATOM   3908  C  C     . GLY A 1  544  ? -24.241 52.929  110.182 1.00 26.80 ? 542  GLY A C     1 
ATOM   3909  O  O     . GLY A 1  544  ? -24.913 53.780  110.779 1.00 23.75 ? 542  GLY A O     1 
ATOM   3910  N  N     . ASP A 1  545  ? -23.301 52.192  110.783 1.00 27.62 ? 543  ASP A N     1 
ATOM   3911  C  CA    . ASP A 1  545  ? -23.112 52.229  112.229 1.00 29.35 ? 543  ASP A CA    1 
ATOM   3912  C  C     . ASP A 1  545  ? -22.471 53.518  112.711 1.00 29.62 ? 543  ASP A C     1 
ATOM   3913  O  O     . ASP A 1  545  ? -22.501 53.789  113.920 1.00 29.84 ? 543  ASP A O     1 
ATOM   3914  C  CB    . ASP A 1  545  ? -22.232 51.066  112.690 1.00 33.03 ? 543  ASP A CB    1 
ATOM   3915  C  CG    . ASP A 1  545  ? -22.843 49.719  112.396 1.00 39.24 ? 543  ASP A CG    1 
ATOM   3916  O  OD1   . ASP A 1  545  ? -24.087 49.608  112.425 1.00 40.01 ? 543  ASP A OD1   1 
ATOM   3917  O  OD2   . ASP A 1  545  ? -22.073 48.769  112.142 1.00 47.91 ? 543  ASP A OD2   1 
ATOM   3918  N  N     . ALA A 1  546  ? -21.872 54.296  111.810 1.00 25.26 ? 544  ALA A N     1 
ATOM   3919  C  CA    . ALA A 1  546  ? -21.154 55.497  112.224 1.00 24.93 ? 544  ALA A CA    1 
ATOM   3920  C  C     . ALA A 1  546  ? -22.101 56.527  112.825 1.00 27.23 ? 544  ALA A C     1 
ATOM   3921  O  O     . ALA A 1  546  ? -21.841 57.067  113.904 1.00 26.41 ? 544  ALA A O     1 
ATOM   3922  C  CB    . ALA A 1  546  ? -20.398 56.095  111.041 1.00 24.24 ? 544  ALA A CB    1 
ATOM   3923  N  N     . ARG A 1  547  ? -23.203 56.818  112.142 1.00 24.58 ? 545  ARG A N     1 
ATOM   3924  C  CA    . ARG A 1  547  ? -24.142 57.813  112.644 1.00 24.09 ? 545  ARG A CA    1 
ATOM   3925  C  C     . ARG A 1  547  ? -25.404 57.759  111.802 1.00 20.82 ? 545  ARG A C     1 
ATOM   3926  O  O     . ARG A 1  547  ? -25.434 57.179  110.715 1.00 21.54 ? 545  ARG A O     1 
ATOM   3927  C  CB    . ARG A 1  547  ? -23.562 59.227  112.624 1.00 26.83 ? 545  ARG A CB    1 
ATOM   3928  C  CG    . ARG A 1  547  ? -23.282 59.736  111.247 1.00 24.92 ? 545  ARG A CG    1 
ATOM   3929  C  CD    . ARG A 1  547  ? -22.613 61.082  111.282 1.00 25.22 ? 545  ARG A CD    1 
ATOM   3930  N  NE    . ARG A 1  547  ? -21.839 61.263  110.064 1.00 24.36 ? 545  ARG A NE    1 
ATOM   3931  C  CZ    . ARG A 1  547  ? -22.268 61.919  108.995 1.00 21.57 ? 545  ARG A CZ    1 
ATOM   3932  N  NH1   . ARG A 1  547  ? -23.422 62.571  109.002 1.00 23.17 ? 545  ARG A NH1   1 
ATOM   3933  N  NH2   . ARG A 1  547  ? -21.521 61.921  107.899 1.00 22.48 ? 545  ARG A NH2   1 
ATOM   3934  N  N     . THR A 1  548  ? -26.445 58.377  112.334 1.00 21.48 ? 546  THR A N     1 
ATOM   3935  C  CA    . THR A 1  548  ? -27.734 58.439  111.672 1.00 19.58 ? 546  THR A CA    1 
ATOM   3936  C  C     . THR A 1  548  ? -27.769 59.647  110.756 1.00 19.49 ? 546  THR A C     1 
ATOM   3937  O  O     . THR A 1  548  ? -27.483 60.768  111.188 1.00 21.24 ? 546  THR A O     1 
ATOM   3938  C  CB    . THR A 1  548  ? -28.845 58.538  112.709 1.00 23.40 ? 546  THR A CB    1 
ATOM   3939  O  OG1   . THR A 1  548  ? -28.749 57.418  113.595 1.00 27.51 ? 546  THR A OG1   1 
ATOM   3940  C  CG2   . THR A 1  548  ? -30.188 58.549  112.026 1.00 23.65 ? 546  THR A CG2   1 
ATOM   3941  N  N     . ASN A 1  549  ? -28.122 59.414  109.493 1.00 18.91 ? 547  ASN A N     1 
ATOM   3942  C  CA    . ASN A 1  549  ? -28.265 60.508  108.550 1.00 20.36 ? 547  ASN A CA    1 
ATOM   3943  C  C     . ASN A 1  549  ? -29.397 61.421  109.003 1.00 20.19 ? 547  ASN A C     1 
ATOM   3944  O  O     . ASN A 1  549  ? -30.390 60.968  109.581 1.00 19.73 ? 547  ASN A O     1 
ATOM   3945  C  CB    . ASN A 1  549  ? -28.523 59.945  107.141 1.00 20.54 ? 547  ASN A CB    1 
ATOM   3946  C  CG    . ASN A 1  549  ? -28.358 60.989  106.038 1.00 20.25 ? 547  ASN A CG    1 
ATOM   3947  O  OD1   . ASN A 1  549  ? -27.824 62.075  106.258 1.00 19.52 ? 547  ASN A OD1   1 
ATOM   3948  N  ND2   . ASN A 1  549  ? -28.791 60.644  104.832 1.00 19.25 ? 547  ASN A ND2   1 
ATOM   3949  N  N     . SER A 1  550  ? -29.226 62.720  108.781 1.00 19.12 ? 548  SER A N     1 
ATOM   3950  C  CA    . SER A 1  550  ? -30.331 63.648  108.993 1.00 18.45 ? 548  SER A CA    1 
ATOM   3951  C  C     . SER A 1  550  ? -31.451 63.343  108.010 1.00 19.15 ? 548  SER A C     1 
ATOM   3952  O  O     . SER A 1  550  ? -31.222 62.815  106.921 1.00 19.34 ? 548  SER A O     1 
ATOM   3953  C  CB    . SER A 1  550  ? -29.865 65.087  108.809 1.00 18.60 ? 548  SER A CB    1 
ATOM   3954  O  OG    . SER A 1  550  ? -29.322 65.278  107.517 1.00 18.45 ? 548  SER A OG    1 
ATOM   3955  N  N     . ALA A 1  551  ? -32.674 63.687  108.400 1.00 20.13 ? 549  ALA A N     1 
ATOM   3956  C  CA    . ALA A 1  551  ? -33.851 63.466  107.567 1.00 20.93 ? 549  ALA A CA    1 
ATOM   3957  C  C     . ALA A 1  551  ? -34.329 64.783  106.971 1.00 21.35 ? 549  ALA A C     1 
ATOM   3958  O  O     . ALA A 1  551  ? -34.289 65.825  107.630 1.00 19.78 ? 549  ALA A O     1 
ATOM   3959  C  CB    . ALA A 1  551  ? -34.983 62.824  108.372 1.00 22.75 ? 549  ALA A CB    1 
ATOM   3960  N  N     . GLY A 1  552  ? -34.769 64.732  105.715 1.00 20.36 ? 550  GLY A N     1 
ATOM   3961  C  CA    . GLY A 1  552  ? -35.344 65.871  105.046 1.00 20.07 ? 550  GLY A CA    1 
ATOM   3962  C  C     . GLY A 1  552  ? -36.856 65.796  105.015 1.00 21.62 ? 550  GLY A C     1 
ATOM   3963  O  O     . GLY A 1  552  ? -37.489 65.075  105.792 1.00 21.58 ? 550  GLY A O     1 
ATOM   3964  N  N     . LEU A 1  553  ? -37.445 66.551  104.089 1.00 19.62 ? 551  LEU A N     1 
ATOM   3965  C  CA    . LEU A 1  553  ? -38.891 66.604  103.955 1.00 20.72 ? 551  LEU A CA    1 
ATOM   3966  C  C     . LEU A 1  553  ? -39.213 66.605  102.474 1.00 21.33 ? 551  LEU A C     1 
ATOM   3967  O  O     . LEU A 1  553  ? -38.473 67.190  101.678 1.00 23.16 ? 551  LEU A O     1 
ATOM   3968  C  CB    . LEU A 1  553  ? -39.469 67.849  104.628 1.00 24.17 ? 551  LEU A CB    1 
ATOM   3969  C  CG    . LEU A 1  553  ? -39.370 67.928  106.149 1.00 21.17 ? 551  LEU A CG    1 
ATOM   3970  C  CD1   . LEU A 1  553  ? -39.758 69.310  106.605 1.00 25.17 ? 551  LEU A CD1   1 
ATOM   3971  C  CD2   . LEU A 1  553  ? -40.253 66.885  106.813 1.00 22.54 ? 551  LEU A CD2   1 
ATOM   3972  N  N     . ASP A 1  554  ? -40.307 65.942  102.109 1.00 19.66 ? 552  ASP A N     1 
ATOM   3973  C  CA    . ASP A 1  554  ? -40.681 65.790  100.705 1.00 21.72 ? 552  ASP A CA    1 
ATOM   3974  C  C     . ASP A 1  554  ? -41.646 66.912  100.349 1.00 21.55 ? 552  ASP A C     1 
ATOM   3975  O  O     . ASP A 1  554  ? -42.822 66.866  100.705 1.00 19.08 ? 552  ASP A O     1 
ATOM   3976  C  CB    . ASP A 1  554  ? -41.303 64.422  100.458 1.00 20.74 ? 552  ASP A CB    1 
ATOM   3977  C  CG    . ASP A 1  554  ? -41.636 64.196  98.995  1.00 19.84 ? 552  ASP A CG    1 
ATOM   3978  O  OD1   . ASP A 1  554  ? -41.359 65.099  98.163  1.00 20.42 ? 552  ASP A OD1   1 
ATOM   3979  O  OD2   . ASP A 1  554  ? -42.151 63.102  98.674  1.00 20.61 ? 552  ASP A OD2   1 
ATOM   3980  N  N     . LEU A 1  555  ? -41.154 67.911  99.622  1.00 19.21 ? 553  LEU A N     1 
ATOM   3981  C  CA    . LEU A 1  555  ? -41.994 69.048  99.275  1.00 18.84 ? 553  LEU A CA    1 
ATOM   3982  C  C     . LEU A 1  555  ? -42.899 68.767  98.085  1.00 17.65 ? 553  LEU A C     1 
ATOM   3983  O  O     . LEU A 1  555  ? -43.580 69.682  97.617  1.00 18.98 ? 553  LEU A O     1 
ATOM   3984  C  CB    . LEU A 1  555  ? -41.124 70.273  99.021  1.00 18.02 ? 553  LEU A CB    1 
ATOM   3985  C  CG    . LEU A 1  555  ? -40.357 70.681  100.285 1.00 20.55 ? 553  LEU A CG    1 
ATOM   3986  C  CD1   . LEU A 1  555  ? -39.647 72.001  100.099 1.00 22.80 ? 553  LEU A CD1   1 
ATOM   3987  C  CD2   . LEU A 1  555  ? -41.324 70.754  101.470 1.00 23.24 ? 553  LEU A CD2   1 
ATOM   3988  N  N     . SER A 1  556  ? -42.912 67.533  97.591  1.00 18.54 ? 554  SER A N     1 
ATOM   3989  C  CA    . SER A 1  556  ? -43.899 67.108  96.609  1.00 17.57 ? 554  SER A CA    1 
ATOM   3990  C  C     . SER A 1  556  ? -45.046 66.346  97.248  1.00 18.89 ? 554  SER A C     1 
ATOM   3991  O  O     . SER A 1  556  ? -45.985 65.967  96.543  1.00 19.22 ? 554  SER A O     1 
ATOM   3992  C  CB    . SER A 1  556  ? -43.246 66.236  95.529  1.00 20.22 ? 554  SER A CB    1 
ATOM   3993  O  OG    . SER A 1  556  ? -42.966 64.932  96.019  1.00 19.64 ? 554  SER A OG    1 
ATOM   3994  N  N     . ASN A 1  557  ? -44.993 66.124  98.562  1.00 17.93 ? 555  ASN A N     1 
ATOM   3995  C  CA    . ASN A 1  557  ? -45.993 65.342  99.283  1.00 17.83 ? 555  ASN A CA    1 
ATOM   3996  C  C     . ASN A 1  557  ? -47.024 66.292  99.882  1.00 18.90 ? 555  ASN A C     1 
ATOM   3997  O  O     . ASN A 1  557  ? -46.680 67.128  100.721 1.00 19.65 ? 555  ASN A O     1 
ATOM   3998  C  CB    . ASN A 1  557  ? -45.309 64.507  100.374 1.00 19.54 ? 555  ASN A CB    1 
ATOM   3999  C  CG    . ASN A 1  557  ? -46.278 63.620  101.136 1.00 20.36 ? 555  ASN A CG    1 
ATOM   4000  O  OD1   . ASN A 1  557  ? -47.306 64.083  101.622 1.00 22.15 ? 555  ASN A OD1   1 
ATOM   4001  N  ND2   . ASN A 1  557  ? -45.939 62.331  101.251 1.00 20.78 ? 555  ASN A ND2   1 
ATOM   4002  N  N     . GLU A 1  558  ? -48.293 66.159  99.461  1.00 19.83 ? 556  GLU A N     1 
ATOM   4003  C  CA    . GLU A 1  558  ? -49.305 67.110  99.913  1.00 20.72 ? 556  GLU A CA    1 
ATOM   4004  C  C     . GLU A 1  558  ? -49.525 67.039  101.417 1.00 20.47 ? 556  GLU A C     1 
ATOM   4005  O  O     . GLU A 1  558  ? -49.825 68.067  102.039 1.00 21.71 ? 556  GLU A O     1 
ATOM   4006  C  CB    . GLU A 1  558  ? -50.639 66.897  99.182  1.00 20.79 ? 556  GLU A CB    1 
ATOM   4007  C  CG    . GLU A 1  558  ? -50.614 67.162  97.692  1.00 18.29 ? 556  GLU A CG    1 
ATOM   4008  C  CD    . GLU A 1  558  ? -50.357 68.615  97.307  1.00 18.71 ? 556  GLU A CD    1 
ATOM   4009  O  OE1   . GLU A 1  558  ? -50.376 69.513  98.175  1.00 19.94 ? 556  GLU A OE1   1 
ATOM   4010  O  OE2   . GLU A 1  558  ? -50.146 68.860  96.096  1.00 18.93 ? 556  GLU A OE2   1 
ATOM   4011  N  N     . GLU A 1  559  ? -49.408 65.851  102.020 1.00 19.52 ? 557  GLU A N     1 
ATOM   4012  C  CA    . GLU A 1  559  ? -49.503 65.769  103.478 1.00 22.21 ? 557  GLU A CA    1 
ATOM   4013  C  C     . GLU A 1  559  ? -48.384 66.573  104.124 1.00 21.50 ? 557  GLU A C     1 
ATOM   4014  O  O     . GLU A 1  559  ? -48.611 67.348  105.061 1.00 21.94 ? 557  GLU A O     1 
ATOM   4015  C  CB    . GLU A 1  559  ? -49.442 64.313  103.958 1.00 24.47 ? 557  GLU A CB    1 
ATOM   4016  C  CG    . GLU A 1  559  ? -50.569 63.403  103.497 1.00 24.12 ? 557  GLU A CG    1 
ATOM   4017  C  CD    . GLU A 1  559  ? -50.378 61.970  103.986 1.00 33.22 ? 557  GLU A CD    1 
ATOM   4018  O  OE1   . GLU A 1  559  ? -49.511 61.747  104.860 1.00 39.37 ? 557  GLU A OE1   1 
ATOM   4019  O  OE2   . GLU A 1  559  ? -51.081 61.062  103.493 1.00 29.79 ? 557  GLU A OE2   1 
ATOM   4020  N  N     . THR A 1  560  ? -47.161 66.394  103.628 1.00 20.81 ? 558  THR A N     1 
ATOM   4021  C  CA    . THR A 1  560  ? -46.038 67.154  104.154 1.00 21.64 ? 558  THR A CA    1 
ATOM   4022  C  C     . THR A 1  560  ? -46.247 68.646  103.957 1.00 23.19 ? 558  THR A C     1 
ATOM   4023  O  O     . THR A 1  560  ? -45.980 69.440  104.864 1.00 22.66 ? 558  THR A O     1 
ATOM   4024  C  CB    . THR A 1  560  ? -44.754 66.699  103.469 1.00 20.36 ? 558  THR A CB    1 
ATOM   4025  O  OG1   . THR A 1  560  ? -44.618 65.287  103.663 1.00 23.10 ? 558  THR A OG1   1 
ATOM   4026  C  CG2   . THR A 1  560  ? -43.545 67.448  104.034 1.00 22.90 ? 558  THR A CG2   1 
ATOM   4027  N  N     . LEU A 1  561  ? -46.726 69.050  102.776 1.00 20.07 ? 559  LEU A N     1 
ATOM   4028  C  CA    . LEU A 1  561  ? -46.931 70.473  102.530 1.00 18.96 ? 559  LEU A CA    1 
ATOM   4029  C  C     . LEU A 1  561  ? -48.006 71.040  103.445 1.00 21.08 ? 559  LEU A C     1 
ATOM   4030  O  O     . LEU A 1  561  ? -47.873 72.162  103.944 1.00 21.17 ? 559  LEU A O     1 
ATOM   4031  C  CB    . LEU A 1  561  ? -47.292 70.715  101.063 1.00 19.40 ? 559  LEU A CB    1 
ATOM   4032  C  CG    . LEU A 1  561  ? -46.149 70.504  100.066 1.00 17.90 ? 559  LEU A CG    1 
ATOM   4033  C  CD1   . LEU A 1  561  ? -46.667 70.663  98.630  1.00 18.27 ? 559  LEU A CD1   1 
ATOM   4034  C  CD2   . LEU A 1  561  ? -45.016 71.497  100.318 1.00 17.22 ? 559  LEU A CD2   1 
ATOM   4035  N  N     . ALA A 1  562  ? -49.088 70.289  103.665 1.00 23.90 ? 560  ALA A N     1 
ATOM   4036  C  CA    . ALA A 1  562  ? -50.150 70.790  104.531 1.00 22.38 ? 560  ALA A CA    1 
ATOM   4037  C  C     . ALA A 1  562  ? -49.684 70.889  105.978 1.00 22.60 ? 560  ALA A C     1 
ATOM   4038  O  O     . ALA A 1  562  ? -49.982 71.874  106.666 1.00 22.40 ? 560  ALA A O     1 
ATOM   4039  C  CB    . ALA A 1  562  ? -51.390 69.898  104.428 1.00 24.39 ? 560  ALA A CB    1 
ATOM   4040  N  N     . SER A 1  563  ? -48.954 69.879  106.457 1.00 22.55 ? 561  SER A N     1 
ATOM   4041  C  CA    . SER A 1  563  ? -48.434 69.936  107.820 1.00 25.85 ? 561  SER A CA    1 
ATOM   4042  C  C     . SER A 1  563  ? -47.405 71.052  107.971 1.00 24.80 ? 561  SER A C     1 
ATOM   4043  O  O     . SER A 1  563  ? -47.408 71.781  108.974 1.00 25.26 ? 561  SER A O     1 
ATOM   4044  C  CB    . SER A 1  563  ? -47.818 68.591  108.199 1.00 27.06 ? 561  SER A CB    1 
ATOM   4045  O  OG    . SER A 1  563  ? -47.257 68.654  109.498 1.00 35.54 ? 561  SER A OG    1 
ATOM   4046  N  N     . LEU A 1  564  ? -46.521 71.198  106.983 1.00 24.22 ? 562  LEU A N     1 
ATOM   4047  C  CA    . LEU A 1  564  ? -45.503 72.241  107.035 1.00 22.22 ? 562  LEU A CA    1 
ATOM   4048  C  C     . LEU A 1  564  ? -46.138 73.626  106.985 1.00 24.56 ? 562  LEU A C     1 
ATOM   4049  O  O     . LEU A 1  564  ? -45.718 74.535  107.706 1.00 25.35 ? 562  LEU A O     1 
ATOM   4050  C  CB    . LEU A 1  564  ? -44.518 72.042  105.882 1.00 22.54 ? 562  LEU A CB    1 
ATOM   4051  C  CG    . LEU A 1  564  ? -43.163 72.724  105.881 1.00 27.08 ? 562  LEU A CG    1 
ATOM   4052  C  CD1   . LEU A 1  564  ? -42.419 72.369  107.144 1.00 24.33 ? 562  LEU A CD1   1 
ATOM   4053  C  CD2   . LEU A 1  564  ? -42.380 72.265  104.660 1.00 21.75 ? 562  LEU A CD2   1 
ATOM   4054  N  N     . THR A 1  565  ? -47.176 73.798  106.166 1.00 21.71 ? 563  THR A N     1 
ATOM   4055  C  CA    . THR A 1  565  ? -47.870 75.080  106.119 1.00 24.12 ? 563  THR A CA    1 
ATOM   4056  C  C     . THR A 1  565  ? -48.302 75.525  107.511 1.00 23.63 ? 563  THR A C     1 
ATOM   4057  O  O     . THR A 1  565  ? -48.086 76.675  107.908 1.00 24.86 ? 563  THR A O     1 
ATOM   4058  C  CB    . THR A 1  565  ? -49.077 74.990  105.187 1.00 23.28 ? 563  THR A CB    1 
ATOM   4059  O  OG1   . THR A 1  565  ? -48.621 74.777  103.848 1.00 23.36 ? 563  THR A OG1   1 
ATOM   4060  C  CG2   . THR A 1  565  ? -49.903 76.277  105.253 1.00 28.68 ? 563  THR A CG2   1 
ATOM   4061  N  N     . GLU A 1  566  ? -48.900 74.617  108.280 1.00 25.06 ? 564  GLU A N     1 
ATOM   4062  C  CA    . GLU A 1  566  ? -49.352 75.003  109.613 1.00 26.98 ? 564  GLU A CA    1 
ATOM   4063  C  C     . GLU A 1  566  ? -48.174 75.265  110.543 1.00 26.90 ? 564  GLU A C     1 
ATOM   4064  O  O     . GLU A 1  566  ? -48.170 76.255  111.284 1.00 26.60 ? 564  GLU A O     1 
ATOM   4065  C  CB    . GLU A 1  566  ? -50.274 73.929  110.184 1.00 26.53 ? 564  GLU A CB    1 
ATOM   4066  C  CG    . GLU A 1  566  ? -51.537 73.742  109.357 1.00 33.17 ? 564  GLU A CG    1 
ATOM   4067  C  CD    . GLU A 1  566  ? -52.258 75.060  109.074 1.00 36.73 ? 564  GLU A CD    1 
ATOM   4068  O  OE1   . GLU A 1  566  ? -52.530 75.818  110.035 1.00 40.80 ? 564  GLU A OE1   1 
ATOM   4069  O  OE2   . GLU A 1  566  ? -52.550 75.337  107.883 1.00 38.33 ? 564  GLU A OE2   1 
ATOM   4070  N  N     . ALA A 1  567  ? -47.156 74.406  110.508 1.00 26.64 ? 565  ALA A N     1 
ATOM   4071  C  CA    . ALA A 1  567  ? -46.006 74.619  111.383 1.00 26.87 ? 565  ALA A CA    1 
ATOM   4072  C  C     . ALA A 1  567  ? -45.291 75.921  111.038 1.00 25.64 ? 565  ALA A C     1 
ATOM   4073  O  O     . ALA A 1  567  ? -44.822 76.643  111.932 1.00 26.05 ? 565  ALA A O     1 
ATOM   4074  C  CB    . ALA A 1  567  ? -45.047 73.433  111.289 1.00 27.77 ? 565  ALA A CB    1 
ATOM   4075  N  N     . LEU A 1  568  ? -45.195 76.237  109.745 1.00 25.73 ? 566  LEU A N     1 
ATOM   4076  C  CA    . LEU A 1  568  ? -44.524 77.466  109.335 1.00 23.02 ? 566  LEU A CA    1 
ATOM   4077  C  C     . LEU A 1  568  ? -45.310 78.687  109.783 1.00 25.34 ? 566  LEU A C     1 
ATOM   4078  O  O     . LEU A 1  568  ? -44.733 79.646  110.308 1.00 27.04 ? 566  LEU A O     1 
ATOM   4079  C  CB    . LEU A 1  568  ? -44.326 77.484  107.814 1.00 23.68 ? 566  LEU A CB    1 
ATOM   4080  C  CG    . LEU A 1  568  ? -43.366 76.461  107.196 1.00 24.46 ? 566  LEU A CG    1 
ATOM   4081  C  CD1   . LEU A 1  568  ? -43.381 76.550  105.684 1.00 21.88 ? 566  LEU A CD1   1 
ATOM   4082  C  CD2   . LEU A 1  568  ? -41.951 76.653  107.716 1.00 23.61 ? 566  LEU A CD2   1 
ATOM   4083  N  N     . ARG A 1  569  ? -46.633 78.664  109.595 1.00 24.44 ? 567  ARG A N     1 
ATOM   4084  C  CA    . ARG A 1  569  ? -47.463 79.752  110.092 1.00 26.30 ? 567  ARG A CA    1 
ATOM   4085  C  C     . ARG A 1  569  ? -47.308 79.905  111.597 1.00 27.96 ? 567  ARG A C     1 
ATOM   4086  O  O     . ARG A 1  569  ? -47.170 81.025  112.106 1.00 27.89 ? 567  ARG A O     1 
ATOM   4087  C  CB    . ARG A 1  569  ? -48.932 79.512  109.726 1.00 29.45 ? 567  ARG A CB    1 
ATOM   4088  C  CG    . ARG A 1  569  ? -49.242 79.700  108.250 1.00 29.32 ? 567  ARG A CG    1 
ATOM   4089  C  CD    . ARG A 1  569  ? -50.719 79.409  107.956 1.00 34.81 ? 567  ARG A CD    1 
ATOM   4090  N  NE    . ARG A 1  569  ? -50.993 79.379  106.524 1.00 36.36 ? 567  ARG A NE    1 
ATOM   4091  C  CZ    . ARG A 1  569  ? -52.137 78.964  105.995 1.00 41.22 ? 567  ARG A CZ    1 
ATOM   4092  N  NH1   . ARG A 1  569  ? -53.123 78.513  106.753 1.00 45.48 ? 567  ARG A NH1   1 
ATOM   4093  N  NH2   . ARG A 1  569  ? -52.294 79.000  104.674 1.00 40.76 ? 567  ARG A NH2   1 
ATOM   4094  N  N     . GLU A 1  570  ? -47.304 78.786  112.325 1.00 28.46 ? 568  GLU A N     1 
ATOM   4095  C  CA    . GLU A 1  570  ? -47.159 78.863  113.773 1.00 27.96 ? 568  GLU A CA    1 
ATOM   4096  C  C     . GLU A 1  570  ? -45.802 79.423  114.164 1.00 29.45 ? 568  GLU A C     1 
ATOM   4097  O  O     . GLU A 1  570  ? -45.692 80.142  115.164 1.00 29.48 ? 568  GLU A O     1 
ATOM   4098  C  CB    . GLU A 1  570  ? -47.382 77.483  114.395 1.00 30.58 ? 568  GLU A CB    1 
ATOM   4099  C  CG    . GLU A 1  570  ? -48.829 76.989  114.272 1.00 34.32 ? 568  GLU A CG    1 
ATOM   4100  C  CD    . GLU A 1  570  ? -48.994 75.531  114.666 1.00 41.91 ? 568  GLU A CD    1 
ATOM   4101  O  OE1   . GLU A 1  570  ? -47.970 74.861  114.927 1.00 45.76 ? 568  GLU A OE1   1 
ATOM   4102  O  OE2   . GLU A 1  570  ? -50.150 75.058  114.714 1.00 48.97 ? 568  GLU A OE2   1 
ATOM   4103  N  N     . SER A 1  571  ? -44.761 79.125  113.382 1.00 29.10 ? 569  SER A N     1 
ATOM   4104  C  CA    . SER A 1  571  ? -43.445 79.677  113.685 1.00 27.67 ? 569  SER A CA    1 
ATOM   4105  C  C     . SER A 1  571  ? -43.434 81.188  113.536 1.00 29.27 ? 569  SER A C     1 
ATOM   4106  O  O     . SER A 1  571  ? -42.694 81.874  114.246 1.00 27.29 ? 569  SER A O     1 
ATOM   4107  C  CB    . SER A 1  571  ? -42.387 79.067  112.775 1.00 25.66 ? 569  SER A CB    1 
ATOM   4108  O  OG    . SER A 1  571  ? -42.458 79.635  111.478 1.00 27.24 ? 569  SER A OG    1 
ATOM   4109  N  N     . ALA A 1  572  ? -44.246 81.725  112.630 1.00 28.48 ? 570  ALA A N     1 
ATOM   4110  C  CA    . ALA A 1  572  ? -44.310 83.170  112.467 1.00 27.80 ? 570  ALA A CA    1 
ATOM   4111  C  C     . ALA A 1  572  ? -45.099 83.851  113.575 1.00 31.19 ? 570  ALA A C     1 
ATOM   4112  O  O     . ALA A 1  572  ? -45.069 85.080  113.664 1.00 33.64 ? 570  ALA A O     1 
ATOM   4113  C  CB    . ALA A 1  572  ? -44.909 83.524  111.106 1.00 30.87 ? 570  ALA A CB    1 
ATOM   4114  N  N     . ALA A 1  573  ? -45.797 83.091  114.415 1.00 31.22 ? 571  ALA A N     1 
ATOM   4115  C  CA    . ALA A 1  573  ? -46.510 83.650  115.557 1.00 33.39 ? 571  ALA A CA    1 
ATOM   4116  C  C     . ALA A 1  573  ? -45.704 83.559  116.843 1.00 35.14 ? 571  ALA A C     1 
ATOM   4117  O  O     . ALA A 1  573  ? -46.188 83.980  117.895 1.00 35.39 ? 571  ALA A O     1 
ATOM   4118  C  CB    . ALA A 1  573  ? -47.862 82.953  115.743 1.00 32.09 ? 571  ALA A CB    1 
ATOM   4119  N  N     . MET A 1  574  ? -44.495 83.016  116.790 1.00 33.31 ? 572  MET A N     1 
ATOM   4120  C  CA    . MET A 1  574  ? -43.663 82.931  117.979 1.00 34.68 ? 572  MET A CA    1 
ATOM   4121  C  C     . MET A 1  574  ? -42.892 84.230  118.176 1.00 35.18 ? 572  MET A C     1 
ATOM   4122  O  O     . MET A 1  574  ? -42.560 84.929  117.216 1.00 32.41 ? 572  MET A O     1 
ATOM   4123  C  CB    . MET A 1  574  ? -42.709 81.744  117.879 1.00 34.38 ? 572  MET A CB    1 
ATOM   4124  C  CG    . MET A 1  574  ? -43.436 80.417  117.827 1.00 33.85 ? 572  MET A CG    1 
ATOM   4125  S  SD    . MET A 1  574  ? -42.352 79.035  117.483 1.00 38.67 ? 572  MET A SD    1 
ATOM   4126  C  CE    . MET A 1  574  ? -43.542 77.702  117.302 1.00 40.43 ? 572  MET A CE    1 
ATOM   4127  N  N     . LYS A 1  575  ? -42.630 84.558  119.443 1.00 35.35 ? 573  LYS A N     1 
ATOM   4128  C  CA    . LYS A 1  575  ? -41.898 85.772  119.810 1.00 33.34 ? 573  LYS A CA    1 
ATOM   4129  C  C     . LYS A 1  575  ? -40.405 85.457  119.926 1.00 33.01 ? 573  LYS A C     1 
ATOM   4130  O  O     . LYS A 1  575  ? -39.823 85.361  121.012 1.00 36.25 ? 573  LYS A O     1 
ATOM   4131  C  CB    . LYS A 1  575  ? -42.455 86.357  121.102 1.00 35.55 ? 573  LYS A CB    1 
ATOM   4132  N  N     . TRP A 1  576  ? -39.786 85.293  118.759 1.00 29.85 ? 574  TRP A N     1 
ATOM   4133  C  CA    . TRP A 1  576  ? -38.363 84.982  118.695 1.00 28.33 ? 574  TRP A CA    1 
ATOM   4134  C  C     . TRP A 1  576  ? -37.528 86.121  119.264 1.00 26.22 ? 574  TRP A C     1 
ATOM   4135  O  O     . TRP A 1  576  ? -37.719 87.288  118.909 1.00 29.12 ? 574  TRP A O     1 
ATOM   4136  C  CB    . TRP A 1  576  ? -37.943 84.712  117.253 1.00 29.34 ? 574  TRP A CB    1 
ATOM   4137  C  CG    . TRP A 1  576  ? -38.655 83.574  116.605 1.00 28.48 ? 574  TRP A CG    1 
ATOM   4138  C  CD1   . TRP A 1  576  ? -39.639 83.650  115.659 1.00 24.72 ? 574  TRP A CD1   1 
ATOM   4139  C  CD2   . TRP A 1  576  ? -38.434 82.180  116.847 1.00 25.56 ? 574  TRP A CD2   1 
ATOM   4140  N  NE1   . TRP A 1  576  ? -40.041 82.388  115.297 1.00 25.31 ? 574  TRP A NE1   1 
ATOM   4141  C  CE2   . TRP A 1  576  ? -39.316 81.467  116.006 1.00 26.25 ? 574  TRP A CE2   1 
ATOM   4142  C  CE3   . TRP A 1  576  ? -37.575 81.465  117.690 1.00 23.98 ? 574  TRP A CE3   1 
ATOM   4143  C  CZ2   . TRP A 1  576  ? -39.366 80.072  115.986 1.00 26.99 ? 574  TRP A CZ2   1 
ATOM   4144  C  CZ3   . TRP A 1  576  ? -37.621 80.082  117.671 1.00 28.12 ? 574  TRP A CZ3   1 
ATOM   4145  C  CH2   . TRP A 1  576  ? -38.506 79.396  116.817 1.00 29.57 ? 574  TRP A CH2   1 
ATOM   4146  N  N     . THR A 1  577  ? -36.592 85.778  120.146 1.00 28.28 ? 575  THR A N     1 
ATOM   4147  C  CA    . THR A 1  577  ? -35.638 86.745  120.667 1.00 29.16 ? 575  THR A CA    1 
ATOM   4148  C  C     . THR A 1  577  ? -34.240 86.138  120.676 1.00 27.70 ? 575  THR A C     1 
ATOM   4149  O  O     . THR A 1  577  ? -34.061 84.915  120.644 1.00 29.08 ? 575  THR A O     1 
ATOM   4150  C  CB    . THR A 1  577  ? -35.981 87.210  122.089 1.00 30.96 ? 575  THR A CB    1 
ATOM   4151  O  OG1   . THR A 1  577  ? -35.906 86.095  122.983 1.00 31.14 ? 575  THR A OG1   1 
ATOM   4152  C  CG2   . THR A 1  577  ? -37.381 87.820  122.147 1.00 33.01 ? 575  THR A CG2   1 
ATOM   4153  N  N     . ALA A 1  578  ? -33.248 87.024  120.720 1.00 28.47 ? 576  ALA A N     1 
ATOM   4154  C  CA    . ALA A 1  578  ? -31.858 86.665  120.953 1.00 27.73 ? 576  ALA A CA    1 
ATOM   4155  C  C     . ALA A 1  578  ? -31.289 87.638  121.975 1.00 31.84 ? 576  ALA A C     1 
ATOM   4156  O  O     . ALA A 1  578  ? -31.403 88.856  121.806 1.00 30.28 ? 576  ALA A O     1 
ATOM   4157  C  CB    . ALA A 1  578  ? -31.046 86.708  119.655 1.00 27.63 ? 576  ALA A CB    1 
ATOM   4158  N  N     . LEU A 1  579  ? -30.696 87.108  123.035 1.00 29.31 ? 577  LEU A N     1 
ATOM   4159  C  CA    . LEU A 1  579  ? -30.186 87.911  124.134 1.00 30.41 ? 577  LEU A CA    1 
ATOM   4160  C  C     . LEU A 1  579  ? -28.753 87.505  124.425 1.00 28.68 ? 577  LEU A C     1 
ATOM   4161  O  O     . LEU A 1  579  ? -28.339 86.385  124.102 1.00 28.19 ? 577  LEU A O     1 
ATOM   4162  C  CB    . LEU A 1  579  ? -31.032 87.731  125.406 1.00 30.22 ? 577  LEU A CB    1 
ATOM   4163  C  CG    . LEU A 1  579  ? -32.556 87.691  125.273 1.00 33.66 ? 577  LEU A CG    1 
ATOM   4164  C  CD1   . LEU A 1  579  ? -33.170 87.411  126.630 1.00 33.06 ? 577  LEU A CD1   1 
ATOM   4165  C  CD2   . LEU A 1  579  ? -33.094 88.989  124.690 1.00 39.43 ? 577  LEU A CD2   1 
ATOM   4166  N  N     . PRO A 1  580  ? -27.965 88.392  125.038 1.00 28.04 ? 578  PRO A N     1 
ATOM   4167  C  CA    . PRO A 1  580  ? -26.649 87.970  125.525 1.00 31.64 ? 578  PRO A CA    1 
ATOM   4168  C  C     . PRO A 1  580  ? -26.827 86.976  126.657 1.00 35.28 ? 578  PRO A C     1 
ATOM   4169  O  O     . PRO A 1  580  ? -27.271 87.348  127.749 1.00 35.59 ? 578  PRO A O     1 
ATOM   4170  C  CB    . PRO A 1  580  ? -25.998 89.276  126.000 1.00 32.33 ? 578  PRO A CB    1 
ATOM   4171  C  CG    . PRO A 1  580  ? -26.883 90.390  125.480 1.00 32.63 ? 578  PRO A CG    1 
ATOM   4172  C  CD    . PRO A 1  580  ? -28.247 89.801  125.370 1.00 31.82 ? 578  PRO A CD    1 
ATOM   4173  N  N     . GLN A 1  581  ? -26.534 85.705  126.392 1.00 28.17 ? 579  GLN A N     1 
ATOM   4174  C  CA    . GLN A 1  581  ? -26.764 84.631  127.357 1.00 31.71 ? 579  GLN A CA    1 
ATOM   4175  C  C     . GLN A 1  581  ? -25.434 84.294  128.020 1.00 34.26 ? 579  GLN A C     1 
ATOM   4176  O  O     . GLN A 1  581  ? -24.744 83.344  127.653 1.00 31.31 ? 579  GLN A O     1 
ATOM   4177  C  CB    . GLN A 1  581  ? -27.379 83.412  126.675 1.00 30.23 ? 579  GLN A CB    1 
ATOM   4178  C  CG    . GLN A 1  581  ? -28.763 83.643  126.073 1.00 28.75 ? 579  GLN A CG    1 
ATOM   4179  C  CD    . GLN A 1  581  ? -29.839 83.824  127.124 1.00 34.35 ? 579  GLN A CD    1 
ATOM   4180  O  OE1   . GLN A 1  581  ? -29.592 83.660  128.319 1.00 33.13 ? 579  GLN A OE1   1 
ATOM   4181  N  NE2   . GLN A 1  581  ? -31.051 84.159  126.681 1.00 33.53 ? 579  GLN A NE2   1 
ATOM   4182  N  N     . LEU A 1  582  ? -25.081 85.099  129.017 1.00 32.60 ? 580  LEU A N     1 
ATOM   4183  C  CA    . LEU A 1  582  ? -23.866 84.887  129.782 1.00 35.27 ? 580  LEU A CA    1 
ATOM   4184  C  C     . LEU A 1  582  ? -24.034 83.697  130.727 1.00 33.64 ? 580  LEU A C     1 
ATOM   4185  O  O     . LEU A 1  582  ? -25.138 83.179  130.935 1.00 36.34 ? 580  LEU A O     1 
ATOM   4186  C  CB    . LEU A 1  582  ? -23.502 86.155  130.553 1.00 35.93 ? 580  LEU A CB    1 
ATOM   4187  C  CG    . LEU A 1  582  ? -22.650 87.206  129.826 1.00 39.12 ? 580  LEU A CG    1 
ATOM   4188  C  CD1   . LEU A 1  582  ? -23.330 87.731  128.570 1.00 36.04 ? 580  LEU A CD1   1 
ATOM   4189  C  CD2   . LEU A 1  582  ? -22.340 88.358  130.766 1.00 39.69 ? 580  LEU A CD2   1 
ATOM   4190  N  N     . ALA A 1  583  ? -22.912 83.248  131.295 1.00 33.48 ? 581  ALA A N     1 
ATOM   4191  C  CA    . ALA A 1  583  ? -22.959 82.095  132.188 1.00 33.83 ? 581  ALA A CA    1 
ATOM   4192  C  C     . ALA A 1  583  ? -23.880 82.345  133.370 1.00 38.27 ? 581  ALA A C     1 
ATOM   4193  O  O     . ALA A 1  583  ? -24.487 81.406  133.895 1.00 40.69 ? 581  ALA A O     1 
ATOM   4194  C  CB    . ALA A 1  583  ? -21.557 81.748  132.687 1.00 33.93 ? 581  ALA A CB    1 
ATOM   4195  N  N     . THR A 1  584  ? -24.000 83.601  133.789 1.00 36.77 ? 582  THR A N     1 
ATOM   4196  C  CA    . THR A 1  584  ? -24.782 83.993  134.952 1.00 40.85 ? 582  THR A CA    1 
ATOM   4197  C  C     . THR A 1  584  ? -26.253 84.226  134.641 1.00 43.02 ? 582  THR A C     1 
ATOM   4198  O  O     . THR A 1  584  ? -27.051 84.356  135.575 1.00 43.51 ? 582  THR A O     1 
ATOM   4199  C  CB    . THR A 1  584  ? -24.191 85.269  135.561 1.00 45.06 ? 582  THR A CB    1 
ATOM   4200  O  OG1   . THR A 1  584  ? -24.014 86.248  134.528 1.00 42.43 ? 582  THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1  584  ? -22.849 84.978  136.208 1.00 42.13 ? 582  THR A CG2   1 
ATOM   4202  N  N     . GLY A 1  585  ? -26.625 84.287  133.365 1.00 40.22 ? 583  GLY A N     1 
ATOM   4203  C  CA    . GLY A 1  585  ? -27.978 84.588  132.962 1.00 39.01 ? 583  GLY A CA    1 
ATOM   4204  C  C     . GLY A 1  585  ? -28.006 85.644  131.876 1.00 40.06 ? 583  GLY A C     1 
ATOM   4205  O  O     . GLY A 1  585  ? -26.975 86.223  131.520 1.00 39.37 ? 583  GLY A O     1 
ATOM   4206  N  N     . PRO A 1  586  ? -29.191 85.933  131.338 1.00 39.09 ? 584  PRO A N     1 
ATOM   4207  C  CA    . PRO A 1  586  ? -29.274 86.908  130.245 1.00 36.39 ? 584  PRO A CA    1 
ATOM   4208  C  C     . PRO A 1  586  ? -28.860 88.288  130.727 1.00 42.85 ? 584  PRO A C     1 
ATOM   4209  O  O     . PRO A 1  586  ? -29.134 88.673  131.864 1.00 39.25 ? 584  PRO A O     1 
ATOM   4210  C  CB    . PRO A 1  586  ? -30.751 86.871  129.835 1.00 37.62 ? 584  PRO A CB    1 
ATOM   4211  C  CG    . PRO A 1  586  ? -31.456 85.980  130.848 1.00 41.01 ? 584  PRO A CG    1 
ATOM   4212  C  CD    . PRO A 1  586  ? -30.502 85.682  131.956 1.00 39.92 ? 584  PRO A CD    1 
ATOM   4213  N  N     . ALA A 1  587  ? -28.187 89.030  129.854 1.00 38.41 ? 585  ALA A N     1 
ATOM   4214  C  CA    . ALA A 1  587  ? -27.701 90.360  130.186 1.00 41.17 ? 585  ALA A CA    1 
ATOM   4215  C  C     . ALA A 1  587  ? -28.514 91.417  129.453 1.00 39.91 ? 585  ALA A C     1 
ATOM   4216  O  O     . ALA A 1  587  ? -29.066 91.168  128.378 1.00 40.88 ? 585  ALA A O     1 
ATOM   4217  C  CB    . ALA A 1  587  ? -26.216 90.509  129.835 1.00 37.57 ? 585  ALA A CB    1 
ATOM   4218  N  N     . ALA A 1  588  ? -28.593 92.601  130.053 1.00 39.60 ? 586  ALA A N     1 
ATOM   4219  C  CA    . ALA A 1  588  ? -29.238 93.719  129.391 1.00 42.23 ? 586  ALA A CA    1 
ATOM   4220  C  C     . ALA A 1  588  ? -28.325 94.281  128.302 1.00 40.32 ? 586  ALA A C     1 
ATOM   4221  O  O     . ALA A 1  588  ? -27.109 94.071  128.302 1.00 42.31 ? 586  ALA A O     1 
ATOM   4222  C  CB    . ALA A 1  588  ? -29.598 94.810  130.401 1.00 37.20 ? 586  ALA A CB    1 
ATOM   4223  N  N     . GLY A 1  589  ? -28.930 95.005  127.371 1.00 38.65 ? 587  GLY A N     1 
ATOM   4224  C  CA    . GLY A 1  589  ? -28.177 95.590  126.277 1.00 38.62 ? 587  GLY A CA    1 
ATOM   4225  C  C     . GLY A 1  589  ? -29.093 96.393  125.383 1.00 41.10 ? 587  GLY A C     1 
ATOM   4226  O  O     . GLY A 1  589  ? -30.262 96.625  125.709 1.00 42.33 ? 587  GLY A O     1 
ATOM   4227  N  N     . GLU A 1  590  ? -28.546 96.826  124.248 1.00 38.15 ? 588  GLU A N     1 
ATOM   4228  C  CA    . GLU A 1  590  ? -29.333 97.572  123.273 1.00 38.87 ? 588  GLU A CA    1 
ATOM   4229  C  C     . GLU A 1  590  ? -30.191 96.610  122.461 1.00 37.97 ? 588  GLU A C     1 
ATOM   4230  O  O     . GLU A 1  590  ? -29.682 95.636  121.898 1.00 37.29 ? 588  GLU A O     1 
ATOM   4231  C  CB    . GLU A 1  590  ? -28.424 98.388  122.351 1.00 43.19 ? 588  GLU A CB    1 
ATOM   4232  N  N     . THR A 1  591  ? -31.492 96.882  122.398 1.00 34.72 ? 589  THR A N     1 
ATOM   4233  C  CA    . THR A 1  591  ? -32.452 95.990  121.760 1.00 35.33 ? 589  THR A CA    1 
ATOM   4234  C  C     . THR A 1  591  ? -33.014 96.622  120.492 1.00 36.59 ? 589  THR A C     1 
ATOM   4235  O  O     . THR A 1  591  ? -33.353 97.810  120.475 1.00 37.47 ? 589  THR A O     1 
ATOM   4236  C  CB    . THR A 1  591  ? -33.589 95.647  122.733 1.00 39.59 ? 589  THR A CB    1 
ATOM   4237  O  OG1   . THR A 1  591  ? -33.048 94.957  123.875 1.00 36.76 ? 589  THR A OG1   1 
ATOM   4238  C  CG2   . THR A 1  591  ? -34.647 94.769  122.050 1.00 35.77 ? 589  THR A CG2   1 
ATOM   4239  N  N     . ARG A 1  592  ? -33.118 95.824  119.426 1.00 33.39 ? 590  ARG A N     1 
ATOM   4240  C  CA    . ARG A 1  592  ? -33.702 96.282  118.174 1.00 34.45 ? 590  ARG A CA    1 
ATOM   4241  C  C     . ARG A 1  592  ? -34.476 95.138  117.532 1.00 32.60 ? 590  ARG A C     1 
ATOM   4242  O  O     . ARG A 1  592  ? -34.334 93.971  117.911 1.00 31.66 ? 590  ARG A O     1 
ATOM   4243  C  CB    . ARG A 1  592  ? -32.631 96.815  117.211 1.00 34.03 ? 590  ARG A CB    1 
ATOM   4244  C  CG    . ARG A 1  592  ? -31.676 95.752  116.702 1.00 36.60 ? 590  ARG A CG    1 
ATOM   4245  C  CD    . ARG A 1  592  ? -30.907 96.221  115.473 1.00 36.81 ? 590  ARG A CD    1 
ATOM   4246  N  NE    . ARG A 1  592  ? -29.838 95.291  115.128 1.00 38.89 ? 590  ARG A NE    1 
ATOM   4247  C  CZ    . ARG A 1  592  ? -30.009 94.210  114.381 1.00 38.70 ? 590  ARG A CZ    1 
ATOM   4248  N  NH1   . ARG A 1  592  ? -31.185 93.917  113.855 1.00 38.01 ? 590  ARG A NH1   1 
ATOM   4249  N  NH2   . ARG A 1  592  ? -28.975 93.402  114.160 1.00 38.87 ? 590  ARG A NH2   1 
ATOM   4250  N  N     . THR A 1  593  ? -35.303 95.477  116.546 1.00 33.48 ? 591  THR A N     1 
ATOM   4251  C  CA    . THR A 1  593  ? -36.038 94.440  115.843 1.00 30.69 ? 591  THR A CA    1 
ATOM   4252  C  C     . THR A 1  593  ? -35.148 93.745  114.812 1.00 31.99 ? 591  THR A C     1 
ATOM   4253  O  O     . THR A 1  593  ? -34.132 94.278  114.359 1.00 33.50 ? 591  THR A O     1 
ATOM   4254  C  CB    . THR A 1  593  ? -37.266 95.017  115.142 1.00 35.06 ? 591  THR A CB    1 
ATOM   4255  O  OG1   . THR A 1  593  ? -36.873 96.159  114.375 1.00 35.93 ? 591  THR A OG1   1 
ATOM   4256  C  CG2   . THR A 1  593  ? -38.338 95.410  116.152 1.00 36.11 ? 591  THR A CG2   1 
ATOM   4257  N  N     . VAL A 1  594  ? -35.552 92.532  114.449 1.00 27.12 ? 592  VAL A N     1 
ATOM   4258  C  CA    . VAL A 1  594  ? -34.960 91.779  113.348 1.00 28.14 ? 592  VAL A CA    1 
ATOM   4259  C  C     . VAL A 1  594  ? -36.022 91.692  112.262 1.00 29.39 ? 592  VAL A C     1 
ATOM   4260  O  O     . VAL A 1  594  ? -37.120 91.173  112.505 1.00 28.90 ? 592  VAL A O     1 
ATOM   4261  C  CB    . VAL A 1  594  ? -34.499 90.385  113.796 1.00 26.01 ? 592  VAL A CB    1 
ATOM   4262  C  CG1   . VAL A 1  594  ? -34.027 89.563  112.597 1.00 26.86 ? 592  VAL A CG1   1 
ATOM   4263  C  CG2   . VAL A 1  594  ? -33.388 90.504  114.843 1.00 27.43 ? 592  VAL A CG2   1 
ATOM   4264  N  N     . LEU A 1  595  ? -35.713 92.217  111.078 1.00 27.94 ? 593  LEU A N     1 
ATOM   4265  C  CA    . LEU A 1  595  ? -36.683 92.333  109.996 1.00 27.35 ? 593  LEU A CA    1 
ATOM   4266  C  C     . LEU A 1  595  ? -36.418 91.289  108.916 1.00 26.51 ? 593  LEU A C     1 
ATOM   4267  O  O     . LEU A 1  595  ? -35.266 90.943  108.636 1.00 28.82 ? 593  LEU A O     1 
ATOM   4268  C  CB    . LEU A 1  595  ? -36.651 93.740  109.383 1.00 28.84 ? 593  LEU A CB    1 
ATOM   4269  C  CG    . LEU A 1  595  ? -36.859 94.946  110.309 1.00 32.05 ? 593  LEU A CG    1 
ATOM   4270  C  CD1   . LEU A 1  595  ? -36.890 96.239  109.512 1.00 31.28 ? 593  LEU A CD1   1 
ATOM   4271  C  CD2   . LEU A 1  595  ? -38.130 94.793  111.130 1.00 32.37 ? 593  LEU A CD2   1 
ATOM   4272  N  N     . ASN A 1  596  ? -37.492 90.794  108.309 1.00 25.22 ? 594  ASN A N     1 
ATOM   4273  C  CA    . ASN A 1  596  ? -37.394 89.871  107.179 1.00 25.52 ? 594  ASN A CA    1 
ATOM   4274  C  C     . ASN A 1  596  ? -36.710 90.566  106.004 1.00 25.21 ? 594  ASN A C     1 
ATOM   4275  O  O     . ASN A 1  596  ? -37.205 91.608  105.545 1.00 25.04 ? 594  ASN A O     1 
ATOM   4276  C  CB    . ASN A 1  596  ? -38.815 89.426  106.812 1.00 24.45 ? 594  ASN A CB    1 
ATOM   4277  C  CG    . ASN A 1  596  ? -38.861 88.338  105.751 1.00 26.60 ? 594  ASN A CG    1 
ATOM   4278  O  OD1   . ASN A 1  596  ? -37.998 88.252  104.879 1.00 25.87 ? 594  ASN A OD1   1 
ATOM   4279  N  ND2   . ASN A 1  596  ? -39.887 87.499  105.827 1.00 24.69 ? 594  ASN A ND2   1 
ATOM   4280  N  N     . PRO A 1  597  ? -35.590 90.043  105.486 1.00 25.25 ? 595  PRO A N     1 
ATOM   4281  C  CA    . PRO A 1  597  ? -34.915 90.723  104.364 1.00 21.90 ? 595  PRO A CA    1 
ATOM   4282  C  C     . PRO A 1  597  ? -35.762 90.801  103.103 1.00 24.23 ? 595  PRO A C     1 
ATOM   4283  O  O     . PRO A 1  597  ? -35.514 91.670  102.254 1.00 23.49 ? 595  PRO A O     1 
ATOM   4284  C  CB    . PRO A 1  597  ? -33.654 89.875  104.142 1.00 23.13 ? 595  PRO A CB    1 
ATOM   4285  C  CG    . PRO A 1  597  ? -33.989 88.531  104.710 1.00 23.37 ? 595  PRO A CG    1 
ATOM   4286  C  CD    . PRO A 1  597  ? -34.859 88.836  105.911 1.00 21.95 ? 595  PRO A CD    1 
ATOM   4287  N  N     . GLY A 1  598  ? -36.763 89.949  102.963 1.00 21.52 ? 596  GLY A N     1 
ATOM   4288  C  CA    . GLY A 1  598  ? -37.626 90.007  101.806 1.00 22.10 ? 596  GLY A CA    1 
ATOM   4289  C  C     . GLY A 1  598  ? -38.833 90.897  101.964 1.00 25.23 ? 596  GLY A C     1 
ATOM   4290  O  O     . GLY A 1  598  ? -39.596 91.064  101.006 1.00 24.47 ? 596  GLY A O     1 
ATOM   4291  N  N     . ASP A 1  599  ? -39.024 91.471  103.149 1.00 24.34 ? 597  ASP A N     1 
ATOM   4292  C  CA    . ASP A 1  599  ? -40.152 92.349  103.440 1.00 25.72 ? 597  ASP A CA    1 
ATOM   4293  C  C     . ASP A 1  599  ? -39.940 92.946  104.819 1.00 25.63 ? 597  ASP A C     1 
ATOM   4294  O  O     . ASP A 1  599  ? -40.256 92.305  105.828 1.00 27.34 ? 597  ASP A O     1 
ATOM   4295  C  CB    . ASP A 1  599  ? -41.466 91.576  103.377 1.00 24.97 ? 597  ASP A CB    1 
ATOM   4296  C  CG    . ASP A 1  599  ? -42.689 92.472  103.510 1.00 29.96 ? 597  ASP A CG    1 
ATOM   4297  O  OD1   . ASP A 1  599  ? -42.551 93.647  103.913 1.00 28.66 ? 597  ASP A OD1   1 
ATOM   4298  O  OD2   . ASP A 1  599  ? -43.793 91.985  103.199 1.00 30.80 ? 597  ASP A OD2   1 
ATOM   4299  N  N     . HIS A 1  600  ? -39.384 94.158  104.871 1.00 25.06 ? 598  HIS A N     1 
ATOM   4300  C  CA    . HIS A 1  600  ? -39.023 94.771  106.143 1.00 28.25 ? 598  HIS A CA    1 
ATOM   4301  C  C     . HIS A 1  600  ? -40.233 95.067  107.019 1.00 31.12 ? 598  HIS A C     1 
ATOM   4302  O  O     . HIS A 1  600  ? -40.058 95.343  108.213 1.00 30.99 ? 598  HIS A O     1 
ATOM   4303  C  CB    . HIS A 1  600  ? -38.222 96.048  105.893 1.00 29.09 ? 598  HIS A CB    1 
ATOM   4304  C  CG    . HIS A 1  600  ? -36.836 95.798  105.387 1.00 33.25 ? 598  HIS A CG    1 
ATOM   4305  N  ND1   . HIS A 1  600  ? -35.931 96.811  105.151 1.00 33.20 ? 598  HIS A ND1   1 
ATOM   4306  C  CD2   . HIS A 1  600  ? -36.201 94.644  105.070 1.00 30.59 ? 598  HIS A CD2   1 
ATOM   4307  C  CE1   . HIS A 1  600  ? -34.796 96.291  104.715 1.00 33.57 ? 598  HIS A CE1   1 
ATOM   4308  N  NE2   . HIS A 1  600  ? -34.934 94.978  104.656 1.00 29.64 ? 598  HIS A NE2   1 
ATOM   4309  N  N     . ARG A 1  601  ? -41.443 95.003  106.463 1.00 28.11 ? 599  ARG A N     1 
ATOM   4310  C  CA    . ARG A 1  601  ? -42.657 95.120  107.262 1.00 29.42 ? 599  ARG A CA    1 
ATOM   4311  C  C     . ARG A 1  601  ? -42.862 93.918  108.172 1.00 32.88 ? 599  ARG A C     1 
ATOM   4312  O  O     . ARG A 1  601  ? -43.592 94.023  109.164 1.00 29.43 ? 599  ARG A O     1 
ATOM   4313  C  CB    . ARG A 1  601  ? -43.874 95.276  106.347 1.00 32.27 ? 599  ARG A CB    1 
ATOM   4314  C  CG    . ARG A 1  601  ? -43.778 96.446  105.403 1.00 29.80 ? 599  ARG A CG    1 
ATOM   4315  C  CD    . ARG A 1  601  ? -44.892 96.418  104.390 1.00 32.46 ? 599  ARG A CD    1 
ATOM   4316  N  NE    . ARG A 1  601  ? -44.867 95.188  103.613 1.00 29.13 ? 599  ARG A NE    1 
ATOM   4317  C  CZ    . ARG A 1  601  ? -45.747 94.881  102.671 1.00 34.28 ? 599  ARG A CZ    1 
ATOM   4318  N  NH1   . ARG A 1  601  ? -46.735 95.705  102.347 1.00 34.05 ? 599  ARG A NH1   1 
ATOM   4319  N  NH2   . ARG A 1  601  ? -45.638 93.718  102.042 1.00 31.30 ? 599  ARG A NH2   1 
ATOM   4320  N  N     . ASP A 1  602  ? -42.246 92.784  107.847 1.00 28.30 ? 600  ASP A N     1 
ATOM   4321  C  CA    . ASP A 1  602  ? -42.420 91.539  108.592 1.00 30.13 ? 600  ASP A CA    1 
ATOM   4322  C  C     . ASP A 1  602  ? -41.358 91.491  109.681 1.00 31.48 ? 600  ASP A C     1 
ATOM   4323  O  O     . ASP A 1  602  ? -40.195 91.177  109.418 1.00 29.54 ? 600  ASP A O     1 
ATOM   4324  C  CB    . ASP A 1  602  ? -42.315 90.337  107.658 1.00 29.99 ? 600  ASP A CB    1 
ATOM   4325  C  CG    . ASP A 1  602  ? -42.470 89.016  108.382 1.00 31.97 ? 600  ASP A CG    1 
ATOM   4326  O  OD1   . ASP A 1  602  ? -43.062 89.016  109.478 1.00 32.26 ? 600  ASP A OD1   1 
ATOM   4327  O  OD2   . ASP A 1  602  ? -41.995 87.978  107.857 1.00 29.15 ? 600  ASP A OD2   1 
ATOM   4328  N  N     . VAL A 1  603  ? -41.757 91.795  110.908 1.00 30.28 ? 601  VAL A N     1 
ATOM   4329  C  CA    . VAL A 1  603  ? -40.833 91.765  112.035 1.00 29.88 ? 601  VAL A CA    1 
ATOM   4330  C  C     . VAL A 1  603  ? -40.711 90.324  112.512 1.00 29.81 ? 601  VAL A C     1 
ATOM   4331  O  O     . VAL A 1  603  ? -41.697 89.710  112.932 1.00 30.81 ? 601  VAL A O     1 
ATOM   4332  C  CB    . VAL A 1  603  ? -41.307 92.693  113.163 1.00 30.39 ? 601  VAL A CB    1 
ATOM   4333  C  CG1   . VAL A 1  603  ? -40.354 92.636  114.353 1.00 30.20 ? 601  VAL A CG1   1 
ATOM   4334  C  CG2   . VAL A 1  603  ? -41.417 94.109  112.650 1.00 33.21 ? 601  VAL A CG2   1 
ATOM   4335  N  N     . VAL A 1  604  ? -39.501 89.781  112.445 1.00 28.97 ? 602  VAL A N     1 
ATOM   4336  C  CA    . VAL A 1  604  ? -39.292 88.378  112.789 1.00 27.61 ? 602  VAL A CA    1 
ATOM   4337  C  C     . VAL A 1  604  ? -39.054 88.208  114.282 1.00 28.11 ? 602  VAL A C     1 
ATOM   4338  O  O     . VAL A 1  604  ? -39.495 87.218  114.873 1.00 28.58 ? 602  VAL A O     1 
ATOM   4339  C  CB    . VAL A 1  604  ? -38.123 87.797  111.969 1.00 27.30 ? 602  VAL A CB    1 
ATOM   4340  C  CG1   . VAL A 1  604  ? -37.893 86.337  112.328 1.00 24.73 ? 602  VAL A CG1   1 
ATOM   4341  C  CG2   . VAL A 1  604  ? -38.394 87.945  110.473 1.00 26.59 ? 602  VAL A CG2   1 
ATOM   4342  N  N     . GLY A 1  605  ? -38.377 89.156  114.908 1.00 28.18 ? 603  GLY A N     1 
ATOM   4343  C  CA    . GLY A 1  605  ? -38.092 89.036  116.318 1.00 27.31 ? 603  GLY A CA    1 
ATOM   4344  C  C     . GLY A 1  605  ? -37.321 90.230  116.814 1.00 26.09 ? 603  GLY A C     1 
ATOM   4345  O  O     . GLY A 1  605  ? -37.306 91.288  116.183 1.00 28.05 ? 603  GLY A O     1 
ATOM   4346  N  N     . SER A 1  606  ? -36.679 90.046  117.960 1.00 26.62 ? 604  SER A N     1 
ATOM   4347  C  CA    . SER A 1  606  ? -35.952 91.116  118.615 1.00 25.93 ? 604  SER A CA    1 
ATOM   4348  C  C     . SER A 1  606  ? -34.632 90.578  119.127 1.00 31.44 ? 604  SER A C     1 
ATOM   4349  O  O     . SER A 1  606  ? -34.569 89.462  119.651 1.00 30.19 ? 604  SER A O     1 
ATOM   4350  C  CB    . SER A 1  606  ? -36.756 91.707  119.776 1.00 32.92 ? 604  SER A CB    1 
ATOM   4351  O  OG    . SER A 1  606  ? -37.894 92.387  119.289 1.00 37.09 ? 604  SER A OG    1 
ATOM   4352  N  N     . VAL A 1  607  ? -33.580 91.371  118.967 1.00 28.56 ? 605  VAL A N     1 
ATOM   4353  C  CA    . VAL A 1  607  ? -32.249 90.990  119.414 1.00 28.58 ? 605  VAL A CA    1 
ATOM   4354  C  C     . VAL A 1  607  ? -31.757 92.031  120.402 1.00 32.50 ? 605  VAL A C     1 
ATOM   4355  O  O     . VAL A 1  607  ? -31.866 93.238  120.153 1.00 29.51 ? 605  VAL A O     1 
ATOM   4356  C  CB    . VAL A 1  607  ? -31.265 90.833  118.238 1.00 30.54 ? 605  VAL A CB    1 
ATOM   4357  C  CG1   . VAL A 1  607  ? -31.218 92.093  117.378 1.00 30.94 ? 605  VAL A CG1   1 
ATOM   4358  C  CG2   . VAL A 1  607  ? -29.880 90.486  118.760 1.00 30.29 ? 605  VAL A CG2   1 
ATOM   4359  N  N     . THR A 1  608  ? -31.248 91.562  121.534 1.00 28.38 ? 606  THR A N     1 
ATOM   4360  C  CA    . THR A 1  608  ? -30.528 92.404  122.474 1.00 34.05 ? 606  THR A CA    1 
ATOM   4361  C  C     . THR A 1  608  ? -29.046 92.127  122.279 1.00 33.53 ? 606  THR A C     1 
ATOM   4362  O  O     . THR A 1  608  ? -28.598 90.989  122.454 1.00 32.42 ? 606  THR A O     1 
ATOM   4363  C  CB    . THR A 1  608  ? -30.953 92.118  123.912 1.00 35.17 ? 606  THR A CB    1 
ATOM   4364  O  OG1   . THR A 1  608  ? -32.366 92.325  124.029 1.00 32.57 ? 606  THR A OG1   1 
ATOM   4365  C  CG2   . THR A 1  608  ? -30.228 93.041  124.874 1.00 36.07 ? 606  THR A CG2   1 
ATOM   4366  N  N     . GLU A 1  609  ? -28.298 93.148  121.897 1.00 34.46 ? 607  GLU A N     1 
ATOM   4367  C  CA    . GLU A 1  609  ? -26.905 92.930  121.560 1.00 33.52 ? 607  GLU A CA    1 
ATOM   4368  C  C     . GLU A 1  609  ? -26.005 93.145  122.774 1.00 32.72 ? 607  GLU A C     1 
ATOM   4369  O  O     . GLU A 1  609  ? -26.395 93.744  123.781 1.00 32.74 ? 607  GLU A O     1 
ATOM   4370  C  CB    . GLU A 1  609  ? -26.513 93.815  120.375 1.00 32.68 ? 607  GLU A CB    1 
ATOM   4371  C  CG    . GLU A 1  609  ? -27.119 93.250  119.073 1.00 32.73 ? 607  GLU A CG    1 
ATOM   4372  C  CD    . GLU A 1  609  ? -26.858 94.092  117.832 1.00 37.10 ? 607  GLU A CD    1 
ATOM   4373  O  OE1   . GLU A 1  609  ? -26.640 95.315  117.968 1.00 38.84 ? 607  GLU A OE1   1 
ATOM   4374  O  OE2   . GLU A 1  609  ? -26.881 93.518  116.711 1.00 34.68 ? 607  GLU A OE2   1 
ATOM   4375  N  N     . THR A 1  610  ? -24.795 92.606  122.673 1.00 30.51 ? 608  THR A N     1 
ATOM   4376  C  CA    . THR A 1  610  ? -23.882 92.481  123.802 1.00 33.18 ? 608  THR A CA    1 
ATOM   4377  C  C     . THR A 1  610  ? -22.988 93.707  123.898 1.00 33.66 ? 608  THR A C     1 
ATOM   4378  O  O     . THR A 1  610  ? -22.371 94.110  122.907 1.00 32.94 ? 608  THR A O     1 
ATOM   4379  C  CB    . THR A 1  610  ? -23.018 91.228  123.630 1.00 32.38 ? 608  THR A CB    1 
ATOM   4380  O  OG1   . THR A 1  610  ? -23.857 90.108  123.325 1.00 31.91 ? 608  THR A OG1   1 
ATOM   4381  C  CG2   . THR A 1  610  ? -22.200 90.937  124.885 1.00 32.49 ? 608  THR A CG2   1 
ATOM   4382  N  N     . SER A 1  611  ? -22.901 94.281  125.094 1.00 34.91 ? 609  SER A N     1 
ATOM   4383  C  CA    . SER A 1  611  ? -21.921 95.326  125.328 1.00 35.44 ? 609  SER A CA    1 
ATOM   4384  C  C     . SER A 1  611  ? -20.518 94.740  125.249 1.00 35.93 ? 609  SER A C     1 
ATOM   4385  O  O     . SER A 1  611  ? -20.303 93.541  125.456 1.00 33.17 ? 609  SER A O     1 
ATOM   4386  C  CB    . SER A 1  611  ? -22.137 95.980  126.695 1.00 35.04 ? 609  SER A CB    1 
ATOM   4387  O  OG    . SER A 1  611  ? -21.696 95.133  127.741 1.00 33.48 ? 609  SER A OG    1 
ATOM   4388  N  N     . GLU A 1  612  ? -19.549 95.598  124.931 1.00 36.19 ? 610  GLU A N     1 
ATOM   4389  C  CA    . GLU A 1  612  ? -18.173 95.120  124.899 1.00 37.13 ? 610  GLU A CA    1 
ATOM   4390  C  C     . GLU A 1  612  ? -17.704 94.707  126.287 1.00 36.05 ? 610  GLU A C     1 
ATOM   4391  O  O     . GLU A 1  612  ? -16.901 93.775  126.416 1.00 36.47 ? 610  GLU A O     1 
ATOM   4392  C  CB    . GLU A 1  612  ? -17.256 96.181  124.291 1.00 42.15 ? 610  GLU A CB    1 
ATOM   4393  C  CG    . GLU A 1  612  ? -17.452 96.327  122.782 1.00 45.61 ? 610  GLU A CG    1 
ATOM   4394  C  CD    . GLU A 1  612  ? -16.392 97.184  122.114 1.00 54.82 ? 610  GLU A CD    1 
ATOM   4395  O  OE1   . GLU A 1  612  ? -15.280 97.313  122.672 1.00 62.41 ? 610  GLU A OE1   1 
ATOM   4396  O  OE2   . GLU A 1  612  ? -16.677 97.729  121.025 1.00 53.23 ? 610  GLU A OE2   1 
ATOM   4397  N  N     . GLU A 1  613  ? -18.231 95.351  127.331 1.00 34.87 ? 611  GLU A N     1 
ATOM   4398  C  CA    . GLU A 1  613  ? -17.910 94.946  128.697 1.00 36.96 ? 611  GLU A CA    1 
ATOM   4399  C  C     . GLU A 1  613  ? -18.403 93.535  128.983 1.00 34.18 ? 611  GLU A C     1 
ATOM   4400  O  O     . GLU A 1  613  ? -17.687 92.733  129.587 1.00 31.62 ? 611  GLU A O     1 
ATOM   4401  C  CB    . GLU A 1  613  ? -18.510 95.935  129.699 1.00 36.68 ? 611  GLU A CB    1 
ATOM   4402  N  N     . ASP A 1  614  ? -19.629 93.211  128.554 1.00 35.75 ? 612  ASP A N     1 
ATOM   4403  C  CA    . ASP A 1  614  ? -20.168 91.884  128.825 1.00 31.34 ? 612  ASP A CA    1 
ATOM   4404  C  C     . ASP A 1  614  ? -19.504 90.818  127.967 1.00 33.21 ? 612  ASP A C     1 
ATOM   4405  O  O     . ASP A 1  614  ? -19.404 89.663  128.392 1.00 30.06 ? 612  ASP A O     1 
ATOM   4406  C  CB    . ASP A 1  614  ? -21.679 91.872  128.615 1.00 34.70 ? 612  ASP A CB    1 
ATOM   4407  C  CG    . ASP A 1  614  ? -22.412 92.641  129.696 1.00 35.37 ? 612  ASP A CG    1 
ATOM   4408  O  OD1   . ASP A 1  614  ? -21.848 92.773  130.800 1.00 35.78 ? 612  ASP A OD1   1 
ATOM   4409  O  OD2   . ASP A 1  614  ? -23.540 93.105  129.438 1.00 37.72 ? 612  ASP A OD2   1 
ATOM   4410  N  N     . ALA A 1  615  ? -19.053 91.176  126.765 1.00 29.20 ? 613  ALA A N     1 
ATOM   4411  C  CA    . ALA A 1  615  ? -18.316 90.215  125.954 1.00 29.62 ? 613  ALA A CA    1 
ATOM   4412  C  C     . ALA A 1  615  ? -17.026 89.813  126.653 1.00 30.50 ? 613  ALA A C     1 
ATOM   4413  O  O     . ALA A 1  615  ? -16.702 88.624  126.752 1.00 29.80 ? 613  ALA A O     1 
ATOM   4414  C  CB    . ALA A 1  615  ? -18.026 90.797  124.572 1.00 31.06 ? 613  ALA A CB    1 
ATOM   4415  N  N     . ARG A 1  616  ? -16.295 90.798  127.182 1.00 34.02 ? 614  ARG A N     1 
ATOM   4416  C  CA    . ARG A 1  616  ? -15.081 90.496  127.934 1.00 34.06 ? 614  ARG A CA    1 
ATOM   4417  C  C     . ARG A 1  616  ? -15.400 89.717  129.208 1.00 31.32 ? 614  ARG A C     1 
ATOM   4418  O  O     . ARG A 1  616  ? -14.666 88.794  129.579 1.00 32.59 ? 614  ARG A O     1 
ATOM   4419  C  CB    . ARG A 1  616  ? -14.333 91.788  128.252 1.00 33.34 ? 614  ARG A CB    1 
ATOM   4420  N  N     . ARG A 1  617  ? -16.503 90.058  129.879 1.00 32.81 ? 615  ARG A N     1 
ATOM   4421  C  CA    . ARG A 1  617  ? -16.916 89.289  131.047 1.00 32.80 ? 615  ARG A CA    1 
ATOM   4422  C  C     . ARG A 1  617  ? -17.248 87.848  130.674 1.00 32.85 ? 615  ARG A C     1 
ATOM   4423  O  O     . ARG A 1  617  ? -16.917 86.917  131.416 1.00 31.23 ? 615  ARG A O     1 
ATOM   4424  C  CB    . ARG A 1  617  ? -18.114 89.956  131.717 1.00 35.11 ? 615  ARG A CB    1 
ATOM   4425  C  CG    . ARG A 1  617  ? -18.577 89.253  132.985 1.00 41.29 ? 615  ARG A CG    1 
ATOM   4426  C  CD    . ARG A 1  617  ? -19.218 90.229  133.965 1.00 44.15 ? 615  ARG A CD    1 
ATOM   4427  N  NE    . ARG A 1  617  ? -20.380 90.899  133.392 1.00 43.38 ? 615  ARG A NE    1 
ATOM   4428  C  CZ    . ARG A 1  617  ? -21.621 90.436  133.470 1.00 48.04 ? 615  ARG A CZ    1 
ATOM   4429  N  NH1   . ARG A 1  617  ? -21.897 89.301  134.095 1.00 48.00 ? 615  ARG A NH1   1 
ATOM   4430  N  NH2   . ARG A 1  617  ? -22.611 91.130  132.909 1.00 42.03 ? 615  ARG A NH2   1 
ATOM   4431  N  N     . ALA A 1  618  ? -17.927 87.644  129.537 1.00 31.02 ? 616  ALA A N     1 
ATOM   4432  C  CA    . ALA A 1  618  ? -18.267 86.283  129.126 1.00 29.48 ? 616  ALA A CA    1 
ATOM   4433  C  C     . ALA A 1  618  ? -17.015 85.428  128.967 1.00 29.00 ? 616  ALA A C     1 
ATOM   4434  O  O     . ALA A 1  618  ? -16.999 84.252  129.354 1.00 28.67 ? 616  ALA A O     1 
ATOM   4435  C  CB    . ALA A 1  618  ? -19.076 86.305  127.827 1.00 28.08 ? 616  ALA A CB    1 
ATOM   4436  N  N     . VAL A 1  619  ? -15.950 85.999  128.402 1.00 27.17 ? 617  VAL A N     1 
ATOM   4437  C  CA    . VAL A 1  619  ? -14.725 85.226  128.222 1.00 29.75 ? 617  VAL A CA    1 
ATOM   4438  C  C     . VAL A 1  619  ? -14.142 84.846  129.576 1.00 30.96 ? 617  VAL A C     1 
ATOM   4439  O  O     . VAL A 1  619  ? -13.653 83.725  129.767 1.00 29.51 ? 617  VAL A O     1 
ATOM   4440  C  CB    . VAL A 1  619  ? -13.713 86.007  127.361 1.00 29.41 ? 617  VAL A CB    1 
ATOM   4441  C  CG1   . VAL A 1  619  ? -12.390 85.247  127.289 1.00 32.34 ? 617  VAL A CG1   1 
ATOM   4442  C  CG2   . VAL A 1  619  ? -14.267 86.234  125.951 1.00 26.93 ? 617  VAL A CG2   1 
ATOM   4443  N  N     . ARG A 1  620  ? -14.213 85.760  130.544 1.00 30.16 ? 618  ARG A N     1 
ATOM   4444  C  CA    . ARG A 1  620  ? -13.707 85.448  131.876 1.00 31.61 ? 618  ARG A CA    1 
ATOM   4445  C  C     . ARG A 1  620  ? -14.509 84.322  132.512 1.00 31.53 ? 618  ARG A C     1 
ATOM   4446  O  O     . ARG A 1  620  ? -13.935 83.407  133.117 1.00 32.64 ? 618  ARG A O     1 
ATOM   4447  C  CB    . ARG A 1  620  ? -13.727 86.700  132.754 1.00 33.91 ? 618  ARG A CB    1 
ATOM   4448  C  CG    . ARG A 1  620  ? -12.703 87.726  132.312 1.00 39.17 ? 618  ARG A CG    1 
ATOM   4449  C  CD    . ARG A 1  620  ? -12.539 88.869  133.301 1.00 44.79 ? 618  ARG A CD    1 
ATOM   4450  N  NE    . ARG A 1  620  ? -13.085 90.107  132.758 1.00 47.77 ? 618  ARG A NE    1 
ATOM   4451  C  CZ    . ARG A 1  620  ? -14.186 90.700  133.196 1.00 44.22 ? 618  ARG A CZ    1 
ATOM   4452  N  NH1   . ARG A 1  620  ? -14.858 90.232  134.238 1.00 47.45 ? 618  ARG A NH1   1 
ATOM   4453  N  NH2   . ARG A 1  620  ? -14.618 91.797  132.582 1.00 50.65 ? 618  ARG A NH2   1 
ATOM   4454  N  N     . LEU A 1  621  ? -15.837 84.354  132.353 1.00 30.50 ? 619  LEU A N     1 
ATOM   4455  C  CA    . LEU A 1  621  ? -16.674 83.288  132.889 1.00 31.50 ? 619  LEU A CA    1 
ATOM   4456  C  C     . LEU A 1  621  ? -16.399 81.966  132.186 1.00 31.02 ? 619  LEU A C     1 
ATOM   4457  O  O     . LEU A 1  621  ? -16.400 80.906  132.825 1.00 34.18 ? 619  LEU A O     1 
ATOM   4458  C  CB    . LEU A 1  621  ? -18.146 83.668  132.761 1.00 28.92 ? 619  LEU A CB    1 
ATOM   4459  C  CG    . LEU A 1  621  ? -18.563 84.945  133.493 1.00 32.52 ? 619  LEU A CG    1 
ATOM   4460  C  CD1   . LEU A 1  621  ? -19.956 85.367  133.043 1.00 32.44 ? 619  LEU A CD1   1 
ATOM   4461  C  CD2   . LEU A 1  621  ? -18.508 84.737  134.995 1.00 35.38 ? 619  LEU A CD2   1 
ATOM   4462  N  N     . ALA A 1  622  ? -16.163 82.008  130.869 1.00 30.34 ? 620  ALA A N     1 
ATOM   4463  C  CA    . ALA A 1  622  ? -15.757 80.803  130.148 1.00 29.88 ? 620  ALA A CA    1 
ATOM   4464  C  C     . ALA A 1  622  ? -14.439 80.257  130.685 1.00 29.63 ? 620  ALA A C     1 
ATOM   4465  O  O     . ALA A 1  622  ? -14.303 79.049  130.903 1.00 30.77 ? 620  ALA A O     1 
ATOM   4466  C  CB    . ALA A 1  622  ? -15.647 81.093  128.650 1.00 26.98 ? 620  ALA A CB    1 
ATOM   4467  N  N     . ALA A 1  623  ? -13.461 81.136  130.913 1.00 27.95 ? 621  ALA A N     1 
ATOM   4468  C  CA    . ALA A 1  623  ? -12.182 80.693  131.459 1.00 31.86 ? 621  ALA A CA    1 
ATOM   4469  C  C     . ALA A 1  623  ? -12.360 80.063  132.833 1.00 32.44 ? 621  ALA A C     1 
ATOM   4470  O  O     . ALA A 1  623  ? -11.759 79.021  133.129 1.00 31.94 ? 621  ALA A O     1 
ATOM   4471  C  CB    . ALA A 1  623  ? -11.209 81.866  131.530 1.00 32.30 ? 621  ALA A CB    1 
ATOM   4472  N  N     . ASP A 1  624  ? -13.193 80.674  133.681 1.00 33.49 ? 622  ASP A N     1 
ATOM   4473  C  CA    . ASP A 1  624  ? -13.450 80.115  135.007 1.00 37.51 ? 622  ASP A CA    1 
ATOM   4474  C  C     . ASP A 1  624  ? -14.126 78.753  134.913 1.00 35.41 ? 622  ASP A C     1 
ATOM   4475  O  O     . ASP A 1  624  ? -13.843 77.853  135.713 1.00 36.96 ? 622  ASP A O     1 
ATOM   4476  C  CB    . ASP A 1  624  ? -14.319 81.071  135.829 1.00 40.03 ? 622  ASP A CB    1 
ATOM   4477  C  CG    . ASP A 1  624  ? -13.659 82.420  136.052 1.00 43.95 ? 622  ASP A CG    1 
ATOM   4478  O  OD1   . ASP A 1  624  ? -12.408 82.486  136.078 1.00 44.70 ? 622  ASP A OD1   1 
ATOM   4479  O  OD2   . ASP A 1  624  ? -14.404 83.416  136.204 1.00 48.20 ? 622  ASP A OD2   1 
ATOM   4480  N  N     . ALA A 1  625  ? -15.021 78.582  133.942 1.00 34.74 ? 623  ALA A N     1 
ATOM   4481  C  CA    . ALA A 1  625  ? -15.772 77.347  133.782 1.00 35.79 ? 623  ALA A CA    1 
ATOM   4482  C  C     . ALA A 1  625  ? -15.055 76.296  132.949 1.00 36.24 ? 623  ALA A C     1 
ATOM   4483  O  O     . ALA A 1  625  ? -15.556 75.172  132.845 1.00 39.06 ? 623  ALA A O     1 
ATOM   4484  C  CB    . ALA A 1  625  ? -17.127 77.641  133.134 1.00 37.56 ? 623  ALA A CB    1 
ATOM   4485  N  N     . ALA A 1  626  ? -13.916 76.627  132.342 1.00 35.04 ? 624  ALA A N     1 
ATOM   4486  C  CA    . ALA A 1  626  ? -13.273 75.683  131.433 1.00 32.71 ? 624  ALA A CA    1 
ATOM   4487  C  C     . ALA A 1  626  ? -12.903 74.355  132.087 1.00 35.85 ? 624  ALA A C     1 
ATOM   4488  O  O     . ALA A 1  626  ? -13.124 73.310  131.451 1.00 33.37 ? 624  ALA A O     1 
ATOM   4489  C  CB    . ALA A 1  626  ? -12.040 76.333  130.795 1.00 32.30 ? 624  ALA A CB    1 
ATOM   4490  N  N     . PRO A 1  627  ? -12.341 74.304  133.304 1.00 35.80 ? 625  PRO A N     1 
ATOM   4491  C  CA    . PRO A 1  627  ? -12.052 72.986  133.897 1.00 34.62 ? 625  PRO A CA    1 
ATOM   4492  C  C     . PRO A 1  627  ? -13.282 72.106  134.046 1.00 35.07 ? 625  PRO A C     1 
ATOM   4493  O  O     . PRO A 1  627  ? -13.214 70.899  133.779 1.00 35.20 ? 625  PRO A O     1 
ATOM   4494  C  CB    . PRO A 1  627  ? -11.448 73.348  135.263 1.00 38.23 ? 625  PRO A CB    1 
ATOM   4495  C  CG    . PRO A 1  627  ? -10.868 74.707  135.063 1.00 35.62 ? 625  PRO A CG    1 
ATOM   4496  C  CD    . PRO A 1  627  ? -11.840 75.401  134.156 1.00 37.26 ? 625  PRO A CD    1 
ATOM   4497  N  N     . ASP A 1  628  ? -14.410 72.682  134.465 1.00 34.09 ? 626  ASP A N     1 
ATOM   4498  C  CA    . ASP A 1  628  ? -15.606 71.883  134.701 1.00 33.42 ? 626  ASP A CA    1 
ATOM   4499  C  C     . ASP A 1  628  ? -16.122 71.263  133.409 1.00 36.72 ? 626  ASP A C     1 
ATOM   4500  O  O     . ASP A 1  628  ? -16.629 70.136  133.414 1.00 36.74 ? 626  ASP A O     1 
ATOM   4501  C  CB    . ASP A 1  628  ? -16.693 72.742  135.354 1.00 34.34 ? 626  ASP A CB    1 
ATOM   4502  C  CG    . ASP A 1  628  ? -16.346 73.136  136.784 1.00 40.78 ? 626  ASP A CG    1 
ATOM   4503  O  OD1   . ASP A 1  628  ? -15.207 72.879  137.220 1.00 45.76 ? 626  ASP A OD1   1 
ATOM   4504  O  OD2   . ASP A 1  628  ? -17.218 73.693  137.475 1.00 42.83 ? 626  ASP A OD2   1 
ATOM   4505  N  N     . TRP A 1  629  ? -16.008 71.982  132.294 1.00 31.37 ? 627  TRP A N     1 
ATOM   4506  C  CA    . TRP A 1  629  ? -16.499 71.432  131.039 1.00 32.13 ? 627  TRP A CA    1 
ATOM   4507  C  C     . TRP A 1  629  ? -15.521 70.417  130.459 1.00 31.12 ? 627  TRP A C     1 
ATOM   4508  O  O     . TRP A 1  629  ? -15.942 69.399  129.895 1.00 30.83 ? 627  TRP A O     1 
ATOM   4509  C  CB    . TRP A 1  629  ? -16.777 72.558  130.041 1.00 29.69 ? 627  TRP A CB    1 
ATOM   4510  C  CG    . TRP A 1  629  ? -17.247 72.045  128.722 1.00 26.57 ? 627  TRP A CG    1 
ATOM   4511  C  CD1   . TRP A 1  629  ? -16.634 72.207  127.504 1.00 25.14 ? 627  TRP A CD1   1 
ATOM   4512  C  CD2   . TRP A 1  629  ? -18.398 71.232  128.487 1.00 25.87 ? 627  TRP A CD2   1 
ATOM   4513  N  NE1   . TRP A 1  629  ? -17.356 71.568  126.525 1.00 23.49 ? 627  TRP A NE1   1 
ATOM   4514  C  CE2   . TRP A 1  629  ? -18.446 70.965  127.098 1.00 23.57 ? 627  TRP A CE2   1 
ATOM   4515  C  CE3   . TRP A 1  629  ? -19.410 70.721  129.308 1.00 28.19 ? 627  TRP A CE3   1 
ATOM   4516  C  CZ2   . TRP A 1  629  ? -19.450 70.203  126.519 1.00 24.08 ? 627  TRP A CZ2   1 
ATOM   4517  C  CZ3   . TRP A 1  629  ? -20.412 69.963  128.727 1.00 28.87 ? 627  TRP A CZ3   1 
ATOM   4518  C  CH2   . TRP A 1  629  ? -20.425 69.715  127.345 1.00 26.88 ? 627  TRP A CH2   1 
ATOM   4519  N  N     . ALA A 1  630  ? -14.215 70.673  130.590 1.00 29.01 ? 628  ALA A N     1 
ATOM   4520  C  CA    . ALA A 1  630  ? -13.218 69.707  130.133 1.00 31.70 ? 628  ALA A CA    1 
ATOM   4521  C  C     . ALA A 1  630  ? -13.340 68.380  130.869 1.00 33.28 ? 628  ALA A C     1 
ATOM   4522  O  O     . ALA A 1  630  ? -12.991 67.325  130.318 1.00 29.61 ? 628  ALA A O     1 
ATOM   4523  C  CB    . ALA A 1  630  ? -11.807 70.275  130.308 1.00 31.86 ? 628  ALA A CB    1 
ATOM   4524  N  N     . ALA A 1  631  ? -13.821 68.411  132.113 1.00 30.65 ? 629  ALA A N     1 
ATOM   4525  C  CA    . ALA A 1  631  ? -13.941 67.200  132.911 1.00 32.02 ? 629  ALA A CA    1 
ATOM   4526  C  C     . ALA A 1  631  ? -15.156 66.366  132.534 1.00 33.73 ? 629  ALA A C     1 
ATOM   4527  O  O     . ALA A 1  631  ? -15.237 65.204  132.943 1.00 33.60 ? 629  ALA A O     1 
ATOM   4528  C  CB    . ALA A 1  631  ? -13.982 67.550  134.401 1.00 34.18 ? 629  ALA A CB    1 
ATOM   4529  N  N     . VAL A 1  632  ? -16.092 66.916  131.766 1.00 30.56 ? 630  VAL A N     1 
ATOM   4530  C  CA    . VAL A 1  632  ? -17.183 66.107  131.229 1.00 29.12 ? 630  VAL A CA    1 
ATOM   4531  C  C     . VAL A 1  632  ? -16.550 65.170  130.208 1.00 28.64 ? 630  VAL A C     1 
ATOM   4532  O  O     . VAL A 1  632  ? -15.915 65.646  129.258 1.00 28.94 ? 630  VAL A O     1 
ATOM   4533  C  CB    . VAL A 1  632  ? -18.295 66.972  130.612 1.00 29.23 ? 630  VAL A CB    1 
ATOM   4534  C  CG1   . VAL A 1  632  ? -19.361 66.094  129.974 1.00 29.74 ? 630  VAL A CG1   1 
ATOM   4535  C  CG2   . VAL A 1  632  ? -18.908 67.874  131.692 1.00 30.38 ? 630  VAL A CG2   1 
ATOM   4536  N  N     . PRO A 1  633  ? -16.662 63.854  130.386 1.00 29.10 ? 631  PRO A N     1 
ATOM   4537  C  CA    . PRO A 1  633  ? -15.957 62.932  129.501 1.00 25.97 ? 631  PRO A CA    1 
ATOM   4538  C  C     . PRO A 1  633  ? -16.373 63.149  128.055 1.00 29.10 ? 631  PRO A C     1 
ATOM   4539  O  O     . PRO A 1  633  ? -17.519 63.539  127.775 1.00 27.84 ? 631  PRO A O     1 
ATOM   4540  C  CB    . PRO A 1  633  ? -16.390 61.551  130.008 1.00 27.41 ? 631  PRO A CB    1 
ATOM   4541  C  CG    . PRO A 1  633  ? -16.823 61.782  131.419 1.00 30.42 ? 631  PRO A CG    1 
ATOM   4542  C  CD    . PRO A 1  633  ? -17.420 63.150  131.436 1.00 31.10 ? 631  PRO A CD    1 
ATOM   4543  N  N     . PRO A 1  634  ? -15.460 62.920  127.111 1.00 25.79 ? 632  PRO A N     1 
ATOM   4544  C  CA    . PRO A 1  634  ? -15.797 63.156  125.696 1.00 24.74 ? 632  PRO A CA    1 
ATOM   4545  C  C     . PRO A 1  634  ? -17.059 62.432  125.242 1.00 25.23 ? 632  PRO A C     1 
ATOM   4546  O  O     . PRO A 1  634  ? -17.852 62.989  124.473 1.00 22.99 ? 632  PRO A O     1 
ATOM   4547  C  CB    . PRO A 1  634  ? -14.553 62.644  124.958 1.00 23.63 ? 632  PRO A CB    1 
ATOM   4548  C  CG    . PRO A 1  634  ? -13.447 62.753  125.962 1.00 28.57 ? 632  PRO A CG    1 
ATOM   4549  C  CD    . PRO A 1  634  ? -14.064 62.491  127.302 1.00 26.60 ? 632  PRO A CD    1 
ATOM   4550  N  N     . SER A 1  635  ? -17.264 61.198  125.704 1.00 25.93 ? 633  SER A N     1 
ATOM   4551  C  CA    . SER A 1  635  ? -18.453 60.452  125.310 1.00 27.27 ? 633  SER A CA    1 
ATOM   4552  C  C     . SER A 1  635  ? -19.727 61.176  125.729 1.00 26.77 ? 633  SER A C     1 
ATOM   4553  O  O     . SER A 1  635  ? -20.717 61.186  124.985 1.00 25.35 ? 633  SER A O     1 
ATOM   4554  C  CB    . SER A 1  635  ? -18.406 59.050  125.914 1.00 29.45 ? 633  SER A CB    1 
ATOM   4555  O  OG    . SER A 1  635  ? -18.429 59.112  127.329 1.00 37.95 ? 633  SER A OG    1 
ATOM   4556  N  N     . GLU A 1  636  ? -19.720 61.790  126.914 1.00 26.36 ? 634  GLU A N     1 
ATOM   4557  C  CA    . GLU A 1  636  ? -20.910 62.498  127.376 1.00 28.42 ? 634  GLU A CA    1 
ATOM   4558  C  C     . GLU A 1  636  ? -21.065 63.844  126.680 1.00 28.42 ? 634  GLU A C     1 
ATOM   4559  O  O     . GLU A 1  636  ? -22.195 64.269  126.409 1.00 27.82 ? 634  GLU A O     1 
ATOM   4560  C  CB    . GLU A 1  636  ? -20.881 62.666  128.902 1.00 30.86 ? 634  GLU A CB    1 
ATOM   4561  C  CG    . GLU A 1  636  ? -22.070 63.436  129.466 1.00 34.28 ? 634  GLU A CG    1 
ATOM   4562  C  CD    . GLU A 1  636  ? -23.428 62.874  129.018 1.00 41.84 ? 634  GLU A CD    1 
ATOM   4563  O  OE1   . GLU A 1  636  ? -23.557 61.634  128.882 1.00 40.86 ? 634  GLU A OE1   1 
ATOM   4564  O  OE2   . GLU A 1  636  ? -24.365 63.675  128.788 1.00 37.39 ? 634  GLU A OE2   1 
ATOM   4565  N  N     . ARG A 1  637  ? -19.958 64.514  126.355 1.00 26.98 ? 635  ARG A N     1 
ATOM   4566  C  CA    . ARG A 1  637  ? -20.057 65.695  125.505 1.00 24.09 ? 635  ARG A CA    1 
ATOM   4567  C  C     . ARG A 1  637  ? -20.660 65.338  124.155 1.00 23.93 ? 635  ARG A C     1 
ATOM   4568  O  O     . ARG A 1  637  ? -21.539 66.044  123.651 1.00 24.58 ? 635  ARG A O     1 
ATOM   4569  C  CB    . ARG A 1  637  ? -18.681 66.342  125.333 1.00 23.31 ? 635  ARG A CB    1 
ATOM   4570  C  CG    . ARG A 1  637  ? -18.049 66.721  126.677 1.00 25.51 ? 635  ARG A CG    1 
ATOM   4571  C  CD    . ARG A 1  637  ? -16.867 67.676  126.539 1.00 24.16 ? 635  ARG A CD    1 
ATOM   4572  N  NE    . ARG A 1  637  ? -15.816 67.158  125.676 1.00 23.17 ? 635  ARG A NE    1 
ATOM   4573  C  CZ    . ARG A 1  637  ? -14.627 66.732  126.084 1.00 28.77 ? 635  ARG A CZ    1 
ATOM   4574  N  NH1   . ARG A 1  637  ? -14.312 66.679  127.370 1.00 26.79 ? 635  ARG A NH1   1 
ATOM   4575  N  NH2   . ARG A 1  637  ? -13.729 66.360  125.176 1.00 25.83 ? 635  ARG A NH2   1 
ATOM   4576  N  N     . ALA A 1  638  ? -20.202 64.234  123.555 1.00 23.64 ? 636  ALA A N     1 
ATOM   4577  C  CA    . ALA A 1  638  ? -20.792 63.784  122.299 1.00 23.45 ? 636  ALA A CA    1 
ATOM   4578  C  C     . ALA A 1  638  ? -22.262 63.424  122.469 1.00 25.88 ? 636  ALA A C     1 
ATOM   4579  O  O     . ALA A 1  638  ? -23.055 63.622  121.541 1.00 22.88 ? 636  ALA A O     1 
ATOM   4580  C  CB    . ALA A 1  638  ? -20.012 62.589  121.751 1.00 21.69 ? 636  ALA A CB    1 
ATOM   4581  N  N     . ALA A 1  639  ? -22.646 62.906  123.642 1.00 24.61 ? 637  ALA A N     1 
ATOM   4582  C  CA    . ALA A 1  639  ? -24.057 62.614  123.887 1.00 25.37 ? 637  ALA A CA    1 
ATOM   4583  C  C     . ALA A 1  639  ? -24.894 63.887  123.863 1.00 24.78 ? 637  ALA A C     1 
ATOM   4584  O  O     . ALA A 1  639  ? -26.032 63.876  123.383 1.00 24.42 ? 637  ALA A O     1 
ATOM   4585  C  CB    . ALA A 1  639  ? -24.230 61.876  125.216 1.00 25.99 ? 637  ALA A CB    1 
ATOM   4586  N  N     . CYS A 1  640  ? -24.351 64.998  124.376 1.00 25.91 ? 638  CYS A N     1 
ATOM   4587  C  CA    . CYS A 1  640  ? -25.070 66.265  124.274 1.00 24.15 ? 638  CYS A CA    1 
ATOM   4588  C  C     . CYS A 1  640  ? -25.294 66.647  122.819 1.00 24.44 ? 638  CYS A C     1 
ATOM   4589  O  O     . CYS A 1  640  ? -26.388 67.088  122.446 1.00 24.85 ? 638  CYS A O     1 
ATOM   4590  C  CB    . CYS A 1  640  ? -24.313 67.382  124.981 1.00 24.50 ? 638  CYS A CB    1 
ATOM   4591  S  SG    . CYS A 1  640  ? -24.128 67.175  126.744 1.00 27.32 ? 638  CYS A SG    1 
ATOM   4592  N  N     . LEU A 1  641  ? -24.259 66.502  121.985 1.00 23.22 ? 639  LEU A N     1 
ATOM   4593  C  CA    . LEU A 1  641  ? -24.408 66.814  120.569 1.00 21.43 ? 639  LEU A CA    1 
ATOM   4594  C  C     . LEU A 1  641  ? -25.475 65.944  119.928 1.00 21.42 ? 639  LEU A C     1 
ATOM   4595  O  O     . LEU A 1  641  ? -26.302 66.434  119.149 1.00 22.98 ? 639  LEU A O     1 
ATOM   4596  C  CB    . LEU A 1  641  ? -23.073 66.632  119.843 1.00 21.08 ? 639  LEU A CB    1 
ATOM   4597  C  CG    . LEU A 1  641  ? -22.175 67.866  119.766 1.00 21.87 ? 639  LEU A CG    1 
ATOM   4598  C  CD1   . LEU A 1  641  ? -21.756 68.365  121.142 1.00 23.66 ? 639  LEU A CD1   1 
ATOM   4599  C  CD2   . LEU A 1  641  ? -20.955 67.558  118.917 1.00 19.59 ? 639  LEU A CD2   1 
ATOM   4600  N  N     . ASP A 1  642  ? -25.471 64.645  120.232 1.00 23.25 ? 640  ASP A N     1 
ATOM   4601  C  CA    . ASP A 1  642  ? -26.471 63.763  119.638 1.00 22.74 ? 640  ASP A CA    1 
ATOM   4602  C  C     . ASP A 1  642  ? -27.877 64.132  120.104 1.00 22.30 ? 640  ASP A C     1 
ATOM   4603  O  O     . ASP A 1  642  ? -28.831 64.061  119.324 1.00 22.08 ? 640  ASP A O     1 
ATOM   4604  C  CB    . ASP A 1  642  ? -26.162 62.301  119.969 1.00 22.83 ? 640  ASP A CB    1 
ATOM   4605  C  CG    . ASP A 1  642  ? -25.049 61.732  119.102 1.00 23.66 ? 640  ASP A CG    1 
ATOM   4606  O  OD1   . ASP A 1  642  ? -24.797 62.290  118.015 1.00 22.96 ? 640  ASP A OD1   1 
ATOM   4607  O  OD2   . ASP A 1  642  ? -24.451 60.718  119.502 1.00 23.12 ? 640  ASP A OD2   1 
ATOM   4608  N  N     . ARG A 1  643  ? -28.021 64.533  121.367 1.00 25.49 ? 641  ARG A N     1 
ATOM   4609  C  CA    . ARG A 1  643  ? -29.334 64.961  121.846 1.00 24.15 ? 641  ARG A CA    1 
ATOM   4610  C  C     . ARG A 1  643  ? -29.771 66.246  121.158 1.00 23.63 ? 641  ARG A C     1 
ATOM   4611  O  O     . ARG A 1  643  ? -30.948 66.404  120.814 1.00 25.64 ? 641  ARG A O     1 
ATOM   4612  C  CB    . ARG A 1  643  ? -29.320 65.142  123.364 1.00 25.20 ? 641  ARG A CB    1 
ATOM   4613  C  CG    . ARG A 1  643  ? -29.389 63.836  124.141 1.00 24.46 ? 641  ARG A CG    1 
ATOM   4614  C  CD    . ARG A 1  643  ? -29.598 64.100  125.625 1.00 28.47 ? 641  ARG A CD    1 
ATOM   4615  N  NE    . ARG A 1  643  ? -28.476 64.790  126.249 1.00 29.04 ? 641  ARG A NE    1 
ATOM   4616  C  CZ    . ARG A 1  643  ? -27.469 64.174  126.853 1.00 26.99 ? 641  ARG A CZ    1 
ATOM   4617  N  NH1   . ARG A 1  643  ? -27.398 62.855  126.899 1.00 28.18 ? 641  ARG A NH1   1 
ATOM   4618  N  NH2   . ARG A 1  643  ? -26.514 64.899  127.430 1.00 30.34 ? 641  ARG A NH2   1 
ATOM   4619  N  N     . ALA A 1  644  ? -28.835 67.171  120.932 1.00 23.19 ? 642  ALA A N     1 
ATOM   4620  C  CA    . ALA A 1  644  ? -29.182 68.389  120.207 1.00 22.26 ? 642  ALA A CA    1 
ATOM   4621  C  C     . ALA A 1  644  ? -29.614 68.072  118.781 1.00 22.89 ? 642  ALA A C     1 
ATOM   4622  O  O     . ALA A 1  644  ? -30.532 68.706  118.248 1.00 21.32 ? 642  ALA A O     1 
ATOM   4623  C  CB    . ALA A 1  644  ? -28.005 69.360  120.208 1.00 22.95 ? 642  ALA A CB    1 
ATOM   4624  N  N     . ALA A 1  645  ? -28.977 67.078  118.156 1.00 22.48 ? 643  ALA A N     1 
ATOM   4625  C  CA    . ALA A 1  645  ? -29.374 66.679  116.808 1.00 20.30 ? 643  ALA A CA    1 
ATOM   4626  C  C     . ALA A 1  645  ? -30.800 66.131  116.786 1.00 21.72 ? 643  ALA A C     1 
ATOM   4627  O  O     . ALA A 1  645  ? -31.568 66.422  115.861 1.00 22.00 ? 643  ALA A O     1 
ATOM   4628  C  CB    . ALA A 1  645  ? -28.392 65.642  116.259 1.00 21.22 ? 643  ALA A CB    1 
ATOM   4629  N  N     . GLU A 1  646  ? -31.156 65.302  117.771 1.00 23.63 ? 644  GLU A N     1 
ATOM   4630  C  CA    . GLU A 1  646  ? -32.527 64.804  117.854 1.00 24.68 ? 644  GLU A CA    1 
ATOM   4631  C  C     . GLU A 1  646  ? -33.508 65.948  118.026 1.00 25.82 ? 644  GLU A C     1 
ATOM   4632  O  O     . GLU A 1  646  ? -34.589 65.949  117.421 1.00 25.00 ? 644  GLU A O     1 
ATOM   4633  C  CB    . GLU A 1  646  ? -32.678 63.834  119.022 1.00 26.82 ? 644  GLU A CB    1 
ATOM   4634  C  CG    . GLU A 1  646  ? -31.980 62.525  118.860 1.00 29.42 ? 644  GLU A CG    1 
ATOM   4635  C  CD    . GLU A 1  646  ? -32.412 61.791  117.617 1.00 35.43 ? 644  GLU A CD    1 
ATOM   4636  O  OE1   . GLU A 1  646  ? -33.631 61.736  117.351 1.00 39.60 ? 644  GLU A OE1   1 
ATOM   4637  O  OE2   . GLU A 1  646  ? -31.524 61.279  116.902 1.00 34.74 ? 644  GLU A OE2   1 
ATOM   4638  N  N     . LEU A 1  647  ? -33.159 66.916  118.877 1.00 25.41 ? 645  LEU A N     1 
ATOM   4639  C  CA    . LEU A 1  647  ? -34.036 68.059  119.102 1.00 24.20 ? 645  LEU A CA    1 
ATOM   4640  C  C     . LEU A 1  647  ? -34.204 68.869  117.824 1.00 26.84 ? 645  LEU A C     1 
ATOM   4641  O  O     . LEU A 1  647  ? -35.324 69.262  117.476 1.00 25.91 ? 645  LEU A O     1 
ATOM   4642  C  CB    . LEU A 1  647  ? -33.486 68.933  120.229 1.00 23.88 ? 645  LEU A CB    1 
ATOM   4643  C  CG    . LEU A 1  647  ? -33.579 68.387  121.656 1.00 25.96 ? 645  LEU A CG    1 
ATOM   4644  C  CD1   . LEU A 1  647  ? -32.786 69.253  122.632 1.00 24.35 ? 645  LEU A CD1   1 
ATOM   4645  C  CD2   . LEU A 1  647  ? -35.039 68.276  122.113 1.00 27.96 ? 645  LEU A CD2   1 
ATOM   4646  N  N     . MET A 1  648  ? -33.107 69.110  117.093 1.00 22.62 ? 646  MET A N     1 
ATOM   4647  C  CA    . MET A 1  648  ? -33.227 69.886  115.864 1.00 23.36 ? 646  MET A CA    1 
ATOM   4648  C  C     . MET A 1  648  ? -34.025 69.133  114.816 1.00 22.23 ? 646  MET A C     1 
ATOM   4649  O  O     . MET A 1  648  ? -34.798 69.741  114.067 1.00 23.54 ? 646  MET A O     1 
ATOM   4650  C  CB    . MET A 1  648  ? -31.851 70.251  115.309 1.00 20.71 ? 646  MET A CB    1 
ATOM   4651  C  CG    . MET A 1  648  ? -31.171 71.374  116.068 1.00 23.92 ? 646  MET A CG    1 
ATOM   4652  S  SD    . MET A 1  648  ? -29.750 72.006  115.148 1.00 24.87 ? 646  MET A SD    1 
ATOM   4653  C  CE    . MET A 1  648  ? -29.037 73.101  116.368 1.00 25.71 ? 646  MET A CE    1 
ATOM   4654  N  N     . GLN A 1  649  ? -33.837 67.813  114.727 1.00 23.32 ? 647  GLN A N     1 
ATOM   4655  C  CA    . GLN A 1  649  ? -34.628 67.036  113.781 1.00 21.33 ? 647  GLN A CA    1 
ATOM   4656  C  C     . GLN A 1  649  ? -36.112 67.159  114.089 1.00 23.48 ? 647  GLN A C     1 
ATOM   4657  O  O     . GLN A 1  649  ? -36.925 67.370  113.185 1.00 23.99 ? 647  GLN A O     1 
ATOM   4658  C  CB    . GLN A 1  649  ? -34.208 65.571  113.814 1.00 23.25 ? 647  GLN A CB    1 
ATOM   4659  C  CG    . GLN A 1  649  ? -34.894 64.732  112.747 1.00 23.19 ? 647  GLN A CG    1 
ATOM   4660  C  CD    . GLN A 1  649  ? -34.344 65.006  111.351 1.00 22.57 ? 647  GLN A CD    1 
ATOM   4661  O  OE1   . GLN A 1  649  ? -33.223 64.620  111.032 1.00 22.76 ? 647  GLN A OE1   1 
ATOM   4662  N  NE2   . GLN A 1  649  ? -35.136 65.677  110.515 1.00 24.42 ? 647  GLN A NE2   1 
ATOM   4663  N  N     . ALA A 1  650  ? -36.474 67.044  115.365 1.00 25.83 ? 648  ALA A N     1 
ATOM   4664  C  CA    . ALA A 1  650  ? -37.881 67.113  115.751 1.00 25.07 ? 648  ALA A CA    1 
ATOM   4665  C  C     . ALA A 1  650  ? -38.459 68.498  115.521 1.00 28.37 ? 648  ALA A C     1 
ATOM   4666  O  O     . ALA A 1  650  ? -39.651 68.630  115.208 1.00 27.18 ? 648  ALA A O     1 
ATOM   4667  C  CB    . ALA A 1  650  ? -38.037 66.727  117.219 1.00 27.35 ? 648  ALA A CB    1 
ATOM   4668  N  N     . ARG A 1  651  ? -37.638 69.531  115.676 1.00 24.51 ? 649  ARG A N     1 
ATOM   4669  C  CA    . ARG A 1  651  ? -38.070 70.912  115.566 1.00 27.02 ? 649  ARG A CA    1 
ATOM   4670  C  C     . ARG A 1  651  ? -37.868 71.482  114.166 1.00 23.13 ? 649  ARG A C     1 
ATOM   4671  O  O     . ARG A 1  651  ? -38.100 72.676  113.959 1.00 24.10 ? 649  ARG A O     1 
ATOM   4672  C  CB    . ARG A 1  651  ? -37.327 71.765  116.598 1.00 25.96 ? 649  ARG A CB    1 
ATOM   4673  C  CG    . ARG A 1  651  ? -38.031 73.062  116.969 1.00 30.78 ? 649  ARG A CG    1 
ATOM   4674  C  CD    . ARG A 1  651  ? -37.686 73.518  118.387 1.00 32.56 ? 649  ARG A CD    1 
ATOM   4675  N  NE    . ARG A 1  651  ? -38.075 74.903  118.627 1.00 34.33 ? 649  ARG A NE    1 
ATOM   4676  C  CZ    . ARG A 1  651  ? -39.316 75.306  118.861 1.00 35.38 ? 649  ARG A CZ    1 
ATOM   4677  N  NH1   . ARG A 1  651  ? -40.338 74.466  118.810 1.00 38.30 ? 649  ARG A NH1   1 
ATOM   4678  N  NH2   . ARG A 1  651  ? -39.540 76.588  119.143 1.00 38.12 ? 649  ARG A NH2   1 
ATOM   4679  N  N     . MET A 1  652  ? -37.440 70.660  113.208 1.00 24.14 ? 650  MET A N     1 
ATOM   4680  C  CA    . MET A 1  652  ? -37.110 71.174  111.879 1.00 23.42 ? 650  MET A CA    1 
ATOM   4681  C  C     . MET A 1  652  ? -38.193 72.064  111.288 1.00 24.02 ? 650  MET A C     1 
ATOM   4682  O  O     . MET A 1  652  ? -37.852 73.152  110.800 1.00 23.18 ? 650  MET A O     1 
ATOM   4683  C  CB    . MET A 1  652  ? -36.781 70.018  110.923 1.00 22.95 ? 650  MET A CB    1 
ATOM   4684  C  CG    . MET A 1  652  ? -36.611 70.463  109.493 1.00 22.83 ? 650  MET A CG    1 
ATOM   4685  S  SD    . MET A 1  652  ? -36.126 69.119  108.392 1.00 24.73 ? 650  MET A SD    1 
ATOM   4686  C  CE    . MET A 1  652  ? -34.433 68.864  108.906 1.00 21.93 ? 650  MET A CE    1 
ATOM   4687  N  N     . PRO A 1  653  ? -39.486 71.699  111.307 1.00 24.06 ? 651  PRO A N     1 
ATOM   4688  C  CA    . PRO A 1  653  ? -40.484 72.589  110.686 1.00 24.85 ? 651  PRO A CA    1 
ATOM   4689  C  C     . PRO A 1  653  ? -40.456 73.997  111.250 1.00 24.22 ? 651  PRO A C     1 
ATOM   4690  O  O     . PRO A 1  653  ? -40.478 74.971  110.486 1.00 24.01 ? 651  PRO A O     1 
ATOM   4691  C  CB    . PRO A 1  653  ? -41.815 71.882  110.985 1.00 23.05 ? 651  PRO A CB    1 
ATOM   4692  C  CG    . PRO A 1  653  ? -41.444 70.430  111.050 1.00 27.41 ? 651  PRO A CG    1 
ATOM   4693  C  CD    . PRO A 1  653  ? -40.105 70.448  111.785 1.00 25.28 ? 651  PRO A CD    1 
ATOM   4694  N  N     . THR A 1  654  ? -40.387 74.122  112.577 1.00 21.54 ? 652  THR A N     1 
ATOM   4695  C  CA    . THR A 1  654  ? -40.295 75.432  113.208 1.00 23.03 ? 652  THR A CA    1 
ATOM   4696  C  C     . THR A 1  654  ? -38.981 76.125  112.856 1.00 22.90 ? 652  THR A C     1 
ATOM   4697  O  O     . THR A 1  654  ? -38.971 77.325  112.556 1.00 24.62 ? 652  THR A O     1 
ATOM   4698  C  CB    . THR A 1  654  ? -40.451 75.282  114.723 1.00 25.39 ? 652  THR A CB    1 
ATOM   4699  O  OG1   . THR A 1  654  ? -41.719 74.682  115.017 1.00 28.61 ? 652  THR A OG1   1 
ATOM   4700  C  CG2   . THR A 1  654  ? -40.359 76.631  115.424 1.00 27.44 ? 652  THR A CG2   1 
ATOM   4701  N  N     . LEU A 1  655  ? -37.863 75.393  112.892 1.00 22.63 ? 653  LEU A N     1 
ATOM   4702  C  CA    . LEU A 1  655  ? -36.589 75.975  112.471 1.00 22.07 ? 653  LEU A CA    1 
ATOM   4703  C  C     . LEU A 1  655  ? -36.645 76.461  111.025 1.00 25.23 ? 653  LEU A C     1 
ATOM   4704  O  O     . LEU A 1  655  ? -36.123 77.538  110.710 1.00 23.31 ? 653  LEU A O     1 
ATOM   4705  C  CB    . LEU A 1  655  ? -35.461 74.961  112.654 1.00 22.82 ? 653  LEU A CB    1 
ATOM   4706  C  CG    . LEU A 1  655  ? -35.293 74.476  114.090 1.00 21.98 ? 653  LEU A CG    1 
ATOM   4707  C  CD1   . LEU A 1  655  ? -34.130 73.485  114.197 1.00 24.28 ? 653  LEU A CD1   1 
ATOM   4708  C  CD2   . LEU A 1  655  ? -35.079 75.647  115.030 1.00 27.86 ? 653  LEU A CD2   1 
ATOM   4709  N  N     . LEU A 1  656  ? -37.268 75.685  110.129 1.00 23.05 ? 654  LEU A N     1 
ATOM   4710  C  CA    . LEU A 1  656  ? -37.422 76.134  108.744 1.00 23.57 ? 654  LEU A CA    1 
ATOM   4711  C  C     . LEU A 1  656  ? -38.089 77.500  108.682 1.00 24.10 ? 654  LEU A C     1 
ATOM   4712  O  O     . LEU A 1  656  ? -37.635 78.402  107.964 1.00 23.09 ? 654  LEU A O     1 
ATOM   4713  C  CB    . LEU A 1  656  ? -38.260 75.143  107.925 1.00 23.36 ? 654  LEU A CB    1 
ATOM   4714  C  CG    . LEU A 1  656  ? -37.818 73.696  107.783 1.00 23.59 ? 654  LEU A CG    1 
ATOM   4715  C  CD1   . LEU A 1  656  ? -38.705 73.003  106.788 1.00 24.21 ? 654  LEU A CD1   1 
ATOM   4716  C  CD2   . LEU A 1  656  ? -36.374 73.651  107.344 1.00 21.55 ? 654  LEU A CD2   1 
ATOM   4717  N  N     . GLY A 1  657  ? -39.195 77.652  109.409 1.00 22.89 ? 655  GLY A N     1 
ATOM   4718  C  CA    . GLY A 1  657  ? -39.928 78.905  109.364 1.00 25.62 ? 655  GLY A CA    1 
ATOM   4719  C  C     . GLY A 1  657  ? -39.087 80.086  109.799 1.00 24.67 ? 655  GLY A C     1 
ATOM   4720  O  O     . GLY A 1  657  ? -39.156 81.162  109.200 1.00 25.04 ? 655  GLY A O     1 
ATOM   4721  N  N     . LEU A 1  658  ? -38.275 79.900  110.845 1.00 22.60 ? 656  LEU A N     1 
ATOM   4722  C  CA    . LEU A 1  658  ? -37.418 80.983  111.308 1.00 24.69 ? 656  LEU A CA    1 
ATOM   4723  C  C     . LEU A 1  658  ? -36.368 81.324  110.261 1.00 22.72 ? 656  LEU A C     1 
ATOM   4724  O  O     . LEU A 1  658  ? -36.188 82.494  109.904 1.00 22.87 ? 656  LEU A O     1 
ATOM   4725  C  CB    . LEU A 1  658  ? -36.750 80.601  112.630 1.00 23.01 ? 656  LEU A CB    1 
ATOM   4726  C  CG    . LEU A 1  658  ? -35.930 81.710  113.287 1.00 25.01 ? 656  LEU A CG    1 
ATOM   4727  C  CD1   . LEU A 1  658  ? -36.739 83.004  113.349 1.00 24.74 ? 656  LEU A CD1   1 
ATOM   4728  C  CD2   . LEU A 1  658  ? -35.537 81.263  114.663 1.00 23.45 ? 656  LEU A CD2   1 
ATOM   4729  N  N     . ILE A 1  659  ? -35.670 80.305  109.754 1.00 22.07 ? 657  ILE A N     1 
ATOM   4730  C  CA    . ILE A 1  659  ? -34.611 80.530  108.778 1.00 19.80 ? 657  ILE A CA    1 
ATOM   4731  C  C     . ILE A 1  659  ? -35.175 81.180  107.521 1.00 23.09 ? 657  ILE A C     1 
ATOM   4732  O  O     . ILE A 1  659  ? -34.573 82.107  106.960 1.00 21.36 ? 657  ILE A O     1 
ATOM   4733  C  CB    . ILE A 1  659  ? -33.906 79.197  108.464 1.00 21.84 ? 657  ILE A CB    1 
ATOM   4734  C  CG1   . ILE A 1  659  ? -33.164 78.702  109.709 1.00 23.73 ? 657  ILE A CG1   1 
ATOM   4735  C  CG2   . ILE A 1  659  ? -32.970 79.352  107.294 1.00 22.83 ? 657  ILE A CG2   1 
ATOM   4736  C  CD1   . ILE A 1  659  ? -32.685 77.292  109.610 1.00 22.21 ? 657  ILE A CD1   1 
ATOM   4737  N  N     . ILE A 1  660  ? -36.348 80.716  107.073 1.00 22.85 ? 658  ILE A N     1 
ATOM   4738  C  CA    . ILE A 1  660  ? -36.986 81.291  105.888 1.00 22.01 ? 658  ILE A CA    1 
ATOM   4739  C  C     . ILE A 1  660  ? -37.177 82.792  106.067 1.00 22.26 ? 658  ILE A C     1 
ATOM   4740  O  O     . ILE A 1  660  ? -36.837 83.589  105.185 1.00 22.74 ? 658  ILE A O     1 
ATOM   4741  C  CB    . ILE A 1  660  ? -38.324 80.583  105.596 1.00 22.62 ? 658  ILE A CB    1 
ATOM   4742  C  CG1   . ILE A 1  660  ? -38.079 79.197  104.993 1.00 22.94 ? 658  ILE A CG1   1 
ATOM   4743  C  CG2   . ILE A 1  660  ? -39.171 81.407  104.650 1.00 22.46 ? 658  ILE A CG2   1 
ATOM   4744  C  CD1   . ILE A 1  660  ? -39.343 78.345  104.919 1.00 26.78 ? 658  ILE A CD1   1 
ATOM   4745  N  N     . ARG A 1  661  ? -37.711 83.202  107.220 1.00 23.31 ? 659  ARG A N     1 
ATOM   4746  C  CA    . ARG A 1  661  ? -38.054 84.606  107.416 1.00 24.80 ? 659  ARG A CA    1 
ATOM   4747  C  C     . ARG A 1  661  ? -36.863 85.449  107.862 1.00 27.52 ? 659  ARG A C     1 
ATOM   4748  O  O     . ARG A 1  661  ? -36.785 86.630  107.497 1.00 25.86 ? 659  ARG A O     1 
ATOM   4749  C  CB    . ARG A 1  661  ? -39.202 84.729  108.421 1.00 26.66 ? 659  ARG A CB    1 
ATOM   4750  C  CG    . ARG A 1  661  ? -40.553 84.376  107.799 1.00 25.19 ? 659  ARG A CG    1 
ATOM   4751  C  CD    . ARG A 1  661  ? -41.681 84.335  108.813 1.00 26.64 ? 659  ARG A CD    1 
ATOM   4752  N  NE    . ARG A 1  661  ? -41.915 85.627  109.443 1.00 27.53 ? 659  ARG A NE    1 
ATOM   4753  C  CZ    . ARG A 1  661  ? -41.867 85.849  110.749 1.00 26.46 ? 659  ARG A CZ    1 
ATOM   4754  N  NH1   . ARG A 1  661  ? -41.577 84.883  111.606 1.00 28.26 ? 659  ARG A NH1   1 
ATOM   4755  N  NH2   . ARG A 1  661  ? -42.141 87.065  111.211 1.00 28.22 ? 659  ARG A NH2   1 
ATOM   4756  N  N     . GLU A 1  662  ? -35.937 84.885  108.645 1.00 22.23 ? 660  GLU A N     1 
ATOM   4757  C  CA    . GLU A 1  662  ? -34.816 85.692  109.118 1.00 24.05 ? 660  GLU A CA    1 
ATOM   4758  C  C     . GLU A 1  662  ? -33.722 85.867  108.065 1.00 22.41 ? 660  GLU A C     1 
ATOM   4759  O  O     . GLU A 1  662  ? -33.105 86.937  107.997 1.00 26.33 ? 660  GLU A O     1 
ATOM   4760  C  CB    . GLU A 1  662  ? -34.212 85.079  110.382 1.00 25.30 ? 660  GLU A CB    1 
ATOM   4761  C  CG    . GLU A 1  662  ? -33.122 85.944  110.991 1.00 25.79 ? 660  GLU A CG    1 
ATOM   4762  C  CD    . GLU A 1  662  ? -32.572 85.390  112.298 1.00 25.11 ? 660  GLU A CD    1 
ATOM   4763  O  OE1   . GLU A 1  662  ? -32.598 84.158  112.498 1.00 23.16 ? 660  GLU A OE1   1 
ATOM   4764  O  OE2   . GLU A 1  662  ? -32.127 86.203  113.127 1.00 24.25 ? 660  GLU A OE2   1 
ATOM   4765  N  N     . ALA A 1  663  ? -33.480 84.858  107.232 1.00 21.02 ? 661  ALA A N     1 
ATOM   4766  C  CA    . ALA A 1  663  ? -32.267 84.808  106.423 1.00 20.51 ? 661  ALA A CA    1 
ATOM   4767  C  C     . ALA A 1  663  ? -32.534 84.750  104.924 1.00 23.22 ? 661  ALA A C     1 
ATOM   4768  O  O     . ALA A 1  663  ? -31.598 84.520  104.151 1.00 25.48 ? 661  ALA A O     1 
ATOM   4769  C  CB    . ALA A 1  663  ? -31.406 83.610  106.843 1.00 23.94 ? 661  ALA A CB    1 
ATOM   4770  N  N     . GLY A 1  664  ? -33.774 84.935  104.486 1.00 25.95 ? 662  GLY A N     1 
ATOM   4771  C  CA    . GLY A 1  664  ? -34.020 84.969  103.053 1.00 23.03 ? 662  GLY A CA    1 
ATOM   4772  C  C     . GLY A 1  664  ? -33.924 83.643  102.348 1.00 23.74 ? 662  GLY A C     1 
ATOM   4773  O  O     . GLY A 1  664  ? -33.672 83.608  101.143 1.00 26.63 ? 662  GLY A O     1 
ATOM   4774  N  N     . LYS A 1  665  ? -34.120 82.545  103.060 1.00 22.10 ? 663  LYS A N     1 
ATOM   4775  C  CA    . LYS A 1  665  ? -33.961 81.223  102.485 1.00 20.76 ? 663  LYS A CA    1 
ATOM   4776  C  C     . LYS A 1  665  ? -35.301 80.691  102.007 1.00 19.76 ? 663  LYS A C     1 
ATOM   4777  O  O     . LYS A 1  665  ? -36.336 80.928  102.636 1.00 18.49 ? 663  LYS A O     1 
ATOM   4778  C  CB    . LYS A 1  665  ? -33.373 80.261  103.512 1.00 22.30 ? 663  LYS A CB    1 
ATOM   4779  C  CG    . LYS A 1  665  ? -32.077 80.738  104.138 1.00 22.45 ? 663  LYS A CG    1 
ATOM   4780  C  CD    . LYS A 1  665  ? -30.967 80.836  103.117 1.00 26.54 ? 663  LYS A CD    1 
ATOM   4781  C  CE    . LYS A 1  665  ? -29.646 81.131  103.803 1.00 24.82 ? 663  LYS A CE    1 
ATOM   4782  N  NZ    . LYS A 1  665  ? -28.627 81.644  102.828 1.00 24.29 ? 663  LYS A NZ    1 
ATOM   4783  N  N     . SER A 1  666  ? -35.268 79.961  100.897 1.00 20.27 ? 664  SER A N     1 
ATOM   4784  C  CA    . SER A 1  666  ? -36.412 79.162  100.488 1.00 23.10 ? 664  SER A CA    1 
ATOM   4785  C  C     . SER A 1  666  ? -36.578 77.967  101.423 1.00 24.17 ? 664  SER A C     1 
ATOM   4786  O  O     . SER A 1  666  ? -35.697 77.646  102.229 1.00 21.78 ? 664  SER A O     1 
ATOM   4787  C  CB    . SER A 1  666  ? -36.230 78.670  99.056  1.00 23.22 ? 664  SER A CB    1 
ATOM   4788  O  OG    . SER A 1  666  ? -35.166 77.734  98.993  1.00 23.74 ? 664  SER A OG    1 
ATOM   4789  N  N     . ALA A 1  667  ? -37.733 77.304  101.316 1.00 23.96 ? 665  ALA A N     1 
ATOM   4790  C  CA    . ALA A 1  667  ? -37.965 76.110  102.122 1.00 20.98 ? 665  ALA A CA    1 
ATOM   4791  C  C     . ALA A 1  667  ? -36.904 75.050  101.851 1.00 22.57 ? 665  ALA A C     1 
ATOM   4792  O  O     . ALA A 1  667  ? -36.367 74.454  102.791 1.00 20.83 ? 665  ALA A O     1 
ATOM   4793  C  CB    . ALA A 1  667  ? -39.358 75.544  101.858 1.00 22.69 ? 665  ALA A CB    1 
ATOM   4794  N  N     . LEU A 1  668  ? -36.587 74.805  100.577 1.00 21.57 ? 666  LEU A N     1 
ATOM   4795  C  CA    . LEU A 1  668  ? -35.543 73.840  100.239 1.00 21.83 ? 666  LEU A CA    1 
ATOM   4796  C  C     . LEU A 1  668  ? -34.217 74.220  100.882 1.00 24.43 ? 666  LEU A C     1 
ATOM   4797  O  O     . LEU A 1  668  ? -33.553 73.371  101.486 1.00 24.08 ? 666  LEU A O     1 
ATOM   4798  C  CB    . LEU A 1  668  ? -35.375 73.724  98.722  1.00 23.90 ? 666  LEU A CB    1 
ATOM   4799  C  CG    . LEU A 1  668  ? -36.418 72.872  98.013  1.00 31.41 ? 666  LEU A CG    1 
ATOM   4800  C  CD1   . LEU A 1  668  ? -36.232 72.988  96.502  1.00 25.82 ? 666  LEU A CD1   1 
ATOM   4801  C  CD2   . LEU A 1  668  ? -36.295 71.428  98.489  1.00 30.59 ? 666  LEU A CD2   1 
ATOM   4802  N  N     . ASN A 1  669  ? -33.809 75.490  100.753 1.00 21.80 ? 667  ASN A N     1 
ATOM   4803  C  CA    . ASN A 1  669  ? -32.565 75.937  101.386 1.00 22.96 ? 667  ASN A CA    1 
ATOM   4804  C  C     . ASN A 1  669  ? -32.603 75.696  102.886 1.00 22.93 ? 667  ASN A C     1 
ATOM   4805  O  O     . ASN A 1  669  ? -31.603 75.278  103.487 1.00 22.00 ? 667  ASN A O     1 
ATOM   4806  C  CB    . ASN A 1  669  ? -32.315 77.432  101.160 1.00 23.19 ? 667  ASN A CB    1 
ATOM   4807  C  CG    . ASN A 1  669  ? -32.275 77.844  99.690  1.00 27.88 ? 667  ASN A CG    1 
ATOM   4808  O  OD1   . ASN A 1  669  ? -32.562 79.005  99.372  1.00 32.66 ? 667  ASN A OD1   1 
ATOM   4809  N  ND2   . ASN A 1  669  ? -31.908 76.925  98.806  1.00 26.67 ? 667  ASN A ND2   1 
ATOM   4810  N  N     . ALA A 1  670  ? -33.736 76.008  103.515 1.00 20.71 ? 668  ALA A N     1 
ATOM   4811  C  CA    . ALA A 1  670  ? -33.829 75.895  104.964 1.00 20.04 ? 668  ALA A CA    1 
ATOM   4812  C  C     . ALA A 1  670  ? -33.761 74.441  105.411 1.00 19.79 ? 668  ALA A C     1 
ATOM   4813  O  O     . ALA A 1  670  ? -33.180 74.138  106.457 1.00 21.12 ? 668  ALA A O     1 
ATOM   4814  C  CB    . ALA A 1  670  ? -35.119 76.551  105.458 1.00 21.40 ? 668  ALA A CB    1 
ATOM   4815  N  N     . ILE A 1  671  ? -34.372 73.529  104.655 1.00 20.70 ? 669  ILE A N     1 
ATOM   4816  C  CA    . ILE A 1  671  ? -34.255 72.112  104.995 1.00 19.34 ? 669  ILE A CA    1 
ATOM   4817  C  C     . ILE A 1  671  ? -32.792 71.689  104.964 1.00 20.29 ? 669  ILE A C     1 
ATOM   4818  O  O     . ILE A 1  671  ? -32.297 71.030  105.885 1.00 22.26 ? 669  ILE A O     1 
ATOM   4819  C  CB    . ILE A 1  671  ? -35.099 71.250  104.041 1.00 20.40 ? 669  ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1  671  ? -36.593 71.474  104.285 1.00 20.99 ? 669  ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1  671  ? -34.743 69.781  104.218 1.00 22.40 ? 669  ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1  671  ? -37.465 70.879  103.191 1.00 21.44 ? 669  ILE A CD1   1 
ATOM   4823  N  N     . ALA A 1  672  ? -32.085 72.067  103.894 1.00 20.53 ? 670  ALA A N     1 
ATOM   4824  C  CA    . ALA A 1  672  ? -30.669 71.740  103.782 1.00 21.50 ? 670  ALA A CA    1 
ATOM   4825  C  C     . ALA A 1  672  ? -29.879 72.353  104.929 1.00 19.56 ? 670  ALA A C     1 
ATOM   4826  O  O     . ALA A 1  672  ? -28.958 71.725  105.468 1.00 21.69 ? 670  ALA A O     1 
ATOM   4827  C  CB    . ALA A 1  672  ? -30.131 72.220  102.438 1.00 24.24 ? 670  ALA A CB    1 
ATOM   4828  N  N     . GLU A 1  673  ? -30.238 73.576  105.318 1.00 20.74 ? 671  GLU A N     1 
ATOM   4829  C  CA    . GLU A 1  673  ? -29.558 74.254  106.420 1.00 19.44 ? 671  GLU A CA    1 
ATOM   4830  C  C     . GLU A 1  673  ? -29.702 73.476  107.724 1.00 21.05 ? 671  GLU A C     1 
ATOM   4831  O  O     . GLU A 1  673  ? -28.717 73.250  108.439 1.00 20.07 ? 671  GLU A O     1 
ATOM   4832  C  CB    . GLU A 1  673  ? -30.120 75.667  106.562 1.00 21.88 ? 671  GLU A CB    1 
ATOM   4833  C  CG    . GLU A 1  673  ? -29.495 76.490  107.675 1.00 24.53 ? 671  GLU A CG    1 
ATOM   4834  C  CD    . GLU A 1  673  ? -28.202 77.128  107.247 1.00 24.32 ? 671  GLU A CD    1 
ATOM   4835  O  OE1   . GLU A 1  673  ? -27.925 77.152  106.019 1.00 24.76 ? 671  GLU A OE1   1 
ATOM   4836  O  OE2   . GLU A 1  673  ? -27.461 77.597  108.141 1.00 22.77 ? 671  GLU A OE2   1 
ATOM   4837  N  N     . VAL A 1  674  ? -30.927 73.049  108.053 1.00 19.73 ? 672  VAL A N     1 
ATOM   4838  C  CA    . VAL A 1  674  ? -31.143 72.340  109.312 1.00 19.16 ? 672  VAL A CA    1 
ATOM   4839  C  C     . VAL A 1  674  ? -30.544 70.940  109.244 1.00 20.30 ? 672  VAL A C     1 
ATOM   4840  O  O     . VAL A 1  674  ? -29.968 70.445  110.225 1.00 19.01 ? 672  VAL A O     1 
ATOM   4841  C  CB    . VAL A 1  674  ? -32.644 72.296  109.669 1.00 20.36 ? 672  VAL A CB    1 
ATOM   4842  C  CG1   . VAL A 1  674  ? -32.859 71.553  110.997 1.00 20.57 ? 672  VAL A CG1   1 
ATOM   4843  C  CG2   . VAL A 1  674  ? -33.240 73.711  109.754 1.00 19.38 ? 672  VAL A CG2   1 
ATOM   4844  N  N     . ARG A 1  675  ? -30.678 70.272  108.097 1.00 20.27 ? 673  ARG A N     1 
ATOM   4845  C  CA    . ARG A 1  675  ? -30.041 68.974  107.940 1.00 17.52 ? 673  ARG A CA    1 
ATOM   4846  C  C     . ARG A 1  675  ? -28.544 69.079  108.175 1.00 18.15 ? 673  ARG A C     1 
ATOM   4847  O  O     . ARG A 1  675  ? -27.948 68.208  108.818 1.00 19.00 ? 673  ARG A O     1 
ATOM   4848  C  CB    . ARG A 1  675  ? -30.300 68.415  106.546 1.00 18.49 ? 673  ARG A CB    1 
ATOM   4849  C  CG    . ARG A 1  675  ? -31.695 67.885  106.341 1.00 18.63 ? 673  ARG A CG    1 
ATOM   4850  C  CD    . ARG A 1  675  ? -31.755 67.110  105.041 1.00 20.44 ? 673  ARG A CD    1 
ATOM   4851  N  NE    . ARG A 1  675  ? -31.008 65.858  105.147 1.00 20.11 ? 673  ARG A NE    1 
ATOM   4852  C  CZ    . ARG A 1  675  ? -30.629 65.117  104.113 1.00 20.04 ? 673  ARG A CZ    1 
ATOM   4853  N  NH1   . ARG A 1  675  ? -30.914 65.469  102.867 1.00 20.03 ? 673  ARG A NH1   1 
ATOM   4854  N  NH2   . ARG A 1  675  ? -29.940 63.998  104.334 1.00 19.25 ? 673  ARG A NH2   1 
ATOM   4855  N  N     . GLU A 1  676  ? -27.926 70.148  107.667 1.00 17.37 ? 674  GLU A N     1 
ATOM   4856  C  CA    . GLU A 1  676  ? -26.483 70.286  107.825 1.00 18.86 ? 674  GLU A CA    1 
ATOM   4857  C  C     . GLU A 1  676  ? -26.106 70.472  109.289 1.00 18.49 ? 674  GLU A C     1 
ATOM   4858  O  O     . GLU A 1  676  ? -25.113 69.902  109.752 1.00 17.72 ? 674  GLU A O     1 
ATOM   4859  C  CB    . GLU A 1  676  ? -25.956 71.444  106.987 1.00 18.05 ? 674  GLU A CB    1 
ATOM   4860  C  CG    . GLU A 1  676  ? -24.433 71.487  107.033 1.00 21.09 ? 674  GLU A CG    1 
ATOM   4861  C  CD    . GLU A 1  676  ? -23.808 71.923  105.740 1.00 29.92 ? 674  GLU A CD    1 
ATOM   4862  O  OE1   . GLU A 1  676  ? -24.391 72.798  105.060 1.00 37.66 ? 674  GLU A OE1   1 
ATOM   4863  O  OE2   . GLU A 1  676  ? -22.730 71.369  105.396 1.00 29.30 ? 674  GLU A OE2   1 
ATOM   4864  N  N     . ALA A 1  677  ? -26.893 71.250  110.043 1.00 19.66 ? 675  ALA A N     1 
ATOM   4865  C  CA    . ALA A 1  677  ? -26.609 71.394  111.469 1.00 19.09 ? 675  ALA A CA    1 
ATOM   4866  C  C     . ALA A 1  677  ? -26.738 70.057  112.182 1.00 18.70 ? 675  ALA A C     1 
ATOM   4867  O  O     . ALA A 1  677  ? -25.891 69.704  113.015 1.00 17.78 ? 675  ALA A O     1 
ATOM   4868  C  CB    . ALA A 1  677  ? -27.529 72.442  112.097 1.00 19.35 ? 675  ALA A CB    1 
ATOM   4869  N  N     . ILE A 1  678  ? -27.773 69.286  111.841 1.00 17.13 ? 676  ILE A N     1 
ATOM   4870  C  CA    . ILE A 1  678  ? -27.954 67.963  112.430 1.00 17.31 ? 676  ILE A CA    1 
ATOM   4871  C  C     . ILE A 1  678  ? -26.752 67.082  112.119 1.00 18.74 ? 676  ILE A C     1 
ATOM   4872  O  O     . ILE A 1  678  ? -26.249 66.359  112.992 1.00 18.95 ? 676  ILE A O     1 
ATOM   4873  C  CB    . ILE A 1  678  ? -29.268 67.340  111.920 1.00 18.90 ? 676  ILE A CB    1 
ATOM   4874  C  CG1   . ILE A 1  678  ? -30.459 68.120  112.483 1.00 21.88 ? 676  ILE A CG1   1 
ATOM   4875  C  CG2   . ILE A 1  678  ? -29.358 65.865  112.282 1.00 20.66 ? 676  ILE A CG2   1 
ATOM   4876  C  CD1   . ILE A 1  678  ? -31.774 67.855  111.743 1.00 20.07 ? 676  ILE A CD1   1 
ATOM   4877  N  N     . ASP A 1  679  ? -26.274 67.143  110.868 1.00 17.11 ? 677  ASP A N     1 
ATOM   4878  C  CA    . ASP A 1  679  ? -25.145 66.319  110.444 1.00 16.54 ? 677  ASP A CA    1 
ATOM   4879  C  C     . ASP A 1  679  ? -23.852 66.749  111.123 1.00 17.94 ? 677  ASP A C     1 
ATOM   4880  O  O     . ASP A 1  679  ? -23.052 65.894  111.516 1.00 19.36 ? 677  ASP A O     1 
ATOM   4881  C  CB    . ASP A 1  679  ? -25.002 66.377  108.923 1.00 17.28 ? 677  ASP A CB    1 
ATOM   4882  C  CG    . ASP A 1  679  ? -26.168 65.730  108.199 1.00 19.27 ? 677  ASP A CG    1 
ATOM   4883  O  OD1   . ASP A 1  679  ? -26.789 64.813  108.756 1.00 21.94 ? 677  ASP A OD1   1 
ATOM   4884  O  OD2   . ASP A 1  679  ? -26.426 66.110  107.041 1.00 20.74 ? 677  ASP A OD2   1 
ATOM   4885  N  N     . PHE A 1  680  ? -23.621 68.060  111.267 1.00 17.04 ? 678  PHE A N     1 
ATOM   4886  C  CA    . PHE A 1  680  ? -22.471 68.517  112.057 1.00 18.02 ? 678  PHE A CA    1 
ATOM   4887  C  C     . PHE A 1  680  ? -22.498 67.923  113.457 1.00 18.67 ? 678  PHE A C     1 
ATOM   4888  O  O     . PHE A 1  680  ? -21.505 67.353  113.921 1.00 17.63 ? 678  PHE A O     1 
ATOM   4889  C  CB    . PHE A 1  680  ? -22.433 70.043  112.149 1.00 16.97 ? 678  PHE A CB    1 
ATOM   4890  C  CG    . PHE A 1  680  ? -21.803 70.718  110.970 1.00 16.62 ? 678  PHE A CG    1 
ATOM   4891  C  CD1   . PHE A 1  680  ? -20.580 70.288  110.465 1.00 19.07 ? 678  PHE A CD1   1 
ATOM   4892  C  CD2   . PHE A 1  680  ? -22.437 71.791  110.358 1.00 18.09 ? 678  PHE A CD2   1 
ATOM   4893  C  CE1   . PHE A 1  680  ? -19.998 70.926  109.379 1.00 19.79 ? 678  PHE A CE1   1 
ATOM   4894  C  CE2   . PHE A 1  680  ? -21.871 72.431  109.277 1.00 18.70 ? 678  PHE A CE2   1 
ATOM   4895  C  CZ    . PHE A 1  680  ? -20.651 72.001  108.774 1.00 19.38 ? 678  PHE A CZ    1 
ATOM   4896  N  N     . LEU A 1  681  ? -23.627 68.075  114.161 1.00 18.10 ? 679  LEU A N     1 
ATOM   4897  C  CA    . LEU A 1  681  ? -23.726 67.573  115.528 1.00 17.66 ? 679  LEU A CA    1 
ATOM   4898  C  C     . LEU A 1  681  ? -23.397 66.088  115.584 1.00 19.96 ? 679  LEU A C     1 
ATOM   4899  O  O     . LEU A 1  681  ? -22.603 65.646  116.416 1.00 18.23 ? 679  LEU A O     1 
ATOM   4900  C  CB    . LEU A 1  681  ? -25.131 67.834  116.076 1.00 18.57 ? 679  LEU A CB    1 
ATOM   4901  C  CG    . LEU A 1  681  ? -25.465 69.301  116.343 1.00 20.68 ? 679  LEU A CG    1 
ATOM   4902  C  CD1   . LEU A 1  681  ? -26.991 69.517  116.448 1.00 19.65 ? 679  LEU A CD1   1 
ATOM   4903  C  CD2   . LEU A 1  681  ? -24.766 69.773  117.610 1.00 19.95 ? 679  LEU A CD2   1 
ATOM   4904  N  N     . ARG A 1  682  ? -23.987 65.301  114.686 1.00 18.46 ? 680  ARG A N     1 
ATOM   4905  C  CA    . ARG A 1  682  ? -23.788 63.860  114.758 1.00 17.59 ? 680  ARG A CA    1 
ATOM   4906  C  C     . ARG A 1  682  ? -22.412 63.449  114.270 1.00 19.64 ? 680  ARG A C     1 
ATOM   4907  O  O     . ARG A 1  682  ? -21.840 62.487  114.790 1.00 18.87 ? 680  ARG A O     1 
ATOM   4908  C  CB    . ARG A 1  682  ? -24.862 63.143  113.953 1.00 18.00 ? 680  ARG A CB    1 
ATOM   4909  C  CG    . ARG A 1  682  ? -26.227 63.256  114.634 1.00 19.58 ? 680  ARG A CG    1 
ATOM   4910  C  CD    . ARG A 1  682  ? -27.302 62.677  113.747 1.00 19.69 ? 680  ARG A CD    1 
ATOM   4911  N  NE    . ARG A 1  682  ? -28.596 62.685  114.418 1.00 21.28 ? 680  ARG A NE    1 
ATOM   4912  C  CZ    . ARG A 1  682  ? -29.748 62.511  113.783 1.00 21.84 ? 680  ARG A CZ    1 
ATOM   4913  N  NH1   . ARG A 1  682  ? -29.788 62.301  112.480 1.00 21.22 ? 680  ARG A NH1   1 
ATOM   4914  N  NH2   . ARG A 1  682  ? -30.882 62.537  114.475 1.00 22.78 ? 680  ARG A NH2   1 
ATOM   4915  N  N     . TYR A 1  683  ? -21.862 64.183  113.309 1.00 18.09 ? 681  TYR A N     1 
ATOM   4916  C  CA    . TYR A 1  683  ? -20.540 63.836  112.800 1.00 16.73 ? 681  TYR A CA    1 
ATOM   4917  C  C     . TYR A 1  683  ? -19.470 64.140  113.841 1.00 18.78 ? 681  TYR A C     1 
ATOM   4918  O  O     . TYR A 1  683  ? -18.599 63.303  114.115 1.00 18.47 ? 681  TYR A O     1 
ATOM   4919  C  CB    . TYR A 1  683  ? -20.273 64.591  111.501 1.00 17.01 ? 681  TYR A CB    1 
ATOM   4920  C  CG    . TYR A 1  683  ? -18.891 64.382  110.948 1.00 18.11 ? 681  TYR A CG    1 
ATOM   4921  C  CD1   . TYR A 1  683  ? -18.576 63.220  110.260 1.00 17.69 ? 681  TYR A CD1   1 
ATOM   4922  C  CD2   . TYR A 1  683  ? -17.902 65.349  111.114 1.00 15.85 ? 681  TYR A CD2   1 
ATOM   4923  C  CE1   . TYR A 1  683  ? -17.301 63.019  109.742 1.00 17.12 ? 681  TYR A CE1   1 
ATOM   4924  C  CE2   . TYR A 1  683  ? -16.634 65.158  110.609 1.00 17.56 ? 681  TYR A CE2   1 
ATOM   4925  C  CZ    . TYR A 1  683  ? -16.341 63.988  109.933 1.00 18.16 ? 681  TYR A CZ    1 
ATOM   4926  O  OH    . TYR A 1  683  ? -15.085 63.803  109.422 1.00 18.44 ? 681  TYR A OH    1 
ATOM   4927  N  N     . TYR A 1  684  ? -19.515 65.333  114.437 1.00 16.36 ? 682  TYR A N     1 
ATOM   4928  C  CA    . TYR A 1  684  ? -18.498 65.654  115.437 1.00 16.66 ? 682  TYR A CA    1 
ATOM   4929  C  C     . TYR A 1  684  ? -18.648 64.784  116.677 1.00 20.79 ? 682  TYR A C     1 
ATOM   4930  O  O     . TYR A 1  684  ? -17.650 64.485  117.348 1.00 19.25 ? 682  TYR A O     1 
ATOM   4931  C  CB    . TYR A 1  684  ? -18.548 67.138  115.815 1.00 17.70 ? 682  TYR A CB    1 
ATOM   4932  C  CG    . TYR A 1  684  ? -18.180 68.059  114.666 1.00 16.42 ? 682  TYR A CG    1 
ATOM   4933  C  CD1   . TYR A 1  684  ? -17.133 67.746  113.803 1.00 17.29 ? 682  TYR A CD1   1 
ATOM   4934  C  CD2   . TYR A 1  684  ? -18.893 69.232  114.438 1.00 18.94 ? 682  TYR A CD2   1 
ATOM   4935  C  CE1   . TYR A 1  684  ? -16.808 68.576  112.738 1.00 18.28 ? 682  TYR A CE1   1 
ATOM   4936  C  CE2   . TYR A 1  684  ? -18.573 70.072  113.376 1.00 15.80 ? 682  TYR A CE2   1 
ATOM   4937  C  CZ    . TYR A 1  684  ? -17.528 69.736  112.531 1.00 19.01 ? 682  TYR A CZ    1 
ATOM   4938  O  OH    . TYR A 1  684  ? -17.191 70.558  111.478 1.00 18.10 ? 682  TYR A OH    1 
ATOM   4939  N  N     . ALA A 1  685  ? -19.876 64.363  116.995 1.00 18.06 ? 683  ALA A N     1 
ATOM   4940  C  CA    . ALA A 1  685  ? -20.071 63.431  118.100 1.00 19.40 ? 683  ALA A CA    1 
ATOM   4941  C  C     . ALA A 1  685  ? -19.397 62.094  117.803 1.00 21.24 ? 683  ALA A C     1 
ATOM   4942  O  O     . ALA A 1  685  ? -18.671 61.552  118.642 1.00 19.96 ? 683  ALA A O     1 
ATOM   4943  C  CB    . ALA A 1  685  ? -21.564 63.236  118.378 1.00 21.32 ? 683  ALA A CB    1 
ATOM   4944  N  N     . GLU A 1  686  ? -19.620 61.551  116.607 1.00 20.01 ? 684  GLU A N     1 
ATOM   4945  C  CA    . GLU A 1  686  ? -18.986 60.282  116.272 1.00 20.75 ? 684  GLU A CA    1 
ATOM   4946  C  C     . GLU A 1  686  ? -17.474 60.431  116.188 1.00 20.35 ? 684  GLU A C     1 
ATOM   4947  O  O     . GLU A 1  686  ? -16.735 59.581  116.704 1.00 19.88 ? 684  GLU A O     1 
ATOM   4948  C  CB    . GLU A 1  686  ? -19.549 59.726  114.961 1.00 20.10 ? 684  GLU A CB    1 
ATOM   4949  C  CG    . GLU A 1  686  ? -18.800 58.473  114.463 1.00 22.20 ? 684  GLU A CG    1 
ATOM   4950  C  CD    . GLU A 1  686  ? -18.923 57.254  115.387 1.00 25.18 ? 684  GLU A CD    1 
ATOM   4951  O  OE1   . GLU A 1  686  ? -19.771 57.241  116.318 1.00 25.92 ? 684  GLU A OE1   1 
ATOM   4952  O  OE2   . GLU A 1  686  ? -18.173 56.278  115.166 1.00 25.69 ? 684  GLU A OE2   1 
ATOM   4953  N  N     . GLN A 1  687  ? -16.995 61.515  115.569 1.00 18.32 ? 685  GLN A N     1 
ATOM   4954  C  CA    . GLN A 1  687  ? -15.550 61.710  115.474 1.00 17.83 ? 685  GLN A CA    1 
ATOM   4955  C  C     . GLN A 1  687  ? -14.938 61.810  116.860 1.00 19.44 ? 685  GLN A C     1 
ATOM   4956  O  O     . GLN A 1  687  ? -13.825 61.322  117.093 1.00 19.32 ? 685  GLN A O     1 
ATOM   4957  C  CB    . GLN A 1  687  ? -15.217 62.960  114.662 1.00 16.77 ? 685  GLN A CB    1 
ATOM   4958  C  CG    . GLN A 1  687  ? -15.489 62.832  113.155 1.00 16.93 ? 685  GLN A CG    1 
ATOM   4959  C  CD    . GLN A 1  687  ? -14.744 61.672  112.529 1.00 20.05 ? 685  GLN A CD    1 
ATOM   4960  O  OE1   . GLN A 1  687  ? -13.517 61.594  112.614 1.00 19.61 ? 685  GLN A OE1   1 
ATOM   4961  N  NE2   . GLN A 1  687  ? -15.477 60.765  111.895 1.00 22.25 ? 685  GLN A NE2   1 
ATOM   4962  N  N     . THR A 1  688  ? -15.649 62.443  117.793 1.00 17.62 ? 686  THR A N     1 
ATOM   4963  C  CA    . THR A 1  688  ? -15.185 62.474  119.180 1.00 18.02 ? 686  THR A CA    1 
ATOM   4964  C  C     . THR A 1  688  ? -15.081 61.072  119.762 1.00 19.00 ? 686  THR A C     1 
ATOM   4965  O  O     . THR A 1  688  ? -14.057 60.707  120.360 1.00 21.76 ? 686  THR A O     1 
ATOM   4966  C  CB    . THR A 1  688  ? -16.125 63.321  120.037 1.00 20.90 ? 686  THR A CB    1 
ATOM   4967  O  OG1   . THR A 1  688  ? -16.020 64.683  119.628 1.00 21.33 ? 686  THR A OG1   1 
ATOM   4968  C  CG2   . THR A 1  688  ? -15.728 63.207  121.528 1.00 19.47 ? 686  THR A CG2   1 
ATOM   4969  N  N     . ARG A 1  689  ? -16.134 60.273  119.598 1.00 19.91 ? 687  ARG A N     1 
ATOM   4970  C  CA    . ARG A 1  689  ? -16.126 58.912  120.114 1.00 22.97 ? 687  ARG A CA    1 
ATOM   4971  C  C     . ARG A 1  689  ? -15.034 58.081  119.473 1.00 20.51 ? 687  ARG A C     1 
ATOM   4972  O  O     . ARG A 1  689  ? -14.563 57.123  120.091 1.00 22.56 ? 687  ARG A O     1 
ATOM   4973  C  CB    . ARG A 1  689  ? -17.487 58.240  119.895 1.00 23.23 ? 687  ARG A CB    1 
ATOM   4974  C  CG    . ARG A 1  689  ? -18.584 58.723  120.837 1.00 21.59 ? 687  ARG A CG    1 
ATOM   4975  C  CD    . ARG A 1  689  ? -19.865 57.935  120.616 1.00 24.11 ? 687  ARG A CD    1 
ATOM   4976  N  NE    . ARG A 1  689  ? -20.361 58.066  119.251 1.00 24.21 ? 687  ARG A NE    1 
ATOM   4977  C  CZ    . ARG A 1  689  ? -21.375 58.842  118.891 1.00 24.46 ? 687  ARG A CZ    1 
ATOM   4978  N  NH1   . ARG A 1  689  ? -22.013 59.599  119.772 1.00 27.49 ? 687  ARG A NH1   1 
ATOM   4979  N  NH2   . ARG A 1  689  ? -21.758 58.859  117.618 1.00 23.22 ? 687  ARG A NH2   1 
ATOM   4980  N  N     . ARG A 1  690  ? -14.600 58.449  118.271 1.00 20.83 ? 688  ARG A N     1 
ATOM   4981  C  CA    . ARG A 1  690  ? -13.508 57.729  117.638 1.00 20.85 ? 688  ARG A CA    1 
ATOM   4982  C  C     . ARG A 1  690  ? -12.138 58.174  118.121 1.00 22.00 ? 688  ARG A C     1 
ATOM   4983  O  O     . ARG A 1  690  ? -11.173 57.429  117.920 1.00 20.72 ? 688  ARG A O     1 
ATOM   4984  C  CB    . ARG A 1  690  ? -13.566 57.894  116.115 1.00 20.68 ? 688  ARG A CB    1 
ATOM   4985  C  CG    . ARG A 1  690  ? -14.808 57.263  115.463 1.00 24.00 ? 688  ARG A CG    1 
ATOM   4986  C  CD    . ARG A 1  690  ? -14.724 55.732  115.406 1.00 24.24 ? 688  ARG A CD    1 
ATOM   4987  N  NE    . ARG A 1  690  ? -13.585 55.302  114.595 1.00 27.70 ? 688  ARG A NE    1 
ATOM   4988  C  CZ    . ARG A 1  690  ? -12.546 54.634  115.072 1.00 27.95 ? 688  ARG A CZ    1 
ATOM   4989  N  NH1   . ARG A 1  690  ? -12.484 54.268  116.346 1.00 29.04 ? 688  ARG A NH1   1 
ATOM   4990  N  NH2   . ARG A 1  690  ? -11.546 54.318  114.251 1.00 26.21 ? 688  ARG A NH2   1 
ATOM   4991  N  N     . THR A 1  691  ? -12.004 59.362  118.725 1.00 19.66 ? 689  THR A N     1 
ATOM   4992  C  CA    . THR A 1  691  ? -10.642 59.875  118.898 1.00 18.54 ? 689  THR A CA    1 
ATOM   4993  C  C     . THR A 1  691  ? -10.257 60.358  120.291 1.00 22.36 ? 689  THR A C     1 
ATOM   4994  O  O     . THR A 1  691  ? -9.151  60.058  120.753 1.00 24.04 ? 689  THR A O     1 
ATOM   4995  C  CB    . THR A 1  691  ? -10.374 61.031  117.932 1.00 18.72 ? 689  THR A CB    1 
ATOM   4996  O  OG1   . THR A 1  691  ? -11.404 62.017  118.078 1.00 20.77 ? 689  THR A OG1   1 
ATOM   4997  C  CG2   . THR A 1  691  ? -10.327 60.539  116.473 1.00 20.45 ? 689  THR A CG2   1 
ATOM   4998  N  N     . LEU A 1  692  ? -11.112 61.129  120.961 1.00 20.48 ? 690  LEU A N     1 
ATOM   4999  C  CA    . LEU A 1  692  ? -10.624 61.983  122.041 1.00 22.29 ? 690  LEU A CA    1 
ATOM   5000  C  C     . LEU A 1  692  ? -10.412 61.208  123.340 1.00 22.87 ? 690  LEU A C     1 
ATOM   5001  O  O     . LEU A 1  692  ? -11.304 60.496  123.816 1.00 25.13 ? 690  LEU A O     1 
ATOM   5002  C  CB    . LEU A 1  692  ? -11.579 63.155  122.264 1.00 22.40 ? 690  LEU A CB    1 
ATOM   5003  C  CG    . LEU A 1  692  ? -11.644 64.157  121.099 1.00 21.98 ? 690  LEU A CG    1 
ATOM   5004  C  CD1   . LEU A 1  692  ? -12.451 65.386  121.498 1.00 24.13 ? 690  LEU A CD1   1 
ATOM   5005  C  CD2   . LEU A 1  692  ? -10.266 64.567  120.620 1.00 22.97 ? 690  LEU A CD2   1 
ATOM   5006  N  N     . GLY A 1  693  ? -9.224  61.370  123.913 1.00 23.87 ? 691  GLY A N     1 
ATOM   5007  C  CA    . GLY A 1  693  ? -8.868  60.747  125.162 1.00 25.84 ? 691  GLY A CA    1 
ATOM   5008  C  C     . GLY A 1  693  ? -8.280  61.761  126.119 1.00 27.84 ? 691  GLY A C     1 
ATOM   5009  O  O     . GLY A 1  693  ? -8.230  62.962  125.837 1.00 28.90 ? 691  GLY A O     1 
ATOM   5010  N  N     . PRO A 1  694  ? -7.800  61.279  127.269 1.00 27.82 ? 692  PRO A N     1 
ATOM   5011  C  CA    . PRO A 1  694  ? -7.309  62.196  128.315 1.00 33.48 ? 692  PRO A CA    1 
ATOM   5012  C  C     . PRO A 1  694  ? -6.178  63.113  127.875 1.00 33.18 ? 692  PRO A C     1 
ATOM   5013  O  O     . PRO A 1  694  ? -6.093  64.249  128.360 1.00 33.46 ? 692  PRO A O     1 
ATOM   5014  C  CB    . PRO A 1  694  ? -6.854  61.235  129.421 1.00 32.64 ? 692  PRO A CB    1 
ATOM   5015  C  CG    . PRO A 1  694  ? -7.671  60.001  129.208 1.00 30.43 ? 692  PRO A CG    1 
ATOM   5016  C  CD    . PRO A 1  694  ? -7.848  59.878  127.725 1.00 29.98 ? 692  PRO A CD    1 
ATOM   5017  N  N     . GLY A 1  695  ? -5.310  62.665  126.973 1.00 25.26 ? 693  GLY A N     1 
ATOM   5018  C  CA    . GLY A 1  695  ? -4.187  63.476  126.552 1.00 29.28 ? 693  GLY A CA    1 
ATOM   5019  C  C     . GLY A 1  695  ? -4.493  64.539  125.523 1.00 29.47 ? 693  GLY A C     1 
ATOM   5020  O  O     . GLY A 1  695  ? -3.598  65.317  125.183 1.00 28.16 ? 693  GLY A O     1 
ATOM   5021  N  N     . HIS A 1  696  ? -5.726  64.599  125.012 1.00 27.70 ? 694  HIS A N     1 
ATOM   5022  C  CA    . HIS A 1  696  ? -6.092  65.619  124.032 1.00 27.05 ? 694  HIS A CA    1 
ATOM   5023  C  C     . HIS A 1  696  ? -6.817  66.724  124.790 1.00 28.55 ? 694  HIS A C     1 
ATOM   5024  O  O     . HIS A 1  696  ? -8.048  66.825  124.798 1.00 28.83 ? 694  HIS A O     1 
ATOM   5025  C  CB    . HIS A 1  696  ? -6.934  65.020  122.910 1.00 25.43 ? 694  HIS A CB    1 
ATOM   5026  C  CG    . HIS A 1  696  ? -6.378  63.738  122.371 1.00 22.99 ? 694  HIS A CG    1 
ATOM   5027  N  ND1   . HIS A 1  696  ? -7.027  62.532  122.512 1.00 26.56 ? 694  HIS A ND1   1 
ATOM   5028  C  CD2   . HIS A 1  696  ? -5.216  63.470  121.727 1.00 24.84 ? 694  HIS A CD2   1 
ATOM   5029  C  CE1   . HIS A 1  696  ? -6.301  61.578  121.957 1.00 24.75 ? 694  HIS A CE1   1 
ATOM   5030  N  NE2   . HIS A 1  696  ? -5.197  62.120  121.473 1.00 25.84 ? 694  HIS A NE2   1 
ATOM   5031  N  N     . GLY A 1  697  ? -6.024  67.551  125.462 1.00 28.01 ? 695  GLY A N     1 
ATOM   5032  C  CA    . GLY A 1  697  ? -6.567  68.570  126.321 1.00 27.07 ? 695  GLY A CA    1 
ATOM   5033  C  C     . GLY A 1  697  ? -7.163  69.692  125.510 1.00 26.81 ? 695  GLY A C     1 
ATOM   5034  O  O     . GLY A 1  697  ? -6.685  70.034  124.423 1.00 25.52 ? 695  GLY A O     1 
ATOM   5035  N  N     . PRO A 1  698  ? -8.237  70.282  126.011 1.00 24.50 ? 696  PRO A N     1 
ATOM   5036  C  CA    . PRO A 1  698  ? -8.854  71.394  125.291 1.00 27.16 ? 696  PRO A CA    1 
ATOM   5037  C  C     . PRO A 1  698  ? -7.945  72.612  125.284 1.00 24.39 ? 696  PRO A C     1 
ATOM   5038  O  O     . PRO A 1  698  ? -7.055  72.777  126.126 1.00 25.55 ? 696  PRO A O     1 
ATOM   5039  C  CB    . PRO A 1  698  ? -10.141 71.663  126.075 1.00 28.55 ? 696  PRO A CB    1 
ATOM   5040  C  CG    . PRO A 1  698  ? -10.339 70.441  126.948 1.00 32.57 ? 696  PRO A CG    1 
ATOM   5041  C  CD    . PRO A 1  698  ? -8.973  69.924  127.233 1.00 29.95 ? 696  PRO A CD    1 
ATOM   5042  N  N     . LEU A 1  699  ? -8.168  73.465  124.283 1.00 23.44 ? 697  LEU A N     1 
ATOM   5043  C  CA    . LEU A 1  699  ? -7.454  74.736  124.224 1.00 23.59 ? 697  LEU A CA    1 
ATOM   5044  C  C     . LEU A 1  699  ? -7.847  75.645  125.378 1.00 26.02 ? 697  LEU A C     1 
ATOM   5045  O  O     . LEU A 1  699  ? -6.990  76.292  125.989 1.00 24.15 ? 697  LEU A O     1 
ATOM   5046  C  CB    . LEU A 1  699  ? -7.737  75.432  122.898 1.00 21.12 ? 697  LEU A CB    1 
ATOM   5047  C  CG    . LEU A 1  699  ? -7.257  74.720  121.641 1.00 22.03 ? 697  LEU A CG    1 
ATOM   5048  C  CD1   . LEU A 1  699  ? -7.665  75.549  120.433 1.00 21.36 ? 697  LEU A CD1   1 
ATOM   5049  C  CD2   . LEU A 1  699  ? -5.734  74.503  121.697 1.00 24.91 ? 697  LEU A CD2   1 
ATOM   5050  N  N     . GLY A 1  700  ? -9.141  75.720  125.683 1.00 24.19 ? 698  GLY A N     1 
ATOM   5051  C  CA    . GLY A 1  700  ? -9.658  76.724  126.583 1.00 24.89 ? 698  GLY A CA    1 
ATOM   5052  C  C     . GLY A 1  700  ? -10.793 77.442  125.888 1.00 24.45 ? 698  GLY A C     1 
ATOM   5053  O  O     . GLY A 1  700  ? -11.348 76.936  124.908 1.00 24.02 ? 698  GLY A O     1 
ATOM   5054  N  N     . PRO A 1  701  ? -11.152 78.633  126.364 1.00 26.64 ? 699  PRO A N     1 
ATOM   5055  C  CA    . PRO A 1  701  ? -12.284 79.355  125.761 1.00 25.76 ? 699  PRO A CA    1 
ATOM   5056  C  C     . PRO A 1  701  ? -12.053 79.602  124.277 1.00 23.68 ? 699  PRO A C     1 
ATOM   5057  O  O     . PRO A 1  701  ? -11.021 80.136  123.870 1.00 24.41 ? 699  PRO A O     1 
ATOM   5058  C  CB    . PRO A 1  701  ? -12.330 80.667  126.548 1.00 26.15 ? 699  PRO A CB    1 
ATOM   5059  C  CG    . PRO A 1  701  ? -11.671 80.338  127.872 1.00 26.91 ? 699  PRO A CG    1 
ATOM   5060  C  CD    . PRO A 1  701  ? -10.584 79.347  127.522 1.00 24.32 ? 699  PRO A CD    1 
ATOM   5061  N  N     . ILE A 1  702  ? -13.023 79.205  123.461 1.00 26.60 ? 700  ILE A N     1 
ATOM   5062  C  CA    . ILE A 1  702  ? -12.932 79.367  122.019 1.00 23.05 ? 700  ILE A CA    1 
ATOM   5063  C  C     . ILE A 1  702  ? -14.025 80.326  121.581 1.00 23.13 ? 700  ILE A C     1 
ATOM   5064  O  O     . ILE A 1  702  ? -15.193 80.169  121.961 1.00 22.81 ? 700  ILE A O     1 
ATOM   5065  C  CB    . ILE A 1  702  ? -13.020 78.015  121.290 1.00 22.05 ? 700  ILE A CB    1 
ATOM   5066  C  CG1   . ILE A 1  702  ? -11.736 77.221  121.554 1.00 21.89 ? 700  ILE A CG1   1 
ATOM   5067  C  CG2   . ILE A 1  702  ? -13.231 78.206  119.778 1.00 22.48 ? 700  ILE A CG2   1 
ATOM   5068  C  CD1   . ILE A 1  702  ? -11.623 75.941  120.794 1.00 23.80 ? 700  ILE A CD1   1 
ATOM   5069  N  N     . VAL A 1  703  ? -13.631 81.331  120.810 1.00 22.38 ? 701  VAL A N     1 
ATOM   5070  C  CA    . VAL A 1  703  ? -14.549 82.312  120.253 1.00 23.79 ? 701  VAL A CA    1 
ATOM   5071  C  C     . VAL A 1  703  ? -14.983 81.800  118.888 1.00 21.43 ? 701  VAL A C     1 
ATOM   5072  O  O     . VAL A 1  703  ? -14.147 81.586  118.009 1.00 21.09 ? 701  VAL A O     1 
ATOM   5073  C  CB    . VAL A 1  703  ? -13.878 83.688  120.150 1.00 22.75 ? 701  VAL A CB    1 
ATOM   5074  C  CG1   . VAL A 1  703  ? -14.732 84.648  119.356 1.00 23.50 ? 701  VAL A CG1   1 
ATOM   5075  C  CG2   . VAL A 1  703  ? -13.599 84.237  121.553 1.00 26.54 ? 701  VAL A CG2   1 
ATOM   5076  N  N     . CYS A 1  704  ? -16.288 81.586  118.717 1.00 20.64 ? 702  CYS A N     1 
ATOM   5077  C  CA    . CYS A 1  704  ? -16.859 81.092  117.466 1.00 22.06 ? 702  CYS A CA    1 
ATOM   5078  C  C     . CYS A 1  704  ? -17.603 82.252  116.820 1.00 21.52 ? 702  CYS A C     1 
ATOM   5079  O  O     . CYS A 1  704  ? -18.600 82.735  117.362 1.00 21.76 ? 702  CYS A O     1 
ATOM   5080  C  CB    . CYS A 1  704  ? -17.796 79.915  117.715 1.00 21.95 ? 702  CYS A CB    1 
ATOM   5081  S  SG    . CYS A 1  704  ? -16.992 78.482  118.421 1.00 22.37 ? 702  CYS A SG    1 
ATOM   5082  N  N     . ILE A 1  705  ? -17.116 82.699  115.670 1.00 18.77 ? 703  ILE A N     1 
ATOM   5083  C  CA    . ILE A 1  705  ? -17.693 83.827  114.954 1.00 21.01 ? 703  ILE A CA    1 
ATOM   5084  C  C     . ILE A 1  705  ? -18.182 83.306  113.614 1.00 20.08 ? 703  ILE A C     1 
ATOM   5085  O  O     . ILE A 1  705  ? -17.414 82.679  112.874 1.00 20.80 ? 703  ILE A O     1 
ATOM   5086  C  CB    . ILE A 1  705  ? -16.661 84.956  114.784 1.00 20.84 ? 703  ILE A CB    1 
ATOM   5087  C  CG1   . ILE A 1  705  ? -16.317 85.571  116.145 1.00 23.05 ? 703  ILE A CG1   1 
ATOM   5088  C  CG2   . ILE A 1  705  ? -17.174 86.008  113.855 1.00 22.37 ? 703  ILE A CG2   1 
ATOM   5089  C  CD1   . ILE A 1  705  ? -15.062 86.416  116.105 1.00 23.74 ? 703  ILE A CD1   1 
ATOM   5090  N  N     . SER A 1  706  ? -19.452 83.538  113.311 1.00 20.29 ? 704  SER A N     1 
ATOM   5091  C  CA    . SER A 1  706  ? -20.084 82.850  112.196 1.00 20.28 ? 704  SER A CA    1 
ATOM   5092  C  C     . SER A 1  706  ? -20.744 83.828  111.239 1.00 23.64 ? 704  SER A C     1 
ATOM   5093  O  O     . SER A 1  706  ? -21.080 84.955  111.616 1.00 22.19 ? 704  SER A O     1 
ATOM   5094  C  CB    . SER A 1  706  ? -21.124 81.843  112.709 1.00 21.92 ? 704  SER A CB    1 
ATOM   5095  O  OG    . SER A 1  706  ? -22.013 82.468  113.606 1.00 22.88 ? 704  SER A OG    1 
ATOM   5096  N  N     . PRO A 1  707  ? -20.960 83.415  109.995 1.00 24.26 ? 705  PRO A N     1 
ATOM   5097  C  CA    . PRO A 1  707  ? -21.520 84.308  108.979 1.00 24.09 ? 705  PRO A CA    1 
ATOM   5098  C  C     . PRO A 1  707  ? -23.045 84.294  109.002 1.00 20.23 ? 705  PRO A C     1 
ATOM   5099  O  O     . PRO A 1  707  ? -23.678 83.421  109.596 1.00 21.84 ? 705  PRO A O     1 
ATOM   5100  C  CB    . PRO A 1  707  ? -20.991 83.699  107.677 1.00 23.00 ? 705  PRO A CB    1 
ATOM   5101  C  CG    . PRO A 1  707  ? -20.994 82.237  107.967 1.00 20.22 ? 705  PRO A CG    1 
ATOM   5102  C  CD    . PRO A 1  707  ? -20.543 82.123  109.416 1.00 19.69 ? 705  PRO A CD    1 
ATOM   5103  N  N     . TRP A 1  708  ? -23.631 85.285  108.330 1.00 21.52 ? 706  TRP A N     1 
ATOM   5104  C  CA    . TRP A 1  708  ? -25.091 85.329  108.282 1.00 19.93 ? 706  TRP A CA    1 
ATOM   5105  C  C     . TRP A 1  708  ? -25.662 84.270  107.339 1.00 20.98 ? 706  TRP A C     1 
ATOM   5106  O  O     . TRP A 1  708  ? -26.799 83.835  107.536 1.00 23.46 ? 706  TRP A O     1 
ATOM   5107  C  CB    . TRP A 1  708  ? -25.584 86.732  107.868 1.00 21.64 ? 706  TRP A CB    1 
ATOM   5108  C  CG    . TRP A 1  708  ? -25.452 86.970  106.402 1.00 22.90 ? 706  TRP A CG    1 
ATOM   5109  C  CD1   . TRP A 1  708  ? -24.428 87.603  105.767 1.00 22.94 ? 706  TRP A CD1   1 
ATOM   5110  C  CD2   . TRP A 1  708  ? -26.353 86.529  105.375 1.00 23.61 ? 706  TRP A CD2   1 
ATOM   5111  N  NE1   . TRP A 1  708  ? -24.624 87.571  104.407 1.00 22.84 ? 706  TRP A NE1   1 
ATOM   5112  C  CE2   . TRP A 1  708  ? -25.802 86.919  104.143 1.00 22.22 ? 706  TRP A CE2   1 
ATOM   5113  C  CE3   . TRP A 1  708  ? -27.570 85.833  105.382 1.00 21.74 ? 706  TRP A CE3   1 
ATOM   5114  C  CZ2   . TRP A 1  708  ? -26.430 86.649  102.923 1.00 19.56 ? 706  TRP A CZ2   1 
ATOM   5115  C  CZ3   . TRP A 1  708  ? -28.185 85.556  104.174 1.00 23.52 ? 706  TRP A CZ3   1 
ATOM   5116  C  CH2   . TRP A 1  708  ? -27.617 85.971  102.961 1.00 22.15 ? 706  TRP A CH2   1 
ATOM   5117  N  N     . ASN A 1  709  ? -24.899 83.815  106.341 1.00 20.81 ? 707  ASN A N     1 
ATOM   5118  C  CA    . ASN A 1  709  ? -25.551 83.183  105.195 1.00 20.47 ? 707  ASN A CA    1 
ATOM   5119  C  C     . ASN A 1  709  ? -25.895 81.724  105.427 1.00 19.80 ? 707  ASN A C     1 
ATOM   5120  O  O     . ASN A 1  709  ? -26.783 81.202  104.752 1.00 21.81 ? 707  ASN A O     1 
ATOM   5121  C  CB    . ASN A 1  709  ? -24.689 83.311  103.943 1.00 19.90 ? 707  ASN A CB    1 
ATOM   5122  C  CG    . ASN A 1  709  ? -23.484 82.430  103.989 1.00 21.35 ? 707  ASN A CG    1 
ATOM   5123  O  OD1   . ASN A 1  709  ? -22.605 82.611  104.834 1.00 23.29 ? 707  ASN A OD1   1 
ATOM   5124  N  ND2   . ASN A 1  709  ? -23.421 81.465  103.079 1.00 22.27 ? 707  ASN A ND2   1 
ATOM   5125  N  N     . PHE A 1  710  ? -25.211 81.052  106.348 1.00 20.57 ? 708  PHE A N     1 
ATOM   5126  C  CA    . PHE A 1  710  ? -25.599 79.725  106.811 1.00 19.19 ? 708  PHE A CA    1 
ATOM   5127  C  C     . PHE A 1  710  ? -25.821 79.881  108.309 1.00 21.56 ? 708  PHE A C     1 
ATOM   5128  O  O     . PHE A 1  710  ? -24.992 79.452  109.126 1.00 20.61 ? 708  PHE A O     1 
ATOM   5129  C  CB    . PHE A 1  710  ? -24.545 78.660  106.501 1.00 20.82 ? 708  PHE A CB    1 
ATOM   5130  C  CG    . PHE A 1  710  ? -24.269 78.462  105.019 1.00 22.69 ? 708  PHE A CG    1 
ATOM   5131  C  CD1   . PHE A 1  710  ? -25.293 78.491  104.089 1.00 21.71 ? 708  PHE A CD1   1 
ATOM   5132  C  CD2   . PHE A 1  710  ? -22.968 78.248  104.565 1.00 24.31 ? 708  PHE A CD2   1 
ATOM   5133  C  CE1   . PHE A 1  710  ? -25.037 78.302  102.737 1.00 21.39 ? 708  PHE A CE1   1 
ATOM   5134  C  CE2   . PHE A 1  710  ? -22.703 78.061  103.212 1.00 21.53 ? 708  PHE A CE2   1 
ATOM   5135  C  CZ    . PHE A 1  710  ? -23.741 78.092  102.297 1.00 23.09 ? 708  PHE A CZ    1 
ATOM   5136  N  N     . PRO A 1  711  ? -26.924 80.524  108.701 1.00 19.81 ? 709  PRO A N     1 
ATOM   5137  C  CA    . PRO A 1  711  ? -27.038 81.061  110.063 1.00 21.09 ? 709  PRO A CA    1 
ATOM   5138  C  C     . PRO A 1  711  ? -27.290 80.022  111.135 1.00 20.65 ? 709  PRO A C     1 
ATOM   5139  O  O     . PRO A 1  711  ? -27.149 80.335  112.325 1.00 20.71 ? 709  PRO A O     1 
ATOM   5140  C  CB    . PRO A 1  711  ? -28.227 82.021  109.948 1.00 21.57 ? 709  PRO A CB    1 
ATOM   5141  C  CG    . PRO A 1  711  ? -29.089 81.387  108.896 1.00 19.37 ? 709  PRO A CG    1 
ATOM   5142  C  CD    . PRO A 1  711  ? -28.102 80.854  107.876 1.00 18.11 ? 709  PRO A CD    1 
ATOM   5143  N  N     . LEU A 1  712  ? -27.663 78.807  110.764 1.00 21.76 ? 710  LEU A N     1 
ATOM   5144  C  CA    . LEU A 1  712  ? -27.756 77.718  111.720 1.00 20.98 ? 710  LEU A CA    1 
ATOM   5145  C  C     . LEU A 1  712  ? -26.669 76.679  111.520 1.00 21.35 ? 710  LEU A C     1 
ATOM   5146  O  O     . LEU A 1  712  ? -26.079 76.226  112.498 1.00 20.50 ? 710  LEU A O     1 
ATOM   5147  C  CB    . LEU A 1  712  ? -29.132 77.041  111.635 1.00 21.32 ? 710  LEU A CB    1 
ATOM   5148  C  CG    . LEU A 1  712  ? -29.317 75.918  112.664 1.00 23.21 ? 710  LEU A CG    1 
ATOM   5149  C  CD1   . LEU A 1  712  ? -29.265 76.477  114.086 1.00 23.61 ? 710  LEU A CD1   1 
ATOM   5150  C  CD2   . LEU A 1  712  ? -30.616 75.153  112.416 1.00 23.10 ? 710  LEU A CD2   1 
ATOM   5151  N  N     . ALA A 1  713  ? -26.358 76.327  110.269 1.00 19.65 ? 711  ALA A N     1 
ATOM   5152  C  CA    . ALA A 1  713  ? -25.465 75.198  110.012 1.00 18.19 ? 711  ALA A CA    1 
ATOM   5153  C  C     . ALA A 1  713  ? -24.035 75.512  110.432 1.00 19.97 ? 711  ALA A C     1 
ATOM   5154  O  O     . ALA A 1  713  ? -23.444 74.790  111.243 1.00 19.96 ? 711  ALA A O     1 
ATOM   5155  C  CB    . ALA A 1  713  ? -25.516 74.811  108.533 1.00 20.14 ? 711  ALA A CB    1 
ATOM   5156  N  N     . ILE A 1  714  ? -23.442 76.566  109.869 1.00 20.56 ? 712  ILE A N     1 
ATOM   5157  C  CA    . ILE A 1  714  ? -22.054 76.869  110.221 1.00 18.06 ? 712  ILE A CA    1 
ATOM   5158  C  C     . ILE A 1  714  ? -21.964 77.314  111.672 1.00 19.58 ? 712  ILE A C     1 
ATOM   5159  O  O     . ILE A 1  714  ? -21.019 76.960  112.394 1.00 19.98 ? 712  ILE A O     1 
ATOM   5160  C  CB    . ILE A 1  714  ? -21.466 77.909  109.253 1.00 18.60 ? 712  ILE A CB    1 
ATOM   5161  C  CG1   . ILE A 1  714  ? -21.320 77.247  107.877 1.00 20.70 ? 712  ILE A CG1   1 
ATOM   5162  C  CG2   . ILE A 1  714  ? -20.120 78.482  109.797 1.00 18.81 ? 712  ILE A CG2   1 
ATOM   5163  C  CD1   . ILE A 1  714  ? -20.383 77.923  106.949 1.00 25.46 ? 712  ILE A CD1   1 
ATOM   5164  N  N     . PHE A 1  715  ? -22.952 78.086  112.125 1.00 17.99 ? 713  PHE A N     1 
ATOM   5165  C  CA    . PHE A 1  715  ? -23.045 78.443  113.533 1.00 18.76 ? 713  PHE A CA    1 
ATOM   5166  C  C     . PHE A 1  715  ? -22.963 77.206  114.425 1.00 21.52 ? 713  PHE A C     1 
ATOM   5167  O  O     . PHE A 1  715  ? -22.116 77.125  115.325 1.00 20.01 ? 713  PHE A O     1 
ATOM   5168  C  CB    . PHE A 1  715  ? -24.356 79.204  113.762 1.00 21.36 ? 713  PHE A CB    1 
ATOM   5169  C  CG    . PHE A 1  715  ? -24.591 79.587  115.186 1.00 19.72 ? 713  PHE A CG    1 
ATOM   5170  C  CD1   . PHE A 1  715  ? -23.981 80.707  115.717 1.00 21.76 ? 713  PHE A CD1   1 
ATOM   5171  C  CD2   . PHE A 1  715  ? -25.428 78.828  115.994 1.00 22.81 ? 713  PHE A CD2   1 
ATOM   5172  C  CE1   . PHE A 1  715  ? -24.204 81.076  117.034 1.00 24.70 ? 713  PHE A CE1   1 
ATOM   5173  C  CE2   . PHE A 1  715  ? -25.654 79.185  117.306 1.00 25.38 ? 713  PHE A CE2   1 
ATOM   5174  C  CZ    . PHE A 1  715  ? -25.040 80.319  117.832 1.00 25.92 ? 713  PHE A CZ    1 
ATOM   5175  N  N     . THR A 1  716  ? -23.833 76.223  114.176 1.00 19.47 ? 714  THR A N     1 
ATOM   5176  C  CA    . THR A 1  716  ? -23.858 75.010  114.989 1.00 19.77 ? 714  THR A CA    1 
ATOM   5177  C  C     . THR A 1  716  ? -22.574 74.207  114.830 1.00 20.24 ? 714  THR A C     1 
ATOM   5178  O  O     . THR A 1  716  ? -22.022 73.704  115.819 1.00 20.24 ? 714  THR A O     1 
ATOM   5179  C  CB    . THR A 1  716  ? -25.070 74.151  114.616 1.00 22.52 ? 714  THR A CB    1 
ATOM   5180  O  OG1   . THR A 1  716  ? -26.278 74.896  114.834 1.00 20.99 ? 714  THR A OG1   1 
ATOM   5181  C  CG2   . THR A 1  716  ? -25.110 72.888  115.455 1.00 21.98 ? 714  THR A CG2   1 
ATOM   5182  N  N     . GLY A 1  717  ? -22.070 74.107  113.600 1.00 18.65 ? 715  GLY A N     1 
ATOM   5183  C  CA    . GLY A 1  717  ? -20.889 73.290  113.357 1.00 20.15 ? 715  GLY A CA    1 
ATOM   5184  C  C     . GLY A 1  717  ? -19.691 73.742  114.169 1.00 19.56 ? 715  GLY A C     1 
ATOM   5185  O  O     . GLY A 1  717  ? -19.058 72.940  114.855 1.00 19.99 ? 715  GLY A O     1 
ATOM   5186  N  N     . GLN A 1  718  ? -19.380 75.040  114.131 1.00 18.06 ? 716  GLN A N     1 
ATOM   5187  C  CA    . GLN A 1  718  ? -18.199 75.508  114.863 1.00 18.16 ? 716  GLN A CA    1 
ATOM   5188  C  C     . GLN A 1  718  ? -18.363 75.291  116.357 1.00 19.71 ? 716  GLN A C     1 
ATOM   5189  O  O     . GLN A 1  718  ? -17.447 74.811  117.032 1.00 19.19 ? 716  GLN A O     1 
ATOM   5190  C  CB    . GLN A 1  718  ? -17.933 76.988  114.589 1.00 18.12 ? 716  GLN A CB    1 
ATOM   5191  C  CG    . GLN A 1  718  ? -17.684 77.289  113.126 1.00 18.79 ? 716  GLN A CG    1 
ATOM   5192  C  CD    . GLN A 1  718  ? -17.230 78.718  112.872 1.00 20.77 ? 716  GLN A CD    1 
ATOM   5193  O  OE1   . GLN A 1  718  ? -16.274 78.941  112.133 1.00 20.13 ? 716  GLN A OE1   1 
ATOM   5194  N  NE2   . GLN A 1  718  ? -17.919 79.691  113.472 1.00 19.61 ? 716  GLN A NE2   1 
ATOM   5195  N  N     . ILE A 1  719  ? -19.530 75.661  116.892 1.00 20.31 ? 717  ILE A N     1 
ATOM   5196  C  CA    . ILE A 1  719  ? -19.756 75.566  118.324 1.00 20.19 ? 717  ILE A CA    1 
ATOM   5197  C  C     . ILE A 1  719  ? -19.741 74.118  118.783 1.00 21.95 ? 717  ILE A C     1 
ATOM   5198  O  O     . ILE A 1  719  ? -19.155 73.794  119.820 1.00 22.05 ? 717  ILE A O     1 
ATOM   5199  C  CB    . ILE A 1  719  ? -21.080 76.258  118.675 1.00 23.01 ? 717  ILE A CB    1 
ATOM   5200  C  CG1   . ILE A 1  719  ? -20.943 77.758  118.450 1.00 20.70 ? 717  ILE A CG1   1 
ATOM   5201  C  CG2   . ILE A 1  719  ? -21.492 75.926  120.099 1.00 24.67 ? 717  ILE A CG2   1 
ATOM   5202  C  CD1   . ILE A 1  719  ? -22.283 78.435  118.302 1.00 27.05 ? 717  ILE A CD1   1 
ATOM   5203  N  N     . ALA A 1  720  ? -20.396 73.230  118.031 1.00 20.25 ? 718  ALA A N     1 
ATOM   5204  C  CA    . ALA A 1  720  ? -20.445 71.819  118.400 1.00 21.29 ? 718  ALA A CA    1 
ATOM   5205  C  C     . ALA A 1  720  ? -19.045 71.224  118.455 1.00 18.51 ? 718  ALA A C     1 
ATOM   5206  O  O     . ALA A 1  720  ? -18.686 70.519  119.406 1.00 21.59 ? 718  ALA A O     1 
ATOM   5207  C  CB    . ALA A 1  720  ? -21.306 71.047  117.391 1.00 20.40 ? 718  ALA A CB    1 
ATOM   5208  N  N     . ALA A 1  721  ? -18.250 71.498  117.429 1.00 19.88 ? 719  ALA A N     1 
ATOM   5209  C  CA    . ALA A 1  721  ? -16.884 70.996  117.388 1.00 18.07 ? 719  ALA A CA    1 
ATOM   5210  C  C     . ALA A 1  721  ? -16.090 71.490  118.593 1.00 20.85 ? 719  ALA A C     1 
ATOM   5211  O  O     . ALA A 1  721  ? -15.444 70.700  119.293 1.00 20.24 ? 719  ALA A O     1 
ATOM   5212  C  CB    . ALA A 1  721  ? -16.222 71.426  116.082 1.00 17.45 ? 719  ALA A CB    1 
ATOM   5213  N  N     . ALA A 1  722  ? -16.133 72.800  118.854 1.00 17.99 ? 720  ALA A N     1 
ATOM   5214  C  CA    . ALA A 1  722  ? -15.383 73.351  119.983 1.00 19.28 ? 720  ALA A CA    1 
ATOM   5215  C  C     . ALA A 1  722  ? -15.850 72.744  121.303 1.00 22.63 ? 720  ALA A C     1 
ATOM   5216  O  O     . ALA A 1  722  ? -15.030 72.323  122.130 1.00 20.45 ? 720  ALA A O     1 
ATOM   5217  C  CB    . ALA A 1  722  ? -15.504 74.879  120.000 1.00 20.57 ? 720  ALA A CB    1 
ATOM   5218  N  N     . LEU A 1  723  ? -17.171 72.666  121.505 1.00 18.92 ? 721  LEU A N     1 
ATOM   5219  C  CA    . LEU A 1  723  ? -17.706 72.107  122.744 1.00 20.80 ? 721  LEU A CA    1 
ATOM   5220  C  C     . LEU A 1  723  ? -17.319 70.647  122.907 1.00 21.95 ? 721  LEU A C     1 
ATOM   5221  O  O     . LEU A 1  723  ? -16.934 70.208  123.997 1.00 20.81 ? 721  LEU A O     1 
ATOM   5222  C  CB    . LEU A 1  723  ? -19.229 72.232  122.758 1.00 21.37 ? 721  LEU A CB    1 
ATOM   5223  C  CG    . LEU A 1  723  ? -19.838 73.612  122.970 1.00 22.62 ? 721  LEU A CG    1 
ATOM   5224  C  CD1   . LEU A 1  723  ? -21.340 73.534  122.718 1.00 23.51 ? 721  LEU A CD1   1 
ATOM   5225  C  CD2   . LEU A 1  723  ? -19.535 74.082  124.371 1.00 24.27 ? 721  LEU A CD2   1 
ATOM   5226  N  N     . VAL A 1  724  ? -17.463 69.860  121.843 1.00 21.79 ? 722  VAL A N     1 
ATOM   5227  C  CA    . VAL A 1  724  ? -17.260 68.432  122.026 1.00 21.76 ? 722  VAL A CA    1 
ATOM   5228  C  C     . VAL A 1  724  ? -15.780 68.142  122.256 1.00 22.49 ? 722  VAL A C     1 
ATOM   5229  O  O     . VAL A 1  724  ? -15.432 67.160  122.921 1.00 23.29 ? 722  VAL A O     1 
ATOM   5230  C  CB    . VAL A 1  724  ? -17.852 67.649  120.838 1.00 20.70 ? 722  VAL A CB    1 
ATOM   5231  C  CG1   . VAL A 1  724  ? -16.895 67.646  119.621 1.00 20.77 ? 722  VAL A CG1   1 
ATOM   5232  C  CG2   . VAL A 1  724  ? -18.225 66.248  121.281 1.00 23.05 ? 722  VAL A CG2   1 
ATOM   5233  N  N     . ALA A 1  725  ? -14.893 69.004  121.746 1.00 20.88 ? 723  ALA A N     1 
ATOM   5234  C  CA    . ALA A 1  725  ? -13.467 68.898  122.035 1.00 22.53 ? 723  ALA A CA    1 
ATOM   5235  C  C     . ALA A 1  725  ? -13.127 69.332  123.453 1.00 23.46 ? 723  ALA A C     1 
ATOM   5236  O  O     . ALA A 1  725  ? -11.947 69.285  123.826 1.00 22.93 ? 723  ALA A O     1 
ATOM   5237  C  CB    . ALA A 1  725  ? -12.654 69.721  121.026 1.00 20.66 ? 723  ALA A CB    1 
ATOM   5238  N  N     . GLY A 1  726  ? -14.110 69.748  124.251 1.00 21.37 ? 724  GLY A N     1 
ATOM   5239  C  CA    . GLY A 1  726  ? -13.869 70.105  125.631 1.00 22.40 ? 724  GLY A CA    1 
ATOM   5240  C  C     . GLY A 1  726  ? -13.655 71.574  125.920 1.00 24.06 ? 724  GLY A C     1 
ATOM   5241  O  O     . GLY A 1  726  ? -13.208 71.907  127.024 1.00 27.43 ? 724  GLY A O     1 
ATOM   5242  N  N     . ASN A 1  727  ? -13.951 72.455  124.979 1.00 23.43 ? 725  ASN A N     1 
ATOM   5243  C  CA    . ASN A 1  727  ? -13.738 73.888  125.132 1.00 22.00 ? 725  ASN A CA    1 
ATOM   5244  C  C     . ASN A 1  727  ? -15.047 74.588  125.449 1.00 22.01 ? 725  ASN A C     1 
ATOM   5245  O  O     . ASN A 1  727  ? -16.054 74.337  124.766 1.00 22.16 ? 725  ASN A O     1 
ATOM   5246  C  CB    . ASN A 1  727  ? -13.155 74.479  123.852 1.00 21.93 ? 725  ASN A CB    1 
ATOM   5247  C  CG    . ASN A 1  727  ? -11.910 73.751  123.386 1.00 21.75 ? 725  ASN A CG    1 
ATOM   5248  O  OD1   . ASN A 1  727  ? -10.831 73.938  123.942 1.00 23.70 ? 725  ASN A OD1   1 
ATOM   5249  N  ND2   . ASN A 1  727  ? -12.052 72.923  122.357 1.00 22.93 ? 725  ASN A ND2   1 
ATOM   5250  N  N     . PRO A 1  728  ? -15.084 75.490  126.422 1.00 23.08 ? 726  PRO A N     1 
ATOM   5251  C  CA    . PRO A 1  728  ? -16.244 76.378  126.531 1.00 25.84 ? 726  PRO A CA    1 
ATOM   5252  C  C     . PRO A 1  728  ? -16.226 77.368  125.382 1.00 24.21 ? 726  PRO A C     1 
ATOM   5253  O  O     . PRO A 1  728  ? -15.169 77.729  124.857 1.00 26.17 ? 726  PRO A O     1 
ATOM   5254  C  CB    . PRO A 1  728  ? -16.049 77.070  127.886 1.00 23.48 ? 726  PRO A CB    1 
ATOM   5255  C  CG    . PRO A 1  728  ? -14.567 77.032  128.107 1.00 24.39 ? 726  PRO A CG    1 
ATOM   5256  C  CD    . PRO A 1  728  ? -14.049 75.793  127.428 1.00 24.50 ? 726  PRO A CD    1 
ATOM   5257  N  N     . VAL A 1  729  ? -17.415 77.792  124.973 1.00 24.93 ? 727  VAL A N     1 
ATOM   5258  C  CA    . VAL A 1  729  ? -17.592 78.525  123.731 1.00 22.74 ? 727  VAL A CA    1 
ATOM   5259  C  C     . VAL A 1  729  ? -18.249 79.866  124.012 1.00 22.74 ? 727  VAL A C     1 
ATOM   5260  O  O     . VAL A 1  729  ? -19.220 79.951  124.773 1.00 23.70 ? 727  VAL A O     1 
ATOM   5261  C  CB    . VAL A 1  729  ? -18.423 77.710  122.721 1.00 22.35 ? 727  VAL A CB    1 
ATOM   5262  C  CG1   . VAL A 1  729  ? -18.851 78.581  121.540 1.00 21.01 ? 727  VAL A CG1   1 
ATOM   5263  C  CG2   . VAL A 1  729  ? -17.612 76.514  122.248 1.00 22.39 ? 727  VAL A CG2   1 
ATOM   5264  N  N     . LEU A 1  730  ? -17.718 80.901  123.381 1.00 23.00 ? 728  LEU A N     1 
ATOM   5265  C  CA    . LEU A 1  730  ? -18.384 82.182  123.225 1.00 23.35 ? 728  LEU A CA    1 
ATOM   5266  C  C     . LEU A 1  730  ? -18.879 82.224  121.782 1.00 22.34 ? 728  LEU A C     1 
ATOM   5267  O  O     . LEU A 1  730  ? -18.075 82.246  120.843 1.00 23.02 ? 728  LEU A O     1 
ATOM   5268  C  CB    . LEU A 1  730  ? -17.440 83.344  123.530 1.00 25.25 ? 728  LEU A CB    1 
ATOM   5269  C  CG    . LEU A 1  730  ? -16.715 83.425  124.888 1.00 24.56 ? 728  LEU A CG    1 
ATOM   5270  C  CD1   . LEU A 1  730  ? -17.684 83.165  126.048 1.00 24.15 ? 728  LEU A CD1   1 
ATOM   5271  C  CD2   . LEU A 1  730  ? -15.503 82.510  124.967 1.00 26.56 ? 728  LEU A CD2   1 
ATOM   5272  N  N     . ALA A 1  731  ? -20.197 82.209  121.612 1.00 23.01 ? 729  ALA A N     1 
ATOM   5273  C  CA    . ALA A 1  731  ? -20.820 82.127  120.297 1.00 22.27 ? 729  ALA A CA    1 
ATOM   5274  C  C     . ALA A 1  731  ? -21.236 83.526  119.861 1.00 23.68 ? 729  ALA A C     1 
ATOM   5275  O  O     . ALA A 1  731  ? -22.140 84.117  120.451 1.00 27.03 ? 729  ALA A O     1 
ATOM   5276  C  CB    . ALA A 1  731  ? -22.024 81.188  120.335 1.00 24.40 ? 729  ALA A CB    1 
ATOM   5277  N  N     . LYS A 1  732  ? -20.584 84.052  118.826 1.00 21.97 ? 730  LYS A N     1 
ATOM   5278  C  CA    . LYS A 1  732  ? -20.925 85.376  118.311 1.00 22.62 ? 730  LYS A CA    1 
ATOM   5279  C  C     . LYS A 1  732  ? -21.558 85.221  116.931 1.00 23.21 ? 730  LYS A C     1 
ATOM   5280  O  O     . LYS A 1  732  ? -20.838 85.122  115.923 1.00 22.29 ? 730  LYS A O     1 
ATOM   5281  C  CB    . LYS A 1  732  ? -19.678 86.260  118.244 1.00 24.76 ? 730  LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1  732  ? -19.913 87.713  118.590 1.00 23.56 ? 730  LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1  732  ? -20.895 88.353  117.606 1.00 25.98 ? 730  LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1  732  ? -20.272 88.534  116.233 1.00 26.11 ? 730  LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1  732  ? -21.295 89.085  115.273 1.00 25.05 ? 730  LYS A NZ    1 
ATOM   5286  N  N     . PRO A 1  733  ? -22.881 85.191  116.826 1.00 22.32 ? 731  PRO A N     1 
ATOM   5287  C  CA    . PRO A 1  733  ? -23.514 85.052  115.514 1.00 23.97 ? 731  PRO A CA    1 
ATOM   5288  C  C     . PRO A 1  733  ? -23.466 86.356  114.734 1.00 22.36 ? 731  PRO A C     1 
ATOM   5289  O  O     . PRO A 1  733  ? -23.327 87.450  115.287 1.00 23.90 ? 731  PRO A O     1 
ATOM   5290  C  CB    . PRO A 1  733  ? -24.961 84.693  115.862 1.00 24.40 ? 731  PRO A CB    1 
ATOM   5291  C  CG    . PRO A 1  733  ? -25.201 85.412  117.139 1.00 21.87 ? 731  PRO A CG    1 
ATOM   5292  C  CD    . PRO A 1  733  ? -23.878 85.336  117.904 1.00 23.94 ? 731  PRO A CD    1 
ATOM   5293  N  N     . ALA A 1  734  ? -23.601 86.217  113.424 1.00 21.96 ? 732  ALA A N     1 
ATOM   5294  C  CA    . ALA A 1  734  ? -23.685 87.384  112.564 1.00 24.42 ? 732  ALA A CA    1 
ATOM   5295  C  C     . ALA A 1  734  ? -24.800 88.312  113.031 1.00 22.99 ? 732  ALA A C     1 
ATOM   5296  O  O     . ALA A 1  734  ? -25.866 87.866  113.466 1.00 26.25 ? 732  ALA A O     1 
ATOM   5297  C  CB    . ALA A 1  734  ? -23.941 86.945  111.127 1.00 21.29 ? 732  ALA A CB    1 
ATOM   5298  N  N     . GLU A 1  735  ? -24.565 89.615  112.920 1.00 24.34 ? 733  GLU A N     1 
ATOM   5299  C  CA    . GLU A 1  735  ? -25.569 90.566  113.385 1.00 26.10 ? 733  GLU A CA    1 
ATOM   5300  C  C     . GLU A 1  735  ? -26.873 90.457  112.601 1.00 23.78 ? 733  GLU A C     1 
ATOM   5301  O  O     . GLU A 1  735  ? -27.930 90.813  113.131 1.00 25.22 ? 733  GLU A O     1 
ATOM   5302  C  CB    . GLU A 1  735  ? -25.028 91.993  113.313 1.00 26.25 ? 733  GLU A CB    1 
ATOM   5303  C  CG    . GLU A 1  735  ? -24.508 92.410  111.942 1.00 29.75 ? 733  GLU A CG    1 
ATOM   5304  C  CD    . GLU A 1  735  ? -23.011 92.168  111.763 1.00 32.14 ? 733  GLU A CD    1 
ATOM   5305  O  OE1   . GLU A 1  735  ? -22.475 91.223  112.378 1.00 28.48 ? 733  GLU A OE1   1 
ATOM   5306  O  OE2   . GLU A 1  735  ? -22.373 92.927  111.005 1.00 27.98 ? 733  GLU A OE2   1 
ATOM   5307  N  N     . GLU A 1  736  ? -26.827 89.947  111.367 1.00 25.60 ? 734  GLU A N     1 
ATOM   5308  C  CA    . GLU A 1  736  ? -28.040 89.868  110.559 1.00 24.07 ? 734  GLU A CA    1 
ATOM   5309  C  C     . GLU A 1  736  ? -28.966 88.743  111.010 1.00 26.72 ? 734  GLU A C     1 
ATOM   5310  O  O     . GLU A 1  736  ? -30.179 88.823  110.784 1.00 25.96 ? 734  GLU A O     1 
ATOM   5311  C  CB    . GLU A 1  736  ? -27.690 89.676  109.081 1.00 25.26 ? 734  GLU A CB    1 
ATOM   5312  C  CG    . GLU A 1  736  ? -26.889 90.803  108.456 1.00 26.18 ? 734  GLU A CG    1 
ATOM   5313  C  CD    . GLU A 1  736  ? -25.394 90.558  108.524 1.00 27.73 ? 734  GLU A CD    1 
ATOM   5314  O  OE1   . GLU A 1  736  ? -24.965 89.694  109.326 1.00 26.09 ? 734  GLU A OE1   1 
ATOM   5315  O  OE2   . GLU A 1  736  ? -24.649 91.212  107.757 1.00 29.38 ? 734  GLU A OE2   1 
ATOM   5316  N  N     . THR A 1  737  ? -28.431 87.680  111.615 1.00 24.59 ? 735  THR A N     1 
ATOM   5317  C  CA    . THR A 1  737  ? -29.195 86.454  111.870 1.00 23.17 ? 735  THR A CA    1 
ATOM   5318  C  C     . THR A 1  737  ? -29.014 85.941  113.301 1.00 25.49 ? 735  THR A C     1 
ATOM   5319  O  O     . THR A 1  737  ? -28.623 84.787  113.512 1.00 21.18 ? 735  THR A O     1 
ATOM   5320  C  CB    . THR A 1  737  ? -28.798 85.371  110.865 1.00 21.54 ? 735  THR A CB    1 
ATOM   5321  O  OG1   . THR A 1  737  ? -27.370 85.185  110.879 1.00 23.75 ? 735  THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1  737  ? -29.230 85.736  109.448 1.00 20.48 ? 735  THR A CG2   1 
ATOM   5323  N  N     . PRO A 1  738  ? -29.351 86.755  114.316 1.00 23.61 ? 736  PRO A N     1 
ATOM   5324  C  CA    . PRO A 1  738  ? -29.175 86.300  115.706 1.00 24.65 ? 736  PRO A CA    1 
ATOM   5325  C  C     . PRO A 1  738  ? -30.253 85.354  116.202 1.00 25.35 ? 736  PRO A C     1 
ATOM   5326  O  O     . PRO A 1  738  ? -30.005 84.624  117.174 1.00 26.35 ? 736  PRO A O     1 
ATOM   5327  C  CB    . PRO A 1  738  ? -29.220 87.609  116.505 1.00 27.35 ? 736  PRO A CB    1 
ATOM   5328  C  CG    . PRO A 1  738  ? -30.204 88.439  115.716 1.00 25.76 ? 736  PRO A CG    1 
ATOM   5329  C  CD    . PRO A 1  738  ? -29.904 88.124  114.266 1.00 23.96 ? 736  PRO A CD    1 
ATOM   5330  N  N     . LEU A 1  739  ? -31.446 85.369  115.602 1.00 22.68 ? 737  LEU A N     1 
ATOM   5331  C  CA    . LEU A 1  739  ? -32.571 84.639  116.182 1.00 24.35 ? 737  LEU A CA    1 
ATOM   5332  C  C     . LEU A 1  739  ? -32.388 83.133  116.057 1.00 22.31 ? 737  LEU A C     1 
ATOM   5333  O  O     . LEU A 1  739  ? -32.548 82.400  117.041 1.00 26.25 ? 737  LEU A O     1 
ATOM   5334  C  CB    . LEU A 1  739  ? -33.879 85.067  115.523 1.00 24.41 ? 737  LEU A CB    1 
ATOM   5335  C  CG    . LEU A 1  739  ? -34.241 86.534  115.686 1.00 24.95 ? 737  LEU A CG    1 
ATOM   5336  C  CD1   . LEU A 1  739  ? -35.520 86.814  114.910 1.00 23.24 ? 737  LEU A CD1   1 
ATOM   5337  C  CD2   . LEU A 1  739  ? -34.435 86.889  117.158 1.00 25.38 ? 737  LEU A CD2   1 
ATOM   5338  N  N     . ILE A 1  740  ? -32.080 82.647  114.850 1.00 23.06 ? 738  ILE A N     1 
ATOM   5339  C  CA    . ILE A 1  740  ? -31.883 81.208  114.692 1.00 22.36 ? 738  ILE A CA    1 
ATOM   5340  C  C     . ILE A 1  740  ? -30.657 80.776  115.481 1.00 23.90 ? 738  ILE A C     1 
ATOM   5341  O  O     . ILE A 1  740  ? -30.616 79.666  116.024 1.00 24.09 ? 738  ILE A O     1 
ATOM   5342  C  CB    . ILE A 1  740  ? -31.798 80.825  113.197 1.00 22.96 ? 738  ILE A CB    1 
ATOM   5343  C  CG1   . ILE A 1  740  ? -31.757 79.303  113.006 1.00 24.69 ? 738  ILE A CG1   1 
ATOM   5344  C  CG2   . ILE A 1  740  ? -30.576 81.441  112.544 1.00 23.08 ? 738  ILE A CG2   1 
ATOM   5345  C  CD1   . ILE A 1  740  ? -33.020 78.579  113.444 1.00 25.13 ? 738  ILE A CD1   1 
ATOM   5346  N  N     . ALA A 1  741  ? -29.679 81.670  115.620 1.00 24.33 ? 739  ALA A N     1 
ATOM   5347  C  CA    . ALA A 1  741  ? -28.526 81.400  116.473 1.00 26.54 ? 739  ALA A CA    1 
ATOM   5348  C  C     . ALA A 1  741  ? -28.949 81.192  117.923 1.00 23.82 ? 739  ALA A C     1 
ATOM   5349  O  O     . ALA A 1  741  ? -28.517 80.235  118.575 1.00 24.94 ? 739  ALA A O     1 
ATOM   5350  C  CB    . ALA A 1  741  ? -27.527 82.547  116.362 1.00 24.09 ? 739  ALA A CB    1 
ATOM   5351  N  N     . ALA A 1  742  ? -29.795 82.084  118.446 1.00 24.01 ? 740  ALA A N     1 
ATOM   5352  C  CA    . ALA A 1  742  ? -30.254 81.948  119.823 1.00 24.52 ? 740  ALA A CA    1 
ATOM   5353  C  C     . ALA A 1  742  ? -31.041 80.662  120.010 1.00 25.15 ? 740  ALA A C     1 
ATOM   5354  O  O     . ALA A 1  742  ? -30.942 80.010  121.056 1.00 26.36 ? 740  ALA A O     1 
ATOM   5355  C  CB    . ALA A 1  742  ? -31.102 83.154  120.220 1.00 26.73 ? 740  ALA A CB    1 
ATOM   5356  N  N     . GLU A 1  743  ? -31.821 80.274  118.995 1.00 24.14 ? 741  GLU A N     1 
ATOM   5357  C  CA    . GLU A 1  743  ? -32.580 79.032  119.081 1.00 26.57 ? 741  GLU A CA    1 
ATOM   5358  C  C     . GLU A 1  743  ? -31.660 77.814  119.075 1.00 25.87 ? 741  GLU A C     1 
ATOM   5359  O  O     . GLU A 1  743  ? -31.898 76.849  119.812 1.00 25.30 ? 741  GLU A O     1 
ATOM   5360  C  CB    . GLU A 1  743  ? -33.594 78.963  117.938 1.00 23.71 ? 741  GLU A CB    1 
ATOM   5361  C  CG    . GLU A 1  743  ? -34.337 77.646  117.845 1.00 27.50 ? 741  GLU A CG    1 
ATOM   5362  C  CD    . GLU A 1  743  ? -35.304 77.399  118.996 1.00 28.54 ? 741  GLU A CD    1 
ATOM   5363  O  OE1   . GLU A 1  743  ? -35.504 78.295  119.851 1.00 25.89 ? 741  GLU A OE1   1 
ATOM   5364  O  OE2   . GLU A 1  743  ? -35.862 76.286  119.047 1.00 32.65 ? 741  GLU A OE2   1 
ATOM   5365  N  N     . GLY A 1  744  ? -30.594 77.845  118.267 1.00 23.04 ? 742  GLY A N     1 
ATOM   5366  C  CA    . GLY A 1  744  ? -29.635 76.754  118.293 1.00 24.13 ? 742  GLY A CA    1 
ATOM   5367  C  C     . GLY A 1  744  ? -28.945 76.620  119.639 1.00 24.35 ? 742  GLY A C     1 
ATOM   5368  O  O     . GLY A 1  744  ? -28.755 75.508  120.142 1.00 24.76 ? 742  GLY A O     1 
ATOM   5369  N  N     . VAL A 1  745  ? -28.568 77.753  120.244 1.00 22.97 ? 743  VAL A N     1 
ATOM   5370  C  CA    . VAL A 1  745  ? -27.996 77.730  121.590 1.00 27.20 ? 743  VAL A CA    1 
ATOM   5371  C  C     . VAL A 1  745  ? -29.012 77.209  122.596 1.00 27.64 ? 743  VAL A C     1 
ATOM   5372  O  O     . VAL A 1  745  ? -28.670 76.446  123.504 1.00 28.00 ? 743  VAL A O     1 
ATOM   5373  C  CB    . VAL A 1  745  ? -27.478 79.129  121.974 1.00 26.78 ? 743  VAL A CB    1 
ATOM   5374  C  CG1   . VAL A 1  745  ? -27.159 79.212  123.480 1.00 26.24 ? 743  VAL A CG1   1 
ATOM   5375  C  CG2   . VAL A 1  745  ? -26.245 79.467  121.141 1.00 27.00 ? 743  VAL A CG2   1 
ATOM   5376  N  N     . ARG A 1  746  ? -30.281 77.603  122.451 1.00 26.09 ? 744  ARG A N     1 
ATOM   5377  C  CA    . ARG A 1  746  ? -31.301 77.085  123.359 1.00 25.81 ? 744  ARG A CA    1 
ATOM   5378  C  C     . ARG A 1  746  ? -31.402 75.567  123.257 1.00 25.31 ? 744  ARG A C     1 
ATOM   5379  O  O     . ARG A 1  746  ? -31.513 74.874  124.275 1.00 28.91 ? 744  ARG A O     1 
ATOM   5380  C  CB    . ARG A 1  746  ? -32.657 77.726  123.061 1.00 26.74 ? 744  ARG A CB    1 
ATOM   5381  C  CG    . ARG A 1  746  ? -33.726 77.371  124.098 1.00 28.35 ? 744  ARG A CG    1 
ATOM   5382  C  CD    . ARG A 1  746  ? -35.145 77.605  123.566 1.00 28.45 ? 744  ARG A CD    1 
ATOM   5383  N  NE    . ARG A 1  746  ? -35.446 76.714  122.448 1.00 28.94 ? 744  ARG A NE    1 
ATOM   5384  C  CZ    . ARG A 1  746  ? -35.747 75.428  122.582 1.00 30.39 ? 744  ARG A CZ    1 
ATOM   5385  N  NH1   . ARG A 1  746  ? -35.746 74.841  123.770 1.00 31.95 ? 744  ARG A NH1   1 
ATOM   5386  N  NH2   . ARG A 1  746  ? -36.056 74.713  121.500 1.00 29.07 ? 744  ARG A NH2   1 
ATOM   5387  N  N     . ILE A 1  747  ? -31.348 75.037  122.032 1.00 24.83 ? 745  ILE A N     1 
ATOM   5388  C  CA    . ILE A 1  747  ? -31.406 73.594  121.811 1.00 25.51 ? 745  ILE A CA    1 
ATOM   5389  C  C     . ILE A 1  747  ? -30.180 72.901  122.388 1.00 25.90 ? 745  ILE A C     1 
ATOM   5390  O  O     . ILE A 1  747  ? -30.293 71.843  123.020 1.00 24.40 ? 745  ILE A O     1 
ATOM   5391  C  CB    . ILE A 1  747  ? -31.561 73.308  120.309 1.00 24.35 ? 745  ILE A CB    1 
ATOM   5392  C  CG1   . ILE A 1  747  ? -32.987 73.662  119.878 1.00 23.02 ? 745  ILE A CG1   1 
ATOM   5393  C  CG2   . ILE A 1  747  ? -31.222 71.851  119.981 1.00 23.89 ? 745  ILE A CG2   1 
ATOM   5394  C  CD1   . ILE A 1  747  ? -33.168 73.644  118.378 1.00 25.61 ? 745  ILE A CD1   1 
ATOM   5395  N  N     . LEU A 1  748  ? -28.990 73.469  122.165 1.00 24.13 ? 746  LEU A N     1 
ATOM   5396  C  CA    . LEU A 1  748  ? -27.778 72.872  122.718 1.00 24.94 ? 746  LEU A CA    1 
ATOM   5397  C  C     . LEU A 1  748  ? -27.823 72.852  124.239 1.00 25.11 ? 746  LEU A C     1 
ATOM   5398  O  O     . LEU A 1  748  ? -27.433 71.862  124.870 1.00 26.61 ? 746  LEU A O     1 
ATOM   5399  C  CB    . LEU A 1  748  ? -26.545 73.625  122.217 1.00 23.72 ? 746  LEU A CB    1 
ATOM   5400  C  CG    . LEU A 1  748  ? -26.095 73.216  120.816 1.00 25.97 ? 746  LEU A CG    1 
ATOM   5401  C  CD1   . LEU A 1  748  ? -25.166 74.264  120.228 1.00 27.93 ? 746  LEU A CD1   1 
ATOM   5402  C  CD2   . LEU A 1  748  ? -25.399 71.878  120.879 1.00 27.76 ? 746  LEU A CD2   1 
ATOM   5403  N  N     . ARG A 1  749  ? -28.320 73.929  124.847 1.00 24.64 ? 747  ARG A N     1 
ATOM   5404  C  CA    . ARG A 1  749  ? -28.448 73.953  126.300 1.00 24.79 ? 747  ARG A CA    1 
ATOM   5405  C  C     . ARG A 1  749  ? -29.494 72.954  126.784 1.00 28.09 ? 747  ARG A C     1 
ATOM   5406  O  O     . ARG A 1  749  ? -29.285 72.271  127.797 1.00 28.06 ? 747  ARG A O     1 
ATOM   5407  C  CB    . ARG A 1  749  ? -28.772 75.371  126.770 1.00 27.25 ? 747  ARG A CB    1 
ATOM   5408  C  CG    . ARG A 1  749  ? -27.572 76.308  126.743 1.00 30.22 ? 747  ARG A CG    1 
ATOM   5409  C  CD    . ARG A 1  749  ? -27.936 77.707  127.196 1.00 35.76 ? 747  ARG A CD    1 
ATOM   5410  N  NE    . ARG A 1  749  ? -26.763 78.533  127.476 1.00 34.27 ? 747  ARG A NE    1 
ATOM   5411  C  CZ    . ARG A 1  749  ? -26.811 79.642  128.203 1.00 37.01 ? 747  ARG A CZ    1 
ATOM   5412  N  NH1   . ARG A 1  749  ? -27.948 80.069  128.730 1.00 31.75 ? 747  ARG A NH1   1 
ATOM   5413  N  NH2   . ARG A 1  749  ? -25.692 80.334  128.416 1.00 32.93 ? 747  ARG A NH2   1 
ATOM   5414  N  N     . GLU A 1  750  ? -30.628 72.852  126.081 1.00 26.31 ? 748  GLU A N     1 
ATOM   5415  C  CA    . GLU A 1  750  ? -31.615 71.835  126.436 1.00 29.89 ? 748  GLU A CA    1 
ATOM   5416  C  C     . GLU A 1  750  ? -31.010 70.436  126.358 1.00 26.43 ? 748  GLU A C     1 
ATOM   5417  O  O     . GLU A 1  750  ? -31.311 69.572  127.190 1.00 28.14 ? 748  GLU A O     1 
ATOM   5418  C  CB    . GLU A 1  750  ? -32.839 71.939  125.523 1.00 25.34 ? 748  GLU A CB    1 
ATOM   5419  C  CG    . GLU A 1  750  ? -34.006 71.057  125.967 1.00 31.89 ? 748  GLU A CG    1 
ATOM   5420  C  CD    . GLU A 1  750  ? -35.128 70.978  124.943 1.00 31.60 ? 748  GLU A CD    1 
ATOM   5421  O  OE1   . GLU A 1  750  ? -35.309 71.932  124.157 1.00 37.52 ? 748  GLU A OE1   1 
ATOM   5422  O  OE2   . GLU A 1  750  ? -35.824 69.945  124.907 1.00 34.20 ? 748  GLU A OE2   1 
ATOM   5423  N  N     . ALA A 1  751  ? -30.131 70.209  125.378 1.00 24.63 ? 749  ALA A N     1 
ATOM   5424  C  CA    . ALA A 1  751  ? -29.492 68.918  125.172 1.00 24.90 ? 749  ALA A CA    1 
ATOM   5425  C  C     . ALA A 1  751  ? -28.454 68.607  126.241 1.00 27.06 ? 749  ALA A C     1 
ATOM   5426  O  O     . ALA A 1  751  ? -27.929 67.490  126.266 1.00 28.84 ? 749  ALA A O     1 
ATOM   5427  C  CB    . ALA A 1  751  ? -28.845 68.877  123.781 1.00 24.58 ? 749  ALA A CB    1 
ATOM   5428  N  N     . GLY A 1  752  ? -28.142 69.564  127.107 1.00 24.85 ? 750  GLY A N     1 
ATOM   5429  C  CA    . GLY A 1  752  ? -27.283 69.318  128.252 1.00 26.86 ? 750  GLY A CA    1 
ATOM   5430  C  C     . GLY A 1  752  ? -26.003 70.125  128.290 1.00 27.88 ? 750  GLY A C     1 
ATOM   5431  O  O     . GLY A 1  752  ? -25.246 69.985  129.257 1.00 27.35 ? 750  GLY A O     1 
ATOM   5432  N  N     . ILE A 1  753  ? -25.706 70.964  127.300 1.00 27.53 ? 751  ILE A N     1 
ATOM   5433  C  CA    . ILE A 1  753  ? -24.537 71.837  127.376 1.00 28.16 ? 751  ILE A CA    1 
ATOM   5434  C  C     . ILE A 1  753  ? -24.770 72.860  128.479 1.00 29.78 ? 751  ILE A C     1 
ATOM   5435  O  O     . ILE A 1  753  ? -25.762 73.597  128.430 1.00 27.69 ? 751  ILE A O     1 
ATOM   5436  C  CB    . ILE A 1  753  ? -24.263 72.548  126.043 1.00 24.48 ? 751  ILE A CB    1 
ATOM   5437  C  CG1   . ILE A 1  753  ? -24.106 71.538  124.907 1.00 25.27 ? 751  ILE A CG1   1 
ATOM   5438  C  CG2   . ILE A 1  753  ? -23.021 73.409  126.163 1.00 30.51 ? 751  ILE A CG2   1 
ATOM   5439  C  CD1   . ILE A 1  753  ? -22.834 70.718  124.990 1.00 22.21 ? 751  ILE A CD1   1 
ATOM   5440  N  N     . PRO A 1  754  ? -23.897 72.949  129.480 1.00 30.03 ? 752  PRO A N     1 
ATOM   5441  C  CA    . PRO A 1  754  ? -24.115 73.924  130.555 1.00 30.73 ? 752  PRO A CA    1 
ATOM   5442  C  C     . PRO A 1  754  ? -24.059 75.353  130.036 1.00 29.24 ? 752  PRO A C     1 
ATOM   5443  O  O     . PRO A 1  754  ? -23.355 75.663  129.071 1.00 26.40 ? 752  PRO A O     1 
ATOM   5444  C  CB    . PRO A 1  754  ? -22.963 73.644  131.530 1.00 32.74 ? 752  PRO A CB    1 
ATOM   5445  C  CG    . PRO A 1  754  ? -22.504 72.263  131.207 1.00 32.19 ? 752  PRO A CG    1 
ATOM   5446  C  CD    . PRO A 1  754  ? -22.725 72.099  129.734 1.00 28.04 ? 752  PRO A CD    1 
ATOM   5447  N  N     . ALA A 1  755  ? -24.812 76.231  130.706 1.00 31.59 ? 753  ALA A N     1 
ATOM   5448  C  CA    . ALA A 1  755  ? -24.789 77.649  130.361 1.00 29.90 ? 753  ALA A CA    1 
ATOM   5449  C  C     . ALA A 1  755  ? -23.384 78.227  130.453 1.00 30.55 ? 753  ALA A C     1 
ATOM   5450  O  O     . ALA A 1  755  ? -23.023 79.116  129.674 1.00 29.28 ? 753  ALA A O     1 
ATOM   5451  C  CB    . ALA A 1  755  ? -25.741 78.424  131.275 1.00 33.69 ? 753  ALA A CB    1 
ATOM   5452  N  N     . SER A 1  756  ? -22.571 77.732  131.385 1.00 30.08 ? 754  SER A N     1 
ATOM   5453  C  CA    . SER A 1  756  ? -21.209 78.224  131.485 1.00 30.28 ? 754  SER A CA    1 
ATOM   5454  C  C     . SER A 1  756  ? -20.344 77.753  130.326 1.00 29.05 ? 754  SER A C     1 
ATOM   5455  O  O     . SER A 1  756  ? -19.359 78.423  130.002 1.00 30.07 ? 754  SER A O     1 
ATOM   5456  C  CB    . SER A 1  756  ? -20.594 77.789  132.812 1.00 30.27 ? 754  SER A CB    1 
ATOM   5457  O  OG    . SER A 1  756  ? -20.467 76.381  132.886 1.00 32.79 ? 754  SER A OG    1 
ATOM   5458  N  N     . ALA A 1  757  ? -20.700 76.639  129.679 1.00 28.78 ? 755  ALA A N     1 
ATOM   5459  C  CA    . ALA A 1  757  ? -19.922 76.128  128.555 1.00 25.79 ? 755  ALA A CA    1 
ATOM   5460  C  C     . ALA A 1  757  ? -20.324 76.729  127.218 1.00 25.81 ? 755  ALA A C     1 
ATOM   5461  O  O     . ALA A 1  757  ? -19.550 76.627  126.260 1.00 26.31 ? 755  ALA A O     1 
ATOM   5462  C  CB    . ALA A 1  757  ? -20.046 74.603  128.467 1.00 27.19 ? 755  ALA A CB    1 
ATOM   5463  N  N     . LEU A 1  758  ? -21.503 77.349  127.128 1.00 25.43 ? 756  LEU A N     1 
ATOM   5464  C  CA    . LEU A 1  758  ? -22.003 77.899  125.868 1.00 24.92 ? 756  LEU A CA    1 
ATOM   5465  C  C     . LEU A 1  758  ? -22.737 79.200  126.151 1.00 27.12 ? 756  LEU A C     1 
ATOM   5466  O  O     . LEU A 1  758  ? -23.863 79.189  126.660 1.00 28.44 ? 756  LEU A O     1 
ATOM   5467  C  CB    . LEU A 1  758  ? -22.913 76.902  125.160 1.00 28.04 ? 756  LEU A CB    1 
ATOM   5468  C  CG    . LEU A 1  758  ? -23.526 77.376  123.845 1.00 25.81 ? 756  LEU A CG    1 
ATOM   5469  C  CD1   . LEU A 1  758  ? -22.466 77.910  122.884 1.00 24.19 ? 756  LEU A CD1   1 
ATOM   5470  C  CD2   . LEU A 1  758  ? -24.279 76.229  123.209 1.00 28.44 ? 756  LEU A CD2   1 
ATOM   5471  N  N     . GLN A 1  759  ? -22.092 80.312  125.832 1.00 25.96 ? 757  GLN A N     1 
ATOM   5472  C  CA    . GLN A 1  759  ? -22.650 81.638  126.011 1.00 28.71 ? 757  GLN A CA    1 
ATOM   5473  C  C     . GLN A 1  759  ? -22.894 82.265  124.649 1.00 27.28 ? 757  GLN A C     1 
ATOM   5474  O  O     . GLN A 1  759  ? -22.054 82.167  123.750 1.00 29.63 ? 757  GLN A O     1 
ATOM   5475  C  CB    . GLN A 1  759  ? -21.712 82.514  126.847 1.00 26.09 ? 757  GLN A CB    1 
ATOM   5476  C  CG    . GLN A 1  759  ? -21.515 81.997  128.252 1.00 29.90 ? 757  GLN A CG    1 
ATOM   5477  C  CD    . GLN A 1  759  ? -20.474 82.786  129.016 1.00 29.72 ? 757  GLN A CD    1 
ATOM   5478  O  OE1   . GLN A 1  759  ? -20.797 83.752  129.704 1.00 29.13 ? 757  GLN A OE1   1 
ATOM   5479  N  NE2   . GLN A 1  759  ? -19.217 82.385  128.889 1.00 27.77 ? 757  GLN A NE2   1 
ATOM   5480  N  N     . LEU A 1  760  ? -24.055 82.885  124.492 1.00 25.48 ? 758  LEU A N     1 
ATOM   5481  C  CA    . LEU A 1  760  ? -24.439 83.519  123.237 1.00 27.73 ? 758  LEU A CA    1 
ATOM   5482  C  C     . LEU A 1  760  ? -24.255 85.023  123.371 1.00 28.15 ? 758  LEU A C     1 
ATOM   5483  O  O     . LEU A 1  760  ? -24.754 85.625  124.321 1.00 29.19 ? 758  LEU A O     1 
ATOM   5484  C  CB    . LEU A 1  760  ? -25.888 83.198  122.880 1.00 26.12 ? 758  LEU A CB    1 
ATOM   5485  C  CG    . LEU A 1  760  ? -26.435 83.855  121.612 1.00 26.99 ? 758  LEU A CG    1 
ATOM   5486  C  CD1   . LEU A 1  760  ? -26.056 83.064  120.377 1.00 26.81 ? 758  LEU A CD1   1 
ATOM   5487  C  CD2   . LEU A 1  760  ? -27.941 84.003  121.704 1.00 27.86 ? 758  LEU A CD2   1 
ATOM   5488  N  N     . LEU A 1  761  ? -23.522 85.625  122.440 1.00 26.97 ? 759  LEU A N     1 
ATOM   5489  C  CA    . LEU A 1  761  ? -23.222 87.057  122.492 1.00 29.05 ? 759  LEU A CA    1 
ATOM   5490  C  C     . LEU A 1  761  ? -23.642 87.681  121.170 1.00 28.48 ? 759  LEU A C     1 
ATOM   5491  O  O     . LEU A 1  761  ? -22.828 87.814  120.247 1.00 27.36 ? 759  LEU A O     1 
ATOM   5492  C  CB    . LEU A 1  761  ? -21.741 87.317  122.764 1.00 28.98 ? 759  LEU A CB    1 
ATOM   5493  C  CG    . LEU A 1  761  ? -21.086 86.848  124.066 1.00 29.55 ? 759  LEU A CG    1 
ATOM   5494  C  CD1   . LEU A 1  761  ? -21.969 87.166  125.279 1.00 29.00 ? 759  LEU A CD1   1 
ATOM   5495  C  CD2   . LEU A 1  761  ? -20.703 85.373  124.002 1.00 31.47 ? 759  LEU A CD2   1 
ATOM   5496  N  N     . PRO A 1  762  ? -24.908 88.056  121.031 1.00 27.73 ? 760  PRO A N     1 
ATOM   5497  C  CA    . PRO A 1  762  ? -25.339 88.722  119.800 1.00 29.16 ? 760  PRO A CA    1 
ATOM   5498  C  C     . PRO A 1  762  ? -24.670 90.078  119.652 1.00 30.65 ? 760  PRO A C     1 
ATOM   5499  O  O     . PRO A 1  762  ? -24.275 90.715  120.633 1.00 32.24 ? 760  PRO A O     1 
ATOM   5500  C  CB    . PRO A 1  762  ? -26.858 88.869  119.977 1.00 27.15 ? 760  PRO A CB    1 
ATOM   5501  C  CG    . PRO A 1  762  ? -27.227 87.876  121.037 1.00 28.17 ? 760  PRO A CG    1 
ATOM   5502  C  CD    . PRO A 1  762  ? -26.029 87.807  121.953 1.00 26.24 ? 760  PRO A CD    1 
ATOM   5503  N  N     . GLY A 1  763  ? -24.540 90.510  118.413 1.00 26.73 ? 761  GLY A N     1 
ATOM   5504  C  CA    . GLY A 1  763  ? -24.000 91.823  118.126 1.00 28.97 ? 761  GLY A CA    1 
ATOM   5505  C  C     . GLY A 1  763  ? -23.213 91.806  116.832 1.00 30.03 ? 761  GLY A C     1 
ATOM   5506  O  O     . GLY A 1  763  ? -23.129 90.794  116.136 1.00 27.95 ? 761  GLY A O     1 
ATOM   5507  N  N     . ASP A 1  764  ? -22.618 92.959  116.531 1.00 31.34 ? 762  ASP A N     1 
ATOM   5508  C  CA    . ASP A 1  764  ? -21.913 93.143  115.269 1.00 31.72 ? 762  ASP A CA    1 
ATOM   5509  C  C     . ASP A 1  764  ? -20.430 92.806  115.448 1.00 31.93 ? 762  ASP A C     1 
ATOM   5510  O  O     . ASP A 1  764  ? -20.036 92.146  116.413 1.00 29.90 ? 762  ASP A O     1 
ATOM   5511  C  CB    . ASP A 1  764  ? -22.139 94.568  114.743 1.00 31.57 ? 762  ASP A CB    1 
ATOM   5512  C  CG    . ASP A 1  764  ? -21.701 95.638  115.728 1.00 35.90 ? 762  ASP A CG    1 
ATOM   5513  O  OD1   . ASP A 1  764  ? -20.686 95.443  116.426 1.00 36.25 ? 762  ASP A OD1   1 
ATOM   5514  O  OD2   . ASP A 1  764  ? -22.368 96.693  115.793 1.00 41.91 ? 762  ASP A OD2   1 
ATOM   5515  N  N     . GLY A 1  765  ? -19.593 93.266  114.517 1.00 29.19 ? 763  GLY A N     1 
ATOM   5516  C  CA    . GLY A 1  765  ? -18.179 92.938  114.537 1.00 27.27 ? 763  GLY A CA    1 
ATOM   5517  C  C     . GLY A 1  765  ? -17.445 93.426  115.767 1.00 29.38 ? 763  GLY A C     1 
ATOM   5518  O  O     . GLY A 1  765  ? -16.395 92.868  116.106 1.00 31.03 ? 763  GLY A O     1 
ATOM   5519  N  N     . ARG A 1  766  ? -17.969 94.458  116.439 1.00 32.24 ? 764  ARG A N     1 
ATOM   5520  C  CA    . ARG A 1  766  ? -17.357 94.923  117.681 1.00 32.34 ? 764  ARG A CA    1 
ATOM   5521  C  C     . ARG A 1  766  ? -17.404 93.848  118.754 1.00 30.31 ? 764  ARG A C     1 
ATOM   5522  O  O     . ARG A 1  766  ? -16.457 93.702  119.536 1.00 29.74 ? 764  ARG A O     1 
ATOM   5523  C  CB    . ARG A 1  766  ? -18.064 96.174  118.199 1.00 36.53 ? 764  ARG A CB    1 
ATOM   5524  C  CG    . ARG A 1  766  ? -17.895 97.415  117.371 1.00 42.61 ? 764  ARG A CG    1 
ATOM   5525  C  CD    . ARG A 1  766  ? -18.847 98.477  117.893 1.00 44.31 ? 764  ARG A CD    1 
ATOM   5526  N  NE    . ARG A 1  766  ? -20.240 98.068  117.742 1.00 43.55 ? 764  ARG A NE    1 
ATOM   5527  C  CZ    . ARG A 1  766  ? -21.230 98.469  118.528 1.00 44.19 ? 764  ARG A CZ    1 
ATOM   5528  N  NH1   . ARG A 1  766  ? -21.012 99.252  119.570 1.00 49.03 ? 764  ARG A NH1   1 
ATOM   5529  N  NH2   . ARG A 1  766  ? -22.472 98.072  118.263 1.00 47.93 ? 764  ARG A NH2   1 
ATOM   5530  N  N     . VAL A 1  767  ? -18.525 93.126  118.846 1.00 28.73 ? 765  VAL A N     1 
ATOM   5531  C  CA    . VAL A 1  767  ? -18.609 92.033  119.806 1.00 31.17 ? 765  VAL A CA    1 
ATOM   5532  C  C     . VAL A 1  767  ? -17.638 90.930  119.422 1.00 28.83 ? 765  VAL A C     1 
ATOM   5533  O  O     . VAL A 1  767  ? -16.944 90.371  120.277 1.00 27.42 ? 765  VAL A O     1 
ATOM   5534  C  CB    . VAL A 1  767  ? -20.053 91.511  119.908 1.00 29.57 ? 765  VAL A CB    1 
ATOM   5535  C  CG1   . VAL A 1  767  ? -20.160 90.465  121.008 1.00 27.88 ? 765  VAL A CG1   1 
ATOM   5536  C  CG2   . VAL A 1  767  ? -21.020 92.661  120.148 1.00 32.78 ? 765  VAL A CG2   1 
ATOM   5537  N  N     . GLY A 1  768  ? -17.572 90.598  118.131 1.00 28.38 ? 766  GLY A N     1 
ATOM   5538  C  CA    . GLY A 1  768  ? -16.583 89.635  117.682 1.00 24.59 ? 766  GLY A CA    1 
ATOM   5539  C  C     . GLY A 1  768  ? -15.171 90.062  118.036 1.00 26.17 ? 766  GLY A C     1 
ATOM   5540  O  O     . GLY A 1  768  ? -14.393 89.282  118.588 1.00 26.11 ? 766  GLY A O     1 
ATOM   5541  N  N     . ALA A 1  769  ? -14.833 91.318  117.737 1.00 26.90 ? 767  ALA A N     1 
ATOM   5542  C  CA    . ALA A 1  769  ? -13.478 91.805  117.980 1.00 27.61 ? 767  ALA A CA    1 
ATOM   5543  C  C     . ALA A 1  769  ? -13.159 91.825  119.468 1.00 28.02 ? 767  ALA A C     1 
ATOM   5544  O  O     . ALA A 1  769  ? -12.043 91.481  119.872 1.00 29.50 ? 767  ALA A O     1 
ATOM   5545  C  CB    . ALA A 1  769  ? -13.307 93.201  117.378 1.00 27.41 ? 767  ALA A CB    1 
ATOM   5546  N  N     . ALA A 1  770  ? -14.127 92.222  120.295 1.00 28.63 ? 768  ALA A N     1 
ATOM   5547  C  CA    . ALA A 1  770  ? -13.892 92.256  121.735 1.00 30.38 ? 768  ALA A CA    1 
ATOM   5548  C  C     . ALA A 1  770  ? -13.656 90.859  122.285 1.00 28.59 ? 768  ALA A C     1 
ATOM   5549  O  O     . ALA A 1  770  ? -12.864 90.687  123.218 1.00 28.85 ? 768  ALA A O     1 
ATOM   5550  C  CB    . ALA A 1  770  ? -15.071 92.916  122.446 1.00 28.78 ? 768  ALA A CB    1 
ATOM   5551  N  N     . LEU A 1  771  ? -14.327 89.856  121.713 1.00 26.60 ? 769  LEU A N     1 
ATOM   5552  C  CA    . LEU A 1  771  ? -14.104 88.472  122.118 1.00 26.76 ? 769  LEU A CA    1 
ATOM   5553  C  C     . LEU A 1  771  ? -12.721 87.994  121.695 1.00 28.96 ? 769  LEU A C     1 
ATOM   5554  O  O     . LEU A 1  771  ? -11.995 87.376  122.482 1.00 28.69 ? 769  LEU A O     1 
ATOM   5555  C  CB    . LEU A 1  771  ? -15.190 87.576  121.514 1.00 26.48 ? 769  LEU A CB    1 
ATOM   5556  C  CG    . LEU A 1  771  ? -16.614 87.788  122.037 1.00 26.75 ? 769  LEU A CG    1 
ATOM   5557  C  CD1   . LEU A 1  771  ? -17.602 86.951  121.215 1.00 25.25 ? 769  LEU A CD1   1 
ATOM   5558  C  CD2   . LEU A 1  771  ? -16.716 87.452  123.518 1.00 29.85 ? 769  LEU A CD2   1 
ATOM   5559  N  N     . VAL A 1  772  ? -12.343 88.267  120.444 1.00 27.02 ? 770  VAL A N     1 
ATOM   5560  C  CA    . VAL A 1  772  ? -11.028 87.859  119.957 1.00 26.04 ? 770  VAL A CA    1 
ATOM   5561  C  C     . VAL A 1  772  ? -9.925  88.466  120.817 1.00 27.93 ? 770  VAL A C     1 
ATOM   5562  O  O     . VAL A 1  772  ? -8.949  87.795  121.164 1.00 30.92 ? 770  VAL A O     1 
ATOM   5563  C  CB    . VAL A 1  772  ? -10.869 88.244  118.475 1.00 27.46 ? 770  VAL A CB    1 
ATOM   5564  C  CG1   . VAL A 1  772  ? -9.428  88.051  118.023 1.00 25.82 ? 770  VAL A CG1   1 
ATOM   5565  C  CG2   . VAL A 1  772  ? -11.798 87.406  117.613 1.00 26.46 ? 770  VAL A CG2   1 
ATOM   5566  N  N     . ALA A 1  773  ? -10.064 89.737  121.181 1.00 30.70 ? 771  ALA A N     1 
ATOM   5567  C  CA    . ALA A 1  773  ? -8.996  90.425  121.898 1.00 28.83 ? 771  ALA A CA    1 
ATOM   5568  C  C     . ALA A 1  773  ? -8.921  90.062  123.375 1.00 32.53 ? 771  ALA A C     1 
ATOM   5569  O  O     . ALA A 1  773  ? -7.939  90.436  124.030 1.00 35.28 ? 771  ALA A O     1 
ATOM   5570  C  CB    . ALA A 1  773  ? -9.163  91.938  121.759 1.00 30.14 ? 771  ALA A CB    1 
ATOM   5571  N  N     . ALA A 1  774  ? -9.916  89.362  123.921 1.00 33.46 ? 772  ALA A N     1 
ATOM   5572  C  CA    . ALA A 1  774  ? -9.958  89.122  125.362 1.00 33.29 ? 772  ALA A CA    1 
ATOM   5573  C  C     . ALA A 1  774  ? -8.834  88.188  125.797 1.00 34.04 ? 772  ALA A C     1 
ATOM   5574  O  O     . ALA A 1  774  ? -8.482  87.238  125.097 1.00 29.30 ? 772  ALA A O     1 
ATOM   5575  C  CB    . ALA A 1  774  ? -11.309 88.545  125.779 1.00 31.83 ? 772  ALA A CB    1 
ATOM   5576  N  N     . ALA A 1  775  ? -8.291  88.451  126.988 1.00 35.32 ? 773  ALA A N     1 
ATOM   5577  C  CA    . ALA A 1  775  ? -7.032  87.829  127.386 1.00 34.29 ? 773  ALA A CA    1 
ATOM   5578  C  C     . ALA A 1  775  ? -7.120  86.307  127.412 1.00 29.54 ? 773  ALA A C     1 
ATOM   5579  O  O     . ALA A 1  775  ? -6.165  85.619  127.039 1.00 32.34 ? 773  ALA A O     1 
ATOM   5580  C  CB    . ALA A 1  775  ? -6.606  88.358  128.754 1.00 34.81 ? 773  ALA A CB    1 
ATOM   5581  N  N     . GLU A 1  776  ? -8.243  85.760  127.857 1.00 31.51 ? 774  GLU A N     1 
ATOM   5582  C  CA    . GLU A 1  776  ? -8.360  84.321  128.057 1.00 27.09 ? 774  GLU A CA    1 
ATOM   5583  C  C     . GLU A 1  776  ? -8.801  83.569  126.803 1.00 28.04 ? 774  GLU A C     1 
ATOM   5584  O  O     . GLU A 1  776  ? -8.963  82.347  126.857 1.00 28.24 ? 774  GLU A O     1 
ATOM   5585  C  CB    . GLU A 1  776  ? -9.336  84.028  129.206 1.00 30.60 ? 774  GLU A CB    1 
ATOM   5586  C  CG    . GLU A 1  776  ? -8.993  84.724  130.523 1.00 34.63 ? 774  GLU A CG    1 
ATOM   5587  C  CD    . GLU A 1  776  ? -9.577  86.132  130.647 1.00 38.06 ? 774  GLU A CD    1 
ATOM   5588  O  OE1   . GLU A 1  776  ? -10.119 86.678  129.655 1.00 32.57 ? 774  GLU A OE1   1 
ATOM   5589  O  OE2   . GLU A 1  776  ? -9.493  86.699  131.757 1.00 39.73 ? 774  GLU A OE2   1 
ATOM   5590  N  N     . THR A 1  777  ? -9.001  84.258  125.684 1.00 26.86 ? 775  THR A N     1 
ATOM   5591  C  CA    . THR A 1  777  ? -9.387  83.580  124.453 1.00 27.27 ? 775  THR A CA    1 
ATOM   5592  C  C     . THR A 1  777  ? -8.261  82.674  123.994 1.00 26.13 ? 775  THR A C     1 
ATOM   5593  O  O     . THR A 1  777  ? -7.133  83.131  123.790 1.00 28.25 ? 775  THR A O     1 
ATOM   5594  C  CB    . THR A 1  777  ? -9.726  84.603  123.377 1.00 26.71 ? 775  THR A CB    1 
ATOM   5595  O  OG1   . THR A 1  777  ? -10.913 85.300  123.765 1.00 28.22 ? 775  THR A OG1   1 
ATOM   5596  C  CG2   . THR A 1  777  ? -9.940  83.897  122.022 1.00 24.48 ? 775  THR A CG2   1 
ATOM   5597  N  N     . ALA A 1  778  ? -8.562  81.382  123.875 1.00 25.64 ? 776  ALA A N     1 
ATOM   5598  C  CA    . ALA A 1  778  ? -7.555  80.370  123.608 1.00 22.92 ? 776  ALA A CA    1 
ATOM   5599  C  C     . ALA A 1  778  ? -7.587  79.863  122.179 1.00 22.61 ? 776  ALA A C     1 
ATOM   5600  O  O     . ALA A 1  778  ? -6.654  79.174  121.764 1.00 22.96 ? 776  ALA A O     1 
ATOM   5601  C  CB    . ALA A 1  778  ? -7.725  79.176  124.562 1.00 24.44 ? 776  ALA A CB    1 
ATOM   5602  N  N     . GLY A 1  779  ? -8.631  80.173  121.428 1.00 22.29 ? 777  GLY A N     1 
ATOM   5603  C  CA    . GLY A 1  779  ? -8.714  79.753  120.048 1.00 21.43 ? 777  GLY A CA    1 
ATOM   5604  C  C     . GLY A 1  779  ? -9.866  80.480  119.408 1.00 19.89 ? 777  GLY A C     1 
ATOM   5605  O  O     . GLY A 1  779  ? -10.802 80.902  120.097 1.00 23.06 ? 777  GLY A O     1 
ATOM   5606  N  N     . VAL A 1  780  ? -9.807  80.656  118.097 1.00 21.69 ? 778  VAL A N     1 
ATOM   5607  C  CA    . VAL A 1  780  ? -10.839 81.371  117.369 1.00 21.11 ? 778  VAL A CA    1 
ATOM   5608  C  C     . VAL A 1  780  ? -11.242 80.525  116.169 1.00 20.34 ? 778  VAL A C     1 
ATOM   5609  O  O     . VAL A 1  780  ? -10.381 80.032  115.431 1.00 20.08 ? 778  VAL A O     1 
ATOM   5610  C  CB    . VAL A 1  780  ? -10.362 82.766  116.924 1.00 23.41 ? 778  VAL A CB    1 
ATOM   5611  C  CG1   . VAL A 1  780  ? -11.417 83.421  116.062 1.00 20.97 ? 778  VAL A CG1   1 
ATOM   5612  C  CG2   . VAL A 1  780  ? -10.034 83.633  118.136 1.00 22.98 ? 778  VAL A CG2   1 
ATOM   5613  N  N     . MET A 1  781  ? -12.546 80.326  116.000 1.00 20.77 ? 779  MET A N     1 
ATOM   5614  C  CA    . MET A 1  781  ? -13.091 79.677  114.811 1.00 19.79 ? 779  MET A CA    1 
ATOM   5615  C  C     . MET A 1  781  ? -13.920 80.730  114.093 1.00 19.72 ? 779  MET A C     1 
ATOM   5616  O  O     . MET A 1  781  ? -14.935 81.191  114.624 1.00 19.44 ? 779  MET A O     1 
ATOM   5617  C  CB    . MET A 1  781  ? -13.934 78.458  115.174 1.00 20.25 ? 779  MET A CB    1 
ATOM   5618  C  CG    . MET A 1  781  ? -13.212 77.453  116.045 1.00 21.28 ? 779  MET A CG    1 
ATOM   5619  S  SD    . MET A 1  781  ? -14.296 76.173  116.679 1.00 21.16 ? 779  MET A SD    1 
ATOM   5620  C  CE    . MET A 1  781  ? -14.583 75.239  115.170 1.00 17.69 ? 779  MET A CE    1 
ATOM   5621  N  N     . PHE A 1  782  ? -13.470 81.116  112.904 1.00 20.78 ? 780  PHE A N     1 
ATOM   5622  C  CA    . PHE A 1  782  ? -14.082 82.168  112.113 1.00 20.22 ? 780  PHE A CA    1 
ATOM   5623  C  C     . PHE A 1  782  ? -14.508 81.620  110.763 1.00 19.95 ? 780  PHE A C     1 
ATOM   5624  O  O     . PHE A 1  782  ? -13.719 80.977  110.064 1.00 18.92 ? 780  PHE A O     1 
ATOM   5625  C  CB    . PHE A 1  782  ? -13.114 83.330  111.883 1.00 19.76 ? 780  PHE A CB    1 
ATOM   5626  C  CG    . PHE A 1  782  ? -13.659 84.387  110.970 1.00 19.96 ? 780  PHE A CG    1 
ATOM   5627  C  CD1   . PHE A 1  782  ? -14.508 85.362  111.471 1.00 21.44 ? 780  PHE A CD1   1 
ATOM   5628  C  CD2   . PHE A 1  782  ? -13.348 84.397  109.613 1.00 18.78 ? 780  PHE A CD2   1 
ATOM   5629  C  CE1   . PHE A 1  782  ? -15.027 86.335  110.658 1.00 21.31 ? 780  PHE A CE1   1 
ATOM   5630  C  CE2   . PHE A 1  782  ? -13.861 85.369  108.786 1.00 21.35 ? 780  PHE A CE2   1 
ATOM   5631  C  CZ    . PHE A 1  782  ? -14.704 86.343  109.306 1.00 19.73 ? 780  PHE A CZ    1 
ATOM   5632  N  N     . THR A 1  783  ? -15.741 81.916  110.384 1.00 19.39 ? 781  THR A N     1 
ATOM   5633  C  CA    . THR A 1  783  ? -16.190 81.731  109.014 1.00 21.46 ? 781  THR A CA    1 
ATOM   5634  C  C     . THR A 1  783  ? -16.818 83.045  108.582 1.00 17.92 ? 781  THR A C     1 
ATOM   5635  O  O     . THR A 1  783  ? -17.637 83.602  109.307 1.00 20.12 ? 781  THR A O     1 
ATOM   5636  C  CB    . THR A 1  783  ? -17.174 80.562  108.908 1.00 19.18 ? 781  THR A CB    1 
ATOM   5637  O  OG1   . THR A 1  783  ? -16.552 79.372  109.417 1.00 20.91 ? 781  THR A OG1   1 
ATOM   5638  C  CG2   . THR A 1  783  ? -17.577 80.337  107.452 1.00 18.51 ? 781  THR A CG2   1 
ATOM   5639  N  N     . GLY A 1  784  ? -16.401 83.561  107.432 1.00 19.99 ? 782  GLY A N     1 
ATOM   5640  C  CA    . GLY A 1  784  ? -16.814 84.892  107.027 1.00 20.83 ? 782  GLY A CA    1 
ATOM   5641  C  C     . GLY A 1  784  ? -15.943 85.377  105.885 1.00 20.10 ? 782  GLY A C     1 
ATOM   5642  O  O     . GLY A 1  784  ? -15.265 84.585  105.233 1.00 22.20 ? 782  GLY A O     1 
ATOM   5643  N  N     . SER A 1  785  ? -15.959 86.684  105.663 1.00 20.38 ? 783  SER A N     1 
ATOM   5644  C  CA    . SER A 1  785  ? -15.199 87.248  104.558 1.00 20.68 ? 783  SER A CA    1 
ATOM   5645  C  C     . SER A 1  785  ? -13.694 87.180  104.817 1.00 23.23 ? 783  SER A C     1 
ATOM   5646  O  O     . SER A 1  785  ? -13.223 87.219  105.959 1.00 22.45 ? 783  SER A O     1 
ATOM   5647  C  CB    . SER A 1  785  ? -15.620 88.697  104.313 1.00 22.86 ? 783  SER A CB    1 
ATOM   5648  O  OG    . SER A 1  785  ? -15.343 89.504  105.441 1.00 24.32 ? 783  SER A OG    1 
ATOM   5649  N  N     . THR A 1  786  ? -12.933 87.085  103.727 1.00 22.34 ? 784  THR A N     1 
ATOM   5650  C  CA    . THR A 1  786  ? -11.479 87.078  103.841 1.00 24.30 ? 784  THR A CA    1 
ATOM   5651  C  C     . THR A 1  786  ? -10.964 88.350  104.502 1.00 22.73 ? 784  THR A C     1 
ATOM   5652  O  O     . THR A 1  786  ? -10.019 88.311  105.304 1.00 22.65 ? 784  THR A O     1 
ATOM   5653  C  CB    . THR A 1  786  ? -10.872 86.896  102.452 1.00 24.91 ? 784  THR A CB    1 
ATOM   5654  O  OG1   . THR A 1  786  ? -11.433 85.717  101.861 1.00 23.00 ? 784  THR A OG1   1 
ATOM   5655  C  CG2   . THR A 1  786  ? -9.353  86.770  102.539 1.00 25.61 ? 784  THR A CG2   1 
ATOM   5656  N  N     . GLU A 1  787  ? -11.594 89.489  104.195 1.00 27.82 ? 785  GLU A N     1 
ATOM   5657  C  CA    . GLU A 1  787  ? -11.154 90.770  104.740 1.00 25.64 ? 785  GLU A CA    1 
ATOM   5658  C  C     . GLU A 1  787  ? -11.310 90.815  106.254 1.00 23.53 ? 785  GLU A C     1 
ATOM   5659  O  O     . GLU A 1  787  ? -10.434 91.321  106.962 1.00 24.20 ? 785  GLU A O     1 
ATOM   5660  C  CB    . GLU A 1  787  ? -11.941 91.917  104.093 1.00 28.29 ? 785  GLU A CB    1 
ATOM   5661  C  CG    . GLU A 1  787  ? -11.733 92.092  102.584 1.00 34.39 ? 785  GLU A CG    1 
ATOM   5662  C  CD    . GLU A 1  787  ? -12.223 90.906  101.758 1.00 33.72 ? 785  GLU A CD    1 
ATOM   5663  O  OE1   . GLU A 1  787  ? -13.216 90.257  102.152 1.00 33.23 ? 785  GLU A OE1   1 
ATOM   5664  O  OE2   . GLU A 1  787  ? -11.600 90.612  100.712 1.00 42.09 ? 785  GLU A OE2   1 
ATOM   5665  N  N     . VAL A 1  788  ? -12.428 90.305  106.771 1.00 24.39 ? 786  VAL A N     1 
ATOM   5666  C  CA    . VAL A 1  788  ? -12.603 90.289  108.220 1.00 23.66 ? 786  VAL A CA    1 
ATOM   5667  C  C     . VAL A 1  788  ? -11.640 89.298  108.860 1.00 22.29 ? 786  VAL A C     1 
ATOM   5668  O  O     . VAL A 1  788  ? -11.072 89.566  109.924 1.00 23.04 ? 786  VAL A O     1 
ATOM   5669  C  CB    . VAL A 1  788  ? -14.064 89.980  108.588 1.00 22.52 ? 786  VAL A CB    1 
ATOM   5670  C  CG1   . VAL A 1  788  ? -14.183 89.711  110.082 1.00 23.02 ? 786  VAL A CG1   1 
ATOM   5671  C  CG2   . VAL A 1  788  ? -14.962 91.155  108.194 1.00 26.87 ? 786  VAL A CG2   1 
ATOM   5672  N  N     . ALA A 1  789  ? -11.443 88.136  108.233 1.00 21.26 ? 787  ALA A N     1 
ATOM   5673  C  CA    . ALA A 1  789  ? -10.491 87.178  108.784 1.00 19.89 ? 787  ALA A CA    1 
ATOM   5674  C  C     . ALA A 1  789  ? -9.107  87.794  108.894 1.00 21.66 ? 787  ALA A C     1 
ATOM   5675  O  O     . ALA A 1  789  ? -8.386  87.547  109.863 1.00 21.76 ? 787  ALA A O     1 
ATOM   5676  C  CB    . ALA A 1  789  ? -10.445 85.917  107.926 1.00 19.61 ? 787  ALA A CB    1 
ATOM   5677  N  N     . ARG A 1  790  ? -8.732  88.627  107.920 1.00 23.88 ? 788  ARG A N     1 
ATOM   5678  C  CA    . ARG A 1  790  ? -7.434  89.284  107.958 1.00 21.29 ? 788  ARG A CA    1 
ATOM   5679  C  C     . ARG A 1  790  ? -7.326  90.246  109.138 1.00 20.44 ? 788  ARG A C     1 
ATOM   5680  O  O     . ARG A 1  790  ? -6.253  90.377  109.734 1.00 23.26 ? 788  ARG A O     1 
ATOM   5681  C  CB    . ARG A 1  790  ? -7.202  90.001  106.627 1.00 24.24 ? 788  ARG A CB    1 
ATOM   5682  C  CG    . ARG A 1  790  ? -5.808  90.568  106.439 1.00 25.13 ? 788  ARG A CG    1 
ATOM   5683  C  CD    . ARG A 1  790  ? -5.618  91.099  105.011 1.00 26.57 ? 788  ARG A CD    1 
ATOM   5684  N  NE    . ARG A 1  790  ? -5.581  90.024  104.028 1.00 24.12 ? 788  ARG A NE    1 
ATOM   5685  C  CZ    . ARG A 1  790  ? -6.387  89.907  102.978 1.00 25.62 ? 788  ARG A CZ    1 
ATOM   5686  N  NH1   . ARG A 1  790  ? -7.328  90.800  102.718 1.00 26.64 ? 788  ARG A NH1   1 
ATOM   5687  N  NH2   . ARG A 1  790  ? -6.239  88.864  102.164 1.00 25.74 ? 788  ARG A NH2   1 
ATOM   5688  N  N     . LEU A 1  791  ? -8.436  90.901  109.509 1.00 21.97 ? 789  LEU A N     1 
ATOM   5689  C  CA    . LEU A 1  791  ? -8.424  91.737  110.702 1.00 23.40 ? 789  LEU A CA    1 
ATOM   5690  C  C     . LEU A 1  791  ? -8.267  90.895  111.959 1.00 25.85 ? 789  LEU A C     1 
ATOM   5691  O  O     . LEU A 1  791  ? -7.527  91.269  112.872 1.00 23.34 ? 789  LEU A O     1 
ATOM   5692  C  CB    . LEU A 1  791  ? -9.702  92.573  110.772 1.00 23.93 ? 789  LEU A CB    1 
ATOM   5693  C  CG    . LEU A 1  791  ? -9.898  93.631  109.679 1.00 28.47 ? 789  LEU A CG    1 
ATOM   5694  C  CD1   . LEU A 1  791  ? -11.308 94.191  109.685 1.00 28.70 ? 789  LEU A CD1   1 
ATOM   5695  C  CD2   . LEU A 1  791  ? -8.884  94.731  109.882 1.00 28.45 ? 789  LEU A CD2   1 
ATOM   5696  N  N     . ILE A 1  792  ? -8.937  89.743  112.017 1.00 22.26 ? 790  ILE A N     1 
ATOM   5697  C  CA    . ILE A 1  792  ? -8.771  88.869  113.178 1.00 22.74 ? 790  ILE A CA    1 
ATOM   5698  C  C     . ILE A 1  792  ? -7.350  88.319  113.243 1.00 24.60 ? 790  ILE A C     1 
ATOM   5699  O  O     . ILE A 1  792  ? -6.734  88.276  114.317 1.00 25.48 ? 790  ILE A O     1 
ATOM   5700  C  CB    . ILE A 1  792  ? -9.824  87.749  113.148 1.00 22.34 ? 790  ILE A CB    1 
ATOM   5701  C  CG1   . ILE A 1  792  ? -11.200 88.346  113.417 1.00 22.87 ? 790  ILE A CG1   1 
ATOM   5702  C  CG2   . ILE A 1  792  ? -9.483  86.651  114.151 1.00 24.17 ? 790  ILE A CG2   1 
ATOM   5703  C  CD1   . ILE A 1  792  ? -12.336 87.428  113.045 1.00 22.35 ? 790  ILE A CD1   1 
ATOM   5704  N  N     . GLN A 1  793  ? -6.804  87.902  112.101 1.00 24.32 ? 791  GLN A N     1 
ATOM   5705  C  CA    . GLN A 1  793  ? -5.421  87.448  112.050 1.00 23.90 ? 791  GLN A CA    1 
ATOM   5706  C  C     . GLN A 1  793  ? -4.475  88.512  112.600 1.00 23.98 ? 791  GLN A C     1 
ATOM   5707  O  O     . GLN A 1  793  ? -3.570  88.204  113.380 1.00 25.83 ? 791  GLN A O     1 
ATOM   5708  C  CB    . GLN A 1  793  ? -5.063  87.075  110.608 1.00 23.40 ? 791  GLN A CB    1 
ATOM   5709  C  CG    . GLN A 1  793  ? -3.605  86.728  110.378 1.00 22.78 ? 791  GLN A CG    1 
ATOM   5710  C  CD    . GLN A 1  793  ? -3.216  86.806  108.900 1.00 24.13 ? 791  GLN A CD    1 
ATOM   5711  O  OE1   . GLN A 1  793  ? -3.661  87.705  108.174 1.00 26.91 ? 791  GLN A OE1   1 
ATOM   5712  N  NE2   . GLN A 1  793  ? -2.391  85.859  108.448 1.00 27.22 ? 791  GLN A NE2   1 
ATOM   5713  N  N     . ALA A 1  794  ? -4.696  89.779  112.232 1.00 22.79 ? 792  ALA A N     1 
ATOM   5714  C  CA    . ALA A 1  794  ? -3.845  90.852  112.739 1.00 25.94 ? 792  ALA A CA    1 
ATOM   5715  C  C     . ALA A 1  794  ? -3.989  91.015  114.247 1.00 25.79 ? 792  ALA A C     1 
ATOM   5716  O  O     . ALA A 1  794  ? -2.995  91.232  114.949 1.00 27.24 ? 792  ALA A O     1 
ATOM   5717  C  CB    . ALA A 1  794  ? -4.177  92.159  112.026 1.00 25.70 ? 792  ALA A CB    1 
ATOM   5718  N  N     . GLN A 1  795  ? -5.215  90.919  114.764 1.00 26.60 ? 793  GLN A N     1 
ATOM   5719  C  CA    . GLN A 1  795  ? -5.413  91.063  116.204 1.00 28.22 ? 793  GLN A CA    1 
ATOM   5720  C  C     . GLN A 1  795  ? -4.733  89.934  116.972 1.00 29.60 ? 793  GLN A C     1 
ATOM   5721  O  O     . GLN A 1  795  ? -4.137  90.167  118.030 1.00 31.46 ? 793  GLN A O     1 
ATOM   5722  C  CB    . GLN A 1  795  ? -6.907  91.118  116.526 1.00 30.28 ? 793  GLN A CB    1 
ATOM   5723  N  N     . LEU A 1  796  ? -4.796  88.707  116.451 1.00 27.35 ? 794  LEU A N     1 
ATOM   5724  C  CA    . LEU A 1  796  ? -4.178  87.572  117.129 1.00 27.13 ? 794  LEU A CA    1 
ATOM   5725  C  C     . LEU A 1  796  ? -2.661  87.575  117.015 1.00 28.28 ? 794  LEU A C     1 
ATOM   5726  O  O     . LEU A 1  796  ? -1.985  86.938  117.833 1.00 32.75 ? 794  LEU A O     1 
ATOM   5727  C  CB    . LEU A 1  796  ? -4.732  86.255  116.567 1.00 26.04 ? 794  LEU A CB    1 
ATOM   5728  C  CG    . LEU A 1  796  ? -6.182  85.904  116.910 1.00 26.28 ? 794  LEU A CG    1 
ATOM   5729  C  CD1   . LEU A 1  796  ? -6.600  84.582  116.273 1.00 26.39 ? 794  LEU A CD1   1 
ATOM   5730  C  CD2   . LEU A 1  796  ? -6.370  85.864  118.420 1.00 30.70 ? 794  LEU A CD2   1 
ATOM   5731  N  N     . ALA A 1  797  ? -2.102  88.265  116.022 1.00 29.11 ? 795  ALA A N     1 
ATOM   5732  C  CA    . ALA A 1  797  ? -0.655  88.254  115.854 1.00 28.77 ? 795  ALA A CA    1 
ATOM   5733  C  C     . ALA A 1  797  ? 0.062   88.862  117.057 1.00 34.10 ? 795  ALA A C     1 
ATOM   5734  O  O     . ALA A 1  797  ? 1.228   88.537  117.297 1.00 39.17 ? 795  ALA A O     1 
ATOM   5735  C  CB    . ALA A 1  797  ? -0.271  88.990  114.569 1.00 32.00 ? 795  ALA A CB    1 
ATOM   5736  N  N     . ASP A 1  798  ? -0.619  89.726  117.820 1.00 40.95 ? 796  ASP A N     1 
ATOM   5737  C  CA    . ASP A 1  798  ? -0.078  90.272  119.063 1.00 43.77 ? 796  ASP A CA    1 
ATOM   5738  C  C     . ASP A 1  798  ? -0.001  89.236  120.171 1.00 43.49 ? 796  ASP A C     1 
ATOM   5739  O  O     . ASP A 1  798  ? 0.726   89.446  121.147 1.00 40.17 ? 796  ASP A O     1 
ATOM   5740  C  CB    . ASP A 1  798  ? -0.952  91.422  119.581 1.00 38.77 ? 796  ASP A CB    1 
ATOM   5741  C  CG    . ASP A 1  798  ? -1.038  92.582  118.622 1.00 51.16 ? 796  ASP A CG    1 
ATOM   5742  O  OD1   . ASP A 1  798  ? -0.003  92.941  118.017 1.00 55.23 ? 796  ASP A OD1   1 
ATOM   5743  O  OD2   . ASP A 1  798  ? -2.148  93.144  118.489 1.00 51.70 ? 796  ASP A OD2   1 
ATOM   5744  N  N     . ARG A 1  799  ? -0.748  88.143  120.051 1.00 32.73 ? 797  ARG A N     1 
ATOM   5745  C  CA    . ARG A 1  799  ? -1.149  87.336  121.189 1.00 34.97 ? 797  ARG A CA    1 
ATOM   5746  C  C     . ARG A 1  799  ? -0.377  86.027  121.253 1.00 31.75 ? 797  ARG A C     1 
ATOM   5747  O  O     . ARG A 1  799  ? -0.049  85.422  120.228 1.00 30.47 ? 797  ARG A O     1 
ATOM   5748  C  CB    . ARG A 1  799  ? -2.642  87.036  121.112 1.00 37.13 ? 797  ARG A CB    1 
ATOM   5749  C  CG    . ARG A 1  799  ? -3.464  88.255  120.739 1.00 36.26 ? 797  ARG A CG    1 
ATOM   5750  C  CD    . ARG A 1  799  ? -3.755  89.041  121.966 1.00 37.89 ? 797  ARG A CD    1 
ATOM   5751  N  NE    . ARG A 1  799  ? -4.375  88.166  122.948 1.00 39.94 ? 797  ARG A NE    1 
ATOM   5752  C  CZ    . ARG A 1  799  ? -5.633  87.758  122.882 1.00 35.07 ? 797  ARG A CZ    1 
ATOM   5753  N  NH1   . ARG A 1  799  ? -6.442  88.164  121.915 1.00 36.82 ? 797  ARG A NH1   1 
ATOM   5754  N  NH2   . ARG A 1  799  ? -6.092  86.924  123.810 1.00 40.35 ? 797  ARG A NH2   1 
ATOM   5755  N  N     . LEU A 1  800  ? -0.116  85.583  122.480 1.00 30.88 ? 798  LEU A N     1 
ATOM   5756  C  CA    . LEU A 1  800  ? 0.402   84.249  122.727 1.00 29.67 ? 798  LEU A CA    1 
ATOM   5757  C  C     . LEU A 1  800  ? -0.404  83.593  123.840 1.00 29.93 ? 798  LEU A C     1 
ATOM   5758  O  O     . LEU A 1  800  ? -0.960  84.272  124.704 1.00 31.55 ? 798  LEU A O     1 
ATOM   5759  C  CB    . LEU A 1  800  ? 1.883   84.274  123.108 1.00 33.42 ? 798  LEU A CB    1 
ATOM   5760  C  CG    . LEU A 1  800  ? 2.863   84.638  121.995 1.00 32.30 ? 798  LEU A CG    1 
ATOM   5761  C  CD1   . LEU A 1  800  ? 4.228   84.958  122.602 1.00 30.90 ? 798  LEU A CD1   1 
ATOM   5762  C  CD2   . LEU A 1  800  ? 2.969   83.510  120.989 1.00 30.05 ? 798  LEU A CD2   1 
ATOM   5763  N  N     . SER A 1  801  ? -0.472  82.264  123.796 1.00 30.94 ? 799  SER A N     1 
ATOM   5764  C  CA    . SER A 1  801  ? -1.065  81.490  124.873 1.00 33.08 ? 799  SER A CA    1 
ATOM   5765  C  C     . SER A 1  801  ? -0.211  81.633  126.129 1.00 33.76 ? 799  SER A C     1 
ATOM   5766  O  O     . SER A 1  801  ? 0.932   82.088  126.060 1.00 34.03 ? 799  SER A O     1 
ATOM   5767  C  CB    . SER A 1  801  ? -1.166  80.021  124.468 1.00 33.30 ? 799  SER A CB    1 
ATOM   5768  O  OG    . SER A 1  801  ? 0.131   79.458  124.356 1.00 34.09 ? 799  SER A OG    1 
ATOM   5769  N  N     . PRO A 1  802  ? -0.732  81.239  127.297 1.00 31.87 ? 800  PRO A N     1 
ATOM   5770  C  CA    . PRO A 1  802  ? 0.129   81.216  128.493 1.00 37.10 ? 800  PRO A CA    1 
ATOM   5771  C  C     . PRO A 1  802  ? 1.379   80.377  128.304 1.00 37.24 ? 800  PRO A C     1 
ATOM   5772  O  O     . PRO A 1  802  ? 2.429   80.696  128.878 1.00 41.32 ? 800  PRO A O     1 
ATOM   5773  C  CB    . PRO A 1  802  ? -0.792  80.638  129.576 1.00 38.92 ? 800  PRO A CB    1 
ATOM   5774  C  CG    . PRO A 1  802  ? -2.167  81.017  129.135 1.00 39.35 ? 800  PRO A CG    1 
ATOM   5775  C  CD    . PRO A 1  802  ? -2.141  80.950  127.627 1.00 34.28 ? 800  PRO A CD    1 
ATOM   5776  N  N     . ALA A 1  803  ? 1.304   79.321  127.496 1.00 36.61 ? 801  ALA A N     1 
ATOM   5777  C  CA    . ALA A 1  803  ? 2.486   78.560  127.123 1.00 38.99 ? 801  ALA A CA    1 
ATOM   5778  C  C     . ALA A 1  803  ? 3.391   79.307  126.147 1.00 38.09 ? 801  ALA A C     1 
ATOM   5779  O  O     . ALA A 1  803  ? 4.465   78.795  125.826 1.00 37.73 ? 801  ALA A O     1 
ATOM   5780  C  CB    . ALA A 1  803  ? 2.070   77.220  126.512 1.00 37.10 ? 801  ALA A CB    1 
ATOM   5781  N  N     . GLY A 1  804  ? 2.991   80.482  125.669 1.00 38.30 ? 802  GLY A N     1 
ATOM   5782  C  CA    . GLY A 1  804  ? 3.803   81.223  124.723 1.00 33.60 ? 802  GLY A CA    1 
ATOM   5783  C  C     . GLY A 1  804  ? 3.745   80.727  123.294 1.00 34.05 ? 802  GLY A C     1 
ATOM   5784  O  O     . GLY A 1  804  ? 4.764   80.760  122.590 1.00 31.60 ? 802  GLY A O     1 
ATOM   5785  N  N     . ARG A 1  805  ? 2.581   80.279  122.832 1.00 30.81 ? 803  ARG A N     1 
ATOM   5786  C  CA    . ARG A 1  805  ? 2.402   79.753  121.487 1.00 30.27 ? 803  ARG A CA    1 
ATOM   5787  C  C     . ARG A 1  805  ? 1.241   80.470  120.816 1.00 26.25 ? 803  ARG A C     1 
ATOM   5788  O  O     . ARG A 1  805  ? 0.380   81.036  121.497 1.00 28.10 ? 803  ARG A O     1 
ATOM   5789  C  CB    . ARG A 1  805  ? 2.141   78.239  121.512 1.00 31.80 ? 803  ARG A CB    1 
ATOM   5790  C  CG    . ARG A 1  805  ? 3.291   77.427  122.090 1.00 34.46 ? 803  ARG A CG    1 
ATOM   5791  C  CD    . ARG A 1  805  ? 4.588   77.684  121.318 1.00 33.15 ? 803  ARG A CD    1 
ATOM   5792  N  NE    . ARG A 1  805  ? 5.717   76.941  121.874 1.00 31.50 ? 803  ARG A NE    1 
ATOM   5793  C  CZ    . ARG A 1  805  ? 6.638   77.450  122.679 1.00 33.85 ? 803  ARG A CZ    1 
ATOM   5794  N  NH1   . ARG A 1  805  ? 6.599   78.717  123.065 1.00 36.62 ? 803  ARG A NH1   1 
ATOM   5795  N  NH2   . ARG A 1  805  ? 7.619   76.666  123.119 1.00 36.80 ? 803  ARG A NH2   1 
ATOM   5796  N  N     . PRO A 1  806  ? 1.207   80.502  119.479 1.00 27.46 ? 804  PRO A N     1 
ATOM   5797  C  CA    . PRO A 1  806  ? 0.131   81.224  118.788 1.00 26.21 ? 804  PRO A CA    1 
ATOM   5798  C  C     . PRO A 1  806  ? -1.245  80.695  119.162 1.00 26.58 ? 804  PRO A C     1 
ATOM   5799  O  O     . PRO A 1  806  ? -1.436  79.498  119.391 1.00 24.53 ? 804  PRO A O     1 
ATOM   5800  C  CB    . PRO A 1  806  ? 0.426   80.969  117.305 1.00 24.91 ? 804  PRO A CB    1 
ATOM   5801  C  CG    . PRO A 1  806  ? 1.889   80.746  117.255 1.00 29.50 ? 804  PRO A CG    1 
ATOM   5802  C  CD    . PRO A 1  806  ? 2.231   80.022  118.537 1.00 27.21 ? 804  PRO A CD    1 
ATOM   5803  N  N     . ILE A 1  807  ? -2.210  81.608  119.201 1.00 23.49 ? 805  ILE A N     1 
ATOM   5804  C  CA    . ILE A 1  807  ? -3.609  81.254  119.422 1.00 23.65 ? 805  ILE A CA    1 
ATOM   5805  C  C     . ILE A 1  807  ? -4.160  80.658  118.134 1.00 23.07 ? 805  ILE A C     1 
ATOM   5806  O  O     . ILE A 1  807  ? -4.176  81.345  117.103 1.00 22.95 ? 805  ILE A O     1 
ATOM   5807  C  CB    . ILE A 1  807  ? -4.437  82.471  119.843 1.00 24.08 ? 805  ILE A CB    1 
ATOM   5808  C  CG1   . ILE A 1  807  ? -3.850  83.121  121.094 1.00 26.75 ? 805  ILE A CG1   1 
ATOM   5809  C  CG2   . ILE A 1  807  ? -5.914  82.072  120.040 1.00 23.96 ? 805  ILE A CG2   1 
ATOM   5810  C  CD1   . ILE A 1  807  ? -3.868  82.233  122.299 1.00 27.05 ? 805  ILE A CD1   1 
ATOM   5811  N  N     . PRO A 1  808  ? -4.603  79.399  118.135 1.00 22.90 ? 806  PRO A N     1 
ATOM   5812  C  CA    . PRO A 1  808  ? -5.081  78.786  116.891 1.00 21.68 ? 806  PRO A CA    1 
ATOM   5813  C  C     . PRO A 1  808  ? -6.263  79.538  116.299 1.00 21.10 ? 806  PRO A C     1 
ATOM   5814  O  O     . PRO A 1  808  ? -7.198  79.923  117.006 1.00 21.69 ? 806  PRO A O     1 
ATOM   5815  C  CB    . PRO A 1  808  ? -5.486  77.371  117.323 1.00 20.76 ? 806  PRO A CB    1 
ATOM   5816  C  CG    . PRO A 1  808  ? -4.704  77.111  118.556 1.00 23.56 ? 806  PRO A CG    1 
ATOM   5817  C  CD    . PRO A 1  808  ? -4.606  78.443  119.256 1.00 23.57 ? 806  PRO A CD    1 
ATOM   5818  N  N     . LEU A 1  809  ? -6.212  79.715  114.981 1.00 21.24 ? 807  LEU A N     1 
ATOM   5819  C  CA    . LEU A 1  809  ? -7.272  80.353  114.212 1.00 21.46 ? 807  LEU A CA    1 
ATOM   5820  C  C     . LEU A 1  809  ? -7.675  79.420  113.082 1.00 20.22 ? 807  LEU A C     1 
ATOM   5821  O  O     . LEU A 1  809  ? -6.833  79.043  112.260 1.00 20.28 ? 807  LEU A O     1 
ATOM   5822  C  CB    . LEU A 1  809  ? -6.795  81.688  113.634 1.00 22.39 ? 807  LEU A CB    1 
ATOM   5823  C  CG    . LEU A 1  809  ? -7.772  82.319  112.635 1.00 20.91 ? 807  LEU A CG    1 
ATOM   5824  C  CD1   . LEU A 1  809  ? -9.072  82.707  113.333 1.00 20.95 ? 807  LEU A CD1   1 
ATOM   5825  C  CD2   . LEU A 1  809  ? -7.133  83.522  111.978 1.00 22.36 ? 807  LEU A CD2   1 
ATOM   5826  N  N     . ILE A 1  810  ? -8.954  79.051  113.034 1.00 18.82 ? 808  ILE A N     1 
ATOM   5827  C  CA    . ILE A 1  810  ? -9.533  78.444  111.846 1.00 19.65 ? 808  ILE A CA    1 
ATOM   5828  C  C     . ILE A 1  810  ? -10.291 79.560  111.156 1.00 19.54 ? 808  ILE A C     1 
ATOM   5829  O  O     . ILE A 1  810  ? -11.184 80.160  111.759 1.00 19.55 ? 808  ILE A O     1 
ATOM   5830  C  CB    . ILE A 1  810  ? -10.465 77.269  112.184 1.00 17.47 ? 808  ILE A CB    1 
ATOM   5831  C  CG1   . ILE A 1  810  ? -9.735  76.180  112.968 1.00 19.05 ? 808  ILE A CG1   1 
ATOM   5832  C  CG2   . ILE A 1  810  ? -11.035 76.654  110.889 1.00 18.33 ? 808  ILE A CG2   1 
ATOM   5833  C  CD1   . ILE A 1  810  ? -10.607 74.976  113.263 1.00 20.49 ? 808  ILE A CD1   1 
ATOM   5834  N  N     . ALA A 1  811  ? -9.920  79.872  109.918 1.00 17.92 ? 809  ALA A N     1 
ATOM   5835  C  CA    . ALA A 1  811  ? -10.504 81.010  109.209 1.00 17.95 ? 809  ALA A CA    1 
ATOM   5836  C  C     . ALA A 1  811  ? -10.936 80.523  107.835 1.00 18.53 ? 809  ALA A C     1 
ATOM   5837  O  O     . ALA A 1  811  ? -10.104 80.338  106.941 1.00 19.46 ? 809  ALA A O     1 
ATOM   5838  C  CB    . ALA A 1  811  ? -9.521  82.164  109.098 1.00 19.56 ? 809  ALA A CB    1 
ATOM   5839  N  N     . GLU A 1  812  ? -12.232 80.305  107.677 1.00 17.23 ? 810  GLU A N     1 
ATOM   5840  C  CA    . GLU A 1  812  ? -12.787 79.752  106.452 1.00 18.07 ? 810  GLU A CA    1 
ATOM   5841  C  C     . GLU A 1  812  ? -13.505 80.885  105.740 1.00 18.04 ? 810  GLU A C     1 
ATOM   5842  O  O     . GLU A 1  812  ? -14.459 81.453  106.281 1.00 19.03 ? 810  GLU A O     1 
ATOM   5843  C  CB    . GLU A 1  812  ? -13.709 78.578  106.777 1.00 20.14 ? 810  GLU A CB    1 
ATOM   5844  C  CG    . GLU A 1  812  ? -12.968 77.461  107.529 1.00 17.20 ? 810  GLU A CG    1 
ATOM   5845  C  CD    . GLU A 1  812  ? -11.812 76.896  106.715 1.00 19.74 ? 810  GLU A CD    1 
ATOM   5846  O  OE1   . GLU A 1  812  ? -12.067 76.072  105.811 1.00 20.04 ? 810  GLU A OE1   1 
ATOM   5847  O  OE2   . GLU A 1  812  ? -10.649 77.284  106.956 1.00 19.34 ? 810  GLU A OE2   1 
ATOM   5848  N  N     . THR A 1  813  ? -13.019 81.241  104.554 1.00 16.89 ? 811  THR A N     1 
ATOM   5849  C  CA    . THR A 1  813  ? -13.362 82.533  103.982 1.00 18.93 ? 811  THR A CA    1 
ATOM   5850  C  C     . THR A 1  813  ? -13.932 82.437  102.569 1.00 18.37 ? 811  THR A C     1 
ATOM   5851  O  O     . THR A 1  813  ? -14.525 81.416  102.210 1.00 19.85 ? 811  THR A O     1 
ATOM   5852  C  CB    . THR A 1  813  ? -12.131 83.443  104.054 1.00 18.26 ? 811  THR A CB    1 
ATOM   5853  O  OG1   . THR A 1  813  ? -10.967 82.739  103.590 1.00 18.94 ? 811  THR A OG1   1 
ATOM   5854  C  CG2   . THR A 1  813  ? -11.891 83.823  105.499 1.00 19.01 ? 811  THR A CG2   1 
ATOM   5855  N  N     . GLY A 1  814  ? -13.776 83.497  101.771 1.00 18.08 ? 812  GLY A N     1 
ATOM   5856  C  CA    . GLY A 1  814  ? -14.525 83.634  100.537 1.00 20.53 ? 812  GLY A CA    1 
ATOM   5857  C  C     . GLY A 1  814  ? -14.034 82.748  99.400  1.00 20.36 ? 812  GLY A C     1 
ATOM   5858  O  O     . GLY A 1  814  ? -13.036 82.035  99.489  1.00 19.37 ? 812  GLY A O     1 
ATOM   5859  N  N     . GLY A 1  815  ? -14.775 82.796  98.294  1.00 18.02 ? 813  GLY A N     1 
ATOM   5860  C  CA    . GLY A 1  815  ? -14.407 82.043  97.116  1.00 18.81 ? 813  GLY A CA    1 
ATOM   5861  C  C     . GLY A 1  815  ? -14.599 82.874  95.864  1.00 18.54 ? 813  GLY A C     1 
ATOM   5862  O  O     . GLY A 1  815  ? -15.254 83.911  95.878  1.00 19.82 ? 813  GLY A O     1 
ATOM   5863  N  N     . GLN A 1  816  ? -13.984 82.406  94.776  1.00 18.29 ? 814  GLN A N     1 
ATOM   5864  C  CA    . GLN A 1  816  ? -14.174 82.990  93.452  1.00 17.46 ? 814  GLN A CA    1 
ATOM   5865  C  C     . GLN A 1  816  ? -14.339 81.794  92.524  1.00 16.78 ? 814  GLN A C     1 
ATOM   5866  O  O     . GLN A 1  816  ? -13.496 81.486  91.690  1.00 18.32 ? 814  GLN A O     1 
ATOM   5867  C  CB    . GLN A 1  816  ? -13.007 83.893  93.046  1.00 19.24 ? 814  GLN A CB    1 
ATOM   5868  C  CG    . GLN A 1  816  ? -13.271 84.721  91.801  1.00 21.80 ? 814  GLN A CG    1 
ATOM   5869  C  CD    . GLN A 1  816  ? -14.378 85.742  91.996  1.00 24.39 ? 814  GLN A CD    1 
ATOM   5870  O  OE1   . GLN A 1  816  ? -15.563 85.400  92.003  1.00 23.57 ? 814  GLN A OE1   1 
ATOM   5871  N  NE2   . GLN A 1  816  ? -13.995 87.006  92.165  1.00 24.84 ? 814  GLN A NE2   1 
ATOM   5872  N  N     . ASN A 1  817  ? -15.443 81.090  92.714  1.00 16.24 ? 815  ASN A N     1 
ATOM   5873  C  CA    . ASN A 1  817  ? -15.521 79.696  92.309  1.00 13.99 ? 815  ASN A CA    1 
ATOM   5874  C  C     . ASN A 1  817  ? -15.883 79.589  90.840  1.00 17.40 ? 815  ASN A C     1 
ATOM   5875  O  O     . ASN A 1  817  ? -16.822 80.236  90.372  1.00 16.63 ? 815  ASN A O     1 
ATOM   5876  C  CB    . ASN A 1  817  ? -16.547 78.972  93.171  1.00 14.17 ? 815  ASN A CB    1 
ATOM   5877  C  CG    . ASN A 1  817  ? -16.333 79.239  94.641  1.00 14.77 ? 815  ASN A CG    1 
ATOM   5878  O  OD1   . ASN A 1  817  ? -15.237 79.014  95.165  1.00 15.91 ? 815  ASN A OD1   1 
ATOM   5879  N  ND2   . ASN A 1  817  ? -17.362 79.749  95.314  1.00 15.74 ? 815  ASN A ND2   1 
ATOM   5880  N  N     . ALA A 1  818  ? -15.154 78.745  90.125  1.00 15.22 ? 816  ALA A N     1 
ATOM   5881  C  CA    . ALA A 1  818  ? -15.314 78.570  88.695  1.00 14.69 ? 816  ALA A CA    1 
ATOM   5882  C  C     . ALA A 1  818  ? -15.899 77.200  88.386  1.00 14.61 ? 816  ALA A C     1 
ATOM   5883  O  O     . ALA A 1  818  ? -15.765 76.249  89.157  1.00 14.67 ? 816  ALA A O     1 
ATOM   5884  C  CB    . ALA A 1  818  ? -13.965 78.716  87.980  1.00 16.31 ? 816  ALA A CB    1 
ATOM   5885  N  N     . MET A 1  819  ? -16.543 77.112  87.226  1.00 15.72 ? 817  MET A N     1 
ATOM   5886  C  CA    . MET A 1  819  ? -16.915 75.846  86.623  1.00 15.17 ? 817  MET A CA    1 
ATOM   5887  C  C     . MET A 1  819  ? -16.435 75.857  85.178  1.00 14.61 ? 817  MET A C     1 
ATOM   5888  O  O     . MET A 1  819  ? -16.697 76.817  84.447  1.00 15.30 ? 817  MET A O     1 
ATOM   5889  C  CB    . MET A 1  819  ? -18.431 75.619  86.666  1.00 15.50 ? 817  MET A CB    1 
ATOM   5890  C  CG    . MET A 1  819  ? -18.843 74.372  85.912  1.00 16.37 ? 817  MET A CG    1 
ATOM   5891  S  SD    . MET A 1  819  ? -20.644 74.194  85.792  1.00 16.40 ? 817  MET A SD    1 
ATOM   5892  C  CE    . MET A 1  819  ? -21.084 73.926  87.504  1.00 18.90 ? 817  MET A CE    1 
ATOM   5893  N  N     . ILE A 1  820  ? -15.730 74.806  84.767  1.00 15.57 ? 818  ILE A N     1 
ATOM   5894  C  CA    . ILE A 1  820  ? -15.259 74.679  83.392  1.00 14.53 ? 818  ILE A CA    1 
ATOM   5895  C  C     . ILE A 1  820  ? -16.144 73.672  82.673  1.00 15.11 ? 818  ILE A C     1 
ATOM   5896  O  O     . ILE A 1  820  ? -16.390 72.569  83.181  1.00 15.18 ? 818  ILE A O     1 
ATOM   5897  C  CB    . ILE A 1  820  ? -13.781 74.259  83.342  1.00 17.03 ? 818  ILE A CB    1 
ATOM   5898  C  CG1   . ILE A 1  820  ? -12.919 75.354  83.950  1.00 17.61 ? 818  ILE A CG1   1 
ATOM   5899  C  CG2   . ILE A 1  820  ? -13.366 73.998  81.906  1.00 15.90 ? 818  ILE A CG2   1 
ATOM   5900  C  CD1   . ILE A 1  820  ? -11.422 75.047  83.897  1.00 17.79 ? 818  ILE A CD1   1 
ATOM   5901  N  N     . VAL A 1  821  ? -16.638 74.060  81.500  1.00 15.65 ? 819  VAL A N     1 
ATOM   5902  C  CA    . VAL A 1  821  ? -17.544 73.243  80.708  1.00 16.67 ? 819  VAL A CA    1 
ATOM   5903  C  C     . VAL A 1  821  ? -16.931 73.092  79.327  1.00 15.91 ? 819  VAL A C     1 
ATOM   5904  O  O     . VAL A 1  821  ? -16.638 74.096  78.670  1.00 18.90 ? 819  VAL A O     1 
ATOM   5905  C  CB    . VAL A 1  821  ? -18.934 73.894  80.601  1.00 16.49 ? 819  VAL A CB    1 
ATOM   5906  C  CG1   . VAL A 1  821  ? -19.847 73.048  79.732  1.00 17.60 ? 819  VAL A CG1   1 
ATOM   5907  C  CG2   . VAL A 1  821  ? -19.522 74.122  81.993  1.00 16.37 ? 819  VAL A CG2   1 
ATOM   5908  N  N     . ASP A 1  822  ? -16.750 71.857  78.875  1.00 16.51 ? 820  ASP A N     1 
ATOM   5909  C  CA    . ASP A 1  822  ? -16.213 71.656  77.534  1.00 16.77 ? 820  ASP A CA    1 
ATOM   5910  C  C     . ASP A 1  822  ? -17.327 71.176  76.610  1.00 17.31 ? 820  ASP A C     1 
ATOM   5911  O  O     . ASP A 1  822  ? -18.488 71.063  77.006  1.00 17.54 ? 820  ASP A O     1 
ATOM   5912  C  CB    . ASP A 1  822  ? -14.989 70.723  77.551  1.00 17.54 ? 820  ASP A CB    1 
ATOM   5913  C  CG    . ASP A 1  822  ? -15.325 69.252  77.807  1.00 17.15 ? 820  ASP A CG    1 
ATOM   5914  O  OD1   . ASP A 1  822  ? -16.511 68.828  77.756  1.00 17.15 ? 820  ASP A OD1   1 
ATOM   5915  O  OD2   . ASP A 1  822  ? -14.341 68.513  78.045  1.00 18.83 ? 820  ASP A OD2   1 
ATOM   5916  N  N     . SER A 1  823  ? -16.971 70.920  75.355  1.00 18.01 ? 821  SER A N     1 
ATOM   5917  C  CA    . SER A 1  823  ? -17.972 70.610  74.344  1.00 19.11 ? 821  SER A CA    1 
ATOM   5918  C  C     . SER A 1  823  ? -18.532 69.195  74.439  1.00 20.36 ? 821  SER A C     1 
ATOM   5919  O  O     . SER A 1  823  ? -19.409 68.851  73.640  1.00 21.79 ? 821  SER A O     1 
ATOM   5920  C  CB    . SER A 1  823  ? -17.387 70.835  72.947  1.00 23.43 ? 821  SER A CB    1 
ATOM   5921  O  OG    . SER A 1  823  ? -16.265 69.989  72.734  1.00 21.85 ? 821  SER A OG    1 
ATOM   5922  N  N     . SER A 1  824  ? -18.058 68.364  75.369  1.00 17.79 ? 822  SER A N     1 
ATOM   5923  C  CA    . SER A 1  824  ? -18.641 67.043  75.564  1.00 18.99 ? 822  SER A CA    1 
ATOM   5924  C  C     . SER A 1  824  ? -19.751 67.040  76.601  1.00 21.05 ? 822  SER A C     1 
ATOM   5925  O  O     . SER A 1  824  ? -20.437 66.025  76.746  1.00 20.90 ? 822  SER A O     1 
ATOM   5926  C  CB    . SER A 1  824  ? -17.579 66.028  75.992  1.00 20.40 ? 822  SER A CB    1 
ATOM   5927  O  OG    . SER A 1  824  ? -17.138 66.259  77.324  1.00 19.29 ? 822  SER A OG    1 
ATOM   5928  N  N     . ALA A 1  825  ? -19.914 68.134  77.339  1.00 19.05 ? 823  ALA A N     1 
ATOM   5929  C  CA    . ALA A 1  825  ? -20.912 68.187  78.392  1.00 16.80 ? 823  ALA A CA    1 
ATOM   5930  C  C     . ALA A 1  825  ? -22.303 68.305  77.781  1.00 18.75 ? 823  ALA A C     1 
ATOM   5931  O  O     . ALA A 1  825  ? -22.465 68.718  76.632  1.00 20.23 ? 823  ALA A O     1 
ATOM   5932  C  CB    . ALA A 1  825  ? -20.629 69.369  79.319  1.00 17.02 ? 823  ALA A CB    1 
ATOM   5933  N  N     . LEU A 1  826  ? -23.314 67.917  78.557  1.00 18.32 ? 824  LEU A N     1 
ATOM   5934  C  CA    . LEU A 1  826  ? -24.706 67.979  78.112  1.00 21.69 ? 824  LEU A CA    1 
ATOM   5935  C  C     . LEU A 1  826  ? -25.291 69.321  78.544  1.00 20.22 ? 824  LEU A C     1 
ATOM   5936  O  O     . LEU A 1  826  ? -25.373 69.603  79.744  1.00 20.34 ? 824  LEU A O     1 
ATOM   5937  C  CB    . LEU A 1  826  ? -25.517 66.817  78.688  1.00 24.71 ? 824  LEU A CB    1 
ATOM   5938  C  CG    . LEU A 1  826  ? -26.987 66.743  78.239  1.00 28.85 ? 824  LEU A CG    1 
ATOM   5939  C  CD1   . LEU A 1  826  ? -27.082 66.682  76.711  1.00 33.26 ? 824  LEU A CD1   1 
ATOM   5940  C  CD2   . LEU A 1  826  ? -27.719 65.554  78.858  1.00 36.38 ? 824  LEU A CD2   1 
ATOM   5941  N  N     . ALA A 1  827  ? -25.693 70.143  77.567  1.00 19.25 ? 825  ALA A N     1 
ATOM   5942  C  CA    . ALA A 1  827  ? -26.048 71.531  77.856  1.00 18.61 ? 825  ALA A CA    1 
ATOM   5943  C  C     . ALA A 1  827  ? -27.149 71.628  78.910  1.00 18.55 ? 825  ALA A C     1 
ATOM   5944  O  O     . ALA A 1  827  ? -27.051 72.436  79.842  1.00 18.27 ? 825  ALA A O     1 
ATOM   5945  C  CB    . ALA A 1  827  ? -26.469 72.243  76.567  1.00 23.22 ? 825  ALA A CB    1 
ATOM   5946  N  N     . GLU A 1  828  ? -28.199 70.806  78.789  1.00 18.68 ? 826  GLU A N     1 
ATOM   5947  C  CA    . GLU A 1  828  ? -29.293 70.880  79.753  1.00 19.36 ? 826  GLU A CA    1 
ATOM   5948  C  C     . GLU A 1  828  ? -28.810 70.572  81.167  1.00 21.11 ? 826  GLU A C     1 
ATOM   5949  O  O     . GLU A 1  828  ? -29.271 71.193  82.133  1.00 19.47 ? 826  GLU A O     1 
ATOM   5950  C  CB    . GLU A 1  828  ? -30.416 69.918  79.363  1.00 23.12 ? 826  GLU A CB    1 
ATOM   5951  C  CG    . GLU A 1  828  ? -31.261 70.381  78.191  1.00 24.51 ? 826  GLU A CG    1 
ATOM   5952  C  CD    . GLU A 1  828  ? -30.640 70.055  76.830  1.00 28.55 ? 826  GLU A CD    1 
ATOM   5953  O  OE1   . GLU A 1  828  ? -29.507 69.521  76.782  1.00 29.20 ? 826  GLU A OE1   1 
ATOM   5954  O  OE2   . GLU A 1  828  ? -31.307 70.323  75.805  1.00 30.78 ? 826  GLU A OE2   1 
ATOM   5955  N  N     . GLN A 1  829  ? -27.925 69.582  81.308  1.00 20.05 ? 827  GLN A N     1 
ATOM   5956  C  CA    . GLN A 1  829  ? -27.326 69.278  82.608  1.00 20.98 ? 827  GLN A CA    1 
ATOM   5957  C  C     . GLN A 1  829  ? -26.522 70.457  83.132  1.00 17.97 ? 827  GLN A C     1 
ATOM   5958  O  O     . GLN A 1  829  ? -26.638 70.838  84.306  1.00 18.69 ? 827  GLN A O     1 
ATOM   5959  C  CB    . GLN A 1  829  ? -26.408 68.060  82.496  1.00 22.91 ? 827  GLN A CB    1 
ATOM   5960  C  CG    . GLN A 1  829  ? -27.043 66.728  82.727  1.00 31.24 ? 827  GLN A CG    1 
ATOM   5961  C  CD    . GLN A 1  829  ? -26.004 65.625  82.806  1.00 33.10 ? 827  GLN A CD    1 
ATOM   5962  O  OE1   . GLN A 1  829  ? -24.831 65.833  82.477  1.00 29.52 ? 827  GLN A OE1   1 
ATOM   5963  N  NE2   . GLN A 1  829  ? -26.428 64.447  83.244  1.00 34.76 ? 827  GLN A NE2   1 
ATOM   5964  N  N     . VAL A 1  830  ? -25.657 71.012  82.282  1.00 17.51 ? 828  VAL A N     1 
ATOM   5965  C  CA    . VAL A 1  830  ? -24.855 72.173  82.659  1.00 15.76 ? 828  VAL A CA    1 
ATOM   5966  C  C     . VAL A 1  830  ? -25.747 73.306  83.143  1.00 17.25 ? 828  VAL A C     1 
ATOM   5967  O  O     . VAL A 1  830  ? -25.509 73.900  84.202  1.00 15.86 ? 828  VAL A O     1 
ATOM   5968  C  CB    . VAL A 1  830  ? -23.985 72.629  81.480  1.00 16.20 ? 828  VAL A CB    1 
ATOM   5969  C  CG1   . VAL A 1  830  ? -23.332 73.961  81.809  1.00 18.44 ? 828  VAL A CG1   1 
ATOM   5970  C  CG2   . VAL A 1  830  ? -22.918 71.569  81.158  1.00 20.35 ? 828  VAL A CG2   1 
ATOM   5971  N  N     . VAL A 1  831  ? -26.776 73.643  82.356  1.00 17.04 ? 829  VAL A N     1 
ATOM   5972  C  CA    . VAL A 1  831  ? -27.588 74.817  82.684  1.00 16.31 ? 829  VAL A CA    1 
ATOM   5973  C  C     . VAL A 1  831  ? -28.267 74.638  84.035  1.00 17.39 ? 829  VAL A C     1 
ATOM   5974  O  O     . VAL A 1  831  ? -28.299 75.566  84.853  1.00 16.11 ? 829  VAL A O     1 
ATOM   5975  C  CB    . VAL A 1  831  ? -28.601 75.099  81.561  1.00 19.36 ? 829  VAL A CB    1 
ATOM   5976  C  CG1   . VAL A 1  831  ? -29.597 76.162  82.008  1.00 19.54 ? 829  VAL A CG1   1 
ATOM   5977  C  CG2   . VAL A 1  831  ? -27.862 75.598  80.334  1.00 21.03 ? 829  VAL A CG2   1 
ATOM   5978  N  N     . GLY A 1  832  ? -28.819 73.450  84.294  1.00 16.14 ? 830  GLY A N     1 
ATOM   5979  C  CA    . GLY A 1  832  ? -29.425 73.209  85.592  1.00 16.77 ? 830  GLY A CA    1 
ATOM   5980  C  C     . GLY A 1  832  ? -28.429 73.359  86.724  1.00 15.82 ? 830  GLY A C     1 
ATOM   5981  O  O     . GLY A 1  832  ? -28.720 73.991  87.741  1.00 15.56 ? 830  GLY A O     1 
ATOM   5982  N  N     . ASP A 1  833  ? -27.231 72.806  86.552  1.00 15.63 ? 831  ASP A N     1 
ATOM   5983  C  CA    . ASP A 1  833  ? -26.243 72.914  87.622  1.00 15.00 ? 831  ASP A CA    1 
ATOM   5984  C  C     . ASP A 1  833  ? -25.717 74.334  87.779  1.00 15.44 ? 831  ASP A C     1 
ATOM   5985  O  O     . ASP A 1  833  ? -25.323 74.731  88.884  1.00 16.40 ? 831  ASP A O     1 
ATOM   5986  C  CB    . ASP A 1  833  ? -25.088 71.945  87.363  1.00 16.08 ? 831  ASP A CB    1 
ATOM   5987  C  CG    . ASP A 1  833  ? -25.503 70.507  87.527  1.00 16.39 ? 831  ASP A CG    1 
ATOM   5988  O  OD1   . ASP A 1  833  ? -26.599 70.266  88.094  1.00 17.53 ? 831  ASP A OD1   1 
ATOM   5989  O  OD2   . ASP A 1  833  ? -24.749 69.629  87.070  1.00 16.49 ? 831  ASP A OD2   1 
ATOM   5990  N  N     . VAL A 1  834  ? -25.654 75.095  86.686  1.00 14.92 ? 832  VAL A N     1 
ATOM   5991  C  CA    . VAL A 1  834  ? -25.205 76.482  86.753  1.00 14.08 ? 832  VAL A CA    1 
ATOM   5992  C  C     . VAL A 1  834  ? -26.254 77.345  87.431  1.00 16.14 ? 832  VAL A C     1 
ATOM   5993  O  O     . VAL A 1  834  ? -25.946 78.142  88.323  1.00 15.65 ? 832  VAL A O     1 
ATOM   5994  C  CB    . VAL A 1  834  ? -24.878 76.998  85.342  1.00 15.58 ? 832  VAL A CB    1 
ATOM   5995  C  CG1   . VAL A 1  834  ? -24.731 78.499  85.338  1.00 15.66 ? 832  VAL A CG1   1 
ATOM   5996  C  CG2   . VAL A 1  834  ? -23.612 76.303  84.831  1.00 16.53 ? 832  VAL A CG2   1 
ATOM   5997  N  N     . ILE A 1  835  ? -27.516 77.203  87.008  1.00 14.91 ? 833  ILE A N     1 
ATOM   5998  C  CA    . ILE A 1  835  ? -28.597 77.974  87.614  1.00 15.90 ? 833  ILE A CA    1 
ATOM   5999  C  C     . ILE A 1  835  ? -28.644 77.723  89.117  1.00 17.32 ? 833  ILE A C     1 
ATOM   6000  O  O     . ILE A 1  835  ? -28.716 78.658  89.929  1.00 18.98 ? 833  ILE A O     1 
ATOM   6001  C  CB    . ILE A 1  835  ? -29.940 77.633  86.937  1.00 16.94 ? 833  ILE A CB    1 
ATOM   6002  C  CG1   . ILE A 1  835  ? -29.999 78.189  85.502  1.00 17.73 ? 833  ILE A CG1   1 
ATOM   6003  C  CG2   . ILE A 1  835  ? -31.103 78.169  87.766  1.00 19.34 ? 833  ILE A CG2   1 
ATOM   6004  C  CD1   . ILE A 1  835  ? -30.040 79.696  85.412  1.00 20.41 ? 833  ILE A CD1   1 
ATOM   6005  N  N     . THR A 1  836  ? -28.578 76.458  89.513  1.00 16.27 ? 834  THR A N     1 
ATOM   6006  C  CA    . THR A 1  836  ? -28.577 76.134  90.932  1.00 18.02 ? 834  THR A CA    1 
ATOM   6007  C  C     . THR A 1  836  ? -27.330 76.691  91.619  1.00 17.03 ? 834  THR A C     1 
ATOM   6008  O  O     . THR A 1  836  ? -27.426 77.375  92.639  1.00 18.19 ? 834  THR A O     1 
ATOM   6009  C  CB    . THR A 1  836  ? -28.678 74.616  91.108  1.00 19.43 ? 834  THR A CB    1 
ATOM   6010  O  OG1   . THR A 1  836  ? -29.970 74.178  90.670  1.00 23.50 ? 834  THR A OG1   1 
ATOM   6011  C  CG2   . THR A 1  836  ? -28.499 74.230  92.550  1.00 22.25 ? 834  THR A CG2   1 
ATOM   6012  N  N     . SER A 1  837  ? -26.150 76.446  91.051  1.00 17.15 ? 835  SER A N     1 
ATOM   6013  C  CA    . SER A 1  837  ? -24.925 76.821  91.758  1.00 17.87 ? 835  SER A CA    1 
ATOM   6014  C  C     . SER A 1  837  ? -24.772 78.330  91.871  1.00 16.53 ? 835  SER A C     1 
ATOM   6015  O  O     . SER A 1  837  ? -24.278 78.827  92.885  1.00 17.29 ? 835  SER A O     1 
ATOM   6016  C  CB    . SER A 1  837  ? -23.700 76.236  91.062  1.00 15.82 ? 835  SER A CB    1 
ATOM   6017  O  OG    . SER A 1  837  ? -23.771 74.828  91.060  1.00 16.03 ? 835  SER A OG    1 
ATOM   6018  N  N     . ALA A 1  838  ? -25.194 79.075  90.849  1.00 15.48 ? 836  ALA A N     1 
ATOM   6019  C  CA    . ALA A 1  838  ? -24.975 80.514  90.839  1.00 17.10 ? 836  ALA A CA    1 
ATOM   6020  C  C     . ALA A 1  838  ? -26.055 81.260  91.612  1.00 18.22 ? 836  ALA A C     1 
ATOM   6021  O  O     . ALA A 1  838  ? -25.758 82.254  92.286  1.00 17.82 ? 836  ALA A O     1 
ATOM   6022  C  CB    . ALA A 1  838  ? -24.907 81.030  89.399  1.00 15.94 ? 836  ALA A CB    1 
ATOM   6023  N  N     . PHE A 1  839  ? -27.311 80.815  91.527  1.00 18.04 ? 837  PHE A N     1 
ATOM   6024  C  CA    . PHE A 1  839  ? -28.406 81.643  92.008  1.00 18.37 ? 837  PHE A CA    1 
ATOM   6025  C  C     . PHE A 1  839  ? -29.206 81.070  93.164  1.00 18.57 ? 837  PHE A C     1 
ATOM   6026  O  O     . PHE A 1  839  ? -30.019 81.809  93.740  1.00 20.12 ? 837  PHE A O     1 
ATOM   6027  C  CB    . PHE A 1  839  ? -29.349 81.983  90.846  1.00 16.95 ? 837  PHE A CB    1 
ATOM   6028  C  CG    . PHE A 1  839  ? -28.631 82.570  89.670  1.00 17.22 ? 837  PHE A CG    1 
ATOM   6029  C  CD1   . PHE A 1  839  ? -27.906 83.743  89.807  1.00 18.99 ? 837  PHE A CD1   1 
ATOM   6030  C  CD2   . PHE A 1  839  ? -28.661 81.943  88.438  1.00 19.14 ? 837  PHE A CD2   1 
ATOM   6031  C  CE1   . PHE A 1  839  ? -27.221 84.288  88.733  1.00 19.79 ? 837  PHE A CE1   1 
ATOM   6032  C  CE2   . PHE A 1  839  ? -27.977 82.471  87.364  1.00 19.18 ? 837  PHE A CE2   1 
ATOM   6033  C  CZ    . PHE A 1  839  ? -27.262 83.654  87.505  1.00 19.95 ? 837  PHE A CZ    1 
ATOM   6034  N  N     . ASP A 1  840  ? -28.995 79.807  93.542  1.00 17.59 ? 838  ASP A N     1 
ATOM   6035  C  CA    . ASP A 1  840  ? -29.560 79.300  94.785  1.00 18.33 ? 838  ASP A CA    1 
ATOM   6036  C  C     . ASP A 1  840  ? -29.180 80.242  95.916  1.00 21.16 ? 838  ASP A C     1 
ATOM   6037  O  O     . ASP A 1  840  ? -28.053 80.737  95.970  1.00 18.23 ? 838  ASP A O     1 
ATOM   6038  C  CB    . ASP A 1  840  ? -29.039 77.883  95.062  1.00 21.06 ? 838  ASP A CB    1 
ATOM   6039  C  CG    . ASP A 1  840  ? -29.589 77.280  96.346  1.00 24.31 ? 838  ASP A CG    1 
ATOM   6040  O  OD1   . ASP A 1  840  ? -29.119 77.653  97.442  1.00 24.66 ? 838  ASP A OD1   1 
ATOM   6041  O  OD2   . ASP A 1  840  ? -30.490 76.418  96.253  1.00 31.15 ? 838  ASP A OD2   1 
ATOM   6042  N  N     . SER A 1  841  ? -30.142 80.535  96.785  1.00 17.71 ? 839  SER A N     1 
ATOM   6043  C  CA    . SER A 1  841  ? -29.924 81.460  97.901  1.00 17.10 ? 839  SER A CA    1 
ATOM   6044  C  C     . SER A 1  841  ? -29.430 82.817  97.417  1.00 17.87 ? 839  SER A C     1 
ATOM   6045  O  O     . SER A 1  841  ? -28.702 83.514  98.129  1.00 20.02 ? 839  SER A O     1 
ATOM   6046  C  CB    . SER A 1  841  ? -28.948 80.873  98.928  1.00 20.48 ? 839  SER A CB    1 
ATOM   6047  O  OG    . SER A 1  841  ? -29.341 79.562  99.290  1.00 23.49 ? 839  SER A OG    1 
ATOM   6048  N  N     . ALA A 1  842  ? -29.830 83.199  96.200  1.00 18.98 ? 840  ALA A N     1 
ATOM   6049  C  CA    . ALA A 1  842  ? -29.397 84.446  95.576  1.00 17.30 ? 840  ALA A CA    1 
ATOM   6050  C  C     . ALA A 1  842  ? -27.875 84.573  95.579  1.00 18.21 ? 840  ALA A C     1 
ATOM   6051  O  O     . ALA A 1  842  ? -27.322 85.647  95.784  1.00 18.31 ? 840  ALA A O     1 
ATOM   6052  C  CB    . ALA A 1  842  ? -30.055 85.657  96.250  1.00 21.00 ? 840  ALA A CB    1 
ATOM   6053  N  N     . GLY A 1  843  ? -27.191 83.462  95.327  1.00 18.30 ? 841  GLY A N     1 
ATOM   6054  C  CA    . GLY A 1  843  ? -25.743 83.498  95.261  1.00 16.39 ? 841  GLY A CA    1 
ATOM   6055  C  C     . GLY A 1  843  ? -25.053 83.680  96.589  1.00 17.77 ? 841  GLY A C     1 
ATOM   6056  O  O     . GLY A 1  843  ? -23.830 83.833  96.614  1.00 18.60 ? 841  GLY A O     1 
ATOM   6057  N  N     . GLN A 1  844  ? -25.793 83.644  97.695  1.00 17.67 ? 842  GLN A N     1 
ATOM   6058  C  CA    . GLN A 1  844  ? -25.221 83.880  99.017  1.00 17.73 ? 842  GLN A CA    1 
ATOM   6059  C  C     . GLN A 1  844  ? -24.830 82.573  99.699  1.00 19.53 ? 842  GLN A C     1 
ATOM   6060  O  O     . GLN A 1  844  ? -25.214 82.259  100.827 1.00 19.96 ? 842  GLN A O     1 
ATOM   6061  C  CB    . GLN A 1  844  ? -26.197 84.695  99.857  1.00 18.40 ? 842  GLN A CB    1 
ATOM   6062  C  CG    . GLN A 1  844  ? -26.423 86.080  99.256  1.00 18.33 ? 842  GLN A CG    1 
ATOM   6063  C  CD    . GLN A 1  844  ? -27.664 86.758  99.782  1.00 19.45 ? 842  GLN A CD    1 
ATOM   6064  O  OE1   . GLN A 1  844  ? -27.595 87.858  100.324 1.00 18.68 ? 842  GLN A OE1   1 
ATOM   6065  N  NE2   . GLN A 1  844  ? -28.816 86.109  99.614  1.00 22.13 ? 842  GLN A NE2   1 
ATOM   6066  N  N     . ARG A 1  845  ? -24.065 81.785  98.959  1.00 16.68 ? 843  ARG A N     1 
ATOM   6067  C  CA    . ARG A 1  845  ? -23.323 80.653  99.472  1.00 17.80 ? 843  ARG A CA    1 
ATOM   6068  C  C     . ARG A 1  845  ? -21.861 80.915  99.185  1.00 17.38 ? 843  ARG A C     1 
ATOM   6069  O  O     . ARG A 1  845  ? -21.517 81.400  98.108  1.00 17.21 ? 843  ARG A O     1 
ATOM   6070  C  CB    . ARG A 1  845  ? -23.718 79.344  98.791  1.00 18.63 ? 843  ARG A CB    1 
ATOM   6071  C  CG    . ARG A 1  845  ? -25.181 78.933  98.948  1.00 18.48 ? 843  ARG A CG    1 
ATOM   6072  C  CD    . ARG A 1  845  ? -25.377 77.588  98.265  1.00 19.92 ? 843  ARG A CD    1 
ATOM   6073  N  NE    . ARG A 1  845  ? -26.691 77.034  98.567  1.00 23.74 ? 843  ARG A NE    1 
ATOM   6074  C  CZ    . ARG A 1  845  ? -26.929 76.170  99.544  1.00 25.60 ? 843  ARG A CZ    1 
ATOM   6075  N  NH1   . ARG A 1  845  ? -25.949 75.670  100.285 1.00 25.48 ? 843  ARG A NH1   1 
ATOM   6076  N  NH2   . ARG A 1  845  ? -28.182 75.797  99.785  1.00 28.28 ? 843  ARG A NH2   1 
ATOM   6077  N  N     . CYS A 1  846  ? -20.993 80.591  100.136 1.00 17.27 ? 844  CYS A N     1 
ATOM   6078  C  CA    . CYS A 1  846  ? -19.572 80.745  99.850  1.00 17.32 ? 844  CYS A CA    1 
ATOM   6079  C  C     . CYS A 1  846  ? -19.148 79.863  98.683  1.00 15.99 ? 844  CYS A C     1 
ATOM   6080  O  O     . CYS A 1  846  ? -18.201 80.193  97.960  1.00 15.79 ? 844  CYS A O     1 
ATOM   6081  C  CB    . CYS A 1  846  ? -18.761 80.411  101.099 1.00 16.63 ? 844  CYS A CB    1 
ATOM   6082  S  SG    . CYS A 1  846  ? -19.208 78.821  101.804 1.00 19.07 ? 844  CYS A SG    1 
ATOM   6083  N  N     . SER A 1  847  ? -19.860 78.758  98.474  1.00 15.78 ? 845  SER A N     1 
ATOM   6084  C  CA    . SER A 1  847  ? -19.618 77.780  97.424  1.00 15.06 ? 845  SER A CA    1 
ATOM   6085  C  C     . SER A 1  847  ? -20.191 78.184  96.074  1.00 16.11 ? 845  SER A C     1 
ATOM   6086  O  O     . SER A 1  847  ? -19.989 77.453  95.095  1.00 15.45 ? 845  SER A O     1 
ATOM   6087  C  CB    . SER A 1  847  ? -20.243 76.457  97.848  1.00 17.30 ? 845  SER A CB    1 
ATOM   6088  O  OG    . SER A 1  847  ? -21.610 76.667  98.206  1.00 17.05 ? 845  SER A OG    1 
ATOM   6089  N  N     . ALA A 1  848  ? -20.925 79.290  96.006  1.00 15.97 ? 846  ALA A N     1 
ATOM   6090  C  CA    . ALA A 1  848  ? -21.702 79.599  94.811  1.00 14.97 ? 846  ALA A CA    1 
ATOM   6091  C  C     . ALA A 1  848  ? -20.813 79.778  93.586  1.00 16.56 ? 846  ALA A C     1 
ATOM   6092  O  O     . ALA A 1  848  ? -19.681 80.258  93.662  1.00 15.60 ? 846  ALA A O     1 
ATOM   6093  C  CB    . ALA A 1  848  ? -22.528 80.869  95.027  1.00 15.93 ? 846  ALA A CB    1 
ATOM   6094  N  N     . LEU A 1  849  ? -21.360 79.417  92.431  1.00 15.32 ? 847  LEU A N     1 
ATOM   6095  C  CA    . LEU A 1  849  ? -20.624 79.564  91.182  1.00 14.36 ? 847  LEU A CA    1 
ATOM   6096  C  C     . LEU A 1  849  ? -20.547 81.035  90.799  1.00 16.82 ? 847  LEU A C     1 
ATOM   6097  O  O     . LEU A 1  849  ? -21.577 81.702  90.654  1.00 16.60 ? 847  LEU A O     1 
ATOM   6098  C  CB    . LEU A 1  849  ? -21.304 78.767  90.076  1.00 16.49 ? 847  LEU A CB    1 
ATOM   6099  C  CG    . LEU A 1  849  ? -20.706 78.959  88.684  1.00 15.25 ? 847  LEU A CG    1 
ATOM   6100  C  CD1   . LEU A 1  849  ? -19.264 78.463  88.611  1.00 17.01 ? 847  LEU A CD1   1 
ATOM   6101  C  CD2   . LEU A 1  849  ? -21.591 78.254  87.643  1.00 16.04 ? 847  LEU A CD2   1 
ATOM   6102  N  N     . ARG A 1  850  ? -19.324 81.539  90.647  1.00 15.46 ? 848  ARG A N     1 
ATOM   6103  C  CA    . ARG A 1  850  ? -19.074 82.929  90.297  1.00 17.85 ? 848  ARG A CA    1 
ATOM   6104  C  C     . ARG A 1  850  ? -18.625 83.124  88.860  1.00 17.18 ? 848  ARG A C     1 
ATOM   6105  O  O     . ARG A 1  850  ? -18.914 84.170  88.280  1.00 18.56 ? 848  ARG A O     1 
ATOM   6106  C  CB    . ARG A 1  850  ? -18.000 83.534  91.214  1.00 17.77 ? 848  ARG A CB    1 
ATOM   6107  C  CG    . ARG A 1  850  ? -18.269 83.368  92.687  1.00 18.92 ? 848  ARG A CG    1 
ATOM   6108  C  CD    . ARG A 1  850  ? -19.648 83.886  93.081  1.00 19.15 ? 848  ARG A CD    1 
ATOM   6109  N  NE    . ARG A 1  850  ? -19.844 83.778  94.520  1.00 17.43 ? 848  ARG A NE    1 
ATOM   6110  C  CZ    . ARG A 1  850  ? -20.988 84.046  95.137  1.00 18.75 ? 848  ARG A CZ    1 
ATOM   6111  N  NH1   . ARG A 1  850  ? -22.073 84.391  94.457  1.00 17.75 ? 848  ARG A NH1   1 
ATOM   6112  N  NH2   . ARG A 1  850  ? -21.042 83.975  96.463  1.00 18.59 ? 848  ARG A NH2   1 
ATOM   6113  N  N     . VAL A 1  851  ? -17.908 82.156  88.278  1.00 17.85 ? 849  VAL A N     1 
ATOM   6114  C  CA    . VAL A 1  851  ? -17.324 82.300  86.944  1.00 17.58 ? 849  VAL A CA    1 
ATOM   6115  C  C     . VAL A 1  851  ? -17.574 81.006  86.187  1.00 18.15 ? 849  VAL A C     1 
ATOM   6116  O  O     . VAL A 1  851  ? -17.014 79.963  86.535  1.00 17.29 ? 849  VAL A O     1 
ATOM   6117  C  CB    . VAL A 1  851  ? -15.816 82.594  86.975  1.00 19.54 ? 849  VAL A CB    1 
ATOM   6118  C  CG1   . VAL A 1  851  ? -15.339 82.929  85.570  1.00 21.54 ? 849  VAL A CG1   1 
ATOM   6119  C  CG2   . VAL A 1  851  ? -15.485 83.701  87.946  1.00 23.84 ? 849  VAL A CG2   1 
ATOM   6120  N  N     . LEU A 1  852  ? -18.404 81.070  85.152  1.00 16.88 ? 850  LEU A N     1 
ATOM   6121  C  CA    . LEU A 1  852  ? -18.656 79.933  84.282  1.00 17.02 ? 850  LEU A CA    1 
ATOM   6122  C  C     . LEU A 1  852  ? -17.765 80.070  83.063  1.00 15.66 ? 850  LEU A C     1 
ATOM   6123  O  O     . LEU A 1  852  ? -17.746 81.129  82.428  1.00 16.71 ? 850  LEU A O     1 
ATOM   6124  C  CB    . LEU A 1  852  ? -20.122 79.889  83.855  1.00 15.02 ? 850  LEU A CB    1 
ATOM   6125  C  CG    . LEU A 1  852  ? -20.528 78.841  82.819  1.00 15.77 ? 850  LEU A CG    1 
ATOM   6126  C  CD1   . LEU A 1  852  ? -20.363 77.436  83.397  1.00 15.30 ? 850  LEU A CD1   1 
ATOM   6127  C  CD2   . LEU A 1  852  ? -21.987 79.098  82.396  1.00 16.01 ? 850  LEU A CD2   1 
ATOM   6128  N  N     . CYS A 1  853  ? -17.029 79.008  82.745  1.00 17.00 ? 851  CYS A N     1 
ATOM   6129  C  CA    . CYS A 1  853  ? -16.043 79.027  81.667  1.00 16.98 ? 851  CYS A CA    1 
ATOM   6130  C  C     . CYS A 1  853  ? -16.504 78.047  80.600  1.00 16.49 ? 851  CYS A C     1 
ATOM   6131  O  O     . CYS A 1  853  ? -16.533 76.838  80.839  1.00 17.48 ? 851  CYS A O     1 
ATOM   6132  C  CB    . CYS A 1  853  ? -14.651 78.651  82.172  1.00 17.57 ? 851  CYS A CB    1 
ATOM   6133  S  SG    . CYS A 1  853  ? -14.119 79.558  83.627  1.00 19.33 ? 851  CYS A SG    1 
ATOM   6134  N  N     . LEU A 1  854  ? -16.850 78.570  79.424  1.00 17.12 ? 852  LEU A N     1 
ATOM   6135  C  CA    . LEU A 1  854  ? -17.493 77.803  78.368  1.00 17.11 ? 852  LEU A CA    1 
ATOM   6136  C  C     . LEU A 1  854  ? -16.545 77.622  77.196  1.00 17.37 ? 852  LEU A C     1 
ATOM   6137  O  O     . LEU A 1  854  ? -16.010 78.603  76.669  1.00 19.30 ? 852  LEU A O     1 
ATOM   6138  C  CB    . LEU A 1  854  ? -18.757 78.501  77.875  1.00 17.34 ? 852  LEU A CB    1 
ATOM   6139  C  CG    . LEU A 1  854  ? -19.845 78.661  78.920  1.00 18.70 ? 852  LEU A CG    1 
ATOM   6140  C  CD1   . LEU A 1  854  ? -21.036 79.396  78.292  1.00 16.06 ? 852  LEU A CD1   1 
ATOM   6141  C  CD2   . LEU A 1  854  ? -20.279 77.298  79.435  1.00 18.82 ? 852  LEU A CD2   1 
ATOM   6142  N  N     . GLN A 1  855  ? -16.364 76.375  76.771  1.00 17.17 ? 853  GLN A N     1 
ATOM   6143  C  CA    . GLN A 1  855  ? -15.550 76.158  75.586  1.00 17.98 ? 853  GLN A CA    1 
ATOM   6144  C  C     . GLN A 1  855  ? -16.205 76.849  74.394  1.00 20.14 ? 853  GLN A C     1 
ATOM   6145  O  O     . GLN A 1  855  ? -17.423 76.779  74.207  1.00 20.07 ? 853  GLN A O     1 
ATOM   6146  C  CB    . GLN A 1  855  ? -15.378 74.667  75.307  1.00 19.18 ? 853  GLN A CB    1 
ATOM   6147  C  CG    . GLN A 1  855  ? -14.277 74.428  74.274  1.00 17.78 ? 853  GLN A CG    1 
ATOM   6148  C  CD    . GLN A 1  855  ? -14.194 72.992  73.808  1.00 22.13 ? 853  GLN A CD    1 
ATOM   6149  O  OE1   . GLN A 1  855  ? -14.227 72.061  74.613  1.00 22.30 ? 853  GLN A OE1   1 
ATOM   6150  N  NE2   . GLN A 1  855  ? -14.086 72.804  72.495  1.00 27.13 ? 853  GLN A NE2   1 
ATOM   6151  N  N     . GLU A 1  856  ? -15.376 77.511  73.582  1.00 20.87 ? 854  GLU A N     1 
ATOM   6152  C  CA    . GLU A 1  856  ? -15.884 78.450  72.584  1.00 22.47 ? 854  GLU A CA    1 
ATOM   6153  C  C     . GLU A 1  856  ? -16.914 77.809  71.660  1.00 23.76 ? 854  GLU A C     1 
ATOM   6154  O  O     . GLU A 1  856  ? -17.922 78.437  71.314  1.00 24.82 ? 854  GLU A O     1 
ATOM   6155  C  CB    . GLU A 1  856  ? -14.713 79.022  71.781  1.00 23.21 ? 854  GLU A CB    1 
ATOM   6156  C  CG    . GLU A 1  856  ? -15.135 79.925  70.628  1.00 26.60 ? 854  GLU A CG    1 
ATOM   6157  C  CD    . GLU A 1  856  ? -15.904 81.145  71.086  1.00 31.12 ? 854  GLU A CD    1 
ATOM   6158  O  OE1   . GLU A 1  856  ? -15.553 81.700  72.147  1.00 29.57 ? 854  GLU A OE1   1 
ATOM   6159  O  OE2   . GLU A 1  856  ? -16.859 81.550  70.389  1.00 30.70 ? 854  GLU A OE2   1 
ATOM   6160  N  N     . ASP A 1  857  ? -16.699 76.546  71.279  1.00 22.44 ? 855  ASP A N     1 
ATOM   6161  C  CA    . ASP A 1  857  ? -17.561 75.890  70.297  1.00 23.59 ? 855  ASP A CA    1 
ATOM   6162  C  C     . ASP A 1  857  ? -18.989 75.691  70.794  1.00 23.83 ? 855  ASP A C     1 
ATOM   6163  O  O     . ASP A 1  857  ? -19.910 75.584  69.975  1.00 26.32 ? 855  ASP A O     1 
ATOM   6164  C  CB    . ASP A 1  857  ? -16.970 74.538  69.894  1.00 30.57 ? 855  ASP A CB    1 
ATOM   6165  N  N     . VAL A 1  858  ? -19.200 75.638  72.107  1.00 20.42 ? 856  VAL A N     1 
ATOM   6166  C  CA    . VAL A 1  858  ? -20.532 75.446  72.669  1.00 20.09 ? 856  VAL A CA    1 
ATOM   6167  C  C     . VAL A 1  858  ? -21.014 76.648  73.464  1.00 20.19 ? 856  VAL A C     1 
ATOM   6168  O  O     . VAL A 1  858  ? -22.122 76.605  74.018  1.00 19.21 ? 856  VAL A O     1 
ATOM   6169  C  CB    . VAL A 1  858  ? -20.600 74.171  73.532  1.00 20.84 ? 856  VAL A CB    1 
ATOM   6170  C  CG1   . VAL A 1  858  ? -20.477 72.937  72.643  1.00 23.19 ? 856  VAL A CG1   1 
ATOM   6171  C  CG2   . VAL A 1  858  ? -19.517 74.187  74.632  1.00 20.51 ? 856  VAL A CG2   1 
ATOM   6172  N  N     . ALA A 1  859  ? -20.228 77.724  73.528  1.00 20.25 ? 857  ALA A N     1 
ATOM   6173  C  CA    . ALA A 1  859  ? -20.557 78.819  74.436  1.00 19.91 ? 857  ALA A CA    1 
ATOM   6174  C  C     . ALA A 1  859  ? -21.870 79.490  74.052  1.00 22.25 ? 857  ALA A C     1 
ATOM   6175  O  O     . ALA A 1  859  ? -22.689 79.800  74.923  1.00 18.61 ? 857  ALA A O     1 
ATOM   6176  C  CB    . ALA A 1  859  ? -19.433 79.848  74.460  1.00 19.78 ? 857  ALA A CB    1 
ATOM   6177  N  N     . ASP A 1  860  ? -22.090 79.726  72.752  1.00 20.13 ? 858  ASP A N     1 
ATOM   6178  C  CA    . ASP A 1  860  ? -23.290 80.450  72.344  1.00 23.58 ? 858  ASP A CA    1 
ATOM   6179  C  C     . ASP A 1  860  ? -24.547 79.661  72.673  1.00 20.64 ? 858  ASP A C     1 
ATOM   6180  O  O     . ASP A 1  860  ? -25.517 80.220  73.196  1.00 21.86 ? 858  ASP A O     1 
ATOM   6181  C  CB    . ASP A 1  860  ? -23.247 80.772  70.847  1.00 23.44 ? 858  ASP A CB    1 
ATOM   6182  C  CG    . ASP A 1  860  ? -22.361 81.965  70.520  1.00 28.55 ? 858  ASP A CG    1 
ATOM   6183  O  OD1   . ASP A 1  860  ? -22.105 82.812  71.404  1.00 29.82 ? 858  ASP A OD1   1 
ATOM   6184  O  OD2   . ASP A 1  860  ? -21.931 82.061  69.356  1.00 39.73 ? 858  ASP A OD2   1 
ATOM   6185  N  N     . ARG A 1  861  ? -24.543 78.357  72.381  1.00 19.38 ? 859  ARG A N     1 
ATOM   6186  C  CA    . ARG A 1  861  ? -25.711 77.522  72.636  1.00 23.57 ? 859  ARG A CA    1 
ATOM   6187  C  C     . ARG A 1  861  ? -26.003 77.438  74.130  1.00 20.87 ? 859  ARG A C     1 
ATOM   6188  O  O     . ARG A 1  861  ? -27.152 77.587  74.562  1.00 20.04 ? 859  ARG A O     1 
ATOM   6189  C  CB    . ARG A 1  861  ? -25.485 76.129  72.036  1.00 26.88 ? 859  ARG A CB    1 
ATOM   6190  C  CG    . ARG A 1  861  ? -26.711 75.225  71.960  1.00 33.18 ? 859  ARG A CG    1 
ATOM   6191  C  CD    . ARG A 1  861  ? -26.789 74.284  73.155  1.00 36.54 ? 859  ARG A CD    1 
ATOM   6192  N  NE    . ARG A 1  861  ? -26.951 72.883  72.773  1.00 41.55 ? 859  ARG A NE    1 
ATOM   6193  C  CZ    . ARG A 1  861  ? -28.117 72.254  72.682  1.00 39.71 ? 859  ARG A CZ    1 
ATOM   6194  N  NH1   . ARG A 1  861  ? -29.260 72.881  72.902  1.00 44.84 ? 859  ARG A NH1   1 
ATOM   6195  N  NH2   . ARG A 1  861  ? -28.136 70.963  72.362  1.00 47.86 ? 859  ARG A NH2   1 
ATOM   6196  N  N     . ILE A 1  862  ? -24.970 77.211  74.942  1.00 19.58 ? 860  ILE A N     1 
ATOM   6197  C  CA    . ILE A 1  862  ? -25.205 77.095  76.377  1.00 17.72 ? 860  ILE A CA    1 
ATOM   6198  C  C     . ILE A 1  862  ? -25.639 78.437  76.958  1.00 18.03 ? 860  ILE A C     1 
ATOM   6199  O  O     . ILE A 1  862  ? -26.535 78.498  77.809  1.00 17.74 ? 860  ILE A O     1 
ATOM   6200  C  CB    . ILE A 1  862  ? -23.949 76.546  77.077  1.00 17.66 ? 860  ILE A CB    1 
ATOM   6201  C  CG1   . ILE A 1  862  ? -23.707 75.093  76.654  1.00 21.38 ? 860  ILE A CG1   1 
ATOM   6202  C  CG2   . ILE A 1  862  ? -24.110 76.631  78.590  1.00 18.13 ? 860  ILE A CG2   1 
ATOM   6203  C  CD1   . ILE A 1  862  ? -22.355 74.527  77.134  1.00 22.16 ? 860  ILE A CD1   1 
ATOM   6204  N  N     . LEU A 1  863  ? -25.019 79.529  76.511  1.00 18.02 ? 861  LEU A N     1 
ATOM   6205  C  CA    . LEU A 1  863  ? -25.380 80.848  77.022  1.00 19.76 ? 861  LEU A CA    1 
ATOM   6206  C  C     . LEU A 1  863  ? -26.828 81.190  76.695  1.00 18.99 ? 861  LEU A C     1 
ATOM   6207  O  O     . LEU A 1  863  ? -27.554 81.730  77.539  1.00 17.34 ? 861  LEU A O     1 
ATOM   6208  C  CB    . LEU A 1  863  ? -24.432 81.897  76.448  1.00 22.59 ? 861  LEU A CB    1 
ATOM   6209  C  CG    . LEU A 1  863  ? -24.422 83.284  77.063  1.00 25.17 ? 861  LEU A CG    1 
ATOM   6210  C  CD1   . LEU A 1  863  ? -24.370 83.211  78.580  1.00 21.60 ? 861  LEU A CD1   1 
ATOM   6211  C  CD2   . LEU A 1  863  ? -23.213 84.035  76.516  1.00 28.57 ? 861  LEU A CD2   1 
ATOM   6212  N  N     . THR A 1  864  ? -27.275 80.881  75.477  1.00 18.91 ? 862  THR A N     1 
ATOM   6213  C  CA    . THR A 1  864  ? -28.677 81.109  75.135  1.00 18.75 ? 862  THR A CA    1 
ATOM   6214  C  C     . THR A 1  864  ? -29.593 80.302  76.044  1.00 17.47 ? 862  THR A C     1 
ATOM   6215  O  O     . THR A 1  864  ? -30.600 80.814  76.553  1.00 18.30 ? 862  THR A O     1 
ATOM   6216  C  CB    . THR A 1  864  ? -28.921 80.745  73.667  1.00 18.71 ? 862  THR A CB    1 
ATOM   6217  O  OG1   . THR A 1  864  ? -28.182 81.637  72.829  1.00 20.46 ? 862  THR A OG1   1 
ATOM   6218  C  CG2   . THR A 1  864  ? -30.423 80.817  73.319  1.00 19.68 ? 862  THR A CG2   1 
ATOM   6219  N  N     . MET A 1  865  ? -29.263 79.023  76.251  1.00 16.16 ? 863  MET A N     1 
ATOM   6220  C  CA    . MET A 1  865  ? -30.076 78.204  77.143  1.00 17.45 ? 863  MET A CA    1 
ATOM   6221  C  C     . MET A 1  865  ? -30.026 78.739  78.564  1.00 16.50 ? 863  MET A C     1 
ATOM   6222  O  O     . MET A 1  865  ? -31.050 78.797  79.253  1.00 15.51 ? 863  MET A O     1 
ATOM   6223  C  CB    . MET A 1  865  ? -29.607 76.749  77.085  1.00 18.88 ? 863  MET A CB    1 
ATOM   6224  C  CG    . MET A 1  865  ? -30.461 75.764  77.881  1.00 21.01 ? 863  MET A CG    1 
ATOM   6225  S  SD    . MET A 1  865  ? -29.825 74.080  77.668  1.00 24.34 ? 863  MET A SD    1 
ATOM   6226  C  CE    . MET A 1  865  ? -29.475 74.144  75.909  1.00 24.54 ? 863  MET A CE    1 
ATOM   6227  N  N     . LEU A 1  866  ? -28.841 79.168  79.009  1.00 15.62 ? 864  LEU A N     1 
ATOM   6228  C  CA    . LEU A 1  866  ? -28.695 79.704  80.359  1.00 16.80 ? 864  LEU A CA    1 
ATOM   6229  C  C     . LEU A 1  866  ? -29.547 80.950  80.571  1.00 16.01 ? 864  LEU A C     1 
ATOM   6230  O  O     . LEU A 1  866  ? -30.220 81.089  81.598  1.00 18.02 ? 864  LEU A O     1 
ATOM   6231  C  CB    . LEU A 1  866  ? -27.221 80.015  80.618  1.00 18.12 ? 864  LEU A CB    1 
ATOM   6232  C  CG    . LEU A 1  866  ? -26.904 80.533  82.011  1.00 23.06 ? 864  LEU A CG    1 
ATOM   6233  C  CD1   . LEU A 1  866  ? -27.324 79.499  83.036  1.00 20.70 ? 864  LEU A CD1   1 
ATOM   6234  C  CD2   . LEU A 1  866  ? -25.409 80.787  82.098  1.00 20.88 ? 864  LEU A CD2   1 
ATOM   6235  N  N     . LYS A 1  867  ? -29.516 81.887  79.617  1.00 17.07 ? 865  LYS A N     1 
ATOM   6236  C  CA    . LYS A 1  867  ? -30.329 83.088  79.747  1.00 17.13 ? 865  LYS A CA    1 
ATOM   6237  C  C     . LYS A 1  867  ? -31.808 82.743  79.751  1.00 18.02 ? 865  LYS A C     1 
ATOM   6238  O  O     . LYS A 1  867  ? -32.591 83.335  80.502  1.00 18.65 ? 865  LYS A O     1 
ATOM   6239  C  CB    . LYS A 1  867  ? -30.013 84.069  78.617  1.00 18.88 ? 865  LYS A CB    1 
ATOM   6240  C  CG    . LYS A 1  867  ? -28.606 84.662  78.710  1.00 20.58 ? 865  LYS A CG    1 
ATOM   6241  C  CD    . LYS A 1  867  ? -28.287 85.536  77.500  1.00 21.45 ? 865  LYS A CD    1 
ATOM   6242  C  CE    . LYS A 1  867  ? -26.841 86.015  77.562  1.00 24.34 ? 865  LYS A CE    1 
ATOM   6243  N  NZ    . LYS A 1  867  ? -26.392 86.762  76.349  1.00 25.93 ? 865  LYS A NZ    1 
ATOM   6244  N  N     . GLY A 1  868  ? -32.209 81.790  78.918  1.00 15.96 ? 866  GLY A N     1 
ATOM   6245  C  CA    . GLY A 1  868  ? -33.599 81.361  78.932  1.00 17.24 ? 866  GLY A CA    1 
ATOM   6246  C  C     . GLY A 1  868  ? -34.005 80.778  80.273  1.00 16.62 ? 866  GLY A C     1 
ATOM   6247  O  O     . GLY A 1  868  ? -35.102 81.054  80.778  1.00 17.60 ? 866  GLY A O     1 
ATOM   6248  N  N     . ALA A 1  869  ? -33.122 79.978  80.875  1.00 16.62 ? 867  ALA A N     1 
ATOM   6249  C  CA    . ALA A 1  869  ? -33.430 79.389  82.175  1.00 17.52 ? 867  ALA A CA    1 
ATOM   6250  C  C     . ALA A 1  869  ? -33.457 80.448  83.266  1.00 16.32 ? 867  ALA A C     1 
ATOM   6251  O  O     . ALA A 1  869  ? -34.256 80.356  84.205  1.00 16.35 ? 867  ALA A O     1 
ATOM   6252  C  CB    . ALA A 1  869  ? -32.412 78.307  82.529  1.00 16.79 ? 867  ALA A CB    1 
ATOM   6253  N  N     . LEU A 1  870  ? -32.564 81.439  83.172  1.00 16.26 ? 868  LEU A N     1 
ATOM   6254  C  CA    . LEU A 1  870  ? -32.561 82.552  84.118  1.00 17.84 ? 868  LEU A CA    1 
ATOM   6255  C  C     . LEU A 1  870  ? -33.946 83.162  84.248  1.00 19.09 ? 868  LEU A C     1 
ATOM   6256  O  O     . LEU A 1  870  ? -34.413 83.442  85.354  1.00 18.16 ? 868  LEU A O     1 
ATOM   6257  C  CB    . LEU A 1  870  ? -31.570 83.625  83.661  1.00 19.11 ? 868  LEU A CB    1 
ATOM   6258  C  CG    . LEU A 1  870  ? -31.244 84.762  84.632  1.00 20.43 ? 868  LEU A CG    1 
ATOM   6259  C  CD1   . LEU A 1  870  ? -30.178 84.310  85.620  1.00 21.49 ? 868  LEU A CD1   1 
ATOM   6260  C  CD2   . LEU A 1  870  ? -30.778 86.013  83.900  1.00 22.50 ? 868  LEU A CD2   1 
ATOM   6261  N  N     . HIS A 1  871  ? -34.618 83.371  83.126  1.00 15.89 ? 869  HIS A N     1 
ATOM   6262  C  CA    . HIS A 1  871  ? -35.888 84.083  83.137  1.00 20.56 ? 869  HIS A CA    1 
ATOM   6263  C  C     . HIS A 1  871  ? -37.050 83.241  83.634  1.00 19.40 ? 869  HIS A C     1 
ATOM   6264  O  O     . HIS A 1  871  ? -38.152 83.775  83.789  1.00 22.21 ? 869  HIS A O     1 
ATOM   6265  C  CB    . HIS A 1  871  ? -36.165 84.637  81.746  1.00 22.60 ? 869  HIS A CB    1 
ATOM   6266  C  CG    . HIS A 1  871  ? -35.294 85.805  81.409  1.00 24.27 ? 869  HIS A CG    1 
ATOM   6267  N  ND1   . HIS A 1  871  ? -35.491 87.057  81.950  1.00 23.82 ? 869  HIS A ND1   1 
ATOM   6268  C  CD2   . HIS A 1  871  ? -34.185 85.900  80.639  1.00 22.24 ? 869  HIS A CD2   1 
ATOM   6269  C  CE1   . HIS A 1  871  ? -34.554 87.877  81.509  1.00 25.68 ? 869  HIS A CE1   1 
ATOM   6270  N  NE2   . HIS A 1  871  ? -33.745 87.199  80.715  1.00 23.87 ? 869  HIS A NE2   1 
ATOM   6271  N  N     . GLU A 1  872  ? -36.824 81.964  83.922  1.00 17.23 ? 870  GLU A N     1 
ATOM   6272  C  CA    . GLU A 1  872  ? -37.839 81.117  84.531  1.00 18.25 ? 870  GLU A CA    1 
ATOM   6273  C  C     . GLU A 1  872  ? -37.782 81.127  86.050  1.00 18.73 ? 870  GLU A C     1 
ATOM   6274  O  O     . GLU A 1  872  ? -38.587 80.440  86.684  1.00 18.45 ? 870  GLU A O     1 
ATOM   6275  C  CB    . GLU A 1  872  ? -37.704 79.674  84.030  1.00 17.11 ? 870  GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1  872  ? -37.909 79.543  82.531  1.00 19.22 ? 870  GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1  872  ? -39.302 79.947  82.102  1.00 23.20 ? 870  GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1  872  ? -40.243 79.854  82.930  1.00 22.83 ? 870  GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1  872  ? -39.457 80.372  80.936  1.00 23.71 ? 870  GLU A OE2   1 
ATOM   6280  N  N     . LEU A 1  873  ? -36.860 81.886  86.644  1.00 17.33 ? 871  LEU A N     1 
ATOM   6281  C  CA    . LEU A 1  873  ? -36.737 81.938  88.095  1.00 17.24 ? 871  LEU A CA    1 
ATOM   6282  C  C     . LEU A 1  873  ? -37.738 82.913  88.700  1.00 17.91 ? 871  LEU A C     1 
ATOM   6283  O  O     . LEU A 1  873  ? -37.977 84.002  88.163  1.00 19.70 ? 871  LEU A O     1 
ATOM   6284  C  CB    . LEU A 1  873  ? -35.323 82.361  88.493  1.00 18.96 ? 871  LEU A CB    1 
ATOM   6285  C  CG    . LEU A 1  873  ? -34.243 81.394  88.034  1.00 17.50 ? 871  LEU A CG    1 
ATOM   6286  C  CD1   . LEU A 1  873  ? -32.873 81.978  88.384  1.00 18.10 ? 871  LEU A CD1   1 
ATOM   6287  C  CD2   . LEU A 1  873  ? -34.442 80.044  88.715  1.00 22.32 ? 871  LEU A CD2   1 
ATOM   6288  N  N     . HIS A 1  874  ? -38.308 82.520  89.837  1.00 20.08 ? 872  HIS A N     1 
ATOM   6289  C  CA    . HIS A 1  874  ? -39.250 83.345  90.576  1.00 19.11 ? 872  HIS A CA    1 
ATOM   6290  C  C     . HIS A 1  874  ? -38.525 83.923  91.789  1.00 18.99 ? 872  HIS A C     1 
ATOM   6291  O  O     . HIS A 1  874  ? -38.032 83.172  92.644  1.00 18.51 ? 872  HIS A O     1 
ATOM   6292  C  CB    . HIS A 1  874  ? -40.470 82.517  90.990  1.00 20.52 ? 872  HIS A CB    1 
ATOM   6293  C  CG    . HIS A 1  874  ? -41.506 83.277  91.766  1.00 21.69 ? 872  HIS A CG    1 
ATOM   6294  N  ND1   . HIS A 1  874  ? -42.719 82.721  92.123  1.00 24.70 ? 872  HIS A ND1   1 
ATOM   6295  C  CD2   . HIS A 1  874  ? -41.526 84.550  92.232  1.00 25.90 ? 872  HIS A CD2   1 
ATOM   6296  C  CE1   . HIS A 1  874  ? -43.427 83.611  92.795  1.00 24.00 ? 872  HIS A CE1   1 
ATOM   6297  N  NE2   . HIS A 1  874  ? -42.730 84.731  92.869  1.00 23.43 ? 872  HIS A NE2   1 
ATOM   6298  N  N     . ILE A 1  875  ? -38.432 85.246  91.838  1.00 19.16 ? 873  ILE A N     1 
ATOM   6299  C  CA    . ILE A 1  875  ? -37.751 85.963  92.909  1.00 20.96 ? 873  ILE A CA    1 
ATOM   6300  C  C     . ILE A 1  875  ? -38.808 86.622  93.778  1.00 21.69 ? 873  ILE A C     1 
ATOM   6301  O  O     . ILE A 1  875  ? -39.750 87.241  93.261  1.00 22.83 ? 873  ILE A O     1 
ATOM   6302  C  CB    . ILE A 1  875  ? -36.756 87.000  92.362  1.00 22.98 ? 873  ILE A CB    1 
ATOM   6303  C  CG1   . ILE A 1  875  ? -35.496 86.319  91.828  1.00 26.36 ? 873  ILE A CG1   1 
ATOM   6304  C  CG2   . ILE A 1  875  ? -36.300 87.952  93.462  1.00 25.24 ? 873  ILE A CG2   1 
ATOM   6305  C  CD1   . ILE A 1  875  ? -35.653 85.540  90.545  1.00 25.83 ? 873  ILE A CD1   1 
ATOM   6306  N  N     . GLY A 1  876  ? -38.671 86.488  95.091  1.00 21.77 ? 874  GLY A N     1 
ATOM   6307  C  CA    . GLY A 1  876  ? -39.617 87.134  95.976  1.00 20.81 ? 874  GLY A CA    1 
ATOM   6308  C  C     . GLY A 1  876  ? -39.426 86.713  97.420  1.00 23.22 ? 874  GLY A C     1 
ATOM   6309  O  O     . GLY A 1  876  ? -38.472 86.015  97.770  1.00 21.81 ? 874  GLY A O     1 
ATOM   6310  N  N     . ARG A 1  877  ? -40.358 87.175  98.258  1.00 23.30 ? 875  ARG A N     1 
ATOM   6311  C  CA    . ARG A 1  877  ? -40.362 86.781  99.659  1.00 23.01 ? 875  ARG A CA    1 
ATOM   6312  C  C     . ARG A 1  877  ? -40.504 85.269  99.757  1.00 22.04 ? 875  ARG A C     1 
ATOM   6313  O  O     . ARG A 1  877  ? -41.323 84.664  99.058  1.00 22.07 ? 875  ARG A O     1 
ATOM   6314  C  CB    . ARG A 1  877  ? -41.499 87.489  100.403 1.00 26.13 ? 875  ARG A CB    1 
ATOM   6315  C  CG    . ARG A 1  877  ? -41.303 87.517  101.903 1.00 26.15 ? 875  ARG A CG    1 
ATOM   6316  C  CD    . ARG A 1  877  ? -42.398 88.327  102.567 1.00 29.27 ? 875  ARG A CD    1 
ATOM   6317  N  NE    . ARG A 1  877  ? -43.610 87.547  102.763 1.00 28.15 ? 875  ARG A NE    1 
ATOM   6318  C  CZ    . ARG A 1  877  ? -44.677 87.997  103.407 1.00 35.94 ? 875  ARG A CZ    1 
ATOM   6319  N  NH1   . ARG A 1  877  ? -44.718 89.225  103.897 1.00 32.71 ? 875  ARG A NH1   1 
ATOM   6320  N  NH2   . ARG A 1  877  ? -45.730 87.196  103.559 1.00 35.26 ? 875  ARG A NH2   1 
ATOM   6321  N  N     . THR A 1  878  ? -39.692 84.650  100.608 1.00 21.07 ? 876  THR A N     1 
ATOM   6322  C  CA    . THR A 1  878  ? -39.442 83.218  100.499 1.00 19.48 ? 876  THR A CA    1 
ATOM   6323  C  C     . THR A 1  878  ? -40.457 82.356  101.233 1.00 22.14 ? 876  THR A C     1 
ATOM   6324  O  O     . THR A 1  878  ? -40.283 81.132  101.277 1.00 22.00 ? 876  THR A O     1 
ATOM   6325  C  CB    . THR A 1  878  ? -38.037 82.894  101.004 1.00 19.18 ? 876  THR A CB    1 
ATOM   6326  O  OG1   . THR A 1  878  ? -37.811 83.577  102.242 1.00 24.46 ? 876  THR A OG1   1 
ATOM   6327  C  CG2   . THR A 1  878  ? -37.023 83.349  99.998  1.00 23.76 ? 876  THR A CG2   1 
ATOM   6328  N  N     . ASP A 1  879  ? -41.514 82.945  101.795 1.00 21.22 ? 877  ASP A N     1 
ATOM   6329  C  CA    . ASP A 1  879  ? -42.537 82.138  102.447 1.00 24.51 ? 877  ASP A CA    1 
ATOM   6330  C  C     . ASP A 1  879  ? -43.577 81.614  101.457 1.00 24.09 ? 877  ASP A C     1 
ATOM   6331  O  O     . ASP A 1  879  ? -44.729 81.364  101.838 1.00 21.65 ? 877  ASP A O     1 
ATOM   6332  C  CB    . ASP A 1  879  ? -43.182 82.925  103.590 1.00 22.14 ? 877  ASP A CB    1 
ATOM   6333  C  CG    . ASP A 1  879  ? -43.897 84.183  103.118 1.00 29.50 ? 877  ASP A CG    1 
ATOM   6334  O  OD1   . ASP A 1  879  ? -43.393 84.864  102.193 1.00 30.72 ? 877  ASP A OD1   1 
ATOM   6335  O  OD2   . ASP A 1  879  ? -44.969 84.488  103.680 1.00 28.43 ? 877  ASP A OD2   1 
ATOM   6336  N  N     . ARG A 1  880  ? -43.185 81.437  100.193 1.00 22.03 ? 878  ARG A N     1 
ATOM   6337  C  CA    . ARG A 1  880  ? -43.996 80.796  99.162  1.00 22.03 ? 878  ARG A CA    1 
ATOM   6338  C  C     . ARG A 1  880  ? -43.149 79.711  98.521  1.00 20.48 ? 878  ARG A C     1 
ATOM   6339  O  O     . ARG A 1  880  ? -42.006 79.973  98.127  1.00 21.40 ? 878  ARG A O     1 
ATOM   6340  C  CB    . ARG A 1  880  ? -44.455 81.781  98.080  1.00 24.58 ? 878  ARG A CB    1 
ATOM   6341  C  CG    . ARG A 1  880  ? -45.653 82.652  98.429  1.00 31.93 ? 878  ARG A CG    1 
ATOM   6342  C  CD    . ARG A 1  880  ? -45.918 83.639  97.285  1.00 34.98 ? 878  ARG A CD    1 
ATOM   6343  N  NE    . ARG A 1  880  ? -47.305 84.094  97.232  1.00 47.66 ? 878  ARG A NE    1 
ATOM   6344  C  CZ    . ARG A 1  880  ? -47.841 84.991  98.051  1.00 45.89 ? 878  ARG A CZ    1 
ATOM   6345  N  NH1   . ARG A 1  880  ? -47.152 85.514  99.053  1.00 46.37 ? 878  ARG A NH1   1 
ATOM   6346  N  NH2   . ARG A 1  880  ? -49.106 85.366  97.866  1.00 45.37 ? 878  ARG A NH2   1 
ATOM   6347  N  N     . LEU A 1  881  ? -43.710 78.498  98.400  1.00 19.58 ? 879  LEU A N     1 
ATOM   6348  C  CA    . LEU A 1  881  ? -42.970 77.392  97.793  1.00 19.61 ? 879  LEU A CA    1 
ATOM   6349  C  C     . LEU A 1  881  ? -42.549 77.712  96.368  1.00 18.47 ? 879  LEU A C     1 
ATOM   6350  O  O     . LEU A 1  881  ? -41.516 77.211  95.893  1.00 18.34 ? 879  LEU A O     1 
ATOM   6351  C  CB    . LEU A 1  881  ? -43.812 76.119  97.819  1.00 20.68 ? 879  LEU A CB    1 
ATOM   6352  C  CG    . LEU A 1  881  ? -43.216 74.840  97.244  1.00 20.92 ? 879  LEU A CG    1 
ATOM   6353  C  CD1   . LEU A 1  881  ? -42.002 74.411  98.060  1.00 21.33 ? 879  LEU A CD1   1 
ATOM   6354  C  CD2   . LEU A 1  881  ? -44.283 73.748  97.207  1.00 20.96 ? 879  LEU A CD2   1 
ATOM   6355  N  N     . SER A 1  882  ? -43.320 78.551  95.673  1.00 18.46 ? 880  SER A N     1 
ATOM   6356  C  CA    . SER A 1  882  ? -43.003 78.869  94.286  1.00 19.49 ? 880  SER A CA    1 
ATOM   6357  C  C     . SER A 1  882  ? -41.808 79.796  94.144  1.00 19.90 ? 880  SER A C     1 
ATOM   6358  O  O     . SER A 1  882  ? -41.346 79.999  93.021  1.00 19.64 ? 880  SER A O     1 
ATOM   6359  C  CB    . SER A 1  882  ? -44.212 79.504  93.592  1.00 21.12 ? 880  SER A CB    1 
ATOM   6360  O  OG    . SER A 1  882  ? -44.560 80.726  94.220  1.00 21.39 ? 880  SER A OG    1 
ATOM   6361  N  N     . VAL A 1  883  ? -41.290 80.353  95.235  1.00 20.47 ? 881  VAL A N     1 
ATOM   6362  C  CA    . VAL A 1  883  ? -40.160 81.270  95.138  1.00 20.85 ? 881  VAL A CA    1 
ATOM   6363  C  C     . VAL A 1  883  ? -38.871 80.471  95.039  1.00 20.29 ? 881  VAL A C     1 
ATOM   6364  O  O     . VAL A 1  883  ? -38.600 79.595  95.869  1.00 22.36 ? 881  VAL A O     1 
ATOM   6365  C  CB    . VAL A 1  883  ? -40.119 82.234  96.334  1.00 20.26 ? 881  VAL A CB    1 
ATOM   6366  C  CG1   . VAL A 1  883  ? -38.785 82.982  96.329  1.00 20.11 ? 881  VAL A CG1   1 
ATOM   6367  C  CG2   . VAL A 1  883  ? -41.279 83.211  96.241  1.00 21.38 ? 881  VAL A CG2   1 
ATOM   6368  N  N     . ASP A 1  884  ? -38.079 80.767  94.012  1.00 19.55 ? 882  ASP A N     1 
ATOM   6369  C  CA    . ASP A 1  884  ? -36.795 80.109  93.797  1.00 20.06 ? 882  ASP A CA    1 
ATOM   6370  C  C     . ASP A 1  884  ? -35.645 80.844  94.456  1.00 22.24 ? 882  ASP A C     1 
ATOM   6371  O  O     . ASP A 1  884  ? -34.722 80.213  94.989  1.00 23.68 ? 882  ASP A O     1 
ATOM   6372  C  CB    . ASP A 1  884  ? -36.511 80.014  92.303  1.00 20.10 ? 882  ASP A CB    1 
ATOM   6373  C  CG    . ASP A 1  884  ? -37.570 79.250  91.571  1.00 17.93 ? 882  ASP A CG    1 
ATOM   6374  O  OD1   . ASP A 1  884  ? -37.797 78.083  91.949  1.00 20.02 ? 882  ASP A OD1   1 
ATOM   6375  O  OD2   . ASP A 1  884  ? -38.157 79.824  90.639  1.00 19.23 ? 882  ASP A OD2   1 
ATOM   6376  N  N     . VAL A 1  885  ? -35.674 82.170  94.385  1.00 20.21 ? 883  VAL A N     1 
ATOM   6377  C  CA    . VAL A 1  885  ? -34.555 83.021  94.759  1.00 20.32 ? 883  VAL A CA    1 
ATOM   6378  C  C     . VAL A 1  885  ? -35.101 84.101  95.680  1.00 19.50 ? 883  VAL A C     1 
ATOM   6379  O  O     . VAL A 1  885  ? -36.028 84.827  95.307  1.00 21.13 ? 883  VAL A O     1 
ATOM   6380  C  CB    . VAL A 1  885  ? -33.882 83.640  93.522  1.00 20.61 ? 883  VAL A CB    1 
ATOM   6381  C  CG1   . VAL A 1  885  ? -32.777 84.613  93.929  1.00 19.78 ? 883  VAL A CG1   1 
ATOM   6382  C  CG2   . VAL A 1  885  ? -33.343 82.543  92.604  1.00 21.97 ? 883  VAL A CG2   1 
ATOM   6383  N  N     . GLY A 1  886  ? -34.545 84.193  96.884  1.00 18.91 ? 884  GLY A N     1 
ATOM   6384  C  CA    . GLY A 1  886  ? -34.989 85.167  97.849  1.00 18.31 ? 884  GLY A CA    1 
ATOM   6385  C  C     . GLY A 1  886  ? -34.165 86.434  97.824  1.00 19.54 ? 884  GLY A C     1 
ATOM   6386  O  O     . GLY A 1  886  ? -33.426 86.709  96.876  1.00 20.76 ? 884  GLY A O     1 
ATOM   6387  N  N     . PRO A 1  887  ? -34.276 87.230  98.877  1.00 20.33 ? 885  PRO A N     1 
ATOM   6388  C  CA    . PRO A 1  887  ? -33.598 88.526  98.913  1.00 19.46 ? 885  PRO A CA    1 
ATOM   6389  C  C     . PRO A 1  887  ? -32.124 88.380  99.263  1.00 19.83 ? 885  PRO A C     1 
ATOM   6390  O  O     . PRO A 1  887  ? -31.660 87.338  99.725  1.00 21.38 ? 885  PRO A O     1 
ATOM   6391  C  CB    . PRO A 1  887  ? -34.350 89.261  100.025 1.00 20.60 ? 885  PRO A CB    1 
ATOM   6392  C  CG    . PRO A 1  887  ? -34.678 88.163  100.986 1.00 20.83 ? 885  PRO A CG    1 
ATOM   6393  C  CD    . PRO A 1  887  ? -35.051 86.985  100.111 1.00 21.96 ? 885  PRO A CD    1 
ATOM   6394  N  N     . VAL A 1  888  ? -31.386 89.463  99.020  1.00 20.51 ? 886  VAL A N     1 
ATOM   6395  C  CA    . VAL A 1  888  ? -30.090 89.615  99.660  1.00 21.04 ? 886  VAL A CA    1 
ATOM   6396  C  C     . VAL A 1  888  ? -30.296 90.156  101.074 1.00 23.42 ? 886  VAL A C     1 
ATOM   6397  O  O     . VAL A 1  888  ? -31.336 90.728  101.410 1.00 21.36 ? 886  VAL A O     1 
ATOM   6398  C  CB    . VAL A 1  888  ? -29.138 90.505  98.834  1.00 22.19 ? 886  VAL A CB    1 
ATOM   6399  C  CG1   . VAL A 1  888  ? -28.933 89.902  97.439  1.00 23.31 ? 886  VAL A CG1   1 
ATOM   6400  C  CG2   . VAL A 1  888  ? -29.648 91.908  98.723  1.00 23.81 ? 886  VAL A CG2   1 
ATOM   6401  N  N     . ILE A 1  889  ? -29.294 89.940  101.926 1.00 21.64 ? 887  ILE A N     1 
ATOM   6402  C  CA    . ILE A 1  889  ? -29.547 89.986  103.364 1.00 23.09 ? 887  ILE A CA    1 
ATOM   6403  C  C     . ILE A 1  889  ? -29.815 91.410  103.846 1.00 25.75 ? 887  ILE A C     1 
ATOM   6404  O  O     . ILE A 1  889  ? -30.621 91.618  104.763 1.00 24.86 ? 887  ILE A O     1 
ATOM   6405  C  CB    . ILE A 1  889  ? -28.380 89.332  104.128 1.00 21.84 ? 887  ILE A CB    1 
ATOM   6406  C  CG1   . ILE A 1  889  ? -28.712 89.249  105.625 1.00 23.45 ? 887  ILE A CG1   1 
ATOM   6407  C  CG2   . ILE A 1  889  ? -27.074 90.078  103.874 1.00 21.64 ? 887  ILE A CG2   1 
ATOM   6408  C  CD1   . ILE A 1  889  ? -29.908 88.375  105.952 1.00 22.63 ? 887  ILE A CD1   1 
ATOM   6409  N  N     . THR A 1  890  ? -29.147 92.408  103.260 1.00 21.29 ? 888  THR A N     1 
ATOM   6410  C  CA    . THR A 1  890  ? -29.280 93.793  103.716 1.00 21.91 ? 888  THR A CA    1 
ATOM   6411  C  C     . THR A 1  890  ? -29.265 94.748  102.532 1.00 23.68 ? 888  THR A C     1 
ATOM   6412  O  O     . THR A 1  890  ? -28.855 94.399  101.421 1.00 23.88 ? 888  THR A O     1 
ATOM   6413  C  CB    . THR A 1  890  ? -28.144 94.222  104.658 1.00 25.35 ? 888  THR A CB    1 
ATOM   6414  O  OG1   . THR A 1  890  ? -26.898 94.119  103.961 1.00 25.20 ? 888  THR A OG1   1 
ATOM   6415  C  CG2   . THR A 1  890  ? -28.108 93.387  105.928 1.00 26.11 ? 888  THR A CG2   1 
ATOM   6416  N  N     . SER A 1  891  ? -29.673 95.991  102.806 1.00 23.88 ? 889  SER A N     1 
ATOM   6417  C  CA    A SER A 1  891  ? -29.560 97.055  101.812 0.50 25.57 ? 889  SER A CA    1 
ATOM   6418  C  CA    B SER A 1  891  ? -29.565 97.032  101.792 0.50 25.56 ? 889  SER A CA    1 
ATOM   6419  C  C     . SER A 1  891  ? -28.110 97.327  101.454 1.00 27.18 ? 889  SER A C     1 
ATOM   6420  O  O     . SER A 1  891  ? -27.804 97.680  100.311 1.00 27.13 ? 889  SER A O     1 
ATOM   6421  C  CB    A SER A 1  891  ? -30.201 98.344  102.331 0.50 27.13 ? 889  SER A CB    1 
ATOM   6422  C  CB    B SER A 1  891  ? -30.271 98.306  102.260 0.50 27.13 ? 889  SER A CB    1 
ATOM   6423  O  OG    A SER A 1  891  ? -31.585 98.181  102.545 0.50 25.18 ? 889  SER A OG    1 
ATOM   6424  O  OG    B SER A 1  891  ? -29.631 98.847  103.398 0.50 30.26 ? 889  SER A OG    1 
ATOM   6425  N  N     . GLU A 1  892  ? -27.206 97.188  102.429 1.00 26.11 ? 890  GLU A N     1 
ATOM   6426  C  CA    . GLU A 1  892  ? -25.790 97.406  102.156 1.00 27.65 ? 890  GLU A CA    1 
ATOM   6427  C  C     . GLU A 1  892  ? -25.251 96.338  101.219 1.00 28.99 ? 890  GLU A C     1 
ATOM   6428  O  O     . GLU A 1  892  ? -24.471 96.638  100.307 1.00 29.54 ? 890  GLU A O     1 
ATOM   6429  C  CB    . GLU A 1  892  ? -24.991 97.410  103.459 1.00 28.33 ? 890  GLU A CB    1 
ATOM   6430  C  CG    . GLU A 1  892  ? -25.482 98.402  104.494 1.00 36.06 ? 890  GLU A CG    1 
ATOM   6431  C  CD    . GLU A 1  892  ? -26.425 97.769  105.506 1.00 35.90 ? 890  GLU A CD    1 
ATOM   6432  O  OE1   . GLU A 1  892  ? -27.604 97.556  105.175 1.00 33.67 ? 890  GLU A OE1   1 
ATOM   6433  O  OE2   . GLU A 1  892  ? -25.978 97.481  106.639 1.00 44.80 ? 890  GLU A OE2   1 
ATOM   6434  N  N     . ALA A 1  893  ? -25.637 95.082  101.446 1.00 26.62 ? 891  ALA A N     1 
ATOM   6435  C  CA    . ALA A 1  893  ? -25.241 94.022  100.528 1.00 25.61 ? 891  ALA A CA    1 
ATOM   6436  C  C     . ALA A 1  893  ? -25.791 94.293  99.140  1.00 27.20 ? 891  ALA A C     1 
ATOM   6437  O  O     . ALA A 1  893  ? -25.065 94.188  98.148  1.00 26.79 ? 891  ALA A O     1 
ATOM   6438  C  CB    . ALA A 1  893  ? -25.710 92.667  101.049 1.00 21.45 ? 891  ALA A CB    1 
ATOM   6439  N  N     . LYS A 1  894  ? -27.065 94.688  99.059  1.00 25.56 ? 892  LYS A N     1 
ATOM   6440  C  CA    . LYS A 1  894  ? -27.665 95.036  97.775  1.00 24.96 ? 892  LYS A CA    1 
ATOM   6441  C  C     . LYS A 1  894  ? -26.871 96.134  97.078  1.00 28.37 ? 892  LYS A C     1 
ATOM   6442  O  O     . LYS A 1  894  ? -26.541 96.023  95.892  1.00 26.55 ? 892  LYS A O     1 
ATOM   6443  C  CB    . LYS A 1  894  ? -29.119 95.466  97.984  1.00 23.81 ? 892  LYS A CB    1 
ATOM   6444  C  CG    . LYS A 1  894  ? -29.833 95.895  96.717  1.00 28.94 ? 892  LYS A CG    1 
ATOM   6445  C  CD    . LYS A 1  894  ? -31.249 96.345  97.027  1.00 29.21 ? 892  LYS A CD    1 
ATOM   6446  C  CE    . LYS A 1  894  ? -32.001 96.721  95.763  1.00 30.03 ? 892  LYS A CE    1 
ATOM   6447  N  NZ    . LYS A 1  894  ? -33.235 97.468  96.089  1.00 42.33 ? 892  LYS A NZ    1 
ATOM   6448  N  N     . ASP A 1  895  ? -26.527 97.195  97.812  1.00 27.38 ? 893  ASP A N     1 
ATOM   6449  C  CA    . ASP A 1  895  ? -25.798 98.301  97.201  1.00 30.20 ? 893  ASP A CA    1 
ATOM   6450  C  C     . ASP A 1  895  ? -24.434 97.849  96.694  1.00 27.90 ? 893  ASP A C     1 
ATOM   6451  O  O     . ASP A 1  895  ? -24.007 98.245  95.603  1.00 28.42 ? 893  ASP A O     1 
ATOM   6452  C  CB    . ASP A 1  895  ? -25.641 99.452  98.200  1.00 29.89 ? 893  ASP A CB    1 
ATOM   6453  C  CG    . ASP A 1  895  ? -26.973 100.114 98.570  1.00 34.78 ? 893  ASP A CG    1 
ATOM   6454  O  OD1   . ASP A 1  895  ? -27.966 99.973  97.820  1.00 40.05 ? 893  ASP A OD1   1 
ATOM   6455  O  OD2   . ASP A 1  895  ? -27.022 100.796 99.618  1.00 40.99 ? 893  ASP A OD2   1 
ATOM   6456  N  N     . ASN A 1  896  ? -23.733 97.022  97.473  1.00 28.04 ? 894  ASN A N     1 
ATOM   6457  C  CA    . ASN A 1  896  ? -22.423 96.538  97.047  1.00 27.67 ? 894  ASN A CA    1 
ATOM   6458  C  C     . ASN A 1  896  ? -22.527 95.701  95.783  1.00 28.12 ? 894  ASN A C     1 
ATOM   6459  O  O     . ASN A 1  896  ? -21.707 95.838  94.866  1.00 27.28 ? 894  ASN A O     1 
ATOM   6460  C  CB    . ASN A 1  896  ? -21.772 95.706  98.148  1.00 29.43 ? 894  ASN A CB    1 
ATOM   6461  C  CG    . ASN A 1  896  ? -21.557 96.479  99.419  1.00 37.15 ? 894  ASN A CG    1 
ATOM   6462  O  OD1   . ASN A 1  896  ? -21.364 97.697  99.400  1.00 44.29 ? 894  ASN A OD1   1 
ATOM   6463  N  ND2   . ASN A 1  896  ? -21.572 95.767  100.545 1.00 37.70 ? 894  ASN A ND2   1 
ATOM   6464  N  N     . ILE A 1  897  ? -23.513 94.804  95.734  1.00 26.07 ? 895  ILE A N     1 
ATOM   6465  C  CA    . ILE A 1  897  ? -23.685 93.942  94.569  1.00 24.09 ? 895  ILE A CA    1 
ATOM   6466  C  C     . ILE A 1  897  ? -24.054 94.776  93.352  1.00 26.94 ? 895  ILE A C     1 
ATOM   6467  O  O     . ILE A 1  897  ? -23.491 94.606  92.264  1.00 25.32 ? 895  ILE A O     1 
ATOM   6468  C  CB    . ILE A 1  897  ? -24.748 92.866  94.853  1.00 24.33 ? 895  ILE A CB    1 
ATOM   6469  C  CG1   . ILE A 1  897  ? -24.349 92.001  96.049  1.00 23.83 ? 895  ILE A CG1   1 
ATOM   6470  C  CG2   . ILE A 1  897  ? -24.967 91.991  93.627  1.00 25.37 ? 895  ILE A CG2   1 
ATOM   6471  C  CD1   . ILE A 1  897  ? -25.534 91.268  96.654  1.00 22.77 ? 895  ILE A CD1   1 
ATOM   6472  N  N     . GLU A 1  898  ? -24.998 95.706  93.527  1.00 25.71 ? 896  GLU A N     1 
ATOM   6473  C  CA    . GLU A 1  898  ? -25.446 96.529  92.410  1.00 28.04 ? 896  GLU A CA    1 
ATOM   6474  C  C     . GLU A 1  898  ? -24.321 97.415  91.887  1.00 26.77 ? 896  GLU A C     1 
ATOM   6475  O  O     . GLU A 1  898  ? -24.223 97.655  90.678  1.00 29.15 ? 896  GLU A O     1 
ATOM   6476  C  CB    . GLU A 1  898  ? -26.652 97.372  92.832  1.00 27.67 ? 896  GLU A CB    1 
ATOM   6477  C  CG    . GLU A 1  898  ? -27.953 96.580  92.957  1.00 29.70 ? 896  GLU A CG    1 
ATOM   6478  C  CD    . GLU A 1  898  ? -29.131 97.448  93.383  1.00 31.17 ? 896  GLU A CD    1 
ATOM   6479  O  OE1   . GLU A 1  898  ? -28.897 98.509  93.995  1.00 39.79 ? 896  GLU A OE1   1 
ATOM   6480  O  OE2   . GLU A 1  898  ? -30.286 97.071  93.102  1.00 39.90 ? 896  GLU A OE2   1 
ATOM   6481  N  N     . LYS A 1  899  ? -23.469 97.921  92.782  1.00 28.55 ? 897  LYS A N     1 
ATOM   6482  C  CA    . LYS A 1  899  ? -22.331 98.717  92.339  1.00 27.98 ? 897  LYS A CA    1 
ATOM   6483  C  C     . LYS A 1  899  ? -21.425 97.907  91.421  1.00 30.44 ? 897  LYS A C     1 
ATOM   6484  O  O     . LYS A 1  899  ? -20.918 98.425  90.418  1.00 30.46 ? 897  LYS A O     1 
ATOM   6485  C  CB    . LYS A 1  899  ? -21.541 99.230  93.544  1.00 28.76 ? 897  LYS A CB    1 
ATOM   6486  N  N     . HIS A 1  900  ? -21.214 96.633  91.748  1.00 26.04 ? 898  HIS A N     1 
ATOM   6487  C  CA    . HIS A 1  900  ? -20.383 95.791  90.893  1.00 26.77 ? 898  HIS A CA    1 
ATOM   6488  C  C     . HIS A 1  900  ? -21.040 95.575  89.536  1.00 26.21 ? 898  HIS A C     1 
ATOM   6489  O  O     . HIS A 1  900  ? -20.382 95.669  88.496  1.00 28.59 ? 898  HIS A O     1 
ATOM   6490  C  CB    . HIS A 1  900  ? -20.116 94.451  91.572  1.00 27.06 ? 898  HIS A CB    1 
ATOM   6491  C  CG    . HIS A 1  900  ? -19.514 93.434  90.660  1.00 26.50 ? 898  HIS A CG    1 
ATOM   6492  N  ND1   . HIS A 1  900  ? -18.173 93.422  90.347  1.00 25.81 ? 898  HIS A ND1   1 
ATOM   6493  C  CD2   . HIS A 1  900  ? -20.074 92.413  89.969  1.00 24.05 ? 898  HIS A CD2   1 
ATOM   6494  C  CE1   . HIS A 1  900  ? -17.929 92.427  89.512  1.00 27.15 ? 898  HIS A CE1   1 
ATOM   6495  N  NE2   . HIS A 1  900  ? -19.065 91.801  89.265  1.00 26.04 ? 898  HIS A NE2   1 
ATOM   6496  N  N     . ILE A 1  901  ? -22.340 95.282  89.533  1.00 24.88 ? 899  ILE A N     1 
ATOM   6497  C  CA    . ILE A 1  901  ? -23.055 95.071  88.280  1.00 28.16 ? 899  ILE A CA    1 
ATOM   6498  C  C     . ILE A 1  901  ? -22.928 96.298  87.387  1.00 30.88 ? 899  ILE A C     1 
ATOM   6499  O  O     . ILE A 1  901  ? -22.646 96.192  86.187  1.00 30.73 ? 899  ILE A O     1 
ATOM   6500  C  CB    . ILE A 1  901  ? -24.527 94.734  88.567  1.00 26.51 ? 899  ILE A CB    1 
ATOM   6501  C  CG1   . ILE A 1  901  ? -24.621 93.377  89.284  1.00 25.12 ? 899  ILE A CG1   1 
ATOM   6502  C  CG2   . ILE A 1  901  ? -25.335 94.795  87.280  1.00 27.11 ? 899  ILE A CG2   1 
ATOM   6503  C  CD1   . ILE A 1  901  ? -26.039 93.019  89.794  1.00 21.91 ? 899  ILE A CD1   1 
ATOM   6504  N  N     . GLU A 1  902  ? -23.114 97.484  87.967  1.00 29.47 ? 900  GLU A N     1 
ATOM   6505  C  CA    . GLU A 1  902  ? -23.095 98.694  87.153  1.00 32.18 ? 900  GLU A CA    1 
ATOM   6506  C  C     . GLU A 1  902  ? -21.691 99.035  86.675  1.00 31.67 ? 900  GLU A C     1 
ATOM   6507  O  O     . GLU A 1  902  ? -21.534 99.567  85.572  1.00 34.01 ? 900  GLU A O     1 
ATOM   6508  C  CB    . GLU A 1  902  ? -23.712 99.855  87.928  1.00 33.71 ? 900  GLU A CB    1 
ATOM   6509  C  CG    . GLU A 1  902  ? -25.209 99.683  88.131  1.00 33.44 ? 900  GLU A CG    1 
ATOM   6510  C  CD    . GLU A 1  902  ? -25.929 99.292  86.847  1.00 39.64 ? 900  GLU A CD    1 
ATOM   6511  O  OE1   . GLU A 1  902  ? -25.750 99.983  85.820  1.00 40.91 ? 900  GLU A OE1   1 
ATOM   6512  O  OE2   . GLU A 1  902  ? -26.665 98.281  86.861  1.00 36.86 ? 900  GLU A OE2   1 
ATOM   6513  N  N     . ARG A 1  903  ? -20.666 98.739  87.478  1.00 32.21 ? 901  ARG A N     1 
ATOM   6514  C  CA    . ARG A 1  903  ? -19.293 98.870  86.999  1.00 32.88 ? 901  ARG A CA    1 
ATOM   6515  C  C     . ARG A 1  903  ? -19.056 97.994  85.772  1.00 35.04 ? 901  ARG A C     1 
ATOM   6516  O  O     . ARG A 1  903  ? -18.517 98.457  84.759  1.00 36.73 ? 901  ARG A O     1 
ATOM   6517  C  CB    . ARG A 1  903  ? -18.312 98.514  88.113  1.00 33.85 ? 901  ARG A CB    1 
ATOM   6518  N  N     . MET A 1  904  ? -19.463 96.722  85.845  1.00 32.88 ? 902  MET A N     1 
ATOM   6519  C  CA    . MET A 1  904  ? -19.345 95.827  84.695  1.00 33.69 ? 902  MET A CA    1 
ATOM   6520  C  C     . MET A 1  904  ? -20.104 96.366  83.490  1.00 32.62 ? 902  MET A C     1 
ATOM   6521  O  O     . MET A 1  904  ? -19.585 96.376  82.368  1.00 34.37 ? 902  MET A O     1 
ATOM   6522  C  CB    . MET A 1  904  ? -19.865 94.436  85.057  1.00 29.37 ? 902  MET A CB    1 
ATOM   6523  C  CG    . MET A 1  904  ? -19.062 93.729  86.115  1.00 28.75 ? 902  MET A CG    1 
ATOM   6524  S  SD    . MET A 1  904  ? -17.358 93.467  85.591  1.00 36.93 ? 902  MET A SD    1 
ATOM   6525  C  CE    . MET A 1  904  ? -16.490 94.610  86.667  1.00 37.13 ? 902  MET A CE    1 
ATOM   6526  N  N     . ARG A 1  905  ? -21.353 96.792  83.701  1.00 30.93 ? 903  ARG A N     1 
ATOM   6527  C  CA    . ARG A 1  905  ? -22.139 97.346  82.605  1.00 33.83 ? 903  ARG A CA    1 
ATOM   6528  C  C     . ARG A 1  905  ? -21.464 98.583  82.027  1.00 38.77 ? 903  ARG A C     1 
ATOM   6529  O  O     . ARG A 1  905  ? -21.502 98.807  80.812  1.00 38.04 ? 903  ARG A O     1 
ATOM   6530  C  CB    . ARG A 1  905  ? -23.551 97.676  83.087  1.00 33.09 ? 903  ARG A CB    1 
ATOM   6531  C  CG    . ARG A 1  905  ? -24.589 97.751  81.977  1.00 37.04 ? 903  ARG A CG    1 
ATOM   6532  C  CD    . ARG A 1  905  ? -25.882 98.352  82.473  1.00 35.07 ? 903  ARG A CD    1 
ATOM   6533  N  NE    . ARG A 1  905  ? -26.338 97.758  83.725  1.00 35.51 ? 903  ARG A NE    1 
ATOM   6534  C  CZ    . ARG A 1  905  ? -27.255 96.803  83.814  1.00 35.27 ? 903  ARG A CZ    1 
ATOM   6535  N  NH1   . ARG A 1  905  ? -27.790 96.254  82.733  1.00 34.06 ? 903  ARG A NH1   1 
ATOM   6536  N  NH2   . ARG A 1  905  ? -27.656 96.399  85.018  1.00 34.14 ? 903  ARG A NH2   1 
ATOM   6537  N  N     . GLY A 1  906  ? -20.823 99.384  82.883  1.00 35.90 ? 904  GLY A N     1 
ATOM   6538  C  CA    . GLY A 1  906  ? -20.153 100.584 82.415  1.00 39.63 ? 904  GLY A CA    1 
ATOM   6539  C  C     . GLY A 1  906  ? -18.953 100.301 81.535  1.00 41.06 ? 904  GLY A C     1 
ATOM   6540  O  O     . GLY A 1  906  ? -18.579 101.135 80.707  1.00 45.98 ? 904  GLY A O     1 
ATOM   6541  N  N     . LEU A 1  907  ? -18.333 99.134  81.694  1.00 40.44 ? 905  LEU A N     1 
ATOM   6542  C  CA    . LEU A 1  907  ? -17.226 98.737  80.832  1.00 39.92 ? 905  LEU A CA    1 
ATOM   6543  C  C     . LEU A 1  907  ? -17.692 98.155  79.504  1.00 40.01 ? 905  LEU A C     1 
ATOM   6544  O  O     . LEU A 1  907  ? -16.851 97.768  78.686  1.00 40.43 ? 905  LEU A O     1 
ATOM   6545  C  CB    . LEU A 1  907  ? -16.340 97.724  81.553  1.00 40.75 ? 905  LEU A CB    1 
ATOM   6546  C  CG    . LEU A 1  907  ? -15.761 98.194  82.887  1.00 41.43 ? 905  LEU A CG    1 
ATOM   6547  C  CD1   . LEU A 1  907  ? -14.953 97.079  83.528  1.00 42.84 ? 905  LEU A CD1   1 
ATOM   6548  C  CD2   . LEU A 1  907  ? -14.918 99.449  82.700  1.00 45.64 ? 905  LEU A CD2   1 
ATOM   6549  N  N     . GLY A 1  908  ? -18.999 98.077  79.274  1.00 35.54 ? 906  GLY A N     1 
ATOM   6550  C  CA    . GLY A 1  908  ? -19.534 97.517  78.054  1.00 38.91 ? 906  GLY A CA    1 
ATOM   6551  C  C     . GLY A 1  908  ? -19.806 96.027  78.085  1.00 33.33 ? 906  GLY A C     1 
ATOM   6552  O  O     . GLY A 1  908  ? -20.193 95.469  77.054  1.00 34.92 ? 906  GLY A O     1 
ATOM   6553  N  N     . ARG A 1  909  ? -19.617 95.366  79.224  1.00 33.03 ? 907  ARG A N     1 
ATOM   6554  C  CA    . ARG A 1  909  ? -19.900 93.942  79.313  1.00 27.89 ? 907  ARG A CA    1 
ATOM   6555  C  C     . ARG A 1  909  ? -21.400 93.690  79.197  1.00 30.47 ? 907  ARG A C     1 
ATOM   6556  O  O     . ARG A 1  909  ? -22.218 94.451  79.725  1.00 32.09 ? 907  ARG A O     1 
ATOM   6557  C  CB    . ARG A 1  909  ? -19.371 93.383  80.633  1.00 30.86 ? 907  ARG A CB    1 
ATOM   6558  C  CG    . ARG A 1  909  ? -17.923 93.728  80.918  1.00 31.31 ? 907  ARG A CG    1 
ATOM   6559  C  CD    . ARG A 1  909  ? -16.977 93.015  79.966  1.00 35.56 ? 907  ARG A CD    1 
ATOM   6560  N  NE    . ARG A 1  909  ? -15.586 93.158  80.388  1.00 41.06 ? 907  ARG A NE    1 
ATOM   6561  C  CZ    . ARG A 1  909  ? -14.731 94.040  79.885  1.00 45.57 ? 907  ARG A CZ    1 
ATOM   6562  N  NH1   . ARG A 1  909  ? -15.082 94.867  78.913  1.00 45.82 ? 907  ARG A NH1   1 
ATOM   6563  N  NH2   . ARG A 1  909  ? -13.494 94.095  80.372  1.00 42.37 ? 907  ARG A NH2   1 
ATOM   6564  N  N     . LYS A 1  910  ? -21.762 92.613  78.499  1.00 26.65 ? 908  LYS A N     1 
ATOM   6565  C  CA    . LYS A 1  910  ? -23.167 92.264  78.341  1.00 27.05 ? 908  LYS A CA    1 
ATOM   6566  C  C     . LYS A 1  910  ? -23.745 91.769  79.661  1.00 29.19 ? 908  LYS A C     1 
ATOM   6567  O  O     . LYS A 1  910  ? -23.171 90.894  80.316  1.00 24.44 ? 908  LYS A O     1 
ATOM   6568  C  CB    . LYS A 1  910  ? -23.338 91.198  77.261  1.00 27.92 ? 908  LYS A CB    1 
ATOM   6569  C  CG    . LYS A 1  910  ? -23.029 91.676  75.857  1.00 33.48 ? 908  LYS A CG    1 
ATOM   6570  C  CD    . LYS A 1  910  ? -23.324 90.590  74.838  1.00 32.05 ? 908  LYS A CD    1 
ATOM   6571  C  CE    . LYS A 1  910  ? -24.760 90.126  74.934  1.00 35.18 ? 908  LYS A CE    1 
ATOM   6572  N  NZ    . LYS A 1  910  ? -25.141 89.310  73.742  1.00 41.37 ? 908  LYS A NZ    1 
ATOM   6573  N  N     . VAL A 1  911  ? -24.889 92.325  80.046  1.00 25.95 ? 909  VAL A N     1 
ATOM   6574  C  CA    . VAL A 1  911  ? -25.528 92.035  81.322  1.00 26.05 ? 909  VAL A CA    1 
ATOM   6575  C  C     . VAL A 1  911  ? -26.955 91.587  81.061  1.00 25.57 ? 909  VAL A C     1 
ATOM   6576  O  O     . VAL A 1  911  ? -27.720 92.291  80.389  1.00 24.41 ? 909  VAL A O     1 
ATOM   6577  C  CB    . VAL A 1  911  ? -25.508 93.259  82.257  1.00 29.28 ? 909  VAL A CB    1 
ATOM   6578  C  CG1   . VAL A 1  911  ? -26.223 92.935  83.572  1.00 25.27 ? 909  VAL A CG1   1 
ATOM   6579  C  CG2   . VAL A 1  911  ? -24.075 93.721  82.505  1.00 28.64 ? 909  VAL A CG2   1 
ATOM   6580  N  N     . GLU A 1  912  ? -27.305 90.420  81.594  1.00 23.92 ? 910  GLU A N     1 
ATOM   6581  C  CA    . GLU A 1  912  ? -28.643 89.859  81.516  1.00 23.73 ? 910  GLU A CA    1 
ATOM   6582  C  C     . GLU A 1  912  ? -29.223 89.843  82.923  1.00 26.70 ? 910  GLU A C     1 
ATOM   6583  O  O     . GLU A 1  912  ? -28.579 89.343  83.853  1.00 23.05 ? 910  GLU A O     1 
ATOM   6584  C  CB    . GLU A 1  912  ? -28.601 88.440  80.937  1.00 23.23 ? 910  GLU A CB    1 
ATOM   6585  C  CG    . GLU A 1  912  ? -29.959 87.830  80.641  1.00 24.34 ? 910  GLU A CG    1 
ATOM   6586  C  CD    . GLU A 1  912  ? -30.579 88.401  79.381  1.00 26.08 ? 910  GLU A CD    1 
ATOM   6587  O  OE1   . GLU A 1  912  ? -29.837 88.994  78.570  1.00 29.16 ? 910  GLU A OE1   1 
ATOM   6588  O  OE2   . GLU A 1  912  ? -31.808 88.264  79.205  1.00 28.07 ? 910  GLU A OE2   1 
ATOM   6589  N  N     . GLN A 1  913  ? -30.420 90.403  83.091  1.00 22.47 ? 911  GLN A N     1 
ATOM   6590  C  CA    . GLN A 1  913  ? -31.052 90.395  84.401  1.00 23.29 ? 911  GLN A CA    1 
ATOM   6591  C  C     . GLN A 1  913  ? -32.527 90.055  84.276  1.00 26.77 ? 911  GLN A C     1 
ATOM   6592  O  O     . GLN A 1  913  ? -33.193 90.500  83.339  1.00 25.46 ? 911  GLN A O     1 
ATOM   6593  C  CB    . GLN A 1  913  ? -30.908 91.753  85.106  1.00 24.03 ? 911  GLN A CB    1 
ATOM   6594  C  CG    . GLN A 1  913  ? -29.477 92.152  85.442  1.00 25.75 ? 911  GLN A CG    1 
ATOM   6595  C  CD    . GLN A 1  913  ? -29.426 93.377  86.340  1.00 26.81 ? 911  GLN A CD    1 
ATOM   6596  O  OE1   . GLN A 1  913  ? -29.902 94.455  85.969  1.00 30.44 ? 911  GLN A OE1   1 
ATOM   6597  N  NE2   . GLN A 1  913  ? -28.884 93.209  87.536  1.00 26.45 ? 911  GLN A NE2   1 
ATOM   6598  N  N     . ILE A 1  914  ? -33.027 89.262  85.228  1.00 26.82 ? 912  ILE A N     1 
ATOM   6599  C  CA    . ILE A 1  914  ? -34.465 89.059  85.365  1.00 27.71 ? 912  ILE A CA    1 
ATOM   6600  C  C     . ILE A 1  914  ? -35.110 90.350  85.844  1.00 28.02 ? 912  ILE A C     1 
ATOM   6601  O  O     . ILE A 1  914  ? -34.553 91.075  86.677  1.00 28.13 ? 912  ILE A O     1 
ATOM   6602  C  CB    . ILE A 1  914  ? -34.776 87.927  86.359  1.00 29.09 ? 912  ILE A CB    1 
ATOM   6603  C  CG1   . ILE A 1  914  ? -33.937 86.684  86.094  1.00 28.03 ? 912  ILE A CG1   1 
ATOM   6604  C  CG2   . ILE A 1  914  ? -36.254 87.556  86.301  1.00 33.73 ? 912  ILE A CG2   1 
ATOM   6605  C  CD1   . ILE A 1  914  ? -34.074 85.692  87.206  1.00 26.68 ? 912  ILE A CD1   1 
ATOM   6606  N  N     . GLY A 1  915  ? -36.303 90.639  85.336  1.00 31.49 ? 913  GLY A N     1 
ATOM   6607  C  CA    . GLY A 1  915  ? -37.088 91.720  85.898  1.00 30.27 ? 913  GLY A CA    1 
ATOM   6608  C  C     . GLY A 1  915  ? -37.713 91.280  87.212  1.00 30.66 ? 913  GLY A C     1 
ATOM   6609  O  O     . GLY A 1  915  ? -38.211 90.162  87.344  1.00 37.11 ? 913  GLY A O     1 
ATOM   6610  N  N     . LEU A 1  916  ? -37.678 92.174  88.192  1.00 31.59 ? 914  LEU A N     1 
ATOM   6611  C  CA    . LEU A 1  916  ? -38.223 91.878  89.506  1.00 32.29 ? 914  LEU A CA    1 
ATOM   6612  C  C     . LEU A 1  916  ? -39.661 92.363  89.615  1.00 34.96 ? 914  LEU A C     1 
ATOM   6613  O  O     . LEU A 1  916  ? -40.044 93.375  89.024  1.00 33.49 ? 914  LEU A O     1 
ATOM   6614  C  CB    . LEU A 1  916  ? -37.379 92.527  90.600  1.00 30.03 ? 914  LEU A CB    1 
ATOM   6615  C  CG    . LEU A 1  916  ? -35.949 92.014  90.694  1.00 29.40 ? 914  LEU A CG    1 
ATOM   6616  C  CD1   . LEU A 1  916  ? -35.272 92.631  91.899  1.00 32.21 ? 914  LEU A CD1   1 
ATOM   6617  C  CD2   . LEU A 1  916  ? -35.953 90.494  90.773  1.00 31.22 ? 914  LEU A CD2   1 
ATOM   6618  N  N     . ALA A 1  917  ? -40.460 91.622  90.376  1.00 34.14 ? 915  ALA A N     1 
ATOM   6619  C  CA    . ALA A 1  917  ? -41.839 92.022  90.601  1.00 33.62 ? 915  ALA A CA    1 
ATOM   6620  C  C     . ALA A 1  917  ? -41.890 93.223  91.537  1.00 34.59 ? 915  ALA A C     1 
ATOM   6621  O  O     . ALA A 1  917  ? -40.984 93.451  92.346  1.00 33.59 ? 915  ALA A O     1 
ATOM   6622  C  CB    . ALA A 1  917  ? -42.648 90.862  91.181  1.00 36.78 ? 915  ALA A CB    1 
ATOM   6623  N  N     . SER A 1  918  ? -42.968 94.003  91.411  1.00 33.55 ? 916  SER A N     1 
ATOM   6624  C  CA    . SER A 1  918  ? -43.132 95.193  92.239  1.00 37.82 ? 916  SER A CA    1 
ATOM   6625  C  C     . SER A 1  918  ? -43.097 94.862  93.727  1.00 36.15 ? 916  SER A C     1 
ATOM   6626  O  O     . SER A 1  918  ? -42.638 95.682  94.531  1.00 33.56 ? 916  SER A O     1 
ATOM   6627  C  CB    . SER A 1  918  ? -44.443 95.897  91.884  1.00 36.34 ? 916  SER A CB    1 
ATOM   6628  O  OG    . SER A 1  918  ? -44.641 97.028  92.704  1.00 45.14 ? 916  SER A OG    1 
ATOM   6629  N  N     . GLU A 1  919  ? -43.565 93.667  94.108  1.00 34.75 ? 917  GLU A N     1 
ATOM   6630  C  CA    . GLU A 1  919  ? -43.610 93.277  95.513  1.00 34.26 ? 917  GLU A CA    1 
ATOM   6631  C  C     . GLU A 1  919  ? -42.228 93.220  96.154  1.00 32.97 ? 917  GLU A C     1 
ATOM   6632  O  O     . GLU A 1  919  ? -42.125 93.294  97.382  1.00 32.35 ? 917  GLU A O     1 
ATOM   6633  C  CB    . GLU A 1  919  ? -44.290 91.912  95.663  1.00 40.78 ? 917  GLU A CB    1 
ATOM   6634  C  CG    . GLU A 1  919  ? -45.804 91.934  95.529  1.00 45.66 ? 917  GLU A CG    1 
ATOM   6635  C  CD    . GLU A 1  919  ? -46.274 91.711  94.103  1.00 50.03 ? 917  GLU A CD    1 
ATOM   6636  O  OE1   . GLU A 1  919  ? -45.446 91.826  93.171  1.00 46.09 ? 917  GLU A OE1   1 
ATOM   6637  O  OE2   . GLU A 1  919  ? -47.476 91.412  93.919  1.00 53.06 ? 917  GLU A OE2   1 
ATOM   6638  N  N     . THR A 1  920  ? -41.166 93.088  95.366  1.00 32.95 ? 918  THR A N     1 
ATOM   6639  C  CA    . THR A 1  920  ? -39.836 93.049  95.963  1.00 30.12 ? 918  THR A CA    1 
ATOM   6640  C  C     . THR A 1  920  ? -39.433 94.383  96.572  1.00 29.73 ? 918  THR A C     1 
ATOM   6641  O  O     . THR A 1  920  ? -38.487 94.423  97.367  1.00 27.93 ? 918  THR A O     1 
ATOM   6642  C  CB    . THR A 1  920  ? -38.797 92.624  94.924  1.00 28.36 ? 918  THR A CB    1 
ATOM   6643  O  OG1   . THR A 1  920  ? -38.752 93.582  93.862  1.00 29.98 ? 918  THR A OG1   1 
ATOM   6644  C  CG2   . THR A 1  920  ? -39.138 91.249  94.360  1.00 28.47 ? 918  THR A CG2   1 
ATOM   6645  N  N     . GLY A 1  921  ? -40.132 95.469  96.229  1.00 31.52 ? 919  GLY A N     1 
ATOM   6646  C  CA    . GLY A 1  921  ? -39.729 96.780  96.704  1.00 31.49 ? 919  GLY A CA    1 
ATOM   6647  C  C     . GLY A 1  921  ? -39.711 96.908  98.215  1.00 29.59 ? 919  GLY A C     1 
ATOM   6648  O  O     . GLY A 1  921  ? -38.960 97.720  98.757  1.00 32.69 ? 919  GLY A O     1 
ATOM   6649  N  N     . VAL A 1  922  ? -40.520 96.105  98.917  1.00 31.01 ? 920  VAL A N     1 
ATOM   6650  C  CA    . VAL A 1  922  ? -40.545 96.165  100.379 1.00 27.18 ? 920  VAL A CA    1 
ATOM   6651  C  C     . VAL A 1  922  ? -39.368 95.457  101.033 1.00 29.61 ? 920  VAL A C     1 
ATOM   6652  O  O     . VAL A 1  922  ? -39.186 95.591  102.251 1.00 29.35 ? 920  VAL A O     1 
ATOM   6653  C  CB    . VAL A 1  922  ? -41.853 95.579  100.944 1.00 30.31 ? 920  VAL A CB    1 
ATOM   6654  C  CG1   . VAL A 1  922  ? -43.037 96.478  100.588 1.00 30.68 ? 920  VAL A CG1   1 
ATOM   6655  C  CG2   . VAL A 1  922  ? -42.078 94.182  100.422 1.00 26.63 ? 920  VAL A CG2   1 
ATOM   6656  N  N     . GLY A 1  923  ? -38.563 94.711  100.268 1.00 27.18 ? 921  GLY A N     1 
ATOM   6657  C  CA    . GLY A 1  923  ? -37.377 94.055  100.795 1.00 26.21 ? 921  GLY A CA    1 
ATOM   6658  C  C     . GLY A 1  923  ? -36.120 94.486  100.067 1.00 25.35 ? 921  GLY A C     1 
ATOM   6659  O  O     . GLY A 1  923  ? -36.129 95.508  99.379  1.00 27.04 ? 921  GLY A O     1 
ATOM   6660  N  N     . THR A 1  924  ? -35.035 93.723  100.189 1.00 24.54 ? 922  THR A N     1 
ATOM   6661  C  CA    . THR A 1  924  ? -33.769 94.055  99.535  1.00 24.16 ? 922  THR A CA    1 
ATOM   6662  C  C     . THR A 1  924  ? -33.412 92.921  98.577  1.00 24.43 ? 922  THR A C     1 
ATOM   6663  O  O     . THR A 1  924  ? -32.850 91.902  98.988  1.00 23.97 ? 922  THR A O     1 
ATOM   6664  C  CB    . THR A 1  924  ? -32.665 94.304  100.568 1.00 23.05 ? 922  THR A CB    1 
ATOM   6665  O  OG1   . THR A 1  924  ? -32.592 93.202  101.477 1.00 22.14 ? 922  THR A OG1   1 
ATOM   6666  C  CG2   . THR A 1  924  ? -32.965 95.576  101.361 1.00 23.29 ? 922  THR A CG2   1 
ATOM   6667  N  N     . PHE A 1  925  ? -33.731 93.102  97.298  1.00 22.51 ? 923  PHE A N     1 
ATOM   6668  C  CA    . PHE A 1  925  ? -33.540 92.070  96.292  1.00 22.10 ? 923  PHE A CA    1 
ATOM   6669  C  C     . PHE A 1  925  ? -32.582 92.549  95.210  1.00 23.25 ? 923  PHE A C     1 
ATOM   6670  O  O     . PHE A 1  925  ? -32.591 93.726  94.826  1.00 25.53 ? 923  PHE A O     1 
ATOM   6671  C  CB    . PHE A 1  925  ? -34.871 91.672  95.633  1.00 21.81 ? 923  PHE A CB    1 
ATOM   6672  C  CG    . PHE A 1  925  ? -35.821 90.944  96.544  1.00 23.23 ? 923  PHE A CG    1 
ATOM   6673  C  CD1   . PHE A 1  925  ? -36.681 91.638  97.386  1.00 22.32 ? 923  PHE A CD1   1 
ATOM   6674  C  CD2   . PHE A 1  925  ? -35.879 89.563  96.529  1.00 20.82 ? 923  PHE A CD2   1 
ATOM   6675  C  CE1   . PHE A 1  925  ? -37.573 90.955  98.214  1.00 21.46 ? 923  PHE A CE1   1 
ATOM   6676  C  CE2   . PHE A 1  925  ? -36.760 88.877  97.350  1.00 21.31 ? 923  PHE A CE2   1 
ATOM   6677  C  CZ    . PHE A 1  925  ? -37.614 89.572  98.184  1.00 21.60 ? 923  PHE A CZ    1 
ATOM   6678  N  N     . VAL A 1  926  ? -31.783 91.616  94.705  1.00 22.02 ? 924  VAL A N     1 
ATOM   6679  C  CA    . VAL A 1  926  ? -30.963 91.814  93.520  1.00 21.89 ? 924  VAL A CA    1 
ATOM   6680  C  C     . VAL A 1  926  ? -31.369 90.737  92.524  1.00 21.00 ? 924  VAL A C     1 
ATOM   6681  O  O     . VAL A 1  926  ? -31.386 89.561  92.880  1.00 21.40 ? 924  VAL A O     1 
ATOM   6682  C  CB    . VAL A 1  926  ? -29.457 91.720  93.828  1.00 21.84 ? 924  VAL A CB    1 
ATOM   6683  C  CG1   . VAL A 1  926  ? -28.654 91.708  92.544  1.00 23.32 ? 924  VAL A CG1   1 
ATOM   6684  C  CG2   . VAL A 1  926  ? -29.037 92.897  94.713  1.00 22.45 ? 924  VAL A CG2   1 
ATOM   6685  N  N     . PRO A 1  927  ? -31.741 91.078  91.297  1.00 22.75 ? 925  PRO A N     1 
ATOM   6686  C  CA    . PRO A 1  927  ? -32.161 90.041  90.354  1.00 23.25 ? 925  PRO A CA    1 
ATOM   6687  C  C     . PRO A 1  927  ? -30.980 89.180  89.961  1.00 21.67 ? 925  PRO A C     1 
ATOM   6688  O  O     . PRO A 1  927  ? -29.857 89.685  89.828  1.00 21.08 ? 925  PRO A O     1 
ATOM   6689  C  CB    . PRO A 1  927  ? -32.685 90.835  89.152  1.00 25.19 ? 925  PRO A CB    1 
ATOM   6690  C  CG    . PRO A 1  927  ? -31.954 92.123  89.220  1.00 25.96 ? 925  PRO A CG    1 
ATOM   6691  C  CD    . PRO A 1  927  ? -31.739 92.414  90.684  1.00 23.77 ? 925  PRO A CD    1 
ATOM   6692  N  N     . PRO A 1  928  ? -31.187 87.877  89.814  1.00 22.13 ? 926  PRO A N     1 
ATOM   6693  C  CA    . PRO A 1  928  ? -30.173 87.034  89.182  1.00 20.65 ? 926  PRO A CA    1 
ATOM   6694  C  C     . PRO A 1  928  ? -29.652 87.670  87.905  1.00 19.21 ? 926  PRO A C     1 
ATOM   6695  O  O     . PRO A 1  928  ? -30.415 88.154  87.065  1.00 20.43 ? 926  PRO A O     1 
ATOM   6696  C  CB    . PRO A 1  928  ? -30.933 85.733  88.915  1.00 19.75 ? 926  PRO A CB    1 
ATOM   6697  C  CG    . PRO A 1  928  ? -31.877 85.662  90.065  1.00 23.94 ? 926  PRO A CG    1 
ATOM   6698  C  CD    . PRO A 1  928  ? -32.331 87.086  90.296  1.00 21.84 ? 926  PRO A CD    1 
ATOM   6699  N  N     . THR A 1  929  ? -28.332 87.658  87.767  1.00 18.99 ? 927  THR A N     1 
ATOM   6700  C  CA    . THR A 1  929  ? -27.617 88.448  86.783  1.00 20.19 ? 927  THR A CA    1 
ATOM   6701  C  C     . THR A 1  929  ? -26.534 87.590  86.150  1.00 20.94 ? 927  THR A C     1 
ATOM   6702  O  O     . THR A 1  929  ? -25.844 86.848  86.850  1.00 20.04 ? 927  THR A O     1 
ATOM   6703  C  CB    . THR A 1  929  ? -26.996 89.688  87.454  1.00 22.10 ? 927  THR A CB    1 
ATOM   6704  O  OG1   . THR A 1  929  ? -28.047 90.488  88.010  1.00 21.68 ? 927  THR A OG1   1 
ATOM   6705  C  CG2   . THR A 1  929  ? -26.195 90.519  86.457  1.00 23.08 ? 927  THR A CG2   1 
ATOM   6706  N  N     . ILE A 1  930  ? -26.412 87.678  84.827  1.00 20.44 ? 928  ILE A N     1 
ATOM   6707  C  CA    . ILE A 1  930  ? -25.328 87.056  84.072  1.00 21.57 ? 928  ILE A CA    1 
ATOM   6708  C  C     . ILE A 1  930  ? -24.523 88.169  83.427  1.00 23.25 ? 928  ILE A C     1 
ATOM   6709  O  O     . ILE A 1  930  ? -25.090 89.024  82.735  1.00 23.58 ? 928  ILE A O     1 
ATOM   6710  C  CB    . ILE A 1  930  ? -25.854 86.089  82.996  1.00 17.46 ? 928  ILE A CB    1 
ATOM   6711  C  CG1   . ILE A 1  930  ? -26.663 84.963  83.627  1.00 19.41 ? 928  ILE A CG1   1 
ATOM   6712  C  CG2   . ILE A 1  930  ? -24.690 85.518  82.180  1.00 20.59 ? 928  ILE A CG2   1 
ATOM   6713  C  CD1   . ILE A 1  930  ? -27.441 84.126  82.591  1.00 20.60 ? 928  ILE A CD1   1 
ATOM   6714  N  N     . ILE A 1  931  ? -23.208 88.149  83.640  1.00 21.95 ? 929  ILE A N     1 
ATOM   6715  C  CA    . ILE A 1  931  ? -22.292 89.163  83.127  1.00 23.29 ? 929  ILE A CA    1 
ATOM   6716  C  C     . ILE A 1  931  ? -21.256 88.451  82.270  1.00 26.41 ? 929  ILE A C     1 
ATOM   6717  O  O     . ILE A 1  931  ? -20.567 87.545  82.748  1.00 22.78 ? 929  ILE A O     1 
ATOM   6718  C  CB    . ILE A 1  931  ? -21.608 89.937  84.266  1.00 24.67 ? 929  ILE A CB    1 
ATOM   6719  C  CG1   . ILE A 1  931  ? -22.652 90.654  85.134  1.00 23.60 ? 929  ILE A CG1   1 
ATOM   6720  C  CG2   . ILE A 1  931  ? -20.605 90.946  83.707  1.00 22.17 ? 929  ILE A CG2   1 
ATOM   6721  C  CD1   . ILE A 1  931  ? -22.035 91.582  86.187  1.00 25.44 ? 929  ILE A CD1   1 
ATOM   6722  N  N     . GLU A 1  932  ? -21.130 88.860  81.017  1.00 26.31 ? 930  GLU A N     1 
ATOM   6723  C  CA    . GLU A 1  932  ? -20.185 88.221  80.109  1.00 23.12 ? 930  GLU A CA    1 
ATOM   6724  C  C     . GLU A 1  932  ? -18.864 88.970  80.166  1.00 21.99 ? 930  GLU A C     1 
ATOM   6725  O  O     . GLU A 1  932  ? -18.794 90.154  79.819  1.00 24.84 ? 930  GLU A O     1 
ATOM   6726  C  CB    . GLU A 1  932  ? -20.756 88.187  78.697  1.00 24.14 ? 930  GLU A CB    1 
ATOM   6727  C  CG    . GLU A 1  932  ? -21.909 87.221  78.605  1.00 22.78 ? 930  GLU A CG    1 
ATOM   6728  C  CD    . GLU A 1  932  ? -22.662 87.358  77.318  1.00 27.60 ? 930  GLU A CD    1 
ATOM   6729  O  OE1   . GLU A 1  932  ? -22.018 87.235  76.259  1.00 25.63 ? 930  GLU A OE1   1 
ATOM   6730  O  OE2   . GLU A 1  932  ? -23.888 87.601  77.376  1.00 26.25 ? 930  GLU A OE2   1 
ATOM   6731  N  N     . LEU A 1  933  ? -17.823 88.296  80.628  1.00 24.89 ? 931  LEU A N     1 
ATOM   6732  C  CA    . LEU A 1  933  ? -16.517 88.915  80.772  1.00 25.63 ? 931  LEU A CA    1 
ATOM   6733  C  C     . LEU A 1  933  ? -15.607 88.533  79.613  1.00 32.11 ? 931  LEU A C     1 
ATOM   6734  O  O     . LEU A 1  933  ? -15.802 87.517  78.945  1.00 28.83 ? 931  LEU A O     1 
ATOM   6735  C  CB    . LEU A 1  933  ? -15.863 88.508  82.092  1.00 27.54 ? 931  LEU A CB    1 
ATOM   6736  C  CG    . LEU A 1  933  ? -16.621 88.869  83.374  1.00 28.91 ? 931  LEU A CG    1 
ATOM   6737  C  CD1   . LEU A 1  933  ? -15.770 88.518  84.581  1.00 30.03 ? 931  LEU A CD1   1 
ATOM   6738  C  CD2   . LEU A 1  933  ? -16.999 90.337  83.396  1.00 32.79 ? 931  LEU A CD2   1 
ATOM   6739  N  N     . GLU A 1  934  ? -14.590 89.368  79.391  1.00 33.76 ? 932  GLU A N     1 
ATOM   6740  C  CA    . GLU A 1  934  ? -13.551 89.057  78.417  1.00 39.64 ? 932  GLU A CA    1 
ATOM   6741  C  C     . GLU A 1  934  ? -12.466 88.174  79.025  1.00 39.68 ? 932  GLU A C     1 
ATOM   6742  O  O     . GLU A 1  934  ? -12.094 87.151  78.444  1.00 39.97 ? 932  GLU A O     1 
ATOM   6743  C  CB    . GLU A 1  934  ? -12.944 90.349  77.863  1.00 41.14 ? 932  GLU A CB    1 
ATOM   6744  C  CG    . GLU A 1  934  ? -13.974 91.309  77.277  1.00 45.46 ? 932  GLU A CG    1 
ATOM   6745  C  CD    . GLU A 1  934  ? -14.748 90.704  76.117  1.00 48.82 ? 932  GLU A CD    1 
ATOM   6746  O  OE1   . GLU A 1  934  ? -14.122 90.035  75.266  1.00 56.40 ? 932  GLU A OE1   1 
ATOM   6747  O  OE2   . GLU A 1  934  ? -15.984 90.886  76.060  1.00 47.01 ? 932  GLU A OE2   1 
ATOM   6748  N  N     . LYS A 1  935  ? -11.971 88.546  80.202  1.00 40.01 ? 933  LYS A N     1 
ATOM   6749  C  CA    . LYS A 1  935  ? -10.922 87.812  80.894  1.00 43.47 ? 933  LYS A CA    1 
ATOM   6750  C  C     . LYS A 1  935  ? -11.322 87.612  82.346  1.00 42.67 ? 933  LYS A C     1 
ATOM   6751  O  O     . LYS A 1  935  ? -12.032 88.436  82.926  1.00 41.97 ? 933  LYS A O     1 
ATOM   6752  C  CB    . LYS A 1  935  ? -9.579  88.551  80.827  1.00 43.25 ? 933  LYS A CB    1 
ATOM   6753  N  N     . LEU A 1  936  ? -10.858 86.504  82.932  1.00 43.20 ? 934  LEU A N     1 
ATOM   6754  C  CA    . LEU A 1  936  ? -11.119 86.255  84.347  1.00 42.15 ? 934  LEU A CA    1 
ATOM   6755  C  C     . LEU A 1  936  ? -10.547 87.362  85.219  1.00 42.68 ? 934  LEU A C     1 
ATOM   6756  O  O     . LEU A 1  936  ? -11.052 87.608  86.320  1.00 41.90 ? 934  LEU A O     1 
ATOM   6757  C  CB    . LEU A 1  936  ? -10.549 84.899  84.760  1.00 42.83 ? 934  LEU A CB    1 
ATOM   6758  C  CG    . LEU A 1  936  ? -11.467 84.024  85.622  1.00 41.29 ? 934  LEU A CG    1 
ATOM   6759  C  CD1   . LEU A 1  936  ? -11.063 82.564  85.514  1.00 38.19 ? 934  LEU A CD1   1 
ATOM   6760  C  CD2   . LEU A 1  936  ? -11.448 84.474  87.078  1.00 39.09 ? 934  LEU A CD2   1 
ATOM   6761  N  N     . SER A 1  937  ? -9.512  88.053  84.739  1.00 46.71 ? 935  SER A N     1 
ATOM   6762  C  CA    . SER A 1  937  ? -8.947  89.188  85.458  1.00 46.11 ? 935  SER A CA    1 
ATOM   6763  C  C     . SER A 1  937  ? -9.915  90.360  85.567  1.00 43.26 ? 935  SER A C     1 
ATOM   6764  O  O     . SER A 1  937  ? -9.653  91.282  86.347  1.00 47.05 ? 935  SER A O     1 
ATOM   6765  C  CB    . SER A 1  937  ? -7.649  89.641  84.783  1.00 48.17 ? 935  SER A CB    1 
ATOM   6766  O  OG    . SER A 1  937  ? -7.888  90.097  83.462  1.00 50.07 ? 935  SER A OG    1 
ATOM   6767  N  N     . ASP A 1  938  ? -11.020 90.352  84.814  1.00 43.79 ? 936  ASP A N     1 
ATOM   6768  C  CA    . ASP A 1  938  ? -12.046 91.374  84.989  1.00 43.09 ? 936  ASP A CA    1 
ATOM   6769  C  C     . ASP A 1  938  ? -12.648 91.358  86.388  1.00 42.85 ? 936  ASP A C     1 
ATOM   6770  O  O     . ASP A 1  938  ? -13.248 92.356  86.800  1.00 40.50 ? 936  ASP A O     1 
ATOM   6771  C  CB    . ASP A 1  938  ? -13.164 91.200  83.952  1.00 42.13 ? 936  ASP A CB    1 
ATOM   6772  C  CG    . ASP A 1  938  ? -12.686 91.441  82.530  1.00 43.70 ? 936  ASP A CG    1 
ATOM   6773  O  OD1   . ASP A 1  938  ? -11.602 92.045  82.361  1.00 46.08 ? 936  ASP A OD1   1 
ATOM   6774  O  OD2   . ASP A 1  938  ? -13.396 91.029  81.583  1.00 40.77 ? 936  ASP A OD2   1 
ATOM   6775  N  N     . LEU A 1  939  ? -12.509 90.257  87.122  1.00 39.16 ? 937  LEU A N     1 
ATOM   6776  C  CA    . LEU A 1  939  ? -12.990 90.158  88.494  1.00 42.43 ? 937  LEU A CA    1 
ATOM   6777  C  C     . LEU A 1  939  ? -11.861 90.437  89.475  1.00 41.99 ? 937  LEU A C     1 
ATOM   6778  O  O     . LEU A 1  939  ? -10.728 89.992  89.275  1.00 48.84 ? 937  LEU A O     1 
ATOM   6779  C  CB    . LEU A 1  939  ? -13.573 88.775  88.776  1.00 40.51 ? 937  LEU A CB    1 
ATOM   6780  C  CG    . LEU A 1  939  ? -14.905 88.455  88.116  1.00 35.99 ? 937  LEU A CG    1 
ATOM   6781  C  CD1   . LEU A 1  939  ? -15.422 87.124  88.618  1.00 33.87 ? 937  LEU A CD1   1 
ATOM   6782  C  CD2   . LEU A 1  939  ? -15.891 89.561  88.411  1.00 32.48 ? 937  LEU A CD2   1 
ATOM   6783  N  N     . GLN A 1  940  ? -12.181 91.157  90.549  1.00 36.85 ? 938  GLN A N     1 
ATOM   6784  C  CA    . GLN A 1  940  ? -11.195 91.546  91.547  1.00 40.06 ? 938  GLN A CA    1 
ATOM   6785  C  C     . GLN A 1  940  ? -11.372 90.827  92.876  1.00 40.54 ? 938  GLN A C     1 
ATOM   6786  O  O     . GLN A 1  940  ? -10.408 90.263  93.404  1.00 47.35 ? 938  GLN A O     1 
ATOM   6787  C  CB    . GLN A 1  940  ? -11.240 93.066  91.771  1.00 42.39 ? 938  GLN A CB    1 
ATOM   6788  N  N     . ARG A 1  941  ? -12.575 90.841  93.444  1.00 37.02 ? 939  ARG A N     1 
ATOM   6789  C  CA    . ARG A 1  941  ? -12.840 90.184  94.718  1.00 35.04 ? 939  ARG A CA    1 
ATOM   6790  C  C     . ARG A 1  941  ? -14.214 89.530  94.663  1.00 26.76 ? 939  ARG A C     1 
ATOM   6791  O  O     . ARG A 1  941  ? -15.019 89.794  93.769  1.00 30.90 ? 939  ARG A O     1 
ATOM   6792  C  CB    . ARG A 1  941  ? -12.758 91.167  95.895  1.00 36.85 ? 939  ARG A CB    1 
ATOM   6793  N  N     . GLU A 1  942  ? -14.468 88.662  95.637  1.00 26.13 ? 940  GLU A N     1 
ATOM   6794  C  CA    . GLU A 1  942  ? -15.734 87.939  95.702  1.00 25.18 ? 940  GLU A CA    1 
ATOM   6795  C  C     . GLU A 1  942  ? -16.911 88.910  95.737  1.00 24.87 ? 940  GLU A C     1 
ATOM   6796  O  O     . GLU A 1  942  ? -16.911 89.877  96.506  1.00 23.86 ? 940  GLU A O     1 
ATOM   6797  C  CB    . GLU A 1  942  ? -15.735 87.048  96.943  1.00 21.51 ? 940  GLU A CB    1 
ATOM   6798  C  CG    . GLU A 1  942  ? -17.042 86.327  97.229  1.00 20.85 ? 940  GLU A CG    1 
ATOM   6799  C  CD    . GLU A 1  942  ? -17.066 85.744  98.630  1.00 20.91 ? 940  GLU A CD    1 
ATOM   6800  O  OE1   . GLU A 1  942  ? -16.869 86.519  99.594  1.00 23.76 ? 940  GLU A OE1   1 
ATOM   6801  O  OE2   . GLU A 1  942  ? -17.269 84.520  98.769  1.00 20.00 ? 940  GLU A OE2   1 
ATOM   6802  N  N     . VAL A 1  943  ? -17.913 88.661  94.890  1.00 22.97 ? 941  VAL A N     1 
ATOM   6803  C  CA    . VAL A 1  943  ? -19.165 89.419  94.893  1.00 23.03 ? 941  VAL A CA    1 
ATOM   6804  C  C     . VAL A 1  943  ? -20.247 88.470  95.395  1.00 25.01 ? 941  VAL A C     1 
ATOM   6805  O  O     . VAL A 1  943  ? -20.662 87.541  94.687  1.00 20.15 ? 941  VAL A O     1 
ATOM   6806  C  CB    . VAL A 1  943  ? -19.498 89.994  93.509  1.00 25.91 ? 941  VAL A CB    1 
ATOM   6807  C  CG1   . VAL A 1  943  ? -20.809 90.776  93.539  1.00 25.82 ? 941  VAL A CG1   1 
ATOM   6808  C  CG2   . VAL A 1  943  ? -18.366 90.897  93.022  1.00 26.93 ? 941  VAL A CG2   1 
ATOM   6809  N  N     . PHE A 1  944  ? -20.659 88.669  96.647  1.00 23.52 ? 942  PHE A N     1 
ATOM   6810  C  CA    . PHE A 1  944  ? -21.473 87.696  97.374  1.00 20.40 ? 942  PHE A CA    1 
ATOM   6811  C  C     . PHE A 1  944  ? -22.937 87.970  97.069  1.00 23.45 ? 942  PHE A C     1 
ATOM   6812  O  O     . PHE A 1  944  ? -23.687 88.531  97.875  1.00 23.36 ? 942  PHE A O     1 
ATOM   6813  C  CB    . PHE A 1  944  ? -21.183 87.780  98.869  1.00 19.89 ? 942  PHE A CB    1 
ATOM   6814  C  CG    . PHE A 1  944  ? -21.557 86.543  99.628  1.00 19.20 ? 942  PHE A CG    1 
ATOM   6815  C  CD1   . PHE A 1  944  ? -20.857 85.361  99.430  1.00 18.64 ? 942  PHE A CD1   1 
ATOM   6816  C  CD2   . PHE A 1  944  ? -22.602 86.559  100.551 1.00 20.00 ? 942  PHE A CD2   1 
ATOM   6817  C  CE1   . PHE A 1  944  ? -21.202 84.221  100.130 1.00 19.01 ? 942  PHE A CE1   1 
ATOM   6818  C  CE2   . PHE A 1  944  ? -22.937 85.415  101.260 1.00 21.35 ? 942  PHE A CE2   1 
ATOM   6819  C  CZ    . PHE A 1  944  ? -22.248 84.246  101.037 1.00 18.22 ? 942  PHE A CZ    1 
ATOM   6820  N  N     . GLY A 1  945  ? -23.350 87.578  95.868  1.00 19.45 ? 943  GLY A N     1 
ATOM   6821  C  CA    . GLY A 1  945  ? -24.698 87.853  95.431  1.00 20.56 ? 943  GLY A CA    1 
ATOM   6822  C  C     . GLY A 1  945  ? -25.024 87.030  94.209  1.00 19.65 ? 943  GLY A C     1 
ATOM   6823  O  O     . GLY A 1  945  ? -24.240 86.180  93.781  1.00 18.83 ? 943  GLY A O     1 
ATOM   6824  N  N     . PRO A 1  946  ? -26.198 87.258  93.629  1.00 19.54 ? 944  PRO A N     1 
ATOM   6825  C  CA    . PRO A 1  946  ? -26.652 86.427  92.506  1.00 19.91 ? 944  PRO A CA    1 
ATOM   6826  C  C     . PRO A 1  946  ? -26.107 86.928  91.172  1.00 17.89 ? 944  PRO A C     1 
ATOM   6827  O  O     . PRO A 1  946  ? -26.856 87.351  90.285  1.00 19.56 ? 944  PRO A O     1 
ATOM   6828  C  CB    . PRO A 1  946  ? -28.175 86.560  92.603  1.00 17.67 ? 944  PRO A CB    1 
ATOM   6829  C  CG    . PRO A 1  946  ? -28.366 87.982  93.066  1.00 20.08 ? 944  PRO A CG    1 
ATOM   6830  C  CD    . PRO A 1  946  ? -27.212 88.251  94.033  1.00 19.44 ? 944  PRO A CD    1 
ATOM   6831  N  N     . VAL A 1  947  ? -24.783 86.872  91.023  1.00 19.19 ? 945  VAL A N     1 
ATOM   6832  C  CA    . VAL A 1  947  ? -24.099 87.432  89.864  1.00 20.31 ? 945  VAL A CA    1 
ATOM   6833  C  C     . VAL A 1  947  ? -23.169 86.378  89.292  1.00 19.12 ? 945  VAL A C     1 
ATOM   6834  O  O     . VAL A 1  947  ? -22.115 86.078  89.877  1.00 20.00 ? 945  VAL A O     1 
ATOM   6835  C  CB    . VAL A 1  947  ? -23.318 88.706  90.201  1.00 20.43 ? 945  VAL A CB    1 
ATOM   6836  C  CG1   . VAL A 1  947  ? -22.737 89.297  88.927  1.00 20.21 ? 945  VAL A CG1   1 
ATOM   6837  C  CG2   . VAL A 1  947  ? -24.206 89.715  90.932  1.00 20.20 ? 945  VAL A CG2   1 
ATOM   6838  N  N     . LEU A 1  948  ? -23.540 85.839  88.140  1.00 19.49 ? 946  LEU A N     1 
ATOM   6839  C  CA    . LEU A 1  948  ? -22.743 84.851  87.438  1.00 19.35 ? 946  LEU A CA    1 
ATOM   6840  C  C     . LEU A 1  948  ? -21.959 85.555  86.346  1.00 18.99 ? 946  LEU A C     1 
ATOM   6841  O  O     . LEU A 1  948  ? -22.527 86.328  85.567  1.00 22.33 ? 946  LEU A O     1 
ATOM   6842  C  CB    . LEU A 1  948  ? -23.630 83.768  86.826  1.00 19.35 ? 946  LEU A CB    1 
ATOM   6843  C  CG    . LEU A 1  948  ? -22.859 82.761  85.967  1.00 18.90 ? 946  LEU A CG    1 
ATOM   6844  C  CD1   . LEU A 1  948  ? -21.861 81.991  86.839  1.00 18.64 ? 946  LEU A CD1   1 
ATOM   6845  C  CD2   . LEU A 1  948  ? -23.844 81.849  85.267  1.00 19.79 ? 946  LEU A CD2   1 
ATOM   6846  N  N     . HIS A 1  949  ? -20.666 85.293  86.292  1.00 20.04 ? 947  HIS A N     1 
ATOM   6847  C  CA    . HIS A 1  949  ? -19.825 85.819  85.232  1.00 19.97 ? 947  HIS A CA    1 
ATOM   6848  C  C     . HIS A 1  949  ? -19.508 84.691  84.269  1.00 20.00 ? 947  HIS A C     1 
ATOM   6849  O  O     . HIS A 1  949  ? -19.351 83.539  84.682  1.00 21.03 ? 947  HIS A O     1 
ATOM   6850  C  CB    . HIS A 1  949  ? -18.544 86.415  85.800  1.00 19.70 ? 947  HIS A CB    1 
ATOM   6851  C  CG    . HIS A 1  949  ? -18.794 87.434  86.859  1.00 21.72 ? 947  HIS A CG    1 
ATOM   6852  N  ND1   . HIS A 1  949  ? -18.998 87.096  88.181  1.00 21.28 ? 947  HIS A ND1   1 
ATOM   6853  C  CD2   . HIS A 1  949  ? -18.907 88.781  86.789  1.00 24.09 ? 947  HIS A CD2   1 
ATOM   6854  C  CE1   . HIS A 1  949  ? -19.205 88.197  88.881  1.00 22.82 ? 947  HIS A CE1   1 
ATOM   6855  N  NE2   . HIS A 1  949  ? -19.160 89.230  88.060  1.00 23.30 ? 947  HIS A NE2   1 
ATOM   6856  N  N     . VAL A 1  950  ? -19.460 85.011  82.979  1.00 20.49 ? 948  VAL A N     1 
ATOM   6857  C  CA    . VAL A 1  950  ? -19.270 83.999  81.949  1.00 20.70 ? 948  VAL A CA    1 
ATOM   6858  C  C     . VAL A 1  950  ? -18.052 84.378  81.132  1.00 19.82 ? 948  VAL A C     1 
ATOM   6859  O  O     . VAL A 1  950  ? -17.936 85.520  80.677  1.00 23.49 ? 948  VAL A O     1 
ATOM   6860  C  CB    . VAL A 1  950  ? -20.503 83.855  81.039  1.00 19.93 ? 948  VAL A CB    1 
ATOM   6861  C  CG1   . VAL A 1  950  ? -20.201 82.875  79.908  1.00 22.92 ? 948  VAL A CG1   1 
ATOM   6862  C  CG2   . VAL A 1  950  ? -21.698 83.383  81.837  1.00 21.11 ? 948  VAL A CG2   1 
ATOM   6863  N  N     . ILE A 1  951  ? -17.136 83.432  80.965  1.00 23.05 ? 949  ILE A N     1 
ATOM   6864  C  CA    . ILE A 1  951  ? -15.998 83.639  80.083  1.00 23.95 ? 949  ILE A CA    1 
ATOM   6865  C  C     . ILE A 1  951  ? -15.923 82.458  79.130  1.00 25.24 ? 949  ILE A C     1 
ATOM   6866  O  O     . ILE A 1  951  ? -16.416 81.367  79.428  1.00 20.59 ? 949  ILE A O     1 
ATOM   6867  C  CB    . ILE A 1  951  ? -14.672 83.830  80.852  1.00 23.45 ? 949  ILE A CB    1 
ATOM   6868  C  CG1   . ILE A 1  951  ? -14.290 82.575  81.616  1.00 24.35 ? 949  ILE A CG1   1 
ATOM   6869  C  CG2   . ILE A 1  951  ? -14.756 85.034  81.793  1.00 28.20 ? 949  ILE A CG2   1 
ATOM   6870  C  CD1   . ILE A 1  951  ? -13.213 81.787  80.919  1.00 32.58 ? 949  ILE A CD1   1 
ATOM   6871  N  N     . ARG A 1  952  ? -15.316 82.689  77.972  1.00 20.24 ? 950  ARG A N     1 
ATOM   6872  C  CA    . ARG A 1  952  ? -15.181 81.686  76.929  1.00 20.90 ? 950  ARG A CA    1 
ATOM   6873  C  C     . ARG A 1  952  ? -13.711 81.341  76.748  1.00 21.24 ? 950  ARG A C     1 
ATOM   6874  O  O     . ARG A 1  952  ? -12.832 82.180  76.961  1.00 23.54 ? 950  ARG A O     1 
ATOM   6875  C  CB    . ARG A 1  952  ? -15.761 82.202  75.608  1.00 24.53 ? 950  ARG A CB    1 
ATOM   6876  C  CG    . ARG A 1  952  ? -17.127 82.851  75.758  1.00 24.75 ? 950  ARG A CG    1 
ATOM   6877  C  CD    . ARG A 1  952  ? -17.435 83.784  74.601  1.00 29.76 ? 950  ARG A CD    1 
ATOM   6878  N  NE    . ARG A 1  952  ? -17.791 83.076  73.378  1.00 32.29 ? 950  ARG A NE    1 
ATOM   6879  C  CZ    . ARG A 1  952  ? -19.026 82.983  72.896  1.00 28.57 ? 950  ARG A CZ    1 
ATOM   6880  N  NH1   . ARG A 1  952  ? -20.059 83.511  73.532  1.00 25.28 ? 950  ARG A NH1   1 
ATOM   6881  N  NH2   . ARG A 1  952  ? -19.226 82.353  71.742  1.00 24.35 ? 950  ARG A NH2   1 
ATOM   6882  N  N     . TYR A 1  953  ? -13.441 80.098  76.351  1.00 20.59 ? 951  TYR A N     1 
ATOM   6883  C  CA    . TYR A 1  953  ? -12.063 79.683  76.143  1.00 21.36 ? 951  TYR A CA    1 
ATOM   6884  C  C     . TYR A 1  953  ? -11.969 78.727  74.965  1.00 20.50 ? 951  TYR A C     1 
ATOM   6885  O  O     . TYR A 1  953  ? -12.890 77.951  74.690  1.00 20.20 ? 951  TYR A O     1 
ATOM   6886  C  CB    . TYR A 1  953  ? -11.473 79.030  77.409  1.00 19.08 ? 951  TYR A CB    1 
ATOM   6887  C  CG    . TYR A 1  953  ? -11.998 77.643  77.686  1.00 19.64 ? 951  TYR A CG    1 
ATOM   6888  C  CD1   . TYR A 1  953  ? -13.216 77.453  78.336  1.00 17.04 ? 951  TYR A CD1   1 
ATOM   6889  C  CD2   . TYR A 1  953  ? -11.279 76.520  77.294  1.00 19.72 ? 951  TYR A CD2   1 
ATOM   6890  C  CE1   . TYR A 1  953  ? -13.697 76.178  78.592  1.00 17.60 ? 951  TYR A CE1   1 
ATOM   6891  C  CE2   . TYR A 1  953  ? -11.749 75.244  77.544  1.00 17.47 ? 951  TYR A CE2   1 
ATOM   6892  C  CZ    . TYR A 1  953  ? -12.958 75.079  78.189  1.00 19.10 ? 951  TYR A CZ    1 
ATOM   6893  O  OH    . TYR A 1  953  ? -13.424 73.811  78.428  1.00 18.22 ? 951  TYR A OH    1 
ATOM   6894  N  N     . ARG A 1  954  ? -10.842 78.809  74.257  1.00 20.82 ? 952  ARG A N     1 
ATOM   6895  C  CA    . ARG A 1  954  ? -10.504 77.834  73.227  1.00 24.42 ? 952  ARG A CA    1 
ATOM   6896  C  C     . ARG A 1  954  ? -9.908  76.581  73.863  1.00 21.70 ? 952  ARG A C     1 
ATOM   6897  O  O     . ARG A 1  954  ? -9.164  76.665  74.845  1.00 23.41 ? 952  ARG A O     1 
ATOM   6898  C  CB    . ARG A 1  954  ? -9.516  78.448  72.230  1.00 26.08 ? 952  ARG A CB    1 
ATOM   6899  C  CG    . ARG A 1  954  ? -10.125 79.537  71.343  1.00 31.12 ? 952  ARG A CG    1 
ATOM   6900  C  CD    . ARG A 1  954  ? -11.006 78.901  70.267  1.00 34.35 ? 952  ARG A CD    1 
ATOM   6901  N  NE    . ARG A 1  954  ? -11.963 79.823  69.664  1.00 43.36 ? 952  ARG A NE    1 
ATOM   6902  C  CZ    . ARG A 1  954  ? -11.752 80.495  68.538  1.00 45.78 ? 952  ARG A CZ    1 
ATOM   6903  N  NH1   . ARG A 1  954  ? -10.613 80.389  67.874  1.00 51.57 ? 952  ARG A NH1   1 
ATOM   6904  N  NH2   . ARG A 1  954  ? -12.707 81.296  68.070  1.00 43.42 ? 952  ARG A NH2   1 
ATOM   6905  N  N     . ARG A 1  955  ? -10.234 75.410  73.297  1.00 22.91 ? 953  ARG A N     1 
ATOM   6906  C  CA    . ARG A 1  955  ? -9.859  74.157  73.954  1.00 22.34 ? 953  ARG A CA    1 
ATOM   6907  C  C     . ARG A 1  955  ? -8.355  74.072  74.193  1.00 21.65 ? 953  ARG A C     1 
ATOM   6908  O  O     . ARG A 1  955  ? -7.919  73.615  75.253  1.00 24.69 ? 953  ARG A O     1 
ATOM   6909  C  CB    . ARG A 1  955  ? -10.333 72.951  73.144  1.00 26.94 ? 953  ARG A CB    1 
ATOM   6910  C  CG    . ARG A 1  955  ? -9.943  71.594  73.778  1.00 31.97 ? 953  ARG A CG    1 
ATOM   6911  C  CD    . ARG A 1  955  ? -10.212 71.578  75.297  1.00 33.23 ? 953  ARG A CD    1 
ATOM   6912  N  NE    . ARG A 1  955  ? -9.927  70.302  75.952  1.00 36.11 ? 953  ARG A NE    1 
ATOM   6913  C  CZ    . ARG A 1  955  ? -8.731  69.915  76.386  1.00 35.30 ? 953  ARG A CZ    1 
ATOM   6914  N  NH1   . ARG A 1  955  ? -7.649  70.657  76.194  1.00 30.57 ? 953  ARG A NH1   1 
ATOM   6915  N  NH2   . ARG A 1  955  ? -8.619  68.756  77.036  1.00 31.35 ? 953  ARG A NH2   1 
ATOM   6916  N  N     . ASP A 1  956  ? -7.543  74.518  73.233  1.00 22.06 ? 954  ASP A N     1 
ATOM   6917  C  CA    . ASP A 1  956  ? -6.098  74.447  73.444  1.00 24.01 ? 954  ASP A CA    1 
ATOM   6918  C  C     . ASP A 1  956  ? -5.642  75.307  74.614  1.00 24.62 ? 954  ASP A C     1 
ATOM   6919  O  O     . ASP A 1  956  ? -4.540  75.090  75.136  1.00 25.32 ? 954  ASP A O     1 
ATOM   6920  C  CB    . ASP A 1  956  ? -5.339  74.877  72.186  1.00 25.72 ? 954  ASP A CB    1 
ATOM   6921  C  CG    . ASP A 1  956  ? -5.522  73.913  71.025  1.00 27.04 ? 954  ASP A CG    1 
ATOM   6922  O  OD1   . ASP A 1  956  ? -5.983  72.777  71.247  1.00 28.94 ? 954  ASP A OD1   1 
ATOM   6923  O  OD2   . ASP A 1  956  ? -5.195  74.306  69.886  1.00 33.45 ? 954  ASP A OD2   1 
ATOM   6924  N  N     . ASP A 1  957  ? -6.452  76.279  75.036  1.00 22.24 ? 955  ASP A N     1 
ATOM   6925  C  CA    . ASP A 1  957  ? -6.108  77.152  76.149  1.00 21.64 ? 955  ASP A CA    1 
ATOM   6926  C  C     . ASP A 1  957  ? -6.659  76.665  77.488  1.00 22.82 ? 955  ASP A C     1 
ATOM   6927  O  O     . ASP A 1  957  ? -6.694  77.440  78.450  1.00 22.30 ? 955  ASP A O     1 
ATOM   6928  C  CB    . ASP A 1  957  ? -6.606  78.569  75.869  1.00 25.43 ? 955  ASP A CB    1 
ATOM   6929  C  CG    . ASP A 1  957  ? -5.879  79.213  74.713  1.00 28.92 ? 955  ASP A CG    1 
ATOM   6930  O  OD1   . ASP A 1  957  ? -4.681  78.926  74.539  1.00 26.89 ? 955  ASP A OD1   1 
ATOM   6931  O  OD2   . ASP A 1  957  ? -6.507  79.991  73.972  1.00 31.40 ? 955  ASP A OD2   1 
ATOM   6932  N  N     . LEU A 1  958  ? -7.084  75.403  77.574  1.00 20.43 ? 956  LEU A N     1 
ATOM   6933  C  CA    . LEU A 1  958  ? -7.641  74.888  78.824  1.00 19.17 ? 956  LEU A CA    1 
ATOM   6934  C  C     . LEU A 1  958  ? -6.634  74.981  79.966  1.00 21.35 ? 956  LEU A C     1 
ATOM   6935  O  O     . LEU A 1  958  ? -6.983  75.394  81.076  1.00 20.46 ? 956  LEU A O     1 
ATOM   6936  C  CB    . LEU A 1  958  ? -8.098  73.443  78.636  1.00 19.96 ? 956  LEU A CB    1 
ATOM   6937  C  CG    . LEU A 1  958  ? -8.577  72.722  79.898  1.00 19.25 ? 956  LEU A CG    1 
ATOM   6938  C  CD1   . LEU A 1  958  ? -9.776  73.435  80.519  1.00 20.22 ? 956  LEU A CD1   1 
ATOM   6939  C  CD2   . LEU A 1  958  ? -8.921  71.273  79.590  1.00 20.03 ? 956  LEU A CD2   1 
ATOM   6940  N  N     . ASP A 1  959  ? -5.376  74.611  79.717  1.00 19.71 ? 957  ASP A N     1 
ATOM   6941  C  CA    . ASP A 1  959  ? -4.410  74.642  80.805  1.00 18.70 ? 957  ASP A CA    1 
ATOM   6942  C  C     . ASP A 1  959  ? -4.184  76.063  81.289  1.00 19.28 ? 957  ASP A C     1 
ATOM   6943  O  O     . ASP A 1  959  ? -4.077  76.301  82.494  1.00 20.56 ? 957  ASP A O     1 
ATOM   6944  C  CB    . ASP A 1  959  ? -3.080  74.015  80.377  1.00 21.97 ? 957  ASP A CB    1 
ATOM   6945  C  CG    . ASP A 1  959  ? -2.183  73.709  81.564  1.00 24.82 ? 957  ASP A CG    1 
ATOM   6946  O  OD1   . ASP A 1  959  ? -2.630  72.980  82.474  1.00 22.10 ? 957  ASP A OD1   1 
ATOM   6947  O  OD2   . ASP A 1  959  ? -1.042  74.204  81.605  1.00 28.63 ? 957  ASP A OD2   1 
ATOM   6948  N  N     . ARG A 1  960  ? -4.118  77.023  80.364  1.00 20.97 ? 958  ARG A N     1 
ATOM   6949  C  CA    . ARG A 1  960  ? -3.953  78.418  80.760  1.00 22.32 ? 958  ARG A CA    1 
ATOM   6950  C  C     . ARG A 1  960  ? -5.171  78.909  81.534  1.00 22.08 ? 958  ARG A C     1 
ATOM   6951  O  O     . ARG A 1  960  ? -5.040  79.694  82.481  1.00 23.98 ? 958  ARG A O     1 
ATOM   6952  C  CB    . ARG A 1  960  ? -3.713  79.293  79.526  1.00 23.58 ? 958  ARG A CB    1 
ATOM   6953  N  N     . LEU A 1  961  ? -6.360  78.442  81.151  1.00 18.81 ? 959  LEU A N     1 
ATOM   6954  C  CA    . LEU A 1  961  ? -7.573  78.798  81.881  1.00 20.45 ? 959  LEU A CA    1 
ATOM   6955  C  C     . LEU A 1  961  ? -7.503  78.322  83.326  1.00 19.98 ? 959  LEU A C     1 
ATOM   6956  O  O     . LEU A 1  961  ? -7.814  79.076  84.254  1.00 20.38 ? 959  LEU A O     1 
ATOM   6957  C  CB    . LEU A 1  961  ? -8.788  78.209  81.176  1.00 18.50 ? 959  LEU A CB    1 
ATOM   6958  C  CG    . LEU A 1  961  ? -10.097 78.324  81.950  1.00 18.94 ? 959  LEU A CG    1 
ATOM   6959  C  CD1   . LEU A 1  961  ? -10.430 79.798  82.125  1.00 21.83 ? 959  LEU A CD1   1 
ATOM   6960  C  CD2   . LEU A 1  961  ? -11.196 77.574  81.202  1.00 21.66 ? 959  LEU A CD2   1 
ATOM   6961  N  N     . VAL A 1  962  ? -7.080  77.072  83.542  1.00 17.73 ? 960  VAL A N     1 
ATOM   6962  C  CA    . VAL A 1  962  ? -6.923  76.578  84.909  1.00 18.20 ? 960  VAL A CA    1 
ATOM   6963  C  C     . VAL A 1  962  ? -5.940  77.452  85.677  1.00 22.55 ? 960  VAL A C     1 
ATOM   6964  O  O     . VAL A 1  962  ? -6.176  77.794  86.845  1.00 19.57 ? 960  VAL A O     1 
ATOM   6965  C  CB    . VAL A 1  962  ? -6.495  75.098  84.901  1.00 21.37 ? 960  VAL A CB    1 
ATOM   6966  C  CG1   . VAL A 1  962  ? -6.239  74.588  86.325  1.00 22.06 ? 960  VAL A CG1   1 
ATOM   6967  C  CG2   . VAL A 1  962  ? -7.561  74.249  84.211  1.00 20.04 ? 960  VAL A CG2   1 
ATOM   6968  N  N     . ASP A 1  963  ? -4.830  77.839  85.034  1.00 21.14 ? 961  ASP A N     1 
ATOM   6969  C  CA    . ASP A 1  963  ? -3.916  78.807  85.642  1.00 22.77 ? 961  ASP A CA    1 
ATOM   6970  C  C     . ASP A 1  963  ? -4.656  80.075  86.049  1.00 23.22 ? 961  ASP A C     1 
ATOM   6971  O  O     . ASP A 1  963  ? -4.496  80.571  87.171  1.00 24.88 ? 961  ASP A O     1 
ATOM   6972  C  CB    . ASP A 1  963  ? -2.787  79.173  84.674  1.00 24.12 ? 961  ASP A CB    1 
ATOM   6973  C  CG    . ASP A 1  963  ? -1.755  78.088  84.521  1.00 29.67 ? 961  ASP A CG    1 
ATOM   6974  O  OD1   . ASP A 1  963  ? -1.664  77.197  85.389  1.00 32.56 ? 961  ASP A OD1   1 
ATOM   6975  O  OD2   . ASP A 1  963  ? -1.008  78.150  83.520  1.00 36.01 ? 961  ASP A OD2   1 
ATOM   6976  N  N     . ASP A 1  964  ? -5.464  80.618  85.131  1.00 23.07 ? 962  ASP A N     1 
ATOM   6977  C  CA    . ASP A 1  964  ? -6.206  81.844  85.412  1.00 24.07 ? 962  ASP A CA    1 
ATOM   6978  C  C     . ASP A 1  964  ? -7.136  81.672  86.610  1.00 26.58 ? 962  ASP A C     1 
ATOM   6979  O  O     . ASP A 1  964  ? -7.257  82.578  87.446  1.00 27.32 ? 962  ASP A O     1 
ATOM   6980  C  CB    . ASP A 1  964  ? -7.010  82.260  84.184  1.00 25.99 ? 962  ASP A CB    1 
ATOM   6981  C  CG    . ASP A 1  964  ? -6.139  82.766  83.052  1.00 24.40 ? 962  ASP A CG    1 
ATOM   6982  O  OD1   . ASP A 1  964  ? -4.928  82.961  83.264  1.00 29.86 ? 962  ASP A OD1   1 
ATOM   6983  O  OD2   . ASP A 1  964  ? -6.686  82.955  81.952  1.00 33.37 ? 962  ASP A OD2   1 
ATOM   6984  N  N     . VAL A 1  965  ? -7.814  80.525  86.699  1.00 22.31 ? 963  VAL A N     1 
ATOM   6985  C  CA    . VAL A 1  965  ? -8.682  80.261  87.843  1.00 24.43 ? 963  VAL A CA    1 
ATOM   6986  C  C     . VAL A 1  965  ? -7.865  80.233  89.129  1.00 24.28 ? 963  VAL A C     1 
ATOM   6987  O  O     . VAL A 1  965  ? -8.240  80.842  90.140  1.00 23.44 ? 963  VAL A O     1 
ATOM   6988  C  CB    . VAL A 1  965  ? -9.456  78.947  87.645  1.00 20.68 ? 963  VAL A CB    1 
ATOM   6989  C  CG1   . VAL A 1  965  ? -10.220 78.603  88.919  1.00 20.12 ? 963  VAL A CG1   1 
ATOM   6990  C  CG2   . VAL A 1  965  ? -10.426 79.064  86.471  1.00 22.34 ? 963  VAL A CG2   1 
ATOM   6991  N  N     . ASN A 1  966  ? -6.732  79.523  89.110  1.00 23.11 ? 964  ASN A N     1 
ATOM   6992  C  CA    . ASN A 1  966  ? -5.877  79.478  90.291  1.00 21.90 ? 964  ASN A CA    1 
ATOM   6993  C  C     . ASN A 1  966  ? -5.322  80.854  90.625  1.00 23.81 ? 964  ASN A C     1 
ATOM   6994  O  O     . ASN A 1  966  ? -5.077  81.153  91.799  1.00 20.82 ? 964  ASN A O     1 
ATOM   6995  C  CB    . ASN A 1  966  ? -4.704  78.510  90.091  1.00 23.98 ? 964  ASN A CB    1 
ATOM   6996  C  CG    . ASN A 1  966  ? -5.129  77.049  90.036  1.00 22.21 ? 964  ASN A CG    1 
ATOM   6997  O  OD1   . ASN A 1  966  ? -6.155  76.647  90.602  1.00 20.05 ? 964  ASN A OD1   1 
ATOM   6998  N  ND2   . ASN A 1  966  ? -4.316  76.237  89.370  1.00 21.99 ? 964  ASN A ND2   1 
ATOM   6999  N  N     . ALA A 1  967  ? -5.123  81.697  89.606  1.00 23.85 ? 965  ALA A N     1 
ATOM   7000  C  CA    . ALA A 1  967  ? -4.409  82.960  89.778  1.00 24.94 ? 965  ALA A CA    1 
ATOM   7001  C  C     . ALA A 1  967  ? -5.161  83.958  90.640  1.00 25.52 ? 965  ALA A C     1 
ATOM   7002  O  O     . ALA A 1  967  ? -4.545  84.916  91.123  1.00 26.49 ? 965  ALA A O     1 
ATOM   7003  C  CB    . ALA A 1  967  ? -4.113  83.593  88.415  1.00 28.68 ? 965  ALA A CB    1 
ATOM   7004  N  N     . THR A 1  968  ? -6.466  83.770  90.842  1.00 23.96 ? 966  THR A N     1 
ATOM   7005  C  CA    . THR A 1  968  ? -7.202  84.672  91.722  1.00 22.87 ? 966  THR A CA    1 
ATOM   7006  C  C     . THR A 1  968  ? -6.702  84.590  93.156  1.00 21.75 ? 966  THR A C     1 
ATOM   7007  O  O     . THR A 1  968  ? -6.937  85.526  93.934  1.00 24.12 ? 966  THR A O     1 
ATOM   7008  C  CB    . THR A 1  968  ? -8.703  84.373  91.718  1.00 22.27 ? 966  THR A CB    1 
ATOM   7009  O  OG1   . THR A 1  968  ? -8.947  83.133  92.399  1.00 20.60 ? 966  THR A OG1   1 
ATOM   7010  C  CG2   . THR A 1  968  ? -9.258  84.296  90.285  1.00 21.95 ? 966  THR A CG2   1 
ATOM   7011  N  N     . GLY A 1  969  ? -6.050  83.487  93.526  1.00 20.14 ? 967  GLY A N     1 
ATOM   7012  C  CA    . GLY A 1  969  ? -5.653  83.244  94.891  1.00 21.56 ? 967  GLY A CA    1 
ATOM   7013  C  C     . GLY A 1  969  ? -6.707  82.585  95.751  1.00 19.80 ? 967  GLY A C     1 
ATOM   7014  O  O     . GLY A 1  969  ? -6.395  82.159  96.865  1.00 19.58 ? 967  GLY A O     1 
ATOM   7015  N  N     . TYR A 1  970  ? -7.947  82.496  95.277  1.00 19.37 ? 968  TYR A N     1 
ATOM   7016  C  CA    . TYR A 1  970  ? -8.963  81.751  95.995  1.00 17.76 ? 968  TYR A CA    1 
ATOM   7017  C  C     . TYR A 1  970  ? -8.820  80.259  95.694  1.00 16.79 ? 968  TYR A C     1 
ATOM   7018  O  O     . TYR A 1  970  ? -8.022  79.845  94.851  1.00 20.22 ? 968  TYR A O     1 
ATOM   7019  C  CB    . TYR A 1  970  ? -10.354 82.244  95.609  1.00 18.38 ? 968  TYR A CB    1 
ATOM   7020  C  CG    . TYR A 1  970  ? -10.661 83.653  96.070  1.00 16.74 ? 968  TYR A CG    1 
ATOM   7021  C  CD1   . TYR A 1  970  ? -11.203 83.890  97.323  1.00 20.73 ? 968  TYR A CD1   1 
ATOM   7022  C  CD2   . TYR A 1  970  ? -10.463 84.734  95.225  1.00 23.02 ? 968  TYR A CD2   1 
ATOM   7023  C  CE1   . TYR A 1  970  ? -11.519 85.182  97.737  1.00 22.60 ? 968  TYR A CE1   1 
ATOM   7024  C  CE2   . TYR A 1  970  ? -10.775 86.017  95.623  1.00 21.33 ? 968  TYR A CE2   1 
ATOM   7025  C  CZ    . TYR A 1  970  ? -11.294 86.236  96.879  1.00 25.00 ? 968  TYR A CZ    1 
ATOM   7026  O  OH    . TYR A 1  970  ? -11.604 87.526  97.266  1.00 31.20 ? 968  TYR A OH    1 
ATOM   7027  N  N     . GLY A 1  971  ? -9.606  79.446  96.388  1.00 15.05 ? 969  GLY A N     1 
ATOM   7028  C  CA    . GLY A 1  971  ? -9.544  78.014  96.160  1.00 16.77 ? 969  GLY A CA    1 
ATOM   7029  C  C     . GLY A 1  971  ? -10.577 77.246  96.948  1.00 15.99 ? 969  GLY A C     1 
ATOM   7030  O  O     . GLY A 1  971  ? -10.247 76.323  97.702  1.00 16.55 ? 969  GLY A O     1 
ATOM   7031  N  N     . LEU A 1  972  ? -11.846 77.619  96.772  1.00 15.10 ? 970  LEU A N     1 
ATOM   7032  C  CA    . LEU A 1  972  ? -12.906 77.016  97.571  1.00 14.75 ? 970  LEU A CA    1 
ATOM   7033  C  C     . LEU A 1  972  ? -13.592 75.900  96.794  1.00 16.92 ? 970  LEU A C     1 
ATOM   7034  O  O     . LEU A 1  972  ? -13.195 74.737  96.910  1.00 16.10 ? 970  LEU A O     1 
ATOM   7035  C  CB    . LEU A 1  972  ? -13.911 78.079  98.024  1.00 15.14 ? 970  LEU A CB    1 
ATOM   7036  C  CG    . LEU A 1  972  ? -14.929 77.623  99.071  1.00 17.06 ? 970  LEU A CG    1 
ATOM   7037  C  CD1   . LEU A 1  972  ? -14.241 76.858  100.197 1.00 16.12 ? 970  LEU A CD1   1 
ATOM   7038  C  CD2   . LEU A 1  972  ? -15.656 78.838  99.651  1.00 17.98 ? 970  LEU A CD2   1 
ATOM   7039  N  N     . THR A 1  973  ? -14.608 76.220  95.993  1.00 15.27 ? 971  THR A N     1 
ATOM   7040  C  CA    . THR A 1  973  ? -15.241 75.192  95.185  1.00 14.50 ? 971  THR A CA    1 
ATOM   7041  C  C     . THR A 1  973  ? -14.862 75.354  93.721  1.00 15.69 ? 971  THR A C     1 
ATOM   7042  O  O     . THR A 1  973  ? -14.501 76.434  93.259  1.00 15.33 ? 971  THR A O     1 
ATOM   7043  C  CB    . THR A 1  973  ? -16.767 75.216  95.321  1.00 14.90 ? 971  THR A CB    1 
ATOM   7044  O  OG1   . THR A 1  973  ? -17.250 76.495  94.919  1.00 15.58 ? 971  THR A OG1   1 
ATOM   7045  C  CG2   . THR A 1  973  ? -17.176 74.947  96.761  1.00 17.14 ? 971  THR A CG2   1 
ATOM   7046  N  N     . PHE A 1  974  ? -14.977 74.250  92.990  1.00 16.04 ? 972  PHE A N     1 
ATOM   7047  C  CA    . PHE A 1  974  ? -14.631 74.225  91.581  1.00 16.25 ? 972  PHE A CA    1 
ATOM   7048  C  C     . PHE A 1  974  ? -15.438 73.128  90.917  1.00 14.66 ? 972  PHE A C     1 
ATOM   7049  O  O     . PHE A 1  974  ? -15.542 72.026  91.458  1.00 16.36 ? 972  PHE A O     1 
ATOM   7050  C  CB    . PHE A 1  974  ? -13.135 73.956  91.364  1.00 15.42 ? 972  PHE A CB    1 
ATOM   7051  C  CG    . PHE A 1  974  ? -12.790 73.747  89.931  1.00 15.62 ? 972  PHE A CG    1 
ATOM   7052  C  CD1   . PHE A 1  974  ? -12.613 74.831  89.094  1.00 14.55 ? 972  PHE A CD1   1 
ATOM   7053  C  CD2   . PHE A 1  974  ? -12.667 72.468  89.416  1.00 15.78 ? 972  PHE A CD2   1 
ATOM   7054  C  CE1   . PHE A 1  974  ? -12.326 74.642  87.749  1.00 14.47 ? 972  PHE A CE1   1 
ATOM   7055  C  CE2   . PHE A 1  974  ? -12.378 72.267  88.068  1.00 14.54 ? 972  PHE A CE2   1 
ATOM   7056  C  CZ    . PHE A 1  974  ? -12.193 73.347  87.248  1.00 16.11 ? 972  PHE A CZ    1 
ATOM   7057  N  N     . GLY A 1  975  ? -15.987 73.417  89.742  1.00 14.34 ? 973  GLY A N     1 
ATOM   7058  C  CA    . GLY A 1  975  ? -16.747 72.438  88.993  1.00 14.69 ? 973  GLY A CA    1 
ATOM   7059  C  C     . GLY A 1  975  ? -16.150 72.160  87.629  1.00 13.58 ? 973  GLY A C     1 
ATOM   7060  O  O     . GLY A 1  975  ? -15.584 73.047  86.985  1.00 15.36 ? 973  GLY A O     1 
ATOM   7061  N  N     . LEU A 1  976  ? -16.339 70.928  87.167  1.00 14.75 ? 974  LEU A N     1 
ATOM   7062  C  CA    . LEU A 1  976  ? -15.956 70.558  85.813  1.00 13.64 ? 974  LEU A CA    1 
ATOM   7063  C  C     . LEU A 1  976  ? -17.056 69.702  85.210  1.00 14.27 ? 974  LEU A C     1 
ATOM   7064  O  O     . LEU A 1  976  ? -17.457 68.696  85.803  1.00 15.59 ? 974  LEU A O     1 
ATOM   7065  C  CB    . LEU A 1  976  ? -14.635 69.793  85.809  1.00 15.61 ? 974  LEU A CB    1 
ATOM   7066  C  CG    . LEU A 1  976  ? -14.251 69.142  84.483  1.00 15.68 ? 974  LEU A CG    1 
ATOM   7067  C  CD1   . LEU A 1  976  ? -13.862 70.196  83.457  1.00 17.70 ? 974  LEU A CD1   1 
ATOM   7068  C  CD2   . LEU A 1  976  ? -13.115 68.179  84.764  1.00 15.99 ? 974  LEU A CD2   1 
ATOM   7069  N  N     . HIS A 1  977  ? -17.550 70.114  84.039  1.00 15.37 ? 975  HIS A N     1 
ATOM   7070  C  CA    . HIS A 1  977  ? -18.495 69.320  83.265  1.00 15.53 ? 975  HIS A CA    1 
ATOM   7071  C  C     . HIS A 1  977  ? -17.785 68.827  82.015  1.00 14.26 ? 975  HIS A C     1 
ATOM   7072  O  O     . HIS A 1  977  ? -17.438 69.619  81.128  1.00 14.59 ? 975  HIS A O     1 
ATOM   7073  C  CB    . HIS A 1  977  ? -19.740 70.132  82.909  1.00 16.22 ? 975  HIS A CB    1 
ATOM   7074  C  CG    . HIS A 1  977  ? -20.853 69.959  83.887  1.00 15.92 ? 975  HIS A CG    1 
ATOM   7075  N  ND1   . HIS A 1  977  ? -21.954 69.177  83.623  1.00 19.17 ? 975  HIS A ND1   1 
ATOM   7076  C  CD2   . HIS A 1  977  ? -21.026 70.445  85.138  1.00 18.77 ? 975  HIS A CD2   1 
ATOM   7077  C  CE1   . HIS A 1  977  ? -22.773 69.215  84.658  1.00 18.32 ? 975  HIS A CE1   1 
ATOM   7078  N  NE2   . HIS A 1  977  ? -22.235 69.979  85.590  1.00 18.53 ? 975  HIS A NE2   1 
ATOM   7079  N  N     . THR A 1  978  ? -17.571 67.518  81.956  1.00 13.41 ? 976  THR A N     1 
ATOM   7080  C  CA    . THR A 1  978  ? -16.955 66.875  80.806  1.00 16.00 ? 976  THR A CA    1 
ATOM   7081  C  C     . THR A 1  978  ? -17.269 65.395  80.881  1.00 15.46 ? 976  THR A C     1 
ATOM   7082  O  O     . THR A 1  978  ? -17.493 64.845  81.961  1.00 16.76 ? 976  THR A O     1 
ATOM   7083  C  CB    . THR A 1  978  ? -15.434 67.071  80.758  1.00 15.25 ? 976  THR A CB    1 
ATOM   7084  O  OG1   . THR A 1  978  ? -14.918 66.412  79.597  1.00 15.81 ? 976  THR A OG1   1 
ATOM   7085  C  CG2   . THR A 1  978  ? -14.744 66.445  81.981  1.00 15.43 ? 976  THR A CG2   1 
ATOM   7086  N  N     . ARG A 1  979  ? -17.250 64.747  79.723  1.00 16.44 ? 977  ARG A N     1 
ATOM   7087  C  CA    . ARG A 1  979  ? -17.347 63.296  79.683  1.00 17.57 ? 977  ARG A CA    1 
ATOM   7088  C  C     . ARG A 1  979  ? -16.001 62.618  79.457  1.00 19.66 ? 977  ARG A C     1 
ATOM   7089  O  O     . ARG A 1  979  ? -15.942 61.381  79.433  1.00 20.19 ? 977  ARG A O     1 
ATOM   7090  C  CB    . ARG A 1  979  ? -18.346 62.883  78.606  1.00 18.88 ? 977  ARG A CB    1 
ATOM   7091  C  CG    . ARG A 1  979  ? -19.789 63.190  79.030  1.00 24.92 ? 977  ARG A CG    1 
ATOM   7092  C  CD    . ARG A 1  979  ? -20.810 62.610  78.076  1.00 32.13 ? 977  ARG A CD    1 
ATOM   7093  N  NE    . ARG A 1  979  ? -21.286 63.601  77.121  1.00 35.75 ? 977  ARG A NE    1 
ATOM   7094  C  CZ    . ARG A 1  979  ? -22.097 63.336  76.105  1.00 33.26 ? 977  ARG A CZ    1 
ATOM   7095  N  NH1   . ARG A 1  979  ? -22.531 62.108  75.870  1.00 31.73 ? 977  ARG A NH1   1 
ATOM   7096  N  NH2   . ARG A 1  979  ? -22.499 64.331  75.318  1.00 39.58 ? 977  ARG A NH2   1 
ATOM   7097  N  N     . LEU A 1  980  ? -14.918 63.383  79.360  1.00 16.39 ? 978  LEU A N     1 
ATOM   7098  C  CA    . LEU A 1  980  ? -13.651 62.894  78.824  1.00 14.93 ? 978  LEU A CA    1 
ATOM   7099  C  C     . LEU A 1  980  ? -12.625 62.716  79.941  1.00 17.12 ? 978  LEU A C     1 
ATOM   7100  O  O     . LEU A 1  980  ? -12.258 63.685  80.608  1.00 16.75 ? 978  LEU A O     1 
ATOM   7101  C  CB    . LEU A 1  980  ? -13.110 63.860  77.774  1.00 16.29 ? 978  LEU A CB    1 
ATOM   7102  C  CG    . LEU A 1  980  ? -14.071 64.214  76.634  1.00 18.25 ? 978  LEU A CG    1 
ATOM   7103  C  CD1   . LEU A 1  980  ? -13.439 65.273  75.748  1.00 19.35 ? 978  LEU A CD1   1 
ATOM   7104  C  CD2   . LEU A 1  980  ? -14.453 62.978  75.831  1.00 17.96 ? 978  LEU A CD2   1 
ATOM   7105  N  N     . ASP A 1  981  ? -12.131 61.487  80.104  1.00 15.83 ? 979  ASP A N     1 
ATOM   7106  C  CA    . ASP A 1  981  ? -11.198 61.189  81.193  1.00 16.11 ? 979  ASP A CA    1 
ATOM   7107  C  C     . ASP A 1  981  ? -9.929  62.016  81.096  1.00 15.51 ? 979  ASP A C     1 
ATOM   7108  O  O     . ASP A 1  981  ? -9.362  62.402  82.124  1.00 18.01 ? 979  ASP A O     1 
ATOM   7109  C  CB    . ASP A 1  981  ? -10.837 59.700  81.192  1.00 16.78 ? 979  ASP A CB    1 
ATOM   7110  C  CG    . ASP A 1  981  ? -11.950 58.823  81.700  1.00 17.90 ? 979  ASP A CG    1 
ATOM   7111  O  OD1   . ASP A 1  981  ? -12.871 59.351  82.326  1.00 18.28 ? 979  ASP A OD1   1 
ATOM   7112  O  OD2   . ASP A 1  981  ? -11.895 57.593  81.467  1.00 19.57 ? 979  ASP A OD2   1 
ATOM   7113  N  N     . GLU A 1  982  ? -9.426  62.249  79.878  1.00 15.68 ? 980  GLU A N     1 
ATOM   7114  C  CA    . GLU A 1  982  ? -8.206  63.040  79.754  1.00 17.06 ? 980  GLU A CA    1 
ATOM   7115  C  C     . GLU A 1  982  ? -8.415  64.431  80.330  1.00 16.04 ? 980  GLU A C     1 
ATOM   7116  O  O     . GLU A 1  982  ? -7.530  64.982  80.996  1.00 16.27 ? 980  GLU A O     1 
ATOM   7117  C  CB    . GLU A 1  982  ? -7.757  63.148  78.297  1.00 19.19 ? 980  GLU A CB    1 
ATOM   7118  C  CG    . GLU A 1  982  ? -6.485  63.994  78.133  1.00 20.14 ? 980  GLU A CG    1 
ATOM   7119  C  CD    . GLU A 1  982  ? -6.190  64.370  76.689  1.00 23.45 ? 980  GLU A CD    1 
ATOM   7120  O  OE1   . GLU A 1  982  ? -7.127  64.787  75.981  1.00 25.77 ? 980  GLU A OE1   1 
ATOM   7121  O  OE2   . GLU A 1  982  ? -5.021  64.257  76.259  1.00 22.22 ? 980  GLU A OE2   1 
ATOM   7122  N  N     . THR A 1  983  ? -9.587  65.003  80.089  1.00 15.25 ? 981  THR A N     1 
ATOM   7123  C  CA    . THR A 1  983  ? -9.879  66.340  80.592  1.00 14.58 ? 981  THR A CA    1 
ATOM   7124  C  C     . THR A 1  983  ? -10.074 66.331  82.106  1.00 15.03 ? 981  THR A C     1 
ATOM   7125  O  O     . THR A 1  983  ? -9.594  67.238  82.801  1.00 15.47 ? 981  THR A O     1 
ATOM   7126  C  CB    . THR A 1  983  ? -11.112 66.891  79.867  1.00 15.72 ? 981  THR A CB    1 
ATOM   7127  O  OG1   . THR A 1  983  ? -10.816 67.007  78.465  1.00 18.27 ? 981  THR A OG1   1 
ATOM   7128  C  CG2   . THR A 1  983  ? -11.526 68.264  80.446  1.00 15.74 ? 981  THR A CG2   1 
ATOM   7129  N  N     . ILE A 1  984  ? -10.746 65.305  82.640  1.00 15.50 ? 982  ILE A N     1 
ATOM   7130  C  CA    . ILE A 1  984  ? -10.874 65.186  84.090  1.00 14.98 ? 982  ILE A CA    1 
ATOM   7131  C  C     . ILE A 1  984  ? -9.501  65.113  84.726  1.00 16.88 ? 982  ILE A C     1 
ATOM   7132  O  O     . ILE A 1  984  ? -9.203  65.833  85.687  1.00 15.72 ? 982  ILE A O     1 
ATOM   7133  C  CB    . ILE A 1  984  ? -11.717 63.961  84.475  1.00 14.29 ? 982  ILE A CB    1 
ATOM   7134  C  CG1   . ILE A 1  984  ? -13.133 64.138  83.955  1.00 16.75 ? 982  ILE A CG1   1 
ATOM   7135  C  CG2   . ILE A 1  984  ? -11.746 63.802  85.996  1.00 15.32 ? 982  ILE A CG2   1 
ATOM   7136  C  CD1   . ILE A 1  984  ? -13.975 62.906  84.102  1.00 18.86 ? 982  ILE A CD1   1 
ATOM   7137  N  N     . ALA A 1  985  ? -8.643  64.240  84.193  1.00 14.05 ? 983  ALA A N     1 
ATOM   7138  C  CA    . ALA A 1  985  ? -7.334  64.041  84.806  1.00 16.61 ? 983  ALA A CA    1 
ATOM   7139  C  C     . ALA A 1  985  ? -6.517  65.326  84.756  1.00 17.07 ? 983  ALA A C     1 
ATOM   7140  O  O     . ALA A 1  985  ? -5.919  65.737  85.756  1.00 17.22 ? 983  ALA A O     1 
ATOM   7141  C  CB    . ALA A 1  985  ? -6.603  62.890  84.104  1.00 17.00 ? 983  ALA A CB    1 
ATOM   7142  N  N     . HIS A 1  986  ? -6.507  65.984  83.598  1.00 16.50 ? 984  HIS A N     1 
ATOM   7143  C  CA    . HIS A 1  986  ? -5.771  67.234  83.426  1.00 17.74 ? 984  HIS A CA    1 
ATOM   7144  C  C     . HIS A 1  986  ? -6.271  68.304  84.387  1.00 17.61 ? 984  HIS A C     1 
ATOM   7145  O  O     . HIS A 1  986  ? -5.506  68.861  85.181  1.00 16.61 ? 984  HIS A O     1 
ATOM   7146  C  CB    . HIS A 1  986  ? -5.917  67.688  81.974  1.00 18.81 ? 984  HIS A CB    1 
ATOM   7147  C  CG    . HIS A 1  986  ? -5.354  69.047  81.684  1.00 17.58 ? 984  HIS A CG    1 
ATOM   7148  N  ND1   . HIS A 1  986  ? -5.593  69.694  80.494  1.00 22.90 ? 984  HIS A ND1   1 
ATOM   7149  C  CD2   . HIS A 1  986  ? -4.566  69.874  82.411  1.00 19.14 ? 984  HIS A CD2   1 
ATOM   7150  C  CE1   . HIS A 1  986  ? -4.982  70.866  80.501  1.00 24.38 ? 984  HIS A CE1   1 
ATOM   7151  N  NE2   . HIS A 1  986  ? -4.359  71.005  81.657  1.00 19.28 ? 984  HIS A NE2   1 
ATOM   7152  N  N     . VAL A 1  987  ? -7.565  68.606  84.324  1.00 16.95 ? 985  VAL A N     1 
ATOM   7153  C  CA    . VAL A 1  987  ? -8.105  69.716  85.102  1.00 17.95 ? 985  VAL A CA    1 
ATOM   7154  C  C     . VAL A 1  987  ? -7.977  69.446  86.598  1.00 17.51 ? 985  VAL A C     1 
ATOM   7155  O  O     . VAL A 1  987  ? -7.548  70.320  87.362  1.00 17.79 ? 985  VAL A O     1 
ATOM   7156  C  CB    . VAL A 1  987  ? -9.561  69.988  84.702  1.00 14.88 ? 985  VAL A CB    1 
ATOM   7157  C  CG1   . VAL A 1  987  ? -10.194 70.995  85.664  1.00 15.04 ? 985  VAL A CG1   1 
ATOM   7158  C  CG2   . VAL A 1  987  ? -9.624  70.499  83.272  1.00 18.63 ? 985  VAL A CG2   1 
ATOM   7159  N  N     . THR A 1  988  ? -8.358  68.248  87.054  1.00 17.37 ? 986  THR A N     1 
ATOM   7160  C  CA    . THR A 1  988  ? -8.343  68.017  88.502  1.00 19.06 ? 986  THR A CA    1 
ATOM   7161  C  C     . THR A 1  988  ? -6.924  67.947  89.044  1.00 20.91 ? 986  THR A C     1 
ATOM   7162  O  O     . THR A 1  988  ? -6.698  68.242  90.225  1.00 20.05 ? 986  THR A O     1 
ATOM   7163  C  CB    . THR A 1  988  ? -9.121  66.748  88.891  1.00 19.52 ? 986  THR A CB    1 
ATOM   7164  O  OG1   . THR A 1  988  ? -8.534  65.581  88.301  1.00 19.66 ? 986  THR A OG1   1 
ATOM   7165  C  CG2   . THR A 1  988  ? -10.583 66.862  88.469  1.00 17.87 ? 986  THR A CG2   1 
ATOM   7166  N  N     . SER A 1  989  ? -5.952  67.599  88.207  1.00 18.13 ? 987  SER A N     1 
ATOM   7167  C  CA    . SER A 1  989  ? -4.584  67.568  88.702  1.00 19.57 ? 987  SER A CA    1 
ATOM   7168  C  C     . SER A 1  989  ? -3.975  68.960  88.783  1.00 21.12 ? 987  SER A C     1 
ATOM   7169  O  O     . SER A 1  989  ? -3.059  69.172  89.584  1.00 25.36 ? 987  SER A O     1 
ATOM   7170  C  CB    . SER A 1  989  ? -3.717  66.654  87.828  1.00 22.64 ? 987  SER A CB    1 
ATOM   7171  O  OG    . SER A 1  989  ? -3.528  67.189  86.537  1.00 26.51 ? 987  SER A OG    1 
ATOM   7172  N  N     . ARG A 1  990  ? -4.492  69.919  88.015  1.00 17.58 ? 988  ARG A N     1 
ATOM   7173  C  CA    . ARG A 1  990  ? -3.902  71.249  87.928  1.00 20.10 ? 988  ARG A CA    1 
ATOM   7174  C  C     . ARG A 1  990  ? -4.653  72.292  88.735  1.00 19.91 ? 988  ARG A C     1 
ATOM   7175  O  O     . ARG A 1  990  ? -4.048  73.286  89.152  1.00 20.95 ? 988  ARG A O     1 
ATOM   7176  C  CB    . ARG A 1  990  ? -3.833  71.701  86.465  1.00 21.82 ? 988  ARG A CB    1 
ATOM   7177  C  CG    . ARG A 1  990  ? -3.055  70.740  85.573  1.00 25.86 ? 988  ARG A CG    1 
ATOM   7178  C  CD    . ARG A 1  990  ? -1.557  70.944  85.699  1.00 25.86 ? 988  ARG A CD    1 
ATOM   7179  N  NE    . ARG A 1  990  ? -1.068  71.908  84.719  1.00 27.62 ? 988  ARG A NE    1 
ATOM   7180  C  CZ    . ARG A 1  990  ? 0.187   72.332  84.658  1.00 26.76 ? 988  ARG A CZ    1 
ATOM   7181  N  NH1   . ARG A 1  990  ? 1.085   71.949  85.549  1.00 27.51 ? 988  ARG A NH1   1 
ATOM   7182  N  NH2   . ARG A 1  990  ? 0.548   73.156  83.675  1.00 25.72 ? 988  ARG A NH2   1 
ATOM   7183  N  N     . ILE A 1  991  ? -5.953  72.090  88.959  1.00 19.00 ? 989  ILE A N     1 
ATOM   7184  C  CA    . ILE A 1  991  ? -6.724  73.027  89.766  1.00 17.35 ? 989  ILE A CA    1 
ATOM   7185  C  C     . ILE A 1  991  ? -6.270  72.942  91.217  1.00 17.80 ? 989  ILE A C     1 
ATOM   7186  O  O     . ILE A 1  991  ? -5.861  71.884  91.705  1.00 18.68 ? 989  ILE A O     1 
ATOM   7187  C  CB    . ILE A 1  991  ? -8.232  72.730  89.639  1.00 15.51 ? 989  ILE A CB    1 
ATOM   7188  C  CG1   . ILE A 1  991  ? -9.059  73.901  90.178  1.00 17.04 ? 989  ILE A CG1   1 
ATOM   7189  C  CG2   . ILE A 1  991  ? -8.586  71.423  90.344  1.00 16.14 ? 989  ILE A CG2   1 
ATOM   7190  C  CD1   . ILE A 1  991  ? -8.984  75.134  89.294  1.00 18.71 ? 989  ILE A CD1   1 
ATOM   7191  N  N     . LYS A 1  992  ? -6.334  74.071  91.913  1.00 16.25 ? 990  LYS A N     1 
ATOM   7192  C  CA    . LYS A 1  992  ? -5.979  74.148  93.328  1.00 15.01 ? 990  LYS A CA    1 
ATOM   7193  C  C     . LYS A 1  992  ? -7.194  74.669  94.103  1.00 15.31 ? 990  LYS A C     1 
ATOM   7194  O  O     . LYS A 1  992  ? -7.348  75.878  94.315  1.00 18.49 ? 990  LYS A O     1 
ATOM   7195  C  CB    . LYS A 1  992  ? -4.754  75.039  93.525  1.00 19.34 ? 990  LYS A CB    1 
ATOM   7196  N  N     . ALA A 1  993  ? -8.057  73.751  94.528  1.00 16.62 ? 991  ALA A N     1 
ATOM   7197  C  CA    . ALA A 1  993  ? -9.247  74.126  95.281  1.00 15.79 ? 991  ALA A CA    1 
ATOM   7198  C  C     . ALA A 1  993  ? -9.610  73.001  96.228  1.00 16.13 ? 991  ALA A C     1 
ATOM   7199  O  O     . ALA A 1  993  ? -9.303  71.834  95.980  1.00 15.85 ? 991  ALA A O     1 
ATOM   7200  C  CB    . ALA A 1  993  ? -10.425 74.432  94.351  1.00 15.84 ? 991  ALA A CB    1 
ATOM   7201  N  N     . GLY A 1  994  ? -10.317 73.362  97.303  1.00 15.96 ? 992  GLY A N     1 
ATOM   7202  C  CA    . GLY A 1  994  ? -10.604 72.398  98.350  1.00 17.40 ? 992  GLY A CA    1 
ATOM   7203  C  C     . GLY A 1  994  ? -11.758 71.463  98.061  1.00 15.20 ? 992  GLY A C     1 
ATOM   7204  O  O     . GLY A 1  994  ? -11.772 70.333  98.556  1.00 14.76 ? 992  GLY A O     1 
ATOM   7205  N  N     . ASN A 1  995  ? -12.730 71.894  97.258  1.00 14.90 ? 993  ASN A N     1 
ATOM   7206  C  CA    . ASN A 1  995  ? -13.906 71.079  96.968  1.00 15.13 ? 993  ASN A CA    1 
ATOM   7207  C  C     . ASN A 1  995  ? -14.124 71.053  95.462  1.00 14.10 ? 993  ASN A C     1 
ATOM   7208  O  O     . ASN A 1  995  ? -14.434 72.085  94.854  1.00 14.75 ? 993  ASN A O     1 
ATOM   7209  C  CB    . ASN A 1  995  ? -15.142 71.599  97.697  1.00 14.65 ? 993  ASN A CB    1 
ATOM   7210  C  CG    . ASN A 1  995  ? -15.179 71.155  99.144  1.00 15.78 ? 993  ASN A CG    1 
ATOM   7211  O  OD1   . ASN A 1  995  ? -14.553 71.777  100.000 1.00 15.97 ? 993  ASN A OD1   1 
ATOM   7212  N  ND2   . ASN A 1  995  ? -15.881 70.054  99.422  1.00 14.63 ? 993  ASN A ND2   1 
ATOM   7213  N  N     . LEU A 1  996  ? -13.928 69.879  94.864  1.00 13.78 ? 994  LEU A N     1 
ATOM   7214  C  CA    . LEU A 1  996  ? -14.108 69.671  93.433  1.00 13.44 ? 994  LEU A CA    1 
ATOM   7215  C  C     . LEU A 1  996  ? -15.397 68.913  93.164  1.00 14.49 ? 994  LEU A C     1 
ATOM   7216  O  O     . LEU A 1  996  ? -15.787 68.031  93.931  1.00 13.43 ? 994  LEU A O     1 
ATOM   7217  C  CB    . LEU A 1  996  ? -12.945 68.877  92.844  1.00 12.69 ? 994  LEU A CB    1 
ATOM   7218  C  CG    . LEU A 1  996  ? -11.561 69.302  93.323  1.00 14.02 ? 994  LEU A CG    1 
ATOM   7219  C  CD1   . LEU A 1  996  ? -10.511 68.389  92.647  1.00 17.32 ? 994  LEU A CD1   1 
ATOM   7220  C  CD2   . LEU A 1  996  ? -11.321 70.763  92.974  1.00 15.52 ? 994  LEU A CD2   1 
ATOM   7221  N  N     . TYR A 1  997  ? -16.040 69.246  92.045  1.00 14.93 ? 995  TYR A N     1 
ATOM   7222  C  CA    . TYR A 1  997  ? -17.309 68.623  91.690  1.00 15.68 ? 995  TYR A CA    1 
ATOM   7223  C  C     . TYR A 1  997  ? -17.311 68.335  90.199  1.00 13.50 ? 995  TYR A C     1 
ATOM   7224  O  O     . TYR A 1  997  ? -17.054 69.231  89.392  1.00 14.18 ? 995  TYR A O     1 
ATOM   7225  C  CB    . TYR A 1  997  ? -18.494 69.521  92.048  1.00 14.13 ? 995  TYR A CB    1 
ATOM   7226  C  CG    . TYR A 1  997  ? -18.536 69.943  93.490  1.00 14.96 ? 995  TYR A CG    1 
ATOM   7227  C  CD1   . TYR A 1  997  ? -17.887 71.101  93.901  1.00 16.27 ? 995  TYR A CD1   1 
ATOM   7228  C  CD2   . TYR A 1  997  ? -19.220 69.192  94.441  1.00 15.55 ? 995  TYR A CD2   1 
ATOM   7229  C  CE1   . TYR A 1  997  ? -17.922 71.507  95.204  1.00 19.59 ? 995  TYR A CE1   1 
ATOM   7230  C  CE2   . TYR A 1  997  ? -19.246 69.592  95.768  1.00 18.06 ? 995  TYR A CE2   1 
ATOM   7231  C  CZ    . TYR A 1  997  ? -18.593 70.758  96.132  1.00 19.41 ? 995  TYR A CZ    1 
ATOM   7232  O  OH    . TYR A 1  997  ? -18.609 71.204  97.442  1.00 21.40 ? 995  TYR A OH    1 
ATOM   7233  N  N     . ILE A 1  998  ? -17.570 67.084  89.843  1.00 13.79 ? 996  ILE A N     1 
ATOM   7234  C  CA    . ILE A 1  998  ? -17.499 66.633  88.459  1.00 13.68 ? 996  ILE A CA    1 
ATOM   7235  C  C     . ILE A 1  998  ? -18.908 66.274  88.007  1.00 13.65 ? 996  ILE A C     1 
ATOM   7236  O  O     . ILE A 1  998  ? -19.542 65.375  88.573  1.00 14.56 ? 996  ILE A O     1 
ATOM   7237  C  CB    . ILE A 1  998  ? -16.548 65.436  88.297  1.00 15.90 ? 996  ILE A CB    1 
ATOM   7238  C  CG1   . ILE A 1  998  ? -15.167 65.735  88.897  1.00 20.51 ? 996  ILE A CG1   1 
ATOM   7239  C  CG2   . ILE A 1  998  ? -16.427 65.055  86.817  1.00 13.73 ? 996  ILE A CG2   1 
ATOM   7240  C  CD1   . ILE A 1  998  ? -14.478 66.918  88.311  1.00 20.67 ? 996  ILE A CD1   1 
ATOM   7241  N  N     . ASN A 1  999  ? -19.397 66.992  86.995  1.00 13.28 ? 997  ASN A N     1 
ATOM   7242  C  CA    . ASN A 1  999  ? -20.683 66.691  86.348  1.00 13.06 ? 997  ASN A CA    1 
ATOM   7243  C  C     . ASN A 1  999  ? -21.856 66.826  87.315  1.00 12.67 ? 997  ASN A C     1 
ATOM   7244  O  O     . ASN A 1  999  ? -22.825 66.068  87.255  1.00 14.26 ? 997  ASN A O     1 
ATOM   7245  C  CB    . ASN A 1  999  ? -20.654 65.311  85.697  1.00 13.87 ? 997  ASN A CB    1 
ATOM   7246  C  CG    . ASN A 1  999  ? -19.702 65.274  84.528  1.00 13.72 ? 997  ASN A CG    1 
ATOM   7247  O  OD1   . ASN A 1  999  ? -19.507 66.292  83.862  1.00 15.15 ? 997  ASN A OD1   1 
ATOM   7248  N  ND2   . ASN A 1  999  ? -19.098 64.119  84.276  1.00 15.05 ? 997  ASN A ND2   1 
ATOM   7249  N  N     . ARG A 1  1000 ? -21.787 67.837  88.176  1.00 13.84 ? 998  ARG A N     1 
ATOM   7250  C  CA    . ARG A 1  1000 ? -22.853 68.129  89.131  1.00 14.58 ? 998  ARG A CA    1 
ATOM   7251  C  C     . ARG A 1  1000 ? -22.715 69.592  89.539  1.00 15.41 ? 998  ARG A C     1 
ATOM   7252  O  O     . ARG A 1  1000 ? -21.801 70.291  89.098  1.00 15.38 ? 998  ARG A O     1 
ATOM   7253  C  CB    . ARG A 1  1000 ? -22.792 67.197  90.344  1.00 14.68 ? 998  ARG A CB    1 
ATOM   7254  C  CG    . ARG A 1  1000 ? -21.395 67.121  90.977  1.00 13.80 ? 998  ARG A CG    1 
ATOM   7255  C  CD    . ARG A 1  1000 ? -21.485 66.731  92.441  1.00 13.99 ? 998  ARG A CD    1 
ATOM   7256  N  NE    . ARG A 1  1000 ? -22.129 67.793  93.200  1.00 14.49 ? 998  ARG A NE    1 
ATOM   7257  C  CZ    . ARG A 1  1000 ? -22.430 67.715  94.486  1.00 15.94 ? 998  ARG A CZ    1 
ATOM   7258  N  NH1   . ARG A 1  1000 ? -22.172 66.622  95.193  1.00 15.22 ? 998  ARG A NH1   1 
ATOM   7259  N  NH2   . ARG A 1  1000 ? -22.991 68.763  95.086  1.00 15.53 ? 998  ARG A NH2   1 
ATOM   7260  N  N     . ASN A 1  1001 ? -23.623 70.055  90.396  1.00 15.18 ? 999  ASN A N     1 
ATOM   7261  C  CA    . ASN A 1  1001 ? -23.478 71.413  90.897  1.00 16.12 ? 999  ASN A CA    1 
ATOM   7262  C  C     . ASN A 1  1001 ? -22.310 71.465  91.888  1.00 16.17 ? 999  ASN A C     1 
ATOM   7263  O  O     . ASN A 1  1001 ? -21.764 70.440  92.284  1.00 15.06 ? 999  ASN A O     1 
ATOM   7264  C  CB    . ASN A 1  1001 ? -24.800 71.901  91.509  1.00 15.87 ? 999  ASN A CB    1 
ATOM   7265  C  CG    . ASN A 1  1001 ? -25.143 71.219  92.828  1.00 19.88 ? 999  ASN A CG    1 
ATOM   7266  O  OD1   . ASN A 1  1001 ? -24.286 70.997  93.688  1.00 18.97 ? 999  ASN A OD1   1 
ATOM   7267  N  ND2   . ASN A 1  1001 ? -26.425 70.929  93.011  1.00 23.71 ? 999  ASN A ND2   1 
ATOM   7268  N  N     A ILE A 1  1002 ? -21.926 72.678  92.281  0.48 15.62 ? 1000 ILE A N     1 
ATOM   7269  N  N     B ILE A 1  1002 ? -21.938 72.675  92.293  0.52 15.63 ? 1000 ILE A N     1 
ATOM   7270  C  CA    A ILE A 1  1002 ? -20.722 72.886  93.084  0.48 15.62 ? 1000 ILE A CA    1 
ATOM   7271  C  CA    B ILE A 1  1002 ? -20.802 72.866  93.189  0.52 15.62 ? 1000 ILE A CA    1 
ATOM   7272  C  C     A ILE A 1  1002 ? -21.048 73.418  94.478  0.48 15.95 ? 1000 ILE A C     1 
ATOM   7273  C  C     B ILE A 1  1002 ? -21.249 73.329  94.577  0.52 15.93 ? 1000 ILE A C     1 
ATOM   7274  O  O     A ILE A 1  1002 ? -20.173 73.979  95.142  0.48 17.71 ? 1000 ILE A O     1 
ATOM   7275  O  O     B ILE A 1  1002 ? -20.448 73.895  95.322  0.52 17.87 ? 1000 ILE A O     1 
ATOM   7276  C  CB    A ILE A 1  1002 ? -19.717 73.810  92.371  0.48 15.47 ? 1000 ILE A CB    1 
ATOM   7277  C  CB    B ILE A 1  1002 ? -19.761 73.830  92.586  0.52 15.45 ? 1000 ILE A CB    1 
ATOM   7278  C  CG1   A ILE A 1  1002 ? -20.216 75.261  92.325  0.48 15.10 ? 1000 ILE A CG1   1 
ATOM   7279  C  CG1   B ILE A 1  1002 ? -20.308 75.259  92.465  0.52 15.09 ? 1000 ILE A CG1   1 
ATOM   7280  C  CG2   A ILE A 1  1002 ? -19.449 73.302  90.977  0.48 14.63 ? 1000 ILE A CG2   1 
ATOM   7281  C  CG2   B ILE A 1  1002 ? -19.300 73.333  91.226  0.52 14.60 ? 1000 ILE A CG2   1 
ATOM   7282  C  CD1   A ILE A 1  1002 ? -19.134 76.263  91.921  0.48 15.47 ? 1000 ILE A CD1   1 
ATOM   7283  C  CD1   B ILE A 1  1002 ? -19.252 76.271  92.018  0.52 15.51 ? 1000 ILE A CD1   1 
ATOM   7284  N  N     A ILE A 1  1003 ? -22.277 73.240  94.953  0.48 16.91 ? 1001 ILE A N     1 
ATOM   7285  N  N     B ILE A 1  1003 ? -22.502 73.075  94.962  0.52 16.82 ? 1001 ILE A N     1 
ATOM   7286  C  CA    A ILE A 1  1003 ? -22.650 73.751  96.267  0.48 17.50 ? 1001 ILE A CA    1 
ATOM   7287  C  CA    B ILE A 1  1003 ? -23.025 73.574  96.230  0.52 17.51 ? 1001 ILE A CA    1 
ATOM   7288  C  C     A ILE A 1  1003 ? -22.750 72.627  97.300  0.48 18.03 ? 1001 ILE A C     1 
ATOM   7289  C  C     B ILE A 1  1003 ? -23.638 72.434  97.037  0.52 16.91 ? 1001 ILE A C     1 
ATOM   7290  O  O     A ILE A 1  1003 ? -23.316 72.821  98.378  0.48 17.94 ? 1001 ILE A O     1 
ATOM   7291  O  O     B ILE A 1  1003 ? -23.751 71.299  96.577  0.52 16.46 ? 1001 ILE A O     1 
ATOM   7292  C  CB    A ILE A 1  1003 ? -23.946 74.577  96.206  0.48 17.26 ? 1001 ILE A CB    1 
ATOM   7293  C  CB    B ILE A 1  1003 ? -24.061 74.700  96.045  0.52 17.42 ? 1001 ILE A CB    1 
ATOM   7294  C  CG1   A ILE A 1  1003 ? -25.092 73.782  95.575  0.48 18.20 ? 1001 ILE A CG1   1 
ATOM   7295  C  CG1   B ILE A 1  1003 ? -25.311 74.185  95.327  0.52 18.54 ? 1001 ILE A CG1   1 
ATOM   7296  C  CG2   A ILE A 1  1003 ? -23.706 75.890  95.455  0.48 16.35 ? 1001 ILE A CG2   1 
ATOM   7297  C  CG2   B ILE A 1  1003 ? -23.445 75.888  95.313  0.52 16.33 ? 1001 ILE A CG2   1 
ATOM   7298  C  CD1   A ILE A 1  1003 ? -26.412 74.550  95.563  0.48 19.07 ? 1001 ILE A CD1   1 
ATOM   7299  C  CD1   B ILE A 1  1003 ? -26.485 75.166  95.385  0.52 18.57 ? 1001 ILE A CD1   1 
ATOM   7300  N  N     A GLY A 1  1004 ? -22.177 71.462  97.003  0.48 18.54 ? 1002 GLY A N     1 
ATOM   7301  N  N     B GLY A 1  1004 ? -24.035 72.764  98.263  0.52 18.03 ? 1002 GLY A N     1 
ATOM   7302  C  CA    A GLY A 1  1004 ? -22.262 70.335  97.914  0.48 17.11 ? 1002 GLY A CA    1 
ATOM   7303  C  CA    B GLY A 1  1004 ? -24.652 71.797  99.154  0.52 17.24 ? 1002 GLY A CA    1 
ATOM   7304  C  C     A GLY A 1  1004 ? -21.340 70.500  99.106  0.48 16.62 ? 1002 GLY A C     1 
ATOM   7305  C  C     B GLY A 1  1004 ? -23.744 70.674  99.614  0.52 17.81 ? 1002 GLY A C     1 
ATOM   7306  O  O     A GLY A 1  1004 ? -20.152 70.799  98.956  0.48 17.35 ? 1002 GLY A O     1 
ATOM   7307  O  O     B GLY A 1  1004 ? -24.204 69.534  99.745  0.52 17.99 ? 1002 GLY A O     1 
ATOM   7308  N  N     A ALA A 1  1005 ? -21.891 70.316  100.299 0.48 16.28 ? 1003 ALA A N     1 
ATOM   7309  N  N     B ALA A 1  1005 ? -22.464 70.966  99.864  0.52 16.31 ? 1003 ALA A N     1 
ATOM   7310  C  CA    A ALA A 1  1005 ? -21.068 70.347  101.506 0.48 17.47 ? 1003 ALA A CA    1 
ATOM   7311  C  CA    B ALA A 1  1005 ? -21.547 69.946  100.358 0.52 16.83 ? 1003 ALA A CA    1 
ATOM   7312  C  C     A ALA A 1  1005 ? -21.545 69.306  102.509 0.48 17.27 ? 1003 ALA A C     1 
ATOM   7313  C  C     B ALA A 1  1005 ? -22.110 69.285  101.609 0.52 17.96 ? 1003 ALA A C     1 
ATOM   7314  O  O     A ALA A 1  1005 ? -21.524 69.554  103.721 0.48 18.17 ? 1003 ALA A O     1 
ATOM   7315  O  O     B ALA A 1  1005 ? -22.700 69.948  102.467 0.52 19.41 ? 1003 ALA A O     1 
ATOM   7316  C  CB    A ALA A 1  1005 ? -21.072 71.746  102.131 0.48 17.68 ? 1003 ALA A CB    1 
ATOM   7317  C  CB    B ALA A 1  1005 ? -20.175 70.553  100.664 0.52 17.84 ? 1003 ALA A CB    1 
ATOM   7318  N  N     A VAL A 1  1006 ? -21.993 68.149  102.016 0.48 16.66 ? 1004 VAL A N     1 
ATOM   7319  N  N     B VAL A 1  1006 ? -21.927 67.965  101.701 0.52 16.69 ? 1004 VAL A N     1 
ATOM   7320  C  CA    A VAL A 1  1006 ? -22.560 67.119  102.878 0.48 17.95 ? 1004 VAL A CA    1 
ATOM   7321  C  CA    B VAL A 1  1006 ? -22.500 67.147  102.765 0.52 17.95 ? 1004 VAL A CA    1 
ATOM   7322  C  C     A VAL A 1  1006 ? -21.517 66.692  103.896 0.48 17.54 ? 1004 VAL A C     1 
ATOM   7323  C  C     B VAL A 1  1006 ? -21.426 66.837  103.796 0.52 17.56 ? 1004 VAL A C     1 
ATOM   7324  O  O     A VAL A 1  1006 ? -20.468 66.141  103.542 0.48 16.82 ? 1004 VAL A O     1 
ATOM   7325  O  O     B VAL A 1  1006 ? -20.288 66.501  103.449 0.52 17.07 ? 1004 VAL A O     1 
ATOM   7326  C  CB    A VAL A 1  1006 ? -23.060 65.937  102.049 0.48 17.71 ? 1004 VAL A CB    1 
ATOM   7327  C  CB    B VAL A 1  1006 ? -23.112 65.853  102.196 0.52 17.68 ? 1004 VAL A CB    1 
ATOM   7328  C  CG1   A VAL A 1  1006 ? -23.575 64.836  102.958 0.48 17.98 ? 1004 VAL A CG1   1 
ATOM   7329  C  CG1   B VAL A 1  1006 ? -23.595 64.942  103.319 0.52 18.12 ? 1004 VAL A CG1   1 
ATOM   7330  C  CG2   A VAL A 1  1006 ? -24.152 66.405  101.086 0.48 17.60 ? 1004 VAL A CG2   1 
ATOM   7331  C  CG2   B VAL A 1  1006 ? -24.253 66.192  101.238 0.52 17.72 ? 1004 VAL A CG2   1 
ATOM   7332  N  N     A VAL A 1  1007 ? -21.813 66.946  105.169 0.48 16.93 ? 1005 VAL A N     1 
ATOM   7333  N  N     B VAL A 1  1007 ? -21.798 66.951  105.072 0.52 16.92 ? 1005 VAL A N     1 
ATOM   7334  C  CA    A VAL A 1  1007 ? -20.882 66.683  106.257 0.48 17.10 ? 1005 VAL A CA    1 
ATOM   7335  C  CA    B VAL A 1  1007 ? -20.875 66.694  106.170 0.52 17.10 ? 1005 VAL A CA    1 
ATOM   7336  C  C     A VAL A 1  1007 ? -20.403 65.242  106.196 0.48 17.06 ? 1005 VAL A C     1 
ATOM   7337  C  C     B VAL A 1  1007 ? -20.396 65.251  106.119 0.52 17.05 ? 1005 VAL A C     1 
ATOM   7338  O  O     A VAL A 1  1007 ? -21.204 64.311  106.065 0.48 17.70 ? 1005 VAL A O     1 
ATOM   7339  O  O     B VAL A 1  1007 ? -21.192 64.322  105.941 0.52 17.67 ? 1005 VAL A O     1 
ATOM   7340  C  CB    A VAL A 1  1007 ? -21.564 67.002  107.597 0.48 16.65 ? 1005 VAL A CB    1 
ATOM   7341  C  CB    B VAL A 1  1007 ? -21.566 67.013  107.504 0.52 16.65 ? 1005 VAL A CB    1 
ATOM   7342  C  CG1   A VAL A 1  1007 ? -20.647 66.647  108.755 0.48 17.80 ? 1005 VAL A CG1   1 
ATOM   7343  C  CG1   B VAL A 1  1007 ? -20.685 66.595  108.675 0.52 17.81 ? 1005 VAL A CG1   1 
ATOM   7344  C  CG2   A VAL A 1  1007 ? -21.935 68.467  107.649 0.48 17.69 ? 1005 VAL A CG2   1 
ATOM   7345  C  CG2   B VAL A 1  1007 ? -21.885 68.490  107.578 0.52 17.68 ? 1005 VAL A CG2   1 
ATOM   7346  N  N     . GLY A 1  1008 ? -19.083 65.055  106.279 1.00 16.37 ? 1006 GLY A N     1 
ATOM   7347  C  CA    . GLY A 1  1008 ? -18.503 63.726  106.256 1.00 16.31 ? 1006 GLY A CA    1 
ATOM   7348  C  C     . GLY A 1  1008 ? -18.536 63.033  104.909 1.00 16.16 ? 1006 GLY A C     1 
ATOM   7349  O  O     . GLY A 1  1008 ? -18.125 61.868  104.816 1.00 18.55 ? 1006 GLY A O     1 
ATOM   7350  N  N     . VAL A 1  1009 ? -19.018 63.705  103.866 1.00 16.71 ? 1007 VAL A N     1 
ATOM   7351  C  CA    . VAL A 1  1009 ? -19.107 63.147  102.524 1.00 15.47 ? 1007 VAL A CA    1 
ATOM   7352  C  C     . VAL A 1  1009 ? -18.370 64.024  101.523 1.00 15.89 ? 1007 VAL A C     1 
ATOM   7353  O  O     . VAL A 1  1009 ? -17.553 63.539  100.731 1.00 15.53 ? 1007 VAL A O     1 
ATOM   7354  C  CB    . VAL A 1  1009 ? -20.576 62.947  102.096 1.00 17.90 ? 1007 VAL A CB    1 
ATOM   7355  C  CG1   . VAL A 1  1009 ? -20.632 62.334  100.702 1.00 18.68 ? 1007 VAL A CG1   1 
ATOM   7356  C  CG2   . VAL A 1  1009 ? -21.291 62.047  103.084 1.00 16.65 ? 1007 VAL A CG2   1 
ATOM   7357  N  N     . GLN A 1  1010 ? -18.643 65.327  101.549 1.00 15.36 ? 1008 GLN A N     1 
ATOM   7358  C  CA    . GLN A 1  1010 ? -17.761 66.346  100.983 1.00 16.40 ? 1008 GLN A CA    1 
ATOM   7359  C  C     . GLN A 1  1010 ? -17.319 67.241  102.137 1.00 15.72 ? 1008 GLN A C     1 
ATOM   7360  O  O     . GLN A 1  1010 ? -17.867 68.335  102.332 1.00 16.80 ? 1008 GLN A O     1 
ATOM   7361  C  CB    . GLN A 1  1010 ? -18.441 67.166  99.889  1.00 17.29 ? 1008 GLN A CB    1 
ATOM   7362  C  CG    . GLN A 1  1010 ? -18.973 66.335  98.717  1.00 16.17 ? 1008 GLN A CG    1 
ATOM   7363  C  CD    . GLN A 1  1010 ? -20.462 66.081  98.827  1.00 18.51 ? 1008 GLN A CD    1 
ATOM   7364  O  OE1   . GLN A 1  1010 ? -21.199 66.898  99.384  1.00 17.18 ? 1008 GLN A OE1   1 
ATOM   7365  N  NE2   . GLN A 1  1010 ? -20.914 64.954  98.291  1.00 16.05 ? 1008 GLN A NE2   1 
ATOM   7366  N  N     . PRO A 1  1011 ? -16.359 66.794  102.948 1.00 16.67 ? 1009 PRO A N     1 
ATOM   7367  C  CA    . PRO A 1  1011 ? -15.738 67.712  103.908 1.00 16.44 ? 1009 PRO A CA    1 
ATOM   7368  C  C     . PRO A 1  1011 ? -15.404 69.006  103.194 1.00 14.96 ? 1009 PRO A C     1 
ATOM   7369  O  O     . PRO A 1  1011 ? -14.863 68.998  102.091 1.00 13.84 ? 1009 PRO A O     1 
ATOM   7370  C  CB    . PRO A 1  1011 ? -14.480 66.959  104.353 1.00 14.60 ? 1009 PRO A CB    1 
ATOM   7371  C  CG    . PRO A 1  1011 ? -14.881 65.520  104.260 1.00 15.55 ? 1009 PRO A CG    1 
ATOM   7372  C  CD    . PRO A 1  1011 ? -15.750 65.456  102.997 1.00 16.19 ? 1009 PRO A CD    1 
ATOM   7373  N  N     . PHE A 1  1012 ? -15.777 70.126  103.794 1.00 17.20 ? 1010 PHE A N     1 
ATOM   7374  C  CA    . PHE A 1  1012 ? -15.871 71.376  103.063 1.00 16.16 ? 1010 PHE A CA    1 
ATOM   7375  C  C     . PHE A 1  1012 ? -14.847 72.376  103.570 1.00 16.55 ? 1010 PHE A C     1 
ATOM   7376  O  O     . PHE A 1  1012 ? -14.726 72.591  104.784 1.00 15.77 ? 1010 PHE A O     1 
ATOM   7377  C  CB    . PHE A 1  1012 ? -17.277 71.978  103.185 1.00 14.72 ? 1010 PHE A CB    1 
ATOM   7378  C  CG    . PHE A 1  1012 ? -17.460 73.193  102.327 1.00 15.93 ? 1010 PHE A CG    1 
ATOM   7379  C  CD1   . PHE A 1  1012 ? -17.698 73.058  100.964 1.00 18.44 ? 1010 PHE A CD1   1 
ATOM   7380  C  CD2   . PHE A 1  1012 ? -17.348 74.469  102.864 1.00 18.39 ? 1010 PHE A CD2   1 
ATOM   7381  C  CE1   . PHE A 1  1012 ? -17.827 74.176  100.147 1.00 17.39 ? 1010 PHE A CE1   1 
ATOM   7382  C  CE2   . PHE A 1  1012 ? -17.493 75.591  102.056 1.00 18.85 ? 1010 PHE A CE2   1 
ATOM   7383  C  CZ    . PHE A 1  1012 ? -17.731 75.449  100.699 1.00 17.36 ? 1010 PHE A CZ    1 
ATOM   7384  N  N     . GLY A 1  1013 ? -14.132 72.994  102.648 1.00 15.64 ? 1011 GLY A N     1 
ATOM   7385  C  CA    . GLY A 1  1013 ? -13.212 74.052  103.012 1.00 15.64 ? 1011 GLY A CA    1 
ATOM   7386  C  C     . GLY A 1  1013 ? -12.109 74.129  101.979 1.00 16.39 ? 1011 GLY A C     1 
ATOM   7387  O  O     . GLY A 1  1013 ? -11.685 73.134  101.399 1.00 17.16 ? 1011 GLY A O     1 
ATOM   7388  N  N     . GLY A 1  1014 ? -11.622 75.345  101.769 1.00 16.58 ? 1012 GLY A N     1 
ATOM   7389  C  CA    . GLY A 1  1014 ? -10.666 75.622  100.722 1.00 18.73 ? 1012 GLY A CA    1 
ATOM   7390  C  C     . GLY A 1  1014 ? -9.322  76.121  101.208 1.00 18.85 ? 1012 GLY A C     1 
ATOM   7391  O  O     . GLY A 1  1014 ? -8.989  76.051  102.398 1.00 18.43 ? 1012 GLY A O     1 
ATOM   7392  N  N     . ARG A 1  1015 ? -8.551  76.650  100.269 1.00 16.18 ? 1013 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1  1015 ? -7.156  77.012  100.462 1.00 16.69 ? 1013 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1  1015 ? -6.939  78.435  99.966  1.00 18.01 ? 1013 ARG A C     1 
ATOM   7395  O  O     . ARG A 1  1015 ? -7.837  79.068  99.408  1.00 16.91 ? 1013 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1  1015 ? -6.246  76.047  99.702  1.00 17.76 ? 1013 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1  1015 ? -6.467  76.109  98.205  1.00 19.00 ? 1013 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1  1015 ? -5.399  75.368  97.427  1.00 20.15 ? 1013 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1  1015 ? -4.073  75.529  98.009  1.00 23.75 ? 1013 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1  1015 ? -3.336  76.625  97.901  1.00 25.53 ? 1013 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1  1015 ? -3.753  77.674  97.207  1.00 25.11 ? 1013 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1  1015 ? -2.152  76.674  98.513  1.00 21.15 ? 1013 ARG A NH2   1 
ATOM   7403  N  N     . GLY A 1  1016 ? -5.720  78.932  100.147 1.00 17.52 ? 1014 GLY A N     1 
ATOM   7404  C  CA    . GLY A 1  1016 ? -5.424  80.267  99.662  1.00 16.34 ? 1014 GLY A CA    1 
ATOM   7405  C  C     . GLY A 1  1016 ? -6.274  81.286  100.386 1.00 17.59 ? 1014 GLY A C     1 
ATOM   7406  O  O     . GLY A 1  1016 ? -6.452  81.229  101.610 1.00 19.55 ? 1014 GLY A O     1 
ATOM   7407  N  N     . LEU A 1  1017 ? -6.835  82.225  99.618  1.00 17.82 ? 1015 LEU A N     1 
ATOM   7408  C  CA    . LEU A 1  1017 ? -7.715  83.237  100.191 1.00 17.79 ? 1015 LEU A CA    1 
ATOM   7409  C  C     . LEU A 1  1017 ? -9.023  82.648  100.698 1.00 17.76 ? 1015 LEU A C     1 
ATOM   7410  O  O     . LEU A 1  1017 ? -9.827  83.392  101.273 1.00 19.62 ? 1015 LEU A O     1 
ATOM   7411  C  CB    . LEU A 1  1017 ? -8.014  84.330  99.158  1.00 19.59 ? 1015 LEU A CB    1 
ATOM   7412  C  CG    . LEU A 1  1017 ? -6.821  85.118  98.612  1.00 21.20 ? 1015 LEU A CG    1 
ATOM   7413  C  CD1   . LEU A 1  1017 ? -7.284  86.030  97.480  1.00 19.60 ? 1015 LEU A CD1   1 
ATOM   7414  C  CD2   . LEU A 1  1017 ? -6.126  85.947  99.713  1.00 20.65 ? 1015 LEU A CD2   1 
ATOM   7415  N  N     . SER A 1  1018 ? -9.255  81.345  100.511 1.00 16.32 ? 1016 SER A N     1 
ATOM   7416  C  CA    . SER A 1  1018 ? -10.520 80.730  100.903 1.00 17.39 ? 1016 SER A CA    1 
ATOM   7417  C  C     . SER A 1  1018 ? -10.454 80.009  102.239 1.00 16.22 ? 1016 SER A C     1 
ATOM   7418  O  O     . SER A 1  1018 ? -11.495 79.587  102.745 1.00 17.54 ? 1016 SER A O     1 
ATOM   7419  C  CB    . SER A 1  1018 ? -10.996 79.736  99.832  1.00 16.07 ? 1016 SER A CB    1 
ATOM   7420  O  OG    . SER A 1  1018 ? -11.197 80.416  98.612  1.00 16.64 ? 1016 SER A OG    1 
ATOM   7421  N  N     . GLY A 1  1019 ? -9.275  79.849  102.832 1.00 17.66 ? 1017 GLY A N     1 
ATOM   7422  C  CA    . GLY A 1  1019 ? -9.273  79.139  104.088 1.00 17.40 ? 1017 GLY A CA    1 
ATOM   7423  C  C     . GLY A 1  1019 ? -7.913  78.758  104.611 1.00 18.12 ? 1017 GLY A C     1 
ATOM   7424  O  O     . GLY A 1  1019 ? -6.939  78.659  103.859 1.00 18.12 ? 1017 GLY A O     1 
ATOM   7425  N  N     . THR A 1  1020 ? -7.847  78.567  105.923 1.00 18.28 ? 1018 THR A N     1 
ATOM   7426  C  CA    . THR A 1  1020 ? -6.694  77.966  106.568 1.00 18.56 ? 1018 THR A CA    1 
ATOM   7427  C  C     . THR A 1  1020 ? -6.843  76.468  106.695 1.00 18.63 ? 1018 THR A C     1 
ATOM   7428  O  O     . THR A 1  1020 ? -5.846  75.759  106.864 1.00 19.46 ? 1018 THR A O     1 
ATOM   7429  C  CB    . THR A 1  1020 ? -6.523  78.519  107.980 1.00 17.31 ? 1018 THR A CB    1 
ATOM   7430  O  OG1   . THR A 1  1020 ? -7.724  78.267  108.729 1.00 18.39 ? 1018 THR A OG1   1 
ATOM   7431  C  CG2   . THR A 1  1020 ? -6.246  80.008  107.942 1.00 21.00 ? 1018 THR A CG2   1 
ATOM   7432  N  N     . GLY A 1  1021 ? -8.073  75.984  106.681 1.00 18.46 ? 1019 GLY A N     1 
ATOM   7433  C  CA    . GLY A 1  1021 ? -8.336  74.649  107.132 1.00 17.88 ? 1019 GLY A CA    1 
ATOM   7434  C  C     . GLY A 1  1021 ? -8.114  74.549  108.633 1.00 18.24 ? 1019 GLY A C     1 
ATOM   7435  O  O     . GLY A 1  1021 ? -7.779  75.528  109.312 1.00 18.21 ? 1019 GLY A O     1 
ATOM   7436  N  N     . PRO A 1  1022 ? -8.331  73.351  109.183 1.00 17.81 ? 1020 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1  1022 ? -8.785  72.137  108.494 1.00 18.31 ? 1020 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1  1022 ? -10.254 72.243  108.096 1.00 17.80 ? 1020 PRO A C     1 
ATOM   7439  O  O     . PRO A 1  1022 ? -10.957 73.138  108.559 1.00 18.76 ? 1020 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1  1022 ? -8.563  71.048  109.548 1.00 16.38 ? 1020 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1  1022 ? -8.798  71.779  110.857 1.00 19.29 ? 1020 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1  1022 ? -8.168  73.129  110.633 1.00 18.24 ? 1020 PRO A CD    1 
ATOM   7443  N  N     . LYS A 1  1023 ? -10.720 71.343  107.239 1.00 16.28 ? 1021 LYS A N     1 
ATOM   7444  C  CA    . LYS A 1  1023 ? -12.091 71.395  106.736 1.00 16.11 ? 1021 LYS A CA    1 
ATOM   7445  C  C     . LYS A 1  1023 ? -13.119 71.118  107.827 1.00 17.07 ? 1021 LYS A C     1 
ATOM   7446  O  O     . LYS A 1  1023 ? -13.029 70.110  108.534 1.00 16.36 ? 1021 LYS A O     1 
ATOM   7447  C  CB    . LYS A 1  1023 ? -12.285 70.357  105.637 1.00 14.97 ? 1021 LYS A CB    1 
ATOM   7448  C  CG    . LYS A 1  1023 ? -11.619 70.656  104.308 1.00 15.75 ? 1021 LYS A CG    1 
ATOM   7449  C  CD    . LYS A 1  1023 ? -11.772 69.441  103.432 1.00 14.84 ? 1021 LYS A CD    1 
ATOM   7450  C  CE    . LYS A 1  1023 ? -11.352 69.711  101.995 1.00 15.08 ? 1021 LYS A CE    1 
ATOM   7451  N  NZ    . LYS A 1  1023 ? -12.423 70.442  101.247 1.00 13.52 ? 1021 LYS A NZ    1 
ATOM   7452  N  N     . ALA A 1  1024 ? -14.147 71.973  107.902 1.00 18.26 ? 1022 ALA A N     1 
ATOM   7453  C  CA    . ALA A 1  1024 ? -15.366 71.622  108.621 1.00 18.58 ? 1022 ALA A CA    1 
ATOM   7454  C  C     . ALA A 1  1024 ? -16.005 70.380  108.014 1.00 18.07 ? 1022 ALA A C     1 
ATOM   7455  O  O     . ALA A 1  1024 ? -15.966 70.171  106.796 1.00 18.74 ? 1022 ALA A O     1 
ATOM   7456  C  CB    . ALA A 1  1024 ? -16.355 72.792  108.589 1.00 17.45 ? 1022 ALA A CB    1 
ATOM   7457  N  N     . GLY A 1  1025 ? -16.605 69.556  108.869 1.00 16.01 ? 1023 GLY A N     1 
ATOM   7458  C  CA    . GLY A 1  1025 ? -17.206 68.324  108.397 1.00 16.66 ? 1023 GLY A CA    1 
ATOM   7459  C  C     . GLY A 1  1025 ? -16.209 67.313  107.897 1.00 18.30 ? 1023 GLY A C     1 
ATOM   7460  O  O     . GLY A 1  1025 ? -16.573 66.412  107.134 1.00 16.47 ? 1023 GLY A O     1 
ATOM   7461  N  N     . GLY A 1  1026 ? -14.952 67.440  108.313 1.00 17.22 ? 1024 GLY A N     1 
ATOM   7462  C  CA    . GLY A 1  1026 ? -13.921 66.496  107.955 1.00 17.30 ? 1024 GLY A CA    1 
ATOM   7463  C  C     . GLY A 1  1026 ? -13.197 66.019  109.196 1.00 17.12 ? 1024 GLY A C     1 
ATOM   7464  O  O     . GLY A 1  1026 ? -13.415 66.520  110.304 1.00 16.47 ? 1024 GLY A O     1 
ATOM   7465  N  N     . PRO A 1  1027 ? -12.300 65.043  109.023 1.00 15.17 ? 1025 PRO A N     1 
ATOM   7466  C  CA    . PRO A 1  1027 ? -11.756 64.319  110.176 1.00 17.47 ? 1025 PRO A CA    1 
ATOM   7467  C  C     . PRO A 1  1027 ? -10.581 65.001  110.858 1.00 15.40 ? 1025 PRO A C     1 
ATOM   7468  O  O     . PRO A 1  1027 ? -10.166 64.544  111.933 1.00 16.98 ? 1025 PRO A O     1 
ATOM   7469  C  CB    . PRO A 1  1027 ? -11.329 62.983  109.565 1.00 17.04 ? 1025 PRO A CB    1 
ATOM   7470  C  CG    . PRO A 1  1027 ? -10.973 63.337  108.152 1.00 19.12 ? 1025 PRO A CG    1 
ATOM   7471  C  CD    . PRO A 1  1027 ? -12.003 64.368  107.747 1.00 16.69 ? 1025 PRO A CD    1 
ATOM   7472  N  N     . LEU A 1  1028 ? -10.039 66.065  110.280 1.00 16.71 ? 1026 LEU A N     1 
ATOM   7473  C  CA    . LEU A 1  1028 ? -8.951  66.804  110.904 1.00 15.67 ? 1026 LEU A CA    1 
ATOM   7474  C  C     . LEU A 1  1028 ? -9.443  67.947  111.769 1.00 16.94 ? 1026 LEU A C     1 
ATOM   7475  O  O     . LEU A 1  1028 ? -8.635  68.565  112.466 1.00 18.34 ? 1026 LEU A O     1 
ATOM   7476  C  CB    . LEU A 1  1028 ? -8.000  67.343  109.836 1.00 15.66 ? 1026 LEU A CB    1 
ATOM   7477  C  CG    . LEU A 1  1028 ? -7.102  66.271  109.212 1.00 17.35 ? 1026 LEU A CG    1 
ATOM   7478  C  CD1   . LEU A 1  1028 ? -6.435  66.882  107.992 1.00 19.10 ? 1026 LEU A CD1   1 
ATOM   7479  C  CD2   . LEU A 1  1028 ? -6.068  65.828  110.253 1.00 21.13 ? 1026 LEU A CD2   1 
ATOM   7480  N  N     . TYR A 1  1029 ? -10.754 68.200  111.777 1.00 16.64 ? 1027 TYR A N     1 
ATOM   7481  C  CA    . TYR A 1  1029 ? -11.293 69.417  112.381 1.00 17.74 ? 1027 TYR A CA    1 
ATOM   7482  C  C     . TYR A 1  1029 ? -11.126 69.422  113.894 1.00 16.68 ? 1027 TYR A C     1 
ATOM   7483  O  O     . TYR A 1  1029 ? -10.594 70.382  114.470 1.00 17.44 ? 1027 TYR A O     1 
ATOM   7484  C  CB    . TYR A 1  1029 ? -12.761 69.529  111.998 1.00 16.53 ? 1027 TYR A CB    1 
ATOM   7485  C  CG    . TYR A 1  1029 ? -13.401 70.879  112.098 1.00 16.47 ? 1027 TYR A CG    1 
ATOM   7486  C  CD1   . TYR A 1  1029 ? -13.035 71.910  111.238 1.00 18.21 ? 1027 TYR A CD1   1 
ATOM   7487  C  CD2   . TYR A 1  1029 ? -14.464 71.092  112.978 1.00 17.64 ? 1027 TYR A CD2   1 
ATOM   7488  C  CE1   . TYR A 1  1029 ? -13.687 73.149  111.286 1.00 17.64 ? 1027 TYR A CE1   1 
ATOM   7489  C  CE2   . TYR A 1  1029 ? -15.104 72.317  113.035 1.00 18.81 ? 1027 TYR A CE2   1 
ATOM   7490  C  CZ    . TYR A 1  1029 ? -14.715 73.334  112.186 1.00 18.97 ? 1027 TYR A CZ    1 
ATOM   7491  O  OH    . TYR A 1  1029 ? -15.383 74.536  112.238 1.00 19.85 ? 1027 TYR A OH    1 
ATOM   7492  N  N     . LEU A 1  1030 ? -11.605 68.373  114.564 1.00 17.05 ? 1028 LEU A N     1 
ATOM   7493  C  CA    . LEU A 1  1030 ? -11.568 68.375  116.023 1.00 18.16 ? 1028 LEU A CA    1 
ATOM   7494  C  C     . LEU A 1  1030 ? -10.143 68.470  116.541 1.00 19.45 ? 1028 LEU A C     1 
ATOM   7495  O  O     . LEU A 1  1030 ? -9.906  69.083  117.584 1.00 18.95 ? 1028 LEU A O     1 
ATOM   7496  C  CB    . LEU A 1  1030 ? -12.230 67.124  116.578 1.00 18.10 ? 1028 LEU A CB    1 
ATOM   7497  C  CG    . LEU A 1  1030 ? -13.725 66.961  116.341 1.00 17.97 ? 1028 LEU A CG    1 
ATOM   7498  C  CD1   . LEU A 1  1030 ? -14.197 65.732  117.098 1.00 20.62 ? 1028 LEU A CD1   1 
ATOM   7499  C  CD2   . LEU A 1  1030 ? -14.480 68.192  116.832 1.00 20.66 ? 1028 LEU A CD2   1 
ATOM   7500  N  N     . GLY A 1  1031 ? -9.186  67.897  115.813 1.00 18.49 ? 1029 GLY A N     1 
ATOM   7501  C  CA    . GLY A 1  1031 ? -7.810  67.885  116.275 1.00 20.74 ? 1029 GLY A CA    1 
ATOM   7502  C  C     . GLY A 1  1031 ? -7.186  69.256  116.392 1.00 20.26 ? 1029 GLY A C     1 
ATOM   7503  O  O     . GLY A 1  1031 ? -6.188  69.412  117.102 1.00 19.97 ? 1029 GLY A O     1 
ATOM   7504  N  N     . ARG A 1  1032 ? -7.749  70.256  115.715 1.00 18.65 ? 1030 ARG A N     1 
ATOM   7505  C  CA    . ARG A 1  1032 ? -7.264  71.624  115.810 1.00 18.09 ? 1030 ARG A CA    1 
ATOM   7506  C  C     . ARG A 1  1032 ? -7.733  72.317  117.081 1.00 19.58 ? 1030 ARG A C     1 
ATOM   7507  O  O     . ARG A 1  1032 ? -7.171  73.355  117.458 1.00 20.37 ? 1030 ARG A O     1 
ATOM   7508  C  CB    . ARG A 1  1032 ? -7.722  72.411  114.573 1.00 18.61 ? 1030 ARG A CB    1 
ATOM   7509  C  CG    . ARG A 1  1032 ? -7.097  73.789  114.409 1.00 17.20 ? 1030 ARG A CG    1 
ATOM   7510  C  CD    . ARG A 1  1032 ? -5.627  73.684  113.995 1.00 17.91 ? 1030 ARG A CD    1 
ATOM   7511  N  NE    . ARG A 1  1032 ? -5.125  74.989  113.580 1.00 18.29 ? 1030 ARG A NE    1 
ATOM   7512  C  CZ    . ARG A 1  1032 ? -4.094  75.615  114.135 1.00 21.04 ? 1030 ARG A CZ    1 
ATOM   7513  N  NH1   . ARG A 1  1032 ? -3.428  75.089  115.152 1.00 22.38 ? 1030 ARG A NH1   1 
ATOM   7514  N  NH2   . ARG A 1  1032 ? -3.725  76.802  113.657 1.00 23.53 ? 1030 ARG A NH2   1 
ATOM   7515  N  N     . LEU A 1  1033 ? -8.732  71.754  117.762 1.00 18.14 ? 1031 LEU A N     1 
ATOM   7516  C  CA    . LEU A 1  1033 ? -9.365  72.387  118.909 1.00 20.37 ? 1031 LEU A CA    1 
ATOM   7517  C  C     . LEU A 1  1033 ? -8.887  71.800  120.227 1.00 21.60 ? 1031 LEU A C     1 
ATOM   7518  O  O     . LEU A 1  1033 ? -9.513  72.026  121.269 1.00 21.42 ? 1031 LEU A O     1 
ATOM   7519  C  CB    . LEU A 1  1033 ? -10.882 72.264  118.784 1.00 21.22 ? 1031 LEU A CB    1 
ATOM   7520  C  CG    . LEU A 1  1033 ? -11.403 72.660  117.399 1.00 20.53 ? 1031 LEU A CG    1 
ATOM   7521  C  CD1   . LEU A 1  1033 ? -12.914 72.488  117.305 1.00 19.79 ? 1031 LEU A CD1   1 
ATOM   7522  C  CD2   . LEU A 1  1033 ? -11.010 74.094  117.075 1.00 20.54 ? 1031 LEU A CD2   1 
ATOM   7523  N  N     . VAL A 1  1034 ? -7.781  71.055  120.196 1.00 21.71 ? 1032 VAL A N     1 
ATOM   7524  C  CA    . VAL A 1  1034 ? -7.170  70.482  121.382 1.00 22.62 ? 1032 VAL A CA    1 
ATOM   7525  C  C     . VAL A 1  1034 ? -5.680  70.757  121.292 1.00 22.17 ? 1032 VAL A C     1 
ATOM   7526  O  O     . VAL A 1  1034 ? -5.148  71.045  120.221 1.00 22.48 ? 1032 VAL A O     1 
ATOM   7527  C  CB    . VAL A 1  1034 ? -7.442  68.970  121.518 1.00 21.34 ? 1032 VAL A CB    1 
ATOM   7528  C  CG1   . VAL A 1  1034 ? -8.927  68.721  121.787 1.00 22.85 ? 1032 VAL A CG1   1 
ATOM   7529  C  CG2   . VAL A 1  1034 ? -7.005  68.234  120.246 1.00 21.68 ? 1032 VAL A CG2   1 
ATOM   7530  N  N     . THR A 1  1035 ? -5.003  70.671  122.440 1.00 23.53 ? 1033 THR A N     1 
ATOM   7531  C  CA    . THR A 1  1035 ? -3.587  71.020  122.465 1.00 23.27 ? 1033 THR A CA    1 
ATOM   7532  C  C     . THR A 1  1035 ? -2.722  69.958  121.794 1.00 25.36 ? 1033 THR A C     1 
ATOM   7533  O  O     . THR A 1  1035 ? -1.702  70.292  121.181 1.00 30.12 ? 1033 THR A O     1 
ATOM   7534  C  CB    . THR A 1  1035 ? -3.135  71.256  123.905 1.00 27.35 ? 1033 THR A CB    1 
ATOM   7535  O  OG1   . THR A 1  1035 ? -3.504  70.135  124.711 1.00 34.28 ? 1033 THR A OG1   1 
ATOM   7536  C  CG2   . THR A 1  1035 ? -3.801  72.493  124.471 1.00 25.59 ? 1033 THR A CG2   1 
ATOM   7537  N  N     . THR A 1  1036 ? -3.109  68.686  121.891 1.00 23.62 ? 1034 THR A N     1 
ATOM   7538  C  CA    . THR A 1  1036 ? -2.402  67.577  121.254 1.00 22.86 ? 1034 THR A CA    1 
ATOM   7539  C  C     . THR A 1  1036 ? -3.389  66.890  120.324 1.00 23.97 ? 1034 THR A C     1 
ATOM   7540  O  O     . THR A 1  1036 ? -4.381  66.317  120.785 1.00 25.25 ? 1034 THR A O     1 
ATOM   7541  C  CB    . THR A 1  1036 ? -1.854  66.598  122.295 1.00 29.18 ? 1034 THR A CB    1 
ATOM   7542  O  OG1   . THR A 1  1036 ? -0.965  67.293  123.175 1.00 29.72 ? 1034 THR A OG1   1 
ATOM   7543  C  CG2   . THR A 1  1036 ? -1.091  65.469  121.615 1.00 29.63 ? 1034 THR A CG2   1 
ATOM   7544  N  N     . ALA A 1  1037 ? -3.128  66.955  119.024 1.00 23.10 ? 1035 ALA A N     1 
ATOM   7545  C  CA    . ALA A 1  1037 ? -4.088  66.435  118.066 1.00 23.67 ? 1035 ALA A CA    1 
ATOM   7546  C  C     . ALA A 1  1037 ? -4.121  64.911  118.136 1.00 24.67 ? 1035 ALA A C     1 
ATOM   7547  O  O     . ALA A 1  1037 ? -3.068  64.266  118.209 1.00 22.57 ? 1035 ALA A O     1 
ATOM   7548  C  CB    . ALA A 1  1037 ? -3.740  66.893  116.654 1.00 22.60 ? 1035 ALA A CB    1 
ATOM   7549  N  N     . PRO A 1  1038 ? -5.303  64.308  118.130 1.00 21.46 ? 1036 PRO A N     1 
ATOM   7550  C  CA    . PRO A 1  1038 ? -5.391  62.850  118.030 1.00 21.13 ? 1036 PRO A CA    1 
ATOM   7551  C  C     . PRO A 1  1038 ? -5.122  62.402  116.599 1.00 21.48 ? 1036 PRO A C     1 
ATOM   7552  O  O     . PRO A 1  1038 ? -5.041  63.207  115.672 1.00 21.52 ? 1036 PRO A O     1 
ATOM   7553  C  CB    . PRO A 1  1038 ? -6.838  62.565  118.431 1.00 22.51 ? 1036 PRO A CB    1 
ATOM   7554  C  CG    . PRO A 1  1038 ? -7.573  63.762  117.892 1.00 22.19 ? 1036 PRO A CG    1 
ATOM   7555  C  CD    . PRO A 1  1038 ? -6.641  64.936  118.155 1.00 20.19 ? 1036 PRO A CD    1 
ATOM   7556  N  N     . VAL A 1  1039 ? -5.030  61.087  116.425 1.00 19.68 ? 1037 VAL A N     1 
ATOM   7557  C  CA    . VAL A 1  1039 ? -4.930  60.477  115.103 1.00 18.44 ? 1037 VAL A CA    1 
ATOM   7558  C  C     . VAL A 1  1039 ? -6.350  60.272  114.575 1.00 18.77 ? 1037 VAL A C     1 
ATOM   7559  O  O     . VAL A 1  1039 ? -7.098  59.467  115.153 1.00 20.32 ? 1037 VAL A O     1 
ATOM   7560  C  CB    . VAL A 1  1039 ? -4.160  59.152  115.150 1.00 19.97 ? 1037 VAL A CB    1 
ATOM   7561  C  CG1   . VAL A 1  1039 ? -4.161  58.500  113.778 1.00 21.51 ? 1037 VAL A CG1   1 
ATOM   7562  C  CG2   . VAL A 1  1039 ? -2.724  59.398  115.616 1.00 22.17 ? 1037 VAL A CG2   1 
ATOM   7563  N  N     . PRO A 1  1040 ? -6.757  60.958  113.510 1.00 18.22 ? 1038 PRO A N     1 
ATOM   7564  C  CA    . PRO A 1  1040 ? -8.126  60.810  113.023 1.00 21.26 ? 1038 PRO A CA    1 
ATOM   7565  C  C     . PRO A 1  1040 ? -8.371  59.410  112.491 1.00 20.73 ? 1038 PRO A C     1 
ATOM   7566  O  O     . PRO A 1  1040 ? -7.424  58.687  112.134 1.00 18.37 ? 1038 PRO A O     1 
ATOM   7567  C  CB    . PRO A 1  1040 ? -8.229  61.860  111.902 1.00 18.97 ? 1038 PRO A CB    1 
ATOM   7568  C  CG    . PRO A 1  1040 ? -7.111  62.822  112.147 1.00 20.61 ? 1038 PRO A CG    1 
ATOM   7569  C  CD    . PRO A 1  1040 ? -6.013  61.993  112.779 1.00 20.73 ? 1038 PRO A CD    1 
ATOM   7570  N  N     . PRO A 1  1041 ? -9.629  58.983  112.430 1.00 18.59 ? 1039 PRO A N     1 
ATOM   7571  C  CA    . PRO A 1  1041 ? -9.926  57.712  111.774 1.00 15.34 ? 1039 PRO A CA    1 
ATOM   7572  C  C     . PRO A 1  1041 ? -9.412  57.722  110.341 1.00 18.94 ? 1039 PRO A C     1 
ATOM   7573  O  O     . PRO A 1  1041 ? -9.451  58.745  109.656 1.00 18.96 ? 1039 PRO A O     1 
ATOM   7574  C  CB    . PRO A 1  1041 ? -11.460 57.626  111.830 1.00 21.83 ? 1039 PRO A CB    1 
ATOM   7575  C  CG    . PRO A 1  1041 ? -11.839 58.536  112.961 1.00 21.89 ? 1039 PRO A CG    1 
ATOM   7576  C  CD    . PRO A 1  1041 ? -10.854 59.650  112.914 1.00 20.55 ? 1039 PRO A CD    1 
ATOM   7577  N  N     . GLN A 1  1042 ? -8.889  56.574  109.916 1.00 16.70 ? 1040 GLN A N     1 
ATOM   7578  C  CA    . GLN A 1  1042 ? -8.375  56.303  108.575 1.00 17.81 ? 1040 GLN A CA    1 
ATOM   7579  C  C     . GLN A 1  1042 ? -7.213  57.197  108.175 1.00 17.66 ? 1040 GLN A C     1 
ATOM   7580  O  O     . GLN A 1  1042 ? -6.823  57.201  107.003 1.00 17.04 ? 1040 GLN A O     1 
ATOM   7581  C  CB    . GLN A 1  1042 ? -9.488  56.413  107.524 1.00 20.87 ? 1040 GLN A CB    1 
ATOM   7582  C  CG    . GLN A 1  1042 ? -10.696 55.575  107.881 1.00 26.20 ? 1040 GLN A CG    1 
ATOM   7583  C  CD    . GLN A 1  1042 ? -11.711 55.530  106.762 1.00 29.78 ? 1040 GLN A CD    1 
ATOM   7584  O  OE1   . GLN A 1  1042 ? -12.670 56.290  106.752 1.00 32.04 ? 1040 GLN A OE1   1 
ATOM   7585  N  NE2   . GLN A 1  1042 ? -11.493 54.641  105.808 1.00 32.01 ? 1040 GLN A NE2   1 
ATOM   7586  N  N     . HIS A 1  1043 ? -6.631  57.947  109.112 1.00 15.46 ? 1041 HIS A N     1 
ATOM   7587  C  CA    . HIS A 1  1043 ? -5.625  58.959  108.785 1.00 18.22 ? 1041 HIS A CA    1 
ATOM   7588  C  C     . HIS A 1  1043 ? -4.236  58.326  108.818 1.00 17.79 ? 1041 HIS A C     1 
ATOM   7589  O  O     . HIS A 1  1043 ? -3.611  58.211  109.873 1.00 17.56 ? 1041 HIS A O     1 
ATOM   7590  C  CB    . HIS A 1  1043 ? -5.725  60.122  109.765 1.00 16.73 ? 1041 HIS A CB    1 
ATOM   7591  C  CG    . HIS A 1  1043 ? -4.761  61.232  109.495 1.00 17.63 ? 1041 HIS A CG    1 
ATOM   7592  N  ND1   . HIS A 1  1043 ? -5.047  62.271  108.636 1.00 16.98 ? 1041 HIS A ND1   1 
ATOM   7593  C  CD2   . HIS A 1  1043 ? -3.520  61.479  109.985 1.00 17.11 ? 1041 HIS A CD2   1 
ATOM   7594  C  CE1   . HIS A 1  1043 ? -4.026  63.107  108.604 1.00 18.57 ? 1041 HIS A CE1   1 
ATOM   7595  N  NE2   . HIS A 1  1043 ? -3.087  62.651  109.416 1.00 17.43 ? 1041 HIS A NE2   1 
ATOM   7596  N  N     . SER A 1  1044 ? -3.756  57.901  107.644 1.00 15.52 ? 1042 SER A N     1 
ATOM   7597  C  CA    . SER A 1  1044 ? -2.415  57.338  107.470 1.00 15.78 ? 1042 SER A CA    1 
ATOM   7598  C  C     . SER A 1  1044 ? -2.136  57.259  105.976 1.00 15.54 ? 1042 SER A C     1 
ATOM   7599  O  O     . SER A 1  1044 ? -3.040  57.383  105.152 1.00 17.92 ? 1042 SER A O     1 
ATOM   7600  C  CB    . SER A 1  1044 ? -2.278  55.946  108.089 1.00 17.84 ? 1042 SER A CB    1 
ATOM   7601  O  OG    . SER A 1  1044 ? -3.087  55.015  107.389 1.00 17.60 ? 1042 SER A OG    1 
ATOM   7602  N  N     . SER A 1  1045 ? -0.869  57.030  105.636 1.00 15.07 ? 1043 SER A N     1 
ATOM   7603  C  CA    . SER A 1  1045 ? -0.495  56.824  104.245 1.00 16.53 ? 1043 SER A CA    1 
ATOM   7604  C  C     . SER A 1  1045 ? 0.717   55.911  104.211 1.00 14.77 ? 1043 SER A C     1 
ATOM   7605  O  O     . SER A 1  1045 ? 1.651   56.091  104.993 1.00 16.65 ? 1043 SER A O     1 
ATOM   7606  C  CB    . SER A 1  1045 ? -0.161  58.145  103.549 1.00 17.53 ? 1043 SER A CB    1 
ATOM   7607  O  OG    . SER A 1  1045 ? 0.299   57.920  102.221 1.00 17.42 ? 1043 SER A OG    1 
ATOM   7608  N  N     . VAL A 1  1046 ? 0.704   54.937  103.298 1.00 16.97 ? 1044 VAL A N     1 
ATOM   7609  C  CA    . VAL A 1  1046 ? 1.882   54.089  103.137 1.00 19.18 ? 1044 VAL A CA    1 
ATOM   7610  C  C     . VAL A 1  1046 ? 2.931   54.726  102.252 1.00 17.43 ? 1044 VAL A C     1 
ATOM   7611  O  O     . VAL A 1  1046 ? 4.004   54.144  102.074 1.00 16.86 ? 1044 VAL A O     1 
ATOM   7612  C  CB    . VAL A 1  1046 ? 1.516   52.705  102.563 1.00 18.38 ? 1044 VAL A CB    1 
ATOM   7613  C  CG1   . VAL A 1  1046 ? 0.515   52.011  103.480 1.00 21.60 ? 1044 VAL A CG1   1 
ATOM   7614  C  CG2   . VAL A 1  1046 ? 0.956   52.833  101.164 1.00 17.32 ? 1044 VAL A CG2   1 
ATOM   7615  N  N     . HIS A 1  1047 ? 2.667   55.909  101.706 1.00 16.53 ? 1045 HIS A N     1 
ATOM   7616  C  CA    . HIS A 1  1047 ? 3.581   56.540  100.766 1.00 19.76 ? 1045 HIS A CA    1 
ATOM   7617  C  C     . HIS A 1  1047 ? 4.531   57.480  101.488 1.00 18.73 ? 1045 HIS A C     1 
ATOM   7618  O  O     . HIS A 1  1047 ? 4.146   58.157  102.445 1.00 19.22 ? 1045 HIS A O     1 
ATOM   7619  C  CB    . HIS A 1  1047 ? 2.779   57.267  99.694  1.00 19.45 ? 1045 HIS A CB    1 
ATOM   7620  C  CG    . HIS A 1  1047 ? 1.818   56.360  98.997  1.00 22.70 ? 1045 HIS A CG    1 
ATOM   7621  N  ND1   . HIS A 1  1047 ? 2.235   55.343  98.162  1.00 25.70 ? 1045 HIS A ND1   1 
ATOM   7622  C  CD2   . HIS A 1  1047 ? 0.467   56.266  99.064  1.00 24.62 ? 1045 HIS A CD2   1 
ATOM   7623  C  CE1   . HIS A 1  1047 ? 1.179   54.684  97.719  1.00 24.77 ? 1045 HIS A CE1   1 
ATOM   7624  N  NE2   . HIS A 1  1047 ? 0.095   55.221  98.254  1.00 24.46 ? 1045 HIS A NE2   1 
ATOM   7625  N  N     . THR A 1  1048 ? 5.790   57.474  101.061 1.00 17.30 ? 1046 THR A N     1 
ATOM   7626  C  CA    . THR A 1  1048 ? 6.815   58.315  101.660 1.00 19.70 ? 1046 THR A CA    1 
ATOM   7627  C  C     . THR A 1  1048 ? 7.300   59.319  100.628 1.00 19.57 ? 1046 THR A C     1 
ATOM   7628  O  O     . THR A 1  1048 ? 7.638   58.947  99.500  1.00 18.62 ? 1046 THR A O     1 
ATOM   7629  C  CB    . THR A 1  1048 ? 7.989   57.496  102.173 1.00 17.24 ? 1046 THR A CB    1 
ATOM   7630  O  OG1   . THR A 1  1048 ? 7.503   56.441  103.007 1.00 19.97 ? 1046 THR A OG1   1 
ATOM   7631  C  CG2   . THR A 1  1048 ? 8.915   58.406  102.992 1.00 17.58 ? 1046 THR A CG2   1 
ATOM   7632  N  N     . ASP A 1  1049 ? 7.332   60.582  101.010 1.00 18.00 ? 1047 ASP A N     1 
ATOM   7633  C  CA    . ASP A 1  1049 ? 7.766   61.598  100.077 1.00 15.97 ? 1047 ASP A CA    1 
ATOM   7634  C  C     . ASP A 1  1049 ? 9.223   61.341  99.693  1.00 17.46 ? 1047 ASP A C     1 
ATOM   7635  O  O     . ASP A 1  1049 ? 10.062  61.109  100.572 1.00 16.13 ? 1047 ASP A O     1 
ATOM   7636  C  CB    . ASP A 1  1049 ? 7.603   62.989  100.681 1.00 15.28 ? 1047 ASP A CB    1 
ATOM   7637  C  CG    . ASP A 1  1049 ? 8.018   64.073  99.725  1.00 16.09 ? 1047 ASP A CG    1 
ATOM   7638  O  OD1   . ASP A 1  1049 ? 9.241   64.316  99.605  1.00 16.10 ? 1047 ASP A OD1   1 
ATOM   7639  O  OD2   . ASP A 1  1049 ? 7.119   64.632  99.043  1.00 18.24 ? 1047 ASP A OD2   1 
ATOM   7640  N  N     . PRO A 1  1050 ? 9.556   61.347  98.414  1.00 15.84 ? 1048 PRO A N     1 
ATOM   7641  C  CA    . PRO A 1  1050 ? 10.915  60.952  98.013  1.00 16.60 ? 1048 PRO A CA    1 
ATOM   7642  C  C     . PRO A 1  1050 ? 11.955  62.031  98.274  1.00 18.00 ? 1048 PRO A C     1 
ATOM   7643  O  O     . PRO A 1  1050 ? 13.148  61.746  98.420  1.00 17.28 ? 1048 PRO A O     1 
ATOM   7644  C  CB    . PRO A 1  1050 ? 10.764  60.664  96.516  1.00 18.19 ? 1048 PRO A CB    1 
ATOM   7645  C  CG    . PRO A 1  1050 ? 9.598   61.524  96.076  1.00 18.26 ? 1048 PRO A CG    1 
ATOM   7646  C  CD    . PRO A 1  1050 ? 8.656   61.546  97.265  1.00 18.00 ? 1048 PRO A CD    1 
ATOM   7647  N  N     . VAL A 1  1051 ? 11.519  63.287  98.282  1.00 16.34 ? 1049 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1  1051 ? 12.437  64.362  98.622  1.00 17.82 ? 1049 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1  1051 ? 12.751  64.310  100.108 1.00 17.40 ? 1049 VAL A C     1 
ATOM   7650  O  O     . VAL A 1  1051 ? 13.893  64.538  100.520 1.00 16.86 ? 1049 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1  1051 ? 11.861  65.724  98.204  1.00 17.06 ? 1049 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1  1051 ? 12.855  66.818  98.530  1.00 19.77 ? 1049 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1  1051 ? 11.541  65.728  96.700  1.00 18.38 ? 1049 VAL A CG2   1 
ATOM   7654  N  N     . LEU A 1  1052 ? 11.748  63.985  100.936 1.00 16.18 ? 1050 LEU A N     1 
ATOM   7655  C  CA    . LEU A 1  1052 ? 12.020  63.733  102.346 1.00 16.78 ? 1050 LEU A CA    1 
ATOM   7656  C  C     . LEU A 1  1052 ? 13.070  62.642  102.494 1.00 17.23 ? 1050 LEU A C     1 
ATOM   7657  O  O     . LEU A 1  1052 ? 14.034  62.794  103.248 1.00 16.23 ? 1050 LEU A O     1 
ATOM   7658  C  CB    . LEU A 1  1052 ? 10.729  63.360  103.073 1.00 16.72 ? 1050 LEU A CB    1 
ATOM   7659  C  CG    . LEU A 1  1052 ? 10.767  62.910  104.541 1.00 15.78 ? 1050 LEU A CG    1 
ATOM   7660  C  CD1   . LEU A 1  1052 ? 11.260  61.441  104.728 1.00 16.91 ? 1050 LEU A CD1   1 
ATOM   7661  C  CD2   . LEU A 1  1052 ? 11.585  63.893  105.394 1.00 15.02 ? 1050 LEU A CD2   1 
ATOM   7662  N  N     . LEU A 1  1053 ? 12.899  61.532  101.767 1.00 16.58 ? 1051 LEU A N     1 
ATOM   7663  C  CA    . LEU A 1  1053 ? 13.872  60.447  101.844 1.00 18.06 ? 1051 LEU A CA    1 
ATOM   7664  C  C     . LEU A 1  1053 ? 15.255  60.918  101.424 1.00 17.25 ? 1051 LEU A C     1 
ATOM   7665  O  O     . LEU A 1  1053 ? 16.245  60.561  102.065 1.00 17.42 ? 1051 LEU A O     1 
ATOM   7666  C  CB    . LEU A 1  1053 ? 13.419  59.257  100.984 1.00 17.53 ? 1051 LEU A CB    1 
ATOM   7667  C  CG    . LEU A 1  1053 ? 12.217  58.479  101.546 1.00 19.79 ? 1051 LEU A CG    1 
ATOM   7668  C  CD1   . LEU A 1  1053 ? 11.724  57.413  100.565 1.00 18.59 ? 1051 LEU A CD1   1 
ATOM   7669  C  CD2   . LEU A 1  1053 ? 12.568  57.843  102.863 1.00 19.70 ? 1051 LEU A CD2   1 
ATOM   7670  N  N     . ASP A 1  1054 ? 15.343  61.729  100.360 1.00 17.10 ? 1052 ASP A N     1 
ATOM   7671  C  CA    . ASP A 1  1054 ? 16.647  62.241  99.939  1.00 17.04 ? 1052 ASP A CA    1 
ATOM   7672  C  C     . ASP A 1  1054 ? 17.250  63.127  101.022 1.00 17.87 ? 1052 ASP A C     1 
ATOM   7673  O  O     . ASP A 1  1054 ? 18.460  63.077  101.277 1.00 19.55 ? 1052 ASP A O     1 
ATOM   7674  C  CB    . ASP A 1  1054 ? 16.533  63.030  98.634  1.00 19.17 ? 1052 ASP A CB    1 
ATOM   7675  C  CG    . ASP A 1  1054 ? 16.255  62.145  97.419  1.00 23.74 ? 1052 ASP A CG    1 
ATOM   7676  O  OD1   . ASP A 1  1054 ? 16.372  60.907  97.526  1.00 20.50 ? 1052 ASP A OD1   1 
ATOM   7677  O  OD2   . ASP A 1  1054 ? 15.910  62.709  96.359  1.00 25.09 ? 1052 ASP A OD2   1 
ATOM   7678  N  N     . PHE A 1  1055 ? 16.415  63.933  101.676 1.00 16.74 ? 1053 PHE A N     1 
ATOM   7679  C  CA    . PHE A 1  1055 ? 16.901  64.812  102.735 1.00 19.32 ? 1053 PHE A CA    1 
ATOM   7680  C  C     . PHE A 1  1055 ? 17.401  64.009  103.930 1.00 17.28 ? 1053 PHE A C     1 
ATOM   7681  O  O     . PHE A 1  1055 ? 18.449  64.332  104.509 1.00 18.11 ? 1053 PHE A O     1 
ATOM   7682  C  CB    . PHE A 1  1055 ? 15.782  65.784  103.134 1.00 17.48 ? 1053 PHE A CB    1 
ATOM   7683  C  CG    . PHE A 1  1055 ? 16.147  66.717  104.248 1.00 18.70 ? 1053 PHE A CG    1 
ATOM   7684  C  CD1   . PHE A 1  1055 ? 17.218  67.583  104.122 1.00 21.23 ? 1053 PHE A CD1   1 
ATOM   7685  C  CD2   . PHE A 1  1055 ? 15.396  66.750  105.407 1.00 18.01 ? 1053 PHE A CD2   1 
ATOM   7686  C  CE1   . PHE A 1  1055 ? 17.545  68.468  105.152 1.00 21.36 ? 1053 PHE A CE1   1 
ATOM   7687  C  CE2   . PHE A 1  1055 ? 15.723  67.629  106.440 1.00 18.89 ? 1053 PHE A CE2   1 
ATOM   7688  C  CZ    . PHE A 1  1055 ? 16.797  68.479  106.304 1.00 19.60 ? 1053 PHE A CZ    1 
ATOM   7689  N  N     . ALA A 1  1056 ? 16.668  62.960  104.322 1.00 18.09 ? 1054 ALA A N     1 
ATOM   7690  C  CA    . ALA A 1  1056 ? 17.126  62.115  105.423 1.00 17.34 ? 1054 ALA A CA    1 
ATOM   7691  C  C     . ALA A 1  1056 ? 18.490  61.497  105.121 1.00 20.63 ? 1054 ALA A C     1 
ATOM   7692  O  O     . ALA A 1  1056 ? 19.362  61.448  105.995 1.00 20.63 ? 1054 ALA A O     1 
ATOM   7693  C  CB    . ALA A 1  1056 ? 16.090  61.030  105.725 1.00 19.18 ? 1054 ALA A CB    1 
ATOM   7694  N  N     . LYS A 1  1057 ? 18.702  61.030  103.886 1.00 19.98 ? 1055 LYS A N     1 
ATOM   7695  C  CA    . LYS A 1  1057 ? 20.021  60.518  103.510 1.00 22.40 ? 1055 LYS A CA    1 
ATOM   7696  C  C     . LYS A 1  1057 ? 21.074  61.611  103.555 1.00 21.75 ? 1055 LYS A C     1 
ATOM   7697  O  O     . LYS A 1  1057 ? 22.205  61.375  104.005 1.00 25.60 ? 1055 LYS A O     1 
ATOM   7698  C  CB    . LYS A 1  1057 ? 19.975  59.900  102.114 1.00 22.89 ? 1055 LYS A CB    1 
ATOM   7699  C  CG    . LYS A 1  1057 ? 19.350  58.525  102.097 1.00 22.49 ? 1055 LYS A CG    1 
ATOM   7700  C  CD    . LYS A 1  1057 ? 19.606  57.836  100.766 1.00 23.35 ? 1055 LYS A CD    1 
ATOM   7701  C  CE    . LYS A 1  1057 ? 19.101  58.680  99.603  1.00 23.66 ? 1055 LYS A CE    1 
ATOM   7702  N  NZ    . LYS A 1  1057 ? 18.654  57.826  98.479  1.00 27.54 ? 1055 LYS A NZ    1 
ATOM   7703  N  N     . TRP A 1  1058 ? 20.738  62.801  103.055 1.00 20.35 ? 1056 TRP A N     1 
ATOM   7704  C  CA    . TRP A 1  1058 ? 21.667  63.925  103.127 1.00 24.92 ? 1056 TRP A CA    1 
ATOM   7705  C  C     . TRP A 1  1058 ? 22.047  64.235  104.570 1.00 23.60 ? 1056 TRP A C     1 
ATOM   7706  O  O     . TRP A 1  1058 ? 23.218  64.493  104.873 1.00 26.30 ? 1056 TRP A O     1 
ATOM   7707  C  CB    . TRP A 1  1058 ? 21.055  65.155  102.456 1.00 23.02 ? 1056 TRP A CB    1 
ATOM   7708  C  CG    . TRP A 1  1058 ? 21.913  66.391  102.571 1.00 25.24 ? 1056 TRP A CG    1 
ATOM   7709  C  CD1   . TRP A 1  1058 ? 22.938  66.767  101.737 1.00 28.89 ? 1056 TRP A CD1   1 
ATOM   7710  C  CD2   . TRP A 1  1058 ? 21.826  67.407  103.580 1.00 26.73 ? 1056 TRP A CD2   1 
ATOM   7711  N  NE1   . TRP A 1  1058 ? 23.484  67.953  102.167 1.00 29.92 ? 1056 TRP A NE1   1 
ATOM   7712  C  CE2   . TRP A 1  1058 ? 22.824  68.366  103.296 1.00 28.89 ? 1056 TRP A CE2   1 
ATOM   7713  C  CE3   . TRP A 1  1058 ? 21.006  67.596  104.698 1.00 24.22 ? 1056 TRP A CE3   1 
ATOM   7714  C  CZ2   . TRP A 1  1058 ? 23.025  69.495  104.092 1.00 27.19 ? 1056 TRP A CZ2   1 
ATOM   7715  C  CZ3   . TRP A 1  1058 ? 21.202  68.721  105.486 1.00 26.43 ? 1056 TRP A CZ3   1 
ATOM   7716  C  CH2   . TRP A 1  1058 ? 22.206  69.656  105.178 1.00 27.29 ? 1056 TRP A CH2   1 
ATOM   7717  N  N     . LEU A 1  1059 ? 21.071  64.196  105.479 1.00 21.35 ? 1057 LEU A N     1 
ATOM   7718  C  CA    . LEU A 1  1059 ? 21.363  64.435  106.891 1.00 25.33 ? 1057 LEU A CA    1 
ATOM   7719  C  C     . LEU A 1  1059 ? 22.314  63.388  107.449 1.00 24.98 ? 1057 LEU A C     1 
ATOM   7720  O  O     . LEU A 1  1059 ? 23.246  63.719  108.189 1.00 26.79 ? 1057 LEU A O     1 
ATOM   7721  C  CB    . LEU A 1  1059 ? 20.065  64.454  107.699 1.00 21.88 ? 1057 LEU A CB    1 
ATOM   7722  C  CG    . LEU A 1  1059 ? 19.195  65.695  107.534 1.00 21.32 ? 1057 LEU A CG    1 
ATOM   7723  C  CD1   . LEU A 1  1059 ? 17.825  65.419  108.112 1.00 19.44 ? 1057 LEU A CD1   1 
ATOM   7724  C  CD2   . LEU A 1  1059 ? 19.821  66.897  108.245 1.00 23.63 ? 1057 LEU A CD2   1 
ATOM   7725  N  N     . ASP A 1  1060 ? 22.096  62.115  107.111 1.00 23.80 ? 1058 ASP A N     1 
ATOM   7726  C  CA    . ASP A 1  1060 ? 23.012  61.082  107.578 1.00 27.42 ? 1058 ASP A CA    1 
ATOM   7727  C  C     . ASP A 1  1060 ? 24.412  61.288  107.015 1.00 27.40 ? 1058 ASP A C     1 
ATOM   7728  O  O     . ASP A 1  1060 ? 25.402  61.017  107.704 1.00 29.73 ? 1058 ASP A O     1 
ATOM   7729  C  CB    . ASP A 1  1060 ? 22.487  59.699  107.209 1.00 29.48 ? 1058 ASP A CB    1 
ATOM   7730  C  CG    . ASP A 1  1060 ? 21.650  59.076  108.314 1.00 25.99 ? 1058 ASP A CG    1 
ATOM   7731  O  OD1   . ASP A 1  1060 ? 21.890  59.369  109.513 1.00 30.40 ? 1058 ASP A OD1   1 
ATOM   7732  O  OD2   . ASP A 1  1060 ? 20.763  58.272  107.980 1.00 32.16 ? 1058 ASP A OD2   1 
ATOM   7733  N  N     . GLY A 1  1061 ? 24.514  61.791  105.782 1.00 28.30 ? 1059 GLY A N     1 
ATOM   7734  C  CA    . GLY A 1  1061 ? 25.819  62.087  105.213 1.00 26.19 ? 1059 GLY A CA    1 
ATOM   7735  C  C     . GLY A 1  1061 ? 26.518  63.248  105.893 1.00 30.50 ? 1059 GLY A C     1 
ATOM   7736  O  O     . GLY A 1  1061 ? 27.751  63.274  105.967 1.00 30.15 ? 1059 GLY A O     1 
ATOM   7737  N  N     . LYS A 1  1062 ? 25.755  64.222  106.395 1.00 26.18 ? 1060 LYS A N     1 
ATOM   7738  C  CA    . LYS A 1  1062 ? 26.335  65.356  107.107 1.00 29.69 ? 1060 LYS A CA    1 
ATOM   7739  C  C     . LYS A 1  1062 ? 26.643  65.049  108.570 1.00 30.76 ? 1060 LYS A C     1 
ATOM   7740  O  O     . LYS A 1  1062 ? 27.212  65.904  109.255 1.00 33.69 ? 1060 LYS A O     1 
ATOM   7741  C  CB    . LYS A 1  1062 ? 25.405  66.572  107.022 1.00 31.36 ? 1060 LYS A CB    1 
ATOM   7742  C  CG    . LYS A 1  1062 ? 25.303  67.209  105.629 1.00 31.07 ? 1060 LYS A CG    1 
ATOM   7743  C  CD    . LYS A 1  1062 ? 26.617  67.881  105.221 1.00 35.52 ? 1060 LYS A CD    1 
ATOM   7744  C  CE    . LYS A 1  1062 ? 26.530  68.468  103.813 1.00 37.24 ? 1060 LYS A CE    1 
ATOM   7745  N  NZ    . LYS A 1  1062 ? 27.762  69.231  103.449 1.00 39.72 ? 1060 LYS A NZ    1 
ATOM   7746  N  N     . GLY A 1  1063 ? 26.300  63.863  109.067 1.00 28.93 ? 1061 GLY A N     1 
ATOM   7747  C  CA    . GLY A 1  1063 ? 26.535  63.530  110.457 1.00 30.14 ? 1061 GLY A CA    1 
ATOM   7748  C  C     . GLY A 1  1063 ? 25.385  63.829  111.394 1.00 32.54 ? 1061 GLY A C     1 
ATOM   7749  O  O     . GLY A 1  1063 ? 25.484  63.511  112.592 1.00 29.76 ? 1061 GLY A O     1 
ATOM   7750  N  N     . ALA A 1  1064 ? 24.290  64.407  110.885 1.00 29.82 ? 1062 ALA A N     1 
ATOM   7751  C  CA    . ALA A 1  1064 ? 23.125  64.775  111.695 1.00 27.52 ? 1062 ALA A CA    1 
ATOM   7752  C  C     . ALA A 1  1064 ? 22.232  63.546  111.881 1.00 28.34 ? 1062 ALA A C     1 
ATOM   7753  O  O     . ALA A 1  1064 ? 21.119  63.442  111.358 1.00 24.53 ? 1062 ALA A O     1 
ATOM   7754  C  CB    . ALA A 1  1064 ? 22.369  65.928  111.048 1.00 26.33 ? 1062 ALA A CB    1 
ATOM   7755  N  N     . ARG A 1  1065 ? 22.753  62.593  112.653 1.00 25.57 ? 1063 ARG A N     1 
ATOM   7756  C  CA    . ARG A 1  1065 ? 22.121  61.281  112.752 1.00 23.16 ? 1063 ARG A CA    1 
ATOM   7757  C  C     . ARG A 1  1065 ? 20.744  61.368  113.403 1.00 25.08 ? 1063 ARG A C     1 
ATOM   7758  O  O     . ARG A 1  1065 ? 19.784  60.754  112.922 1.00 26.52 ? 1063 ARG A O     1 
ATOM   7759  C  CB    . ARG A 1  1065 ? 23.033  60.327  113.529 1.00 28.99 ? 1063 ARG A CB    1 
ATOM   7760  N  N     . ALA A 1  1066 ? 20.622  62.127  114.492 1.00 24.66 ? 1064 ALA A N     1 
ATOM   7761  C  CA    . ALA A 1  1066 ? 19.327  62.228  115.159 1.00 21.55 ? 1064 ALA A CA    1 
ATOM   7762  C  C     . ALA A 1  1066 ? 18.297  62.907  114.267 1.00 21.98 ? 1064 ALA A C     1 
ATOM   7763  O  O     . ALA A 1  1066 ? 17.126  62.515  114.259 1.00 21.66 ? 1064 ALA A O     1 
ATOM   7764  C  CB    . ALA A 1  1066 ? 19.459  62.992  116.473 1.00 26.14 ? 1064 ALA A CB    1 
ATOM   7765  N  N     . GLU A 1  1067 ? 18.709  63.938  113.527 1.00 23.43 ? 1065 GLU A N     1 
ATOM   7766  C  CA    . GLU A 1  1067 ? 17.760  64.634  112.662 1.00 21.78 ? 1065 GLU A CA    1 
ATOM   7767  C  C     . GLU A 1  1067 ? 17.361  63.763  111.482 1.00 23.22 ? 1065 GLU A C     1 
ATOM   7768  O  O     . GLU A 1  1067 ? 16.214  63.823  111.026 1.00 20.41 ? 1065 GLU A O     1 
ATOM   7769  C  CB    . GLU A 1  1067 ? 18.349  65.959  112.176 1.00 23.88 ? 1065 GLU A CB    1 
ATOM   7770  C  CG    . GLU A 1  1067 ? 18.391  67.059  113.241 1.00 22.01 ? 1065 GLU A CG    1 
ATOM   7771  C  CD    . GLU A 1  1067 ? 19.575  66.913  114.189 1.00 26.42 ? 1065 GLU A CD    1 
ATOM   7772  O  OE1   . GLU A 1  1067 ? 20.434  66.024  113.967 1.00 21.96 ? 1065 GLU A OE1   1 
ATOM   7773  O  OE2   . GLU A 1  1067 ? 19.643  67.691  115.165 1.00 29.97 ? 1065 GLU A OE2   1 
ATOM   7774  N  N     . ALA A 1  1068 ? 18.300  62.959  110.969 1.00 23.45 ? 1066 ALA A N     1 
ATOM   7775  C  CA    . ALA A 1  1068 ? 17.972  62.014  109.903 1.00 22.21 ? 1066 ALA A CA    1 
ATOM   7776  C  C     . ALA A 1  1068 ? 16.934  61.004  110.368 1.00 21.70 ? 1066 ALA A C     1 
ATOM   7777  O  O     . ALA A 1  1068 ? 16.004  60.659  109.623 1.00 18.78 ? 1066 ALA A O     1 
ATOM   7778  C  CB    . ALA A 1  1068 ? 19.239  61.300  109.437 1.00 24.08 ? 1066 ALA A CB    1 
ATOM   7779  N  N     . GLU A 1  1069 ? 17.077  60.517  111.598 1.00 21.82 ? 1067 GLU A N     1 
ATOM   7780  C  CA    . GLU A 1  1069 ? 16.062  59.636  112.163 1.00 21.87 ? 1067 GLU A CA    1 
ATOM   7781  C  C     . GLU A 1  1069 ? 14.722  60.346  112.291 1.00 23.74 ? 1067 GLU A C     1 
ATOM   7782  O  O     . GLU A 1  1069 ? 13.672  59.772  111.979 1.00 20.56 ? 1067 GLU A O     1 
ATOM   7783  C  CB    . GLU A 1  1069 ? 16.513  59.117  113.528 1.00 23.51 ? 1067 GLU A CB    1 
ATOM   7784  C  CG    . GLU A 1  1069 ? 15.421  58.367  114.287 1.00 27.52 ? 1067 GLU A CG    1 
ATOM   7785  C  CD    . GLU A 1  1069 ? 15.182  56.973  113.738 1.00 35.20 ? 1067 GLU A CD    1 
ATOM   7786  O  OE1   . GLU A 1  1069 ? 15.863  56.589  112.760 1.00 39.59 ? 1067 GLU A OE1   1 
ATOM   7787  O  OE2   . GLU A 1  1069 ? 14.311  56.258  114.282 1.00 41.39 ? 1067 GLU A OE2   1 
ATOM   7788  N  N     . ALA A 1  1070 ? 14.731  61.581  112.788 1.00 21.66 ? 1068 ALA A N     1 
ATOM   7789  C  CA    . ALA A 1  1070 ? 13.478  62.316  112.907 1.00 17.71 ? 1068 ALA A CA    1 
ATOM   7790  C  C     . ALA A 1  1070 ? 12.869  62.570  111.541 1.00 16.20 ? 1068 ALA A C     1 
ATOM   7791  O  O     . ALA A 1  1070 ? 11.642  62.553  111.393 1.00 18.73 ? 1068 ALA A O     1 
ATOM   7792  C  CB    . ALA A 1  1070 ? 13.718  63.634  113.639 1.00 21.22 ? 1068 ALA A CB    1 
ATOM   7793  N  N     . ALA A 1  1071 ? 13.714  62.789  110.534 1.00 17.87 ? 1069 ALA A N     1 
ATOM   7794  C  CA    . ALA A 1  1071 ? 13.209  62.974  109.183 1.00 17.76 ? 1069 ALA A CA    1 
ATOM   7795  C  C     . ALA A 1  1071 ? 12.526  61.707  108.681 1.00 19.78 ? 1069 ALA A C     1 
ATOM   7796  O  O     . ALA A 1  1071 ? 11.434  61.771  108.111 1.00 17.45 ? 1069 ALA A O     1 
ATOM   7797  C  CB    . ALA A 1  1071 ? 14.349  63.382  108.253 1.00 18.21 ? 1069 ALA A CB    1 
ATOM   7798  N  N     . ARG A 1  1072 ? 13.154  60.541  108.886 1.00 19.85 ? 1070 ARG A N     1 
ATOM   7799  C  CA    . ARG A 1  1072 ? 12.508  59.292  108.489 1.00 18.99 ? 1070 ARG A CA    1 
ATOM   7800  C  C     . ARG A 1  1072 ? 11.198  59.085  109.247 1.00 18.50 ? 1070 ARG A C     1 
ATOM   7801  O  O     . ARG A 1  1072 ? 10.190  58.677  108.657 1.00 19.61 ? 1070 ARG A O     1 
ATOM   7802  C  CB    . ARG A 1  1072 ? 13.463  58.111  108.694 1.00 21.09 ? 1070 ARG A CB    1 
ATOM   7803  C  CG    . ARG A 1  1072 ? 14.538  58.024  107.606 1.00 24.04 ? 1070 ARG A CG    1 
ATOM   7804  C  CD    . ARG A 1  1072 ? 15.422  56.783  107.778 1.00 25.72 ? 1070 ARG A CD    1 
ATOM   7805  N  NE    . ARG A 1  1072 ? 16.110  56.778  109.062 1.00 26.61 ? 1070 ARG A NE    1 
ATOM   7806  C  CZ    . ARG A 1  1072 ? 17.325  57.269  109.268 1.00 27.38 ? 1070 ARG A CZ    1 
ATOM   7807  N  NH1   . ARG A 1  1072 ? 18.021  57.838  108.291 1.00 26.21 ? 1070 ARG A NH1   1 
ATOM   7808  N  NH2   . ARG A 1  1072 ? 17.854  57.190  110.485 1.00 26.36 ? 1070 ARG A NH2   1 
ATOM   7809  N  N     . ASN A 1  1073 ? 11.173  59.405  110.540 1.00 18.06 ? 1071 ASN A N     1 
ATOM   7810  C  CA    . ASN A 1  1073 ? 9.929   59.265  111.290 1.00 19.90 ? 1071 ASN A CA    1 
ATOM   7811  C  C     . ASN A 1  1073 ? 8.849   60.193  110.747 1.00 19.42 ? 1071 ASN A C     1 
ATOM   7812  O  O     . ASN A 1  1073 ? 7.681   59.799  110.651 1.00 20.50 ? 1071 ASN A O     1 
ATOM   7813  C  CB    . ASN A 1  1073 ? 10.169  59.532  112.774 1.00 20.46 ? 1071 ASN A CB    1 
ATOM   7814  C  CG    . ASN A 1  1073 ? 10.982  58.428  113.438 1.00 25.74 ? 1071 ASN A CG    1 
ATOM   7815  O  OD1   . ASN A 1  1073 ? 11.079  57.314  112.914 1.00 27.26 ? 1071 ASN A OD1   1 
ATOM   7816  N  ND2   . ASN A 1  1073 ? 11.578  58.736  114.579 1.00 26.76 ? 1071 ASN A ND2   1 
ATOM   7817  N  N     . ALA A 1  1074 ? 9.224   61.423  110.368 1.00 18.52 ? 1072 ALA A N     1 
ATOM   7818  C  CA    . ALA A 1  1074 ? 8.247   62.330  109.770 1.00 17.09 ? 1072 ALA A CA    1 
ATOM   7819  C  C     . ALA A 1  1074 ? 7.731   61.777  108.452 1.00 17.73 ? 1072 ALA A C     1 
ATOM   7820  O  O     . ALA A 1  1074 ? 6.534   61.862  108.167 1.00 17.20 ? 1072 ALA A O     1 
ATOM   7821  C  CB    . ALA A 1  1074 ? 8.859   63.716  109.559 1.00 19.13 ? 1072 ALA A CB    1 
ATOM   7822  N  N     . GLY A 1  1075 ? 8.623   61.197  107.645 1.00 16.65 ? 1073 GLY A N     1 
ATOM   7823  C  CA    . GLY A 1  1075 ? 8.198   60.587  106.394 1.00 16.35 ? 1073 GLY A CA    1 
ATOM   7824  C  C     . GLY A 1  1075 ? 7.143   59.513  106.589 1.00 18.83 ? 1073 GLY A C     1 
ATOM   7825  O  O     . GLY A 1  1075 ? 6.181   59.429  105.820 1.00 19.02 ? 1073 GLY A O     1 
ATOM   7826  N  N     . SER A 1  1076 ? 7.303   58.685  107.629 1.00 18.64 ? 1074 SER A N     1 
ATOM   7827  C  CA    . SER A 1  1076 ? 6.324   57.638  107.925 1.00 18.12 ? 1074 SER A CA    1 
ATOM   7828  C  C     . SER A 1  1076 ? 5.058   58.211  108.542 1.00 19.82 ? 1074 SER A C     1 
ATOM   7829  O  O     . SER A 1  1076 ? 3.949   57.762  108.221 1.00 20.61 ? 1074 SER A O     1 
ATOM   7830  C  CB    . SER A 1  1076 ? 6.929   56.605  108.876 1.00 20.99 ? 1074 SER A CB    1 
ATOM   7831  O  OG    . SER A 1  1076 ? 7.985   55.915  108.254 1.00 27.88 ? 1074 SER A OG    1 
ATOM   7832  N  N     . SER A 1  1077 ? 5.206   59.196  109.434 1.00 18.52 ? 1075 SER A N     1 
ATOM   7833  C  CA    A SER A 1  1077 ? 4.044   59.746  110.122 0.45 20.60 ? 1075 SER A CA    1 
ATOM   7834  C  CA    B SER A 1  1077 ? 4.065   59.782  110.133 0.55 20.61 ? 1075 SER A CA    1 
ATOM   7835  C  C     . SER A 1  1077 ? 3.183   60.601  109.200 1.00 20.17 ? 1075 SER A C     1 
ATOM   7836  O  O     . SER A 1  1077 ? 1.978   60.738  109.444 1.00 20.84 ? 1075 SER A O     1 
ATOM   7837  C  CB    A SER A 1  1077 ? 4.490   60.551  111.338 0.45 20.27 ? 1075 SER A CB    1 
ATOM   7838  C  CB    B SER A 1  1077 ? 4.558   60.660  111.287 0.55 20.23 ? 1075 SER A CB    1 
ATOM   7839  O  OG    A SER A 1  1077 ? 4.922   59.678  112.369 0.45 20.79 ? 1075 SER A OG    1 
ATOM   7840  O  OG    B SER A 1  1077 ? 3.479   61.302  111.948 0.55 22.66 ? 1075 SER A OG    1 
ATOM   7841  N  N     . SER A 1  1078 ? 3.765   61.166  108.149 1.00 16.79 ? 1076 SER A N     1 
ATOM   7842  C  CA    . SER A 1  1078 ? 2.998   61.992  107.230 1.00 17.83 ? 1076 SER A CA    1 
ATOM   7843  C  C     . SER A 1  1078 ? 1.865   61.190  106.615 1.00 17.57 ? 1076 SER A C     1 
ATOM   7844  O  O     . SER A 1  1078 ? 2.031   60.024  106.260 1.00 16.76 ? 1076 SER A O     1 
ATOM   7845  C  CB    . SER A 1  1078 ? 3.901   62.513  106.124 1.00 15.66 ? 1076 SER A CB    1 
ATOM   7846  O  OG    . SER A 1  1078 ? 3.123   63.136  105.109 1.00 15.06 ? 1076 SER A OG    1 
ATOM   7847  N  N     . ALA A 1  1079 ? 0.703   61.818  106.490 1.00 14.95 ? 1077 ALA A N     1 
ATOM   7848  C  CA    . ALA A 1  1079 ? -0.423  61.189  105.819 1.00 15.02 ? 1077 ALA A CA    1 
ATOM   7849  C  C     . ALA A 1  1079 ? -0.581  61.702  104.403 1.00 15.50 ? 1077 ALA A C     1 
ATOM   7850  O  O     . ALA A 1  1079 ? -1.628  61.502  103.785 1.00 14.26 ? 1077 ALA A O     1 
ATOM   7851  C  CB    . ALA A 1  1079 ? -1.713  61.400  106.623 1.00 15.58 ? 1077 ALA A CB    1 
ATOM   7852  N  N     . LEU A 1  1080 ? 0.431   62.383  103.883 1.00 15.78 ? 1078 LEU A N     1 
ATOM   7853  C  CA    . LEU A 1  1080 ? 0.406   62.793  102.491 1.00 13.41 ? 1078 LEU A CA    1 
ATOM   7854  C  C     . LEU A 1  1080 ? 0.160   61.576  101.614 1.00 14.91 ? 1078 LEU A C     1 
ATOM   7855  O  O     . LEU A 1  1080 ? 0.796   60.535  101.792 1.00 16.24 ? 1078 LEU A O     1 
ATOM   7856  C  CB    . LEU A 1  1080 ? 1.743   63.440  102.132 1.00 14.85 ? 1078 LEU A CB    1 
ATOM   7857  C  CG    . LEU A 1  1080 ? 1.999   63.687  100.651 1.00 14.68 ? 1078 LEU A CG    1 
ATOM   7858  C  CD1   . LEU A 1  1080 ? 1.182   64.870  100.171 1.00 17.84 ? 1078 LEU A CD1   1 
ATOM   7859  C  CD2   . LEU A 1  1080 ? 3.500   63.945  100.455 1.00 14.89 ? 1078 LEU A CD2   1 
ATOM   7860  N  N     . GLY A 1  1081 ? -0.775  61.698  100.674 1.00 14.16 ? 1079 GLY A N     1 
ATOM   7861  C  CA    . GLY A 1  1081 ? -1.082  60.583  99.812  1.00 17.14 ? 1079 GLY A CA    1 
ATOM   7862  C  C     . GLY A 1  1081 ? -2.275  59.767  100.254 1.00 18.70 ? 1079 GLY A C     1 
ATOM   7863  O  O     . GLY A 1  1081 ? -2.683  58.852  99.522  1.00 17.40 ? 1079 GLY A O     1 
ATOM   7864  N  N     . LEU A 1  1082 ? -2.822  60.046  101.433 1.00 16.69 ? 1080 LEU A N     1 
ATOM   7865  C  CA    . LEU A 1  1082 ? -4.098  59.460  101.828 1.00 15.26 ? 1080 LEU A CA    1 
ATOM   7866  C  C     . LEU A 1  1082 ? -5.110  59.674  100.712 1.00 15.25 ? 1080 LEU A C     1 
ATOM   7867  O  O     . LEU A 1  1082 ? -5.170  60.753  100.121 1.00 15.25 ? 1080 LEU A O     1 
ATOM   7868  C  CB    . LEU A 1  1082 ? -4.580  60.098  103.132 1.00 15.40 ? 1080 LEU A CB    1 
ATOM   7869  C  CG    . LEU A 1  1082 ? -5.906  59.619  103.712 1.00 16.71 ? 1080 LEU A CG    1 
ATOM   7870  C  CD1   . LEU A 1  1082 ? -5.952  58.123  103.719 1.00 23.65 ? 1080 LEU A CD1   1 
ATOM   7871  C  CD2   . LEU A 1  1082 ? -6.093  60.145  105.116 1.00 16.91 ? 1080 LEU A CD2   1 
ATOM   7872  N  N     . ASP A 1  1083 ? -5.850  58.619  100.379 1.00 16.72 ? 1081 ASP A N     1 
ATOM   7873  C  CA    . ASP A 1  1083 ? -6.738  58.650  99.215  1.00 17.00 ? 1081 ASP A CA    1 
ATOM   7874  C  C     . ASP A 1  1083 ? -7.915  57.730  99.525  1.00 18.18 ? 1081 ASP A C     1 
ATOM   7875  O  O     . ASP A 1  1083 ? -7.797  56.509  99.393  1.00 21.07 ? 1081 ASP A O     1 
ATOM   7876  C  CB    . ASP A 1  1083 ? -5.995  58.207  97.962  1.00 18.94 ? 1081 ASP A CB    1 
ATOM   7877  C  CG    . ASP A 1  1083 ? -6.821  58.361  96.706  1.00 24.54 ? 1081 ASP A CG    1 
ATOM   7878  O  OD1   . ASP A 1  1083 ? -7.904  58.978  96.769  1.00 28.08 ? 1081 ASP A OD1   1 
ATOM   7879  O  OD2   . ASP A 1  1083 ? -6.373  57.860  95.655  1.00 30.99 ? 1081 ASP A OD2   1 
ATOM   7880  N  N     . LEU A 1  1084 ? -9.032  58.318  99.943  1.00 17.35 ? 1082 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1  1084 ? -10.153 57.567  100.485 1.00 16.83 ? 1082 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1  1084 ? -11.412 57.838  99.680  1.00 16.49 ? 1082 LEU A C     1 
ATOM   7883  O  O     . LEU A 1  1084 ? -11.576 58.907  99.095  1.00 18.00 ? 1082 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1  1084 ? -10.437 57.946  101.940 1.00 18.85 ? 1082 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1  1084 ? -9.368  57.636  102.979 1.00 19.44 ? 1082 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1  1084 ? -9.817  58.181  104.332 1.00 21.73 ? 1082 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1  1084 ? -9.137  56.140  103.038 1.00 21.33 ? 1082 LEU A CD2   1 
ATOM   7888  N  N     . GLU A 1  1085 ? -12.305 56.861  99.663  1.00 17.27 ? 1083 GLU A N     1 
ATOM   7889  C  CA    . GLU A 1  1085 ? -13.667 57.094  99.206  1.00 16.18 ? 1083 GLU A CA    1 
ATOM   7890  C  C     . GLU A 1  1085 ? -14.568 57.050  100.425 1.00 17.23 ? 1083 GLU A C     1 
ATOM   7891  O  O     . GLU A 1  1085 ? -14.506 56.100  101.214 1.00 18.76 ? 1083 GLU A O     1 
ATOM   7892  C  CB    . GLU A 1  1085 ? -14.122 56.062  98.171  1.00 16.03 ? 1083 GLU A CB    1 
ATOM   7893  C  CG    . GLU A 1  1085 ? -15.584 56.315  97.792  1.00 17.85 ? 1083 GLU A CG    1 
ATOM   7894  C  CD    . GLU A 1  1085 ? -16.120 55.444  96.681  1.00 22.51 ? 1083 GLU A CD    1 
ATOM   7895  O  OE1   . GLU A 1  1085 ? -15.334 54.728  96.020  1.00 23.94 ? 1083 GLU A OE1   1 
ATOM   7896  O  OE2   . GLU A 1  1085 ? -17.355 55.476  96.488  1.00 21.53 ? 1083 GLU A OE2   1 
ATOM   7897  N  N     . LEU A 1  1086 ? -15.385 58.083  100.584 1.00 16.86 ? 1084 LEU A N     1 
ATOM   7898  C  CA    . LEU A 1  1086 ? -16.249 58.236  101.741 1.00 17.58 ? 1084 LEU A CA    1 
ATOM   7899  C  C     . LEU A 1  1086 ? -17.649 57.719  101.429 1.00 18.40 ? 1084 LEU A C     1 
ATOM   7900  O  O     . LEU A 1  1086 ? -18.142 57.913  100.317 1.00 19.13 ? 1084 LEU A O     1 
ATOM   7901  C  CB    . LEU A 1  1086 ? -16.336 59.705  102.149 1.00 17.44 ? 1084 LEU A CB    1 
ATOM   7902  C  CG    . LEU A 1  1086 ? -14.994 60.368  102.466 1.00 18.54 ? 1084 LEU A CG    1 
ATOM   7903  C  CD1   . LEU A 1  1086 ? -15.221 61.833  102.862 1.00 17.69 ? 1084 LEU A CD1   1 
ATOM   7904  C  CD2   . LEU A 1  1086 ? -14.275 59.620  103.571 1.00 19.23 ? 1084 LEU A CD2   1 
ATOM   7905  N  N     . PRO A 1  1087 ? -18.284 57.055  102.392 1.00 18.88 ? 1085 PRO A N     1 
ATOM   7906  C  CA    . PRO A 1  1087 ? -19.649 56.552  102.174 1.00 21.67 ? 1085 PRO A CA    1 
ATOM   7907  C  C     . PRO A 1  1087 ? -20.620 57.687  101.905 1.00 21.52 ? 1085 PRO A C     1 
ATOM   7908  O  O     . PRO A 1  1087 ? -20.565 58.743  102.536 1.00 22.23 ? 1085 PRO A O     1 
ATOM   7909  C  CB    . PRO A 1  1087 ? -19.986 55.842  103.491 1.00 21.58 ? 1085 PRO A CB    1 
ATOM   7910  C  CG    . PRO A 1  1087 ? -18.680 55.583  104.147 1.00 24.05 ? 1085 PRO A CG    1 
ATOM   7911  C  CD    . PRO A 1  1087 ? -17.725 56.640  103.688 1.00 19.02 ? 1085 PRO A CD    1 
ATOM   7912  N  N     . GLY A 1  1088 ? -21.529 57.455  100.961 1.00 19.78 ? 1086 GLY A N     1 
ATOM   7913  C  CA    . GLY A 1  1088 ? -22.510 58.447  100.606 1.00 19.96 ? 1086 GLY A CA    1 
ATOM   7914  C  C     . GLY A 1  1088 ? -23.600 57.838  99.756  1.00 16.30 ? 1086 GLY A C     1 
ATOM   7915  O  O     . GLY A 1  1088 ? -23.790 56.619  99.719  1.00 18.55 ? 1086 GLY A O     1 
ATOM   7916  N  N     . PRO A 1  1089 ? -24.310 58.684  99.025  1.00 18.76 ? 1087 PRO A N     1 
ATOM   7917  C  CA    . PRO A 1  1089 ? -25.429 58.195  98.217  1.00 18.79 ? 1087 PRO A CA    1 
ATOM   7918  C  C     . PRO A 1  1089 ? -24.949 57.415  97.004  1.00 20.07 ? 1087 PRO A C     1 
ATOM   7919  O  O     . PRO A 1  1089 ? -23.831 57.607  96.510  1.00 19.46 ? 1087 PRO A O     1 
ATOM   7920  C  CB    . PRO A 1  1089 ? -26.146 59.484  97.799  1.00 19.64 ? 1087 PRO A CB    1 
ATOM   7921  C  CG    . PRO A 1  1089 ? -25.018 60.518  97.772  1.00 20.29 ? 1087 PRO A CG    1 
ATOM   7922  C  CD    . PRO A 1  1089 ? -24.121 60.141  98.914  1.00 18.93 ? 1087 PRO A CD    1 
ATOM   7923  N  N     . VAL A 1  1090 ? -25.820 56.524  96.516  1.00 18.03 ? 1088 VAL A N     1 
ATOM   7924  C  CA    . VAL A 1  1090 ? -25.538 55.856  95.248  1.00 16.96 ? 1088 VAL A CA    1 
ATOM   7925  C  C     . VAL A 1  1090 ? -25.456 56.899  94.137  1.00 17.65 ? 1088 VAL A C     1 
ATOM   7926  O  O     . VAL A 1  1090 ? -25.955 58.024  94.256  1.00 18.22 ? 1088 VAL A O     1 
ATOM   7927  C  CB    . VAL A 1  1090 ? -26.603 54.799  94.914  1.00 19.77 ? 1088 VAL A CB    1 
ATOM   7928  C  CG1   . VAL A 1  1090 ? -26.673 53.742  96.004  1.00 21.47 ? 1088 VAL A CG1   1 
ATOM   7929  C  CG2   . VAL A 1  1090 ? -27.968 55.459  94.714  1.00 19.06 ? 1088 VAL A CG2   1 
ATOM   7930  N  N     . GLY A 1  1091 ? -24.817 56.509  93.035  1.00 17.35 ? 1089 GLY A N     1 
ATOM   7931  C  CA    . GLY A 1  1091 ? -24.740 57.408  91.906  1.00 20.41 ? 1089 GLY A CA    1 
ATOM   7932  C  C     . GLY A 1  1091 ? -23.764 58.543  92.070  1.00 17.94 ? 1089 GLY A C     1 
ATOM   7933  O  O     . GLY A 1  1091 ? -23.793 59.482  91.280  1.00 17.08 ? 1089 GLY A O     1 
ATOM   7934  N  N     . GLU A 1  1092 ? -22.883 58.471  93.065  1.00 16.90 ? 1090 GLU A N     1 
ATOM   7935  C  CA    . GLU A 1  1092 ? -21.890 59.500  93.320  1.00 17.49 ? 1090 GLU A CA    1 
ATOM   7936  C  C     . GLU A 1  1092 ? -20.667 58.809  93.897  1.00 18.20 ? 1090 GLU A C     1 
ATOM   7937  O  O     . GLU A 1  1092 ? -20.804 57.845  94.651  1.00 19.46 ? 1090 GLU A O     1 
ATOM   7938  C  CB    . GLU A 1  1092 ? -22.432 60.518  94.318  1.00 20.88 ? 1090 GLU A CB    1 
ATOM   7939  C  CG    . GLU A 1  1092 ? -21.938 61.924  94.202  1.00 22.82 ? 1090 GLU A CG    1 
ATOM   7940  C  CD    . GLU A 1  1092 ? -22.764 62.834  95.099  1.00 21.06 ? 1090 GLU A CD    1 
ATOM   7941  O  OE1   . GLU A 1  1092 ? -22.578 62.742  96.325  1.00 18.53 ? 1090 GLU A OE1   1 
ATOM   7942  O  OE2   . GLU A 1  1092 ? -23.629 63.591  94.590  1.00 21.41 ? 1090 GLU A OE2   1 
ATOM   7943  N  N     . ARG A 1  1093 ? -19.478 59.284  93.540  1.00 15.16 ? 1091 ARG A N     1 
ATOM   7944  C  CA    . ARG A 1  1093 ? -18.252 58.844  94.194  1.00 16.45 ? 1091 ARG A CA    1 
ATOM   7945  C  C     . ARG A 1  1093 ? -17.665 60.052  94.907  1.00 15.76 ? 1091 ARG A C     1 
ATOM   7946  O  O     . ARG A 1  1093 ? -17.417 61.088  94.282  1.00 16.07 ? 1091 ARG A O     1 
ATOM   7947  C  CB    . ARG A 1  1093 ? -17.249 58.268  93.193  1.00 17.19 ? 1091 ARG A CB    1 
ATOM   7948  N  N     . ASN A 1  1094 ? -17.449 59.923  96.209  1.00 14.69 ? 1092 ASN A N     1 
ATOM   7949  C  CA    . ASN A 1  1094 ? -17.014 61.042  97.022  1.00 13.68 ? 1092 ASN A CA    1 
ATOM   7950  C  C     . ASN A 1  1094 ? -15.645 60.710  97.587  1.00 15.21 ? 1092 ASN A C     1 
ATOM   7951  O  O     . ASN A 1  1094 ? -15.504 59.743  98.337  1.00 16.39 ? 1092 ASN A O     1 
ATOM   7952  C  CB    . ASN A 1  1094 ? -18.041 61.327  98.104  1.00 14.00 ? 1092 ASN A CB    1 
ATOM   7953  C  CG    . ASN A 1  1094 ? -19.260 62.004  97.532  1.00 15.24 ? 1092 ASN A CG    1 
ATOM   7954  O  OD1   . ASN A 1  1094 ? -19.163 63.125  97.040  1.00 14.40 ? 1092 ASN A OD1   1 
ATOM   7955  N  ND2   . ASN A 1  1094 ? -20.407 61.318  97.553  1.00 16.96 ? 1092 ASN A ND2   1 
ATOM   7956  N  N     . LEU A 1  1095 ? -14.644 61.476  97.167  1.00 14.75 ? 1093 LEU A N     1 
ATOM   7957  C  CA    . LEU A 1  1095 ? -13.246 61.169  97.417  1.00 14.42 ? 1093 LEU A CA    1 
ATOM   7958  C  C     . LEU A 1  1095 ? -12.639 62.217  98.330  1.00 15.01 ? 1093 LEU A C     1 
ATOM   7959  O  O     . LEU A 1  1095 ? -12.994 63.398  98.290  1.00 14.58 ? 1093 LEU A O     1 
ATOM   7960  C  CB    . LEU A 1  1095 ? -12.451 61.109  96.107  1.00 15.33 ? 1093 LEU A CB    1 
ATOM   7961  C  CG    . LEU A 1  1095 ? -13.172 60.256  95.056  1.00 17.84 ? 1093 LEU A CG    1 
ATOM   7962  C  CD1   . LEU A 1  1095 ? -12.425 60.308  93.736  1.00 24.43 ? 1093 LEU A CD1   1 
ATOM   7963  C  CD2   . LEU A 1  1095 ? -13.340 58.799  95.545  1.00 19.31 ? 1093 LEU A CD2   1 
ATOM   7964  N  N     . TYR A 1  1096 ? -11.693 61.770  99.144  1.00 16.35 ? 1094 TYR A N     1 
ATOM   7965  C  CA    . TYR A 1  1096 ? -11.048 62.633  100.117 1.00 14.10 ? 1094 TYR A CA    1 
ATOM   7966  C  C     . TYR A 1  1096 ? -9.573  62.290  100.084 1.00 14.54 ? 1094 TYR A C     1 
ATOM   7967  O  O     . TYR A 1  1096 ? -9.208  61.126  100.294 1.00 15.61 ? 1094 TYR A O     1 
ATOM   7968  C  CB    . TYR A 1  1096 ? -11.641 62.398  101.502 1.00 16.19 ? 1094 TYR A CB    1 
ATOM   7969  C  CG    . TYR A 1  1096 ? -10.929 63.073  102.642 1.00 14.46 ? 1094 TYR A CG    1 
ATOM   7970  C  CD1   . TYR A 1  1096 ? -11.223 64.380  102.984 1.00 13.94 ? 1094 TYR A CD1   1 
ATOM   7971  C  CD2   . TYR A 1  1096 ? -9.988  62.390  103.404 1.00 17.07 ? 1094 TYR A CD2   1 
ATOM   7972  C  CE1   . TYR A 1  1096 ? -10.591 64.999  104.042 1.00 15.20 ? 1094 TYR A CE1   1 
ATOM   7973  C  CE2   . TYR A 1  1096 ? -9.354  63.004  104.481 1.00 17.05 ? 1094 TYR A CE2   1 
ATOM   7974  C  CZ    . TYR A 1  1096 ? -9.657  64.316  104.781 1.00 15.78 ? 1094 TYR A CZ    1 
ATOM   7975  O  OH    . TYR A 1  1096 ? -9.058  64.937  105.840 1.00 15.13 ? 1094 TYR A OH    1 
ATOM   7976  N  N     . THR A 1  1097 ? -8.741  63.282  99.790  1.00 14.75 ? 1095 THR A N     1 
ATOM   7977  C  CA    . THR A 1  1097 ? -7.315  63.039  99.588  1.00 14.70 ? 1095 THR A CA    1 
ATOM   7978  C  C     . THR A 1  1097 ? -6.502  64.100  100.313 1.00 15.32 ? 1095 THR A C     1 
ATOM   7979  O  O     . THR A 1  1097 ? -6.952  65.234  100.475 1.00 15.26 ? 1095 THR A O     1 
ATOM   7980  C  CB    . THR A 1  1097 ? -6.965  63.057  98.102  1.00 18.57 ? 1095 THR A CB    1 
ATOM   7981  O  OG1   . THR A 1  1097 ? -7.311  64.328  97.556  1.00 23.75 ? 1095 THR A OG1   1 
ATOM   7982  C  CG2   . THR A 1  1097 ? -7.745  62.015  97.366  1.00 18.29 ? 1095 THR A CG2   1 
ATOM   7983  N  N     . LEU A 1  1098 ? -5.283  63.734  100.729 1.00 15.48 ? 1096 LEU A N     1 
ATOM   7984  C  CA    . LEU A 1  1098 ? -4.374  64.664  101.387 1.00 16.03 ? 1096 LEU A CA    1 
ATOM   7985  C  C     . LEU A 1  1098 ? -3.198  64.955  100.465 1.00 13.43 ? 1096 LEU A C     1 
ATOM   7986  O  O     . LEU A 1  1098 ? -2.495  64.031  100.040 1.00 15.27 ? 1096 LEU A O     1 
ATOM   7987  C  CB    . LEU A 1  1098 ? -3.868  64.107  102.715 1.00 15.02 ? 1096 LEU A CB    1 
ATOM   7988  C  CG    . LEU A 1  1098 ? -4.980  63.891  103.742 1.00 13.98 ? 1096 LEU A CG    1 
ATOM   7989  C  CD1   . LEU A 1  1098 ? -4.349  63.409  105.068 1.00 14.52 ? 1096 LEU A CD1   1 
ATOM   7990  C  CD2   . LEU A 1  1098 ? -5.802  65.175  103.924 1.00 15.21 ? 1096 LEU A CD2   1 
ATOM   7991  N  N     . HIS A 1  1099 ? -2.988  66.236  100.178 1.00 15.15 ? 1097 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1  1099 ? -1.965  66.742  99.276  1.00 16.53 ? 1097 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1  1099 ? -0.994  67.650  100.024 1.00 15.32 ? 1097 HIS A C     1 
ATOM   7994  O  O     . HIS A 1  1099 ? -1.211  68.015  101.177 1.00 15.50 ? 1097 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1  1099 ? -2.608  67.542  98.140  1.00 16.01 ? 1097 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1  1099 ? -3.557  66.747  97.303  1.00 20.12 ? 1097 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1  1099 ? -3.226  66.274  96.051  1.00 25.15 ? 1097 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1  1099 ? -4.825  66.335  97.539  1.00 21.60 ? 1097 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1  1099 ? -4.255  65.617  95.543  1.00 25.16 ? 1097 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1  1099 ? -5.237  65.636  96.426  1.00 21.50 ? 1097 HIS A NE2   1 
ATOM   8001  N  N     . ALA A 1  1100 ? 0.074   68.045  99.340  1.00 14.21 ? 1098 ALA A N     1 
ATOM   8002  C  CA    . ALA A 1  1100 ? 0.902   69.115  99.880  1.00 17.41 ? 1098 ALA A CA    1 
ATOM   8003  C  C     . ALA A 1  1100 ? 0.118   70.419  99.926  1.00 18.60 ? 1098 ALA A C     1 
ATOM   8004  O  O     . ALA A 1  1100 ? -0.771  70.668  99.105  1.00 18.16 ? 1098 ALA A O     1 
ATOM   8005  C  CB    . ALA A 1  1100 ? 2.151   69.312  99.029  1.00 15.79 ? 1098 ALA A CB    1 
ATOM   8006  N  N     . ARG A 1  1101 ? 0.459   71.261  100.902 1.00 16.04 ? 1099 ARG A N     1 
ATOM   8007  C  CA    A ARG A 1  1101 ? -0.147  72.588  100.976 0.58 18.81 ? 1099 ARG A CA    1 
ATOM   8008  C  CA    B ARG A 1  1101 ? -0.153  72.582  100.968 0.42 18.79 ? 1099 ARG A CA    1 
ATOM   8009  C  C     . ARG A 1  1101 ? 0.424   73.508  99.907  1.00 16.82 ? 1099 ARG A C     1 
ATOM   8010  O  O     . ARG A 1  1101 ? -0.310  74.291  99.299  1.00 18.14 ? 1099 ARG A O     1 
ATOM   8011  C  CB    A ARG A 1  1101 ? 0.061   73.194  102.368 0.58 18.06 ? 1099 ARG A CB    1 
ATOM   8012  C  CB    B ARG A 1  1101 ? 0.028   73.184  102.365 0.42 18.07 ? 1099 ARG A CB    1 
ATOM   8013  C  CG    A ARG A 1  1101 ? -0.646  72.450  103.489 0.58 18.71 ? 1099 ARG A CG    1 
ATOM   8014  C  CG    B ARG A 1  1101 ? -0.917  72.617  103.420 0.42 18.92 ? 1099 ARG A CG    1 
ATOM   8015  C  CD    A ARG A 1  1101 ? -0.539  73.177  104.823 0.58 16.96 ? 1099 ARG A CD    1 
ATOM   8016  C  CD    B ARG A 1  1101 ? -1.708  73.727  104.104 0.42 19.73 ? 1099 ARG A CD    1 
ATOM   8017  N  NE    A ARG A 1  1101 ? -1.439  74.319  104.944 0.58 17.26 ? 1099 ARG A NE    1 
ATOM   8018  N  NE    B ARG A 1  1101 ? -2.762  73.217  104.975 0.42 18.55 ? 1099 ARG A NE    1 
ATOM   8019  C  CZ    A ARG A 1  1101 ? -2.700  74.244  105.357 0.58 19.51 ? 1099 ARG A CZ    1 
ATOM   8020  C  CZ    B ARG A 1  1101 ? -3.507  73.972  105.774 0.42 19.32 ? 1099 ARG A CZ    1 
ATOM   8021  N  NH1   A ARG A 1  1101 ? -3.251  73.089  105.698 0.58 19.18 ? 1099 ARG A NH1   1 
ATOM   8022  N  NH1   B ARG A 1  1101 ? -3.340  75.284  105.841 0.42 19.84 ? 1099 ARG A NH1   1 
ATOM   8023  N  NH2   A ARG A 1  1101 ? -3.429  75.355  105.426 0.58 19.83 ? 1099 ARG A NH2   1 
ATOM   8024  N  NH2   B ARG A 1  1101 ? -4.438  73.397  106.530 0.42 17.58 ? 1099 ARG A NH2   1 
ATOM   8025  N  N     . GLY A 1  1102 ? 1.725   73.418  99.659  1.00 16.67 ? 1100 GLY A N     1 
ATOM   8026  C  CA    . GLY A 1  1102 ? 2.350   74.333  98.732  1.00 18.01 ? 1100 GLY A CA    1 
ATOM   8027  C  C     . GLY A 1  1102 ? 3.738   74.679  99.216  1.00 15.87 ? 1100 GLY A C     1 
ATOM   8028  O  O     . GLY A 1  1102 ? 4.537   73.780  99.500  1.00 17.14 ? 1100 GLY A O     1 
ATOM   8029  N  N     . ARG A 1  1103 ? 4.038   75.973  99.329  1.00 15.94 ? 1101 ARG A N     1 
ATOM   8030  C  CA    . ARG A 1  1103 ? 5.336   76.419  99.816  1.00 14.16 ? 1101 ARG A CA    1 
ATOM   8031  C  C     . ARG A 1  1103 ? 5.165   76.901  101.248 1.00 18.63 ? 1101 ARG A C     1 
ATOM   8032  O  O     . ARG A 1  1103 ? 4.349   77.798  101.516 1.00 17.76 ? 1101 ARG A O     1 
ATOM   8033  C  CB    . ARG A 1  1103 ? 5.924   77.524  98.933  1.00 18.57 ? 1101 ARG A CB    1 
ATOM   8034  C  CG    . ARG A 1  1103 ? 7.373   77.877  99.341  1.00 21.29 ? 1101 ARG A CG    1 
ATOM   8035  C  CD    . ARG A 1  1103 ? 8.101   78.757  98.313  1.00 24.43 ? 1101 ARG A CD    1 
ATOM   8036  N  NE    . ARG A 1  1103 ? 8.168   78.130  96.996  1.00 27.99 ? 1101 ARG A NE    1 
ATOM   8037  C  CZ    . ARG A 1  1103 ? 9.185   77.414  96.522  1.00 29.46 ? 1101 ARG A CZ    1 
ATOM   8038  N  NH1   . ARG A 1  1103 ? 10.277  77.171  97.245  1.00 25.36 ? 1101 ARG A NH1   1 
ATOM   8039  N  NH2   . ARG A 1  1103 ? 9.107   76.930  95.283  1.00 31.88 ? 1101 ARG A NH2   1 
ATOM   8040  N  N     . ILE A 1  1104 ? 5.919   76.292  102.167 1.00 16.16 ? 1102 ILE A N     1 
ATOM   8041  C  CA    . ILE A 1  1104 ? 5.829   76.604  103.592 1.00 19.18 ? 1102 ILE A CA    1 
ATOM   8042  C  C     . ILE A 1  1104 ? 6.965   77.554  103.942 1.00 17.97 ? 1102 ILE A C     1 
ATOM   8043  O  O     . ILE A 1  1104 ? 8.121   77.302  103.587 1.00 17.45 ? 1102 ILE A O     1 
ATOM   8044  C  CB    . ILE A 1  1104 ? 5.901   75.326  104.445 1.00 16.77 ? 1102 ILE A CB    1 
ATOM   8045  C  CG1   . ILE A 1  1104 ? 4.833   74.309  103.992 1.00 16.78 ? 1102 ILE A CG1   1 
ATOM   8046  C  CG2   . ILE A 1  1104 ? 5.775   75.658  105.939 1.00 16.46 ? 1102 ILE A CG2   1 
ATOM   8047  C  CD1   . ILE A 1  1104 ? 3.388   74.746  104.237 1.00 18.38 ? 1102 ILE A CD1   1 
ATOM   8048  N  N     . LEU A 1  1105 ? 6.635   78.657  104.610 1.00 16.47 ? 1103 LEU A N     1 
ATOM   8049  C  CA    . LEU A 1  1105 ? 7.650   79.577  105.107 1.00 18.96 ? 1103 LEU A CA    1 
ATOM   8050  C  C     . LEU A 1  1105 ? 8.286   78.986  106.358 1.00 17.25 ? 1103 LEU A C     1 
ATOM   8051  O  O     . LEU A 1  1105 ? 7.588   78.710  107.339 1.00 18.90 ? 1103 LEU A O     1 
ATOM   8052  C  CB    . LEU A 1  1105 ? 7.034   80.939  105.414 1.00 20.26 ? 1103 LEU A CB    1 
ATOM   8053  C  CG    . LEU A 1  1105 ? 7.936   81.970  106.113 1.00 19.95 ? 1103 LEU A CG    1 
ATOM   8054  C  CD1   . LEU A 1  1105 ? 9.067   82.419  105.195 1.00 22.53 ? 1103 LEU A CD1   1 
ATOM   8055  C  CD2   . LEU A 1  1105 ? 7.098   83.161  106.563 1.00 21.39 ? 1103 LEU A CD2   1 
ATOM   8056  N  N     . LEU A 1  1106 ? 9.597   78.786  106.326 1.00 18.27 ? 1104 LEU A N     1 
ATOM   8057  C  CA    . LEU A 1  1106 ? 10.340  78.303  107.483 1.00 17.33 ? 1104 LEU A CA    1 
ATOM   8058  C  C     . LEU A 1  1106 ? 11.071  79.474  108.116 1.00 20.58 ? 1104 LEU A C     1 
ATOM   8059  O  O     . LEU A 1  1106 ? 11.811  80.189  107.435 1.00 18.31 ? 1104 LEU A O     1 
ATOM   8060  C  CB    . LEU A 1  1106 ? 11.357  77.227  107.100 1.00 17.36 ? 1104 LEU A CB    1 
ATOM   8061  C  CG    . LEU A 1  1106 ? 10.811  75.949  106.474 1.00 20.98 ? 1104 LEU A CG    1 
ATOM   8062  C  CD1   . LEU A 1  1106 ? 11.869  74.856  106.439 1.00 16.78 ? 1104 LEU A CD1   1 
ATOM   8063  C  CD2   . LEU A 1  1106 ? 9.582   75.462  107.182 1.00 22.95 ? 1104 LEU A CD2   1 
ATOM   8064  N  N     . VAL A 1  1107 ? 10.874  79.654  109.414 1.00 19.04 ? 1105 VAL A N     1 
ATOM   8065  C  CA    . VAL A 1  1107 ? 11.584  80.692  110.159 1.00 18.79 ? 1105 VAL A CA    1 
ATOM   8066  C  C     . VAL A 1  1107 ? 12.333  79.996  111.288 1.00 20.42 ? 1105 VAL A C     1 
ATOM   8067  O  O     . VAL A 1  1107 ? 11.861  79.971  112.434 1.00 21.47 ? 1105 VAL A O     1 
ATOM   8068  C  CB    . VAL A 1  1107 ? 10.626  81.779  110.674 1.00 19.93 ? 1105 VAL A CB    1 
ATOM   8069  C  CG1   . VAL A 1  1107 ? 11.413  82.945  111.264 1.00 19.98 ? 1105 VAL A CG1   1 
ATOM   8070  C  CG2   . VAL A 1  1107 ? 9.714   82.277  109.534 1.00 18.91 ? 1105 VAL A CG2   1 
ATOM   8071  N  N     . PRO A 1  1108 ? 13.495  79.422  111.010 1.00 18.36 ? 1106 PRO A N     1 
ATOM   8072  C  CA    . PRO A 1  1108 ? 14.238  78.698  112.040 1.00 20.40 ? 1106 PRO A CA    1 
ATOM   8073  C  C     . PRO A 1  1108 ? 15.065  79.647  112.891 1.00 21.91 ? 1106 PRO A C     1 
ATOM   8074  O  O     . PRO A 1  1108 ? 15.292  80.802  112.536 1.00 21.02 ? 1106 PRO A O     1 
ATOM   8075  C  CB    . PRO A 1  1108 ? 15.145  77.776  111.219 1.00 20.46 ? 1106 PRO A CB    1 
ATOM   8076  C  CG    . PRO A 1  1108 ? 15.462  78.615  110.013 1.00 20.85 ? 1106 PRO A CG    1 
ATOM   8077  C  CD    . PRO A 1  1108 ? 14.160  79.346  109.696 1.00 22.18 ? 1106 PRO A CD    1 
ATOM   8078  N  N     . ALA A 1  1109 ? 15.511  79.131  114.033 1.00 19.21 ? 1107 ALA A N     1 
ATOM   8079  C  CA    . ALA A 1  1109 ? 16.498  79.804  114.868 1.00 20.59 ? 1107 ALA A CA    1 
ATOM   8080  C  C     . ALA A 1  1109 ? 17.796  79.028  115.011 1.00 22.10 ? 1107 ALA A C     1 
ATOM   8081  O  O     . ALA A 1  1109 ? 18.861  79.644  115.156 1.00 23.91 ? 1107 ALA A O     1 
ATOM   8082  C  CB    . ALA A 1  1109 ? 15.919  80.080  116.268 1.00 20.80 ? 1107 ALA A CB    1 
ATOM   8083  N  N     . THR A 1  1110 ? 17.746  77.698  114.969 1.00 20.36 ? 1108 THR A N     1 
ATOM   8084  C  CA    . THR A 1  1110 ? 18.919  76.856  115.141 1.00 21.43 ? 1108 THR A CA    1 
ATOM   8085  C  C     . THR A 1  1110 ? 19.039  75.897  113.966 1.00 22.10 ? 1108 THR A C     1 
ATOM   8086  O  O     . THR A 1  1110 ? 18.075  75.646  113.234 1.00 21.01 ? 1108 THR A O     1 
ATOM   8087  C  CB    . THR A 1  1110 ? 18.866  76.047  116.452 1.00 22.87 ? 1108 THR A CB    1 
ATOM   8088  O  OG1   . THR A 1  1110 ? 17.755  75.141  116.417 1.00 20.66 ? 1108 THR A OG1   1 
ATOM   8089  C  CG2   . THR A 1  1110 ? 18.715  76.972  117.661 1.00 24.36 ? 1108 THR A CG2   1 
ATOM   8090  N  N     . GLU A 1  1111 ? 20.242  75.343  113.810 1.00 22.18 ? 1109 GLU A N     1 
ATOM   8091  C  CA    . GLU A 1  1111 ? 20.462  74.347  112.762 1.00 21.79 ? 1109 GLU A CA    1 
ATOM   8092  C  C     . GLU A 1  1111 ? 19.538  73.142  112.931 1.00 23.56 ? 1109 GLU A C     1 
ATOM   8093  O  O     . GLU A 1  1111 ? 18.862  72.729  111.980 1.00 21.78 ? 1109 GLU A O     1 
ATOM   8094  C  CB    . GLU A 1  1111 ? 21.922  73.907  112.763 1.00 25.20 ? 1109 GLU A CB    1 
ATOM   8095  C  CG    . GLU A 1  1111 ? 22.174  72.723  111.847 1.00 24.46 ? 1109 GLU A CG    1 
ATOM   8096  C  CD    . GLU A 1  1111 ? 23.649  72.429  111.676 1.00 29.28 ? 1109 GLU A CD    1 
ATOM   8097  O  OE1   . GLU A 1  1111 ? 24.343  73.241  111.039 1.00 28.94 ? 1109 GLU A OE1   1 
ATOM   8098  O  OE2   . GLU A 1  1111 ? 24.100  71.389  112.177 1.00 30.17 ? 1109 GLU A OE2   1 
ATOM   8099  N  N     . SER A 1  1112 ? 19.500  72.561  114.136 1.00 23.14 ? 1110 SER A N     1 
ATOM   8100  C  CA    . SER A 1  1112 ? 18.621  71.416  114.369 1.00 20.71 ? 1110 SER A CA    1 
ATOM   8101  C  C     . SER A 1  1112 ? 17.164  71.801  114.182 1.00 21.12 ? 1110 SER A C     1 
ATOM   8102  O  O     . SER A 1  1112 ? 16.373  71.019  113.645 1.00 19.37 ? 1110 SER A O     1 
ATOM   8103  C  CB    . SER A 1  1112 ? 18.836  70.841  115.770 1.00 23.68 ? 1110 SER A CB    1 
ATOM   8104  O  OG    . SER A 1  1112 ? 18.067  69.663  115.939 1.00 23.04 ? 1110 SER A OG    1 
ATOM   8105  N  N     . GLY A 1  1113 ? 16.782  73.002  114.620 1.00 19.91 ? 1111 GLY A N     1 
ATOM   8106  C  CA    . GLY A 1  1113 ? 15.420  73.452  114.370 1.00 17.35 ? 1111 GLY A CA    1 
ATOM   8107  C  C     . GLY A 1  1113 ? 15.105  73.509  112.890 1.00 17.24 ? 1111 GLY A C     1 
ATOM   8108  O  O     . GLY A 1  1113 ? 14.038  73.068  112.452 1.00 17.18 ? 1111 GLY A O     1 
ATOM   8109  N  N     . LEU A 1  1114 ? 16.042  74.028  112.092 1.00 17.92 ? 1112 LEU A N     1 
ATOM   8110  C  CA    . LEU A 1  1114 ? 15.841  74.064  110.648 1.00 16.84 ? 1112 LEU A CA    1 
ATOM   8111  C  C     . LEU A 1  1114 ? 15.679  72.664  110.073 1.00 15.92 ? 1112 LEU A C     1 
ATOM   8112  O  O     . LEU A 1  1114 ? 14.786  72.424  109.247 1.00 17.68 ? 1112 LEU A O     1 
ATOM   8113  C  CB    . LEU A 1  1114 ? 17.016  74.774  109.983 1.00 18.41 ? 1112 LEU A CB    1 
ATOM   8114  C  CG    . LEU A 1  1114 ? 17.049  74.712  108.454 1.00 18.34 ? 1112 LEU A CG    1 
ATOM   8115  C  CD1   . LEU A 1  1114 ? 15.747  75.212  107.800 1.00 18.73 ? 1112 LEU A CD1   1 
ATOM   8116  C  CD2   . LEU A 1  1114 ? 18.257  75.476  107.907 1.00 21.85 ? 1112 LEU A CD2   1 
ATOM   8117  N  N     . TYR A 1  1115 ? 16.528  71.723  110.496 1.00 17.18 ? 1113 TYR A N     1 
ATOM   8118  C  CA    . TYR A 1  1115 ? 16.429  70.364  109.968 1.00 16.45 ? 1113 TYR A CA    1 
ATOM   8119  C  C     . TYR A 1  1115 ? 15.075  69.743  110.300 1.00 18.92 ? 1113 TYR A C     1 
ATOM   8120  O  O     . TYR A 1  1115 ? 14.464  69.083  109.451 1.00 16.85 ? 1113 TYR A O     1 
ATOM   8121  C  CB    . TYR A 1  1115 ? 17.559  69.488  110.513 1.00 18.08 ? 1113 TYR A CB    1 
ATOM   8122  C  CG    . TYR A 1  1115 ? 18.954  69.878  110.049 1.00 19.59 ? 1113 TYR A CG    1 
ATOM   8123  C  CD1   . TYR A 1  1115 ? 19.138  70.722  108.958 1.00 18.25 ? 1113 TYR A CD1   1 
ATOM   8124  C  CD2   . TYR A 1  1115 ? 20.076  69.408  110.711 1.00 20.83 ? 1113 TYR A CD2   1 
ATOM   8125  C  CE1   . TYR A 1  1115 ? 20.426  71.073  108.526 1.00 21.88 ? 1113 TYR A CE1   1 
ATOM   8126  C  CE2   . TYR A 1  1115 ? 21.355  69.748  110.286 1.00 20.85 ? 1113 TYR A CE2   1 
ATOM   8127  C  CZ    . TYR A 1  1115 ? 21.520  70.580  109.195 1.00 23.23 ? 1113 TYR A CZ    1 
ATOM   8128  O  OH    . TYR A 1  1115 ? 22.793  70.935  108.773 1.00 25.10 ? 1113 TYR A OH    1 
ATOM   8129  N  N     . HIS A 1  1116 ? 14.604  69.928  111.541 1.00 17.50 ? 1114 HIS A N     1 
ATOM   8130  C  CA    . HIS A 1  1116 ? 13.277  69.447  111.930 1.00 17.09 ? 1114 HIS A CA    1 
ATOM   8131  C  C     . HIS A 1  1116 ? 12.173  70.133  111.130 1.00 18.79 ? 1114 HIS A C     1 
ATOM   8132  O  O     . HIS A 1  1116 ? 11.204  69.483  110.704 1.00 17.46 ? 1114 HIS A O     1 
ATOM   8133  C  CB    . HIS A 1  1116 ? 13.071  69.650  113.438 1.00 19.15 ? 1114 HIS A CB    1 
ATOM   8134  C  CG    . HIS A 1  1116 ? 13.672  68.570  114.289 1.00 19.49 ? 1114 HIS A CG    1 
ATOM   8135  N  ND1   . HIS A 1  1116 ? 14.966  68.623  114.769 1.00 24.10 ? 1114 HIS A ND1   1 
ATOM   8136  C  CD2   . HIS A 1  1116 ? 13.145  67.417  114.766 1.00 19.91 ? 1114 HIS A CD2   1 
ATOM   8137  C  CE1   . HIS A 1  1116 ? 15.213  67.541  115.491 1.00 22.27 ? 1114 HIS A CE1   1 
ATOM   8138  N  NE2   . HIS A 1  1116 ? 14.123  66.797  115.507 1.00 21.30 ? 1114 HIS A NE2   1 
ATOM   8139  N  N     . GLN A 1  1117 ? 12.294  71.449  110.910 1.00 16.72 ? 1115 GLN A N     1 
ATOM   8140  C  CA    . GLN A 1  1117 ? 11.287  72.151  110.123 1.00 15.47 ? 1115 GLN A CA    1 
ATOM   8141  C  C     . GLN A 1  1117 ? 11.258  71.629  108.699 1.00 15.36 ? 1115 GLN A C     1 
ATOM   8142  O  O     . GLN A 1  1117 ? 10.186  71.371  108.140 1.00 16.58 ? 1115 GLN A O     1 
ATOM   8143  C  CB    . GLN A 1  1117 ? 11.552  73.657  110.127 1.00 17.71 ? 1115 GLN A CB    1 
ATOM   8144  C  CG    . GLN A 1  1117 ? 11.276  74.346  111.447 1.00 16.22 ? 1115 GLN A CG    1 
ATOM   8145  C  CD    . GLN A 1  1117 ? 11.553  75.824  111.351 1.00 19.52 ? 1115 GLN A CD    1 
ATOM   8146  O  OE1   . GLN A 1  1117 ? 12.104  76.281  110.356 1.00 19.22 ? 1115 GLN A OE1   1 
ATOM   8147  N  NE2   . GLN A 1  1117 ? 11.185  76.584  112.389 1.00 18.24 ? 1115 GLN A NE2   1 
ATOM   8148  N  N     . LEU A 1  1118 ? 12.440  71.477  108.096 1.00 15.31 ? 1116 LEU A N     1 
ATOM   8149  C  CA    A LEU A 1  1118 ? 12.503  70.994  106.724 0.51 15.79 ? 1116 LEU A CA    1 
ATOM   8150  C  CA    B LEU A 1  1118 ? 12.522  70.979  106.726 0.49 15.80 ? 1116 LEU A CA    1 
ATOM   8151  C  C     . LEU A 1  1118 ? 11.963  69.573  106.623 1.00 16.90 ? 1116 LEU A C     1 
ATOM   8152  O  O     . LEU A 1  1118 ? 11.219  69.255  105.686 1.00 16.11 ? 1116 LEU A O     1 
ATOM   8153  C  CB    A LEU A 1  1118 ? 13.942  71.088  106.214 0.51 16.92 ? 1116 LEU A CB    1 
ATOM   8154  C  CB    B LEU A 1  1118 ? 13.972  70.995  106.247 0.49 16.92 ? 1116 LEU A CB    1 
ATOM   8155  C  CG    A LEU A 1  1118 ? 14.234  70.808  104.743 0.51 16.85 ? 1116 LEU A CG    1 
ATOM   8156  C  CG    B LEU A 1  1118 ? 14.490  72.267  105.602 0.49 17.04 ? 1116 LEU A CG    1 
ATOM   8157  C  CD1   A LEU A 1  1118 ? 13.255  71.540  103.824 0.51 16.70 ? 1116 LEU A CD1   1 
ATOM   8158  C  CD1   B LEU A 1  1118 ? 15.999  72.158  105.466 0.49 17.92 ? 1116 LEU A CD1   1 
ATOM   8159  C  CD2   A LEU A 1  1118 ? 15.659  71.224  104.429 0.51 19.21 ? 1116 LEU A CD2   1 
ATOM   8160  C  CD2   B LEU A 1  1118 ? 13.837  72.464  104.254 0.49 17.75 ? 1116 LEU A CD2   1 
ATOM   8161  N  N     . ALA A 1  1119 ? 12.303  68.715  107.587 1.00 16.58 ? 1117 ALA A N     1 
ATOM   8162  C  CA    . ALA A 1  1119 ? 11.786  67.348  107.569 1.00 17.28 ? 1117 ALA A CA    1 
ATOM   8163  C  C     . ALA A 1  1119 ? 10.265  67.346  107.629 1.00 17.24 ? 1117 ALA A C     1 
ATOM   8164  O  O     . ALA A 1  1119 ? 9.608   66.635  106.860 1.00 17.97 ? 1117 ALA A O     1 
ATOM   8165  C  CB    . ALA A 1  1119 ? 12.366  66.543  108.729 1.00 17.68 ? 1117 ALA A CB    1 
ATOM   8166  N  N     . ALA A 1  1120 ? 9.681   68.168  108.506 1.00 14.90 ? 1118 ALA A N     1 
ATOM   8167  C  CA    . ALA A 1  1120 ? 8.219   68.213  108.592 1.00 14.03 ? 1118 ALA A CA    1 
ATOM   8168  C  C     . ALA A 1  1120 ? 7.608   68.668  107.277 1.00 15.51 ? 1118 ALA A C     1 
ATOM   8169  O  O     . ALA A 1  1120 ? 6.655   68.055  106.778 1.00 15.66 ? 1118 ALA A O     1 
ATOM   8170  C  CB    . ALA A 1  1120 ? 7.780   69.129  109.733 1.00 15.00 ? 1118 ALA A CB    1 
ATOM   8171  N  N     . ALA A 1  1121 ? 8.176   69.710  106.673 1.00 16.96 ? 1119 ALA A N     1 
ATOM   8172  C  CA    . ALA A 1  1121 ? 7.606   70.262  105.449 1.00 17.60 ? 1119 ALA A CA    1 
ATOM   8173  C  C     . ALA A 1  1121 ? 7.788   69.319  104.262 1.00 14.66 ? 1119 ALA A C     1 
ATOM   8174  O  O     . ALA A 1  1121 ? 6.862   69.135  103.463 1.00 14.48 ? 1119 ALA A O     1 
ATOM   8175  C  CB    . ALA A 1  1121 ? 8.239   71.620  105.152 1.00 16.23 ? 1119 ALA A CB    1 
ATOM   8176  N  N     . LEU A 1  1122 ? 8.975   68.737  104.117 1.00 15.89 ? 1120 LEU A N     1 
ATOM   8177  C  CA    . LEU A 1  1122 ? 9.209   67.824  102.999 1.00 14.34 ? 1120 LEU A CA    1 
ATOM   8178  C  C     . LEU A 1  1122 ? 8.396   66.542  103.143 1.00 15.87 ? 1120 LEU A C     1 
ATOM   8179  O  O     . LEU A 1  1122 ? 7.883   66.025  102.150 1.00 16.61 ? 1120 LEU A O     1 
ATOM   8180  C  CB    . LEU A 1  1122 ? 10.697  67.496  102.890 1.00 16.48 ? 1120 LEU A CB    1 
ATOM   8181  C  CG    . LEU A 1  1122 ? 11.609  68.673  102.546 1.00 18.34 ? 1120 LEU A CG    1 
ATOM   8182  C  CD1   . LEU A 1  1122 ? 13.049  68.204  102.619 1.00 19.85 ? 1120 LEU A CD1   1 
ATOM   8183  C  CD2   . LEU A 1  1122 ? 11.275  69.251  101.170 1.00 17.15 ? 1120 LEU A CD2   1 
ATOM   8184  N  N     . ALA A 1  1123 ? 8.276   66.008  104.362 1.00 16.25 ? 1121 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1  1123 ? 7.524   64.768  104.548 1.00 14.04 ? 1121 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1  1123 ? 6.072   64.932  104.126 1.00 15.84 ? 1121 ALA A C     1 
ATOM   8187  O  O     . ALA A 1  1123 ? 5.405   63.934  103.814 1.00 17.42 ? 1121 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1  1123 ? 7.580   64.318  106.007 1.00 16.29 ? 1121 ALA A CB    1 
ATOM   8189  N  N     . THR A 1  1124 ? 5.571   66.166  104.113 1.00 14.19 ? 1122 THR A N     1 
ATOM   8190  C  CA    . THR A 1  1124 ? 4.193   66.432  103.733 1.00 13.41 ? 1122 THR A CA    1 
ATOM   8191  C  C     . THR A 1  1124 ? 4.094   67.003  102.328 1.00 14.28 ? 1122 THR A C     1 
ATOM   8192  O  O     . THR A 1  1124 ? 3.046   67.538  101.955 1.00 16.03 ? 1122 THR A O     1 
ATOM   8193  C  CB    . THR A 1  1124 ? 3.528   67.350  104.767 1.00 15.60 ? 1122 THR A CB    1 
ATOM   8194  O  OG1   . THR A 1  1124 ? 4.424   68.407  105.111 1.00 15.82 ? 1122 THR A OG1   1 
ATOM   8195  C  CG2   . THR A 1  1124 ? 3.204   66.567  106.047 1.00 16.23 ? 1122 THR A CG2   1 
ATOM   8196  N  N     . GLY A 1  1125 ? 5.167   66.887  101.538 1.00 14.95 ? 1123 GLY A N     1 
ATOM   8197  C  CA    . GLY A 1  1125 ? 5.129   67.142  100.110 1.00 15.35 ? 1123 GLY A CA    1 
ATOM   8198  C  C     . GLY A 1  1125 ? 5.394   68.575  99.718  1.00 15.91 ? 1123 GLY A C     1 
ATOM   8199  O  O     . GLY A 1  1125 ? 5.346   68.896  98.519  1.00 16.50 ? 1123 GLY A O     1 
ATOM   8200  N  N     . ASN A 1  1126 ? 5.683   69.440  100.685 1.00 15.45 ? 1124 ASN A N     1 
ATOM   8201  C  CA    . ASN A 1  1126 ? 5.773   70.868  100.443 1.00 14.82 ? 1124 ASN A CA    1 
ATOM   8202  C  C     . ASN A 1  1126 ? 7.157   71.260  99.956  1.00 14.42 ? 1124 ASN A C     1 
ATOM   8203  O  O     . ASN A 1  1126 ? 8.157   70.583  100.210 1.00 17.10 ? 1124 ASN A O     1 
ATOM   8204  C  CB    . ASN A 1  1126 ? 5.476   71.642  101.725 1.00 14.24 ? 1124 ASN A CB    1 
ATOM   8205  C  CG    . ASN A 1  1126 ? 4.092   71.348  102.249 1.00 15.63 ? 1124 ASN A CG    1 
ATOM   8206  O  OD1   . ASN A 1  1126 ? 3.112   71.738  101.631 1.00 16.51 ? 1124 ASN A OD1   1 
ATOM   8207  N  ND2   . ASN A 1  1126 ? 4.003   70.601  103.349 1.00 14.39 ? 1124 ASN A ND2   1 
ATOM   8208  N  N     . SER A 1  1127 ? 7.207   72.408  99.289  1.00 16.26 ? 1125 SER A N     1 
ATOM   8209  C  CA    . SER A 1  1127 ? 8.451   73.144  99.146  1.00 17.21 ? 1125 SER A CA    1 
ATOM   8210  C  C     . SER A 1  1127 ? 8.535   74.145  100.289 1.00 15.92 ? 1125 SER A C     1 
ATOM   8211  O  O     . SER A 1  1127 ? 7.606   74.284  101.084 1.00 16.36 ? 1125 SER A O     1 
ATOM   8212  C  CB    . SER A 1  1127 ? 8.514   73.852  97.793  1.00 20.77 ? 1125 SER A CB    1 
ATOM   8213  O  OG    . SER A 1  1127 ? 7.435   74.752  97.650  1.00 21.60 ? 1125 SER A OG    1 
ATOM   8214  N  N     . VAL A 1  1128 ? 9.673   74.827  100.395 1.00 18.18 ? 1126 VAL A N     1 
ATOM   8215  C  CA    . VAL A 1  1128 ? 9.883   75.743  101.507 1.00 16.64 ? 1126 VAL A CA    1 
ATOM   8216  C  C     . VAL A 1  1128 ? 10.546  77.020  101.024 1.00 19.72 ? 1126 VAL A C     1 
ATOM   8217  O  O     . VAL A 1  1128 ? 11.294  77.030  100.042 1.00 19.69 ? 1126 VAL A O     1 
ATOM   8218  C  CB    . VAL A 1  1128 ? 10.734  75.111  102.628 1.00 19.26 ? 1126 VAL A CB    1 
ATOM   8219  C  CG1   . VAL A 1  1128 ? 10.071  73.859  103.169 1.00 20.11 ? 1126 VAL A CG1   1 
ATOM   8220  C  CG2   . VAL A 1  1128 ? 12.152  74.809  102.132 1.00 21.30 ? 1126 VAL A CG2   1 
ATOM   8221  N  N     . ALA A 1  1129 ? 10.280  78.105  101.743 1.00 16.98 ? 1127 ALA A N     1 
ATOM   8222  C  CA    . ALA A 1  1129 ? 11.109  79.299  101.671 1.00 20.12 ? 1127 ALA A CA    1 
ATOM   8223  C  C     . ALA A 1  1129 ? 11.671  79.521  103.065 1.00 20.62 ? 1127 ALA A C     1 
ATOM   8224  O  O     . ALA A 1  1129 ? 10.906  79.662  104.026 1.00 21.42 ? 1127 ALA A O     1 
ATOM   8225  C  CB    . ALA A 1  1129 ? 10.313  80.507  101.191 1.00 23.14 ? 1127 ALA A CB    1 
ATOM   8226  N  N     . ILE A 1  1130 ? 12.995  79.516  103.183 1.00 20.14 ? 1128 ILE A N     1 
ATOM   8227  C  CA    . ILE A 1  1130 ? 13.660  79.615  104.477 1.00 20.78 ? 1128 ILE A CA    1 
ATOM   8228  C  C     . ILE A 1  1130 ? 14.084  81.058  104.701 1.00 23.36 ? 1128 ILE A C     1 
ATOM   8229  O  O     . ILE A 1  1130 ? 14.698  81.674  103.825 1.00 23.58 ? 1128 ILE A O     1 
ATOM   8230  C  CB    . ILE A 1  1130 ? 14.875  78.678  104.569 1.00 19.88 ? 1128 ILE A CB    1 
ATOM   8231  C  CG1   . ILE A 1  1130 ? 14.499  77.260  104.135 1.00 21.06 ? 1128 ILE A CG1   1 
ATOM   8232  C  CG2   . ILE A 1  1130 ? 15.412  78.678  106.005 1.00 18.82 ? 1128 ILE A CG2   1 
ATOM   8233  C  CD1   . ILE A 1  1130 ? 15.708  76.344  103.988 1.00 21.27 ? 1128 ILE A CD1   1 
ATOM   8234  N  N     . ASP A 1  1131 ? 13.774  81.588  105.882 1.00 22.61 ? 1129 ASP A N     1 
ATOM   8235  C  CA    . ASP A 1  1131 ? 14.172  82.940  106.261 1.00 22.37 ? 1129 ASP A CA    1 
ATOM   8236  C  C     . ASP A 1  1131 ? 15.683  83.122  106.161 1.00 23.55 ? 1129 ASP A C     1 
ATOM   8237  O  O     . ASP A 1  1131 ? 16.439  82.514  106.925 1.00 23.58 ? 1129 ASP A O     1 
ATOM   8238  C  CB    . ASP A 1  1131 ? 13.699  83.244  107.687 1.00 22.70 ? 1129 ASP A CB    1 
ATOM   8239  C  CG    . ASP A 1  1131 ? 14.071  84.634  108.135 1.00 26.69 ? 1129 ASP A CG    1 
ATOM   8240  O  OD1   . ASP A 1  1131 ? 14.204  85.513  107.262 1.00 23.98 ? 1129 ASP A OD1   1 
ATOM   8241  O  OD2   . ASP A 1  1131 ? 14.241  84.843  109.354 1.00 23.51 ? 1129 ASP A OD2   1 
ATOM   8242  N  N     . ALA A 1  1132 ? 16.134  83.965  105.229 1.00 24.73 ? 1130 ALA A N     1 
ATOM   8243  C  CA    . ALA A 1  1132 ? 17.563  84.201  105.065 1.00 26.28 ? 1130 ALA A CA    1 
ATOM   8244  C  C     . ALA A 1  1132 ? 18.156  84.965  106.240 1.00 27.08 ? 1130 ALA A C     1 
ATOM   8245  O  O     . ALA A 1  1132 ? 19.367  84.877  106.476 1.00 31.69 ? 1130 ALA A O     1 
ATOM   8246  C  CB    . ALA A 1  1132 ? 17.826  84.957  103.762 1.00 29.15 ? 1130 ALA A CB    1 
ATOM   8247  N  N     . ALA A 1  1133 ? 17.330  85.699  106.988 1.00 27.06 ? 1131 ALA A N     1 
ATOM   8248  C  CA    . ALA A 1  1133 ? 17.811  86.421  108.158 1.00 27.82 ? 1131 ALA A CA    1 
ATOM   8249  C  C     . ALA A 1  1133 ? 18.180  85.495  109.306 1.00 29.67 ? 1131 ALA A C     1 
ATOM   8250  O  O     . ALA A 1  1133 ? 18.783  85.955  110.279 1.00 31.57 ? 1131 ALA A O     1 
ATOM   8251  C  CB    . ALA A 1  1133 ? 16.763  87.437  108.616 1.00 27.64 ? 1131 ALA A CB    1 
ATOM   8252  N  N     . SER A 1  1134 ? 17.843  84.205  109.214 1.00 27.02 ? 1132 SER A N     1 
ATOM   8253  C  CA    . SER A 1  1134 ? 18.260  83.242  110.222 1.00 25.84 ? 1132 SER A CA    1 
ATOM   8254  C  C     . SER A 1  1134 ? 19.763  83.036  110.235 1.00 25.85 ? 1132 SER A C     1 
ATOM   8255  O  O     . SER A 1  1134 ? 20.298  82.561  111.240 1.00 24.85 ? 1132 SER A O     1 
ATOM   8256  C  CB    . SER A 1  1134 ? 17.585  81.893  109.972 1.00 24.59 ? 1132 SER A CB    1 
ATOM   8257  O  OG    . SER A 1  1134 ? 18.077  81.309  108.779 1.00 25.06 ? 1132 SER A OG    1 
ATOM   8258  N  N     . GLY A 1  1135 ? 20.444  83.351  109.135 1.00 27.08 ? 1133 GLY A N     1 
ATOM   8259  C  CA    . GLY A 1  1135 ? 21.871  83.120  109.045 1.00 26.59 ? 1133 GLY A CA    1 
ATOM   8260  C  C     . GLY A 1  1135 ? 22.276  81.663  109.007 1.00 27.89 ? 1133 GLY A C     1 
ATOM   8261  O  O     . GLY A 1  1135 ? 23.429  81.343  109.302 1.00 28.44 ? 1133 GLY A O     1 
ATOM   8262  N  N     . LEU A 1  1136 ? 21.359  80.760  108.654 1.00 24.00 ? 1134 LEU A N     1 
ATOM   8263  C  CA    . LEU A 1  1136 ? 21.639  79.331  108.706 1.00 28.10 ? 1134 LEU A CA    1 
ATOM   8264  C  C     . LEU A 1  1136 ? 21.990  78.749  107.339 1.00 28.71 ? 1134 LEU A C     1 
ATOM   8265  O  O     . LEU A 1  1136 ? 21.995  77.523  107.185 1.00 25.33 ? 1134 LEU A O     1 
ATOM   8266  C  CB    . LEU A 1  1136 ? 20.452  78.580  109.317 1.00 22.53 ? 1134 LEU A CB    1 
ATOM   8267  C  CG    . LEU A 1  1136 ? 20.188  78.880  110.798 1.00 23.74 ? 1134 LEU A CG    1 
ATOM   8268  C  CD1   . LEU A 1  1136 ? 18.854  78.278  111.243 1.00 22.26 ? 1134 LEU A CD1   1 
ATOM   8269  C  CD2   . LEU A 1  1136 ? 21.325  78.373  111.660 1.00 26.51 ? 1134 LEU A CD2   1 
ATOM   8270  N  N     . GLN A 1  1137 ? 22.305  79.603  106.357 1.00 26.97 ? 1135 GLN A N     1 
ATOM   8271  C  CA    . GLN A 1  1137 ? 22.631  79.127  105.013 1.00 29.96 ? 1135 GLN A CA    1 
ATOM   8272  C  C     . GLN A 1  1137 ? 23.694  78.034  105.037 1.00 26.62 ? 1135 GLN A C     1 
ATOM   8273  O  O     . GLN A 1  1137 ? 23.585  77.036  104.316 1.00 26.34 ? 1135 GLN A O     1 
ATOM   8274  C  CB    . GLN A 1  1137 ? 23.101  80.291  104.135 1.00 30.44 ? 1135 GLN A CB    1 
ATOM   8275  C  CG    . GLN A 1  1137 ? 21.989  81.201  103.621 1.00 28.44 ? 1135 GLN A CG    1 
ATOM   8276  C  CD    . GLN A 1  1137 ? 21.612  82.279  104.615 1.00 26.72 ? 1135 GLN A CD    1 
ATOM   8277  O  OE1   . GLN A 1  1137 ? 22.073  82.272  105.756 1.00 30.07 ? 1135 GLN A OE1   1 
ATOM   8278  N  NE2   . GLN A 1  1137 ? 20.788  83.224  104.181 1.00 29.98 ? 1135 GLN A NE2   1 
ATOM   8279  N  N     . ALA A 1  1138 ? 24.729  78.193  105.868 1.00 27.42 ? 1136 ALA A N     1 
ATOM   8280  C  CA    . ALA A 1  1138 ? 25.799  77.201  105.872 1.00 28.60 ? 1136 ALA A CA    1 
ATOM   8281  C  C     . ALA A 1  1138 ? 25.367  75.847  106.432 1.00 30.45 ? 1136 ALA A C     1 
ATOM   8282  O  O     . ALA A 1  1138 ? 26.102  74.871  106.267 1.00 32.15 ? 1136 ALA A O     1 
ATOM   8283  C  CB    . ALA A 1  1138 ? 27.009  77.728  106.652 1.00 27.92 ? 1136 ALA A CB    1 
ATOM   8284  N  N     . SER A 1  1139 ? 24.197  75.753  107.070 1.00 29.17 ? 1137 SER A N     1 
ATOM   8285  C  CA    . SER A 1  1139 ? 23.702  74.464  107.535 1.00 29.67 ? 1137 SER A CA    1 
ATOM   8286  C  C     . SER A 1  1139 ? 23.117  73.605  106.417 1.00 27.69 ? 1137 SER A C     1 
ATOM   8287  O  O     . SER A 1  1139 ? 22.826  72.428  106.661 1.00 26.98 ? 1137 SER A O     1 
ATOM   8288  C  CB    . SER A 1  1139 ? 22.638  74.660  108.621 1.00 25.41 ? 1137 SER A CB    1 
ATOM   8289  O  OG    . SER A 1  1139 ? 23.191  75.232  109.793 1.00 27.94 ? 1137 SER A OG    1 
ATOM   8290  N  N     . LEU A 1  1140 ? 22.933  74.150  105.215 1.00 26.97 ? 1138 LEU A N     1 
ATOM   8291  C  CA    . LEU A 1  1140 ? 22.295  73.438  104.109 1.00 28.74 ? 1138 LEU A CA    1 
ATOM   8292  C  C     . LEU A 1  1140 ? 23.178  73.405  102.871 1.00 31.79 ? 1138 LEU A C     1 
ATOM   8293  O  O     . LEU A 1  1140 ? 22.700  73.596  101.750 1.00 34.03 ? 1138 LEU A O     1 
ATOM   8294  C  CB    . LEU A 1  1140 ? 20.949  74.059  103.748 1.00 29.43 ? 1138 LEU A CB    1 
ATOM   8295  C  CG    . LEU A 1  1140 ? 19.696  73.745  104.553 1.00 29.20 ? 1138 LEU A CG    1 
ATOM   8296  C  CD1   . LEU A 1  1140 ? 18.504  74.200  103.746 1.00 27.11 ? 1138 LEU A CD1   1 
ATOM   8297  C  CD2   . LEU A 1  1140 ? 19.587  72.264  104.901 1.00 25.08 ? 1138 LEU A CD2   1 
ATOM   8298  N  N     . LYS A 1  1141 ? 24.472  73.157  103.059 1.00 30.76 ? 1139 LYS A N     1 
ATOM   8299  C  CA    . LYS A 1  1141 ? 25.411  73.084  101.948 1.00 37.04 ? 1139 LYS A CA    1 
ATOM   8300  C  C     . LYS A 1  1141 ? 25.339  71.723  101.262 1.00 34.39 ? 1139 LYS A C     1 
ATOM   8301  O  O     . LYS A 1  1141 ? 25.195  70.688  101.917 1.00 32.23 ? 1139 LYS A O     1 
ATOM   8302  C  CB    . LYS A 1  1141 ? 26.836  73.343  102.443 1.00 37.93 ? 1139 LYS A CB    1 
ATOM   8303  N  N     . ASN A 1  1142 ? 25.446  71.737  99.932  1.00 32.99 ? 1140 ASN A N     1 
ATOM   8304  C  CA    . ASN A 1  1142 ? 25.563  70.520  99.120  1.00 33.47 ? 1140 ASN A CA    1 
ATOM   8305  C  C     . ASN A 1  1142 ? 24.283  69.679  99.147  1.00 32.57 ? 1140 ASN A C     1 
ATOM   8306  O  O     . ASN A 1  1142 ? 24.344  68.448  99.194  1.00 30.29 ? 1140 ASN A O     1 
ATOM   8307  C  CB    . ASN A 1  1142 ? 26.761  69.663  99.548  1.00 36.66 ? 1140 ASN A CB    1 
ATOM   8308  C  CG    . ASN A 1  1142 ? 28.031  70.480  99.770  1.00 43.56 ? 1140 ASN A CG    1 
ATOM   8309  O  OD1   . ASN A 1  1142 ? 28.504  70.613  100.903 1.00 45.12 ? 1140 ASN A OD1   1 
ATOM   8310  N  ND2   . ASN A 1  1142 ? 28.597  71.014  98.690  1.00 41.53 ? 1140 ASN A ND2   1 
ATOM   8311  N  N     . LEU A 1  1143 ? 23.120  70.327  99.091  1.00 32.44 ? 1141 LEU A N     1 
ATOM   8312  C  CA    . LEU A 1  1143 ? 21.881  69.563  99.067  1.00 29.77 ? 1141 LEU A CA    1 
ATOM   8313  C  C     . LEU A 1  1143 ? 21.768  68.750  97.779  1.00 31.92 ? 1141 LEU A C     1 
ATOM   8314  O  O     . LEU A 1  1143 ? 22.220  69.181  96.713  1.00 30.48 ? 1141 LEU A O     1 
ATOM   8315  C  CB    . LEU A 1  1143 ? 20.657  70.472  99.186  1.00 26.45 ? 1141 LEU A CB    1 
ATOM   8316  C  CG    . LEU A 1  1143 ? 20.228  70.966  100.564 1.00 25.40 ? 1141 LEU A CG    1 
ATOM   8317  C  CD1   . LEU A 1  1143 ? 19.087  71.970  100.405 1.00 26.99 ? 1141 LEU A CD1   1 
ATOM   8318  C  CD2   . LEU A 1  1143 ? 19.822  69.806  101.483 1.00 25.50 ? 1141 LEU A CD2   1 
ATOM   8319  N  N     . PRO A 1  1144 ? 21.158  67.572  97.852  1.00 28.81 ? 1142 PRO A N     1 
ATOM   8320  C  CA    . PRO A 1  1144 ? 20.752  66.879  96.627  1.00 30.19 ? 1142 PRO A CA    1 
ATOM   8321  C  C     . PRO A 1  1144 ? 19.880  67.797  95.784  1.00 28.55 ? 1142 PRO A C     1 
ATOM   8322  O  O     . PRO A 1  1144 ? 19.089  68.585  96.312  1.00 27.44 ? 1142 PRO A O     1 
ATOM   8323  C  CB    . PRO A 1  1144 ? 19.967  65.671  97.149  1.00 29.12 ? 1142 PRO A CB    1 
ATOM   8324  C  CG    . PRO A 1  1144 ? 20.451  65.480  98.572  1.00 30.25 ? 1142 PRO A CG    1 
ATOM   8325  C  CD    . PRO A 1  1144 ? 20.738  66.860  99.071  1.00 29.81 ? 1142 PRO A CD    1 
ATOM   8326  N  N     . GLN A 1  1145 ? 20.037  67.706  94.460  1.00 27.74 ? 1143 GLN A N     1 
ATOM   8327  C  CA    . GLN A 1  1145 ? 19.249  68.555  93.576  1.00 28.27 ? 1143 GLN A CA    1 
ATOM   8328  C  C     . GLN A 1  1145 ? 17.753  68.391  93.821  1.00 26.19 ? 1143 GLN A C     1 
ATOM   8329  O  O     . GLN A 1  1145 ? 17.005  69.368  93.709  1.00 26.18 ? 1143 GLN A O     1 
ATOM   8330  C  CB    . GLN A 1  1145 ? 19.579  68.256  92.111  1.00 32.07 ? 1143 GLN A CB    1 
ATOM   8331  N  N     . THR A 1  1146 ? 17.297  67.174  94.148  1.00 26.09 ? 1144 THR A N     1 
ATOM   8332  C  CA    . THR A 1  1146 ? 15.871  66.968  94.403  1.00 29.66 ? 1144 THR A CA    1 
ATOM   8333  C  C     . THR A 1  1146 ? 15.395  67.810  95.576  1.00 24.85 ? 1144 THR A C     1 
ATOM   8334  O  O     . THR A 1  1146 ? 14.267  68.322  95.569  1.00 25.76 ? 1144 THR A O     1 
ATOM   8335  C  CB    . THR A 1  1146 ? 15.581  65.499  94.691  1.00 28.16 ? 1144 THR A CB    1 
ATOM   8336  O  OG1   . THR A 1  1146 ? 16.457  65.051  95.732  1.00 24.01 ? 1144 THR A OG1   1 
ATOM   8337  C  CG2   . THR A 1  1146 ? 15.772  64.649  93.443  1.00 27.41 ? 1144 THR A CG2   1 
ATOM   8338  N  N     . VAL A 1  1147 ? 16.233  67.939  96.606  1.00 23.47 ? 1145 VAL A N     1 
ATOM   8339  C  CA    . VAL A 1  1147 ? 15.863  68.755  97.754  1.00 22.35 ? 1145 VAL A CA    1 
ATOM   8340  C  C     . VAL A 1  1147 ? 16.050  70.227  97.429  1.00 23.62 ? 1145 VAL A C     1 
ATOM   8341  O  O     . VAL A 1  1147 ? 15.192  71.053  97.745  1.00 21.75 ? 1145 VAL A O     1 
ATOM   8342  C  CB    . VAL A 1  1147 ? 16.671  68.341  99.000  1.00 21.76 ? 1145 VAL A CB    1 
ATOM   8343  C  CG1   . VAL A 1  1147 ? 16.246  69.170  100.192 1.00 20.70 ? 1145 VAL A CG1   1 
ATOM   8344  C  CG2   . VAL A 1  1147 ? 16.468  66.859  99.325  1.00 22.61 ? 1145 VAL A CG2   1 
ATOM   8345  N  N     . GLY A 1  1148 ? 17.170  70.576  96.787  1.00 22.81 ? 1146 GLY A N     1 
ATOM   8346  C  CA    . GLY A 1  1148 ? 17.373  71.952  96.366  1.00 22.07 ? 1146 GLY A CA    1 
ATOM   8347  C  C     . GLY A 1  1148 ? 16.223  72.503  95.543  1.00 23.30 ? 1146 GLY A C     1 
ATOM   8348  O  O     . GLY A 1  1148 ? 15.874  73.682  95.664  1.00 23.13 ? 1146 GLY A O     1 
ATOM   8349  N  N     . LEU A 1  1149 ? 15.619  71.661  94.690  1.00 22.22 ? 1147 LEU A N     1 
ATOM   8350  C  CA    . LEU A 1  1149 ? 14.477  72.106  93.897  1.00 23.81 ? 1147 LEU A CA    1 
ATOM   8351  C  C     . LEU A 1  1149 ? 13.335  72.579  94.778  1.00 23.18 ? 1147 LEU A C     1 
ATOM   8352  O  O     . LEU A 1  1149 ? 12.550  73.434  94.361  1.00 24.84 ? 1147 LEU A O     1 
ATOM   8353  C  CB    . LEU A 1  1149 ? 13.973  70.987  92.985  1.00 24.10 ? 1147 LEU A CB    1 
ATOM   8354  C  CG    . LEU A 1  1149 ? 14.865  70.555  91.819  1.00 33.50 ? 1147 LEU A CG    1 
ATOM   8355  C  CD1   . LEU A 1  1149 ? 14.177  69.452  91.024  1.00 32.46 ? 1147 LEU A CD1   1 
ATOM   8356  C  CD2   . LEU A 1  1149 ? 15.190  71.740  90.935  1.00 34.79 ? 1147 LEU A CD2   1 
ATOM   8357  N  N     . ARG A 1  1150 ? 13.226  72.033  95.989  1.00 22.62 ? 1148 ARG A N     1 
ATOM   8358  C  CA    . ARG A 1  1150 ? 12.159  72.385  96.916  1.00 21.42 ? 1148 ARG A CA    1 
ATOM   8359  C  C     . ARG A 1  1150 ? 12.528  73.525  97.850  1.00 21.71 ? 1148 ARG A C     1 
ATOM   8360  O  O     . ARG A 1  1150 ? 11.663  73.983  98.599  1.00 21.42 ? 1148 ARG A O     1 
ATOM   8361  C  CB    . ARG A 1  1150 ? 11.768  71.175  97.769  1.00 21.20 ? 1148 ARG A CB    1 
ATOM   8362  C  CG    . ARG A 1  1150 ? 11.135  70.033  97.008  1.00 20.99 ? 1148 ARG A CG    1 
ATOM   8363  C  CD    . ARG A 1  1150 ? 9.758   69.748  97.589  1.00 21.51 ? 1148 ARG A CD    1 
ATOM   8364  N  NE    . ARG A 1  1150 ? 9.196   68.508  97.068  1.00 19.40 ? 1148 ARG A NE    1 
ATOM   8365  C  CZ    . ARG A 1  1150 ? 8.706   67.533  97.822  1.00 19.41 ? 1148 ARG A CZ    1 
ATOM   8366  N  NH1   . ARG A 1  1150 ? 8.632   67.644  99.144  1.00 16.56 ? 1148 ARG A NH1   1 
ATOM   8367  N  NH2   . ARG A 1  1150 ? 8.268   66.420  97.234  1.00 17.90 ? 1148 ARG A NH2   1 
ATOM   8368  N  N     . VAL A 1  1151 ? 13.772  73.993  97.826  1.00 19.93 ? 1149 VAL A N     1 
ATOM   8369  C  CA    . VAL A 1  1151 ? 14.276  74.922  98.835  1.00 21.21 ? 1149 VAL A CA    1 
ATOM   8370  C  C     . VAL A 1  1151 ? 14.608  76.254  98.180  1.00 25.24 ? 1149 VAL A C     1 
ATOM   8371  O  O     . VAL A 1  1151 ? 15.362  76.309  97.199  1.00 25.21 ? 1149 VAL A O     1 
ATOM   8372  C  CB    . VAL A 1  1151 ? 15.506  74.359  99.568  1.00 21.35 ? 1149 VAL A CB    1 
ATOM   8373  C  CG1   . VAL A 1  1151 ? 16.133  75.438  100.480 1.00 21.45 ? 1149 VAL A CG1   1 
ATOM   8374  C  CG2   . VAL A 1  1151 ? 15.129  73.133  100.379 1.00 21.42 ? 1149 VAL A CG2   1 
ATOM   8375  N  N     . SER A 1  1152 ? 14.052  77.327  98.728  1.00 23.13 ? 1150 SER A N     1 
ATOM   8376  C  CA    . SER A 1  1152 ? 14.486  78.668  98.396  1.00 25.08 ? 1150 SER A CA    1 
ATOM   8377  C  C     . SER A 1  1152 ? 14.767  79.403  99.696  1.00 26.62 ? 1150 SER A C     1 
ATOM   8378  O  O     . SER A 1  1152 ? 14.258  79.041  100.759 1.00 23.17 ? 1150 SER A O     1 
ATOM   8379  C  CB    . SER A 1  1152 ? 13.445  79.417  97.560  1.00 25.64 ? 1150 SER A CB    1 
ATOM   8380  O  OG    . SER A 1  1152 ? 12.262  79.639  98.291  1.00 29.15 ? 1150 SER A OG    1 
ATOM   8381  N  N     . TRP A 1  1153 ? 15.616  80.418  99.607  1.00 26.12 ? 1151 TRP A N     1 
ATOM   8382  C  CA    . TRP A 1  1153 ? 15.896  81.297  100.727 1.00 27.26 ? 1151 TRP A CA    1 
ATOM   8383  C  C     . TRP A 1  1153 ? 15.239  82.645  100.472 1.00 27.76 ? 1151 TRP A C     1 
ATOM   8384  O  O     . TRP A 1  1153 ? 15.294  83.169  99.354  1.00 30.76 ? 1151 TRP A O     1 
ATOM   8385  C  CB    . TRP A 1  1153 ? 17.398  81.456  100.919 1.00 24.90 ? 1151 TRP A CB    1 
ATOM   8386  C  CG    . TRP A 1  1153 ? 18.049  80.225  101.428 1.00 27.50 ? 1151 TRP A CG    1 
ATOM   8387  C  CD1   . TRP A 1  1153 ? 18.516  79.166  100.688 1.00 26.89 ? 1151 TRP A CD1   1 
ATOM   8388  C  CD2   . TRP A 1  1153 ? 18.307  79.906  102.795 1.00 23.97 ? 1151 TRP A CD2   1 
ATOM   8389  N  NE1   . TRP A 1  1153 ? 19.053  78.214  101.524 1.00 27.46 ? 1151 TRP A NE1   1 
ATOM   8390  C  CE2   . TRP A 1  1153 ? 18.941  78.646  102.821 1.00 25.13 ? 1151 TRP A CE2   1 
ATOM   8391  C  CE3   . TRP A 1  1153 ? 18.079  80.570  104.003 1.00 23.84 ? 1151 TRP A CE3   1 
ATOM   8392  C  CZ2   . TRP A 1  1153 ? 19.342  78.034  104.011 1.00 24.95 ? 1151 TRP A CZ2   1 
ATOM   8393  C  CZ3   . TRP A 1  1153 ? 18.482  79.962  105.180 1.00 25.39 ? 1151 TRP A CZ3   1 
ATOM   8394  C  CH2   . TRP A 1  1153 ? 19.105  78.707  105.176 1.00 24.12 ? 1151 TRP A CH2   1 
ATOM   8395  N  N     . SER A 1  1154 ? 14.597  83.194  101.502 1.00 25.96 ? 1152 SER A N     1 
ATOM   8396  C  CA    . SER A 1  1154 ? 13.802  84.408  101.365 1.00 27.72 ? 1152 SER A CA    1 
ATOM   8397  C  C     . SER A 1  1154 ? 14.337  85.485  102.297 1.00 28.23 ? 1152 SER A C     1 
ATOM   8398  O  O     . SER A 1  1154 ? 14.397  85.284  103.515 1.00 25.72 ? 1152 SER A O     1 
ATOM   8399  C  CB    . SER A 1  1154 ? 12.326  84.133  101.663 1.00 26.59 ? 1152 SER A CB    1 
ATOM   8400  O  OG    . SER A 1  1154 ? 11.543  85.301  101.462 1.00 28.44 ? 1152 SER A OG    1 
ATOM   8401  N  N     . LYS A 1  1155 ? 14.726  86.624  101.721 1.00 27.77 ? 1153 LYS A N     1 
ATOM   8402  C  CA    . LYS A 1  1155 ? 15.003  87.824  102.500 1.00 29.50 ? 1153 LYS A CA    1 
ATOM   8403  C  C     . LYS A 1  1155 ? 13.756  88.682  102.658 1.00 33.21 ? 1153 LYS A C     1 
ATOM   8404  O  O     . LYS A 1  1155 ? 13.500  89.207  103.747 1.00 39.70 ? 1153 LYS A O     1 
ATOM   8405  C  CB    . LYS A 1  1155 ? 16.127  88.637  101.847 1.00 30.95 ? 1153 LYS A CB    1 
ATOM   8406  N  N     . ASP A 1  1156 ? 12.961  88.811  101.601 1.00 31.03 ? 1154 ASP A N     1 
ATOM   8407  C  CA    . ASP A 1  1156 ? 11.711  89.564  101.619 1.00 29.63 ? 1154 ASP A CA    1 
ATOM   8408  C  C     . ASP A 1  1156 ? 10.573  88.555  101.505 1.00 32.23 ? 1154 ASP A C     1 
ATOM   8409  O  O     . ASP A 1  1156 ? 10.214  88.142  100.400 1.00 31.16 ? 1154 ASP A O     1 
ATOM   8410  C  CB    . ASP A 1  1156 ? 11.668  90.584  100.482 1.00 33.11 ? 1154 ASP A CB    1 
ATOM   8411  C  CG    . ASP A 1  1156 ? 10.415  91.468  100.519 1.00 38.21 ? 1154 ASP A CG    1 
ATOM   8412  O  OD1   . ASP A 1  1156 ? 9.493   91.215  101.334 1.00 37.10 ? 1154 ASP A OD1   1 
ATOM   8413  O  OD2   . ASP A 1  1156 ? 10.350  92.431  99.721  1.00 39.54 ? 1154 ASP A OD2   1 
ATOM   8414  N  N     . TRP A 1  1157 ? 9.998   88.170  102.649 1.00 29.70 ? 1155 TRP A N     1 
ATOM   8415  C  CA    . TRP A 1  1157 ? 8.949   87.151  102.637 1.00 24.94 ? 1155 TRP A CA    1 
ATOM   8416  C  C     . TRP A 1  1157 ? 7.756   87.586  101.799 1.00 28.76 ? 1155 TRP A C     1 
ATOM   8417  O  O     . TRP A 1  1157 ? 7.132   86.760  101.124 1.00 30.94 ? 1155 TRP A O     1 
ATOM   8418  C  CB    . TRP A 1  1157 ? 8.485   86.849  104.057 1.00 26.57 ? 1155 TRP A CB    1 
ATOM   8419  C  CG    . TRP A 1  1157 ? 9.557   86.479  105.022 1.00 24.68 ? 1155 TRP A CG    1 
ATOM   8420  C  CD1   . TRP A 1  1157 ? 10.846  86.145  104.742 1.00 23.91 ? 1155 TRP A CD1   1 
ATOM   8421  C  CD2   . TRP A 1  1157 ? 9.416   86.393  106.441 1.00 23.35 ? 1155 TRP A CD2   1 
ATOM   8422  N  NE1   . TRP A 1  1157 ? 11.524  85.858  105.905 1.00 25.60 ? 1155 TRP A NE1   1 
ATOM   8423  C  CE2   . TRP A 1  1157 ? 10.663  86.003  106.962 1.00 24.60 ? 1155 TRP A CE2   1 
ATOM   8424  C  CE3   . TRP A 1  1157 ? 8.352   86.626  107.323 1.00 24.46 ? 1155 TRP A CE3   1 
ATOM   8425  C  CZ2   . TRP A 1  1157 ? 10.881  85.832  108.334 1.00 24.16 ? 1155 TRP A CZ2   1 
ATOM   8426  C  CZ3   . TRP A 1  1157 ? 8.564   86.451  108.681 1.00 23.34 ? 1155 TRP A CZ3   1 
ATOM   8427  C  CH2   . TRP A 1  1157 ? 9.820   86.062  109.173 1.00 25.22 ? 1155 TRP A CH2   1 
ATOM   8428  N  N     . ALA A 1  1158 ? 7.403   88.873  101.847 1.00 26.64 ? 1156 ALA A N     1 
ATOM   8429  C  CA    . ALA A 1  1158 ? 6.219   89.322  101.117 1.00 28.85 ? 1156 ALA A CA    1 
ATOM   8430  C  C     . ALA A 1  1158 ? 6.406   89.209  99.611  1.00 30.94 ? 1156 ALA A C     1 
ATOM   8431  O  O     . ALA A 1  1158 ? 5.420   89.081  98.874  1.00 35.51 ? 1156 ALA A O     1 
ATOM   8432  C  CB    . ALA A 1  1158 ? 5.869   90.759  101.504 1.00 32.83 ? 1156 ALA A CB    1 
ATOM   8433  N  N     . ALA A 1  1159 ? 7.651   89.235  99.137  1.00 30.69 ? 1157 ALA A N     1 
ATOM   8434  C  CA    . ALA A 1  1159 ? 7.926   89.120  97.711  1.00 34.33 ? 1157 ALA A CA    1 
ATOM   8435  C  C     . ALA A 1  1159 ? 7.876   87.684  97.213  1.00 34.49 ? 1157 ALA A C     1 
ATOM   8436  O  O     . ALA A 1  1159 ? 7.659   87.464  96.017  1.00 31.81 ? 1157 ALA A O     1 
ATOM   8437  C  CB    . ALA A 1  1159 ? 9.301   89.715  97.391  1.00 32.14 ? 1157 ALA A CB    1 
ATOM   8438  N  N     . ASP A 1  1160 ? 8.068   86.709  98.096  1.00 32.40 ? 1158 ASP A N     1 
ATOM   8439  C  CA    . ASP A 1  1160 ? 8.271   85.323  97.706  1.00 31.85 ? 1158 ASP A CA    1 
ATOM   8440  C  C     . ASP A 1  1160 ? 7.047   84.452  97.954  1.00 28.44 ? 1158 ASP A C     1 
ATOM   8441  O  O     . ASP A 1  1160 ? 7.120   83.235  97.767  1.00 30.14 ? 1158 ASP A O     1 
ATOM   8442  C  CB    . ASP A 1  1160 ? 9.484   84.750  98.441  1.00 28.33 ? 1158 ASP A CB    1 
ATOM   8443  C  CG    . ASP A 1  1160 ? 10.756  85.499  98.120  1.00 33.09 ? 1158 ASP A CG    1 
ATOM   8444  O  OD1   . ASP A 1  1160 ? 10.804  86.149  97.057  1.00 37.33 ? 1158 ASP A OD1   1 
ATOM   8445  O  OD2   . ASP A 1  1160 ? 11.705  85.447  98.924  1.00 31.03 ? 1158 ASP A OD2   1 
ATOM   8446  N  N     . GLY A 1  1161 ? 5.931   85.044  98.370  1.00 26.55 ? 1159 GLY A N     1 
ATOM   8447  C  CA    . GLY A 1  1161 ? 4.711   84.308  98.590  1.00 26.29 ? 1159 GLY A CA    1 
ATOM   8448  C  C     . GLY A 1  1161 ? 3.931   84.125  97.301  1.00 27.84 ? 1159 GLY A C     1 
ATOM   8449  O  O     . GLY A 1  1161 ? 4.414   84.453  96.215  1.00 31.19 ? 1159 GLY A O     1 
ATOM   8450  N  N     . PRO A 1  1162 ? 2.695   83.615  97.397  1.00 24.80 ? 1160 PRO A N     1 
ATOM   8451  C  CA    . PRO A 1  1162 ? 1.963   83.275  98.617  1.00 25.88 ? 1160 PRO A CA    1 
ATOM   8452  C  C     . PRO A 1  1162 ? 2.476   81.988  99.232  1.00 24.86 ? 1160 PRO A C     1 
ATOM   8453  O  O     . PRO A 1  1162 ? 2.832   81.041  98.538  1.00 26.63 ? 1160 PRO A O     1 
ATOM   8454  C  CB    . PRO A 1  1162 ? 0.516   83.132  98.120  1.00 24.26 ? 1160 PRO A CB    1 
ATOM   8455  C  CG    . PRO A 1  1162 ? 0.673   82.590  96.734  1.00 26.28 ? 1160 PRO A CG    1 
ATOM   8456  C  CD    . PRO A 1  1162 ? 1.905   83.301  96.191  1.00 26.65 ? 1160 PRO A CD    1 
ATOM   8457  N  N     . PHE A 1  1163 ? 2.549   81.947  100.554 1.00 20.58 ? 1161 PHE A N     1 
ATOM   8458  C  CA    . PHE A 1  1163 ? 2.872   80.712  101.236 1.00 18.46 ? 1161 PHE A CA    1 
ATOM   8459  C  C     . PHE A 1  1163 ? 1.587   79.988  101.589 1.00 19.69 ? 1161 PHE A C     1 
ATOM   8460  O  O     . PHE A 1  1163 ? 0.483   80.521  101.454 1.00 21.71 ? 1161 PHE A O     1 
ATOM   8461  C  CB    . PHE A 1  1163 ? 3.725   81.003  102.468 1.00 19.20 ? 1161 PHE A CB    1 
ATOM   8462  C  CG    . PHE A 1  1163 ? 4.972   81.750  102.141 1.00 20.76 ? 1161 PHE A CG    1 
ATOM   8463  C  CD1   . PHE A 1  1163 ? 5.944   81.166  101.347 1.00 20.71 ? 1161 PHE A CD1   1 
ATOM   8464  C  CD2   . PHE A 1  1163 ? 5.163   83.044  102.593 1.00 19.64 ? 1161 PHE A CD2   1 
ATOM   8465  C  CE1   . PHE A 1  1163 ? 7.098   81.853  101.016 1.00 23.51 ? 1161 PHE A CE1   1 
ATOM   8466  C  CE2   . PHE A 1  1163 ? 6.321   83.738  102.279 1.00 23.57 ? 1161 PHE A CE2   1 
ATOM   8467  C  CZ    . PHE A 1  1163 ? 7.285   83.144  101.484 1.00 21.93 ? 1161 PHE A CZ    1 
ATOM   8468  N  N     . ALA A 1  1164 ? 1.728   78.732  101.999 1.00 16.79 ? 1162 ALA A N     1 
ATOM   8469  C  CA    . ALA A 1  1164 ? 0.571   77.935  102.374 1.00 17.60 ? 1162 ALA A CA    1 
ATOM   8470  C  C     . ALA A 1  1164 ? 0.603   77.525  103.837 1.00 18.01 ? 1162 ALA A C     1 
ATOM   8471  O  O     . ALA A 1  1164 ? -0.228  76.718  104.267 1.00 19.25 ? 1162 ALA A O     1 
ATOM   8472  C  CB    . ALA A 1  1164 ? 0.475   76.699  101.474 1.00 20.67 ? 1162 ALA A CB    1 
ATOM   8473  N  N     . GLY A 1  1165 ? 1.542   78.055  104.600 1.00 17.12 ? 1163 GLY A N     1 
ATOM   8474  C  CA    . GLY A 1  1165 ? 1.670   77.748  106.008 1.00 16.39 ? 1163 GLY A CA    1 
ATOM   8475  C  C     . GLY A 1  1165 ? 3.048   78.196  106.438 1.00 16.92 ? 1163 GLY A C     1 
ATOM   8476  O  O     . GLY A 1  1165 ? 3.855   78.633  105.622 1.00 17.51 ? 1163 GLY A O     1 
ATOM   8477  N  N     . ALA A 1  1166 ? 3.309   78.076  107.736 1.00 17.26 ? 1164 ALA A N     1 
ATOM   8478  C  CA    . ALA A 1  1166 ? 4.603   78.508  108.233 1.00 17.00 ? 1164 ALA A CA    1 
ATOM   8479  C  C     . ALA A 1  1166 ? 4.993   77.674  109.442 1.00 16.93 ? 1164 ALA A C     1 
ATOM   8480  O  O     . ALA A 1  1166 ? 4.133   77.210  110.196 1.00 19.15 ? 1164 ALA A O     1 
ATOM   8481  C  CB    . ALA A 1  1166 ? 4.610   79.996  108.616 1.00 18.17 ? 1164 ALA A CB    1 
ATOM   8482  N  N     . LEU A 1  1167 ? 6.301   77.505  109.615 1.00 16.70 ? 1165 LEU A N     1 
ATOM   8483  C  CA    . LEU A 1  1167 ? 6.891   76.876  110.788 1.00 16.55 ? 1165 LEU A CA    1 
ATOM   8484  C  C     . LEU A 1  1167 ? 7.877   77.861  111.401 1.00 17.79 ? 1165 LEU A C     1 
ATOM   8485  O  O     . LEU A 1  1167 ? 8.725   78.412  110.695 1.00 19.60 ? 1165 LEU A O     1 
ATOM   8486  C  CB    . LEU A 1  1167 ? 7.603   75.575  110.427 1.00 16.76 ? 1165 LEU A CB    1 
ATOM   8487  C  CG    . LEU A 1  1167 ? 6.727   74.514  109.754 1.00 17.62 ? 1165 LEU A CG    1 
ATOM   8488  C  CD1   . LEU A 1  1167 ? 7.590   73.314  109.327 1.00 18.23 ? 1165 LEU A CD1   1 
ATOM   8489  C  CD2   . LEU A 1  1167 ? 5.602   74.084  110.678 1.00 18.47 ? 1165 LEU A CD2   1 
ATOM   8490  N  N     . VAL A 1  1168 ? 7.761   78.091  112.701 1.00 18.65 ? 1166 VAL A N     1 
ATOM   8491  C  CA    . VAL A 1  1168 ? 8.560   79.102  113.384 1.00 19.17 ? 1166 VAL A CA    1 
ATOM   8492  C  C     . VAL A 1  1168 ? 9.251   78.463  114.577 1.00 18.87 ? 1166 VAL A C     1 
ATOM   8493  O  O     . VAL A 1  1168 ? 8.644   77.670  115.304 1.00 17.86 ? 1166 VAL A O     1 
ATOM   8494  C  CB    . VAL A 1  1168 ? 7.687   80.295  113.833 1.00 17.84 ? 1166 VAL A CB    1 
ATOM   8495  C  CG1   . VAL A 1  1168 ? 8.531   81.353  114.563 1.00 19.60 ? 1166 VAL A CG1   1 
ATOM   8496  C  CG2   . VAL A 1  1168 ? 6.942   80.908  112.637 1.00 18.10 ? 1166 VAL A CG2   1 
ATOM   8497  N  N     . GLU A 1  1169 ? 10.531  78.788  114.760 1.00 17.59 ? 1167 GLU A N     1 
ATOM   8498  C  CA    . GLU A 1  1169 ? 11.293  78.384  115.936 1.00 18.50 ? 1167 GLU A CA    1 
ATOM   8499  C  C     . GLU A 1  1169 ? 11.743  79.632  116.683 1.00 20.61 ? 1167 GLU A C     1 
ATOM   8500  O  O     . GLU A 1  1169 ? 12.237  80.581  116.066 1.00 20.99 ? 1167 GLU A O     1 
ATOM   8501  C  CB    . GLU A 1  1169 ? 12.509  77.545  115.539 1.00 18.81 ? 1167 GLU A CB    1 
ATOM   8502  C  CG    . GLU A 1  1169 ? 13.393  77.111  116.708 1.00 17.82 ? 1167 GLU A CG    1 
ATOM   8503  C  CD    . GLU A 1  1169 ? 14.721  76.550  116.245 1.00 20.41 ? 1167 GLU A CD    1 
ATOM   8504  O  OE1   . GLU A 1  1169 ? 15.036  76.674  115.043 1.00 19.81 ? 1167 GLU A OE1   1 
ATOM   8505  O  OE2   . GLU A 1  1169 ? 15.454  75.998  117.082 1.00 20.60 ? 1167 GLU A OE2   1 
ATOM   8506  N  N     . GLY A 1  1170 ? 11.571  79.635  117.996 1.00 18.64 ? 1168 GLY A N     1 
ATOM   8507  C  CA    . GLY A 1  1170 ? 12.126  80.714  118.792 1.00 21.24 ? 1168 GLY A CA    1 
ATOM   8508  C  C     . GLY A 1  1170 ? 11.555  80.724  120.191 1.00 22.67 ? 1168 GLY A C     1 
ATOM   8509  O  O     . GLY A 1  1170 ? 10.668  79.937  120.535 1.00 22.95 ? 1168 GLY A O     1 
ATOM   8510  N  N     . ASP A 1  1171 ? 12.062  81.661  120.993 1.00 24.25 ? 1169 ASP A N     1 
ATOM   8511  C  CA    . ASP A 1  1171 ? 11.433  81.889  122.286 1.00 22.17 ? 1169 ASP A CA    1 
ATOM   8512  C  C     . ASP A 1  1171 ? 10.135  82.678  122.091 1.00 26.10 ? 1169 ASP A C     1 
ATOM   8513  O  O     . ASP A 1  1171 ? 9.737   83.008  120.964 1.00 25.32 ? 1169 ASP A O     1 
ATOM   8514  C  CB    . ASP A 1  1171 ? 12.422  82.546  123.265 1.00 24.65 ? 1169 ASP A CB    1 
ATOM   8515  C  CG    . ASP A 1  1171 ? 12.914  83.937  122.827 1.00 30.00 ? 1169 ASP A CG    1 
ATOM   8516  O  OD1   . ASP A 1  1171 ? 12.285  84.606  121.992 1.00 26.18 ? 1169 ASP A OD1   1 
ATOM   8517  O  OD2   . ASP A 1  1171 ? 13.963  84.378  123.358 1.00 33.56 ? 1169 ASP A OD2   1 
ATOM   8518  N  N     . ALA A 1  1172 ? 9.429   82.940  123.195 1.00 25.09 ? 1170 ALA A N     1 
ATOM   8519  C  CA    . ALA A 1  1172 ? 8.086   83.499  123.091 1.00 26.04 ? 1170 ALA A CA    1 
ATOM   8520  C  C     . ALA A 1  1172 ? 8.089   84.843  122.370 1.00 28.43 ? 1170 ALA A C     1 
ATOM   8521  O  O     . ALA A 1  1172 ? 7.222   85.103  121.528 1.00 26.96 ? 1170 ALA A O     1 
ATOM   8522  C  CB    . ALA A 1  1172 ? 7.455   83.637  124.478 1.00 27.11 ? 1170 ALA A CB    1 
ATOM   8523  N  N     . GLU A 1  1173 ? 9.063   85.705  122.667 1.00 28.36 ? 1171 GLU A N     1 
ATOM   8524  C  CA    . GLU A 1  1173 ? 9.052   87.018  122.028 1.00 28.59 ? 1171 GLU A CA    1 
ATOM   8525  C  C     . GLU A 1  1173 ? 9.486   86.940  120.568 1.00 28.41 ? 1171 GLU A C     1 
ATOM   8526  O  O     . GLU A 1  1173 ? 9.006   87.723  119.739 1.00 28.37 ? 1171 GLU A O     1 
ATOM   8527  C  CB    . GLU A 1  1173 ? 9.920   88.001  122.816 1.00 30.79 ? 1171 GLU A CB    1 
ATOM   8528  C  CG    . GLU A 1  1173 ? 9.274   88.414  124.133 1.00 33.63 ? 1171 GLU A CG    1 
ATOM   8529  C  CD    . GLU A 1  1173 ? 7.809   88.828  123.972 1.00 37.25 ? 1171 GLU A CD    1 
ATOM   8530  O  OE1   . GLU A 1  1173 ? 7.489   89.589  123.024 1.00 36.09 ? 1171 GLU A OE1   1 
ATOM   8531  O  OE2   . GLU A 1  1173 ? 6.972   88.391  124.795 1.00 34.84 ? 1171 GLU A OE2   1 
ATOM   8532  N  N     . ARG A 1  1174 ? 10.367  85.999  120.228 1.00 25.38 ? 1172 ARG A N     1 
ATOM   8533  C  CA    . ARG A 1  1174 ? 10.691  85.780  118.822 1.00 25.41 ? 1172 ARG A CA    1 
ATOM   8534  C  C     . ARG A 1  1174 ? 9.473   85.293  118.055 1.00 24.84 ? 1172 ARG A C     1 
ATOM   8535  O  O     . ARG A 1  1174 ? 9.213   85.745  116.932 1.00 23.59 ? 1172 ARG A O     1 
ATOM   8536  C  CB    . ARG A 1  1174 ? 11.828  84.769  118.688 1.00 23.50 ? 1172 ARG A CB    1 
ATOM   8537  C  CG    . ARG A 1  1174 ? 12.159  84.374  117.254 1.00 24.11 ? 1172 ARG A CG    1 
ATOM   8538  C  CD    . ARG A 1  1174 ? 12.656  85.550  116.452 1.00 29.15 ? 1172 ARG A CD    1 
ATOM   8539  N  NE    . ARG A 1  1174 ? 12.980  85.174  115.080 1.00 26.85 ? 1172 ARG A NE    1 
ATOM   8540  C  CZ    . ARG A 1  1174 ? 13.065  86.037  114.079 1.00 27.43 ? 1172 ARG A CZ    1 
ATOM   8541  N  NH1   . ARG A 1  1174 ? 12.837  87.330  114.259 1.00 28.23 ? 1172 ARG A NH1   1 
ATOM   8542  N  NH2   . ARG A 1  1174 ? 13.382  85.595  112.867 1.00 23.71 ? 1172 ARG A NH2   1 
ATOM   8543  N  N     . ILE A 1  1175 ? 8.727   84.352  118.637 1.00 23.98 ? 1173 ILE A N     1 
ATOM   8544  C  CA    . ILE A 1  1175 ? 7.518   83.851  117.989 1.00 22.86 ? 1173 ILE A CA    1 
ATOM   8545  C  C     . ILE A 1  1175 ? 6.524   84.986  117.789 1.00 23.35 ? 1173 ILE A C     1 
ATOM   8546  O  O     . ILE A 1  1175 ? 5.897   85.108  116.727 1.00 23.85 ? 1173 ILE A O     1 
ATOM   8547  C  CB    . ILE A 1  1175 ? 6.906   82.708  118.820 1.00 22.82 ? 1173 ILE A CB    1 
ATOM   8548  C  CG1   . ILE A 1  1175 ? 7.830   81.487  118.811 1.00 24.50 ? 1173 ILE A CG1   1 
ATOM   8549  C  CG2   . ILE A 1  1175 ? 5.528   82.359  118.304 1.00 23.67 ? 1173 ILE A CG2   1 
ATOM   8550  C  CD1   . ILE A 1  1175 ? 7.428   80.390  119.810 1.00 23.82 ? 1173 ILE A CD1   1 
ATOM   8551  N  N     . ARG A 1  1176 ? 6.382   85.849  118.803 1.00 26.00 ? 1174 ARG A N     1 
ATOM   8552  C  CA    . ARG A 1  1176 ? 5.443   86.955  118.695 1.00 24.74 ? 1174 ARG A CA    1 
ATOM   8553  C  C     . ARG A 1  1176 ? 5.832   87.882  117.553 1.00 24.06 ? 1174 ARG A C     1 
ATOM   8554  O  O     . ARG A 1  1176 ? 4.984   88.268  116.738 1.00 26.30 ? 1174 ARG A O     1 
ATOM   8555  C  CB    . ARG A 1  1176 ? 5.366   87.720  120.020 1.00 22.41 ? 1174 ARG A CB    1 
ATOM   8556  C  CG    . ARG A 1  1176 ? 4.128   88.598  120.121 1.00 30.10 ? 1174 ARG A CG    1 
ATOM   8557  C  CD    . ARG A 1  1176 ? 4.189   89.556  121.305 1.00 30.23 ? 1174 ARG A CD    1 
ATOM   8558  N  NE    . ARG A 1  1176 ? 4.480   88.864  122.554 1.00 34.40 ? 1174 ARG A NE    1 
ATOM   8559  C  CZ    . ARG A 1  1176 ? 3.558   88.371  123.371 1.00 38.42 ? 1174 ARG A CZ    1 
ATOM   8560  N  NH1   . ARG A 1  1176 ? 2.270   88.448  123.084 1.00 33.79 ? 1174 ARG A NH1   1 
ATOM   8561  N  NH2   . ARG A 1  1176 ? 3.939   87.799  124.511 1.00 39.51 ? 1174 ARG A NH2   1 
ATOM   8562  N  N     . ALA A 1  1177 ? 7.120   88.200  117.446 1.00 25.84 ? 1175 ALA A N     1 
ATOM   8563  C  CA    . ALA A 1  1177 ? 7.589   89.105  116.403 1.00 26.28 ? 1175 ALA A CA    1 
ATOM   8564  C  C     . ALA A 1  1177 ? 7.399   88.491  115.027 1.00 25.60 ? 1175 ALA A C     1 
ATOM   8565  O  O     . ALA A 1  1177 ? 6.923   89.156  114.098 1.00 26.84 ? 1175 ALA A O     1 
ATOM   8566  C  CB    . ALA A 1  1177 ? 9.062   89.450  116.632 1.00 23.00 ? 1175 ALA A CB    1 
ATOM   8567  N  N     . VAL A 1  1178 ? 7.774   87.221  114.880 1.00 23.14 ? 1176 VAL A N     1 
ATOM   8568  C  CA    . VAL A 1  1178 ? 7.633   86.554  113.588 1.00 21.74 ? 1176 VAL A CA    1 
ATOM   8569  C  C     . VAL A 1  1178 ? 6.168   86.478  113.198 1.00 24.74 ? 1176 VAL A C     1 
ATOM   8570  O  O     . VAL A 1  1178 ? 5.807   86.717  112.040 1.00 23.82 ? 1176 VAL A O     1 
ATOM   8571  C  CB    . VAL A 1  1178 ? 8.279   85.156  113.618 1.00 22.70 ? 1176 VAL A CB    1 
ATOM   8572  C  CG1   . VAL A 1  1178 ? 7.913   84.386  112.350 1.00 20.28 ? 1176 VAL A CG1   1 
ATOM   8573  C  CG2   . VAL A 1  1178 ? 9.785   85.265  113.739 1.00 22.56 ? 1176 VAL A CG2   1 
ATOM   8574  N  N     . ASN A 1  1179 ? 5.303   86.157  114.163 1.00 24.52 ? 1177 ASN A N     1 
ATOM   8575  C  CA    . ASN A 1  1179 ? 3.874   86.044  113.887 1.00 24.10 ? 1177 ASN A CA    1 
ATOM   8576  C  C     . ASN A 1  1179 ? 3.295   87.374  113.408 1.00 26.51 ? 1177 ASN A C     1 
ATOM   8577  O  O     . ASN A 1  1179 ? 2.433   87.397  112.521 1.00 25.76 ? 1177 ASN A O     1 
ATOM   8578  C  CB    . ASN A 1  1179 ? 3.155   85.545  115.144 1.00 27.69 ? 1177 ASN A CB    1 
ATOM   8579  C  CG    . ASN A 1  1179 ? 1.876   84.783  114.840 1.00 31.12 ? 1177 ASN A CG    1 
ATOM   8580  O  OD1   . ASN A 1  1179 ? 1.681   84.274  113.730 1.00 33.65 ? 1177 ASN A OD1   1 
ATOM   8581  N  ND2   . ASN A 1  1179 ? 0.986   84.703  115.836 1.00 32.94 ? 1177 ASN A ND2   1 
ATOM   8582  N  N     . LYS A 1  1180 ? 3.762   88.491  113.973 1.00 24.70 ? 1178 LYS A N     1 
ATOM   8583  C  CA    . LYS A 1  1180 ? 3.340   89.804  113.490 1.00 24.69 ? 1178 LYS A CA    1 
ATOM   8584  C  C     . LYS A 1  1180 ? 3.795   90.032  112.050 1.00 27.13 ? 1178 LYS A C     1 
ATOM   8585  O  O     . LYS A 1  1180 ? 3.011   90.476  111.200 1.00 26.13 ? 1178 LYS A O     1 
ATOM   8586  C  CB    . LYS A 1  1180 ? 3.873   90.897  114.422 1.00 28.71 ? 1178 LYS A CB    1 
ATOM   8587  C  CG    . LYS A 1  1180 ? 3.133   90.932  115.751 1.00 30.17 ? 1178 LYS A CG    1 
ATOM   8588  C  CD    . LYS A 1  1180 ? 3.892   91.712  116.823 1.00 26.61 ? 1178 LYS A CD    1 
ATOM   8589  C  CE    . LYS A 1  1180 ? 4.173   93.159  116.404 1.00 35.18 ? 1178 LYS A CE    1 
ATOM   8590  N  NZ    . LYS A 1  1180 ? 4.947   93.914  117.442 1.00 41.32 ? 1178 LYS A NZ    1 
ATOM   8591  N  N     . ALA A 1  1181 ? 5.056   89.702  111.752 1.00 24.50 ? 1179 ALA A N     1 
ATOM   8592  C  CA    . ALA A 1  1181 ? 5.558   89.807  110.383 1.00 24.25 ? 1179 ALA A CA    1 
ATOM   8593  C  C     . ALA A 1  1181 ? 4.783   88.911  109.428 1.00 22.74 ? 1179 ALA A C     1 
ATOM   8594  O  O     . ALA A 1  1181 ? 4.488   89.310  108.298 1.00 23.15 ? 1179 ALA A O     1 
ATOM   8595  C  CB    . ALA A 1  1181 ? 7.039   89.449  110.333 1.00 22.08 ? 1179 ALA A CB    1 
ATOM   8596  N  N     . ILE A 1  1182 ? 4.464   87.688  109.850 1.00 23.72 ? 1180 ILE A N     1 
ATOM   8597  C  CA    . ILE A 1  1182 ? 3.750   86.779  108.958 1.00 22.22 ? 1180 ILE A CA    1 
ATOM   8598  C  C     . ILE A 1  1182 ? 2.346   87.294  108.689 1.00 22.80 ? 1180 ILE A C     1 
ATOM   8599  O  O     . ILE A 1  1182 ? 1.859   87.247  107.551 1.00 23.39 ? 1180 ILE A O     1 
ATOM   8600  C  CB    . ILE A 1  1182 ? 3.725   85.359  109.546 1.00 19.80 ? 1180 ILE A CB    1 
ATOM   8601  C  CG1   . ILE A 1  1182 ? 5.130   84.767  109.520 1.00 22.79 ? 1180 ILE A CG1   1 
ATOM   8602  C  CG2   . ILE A 1  1182 ? 2.738   84.492  108.779 1.00 24.51 ? 1180 ILE A CG2   1 
ATOM   8603  C  CD1   . ILE A 1  1182 ? 5.232   83.388  110.149 1.00 23.66 ? 1180 ILE A CD1   1 
ATOM   8604  N  N     . ALA A 1  1183 ? 1.668   87.789  109.727 1.00 22.03 ? 1181 ALA A N     1 
ATOM   8605  C  CA    . ALA A 1  1183 ? 0.309   88.283  109.543 1.00 22.66 ? 1181 ALA A CA    1 
ATOM   8606  C  C     . ALA A 1  1183 ? 0.283   89.452  108.574 1.00 26.25 ? 1181 ALA A C     1 
ATOM   8607  O  O     . ALA A 1  1183 ? -0.723  89.665  107.888 1.00 22.88 ? 1181 ALA A O     1 
ATOM   8608  C  CB    . ALA A 1  1183 ? -0.303  88.687  110.886 1.00 24.36 ? 1181 ALA A CB    1 
ATOM   8609  N  N     . ALA A 1  1184 ? 1.393   90.194  108.477 1.00 24.64 ? 1182 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1  1184 ? 1.475   91.350  107.590 1.00 25.91 ? 1182 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1  1184 ? 1.735   90.970  106.140 1.00 25.55 ? 1182 ALA A C     1 
ATOM   8612  O  O     . ALA A 1  1184 ? 1.670   91.846  105.271 1.00 25.08 ? 1182 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1  1184 ? 2.574   92.312  108.063 1.00 26.31 ? 1182 ALA A CB    1 
ATOM   8614  N  N     . LEU A 1  1185 ? 2.039   89.708  105.857 1.00 22.58 ? 1183 LEU A N     1 
ATOM   8615  C  CA    . LEU A 1  1185 ? 2.265   89.313  104.477 1.00 24.78 ? 1183 LEU A CA    1 
ATOM   8616  C  C     . LEU A 1  1185 ? 0.969   89.457  103.686 1.00 24.90 ? 1183 LEU A C     1 
ATOM   8617  O  O     . LEU A 1  1185 ? -0.115  89.173  104.209 1.00 22.91 ? 1183 LEU A O     1 
ATOM   8618  C  CB    . LEU A 1  1185 ? 2.772   87.875  104.395 1.00 21.44 ? 1183 LEU A CB    1 
ATOM   8619  C  CG    . LEU A 1  1185 ? 4.076   87.579  105.130 1.00 22.34 ? 1183 LEU A CG    1 
ATOM   8620  C  CD1   . LEU A 1  1185 ? 4.393   86.088  105.092 1.00 23.48 ? 1183 LEU A CD1   1 
ATOM   8621  C  CD2   . LEU A 1  1185 ? 5.204   88.403  104.528 1.00 25.11 ? 1183 LEU A CD2   1 
ATOM   8622  N  N     . PRO A 1  1186 ? 1.041   89.905  102.434 1.00 25.72 ? 1184 PRO A N     1 
ATOM   8623  C  CA    . PRO A 1  1186 ? -0.180  90.029  101.632 1.00 22.11 ? 1184 PRO A CA    1 
ATOM   8624  C  C     . PRO A 1  1186 ? -0.780  88.667  101.330 1.00 20.72 ? 1184 PRO A C     1 
ATOM   8625  O  O     . PRO A 1  1186 ? -0.086  87.651  101.298 1.00 22.68 ? 1184 PRO A O     1 
ATOM   8626  C  CB    . PRO A 1  1186 ? 0.309   90.703  100.346 1.00 26.89 ? 1184 PRO A CB    1 
ATOM   8627  C  CG    . PRO A 1  1186 ? 1.750   90.273  100.242 1.00 29.75 ? 1184 PRO A CG    1 
ATOM   8628  C  CD    . PRO A 1  1186 ? 2.252   90.225  101.662 1.00 26.71 ? 1184 PRO A CD    1 
ATOM   8629  N  N     . GLY A 1  1187 ? -2.088  88.661  101.097 1.00 21.71 ? 1185 GLY A N     1 
ATOM   8630  C  CA    . GLY A 1  1187 ? -2.737  87.485  100.568 1.00 24.92 ? 1185 GLY A CA    1 
ATOM   8631  C  C     . GLY A 1  1187 ? -3.340  86.580  101.623 1.00 20.01 ? 1185 GLY A C     1 
ATOM   8632  O  O     . GLY A 1  1187 ? -4.063  87.027  102.521 1.00 22.01 ? 1185 GLY A O     1 
ATOM   8633  N  N     . PRO A 1  1188 ? -3.071  85.278  101.516 1.00 22.35 ? 1186 PRO A N     1 
ATOM   8634  C  CA    . PRO A 1  1188 ? -3.815  84.309  102.323 1.00 19.82 ? 1186 PRO A CA    1 
ATOM   8635  C  C     . PRO A 1  1188 ? -3.373  84.330  103.771 1.00 20.44 ? 1186 PRO A C     1 
ATOM   8636  O  O     . PRO A 1  1188 ? -2.218  84.630  104.094 1.00 19.50 ? 1186 PRO A O     1 
ATOM   8637  C  CB    . PRO A 1  1188 ? -3.483  82.964  101.666 1.00 21.29 ? 1186 PRO A CB    1 
ATOM   8638  C  CG    . PRO A 1  1188 ? -2.136  83.171  101.073 1.00 20.13 ? 1186 PRO A CG    1 
ATOM   8639  C  CD    . PRO A 1  1188 ? -2.071  84.633  100.654 1.00 20.30 ? 1186 PRO A CD    1 
ATOM   8640  N  N     . LEU A 1  1189 ? -4.320  84.027  104.649 1.00 20.40 ? 1187 LEU A N     1 
ATOM   8641  C  CA    . LEU A 1  1189 ? -3.969  83.768  106.034 1.00 17.73 ? 1187 LEU A CA    1 
ATOM   8642  C  C     . LEU A 1  1189 ? -3.134  82.500  106.090 1.00 20.80 ? 1187 LEU A C     1 
ATOM   8643  O  O     . LEU A 1  1189 ? -3.430  81.516  105.410 1.00 22.19 ? 1187 LEU A O     1 
ATOM   8644  C  CB    . LEU A 1  1189 ? -5.222  83.608  106.887 1.00 19.08 ? 1187 LEU A CB    1 
ATOM   8645  C  CG    . LEU A 1  1189 ? -5.928  84.894  107.337 1.00 20.88 ? 1187 LEU A CG    1 
ATOM   8646  C  CD1   . LEU A 1  1189 ? -6.642  85.604  106.184 1.00 19.89 ? 1187 LEU A CD1   1 
ATOM   8647  C  CD2   . LEU A 1  1189 ? -6.907  84.566  108.433 1.00 25.86 ? 1187 LEU A CD2   1 
ATOM   8648  N  N     . LEU A 1  1190 ? -2.064  82.526  106.879 1.00 19.27 ? 1188 LEU A N     1 
ATOM   8649  C  CA    . LEU A 1  1190 ? -1.172  81.379  106.968 1.00 19.13 ? 1188 LEU A CA    1 
ATOM   8650  C  C     . LEU A 1  1190 ? -1.414  80.638  108.272 1.00 19.63 ? 1188 LEU A C     1 
ATOM   8651  O  O     . LEU A 1  1190 ? -1.462  81.252  109.342 1.00 20.64 ? 1188 LEU A O     1 
ATOM   8652  C  CB    . LEU A 1  1190 ? 0.297   81.799  106.877 1.00 20.78 ? 1188 LEU A CB    1 
ATOM   8653  C  CG    . LEU A 1  1190 ? 0.715   82.508  105.595 1.00 22.69 ? 1188 LEU A CG    1 
ATOM   8654  C  CD1   . LEU A 1  1190 ? 2.236   82.592  105.548 1.00 23.41 ? 1188 LEU A CD1   1 
ATOM   8655  C  CD2   . LEU A 1  1190 ? 0.175   81.753  104.376 1.00 21.50 ? 1188 LEU A CD2   1 
ATOM   8656  N  N     . LEU A 1  1191 ? -1.561  79.321  108.178 1.00 19.43 ? 1189 LEU A N     1 
ATOM   8657  C  CA    . LEU A 1  1191 ? -1.587  78.479  109.367 1.00 16.38 ? 1189 LEU A CA    1 
ATOM   8658  C  C     . LEU A 1  1191 ? -0.157  78.353  109.866 1.00 17.38 ? 1189 LEU A C     1 
ATOM   8659  O  O     . LEU A 1  1191 ? 0.675   77.690  109.232 1.00 19.32 ? 1189 LEU A O     1 
ATOM   8660  C  CB    . LEU A 1  1191 ? -2.191  77.117  109.052 1.00 16.76 ? 1189 LEU A CB    1 
ATOM   8661  C  CG    . LEU A 1  1191 ? -2.729  76.289  110.221 1.00 17.51 ? 1189 LEU A CG    1 
ATOM   8662  C  CD1   . LEU A 1  1191 ? -3.538  75.137  109.623 1.00 18.45 ? 1189 LEU A CD1   1 
ATOM   8663  C  CD2   . LEU A 1  1191 ? -1.601  75.753  111.110 1.00 17.44 ? 1189 LEU A CD2   1 
ATOM   8664  N  N     . VAL A 1  1192 ? 0.124   79.009  110.989 1.00 18.51 ? 1190 VAL A N     1 
ATOM   8665  C  CA    . VAL A 1  1192 ? 1.460   79.074  111.566 1.00 18.06 ? 1190 VAL A CA    1 
ATOM   8666  C  C     . VAL A 1  1192 ? 1.541   78.099  112.727 1.00 18.45 ? 1190 VAL A C     1 
ATOM   8667  O  O     . VAL A 1  1192 ? 0.657   78.075  113.594 1.00 20.49 ? 1190 VAL A O     1 
ATOM   8668  C  CB    . VAL A 1  1192 ? 1.786   80.498  112.047 1.00 21.93 ? 1190 VAL A CB    1 
ATOM   8669  C  CG1   . VAL A 1  1192 ? 3.243   80.571  112.543 1.00 20.88 ? 1190 VAL A CG1   1 
ATOM   8670  C  CG2   . VAL A 1  1192 ? 1.542   81.503  110.942 1.00 23.67 ? 1190 VAL A CG2   1 
ATOM   8671  N  N     . GLN A 1  1193 ? 2.626   77.329  112.775 1.00 19.46 ? 1191 GLN A N     1 
ATOM   8672  C  CA    . GLN A 1  1193 ? 2.981   76.539  113.943 1.00 16.45 ? 1191 GLN A CA    1 
ATOM   8673  C  C     . GLN A 1  1193 ? 4.323   77.007  114.470 1.00 19.30 ? 1191 GLN A C     1 
ATOM   8674  O  O     . GLN A 1  1193 ? 5.267   77.212  113.701 1.00 18.28 ? 1191 GLN A O     1 
ATOM   8675  C  CB    . GLN A 1  1193 ? 3.069   75.062  113.619 1.00 17.33 ? 1191 GLN A CB    1 
ATOM   8676  C  CG    . GLN A 1  1193 ? 1.803   74.488  113.017 1.00 18.46 ? 1191 GLN A CG    1 
ATOM   8677  C  CD    . GLN A 1  1193 ? 1.896   72.988  112.929 1.00 18.54 ? 1191 GLN A CD    1 
ATOM   8678  O  OE1   . GLN A 1  1193 ? 1.835   72.301  113.953 1.00 19.85 ? 1191 GLN A OE1   1 
ATOM   8679  N  NE2   . GLN A 1  1193 ? 2.070   72.469  111.718 1.00 20.06 ? 1191 GLN A NE2   1 
ATOM   8680  N  N     . ALA A 1  1194 ? 4.411   77.153  115.783 1.00 18.45 ? 1192 ALA A N     1 
ATOM   8681  C  CA    . ALA A 1  1194 ? 5.616   77.647  116.409 1.00 17.59 ? 1192 ALA A CA    1 
ATOM   8682  C  C     . ALA A 1  1194 ? 6.054   76.700  117.512 1.00 21.51 ? 1192 ALA A C     1 
ATOM   8683  O  O     . ALA A 1  1194 ? 5.232   76.035  118.147 1.00 20.66 ? 1192 ALA A O     1 
ATOM   8684  C  CB    . ALA A 1  1194 ? 5.386   79.040  116.982 1.00 17.82 ? 1192 ALA A CB    1 
ATOM   8685  N  N     . ALA A 1  1195 ? 7.361   76.674  117.753 1.00 19.12 ? 1193 ALA A N     1 
ATOM   8686  C  CA    . ALA A 1  1195 ? 7.929   75.847  118.805 1.00 19.65 ? 1193 ALA A CA    1 
ATOM   8687  C  C     . ALA A 1  1195 ? 9.232   76.478  119.260 1.00 21.52 ? 1193 ALA A C     1 
ATOM   8688  O  O     . ALA A 1  1195 ? 9.921   77.139  118.477 1.00 20.54 ? 1193 ALA A O     1 
ATOM   8689  C  CB    . ALA A 1  1195 ? 8.166   74.412  118.317 1.00 19.73 ? 1193 ALA A CB    1 
ATOM   8690  N  N     . SER A 1  1196 ? 9.571   76.268  120.527 1.00 19.58 ? 1194 SER A N     1 
ATOM   8691  C  CA    . SER A 1  1196 ? 10.890  76.653  120.994 1.00 23.10 ? 1194 SER A CA    1 
ATOM   8692  C  C     . SER A 1  1196 ? 11.916  75.611  120.569 1.00 20.07 ? 1194 SER A C     1 
ATOM   8693  O  O     . SER A 1  1196 ? 11.577  74.493  120.179 1.00 21.11 ? 1194 SER A O     1 
ATOM   8694  C  CB    . SER A 1  1196 ? 10.902  76.791  122.515 1.00 26.03 ? 1194 SER A CB    1 
ATOM   8695  O  OG    . SER A 1  1196 ? 10.668  75.527  123.115 1.00 23.23 ? 1194 SER A OG    1 
ATOM   8696  N  N     . SER A 1  1197 ? 13.192  75.984  120.656 1.00 18.89 ? 1195 SER A N     1 
ATOM   8697  C  CA    . SER A 1  1197 ? 14.239  75.005  120.390 1.00 20.81 ? 1195 SER A CA    1 
ATOM   8698  C  C     . SER A 1  1197 ? 14.122  73.819  121.338 1.00 21.32 ? 1195 SER A C     1 
ATOM   8699  O  O     . SER A 1  1197 ? 14.270  72.667  120.918 1.00 21.78 ? 1195 SER A O     1 
ATOM   8700  C  CB    . SER A 1  1197 ? 15.618  75.657  120.508 1.00 23.76 ? 1195 SER A CB    1 
ATOM   8701  O  OG    . SER A 1  1197 ? 15.752  76.720  119.577 1.00 23.17 ? 1195 SER A OG    1 
ATOM   8702  N  N     . GLY A 1  1198 ? 13.836  74.087  122.616 1.00 23.49 ? 1196 GLY A N     1 
ATOM   8703  C  CA    . GLY A 1  1198 ? 13.688  73.006  123.585 1.00 22.23 ? 1196 GLY A CA    1 
ATOM   8704  C  C     . GLY A 1  1198 ? 12.513  72.100  123.273 1.00 24.48 ? 1196 GLY A C     1 
ATOM   8705  O  O     . GLY A 1  1198 ? 12.592  70.878  123.432 1.00 22.19 ? 1196 GLY A O     1 
ATOM   8706  N  N     . GLU A 1  1199 ? 11.412  72.685  122.806 1.00 22.86 ? 1197 GLU A N     1 
ATOM   8707  C  CA    . GLU A 1  1199 ? 10.264  71.883  122.417 1.00 22.33 ? 1197 GLU A CA    1 
ATOM   8708  C  C     . GLU A 1  1199 ? 10.597  70.987  121.228 1.00 22.80 ? 1197 GLU A C     1 
ATOM   8709  O  O     . GLU A 1  1199 ? 10.218  69.810  121.199 1.00 21.47 ? 1197 GLU A O     1 
ATOM   8710  C  CB    . GLU A 1  1199 ? 9.099   72.817  122.105 1.00 22.11 ? 1197 GLU A CB    1 
ATOM   8711  C  CG    . GLU A 1  1199 ? 7.804   72.162  121.772 1.00 27.12 ? 1197 GLU A CG    1 
ATOM   8712  C  CD    . GLU A 1  1199 ? 6.692   73.193  121.690 1.00 32.90 ? 1197 GLU A CD    1 
ATOM   8713  O  OE1   . GLU A 1  1199 ? 7.014   74.409  121.772 1.00 32.03 ? 1197 GLU A OE1   1 
ATOM   8714  O  OE2   . GLU A 1  1199 ? 5.513   72.793  121.569 1.00 38.61 ? 1197 GLU A OE2   1 
ATOM   8715  N  N     . ILE A 1  1200 ? 11.315  71.522  120.239 1.00 21.45 ? 1198 ILE A N     1 
ATOM   8716  C  CA    . ILE A 1  1200 ? 11.736  70.700  119.108 1.00 19.43 ? 1198 ILE A CA    1 
ATOM   8717  C  C     . ILE A 1  1200 ? 12.579  69.524  119.589 1.00 23.19 ? 1198 ILE A C     1 
ATOM   8718  O  O     . ILE A 1  1200 ? 12.433  68.395  119.103 1.00 21.04 ? 1198 ILE A O     1 
ATOM   8719  C  CB    . ILE A 1  1200 ? 12.488  71.563  118.077 1.00 19.97 ? 1198 ILE A CB    1 
ATOM   8720  C  CG1   . ILE A 1  1200 ? 11.517  72.557  117.426 1.00 19.98 ? 1198 ILE A CG1   1 
ATOM   8721  C  CG2   . ILE A 1  1200 ? 13.159  70.684  117.006 1.00 19.90 ? 1198 ILE A CG2   1 
ATOM   8722  C  CD1   . ILE A 1  1200 ? 12.184  73.599  116.526 1.00 21.45 ? 1198 ILE A CD1   1 
ATOM   8723  N  N     . ALA A 1  1201 ? 13.446  69.759  120.582 1.00 20.72 ? 1199 ALA A N     1 
ATOM   8724  C  CA    . ALA A 1  1201 ? 14.293  68.685  121.088 1.00 21.51 ? 1199 ALA A CA    1 
ATOM   8725  C  C     . ALA A 1  1201 ? 13.487  67.651  121.866 1.00 22.00 ? 1199 ALA A C     1 
ATOM   8726  O  O     . ALA A 1  1201 ? 13.788  66.453  121.810 1.00 22.38 ? 1199 ALA A O     1 
ATOM   8727  C  CB    . ALA A 1  1201 ? 15.402  69.263  121.971 1.00 21.64 ? 1199 ALA A CB    1 
ATOM   8728  N  N     . ARG A 1  1202 ? 12.469  68.095  122.605 1.00 21.93 ? 1200 ARG A N     1 
ATOM   8729  C  CA    . ARG A 1  1202 ? 11.723  67.202  123.484 1.00 21.88 ? 1200 ARG A CA    1 
ATOM   8730  C  C     . ARG A 1  1202 ? 10.590  66.480  122.775 1.00 24.26 ? 1200 ARG A C     1 
ATOM   8731  O  O     . ARG A 1  1202 ? 10.328  65.308  123.067 1.00 24.85 ? 1200 ARG A O     1 
ATOM   8732  C  CB    . ARG A 1  1202 ? 11.154  67.975  124.680 1.00 21.71 ? 1200 ARG A CB    1 
ATOM   8733  C  CG    . ARG A 1  1202 ? 12.208  68.406  125.692 1.00 22.37 ? 1200 ARG A CG    1 
ATOM   8734  C  CD    . ARG A 1  1202 ? 11.559  69.032  126.928 1.00 24.84 ? 1200 ARG A CD    1 
ATOM   8735  N  NE    . ARG A 1  1202 ? 10.717  70.155  126.544 1.00 26.04 ? 1200 ARG A NE    1 
ATOM   8736  C  CZ    . ARG A 1  1202 ? 11.105  71.424  126.530 1.00 27.50 ? 1200 ARG A CZ    1 
ATOM   8737  N  NH1   . ARG A 1  1202 ? 12.272  71.802  127.038 1.00 25.97 ? 1200 ARG A NH1   1 
ATOM   8738  N  NH2   . ARG A 1  1202 ? 10.302  72.337  125.989 1.00 26.60 ? 1200 ARG A NH2   1 
ATOM   8739  N  N     . ASN A 1  1203 ? 9.907   67.148  121.856 1.00 20.83 ? 1201 ASN A N     1 
ATOM   8740  C  CA    . ASN A 1  1203 ? 8.651   66.631  121.318 1.00 22.30 ? 1201 ASN A CA    1 
ATOM   8741  C  C     . ASN A 1  1203 ? 8.765   66.362  119.826 1.00 24.06 ? 1201 ASN A C     1 
ATOM   8742  O  O     . ASN A 1  1203 ? 8.810   67.316  119.025 1.00 21.33 ? 1201 ASN A O     1 
ATOM   8743  C  CB    . ASN A 1  1203 ? 7.513   67.610  121.592 1.00 23.08 ? 1201 ASN A CB    1 
ATOM   8744  C  CG    . ASN A 1  1203 ? 6.183   67.107  121.065 1.00 24.49 ? 1201 ASN A CG    1 
ATOM   8745  O  OD1   . ASN A 1  1203 ? 6.067   65.946  120.659 1.00 25.23 ? 1201 ASN A OD1   1 
ATOM   8746  N  ND2   . ASN A 1  1203 ? 5.177   67.974  121.064 1.00 25.61 ? 1201 ASN A ND2   1 
ATOM   8747  N  N     . PRO A 1  1204 ? 8.785   65.098  119.402 1.00 24.58 ? 1202 PRO A N     1 
ATOM   8748  C  CA    . PRO A 1  1204 ? 8.836   64.812  117.962 1.00 24.71 ? 1202 PRO A CA    1 
ATOM   8749  C  C     . PRO A 1  1204 ? 7.684   65.423  117.190 1.00 24.81 ? 1202 PRO A C     1 
ATOM   8750  O  O     . PRO A 1  1204 ? 7.828   65.669  115.990 1.00 25.02 ? 1202 PRO A O     1 
ATOM   8751  C  CB    . PRO A 1  1204 ? 8.794   63.279  117.910 1.00 28.84 ? 1202 PRO A CB    1 
ATOM   8752  C  CG    . PRO A 1  1204 ? 9.361   62.847  119.231 1.00 30.55 ? 1202 PRO A CG    1 
ATOM   8753  C  CD    . PRO A 1  1204 ? 8.841   63.871  120.216 1.00 28.43 ? 1202 PRO A CD    1 
ATOM   8754  N  N     . ASP A 1  1205 ? 6.556   65.693  117.845 1.00 24.33 ? 1203 ASP A N     1 
ATOM   8755  C  CA    . ASP A 1  1205 ? 5.401   66.310  117.206 1.00 24.23 ? 1203 ASP A CA    1 
ATOM   8756  C  C     . ASP A 1  1205 ? 5.308   67.809  117.485 1.00 23.82 ? 1203 ASP A C     1 
ATOM   8757  O  O     . ASP A 1  1205 ? 4.212   68.379  117.413 1.00 26.24 ? 1203 ASP A O     1 
ATOM   8758  C  CB    . ASP A 1  1205 ? 4.118   65.613  117.664 1.00 27.13 ? 1203 ASP A CB    1 
ATOM   8759  C  CG    . ASP A 1  1205 ? 4.091   64.134  117.314 1.00 28.31 ? 1203 ASP A CG    1 
ATOM   8760  O  OD1   . ASP A 1  1205 ? 4.811   63.713  116.386 1.00 27.21 ? 1203 ASP A OD1   1 
ATOM   8761  O  OD2   . ASP A 1  1205 ? 3.342   63.393  117.981 1.00 33.05 ? 1203 ASP A OD2   1 
ATOM   8762  N  N     . ALA A 1  1206 ? 6.430   68.450  117.822 1.00 21.95 ? 1204 ALA A N     1 
ATOM   8763  C  CA    . ALA A 1  1206 ? 6.444   69.895  118.042 1.00 23.70 ? 1204 ALA A CA    1 
ATOM   8764  C  C     . ALA A 1  1206 ? 5.733   70.629  116.914 1.00 21.28 ? 1204 ALA A C     1 
ATOM   8765  O  O     . ALA A 1  1206 ? 4.909   71.521  117.154 1.00 24.58 ? 1204 ALA A O     1 
ATOM   8766  C  CB    . ALA A 1  1206 ? 7.885   70.384  118.171 1.00 21.83 ? 1204 ALA A CB    1 
ATOM   8767  N  N     . TYR A 1  1207 ? 6.036   70.260  115.672 1.00 20.58 ? 1205 TYR A N     1 
ATOM   8768  C  CA    . TYR A 1  1207 ? 5.260   70.684  114.512 1.00 21.49 ? 1205 TYR A CA    1 
ATOM   8769  C  C     . TYR A 1  1207 ? 4.360   69.532  114.086 1.00 21.05 ? 1205 TYR A C     1 
ATOM   8770  O  O     . TYR A 1  1207 ? 4.849   68.442  113.778 1.00 24.70 ? 1205 TYR A O     1 
ATOM   8771  C  CB    . TYR A 1  1207 ? 6.178   71.111  113.366 1.00 18.98 ? 1205 TYR A CB    1 
ATOM   8772  C  CG    . TYR A 1  1207 ? 7.132   72.221  113.750 1.00 19.16 ? 1205 TYR A CG    1 
ATOM   8773  C  CD1   . TYR A 1  1207 ? 6.647   73.483  114.119 1.00 21.32 ? 1205 TYR A CD1   1 
ATOM   8774  C  CD2   . TYR A 1  1207 ? 8.513   72.018  113.752 1.00 19.77 ? 1205 TYR A CD2   1 
ATOM   8775  C  CE1   . TYR A 1  1207 ? 7.507   74.507  114.471 1.00 20.07 ? 1205 TYR A CE1   1 
ATOM   8776  C  CE2   . TYR A 1  1207 ? 9.380   73.049  114.112 1.00 19.52 ? 1205 TYR A CE2   1 
ATOM   8777  C  CZ    . TYR A 1  1207 ? 8.865   74.287  114.460 1.00 19.05 ? 1205 TYR A CZ    1 
ATOM   8778  O  OH    . TYR A 1  1207 ? 9.697   75.312  114.819 1.00 19.70 ? 1205 TYR A OH    1 
ATOM   8779  N  N     . CYS A 1  1208 ? 3.055   69.768  114.070 1.00 20.08 ? 1206 CYS A N     1 
ATOM   8780  C  CA    . CYS A 1  1208 ? 2.103   68.703  113.799 1.00 20.80 ? 1206 CYS A CA    1 
ATOM   8781  C  C     . CYS A 1  1208 ? 1.884   68.574  112.296 1.00 20.39 ? 1206 CYS A C     1 
ATOM   8782  O  O     . CYS A 1  1208 ? 1.603   69.560  111.611 1.00 18.86 ? 1206 CYS A O     1 
ATOM   8783  C  CB    . CYS A 1  1208 ? 0.789   68.967  114.540 1.00 23.26 ? 1206 CYS A CB    1 
ATOM   8784  S  SG    . CYS A 1  1208 ? -0.516  67.769  114.182 1.00 24.32 ? 1206 CYS A SG    1 
ATOM   8785  N  N     . LEU A 1  1209 ? 2.053   67.361  111.777 1.00 18.20 ? 1207 LEU A N     1 
ATOM   8786  C  CA    . LEU A 1  1209 ? 1.973   67.179  110.338 1.00 16.14 ? 1207 LEU A CA    1 
ATOM   8787  C  C     . LEU A 1  1209 ? 0.546   67.288  109.810 1.00 14.49 ? 1207 LEU A C     1 
ATOM   8788  O  O     . LEU A 1  1209 ? 0.380   67.439  108.596 1.00 16.09 ? 1207 LEU A O     1 
ATOM   8789  C  CB    . LEU A 1  1209 ? 2.581   65.826  109.944 1.00 16.67 ? 1207 LEU A CB    1 
ATOM   8790  C  CG    . LEU A 1  1209 ? 4.016   65.586  110.406 1.00 16.13 ? 1207 LEU A CG    1 
ATOM   8791  C  CD1   . LEU A 1  1209 ? 4.508   64.243  109.892 1.00 17.72 ? 1207 LEU A CD1   1 
ATOM   8792  C  CD2   . LEU A 1  1209 ? 4.929   66.696  109.921 1.00 16.69 ? 1207 LEU A CD2   1 
ATOM   8793  N  N     . ASN A 1  1210 ? -0.471  67.233  110.686 1.00 18.02 ? 1208 ASN A N     1 
ATOM   8794  C  CA    . ASN A 1  1210 ? -1.857  67.409  110.248 1.00 18.59 ? 1208 ASN A CA    1 
ATOM   8795  C  C     . ASN A 1  1210 ? -2.036  68.715  109.495 1.00 17.21 ? 1208 ASN A C     1 
ATOM   8796  O  O     . ASN A 1  1210 ? -2.839  68.798  108.559 1.00 18.28 ? 1208 ASN A O     1 
ATOM   8797  C  CB    . ASN A 1  1210 ? -2.833  67.423  111.433 1.00 20.00 ? 1208 ASN A CB    1 
ATOM   8798  C  CG    . ASN A 1  1210 ? -2.941  66.090  112.156 1.00 23.23 ? 1208 ASN A CG    1 
ATOM   8799  O  OD1   . ASN A 1  1210 ? -2.097  65.206  112.022 1.00 27.16 ? 1208 ASN A OD1   1 
ATOM   8800  N  ND2   . ASN A 1  1210 ? -3.986  65.966  112.974 1.00 28.31 ? 1208 ASN A ND2   1 
ATOM   8801  N  N     . TRP A 1  1211 ? -1.331  69.762  109.918 1.00 15.88 ? 1209 TRP A N     1 
ATOM   8802  C  CA    . TRP A 1  1211 ? -1.574  71.098  109.395 1.00 16.53 ? 1209 TRP A CA    1 
ATOM   8803  C  C     . TRP A 1  1211 ? -0.619  71.465  108.274 1.00 19.01 ? 1209 TRP A C     1 
ATOM   8804  O  O     . TRP A 1  1211 ? -0.643  72.608  107.810 1.00 20.06 ? 1209 TRP A O     1 
ATOM   8805  C  CB    . TRP A 1  1211 ? -1.495  72.137  110.527 1.00 18.30 ? 1209 TRP A CB    1 
ATOM   8806  C  CG    . TRP A 1  1211 ? -2.069  71.631  111.808 1.00 17.13 ? 1209 TRP A CG    1 
ATOM   8807  C  CD1   . TRP A 1  1211 ? -1.439  71.568  113.024 1.00 19.05 ? 1209 TRP A CD1   1 
ATOM   8808  C  CD2   . TRP A 1  1211 ? -3.366  71.053  112.000 1.00 18.05 ? 1209 TRP A CD2   1 
ATOM   8809  N  NE1   . TRP A 1  1211 ? -2.280  71.017  113.966 1.00 20.89 ? 1209 TRP A NE1   1 
ATOM   8810  C  CE2   . TRP A 1  1211 ? -3.466  70.689  113.360 1.00 18.58 ? 1209 TRP A CE2   1 
ATOM   8811  C  CE3   . TRP A 1  1211 ? -4.463  70.820  111.156 1.00 19.09 ? 1209 TRP A CE3   1 
ATOM   8812  C  CZ2   . TRP A 1  1211 ? -4.614  70.106  113.900 1.00 18.93 ? 1209 TRP A CZ2   1 
ATOM   8813  C  CZ3   . TRP A 1  1211 ? -5.608  70.243  111.697 1.00 20.77 ? 1209 TRP A CZ3   1 
ATOM   8814  C  CH2   . TRP A 1  1211 ? -5.668  69.885  113.049 1.00 19.83 ? 1209 TRP A CH2   1 
ATOM   8815  N  N     . LEU A 1  1212 ? 0.212   70.524  107.830 1.00 16.23 ? 1210 LEU A N     1 
ATOM   8816  C  CA    . LEU A 1  1212 ? 1.136   70.714  106.720 1.00 16.28 ? 1210 LEU A CA    1 
ATOM   8817  C  C     . LEU A 1  1212 ? 0.679   69.999  105.453 1.00 15.49 ? 1210 LEU A C     1 
ATOM   8818  O  O     . LEU A 1  1212 ? 1.373   70.052  104.430 1.00 15.10 ? 1210 LEU A O     1 
ATOM   8819  C  CB    . LEU A 1  1212 ? 2.536   70.236  107.126 1.00 13.91 ? 1210 LEU A CB    1 
ATOM   8820  C  CG    . LEU A 1  1212 ? 3.202   71.208  108.092 1.00 14.77 ? 1210 LEU A CG    1 
ATOM   8821  C  CD1   . LEU A 1  1212 ? 4.384   70.561  108.828 1.00 17.43 ? 1210 LEU A CD1   1 
ATOM   8822  C  CD2   . LEU A 1  1212 ? 3.656   72.443  107.314 1.00 16.27 ? 1210 LEU A CD2   1 
ATOM   8823  N  N     . VAL A 1  1213 ? -0.470  69.330  105.501 1.00 16.21 ? 1211 VAL A N     1 
ATOM   8824  C  CA    . VAL A 1  1213 ? -1.097  68.782  104.311 1.00 14.60 ? 1211 VAL A CA    1 
ATOM   8825  C  C     . VAL A 1  1213 ? -2.358  69.575  104.056 1.00 14.91 ? 1211 VAL A C     1 
ATOM   8826  O  O     . VAL A 1  1213 ? -2.888  70.271  104.930 1.00 16.11 ? 1211 VAL A O     1 
ATOM   8827  C  CB    . VAL A 1  1213 ? -1.434  67.282  104.433 1.00 15.77 ? 1211 VAL A CB    1 
ATOM   8828  C  CG1   . VAL A 1  1213 ? -0.155  66.436  104.503 1.00 15.88 ? 1211 VAL A CG1   1 
ATOM   8829  C  CG2   . VAL A 1  1213 ? -2.344  67.018  105.629 1.00 15.64 ? 1211 VAL A CG2   1 
ATOM   8830  N  N     . GLU A 1  1214 ? -2.855  69.434  102.839 1.00 16.54 ? 1212 GLU A N     1 
ATOM   8831  C  CA    . GLU A 1  1214 ? -4.057  70.104  102.382 1.00 19.92 ? 1212 GLU A CA    1 
ATOM   8832  C  C     . GLU A 1  1214 ? -5.092  69.050  102.035 1.00 13.80 ? 1212 GLU A C     1 
ATOM   8833  O  O     . GLU A 1  1214 ? -4.805  68.109  101.286 1.00 14.84 ? 1212 GLU A O     1 
ATOM   8834  C  CB    . GLU A 1  1214 ? -3.718  70.959  101.173 1.00 20.91 ? 1212 GLU A CB    1 
ATOM   8835  C  CG    . GLU A 1  1214 ? -4.848  71.687  100.529 1.00 25.92 ? 1212 GLU A CG    1 
ATOM   8836  C  CD    . GLU A 1  1214 ? -4.302  72.641  99.494  1.00 24.50 ? 1212 GLU A CD    1 
ATOM   8837  O  OE1   . GLU A 1  1214 ? -3.663  73.636  99.903  1.00 30.69 ? 1212 GLU A OE1   1 
ATOM   8838  O  OE2   . GLU A 1  1214 ? -4.472  72.370  98.296  1.00 28.51 ? 1212 GLU A OE2   1 
ATOM   8839  N  N     . GLU A 1  1215 ? -6.290  69.201  102.583 1.00 14.22 ? 1213 GLU A N     1 
ATOM   8840  C  CA    . GLU A 1  1215 ? -7.374  68.291  102.260 1.00 15.26 ? 1213 GLU A CA    1 
ATOM   8841  C  C     . GLU A 1  1215 ? -8.039  68.699  100.956 1.00 15.43 ? 1213 GLU A C     1 
ATOM   8842  O  O     . GLU A 1  1215 ? -8.281  69.886  100.709 1.00 14.62 ? 1213 GLU A O     1 
ATOM   8843  C  CB    . GLU A 1  1215 ? -8.422  68.320  103.361 1.00 13.82 ? 1213 GLU A CB    1 
ATOM   8844  C  CG    . GLU A 1  1215 ? -7.923  67.901  104.724 1.00 14.92 ? 1213 GLU A CG    1 
ATOM   8845  C  CD    . GLU A 1  1215 ? -8.904  68.304  105.790 1.00 14.00 ? 1213 GLU A CD    1 
ATOM   8846  O  OE1   . GLU A 1  1215 ? -8.907  69.500  106.172 1.00 15.22 ? 1213 GLU A OE1   1 
ATOM   8847  O  OE2   . GLU A 1  1215 ? -9.676  67.430  106.224 1.00 16.39 ? 1213 GLU A OE2   1 
ATOM   8848  N  N     . VAL A 1  1216 ? -8.365  67.712  100.132 1.00 13.89 ? 1214 VAL A N     1 
ATOM   8849  C  CA    . VAL A 1  1216 ? -9.126  67.956  98.912  1.00 15.39 ? 1214 VAL A CA    1 
ATOM   8850  C  C     . VAL A 1  1216 ? -10.291 66.982  98.874  1.00 15.03 ? 1214 VAL A C     1 
ATOM   8851  O  O     . VAL A 1  1216 ? -10.108 65.779  99.065  1.00 15.21 ? 1214 VAL A O     1 
ATOM   8852  C  CB    . VAL A 1  1216 ? -8.263  67.813  97.652  1.00 15.55 ? 1214 VAL A CB    1 
ATOM   8853  C  CG1   . VAL A 1  1216 ? -9.133  67.960  96.414  1.00 16.58 ? 1214 VAL A CG1   1 
ATOM   8854  C  CG2   . VAL A 1  1216 ? -7.178  68.854  97.643  1.00 16.58 ? 1214 VAL A CG2   1 
ATOM   8855  N  N     . SER A 1  1217 ? -11.489 67.506  98.661  1.00 14.69 ? 1215 SER A N     1 
ATOM   8856  C  CA    . SER A 1  1217 ? -12.689 66.705  98.479  1.00 14.07 ? 1215 SER A CA    1 
ATOM   8857  C  C     . SER A 1  1217 ? -13.078 66.747  97.007  1.00 13.79 ? 1215 SER A C     1 
ATOM   8858  O  O     . SER A 1  1217 ? -13.033 67.809  96.381  1.00 14.64 ? 1215 SER A O     1 
ATOM   8859  C  CB    . SER A 1  1217 ? -13.833 67.251  99.328  1.00 15.46 ? 1215 SER A CB    1 
ATOM   8860  O  OG    . SER A 1  1217 ? -15.087 66.758  98.876  1.00 17.76 ? 1215 SER A OG    1 
ATOM   8861  N  N     . ALA A 1  1218 ? -13.436 65.597  96.447  1.00 15.28 ? 1216 ALA A N     1 
ATOM   8862  C  CA    . ALA A 1  1218 ? -13.934 65.559  95.074  1.00 15.00 ? 1216 ALA A CA    1 
ATOM   8863  C  C     . ALA A 1  1218 ? -15.210 64.734  95.028  1.00 14.19 ? 1216 ALA A C     1 
ATOM   8864  O  O     . ALA A 1  1218 ? -15.235 63.598  95.505  1.00 15.16 ? 1216 ALA A O     1 
ATOM   8865  C  CB    . ALA A 1  1218 ? -12.900 64.972  94.115  1.00 15.50 ? 1216 ALA A CB    1 
ATOM   8866  N  N     . SER A 1  1219 ? -16.264 65.301  94.452  1.00 14.82 ? 1217 SER A N     1 
ATOM   8867  C  CA    . SER A 1  1219 ? -17.535 64.607  94.316  1.00 14.81 ? 1217 SER A CA    1 
ATOM   8868  C  C     . SER A 1  1219 ? -17.848 64.459  92.839  1.00 13.08 ? 1217 SER A C     1 
ATOM   8869  O  O     . SER A 1  1219 ? -18.017 65.462  92.135  1.00 14.61 ? 1217 SER A O     1 
ATOM   8870  C  CB    . SER A 1  1219 ? -18.659 65.367  95.021  1.00 16.07 ? 1217 SER A CB    1 
ATOM   8871  O  OG    . SER A 1  1219 ? -19.877 64.654  94.915  1.00 15.51 ? 1217 SER A OG    1 
ATOM   8872  N  N     . ILE A 1  1220 ? -17.946 63.219  92.391  1.00 14.31 ? 1218 ILE A N     1 
ATOM   8873  C  CA    . ILE A 1  1220 ? -18.154 62.876  90.990  1.00 14.53 ? 1218 ILE A CA    1 
ATOM   8874  C  C     . ILE A 1  1220 ? -19.554 62.295  90.856  1.00 13.47 ? 1218 ILE A C     1 
ATOM   8875  O  O     . ILE A 1  1220 ? -19.876 61.289  91.498  1.00 15.74 ? 1218 ILE A O     1 
ATOM   8876  C  CB    . ILE A 1  1220 ? -17.105 61.869  90.507  1.00 18.30 ? 1218 ILE A CB    1 
ATOM   8877  C  CG1   . ILE A 1  1220 ? -15.704 62.422  90.787  1.00 20.87 ? 1218 ILE A CG1   1 
ATOM   8878  C  CG2   . ILE A 1  1220 ? -17.346 61.557  89.034  1.00 20.21 ? 1218 ILE A CG2   1 
ATOM   8879  C  CD1   . ILE A 1  1220 ? -14.643 61.370  90.987  1.00 28.35 ? 1218 ILE A CD1   1 
ATOM   8880  N  N     . ASN A 1  1221 ? -20.379 62.910  90.016  1.00 14.61 ? 1219 ASN A N     1 
ATOM   8881  C  CA    . ASN A 1  1221 ? -21.711 62.380  89.717  1.00 15.82 ? 1219 ASN A CA    1 
ATOM   8882  C  C     . ASN A 1  1221 ? -21.557 61.240  88.713  1.00 17.36 ? 1219 ASN A C     1 
ATOM   8883  O  O     . ASN A 1  1221 ? -21.406 61.470  87.515  1.00 19.18 ? 1219 ASN A O     1 
ATOM   8884  C  CB    . ASN A 1  1221 ? -22.603 63.489  89.173  1.00 15.48 ? 1219 ASN A CB    1 
ATOM   8885  C  CG    . ASN A 1  1221 ? -23.949 62.966  88.692  1.00 16.80 ? 1219 ASN A CG    1 
ATOM   8886  O  OD1   . ASN A 1  1221 ? -24.310 61.820  88.947  1.00 16.55 ? 1219 ASN A OD1   1 
ATOM   8887  N  ND2   . ASN A 1  1221 ? -24.687 63.809  87.981  1.00 19.86 ? 1219 ASN A ND2   1 
ATOM   8888  N  N     . THR A 1  1222 ? -21.590 60.000  89.197  1.00 16.68 ? 1220 THR A N     1 
ATOM   8889  C  CA    . THR A 1  1222 ? -21.354 58.857  88.325  1.00 18.95 ? 1220 THR A CA    1 
ATOM   8890  C  C     . THR A 1  1222 ? -22.606 58.426  87.593  1.00 22.64 ? 1220 THR A C     1 
ATOM   8891  O  O     . THR A 1  1222 ? -22.553 57.489  86.798  1.00 25.11 ? 1220 THR A O     1 
ATOM   8892  C  CB    . THR A 1  1222 ? -20.795 57.679  89.121  1.00 21.01 ? 1220 THR A CB    1 
ATOM   8893  O  OG1   . THR A 1  1222 ? -21.707 57.341  90.170  1.00 19.50 ? 1220 THR A OG1   1 
ATOM   8894  C  CG2   . THR A 1  1222 ? -19.462 58.053  89.719  1.00 18.66 ? 1220 THR A CG2   1 
ATOM   8895  N  N     . ALA A 1  1223 ? -23.729 59.077  87.849  1.00 18.57 ? 1221 ALA A N     1 
ATOM   8896  C  CA    . ALA A 1  1223 ? -24.936 58.856  87.075  1.00 22.52 ? 1221 ALA A CA    1 
ATOM   8897  C  C     . ALA A 1  1223 ? -25.084 59.865  85.942  1.00 26.13 ? 1221 ALA A C     1 
ATOM   8898  O  O     . ALA A 1  1223 ? -26.133 59.901  85.290  1.00 29.21 ? 1221 ALA A O     1 
ATOM   8899  C  CB    . ALA A 1  1223 ? -26.149 58.907  87.998  1.00 22.76 ? 1221 ALA A CB    1 
ATOM   8900  N  N     . ALA A 1  1224 ? -24.050 60.678  85.685  1.00 25.32 ? 1222 ALA A N     1 
ATOM   8901  C  CA    . ALA A 1  1224 ? -24.188 61.793  84.751  1.00 26.35 ? 1222 ALA A CA    1 
ATOM   8902  C  C     . ALA A 1  1224 ? -24.417 61.318  83.322  1.00 29.61 ? 1222 ALA A C     1 
ATOM   8903  O  O     . ALA A 1  1224 ? -25.031 62.037  82.526  1.00 30.24 ? 1222 ALA A O     1 
ATOM   8904  C  CB    . ALA A 1  1224 ? -22.957 62.692  84.812  1.00 25.64 ? 1222 ALA A CB    1 
ATOM   8905  N  N     . ALA A 1  1225 ? -23.936 60.123  82.976  1.00 29.64 ? 1223 ALA A N     1 
ATOM   8906  C  CA    . ALA A 1  1225 ? -24.154 59.602  81.630  1.00 33.96 ? 1223 ALA A CA    1 
ATOM   8907  C  C     . ALA A 1  1225 ? -25.589 59.160  81.401  1.00 35.24 ? 1223 ALA A C     1 
ATOM   8908  O  O     . ALA A 1  1225 ? -25.925 58.773  80.274  1.00 37.53 ? 1223 ALA A O     1 
ATOM   8909  C  CB    . ALA A 1  1225 ? -23.195 58.441  81.350  1.00 29.70 ? 1223 ALA A CB    1 
ATOM   8910  N  N     . GLY A 1  1226 ? -26.433 59.214  82.430  1.00 31.61 ? 1224 GLY A N     1 
ATOM   8911  C  CA    . GLY A 1  1226 ? -27.846 58.882  82.311  1.00 33.28 ? 1224 GLY A CA    1 
ATOM   8912  C  C     . GLY A 1  1226 ? -28.275 57.673  83.114  1.00 35.20 ? 1224 GLY A C     1 
ATOM   8913  O  O     . GLY A 1  1226 ? -29.465 57.322  83.089  1.00 37.43 ? 1224 GLY A O     1 
ATOM   8914  N  N     . GLY A 1  1227 ? -27.367 57.016  83.822  1.00 29.10 ? 1225 GLY A N     1 
ATOM   8915  C  CA    . GLY A 1  1227 ? -27.723 55.843  84.597  1.00 30.83 ? 1225 GLY A CA    1 
ATOM   8916  C  C     . GLY A 1  1227 ? -26.571 55.459  85.496  1.00 32.93 ? 1225 GLY A C     1 
ATOM   8917  O  O     . GLY A 1  1227 ? -25.454 55.972  85.372  1.00 32.40 ? 1225 GLY A O     1 
ATOM   8918  N  N     . ASN A 1  1228 ? -26.864 54.531  86.398  1.00 27.77 ? 1226 ASN A N     1 
ATOM   8919  C  CA    . ASN A 1  1228 ? -25.940 54.097  87.442  1.00 29.94 ? 1226 ASN A CA    1 
ATOM   8920  C  C     . ASN A 1  1228 ? -25.519 52.656  87.153  1.00 36.18 ? 1226 ASN A C     1 
ATOM   8921  O  O     . ASN A 1  1228 ? -26.300 51.719  87.365  1.00 35.67 ? 1226 ASN A O     1 
ATOM   8922  C  CB    . ASN A 1  1228 ? -26.610 54.223  88.811  1.00 32.85 ? 1226 ASN A CB    1 
ATOM   8923  C  CG    . ASN A 1  1228 ? -25.666 53.939  89.969  1.00 34.80 ? 1226 ASN A CG    1 
ATOM   8924  O  OD1   . ASN A 1  1228 ? -24.620 53.307  89.804  1.00 33.36 ? 1226 ASN A OD1   1 
ATOM   8925  N  ND2   . ASN A 1  1228 ? -26.047 54.399  91.163  1.00 29.41 ? 1226 ASN A ND2   1 
ATOM   8926  N  N     . ALA A 1  1229 ? -24.276 52.480  86.693  1.00 34.08 ? 1227 ALA A N     1 
ATOM   8927  C  CA    . ALA A 1  1229 ? -23.802 51.143  86.346  1.00 39.41 ? 1227 ALA A CA    1 
ATOM   8928  C  C     . ALA A 1  1229 ? -23.749 50.237  87.570  1.00 38.43 ? 1227 ALA A C     1 
ATOM   8929  O  O     . ALA A 1  1229 ? -24.144 49.067  87.500  1.00 39.50 ? 1227 ALA A O     1 
ATOM   8930  C  CB    . ALA A 1  1229 ? -22.427 51.226  85.683  1.00 35.82 ? 1227 ALA A CB    1 
ATOM   8931  N  N     . SER A 1  1230 ? -23.265 50.764  88.701  1.00 36.45 ? 1228 SER A N     1 
ATOM   8932  C  CA    . SER A 1  1230 ? -23.164 49.961  89.918  1.00 38.31 ? 1228 SER A CA    1 
ATOM   8933  C  C     . SER A 1  1230 ? -24.520 49.406  90.336  1.00 41.88 ? 1228 SER A C     1 
ATOM   8934  O  O     . SER A 1  1230 ? -24.637 48.223  90.682  1.00 43.24 ? 1228 SER A O     1 
ATOM   8935  C  CB    . SER A 1  1230 ? -22.565 50.797  91.051  1.00 37.54 ? 1228 SER A CB    1 
ATOM   8936  O  OG    . SER A 1  1230 ? -21.287 51.297  90.699  1.00 48.87 ? 1228 SER A OG    1 
ATOM   8937  N  N     . LEU A 1  1231 ? -25.560 50.240  90.300  1.00 37.65 ? 1229 LEU A N     1 
ATOM   8938  C  CA    . LEU A 1  1231 ? -26.878 49.811  90.751  1.00 42.34 ? 1229 LEU A CA    1 
ATOM   8939  C  C     . LEU A 1  1231 ? -27.592 48.918  89.743  1.00 48.67 ? 1229 LEU A C     1 
ATOM   8940  O  O     . LEU A 1  1231 ? -28.502 48.177  90.135  1.00 49.80 ? 1229 LEU A O     1 
ATOM   8941  C  CB    . LEU A 1  1231 ? -27.747 51.027  91.068  1.00 36.90 ? 1229 LEU A CB    1 
ATOM   8942  C  CG    . LEU A 1  1231 ? -27.985 51.396  92.534  1.00 35.48 ? 1229 LEU A CG    1 
ATOM   8943  C  CD1   . LEU A 1  1231 ? -29.180 52.321  92.619  1.00 30.35 ? 1229 LEU A CD1   1 
ATOM   8944  C  CD2   . LEU A 1  1231 ? -28.196 50.170  93.417  1.00 34.26 ? 1229 LEU A CD2   1 
ATOM   8945  N  N     . MET A 1  1232 ? -27.203 48.964  88.465  1.00 46.85 ? 1230 MET A N     1 
ATOM   8946  C  CA    . MET A 1  1232 ? -27.751 48.028  87.486  1.00 51.66 ? 1230 MET A CA    1 
ATOM   8947  C  C     . MET A 1  1232 ? -27.439 46.578  87.847  1.00 55.17 ? 1230 MET A C     1 
ATOM   8948  O  O     . MET A 1  1232 ? -28.113 45.667  87.352  1.00 54.64 ? 1230 MET A O     1 
ATOM   8949  C  CB    . MET A 1  1232 ? -27.216 48.353  86.088  1.00 51.49 ? 1230 MET A CB    1 
ATOM   8950  N  N     . ALA A 1  1233 ? -26.439 46.350  88.697  1.00 59.24 ? 1231 ALA A N     1 
ATOM   8951  C  CA    . ALA A 1  1233 ? -26.148 45.028  89.242  1.00 57.67 ? 1231 ALA A CA    1 
ATOM   8952  C  C     . ALA A 1  1233 ? -26.714 44.888  90.656  1.00 60.54 ? 1231 ALA A C     1 
ATOM   8953  O  O     . ALA A 1  1233 ? -27.872 45.226  90.917  1.00 61.90 ? 1231 ALA A O     1 
ATOM   8954  C  CB    . ALA A 1  1233 ? -24.649 44.772  89.247  1.00 57.32 ? 1231 ALA A CB    1 
ATOM   8955  N  N     . ALA B 1  16   ? 29.838  4.890   81.445  1.00 45.44 ? 14   ALA B N     1 
ATOM   8956  C  CA    . ALA B 1  16   ? 28.915  6.019   81.433  1.00 49.46 ? 14   ALA B CA    1 
ATOM   8957  C  C     . ALA B 1  16   ? 27.466  5.540   81.421  1.00 54.99 ? 14   ALA B C     1 
ATOM   8958  O  O     . ALA B 1  16   ? 27.058  4.822   80.505  1.00 57.76 ? 14   ALA B O     1 
ATOM   8959  C  CB    . ALA B 1  16   ? 29.187  6.915   80.230  1.00 45.06 ? 14   ALA B CB    1 
ATOM   8960  N  N     . PRO B 1  17   ? 26.698  5.926   82.442  1.00 47.27 ? 15   PRO B N     1 
ATOM   8961  C  CA    . PRO B 1  17   ? 25.280  5.548   82.485  1.00 42.47 ? 15   PRO B CA    1 
ATOM   8962  C  C     . PRO B 1  17   ? 24.546  5.992   81.228  1.00 39.07 ? 15   PRO B C     1 
ATOM   8963  O  O     . PRO B 1  17   ? 24.725  7.113   80.748  1.00 36.59 ? 15   PRO B O     1 
ATOM   8964  C  CB    . PRO B 1  17   ? 24.757  6.278   83.727  1.00 45.12 ? 15   PRO B CB    1 
ATOM   8965  C  CG    . PRO B 1  17   ? 25.962  6.449   84.592  1.00 48.25 ? 15   PRO B CG    1 
ATOM   8966  C  CD    . PRO B 1  17   ? 27.117  6.655   83.651  1.00 45.14 ? 15   PRO B CD    1 
ATOM   8967  N  N     . ALA B 1  18   ? 23.736  5.085   80.686  1.00 36.31 ? 16   ALA B N     1 
ATOM   8968  C  CA    . ALA B 1  18   ? 22.927  5.406   79.522  1.00 34.57 ? 16   ALA B CA    1 
ATOM   8969  C  C     . ALA B 1  18   ? 21.978  6.557   79.854  1.00 29.25 ? 16   ALA B C     1 
ATOM   8970  O  O     . ALA B 1  18   ? 21.404  6.589   80.949  1.00 27.61 ? 16   ALA B O     1 
ATOM   8971  C  CB    . ALA B 1  18   ? 22.124  4.188   79.067  1.00 32.91 ? 16   ALA B CB    1 
ATOM   8972  N  N     . PRO B 1  19   ? 21.804  7.514   78.945  1.00 27.71 ? 17   PRO B N     1 
ATOM   8973  C  CA    . PRO B 1  19   ? 20.955  8.678   79.239  1.00 26.27 ? 17   PRO B CA    1 
ATOM   8974  C  C     . PRO B 1  19   ? 19.535  8.273   79.609  1.00 23.05 ? 17   PRO B C     1 
ATOM   8975  O  O     . PRO B 1  19   ? 18.902  7.473   78.920  1.00 25.47 ? 17   PRO B O     1 
ATOM   8976  C  CB    . PRO B 1  19   ? 20.987  9.474   77.928  1.00 26.13 ? 17   PRO B CB    1 
ATOM   8977  C  CG    . PRO B 1  19   ? 22.287  9.096   77.301  1.00 29.05 ? 17   PRO B CG    1 
ATOM   8978  C  CD    . PRO B 1  19   ? 22.503  7.650   77.656  1.00 30.66 ? 17   PRO B CD    1 
ATOM   8979  N  N     . PHE B 1  20   ? 19.046  8.837   80.717  1.00 25.61 ? 18   PHE B N     1 
ATOM   8980  C  CA    . PHE B 1  20   ? 17.671  8.681   81.191  1.00 23.39 ? 18   PHE B CA    1 
ATOM   8981  C  C     . PHE B 1  20   ? 17.341  7.258   81.617  1.00 24.84 ? 18   PHE B C     1 
ATOM   8982  O  O     . PHE B 1  20   ? 16.167  6.924   81.779  1.00 27.32 ? 18   PHE B O     1 
ATOM   8983  C  CB    . PHE B 1  20   ? 16.657  9.145   80.136  1.00 22.60 ? 18   PHE B CB    1 
ATOM   8984  C  CG    . PHE B 1  20   ? 16.843  10.571  79.717  1.00 22.58 ? 18   PHE B CG    1 
ATOM   8985  C  CD1   . PHE B 1  20   ? 16.513  11.605  80.580  1.00 20.83 ? 18   PHE B CD1   1 
ATOM   8986  C  CD2   . PHE B 1  20   ? 17.354  10.880  78.469  1.00 21.22 ? 18   PHE B CD2   1 
ATOM   8987  C  CE1   . PHE B 1  20   ? 16.673  12.922  80.198  1.00 20.25 ? 18   PHE B CE1   1 
ATOM   8988  C  CE2   . PHE B 1  20   ? 17.521  12.196  78.088  1.00 20.11 ? 18   PHE B CE2   1 
ATOM   8989  C  CZ    . PHE B 1  20   ? 17.186  13.211  78.950  1.00 21.39 ? 18   PHE B CZ    1 
ATOM   8990  N  N     . ALA B 1  21   ? 18.350  6.412   81.814  1.00 27.50 ? 19   ALA B N     1 
ATOM   8991  C  CA    . ALA B 1  21   ? 18.089  5.032   82.200  1.00 27.50 ? 19   ALA B CA    1 
ATOM   8992  C  C     . ALA B 1  21   ? 17.485  4.918   83.596  1.00 29.49 ? 19   ALA B C     1 
ATOM   8993  O  O     . ALA B 1  21   ? 16.795  3.932   83.878  1.00 32.79 ? 19   ALA B O     1 
ATOM   8994  C  CB    . ALA B 1  21   ? 19.384  4.220   82.115  1.00 29.65 ? 19   ALA B CB    1 
ATOM   8995  N  N     . ASP B 1  22   ? 17.704  5.901   84.465  1.00 26.03 ? 20   ASP B N     1 
ATOM   8996  C  CA    . ASP B 1  22   ? 17.108  5.894   85.795  1.00 26.38 ? 20   ASP B CA    1 
ATOM   8997  C  C     . ASP B 1  22   ? 16.385  7.201   86.056  1.00 22.25 ? 20   ASP B C     1 
ATOM   8998  O  O     . ASP B 1  22   ? 16.512  7.793   87.132  1.00 24.17 ? 20   ASP B O     1 
ATOM   8999  C  CB    . ASP B 1  22   ? 18.162  5.642   86.869  1.00 28.78 ? 20   ASP B CB    1 
ATOM   9000  N  N     . PHE B 1  23   ? 15.612  7.675   85.075  1.00 18.54 ? 21   PHE B N     1 
ATOM   9001  C  CA    . PHE B 1  23   ? 15.084  9.034   85.158  1.00 19.79 ? 21   PHE B CA    1 
ATOM   9002  C  C     . PHE B 1  23   ? 14.128  9.186   86.336  1.00 20.30 ? 21   PHE B C     1 
ATOM   9003  O  O     . PHE B 1  23   ? 14.305  10.062  87.194  1.00 20.39 ? 21   PHE B O     1 
ATOM   9004  C  CB    . PHE B 1  23   ? 14.386  9.416   83.854  1.00 19.35 ? 21   PHE B CB    1 
ATOM   9005  C  CG    . PHE B 1  23   ? 13.695  10.737  83.927  1.00 20.30 ? 21   PHE B CG    1 
ATOM   9006  C  CD1   . PHE B 1  23   ? 14.429  11.892  84.107  1.00 19.73 ? 21   PHE B CD1   1 
ATOM   9007  C  CD2   . PHE B 1  23   ? 12.308  10.822  83.842  1.00 19.65 ? 21   PHE B CD2   1 
ATOM   9008  C  CE1   . PHE B 1  23   ? 13.798  13.128  84.196  1.00 19.25 ? 21   PHE B CE1   1 
ATOM   9009  C  CE2   . PHE B 1  23   ? 11.675  12.051  83.931  1.00 21.10 ? 21   PHE B CE2   1 
ATOM   9010  C  CZ    . PHE B 1  23   ? 12.419  13.199  84.116  1.00 19.77 ? 21   PHE B CZ    1 
ATOM   9011  N  N     . ALA B 1  24   ? 13.099  8.348   86.384  1.00 20.53 ? 22   ALA B N     1 
ATOM   9012  C  CA    . ALA B 1  24   ? 12.107  8.446   87.448  1.00 19.90 ? 22   ALA B CA    1 
ATOM   9013  C  C     . ALA B 1  24   ? 11.389  7.115   87.642  1.00 19.43 ? 22   ALA B C     1 
ATOM   9014  O  O     . ALA B 1  24   ? 10.164  7.049   87.496  1.00 21.00 ? 22   ALA B O     1 
ATOM   9015  C  CB    . ALA B 1  24   ? 11.091  9.543   87.132  1.00 20.87 ? 22   ALA B CB    1 
ATOM   9016  N  N     . PRO B 1  25   ? 12.102  6.049   87.993  1.00 19.96 ? 23   PRO B N     1 
ATOM   9017  C  CA    . PRO B 1  25   ? 11.446  4.754   88.188  1.00 23.98 ? 23   PRO B CA    1 
ATOM   9018  C  C     . PRO B 1  25   ? 10.471  4.827   89.349  1.00 21.90 ? 23   PRO B C     1 
ATOM   9019  O  O     . PRO B 1  25   ? 10.779  5.441   90.382  1.00 21.91 ? 23   PRO B O     1 
ATOM   9020  C  CB    . PRO B 1  25   ? 12.618  3.811   88.495  1.00 25.67 ? 23   PRO B CB    1 
ATOM   9021  C  CG    . PRO B 1  25   ? 13.626  4.682   89.122  1.00 25.98 ? 23   PRO B CG    1 
ATOM   9022  C  CD    . PRO B 1  25   ? 13.511  6.023   88.422  1.00 20.94 ? 23   PRO B CD    1 
ATOM   9023  N  N     . PRO B 1  26   ? 9.283   4.241   89.217  1.00 20.91 ? 24   PRO B N     1 
ATOM   9024  C  CA    . PRO B 1  26   ? 8.316   4.292   90.322  1.00 20.96 ? 24   PRO B CA    1 
ATOM   9025  C  C     . PRO B 1  26   ? 8.790   3.476   91.515  1.00 24.03 ? 24   PRO B C     1 
ATOM   9026  O  O     . PRO B 1  26   ? 9.623   2.573   91.402  1.00 23.32 ? 24   PRO B O     1 
ATOM   9027  C  CB    . PRO B 1  26   ? 7.044   3.699   89.713  1.00 23.11 ? 24   PRO B CB    1 
ATOM   9028  C  CG    . PRO B 1  26   ? 7.550   2.745   88.656  1.00 24.09 ? 24   PRO B CG    1 
ATOM   9029  C  CD    . PRO B 1  26   ? 8.821   3.382   88.110  1.00 24.93 ? 24   PRO B CD    1 
ATOM   9030  N  N     . VAL B 1  27   ? 8.237   3.813   92.684  1.00 22.44 ? 25   VAL B N     1 
ATOM   9031  C  CA    . VAL B 1  27   ? 8.590   3.085   93.901  1.00 21.75 ? 25   VAL B CA    1 
ATOM   9032  C  C     . VAL B 1  27   ? 8.243   1.607   93.754  1.00 22.98 ? 25   VAL B C     1 
ATOM   9033  O  O     . VAL B 1  27   ? 8.995   0.729   94.192  1.00 25.53 ? 25   VAL B O     1 
ATOM   9034  C  CB    . VAL B 1  27   ? 7.897   3.720   95.121  1.00 22.45 ? 25   VAL B CB    1 
ATOM   9035  C  CG1   . VAL B 1  27   ? 8.078   2.839   96.357  1.00 23.26 ? 25   VAL B CG1   1 
ATOM   9036  C  CG2   . VAL B 1  27   ? 8.463   5.105   95.372  1.00 21.40 ? 25   VAL B CG2   1 
ATOM   9037  N  N     . ARG B 1  28   ? 7.115   1.308   93.123  1.00 22.99 ? 26   ARG B N     1 
ATOM   9038  C  CA    . ARG B 1  28   ? 6.674   -0.066  92.945  1.00 23.54 ? 26   ARG B CA    1 
ATOM   9039  C  C     . ARG B 1  28   ? 5.895   -0.149  91.644  1.00 26.32 ? 26   ARG B C     1 
ATOM   9040  O  O     . ARG B 1  28   ? 5.418   0.874   91.138  1.00 24.23 ? 26   ARG B O     1 
ATOM   9041  C  CB    . ARG B 1  28   ? 5.810   -0.529  94.130  1.00 26.06 ? 26   ARG B CB    1 
ATOM   9042  C  CG    . ARG B 1  28   ? 4.446   0.163   94.203  1.00 24.88 ? 26   ARG B CG    1 
ATOM   9043  C  CD    . ARG B 1  28   ? 3.672   -0.222  95.459  1.00 24.05 ? 26   ARG B CD    1 
ATOM   9044  N  NE    . ARG B 1  28   ? 4.247   0.388   96.654  1.00 28.73 ? 26   ARG B NE    1 
ATOM   9045  C  CZ    . ARG B 1  28   ? 4.988   -0.254  97.547  1.00 29.29 ? 26   ARG B CZ    1 
ATOM   9046  N  NH1   . ARG B 1  28   ? 5.226   -1.553  97.444  1.00 31.58 ? 26   ARG B NH1   1 
ATOM   9047  N  NH2   . ARG B 1  28   ? 5.500   0.421   98.572  1.00 26.38 ? 26   ARG B NH2   1 
ATOM   9048  N  N     . PRO B 1  29   ? 5.776   -1.337  91.056  1.00 26.30 ? 27   PRO B N     1 
ATOM   9049  C  CA    . PRO B 1  29   ? 4.874   -1.483  89.909  1.00 25.67 ? 27   PRO B CA    1 
ATOM   9050  C  C     . PRO B 1  29   ? 3.465   -1.065  90.297  1.00 27.69 ? 27   PRO B C     1 
ATOM   9051  O  O     . PRO B 1  29   ? 2.964   -1.396  91.376  1.00 27.63 ? 27   PRO B O     1 
ATOM   9052  C  CB    . PRO B 1  29   ? 4.957   -2.976  89.569  1.00 29.29 ? 27   PRO B CB    1 
ATOM   9053  C  CG    . PRO B 1  29   ? 6.266   -3.420  90.146  1.00 32.70 ? 27   PRO B CG    1 
ATOM   9054  C  CD    . PRO B 1  29   ? 6.439   -2.610  91.396  1.00 27.59 ? 27   PRO B CD    1 
ATOM   9055  N  N     . GLN B 1  30   ? 2.837   -0.305  89.413  1.00 26.00 ? 28   GLN B N     1 
ATOM   9056  C  CA    . GLN B 1  30   ? 1.529   0.262   89.699  1.00 27.98 ? 28   GLN B CA    1 
ATOM   9057  C  C     . GLN B 1  30   ? 0.452   -0.795  89.473  1.00 27.90 ? 28   GLN B C     1 
ATOM   9058  O  O     . GLN B 1  30   ? 0.294   -1.307  88.355  1.00 27.93 ? 28   GLN B O     1 
ATOM   9059  C  CB    . GLN B 1  30   ? 1.298   1.494   88.825  1.00 27.04 ? 28   GLN B CB    1 
ATOM   9060  C  CG    . GLN B 1  30   ? 2.419   2.529   88.936  1.00 23.40 ? 28   GLN B CG    1 
ATOM   9061  C  CD    . GLN B 1  30   ? 2.436   3.199   90.291  1.00 24.02 ? 28   GLN B CD    1 
ATOM   9062  O  OE1   . GLN B 1  30   ? 1.575   4.022   90.586  1.00 24.23 ? 28   GLN B OE1   1 
ATOM   9063  N  NE2   . GLN B 1  30   ? 3.392   2.829   91.132  1.00 22.85 ? 28   GLN B NE2   1 
ATOM   9064  N  N     . SER B 1  31   ? -0.282  -1.124  90.535  1.00 25.57 ? 29   SER B N     1 
ATOM   9065  C  CA    . SER B 1  31   ? -1.381  -2.068  90.457  1.00 26.19 ? 29   SER B CA    1 
ATOM   9066  C  C     . SER B 1  31   ? -2.539  -1.483  89.651  1.00 24.79 ? 29   SER B C     1 
ATOM   9067  O  O     . SER B 1  31   ? -2.559  -0.296  89.297  1.00 25.17 ? 29   SER B O     1 
ATOM   9068  C  CB    . SER B 1  31   ? -1.880  -2.426  91.853  1.00 27.71 ? 29   SER B CB    1 
ATOM   9069  O  OG    . SER B 1  31   ? -2.579  -1.322  92.409  1.00 25.59 ? 29   SER B OG    1 
ATOM   9070  N  N     . THR B 1  32   ? -3.518  -2.342  89.365  1.00 28.21 ? 30   THR B N     1 
ATOM   9071  C  CA    . THR B 1  32   ? -4.740  -1.886  88.712  1.00 26.80 ? 30   THR B CA    1 
ATOM   9072  C  C     . THR B 1  32   ? -5.398  -0.768  89.512  1.00 25.02 ? 30   THR B C     1 
ATOM   9073  O  O     . THR B 1  32   ? -5.779  0.267   88.956  1.00 26.77 ? 30   THR B O     1 
ATOM   9074  C  CB    . THR B 1  32   ? -5.700  -3.062  88.531  1.00 29.96 ? 30   THR B CB    1 
ATOM   9075  O  OG1   . THR B 1  32   ? -5.156  -3.963  87.564  1.00 33.66 ? 30   THR B OG1   1 
ATOM   9076  C  CG2   . THR B 1  32   ? -7.079  -2.577  88.074  1.00 33.78 ? 30   THR B CG2   1 
ATOM   9077  N  N     . LEU B 1  33   ? -5.512  -0.951  90.827  1.00 24.47 ? 31   LEU B N     1 
ATOM   9078  C  CA    . LEU B 1  33   ? -6.127  0.076   91.660  1.00 23.23 ? 31   LEU B CA    1 
ATOM   9079  C  C     . LEU B 1  33   ? -5.284  1.348   91.703  1.00 22.98 ? 31   LEU B C     1 
ATOM   9080  O  O     . LEU B 1  33   ? -5.832  2.456   91.693  1.00 22.87 ? 31   LEU B O     1 
ATOM   9081  C  CB    . LEU B 1  33   ? -6.366  -0.473  93.066  1.00 22.98 ? 31   LEU B CB    1 
ATOM   9082  C  CG    . LEU B 1  33   ? -7.434  -1.562  93.021  1.00 24.09 ? 31   LEU B CG    1 
ATOM   9083  C  CD1   . LEU B 1  33   ? -7.469  -2.323  94.324  1.00 26.27 ? 31   LEU B CD1   1 
ATOM   9084  C  CD2   . LEU B 1  33   ? -8.792  -0.975  92.705  1.00 28.22 ? 31   LEU B CD2   1 
ATOM   9085  N  N     . ARG B 1  34   ? -3.953  1.219   91.773  1.00 21.67 ? 32   ARG B N     1 
ATOM   9086  C  CA    . ARG B 1  34   ? -3.120  2.419   91.750  1.00 21.73 ? 32   ARG B CA    1 
ATOM   9087  C  C     . ARG B 1  34   ? -3.245  3.128   90.411  1.00 22.20 ? 32   ARG B C     1 
ATOM   9088  O  O     . ARG B 1  34   ? -3.291  4.361   90.355  1.00 21.15 ? 32   ARG B O     1 
ATOM   9089  C  CB    . ARG B 1  34   ? -1.657  2.075   92.031  1.00 20.43 ? 32   ARG B CB    1 
ATOM   9090  C  CG    . ARG B 1  34   ? -1.337  1.710   93.480  1.00 22.64 ? 32   ARG B CG    1 
ATOM   9091  C  CD    . ARG B 1  34   ? -1.415  2.909   94.420  1.00 22.66 ? 32   ARG B CD    1 
ATOM   9092  N  NE    . ARG B 1  34   ? -0.367  3.888   94.164  1.00 22.60 ? 32   ARG B NE    1 
ATOM   9093  C  CZ    . ARG B 1  34   ? 0.841   3.866   94.714  1.00 21.89 ? 32   ARG B CZ    1 
ATOM   9094  N  NH1   . ARG B 1  34   ? 1.200   2.918   95.570  1.00 21.08 ? 32   ARG B NH1   1 
ATOM   9095  N  NH2   . ARG B 1  34   ? 1.717   4.811   94.387  1.00 19.93 ? 32   ARG B NH2   1 
ATOM   9096  N  N     . ARG B 1  35   ? -3.323  2.362   89.322  1.00 21.65 ? 33   ARG B N     1 
ATOM   9097  C  CA    . ARG B 1  35   ? -3.472  2.973   88.004  1.00 25.14 ? 33   ARG B CA    1 
ATOM   9098  C  C     . ARG B 1  35   ? -4.792  3.713   87.879  1.00 23.07 ? 33   ARG B C     1 
ATOM   9099  O  O     . ARG B 1  35   ? -4.862  4.754   87.214  1.00 21.91 ? 33   ARG B O     1 
ATOM   9100  C  CB    . ARG B 1  35   ? -3.362  1.911   86.911  1.00 26.76 ? 33   ARG B CB    1 
ATOM   9101  C  CG    . ARG B 1  35   ? -1.936  1.505   86.641  1.00 26.80 ? 33   ARG B CG    1 
ATOM   9102  C  CD    . ARG B 1  35   ? -1.829  0.440   85.545  1.00 28.30 ? 33   ARG B CD    1 
ATOM   9103  N  NE    . ARG B 1  35   ? -0.448  -0.016  85.471  1.00 34.33 ? 33   ARG B NE    1 
ATOM   9104  C  CZ    . ARG B 1  35   ? 0.532   0.678   84.909  1.00 41.56 ? 33   ARG B CZ    1 
ATOM   9105  N  NH1   . ARG B 1  35   ? 0.293   1.806   84.257  1.00 43.66 ? 33   ARG B NH1   1 
ATOM   9106  N  NH2   . ARG B 1  35   ? 1.786   0.241   85.016  1.00 35.69 ? 33   ARG B NH2   1 
ATOM   9107  N  N     . ALA B 1  36   ? -5.849  3.194   88.509  1.00 22.85 ? 34   ALA B N     1 
ATOM   9108  C  CA    . ALA B 1  36   ? -7.141  3.865   88.433  1.00 22.28 ? 34   ALA B CA    1 
ATOM   9109  C  C     . ALA B 1  36   ? -7.111  5.194   89.172  1.00 21.66 ? 34   ALA B C     1 
ATOM   9110  O  O     . ALA B 1  36   ? -7.783  6.146   88.767  1.00 22.76 ? 34   ALA B O     1 
ATOM   9111  C  CB    . ALA B 1  36   ? -8.246  2.963   88.987  1.00 23.37 ? 34   ALA B CB    1 
ATOM   9112  N  N     . ILE B 1  37   ? -6.338  5.276   90.254  1.00 20.23 ? 35   ILE B N     1 
ATOM   9113  C  CA    . ILE B 1  37   ? -6.118  6.559   90.914  1.00 18.43 ? 35   ILE B CA    1 
ATOM   9114  C  C     . ILE B 1  37   ? -5.445  7.536   89.965  1.00 21.64 ? 35   ILE B C     1 
ATOM   9115  O  O     . ILE B 1  37   ? -5.925  8.656   89.749  1.00 19.36 ? 35   ILE B O     1 
ATOM   9116  C  CB    . ILE B 1  37   ? -5.283  6.356   92.186  1.00 17.52 ? 35   ILE B CB    1 
ATOM   9117  C  CG1   . ILE B 1  37   ? -6.077  5.533   93.197  1.00 19.11 ? 35   ILE B CG1   1 
ATOM   9118  C  CG2   . ILE B 1  37   ? -4.831  7.706   92.757  1.00 18.66 ? 35   ILE B CG2   1 
ATOM   9119  C  CD1   . ILE B 1  37   ? -5.199  5.007   94.326  1.00 21.15 ? 35   ILE B CD1   1 
ATOM   9120  N  N     . THR B 1  38   ? -4.311  7.132   89.392  1.00 19.46 ? 36   THR B N     1 
ATOM   9121  C  CA    . THR B 1  38   ? -3.559  8.051   88.551  1.00 18.75 ? 36   THR B CA    1 
ATOM   9122  C  C     . THR B 1  38   ? -4.388  8.520   87.358  1.00 19.13 ? 36   THR B C     1 
ATOM   9123  O  O     . THR B 1  38   ? -4.321  9.693   86.972  1.00 20.02 ? 36   THR B O     1 
ATOM   9124  C  CB    . THR B 1  38   ? -2.264  7.387   88.089  1.00 20.46 ? 36   THR B CB    1 
ATOM   9125  O  OG1   . THR B 1  38   ? -1.582  6.846   89.235  1.00 20.02 ? 36   THR B OG1   1 
ATOM   9126  C  CG2   . THR B 1  38   ? -1.365  8.401   87.374  1.00 20.17 ? 36   THR B CG2   1 
ATOM   9127  N  N     . ALA B 1  39   ? -5.182  7.622   86.776  1.00 20.22 ? 37   ALA B N     1 
ATOM   9128  C  CA    . ALA B 1  39   ? -6.002  7.982   85.622  1.00 22.71 ? 37   ALA B CA    1 
ATOM   9129  C  C     . ALA B 1  39   ? -7.005  9.087   85.940  1.00 22.48 ? 37   ALA B C     1 
ATOM   9130  O  O     . ALA B 1  39   ? -7.434  9.808   85.031  1.00 22.27 ? 37   ALA B O     1 
ATOM   9131  C  CB    . ALA B 1  39   ? -6.742  6.744   85.105  1.00 22.95 ? 37   ALA B CB    1 
ATOM   9132  N  N     . ALA B 1  40   ? -7.405  9.227   87.207  1.00 20.09 ? 38   ALA B N     1 
ATOM   9133  C  CA    . ALA B 1  40   ? -8.404  10.216  87.599  1.00 21.21 ? 38   ALA B CA    1 
ATOM   9134  C  C     . ALA B 1  40   ? -7.796  11.564  87.972  1.00 20.75 ? 38   ALA B C     1 
ATOM   9135  O  O     . ALA B 1  40   ? -8.555  12.494  88.270  1.00 20.41 ? 38   ALA B O     1 
ATOM   9136  C  CB    . ALA B 1  40   ? -9.234  9.691   88.779  1.00 20.84 ? 38   ALA B CB    1 
ATOM   9137  N  N     . TYR B 1  41   ? -6.460  11.680  87.969  1.00 19.72 ? 39   TYR B N     1 
ATOM   9138  C  CA    . TYR B 1  41   ? -5.763  12.823  88.567  1.00 17.97 ? 39   TYR B CA    1 
ATOM   9139  C  C     . TYR B 1  41   ? -6.377  14.153  88.138  1.00 19.15 ? 39   TYR B C     1 
ATOM   9140  O  O     . TYR B 1  41   ? -6.710  15.000  88.978  1.00 17.45 ? 39   TYR B O     1 
ATOM   9141  C  CB    . TYR B 1  41   ? -4.278  12.760  88.181  1.00 17.36 ? 39   TYR B CB    1 
ATOM   9142  C  CG    . TYR B 1  41   ? -3.277  13.450  89.084  1.00 19.34 ? 39   TYR B CG    1 
ATOM   9143  C  CD1   . TYR B 1  41   ? -3.590  14.613  89.779  1.00 18.07 ? 39   TYR B CD1   1 
ATOM   9144  C  CD2   . TYR B 1  41   ? -1.986  12.947  89.197  1.00 16.59 ? 39   TYR B CD2   1 
ATOM   9145  C  CE1   . TYR B 1  41   ? -2.632  15.249  90.583  1.00 18.42 ? 39   TYR B CE1   1 
ATOM   9146  C  CE2   . TYR B 1  41   ? -1.032  13.561  89.990  1.00 17.95 ? 39   TYR B CE2   1 
ATOM   9147  C  CZ    . TYR B 1  41   ? -1.354  14.717  90.681  1.00 16.28 ? 39   TYR B CZ    1 
ATOM   9148  O  OH    . TYR B 1  41   ? -0.397  15.319  91.465  1.00 17.87 ? 39   TYR B OH    1 
ATOM   9149  N  N     . ARG B 1  42   ? -6.520  14.361  86.830  1.00 19.43 ? 40   ARG B N     1 
ATOM   9150  C  CA    . ARG B 1  42   ? -7.015  15.627  86.300  1.00 18.86 ? 40   ARG B CA    1 
ATOM   9151  C  C     . ARG B 1  42   ? -8.217  15.405  85.396  1.00 20.18 ? 40   ARG B C     1 
ATOM   9152  O  O     . ARG B 1  42   ? -8.426  16.129  84.423  1.00 21.92 ? 40   ARG B O     1 
ATOM   9153  C  CB    . ARG B 1  42   ? -5.897  16.380  85.585  1.00 19.85 ? 40   ARG B CB    1 
ATOM   9154  C  CG    . ARG B 1  42   ? -4.835  16.801  86.588  1.00 19.83 ? 40   ARG B CG    1 
ATOM   9155  C  CD    . ARG B 1  42   ? -3.611  17.437  85.992  1.00 20.78 ? 40   ARG B CD    1 
ATOM   9156  N  NE    . ARG B 1  42   ? -2.525  17.365  86.961  1.00 18.45 ? 40   ARG B NE    1 
ATOM   9157  C  CZ    . ARG B 1  42   ? -2.315  18.243  87.933  1.00 20.16 ? 40   ARG B CZ    1 
ATOM   9158  N  NH1   . ARG B 1  42   ? -3.050  19.340  88.046  1.00 18.67 ? 40   ARG B NH1   1 
ATOM   9159  N  NH2   . ARG B 1  42   ? -1.340  18.015  88.815  1.00 19.44 ? 40   ARG B NH2   1 
ATOM   9160  N  N     . ARG B 1  43   ? -9.030  14.406  85.736  1.00 19.25 ? 41   ARG B N     1 
ATOM   9161  C  CA    . ARG B 1  43   ? -10.196 14.074  84.928  1.00 18.94 ? 41   ARG B CA    1 
ATOM   9162  C  C     . ARG B 1  43   ? -11.118 15.286  84.817  1.00 21.96 ? 41   ARG B C     1 
ATOM   9163  O  O     . ARG B 1  43   ? -11.318 16.009  85.798  1.00 21.05 ? 41   ARG B O     1 
ATOM   9164  C  CB    . ARG B 1  43   ? -10.947 12.898  85.554  1.00 19.62 ? 41   ARG B CB    1 
ATOM   9165  C  CG    . ARG B 1  43   ? -12.217 12.480  84.826  1.00 20.19 ? 41   ARG B CG    1 
ATOM   9166  C  CD    . ARG B 1  43   ? -12.630 11.109  85.307  1.00 23.00 ? 41   ARG B CD    1 
ATOM   9167  N  NE    . ARG B 1  43   ? -11.636 10.122  84.913  1.00 25.01 ? 41   ARG B NE    1 
ATOM   9168  C  CZ    . ARG B 1  43   ? -11.350 9.031   85.611  1.00 27.13 ? 41   ARG B CZ    1 
ATOM   9169  N  NH1   . ARG B 1  43   ? -11.963 8.761   86.749  1.00 21.18 ? 41   ARG B NH1   1 
ATOM   9170  N  NH2   . ARG B 1  43   ? -10.415 8.199   85.159  1.00 24.81 ? 41   ARG B NH2   1 
ATOM   9171  N  N     . PRO B 1  44   ? -11.674 15.560  83.642  1.00 22.77 ? 42   PRO B N     1 
ATOM   9172  C  CA    . PRO B 1  44   ? -12.601 16.690  83.527  1.00 22.21 ? 42   PRO B CA    1 
ATOM   9173  C  C     . PRO B 1  44   ? -13.711 16.613  84.566  1.00 20.60 ? 42   PRO B C     1 
ATOM   9174  O  O     . PRO B 1  44   ? -14.205 15.536  84.907  1.00 22.82 ? 42   PRO B O     1 
ATOM   9175  C  CB    . PRO B 1  44   ? -13.137 16.551  82.100  1.00 24.19 ? 42   PRO B CB    1 
ATOM   9176  C  CG    . PRO B 1  44   ? -11.947 15.987  81.352  1.00 24.08 ? 42   PRO B CG    1 
ATOM   9177  C  CD    . PRO B 1  44   ? -11.314 15.006  82.323  1.00 24.90 ? 42   PRO B CD    1 
ATOM   9178  N  N     . GLU B 1  45   ? -14.083 17.783  85.080  1.00 21.80 ? 43   GLU B N     1 
ATOM   9179  C  CA    . GLU B 1  45   ? -15.069 17.855  86.149  1.00 21.76 ? 43   GLU B CA    1 
ATOM   9180  C  C     . GLU B 1  45   ? -16.420 17.299  85.702  1.00 24.08 ? 43   GLU B C     1 
ATOM   9181  O  O     . GLU B 1  45   ? -17.125 16.660  86.488  1.00 25.44 ? 43   GLU B O     1 
ATOM   9182  C  CB    . GLU B 1  45   ? -15.178 19.307  86.615  1.00 24.87 ? 43   GLU B CB    1 
ATOM   9183  C  CG    . GLU B 1  45   ? -15.648 19.487  88.035  1.00 26.36 ? 43   GLU B CG    1 
ATOM   9184  C  CD    . GLU B 1  45   ? -15.117 20.759  88.671  1.00 21.79 ? 43   GLU B CD    1 
ATOM   9185  O  OE1   . GLU B 1  45   ? -14.266 21.452  88.067  1.00 21.65 ? 43   GLU B OE1   1 
ATOM   9186  O  OE2   . GLU B 1  45   ? -15.553 21.053  89.800  1.00 22.71 ? 43   GLU B OE2   1 
ATOM   9187  N  N     . THR B 1  46   ? -16.788 17.504  84.436  1.00 25.62 ? 44   THR B N     1 
ATOM   9188  C  CA    . THR B 1  46   ? -18.052 16.961  83.949  1.00 25.25 ? 44   THR B CA    1 
ATOM   9189  C  C     . THR B 1  46   ? -18.040 15.438  83.885  1.00 25.86 ? 44   THR B C     1 
ATOM   9190  O  O     . THR B 1  46   ? -19.110 14.821  83.883  1.00 28.07 ? 44   THR B O     1 
ATOM   9191  C  CB    . THR B 1  46   ? -18.382 17.528  82.569  1.00 25.88 ? 44   THR B CB    1 
ATOM   9192  O  OG1   . THR B 1  46   ? -17.264 17.318  81.698  1.00 25.24 ? 44   THR B OG1   1 
ATOM   9193  C  CG2   . THR B 1  46   ? -18.688 19.021  82.667  1.00 26.52 ? 44   THR B CG2   1 
ATOM   9194  N  N     . GLU B 1  47   ? -16.859 14.817  83.823  1.00 25.30 ? 45   GLU B N     1 
ATOM   9195  C  CA    . GLU B 1  47   ? -16.790 13.363  83.898  1.00 23.83 ? 45   GLU B CA    1 
ATOM   9196  C  C     . GLU B 1  47   ? -16.779 12.863  85.339  1.00 24.51 ? 45   GLU B C     1 
ATOM   9197  O  O     . GLU B 1  47   ? -17.254 11.755  85.609  1.00 25.99 ? 45   GLU B O     1 
ATOM   9198  C  CB    . GLU B 1  47   ? -15.546 12.854  83.164  1.00 24.74 ? 45   GLU B CB    1 
ATOM   9199  C  CG    . GLU B 1  47   ? -15.542 13.146  81.673  1.00 29.87 ? 45   GLU B CG    1 
ATOM   9200  C  CD    . GLU B 1  47   ? -14.247 12.722  81.018  1.00 34.24 ? 45   GLU B CD    1 
ATOM   9201  O  OE1   . GLU B 1  47   ? -13.618 11.756  81.509  1.00 34.68 ? 45   GLU B OE1   1 
ATOM   9202  O  OE2   . GLU B 1  47   ? -13.854 13.360  80.020  1.00 39.10 ? 45   GLU B OE2   1 
ATOM   9203  N  N     . CYS B 1  48   ? -16.230 13.649  86.270  1.00 24.07 ? 46   CYS B N     1 
ATOM   9204  C  CA    . CYS B 1  48   ? -16.133 13.193  87.655  1.00 22.89 ? 46   CYS B CA    1 
ATOM   9205  C  C     . CYS B 1  48   ? -17.492 13.164  88.337  1.00 26.20 ? 46   CYS B C     1 
ATOM   9206  O  O     . CYS B 1  48   ? -17.763 12.277  89.151  1.00 24.61 ? 46   CYS B O     1 
ATOM   9207  C  CB    . CYS B 1  48   ? -15.189 14.092  88.454  1.00 24.21 ? 46   CYS B CB    1 
ATOM   9208  S  SG    . CYS B 1  48   ? -13.460 14.055  87.956  1.00 22.61 ? 46   CYS B SG    1 
ATOM   9209  N  N     . LEU B 1  49   ? -18.345 14.126  88.040  1.00 27.27 ? 47   LEU B N     1 
ATOM   9210  C  CA    . LEU B 1  49   ? -19.519 14.332  88.881  1.00 26.40 ? 47   LEU B CA    1 
ATOM   9211  C  C     . LEU B 1  49   ? -20.642 13.307  88.718  1.00 26.72 ? 47   LEU B C     1 
ATOM   9212  O  O     . LEU B 1  49   ? -21.232 12.921  89.729  1.00 25.38 ? 47   LEU B O     1 
ATOM   9213  C  CB    . LEU B 1  49   ? -20.069 15.746  88.672  1.00 27.33 ? 47   LEU B CB    1 
ATOM   9214  C  CG    . LEU B 1  49   ? -19.622 16.729  89.760  1.00 27.20 ? 47   LEU B CG    1 
ATOM   9215  C  CD1   . LEU B 1  49   ? -20.123 16.265  91.130  1.00 28.37 ? 47   LEU B CD1   1 
ATOM   9216  C  CD2   . LEU B 1  49   ? -18.089 16.890  89.759  1.00 24.41 ? 47   LEU B CD2   1 
ATOM   9217  N  N     . PRO B 1  50   ? -20.985 12.837  87.517  1.00 28.33 ? 48   PRO B N     1 
ATOM   9218  C  CA    . PRO B 1  50   ? -22.162 11.947  87.389  1.00 29.70 ? 48   PRO B CA    1 
ATOM   9219  C  C     . PRO B 1  50   ? -22.043 10.681  88.228  1.00 30.14 ? 48   PRO B C     1 
ATOM   9220  O  O     . PRO B 1  50   ? -23.024 10.294  88.880  1.00 32.66 ? 48   PRO B O     1 
ATOM   9221  C  CB    . PRO B 1  50   ? -22.216 11.640  85.882  1.00 25.87 ? 48   PRO B CB    1 
ATOM   9222  C  CG    . PRO B 1  50   ? -21.621 12.851  85.261  1.00 27.74 ? 48   PRO B CG    1 
ATOM   9223  C  CD    . PRO B 1  50   ? -20.509 13.279  86.190  1.00 26.37 ? 48   PRO B CD    1 
ATOM   9224  N  N     . PRO B 1  51   ? -20.890 9.994   88.262  1.00 27.69 ? 49   PRO B N     1 
ATOM   9225  C  CA    . PRO B 1  51   ? -20.811 8.835   89.167  1.00 29.41 ? 49   PRO B CA    1 
ATOM   9226  C  C     . PRO B 1  51   ? -20.875 9.217   90.638  1.00 27.67 ? 49   PRO B C     1 
ATOM   9227  O  O     . PRO B 1  51   ? -21.392 8.432   91.445  1.00 29.69 ? 49   PRO B O     1 
ATOM   9228  C  CB    . PRO B 1  51   ? -19.471 8.180   88.807  1.00 30.51 ? 49   PRO B CB    1 
ATOM   9229  C  CG    . PRO B 1  51   ? -18.690 9.247   88.114  1.00 29.95 ? 49   PRO B CG    1 
ATOM   9230  C  CD    . PRO B 1  51   ? -19.703 10.059  87.381  1.00 27.45 ? 49   PRO B CD    1 
ATOM   9231  N  N     . LEU B 1  52   ? -20.387 10.403  91.008  1.00 28.64 ? 50   LEU B N     1 
ATOM   9232  C  CA    . LEU B 1  52   ? -20.516 10.859  92.390  1.00 27.90 ? 50   LEU B CA    1 
ATOM   9233  C  C     . LEU B 1  52   ? -21.964 11.190  92.724  1.00 31.22 ? 50   LEU B C     1 
ATOM   9234  O  O     . LEU B 1  52   ? -22.440 10.881  93.824  1.00 30.85 ? 50   LEU B O     1 
ATOM   9235  C  CB    . LEU B 1  52   ? -19.636 12.083  92.635  1.00 26.68 ? 50   LEU B CB    1 
ATOM   9236  C  CG    . LEU B 1  52   ? -18.138 11.898  92.381  1.00 26.49 ? 50   LEU B CG    1 
ATOM   9237  C  CD1   . LEU B 1  52   ? -17.399 13.229  92.451  1.00 25.09 ? 50   LEU B CD1   1 
ATOM   9238  C  CD2   . LEU B 1  52   ? -17.579 10.922  93.376  1.00 27.20 ? 50   LEU B CD2   1 
ATOM   9239  N  N     . VAL B 1  53   ? -22.670 11.840  91.796  1.00 26.83 ? 51   VAL B N     1 
ATOM   9240  C  CA    . VAL B 1  53   ? -24.095 12.105  91.994  1.00 30.40 ? 51   VAL B CA    1 
ATOM   9241  C  C     . VAL B 1  53   ? -24.842 10.803  92.248  1.00 33.12 ? 51   VAL B C     1 
ATOM   9242  O  O     . VAL B 1  53   ? -25.649 10.702  93.180  1.00 31.20 ? 51   VAL B O     1 
ATOM   9243  C  CB    . VAL B 1  53   ? -24.678 12.857  90.784  1.00 26.71 ? 51   VAL B CB    1 
ATOM   9244  C  CG1   . VAL B 1  53   ? -26.210 12.801  90.810  1.00 32.85 ? 51   VAL B CG1   1 
ATOM   9245  C  CG2   . VAL B 1  53   ? -24.205 14.297  90.777  1.00 29.53 ? 51   VAL B CG2   1 
ATOM   9246  N  N     . GLU B 1  54   ? -24.565 9.778   91.436  1.00 30.94 ? 52   GLU B N     1 
ATOM   9247  C  CA    . GLU B 1  54   ? -25.257 8.502   91.605  1.00 34.61 ? 52   GLU B CA    1 
ATOM   9248  C  C     . GLU B 1  54   ? -24.949 7.883   92.959  1.00 34.81 ? 52   GLU B C     1 
ATOM   9249  O  O     . GLU B 1  54   ? -25.848 7.363   93.630  1.00 32.87 ? 52   GLU B O     1 
ATOM   9250  C  CB    . GLU B 1  54   ? -24.877 7.538   90.479  1.00 35.04 ? 52   GLU B CB    1 
ATOM   9251  N  N     . ALA B 1  55   ? -23.682 7.935   93.381  1.00 32.17 ? 53   ALA B N     1 
ATOM   9252  C  CA    . ALA B 1  55   ? -23.303 7.347   94.661  1.00 33.34 ? 53   ALA B CA    1 
ATOM   9253  C  C     . ALA B 1  55   ? -23.876 8.124   95.840  1.00 32.13 ? 53   ALA B C     1 
ATOM   9254  O  O     . ALA B 1  55   ? -24.176 7.531   96.882  1.00 32.48 ? 53   ALA B O     1 
ATOM   9255  C  CB    . ALA B 1  55   ? -21.779 7.274   94.774  1.00 31.45 ? 53   ALA B CB    1 
ATOM   9256  N  N     . ALA B 1  56   ? -24.042 9.433   95.700  1.00 32.66 ? 54   ALA B N     1 
ATOM   9257  C  CA    . ALA B 1  56   ? -24.511 10.280  96.788  1.00 32.00 ? 54   ALA B CA    1 
ATOM   9258  C  C     . ALA B 1  56   ? -26.029 10.337  96.895  1.00 34.98 ? 54   ALA B C     1 
ATOM   9259  O  O     . ALA B 1  56   ? -26.541 11.003  97.800  1.00 37.47 ? 54   ALA B O     1 
ATOM   9260  C  CB    . ALA B 1  56   ? -23.963 11.698  96.619  1.00 32.67 ? 54   ALA B CB    1 
ATOM   9261  N  N     . THR B 1  57   ? -26.752 9.670   95.995  1.00 35.82 ? 55   THR B N     1 
ATOM   9262  C  CA    . THR B 1  57   ? -28.210 9.745   95.976  1.00 39.36 ? 55   THR B CA    1 
ATOM   9263  C  C     . THR B 1  57   ? -28.819 9.112   97.217  1.00 38.75 ? 55   THR B C     1 
ATOM   9264  O  O     . THR B 1  57   ? -28.402 8.034   97.647  1.00 38.96 ? 55   THR B O     1 
ATOM   9265  C  CB    . THR B 1  57   ? -28.760 9.034   94.741  1.00 44.42 ? 55   THR B CB    1 
ATOM   9266  O  OG1   . THR B 1  57   ? -28.144 7.745   94.633  1.00 48.12 ? 55   THR B OG1   1 
ATOM   9267  C  CG2   . THR B 1  57   ? -28.476 9.830   93.496  1.00 35.56 ? 55   THR B CG2   1 
ATOM   9268  N  N     . GLN B 1  58   ? -29.826 9.783   97.782  1.00 41.61 ? 56   GLN B N     1 
ATOM   9269  C  CA    . GLN B 1  58   ? -30.549 9.297   98.949  1.00 42.38 ? 56   GLN B CA    1 
ATOM   9270  C  C     . GLN B 1  58   ? -32.051 9.406   98.706  1.00 45.68 ? 56   GLN B C     1 
ATOM   9271  O  O     . GLN B 1  58   ? -32.514 10.276  97.962  1.00 45.03 ? 56   GLN B O     1 
ATOM   9272  C  CB    . GLN B 1  58   ? -30.162 10.076  100.223 1.00 44.88 ? 56   GLN B CB    1 
ATOM   9273  C  CG    . GLN B 1  58   ? -28.652 10.217  100.456 1.00 40.22 ? 56   GLN B CG    1 
ATOM   9274  C  CD    . GLN B 1  58   ? -28.256 9.989   101.908 1.00 43.69 ? 56   GLN B CD    1 
ATOM   9275  O  OE1   . GLN B 1  58   ? -28.481 8.913   102.461 1.00 48.31 ? 56   GLN B OE1   1 
ATOM   9276  N  NE2   . GLN B 1  58   ? -27.666 11.004  102.533 1.00 42.69 ? 56   GLN B NE2   1 
ATOM   9277  N  N     . SER B 1  59   ? -32.808 8.516   99.348  1.00 48.44 ? 57   SER B N     1 
ATOM   9278  C  CA    . SER B 1  59   ? -34.259 8.496   99.193  1.00 47.24 ? 57   SER B CA    1 
ATOM   9279  C  C     . SER B 1  59   ? -34.885 9.791   99.711  1.00 47.71 ? 57   SER B C     1 
ATOM   9280  O  O     . SER B 1  59   ? -34.287 10.538  100.491 1.00 46.62 ? 57   SER B O     1 
ATOM   9281  C  CB    . SER B 1  59   ? -34.867 7.309   99.939  1.00 50.10 ? 57   SER B CB    1 
ATOM   9282  O  OG    . SER B 1  59   ? -34.755 7.481   101.344 1.00 49.71 ? 57   SER B OG    1 
ATOM   9283  N  N     . LYS B 1  60   ? -36.118 10.047  99.268  1.00 46.81 ? 58   LYS B N     1 
ATOM   9284  C  CA    . LYS B 1  60   ? -36.845 11.222  99.740  1.00 50.44 ? 58   LYS B CA    1 
ATOM   9285  C  C     . LYS B 1  60   ? -36.989 11.217  101.256 1.00 47.74 ? 58   LYS B C     1 
ATOM   9286  O  O     . LYS B 1  60   ? -36.962 12.282  101.885 1.00 49.43 ? 58   LYS B O     1 
ATOM   9287  C  CB    . LYS B 1  60   ? -38.226 11.295  99.082  1.00 45.27 ? 58   LYS B CB    1 
ATOM   9288  N  N     . GLU B 1  61   ? -37.146 10.035  101.857 1.00 47.25 ? 59   GLU B N     1 
ATOM   9289  C  CA    . GLU B 1  61   ? -37.301 9.952   103.306 1.00 49.10 ? 59   GLU B CA    1 
ATOM   9290  C  C     . GLU B 1  61   ? -36.055 10.467  104.014 1.00 49.09 ? 59   GLU B C     1 
ATOM   9291  O  O     . GLU B 1  61   ? -36.130 11.356  104.871 1.00 48.72 ? 59   GLU B O     1 
ATOM   9292  C  CB    . GLU B 1  61   ? -37.600 8.509   103.717 1.00 49.29 ? 59   GLU B CB    1 
ATOM   9293  N  N     . ILE B 1  62   ? -34.892 9.930   103.645 1.00 50.03 ? 60   ILE B N     1 
ATOM   9294  C  CA    . ILE B 1  62   ? -33.638 10.337  104.273 1.00 46.93 ? 60   ILE B CA    1 
ATOM   9295  C  C     . ILE B 1  62   ? -33.381 11.824  104.057 1.00 45.24 ? 60   ILE B C     1 
ATOM   9296  O  O     . ILE B 1  62   ? -32.968 12.536  104.982 1.00 46.05 ? 60   ILE B O     1 
ATOM   9297  C  CB    . ILE B 1  62   ? -32.487 9.467   103.737 1.00 49.85 ? 60   ILE B CB    1 
ATOM   9298  C  CG1   . ILE B 1  62   ? -32.655 8.025   104.229 1.00 48.14 ? 60   ILE B CG1   1 
ATOM   9299  C  CG2   . ILE B 1  62   ? -31.129 10.049  104.127 1.00 47.83 ? 60   ILE B CG2   1 
ATOM   9300  C  CD1   . ILE B 1  62   ? -31.492 7.121   103.889 1.00 47.68 ? 60   ILE B CD1   1 
ATOM   9301  N  N     . ARG B 1  63   ? -33.643 12.321  102.845 1.00 44.79 ? 61   ARG B N     1 
ATOM   9302  C  CA    . ARG B 1  63   ? -33.321 13.709  102.521 1.00 44.16 ? 61   ARG B CA    1 
ATOM   9303  C  C     . ARG B 1  63   ? -34.149 14.681  103.352 1.00 45.49 ? 61   ARG B C     1 
ATOM   9304  O  O     . ARG B 1  63   ? -33.628 15.677  103.865 1.00 45.38 ? 61   ARG B O     1 
ATOM   9305  C  CB    . ARG B 1  63   ? -33.526 13.967  101.027 1.00 45.61 ? 61   ARG B CB    1 
ATOM   9306  C  CG    . ARG B 1  63   ? -32.618 13.147  100.120 1.00 47.08 ? 61   ARG B CG    1 
ATOM   9307  C  CD    . ARG B 1  63   ? -32.578 13.711  98.706  1.00 46.10 ? 61   ARG B CD    1 
ATOM   9308  N  NE    . ARG B 1  63   ? -33.904 13.915  98.134  1.00 47.42 ? 61   ARG B NE    1 
ATOM   9309  C  CZ    . ARG B 1  63   ? -34.550 13.024  97.395  1.00 50.92 ? 61   ARG B CZ    1 
ATOM   9310  N  NH1   . ARG B 1  63   ? -34.031 11.836  97.134  1.00 53.33 ? 61   ARG B NH1   1 
ATOM   9311  N  NH2   . ARG B 1  63   ? -35.749 13.331  96.906  1.00 52.15 ? 61   ARG B NH2   1 
ATOM   9312  N  N     . ASP B 1  64   ? -35.453 14.420  103.481 1.00 45.82 ? 62   ASP B N     1 
ATOM   9313  C  CA    . ASP B 1  64   ? -36.275 15.273  104.332 1.00 46.18 ? 62   ASP B CA    1 
ATOM   9314  C  C     . ASP B 1  64   ? -35.829 15.184  105.786 1.00 43.79 ? 62   ASP B C     1 
ATOM   9315  O  O     . ASP B 1  64   ? -35.700 16.209  106.467 1.00 45.65 ? 62   ASP B O     1 
ATOM   9316  C  CB    . ASP B 1  64   ? -37.747 14.894  104.191 1.00 45.88 ? 62   ASP B CB    1 
ATOM   9317  C  CG    . ASP B 1  64   ? -38.298 15.214  102.816 1.00 52.31 ? 62   ASP B CG    1 
ATOM   9318  O  OD1   . ASP B 1  64   ? -37.958 16.289  102.274 1.00 52.82 ? 62   ASP B OD1   1 
ATOM   9319  O  OD2   . ASP B 1  64   ? -39.070 14.393  102.277 1.00 56.47 ? 62   ASP B OD2   1 
ATOM   9320  N  N     . ALA B 1  65   ? -35.570 13.969  106.272 1.00 39.90 ? 63   ALA B N     1 
ATOM   9321  C  CA    . ALA B 1  65   ? -35.086 13.807  107.639 1.00 44.44 ? 63   ALA B CA    1 
ATOM   9322  C  C     . ALA B 1  65   ? -33.778 14.558  107.855 1.00 48.27 ? 63   ALA B C     1 
ATOM   9323  O  O     . ALA B 1  65   ? -33.557 15.142  108.924 1.00 48.13 ? 63   ALA B O     1 
ATOM   9324  C  CB    . ALA B 1  65   ? -34.913 12.324  107.960 1.00 46.09 ? 63   ALA B CB    1 
ATOM   9325  N  N     . ALA B 1  66   ? -32.903 14.567  106.844 1.00 45.48 ? 64   ALA B N     1 
ATOM   9326  C  CA    . ALA B 1  66   ? -31.608 15.219  106.994 1.00 42.85 ? 64   ALA B CA    1 
ATOM   9327  C  C     . ALA B 1  66   ? -31.743 16.736  106.953 1.00 45.10 ? 64   ALA B C     1 
ATOM   9328  O  O     . ALA B 1  66   ? -31.036 17.446  107.679 1.00 42.79 ? 64   ALA B O     1 
ATOM   9329  C  CB    . ALA B 1  66   ? -30.650 14.730  105.908 1.00 46.55 ? 64   ALA B CB    1 
ATOM   9330  N  N     . ALA B 1  67   ? -32.647 17.256  106.119 1.00 42.90 ? 65   ALA B N     1 
ATOM   9331  C  CA    . ALA B 1  67   ? -32.839 18.702  106.078 1.00 47.38 ? 65   ALA B CA    1 
ATOM   9332  C  C     . ALA B 1  67   ? -33.395 19.226  107.395 1.00 48.41 ? 65   ALA B C     1 
ATOM   9333  O  O     . ALA B 1  67   ? -33.107 20.367  107.778 1.00 47.05 ? 65   ALA B O     1 
ATOM   9334  C  CB    . ALA B 1  67   ? -33.760 19.087  104.919 1.00 47.10 ? 65   ALA B CB    1 
ATOM   9335  N  N     . SER B 1  68   ? -34.179 18.407  108.099 1.00 50.77 ? 66   SER B N     1 
ATOM   9336  C  CA    . SER B 1  68   ? -34.707 18.795  109.402 1.00 50.19 ? 66   SER B CA    1 
ATOM   9337  C  C     . SER B 1  68   ? -33.632 18.711  110.478 1.00 51.63 ? 66   SER B C     1 
ATOM   9338  O  O     . SER B 1  68   ? -33.473 19.637  111.282 1.00 53.62 ? 66   SER B O     1 
ATOM   9339  C  CB    . SER B 1  68   ? -35.901 17.911  109.764 1.00 51.61 ? 66   SER B CB    1 
ATOM   9340  O  OG    . SER B 1  68   ? -36.441 18.279  111.020 1.00 57.13 ? 66   SER B OG    1 
ATOM   9341  N  N     . THR B 1  69   ? -32.895 17.597  110.514 1.00 47.76 ? 67   THR B N     1 
ATOM   9342  C  CA    . THR B 1  69   ? -31.762 17.476  111.426 1.00 45.86 ? 67   THR B CA    1 
ATOM   9343  C  C     . THR B 1  69   ? -30.808 18.653  111.274 1.00 46.76 ? 67   THR B C     1 
ATOM   9344  O  O     . THR B 1  69   ? -30.389 19.265  112.264 1.00 47.63 ? 67   THR B O     1 
ATOM   9345  C  CB    . THR B 1  69   ? -31.026 16.160  111.177 1.00 44.42 ? 67   THR B CB    1 
ATOM   9346  O  OG1   . THR B 1  69   ? -31.852 15.063  111.576 1.00 44.25 ? 67   THR B OG1   1 
ATOM   9347  C  CG2   . THR B 1  69   ? -29.720 16.121  111.963 1.00 45.58 ? 67   THR B CG2   1 
ATOM   9348  N  N     . ALA B 1  70   ? -30.453 18.985  110.030 1.00 45.07 ? 68   ALA B N     1 
ATOM   9349  C  CA    . ALA B 1  70   ? -29.575 20.125  109.796 1.00 44.68 ? 68   ALA B CA    1 
ATOM   9350  C  C     . ALA B 1  70   ? -30.236 21.426  110.231 1.00 47.42 ? 68   ALA B C     1 
ATOM   9351  O  O     . ALA B 1  70   ? -29.566 22.326  110.755 1.00 46.04 ? 68   ALA B O     1 
ATOM   9352  C  CB    . ALA B 1  70   ? -29.174 20.185  108.321 1.00 44.43 ? 68   ALA B CB    1 
ATOM   9353  N  N     . ARG B 1  71   ? -31.552 21.545  110.023 1.00 49.03 ? 69   ARG B N     1 
ATOM   9354  C  CA    . ARG B 1  71   ? -32.283 22.701  110.535 1.00 50.13 ? 69   ARG B CA    1 
ATOM   9355  C  C     . ARG B 1  71   ? -32.125 22.813  112.045 1.00 42.01 ? 69   ARG B C     1 
ATOM   9356  O  O     . ARG B 1  71   ? -31.859 23.898  112.573 1.00 46.84 ? 69   ARG B O     1 
ATOM   9357  C  CB    . ARG B 1  71   ? -33.764 22.605  110.156 1.00 48.05 ? 69   ARG B CB    1 
ATOM   9358  N  N     . LYS B 1  72   ? -32.270 21.691  112.753 1.00 42.41 ? 70   LYS B N     1 
ATOM   9359  C  CA    . LYS B 1  72   ? -32.153 21.707  114.208 1.00 46.45 ? 70   LYS B CA    1 
ATOM   9360  C  C     . LYS B 1  72   ? -30.765 22.159  114.646 1.00 48.73 ? 70   LYS B C     1 
ATOM   9361  O  O     . LYS B 1  72   ? -30.622 22.923  115.610 1.00 46.21 ? 70   LYS B O     1 
ATOM   9362  C  CB    . LYS B 1  72   ? -32.473 20.322  114.771 1.00 47.43 ? 70   LYS B CB    1 
ATOM   9363  N  N     . LEU B 1  73   ? -29.728 21.707  113.937 1.00 48.23 ? 71   LEU B N     1 
ATOM   9364  C  CA    . LEU B 1  73   ? -28.365 22.063  114.312 1.00 45.26 ? 71   LEU B CA    1 
ATOM   9365  C  C     . LEU B 1  73   ? -28.102 23.546  114.092 1.00 46.09 ? 71   LEU B C     1 
ATOM   9366  O  O     . LEU B 1  73   ? -27.518 24.211  114.954 1.00 46.95 ? 71   LEU B O     1 
ATOM   9367  C  CB    . LEU B 1  73   ? -27.377 21.212  113.517 1.00 42.50 ? 71   LEU B CB    1 
ATOM   9368  C  CG    . LEU B 1  73   ? -27.517 19.708  113.753 1.00 44.13 ? 71   LEU B CG    1 
ATOM   9369  C  CD1   . LEU B 1  73   ? -26.717 18.921  112.729 1.00 42.18 ? 71   LEU B CD1   1 
ATOM   9370  C  CD2   . LEU B 1  73   ? -27.076 19.361  115.165 1.00 41.32 ? 71   LEU B CD2   1 
ATOM   9371  N  N     . ILE B 1  74   ? -28.549 24.084  112.957 1.00 46.89 ? 72   ILE B N     1 
ATOM   9372  C  CA    . ILE B 1  74   ? -28.225 25.464  112.608 1.00 50.41 ? 72   ILE B CA    1 
ATOM   9373  C  C     . ILE B 1  74   ? -28.992 26.441  113.494 1.00 49.39 ? 72   ILE B C     1 
ATOM   9374  O  O     . ILE B 1  74   ? -28.460 27.485  113.893 1.00 48.49 ? 72   ILE B O     1 
ATOM   9375  C  CB    . ILE B 1  74   ? -28.490 25.703  111.110 1.00 48.74 ? 72   ILE B CB    1 
ATOM   9376  C  CG1   . ILE B 1  74   ? -27.584 24.796  110.268 1.00 48.24 ? 72   ILE B CG1   1 
ATOM   9377  C  CG2   . ILE B 1  74   ? -28.251 27.162  110.750 1.00 49.12 ? 72   ILE B CG2   1 
ATOM   9378  C  CD1   . ILE B 1  74   ? -28.117 24.509  108.882 1.00 44.29 ? 72   ILE B CD1   1 
ATOM   9379  N  N     . GLU B 1  75   ? -30.250 26.126  113.812 1.00 48.69 ? 73   GLU B N     1 
ATOM   9380  C  CA    . GLU B 1  75   ? -30.997 26.951  114.759 1.00 49.73 ? 73   GLU B CA    1 
ATOM   9381  C  C     . GLU B 1  75   ? -30.301 26.979  116.115 1.00 48.46 ? 73   GLU B C     1 
ATOM   9382  O  O     . GLU B 1  75   ? -30.131 28.045  116.720 1.00 50.75 ? 73   GLU B O     1 
ATOM   9383  C  CB    . GLU B 1  75   ? -32.432 26.437  114.892 1.00 45.06 ? 73   GLU B CB    1 
ATOM   9384  N  N     . ALA B 1  76   ? -29.878 25.807  116.599 1.00 47.12 ? 74   ALA B N     1 
ATOM   9385  C  CA    . ALA B 1  76   ? -29.092 25.738  117.828 1.00 51.15 ? 74   ALA B CA    1 
ATOM   9386  C  C     . ALA B 1  76   ? -27.833 26.595  117.736 1.00 48.46 ? 74   ALA B C     1 
ATOM   9387  O  O     . ALA B 1  76   ? -27.514 27.350  118.661 1.00 50.41 ? 74   ALA B O     1 
ATOM   9388  C  CB    . ALA B 1  76   ? -28.735 24.283  118.136 1.00 44.45 ? 74   ALA B CB    1 
ATOM   9389  N  N     . LEU B 1  77   ? -27.100 26.491  116.624 1.00 46.69 ? 75   LEU B N     1 
ATOM   9390  C  CA    . LEU B 1  77   ? -25.864 27.252  116.480 1.00 48.05 ? 75   LEU B CA    1 
ATOM   9391  C  C     . LEU B 1  77   ? -26.138 28.751  116.453 1.00 50.53 ? 75   LEU B C     1 
ATOM   9392  O  O     . LEU B 1  77   ? -25.443 29.535  117.113 1.00 48.56 ? 75   LEU B O     1 
ATOM   9393  C  CB    . LEU B 1  77   ? -25.127 26.824  115.208 1.00 46.45 ? 75   LEU B CB    1 
ATOM   9394  C  CG    . LEU B 1  77   ? -24.542 25.412  115.176 1.00 47.16 ? 75   LEU B CG    1 
ATOM   9395  C  CD1   . LEU B 1  77   ? -24.096 25.053  113.766 1.00 43.74 ? 75   LEU B CD1   1 
ATOM   9396  C  CD2   . LEU B 1  77   ? -23.376 25.311  116.132 1.00 44.08 ? 75   LEU B CD2   1 
ATOM   9397  N  N     . ARG B 1  78   ? -27.132 29.175  115.668 1.00 46.54 ? 76   ARG B N     1 
ATOM   9398  C  CA    . ARG B 1  78   ? -27.458 30.593  115.601 1.00 49.57 ? 76   ARG B CA    1 
ATOM   9399  C  C     . ARG B 1  78   ? -28.158 31.088  116.859 1.00 50.23 ? 76   ARG B C     1 
ATOM   9400  O  O     . ARG B 1  78   ? -28.221 32.304  117.071 1.00 51.17 ? 76   ARG B O     1 
ATOM   9401  C  CB    . ARG B 1  78   ? -28.321 30.876  114.369 1.00 49.62 ? 76   ARG B CB    1 
ATOM   9402  C  CG    . ARG B 1  78   ? -27.593 30.599  113.062 1.00 50.16 ? 76   ARG B CG    1 
ATOM   9403  C  CD    . ARG B 1  78   ? -28.362 31.095  111.853 1.00 53.24 ? 76   ARG B CD    1 
ATOM   9404  N  NE    . ARG B 1  78   ? -27.452 31.576  110.818 1.00 57.55 ? 76   ARG B NE    1 
ATOM   9405  C  CZ    . ARG B 1  78   ? -27.836 32.096  109.659 1.00 58.37 ? 76   ARG B CZ    1 
ATOM   9406  N  NH1   . ARG B 1  78   ? -29.115 32.183  109.329 1.00 58.37 ? 76   ARG B NH1   1 
ATOM   9407  N  NH2   . ARG B 1  78   ? -26.913 32.547  108.813 1.00 60.61 ? 76   ARG B NH2   1 
ATOM   9408  N  N     . GLY B 1  79   ? -28.652 30.180  117.701 1.00 44.37 ? 77   GLY B N     1 
ATOM   9409  C  CA    . GLY B 1  79   ? -29.306 30.537  118.944 1.00 50.03 ? 77   GLY B CA    1 
ATOM   9410  C  C     . GLY B 1  79   ? -28.389 30.759  120.125 1.00 51.99 ? 77   GLY B C     1 
ATOM   9411  O  O     . GLY B 1  79   ? -28.850 31.209  121.179 1.00 44.97 ? 77   GLY B O     1 
ATOM   9412  N  N     . LYS B 1  80   ? -27.101 30.463  119.974 1.00 51.41 ? 78   LYS B N     1 
ATOM   9413  C  CA    . LYS B 1  80   ? -26.135 30.623  121.052 1.00 49.42 ? 78   LYS B CA    1 
ATOM   9414  C  C     . LYS B 1  80   ? -24.912 31.396  120.564 1.00 50.94 ? 78   LYS B C     1 
ATOM   9415  O  O     . LYS B 1  80   ? -24.541 32.417  121.143 1.00 58.65 ? 78   LYS B O     1 
ATOM   9416  C  CB    . LYS B 1  80   ? -25.721 29.255  121.602 1.00 50.32 ? 78   LYS B CB    1 
ATOM   9417  C  CG    . LYS B 1  80   ? -25.093 28.344  120.558 1.00 48.63 ? 78   LYS B CG    1 
ATOM   9418  C  CD    . LYS B 1  80   ? -25.073 26.888  121.001 1.00 46.45 ? 78   LYS B CD    1 
ATOM   9419  C  CE    . LYS B 1  80   ? -24.290 26.027  120.000 1.00 45.30 ? 78   LYS B CE    1 
ATOM   9420  N  NZ    . LYS B 1  80   ? -24.227 24.583  120.387 1.00 41.81 ? 78   LYS B NZ    1 
ATOM   9421  N  N     . GLY B 1  85   ? -15.708 36.267  121.545 1.00 46.83 ? 83   GLY B N     1 
ATOM   9422  C  CA    . GLY B 1  85   ? -14.881 36.978  122.499 1.00 45.36 ? 83   GLY B CA    1 
ATOM   9423  C  C     . GLY B 1  85   ? -14.335 38.289  121.965 1.00 47.18 ? 83   GLY B C     1 
ATOM   9424  O  O     . GLY B 1  85   ? -14.447 39.334  122.611 1.00 44.75 ? 83   GLY B O     1 
ATOM   9425  N  N     . VAL B 1  86   ? -13.727 38.234  120.779 1.00 46.22 ? 84   VAL B N     1 
ATOM   9426  C  CA    . VAL B 1  86   ? -13.170 39.446  120.192 1.00 44.74 ? 84   VAL B CA    1 
ATOM   9427  C  C     . VAL B 1  86   ? -14.286 40.384  119.745 1.00 44.56 ? 84   VAL B C     1 
ATOM   9428  O  O     . VAL B 1  86   ? -14.150 41.611  119.837 1.00 42.76 ? 84   VAL B O     1 
ATOM   9429  C  CB    . VAL B 1  86   ? -12.211 39.083  119.042 1.00 45.49 ? 84   VAL B CB    1 
ATOM   9430  C  CG1   . VAL B 1  86   ? -12.960 38.415  117.896 1.00 48.09 ? 84   VAL B CG1   1 
ATOM   9431  C  CG2   . VAL B 1  86   ? -11.454 40.314  118.560 1.00 45.57 ? 84   VAL B CG2   1 
ATOM   9432  N  N     . GLU B 1  87   ? -15.417 39.831  119.290 1.00 46.90 ? 85   GLU B N     1 
ATOM   9433  C  CA    . GLU B 1  87   ? -16.550 40.660  118.887 1.00 46.54 ? 85   GLU B CA    1 
ATOM   9434  C  C     . GLU B 1  87   ? -17.057 41.509  120.045 1.00 41.15 ? 85   GLU B C     1 
ATOM   9435  O  O     . GLU B 1  87   ? -17.423 42.675  119.857 1.00 42.10 ? 85   GLU B O     1 
ATOM   9436  C  CB    . GLU B 1  87   ? -17.674 39.777  118.338 1.00 51.36 ? 85   GLU B CB    1 
ATOM   9437  N  N     . GLY B 1  88   ? -17.088 40.940  121.253 1.00 46.39 ? 86   GLY B N     1 
ATOM   9438  C  CA    . GLY B 1  88   ? -17.516 41.704  122.411 1.00 41.69 ? 86   GLY B CA    1 
ATOM   9439  C  C     . GLY B 1  88   ? -16.495 42.730  122.856 1.00 40.50 ? 86   GLY B C     1 
ATOM   9440  O  O     . GLY B 1  88   ? -16.860 43.790  123.375 1.00 39.00 ? 86   GLY B O     1 
ATOM   9441  N  N     . LEU B 1  89   ? -15.207 42.428  122.680 1.00 38.33 ? 87   LEU B N     1 
ATOM   9442  C  CA    . LEU B 1  89   ? -14.172 43.421  122.945 1.00 41.23 ? 87   LEU B CA    1 
ATOM   9443  C  C     . LEU B 1  89   ? -14.314 44.614  122.009 1.00 36.16 ? 87   LEU B C     1 
ATOM   9444  O  O     . LEU B 1  89   ? -14.233 45.769  122.443 1.00 36.83 ? 87   LEU B O     1 
ATOM   9445  C  CB    . LEU B 1  89   ? -12.794 42.780  122.794 1.00 41.05 ? 87   LEU B CB    1 
ATOM   9446  C  CG    . LEU B 1  89   ? -11.574 43.675  122.990 1.00 38.97 ? 87   LEU B CG    1 
ATOM   9447  C  CD1   . LEU B 1  89   ? -11.440 44.062  124.436 1.00 40.54 ? 87   LEU B CD1   1 
ATOM   9448  C  CD2   . LEU B 1  89   ? -10.328 42.957  122.497 1.00 41.71 ? 87   LEU B CD2   1 
ATOM   9449  N  N     . VAL B 1  90   ? -14.546 44.345  120.722 1.00 37.32 ? 88   VAL B N     1 
ATOM   9450  C  CA    . VAL B 1  90   ? -14.723 45.408  119.735 1.00 38.49 ? 88   VAL B CA    1 
ATOM   9451  C  C     . VAL B 1  90   ? -15.922 46.278  120.094 1.00 38.53 ? 88   VAL B C     1 
ATOM   9452  O  O     . VAL B 1  90   ? -15.875 47.509  119.971 1.00 35.23 ? 88   VAL B O     1 
ATOM   9453  C  CB    . VAL B 1  90   ? -14.859 44.798  118.327 1.00 36.05 ? 88   VAL B CB    1 
ATOM   9454  C  CG1   . VAL B 1  90   ? -15.294 45.845  117.321 1.00 36.36 ? 88   VAL B CG1   1 
ATOM   9455  C  CG2   . VAL B 1  90   ? -13.544 44.163  117.892 1.00 35.12 ? 88   VAL B CG2   1 
ATOM   9456  N  N     . GLN B 1  91   ? -17.009 45.659  120.562 1.00 39.68 ? 89   GLN B N     1 
ATOM   9457  C  CA    . GLN B 1  91   ? -18.198 46.432  120.910 1.00 40.39 ? 89   GLN B CA    1 
ATOM   9458  C  C     . GLN B 1  91   ? -17.986 47.247  122.183 1.00 37.22 ? 89   GLN B C     1 
ATOM   9459  O  O     . GLN B 1  91   ? -18.353 48.426  122.237 1.00 38.96 ? 89   GLN B O     1 
ATOM   9460  C  CB    . GLN B 1  91   ? -19.403 45.501  121.051 1.00 41.80 ? 89   GLN B CB    1 
ATOM   9461  N  N     . GLU B 1  92   ? -17.381 46.650  123.211 1.00 38.11 ? 90   GLU B N     1 
ATOM   9462  C  CA    . GLU B 1  92   ? -17.221 47.355  124.479 1.00 38.72 ? 90   GLU B CA    1 
ATOM   9463  C  C     . GLU B 1  92   ? -16.389 48.623  124.318 1.00 39.03 ? 90   GLU B C     1 
ATOM   9464  O  O     . GLU B 1  92   ? -16.711 49.662  124.909 1.00 39.62 ? 90   GLU B O     1 
ATOM   9465  C  CB    . GLU B 1  92   ? -16.590 46.436  125.529 1.00 39.69 ? 90   GLU B CB    1 
ATOM   9466  C  CG    . GLU B 1  92   ? -16.394 47.118  126.880 1.00 43.09 ? 90   GLU B CG    1 
ATOM   9467  C  CD    . GLU B 1  92   ? -15.713 46.236  127.918 1.00 42.91 ? 90   GLU B CD    1 
ATOM   9468  O  OE1   . GLU B 1  92   ? -15.386 45.072  127.603 1.00 44.34 ? 90   GLU B OE1   1 
ATOM   9469  O  OE2   . GLU B 1  92   ? -15.508 46.714  129.053 1.00 40.19 ? 90   GLU B OE2   1 
ATOM   9470  N  N     . TYR B 1  93   ? -15.321 48.567  123.524 1.00 37.78 ? 91   TYR B N     1 
ATOM   9471  C  CA    . TYR B 1  93   ? -14.441 49.715  123.356 1.00 37.02 ? 91   TYR B CA    1 
ATOM   9472  C  C     . TYR B 1  93   ? -14.645 50.424  122.024 1.00 36.97 ? 91   TYR B C     1 
ATOM   9473  O  O     . TYR B 1  93   ? -13.854 51.313  121.686 1.00 36.87 ? 91   TYR B O     1 
ATOM   9474  C  CB    . TYR B 1  93   ? -12.980 49.291  123.524 1.00 34.22 ? 91   TYR B CB    1 
ATOM   9475  C  CG    . TYR B 1  93   ? -12.649 48.937  124.959 1.00 36.16 ? 91   TYR B CG    1 
ATOM   9476  C  CD1   . TYR B 1  93   ? -12.240 49.913  125.862 1.00 36.23 ? 91   TYR B CD1   1 
ATOM   9477  C  CD2   . TYR B 1  93   ? -12.772 47.633  125.419 1.00 37.54 ? 91   TYR B CD2   1 
ATOM   9478  C  CE1   . TYR B 1  93   ? -11.954 49.597  127.183 1.00 33.08 ? 91   TYR B CE1   1 
ATOM   9479  C  CE2   . TYR B 1  93   ? -12.485 47.309  126.738 1.00 36.76 ? 91   TYR B CE2   1 
ATOM   9480  C  CZ    . TYR B 1  93   ? -12.076 48.294  127.611 1.00 33.96 ? 91   TYR B CZ    1 
ATOM   9481  O  OH    . TYR B 1  93   ? -11.788 47.974  128.919 1.00 36.48 ? 91   TYR B OH    1 
ATOM   9482  N  N     . SER B 1  94   ? -15.691 50.058  121.275 1.00 34.60 ? 92   SER B N     1 
ATOM   9483  C  CA    . SER B 1  94   ? -16.061 50.725  120.025 1.00 32.63 ? 92   SER B CA    1 
ATOM   9484  C  C     . SER B 1  94   ? -14.889 50.757  119.047 1.00 33.24 ? 92   SER B C     1 
ATOM   9485  O  O     . SER B 1  94   ? -14.577 51.786  118.446 1.00 33.35 ? 92   SER B O     1 
ATOM   9486  C  CB    . SER B 1  94   ? -16.589 52.134  120.287 1.00 35.44 ? 92   SER B CB    1 
ATOM   9487  O  OG    . SER B 1  94   ? -17.700 52.098  121.161 1.00 39.71 ? 92   SER B OG    1 
ATOM   9488  N  N     . LEU B 1  95   ? -14.244 49.608  118.884 1.00 27.27 ? 93   LEU B N     1 
ATOM   9489  C  CA    . LEU B 1  95   ? -13.067 49.529  118.035 1.00 29.57 ? 93   LEU B CA    1 
ATOM   9490  C  C     . LEU B 1  95   ? -13.453 49.446  116.569 1.00 29.90 ? 93   LEU B C     1 
ATOM   9491  O  O     . LEU B 1  95   ? -14.401 48.751  116.193 1.00 30.27 ? 93   LEU B O     1 
ATOM   9492  C  CB    . LEU B 1  95   ? -12.225 48.312  118.399 1.00 26.30 ? 93   LEU B CB    1 
ATOM   9493  C  CG    . LEU B 1  95   ? -11.740 48.246  119.844 1.00 31.83 ? 93   LEU B CG    1 
ATOM   9494  C  CD1   . LEU B 1  95   ? -10.777 47.081  120.012 1.00 28.38 ? 93   LEU B CD1   1 
ATOM   9495  C  CD2   . LEU B 1  95   ? -11.090 49.564  120.253 1.00 29.49 ? 93   LEU B CD2   1 
ATOM   9496  N  N     . SER B 1  96   ? -12.696 50.148  115.734 1.00 26.69 ? 94   SER B N     1 
ATOM   9497  C  CA    . SER B 1  96   ? -12.728 49.849  114.320 1.00 26.86 ? 94   SER B CA    1 
ATOM   9498  C  C     . SER B 1  96   ? -12.072 48.492  114.078 1.00 27.86 ? 94   SER B C     1 
ATOM   9499  O  O     . SER B 1  96   ? -11.420 47.924  114.959 1.00 25.96 ? 94   SER B O     1 
ATOM   9500  C  CB    . SER B 1  96   ? -11.997 50.930  113.531 1.00 27.01 ? 94   SER B CB    1 
ATOM   9501  O  OG    . SER B 1  96   ? -10.607 50.878  113.824 1.00 22.93 ? 94   SER B OG    1 
ATOM   9502  N  N     . SER B 1  97   ? -12.224 47.977  112.860 1.00 24.18 ? 95   SER B N     1 
ATOM   9503  C  CA    . SER B 1  97   ? -11.560 46.725  112.510 1.00 24.51 ? 95   SER B CA    1 
ATOM   9504  C  C     . SER B 1  97   ? -10.044 46.850  112.634 1.00 24.56 ? 95   SER B C     1 
ATOM   9505  O  O     . SER B 1  97   ? -9.387  45.994  113.235 1.00 24.17 ? 95   SER B O     1 
ATOM   9506  C  CB    . SER B 1  97   ? -11.950 46.296  111.094 1.00 30.09 ? 95   SER B CB    1 
ATOM   9507  O  OG    . SER B 1  97   ? -13.340 46.007  111.044 1.00 35.22 ? 95   SER B OG    1 
ATOM   9508  N  N     . GLN B 1  98   ? -9.472  47.918  112.079 1.00 21.92 ? 96   GLN B N     1 
ATOM   9509  C  CA    . GLN B 1  98   ? -8.024  48.103  112.163 1.00 23.44 ? 96   GLN B CA    1 
ATOM   9510  C  C     . GLN B 1  98   ? -7.564  48.271  113.609 1.00 21.32 ? 96   GLN B C     1 
ATOM   9511  O  O     . GLN B 1  98   ? -6.476  47.814  113.977 1.00 22.98 ? 96   GLN B O     1 
ATOM   9512  C  CB    . GLN B 1  98   ? -7.596  49.307  111.321 1.00 21.88 ? 96   GLN B CB    1 
ATOM   9513  C  CG    . GLN B 1  98   ? -7.659  49.066  109.826 1.00 23.17 ? 96   GLN B CG    1 
ATOM   9514  C  CD    . GLN B 1  98   ? -6.681  48.009  109.387 1.00 24.49 ? 96   GLN B CD    1 
ATOM   9515  O  OE1   . GLN B 1  98   ? -6.959  46.815  109.486 1.00 27.48 ? 96   GLN B OE1   1 
ATOM   9516  N  NE2   . GLN B 1  98   ? -5.518  48.436  108.897 1.00 21.16 ? 96   GLN B NE2   1 
ATOM   9517  N  N     . GLU B 1  99   ? -8.371  48.927  114.442 1.00 21.46 ? 97   GLU B N     1 
ATOM   9518  C  CA    . GLU B 1  99   ? -8.022  49.026  115.854 1.00 21.75 ? 97   GLU B CA    1 
ATOM   9519  C  C     . GLU B 1  99   ? -8.070  47.659  116.523 1.00 24.95 ? 97   GLU B C     1 
ATOM   9520  O  O     . GLU B 1  99   ? -7.209  47.336  117.349 1.00 23.35 ? 97   GLU B O     1 
ATOM   9521  C  CB    . GLU B 1  99   ? -8.949  50.005  116.562 1.00 24.08 ? 97   GLU B CB    1 
ATOM   9522  C  CG    . GLU B 1  99   ? -8.684  51.452  116.206 1.00 23.38 ? 97   GLU B CG    1 
ATOM   9523  C  CD    . GLU B 1  99   ? -9.760  52.380  116.729 1.00 24.07 ? 97   GLU B CD    1 
ATOM   9524  O  OE1   . GLU B 1  99   ? -10.772 51.885  117.280 1.00 26.05 ? 97   GLU B OE1   1 
ATOM   9525  O  OE2   . GLU B 1  99   ? -9.599  53.613  116.602 1.00 23.97 ? 97   GLU B OE2   1 
ATOM   9526  N  N     . GLY B 1  100  ? -9.071  46.844  116.179 1.00 22.98 ? 98   GLY B N     1 
ATOM   9527  C  CA    . GLY B 1  100  ? -9.116  45.495  116.715 1.00 23.31 ? 98   GLY B CA    1 
ATOM   9528  C  C     . GLY B 1  100  ? -7.914  44.668  116.299 1.00 24.53 ? 98   GLY B C     1 
ATOM   9529  O  O     . GLY B 1  100  ? -7.340  43.941  117.112 1.00 23.10 ? 98   GLY B O     1 
ATOM   9530  N  N     . VAL B 1  101  ? -7.514  44.774  115.029 1.00 23.10 ? 99   VAL B N     1 
ATOM   9531  C  CA    . VAL B 1  101  ? -6.344  44.043  114.555 1.00 22.32 ? 99   VAL B CA    1 
ATOM   9532  C  C     . VAL B 1  101  ? -5.090  44.541  115.263 1.00 24.77 ? 99   VAL B C     1 
ATOM   9533  O  O     . VAL B 1  101  ? -4.255  43.751  115.724 1.00 23.78 ? 99   VAL B O     1 
ATOM   9534  C  CB    . VAL B 1  101  ? -6.205  44.179  113.029 1.00 23.20 ? 99   VAL B CB    1 
ATOM   9535  C  CG1   . VAL B 1  101  ? -4.892  43.587  112.580 1.00 23.69 ? 99   VAL B CG1   1 
ATOM   9536  C  CG2   . VAL B 1  101  ? -7.376  43.509  112.310 1.00 24.92 ? 99   VAL B CG2   1 
ATOM   9537  N  N     . ALA B 1  102  ? -4.928  45.868  115.330 1.00 22.62 ? 100  ALA B N     1 
ATOM   9538  C  CA    . ALA B 1  102  ? -3.746  46.444  115.963 1.00 22.45 ? 100  ALA B CA    1 
ATOM   9539  C  C     . ALA B 1  102  ? -3.652  46.017  117.418 1.00 21.74 ? 100  ALA B C     1 
ATOM   9540  O  O     . ALA B 1  102  ? -2.565  45.699  117.916 1.00 23.14 ? 100  ALA B O     1 
ATOM   9541  C  CB    . ALA B 1  102  ? -3.794  47.970  115.870 1.00 19.75 ? 100  ALA B CB    1 
ATOM   9542  N  N     . LEU B 1  103  ? -4.788  46.007  118.116 1.00 20.81 ? 101  LEU B N     1 
ATOM   9543  C  CA    . LEU B 1  103  ? -4.780  45.656  119.529 1.00 23.21 ? 101  LEU B CA    1 
ATOM   9544  C  C     . LEU B 1  103  ? -4.356  44.209  119.733 1.00 24.47 ? 101  LEU B C     1 
ATOM   9545  O  O     . LEU B 1  103  ? -3.588  43.901  120.658 1.00 25.20 ? 101  LEU B O     1 
ATOM   9546  C  CB    . LEU B 1  103  ? -6.161  45.906  120.131 1.00 22.93 ? 101  LEU B CB    1 
ATOM   9547  C  CG    . LEU B 1  103  ? -6.370  45.469  121.569 1.00 22.93 ? 101  LEU B CG    1 
ATOM   9548  C  CD1   . LEU B 1  103  ? -5.469  46.273  122.492 1.00 25.56 ? 101  LEU B CD1   1 
ATOM   9549  C  CD2   . LEU B 1  103  ? -7.834  45.632  121.937 1.00 23.96 ? 101  LEU B CD2   1 
ATOM   9550  N  N     . MET B 1  104  ? -4.842  43.306  118.882 1.00 22.49 ? 102  MET B N     1 
ATOM   9551  C  CA    . MET B 1  104  ? -4.450  41.906  119.002 1.00 26.22 ? 102  MET B CA    1 
ATOM   9552  C  C     . MET B 1  104  ? -2.973  41.723  118.685 1.00 25.44 ? 102  MET B C     1 
ATOM   9553  O  O     . MET B 1  104  ? -2.295  40.900  119.313 1.00 25.71 ? 102  MET B O     1 
ATOM   9554  C  CB    . MET B 1  104  ? -5.321  41.037  118.096 1.00 25.57 ? 102  MET B CB    1 
ATOM   9555  C  CG    . MET B 1  104  ? -6.795  41.075  118.488 1.00 26.56 ? 102  MET B CG    1 
ATOM   9556  S  SD    . MET B 1  104  ? -7.114  40.710  120.243 1.00 35.83 ? 102  MET B SD    1 
ATOM   9557  C  CE    . MET B 1  104  ? -6.645  38.988  120.291 1.00 38.13 ? 102  MET B CE    1 
ATOM   9558  N  N     . CYS B 1  105  ? -2.450  42.498  117.734 1.00 21.39 ? 103  CYS B N     1 
ATOM   9559  C  CA    . CYS B 1  105  ? -1.014  42.464  117.472 1.00 23.55 ? 103  CYS B CA    1 
ATOM   9560  C  C     . CYS B 1  105  ? -0.230  42.905  118.696 1.00 24.94 ? 103  CYS B C     1 
ATOM   9561  O  O     . CYS B 1  105  ? 0.777   42.285  119.059 1.00 25.39 ? 103  CYS B O     1 
ATOM   9562  C  CB    . CYS B 1  105  ? -0.669  43.354  116.275 1.00 21.91 ? 103  CYS B CB    1 
ATOM   9563  S  SG    . CYS B 1  105  ? -1.234  42.739  114.698 1.00 23.85 ? 103  CYS B SG    1 
ATOM   9564  N  N     . LEU B 1  106  ? -0.673  43.993  119.338 1.00 21.85 ? 104  LEU B N     1 
ATOM   9565  C  CA    . LEU B 1  106  ? -0.037  44.440  120.572 1.00 22.46 ? 104  LEU B CA    1 
ATOM   9566  C  C     . LEU B 1  106  ? -0.142  43.377  121.652 1.00 26.50 ? 104  LEU B C     1 
ATOM   9567  O  O     . LEU B 1  106  ? 0.831   43.112  122.371 1.00 27.07 ? 104  LEU B O     1 
ATOM   9568  C  CB    . LEU B 1  106  ? -0.679  45.742  121.057 1.00 23.90 ? 104  LEU B CB    1 
ATOM   9569  C  CG    . LEU B 1  106  ? -0.209  46.216  122.436 1.00 24.12 ? 104  LEU B CG    1 
ATOM   9570  C  CD1   . LEU B 1  106  ? 1.231   46.681  122.358 1.00 26.11 ? 104  LEU B CD1   1 
ATOM   9571  C  CD2   . LEU B 1  106  ? -1.092  47.316  122.983 1.00 25.61 ? 104  LEU B CD2   1 
ATOM   9572  N  N     . ALA B 1  107  ? -1.327  42.777  121.797 1.00 24.66 ? 105  ALA B N     1 
ATOM   9573  C  CA    . ALA B 1  107  ? -1.513  41.733  122.799 1.00 26.01 ? 105  ALA B CA    1 
ATOM   9574  C  C     . ALA B 1  107  ? -0.609  40.542  122.516 1.00 29.50 ? 105  ALA B C     1 
ATOM   9575  O  O     . ALA B 1  107  ? -0.028  39.965  123.442 1.00 31.45 ? 105  ALA B O     1 
ATOM   9576  C  CB    . ALA B 1  107  ? -2.976  41.293  122.835 1.00 24.38 ? 105  ALA B CB    1 
ATOM   9577  N  N     . GLU B 1  108  ? -0.471  40.170  121.238 1.00 27.39 ? 106  GLU B N     1 
ATOM   9578  C  CA    . GLU B 1  108  ? 0.430   39.084  120.857 1.00 29.21 ? 106  GLU B CA    1 
ATOM   9579  C  C     . GLU B 1  108  ? 1.853   39.387  121.299 1.00 31.75 ? 106  GLU B C     1 
ATOM   9580  O  O     . GLU B 1  108  ? 2.541   38.528  121.867 1.00 32.11 ? 106  GLU B O     1 
ATOM   9581  C  CB    . GLU B 1  108  ? 0.374   38.863  119.342 1.00 29.06 ? 106  GLU B CB    1 
ATOM   9582  C  CG    . GLU B 1  108  ? 1.488   37.980  118.791 1.00 31.33 ? 106  GLU B CG    1 
ATOM   9583  C  CD    . GLU B 1  108  ? 1.598   38.032  117.270 1.00 35.47 ? 106  GLU B CD    1 
ATOM   9584  O  OE1   . GLU B 1  108  ? 0.622   38.457  116.611 1.00 33.96 ? 106  GLU B OE1   1 
ATOM   9585  O  OE2   . GLU B 1  108  ? 2.670   37.652  116.728 1.00 35.34 ? 106  GLU B OE2   1 
ATOM   9586  N  N     . ALA B 1  109  ? 2.310   40.614  121.051 1.00 30.89 ? 107  ALA B N     1 
ATOM   9587  C  CA    . ALA B 1  109  ? 3.673   40.974  121.421 1.00 33.04 ? 107  ALA B CA    1 
ATOM   9588  C  C     . ALA B 1  109  ? 3.849   40.989  122.934 1.00 33.91 ? 107  ALA B C     1 
ATOM   9589  O  O     . ALA B 1  109  ? 4.887   40.553  123.446 1.00 31.51 ? 107  ALA B O     1 
ATOM   9590  C  CB    . ALA B 1  109  ? 4.037   42.329  120.822 1.00 33.51 ? 107  ALA B CB    1 
ATOM   9591  N  N     . LEU B 1  110  ? 2.845   41.484  123.665 1.00 30.06 ? 108  LEU B N     1 
ATOM   9592  C  CA    . LEU B 1  110  ? 2.929   41.499  125.121 1.00 30.73 ? 108  LEU B CA    1 
ATOM   9593  C  C     . LEU B 1  110  ? 2.913   40.092  125.697 1.00 33.84 ? 108  LEU B C     1 
ATOM   9594  O  O     . LEU B 1  110  ? 3.494   39.852  126.761 1.00 35.99 ? 108  LEU B O     1 
ATOM   9595  C  CB    . LEU B 1  110  ? 1.783   42.321  125.710 1.00 29.88 ? 108  LEU B CB    1 
ATOM   9596  C  CG    . LEU B 1  110  ? 1.892   43.832  125.478 1.00 27.87 ? 108  LEU B CG    1 
ATOM   9597  C  CD1   . LEU B 1  110  ? 0.606   44.538  125.905 1.00 30.57 ? 108  LEU B CD1   1 
ATOM   9598  C  CD2   . LEU B 1  110  ? 3.102   44.398  126.221 1.00 32.28 ? 108  LEU B CD2   1 
ATOM   9599  N  N     . LEU B 1  111  ? 2.271   39.149  125.011 1.00 31.85 ? 109  LEU B N     1 
ATOM   9600  C  CA    . LEU B 1  111  ? 2.269   37.777  125.494 1.00 35.83 ? 109  LEU B CA    1 
ATOM   9601  C  C     . LEU B 1  111  ? 3.602   37.080  125.263 1.00 36.95 ? 109  LEU B C     1 
ATOM   9602  O  O     . LEU B 1  111  ? 3.850   36.033  125.870 1.00 37.12 ? 109  LEU B O     1 
ATOM   9603  C  CB    . LEU B 1  111  ? 1.141   36.989  124.841 1.00 36.25 ? 109  LEU B CB    1 
ATOM   9604  C  CG    . LEU B 1  111  ? -0.233  37.364  125.392 1.00 35.38 ? 109  LEU B CG    1 
ATOM   9605  C  CD1   . LEU B 1  111  ? -1.314  36.594  124.666 1.00 38.32 ? 109  LEU B CD1   1 
ATOM   9606  C  CD2   . LEU B 1  111  ? -0.293  37.116  126.894 1.00 38.53 ? 109  LEU B CD2   1 
ATOM   9607  N  N     . ARG B 1  112  ? 4.468   37.632  124.410 1.00 34.79 ? 110  ARG B N     1 
ATOM   9608  C  CA    . ARG B 1  112  ? 5.824   37.105  124.305 1.00 37.84 ? 110  ARG B CA    1 
ATOM   9609  C  C     . ARG B 1  112  ? 6.669   37.452  125.527 1.00 37.77 ? 110  ARG B C     1 
ATOM   9610  O  O     . ARG B 1  112  ? 7.800   36.968  125.645 1.00 40.37 ? 110  ARG B O     1 
ATOM   9611  C  CB    . ARG B 1  112  ? 6.493   37.608  123.019 1.00 37.86 ? 110  ARG B CB    1 
ATOM   9612  C  CG    . ARG B 1  112  ? 5.725   37.237  121.745 1.00 40.96 ? 110  ARG B CG    1 
ATOM   9613  C  CD    . ARG B 1  112  ? 6.564   37.381  120.466 1.00 46.23 ? 110  ARG B CD    1 
ATOM   9614  N  NE    . ARG B 1  112  ? 6.675   38.759  119.997 1.00 47.56 ? 110  ARG B NE    1 
ATOM   9615  C  CZ    . ARG B 1  112  ? 5.870   39.319  119.101 1.00 53.07 ? 110  ARG B CZ    1 
ATOM   9616  N  NH1   . ARG B 1  112  ? 4.869   38.647  118.551 1.00 47.12 ? 110  ARG B NH1   1 
ATOM   9617  N  NH2   . ARG B 1  112  ? 6.073   40.586  118.746 1.00 51.98 ? 110  ARG B NH2   1 
ATOM   9618  N  N     . ILE B 1  113  ? 6.150   38.267  126.440 1.00 38.07 ? 111  ILE B N     1 
ATOM   9619  C  CA    . ILE B 1  113  ? 6.789   38.511  127.729 1.00 40.28 ? 111  ILE B CA    1 
ATOM   9620  C  C     . ILE B 1  113  ? 6.302   37.429  128.689 1.00 41.35 ? 111  ILE B C     1 
ATOM   9621  O  O     . ILE B 1  113  ? 5.114   37.435  129.056 1.00 41.87 ? 111  ILE B O     1 
ATOM   9622  C  CB    . ILE B 1  113  ? 6.472   39.915  128.258 1.00 41.80 ? 111  ILE B CB    1 
ATOM   9623  C  CG1   . ILE B 1  113  ? 7.039   40.975  127.304 1.00 38.85 ? 111  ILE B CG1   1 
ATOM   9624  C  CG2   . ILE B 1  113  ? 7.007   40.085  129.674 1.00 37.02 ? 111  ILE B CG2   1 
ATOM   9625  C  CD1   . ILE B 1  113  ? 6.597   42.391  127.625 1.00 38.03 ? 111  ILE B CD1   1 
ATOM   9626  N  N     . PRO B 1  114  ? 7.158   36.485  129.098 1.00 42.59 ? 112  PRO B N     1 
ATOM   9627  C  CA    . PRO B 1  114  ? 6.657   35.346  129.887 1.00 39.94 ? 112  PRO B CA    1 
ATOM   9628  C  C     . PRO B 1  114  ? 6.225   35.727  131.289 1.00 38.25 ? 112  PRO B C     1 
ATOM   9629  O  O     . PRO B 1  114  ? 5.198   35.235  131.774 1.00 44.27 ? 112  PRO B O     1 
ATOM   9630  C  CB    . PRO B 1  114  ? 7.856   34.381  129.909 1.00 36.65 ? 112  PRO B CB    1 
ATOM   9631  C  CG    . PRO B 1  114  ? 8.822   34.899  128.886 1.00 39.83 ? 112  PRO B CG    1 
ATOM   9632  C  CD    . PRO B 1  114  ? 8.596   36.372  128.813 1.00 39.76 ? 112  PRO B CD    1 
ATOM   9633  N  N     . ASP B 1  115  ? 6.984   36.584  131.961 1.00 39.77 ? 113  ASP B N     1 
ATOM   9634  C  CA    . ASP B 1  115  ? 6.700   36.930  133.348 1.00 44.43 ? 113  ASP B CA    1 
ATOM   9635  C  C     . ASP B 1  115  ? 5.508   37.878  133.404 1.00 43.76 ? 113  ASP B C     1 
ATOM   9636  O  O     . ASP B 1  115  ? 5.526   38.945  132.781 1.00 44.22 ? 113  ASP B O     1 
ATOM   9637  C  CB    . ASP B 1  115  ? 7.930   37.556  134.001 1.00 42.74 ? 113  ASP B CB    1 
ATOM   9638  C  CG    . ASP B 1  115  ? 7.645   38.087  135.390 1.00 48.35 ? 113  ASP B CG    1 
ATOM   9639  O  OD1   . ASP B 1  115  ? 7.108   37.333  136.232 1.00 51.52 ? 113  ASP B OD1   1 
ATOM   9640  O  OD2   . ASP B 1  115  ? 7.961   39.266  135.645 1.00 51.34 ? 113  ASP B OD2   1 
ATOM   9641  N  N     . THR B 1  116  ? 4.476   37.486  134.156 1.00 45.52 ? 114  THR B N     1 
ATOM   9642  C  CA    . THR B 1  116  ? 3.260   38.288  134.234 1.00 47.17 ? 114  THR B CA    1 
ATOM   9643  C  C     . THR B 1  116  ? 3.532   39.658  134.848 1.00 49.28 ? 114  THR B C     1 
ATOM   9644  O  O     . THR B 1  116  ? 3.011   40.675  134.372 1.00 46.62 ? 114  THR B O     1 
ATOM   9645  C  CB    . THR B 1  116  ? 2.195   37.533  135.032 1.00 48.32 ? 114  THR B CB    1 
ATOM   9646  O  OG1   . THR B 1  116  ? 1.804   36.357  134.309 1.00 53.99 ? 114  THR B OG1   1 
ATOM   9647  C  CG2   . THR B 1  116  ? 0.967   38.409  135.279 1.00 51.60 ? 114  THR B CG2   1 
ATOM   9648  N  N     . ALA B 1  117  ? 4.357   39.710  135.897 1.00 48.99 ? 115  ALA B N     1 
ATOM   9649  C  CA    . ALA B 1  117  ? 4.616   40.981  136.565 1.00 49.48 ? 115  ALA B CA    1 
ATOM   9650  C  C     . ALA B 1  117  ? 5.367   41.947  135.657 1.00 45.13 ? 115  ALA B C     1 
ATOM   9651  O  O     . ALA B 1  117  ? 5.086   43.152  135.659 1.00 47.83 ? 115  ALA B O     1 
ATOM   9652  C  CB    . ALA B 1  117  ? 5.396   40.747  137.859 1.00 48.79 ? 115  ALA B CB    1 
ATOM   9653  N  N     . THR B 1  118  ? 6.331   41.443  134.883 1.00 45.65 ? 116  THR B N     1 
ATOM   9654  C  CA    . THR B 1  118  ? 7.072   42.310  133.973 1.00 44.66 ? 116  THR B CA    1 
ATOM   9655  C  C     . THR B 1  118  ? 6.159   42.861  132.886 1.00 45.82 ? 116  THR B C     1 
ATOM   9656  O  O     . THR B 1  118  ? 6.219   44.053  132.559 1.00 43.22 ? 116  THR B O     1 
ATOM   9657  C  CB    . THR B 1  118  ? 8.242   41.545  133.352 1.00 43.97 ? 116  THR B CB    1 
ATOM   9658  O  OG1   . THR B 1  118  ? 9.145   41.128  134.385 1.00 46.14 ? 116  THR B OG1   1 
ATOM   9659  C  CG2   . THR B 1  118  ? 8.992   42.417  132.361 1.00 40.41 ? 116  THR B CG2   1 
ATOM   9660  N  N     . ARG B 1  119  ? 5.303   42.006  132.325 1.00 43.46 ? 117  ARG B N     1 
ATOM   9661  C  CA    . ARG B 1  119  ? 4.397   42.436  131.265 1.00 42.06 ? 117  ARG B CA    1 
ATOM   9662  C  C     . ARG B 1  119  ? 3.390   43.454  131.785 1.00 42.27 ? 117  ARG B C     1 
ATOM   9663  O  O     . ARG B 1  119  ? 3.189   44.509  131.173 1.00 42.19 ? 117  ARG B O     1 
ATOM   9664  C  CB    . ARG B 1  119  ? 3.683   41.221  130.677 1.00 41.03 ? 117  ARG B CB    1 
ATOM   9665  C  CG    . ARG B 1  119  ? 2.700   41.540  129.573 1.00 36.85 ? 117  ARG B CG    1 
ATOM   9666  C  CD    . ARG B 1  119  ? 1.698   40.418  129.465 1.00 37.43 ? 117  ARG B CD    1 
ATOM   9667  N  NE    . ARG B 1  119  ? 2.363   39.129  129.316 1.00 40.89 ? 117  ARG B NE    1 
ATOM   9668  C  CZ    . ARG B 1  119  ? 1.946   38.002  129.878 1.00 43.47 ? 117  ARG B CZ    1 
ATOM   9669  N  NH1   . ARG B 1  119  ? 0.877   37.971  130.658 1.00 40.02 ? 117  ARG B NH1   1 
ATOM   9670  N  NH2   . ARG B 1  119  ? 2.620   36.877  129.654 1.00 43.06 ? 117  ARG B NH2   1 
ATOM   9671  N  N     . ASP B 1  120  ? 2.753   43.156  132.922 1.00 43.06 ? 118  ASP B N     1 
ATOM   9672  C  CA    . ASP B 1  120  ? 1.800   44.093  133.509 1.00 44.54 ? 118  ASP B CA    1 
ATOM   9673  C  C     . ASP B 1  120  ? 2.456   45.425  133.848 1.00 43.79 ? 118  ASP B C     1 
ATOM   9674  O  O     . ASP B 1  120  ? 1.796   46.468  133.800 1.00 42.61 ? 118  ASP B O     1 
ATOM   9675  C  CB    . ASP B 1  120  ? 1.155   43.484  134.755 1.00 45.92 ? 118  ASP B CB    1 
ATOM   9676  C  CG    . ASP B 1  120  ? 0.213   42.339  134.426 1.00 46.90 ? 118  ASP B CG    1 
ATOM   9677  O  OD1   . ASP B 1  120  ? -0.035  42.096  133.225 1.00 44.48 ? 118  ASP B OD1   1 
ATOM   9678  O  OD2   . ASP B 1  120  ? -0.280  41.683  135.369 1.00 47.27 ? 118  ASP B OD2   1 
ATOM   9679  N  N     . ALA B 1  121  ? 3.750   45.415  134.182 1.00 45.52 ? 119  ALA B N     1 
ATOM   9680  C  CA    . ALA B 1  121  ? 4.444   46.663  134.484 1.00 45.35 ? 119  ALA B CA    1 
ATOM   9681  C  C     . ALA B 1  121  ? 4.769   47.442  133.217 1.00 45.46 ? 119  ALA B C     1 
ATOM   9682  O  O     . ALA B 1  121  ? 4.697   48.674  133.210 1.00 45.94 ? 119  ALA B O     1 
ATOM   9683  C  CB    . ALA B 1  121  ? 5.721   46.388  135.282 1.00 41.22 ? 119  ALA B CB    1 
ATOM   9684  N  N     . LEU B 1  122  ? 5.135   46.746  132.139 1.00 43.54 ? 120  LEU B N     1 
ATOM   9685  C  CA    . LEU B 1  122  ? 5.352   47.432  130.870 1.00 43.15 ? 120  LEU B CA    1 
ATOM   9686  C  C     . LEU B 1  122  ? 4.057   48.059  130.367 1.00 43.07 ? 120  LEU B C     1 
ATOM   9687  O  O     . LEU B 1  122  ? 4.062   49.182  129.848 1.00 43.94 ? 120  LEU B O     1 
ATOM   9688  C  CB    . LEU B 1  122  ? 5.918   46.458  129.833 1.00 43.03 ? 120  LEU B CB    1 
ATOM   9689  C  CG    . LEU B 1  122  ? 6.366   47.087  128.512 1.00 43.18 ? 120  LEU B CG    1 
ATOM   9690  C  CD1   . LEU B 1  122  ? 7.587   47.975  128.726 1.00 45.72 ? 120  LEU B CD1   1 
ATOM   9691  C  CD2   . LEU B 1  122  ? 6.636   46.031  127.448 1.00 43.34 ? 120  LEU B CD2   1 
ATOM   9692  N  N     . ILE B 1  123  ? 2.938   47.344  130.522 1.00 42.13 ? 121  ILE B N     1 
ATOM   9693  C  CA    . ILE B 1  123  ? 1.637   47.850  130.086 1.00 41.31 ? 121  ILE B CA    1 
ATOM   9694  C  C     . ILE B 1  123  ? 1.300   49.143  130.815 1.00 47.10 ? 121  ILE B C     1 
ATOM   9695  O  O     . ILE B 1  123  ? 0.990   50.169  130.196 1.00 45.46 ? 121  ILE B O     1 
ATOM   9696  C  CB    . ILE B 1  123  ? 0.548   46.786  130.321 1.00 39.92 ? 121  ILE B CB    1 
ATOM   9697  C  CG1   . ILE B 1  123  ? 0.726   45.597  129.374 1.00 34.12 ? 121  ILE B CG1   1 
ATOM   9698  C  CG2   . ILE B 1  123  ? -0.847  47.398  130.190 1.00 39.84 ? 121  ILE B CG2   1 
ATOM   9699  C  CD1   . ILE B 1  123  ? -0.222  44.456  129.662 1.00 35.09 ? 121  ILE B CD1   1 
ATOM   9700  N  N     . ARG B 1  124  ? 1.362   49.109  132.146 1.00 41.72 ? 122  ARG B N     1 
ATOM   9701  C  CA    . ARG B 1  124  ? 0.891   50.220  132.962 1.00 46.98 ? 122  ARG B CA    1 
ATOM   9702  C  C     . ARG B 1  124  ? 1.858   51.400  132.954 1.00 49.92 ? 122  ARG B C     1 
ATOM   9703  O  O     . ARG B 1  124  ? 1.421   52.550  133.073 1.00 53.39 ? 122  ARG B O     1 
ATOM   9704  C  CB    . ARG B 1  124  ? 0.650   49.725  134.390 1.00 50.78 ? 122  ARG B CB    1 
ATOM   9705  C  CG    . ARG B 1  124  ? 0.055   50.737  135.343 1.00 53.15 ? 122  ARG B CG    1 
ATOM   9706  C  CD    . ARG B 1  124  ? -0.318  50.061  136.651 1.00 55.81 ? 122  ARG B CD    1 
ATOM   9707  N  NE    . ARG B 1  124  ? -1.347  49.043  136.466 1.00 54.75 ? 122  ARG B NE    1 
ATOM   9708  C  CZ    . ARG B 1  124  ? -2.564  49.103  136.988 1.00 57.03 ? 122  ARG B CZ    1 
ATOM   9709  N  NH1   . ARG B 1  124  ? -2.939  50.115  137.757 1.00 57.43 ? 122  ARG B NH1   1 
ATOM   9710  N  NH2   . ARG B 1  124  ? -3.426  48.120  136.742 1.00 56.37 ? 122  ARG B NH2   1 
ATOM   9711  N  N     . ASP B 1  125  ? 3.159   51.150  132.801 1.00 49.16 ? 123  ASP B N     1 
ATOM   9712  C  CA    . ASP B 1  125  ? 4.158   52.201  132.928 1.00 51.70 ? 123  ASP B CA    1 
ATOM   9713  C  C     . ASP B 1  125  ? 4.774   52.635  131.605 1.00 50.68 ? 123  ASP B C     1 
ATOM   9714  O  O     . ASP B 1  125  ? 5.497   53.637  131.582 1.00 54.88 ? 123  ASP B O     1 
ATOM   9715  C  CB    . ASP B 1  125  ? 5.281   51.756  133.879 1.00 53.94 ? 123  ASP B CB    1 
ATOM   9716  C  CG    . ASP B 1  125  ? 4.758   51.304  135.225 1.00 57.00 ? 123  ASP B CG    1 
ATOM   9717  O  OD1   . ASP B 1  125  ? 3.607   51.649  135.559 1.00 57.65 ? 123  ASP B OD1   1 
ATOM   9718  O  OD2   . ASP B 1  125  ? 5.495   50.604  135.952 1.00 59.28 ? 123  ASP B OD2   1 
ATOM   9719  N  N     . LYS B 1  126  ? 4.515   51.933  130.519 1.00 47.25 ? 124  LYS B N     1 
ATOM   9720  C  CA    . LYS B 1  126  ? 5.102   52.345  129.252 1.00 47.92 ? 124  LYS B CA    1 
ATOM   9721  C  C     . LYS B 1  126  ? 4.110   52.331  128.098 1.00 52.38 ? 124  LYS B C     1 
ATOM   9722  O  O     . LYS B 1  126  ? 4.134   53.244  127.269 1.00 55.83 ? 124  LYS B O     1 
ATOM   9723  C  CB    . LYS B 1  126  ? 6.302   51.448  128.914 1.00 49.48 ? 124  LYS B CB    1 
ATOM   9724  N  N     . ILE B 1  127  ? 3.235   51.326  128.025 1.00 47.26 ? 125  ILE B N     1 
ATOM   9725  C  CA    . ILE B 1  127  ? 2.367   51.201  126.857 1.00 48.69 ? 125  ILE B CA    1 
ATOM   9726  C  C     . ILE B 1  127  ? 1.135   52.089  126.998 1.00 44.15 ? 125  ILE B C     1 
ATOM   9727  O  O     . ILE B 1  127  ? 0.729   52.757  126.041 1.00 44.21 ? 125  ILE B O     1 
ATOM   9728  C  CB    . ILE B 1  127  ? 1.980   49.728  126.627 1.00 42.43 ? 125  ILE B CB    1 
ATOM   9729  C  CG1   . ILE B 1  127  ? 3.213   48.824  126.709 1.00 44.23 ? 125  ILE B CG1   1 
ATOM   9730  C  CG2   . ILE B 1  127  ? 1.309   49.562  125.271 1.00 40.19 ? 125  ILE B CG2   1 
ATOM   9731  C  CD1   . ILE B 1  127  ? 4.206   49.062  125.607 1.00 47.99 ? 125  ILE B CD1   1 
ATOM   9732  N  N     . ALA B 1  128  ? 0.520   52.109  128.184 1.00 44.07 ? 126  ALA B N     1 
ATOM   9733  C  CA    . ALA B 1  128  ? -0.690  52.899  128.390 1.00 43.71 ? 126  ALA B CA    1 
ATOM   9734  C  C     . ALA B 1  128  ? -0.455  54.386  128.161 1.00 48.67 ? 126  ALA B C     1 
ATOM   9735  O  O     . ALA B 1  128  ? -1.405  55.115  127.855 1.00 48.09 ? 126  ALA B O     1 
ATOM   9736  C  CB    . ALA B 1  128  ? -1.246  52.663  129.795 1.00 43.76 ? 126  ALA B CB    1 
ATOM   9737  N  N     . ASP B 1  129  ? 0.787   54.850  128.297 1.00 50.79 ? 127  ASP B N     1 
ATOM   9738  C  CA    . ASP B 1  129  ? 1.165   56.211  127.941 1.00 57.04 ? 127  ASP B CA    1 
ATOM   9739  C  C     . ASP B 1  129  ? 1.556   56.343  126.474 1.00 59.85 ? 127  ASP B C     1 
ATOM   9740  O  O     . ASP B 1  129  ? 2.410   57.174  126.137 1.00 62.85 ? 127  ASP B O     1 
ATOM   9741  C  CB    . ASP B 1  129  ? 2.305   56.694  128.839 1.00 61.18 ? 127  ASP B CB    1 
ATOM   9742  C  CG    . ASP B 1  129  ? 1.837   57.038  130.239 1.00 66.48 ? 127  ASP B CG    1 
ATOM   9743  O  OD1   . ASP B 1  129  ? 0.612   57.001  130.484 1.00 67.27 ? 127  ASP B OD1   1 
ATOM   9744  O  OD2   . ASP B 1  129  ? 2.694   57.345  131.095 1.00 72.69 ? 127  ASP B OD2   1 
ATOM   9745  N  N     . GLY B 1  130  ? 0.974   55.527  125.595 1.00 57.20 ? 128  GLY B N     1 
ATOM   9746  C  CA    . GLY B 1  130  ? 1.189   55.658  124.166 1.00 57.14 ? 128  GLY B CA    1 
ATOM   9747  C  C     . GLY B 1  130  ? 2.578   55.305  123.673 1.00 60.11 ? 128  GLY B C     1 
ATOM   9748  O  O     . GLY B 1  130  ? 2.752   54.988  122.493 1.00 56.71 ? 128  GLY B O     1 
ATOM   9749  N  N     . ASN B 1  131  ? 3.577   55.350  124.555 1.00 78.15 ? 129  ASN B N     1 
ATOM   9750  C  CA    . ASN B 1  131  ? 4.952   55.050  124.169 1.00 77.14 ? 129  ASN B CA    1 
ATOM   9751  C  C     . ASN B 1  131  ? 5.107   53.579  123.800 1.00 75.77 ? 129  ASN B C     1 
ATOM   9752  O  O     . ASN B 1  131  ? 5.951   52.876  124.366 1.00 80.00 ? 129  ASN B O     1 
ATOM   9753  C  CB    . ASN B 1  131  ? 5.916   55.420  125.304 1.00 74.00 ? 129  ASN B CB    1 
ATOM   9754  N  N     . TRP B 1  132  ? 4.307   53.108  122.844 1.00 59.56 ? 130  TRP B N     1 
ATOM   9755  C  CA    . TRP B 1  132  ? 4.307   51.700  122.474 1.00 55.17 ? 130  TRP B CA    1 
ATOM   9756  C  C     . TRP B 1  132  ? 5.322   51.364  121.395 1.00 55.10 ? 130  TRP B C     1 
ATOM   9757  O  O     . TRP B 1  132  ? 5.751   50.206  121.311 1.00 57.86 ? 130  TRP B O     1 
ATOM   9758  C  CB    . TRP B 1  132  ? 2.910   51.268  122.002 1.00 49.44 ? 130  TRP B CB    1 
ATOM   9759  C  CG    . TRP B 1  132  ? 2.463   51.878  120.693 1.00 40.68 ? 130  TRP B CG    1 
ATOM   9760  C  CD1   . TRP B 1  132  ? 1.666   52.975  120.531 1.00 40.46 ? 130  TRP B CD1   1 
ATOM   9761  C  CD2   . TRP B 1  132  ? 2.786   51.419  119.372 1.00 38.69 ? 130  TRP B CD2   1 
ATOM   9762  N  NE1   . TRP B 1  132  ? 1.471   53.227  119.192 1.00 37.27 ? 130  TRP B NE1   1 
ATOM   9763  C  CE2   . TRP B 1  132  ? 2.149   52.287  118.461 1.00 39.11 ? 130  TRP B CE2   1 
ATOM   9764  C  CE3   . TRP B 1  132  ? 3.548   50.360  118.873 1.00 37.48 ? 130  TRP B CE3   1 
ATOM   9765  C  CZ2   . TRP B 1  132  ? 2.254   52.126  117.080 1.00 36.64 ? 130  TRP B CZ2   1 
ATOM   9766  C  CZ3   . TRP B 1  132  ? 3.655   50.203  117.501 1.00 36.70 ? 130  TRP B CZ3   1 
ATOM   9767  C  CH2   . TRP B 1  132  ? 3.010   51.080  116.622 1.00 34.83 ? 130  TRP B CH2   1 
ATOM   9768  N  N     . LYS B 1  133  ? 5.711   52.336  120.569 1.00 53.33 ? 131  LYS B N     1 
ATOM   9769  C  CA    . LYS B 1  133  ? 6.600   52.039  119.449 1.00 55.17 ? 131  LYS B CA    1 
ATOM   9770  C  C     . LYS B 1  133  ? 7.963   51.571  119.945 1.00 64.63 ? 131  LYS B C     1 
ATOM   9771  O  O     . LYS B 1  133  ? 8.524   50.594  119.435 1.00 65.80 ? 131  LYS B O     1 
ATOM   9772  C  CB    . LYS B 1  133  ? 6.739   53.269  118.546 1.00 50.61 ? 131  LYS B CB    1 
ATOM   9773  C  CG    . LYS B 1  133  ? 5.412   53.958  118.216 1.00 48.95 ? 131  LYS B CG    1 
ATOM   9774  C  CD    . LYS B 1  133  ? 5.352   54.436  116.763 1.00 49.81 ? 131  LYS B CD    1 
ATOM   9775  C  CE    . LYS B 1  133  ? 4.012   55.104  116.450 1.00 49.63 ? 131  LYS B CE    1 
ATOM   9776  N  NZ    . LYS B 1  133  ? 3.776   55.318  114.986 1.00 42.00 ? 131  LYS B NZ    1 
ATOM   9777  N  N     . SER B 1  134  ? 8.502   52.243  120.963 1.00 69.89 ? 132  SER B N     1 
ATOM   9778  C  CA    . SER B 1  134  ? 9.825   51.887  121.467 1.00 70.21 ? 132  SER B CA    1 
ATOM   9779  C  C     . SER B 1  134  ? 9.822   50.505  122.109 1.00 69.52 ? 132  SER B C     1 
ATOM   9780  O  O     . SER B 1  134  ? 10.695  49.675  121.831 1.00 69.84 ? 132  SER B O     1 
ATOM   9781  C  CB    . SER B 1  134  ? 10.299  52.941  122.469 1.00 68.41 ? 132  SER B CB    1 
ATOM   9782  N  N     . HIS B 1  135  ? 8.824   50.232  122.956 1.00 68.07 ? 133  HIS B N     1 
ATOM   9783  C  CA    . HIS B 1  135  ? 8.929   49.132  123.913 1.00 67.98 ? 133  HIS B CA    1 
ATOM   9784  C  C     . HIS B 1  135  ? 8.902   47.757  123.249 1.00 64.90 ? 133  HIS B C     1 
ATOM   9785  O  O     . HIS B 1  135  ? 9.510   46.814  123.772 1.00 63.22 ? 133  HIS B O     1 
ATOM   9786  C  CB    . HIS B 1  135  ? 7.808   49.239  124.948 1.00 60.97 ? 133  HIS B CB    1 
ATOM   9787  N  N     . LEU B 1  136  ? 8.217   47.608  122.117 1.00 62.87 ? 134  LEU B N     1 
ATOM   9788  C  CA    . LEU B 1  136  ? 8.002   46.284  121.539 1.00 59.25 ? 134  LEU B CA    1 
ATOM   9789  C  C     . LEU B 1  136  ? 8.433   46.240  120.075 1.00 58.85 ? 134  LEU B C     1 
ATOM   9790  O  O     . LEU B 1  136  ? 7.734   45.695  119.215 1.00 53.48 ? 134  LEU B O     1 
ATOM   9791  C  CB    . LEU B 1  136  ? 6.542   45.866  121.692 1.00 51.71 ? 134  LEU B CB    1 
ATOM   9792  C  CG    . LEU B 1  136  ? 6.046   45.800  123.139 1.00 50.89 ? 134  LEU B CG    1 
ATOM   9793  C  CD1   . LEU B 1  136  ? 4.556   46.052  123.201 1.00 45.26 ? 134  LEU B CD1   1 
ATOM   9794  C  CD2   . LEU B 1  136  ? 6.388   44.457  123.778 1.00 48.55 ? 134  LEU B CD2   1 
ATOM   9795  N  N     . GLY B 1  137  ? 9.602   46.804  119.771 1.00 62.75 ? 135  GLY B N     1 
ATOM   9796  C  CA    . GLY B 1  137  ? 10.173  46.721  118.447 1.00 58.33 ? 135  GLY B CA    1 
ATOM   9797  C  C     . GLY B 1  137  ? 9.587   47.659  117.414 1.00 60.79 ? 135  GLY B C     1 
ATOM   9798  O  O     . GLY B 1  137  ? 10.175  47.809  116.334 1.00 60.39 ? 135  GLY B O     1 
ATOM   9799  N  N     . GLY B 1  138  ? 8.453   48.290  117.691 1.00 68.23 ? 136  GLY B N     1 
ATOM   9800  C  CA    . GLY B 1  138  ? 7.890   49.251  116.764 1.00 65.95 ? 136  GLY B CA    1 
ATOM   9801  C  C     . GLY B 1  138  ? 6.888   48.650  115.802 1.00 60.46 ? 136  GLY B C     1 
ATOM   9802  O  O     . GLY B 1  138  ? 6.617   47.447  115.784 1.00 61.21 ? 136  GLY B O     1 
ATOM   9803  N  N     . SER B 1  139  ? 6.339   49.537  114.967 1.00 48.37 ? 137  SER B N     1 
ATOM   9804  C  CA    . SER B 1  139  ? 5.265   49.171  114.048 1.00 45.74 ? 137  SER B CA    1 
ATOM   9805  C  C     . SER B 1  139  ? 5.666   48.013  113.145 1.00 47.22 ? 137  SER B C     1 
ATOM   9806  O  O     . SER B 1  139  ? 4.900   47.061  112.951 1.00 47.13 ? 137  SER B O     1 
ATOM   9807  C  CB    . SER B 1  139  ? 4.873   50.382  113.199 1.00 43.61 ? 137  SER B CB    1 
ATOM   9808  O  OG    . SER B 1  139  ? 5.234   51.592  113.836 1.00 47.96 ? 137  SER B OG    1 
ATOM   9809  N  N     . ARG B 1  140  ? 6.865   48.089  112.567 1.00 53.15 ? 138  ARG B N     1 
ATOM   9810  C  CA    . ARG B 1  140  ? 7.319   47.043  111.660 1.00 53.27 ? 138  ARG B CA    1 
ATOM   9811  C  C     . ARG B 1  140  ? 7.254   45.678  112.334 1.00 48.04 ? 138  ARG B C     1 
ATOM   9812  O  O     . ARG B 1  140  ? 6.639   44.741  111.814 1.00 49.71 ? 138  ARG B O     1 
ATOM   9813  C  CB    . ARG B 1  140  ? 8.735   47.363  111.182 1.00 47.51 ? 138  ARG B CB    1 
ATOM   9814  C  CG    . ARG B 1  140  ? 8.891   48.820  110.748 1.00 46.84 ? 138  ARG B CG    1 
ATOM   9815  C  CD    . ARG B 1  140  ? 9.373   48.950  109.312 1.00 46.49 ? 138  ARG B CD    1 
ATOM   9816  N  NE    . ARG B 1  140  ? 9.081   50.267  108.757 1.00 51.68 ? 138  ARG B NE    1 
ATOM   9817  C  CZ    . ARG B 1  140  ? 9.871   51.328  108.868 1.00 53.52 ? 138  ARG B CZ    1 
ATOM   9818  N  NH1   . ARG B 1  140  ? 11.031  51.265  109.503 1.00 50.53 ? 138  ARG B NH1   1 
ATOM   9819  N  NH2   . ARG B 1  140  ? 9.488   52.481  108.326 1.00 46.92 ? 138  ARG B NH2   1 
ATOM   9820  N  N     . SER B 1  141  ? 7.842   45.566  113.523 1.00 43.10 ? 139  SER B N     1 
ATOM   9821  C  CA    . SER B 1  141  ? 7.792   44.310  114.262 1.00 42.88 ? 139  SER B CA    1 
ATOM   9822  C  C     . SER B 1  141  ? 6.382   44.000  114.754 1.00 37.65 ? 139  SER B C     1 
ATOM   9823  O  O     . SER B 1  141  ? 5.928   42.853  114.671 1.00 38.93 ? 139  SER B O     1 
ATOM   9824  C  CB    . SER B 1  141  ? 8.752   44.366  115.449 1.00 39.82 ? 139  SER B CB    1 
ATOM   9825  O  OG    . SER B 1  141  ? 8.183   43.723  116.580 1.00 50.46 ? 139  SER B OG    1 
ATOM   9826  N  N     . LEU B 1  142  ? 5.668   45.013  115.254 1.00 36.88 ? 140  LEU B N     1 
ATOM   9827  C  CA    A LEU B 1  142  ? 4.428   44.774  115.986 0.20 33.53 ? 140  LEU B CA    1 
ATOM   9828  C  CA    B LEU B 1  142  ? 4.446   44.734  115.995 0.80 33.47 ? 140  LEU B CA    1 
ATOM   9829  C  C     . LEU B 1  142  ? 3.389   44.080  115.118 1.00 28.62 ? 140  LEU B C     1 
ATOM   9830  O  O     . LEU B 1  142  ? 2.633   43.228  115.596 1.00 24.47 ? 140  LEU B O     1 
ATOM   9831  C  CB    A LEU B 1  142  ? 3.880   46.105  116.501 0.20 32.40 ? 140  LEU B CB    1 
ATOM   9832  C  CB    B LEU B 1  142  ? 3.893   46.012  116.620 0.80 32.20 ? 140  LEU B CB    1 
ATOM   9833  C  CG    A LEU B 1  142  ? 3.538   46.256  117.981 0.20 31.90 ? 140  LEU B CG    1 
ATOM   9834  C  CG    B LEU B 1  142  ? 3.175   45.697  117.927 0.80 30.59 ? 140  LEU B CG    1 
ATOM   9835  C  CD1   A LEU B 1  142  ? 2.037   46.167  118.202 0.20 29.99 ? 140  LEU B CD1   1 
ATOM   9836  C  CD1   B LEU B 1  142  ? 4.186   45.365  119.000 0.80 34.66 ? 140  LEU B CD1   1 
ATOM   9837  C  CD2   A LEU B 1  142  ? 4.264   45.215  118.807 0.20 34.84 ? 140  LEU B CD2   1 
ATOM   9838  C  CD2   B LEU B 1  142  ? 2.308   46.836  118.377 0.80 30.30 ? 140  LEU B CD2   1 
ATOM   9839  N  N     . PHE B 1  143  ? 3.319   44.451  113.839 1.00 24.90 ? 141  PHE B N     1 
ATOM   9840  C  CA    . PHE B 1  143  ? 2.224   44.022  112.983 1.00 26.25 ? 141  PHE B CA    1 
ATOM   9841  C  C     . PHE B 1  143  ? 2.622   42.915  112.005 1.00 26.49 ? 141  PHE B C     1 
ATOM   9842  O  O     . PHE B 1  143  ? 1.890   42.652  111.045 1.00 24.12 ? 141  PHE B O     1 
ATOM   9843  C  CB    . PHE B 1  143  ? 1.660   45.241  112.252 1.00 23.48 ? 141  PHE B CB    1 
ATOM   9844  C  CG    . PHE B 1  143  ? 1.321   46.369  113.176 1.00 23.31 ? 141  PHE B CG    1 
ATOM   9845  C  CD1   . PHE B 1  143  ? 0.398   46.192  114.196 1.00 22.33 ? 141  PHE B CD1   1 
ATOM   9846  C  CD2   . PHE B 1  143  ? 1.935   47.606  113.048 1.00 22.28 ? 141  PHE B CD2   1 
ATOM   9847  C  CE1   . PHE B 1  143  ? 0.088   47.217  115.065 1.00 24.72 ? 141  PHE B CE1   1 
ATOM   9848  C  CE2   . PHE B 1  143  ? 1.627   48.641  113.928 1.00 23.28 ? 141  PHE B CE2   1 
ATOM   9849  C  CZ    . PHE B 1  143  ? 0.705   48.450  114.923 1.00 23.55 ? 141  PHE B CZ    1 
ATOM   9850  N  N     . VAL B 1  144  ? 3.743   42.234  112.258 1.00 26.11 ? 142  VAL B N     1 
ATOM   9851  C  CA    . VAL B 1  144  ? 4.196   41.155  111.380 1.00 28.75 ? 142  VAL B CA    1 
ATOM   9852  C  C     . VAL B 1  144  ? 3.087   40.136  111.131 1.00 29.68 ? 142  VAL B C     1 
ATOM   9853  O  O     . VAL B 1  144  ? 2.882   39.689  109.995 1.00 27.35 ? 142  VAL B O     1 
ATOM   9854  C  CB    . VAL B 1  144  ? 5.459   40.501  111.971 1.00 29.04 ? 142  VAL B CB    1 
ATOM   9855  C  CG1   . VAL B 1  144  ? 5.745   39.167  111.313 1.00 33.35 ? 142  VAL B CG1   1 
ATOM   9856  C  CG2   . VAL B 1  144  ? 6.652   41.425  111.787 1.00 31.68 ? 142  VAL B CG2   1 
ATOM   9857  N  N     . ASN B 1  145  ? 2.336   39.774  112.175 1.00 27.69 ? 143  ASN B N     1 
ATOM   9858  C  CA    . ASN B 1  145  ? 1.307   38.743  112.077 1.00 28.48 ? 143  ASN B CA    1 
ATOM   9859  C  C     . ASN B 1  145  ? -0.101  39.317  111.950 1.00 29.20 ? 143  ASN B C     1 
ATOM   9860  O  O     . ASN B 1  145  ? -1.076  38.658  112.330 1.00 27.93 ? 143  ASN B O     1 
ATOM   9861  C  CB    . ASN B 1  145  ? 1.382   37.807  113.281 1.00 29.42 ? 143  ASN B CB    1 
ATOM   9862  C  CG    . ASN B 1  145  ? 2.613   36.928  113.254 1.00 32.59 ? 143  ASN B CG    1 
ATOM   9863  O  OD1   . ASN B 1  145  ? 3.013   36.430  112.197 1.00 37.67 ? 143  ASN B OD1   1 
ATOM   9864  N  ND2   . ASN B 1  145  ? 3.231   36.743  114.413 1.00 33.75 ? 143  ASN B ND2   1 
ATOM   9865  N  N     . ALA B 1  146  ? -0.237  40.527  111.405 1.00 24.84 ? 144  ALA B N     1 
ATOM   9866  C  CA    . ALA B 1  146  ? -1.546  41.169  111.386 1.00 25.82 ? 144  ALA B CA    1 
ATOM   9867  C  C     . ALA B 1  146  ? -2.523  40.514  110.411 1.00 25.32 ? 144  ALA B C     1 
ATOM   9868  O  O     . ALA B 1  146  ? -3.739  40.678  110.569 1.00 28.02 ? 144  ALA B O     1 
ATOM   9869  C  CB    . ALA B 1  146  ? -1.393  42.654  111.057 1.00 23.72 ? 144  ALA B CB    1 
ATOM   9870  N  N     . ALA B 1  147  ? -2.038  39.791  109.399 1.00 26.22 ? 145  ALA B N     1 
ATOM   9871  C  CA    . ALA B 1  147  ? -2.971  39.108  108.507 1.00 29.26 ? 145  ALA B CA    1 
ATOM   9872  C  C     . ALA B 1  147  ? -3.791  38.083  109.275 1.00 29.69 ? 145  ALA B C     1 
ATOM   9873  O  O     . ALA B 1  147  ? -5.004  37.956  109.061 1.00 30.19 ? 145  ALA B O     1 
ATOM   9874  C  CB    . ALA B 1  147  ? -2.224  38.444  107.350 1.00 31.02 ? 145  ALA B CB    1 
ATOM   9875  N  N     . THR B 1  148  ? -3.151  37.373  110.205 1.00 29.60 ? 146  THR B N     1 
ATOM   9876  C  CA    . THR B 1  148  ? -3.860  36.386  111.011 1.00 31.12 ? 146  THR B CA    1 
ATOM   9877  C  C     . THR B 1  148  ? -4.914  37.051  111.887 1.00 31.03 ? 146  THR B C     1 
ATOM   9878  O  O     . THR B 1  148  ? -6.071  36.617  111.925 1.00 35.72 ? 146  THR B O     1 
ATOM   9879  C  CB    . THR B 1  148  ? -2.863  35.600  111.865 1.00 35.87 ? 146  THR B CB    1 
ATOM   9880  O  OG1   . THR B 1  148  ? -1.865  35.018  111.016 1.00 41.96 ? 146  THR B OG1   1 
ATOM   9881  C  CG2   . THR B 1  148  ? -3.577  34.499  112.642 1.00 42.59 ? 146  THR B CG2   1 
ATOM   9882  N  N     . TRP B 1  149  ? -4.537  38.124  112.592 1.00 30.26 ? 147  TRP B N     1 
ATOM   9883  C  CA    . TRP B 1  149  ? -5.521  38.829  113.399 1.00 30.94 ? 147  TRP B CA    1 
ATOM   9884  C  C     . TRP B 1  149  ? -6.563  39.513  112.524 1.00 28.23 ? 147  TRP B C     1 
ATOM   9885  O  O     . TRP B 1  149  ? -7.712  39.675  112.945 1.00 33.72 ? 147  TRP B O     1 
ATOM   9886  C  CB    . TRP B 1  149  ? -4.829  39.831  114.320 1.00 29.92 ? 147  TRP B CB    1 
ATOM   9887  C  CG    . TRP B 1  149  ? -3.875  39.171  115.264 1.00 28.66 ? 147  TRP B CG    1 
ATOM   9888  C  CD1   . TRP B 1  149  ? -2.516  39.288  115.274 1.00 29.13 ? 147  TRP B CD1   1 
ATOM   9889  C  CD2   . TRP B 1  149  ? -4.208  38.255  116.310 1.00 30.41 ? 147  TRP B CD2   1 
ATOM   9890  N  NE1   . TRP B 1  149  ? -1.982  38.518  116.285 1.00 31.30 ? 147  TRP B NE1   1 
ATOM   9891  C  CE2   . TRP B 1  149  ? -3.002  37.873  116.933 1.00 31.03 ? 147  TRP B CE2   1 
ATOM   9892  C  CE3   . TRP B 1  149  ? -5.408  37.733  116.793 1.00 31.41 ? 147  TRP B CE3   1 
ATOM   9893  C  CZ2   . TRP B 1  149  ? -2.964  36.989  118.009 1.00 30.97 ? 147  TRP B CZ2   1 
ATOM   9894  C  CZ3   . TRP B 1  149  ? -5.367  36.851  117.865 1.00 32.94 ? 147  TRP B CZ3   1 
ATOM   9895  C  CH2   . TRP B 1  149  ? -4.154  36.490  118.457 1.00 33.01 ? 147  TRP B CH2   1 
ATOM   9896  N  N     . GLY B 1  150  ? -6.185  39.910  111.307 1.00 28.09 ? 148  GLY B N     1 
ATOM   9897  C  CA    . GLY B 1  150  ? -7.177  40.415  110.372 1.00 33.24 ? 148  GLY B CA    1 
ATOM   9898  C  C     . GLY B 1  150  ? -8.275  39.404  110.101 1.00 32.34 ? 148  GLY B C     1 
ATOM   9899  O  O     . GLY B 1  150  ? -9.459  39.748  110.065 1.00 34.37 ? 148  GLY B O     1 
ATOM   9900  N  N     . LEU B 1  151  ? -7.899  38.139  109.913 1.00 33.62 ? 149  LEU B N     1 
ATOM   9901  C  CA    . LEU B 1  151  ? -8.909  37.099  109.744 1.00 36.32 ? 149  LEU B CA    1 
ATOM   9902  C  C     . LEU B 1  151  ? -9.730  36.929  111.013 1.00 35.03 ? 149  LEU B C     1 
ATOM   9903  O  O     . LEU B 1  151  ? -10.955 36.771  110.954 1.00 36.60 ? 149  LEU B O     1 
ATOM   9904  C  CB    . LEU B 1  151  ? -8.249  35.780  109.346 1.00 37.64 ? 149  LEU B CB    1 
ATOM   9905  C  CG    . LEU B 1  151  ? -8.203  35.542  107.838 1.00 42.35 ? 149  LEU B CG    1 
ATOM   9906  C  CD1   . LEU B 1  151  ? -7.230  34.425  107.487 1.00 51.44 ? 149  LEU B CD1   1 
ATOM   9907  C  CD2   . LEU B 1  151  ? -9.601  35.227  107.325 1.00 44.56 ? 149  LEU B CD2   1 
ATOM   9908  N  N     . VAL B 1  152  ? -9.071  36.981  112.173 1.00 35.90 ? 150  VAL B N     1 
ATOM   9909  C  CA    . VAL B 1  152  ? -9.770  36.812  113.442 1.00 36.30 ? 150  VAL B CA    1 
ATOM   9910  C  C     . VAL B 1  152  ? -10.804 37.912  113.637 1.00 36.34 ? 150  VAL B C     1 
ATOM   9911  O  O     . VAL B 1  152  ? -11.940 37.650  114.051 1.00 38.22 ? 150  VAL B O     1 
ATOM   9912  C  CB    . VAL B 1  152  ? -8.757  36.778  114.599 1.00 35.51 ? 150  VAL B CB    1 
ATOM   9913  C  CG1   . VAL B 1  152  ? -9.484  36.773  115.932 1.00 39.44 ? 150  VAL B CG1   1 
ATOM   9914  C  CG2   . VAL B 1  152  ? -7.847  35.572  114.470 1.00 36.32 ? 150  VAL B CG2   1 
ATOM   9915  N  N     . VAL B 1  153  ? -10.438 39.155  113.328 1.00 33.58 ? 151  VAL B N     1 
ATOM   9916  C  CA    . VAL B 1  153  ? -11.297 40.290  113.647 1.00 35.55 ? 151  VAL B CA    1 
ATOM   9917  C  C     . VAL B 1  153  ? -12.342 40.523  112.561 1.00 37.31 ? 151  VAL B C     1 
ATOM   9918  O  O     . VAL B 1  153  ? -13.497 40.843  112.859 1.00 36.16 ? 151  VAL B O     1 
ATOM   9919  C  CB    . VAL B 1  153  ? -10.432 41.544  113.878 1.00 34.52 ? 151  VAL B CB    1 
ATOM   9920  C  CG1   . VAL B 1  153  ? -11.307 42.774  114.079 1.00 32.65 ? 151  VAL B CG1   1 
ATOM   9921  C  CG2   . VAL B 1  153  ? -9.506  41.335  115.069 1.00 31.19 ? 151  VAL B CG2   1 
ATOM   9922  N  N     . THR B 1  154  ? -11.961 40.387  111.287 1.00 32.36 ? 152  THR B N     1 
ATOM   9923  C  CA    . THR B 1  154  ? -12.843 40.756  110.186 1.00 36.41 ? 152  THR B CA    1 
ATOM   9924  C  C     . THR B 1  154  ? -13.362 39.571  109.389 1.00 35.20 ? 152  THR B C     1 
ATOM   9925  O  O     . THR B 1  154  ? -14.352 39.724  108.668 1.00 41.72 ? 152  THR B O     1 
ATOM   9926  C  CB    . THR B 1  154  ? -12.127 41.710  109.212 1.00 37.35 ? 152  THR B CB    1 
ATOM   9927  O  OG1   . THR B 1  154  ? -11.254 40.960  108.356 1.00 33.06 ? 152  THR B OG1   1 
ATOM   9928  C  CG2   . THR B 1  154  ? -11.306 42.743  109.970 1.00 37.33 ? 152  THR B CG2   1 
ATOM   9929  N  N     . GLY B 1  155  ? -12.727 38.408  109.493 1.00 35.51 ? 153  GLY B N     1 
ATOM   9930  C  CA    . GLY B 1  155  ? -13.073 37.284  108.654 1.00 37.77 ? 153  GLY B CA    1 
ATOM   9931  C  C     . GLY B 1  155  ? -12.510 37.342  107.252 1.00 41.19 ? 153  GLY B C     1 
ATOM   9932  O  O     . GLY B 1  155  ? -12.747 36.413  106.468 1.00 44.45 ? 153  GLY B O     1 
ATOM   9933  N  N     . LYS B 1  156  ? -11.779 38.398  106.910 1.00 37.94 ? 154  LYS B N     1 
ATOM   9934  C  CA    . LYS B 1  156  ? -11.192 38.561  105.592 1.00 37.73 ? 154  LYS B CA    1 
ATOM   9935  C  C     . LYS B 1  156  ? -9.678  38.467  105.694 1.00 36.22 ? 154  LYS B C     1 
ATOM   9936  O  O     . LYS B 1  156  ? -9.079  38.851  106.702 1.00 36.71 ? 154  LYS B O     1 
ATOM   9937  C  CB    . LYS B 1  156  ? -11.589 39.900  104.965 1.00 40.64 ? 154  LYS B CB    1 
ATOM   9938  N  N     . LEU B 1  157  ? -9.064  37.941  104.645 1.00 35.70 ? 155  LEU B N     1 
ATOM   9939  C  CA    . LEU B 1  157  ? -7.620  37.796  104.582 1.00 37.58 ? 155  LEU B CA    1 
ATOM   9940  C  C     . LEU B 1  157  ? -7.054  38.815  103.606 1.00 40.17 ? 155  LEU B C     1 
ATOM   9941  O  O     . LEU B 1  157  ? -7.482  38.876  102.450 1.00 38.90 ? 155  LEU B O     1 
ATOM   9942  C  CB    . LEU B 1  157  ? -7.227  36.386  104.147 1.00 38.95 ? 155  LEU B CB    1 
ATOM   9943  C  CG    . LEU B 1  157  ? -5.739  36.242  103.827 1.00 40.14 ? 155  LEU B CG    1 
ATOM   9944  C  CD1   . LEU B 1  157  ? -4.916  36.343  105.104 1.00 39.76 ? 155  LEU B CD1   1 
ATOM   9945  C  CD2   . LEU B 1  157  ? -5.454  34.936  103.095 1.00 42.63 ? 155  LEU B CD2   1 
ATOM   9946  N  N     . THR B 1  158  ? -6.103  39.614  104.074 1.00 38.76 ? 156  THR B N     1 
ATOM   9947  C  CA    . THR B 1  158  ? -5.315  40.480  103.211 1.00 39.13 ? 156  THR B CA    1 
ATOM   9948  C  C     . THR B 1  158  ? -3.905  39.916  103.131 1.00 35.44 ? 156  THR B C     1 
ATOM   9949  O  O     . THR B 1  158  ? -3.387  39.379  104.115 1.00 36.86 ? 156  THR B O     1 
ATOM   9950  C  CB    . THR B 1  158  ? -5.293  41.920  103.732 1.00 41.56 ? 156  THR B CB    1 
ATOM   9951  O  OG1   . THR B 1  158  ? -6.628  42.328  104.059 1.00 46.36 ? 156  THR B OG1   1 
ATOM   9952  C  CG2   . THR B 1  158  ? -4.748  42.860  102.675 1.00 41.94 ? 156  THR B CG2   1 
ATOM   9953  N  N     . SER B 1  159  ? -3.292  40.026  101.953 1.00 30.22 ? 157  SER B N     1 
ATOM   9954  C  CA    . SER B 1  159  ? -2.012  39.368  101.718 1.00 30.68 ? 157  SER B CA    1 
ATOM   9955  C  C     . SER B 1  159  ? -0.876  40.062  102.461 1.00 31.48 ? 157  SER B C     1 
ATOM   9956  O  O     . SER B 1  159  ? 0.021   39.408  103.007 1.00 31.81 ? 157  SER B O     1 
ATOM   9957  C  CB    . SER B 1  159  ? -1.722  39.332  100.219 1.00 31.38 ? 157  SER B CB    1 
ATOM   9958  O  OG    . SER B 1  159  ? -0.385  38.928  99.999  1.00 34.97 ? 157  SER B OG    1 
ATOM   9959  N  N     . THR B 1  160  ? -0.884  41.382  102.470 1.00 29.84 ? 158  THR B N     1 
ATOM   9960  C  CA    . THR B 1  160  ? 0.103   42.163  103.190 1.00 24.44 ? 158  THR B CA    1 
ATOM   9961  C  C     . THR B 1  160  ? -0.615  43.064  104.181 1.00 24.26 ? 158  THR B C     1 
ATOM   9962  O  O     . THR B 1  160  ? -1.847  43.162  104.197 1.00 28.82 ? 158  THR B O     1 
ATOM   9963  C  CB    . THR B 1  160  ? 0.957   42.985  102.219 1.00 25.00 ? 158  THR B CB    1 
ATOM   9964  O  OG1   . THR B 1  160  ? 0.097   43.818  101.434 1.00 28.83 ? 158  THR B OG1   1 
ATOM   9965  C  CG2   . THR B 1  160  ? 1.726   42.067  101.290 1.00 27.23 ? 158  THR B CG2   1 
ATOM   9966  N  N     . VAL B 1  161  ? 0.183   43.739  104.995 1.00 17.56 ? 159  VAL B N     1 
ATOM   9967  C  CA    . VAL B 1  161  ? -0.278  44.501  106.147 1.00 20.94 ? 159  VAL B CA    1 
ATOM   9968  C  C     . VAL B 1  161  ? -0.116  45.981  105.836 1.00 20.51 ? 159  VAL B C     1 
ATOM   9969  O  O     . VAL B 1  161  ? 0.962   46.406  105.406 1.00 21.34 ? 159  VAL B O     1 
ATOM   9970  C  CB    . VAL B 1  161  ? 0.540   44.105  107.390 1.00 22.67 ? 159  VAL B CB    1 
ATOM   9971  C  CG1   . VAL B 1  161  ? 0.281   45.026  108.529 1.00 26.83 ? 159  VAL B CG1   1 
ATOM   9972  C  CG2   . VAL B 1  161  ? 0.254   42.649  107.764 1.00 29.03 ? 159  VAL B CG2   1 
ATOM   9973  N  N     . ASN B 1  162  ? -1.178  46.769  106.046 1.00 19.58 ? 160  ASN B N     1 
ATOM   9974  C  CA    . ASN B 1  162  ? -1.015  48.222  106.021 1.00 19.07 ? 160  ASN B CA    1 
ATOM   9975  C  C     . ASN B 1  162  ? -0.554  48.641  107.410 1.00 17.33 ? 160  ASN B C     1 
ATOM   9976  O  O     . ASN B 1  162  ? -1.353  48.950  108.308 1.00 18.52 ? 160  ASN B O     1 
ATOM   9977  C  CB    . ASN B 1  162  ? -2.288  48.941  105.594 1.00 19.80 ? 160  ASN B CB    1 
ATOM   9978  C  CG    . ASN B 1  162  ? -2.084  50.449  105.487 1.00 18.64 ? 160  ASN B CG    1 
ATOM   9979  O  OD1   . ASN B 1  162  ? -1.150  50.991  106.078 1.00 19.47 ? 160  ASN B OD1   1 
ATOM   9980  N  ND2   . ASN B 1  162  ? -2.937  51.122  104.731 1.00 20.95 ? 160  ASN B ND2   1 
ATOM   9981  N  N     . ASP B 1  163  ? 0.771   48.652  107.580 1.00 18.43 ? 161  ASP B N     1 
ATOM   9982  C  CA    . ASP B 1  163  ? 1.345   48.933  108.885 1.00 18.17 ? 161  ASP B CA    1 
ATOM   9983  C  C     . ASP B 1  163  ? 1.211   50.392  109.276 1.00 17.98 ? 161  ASP B C     1 
ATOM   9984  O  O     . ASP B 1  163  ? 1.233   50.691  110.466 1.00 18.31 ? 161  ASP B O     1 
ATOM   9985  C  CB    . ASP B 1  163  ? 2.815   48.501  108.944 1.00 17.91 ? 161  ASP B CB    1 
ATOM   9986  C  CG    . ASP B 1  163  ? 3.652   49.007  107.774 1.00 21.08 ? 161  ASP B CG    1 
ATOM   9987  O  OD1   . ASP B 1  163  ? 3.202   48.970  106.613 1.00 18.54 ? 161  ASP B OD1   1 
ATOM   9988  O  OD2   . ASP B 1  163  ? 4.813   49.401  108.028 1.00 22.14 ? 161  ASP B OD2   1 
ATOM   9989  N  N     . ARG B 1  164  ? 1.077   51.311  108.316 1.00 17.49 ? 162  ARG B N     1 
ATOM   9990  C  CA    . ARG B 1  164  ? 0.814   52.691  108.707 1.00 16.40 ? 162  ARG B CA    1 
ATOM   9991  C  C     . ARG B 1  164  ? -0.598  52.851  109.259 1.00 15.53 ? 162  ARG B C     1 
ATOM   9992  O  O     . ARG B 1  164  ? -0.814  53.582  110.230 1.00 15.76 ? 162  ARG B O     1 
ATOM   9993  C  CB    . ARG B 1  164  ? 1.028   53.643  107.531 1.00 17.06 ? 162  ARG B CB    1 
ATOM   9994  C  CG    . ARG B 1  164  ? 2.467   53.680  107.024 1.00 17.81 ? 162  ARG B CG    1 
ATOM   9995  C  CD    . ARG B 1  164  ? 3.463   53.722  108.167 1.00 22.97 ? 162  ARG B CD    1 
ATOM   9996  N  NE    . ARG B 1  164  ? 3.187   54.804  109.096 1.00 28.30 ? 162  ARG B NE    1 
ATOM   9997  C  CZ    . ARG B 1  164  ? 3.668   54.872  110.329 1.00 31.51 ? 162  ARG B CZ    1 
ATOM   9998  N  NH1   . ARG B 1  164  ? 4.416   53.901  110.836 1.00 30.49 ? 162  ARG B NH1   1 
ATOM   9999  N  NH2   . ARG B 1  164  ? 3.397   55.942  111.069 1.00 29.02 ? 162  ARG B NH2   1 
ATOM   10000 N  N     . SER B 1  165  ? -1.572  52.192  108.628 1.00 16.86 ? 163  SER B N     1 
ATOM   10001 C  CA    . SER B 1  165  ? -2.939  52.205  109.138 1.00 16.93 ? 163  SER B CA    1 
ATOM   10002 C  C     . SER B 1  165  ? -3.016  51.581  110.523 1.00 16.06 ? 163  SER B C     1 
ATOM   10003 O  O     . SER B 1  165  ? -3.700  52.100  111.418 1.00 16.13 ? 163  SER B O     1 
ATOM   10004 C  CB    . SER B 1  165  ? -3.850  51.455  108.163 1.00 17.26 ? 163  SER B CB    1 
ATOM   10005 O  OG    . SER B 1  165  ? -5.129  51.260  108.733 1.00 19.17 ? 163  SER B OG    1 
ATOM   10006 N  N     . LEU B 1  166  ? -2.327  50.451  110.708 1.00 18.87 ? 164  LEU B N     1 
ATOM   10007 C  CA    . LEU B 1  166  ? -2.338  49.770  111.999 1.00 18.08 ? 164  LEU B CA    1 
ATOM   10008 C  C     . LEU B 1  166  ? -1.644  50.592  113.075 1.00 18.55 ? 164  LEU B C     1 
ATOM   10009 O  O     . LEU B 1  166  ? -2.107  50.632  114.219 1.00 18.18 ? 164  LEU B O     1 
ATOM   10010 C  CB    . LEU B 1  166  ? -1.675  48.407  111.859 1.00 18.83 ? 164  LEU B CB    1 
ATOM   10011 C  CG    . LEU B 1  166  ? -2.571  47.411  111.138 1.00 18.69 ? 164  LEU B CG    1 
ATOM   10012 C  CD1   . LEU B 1  166  ? -1.857  46.114  110.952 1.00 21.90 ? 164  LEU B CD1   1 
ATOM   10013 C  CD2   . LEU B 1  166  ? -3.851  47.200  111.938 1.00 20.42 ? 164  LEU B CD2   1 
ATOM   10014 N  N     . ALA B 1  167  ? -0.513  51.224  112.741 1.00 18.44 ? 165  ALA B N     1 
ATOM   10015 C  CA    . ALA B 1  167  ? 0.163   52.076  113.717 1.00 17.78 ? 165  ALA B CA    1 
ATOM   10016 C  C     . ALA B 1  167  ? -0.725  53.244  114.126 1.00 19.09 ? 165  ALA B C     1 
ATOM   10017 O  O     . ALA B 1  167  ? -0.816  53.584  115.308 1.00 20.63 ? 165  ALA B O     1 
ATOM   10018 C  CB    . ALA B 1  167  ? 1.490   52.580  113.152 1.00 21.45 ? 165  ALA B CB    1 
ATOM   10019 N  N     . ALA B 1  168  ? -1.406  53.854  113.154 1.00 18.24 ? 166  ALA B N     1 
ATOM   10020 C  CA    . ALA B 1  168  ? -2.344  54.922  113.461 1.00 18.68 ? 166  ALA B CA    1 
ATOM   10021 C  C     . ALA B 1  168  ? -3.465  54.414  114.353 1.00 17.38 ? 166  ALA B C     1 
ATOM   10022 O  O     . ALA B 1  168  ? -3.855  55.080  115.309 1.00 18.85 ? 166  ALA B O     1 
ATOM   10023 C  CB    . ALA B 1  168  ? -2.916  55.502  112.156 1.00 17.87 ? 166  ALA B CB    1 
ATOM   10024 N  N     . ALA B 1  169  ? -3.989  53.222  114.049 1.00 18.09 ? 167  ALA B N     1 
ATOM   10025 C  CA    . ALA B 1  169  ? -5.104  52.686  114.819 1.00 18.25 ? 167  ALA B CA    1 
ATOM   10026 C  C     . ALA B 1  169  ? -4.675  52.347  116.239 1.00 19.59 ? 167  ALA B C     1 
ATOM   10027 O  O     . ALA B 1  169  ? -5.431  52.566  117.187 1.00 20.02 ? 167  ALA B O     1 
ATOM   10028 C  CB    . ALA B 1  169  ? -5.671  51.450  114.112 1.00 19.28 ? 167  ALA B CB    1 
ATOM   10029 N  N     . LEU B 1  170  ? -3.467  51.811  116.406 1.00 19.24 ? 168  LEU B N     1 
ATOM   10030 C  CA    . LEU B 1  170  ? -3.014  51.471  117.750 1.00 18.98 ? 168  LEU B CA    1 
ATOM   10031 C  C     . LEU B 1  170  ? -2.787  52.727  118.579 1.00 20.00 ? 168  LEU B C     1 
ATOM   10032 O  O     . LEU B 1  170  ? -3.176  52.795  119.751 1.00 18.75 ? 168  LEU B O     1 
ATOM   10033 C  CB    . LEU B 1  170  ? -1.744  50.636  117.675 1.00 19.61 ? 168  LEU B CB    1 
ATOM   10034 C  CG    . LEU B 1  170  ? -1.242  50.062  119.007 1.00 20.05 ? 168  LEU B CG    1 
ATOM   10035 C  CD1   . LEU B 1  170  ? -2.314  49.217  119.666 1.00 21.71 ? 168  LEU B CD1   1 
ATOM   10036 C  CD2   . LEU B 1  170  ? -0.023  49.244  118.738 1.00 24.69 ? 168  LEU B CD2   1 
ATOM   10037 N  N     . THR B 1  171  ? -2.153  53.735  117.984 1.00 18.96 ? 169  THR B N     1 
ATOM   10038 C  CA    . THR B 1  171  ? -2.017  55.008  118.674 1.00 19.52 ? 169  THR B CA    1 
ATOM   10039 C  C     . THR B 1  171  ? -3.382  55.559  119.062 1.00 21.54 ? 169  THR B C     1 
ATOM   10040 O  O     . THR B 1  171  ? -3.581  56.005  120.190 1.00 20.62 ? 169  THR B O     1 
ATOM   10041 C  CB    . THR B 1  171  ? -1.262  56.002  117.794 1.00 19.86 ? 169  THR B CB    1 
ATOM   10042 O  OG1   . THR B 1  171  ? 0.046   55.487  117.527 1.00 23.68 ? 169  THR B OG1   1 
ATOM   10043 C  CG2   . THR B 1  171  ? -1.144  57.345  118.489 1.00 21.90 ? 169  THR B CG2   1 
ATOM   10044 N  N     . ARG B 1  172  ? -4.344  55.504  118.138 1.00 21.42 ? 170  ARG B N     1 
ATOM   10045 C  CA    . ARG B 1  172  ? -5.652  56.078  118.418 1.00 20.29 ? 170  ARG B CA    1 
ATOM   10046 C  C     . ARG B 1  172  ? -6.331  55.342  119.565 1.00 20.06 ? 170  ARG B C     1 
ATOM   10047 O  O     . ARG B 1  172  ? -6.839  55.961  120.502 1.00 21.97 ? 170  ARG B O     1 
ATOM   10048 C  CB    . ARG B 1  172  ? -6.515  56.044  117.153 1.00 20.30 ? 170  ARG B CB    1 
ATOM   10049 C  CG    . ARG B 1  172  ? -7.797  56.847  117.283 1.00 19.97 ? 170  ARG B CG    1 
ATOM   10050 C  CD    . ARG B 1  172  ? -8.689  56.682  116.055 1.00 21.82 ? 170  ARG B CD    1 
ATOM   10051 N  NE    . ARG B 1  172  ? -7.951  56.783  114.803 1.00 19.23 ? 170  ARG B NE    1 
ATOM   10052 C  CZ    . ARG B 1  172  ? -7.663  55.751  114.022 1.00 18.67 ? 170  ARG B CZ    1 
ATOM   10053 N  NH1   . ARG B 1  172  ? -7.998  54.516  114.359 1.00 20.18 ? 170  ARG B NH1   1 
ATOM   10054 N  NH2   . ARG B 1  172  ? -7.006  55.959  112.883 1.00 18.82 ? 170  ARG B NH2   1 
ATOM   10055 N  N     . LEU B 1  173  ? -6.324  54.009  119.524 1.00 20.69 ? 171  LEU B N     1 
ATOM   10056 C  CA    . LEU B 1  173  ? -7.055  53.272  120.548 1.00 21.61 ? 171  LEU B CA    1 
ATOM   10057 C  C     . LEU B 1  173  ? -6.408  53.418  121.922 1.00 21.04 ? 171  LEU B C     1 
ATOM   10058 O  O     . LEU B 1  173  ? -7.114  53.510  122.924 1.00 21.25 ? 171  LEU B O     1 
ATOM   10059 C  CB    . LEU B 1  173  ? -7.185  51.799  120.158 1.00 20.87 ? 171  LEU B CB    1 
ATOM   10060 C  CG    . LEU B 1  173  ? -6.017  50.819  120.262 1.00 23.16 ? 171  LEU B CG    1 
ATOM   10061 C  CD1   . LEU B 1  173  ? -5.978  50.146  121.635 1.00 23.85 ? 171  LEU B CD1   1 
ATOM   10062 C  CD2   . LEU B 1  173  ? -6.141  49.771  119.170 1.00 27.04 ? 171  LEU B CD2   1 
ATOM   10063 N  N     . ILE B 1  174  ? -5.075  53.436  121.994 1.00 21.85 ? 172  ILE B N     1 
ATOM   10064 C  CA    . ILE B 1  174  ? -4.434  53.578  123.299 1.00 21.57 ? 172  ILE B CA    1 
ATOM   10065 C  C     . ILE B 1  174  ? -4.650  54.981  123.850 1.00 21.77 ? 172  ILE B C     1 
ATOM   10066 O  O     . ILE B 1  174  ? -4.948  55.163  125.038 1.00 23.61 ? 172  ILE B O     1 
ATOM   10067 C  CB    . ILE B 1  174  ? -2.936  53.242  123.210 1.00 19.79 ? 172  ILE B CB    1 
ATOM   10068 C  CG1   . ILE B 1  174  ? -2.734  51.776  122.828 1.00 22.60 ? 172  ILE B CG1   1 
ATOM   10069 C  CG2   . ILE B 1  174  ? -2.248  53.558  124.548 1.00 26.40 ? 172  ILE B CG2   1 
ATOM   10070 C  CD1   . ILE B 1  174  ? -1.300  51.420  122.536 1.00 24.48 ? 172  ILE B CD1   1 
ATOM   10071 N  N     . SER B 1  175  ? -4.498  56.001  123.002 1.00 21.35 ? 173  SER B N     1 
ATOM   10072 C  CA    . SER B 1  175  ? -4.719  57.361  123.481 1.00 21.76 ? 173  SER B CA    1 
ATOM   10073 C  C     . SER B 1  175  ? -6.169  57.577  123.904 1.00 21.96 ? 173  SER B C     1 
ATOM   10074 O  O     . SER B 1  175  ? -6.438  58.397  124.787 1.00 25.20 ? 173  SER B O     1 
ATOM   10075 C  CB    . SER B 1  175  ? -4.316  58.375  122.412 1.00 25.11 ? 173  SER B CB    1 
ATOM   10076 O  OG    . SER B 1  175  ? -2.916  58.346  122.174 1.00 28.16 ? 173  SER B OG    1 
ATOM   10077 N  N     . ARG B 1  176  ? -7.109  56.840  123.302 1.00 22.12 ? 174  ARG B N     1 
ATOM   10078 C  CA    . ARG B 1  176  ? -8.524  56.989  123.640 1.00 22.39 ? 174  ARG B CA    1 
ATOM   10079 C  C     . ARG B 1  176  ? -8.902  56.178  124.880 1.00 22.75 ? 174  ARG B C     1 
ATOM   10080 O  O     . ARG B 1  176  ? -9.622  56.672  125.754 1.00 23.44 ? 174  ARG B O     1 
ATOM   10081 C  CB    . ARG B 1  176  ? -9.390  56.570  122.440 1.00 22.12 ? 174  ARG B CB    1 
ATOM   10082 C  CG    . ARG B 1  176  ? -10.915 56.807  122.604 1.00 22.90 ? 174  ARG B CG    1 
ATOM   10083 C  CD    . ARG B 1  176  ? -11.668 56.481  121.284 1.00 22.85 ? 174  ARG B CD    1 
ATOM   10084 N  NE    . ARG B 1  176  ? -11.821 55.046  121.043 1.00 25.21 ? 174  ARG B NE    1 
ATOM   10085 C  CZ    . ARG B 1  176  ? -11.246 54.339  120.072 1.00 28.33 ? 174  ARG B CZ    1 
ATOM   10086 N  NH1   . ARG B 1  176  ? -10.494 54.906  119.124 1.00 24.45 ? 174  ARG B NH1   1 
ATOM   10087 N  NH2   . ARG B 1  176  ? -11.435 53.021  120.036 1.00 27.94 ? 174  ARG B NH2   1 
ATOM   10088 N  N     . CYS B 1  177  ? -8.428  54.933  124.975 1.00 23.73 ? 175  CYS B N     1 
ATOM   10089 C  CA    . CYS B 1  177  ? -8.927  53.996  125.971 1.00 24.05 ? 175  CYS B CA    1 
ATOM   10090 C  C     . CYS B 1  177  ? -7.893  53.561  126.992 1.00 26.97 ? 175  CYS B C     1 
ATOM   10091 O  O     . CYS B 1  177  ? -8.282  53.023  128.030 1.00 28.20 ? 175  CYS B O     1 
ATOM   10092 C  CB    . CYS B 1  177  ? -9.502  52.746  125.293 1.00 26.29 ? 175  CYS B CB    1 
ATOM   10093 S  SG    . CYS B 1  177  ? -10.845 53.125  124.112 1.00 31.30 ? 175  CYS B SG    1 
ATOM   10094 N  N     . GLY B 1  178  ? -6.607  53.759  126.730 1.00 26.30 ? 176  GLY B N     1 
ATOM   10095 C  CA    . GLY B 1  178  ? -5.650  53.592  127.814 1.00 28.58 ? 176  GLY B CA    1 
ATOM   10096 C  C     . GLY B 1  178  ? -5.429  52.141  128.217 1.00 30.51 ? 176  GLY B C     1 
ATOM   10097 O  O     . GLY B 1  178  ? -5.671  51.197  127.461 1.00 29.37 ? 176  GLY B O     1 
ATOM   10098 N  N     . GLU B 1  179  ? -4.956  51.979  129.452 1.00 30.55 ? 177  GLU B N     1 
ATOM   10099 C  CA    . GLU B 1  179  ? -4.627  50.643  129.940 1.00 32.86 ? 177  GLU B CA    1 
ATOM   10100 C  C     . GLU B 1  179  ? -5.800  49.667  129.938 1.00 28.93 ? 177  GLU B C     1 
ATOM   10101 O  O     . GLU B 1  179  ? -5.574  48.491  129.609 1.00 28.91 ? 177  GLU B O     1 
ATOM   10102 C  CB    . GLU B 1  179  ? -4.025  50.732  131.348 1.00 38.12 ? 177  GLU B CB    1 
ATOM   10103 C  CG    . GLU B 1  179  ? -3.797  49.362  131.958 1.00 40.57 ? 177  GLU B CG    1 
ATOM   10104 C  CD    . GLU B 1  179  ? -3.352  49.429  133.392 1.00 49.90 ? 177  GLU B CD    1 
ATOM   10105 O  OE1   . GLU B 1  179  ? -2.627  50.384  133.736 1.00 54.43 ? 177  GLU B OE1   1 
ATOM   10106 O  OE2   . GLU B 1  179  ? -3.735  48.532  134.173 1.00 56.02 ? 177  GLU B OE2   1 
ATOM   10107 N  N     . PRO B 1  180  ? -7.035  50.045  130.299 1.00 27.93 ? 178  PRO B N     1 
ATOM   10108 C  CA    . PRO B 1  180  ? -8.105  49.033  130.332 1.00 28.82 ? 178  PRO B CA    1 
ATOM   10109 C  C     . PRO B 1  180  ? -8.313  48.303  129.015 1.00 33.89 ? 178  PRO B C     1 
ATOM   10110 O  O     . PRO B 1  180  ? -8.634  47.108  129.031 1.00 31.03 ? 178  PRO B O     1 
ATOM   10111 C  CB    . PRO B 1  180  ? -9.340  49.848  130.738 1.00 32.03 ? 178  PRO B CB    1 
ATOM   10112 C  CG    . PRO B 1  180  ? -8.780  50.940  131.583 1.00 31.45 ? 178  PRO B CG    1 
ATOM   10113 C  CD    . PRO B 1  180  ? -7.486  51.315  130.902 1.00 30.09 ? 178  PRO B CD    1 
ATOM   10114 N  N     . VAL B 1  181  ? -8.135  48.967  127.870 1.00 27.22 ? 179  VAL B N     1 
ATOM   10115 C  CA    . VAL B 1  181  ? -8.316  48.232  126.625 1.00 28.55 ? 179  VAL B CA    1 
ATOM   10116 C  C     . VAL B 1  181  ? -7.113  47.336  126.344 1.00 28.56 ? 179  VAL B C     1 
ATOM   10117 O  O     . VAL B 1  181  ? -7.263  46.269  125.739 1.00 29.19 ? 179  VAL B O     1 
ATOM   10118 C  CB    . VAL B 1  181  ? -8.597  49.176  125.437 1.00 30.87 ? 179  VAL B CB    1 
ATOM   10119 C  CG1   . VAL B 1  181  ? -7.336  49.934  125.005 1.00 29.53 ? 179  VAL B CG1   1 
ATOM   10120 C  CG2   . VAL B 1  181  ? -9.145  48.378  124.261 1.00 30.92 ? 179  VAL B CG2   1 
ATOM   10121 N  N     . ILE B 1  182  ? -5.913  47.738  126.767 1.00 28.77 ? 180  ILE B N     1 
ATOM   10122 C  CA    . ILE B 1  182  ? -4.743  46.884  126.582 1.00 29.74 ? 180  ILE B CA    1 
ATOM   10123 C  C     . ILE B 1  182  ? -4.881  45.619  127.417 1.00 30.21 ? 180  ILE B C     1 
ATOM   10124 O  O     . ILE B 1  182  ? -4.635  44.505  126.937 1.00 29.00 ? 180  ILE B O     1 
ATOM   10125 C  CB    . ILE B 1  182  ? -3.451  47.645  126.927 1.00 28.07 ? 180  ILE B CB    1 
ATOM   10126 C  CG1   . ILE B 1  182  ? -3.270  48.850  126.012 1.00 26.81 ? 180  ILE B CG1   1 
ATOM   10127 C  CG2   . ILE B 1  182  ? -2.244  46.720  126.785 1.00 28.29 ? 180  ILE B CG2   1 
ATOM   10128 C  CD1   . ILE B 1  182  ? -2.195  49.789  126.485 1.00 29.96 ? 180  ILE B CD1   1 
ATOM   10129 N  N     . ARG B 1  183  ? -5.286  45.775  128.678 1.00 29.90 ? 181  ARG B N     1 
ATOM   10130 C  CA    . ARG B 1  183  ? -5.483  44.624  129.552 1.00 32.64 ? 181  ARG B CA    1 
ATOM   10131 C  C     . ARG B 1  183  ? -6.521  43.665  128.975 1.00 32.76 ? 181  ARG B C     1 
ATOM   10132 O  O     . ARG B 1  183  ? -6.301  42.448  128.940 1.00 34.15 ? 181  ARG B O     1 
ATOM   10133 C  CB    . ARG B 1  183  ? -5.865  45.123  130.952 1.00 35.35 ? 181  ARG B CB    1 
ATOM   10134 C  CG    . ARG B 1  183  ? -6.506  44.115  131.918 1.00 41.96 ? 181  ARG B CG    1 
ATOM   10135 C  CD    . ARG B 1  183  ? -5.721  42.817  132.057 1.00 43.71 ? 181  ARG B CD    1 
ATOM   10136 N  NE    . ARG B 1  183  ? -4.279  43.012  132.114 1.00 44.52 ? 181  ARG B NE    1 
ATOM   10137 C  CZ    . ARG B 1  183  ? -3.394  42.092  131.757 1.00 43.18 ? 181  ARG B CZ    1 
ATOM   10138 N  NH1   . ARG B 1  183  ? -3.774  40.908  131.303 1.00 40.42 ? 181  ARG B NH1   1 
ATOM   10139 N  NH2   . ARG B 1  183  ? -2.097  42.369  131.849 1.00 47.81 ? 181  ARG B NH2   1 
ATOM   10140 N  N     . ARG B 1  184  ? -7.641  44.193  128.479 1.00 32.73 ? 182  ARG B N     1 
ATOM   10141 C  CA    . ARG B 1  184  ? -8.666  43.331  127.894 1.00 34.19 ? 182  ARG B CA    1 
ATOM   10142 C  C     . ARG B 1  184  ? -8.164  42.625  126.634 1.00 35.11 ? 182  ARG B C     1 
ATOM   10143 O  O     . ARG B 1  184  ? -8.524  41.470  126.383 1.00 34.00 ? 182  ARG B O     1 
ATOM   10144 C  CB    . ARG B 1  184  ? -9.929  44.144  127.596 1.00 35.07 ? 182  ARG B CB    1 
ATOM   10145 C  CG    . ARG B 1  184  ? -10.795 44.422  128.821 1.00 40.43 ? 182  ARG B CG    1 
ATOM   10146 C  CD    . ARG B 1  184  ? -11.889 43.368  129.005 1.00 42.68 ? 182  ARG B CD    1 
ATOM   10147 N  NE    . ARG B 1  184  ? -13.043 43.604  128.142 1.00 42.39 ? 182  ARG B NE    1 
ATOM   10148 C  CZ    . ARG B 1  184  ? -13.504 42.750  127.235 1.00 42.97 ? 182  ARG B CZ    1 
ATOM   10149 N  NH1   . ARG B 1  184  ? -12.940 41.566  127.046 1.00 41.34 ? 182  ARG B NH1   1 
ATOM   10150 N  NH2   . ARG B 1  184  ? -14.565 43.090  126.505 1.00 38.43 ? 182  ARG B NH2   1 
ATOM   10151 N  N     . GLY B 1  185  ? -7.340  43.296  125.825 1.00 31.30 ? 183  GLY B N     1 
ATOM   10152 C  CA    . GLY B 1  185  ? -6.811  42.646  124.637 1.00 31.09 ? 183  GLY B CA    1 
ATOM   10153 C  C     . GLY B 1  185  ? -5.854  41.518  124.974 1.00 32.47 ? 183  GLY B C     1 
ATOM   10154 O  O     . GLY B 1  185  ? -5.893  40.452  124.358 1.00 32.02 ? 183  GLY B O     1 
ATOM   10155 N  N     . VAL B 1  186  ? -4.987  41.739  125.963 1.00 28.34 ? 184  VAL B N     1 
ATOM   10156 C  CA    . VAL B 1  186  ? -4.061  40.702  126.409 1.00 31.00 ? 184  VAL B CA    1 
ATOM   10157 C  C     . VAL B 1  186  ? -4.824  39.485  126.927 1.00 34.59 ? 184  VAL B C     1 
ATOM   10158 O  O     . VAL B 1  186  ? -4.510  38.340  126.582 1.00 34.93 ? 184  VAL B O     1 
ATOM   10159 C  CB    . VAL B 1  186  ? -3.114  41.270  127.480 1.00 32.65 ? 184  VAL B CB    1 
ATOM   10160 C  CG1   . VAL B 1  186  ? -2.364  40.137  128.186 1.00 35.31 ? 184  VAL B CG1   1 
ATOM   10161 C  CG2   . VAL B 1  186  ? -2.146  42.263  126.852 1.00 30.35 ? 184  VAL B CG2   1 
ATOM   10162 N  N     . ASP B 1  187  ? -5.831  39.716  127.773 1.00 34.61 ? 185  ASP B N     1 
ATOM   10163 C  CA    . ASP B 1  187  ? -6.610  38.603  128.312 1.00 36.08 ? 185  ASP B CA    1 
ATOM   10164 C  C     . ASP B 1  187  ? -7.356  37.866  127.209 1.00 40.37 ? 185  ASP B C     1 
ATOM   10165 O  O     . ASP B 1  187  ? -7.394  36.630  127.193 1.00 36.72 ? 185  ASP B O     1 
ATOM   10166 C  CB    . ASP B 1  187  ? -7.583  39.108  129.373 1.00 36.51 ? 185  ASP B CB    1 
ATOM   10167 C  CG    . ASP B 1  187  ? -6.872  39.690  130.583 1.00 39.72 ? 185  ASP B CG    1 
ATOM   10168 O  OD1   . ASP B 1  187  ? -5.659  39.434  130.752 1.00 41.02 ? 185  ASP B OD1   1 
ATOM   10169 O  OD2   . ASP B 1  187  ? -7.530  40.397  131.366 1.00 41.98 ? 185  ASP B OD2   1 
ATOM   10170 N  N     . MET B 1  188  ? -7.943  38.611  126.270 1.00 39.39 ? 186  MET B N     1 
ATOM   10171 C  CA    . MET B 1  188  ? -8.632  38.003  125.136 1.00 38.69 ? 186  MET B CA    1 
ATOM   10172 C  C     . MET B 1  188  ? -7.676  37.173  124.281 1.00 41.22 ? 186  MET B C     1 
ATOM   10173 O  O     . MET B 1  188  ? -7.995  36.045  123.885 1.00 43.88 ? 186  MET B O     1 
ATOM   10174 C  CB    . MET B 1  188  ? -9.297  39.096  124.301 1.00 39.78 ? 186  MET B CB    1 
ATOM   10175 C  CG    . MET B 1  188  ? -10.102 38.583  123.127 1.00 44.11 ? 186  MET B CG    1 
ATOM   10176 S  SD    . MET B 1  188  ? -11.502 37.615  123.697 1.00 56.20 ? 186  MET B SD    1 
ATOM   10177 C  CE    . MET B 1  188  ? -12.164 38.669  124.997 1.00 48.22 ? 186  MET B CE    1 
ATOM   10178 N  N     . ALA B 1  189  ? -6.498  37.721  123.973 1.00 38.48 ? 187  ALA B N     1 
ATOM   10179 C  CA    . ALA B 1  189  ? -5.528  36.974  123.178 1.00 41.05 ? 187  ALA B CA    1 
ATOM   10180 C  C     . ALA B 1  189  ? -5.059  35.727  123.916 1.00 46.24 ? 187  ALA B C     1 
ATOM   10181 O  O     . ALA B 1  189  ? -4.885  34.663  123.310 1.00 45.06 ? 187  ALA B O     1 
ATOM   10182 C  CB    . ALA B 1  189  ? -4.337  37.862  122.828 1.00 35.26 ? 187  ALA B CB    1 
ATOM   10183 N  N     . MET B 1  190  ? -4.848  35.844  125.228 1.00 41.09 ? 188  MET B N     1 
ATOM   10184 C  CA    . MET B 1  190  ? -4.417  34.695  126.016 1.00 46.44 ? 188  MET B CA    1 
ATOM   10185 C  C     . MET B 1  190  ? -5.433  33.563  125.930 1.00 45.07 ? 188  MET B C     1 
ATOM   10186 O  O     . MET B 1  190  ? -5.069  32.402  125.712 1.00 47.19 ? 188  MET B O     1 
ATOM   10187 C  CB    . MET B 1  190  ? -4.196  35.113  127.470 1.00 38.52 ? 188  MET B CB    1 
ATOM   10188 C  CG    . MET B 1  190  ? -2.985  34.464  128.118 1.00 45.60 ? 188  MET B CG    1 
ATOM   10189 S  SD    . MET B 1  190  ? -2.893  34.790  129.890 1.00 56.14 ? 188  MET B SD    1 
ATOM   10190 C  CE    . MET B 1  190  ? -2.727  36.575  129.922 1.00 43.00 ? 188  MET B CE    1 
ATOM   10191 N  N     . ARG B 1  191  ? -6.718  33.890  126.083 1.00 43.62 ? 189  ARG B N     1 
ATOM   10192 C  CA    . ARG B 1  191  ? -7.758  32.869  125.994 1.00 47.50 ? 189  ARG B CA    1 
ATOM   10193 C  C     . ARG B 1  191  ? -7.747  32.180  124.634 1.00 51.88 ? 189  ARG B C     1 
ATOM   10194 O  O     . ARG B 1  191  ? -7.895  30.956  124.549 1.00 53.54 ? 189  ARG B O     1 
ATOM   10195 C  CB    . ARG B 1  191  ? -9.125  33.491  126.270 1.00 44.06 ? 189  ARG B CB    1 
ATOM   10196 N  N     . MET B 1  192  ? -7.565  32.943  123.557 1.00 47.10 ? 190  MET B N     1 
ATOM   10197 C  CA    . MET B 1  192  ? -7.571  32.340  122.228 1.00 45.47 ? 190  MET B CA    1 
ATOM   10198 C  C     . MET B 1  192  ? -6.307  31.521  121.989 1.00 48.42 ? 190  MET B C     1 
ATOM   10199 O  O     . MET B 1  192  ? -6.371  30.321  121.694 1.00 48.05 ? 190  MET B O     1 
ATOM   10200 C  CB    . MET B 1  192  ? -7.719  33.425  121.160 1.00 47.00 ? 190  MET B CB    1 
ATOM   10201 C  CG    . MET B 1  192  ? -8.931  34.329  121.320 1.00 46.64 ? 190  MET B CG    1 
ATOM   10202 S  SD    . MET B 1  192  ? -9.052  35.497  119.943 1.00 55.34 ? 190  MET B SD    1 
ATOM   10203 C  CE    . MET B 1  192  ? -9.446  34.383  118.604 1.00 41.35 ? 190  MET B CE    1 
ATOM   10204 N  N     . MET B 1  193  ? -5.141  32.156  122.114 1.00 47.36 ? 191  MET B N     1 
ATOM   10205 C  CA    . MET B 1  193  ? -3.883  31.523  121.731 1.00 49.66 ? 191  MET B CA    1 
ATOM   10206 C  C     . MET B 1  193  ? -3.444  30.425  122.684 1.00 51.11 ? 191  MET B C     1 
ATOM   10207 O  O     . MET B 1  193  ? -2.372  29.844  122.471 1.00 51.45 ? 191  MET B O     1 
ATOM   10208 C  CB    . MET B 1  193  ? -2.771  32.565  121.621 1.00 44.64 ? 191  MET B CB    1 
ATOM   10209 C  CG    . MET B 1  193  ? -2.746  33.296  120.307 1.00 45.33 ? 191  MET B CG    1 
ATOM   10210 S  SD    . MET B 1  193  ? -1.147  34.083  120.020 1.00 51.74 ? 191  MET B SD    1 
ATOM   10211 C  CE    . MET B 1  193  ? -1.087  35.226  121.394 1.00 41.41 ? 191  MET B CE    1 
ATOM   10212 N  N     . GLY B 1  194  ? -4.221  30.130  123.719 1.00 54.64 ? 192  GLY B N     1 
ATOM   10213 C  CA    . GLY B 1  194  ? -3.866  29.063  124.631 1.00 50.65 ? 192  GLY B CA    1 
ATOM   10214 C  C     . GLY B 1  194  ? -4.970  28.043  124.801 1.00 53.74 ? 192  GLY B C     1 
ATOM   10215 O  O     . GLY B 1  194  ? -4.725  26.946  125.312 1.00 55.13 ? 192  GLY B O     1 
ATOM   10216 N  N     . GLU B 1  195  ? -6.193  28.386  124.375 1.00 47.56 ? 193  GLU B N     1 
ATOM   10217 C  CA    . GLU B 1  195  ? -7.343  27.531  124.661 1.00 50.33 ? 193  GLU B CA    1 
ATOM   10218 C  C     . GLU B 1  195  ? -8.277  27.293  123.483 1.00 45.48 ? 193  GLU B C     1 
ATOM   10219 O  O     . GLU B 1  195  ? -8.922  26.242  123.459 1.00 40.17 ? 193  GLU B O     1 
ATOM   10220 C  CB    . GLU B 1  195  ? -8.162  28.106  125.827 1.00 55.32 ? 193  GLU B CB    1 
ATOM   10221 C  CG    . GLU B 1  195  ? -7.375  28.261  127.121 1.00 57.71 ? 193  GLU B CG    1 
ATOM   10222 C  CD    . GLU B 1  195  ? -8.182  28.921  128.218 1.00 59.05 ? 193  GLU B CD    1 
ATOM   10223 O  OE1   . GLU B 1  195  ? -9.429  28.884  128.144 1.00 62.73 ? 193  GLU B OE1   1 
ATOM   10224 O  OE2   . GLU B 1  195  ? -7.567  29.478  129.153 1.00 59.58 ? 193  GLU B OE2   1 
ATOM   10225 N  N     . GLN B 1  196  ? -8.389  28.209  122.518 1.00 54.29 ? 194  GLN B N     1 
ATOM   10226 C  CA    . GLN B 1  196  ? -9.262  28.021  121.361 1.00 48.35 ? 194  GLN B CA    1 
ATOM   10227 C  C     . GLN B 1  196  ? -8.509  27.666  120.085 1.00 49.67 ? 194  GLN B C     1 
ATOM   10228 O  O     . GLN B 1  196  ? -9.031  26.914  119.257 1.00 51.93 ? 194  GLN B O     1 
ATOM   10229 C  CB    . GLN B 1  196  ? -10.094 29.282  121.109 1.00 44.67 ? 194  GLN B CB    1 
ATOM   10230 N  N     . PHE B 1  197  ? -7.308  28.205  119.897 1.00 38.42 ? 195  PHE B N     1 
ATOM   10231 C  CA    . PHE B 1  197  ? -6.491  27.822  118.753 1.00 39.03 ? 195  PHE B CA    1 
ATOM   10232 C  C     . PHE B 1  197  ? -5.726  26.535  119.027 1.00 37.90 ? 195  PHE B C     1 
ATOM   10233 O  O     . PHE B 1  197  ? -5.541  25.710  118.125 1.00 35.94 ? 195  PHE B O     1 
ATOM   10234 C  CB    . PHE B 1  197  ? -5.522  28.948  118.409 1.00 39.38 ? 195  PHE B CB    1 
ATOM   10235 C  CG    . PHE B 1  197  ? -6.177  30.152  117.810 1.00 40.51 ? 195  PHE B CG    1 
ATOM   10236 C  CD1   . PHE B 1  197  ? -7.251  30.015  116.951 1.00 42.50 ? 195  PHE B CD1   1 
ATOM   10237 C  CD2   . PHE B 1  197  ? -5.713  31.423  118.104 1.00 44.22 ? 195  PHE B CD2   1 
ATOM   10238 C  CE1   . PHE B 1  197  ? -7.855  31.127  116.392 1.00 43.80 ? 195  PHE B CE1   1 
ATOM   10239 C  CE2   . PHE B 1  197  ? -6.311  32.539  117.552 1.00 45.10 ? 195  PHE B CE2   1 
ATOM   10240 C  CZ    . PHE B 1  197  ? -7.383  32.388  116.694 1.00 45.41 ? 195  PHE B CZ    1 
ATOM   10241 N  N     . VAL B 1  198  ? -5.273  26.349  120.263 1.00 34.40 ? 196  VAL B N     1 
ATOM   10242 C  CA    . VAL B 1  198  ? -4.589  25.132  120.666 1.00 32.85 ? 196  VAL B CA    1 
ATOM   10243 C  C     . VAL B 1  198  ? -5.336  24.533  121.846 1.00 35.95 ? 196  VAL B C     1 
ATOM   10244 O  O     . VAL B 1  198  ? -5.981  25.239  122.630 1.00 36.94 ? 196  VAL B O     1 
ATOM   10245 C  CB    . VAL B 1  198  ? -3.109  25.378  121.035 1.00 32.36 ? 196  VAL B CB    1 
ATOM   10246 C  CG1   . VAL B 1  198  ? -2.344  25.900  119.841 1.00 35.38 ? 196  VAL B CG1   1 
ATOM   10247 C  CG2   . VAL B 1  198  ? -3.009  26.345  122.209 1.00 38.71 ? 196  VAL B CG2   1 
ATOM   10248 N  N     . THR B 1  199  ? -5.256  23.214  121.962 1.00 29.70 ? 197  THR B N     1 
ATOM   10249 C  CA    . THR B 1  199  ? -5.811  22.555  123.134 1.00 30.17 ? 197  THR B CA    1 
ATOM   10250 C  C     . THR B 1  199  ? -4.896  22.708  124.334 1.00 33.02 ? 197  THR B C     1 
ATOM   10251 O  O     . THR B 1  199  ? -5.361  22.637  125.474 1.00 35.35 ? 197  THR B O     1 
ATOM   10252 C  CB    . THR B 1  199  ? -6.066  21.086  122.809 1.00 29.14 ? 197  THR B CB    1 
ATOM   10253 O  OG1   . THR B 1  199  ? -6.840  21.028  121.606 1.00 33.71 ? 197  THR B OG1   1 
ATOM   10254 C  CG2   . THR B 1  199  ? -6.837  20.395  123.927 1.00 29.23 ? 197  THR B CG2   1 
ATOM   10255 N  N     . GLY B 1  200  ? -3.620  22.941  124.091 1.00 30.19 ? 198  GLY B N     1 
ATOM   10256 C  CA    . GLY B 1  200  ? -2.685  23.247  125.147 1.00 34.00 ? 198  GLY B CA    1 
ATOM   10257 C  C     . GLY B 1  200  ? -1.353  23.591  124.520 1.00 31.11 ? 198  GLY B C     1 
ATOM   10258 O  O     . GLY B 1  200  ? -1.098  23.287  123.351 1.00 29.85 ? 198  GLY B O     1 
ATOM   10259 N  N     . GLU B 1  201  ? -0.510  24.251  125.318 1.00 31.86 ? 199  GLU B N     1 
ATOM   10260 C  CA    . GLU B 1  201  ? 0.820   24.604  124.830 1.00 31.95 ? 199  GLU B CA    1 
ATOM   10261 C  C     . GLU B 1  201  ? 1.755   23.403  124.817 1.00 28.96 ? 199  GLU B C     1 
ATOM   10262 O  O     . GLU B 1  201  ? 2.687   23.358  124.007 1.00 32.89 ? 199  GLU B O     1 
ATOM   10263 C  CB    . GLU B 1  201  ? 1.420   25.729  125.677 1.00 34.01 ? 199  GLU B CB    1 
ATOM   10264 N  N     . THR B 1  202  ? 1.531   22.438  125.708 1.00 27.35 ? 200  THR B N     1 
ATOM   10265 C  CA    . THR B 1  202  ? 2.296   21.201  125.769 1.00 28.27 ? 200  THR B CA    1 
ATOM   10266 C  C     . THR B 1  202  ? 1.331   20.027  125.716 1.00 26.95 ? 200  THR B C     1 
ATOM   10267 O  O     . THR B 1  202  ? 0.139   20.171  126.000 1.00 27.89 ? 200  THR B O     1 
ATOM   10268 C  CB    . THR B 1  202  ? 3.106   21.079  127.061 1.00 27.75 ? 200  THR B CB    1 
ATOM   10269 O  OG1   . THR B 1  202  ? 2.198   21.030  128.165 1.00 30.69 ? 200  THR B OG1   1 
ATOM   10270 C  CG2   . THR B 1  202  ? 4.053   22.264  127.238 1.00 31.44 ? 200  THR B CG2   1 
ATOM   10271 N  N     . ILE B 1  203  ? 1.866   18.849  125.386 1.00 28.00 ? 201  ILE B N     1 
ATOM   10272 C  CA    . ILE B 1  203  ? 1.021   17.657  125.353 1.00 25.05 ? 201  ILE B CA    1 
ATOM   10273 C  C     . ILE B 1  203  ? 0.489   17.358  126.748 1.00 27.88 ? 201  ILE B C     1 
ATOM   10274 O  O     . ILE B 1  203  ? -0.648  16.895  126.904 1.00 26.52 ? 201  ILE B O     1 
ATOM   10275 C  CB    . ILE B 1  203  ? 1.782   16.459  124.745 1.00 25.95 ? 201  ILE B CB    1 
ATOM   10276 C  CG1   . ILE B 1  203  ? 0.804   15.327  124.425 1.00 25.20 ? 201  ILE B CG1   1 
ATOM   10277 C  CG2   . ILE B 1  203  ? 2.909   15.968  125.676 1.00 24.81 ? 201  ILE B CG2   1 
ATOM   10278 C  CD1   . ILE B 1  203  ? -0.247  15.730  123.384 1.00 22.21 ? 201  ILE B CD1   1 
ATOM   10279 N  N     . ARG B 1  204  ? 1.280   17.663  127.785 1.00 27.84 ? 202  ARG B N     1 
ATOM   10280 C  CA    . ARG B 1  204  ? 0.822   17.550  129.166 1.00 31.07 ? 202  ARG B CA    1 
ATOM   10281 C  C     . ARG B 1  204  ? -0.451  18.362  129.384 1.00 29.66 ? 202  ARG B C     1 
ATOM   10282 O  O     . ARG B 1  204  ? -1.453  17.850  129.898 1.00 30.90 ? 202  ARG B O     1 
ATOM   10283 C  CB    . ARG B 1  204  ? 1.949   18.017  130.104 1.00 29.77 ? 202  ARG B CB    1 
ATOM   10284 C  CG    . ARG B 1  204  ? 1.622   18.072  131.584 1.00 39.62 ? 202  ARG B CG    1 
ATOM   10285 C  CD    . ARG B 1  204  ? 2.639   18.957  132.344 1.00 40.39 ? 202  ARG B CD    1 
ATOM   10286 N  NE    . ARG B 1  204  ? 1.963   20.068  133.007 1.00 46.47 ? 202  ARG B NE    1 
ATOM   10287 C  CZ    . ARG B 1  204  ? 1.731   21.256  132.458 1.00 43.74 ? 202  ARG B CZ    1 
ATOM   10288 N  NH1   . ARG B 1  204  ? 2.181   21.567  131.250 1.00 40.48 ? 202  ARG B NH1   1 
ATOM   10289 N  NH2   . ARG B 1  204  ? 1.017   22.153  133.134 1.00 50.52 ? 202  ARG B NH2   1 
ATOM   10290 N  N     . GLU B 1  205  ? -0.437  19.632  128.973 1.00 29.62 ? 203  GLU B N     1 
ATOM   10291 C  CA    . GLU B 1  205  ? -1.603  20.485  129.177 1.00 32.16 ? 203  GLU B CA    1 
ATOM   10292 C  C     . GLU B 1  205  ? -2.773  20.039  128.307 1.00 28.64 ? 203  GLU B C     1 
ATOM   10293 O  O     . GLU B 1  205  ? -3.917  19.981  128.773 1.00 32.29 ? 203  GLU B O     1 
ATOM   10294 C  CB    . GLU B 1  205  ? -1.237  21.940  128.886 1.00 33.47 ? 203  GLU B CB    1 
ATOM   10295 C  CG    . GLU B 1  205  ? -2.283  22.959  129.319 1.00 39.69 ? 203  GLU B CG    1 
ATOM   10296 C  CD    . GLU B 1  205  ? -1.871  24.391  129.006 1.00 43.25 ? 203  GLU B CD    1 
ATOM   10297 O  OE1   . GLU B 1  205  ? -1.236  24.620  127.957 1.00 40.41 ? 203  GLU B OE1   1 
ATOM   10298 O  OE2   . GLU B 1  205  ? -2.184  25.291  129.814 1.00 52.06 ? 203  GLU B OE2   1 
ATOM   10299 N  N     . ALA B 1  206  ? -2.505  19.718  127.043 1.00 27.78 ? 204  ALA B N     1 
ATOM   10300 C  CA    . ALA B 1  206  ? -3.575  19.289  126.151 1.00 28.83 ? 204  ALA B CA    1 
ATOM   10301 C  C     . ALA B 1  206  ? -4.260  18.041  126.685 1.00 29.03 ? 204  ALA B C     1 
ATOM   10302 O  O     . ALA B 1  206  ? -5.494  17.967  126.713 1.00 29.71 ? 204  ALA B O     1 
ATOM   10303 C  CB    . ALA B 1  206  ? -3.027  19.051  124.742 1.00 26.87 ? 204  ALA B CB    1 
ATOM   10304 N  N     . LEU B 1  207  ? -3.473  17.068  127.153 1.00 26.35 ? 205  LEU B N     1 
ATOM   10305 C  CA    . LEU B 1  207  ? -4.050  15.847  127.706 1.00 30.34 ? 205  LEU B CA    1 
ATOM   10306 C  C     . LEU B 1  207  ? -4.935  16.142  128.911 1.00 31.71 ? 205  LEU B C     1 
ATOM   10307 O  O     . LEU B 1  207  ? -6.000  15.531  129.069 1.00 32.00 ? 205  LEU B O     1 
ATOM   10308 C  CB    . LEU B 1  207  ? -2.936  14.864  128.074 1.00 30.05 ? 205  LEU B CB    1 
ATOM   10309 C  CG    . LEU B 1  207  ? -2.265  14.188  126.872 1.00 31.07 ? 205  LEU B CG    1 
ATOM   10310 C  CD1   . LEU B 1  207  ? -1.000  13.421  127.285 1.00 28.82 ? 205  LEU B CD1   1 
ATOM   10311 C  CD2   . LEU B 1  207  ? -3.255  13.269  126.149 1.00 27.70 ? 205  LEU B CD2   1 
ATOM   10312 N  N     . LYS B 1  208  ? -4.517  17.080  129.773 1.00 30.72 ? 206  LYS B N     1 
ATOM   10313 C  CA    . LYS B 1  208  ? -5.311  17.409  130.953 1.00 33.75 ? 206  LYS B CA    1 
ATOM   10314 C  C     . LYS B 1  208  ? -6.608  18.125  130.576 1.00 34.13 ? 206  LYS B C     1 
ATOM   10315 O  O     . LYS B 1  208  ? -7.660  17.878  131.179 1.00 35.59 ? 206  LYS B O     1 
ATOM   10316 C  CB    . LYS B 1  208  ? -4.486  18.260  131.923 1.00 32.80 ? 206  LYS B CB    1 
ATOM   10317 N  N     . ARG B 1  209  ? -6.560  19.012  129.583 1.00 33.41 ? 207  ARG B N     1 
ATOM   10318 C  CA    . ARG B 1  209  ? -7.774  19.716  129.189 1.00 33.33 ? 207  ARG B CA    1 
ATOM   10319 C  C     . ARG B 1  209  ? -8.743  18.827  128.422 1.00 35.58 ? 207  ARG B C     1 
ATOM   10320 O  O     . ARG B 1  209  ? -9.914  19.197  128.269 1.00 35.73 ? 207  ARG B O     1 
ATOM   10321 C  CB    . ARG B 1  209  ? -7.418  20.940  128.355 1.00 34.78 ? 207  ARG B CB    1 
ATOM   10322 C  CG    . ARG B 1  209  ? -6.644  21.991  129.135 1.00 39.49 ? 207  ARG B CG    1 
ATOM   10323 C  CD    . ARG B 1  209  ? -6.395  23.202  128.273 1.00 38.25 ? 207  ARG B CD    1 
ATOM   10324 N  NE    . ARG B 1  209  ? -5.835  24.320  129.017 1.00 50.84 ? 207  ARG B NE    1 
ATOM   10325 C  CZ    . ARG B 1  209  ? -5.319  25.401  128.449 1.00 54.32 ? 207  ARG B CZ    1 
ATOM   10326 N  NH1   . ARG B 1  209  ? -5.238  25.516  127.133 1.00 48.07 ? 207  ARG B NH1   1 
ATOM   10327 N  NH2   . ARG B 1  209  ? -4.873  26.390  129.219 1.00 57.78 ? 207  ARG B NH2   1 
ATOM   10328 N  N     . SER B 1  210  ? -8.296  17.656  127.976 1.00 32.17 ? 208  SER B N     1 
ATOM   10329 C  CA    . SER B 1  210  ? -9.141  16.777  127.183 1.00 33.42 ? 208  SER B CA    1 
ATOM   10330 C  C     . SER B 1  210  ? -10.104 15.956  128.026 1.00 32.50 ? 208  SER B C     1 
ATOM   10331 O  O     . SER B 1  210  ? -11.111 15.475  127.495 1.00 34.24 ? 208  SER B O     1 
ATOM   10332 C  CB    . SER B 1  210  ? -8.258  15.857  126.343 1.00 30.88 ? 208  SER B CB    1 
ATOM   10333 O  OG    . SER B 1  210  ? -7.485  16.635  125.435 1.00 31.58 ? 208  SER B OG    1 
ATOM   10334 N  N     . LYS B 1  211  ? -9.833  15.796  129.324 1.00 34.78 ? 209  LYS B N     1 
ATOM   10335 C  CA    . LYS B 1  211  ? -10.673 14.937  130.149 1.00 33.76 ? 209  LYS B CA    1 
ATOM   10336 C  C     . LYS B 1  211  ? -12.122 15.407  130.166 1.00 34.64 ? 209  LYS B C     1 
ATOM   10337 O  O     . LYS B 1  211  ? -13.036 14.582  130.246 1.00 36.47 ? 209  LYS B O     1 
ATOM   10338 C  CB    . LYS B 1  211  ? -10.122 14.871  131.574 1.00 35.52 ? 209  LYS B CB    1 
ATOM   10339 N  N     . GLU B 1  212  ? -12.352 16.719  130.071 1.00 35.06 ? 210  GLU B N     1 
ATOM   10340 C  CA    . GLU B 1  212  ? -13.708 17.240  130.212 1.00 35.89 ? 210  GLU B CA    1 
ATOM   10341 C  C     . GLU B 1  212  ? -14.618 16.720  129.104 1.00 36.40 ? 210  GLU B C     1 
ATOM   10342 O  O     . GLU B 1  212  ? -15.677 16.144  129.373 1.00 36.38 ? 210  GLU B O     1 
ATOM   10343 C  CB    . GLU B 1  212  ? -13.685 18.769  130.220 1.00 41.05 ? 210  GLU B CB    1 
ATOM   10344 C  CG    . GLU B 1  212  ? -15.057 19.399  130.411 1.00 46.62 ? 210  GLU B CG    1 
ATOM   10345 C  CD    . GLU B 1  212  ? -15.030 20.910  130.294 1.00 53.61 ? 210  GLU B CD    1 
ATOM   10346 O  OE1   . GLU B 1  212  ? -14.254 21.553  131.031 1.00 62.66 ? 210  GLU B OE1   1 
ATOM   10347 O  OE2   . GLU B 1  212  ? -15.781 21.456  129.458 1.00 60.92 ? 210  GLU B OE2   1 
ATOM   10348 N  N     . LEU B 1  213  ? -14.220 16.913  127.846 1.00 34.65 ? 211  LEU B N     1 
ATOM   10349 C  CA    . LEU B 1  213  ? -15.069 16.464  126.747 1.00 36.12 ? 211  LEU B CA    1 
ATOM   10350 C  C     . LEU B 1  213  ? -14.998 14.952  126.566 1.00 34.66 ? 211  LEU B C     1 
ATOM   10351 O  O     . LEU B 1  213  ? -15.978 14.340  126.121 1.00 33.87 ? 211  LEU B O     1 
ATOM   10352 C  CB    . LEU B 1  213  ? -14.701 17.201  125.458 1.00 33.13 ? 211  LEU B CB    1 
ATOM   10353 C  CG    . LEU B 1  213  ? -15.085 18.686  125.481 1.00 34.81 ? 211  LEU B CG    1 
ATOM   10354 C  CD1   . LEU B 1  213  ? -14.729 19.409  124.202 1.00 35.39 ? 211  LEU B CD1   1 
ATOM   10355 C  CD2   . LEU B 1  213  ? -16.567 18.846  125.780 1.00 38.82 ? 211  LEU B CD2   1 
ATOM   10356 N  N     . GLU B 1  214  ? -13.868 14.329  126.926 1.00 30.98 ? 212  GLU B N     1 
ATOM   10357 C  CA    . GLU B 1  214  ? -13.794 12.871  126.895 1.00 32.51 ? 212  GLU B CA    1 
ATOM   10358 C  C     . GLU B 1  214  ? -14.857 12.246  127.792 1.00 31.57 ? 212  GLU B C     1 
ATOM   10359 O  O     . GLU B 1  214  ? -15.536 11.298  127.381 1.00 32.45 ? 212  GLU B O     1 
ATOM   10360 C  CB    . GLU B 1  214  ? -12.396 12.390  127.296 1.00 32.96 ? 212  GLU B CB    1 
ATOM   10361 C  CG    . GLU B 1  214  ? -11.351 12.590  126.197 1.00 28.72 ? 212  GLU B CG    1 
ATOM   10362 C  CD    . GLU B 1  214  ? -10.022 11.898  126.484 1.00 30.20 ? 212  GLU B CD    1 
ATOM   10363 O  OE1   . GLU B 1  214  ? -9.782  11.488  127.640 1.00 33.64 ? 212  GLU B OE1   1 
ATOM   10364 O  OE2   . GLU B 1  214  ? -9.210  11.771  125.540 1.00 29.09 ? 212  GLU B OE2   1 
ATOM   10365 N  N     . GLU B 1  215  ? -15.035 12.776  129.008 1.00 34.10 ? 213  GLU B N     1 
ATOM   10366 C  CA    . GLU B 1  215  ? -16.099 12.284  129.882 1.00 34.59 ? 213  GLU B CA    1 
ATOM   10367 C  C     . GLU B 1  215  ? -17.480 12.468  129.266 1.00 34.87 ? 213  GLU B C     1 
ATOM   10368 O  O     . GLU B 1  215  ? -18.410 11.747  129.639 1.00 35.83 ? 213  GLU B O     1 
ATOM   10369 C  CB    . GLU B 1  215  ? -16.049 12.980  131.247 1.00 40.68 ? 213  GLU B CB    1 
ATOM   10370 C  CG    . GLU B 1  215  ? -14.932 12.488  132.168 1.00 41.63 ? 213  GLU B CG    1 
ATOM   10371 C  CD    . GLU B 1  215  ? -14.920 13.205  133.505 1.00 47.81 ? 213  GLU B CD    1 
ATOM   10372 O  OE1   . GLU B 1  215  ? -15.952 13.175  134.213 1.00 56.32 ? 213  GLU B OE1   1 
ATOM   10373 O  OE2   . GLU B 1  215  ? -13.878 13.807  133.842 1.00 50.19 ? 213  GLU B OE2   1 
ATOM   10374 N  N     . LYS B 1  216  ? -17.633 13.418  128.340 1.00 33.34 ? 214  LYS B N     1 
ATOM   10375 C  CA    . LYS B 1  216  ? -18.889 13.600  127.625 1.00 35.73 ? 214  LYS B CA    1 
ATOM   10376 C  C     . LYS B 1  216  ? -19.032 12.668  126.428 1.00 37.97 ? 214  LYS B C     1 
ATOM   10377 O  O     . LYS B 1  216  ? -20.122 12.595  125.849 1.00 39.61 ? 214  LYS B O     1 
ATOM   10378 C  CB    . LYS B 1  216  ? -19.028 15.055  127.164 1.00 36.05 ? 214  LYS B CB    1 
ATOM   10379 N  N     . GLY B 1  217  ? -17.978 11.946  126.047 1.00 35.47 ? 215  GLY B N     1 
ATOM   10380 C  CA    . GLY B 1  217  ? -18.028 11.052  124.905 1.00 30.50 ? 215  GLY B CA    1 
ATOM   10381 C  C     . GLY B 1  217  ? -17.206 11.488  123.711 1.00 34.53 ? 215  GLY B C     1 
ATOM   10382 O  O     . GLY B 1  217  ? -17.194 10.774  122.702 1.00 34.57 ? 215  GLY B O     1 
ATOM   10383 N  N     . PHE B 1  218  ? -16.549 12.643  123.773 1.00 32.46 ? 216  PHE B N     1 
ATOM   10384 C  CA    . PHE B 1  218  ? -15.607 13.024  122.732 1.00 30.74 ? 216  PHE B CA    1 
ATOM   10385 C  C     . PHE B 1  218  ? -14.338 12.184  122.841 1.00 29.09 ? 216  PHE B C     1 
ATOM   10386 O  O     . PHE B 1  218  ? -14.057 11.567  123.871 1.00 29.71 ? 216  PHE B O     1 
ATOM   10387 C  CB    . PHE B 1  218  ? -15.238 14.506  122.838 1.00 32.04 ? 216  PHE B CB    1 
ATOM   10388 C  CG    . PHE B 1  218  ? -16.344 15.453  122.444 1.00 34.90 ? 216  PHE B CG    1 
ATOM   10389 C  CD1   . PHE B 1  218  ? -17.272 15.889  123.384 1.00 35.41 ? 216  PHE B CD1   1 
ATOM   10390 C  CD2   . PHE B 1  218  ? -16.435 15.932  121.146 1.00 32.96 ? 216  PHE B CD2   1 
ATOM   10391 C  CE1   . PHE B 1  218  ? -18.273 16.776  123.033 1.00 34.58 ? 216  PHE B CE1   1 
ATOM   10392 C  CE2   . PHE B 1  218  ? -17.442 16.815  120.786 1.00 35.86 ? 216  PHE B CE2   1 
ATOM   10393 C  CZ    . PHE B 1  218  ? -18.368 17.231  121.735 1.00 32.60 ? 216  PHE B CZ    1 
ATOM   10394 N  N     . SER B 1  219  ? -13.566 12.167  121.756 1.00 28.48 ? 217  SER B N     1 
ATOM   10395 C  CA    . SER B 1  219  ? -12.207 11.639  121.768 1.00 27.22 ? 217  SER B CA    1 
ATOM   10396 C  C     . SER B 1  219  ? -11.285 12.666  121.121 1.00 28.00 ? 217  SER B C     1 
ATOM   10397 O  O     . SER B 1  219  ? -11.717 13.748  120.708 1.00 30.03 ? 217  SER B O     1 
ATOM   10398 C  CB    . SER B 1  219  ? -12.116 10.282  121.061 1.00 24.61 ? 217  SER B CB    1 
ATOM   10399 O  OG    . SER B 1  219  ? -12.537 10.389  119.710 1.00 28.11 ? 217  SER B OG    1 
ATOM   10400 N  N     . TYR B 1  220  ? -9.997  12.336  121.035 1.00 24.09 ? 218  TYR B N     1 
ATOM   10401 C  CA    . TYR B 1  220  ? -9.019  13.319  120.607 1.00 23.59 ? 218  TYR B CA    1 
ATOM   10402 C  C     . TYR B 1  220  ? -8.003  12.707  119.660 1.00 21.84 ? 218  TYR B C     1 
ATOM   10403 O  O     . TYR B 1  220  ? -7.696  11.516  119.718 1.00 22.77 ? 218  TYR B O     1 
ATOM   10404 C  CB    . TYR B 1  220  ? -8.285  13.936  121.807 1.00 22.77 ? 218  TYR B CB    1 
ATOM   10405 C  CG    . TYR B 1  220  ? -9.062  15.049  122.451 1.00 24.94 ? 218  TYR B CG    1 
ATOM   10406 C  CD1   . TYR B 1  220  ? -10.026 14.780  123.415 1.00 27.52 ? 218  TYR B CD1   1 
ATOM   10407 C  CD2   . TYR B 1  220  ? -8.832  16.369  122.102 1.00 24.31 ? 218  TYR B CD2   1 
ATOM   10408 C  CE1   . TYR B 1  220  ? -10.750 15.800  124.006 1.00 26.16 ? 218  TYR B CE1   1 
ATOM   10409 C  CE2   . TYR B 1  220  ? -9.550  17.398  122.688 1.00 28.49 ? 218  TYR B CE2   1 
ATOM   10410 C  CZ    . TYR B 1  220  ? -10.510 17.101  123.640 1.00 25.84 ? 218  TYR B CZ    1 
ATOM   10411 O  OH    . TYR B 1  220  ? -11.226 18.115  124.229 1.00 31.75 ? 218  TYR B OH    1 
ATOM   10412 N  N     . SER B 1  221  ? -7.491  13.554  118.780 1.00 19.32 ? 219  SER B N     1 
ATOM   10413 C  CA    . SER B 1  221  ? -6.321  13.247  117.971 1.00 18.71 ? 219  SER B CA    1 
ATOM   10414 C  C     . SER B 1  221  ? -5.423  14.469  118.022 1.00 20.38 ? 219  SER B C     1 
ATOM   10415 O  O     . SER B 1  221  ? -5.846  15.557  117.624 1.00 23.53 ? 219  SER B O     1 
ATOM   10416 C  CB    . SER B 1  221  ? -6.711  12.923  116.529 1.00 20.67 ? 219  SER B CB    1 
ATOM   10417 O  OG    . SER B 1  221  ? -5.561  12.685  115.749 1.00 19.64 ? 219  SER B OG    1 
ATOM   10418 N  N     . TYR B 1  222  ? -4.192  14.300  118.504 1.00 20.75 ? 220  TYR B N     1 
ATOM   10419 C  CA    . TYR B 1  222  ? -3.307  15.427  118.757 1.00 19.62 ? 220  TYR B CA    1 
ATOM   10420 C  C     . TYR B 1  222  ? -2.387  15.690  117.579 1.00 20.25 ? 220  TYR B C     1 
ATOM   10421 O  O     . TYR B 1  222  ? -1.858  14.760  116.961 1.00 21.07 ? 220  TYR B O     1 
ATOM   10422 C  CB    . TYR B 1  222  ? -2.486  15.192  120.027 1.00 17.76 ? 220  TYR B CB    1 
ATOM   10423 C  CG    . TYR B 1  222  ? -3.397  15.077  121.207 1.00 21.00 ? 220  TYR B CG    1 
ATOM   10424 C  CD1   . TYR B 1  222  ? -3.952  16.208  121.778 1.00 21.99 ? 220  TYR B CD1   1 
ATOM   10425 C  CD2   . TYR B 1  222  ? -3.748  13.839  121.721 1.00 19.12 ? 220  TYR B CD2   1 
ATOM   10426 C  CE1   . TYR B 1  222  ? -4.821  16.119  122.836 1.00 22.32 ? 220  TYR B CE1   1 
ATOM   10427 C  CE2   . TYR B 1  222  ? -4.616  13.735  122.804 1.00 22.65 ? 220  TYR B CE2   1 
ATOM   10428 C  CZ    . TYR B 1  222  ? -5.146  14.883  123.351 1.00 24.19 ? 220  TYR B CZ    1 
ATOM   10429 O  OH    . TYR B 1  222  ? -6.021  14.800  124.406 1.00 23.79 ? 220  TYR B OH    1 
ATOM   10430 N  N     . ASP B 1  223  ? -2.187  16.978  117.308 1.00 19.97 ? 221  ASP B N     1 
ATOM   10431 C  CA    . ASP B 1  223  ? -1.396  17.497  116.203 1.00 22.27 ? 221  ASP B CA    1 
ATOM   10432 C  C     . ASP B 1  223  ? -0.315  18.380  116.811 1.00 24.61 ? 221  ASP B C     1 
ATOM   10433 O  O     . ASP B 1  223  ? -0.614  19.459  117.332 1.00 25.32 ? 221  ASP B O     1 
ATOM   10434 C  CB    . ASP B 1  223  ? -2.306  18.278  115.253 1.00 26.02 ? 221  ASP B CB    1 
ATOM   10435 C  CG    . ASP B 1  223  ? -1.560  19.221  114.319 1.00 29.71 ? 221  ASP B CG    1 
ATOM   10436 O  OD1   . ASP B 1  223  ? -0.400  18.951  113.958 1.00 29.34 ? 221  ASP B OD1   1 
ATOM   10437 O  OD2   . ASP B 1  223  ? -2.165  20.248  113.935 1.00 30.05 ? 221  ASP B OD2   1 
ATOM   10438 N  N     . MET B 1  224  ? 0.927   17.906  116.788 1.00 23.93 ? 222  MET B N     1 
ATOM   10439 C  CA    . MET B 1  224  ? 2.045   18.707  117.278 1.00 27.12 ? 222  MET B CA    1 
ATOM   10440 C  C     . MET B 1  224  ? 2.378   19.713  116.184 1.00 27.47 ? 222  MET B C     1 
ATOM   10441 O  O     . MET B 1  224  ? 3.008   19.377  115.181 1.00 30.08 ? 222  MET B O     1 
ATOM   10442 C  CB    . MET B 1  224  ? 3.239   17.828  117.648 1.00 27.02 ? 222  MET B CB    1 
ATOM   10443 C  CG    . MET B 1  224  ? 2.925   16.727  118.682 1.00 26.06 ? 222  MET B CG    1 
ATOM   10444 S  SD    . MET B 1  224  ? 2.038   17.261  120.175 1.00 32.04 ? 222  MET B SD    1 
ATOM   10445 C  CE    . MET B 1  224  ? 3.300   18.264  120.957 1.00 30.88 ? 222  MET B CE    1 
ATOM   10446 N  N     . LEU B 1  225  ? 1.939   20.952  116.392 1.00 28.38 ? 223  LEU B N     1 
ATOM   10447 C  CA    . LEU B 1  225  ? 2.025   21.995  115.376 1.00 31.22 ? 223  LEU B CA    1 
ATOM   10448 C  C     . LEU B 1  225  ? 3.465   22.274  114.966 1.00 35.95 ? 223  LEU B C     1 
ATOM   10449 O  O     . LEU B 1  225  ? 4.361   22.353  115.810 1.00 35.21 ? 223  LEU B O     1 
ATOM   10450 C  CB    . LEU B 1  225  ? 1.400   23.285  115.908 1.00 31.51 ? 223  LEU B CB    1 
ATOM   10451 C  CG    . LEU B 1  225  ? -0.110  23.289  116.124 1.00 32.70 ? 223  LEU B CG    1 
ATOM   10452 C  CD1   . LEU B 1  225  ? -0.520  24.532  116.902 1.00 34.93 ? 223  LEU B CD1   1 
ATOM   10453 C  CD2   . LEU B 1  225  ? -0.846  23.198  114.780 1.00 33.39 ? 223  LEU B CD2   1 
ATOM   10454 N  N     . GLY B 1  226  ? 3.672   22.457  113.661 1.00 35.97 ? 224  GLY B N     1 
ATOM   10455 C  CA    . GLY B 1  226  ? 4.969   22.834  113.129 1.00 42.33 ? 224  GLY B CA    1 
ATOM   10456 C  C     . GLY B 1  226  ? 4.974   23.036  111.623 1.00 46.24 ? 224  GLY B C     1 
ATOM   10457 O  O     . GLY B 1  226  ? 4.225   22.376  110.896 1.00 47.76 ? 224  GLY B O     1 
ATOM   10458 N  N     . GLU B 1  227  ? 5.812   23.949  111.139 1.00 44.71 ? 225  GLU B N     1 
ATOM   10459 C  CA    . GLU B 1  227  ? 5.974   24.111  109.702 1.00 42.97 ? 225  GLU B CA    1 
ATOM   10460 C  C     . GLU B 1  227  ? 6.571   22.843  109.090 1.00 41.58 ? 225  GLU B C     1 
ATOM   10461 O  O     . GLU B 1  227  ? 7.203   22.032  109.767 1.00 43.09 ? 225  GLU B O     1 
ATOM   10462 C  CB    . GLU B 1  227  ? 6.867   25.316  109.396 1.00 42.13 ? 225  GLU B CB    1 
ATOM   10463 N  N     . ALA B 1  228  ? 6.339   22.668  107.793 1.00 33.74 ? 226  ALA B N     1 
ATOM   10464 C  CA    . ALA B 1  228  ? 6.999   21.601  107.055 1.00 31.86 ? 226  ALA B CA    1 
ATOM   10465 C  C     . ALA B 1  228  ? 8.507   21.725  107.210 1.00 27.28 ? 226  ALA B C     1 
ATOM   10466 O  O     . ALA B 1  228  ? 9.049   22.831  107.268 1.00 28.74 ? 226  ALA B O     1 
ATOM   10467 C  CB    . ALA B 1  228  ? 6.625   21.671  105.579 1.00 25.94 ? 226  ALA B CB    1 
ATOM   10468 N  N     . ALA B 1  229  ? 9.191   20.585  107.273 1.00 20.76 ? 227  ALA B N     1 
ATOM   10469 C  CA    . ALA B 1  229  ? 10.633  20.616  107.491 1.00 20.58 ? 227  ALA B CA    1 
ATOM   10470 C  C     . ALA B 1  229  ? 11.346  21.284  106.320 1.00 18.74 ? 227  ALA B C     1 
ATOM   10471 O  O     . ALA B 1  229  ? 11.096  20.965  105.155 1.00 19.68 ? 227  ALA B O     1 
ATOM   10472 C  CB    . ALA B 1  229  ? 11.170  19.199  107.699 1.00 18.07 ? 227  ALA B CB    1 
ATOM   10473 N  N     . THR B 1  230  ? 12.211  22.239  106.640 1.00 18.36 ? 228  THR B N     1 
ATOM   10474 C  CA    . THR B 1  230  ? 13.096  22.862  105.665 1.00 20.55 ? 228  THR B CA    1 
ATOM   10475 C  C     . THR B 1  230  ? 14.487  22.255  105.681 1.00 19.80 ? 228  THR B C     1 
ATOM   10476 O  O     . THR B 1  230  ? 15.145  22.192  104.636 1.00 17.93 ? 228  THR B O     1 
ATOM   10477 C  CB    . THR B 1  230  ? 13.200  24.368  105.949 1.00 22.92 ? 228  THR B CB    1 
ATOM   10478 O  OG1   . THR B 1  230  ? 11.883  24.929  105.982 1.00 23.94 ? 228  THR B OG1   1 
ATOM   10479 C  CG2   . THR B 1  230  ? 14.031  25.083  104.885 1.00 19.04 ? 228  THR B CG2   1 
ATOM   10480 N  N     . THR B 1  231  ? 14.936  21.805  106.847 1.00 17.71 ? 229  THR B N     1 
ATOM   10481 C  CA    . THR B 1  231  ? 16.269  21.256  107.022 1.00 15.58 ? 229  THR B CA    1 
ATOM   10482 C  C     . THR B 1  231  ? 16.169  19.886  107.670 1.00 16.42 ? 229  THR B C     1 
ATOM   10483 O  O     . THR B 1  231  ? 15.135  19.504  108.223 1.00 15.95 ? 229  THR B O     1 
ATOM   10484 C  CB    . THR B 1  231  ? 17.146  22.146  107.909 1.00 17.04 ? 229  THR B CB    1 
ATOM   10485 O  OG1   . THR B 1  231  ? 16.664  22.077  109.263 1.00 19.87 ? 229  THR B OG1   1 
ATOM   10486 C  CG2   . THR B 1  231  ? 17.133  23.599  107.434 1.00 18.69 ? 229  THR B CG2   1 
ATOM   10487 N  N     . ALA B 1  232  ? 17.288  19.168  107.632 1.00 16.88 ? 230  ALA B N     1 
ATOM   10488 C  CA    . ALA B 1  232  ? 17.368  17.892  108.332 1.00 18.27 ? 230  ALA B CA    1 
ATOM   10489 C  C     . ALA B 1  232  ? 17.120  18.072  109.822 1.00 17.38 ? 230  ALA B C     1 
ATOM   10490 O  O     . ALA B 1  232  ? 16.482  17.225  110.457 1.00 17.80 ? 230  ALA B O     1 
ATOM   10491 C  CB    . ALA B 1  232  ? 18.738  17.254  108.087 1.00 17.73 ? 230  ALA B CB    1 
ATOM   10492 N  N     . ALA B 1  233  ? 17.644  19.159  110.406 1.00 17.32 ? 231  ALA B N     1 
ATOM   10493 C  CA    . ALA B 1  233  ? 17.446  19.407  111.830 1.00 18.93 ? 231  ALA B CA    1 
ATOM   10494 C  C     . ALA B 1  233  ? 15.972  19.613  112.156 1.00 19.26 ? 231  ALA B C     1 
ATOM   10495 O  O     . ALA B 1  233  ? 15.493  19.156  113.202 1.00 18.54 ? 231  ALA B O     1 
ATOM   10496 C  CB    . ALA B 1  233  ? 18.273  20.614  112.277 1.00 20.86 ? 231  ALA B CB    1 
ATOM   10497 N  N     . ASP B 1  234  ? 15.238  20.306  111.275 1.00 17.49 ? 232  ASP B N     1 
ATOM   10498 C  CA    . ASP B 1  234  ? 13.798  20.454  111.460 1.00 18.78 ? 232  ASP B CA    1 
ATOM   10499 C  C     . ASP B 1  234  ? 13.126  19.094  111.546 1.00 18.04 ? 232  ASP B C     1 
ATOM   10500 O  O     . ASP B 1  234  ? 12.321  18.834  112.450 1.00 18.62 ? 232  ASP B O     1 
ATOM   10501 C  CB    . ASP B 1  234  ? 13.173  21.214  110.287 1.00 19.75 ? 232  ASP B CB    1 
ATOM   10502 C  CG    . ASP B 1  234  ? 13.564  22.657  110.224 1.00 21.08 ? 232  ASP B CG    1 
ATOM   10503 O  OD1   . ASP B 1  234  ? 13.911  23.256  111.260 1.00 22.62 ? 232  ASP B OD1   1 
ATOM   10504 O  OD2   . ASP B 1  234  ? 13.459  23.198  109.106 1.00 21.16 ? 232  ASP B OD2   1 
ATOM   10505 N  N     . ALA B 1  235  ? 13.408  18.235  110.564 1.00 16.54 ? 233  ALA B N     1 
ATOM   10506 C  CA    . ALA B 1  235  ? 12.733  16.949  110.473 1.00 17.85 ? 233  ALA B CA    1 
ATOM   10507 C  C     . ALA B 1  235  ? 13.070  16.078  111.668 1.00 17.84 ? 233  ALA B C     1 
ATOM   10508 O  O     . ALA B 1  235  ? 12.202  15.389  112.215 1.00 18.08 ? 233  ALA B O     1 
ATOM   10509 C  CB    . ALA B 1  235  ? 13.111  16.247  109.164 1.00 18.52 ? 233  ALA B CB    1 
ATOM   10510 N  N     . GLU B 1  236  ? 14.333  16.098  112.092 1.00 17.54 ? 234  GLU B N     1 
ATOM   10511 C  CA    . GLU B 1  236  ? 14.720  15.309  113.248 1.00 18.16 ? 234  GLU B CA    1 
ATOM   10512 C  C     . GLU B 1  236  ? 14.006  15.794  114.498 1.00 18.22 ? 234  GLU B C     1 
ATOM   10513 O  O     . GLU B 1  236  ? 13.567  14.988  115.329 1.00 18.11 ? 234  GLU B O     1 
ATOM   10514 C  CB    . GLU B 1  236  ? 16.235  15.373  113.435 1.00 19.18 ? 234  GLU B CB    1 
ATOM   10515 C  CG    . GLU B 1  236  ? 16.725  14.372  114.449 1.00 21.93 ? 234  GLU B CG    1 
ATOM   10516 C  CD    . GLU B 1  236  ? 18.229  14.380  114.585 1.00 29.84 ? 234  GLU B CD    1 
ATOM   10517 O  OE1   . GLU B 1  236  ? 18.896  15.059  113.780 1.00 33.33 ? 234  GLU B OE1   1 
ATOM   10518 O  OE2   . GLU B 1  236  ? 18.735  13.709  115.500 1.00 29.22 ? 234  GLU B OE2   1 
ATOM   10519 N  N     . ARG B 1  237  ? 13.873  17.112  114.647 1.00 17.52 ? 235  ARG B N     1 
ATOM   10520 C  CA    . ARG B 1  237  ? 13.177  17.632  115.811 1.00 16.13 ? 235  ARG B CA    1 
ATOM   10521 C  C     . ARG B 1  237  ? 11.710  17.229  115.791 1.00 20.11 ? 235  ARG B C     1 
ATOM   10522 O  O     . ARG B 1  237  ? 11.172  16.777  116.808 1.00 18.36 ? 235  ARG B O     1 
ATOM   10523 C  CB    . ARG B 1  237  ? 13.313  19.149  115.880 1.00 20.14 ? 235  ARG B CB    1 
ATOM   10524 C  CG    . ARG B 1  237  ? 12.590  19.718  117.074 1.00 23.92 ? 235  ARG B CG    1 
ATOM   10525 C  CD    . ARG B 1  237  ? 12.258  21.185  116.939 1.00 28.72 ? 235  ARG B CD    1 
ATOM   10526 N  NE    . ARG B 1  237  ? 11.560  21.626  118.141 1.00 29.21 ? 235  ARG B NE    1 
ATOM   10527 C  CZ    . ARG B 1  237  ? 11.570  22.868  118.605 1.00 30.37 ? 235  ARG B CZ    1 
ATOM   10528 N  NH1   . ARG B 1  237  ? 12.228  23.832  117.981 1.00 32.54 ? 235  ARG B NH1   1 
ATOM   10529 N  NH2   . ARG B 1  237  ? 10.913  23.144  119.729 1.00 29.40 ? 235  ARG B NH2   1 
ATOM   10530 N  N     . TYR B 1  238  ? 11.048  17.381  114.637 1.00 18.52 ? 236  TYR B N     1 
ATOM   10531 C  CA    . TYR B 1  238  ? 9.635   17.006  114.555 1.00 17.91 ? 236  TYR B CA    1 
ATOM   10532 C  C     . TYR B 1  238  ? 9.455   15.528  114.861 1.00 18.05 ? 236  TYR B C     1 
ATOM   10533 O  O     . TYR B 1  238  ? 8.484   15.135  115.524 1.00 18.12 ? 236  TYR B O     1 
ATOM   10534 C  CB    . TYR B 1  238  ? 9.058   17.342  113.171 1.00 17.46 ? 236  TYR B CB    1 
ATOM   10535 C  CG    . TYR B 1  238  ? 8.995   18.829  112.892 1.00 24.51 ? 236  TYR B CG    1 
ATOM   10536 C  CD1   . TYR B 1  238  ? 8.764   19.737  113.914 1.00 34.00 ? 236  TYR B CD1   1 
ATOM   10537 C  CD2   . TYR B 1  238  ? 9.215   19.324  111.620 1.00 26.75 ? 236  TYR B CD2   1 
ATOM   10538 C  CE1   . TYR B 1  238  ? 8.734   21.103  113.669 1.00 37.78 ? 236  TYR B CE1   1 
ATOM   10539 C  CE2   . TYR B 1  238  ? 9.191   20.676  111.363 1.00 30.39 ? 236  TYR B CE2   1 
ATOM   10540 C  CZ    . TYR B 1  238  ? 8.945   21.565  112.387 1.00 38.74 ? 236  TYR B CZ    1 
ATOM   10541 O  OH    . TYR B 1  238  ? 8.918   22.921  112.130 1.00 40.16 ? 236  TYR B OH    1 
ATOM   10542 N  N     . TYR B 1  239  ? 10.381  14.692  114.390 1.00 17.02 ? 237  TYR B N     1 
ATOM   10543 C  CA    . TYR B 1  239  ? 10.328  13.275  114.730 1.00 17.14 ? 237  TYR B CA    1 
ATOM   10544 C  C     . TYR B 1  239  ? 10.357  13.081  116.238 1.00 18.14 ? 237  TYR B C     1 
ATOM   10545 O  O     . TYR B 1  239  ? 9.507   12.379  116.809 1.00 18.13 ? 237  TYR B O     1 
ATOM   10546 C  CB    . TYR B 1  239  ? 11.493  12.517  114.082 1.00 18.28 ? 237  TYR B CB    1 
ATOM   10547 C  CG    . TYR B 1  239  ? 11.529  11.071  114.532 1.00 20.23 ? 237  TYR B CG    1 
ATOM   10548 C  CD1   . TYR B 1  239  ? 10.809  10.108  113.863 1.00 21.01 ? 237  TYR B CD1   1 
ATOM   10549 C  CD2   . TYR B 1  239  ? 12.235  10.685  115.667 1.00 23.00 ? 237  TYR B CD2   1 
ATOM   10550 C  CE1   . TYR B 1  239  ? 10.806  8.798   114.282 1.00 18.60 ? 237  TYR B CE1   1 
ATOM   10551 C  CE2   . TYR B 1  239  ? 12.226  9.364   116.102 1.00 23.37 ? 237  TYR B CE2   1 
ATOM   10552 C  CZ    . TYR B 1  239  ? 11.518  8.428   115.388 1.00 23.55 ? 237  TYR B CZ    1 
ATOM   10553 O  OH    . TYR B 1  239  ? 11.507  7.116   115.794 1.00 29.17 ? 237  TYR B OH    1 
ATOM   10554 N  N     . ARG B 1  240  ? 11.348  13.686  116.901 1.00 18.94 ? 238  ARG B N     1 
ATOM   10555 C  CA    . ARG B 1  240  ? 11.480  13.527  118.340 1.00 20.43 ? 238  ARG B CA    1 
ATOM   10556 C  C     . ARG B 1  240  ? 10.268  14.082  119.067 1.00 20.25 ? 238  ARG B C     1 
ATOM   10557 O  O     . ARG B 1  240  ? 9.851   13.539  120.093 1.00 18.77 ? 238  ARG B O     1 
ATOM   10558 C  CB    . ARG B 1  240  ? 12.760  14.212  118.829 1.00 19.93 ? 238  ARG B CB    1 
ATOM   10559 C  CG    . ARG B 1  240  ? 14.016  13.577  118.282 1.00 21.49 ? 238  ARG B CG    1 
ATOM   10560 C  CD    . ARG B 1  240  ? 14.127  12.120  118.712 1.00 24.36 ? 238  ARG B CD    1 
ATOM   10561 N  NE    . ARG B 1  240  ? 15.287  11.473  118.109 1.00 24.61 ? 238  ARG B NE    1 
ATOM   10562 C  CZ    . ARG B 1  240  ? 15.546  10.174  118.184 1.00 31.61 ? 238  ARG B CZ    1 
ATOM   10563 N  NH1   . ARG B 1  240  ? 14.721  9.338   118.795 1.00 28.71 ? 238  ARG B NH1   1 
ATOM   10564 N  NH2   . ARG B 1  240  ? 16.669  9.704   117.645 1.00 30.81 ? 238  ARG B NH2   1 
ATOM   10565 N  N     . ASP B 1  241  ? 9.699   15.173  118.554 1.00 18.25 ? 239  ASP B N     1 
ATOM   10566 C  CA    . ASP B 1  241  ? 8.510   15.745  119.175 1.00 20.78 ? 239  ASP B CA    1 
ATOM   10567 C  C     . ASP B 1  241  ? 7.302   14.825  119.013 1.00 19.90 ? 239  ASP B C     1 
ATOM   10568 O  O     . ASP B 1  241  ? 6.512   14.664  119.951 1.00 18.95 ? 239  ASP B O     1 
ATOM   10569 C  CB    . ASP B 1  241  ? 8.221   17.128  118.589 1.00 21.73 ? 239  ASP B CB    1 
ATOM   10570 C  CG    . ASP B 1  241  ? 9.193   18.199  119.094 1.00 25.38 ? 239  ASP B CG    1 
ATOM   10571 O  OD1   . ASP B 1  241  ? 9.879   17.968  120.116 1.00 23.69 ? 239  ASP B OD1   1 
ATOM   10572 O  OD2   . ASP B 1  241  ? 9.259   19.270  118.464 1.00 31.13 ? 239  ASP B OD2   1 
ATOM   10573 N  N     . TYR B 1  242  ? 7.142   14.202  117.841 1.00 19.89 ? 240  TYR B N     1 
ATOM   10574 C  CA    . TYR B 1  242  ? 6.070   13.218  117.690 1.00 20.79 ? 240  TYR B CA    1 
ATOM   10575 C  C     . TYR B 1  242  ? 6.300   12.022  118.598 1.00 20.92 ? 240  TYR B C     1 
ATOM   10576 O  O     . TYR B 1  242  ? 5.360   11.506  119.216 1.00 18.09 ? 240  TYR B O     1 
ATOM   10577 C  CB    . TYR B 1  242  ? 5.986   12.733  116.248 1.00 19.15 ? 240  TYR B CB    1 
ATOM   10578 C  CG    . TYR B 1  242  ? 5.319   13.656  115.243 1.00 18.94 ? 240  TYR B CG    1 
ATOM   10579 C  CD1   . TYR B 1  242  ? 4.166   14.365  115.557 1.00 22.70 ? 240  TYR B CD1   1 
ATOM   10580 C  CD2   . TYR B 1  242  ? 5.833   13.780  113.966 1.00 20.68 ? 240  TYR B CD2   1 
ATOM   10581 C  CE1   . TYR B 1  242  ? 3.550   15.190  114.610 1.00 24.62 ? 240  TYR B CE1   1 
ATOM   10582 C  CE2   . TYR B 1  242  ? 5.229   14.593  113.022 1.00 23.16 ? 240  TYR B CE2   1 
ATOM   10583 C  CZ    . TYR B 1  242  ? 4.089   15.295  113.350 1.00 24.29 ? 240  TYR B CZ    1 
ATOM   10584 O  OH    . TYR B 1  242  ? 3.486   16.103  112.401 1.00 23.63 ? 240  TYR B OH    1 
ATOM   10585 N  N     . GLU B 1  243  ? 7.549   11.551  118.660 1.00 21.24 ? 241  GLU B N     1 
ATOM   10586 C  CA    . GLU B 1  243  ? 7.890   10.418  119.508 1.00 18.53 ? 241  GLU B CA    1 
ATOM   10587 C  C     . GLU B 1  243  ? 7.533   10.705  120.956 1.00 20.48 ? 241  GLU B C     1 
ATOM   10588 O  O     . GLU B 1  243  ? 6.914   9.883   121.638 1.00 18.57 ? 241  GLU B O     1 
ATOM   10589 C  CB    . GLU B 1  243  ? 9.382   10.120  119.370 1.00 19.38 ? 241  GLU B CB    1 
ATOM   10590 C  CG    . GLU B 1  243  ? 9.876   8.987   120.241 1.00 22.56 ? 241  GLU B CG    1 
ATOM   10591 C  CD    . GLU B 1  243  ? 11.388  8.852   120.196 1.00 27.66 ? 241  GLU B CD    1 
ATOM   10592 O  OE1   . GLU B 1  243  ? 12.076  9.885   120.113 1.00 27.50 ? 241  GLU B OE1   1 
ATOM   10593 O  OE2   . GLU B 1  243  ? 11.883  7.711   120.236 1.00 30.36 ? 241  GLU B OE2   1 
ATOM   10594 N  N     . SER B 1  244  ? 7.932   11.878  121.445 1.00 20.34 ? 242  SER B N     1 
ATOM   10595 C  CA    A SER B 1  244  ? 7.615   12.258  122.814 0.67 20.06 ? 242  SER B CA    1 
ATOM   10596 C  CA    B SER B 1  244  ? 7.611   12.247  122.819 0.33 20.08 ? 242  SER B CA    1 
ATOM   10597 C  C     . SER B 1  244  ? 6.107   12.344  123.022 1.00 19.43 ? 242  SER B C     1 
ATOM   10598 O  O     . SER B 1  244  ? 5.587   11.917  124.057 1.00 19.20 ? 242  SER B O     1 
ATOM   10599 C  CB    A SER B 1  244  ? 8.294   13.591  123.133 0.67 20.14 ? 242  SER B CB    1 
ATOM   10600 C  CB    B SER B 1  244  ? 8.286   13.569  123.183 0.33 20.20 ? 242  SER B CB    1 
ATOM   10601 O  OG    A SER B 1  244  ? 7.980   14.038  124.430 0.67 22.77 ? 242  SER B OG    1 
ATOM   10602 O  OG    B SER B 1  244  ? 9.679   13.393  123.345 0.33 21.61 ? 242  SER B OG    1 
ATOM   10603 N  N     . ALA B 1  245  ? 5.393   12.894  122.039 1.00 19.04 ? 243  ALA B N     1 
ATOM   10604 C  CA    . ALA B 1  245  ? 3.944   13.002  122.160 1.00 20.97 ? 243  ALA B CA    1 
ATOM   10605 C  C     . ALA B 1  245  ? 3.289   11.629  122.222 1.00 20.09 ? 243  ALA B C     1 
ATOM   10606 O  O     . ALA B 1  245  ? 2.338   11.420  122.983 1.00 20.81 ? 243  ALA B O     1 
ATOM   10607 C  CB    . ALA B 1  245  ? 3.378   13.802  120.991 1.00 21.15 ? 243  ALA B CB    1 
ATOM   10608 N  N     . ILE B 1  246  ? 3.779   10.678  121.429 1.00 19.24 ? 244  ILE B N     1 
ATOM   10609 C  CA    . ILE B 1  246  ? 3.166   9.351   121.427 1.00 20.36 ? 244  ILE B CA    1 
ATOM   10610 C  C     . ILE B 1  246  ? 3.308   8.694   122.790 1.00 20.95 ? 244  ILE B C     1 
ATOM   10611 O  O     . ILE B 1  246  ? 2.358   8.086   123.301 1.00 21.74 ? 244  ILE B O     1 
ATOM   10612 C  CB    . ILE B 1  246  ? 3.765   8.484   120.308 1.00 18.05 ? 244  ILE B CB    1 
ATOM   10613 C  CG1   . ILE B 1  246  ? 3.270   8.991   118.955 1.00 21.01 ? 244  ILE B CG1   1 
ATOM   10614 C  CG2   . ILE B 1  246  ? 3.395   7.016   120.540 1.00 19.45 ? 244  ILE B CG2   1 
ATOM   10615 C  CD1   . ILE B 1  246  ? 4.002   8.389   117.764 1.00 21.68 ? 244  ILE B CD1   1 
ATOM   10616 N  N     . HIS B 1  247  ? 4.487   8.813   123.412 1.00 19.88 ? 245  HIS B N     1 
ATOM   10617 C  CA    . HIS B 1  247  ? 4.643   8.280   124.759 1.00 19.17 ? 245  HIS B CA    1 
ATOM   10618 C  C     . HIS B 1  247  ? 3.635   8.905   125.714 1.00 20.33 ? 245  HIS B C     1 
ATOM   10619 O  O     . HIS B 1  247  ? 3.005   8.200   126.508 1.00 21.90 ? 245  HIS B O     1 
ATOM   10620 C  CB    . HIS B 1  247  ? 6.070   8.507   125.263 1.00 20.15 ? 245  HIS B CB    1 
ATOM   10621 C  CG    . HIS B 1  247  ? 7.070   7.568   124.669 1.00 21.38 ? 245  HIS B CG    1 
ATOM   10622 N  ND1   . HIS B 1  247  ? 7.031   6.209   124.889 1.00 21.98 ? 245  HIS B ND1   1 
ATOM   10623 C  CD2   . HIS B 1  247  ? 8.146   7.792   123.878 1.00 23.16 ? 245  HIS B CD2   1 
ATOM   10624 C  CE1   . HIS B 1  247  ? 8.031   5.632   124.248 1.00 25.73 ? 245  HIS B CE1   1 
ATOM   10625 N  NE2   . HIS B 1  247  ? 8.721   6.571   123.624 1.00 25.16 ? 245  HIS B NE2   1 
ATOM   10626 N  N     . ALA B 1  248  ? 3.455   10.228  125.642 1.00 19.17 ? 246  ALA B N     1 
ATOM   10627 C  CA    . ALA B 1  248  ? 2.510   10.880  126.544 1.00 21.21 ? 246  ALA B CA    1 
ATOM   10628 C  C     . ALA B 1  248  ? 1.078   10.468  126.226 1.00 19.73 ? 246  ALA B C     1 
ATOM   10629 O  O     . ALA B 1  248  ? 0.302   10.126  127.130 1.00 22.34 ? 246  ALA B O     1 
ATOM   10630 C  CB    . ALA B 1  248  ? 2.665   12.398  126.465 1.00 21.61 ? 246  ALA B CB    1 
ATOM   10631 N  N     . ILE B 1  249  ? 0.714   10.490  124.938 1.00 21.23 ? 247  ILE B N     1 
ATOM   10632 C  CA    . ILE B 1  249  ? -0.650  10.134  124.550 1.00 20.15 ? 247  ILE B CA    1 
ATOM   10633 C  C     . ILE B 1  249  ? -0.927  8.670   124.859 1.00 22.39 ? 247  ILE B C     1 
ATOM   10634 O  O     . ILE B 1  249  ? -2.016  8.313   125.330 1.00 22.88 ? 247  ILE B O     1 
ATOM   10635 C  CB    . ILE B 1  249  ? -0.879  10.448  123.063 1.00 20.54 ? 247  ILE B CB    1 
ATOM   10636 C  CG1   . ILE B 1  249  ? -0.755  11.946  122.806 1.00 22.12 ? 247  ILE B CG1   1 
ATOM   10637 C  CG2   . ILE B 1  249  ? -2.264  9.924   122.608 1.00 21.29 ? 247  ILE B CG2   1 
ATOM   10638 C  CD1   . ILE B 1  249  ? -0.476  12.301  121.355 1.00 21.45 ? 247  ILE B CD1   1 
ATOM   10639 N  N     . GLY B 1  250  ? 0.055   7.803   124.603 1.00 20.83 ? 248  GLY B N     1 
ATOM   10640 C  CA    . GLY B 1  250  ? -0.129  6.387   124.870 1.00 22.21 ? 248  GLY B CA    1 
ATOM   10641 C  C     . GLY B 1  250  ? -0.326  6.085   126.342 1.00 25.81 ? 248  GLY B C     1 
ATOM   10642 O  O     . GLY B 1  250  ? -1.197  5.292   126.714 1.00 25.64 ? 248  GLY B O     1 
ATOM   10643 N  N     . LYS B 1  251  ? 0.478   6.707   127.205 1.00 24.15 ? 249  LYS B N     1 
ATOM   10644 C  CA    . LYS B 1  251  ? 0.304   6.480   128.633 1.00 25.10 ? 249  LYS B CA    1 
ATOM   10645 C  C     . LYS B 1  251  ? -1.034  7.030   129.114 1.00 24.66 ? 249  LYS B C     1 
ATOM   10646 O  O     . LYS B 1  251  ? -1.715  6.389   129.923 1.00 25.75 ? 249  LYS B O     1 
ATOM   10647 C  CB    . LYS B 1  251  ? 1.466   7.101   129.416 1.00 27.04 ? 249  LYS B CB    1 
ATOM   10648 N  N     . ALA B 1  252  ? -1.438  8.197   128.607 1.00 23.36 ? 250  ALA B N     1 
ATOM   10649 C  CA    . ALA B 1  252  ? -2.744  8.748   128.971 1.00 25.47 ? 250  ALA B CA    1 
ATOM   10650 C  C     . ALA B 1  252  ? -3.882  7.869   128.463 1.00 26.02 ? 250  ALA B C     1 
ATOM   10651 O  O     . ALA B 1  252  ? -4.914  7.733   129.132 1.00 26.76 ? 250  ALA B O     1 
ATOM   10652 C  CB    . ALA B 1  252  ? -2.892  10.169  128.424 1.00 27.39 ? 250  ALA B CB    1 
ATOM   10653 N  N     . SER B 1  253  ? -3.719  7.278   127.277 1.00 24.75 ? 251  SER B N     1 
ATOM   10654 C  CA    . SER B 1  253  ? -4.734  6.362   126.762 1.00 26.35 ? 251  SER B CA    1 
ATOM   10655 C  C     . SER B 1  253  ? -5.009  5.235   127.751 1.00 26.60 ? 251  SER B C     1 
ATOM   10656 O  O     . SER B 1  253  ? -6.169  4.894   128.013 1.00 30.94 ? 251  SER B O     1 
ATOM   10657 C  CB    . SER B 1  253  ? -4.297  5.789   125.419 1.00 26.91 ? 251  SER B CB    1 
ATOM   10658 O  OG    . SER B 1  253  ? -5.276  4.879   124.942 1.00 25.37 ? 251  SER B OG    1 
ATOM   10659 N  N     . ALA B 1  254  ? -3.949  4.638   128.301 1.00 25.58 ? 252  ALA B N     1 
ATOM   10660 C  CA    . ALA B 1  254  ? -4.045  3.636   129.363 1.00 29.69 ? 252  ALA B CA    1 
ATOM   10661 C  C     . ALA B 1  254  ? -4.965  2.482   128.969 1.00 32.58 ? 252  ALA B C     1 
ATOM   10662 O  O     . ALA B 1  254  ? -5.810  2.031   129.743 1.00 32.07 ? 252  ALA B O     1 
ATOM   10663 C  CB    . ALA B 1  254  ? -4.496  4.272   130.680 1.00 31.65 ? 252  ALA B CB    1 
ATOM   10664 N  N     . GLY B 1  255  ? -4.796  2.009   127.740 1.00 31.64 ? 253  GLY B N     1 
ATOM   10665 C  CA    . GLY B 1  255  ? -5.524  0.851   127.266 1.00 33.66 ? 253  GLY B CA    1 
ATOM   10666 C  C     . GLY B 1  255  ? -6.937  1.110   126.795 1.00 31.55 ? 253  GLY B C     1 
ATOM   10667 O  O     . GLY B 1  255  ? -7.679  0.147   126.569 1.00 34.52 ? 253  GLY B O     1 
ATOM   10668 N  N     . ARG B 1  256  ? -7.347  2.368   126.648 1.00 29.87 ? 254  ARG B N     1 
ATOM   10669 C  CA    . ARG B 1  256  ? -8.700  2.633   126.173 1.00 30.04 ? 254  ARG B CA    1 
ATOM   10670 C  C     . ARG B 1  256  ? -8.909  2.233   124.720 1.00 31.33 ? 254  ARG B C     1 
ATOM   10671 O  O     . ARG B 1  256  ? -10.059 2.191   124.269 1.00 32.19 ? 254  ARG B O     1 
ATOM   10672 C  CB    . ARG B 1  256  ? -9.049  4.106   126.363 1.00 29.12 ? 254  ARG B CB    1 
ATOM   10673 C  CG    . ARG B 1  256  ? -9.443  4.444   127.799 1.00 31.76 ? 254  ARG B CG    1 
ATOM   10674 C  CD    . ARG B 1  256  ? -9.758  5.914   127.937 1.00 32.21 ? 254  ARG B CD    1 
ATOM   10675 N  NE    . ARG B 1  256  ? -8.542  6.718   127.952 1.00 30.21 ? 254  ARG B NE    1 
ATOM   10676 C  CZ    . ARG B 1  256  ? -8.507  8.027   127.756 1.00 29.14 ? 254  ARG B CZ    1 
ATOM   10677 N  NH1   . ARG B 1  256  ? -9.606  8.714   127.478 1.00 27.03 ? 254  ARG B NH1   1 
ATOM   10678 N  NH2   . ARG B 1  256  ? -7.340  8.665   127.843 1.00 29.61 ? 254  ARG B NH2   1 
ATOM   10679 N  N     . GLY B 1  257  ? -7.843  1.931   123.982 1.00 30.16 ? 255  GLY B N     1 
ATOM   10680 C  CA    . GLY B 1  257  ? -7.985  1.493   122.609 1.00 29.43 ? 255  GLY B CA    1 
ATOM   10681 C  C     . GLY B 1  257  ? -8.119  2.654   121.648 1.00 28.16 ? 255  GLY B C     1 
ATOM   10682 O  O     . GLY B 1  257  ? -8.142  3.828   122.019 1.00 27.93 ? 255  GLY B O     1 
ATOM   10683 N  N     . ILE B 1  258  ? -8.229  2.308   120.365 1.00 29.25 ? 256  ILE B N     1 
ATOM   10684 C  CA    . ILE B 1  258  ? -8.122  3.326   119.321 1.00 27.41 ? 256  ILE B CA    1 
ATOM   10685 C  C     . ILE B 1  258  ? -9.402  4.113   119.095 1.00 25.04 ? 256  ILE B C     1 
ATOM   10686 O  O     . ILE B 1  258  ? -9.353  5.159   118.435 1.00 25.63 ? 256  ILE B O     1 
ATOM   10687 C  CB    . ILE B 1  258  ? -7.671  2.672   118.004 1.00 29.94 ? 256  ILE B CB    1 
ATOM   10688 C  CG1   . ILE B 1  258  ? -8.709  1.658   117.526 1.00 30.77 ? 256  ILE B CG1   1 
ATOM   10689 C  CG2   . ILE B 1  258  ? -6.330  1.979   118.199 1.00 26.77 ? 256  ILE B CG2   1 
ATOM   10690 C  CD1   . ILE B 1  258  ? -8.388  1.074   116.163 1.00 33.17 ? 256  ILE B CD1   1 
ATOM   10691 N  N     . TYR B 1  259  ? -10.544 3.652   119.618 1.00 27.32 ? 257  TYR B N     1 
ATOM   10692 C  CA    . TYR B 1  259  ? -11.803 4.369   119.412 1.00 28.54 ? 257  TYR B CA    1 
ATOM   10693 C  C     . TYR B 1  259  ? -12.113 5.300   120.580 1.00 26.08 ? 257  TYR B C     1 
ATOM   10694 O  O     . TYR B 1  259  ? -12.313 6.503   120.383 1.00 28.26 ? 257  TYR B O     1 
ATOM   10695 C  CB    . TYR B 1  259  ? -12.948 3.372   119.176 1.00 28.56 ? 257  TYR B CB    1 
ATOM   10696 C  CG    . TYR B 1  259  ? -12.624 2.411   118.058 1.00 29.72 ? 257  TYR B CG    1 
ATOM   10697 C  CD1   . TYR B 1  259  ? -12.528 2.856   116.746 1.00 30.51 ? 257  TYR B CD1   1 
ATOM   10698 C  CD2   . TYR B 1  259  ? -12.380 1.068   118.314 1.00 32.35 ? 257  TYR B CD2   1 
ATOM   10699 C  CE1   . TYR B 1  259  ? -12.208 1.992   115.719 1.00 33.57 ? 257  TYR B CE1   1 
ATOM   10700 C  CE2   . TYR B 1  259  ? -12.060 0.192   117.288 1.00 31.80 ? 257  TYR B CE2   1 
ATOM   10701 C  CZ    . TYR B 1  259  ? -11.974 0.664   115.993 1.00 33.82 ? 257  TYR B CZ    1 
ATOM   10702 O  OH    . TYR B 1  259  ? -11.656 -0.196  114.962 1.00 35.98 ? 257  TYR B OH    1 
ATOM   10703 N  N     . GLU B 1  260  ? -12.158 4.757   121.799 1.00 27.58 ? 258  GLU B N     1 
ATOM   10704 C  CA    . GLU B 1  260  ? -12.395 5.602   122.964 1.00 29.78 ? 258  GLU B CA    1 
ATOM   10705 C  C     . GLU B 1  260  ? -11.193 6.490   123.251 1.00 30.80 ? 258  GLU B C     1 
ATOM   10706 O  O     . GLU B 1  260  ? -11.348 7.681   123.554 1.00 31.95 ? 258  GLU B O     1 
ATOM   10707 C  CB    . GLU B 1  260  ? -12.722 4.742   124.183 1.00 31.74 ? 258  GLU B CB    1 
ATOM   10708 C  CG    . GLU B 1  260  ? -12.953 5.557   125.440 1.00 36.78 ? 258  GLU B CG    1 
ATOM   10709 C  CD    . GLU B 1  260  ? -13.212 4.700   126.664 1.00 39.89 ? 258  GLU B CD    1 
ATOM   10710 O  OE1   . GLU B 1  260  ? -13.359 3.463   126.516 1.00 42.54 ? 258  GLU B OE1   1 
ATOM   10711 O  OE2   . GLU B 1  260  ? -13.270 5.267   127.777 1.00 43.02 ? 258  GLU B OE2   1 
ATOM   10712 N  N     . GLY B 1  261  ? -9.996  5.932   123.146 1.00 27.66 ? 259  GLY B N     1 
ATOM   10713 C  CA    . GLY B 1  261  ? -8.796  6.614   123.566 1.00 26.51 ? 259  GLY B CA    1 
ATOM   10714 C  C     . GLY B 1  261  ? -8.259  7.551   122.510 1.00 27.27 ? 259  GLY B C     1 
ATOM   10715 O  O     . GLY B 1  261  ? -8.646  7.523   121.334 1.00 26.19 ? 259  GLY B O     1 
ATOM   10716 N  N     . PRO B 1  262  ? -7.325  8.398   122.929 1.00 24.58 ? 260  PRO B N     1 
ATOM   10717 C  CA    . PRO B 1  262  ? -6.761  9.405   122.028 1.00 25.20 ? 260  PRO B CA    1 
ATOM   10718 C  C     . PRO B 1  262  ? -5.784  8.806   121.027 1.00 24.91 ? 260  PRO B C     1 
ATOM   10719 O  O     . PRO B 1  262  ? -5.237  7.717   121.211 1.00 26.03 ? 260  PRO B O     1 
ATOM   10720 C  CB    . PRO B 1  262  ? -6.036  10.357  122.990 1.00 25.28 ? 260  PRO B CB    1 
ATOM   10721 C  CG    . PRO B 1  262  ? -5.630  9.471   124.127 1.00 24.53 ? 260  PRO B CG    1 
ATOM   10722 C  CD    . PRO B 1  262  ? -6.779  8.504   124.293 1.00 25.93 ? 260  PRO B CD    1 
ATOM   10723 N  N     . GLY B 1  263  ? -5.565  9.564   119.953 1.00 22.17 ? 261  GLY B N     1 
ATOM   10724 C  CA    . GLY B 1  263  ? -4.593  9.211   118.942 1.00 21.54 ? 261  GLY B CA    1 
ATOM   10725 C  C     . GLY B 1  263  ? -3.699  10.394  118.609 1.00 22.64 ? 261  GLY B C     1 
ATOM   10726 O  O     . GLY B 1  263  ? -3.804  11.473  119.203 1.00 21.56 ? 261  GLY B O     1 
ATOM   10727 N  N     . ILE B 1  264  ? -2.831  10.169  117.635 1.00 21.06 ? 262  ILE B N     1 
ATOM   10728 C  CA    . ILE B 1  264  ? -1.945  11.214  117.146 1.00 20.62 ? 262  ILE B CA    1 
ATOM   10729 C  C     . ILE B 1  264  ? -2.096  11.305  115.637 1.00 20.68 ? 262  ILE B C     1 
ATOM   10730 O  O     . ILE B 1  264  ? -2.470  10.335  114.968 1.00 21.03 ? 262  ILE B O     1 
ATOM   10731 C  CB    . ILE B 1  264  ? -0.474  10.957  117.563 1.00 22.77 ? 262  ILE B CB    1 
ATOM   10732 C  CG1   . ILE B 1  264  ? 0.334   12.254  117.474 1.00 21.62 ? 262  ILE B CG1   1 
ATOM   10733 C  CG2   . ILE B 1  264  ? 0.145   9.864   116.714 1.00 23.30 ? 262  ILE B CG2   1 
ATOM   10734 C  CD1   . ILE B 1  264  ? 1.787   12.120  117.902 1.00 24.17 ? 262  ILE B CD1   1 
ATOM   10735 N  N     . SER B 1  265  ? -1.868  12.503  115.112 1.00 17.42 ? 263  SER B N     1 
ATOM   10736 C  CA    . SER B 1  265  ? -1.867  12.777  113.684 1.00 18.98 ? 263  SER B CA    1 
ATOM   10737 C  C     . SER B 1  265  ? -0.507  13.346  113.307 1.00 19.19 ? 263  SER B C     1 
ATOM   10738 O  O     . SER B 1  265  ? 0.082   14.122  114.066 1.00 21.82 ? 263  SER B O     1 
ATOM   10739 C  CB    . SER B 1  265  ? -2.976  13.759  113.295 1.00 22.38 ? 263  SER B CB    1 
ATOM   10740 O  OG    . SER B 1  265  ? -4.265  13.148  113.355 1.00 22.91 ? 263  SER B OG    1 
ATOM   10741 N  N     . ILE B 1  266  ? -0.001  12.944  112.150 1.00 18.60 ? 264  ILE B N     1 
ATOM   10742 C  CA    . ILE B 1  266  ? 1.310   13.390  111.704 1.00 18.39 ? 264  ILE B CA    1 
ATOM   10743 C  C     . ILE B 1  266  ? 1.217   13.892  110.273 1.00 20.00 ? 264  ILE B C     1 
ATOM   10744 O  O     . ILE B 1  266  ? 0.402   13.424  109.473 1.00 18.31 ? 264  ILE B O     1 
ATOM   10745 C  CB    . ILE B 1  266  ? 2.365   12.267  111.828 1.00 21.84 ? 264  ILE B CB    1 
ATOM   10746 C  CG1   . ILE B 1  266  ? 2.029   11.085  110.921 1.00 22.19 ? 264  ILE B CG1   1 
ATOM   10747 C  CG2   . ILE B 1  266  ? 2.486   11.808  113.278 1.00 22.12 ? 264  ILE B CG2   1 
ATOM   10748 C  CD1   . ILE B 1  266  ? 3.181   10.099  110.747 1.00 23.71 ? 264  ILE B CD1   1 
ATOM   10749 N  N     . LYS B 1  267  ? 2.057   14.860  109.948 1.00 20.52 ? 265  LYS B N     1 
ATOM   10750 C  CA    . LYS B 1  267  ? 2.184   15.332  108.576 1.00 17.12 ? 265  LYS B CA    1 
ATOM   10751 C  C     . LYS B 1  267  ? 3.536   14.869  108.060 1.00 17.01 ? 265  LYS B C     1 
ATOM   10752 O  O     . LYS B 1  267  ? 4.568   15.171  108.669 1.00 17.85 ? 265  LYS B O     1 
ATOM   10753 C  CB    . LYS B 1  267  ? 2.025   16.851  108.498 1.00 22.96 ? 265  LYS B CB    1 
ATOM   10754 C  CG    . LYS B 1  267  ? 0.559   17.280  108.704 1.00 25.09 ? 265  LYS B CG    1 
ATOM   10755 C  CD    . LYS B 1  267  ? 0.373   18.780  108.744 1.00 29.10 ? 265  LYS B CD    1 
ATOM   10756 C  CE    . LYS B 1  267  ? -0.892  19.144  109.503 1.00 25.20 ? 265  LYS B CE    1 
ATOM   10757 N  NZ    . LYS B 1  267  ? -2.096  18.564  108.859 1.00 22.04 ? 265  LYS B NZ    1 
ATOM   10758 N  N     . LEU B 1  268  ? 3.523   14.085  106.975 1.00 16.15 ? 266  LEU B N     1 
ATOM   10759 C  CA    . LEU B 1  268  ? 4.771   13.523  106.475 1.00 17.02 ? 266  LEU B CA    1 
ATOM   10760 C  C     . LEU B 1  268  ? 5.761   14.614  106.084 1.00 18.70 ? 266  LEU B C     1 
ATOM   10761 O  O     . LEU B 1  268  ? 6.977   14.417  106.211 1.00 17.75 ? 266  LEU B O     1 
ATOM   10762 C  CB    . LEU B 1  268  ? 4.495   12.597  105.290 1.00 16.43 ? 266  LEU B CB    1 
ATOM   10763 C  CG    . LEU B 1  268  ? 3.647   11.374  105.637 1.00 17.67 ? 266  LEU B CG    1 
ATOM   10764 C  CD1   . LEU B 1  268  ? 3.573   10.445  104.452 1.00 19.48 ? 266  LEU B CD1   1 
ATOM   10765 C  CD2   . LEU B 1  268  ? 4.240   10.644  106.837 1.00 21.23 ? 266  LEU B CD2   1 
ATOM   10766 N  N     . SER B 1  269  ? 5.275   15.779  105.637 1.00 17.56 ? 267  SER B N     1 
ATOM   10767 C  CA    . SER B 1  269  ? 6.199   16.854  105.275 1.00 18.03 ? 267  SER B CA    1 
ATOM   10768 C  C     . SER B 1  269  ? 6.979   17.384  106.478 1.00 18.08 ? 267  SER B C     1 
ATOM   10769 O  O     . SER B 1  269  ? 8.007   18.047  106.291 1.00 20.26 ? 267  SER B O     1 
ATOM   10770 C  CB    . SER B 1  269  ? 5.450   18.001  104.583 1.00 19.12 ? 267  SER B CB    1 
ATOM   10771 O  OG    . SER B 1  269  ? 4.584   18.688  105.488 1.00 19.00 ? 267  SER B OG    1 
ATOM   10772 N  N     . ALA B 1  270  ? 6.512   17.122  107.703 1.00 16.13 ? 268  ALA B N     1 
ATOM   10773 C  CA    . ALA B 1  270  ? 7.283   17.455  108.896 1.00 17.69 ? 268  ALA B CA    1 
ATOM   10774 C  C     . ALA B 1  270  ? 8.493   16.551  109.068 1.00 18.40 ? 268  ALA B C     1 
ATOM   10775 O  O     . ALA B 1  270  ? 9.448   16.925  109.762 1.00 16.52 ? 268  ALA B O     1 
ATOM   10776 C  CB    . ALA B 1  270  ? 6.406   17.344  110.149 1.00 19.92 ? 268  ALA B CB    1 
ATOM   10777 N  N     . LEU B 1  271  ? 8.468   15.359  108.479 1.00 16.51 ? 269  LEU B N     1 
ATOM   10778 C  CA    . LEU B 1  271  ? 9.440   14.339  108.839 1.00 17.37 ? 269  LEU B CA    1 
ATOM   10779 C  C     . LEU B 1  271  ? 10.566  14.207  107.835 1.00 17.36 ? 269  LEU B C     1 
ATOM   10780 O  O     . LEU B 1  271  ? 11.456  13.379  108.036 1.00 18.06 ? 269  LEU B O     1 
ATOM   10781 C  CB    . LEU B 1  271  ? 8.754   12.991  109.016 1.00 16.84 ? 269  LEU B CB    1 
ATOM   10782 C  CG    . LEU B 1  271  ? 7.791   12.998  110.199 1.00 17.74 ? 269  LEU B CG    1 
ATOM   10783 C  CD1   . LEU B 1  271  ? 7.039   11.678  110.251 1.00 23.97 ? 269  LEU B CD1   1 
ATOM   10784 C  CD2   . LEU B 1  271  ? 8.548   13.257  111.504 1.00 20.27 ? 269  LEU B CD2   1 
ATOM   10785 N  N     . HIS B 1  272  ? 10.551  15.000  106.766 1.00 16.25 ? 270  HIS B N     1 
ATOM   10786 C  CA    . HIS B 1  272  ? 11.647  14.943  105.814 1.00 17.73 ? 270  HIS B CA    1 
ATOM   10787 C  C     . HIS B 1  272  ? 11.656  16.240  105.030 1.00 17.35 ? 270  HIS B C     1 
ATOM   10788 O  O     . HIS B 1  272  ? 10.585  16.698  104.610 1.00 18.50 ? 270  HIS B O     1 
ATOM   10789 C  CB    . HIS B 1  272  ? 11.509  13.756  104.858 1.00 17.62 ? 270  HIS B CB    1 
ATOM   10790 C  CG    . HIS B 1  272  ? 12.777  13.433  104.139 1.00 20.36 ? 270  HIS B CG    1 
ATOM   10791 N  ND1   . HIS B 1  272  ? 13.240  14.184  103.081 1.00 20.18 ? 270  HIS B ND1   1 
ATOM   10792 C  CD2   . HIS B 1  272  ? 13.711  12.477  104.364 1.00 21.55 ? 270  HIS B CD2   1 
ATOM   10793 C  CE1   . HIS B 1  272  ? 14.400  13.698  102.673 1.00 19.23 ? 270  HIS B CE1   1 
ATOM   10794 N  NE2   . HIS B 1  272  ? 14.707  12.657  103.433 1.00 23.85 ? 270  HIS B NE2   1 
ATOM   10795 N  N     . PRO B 1  273  ? 12.826  16.845  104.801 1.00 16.16 ? 271  PRO B N     1 
ATOM   10796 C  CA    . PRO B 1  273  ? 12.874  18.127  104.081 1.00 15.24 ? 271  PRO B CA    1 
ATOM   10797 C  C     . PRO B 1  273  ? 12.670  18.005  102.586 1.00 15.94 ? 271  PRO B C     1 
ATOM   10798 O  O     . PRO B 1  273  ? 12.465  19.032  101.930 1.00 18.13 ? 271  PRO B O     1 
ATOM   10799 C  CB    . PRO B 1  273  ? 14.281  18.653  104.399 1.00 17.06 ? 271  PRO B CB    1 
ATOM   10800 C  CG    . PRO B 1  273  ? 15.085  17.419  104.695 1.00 19.15 ? 271  PRO B CG    1 
ATOM   10801 C  CD    . PRO B 1  273  ? 14.132  16.455  105.354 1.00 17.88 ? 271  PRO B CD    1 
ATOM   10802 N  N     . ARG B 1  274  ? 12.704  16.802  102.020 1.00 15.99 ? 272  ARG B N     1 
ATOM   10803 C  CA    . ARG B 1  274  ? 12.479  16.606  100.595 1.00 16.77 ? 272  ARG B CA    1 
ATOM   10804 C  C     . ARG B 1  274  ? 11.376  15.581  100.381 1.00 16.89 ? 272  ARG B C     1 
ATOM   10805 O  O     . ARG B 1  274  ? 11.540  14.584  99.673  1.00 16.74 ? 272  ARG B O     1 
ATOM   10806 C  CB    . ARG B 1  274  ? 13.767  16.176  99.886  1.00 16.87 ? 272  ARG B CB    1 
ATOM   10807 C  CG    . ARG B 1  274  ? 14.908  17.199  99.920  1.00 17.55 ? 272  ARG B CG    1 
ATOM   10808 C  CD    . ARG B 1  274  ? 14.505  18.545  99.311  1.00 16.13 ? 272  ARG B CD    1 
ATOM   10809 N  NE    . ARG B 1  274  ? 14.033  18.423  97.935  1.00 17.44 ? 272  ARG B NE    1 
ATOM   10810 C  CZ    . ARG B 1  274  ? 14.827  18.327  96.876  1.00 17.77 ? 272  ARG B CZ    1 
ATOM   10811 N  NH1   . ARG B 1  274  ? 16.153  18.295  96.999  1.00 17.95 ? 272  ARG B NH1   1 
ATOM   10812 N  NH2   . ARG B 1  274  ? 14.283  18.268  95.665  1.00 18.49 ? 272  ARG B NH2   1 
ATOM   10813 N  N     . TYR B 1  275  ? 10.219  15.815  101.005 1.00 14.92 ? 273  TYR B N     1 
ATOM   10814 C  CA    . TYR B 1  275  ? 9.082   14.915  100.846 1.00 17.29 ? 273  TYR B CA    1 
ATOM   10815 C  C     . TYR B 1  275  ? 8.393   15.244  99.526  1.00 19.02 ? 273  TYR B C     1 
ATOM   10816 O  O     . TYR B 1  275  ? 7.536   16.125  99.443  1.00 16.17 ? 273  TYR B O     1 
ATOM   10817 C  CB    . TYR B 1  275  ? 8.136   15.032  102.033 1.00 16.24 ? 273  TYR B CB    1 
ATOM   10818 C  CG    . TYR B 1  275  ? 6.871   14.224  101.861 1.00 15.84 ? 273  TYR B CG    1 
ATOM   10819 C  CD1   . TYR B 1  275  ? 6.930   12.877  101.525 1.00 17.70 ? 273  TYR B CD1   1 
ATOM   10820 C  CD2   . TYR B 1  275  ? 5.632   14.801  102.039 1.00 17.14 ? 273  TYR B CD2   1 
ATOM   10821 C  CE1   . TYR B 1  275  ? 5.794   12.132  101.358 1.00 17.60 ? 273  TYR B CE1   1 
ATOM   10822 C  CE2   . TYR B 1  275  ? 4.474   14.062  101.885 1.00 16.90 ? 273  TYR B CE2   1 
ATOM   10823 C  CZ    . TYR B 1  275  ? 4.562   12.722  101.543 1.00 16.64 ? 273  TYR B CZ    1 
ATOM   10824 O  OH    . TYR B 1  275  ? 3.431   11.975  101.364 1.00 17.50 ? 273  TYR B OH    1 
ATOM   10825 N  N     . SER B 1  276  ? 8.781   14.534  98.468  1.00 16.68 ? 274  SER B N     1 
ATOM   10826 C  CA    . SER B 1  276  ? 8.234   14.816  97.144  1.00 16.65 ? 274  SER B CA    1 
ATOM   10827 C  C     . SER B 1  276  ? 8.505   13.634  96.229  1.00 16.22 ? 274  SER B C     1 
ATOM   10828 O  O     . SER B 1  276  ? 9.421   12.843  96.461  1.00 16.79 ? 274  SER B O     1 
ATOM   10829 C  CB    . SER B 1  276  ? 8.840   16.076  96.531  1.00 21.02 ? 274  SER B CB    1 
ATOM   10830 O  OG    . SER B 1  276  ? 10.176  15.826  96.171  1.00 22.18 ? 274  SER B OG    1 
ATOM   10831 N  N     . ARG B 1  277  ? 7.701   13.543  95.164  1.00 15.93 ? 275  ARG B N     1 
ATOM   10832 C  CA    . ARG B 1  277  ? 7.874   12.469  94.194  1.00 15.94 ? 275  ARG B CA    1 
ATOM   10833 C  C     . ARG B 1  277  ? 9.248   12.529  93.546  1.00 17.62 ? 275  ARG B C     1 
ATOM   10834 O  O     . ARG B 1  277  ? 9.837   11.484  93.260  1.00 17.05 ? 275  ARG B O     1 
ATOM   10835 C  CB    . ARG B 1  277  ? 6.774   12.531  93.132  1.00 15.53 ? 275  ARG B CB    1 
ATOM   10836 C  CG    . ARG B 1  277  ? 6.927   11.552  91.954  1.00 17.54 ? 275  ARG B CG    1 
ATOM   10837 C  CD    . ARG B 1  277  ? 6.957   10.100  92.429  1.00 19.15 ? 275  ARG B CD    1 
ATOM   10838 N  NE    . ARG B 1  277  ? 7.114   9.164   91.320  1.00 17.66 ? 275  ARG B NE    1 
ATOM   10839 C  CZ    . ARG B 1  277  ? 8.284   8.783   90.822  1.00 19.78 ? 275  ARG B CZ    1 
ATOM   10840 N  NH1   . ARG B 1  277  ? 9.424   9.292   91.267  1.00 19.02 ? 275  ARG B NH1   1 
ATOM   10841 N  NH2   . ARG B 1  277  ? 8.313   7.841   89.877  1.00 17.48 ? 275  ARG B NH2   1 
ATOM   10842 N  N     . ALA B 1  278  ? 9.784   13.732  93.330  1.00 18.06 ? 276  ALA B N     1 
ATOM   10843 C  CA    . ALA B 1  278  ? 11.109  13.845  92.728  1.00 16.63 ? 276  ALA B CA    1 
ATOM   10844 C  C     . ALA B 1  278  ? 12.188  13.208  93.589  1.00 18.22 ? 276  ALA B C     1 
ATOM   10845 O  O     . ALA B 1  278  ? 13.239  12.825  93.055  1.00 18.84 ? 276  ALA B O     1 
ATOM   10846 C  CB    . ALA B 1  278  ? 11.453  15.313  92.469  1.00 18.56 ? 276  ALA B CB    1 
ATOM   10847 N  N     . GLN B 1  279  ? 11.958  13.071  94.896  1.00 17.71 ? 277  GLN B N     1 
ATOM   10848 C  CA    . GLN B 1  279  ? 12.924  12.441  95.794  1.00 17.27 ? 277  GLN B CA    1 
ATOM   10849 C  C     . GLN B 1  279  ? 12.341  11.170  96.404  1.00 17.30 ? 277  GLN B C     1 
ATOM   10850 O  O     . GLN B 1  279  ? 12.592  10.849  97.566  1.00 17.01 ? 277  GLN B O     1 
ATOM   10851 C  CB    . GLN B 1  279  ? 13.371  13.406  96.891  1.00 17.63 ? 277  GLN B CB    1 
ATOM   10852 C  CG    . GLN B 1  279  ? 13.985  14.679  96.351  1.00 17.23 ? 277  GLN B CG    1 
ATOM   10853 C  CD    . GLN B 1  279  ? 15.293  14.413  95.628  1.00 19.94 ? 277  GLN B CD    1 
ATOM   10854 O  OE1   . GLN B 1  279  ? 15.979  13.428  95.917  1.00 21.97 ? 277  GLN B OE1   1 
ATOM   10855 N  NE2   . GLN B 1  279  ? 15.637  15.273  94.669  1.00 16.74 ? 277  GLN B NE2   1 
ATOM   10856 N  N     . ALA B 1  280  ? 11.562  10.421  95.612  1.00 18.01 ? 278  ALA B N     1 
ATOM   10857 C  CA    . ALA B 1  280  ? 10.864  9.253   96.143  1.00 18.21 ? 278  ALA B CA    1 
ATOM   10858 C  C     . ALA B 1  280  ? 11.823  8.263   96.796  1.00 20.12 ? 278  ALA B C     1 
ATOM   10859 O  O     . ALA B 1  280  ? 11.490  7.656   97.820  1.00 18.39 ? 278  ALA B O     1 
ATOM   10860 C  CB    . ALA B 1  280  ? 10.064  8.564   95.032  1.00 19.13 ? 278  ALA B CB    1 
ATOM   10861 N  N     . ALA B 1  281  ? 13.021  8.092   96.228  1.00 18.70 ? 279  ALA B N     1 
ATOM   10862 C  CA    . ALA B 1  281  ? 13.963  7.135   96.802  1.00 21.01 ? 279  ALA B CA    1 
ATOM   10863 C  C     . ALA B 1  281  ? 14.363  7.550   98.210  1.00 19.04 ? 279  ALA B C     1 
ATOM   10864 O  O     . ALA B 1  281  ? 14.405  6.719   99.124  1.00 19.92 ? 279  ALA B O     1 
ATOM   10865 C  CB    . ALA B 1  281  ? 15.200  6.996   95.912  1.00 22.17 ? 279  ALA B CB    1 
ATOM   10866 N  N     . ARG B 1  282  ? 14.665  8.839   98.402  1.00 19.00 ? 280  ARG B N     1 
ATOM   10867 C  CA    . ARG B 1  282  ? 14.993  9.320   99.737  1.00 17.31 ? 280  ARG B CA    1 
ATOM   10868 C  C     . ARG B 1  282  ? 13.797  9.207   100.665 1.00 17.33 ? 280  ARG B C     1 
ATOM   10869 O  O     . ARG B 1  282  ? 13.958  8.940   101.858 1.00 18.91 ? 280  ARG B O     1 
ATOM   10870 C  CB    . ARG B 1  282  ? 15.479  10.772  99.684  1.00 18.40 ? 280  ARG B CB    1 
ATOM   10871 C  CG    . ARG B 1  282  ? 16.815  10.975  98.967  1.00 19.15 ? 280  ARG B CG    1 
ATOM   10872 C  CD    . ARG B 1  282  ? 17.342  12.376  99.243  1.00 20.00 ? 280  ARG B CD    1 
ATOM   10873 N  NE    . ARG B 1  282  ? 17.605  12.559  100.664 1.00 20.01 ? 280  ARG B NE    1 
ATOM   10874 C  CZ    . ARG B 1  282  ? 17.767  13.736  101.252 1.00 20.09 ? 280  ARG B CZ    1 
ATOM   10875 N  NH1   . ARG B 1  282  ? 17.684  14.871  100.568 1.00 19.71 ? 280  ARG B NH1   1 
ATOM   10876 N  NH2   . ARG B 1  282  ? 18.025  13.779  102.559 1.00 20.07 ? 280  ARG B NH2   1 
ATOM   10877 N  N     . VAL B 1  283  ? 12.592  9.438   100.138 1.00 16.95 ? 281  VAL B N     1 
ATOM   10878 C  CA    . VAL B 1  283  ? 11.392  9.322   100.963 1.00 17.47 ? 281  VAL B CA    1 
ATOM   10879 C  C     . VAL B 1  283  ? 11.244  7.899   101.479 1.00 17.72 ? 281  VAL B C     1 
ATOM   10880 O  O     . VAL B 1  283  ? 11.060  7.671   102.680 1.00 20.29 ? 281  VAL B O     1 
ATOM   10881 C  CB    . VAL B 1  283  ? 10.156  9.775   100.165 1.00 16.86 ? 281  VAL B CB    1 
ATOM   10882 C  CG1   . VAL B 1  283  ? 8.876   9.325   100.863 1.00 20.37 ? 281  VAL B CG1   1 
ATOM   10883 C  CG2   . VAL B 1  283  ? 10.182  11.302  100.023 1.00 16.28 ? 281  VAL B CG2   1 
ATOM   10884 N  N     . MET B 1  284  ? 11.346  6.917   100.583 1.00 17.77 ? 282  MET B N     1 
ATOM   10885 C  CA    . MET B 1  284  ? 11.178  5.534   101.013 1.00 19.86 ? 282  MET B CA    1 
ATOM   10886 C  C     . MET B 1  284  ? 12.330  5.079   101.889 1.00 21.21 ? 282  MET B C     1 
ATOM   10887 O  O     . MET B 1  284  ? 12.139  4.230   102.767 1.00 22.23 ? 282  MET B O     1 
ATOM   10888 C  CB    . MET B 1  284  ? 11.056  4.605   99.807  1.00 18.19 ? 282  MET B CB    1 
ATOM   10889 C  CG    . MET B 1  284  ? 9.846   4.884   98.933  1.00 18.75 ? 282  MET B CG    1 
ATOM   10890 S  SD    . MET B 1  284  ? 8.281   4.833   99.822  1.00 22.76 ? 282  MET B SD    1 
ATOM   10891 C  CE    . MET B 1  284  ? 8.106   3.077   100.117 1.00 22.82 ? 282  MET B CE    1 
ATOM   10892 N  N     . GLY B 1  285  ? 13.525  5.624   101.665 1.00 17.67 ? 283  GLY B N     1 
ATOM   10893 C  CA    . GLY B 1  285  ? 14.696  5.184   102.402 1.00 21.45 ? 283  GLY B CA    1 
ATOM   10894 C  C     . GLY B 1  285  ? 14.886  5.846   103.751 1.00 19.89 ? 283  GLY B C     1 
ATOM   10895 O  O     . GLY B 1  285  ? 15.424  5.229   104.678 1.00 22.03 ? 283  GLY B O     1 
ATOM   10896 N  N     . GLU B 1  286  ? 14.463  7.103   103.876 1.00 18.05 ? 284  GLU B N     1 
ATOM   10897 C  CA    . GLU B 1  286  ? 14.733  7.923   105.052 1.00 17.97 ? 284  GLU B CA    1 
ATOM   10898 C  C     . GLU B 1  286  ? 13.484  8.310   105.821 1.00 21.11 ? 284  GLU B C     1 
ATOM   10899 O  O     . GLU B 1  286  ? 13.491  8.285   107.054 1.00 22.77 ? 284  GLU B O     1 
ATOM   10900 C  CB    . GLU B 1  286  ? 15.474  9.202   104.630 1.00 20.74 ? 284  GLU B CB    1 
ATOM   10901 C  CG    . GLU B 1  286  ? 16.656  8.924   103.717 1.00 20.55 ? 284  GLU B CG    1 
ATOM   10902 C  CD    . GLU B 1  286  ? 17.304  10.186  103.188 1.00 22.02 ? 284  GLU B CD    1 
ATOM   10903 O  OE1   . GLU B 1  286  ? 17.054  11.276  103.753 1.00 21.37 ? 284  GLU B OE1   1 
ATOM   10904 O  OE2   . GLU B 1  286  ? 18.067  10.083  102.207 1.00 24.29 ? 284  GLU B OE2   1 
ATOM   10905 N  N     . LEU B 1  287  ? 12.414  8.682   105.120 1.00 18.58 ? 285  LEU B N     1 
ATOM   10906 C  CA    . LEU B 1  287  ? 11.174  9.078   105.769 1.00 18.44 ? 285  LEU B CA    1 
ATOM   10907 C  C     . LEU B 1  287  ? 10.401  7.868   106.275 1.00 20.40 ? 285  LEU B C     1 
ATOM   10908 O  O     . LEU B 1  287  ? 9.972   7.842   107.432 1.00 18.96 ? 285  LEU B O     1 
ATOM   10909 C  CB    . LEU B 1  287  ? 10.315  9.880   104.788 1.00 18.93 ? 285  LEU B CB    1 
ATOM   10910 C  CG    . LEU B 1  287  ? 9.366   10.957  105.341 1.00 26.16 ? 285  LEU B CG    1 
ATOM   10911 C  CD1   . LEU B 1  287  ? 8.649   11.656  104.208 1.00 22.18 ? 285  LEU B CD1   1 
ATOM   10912 C  CD2   . LEU B 1  287  ? 8.360   10.400  106.286 1.00 25.29 ? 285  LEU B CD2   1 
ATOM   10913 N  N     . LEU B 1  288  ? 10.167  6.885   105.407 1.00 20.62 ? 286  LEU B N     1 
ATOM   10914 C  CA    . LEU B 1  288  ? 9.377   5.718   105.796 1.00 19.03 ? 286  LEU B CA    1 
ATOM   10915 C  C     . LEU B 1  288  ? 9.871   5.046   107.073 1.00 21.18 ? 286  LEU B C     1 
ATOM   10916 O  O     . LEU B 1  288  ? 9.031   4.716   107.923 1.00 19.78 ? 286  LEU B O     1 
ATOM   10917 C  CB    . LEU B 1  288  ? 9.325   4.721   104.630 1.00 20.07 ? 286  LEU B CB    1 
ATOM   10918 C  CG    . LEU B 1  288  ? 8.704   3.371   104.962 1.00 23.48 ? 286  LEU B CG    1 
ATOM   10919 C  CD1   . LEU B 1  288  ? 7.243   3.537   105.378 1.00 23.43 ? 286  LEU B CD1   1 
ATOM   10920 C  CD2   . LEU B 1  288  ? 8.834   2.451   103.772 1.00 27.09 ? 286  LEU B CD2   1 
ATOM   10921 N  N     . PRO B 1  289  ? 11.177  4.814   107.282 1.00 22.59 ? 287  PRO B N     1 
ATOM   10922 C  CA    . PRO B 1  289  ? 11.602  4.217   108.560 1.00 22.43 ? 287  PRO B CA    1 
ATOM   10923 C  C     . PRO B 1  289  ? 11.225  5.045   109.773 1.00 20.89 ? 287  PRO B C     1 
ATOM   10924 O  O     . PRO B 1  289  ? 10.957  4.478   110.840 1.00 21.43 ? 287  PRO B O     1 
ATOM   10925 C  CB    . PRO B 1  289  ? 13.124  4.112   108.403 1.00 23.05 ? 287  PRO B CB    1 
ATOM   10926 C  CG    . PRO B 1  289  ? 13.321  3.959   106.928 1.00 24.73 ? 287  PRO B CG    1 
ATOM   10927 C  CD    . PRO B 1  289  ? 12.295  4.871   106.316 1.00 20.45 ? 287  PRO B CD    1 
ATOM   10928 N  N     . ARG B 1  290  ? 11.203  6.374   109.649 1.00 19.84 ? 288  ARG B N     1 
ATOM   10929 C  CA    . ARG B 1  290  ? 10.781  7.195   110.775 1.00 21.05 ? 288  ARG B CA    1 
ATOM   10930 C  C     . ARG B 1  290  ? 9.298   7.014   111.048 1.00 19.67 ? 288  ARG B C     1 
ATOM   10931 O  O     . ARG B 1  290  ? 8.889   6.878   112.204 1.00 18.57 ? 288  ARG B O     1 
ATOM   10932 C  CB    . ARG B 1  290  ? 11.106  8.661   110.510 1.00 20.51 ? 288  ARG B CB    1 
ATOM   10933 C  CG    . ARG B 1  290  ? 12.612  8.916   110.470 1.00 21.66 ? 288  ARG B CG    1 
ATOM   10934 C  CD    . ARG B 1  290  ? 12.911  10.260  109.841 1.00 27.61 ? 288  ARG B CD    1 
ATOM   10935 N  NE    . ARG B 1  290  ? 14.335  10.441  109.581 1.00 33.12 ? 288  ARG B NE    1 
ATOM   10936 C  CZ    . ARG B 1  290  ? 14.823  11.180  108.593 1.00 31.48 ? 288  ARG B CZ    1 
ATOM   10937 N  NH1   . ARG B 1  290  ? 14.027  11.839  107.762 1.00 27.45 ? 288  ARG B NH1   1 
ATOM   10938 N  NH2   . ARG B 1  290  ? 16.142  11.254  108.428 1.00 34.20 ? 288  ARG B NH2   1 
ATOM   10939 N  N     . VAL B 1  291  ? 8.484   6.979   109.994 1.00 19.06 ? 289  VAL B N     1 
ATOM   10940 C  CA    . VAL B 1  291  ? 7.055   6.763   110.197 1.00 16.90 ? 289  VAL B CA    1 
ATOM   10941 C  C     . VAL B 1  291  ? 6.817   5.397   110.811 1.00 17.25 ? 289  VAL B C     1 
ATOM   10942 O  O     . VAL B 1  291  ? 5.984   5.240   111.716 1.00 20.21 ? 289  VAL B O     1 
ATOM   10943 C  CB    . VAL B 1  291  ? 6.291   6.920   108.872 1.00 19.77 ? 289  VAL B CB    1 
ATOM   10944 C  CG1   . VAL B 1  291  ? 4.825   6.649   109.099 1.00 21.04 ? 289  VAL B CG1   1 
ATOM   10945 C  CG2   . VAL B 1  291  ? 6.487   8.317   108.328 1.00 20.91 ? 289  VAL B CG2   1 
ATOM   10946 N  N     . LYS B 1  292  ? 7.538   4.385   110.326 1.00 19.08 ? 290  LYS B N     1 
ATOM   10947 C  CA    . LYS B 1  292  ? 7.390   3.047   110.892 1.00 19.15 ? 290  LYS B CA    1 
ATOM   10948 C  C     . LYS B 1  292  ? 7.701   3.052   112.383 1.00 22.21 ? 290  LYS B C     1 
ATOM   10949 O  O     . LYS B 1  292  ? 6.965   2.459   113.181 1.00 20.50 ? 290  LYS B O     1 
ATOM   10950 C  CB    . LYS B 1  292  ? 8.296   2.059   110.157 1.00 20.72 ? 290  LYS B CB    1 
ATOM   10951 C  CG    . LYS B 1  292  ? 8.121   0.602   110.611 1.00 25.51 ? 290  LYS B CG    1 
ATOM   10952 C  CD    . LYS B 1  292  ? 9.097   0.222   111.706 1.00 25.21 ? 290  LYS B CD    1 
ATOM   10953 C  CE    . LYS B 1  292  ? 8.765   -1.174  112.264 1.00 26.95 ? 290  LYS B CE    1 
ATOM   10954 N  NZ    . LYS B 1  292  ? 8.994   -2.237  111.250 1.00 29.50 ? 290  LYS B NZ    1 
ATOM   10955 N  N     . ALA B 1  293  ? 8.787   3.724   112.775 1.00 20.19 ? 291  ALA B N     1 
ATOM   10956 C  CA    . ALA B 1  293  ? 9.153   3.775   114.187 1.00 21.46 ? 291  ALA B CA    1 
ATOM   10957 C  C     . ALA B 1  293  ? 8.046   4.408   115.022 1.00 22.01 ? 291  ALA B C     1 
ATOM   10958 O  O     . ALA B 1  293  ? 7.723   3.923   116.117 1.00 19.93 ? 291  ALA B O     1 
ATOM   10959 C  CB    . ALA B 1  293  ? 10.458  4.549   114.351 1.00 21.44 ? 291  ALA B CB    1 
ATOM   10960 N  N     . LEU B 1  294  ? 7.468   5.508   114.530 1.00 20.60 ? 292  LEU B N     1 
ATOM   10961 C  CA    . LEU B 1  294  ? 6.358   6.133   115.240 1.00 19.98 ? 292  LEU B CA    1 
ATOM   10962 C  C     . LEU B 1  294  ? 5.152   5.212   115.276 1.00 20.21 ? 292  LEU B C     1 
ATOM   10963 O  O     . LEU B 1  294  ? 4.497   5.079   116.317 1.00 21.34 ? 292  LEU B O     1 
ATOM   10964 C  CB    . LEU B 1  294  ? 5.983   7.465   114.585 1.00 19.30 ? 292  LEU B CB    1 
ATOM   10965 C  CG    . LEU B 1  294  ? 7.097   8.513   114.571 1.00 19.52 ? 292  LEU B CG    1 
ATOM   10966 C  CD1   . LEU B 1  294  ? 6.684   9.703   113.748 1.00 19.80 ? 292  LEU B CD1   1 
ATOM   10967 C  CD2   . LEU B 1  294  ? 7.488   8.940   116.004 1.00 18.60 ? 292  LEU B CD2   1 
ATOM   10968 N  N     . ALA B 1  295  ? 4.836   4.572   114.146 1.00 20.93 ? 293  ALA B N     1 
ATOM   10969 C  CA    . ALA B 1  295  ? 3.684   3.680   114.116 1.00 22.61 ? 293  ALA B CA    1 
ATOM   10970 C  C     . ALA B 1  295  ? 3.872   2.523   115.089 1.00 22.89 ? 293  ALA B C     1 
ATOM   10971 O  O     . ALA B 1  295  ? 2.918   2.092   115.744 1.00 21.49 ? 293  ALA B O     1 
ATOM   10972 C  CB    . ALA B 1  295  ? 3.450   3.178   112.687 1.00 20.90 ? 293  ALA B CB    1 
ATOM   10973 N  N     . LEU B 1  296  ? 5.105   2.034   115.227 1.00 23.05 ? 294  LEU B N     1 
ATOM   10974 C  CA    . LEU B 1  296  ? 5.367   0.944   116.163 1.00 24.43 ? 294  LEU B CA    1 
ATOM   10975 C  C     . LEU B 1  296  ? 5.126   1.374   117.610 1.00 25.42 ? 294  LEU B C     1 
ATOM   10976 O  O     . LEU B 1  296  ? 4.585   0.600   118.411 1.00 25.24 ? 294  LEU B O     1 
ATOM   10977 C  CB    . LEU B 1  296  ? 6.791   0.432   115.964 1.00 24.63 ? 294  LEU B CB    1 
ATOM   10978 C  CG    . LEU B 1  296  ? 7.255   -0.721  116.856 1.00 28.60 ? 294  LEU B CG    1 
ATOM   10979 C  CD1   . LEU B 1  296  ? 6.317   -1.920  116.738 1.00 29.36 ? 294  LEU B CD1   1 
ATOM   10980 C  CD2   . LEU B 1  296  ? 8.693   -1.105  116.494 1.00 30.42 ? 294  LEU B CD2   1 
ATOM   10981 N  N     . LEU B 1  297  ? 5.504   2.608   117.960 1.00 23.58 ? 295  LEU B N     1 
ATOM   10982 C  CA    . LEU B 1  297  ? 5.196   3.128   119.292 1.00 23.65 ? 295  LEU B CA    1 
ATOM   10983 C  C     . LEU B 1  297  ? 3.690   3.256   119.499 1.00 23.40 ? 295  LEU B C     1 
ATOM   10984 O  O     . LEU B 1  297  ? 3.159   2.863   120.544 1.00 22.79 ? 295  LEU B O     1 
ATOM   10985 C  CB    . LEU B 1  297  ? 5.877   4.483   119.497 1.00 20.64 ? 295  LEU B CB    1 
ATOM   10986 C  CG    . LEU B 1  297  ? 7.378   4.507   119.773 1.00 28.15 ? 295  LEU B CG    1 
ATOM   10987 C  CD1   . LEU B 1  297  ? 7.912   5.946   119.664 1.00 26.61 ? 295  LEU B CD1   1 
ATOM   10988 C  CD2   . LEU B 1  297  ? 7.681   3.914   121.144 1.00 26.37 ? 295  LEU B CD2   1 
ATOM   10989 N  N     . ALA B 1  298  ? 2.986   3.816   118.512 1.00 22.42 ? 296  ALA B N     1 
ATOM   10990 C  CA    . ALA B 1  298  ? 1.535   3.919   118.602 1.00 21.97 ? 296  ALA B CA    1 
ATOM   10991 C  C     . ALA B 1  298  ? 0.906   2.544   118.753 1.00 25.73 ? 296  ALA B C     1 
ATOM   10992 O  O     . ALA B 1  298  ? -0.050  2.365   119.520 1.00 24.81 ? 296  ALA B O     1 
ATOM   10993 C  CB    . ALA B 1  298  ? 0.978   4.622   117.365 1.00 22.07 ? 296  ALA B CB    1 
ATOM   10994 N  N     . LYS B 1  299  ? 1.440   1.560   118.031 1.00 22.98 ? 297  LYS B N     1 
ATOM   10995 C  CA    . LYS B 1  299  ? 0.921   0.201   118.128 1.00 26.37 ? 297  LYS B CA    1 
ATOM   10996 C  C     . LYS B 1  299  ? 1.126   -0.368  119.524 1.00 28.12 ? 297  LYS B C     1 
ATOM   10997 O  O     . LYS B 1  299  ? 0.216   -0.990  120.091 1.00 28.52 ? 297  LYS B O     1 
ATOM   10998 C  CB    . LYS B 1  299  ? 1.592   -0.679  117.072 1.00 27.57 ? 297  LYS B CB    1 
ATOM   10999 C  CG    . LYS B 1  299  ? 1.076   -2.100  117.005 1.00 30.39 ? 297  LYS B CG    1 
ATOM   11000 C  CD    . LYS B 1  299  ? 2.019   -3.075  117.648 1.00 31.22 ? 297  LYS B CD    1 
ATOM   11001 C  CE    . LYS B 1  299  ? 1.503   -4.499  117.472 1.00 32.84 ? 297  LYS B CE    1 
ATOM   11002 N  NZ    . LYS B 1  299  ? 2.209   -5.418  118.395 1.00 35.24 ? 297  LYS B NZ    1 
ATOM   11003 N  N     . ASN B 1  300  ? 2.313   -0.161  120.098 1.00 26.77 ? 298  ASN B N     1 
ATOM   11004 C  CA    . ASN B 1  300  ? 2.587   -0.699  121.425 1.00 26.42 ? 298  ASN B CA    1 
ATOM   11005 C  C     . ASN B 1  300  ? 1.669   -0.090  122.479 1.00 27.50 ? 298  ASN B C     1 
ATOM   11006 O  O     . ASN B 1  300  ? 1.336   -0.754  123.465 1.00 29.55 ? 298  ASN B O     1 
ATOM   11007 C  CB    . ASN B 1  300  ? 4.057   -0.476  121.785 1.00 29.38 ? 298  ASN B CB    1 
ATOM   11008 C  CG    . ASN B 1  300  ? 4.998   -1.318  120.933 1.00 30.99 ? 298  ASN B CG    1 
ATOM   11009 O  OD1   . ASN B 1  300  ? 4.594   -2.331  120.356 1.00 34.04 ? 298  ASN B OD1   1 
ATOM   11010 N  ND2   . ASN B 1  300  ? 6.261   -0.908  120.860 1.00 37.02 ? 298  ASN B ND2   1 
ATOM   11011 N  N     . TYR B 1  301  ? 1.236   1.153   122.290 1.00 23.53 ? 299  TYR B N     1 
ATOM   11012 C  CA    . TYR B 1  301  ? 0.278   1.758   123.209 1.00 26.94 ? 299  TYR B CA    1 
ATOM   11013 C  C     . TYR B 1  301  ? -1.164  1.526   122.794 1.00 23.52 ? 299  TYR B C     1 
ATOM   11014 O  O     . TYR B 1  301  ? -2.070  1.935   123.523 1.00 24.79 ? 299  TYR B O     1 
ATOM   11015 C  CB    . TYR B 1  301  ? 0.518   3.267   123.326 1.00 23.92 ? 299  TYR B CB    1 
ATOM   11016 C  CG    . TYR B 1  301  ? 1.762   3.651   124.097 1.00 23.84 ? 299  TYR B CG    1 
ATOM   11017 C  CD1   . TYR B 1  301  ? 1.856   3.419   125.463 1.00 24.13 ? 299  TYR B CD1   1 
ATOM   11018 C  CD2   . TYR B 1  301  ? 2.829   4.275   123.460 1.00 23.37 ? 299  TYR B CD2   1 
ATOM   11019 C  CE1   . TYR B 1  301  ? 2.997   3.786   126.174 1.00 24.48 ? 299  TYR B CE1   1 
ATOM   11020 C  CE2   . TYR B 1  301  ? 3.963   4.646   124.152 1.00 26.19 ? 299  TYR B CE2   1 
ATOM   11021 C  CZ    . TYR B 1  301  ? 4.045   4.399   125.506 1.00 22.77 ? 299  TYR B CZ    1 
ATOM   11022 O  OH    . TYR B 1  301  ? 5.174   4.769   126.192 1.00 25.12 ? 299  TYR B OH    1 
ATOM   11023 N  N     . ASP B 1  302  ? -1.386  0.896   121.642 1.00 23.58 ? 300  ASP B N     1 
ATOM   11024 C  CA    . ASP B 1  302  ? -2.701  0.746   121.021 1.00 26.03 ? 300  ASP B CA    1 
ATOM   11025 C  C     . ASP B 1  302  ? -3.446  2.080   120.937 1.00 25.24 ? 300  ASP B C     1 
ATOM   11026 O  O     . ASP B 1  302  ? -4.576  2.230   121.406 1.00 27.70 ? 300  ASP B O     1 
ATOM   11027 C  CB    . ASP B 1  302  ? -3.550  -0.306  121.740 1.00 28.17 ? 300  ASP B CB    1 
ATOM   11028 C  CG    . ASP B 1  302  ? -4.654  -0.846  120.848 1.00 30.44 ? 300  ASP B CG    1 
ATOM   11029 O  OD1   . ASP B 1  302  ? -4.446  -0.880  119.613 1.00 32.51 ? 300  ASP B OD1   1 
ATOM   11030 O  OD2   . ASP B 1  302  ? -5.732  -1.196  121.365 1.00 32.79 ? 300  ASP B OD2   1 
ATOM   11031 N  N     . ILE B 1  303  ? -2.793  3.061   120.319 1.00 22.63 ? 301  ILE B N     1 
ATOM   11032 C  CA    . ILE B 1  303  ? -3.457  4.302   119.959 1.00 23.40 ? 301  ILE B CA    1 
ATOM   11033 C  C     . ILE B 1  303  ? -3.500  4.399   118.444 1.00 24.60 ? 301  ILE B C     1 
ATOM   11034 O  O     . ILE B 1  303  ? -2.772  3.706   117.726 1.00 24.79 ? 301  ILE B O     1 
ATOM   11035 C  CB    . ILE B 1  303  ? -2.772  5.545   120.561 1.00 21.50 ? 301  ILE B CB    1 
ATOM   11036 C  CG1   . ILE B 1  303  ? -1.425  5.806   119.877 1.00 25.38 ? 301  ILE B CG1   1 
ATOM   11037 C  CG2   . ILE B 1  303  ? -2.583  5.356   122.047 1.00 21.03 ? 301  ILE B CG2   1 
ATOM   11038 C  CD1   . ILE B 1  303  ? -0.737  7.092   120.344 1.00 24.90 ? 301  ILE B CD1   1 
ATOM   11039 N  N     . GLY B 1  304  ? -4.360  5.292   117.958 1.00 24.18 ? 302  GLY B N     1 
ATOM   11040 C  CA    . GLY B 1  304  ? -4.402  5.580   116.533 1.00 24.34 ? 302  GLY B CA    1 
ATOM   11041 C  C     . GLY B 1  304  ? -3.280  6.525   116.132 1.00 24.52 ? 302  GLY B C     1 
ATOM   11042 O  O     . GLY B 1  304  ? -2.917  7.443   116.866 1.00 23.65 ? 302  GLY B O     1 
ATOM   11043 N  N     . LEU B 1  305  ? -2.717  6.277   114.953 1.00 20.57 ? 303  LEU B N     1 
ATOM   11044 C  CA    . LEU B 1  305  ? -1.738  7.174   114.338 1.00 22.94 ? 303  LEU B CA    1 
ATOM   11045 C  C     . LEU B 1  305  ? -2.197  7.450   112.918 1.00 24.16 ? 303  LEU B C     1 
ATOM   11046 O  O     . LEU B 1  305  ? -2.290  6.525   112.105 1.00 25.17 ? 303  LEU B O     1 
ATOM   11047 C  CB    . LEU B 1  305  ? -0.324  6.571   114.349 1.00 23.38 ? 303  LEU B CB    1 
ATOM   11048 C  CG    . LEU B 1  305  ? 0.790   7.426   113.720 1.00 23.98 ? 303  LEU B CG    1 
ATOM   11049 C  CD1   . LEU B 1  305  ? 2.066   7.403   114.569 1.00 24.30 ? 303  LEU B CD1   1 
ATOM   11050 C  CD2   . LEU B 1  305  ? 1.090   6.980   112.306 1.00 27.63 ? 303  LEU B CD2   1 
ATOM   11051 N  N     . ASN B 1  306  ? -2.485  8.711   112.624 1.00 21.84 ? 304  ASN B N     1 
ATOM   11052 C  CA    . ASN B 1  306  ? -3.127  9.093   111.375 1.00 23.66 ? 304  ASN B CA    1 
ATOM   11053 C  C     . ASN B 1  306  ? -2.180  9.925   110.523 1.00 21.19 ? 304  ASN B C     1 
ATOM   11054 O  O     . ASN B 1  306  ? -1.615  10.910  111.005 1.00 20.10 ? 304  ASN B O     1 
ATOM   11055 C  CB    . ASN B 1  306  ? -4.401  9.890   111.655 1.00 24.74 ? 304  ASN B CB    1 
ATOM   11056 C  CG    . ASN B 1  306  ? -4.920  10.581  110.429 1.00 23.73 ? 304  ASN B CG    1 
ATOM   11057 O  OD1   . ASN B 1  306  ? -4.521  11.709  110.119 1.00 25.61 ? 304  ASN B OD1   1 
ATOM   11058 N  ND2   . ASN B 1  306  ? -5.792  9.903   109.696 1.00 24.94 ? 304  ASN B ND2   1 
ATOM   11059 N  N     . ILE B 1  307  ? -2.043  9.562   109.252 1.00 19.81 ? 305  ILE B N     1 
ATOM   11060 C  CA    . ILE B 1  307  ? -1.253  10.344  108.306 1.00 20.08 ? 305  ILE B CA    1 
ATOM   11061 C  C     . ILE B 1  307  ? -2.160  11.392  107.670 1.00 20.83 ? 305  ILE B C     1 
ATOM   11062 O  O     . ILE B 1  307  ? -3.068  11.061  106.902 1.00 19.08 ? 305  ILE B O     1 
ATOM   11063 C  CB    . ILE B 1  307  ? -0.600  9.461   107.239 1.00 21.06 ? 305  ILE B CB    1 
ATOM   11064 C  CG1   . ILE B 1  307  ? 0.418   8.519   107.882 1.00 22.15 ? 305  ILE B CG1   1 
ATOM   11065 C  CG2   . ILE B 1  307  ? 0.044   10.339  106.150 1.00 19.96 ? 305  ILE B CG2   1 
ATOM   11066 C  CD1   . ILE B 1  307  ? 1.004   7.506   106.912 1.00 22.04 ? 305  ILE B CD1   1 
ATOM   11067 N  N     . ASP B 1  308  ? -1.910  12.662  107.988 1.00 18.46 ? 306  ASP B N     1 
ATOM   11068 C  CA    . ASP B 1  308  ? -2.674  13.744  107.388 1.00 20.21 ? 306  ASP B CA    1 
ATOM   11069 C  C     . ASP B 1  308  ? -2.345  13.867  105.899 1.00 18.16 ? 306  ASP B C     1 
ATOM   11070 O  O     . ASP B 1  308  ? -1.262  13.500  105.439 1.00 19.06 ? 306  ASP B O     1 
ATOM   11071 C  CB    . ASP B 1  308  ? -2.386  15.068  108.107 1.00 18.97 ? 306  ASP B CB    1 
ATOM   11072 C  CG    . ASP B 1  308  ? -2.866  15.069  109.564 1.00 21.38 ? 306  ASP B CG    1 
ATOM   11073 O  OD1   . ASP B 1  308  ? -3.803  14.323  109.894 1.00 22.76 ? 306  ASP B OD1   1 
ATOM   11074 O  OD2   . ASP B 1  308  ? -2.302  15.825  110.381 1.00 25.22 ? 306  ASP B OD2   1 
ATOM   11075 N  N     . ALA B 1  309  ? -3.291  14.409  105.140 1.00 17.46 ? 307  ALA B N     1 
ATOM   11076 C  CA    . ALA B 1  309  ? -3.137  14.533  103.698 1.00 15.76 ? 307  ALA B CA    1 
ATOM   11077 C  C     . ALA B 1  309  ? -2.781  15.964  103.334 1.00 16.63 ? 307  ALA B C     1 
ATOM   11078 O  O     . ALA B 1  309  ? -3.300  16.916  103.923 1.00 18.58 ? 307  ALA B O     1 
ATOM   11079 C  CB    . ALA B 1  309  ? -4.417  14.108  102.972 1.00 17.97 ? 307  ALA B CB    1 
ATOM   11080 N  N     . GLU B 1  310  ? -1.866  16.109  102.383 1.00 15.76 ? 308  GLU B N     1 
ATOM   11081 C  CA    . GLU B 1  310  ? -1.316  17.424  102.091 1.00 15.71 ? 308  GLU B CA    1 
ATOM   11082 C  C     . GLU B 1  310  ? -1.596  17.807  100.646 1.00 14.63 ? 308  GLU B C     1 
ATOM   11083 O  O     . GLU B 1  310  ? -2.737  17.654  100.186 1.00 16.57 ? 308  GLU B O     1 
ATOM   11084 C  CB    . GLU B 1  310  ? 0.182   17.445  102.435 1.00 15.66 ? 308  GLU B CB    1 
ATOM   11085 C  CG    . GLU B 1  310  ? 0.384   17.107  103.918 1.00 17.72 ? 308  GLU B CG    1 
ATOM   11086 C  CD    . GLU B 1  310  ? 1.812   17.267  104.384 1.00 18.77 ? 308  GLU B CD    1 
ATOM   11087 O  OE1   . GLU B 1  310  ? 2.291   18.413  104.382 1.00 20.22 ? 308  GLU B OE1   1 
ATOM   11088 O  OE2   . GLU B 1  310  ? 2.435   16.253  104.766 1.00 17.49 ? 308  GLU B OE2   1 
ATOM   11089 N  N     . GLU B 1  311  ? -0.598  18.330  99.932  1.00 14.85 ? 309  GLU B N     1 
ATOM   11090 C  CA    . GLU B 1  311  ? -0.825  18.793  98.572  1.00 15.22 ? 309  GLU B CA    1 
ATOM   11091 C  C     . GLU B 1  311  ? -1.170  17.625  97.655  1.00 16.60 ? 309  GLU B C     1 
ATOM   11092 O  O     . GLU B 1  311  ? -0.854  16.463  97.929  1.00 15.78 ? 309  GLU B O     1 
ATOM   11093 C  CB    . GLU B 1  311  ? 0.411   19.518  98.026  1.00 15.50 ? 309  GLU B CB    1 
ATOM   11094 C  CG    . GLU B 1  311  ? 0.694   20.863  98.691  1.00 18.87 ? 309  GLU B CG    1 
ATOM   11095 C  CD    . GLU B 1  311  ? 1.486   20.749  99.977  1.00 20.73 ? 309  GLU B CD    1 
ATOM   11096 O  OE1   . GLU B 1  311  ? 1.700   19.623  100.487 1.00 18.94 ? 309  GLU B OE1   1 
ATOM   11097 O  OE2   . GLU B 1  311  ? 1.910   21.812  100.489 1.00 22.91 ? 309  GLU B OE2   1 
ATOM   11098 N  N     . ALA B 1  312  ? -1.833  17.953  96.547  1.00 15.92 ? 310  ALA B N     1 
ATOM   11099 C  CA    . ALA B 1  312  ? -2.262  16.925  95.606  1.00 15.76 ? 310  ALA B CA    1 
ATOM   11100 C  C     . ALA B 1  312  ? -1.089  16.118  95.060  1.00 15.37 ? 310  ALA B C     1 
ATOM   11101 O  O     . ALA B 1  312  ? -1.236  14.913  94.818  1.00 15.57 ? 310  ALA B O     1 
ATOM   11102 C  CB    . ALA B 1  312  ? -3.046  17.561  94.451  1.00 17.16 ? 310  ALA B CB    1 
ATOM   11103 N  N     . ASP B 1  313  ? 0.079   16.747  94.865  1.00 15.69 ? 311  ASP B N     1 
ATOM   11104 C  CA    . ASP B 1  313  ? 1.211   16.014  94.304  1.00 16.66 ? 311  ASP B CA    1 
ATOM   11105 C  C     . ASP B 1  313  ? 1.932   15.161  95.340  1.00 16.92 ? 311  ASP B C     1 
ATOM   11106 O  O     . ASP B 1  313  ? 2.955   14.563  95.020  1.00 17.17 ? 311  ASP B O     1 
ATOM   11107 C  CB    . ASP B 1  313  ? 2.189   16.964  93.591  1.00 17.44 ? 311  ASP B CB    1 
ATOM   11108 C  CG    . ASP B 1  313  ? 2.853   17.985  94.517  1.00 17.52 ? 311  ASP B CG    1 
ATOM   11109 O  OD1   . ASP B 1  313  ? 2.687   17.922  95.749  1.00 16.82 ? 311  ASP B OD1   1 
ATOM   11110 O  OD2   . ASP B 1  313  ? 3.590   18.861  93.995  1.00 20.85 ? 311  ASP B OD2   1 
ATOM   11111 N  N     . ARG B 1  314  ? 1.413   15.075  96.558  1.00 15.43 ? 312  ARG B N     1 
ATOM   11112 C  CA    . ARG B 1  314  ? 1.928   14.145  97.548  1.00 17.02 ? 312  ARG B CA    1 
ATOM   11113 C  C     . ARG B 1  314  ? 0.983   12.985  97.812  1.00 14.49 ? 312  ARG B C     1 
ATOM   11114 O  O     . ARG B 1  314  ? 1.349   12.063  98.543  1.00 15.25 ? 312  ARG B O     1 
ATOM   11115 C  CB    . ARG B 1  314  ? 2.227   14.888  98.861  1.00 14.66 ? 312  ARG B CB    1 
ATOM   11116 C  CG    . ARG B 1  314  ? 3.500   15.708  98.771  1.00 16.15 ? 312  ARG B CG    1 
ATOM   11117 C  CD    . ARG B 1  314  ? 3.557   16.811  99.813  1.00 19.72 ? 312  ARG B CD    1 
ATOM   11118 N  NE    . ARG B 1  314  ? 4.930   17.286  99.983  1.00 17.73 ? 312  ARG B NE    1 
ATOM   11119 C  CZ    . ARG B 1  314  ? 5.281   18.307  100.753 1.00 17.35 ? 312  ARG B CZ    1 
ATOM   11120 N  NH1   . ARG B 1  314  ? 4.375   19.061  101.358 1.00 17.65 ? 312  ARG B NH1   1 
ATOM   11121 N  NH2   . ARG B 1  314  ? 6.575   18.556  100.949 1.00 17.32 ? 312  ARG B NH2   1 
ATOM   11122 N  N     . LEU B 1  315  ? -0.212  13.004  97.226  1.00 14.25 ? 313  LEU B N     1 
ATOM   11123 C  CA    . LEU B 1  315  ? -1.200  11.978  97.522  1.00 16.61 ? 313  LEU B CA    1 
ATOM   11124 C  C     . LEU B 1  315  ? -0.662  10.588  97.203  1.00 16.68 ? 313  LEU B C     1 
ATOM   11125 O  O     . LEU B 1  315  ? -0.618  9.710   98.073  1.00 16.42 ? 313  LEU B O     1 
ATOM   11126 C  CB    . LEU B 1  315  ? -2.475  12.255  96.725  1.00 16.28 ? 313  LEU B CB    1 
ATOM   11127 C  CG    . LEU B 1  315  ? -3.780  11.684  97.266  1.00 15.86 ? 313  LEU B CG    1 
ATOM   11128 C  CD1   . LEU B 1  315  ? -4.920  12.170  96.350  1.00 16.85 ? 313  LEU B CD1   1 
ATOM   11129 C  CD2   . LEU B 1  315  ? -3.783  10.160  97.337  1.00 19.03 ? 313  LEU B CD2   1 
ATOM   11130 N  N     . GLU B 1  316  ? -0.280  10.360  95.945  1.00 16.53 ? 314  GLU B N     1 
ATOM   11131 C  CA    . GLU B 1  316  ? 0.034   8.994   95.552  1.00 16.53 ? 314  GLU B CA    1 
ATOM   11132 C  C     . GLU B 1  316  ? 1.345   8.537   96.166  1.00 17.91 ? 314  GLU B C     1 
ATOM   11133 O  O     . GLU B 1  316  ? 1.479   7.361   96.513  1.00 19.05 ? 314  GLU B O     1 
ATOM   11134 C  CB    . GLU B 1  316  ? 0.041   8.881   94.029  1.00 17.01 ? 314  GLU B CB    1 
ATOM   11135 C  CG    . GLU B 1  316  ? -1.375  9.037   93.487  1.00 18.47 ? 314  GLU B CG    1 
ATOM   11136 C  CD    . GLU B 1  316  ? -1.467  8.957   91.974  1.00 19.71 ? 314  GLU B CD    1 
ATOM   11137 O  OE1   . GLU B 1  316  ? -0.828  8.075   91.366  1.00 20.46 ? 314  GLU B OE1   1 
ATOM   11138 O  OE2   . GLU B 1  316  ? -2.209  9.763   91.395  1.00 20.83 ? 314  GLU B OE2   1 
ATOM   11139 N  N     . LEU B 1  317  ? 2.300   9.452   96.332  1.00 17.29 ? 315  LEU B N     1 
ATOM   11140 C  CA    . LEU B 1  317  ? 3.516   9.129   97.078  1.00 18.57 ? 315  LEU B CA    1 
ATOM   11141 C  C     . LEU B 1  317  ? 3.181   8.601   98.464  1.00 18.74 ? 315  LEU B C     1 
ATOM   11142 O  O     . LEU B 1  317  ? 3.756   7.606   98.917  1.00 18.96 ? 315  LEU B O     1 
ATOM   11143 C  CB    . LEU B 1  317  ? 4.409   10.361  97.188  1.00 16.84 ? 315  LEU B CB    1 
ATOM   11144 C  CG    . LEU B 1  317  ? 5.715   10.201  97.968  1.00 18.99 ? 315  LEU B CG    1 
ATOM   11145 C  CD1   . LEU B 1  317  ? 6.524   9.047   97.380  1.00 20.20 ? 315  LEU B CD1   1 
ATOM   11146 C  CD2   . LEU B 1  317  ? 6.502   11.495  97.914  1.00 18.91 ? 315  LEU B CD2   1 
ATOM   11147 N  N     . SER B 1  318  ? 2.243   9.253   99.158  1.00 16.50 ? 316  SER B N     1 
ATOM   11148 C  CA    . SER B 1  318  ? 1.927   8.806   100.508 1.00 17.67 ? 316  SER B CA    1 
ATOM   11149 C  C     . SER B 1  318  ? 1.373   7.382   100.512 1.00 16.88 ? 316  SER B C     1 
ATOM   11150 O  O     . SER B 1  318  ? 1.548   6.658   101.496 1.00 19.19 ? 316  SER B O     1 
ATOM   11151 C  CB    . SER B 1  318  ? 0.949   9.774   101.176 1.00 15.42 ? 316  SER B CB    1 
ATOM   11152 O  OG    . SER B 1  318  ? -0.352  9.650   100.637 1.00 16.63 ? 316  SER B OG    1 
ATOM   11153 N  N     . LEU B 1  319  ? 0.707   6.965   99.430  1.00 16.57 ? 317  LEU B N     1 
ATOM   11154 C  CA    . LEU B 1  319  ? 0.152   5.614   99.381  1.00 17.59 ? 317  LEU B CA    1 
ATOM   11155 C  C     . LEU B 1  319  ? 1.242   4.555   99.415  1.00 18.53 ? 317  LEU B C     1 
ATOM   11156 O  O     . LEU B 1  319  ? 1.025   3.458   99.941  1.00 19.26 ? 317  LEU B O     1 
ATOM   11157 C  CB    . LEU B 1  319  ? -0.699  5.443   98.125  1.00 16.84 ? 317  LEU B CB    1 
ATOM   11158 C  CG    . LEU B 1  319  ? -1.905  6.375   97.985  1.00 17.58 ? 317  LEU B CG    1 
ATOM   11159 C  CD1   . LEU B 1  319  ? -2.549  6.164   96.617  1.00 19.47 ? 317  LEU B CD1   1 
ATOM   11160 C  CD2   . LEU B 1  319  ? -2.930  6.125   99.092  1.00 18.38 ? 317  LEU B CD2   1 
ATOM   11161 N  N     . ASP B 1  320  ? 2.405   4.851   98.837  1.00 19.31 ? 318  ASP B N     1 
ATOM   11162 C  CA    . ASP B 1  320  ? 3.499   3.892   98.888  1.00 21.07 ? 318  ASP B CA    1 
ATOM   11163 C  C     . ASP B 1  320  ? 3.981   3.676   100.316 1.00 21.16 ? 318  ASP B C     1 
ATOM   11164 O  O     . ASP B 1  320  ? 4.414   2.572   100.662 1.00 21.54 ? 318  ASP B O     1 
ATOM   11165 C  CB    . ASP B 1  320  ? 4.636   4.362   97.991  1.00 18.05 ? 318  ASP B CB    1 
ATOM   11166 C  CG    . ASP B 1  320  ? 4.322   4.144   96.521  1.00 19.58 ? 318  ASP B CG    1 
ATOM   11167 O  OD1   . ASP B 1  320  ? 4.002   2.999   96.167  1.00 23.11 ? 318  ASP B OD1   1 
ATOM   11168 O  OD2   . ASP B 1  320  ? 4.356   5.113   95.740  1.00 22.22 ? 318  ASP B OD2   1 
ATOM   11169 N  N     . LEU B 1  321  ? 3.905   4.703   101.161 1.00 17.26 ? 319  LEU B N     1 
ATOM   11170 C  CA    . LEU B 1  321  ? 4.231   4.489   102.567 1.00 17.86 ? 319  LEU B CA    1 
ATOM   11171 C  C     . LEU B 1  321  ? 3.129   3.710   103.263 1.00 18.85 ? 319  LEU B C     1 
ATOM   11172 O  O     . LEU B 1  321  ? 3.409   2.804   104.058 1.00 20.02 ? 319  LEU B O     1 
ATOM   11173 C  CB    . LEU B 1  321  ? 4.472   5.824   103.273 1.00 20.53 ? 319  LEU B CB    1 
ATOM   11174 C  CG    . LEU B 1  321  ? 5.820   6.483   102.983 1.00 21.21 ? 319  LEU B CG    1 
ATOM   11175 C  CD1   . LEU B 1  321  ? 5.707   7.381   101.766 1.00 22.18 ? 319  LEU B CD1   1 
ATOM   11176 C  CD2   . LEU B 1  321  ? 6.301   7.264   104.191 1.00 22.12 ? 319  LEU B CD2   1 
ATOM   11177 N  N     . LEU B 1  322  ? 1.869   4.041   102.969 1.00 18.92 ? 320  LEU B N     1 
ATOM   11178 C  CA    . LEU B 1  322  ? 0.752   3.330   103.581 1.00 19.11 ? 320  LEU B CA    1 
ATOM   11179 C  C     . LEU B 1  322  ? 0.812   1.846   103.260 1.00 18.87 ? 320  LEU B C     1 
ATOM   11180 O  O     . LEU B 1  322  ? 0.545   1.002   104.125 1.00 21.91 ? 320  LEU B O     1 
ATOM   11181 C  CB    . LEU B 1  322  ? -0.570  3.908   103.087 1.00 19.13 ? 320  LEU B CB    1 
ATOM   11182 C  CG    . LEU B 1  322  ? -1.817  3.250   103.681 1.00 22.71 ? 320  LEU B CG    1 
ATOM   11183 C  CD1   . LEU B 1  322  ? -1.858  3.498   105.184 1.00 20.68 ? 320  LEU B CD1   1 
ATOM   11184 C  CD2   . LEU B 1  322  ? -3.053  3.783   102.994 1.00 22.43 ? 320  LEU B CD2   1 
ATOM   11185 N  N     . GLU B 1  323  ? 1.154   1.517   102.009 1.00 19.51 ? 321  GLU B N     1 
ATOM   11186 C  CA    . GLU B 1  323  ? 1.269   0.125   101.586 1.00 19.39 ? 321  GLU B CA    1 
ATOM   11187 C  C     . GLU B 1  323  ? 2.277   -0.629  102.439 1.00 22.26 ? 321  GLU B C     1 
ATOM   11188 O  O     . GLU B 1  323  ? 1.994   -1.723  102.936 1.00 23.17 ? 321  GLU B O     1 
ATOM   11189 C  CB    . GLU B 1  323  ? 1.670   0.069   100.109 1.00 21.08 ? 321  GLU B CB    1 
ATOM   11190 C  CG    . GLU B 1  323  ? 1.969   -1.324  99.583  1.00 26.00 ? 321  GLU B CG    1 
ATOM   11191 C  CD    . GLU B 1  323  ? 0.752   -2.001  98.978  1.00 27.68 ? 321  GLU B CD    1 
ATOM   11192 O  OE1   . GLU B 1  323  ? -0.259  -1.314  98.708  1.00 27.65 ? 321  GLU B OE1   1 
ATOM   11193 O  OE2   . GLU B 1  323  ? 0.797   -3.232  98.782  1.00 25.99 ? 321  GLU B OE2   1 
ATOM   11194 N  N     . VAL B 1  324  ? 3.469   -0.054  102.613 1.00 22.15 ? 322  VAL B N     1 
ATOM   11195 C  CA    . VAL B 1  324  ? 4.515   -0.735  103.368 1.00 21.99 ? 322  VAL B CA    1 
ATOM   11196 C  C     . VAL B 1  324  ? 4.086   -0.913  104.814 1.00 23.03 ? 322  VAL B C     1 
ATOM   11197 O  O     . VAL B 1  324  ? 4.260   -1.989  105.404 1.00 24.54 ? 322  VAL B O     1 
ATOM   11198 C  CB    . VAL B 1  324  ? 5.841   0.047   103.268 1.00 24.55 ? 322  VAL B CB    1 
ATOM   11199 C  CG1   . VAL B 1  324  ? 6.872   -0.538  104.221 1.00 23.80 ? 322  VAL B CG1   1 
ATOM   11200 C  CG2   . VAL B 1  324  ? 6.362   0.045   101.833 1.00 25.81 ? 322  VAL B CG2   1 
ATOM   11201 N  N     . LEU B 1  325  ? 3.529   0.140   105.418 1.00 20.17 ? 323  LEU B N     1 
ATOM   11202 C  CA    . LEU B 1  325  ? 3.137   0.050   106.822 1.00 22.66 ? 323  LEU B CA    1 
ATOM   11203 C  C     . LEU B 1  325  ? 2.080   -1.026  107.042 1.00 23.59 ? 323  LEU B C     1 
ATOM   11204 O  O     . LEU B 1  325  ? 2.140   -1.774  108.024 1.00 23.02 ? 323  LEU B O     1 
ATOM   11205 C  CB    . LEU B 1  325  ? 2.646   1.411   107.310 1.00 20.60 ? 323  LEU B CB    1 
ATOM   11206 C  CG    . LEU B 1  325  ? 3.741   2.483   107.307 1.00 21.23 ? 323  LEU B CG    1 
ATOM   11207 C  CD1   . LEU B 1  325  ? 3.144   3.872   107.449 1.00 19.86 ? 323  LEU B CD1   1 
ATOM   11208 C  CD2   . LEU B 1  325  ? 4.736   2.228   108.429 1.00 20.91 ? 323  LEU B CD2   1 
ATOM   11209 N  N     . CYS B 1  326  ? 1.104   -1.131  106.137 1.00 22.85 ? 324  CYS B N     1 
ATOM   11210 C  CA    . CYS B 1  326  ? 0.034   -2.100  106.346 1.00 23.45 ? 324  CYS B CA    1 
ATOM   11211 C  C     . CYS B 1  326  ? 0.507   -3.540  106.195 1.00 24.56 ? 324  CYS B C     1 
ATOM   11212 O  O     . CYS B 1  326  ? -0.107  -4.441  106.777 1.00 24.28 ? 324  CYS B O     1 
ATOM   11213 C  CB    . CYS B 1  326  ? -1.119  -1.815  105.386 1.00 24.75 ? 324  CYS B CB    1 
ATOM   11214 S  SG    . CYS B 1  326  ? -2.037  -0.332  105.844 1.00 24.66 ? 324  CYS B SG    1 
ATOM   11215 N  N     . LEU B 1  327  ? 1.588   -3.776  105.456 1.00 22.05 ? 325  LEU B N     1 
ATOM   11216 C  CA    . LEU B 1  327  ? 2.147   -5.112  105.293 1.00 26.33 ? 325  LEU B CA    1 
ATOM   11217 C  C     . LEU B 1  327  ? 3.279   -5.398  106.267 1.00 27.43 ? 325  LEU B C     1 
ATOM   11218 O  O     . LEU B 1  327  ? 3.882   -6.476  106.207 1.00 28.24 ? 325  LEU B O     1 
ATOM   11219 C  CB    . LEU B 1  327  ? 2.643   -5.287  103.856 1.00 23.86 ? 325  LEU B CB    1 
ATOM   11220 C  CG    . LEU B 1  327  ? 1.516   -5.129  102.831 1.00 25.93 ? 325  LEU B CG    1 
ATOM   11221 C  CD1   . LEU B 1  327  ? 2.070   -5.032  101.417 1.00 29.59 ? 325  LEU B CD1   1 
ATOM   11222 C  CD2   . LEU B 1  327  ? 0.523   -6.255  102.946 1.00 33.06 ? 325  LEU B CD2   1 
ATOM   11223 N  N     . ASP B 1  328  ? 3.574   -4.467  107.166 1.00 24.24 ? 326  ASP B N     1 
ATOM   11224 C  CA    . ASP B 1  328  ? 4.686   -4.616  108.101 1.00 26.86 ? 326  ASP B CA    1 
ATOM   11225 C  C     . ASP B 1  328  ? 4.232   -5.457  109.286 1.00 26.63 ? 326  ASP B C     1 
ATOM   11226 O  O     . ASP B 1  328  ? 3.389   -5.021  110.078 1.00 27.32 ? 326  ASP B O     1 
ATOM   11227 C  CB    . ASP B 1  328  ? 5.167   -3.242  108.550 1.00 24.85 ? 326  ASP B CB    1 
ATOM   11228 C  CG    . ASP B 1  328  ? 6.442   -3.301  109.373 1.00 30.04 ? 326  ASP B CG    1 
ATOM   11229 O  OD1   . ASP B 1  328  ? 6.732   -4.355  109.971 1.00 27.20 ? 326  ASP B OD1   1 
ATOM   11230 O  OD2   . ASP B 1  328  ? 7.153   -2.281  109.426 1.00 29.13 ? 326  ASP B OD2   1 
ATOM   11231 N  N     . GLY B 1  329  ? 4.803   -6.657  109.420 1.00 30.27 ? 327  GLY B N     1 
ATOM   11232 C  CA    . GLY B 1  329  ? 4.412   -7.567  110.482 1.00 26.30 ? 327  GLY B CA    1 
ATOM   11233 C  C     . GLY B 1  329  ? 4.647   -7.037  111.881 1.00 31.85 ? 327  GLY B C     1 
ATOM   11234 O  O     . GLY B 1  329  ? 3.985   -7.489  112.819 1.00 29.33 ? 327  GLY B O     1 
ATOM   11235 N  N     . ASP B 1  330  ? 5.570   -6.084  112.051 1.00 30.18 ? 328  ASP B N     1 
ATOM   11236 C  CA    . ASP B 1  330  ? 5.768   -5.498  113.374 1.00 26.75 ? 328  ASP B CA    1 
ATOM   11237 C  C     . ASP B 1  330  ? 4.509   -4.807  113.874 1.00 30.65 ? 328  ASP B C     1 
ATOM   11238 O  O     . ASP B 1  330  ? 4.323   -4.662  115.087 1.00 32.93 ? 328  ASP B O     1 
ATOM   11239 C  CB    . ASP B 1  330  ? 6.931   -4.504  113.354 1.00 28.91 ? 328  ASP B CB    1 
ATOM   11240 C  CG    . ASP B 1  330  ? 8.268   -5.176  113.154 1.00 30.21 ? 328  ASP B CG    1 
ATOM   11241 O  OD1   . ASP B 1  330  ? 8.339   -6.427  113.262 1.00 31.67 ? 328  ASP B OD1   1 
ATOM   11242 O  OD2   . ASP B 1  330  ? 9.251   -4.459  112.888 1.00 32.26 ? 328  ASP B OD2   1 
ATOM   11243 N  N     . LEU B 1  331  ? 3.632   -4.384  112.962 1.00 28.39 ? 329  LEU B N     1 
ATOM   11244 C  CA    . LEU B 1  331  ? 2.391   -3.719  113.318 1.00 28.00 ? 329  LEU B CA    1 
ATOM   11245 C  C     . LEU B 1  331  ? 1.210   -4.680  113.319 1.00 26.41 ? 329  LEU B C     1 
ATOM   11246 O  O     . LEU B 1  331  ? 0.060   -4.236  113.274 1.00 27.78 ? 329  LEU B O     1 
ATOM   11247 C  CB    . LEU B 1  331  ? 2.139   -2.547  112.367 1.00 27.70 ? 329  LEU B CB    1 
ATOM   11248 C  CG    . LEU B 1  331  ? 3.299   -1.548  112.312 1.00 28.49 ? 329  LEU B CG    1 
ATOM   11249 C  CD1   . LEU B 1  331  ? 3.076   -0.458  111.275 1.00 27.02 ? 329  LEU B CD1   1 
ATOM   11250 C  CD2   . LEU B 1  331  ? 3.523   -0.948  113.700 1.00 24.02 ? 329  LEU B CD2   1 
ATOM   11251 N  N     . SER B 1  332  ? 1.487   -5.984  113.389 1.00 28.01 ? 330  SER B N     1 
ATOM   11252 C  CA    . SER B 1  332  ? 0.472   -7.032  113.320 1.00 30.27 ? 330  SER B CA    1 
ATOM   11253 C  C     . SER B 1  332  ? -0.701  -6.779  114.261 1.00 32.62 ? 330  SER B C     1 
ATOM   11254 O  O     . SER B 1  332  ? -0.517  -6.540  115.458 1.00 33.24 ? 330  SER B O     1 
ATOM   11255 C  CB    . SER B 1  332  ? 1.117   -8.376  113.664 1.00 32.03 ? 330  SER B CB    1 
ATOM   11256 O  OG    . SER B 1  332  ? 0.151   -9.411  113.680 1.00 36.96 ? 330  SER B OG    1 
ATOM   11257 N  N     . GLY B 1  333  ? -1.913  -6.856  113.713 1.00 30.00 ? 331  GLY B N     1 
ATOM   11258 C  CA    . GLY B 1  333  ? -3.119  -6.779  114.514 1.00 33.27 ? 331  GLY B CA    1 
ATOM   11259 C  C     . GLY B 1  333  ? -3.501  -5.396  114.998 1.00 34.18 ? 331  GLY B C     1 
ATOM   11260 O  O     . GLY B 1  333  ? -4.498  -5.262  115.719 1.00 33.52 ? 331  GLY B O     1 
ATOM   11261 N  N     . TRP B 1  334  ? -2.753  -4.367  114.624 1.00 32.21 ? 332  TRP B N     1 
ATOM   11262 C  CA    . TRP B 1  334  ? -3.040  -2.999  115.038 1.00 32.43 ? 332  TRP B CA    1 
ATOM   11263 C  C     . TRP B 1  334  ? -3.990  -2.355  114.037 1.00 30.02 ? 332  TRP B C     1 
ATOM   11264 O  O     . TRP B 1  334  ? -3.682  -2.262  112.846 1.00 30.47 ? 332  TRP B O     1 
ATOM   11265 C  CB    . TRP B 1  334  ? -1.737  -2.217  115.146 1.00 30.10 ? 332  TRP B CB    1 
ATOM   11266 C  CG    . TRP B 1  334  ? -1.853  -0.749  115.463 1.00 27.83 ? 332  TRP B CG    1 
ATOM   11267 C  CD1   . TRP B 1  334  ? -2.472  -0.174  116.546 1.00 27.15 ? 332  TRP B CD1   1 
ATOM   11268 C  CD2   . TRP B 1  334  ? -1.271  0.324   114.719 1.00 28.13 ? 332  TRP B CD2   1 
ATOM   11269 N  NE1   . TRP B 1  334  ? -2.324  1.202   116.497 1.00 26.47 ? 332  TRP B NE1   1 
ATOM   11270 C  CE2   . TRP B 1  334  ? -1.595  1.525   115.383 1.00 24.91 ? 332  TRP B CE2   1 
ATOM   11271 C  CE3   . TRP B 1  334  ? -0.522  0.388   113.538 1.00 25.02 ? 332  TRP B CE3   1 
ATOM   11272 C  CZ2   . TRP B 1  334  ? -1.189  2.772   114.904 1.00 24.21 ? 332  TRP B CZ2   1 
ATOM   11273 C  CZ3   . TRP B 1  334  ? -0.122  1.622   113.068 1.00 29.62 ? 332  TRP B CZ3   1 
ATOM   11274 C  CH2   . TRP B 1  334  ? -0.455  2.798   113.752 1.00 26.98 ? 332  TRP B CH2   1 
ATOM   11275 N  N     . ASN B 1  335  ? -5.152  -1.923  114.508 1.00 29.29 ? 333  ASN B N     1 
ATOM   11276 C  CA    . ASN B 1  335  ? -6.115  -1.276  113.632 1.00 26.96 ? 333  ASN B CA    1 
ATOM   11277 C  C     . ASN B 1  335  ? -6.080  0.238   113.757 1.00 27.06 ? 333  ASN B C     1 
ATOM   11278 O  O     . ASN B 1  335  ? -7.003  0.919   113.296 1.00 27.90 ? 333  ASN B O     1 
ATOM   11279 C  CB    . ASN B 1  335  ? -7.511  -1.819  113.912 1.00 28.77 ? 333  ASN B CB    1 
ATOM   11280 C  CG    . ASN B 1  335  ? -7.620  -3.280  113.562 1.00 34.03 ? 333  ASN B CG    1 
ATOM   11281 O  OD1   . ASN B 1  335  ? -6.936  -3.750  112.654 1.00 29.89 ? 333  ASN B OD1   1 
ATOM   11282 N  ND2   . ASN B 1  335  ? -8.457  -4.012  114.288 1.00 31.99 ? 333  ASN B ND2   1 
ATOM   11283 N  N     . GLY B 1  336  ? -5.027  0.774   114.358 1.00 27.90 ? 334  GLY B N     1 
ATOM   11284 C  CA    . GLY B 1  336  ? -4.919  2.199   114.562 1.00 27.27 ? 334  GLY B CA    1 
ATOM   11285 C  C     . GLY B 1  336  ? -4.241  2.972   113.461 1.00 25.73 ? 334  GLY B C     1 
ATOM   11286 O  O     . GLY B 1  336  ? -4.170  4.200   113.553 1.00 25.40 ? 334  GLY B O     1 
ATOM   11287 N  N     . MET B 1  337  ? -3.735  2.309   112.422 1.00 25.95 ? 335  MET B N     1 
ATOM   11288 C  CA    . MET B 1  337  ? -3.189  3.046   111.285 1.00 24.32 ? 335  MET B CA    1 
ATOM   11289 C  C     . MET B 1  337  ? -4.297  3.850   110.622 1.00 26.24 ? 335  MET B C     1 
ATOM   11290 O  O     . MET B 1  337  ? -5.325  3.289   110.218 1.00 26.02 ? 335  MET B O     1 
ATOM   11291 C  CB    . MET B 1  337  ? -2.552  2.095   110.276 1.00 27.16 ? 335  MET B CB    1 
ATOM   11292 C  CG    . MET B 1  337  ? -1.911  2.827   109.109 1.00 29.89 ? 335  MET B CG    1 
ATOM   11293 S  SD    . MET B 1  337  ? -0.348  3.552   109.621 1.00 33.86 ? 335  MET B SD    1 
ATOM   11294 C  CE    . MET B 1  337  ? -0.575  5.264   109.151 1.00 30.08 ? 335  MET B CE    1 
ATOM   11295 N  N     . GLY B 1  338  ? -4.091  5.161   110.526 1.00 22.67 ? 336  GLY B N     1 
ATOM   11296 C  CA    . GLY B 1  338  ? -5.084  6.065   109.982 1.00 23.48 ? 336  GLY B CA    1 
ATOM   11297 C  C     . GLY B 1  338  ? -4.560  6.811   108.770 1.00 22.85 ? 336  GLY B C     1 
ATOM   11298 O  O     . GLY B 1  338  ? -3.355  6.997   108.609 1.00 22.43 ? 336  GLY B O     1 
ATOM   11299 N  N     . PHE B 1  339  ? -5.481  7.249   107.919 1.00 20.25 ? 337  PHE B N     1 
ATOM   11300 C  CA    . PHE B 1  339  ? -5.078  7.871   106.669 1.00 19.67 ? 337  PHE B CA    1 
ATOM   11301 C  C     . PHE B 1  339  ? -6.180  8.808   106.208 1.00 22.69 ? 337  PHE B C     1 
ATOM   11302 O  O     . PHE B 1  339  ? -7.350  8.418   106.169 1.00 24.26 ? 337  PHE B O     1 
ATOM   11303 C  CB    . PHE B 1  339  ? -4.799  6.791   105.615 1.00 18.71 ? 337  PHE B CB    1 
ATOM   11304 C  CG    . PHE B 1  339  ? -4.075  7.285   104.397 1.00 19.17 ? 337  PHE B CG    1 
ATOM   11305 C  CD1   . PHE B 1  339  ? -2.693  7.348   104.371 1.00 21.38 ? 337  PHE B CD1   1 
ATOM   11306 C  CD2   . PHE B 1  339  ? -4.773  7.643   103.259 1.00 18.06 ? 337  PHE B CD2   1 
ATOM   11307 C  CE1   . PHE B 1  339  ? -2.027  7.800   103.226 1.00 21.32 ? 337  PHE B CE1   1 
ATOM   11308 C  CE2   . PHE B 1  339  ? -4.108  8.084   102.112 1.00 19.12 ? 337  PHE B CE2   1 
ATOM   11309 C  CZ    . PHE B 1  339  ? -2.740  8.161   102.106 1.00 20.61 ? 337  PHE B CZ    1 
ATOM   11310 N  N     . VAL B 1  340  ? -5.810  10.022  105.862 1.00 20.28 ? 338  VAL B N     1 
ATOM   11311 C  CA    . VAL B 1  340  ? -6.752  11.041  105.409 1.00 18.43 ? 338  VAL B CA    1 
ATOM   11312 C  C     . VAL B 1  340  ? -6.909  10.963  103.897 1.00 21.09 ? 338  VAL B C     1 
ATOM   11313 O  O     . VAL B 1  340  ? -5.929  10.793  103.164 1.00 19.01 ? 338  VAL B O     1 
ATOM   11314 C  CB    . VAL B 1  340  ? -6.267  12.440  105.829 1.00 21.81 ? 338  VAL B CB    1 
ATOM   11315 C  CG1   . VAL B 1  340  ? -7.154  13.524  105.228 1.00 21.63 ? 338  VAL B CG1   1 
ATOM   11316 C  CG2   . VAL B 1  340  ? -6.205  12.558  107.338 1.00 21.55 ? 338  VAL B CG2   1 
ATOM   11317 N  N     . VAL B 1  341  ? -8.143  11.119  103.424 1.00 19.28 ? 339  VAL B N     1 
ATOM   11318 C  CA    . VAL B 1  341  ? -8.422  11.298  102.010 1.00 18.01 ? 339  VAL B CA    1 
ATOM   11319 C  C     . VAL B 1  341  ? -9.274  12.547  101.860 1.00 18.97 ? 339  VAL B C     1 
ATOM   11320 O  O     . VAL B 1  341  ? -10.147 12.819  102.692 1.00 21.68 ? 339  VAL B O     1 
ATOM   11321 C  CB    . VAL B 1  341  ? -9.111  10.066  101.384 1.00 22.66 ? 339  VAL B CB    1 
ATOM   11322 C  CG1   . VAL B 1  341  ? -8.191  8.866   101.457 1.00 22.59 ? 339  VAL B CG1   1 
ATOM   11323 C  CG2   . VAL B 1  341  ? -10.438 9.765   102.075 1.00 25.08 ? 339  VAL B CG2   1 
ATOM   11324 N  N     . GLN B 1  342  ? -8.991  13.313  100.814 1.00 19.07 ? 340  GLN B N     1 
ATOM   11325 C  CA    . GLN B 1  342  ? -9.554  14.643  100.596 1.00 18.90 ? 340  GLN B CA    1 
ATOM   11326 C  C     . GLN B 1  342  ? -10.651 14.556  99.542  1.00 21.89 ? 340  GLN B C     1 
ATOM   11327 O  O     . GLN B 1  342  ? -10.373 14.283  98.368  1.00 20.25 ? 340  GLN B O     1 
ATOM   11328 C  CB    . GLN B 1  342  ? -8.459  15.615  100.163 1.00 17.53 ? 340  GLN B CB    1 
ATOM   11329 C  CG    . GLN B 1  342  ? -7.422  15.832  101.237 1.00 17.08 ? 340  GLN B CG    1 
ATOM   11330 C  CD    . GLN B 1  342  ? -6.050  16.164  100.661 1.00 16.41 ? 340  GLN B CD    1 
ATOM   11331 O  OE1   . GLN B 1  342  ? -5.593  15.518  99.717  1.00 18.16 ? 340  GLN B OE1   1 
ATOM   11332 N  NE2   . GLN B 1  342  ? -5.387  17.176  101.230 1.00 16.53 ? 340  GLN B NE2   1 
ATOM   11333 N  N     . ALA B 1  343  ? -11.892 14.809  99.967  1.00 18.39 ? 341  ALA B N     1 
ATOM   11334 C  CA    . ALA B 1  343  ? -13.040 14.708  99.072  1.00 20.62 ? 341  ALA B CA    1 
ATOM   11335 C  C     . ALA B 1  343  ? -13.040 15.771  97.985  1.00 20.00 ? 341  ALA B C     1 
ATOM   11336 O  O     . ALA B 1  343  ? -13.711 15.582  96.960  1.00 20.31 ? 341  ALA B O     1 
ATOM   11337 C  CB    . ALA B 1  343  ? -14.335 14.794  99.879  1.00 23.25 ? 341  ALA B CB    1 
ATOM   11338 N  N     . TYR B 1  344  ? -12.317 16.884  98.166  1.00 20.47 ? 342  TYR B N     1 
ATOM   11339 C  CA    . TYR B 1  344  ? -12.263 17.837  97.062  1.00 19.28 ? 342  TYR B CA    1 
ATOM   11340 C  C     . TYR B 1  344  ? -11.368 17.360  95.929  1.00 16.99 ? 342  TYR B C     1 
ATOM   11341 O  O     . TYR B 1  344  ? -11.278 18.049  94.909  1.00 18.05 ? 342  TYR B O     1 
ATOM   11342 C  CB    . TYR B 1  344  ? -11.848 19.245  97.542  1.00 19.34 ? 342  TYR B CB    1 
ATOM   11343 C  CG    . TYR B 1  344  ? -10.392 19.526  97.937  1.00 19.89 ? 342  TYR B CG    1 
ATOM   11344 C  CD1   . TYR B 1  344  ? -9.425  18.524  98.005  1.00 19.37 ? 342  TYR B CD1   1 
ATOM   11345 C  CD2   . TYR B 1  344  ? -9.998  20.834  98.246  1.00 17.98 ? 342  TYR B CD2   1 
ATOM   11346 C  CE1   . TYR B 1  344  ? -8.099  18.830  98.372  1.00 16.81 ? 342  TYR B CE1   1 
ATOM   11347 C  CE2   . TYR B 1  344  ? -8.698  21.142  98.622  1.00 17.65 ? 342  TYR B CE2   1 
ATOM   11348 C  CZ    . TYR B 1  344  ? -7.753  20.146  98.681  1.00 18.41 ? 342  TYR B CZ    1 
ATOM   11349 O  OH    . TYR B 1  344  ? -6.467  20.488  99.071  1.00 17.11 ? 342  TYR B OH    1 
ATOM   11350 N  N     . GLY B 1  345  ? -10.745 16.194  96.074  1.00 18.55 ? 343  GLY B N     1 
ATOM   11351 C  CA    . GLY B 1  345  ? -9.832  15.663  95.081  1.00 19.33 ? 343  GLY B CA    1 
ATOM   11352 C  C     . GLY B 1  345  ? -10.536 14.687  94.157  1.00 18.63 ? 343  GLY B C     1 
ATOM   11353 O  O     . GLY B 1  345  ? -11.345 13.873  94.591  1.00 19.49 ? 343  GLY B O     1 
ATOM   11354 N  N     . LYS B 1  346  ? -10.190 14.773  92.878  1.00 18.25 ? 344  LYS B N     1 
ATOM   11355 C  CA    . LYS B 1  346  ? -10.825 13.949  91.863  1.00 19.64 ? 344  LYS B CA    1 
ATOM   11356 C  C     . LYS B 1  346  ? -10.494 12.472  92.006  1.00 20.16 ? 344  LYS B C     1 
ATOM   11357 O  O     . LYS B 1  346  ? -11.256 11.626  91.519  1.00 20.28 ? 344  LYS B O     1 
ATOM   11358 C  CB    . LYS B 1  346  ? -10.410 14.438  90.484  1.00 19.07 ? 344  LYS B CB    1 
ATOM   11359 C  CG    . LYS B 1  346  ? -10.962 15.804  90.172  1.00 18.38 ? 344  LYS B CG    1 
ATOM   11360 C  CD    . LYS B 1  346  ? -10.460 16.311  88.842  1.00 19.42 ? 344  LYS B CD    1 
ATOM   11361 C  CE    . LYS B 1  346  ? -11.136 17.631  88.486  1.00 19.27 ? 344  LYS B CE    1 
ATOM   11362 N  NZ    . LYS B 1  346  ? -10.513 18.254  87.269  1.00 19.24 ? 344  LYS B NZ    1 
ATOM   11363 N  N     . ARG B 1  347  ? -9.388  12.143  92.651  1.00 19.55 ? 345  ARG B N     1 
ATOM   11364 C  CA    . ARG B 1  347  ? -9.018  10.748  92.812  1.00 21.43 ? 345  ARG B CA    1 
ATOM   11365 C  C     . ARG B 1  347  ? -9.642  10.105  94.038  1.00 20.06 ? 345  ARG B C     1 
ATOM   11366 O  O     . ARG B 1  347  ? -9.498  8.891   94.213  1.00 20.83 ? 345  ARG B O     1 
ATOM   11367 C  CB    . ARG B 1  347  ? -7.498  10.627  92.867  1.00 17.26 ? 345  ARG B CB    1 
ATOM   11368 C  CG    . ARG B 1  347  ? -6.844  11.067  91.576  1.00 16.37 ? 345  ARG B CG    1 
ATOM   11369 C  CD    . ARG B 1  347  ? -5.351  11.321  91.765  1.00 17.60 ? 345  ARG B CD    1 
ATOM   11370 N  NE    . ARG B 1  347  ? -5.081  12.572  92.472  1.00 16.15 ? 345  ARG B NE    1 
ATOM   11371 C  CZ    . ARG B 1  347  ? -3.898  12.914  92.954  1.00 17.49 ? 345  ARG B CZ    1 
ATOM   11372 N  NH1   . ARG B 1  347  ? -2.833  12.139  92.784  1.00 16.53 ? 345  ARG B NH1   1 
ATOM   11373 N  NH2   . ARG B 1  347  ? -3.773  14.069  93.610  1.00 14.81 ? 345  ARG B NH2   1 
ATOM   11374 N  N     . CYS B 1  348  ? -10.348 10.881  94.864  1.00 19.26 ? 346  CYS B N     1 
ATOM   11375 C  CA    . CYS B 1  348  ? -10.779 10.414  96.183  1.00 20.77 ? 346  CYS B CA    1 
ATOM   11376 C  C     . CYS B 1  348  ? -11.492 9.064   96.169  1.00 22.21 ? 346  CYS B C     1 
ATOM   11377 O  O     . CYS B 1  348  ? -11.078 8.175   96.926  1.00 21.68 ? 346  CYS B O     1 
ATOM   11378 C  CB    . CYS B 1  348  ? -11.642 11.495  96.848  1.00 18.60 ? 346  CYS B CB    1 
ATOM   11379 S  SG    . CYS B 1  348  ? -11.923 11.200  98.641  1.00 24.30 ? 346  CYS B SG    1 
ATOM   11380 N  N     . PRO B 1  349  ? -12.535 8.826   95.359  1.00 21.43 ? 347  PRO B N     1 
ATOM   11381 C  CA    . PRO B 1  349  ? -13.175 7.502   95.405  1.00 23.44 ? 347  PRO B CA    1 
ATOM   11382 C  C     . PRO B 1  349  ? -12.246 6.377   94.994  1.00 21.70 ? 347  PRO B C     1 
ATOM   11383 O  O     . PRO B 1  349  ? -12.339 5.276   95.554  1.00 22.52 ? 347  PRO B O     1 
ATOM   11384 C  CB    . PRO B 1  349  ? -14.361 7.643   94.437  1.00 22.17 ? 347  PRO B CB    1 
ATOM   11385 C  CG    . PRO B 1  349  ? -14.045 8.788   93.583  1.00 23.21 ? 347  PRO B CG    1 
ATOM   11386 C  CD    . PRO B 1  349  ? -13.181 9.715   94.373  1.00 21.30 ? 347  PRO B CD    1 
ATOM   11387 N  N     . PHE B 1  350  ? -11.342 6.628   94.048  1.00 22.92 ? 348  PHE B N     1 
ATOM   11388 C  CA    . PHE B 1  350  ? -10.403 5.600   93.612  1.00 22.61 ? 348  PHE B CA    1 
ATOM   11389 C  C     . PHE B 1  350  ? -9.335  5.338   94.668  1.00 22.48 ? 348  PHE B C     1 
ATOM   11390 O  O     . PHE B 1  350  ? -8.901  4.191   94.842  1.00 22.29 ? 348  PHE B O     1 
ATOM   11391 C  CB    . PHE B 1  350  ? -9.800  6.020   92.273  1.00 20.75 ? 348  PHE B CB    1 
ATOM   11392 C  CG    . PHE B 1  350  ? -10.841 6.405   91.272  1.00 23.14 ? 348  PHE B CG    1 
ATOM   11393 C  CD1   . PHE B 1  350  ? -11.550 5.425   90.594  1.00 26.39 ? 348  PHE B CD1   1 
ATOM   11394 C  CD2   . PHE B 1  350  ? -11.151 7.738   91.045  1.00 22.35 ? 348  PHE B CD2   1 
ATOM   11395 C  CE1   . PHE B 1  350  ? -12.545 5.766   89.689  1.00 26.70 ? 348  PHE B CE1   1 
ATOM   11396 C  CE2   . PHE B 1  350  ? -12.151 8.087   90.137  1.00 25.04 ? 348  PHE B CE2   1 
ATOM   11397 C  CZ    . PHE B 1  350  ? -12.838 7.102   89.458  1.00 24.20 ? 348  PHE B CZ    1 
ATOM   11398 N  N     . VAL B 1  351  ? -8.937  6.375   95.405  1.00 20.10 ? 349  VAL B N     1 
ATOM   11399 C  CA    . VAL B 1  351  ? -8.036  6.191   96.546  1.00 20.16 ? 349  VAL B CA    1 
ATOM   11400 C  C     . VAL B 1  351  ? -8.709  5.353   97.631  1.00 21.66 ? 349  VAL B C     1 
ATOM   11401 O  O     . VAL B 1  351  ? -8.090  4.460   98.219  1.00 23.43 ? 349  VAL B O     1 
ATOM   11402 C  CB    . VAL B 1  351  ? -7.585  7.558   97.085  1.00 19.75 ? 349  VAL B CB    1 
ATOM   11403 C  CG1   . VAL B 1  351  ? -6.718  7.386   98.355  1.00 20.66 ? 349  VAL B CG1   1 
ATOM   11404 C  CG2   . VAL B 1  351  ? -6.799  8.324   96.015  1.00 19.79 ? 349  VAL B CG2   1 
ATOM   11405 N  N     . LEU B 1  352  ? -9.986  5.624   97.909  1.00 20.98 ? 350  LEU B N     1 
ATOM   11406 C  CA    . LEU B 1  352  ? -10.724 4.805   98.865  1.00 20.87 ? 350  LEU B CA    1 
ATOM   11407 C  C     . LEU B 1  352  ? -10.797 3.352   98.410  1.00 22.18 ? 350  LEU B C     1 
ATOM   11408 O  O     . LEU B 1  352  ? -10.630 2.435   99.221  1.00 22.28 ? 350  LEU B O     1 
ATOM   11409 C  CB    . LEU B 1  352  ? -12.126 5.371   99.068  1.00 23.14 ? 350  LEU B CB    1 
ATOM   11410 C  CG    . LEU B 1  352  ? -12.211 6.694   99.832  1.00 25.99 ? 350  LEU B CG    1 
ATOM   11411 C  CD1   . LEU B 1  352  ? -13.641 7.164   99.900  1.00 25.55 ? 350  LEU B CD1   1 
ATOM   11412 C  CD2   . LEU B 1  352  ? -11.654 6.513   101.243 1.00 26.14 ? 350  LEU B CD2   1 
ATOM   11413 N  N     . ASP B 1  353  ? -11.038 3.124   97.113  1.00 23.26 ? 351  ASP B N     1 
ATOM   11414 C  CA    . ASP B 1  353  ? -11.008 1.764   96.583  1.00 24.67 ? 351  ASP B CA    1 
ATOM   11415 C  C     . ASP B 1  353  ? -9.671  1.099   96.865  1.00 25.89 ? 351  ASP B C     1 
ATOM   11416 O  O     . ASP B 1  353  ? -9.622  -0.078  97.245  1.00 24.57 ? 351  ASP B O     1 
ATOM   11417 C  CB    . ASP B 1  353  ? -11.269 1.769   95.075  1.00 26.37 ? 351  ASP B CB    1 
ATOM   11418 C  CG    . ASP B 1  353  ? -12.718 2.066   94.728  1.00 27.85 ? 351  ASP B CG    1 
ATOM   11419 O  OD1   . ASP B 1  353  ? -13.594 1.860   95.588  1.00 27.21 ? 351  ASP B OD1   1 
ATOM   11420 O  OD2   . ASP B 1  353  ? -12.974 2.505   93.586  1.00 29.95 ? 351  ASP B OD2   1 
ATOM   11421 N  N     . PHE B 1  354  ? -8.577  1.836   96.665  1.00 23.49 ? 352  PHE B N     1 
ATOM   11422 C  CA    . PHE B 1  354  ? -7.251  1.293   96.933  1.00 23.05 ? 352  PHE B CA    1 
ATOM   11423 C  C     . PHE B 1  354  ? -7.075  0.978   98.413  1.00 23.00 ? 352  PHE B C     1 
ATOM   11424 O  O     . PHE B 1  354  ? -6.551  -0.084  98.768  1.00 24.22 ? 352  PHE B O     1 
ATOM   11425 C  CB    . PHE B 1  354  ? -6.168  2.269   96.464  1.00 22.38 ? 352  PHE B CB    1 
ATOM   11426 C  CG    . PHE B 1  354  ? -4.793  1.928   96.978  1.00 20.98 ? 352  PHE B CG    1 
ATOM   11427 C  CD1   . PHE B 1  354  ? -4.002  1.002   96.315  1.00 23.43 ? 352  PHE B CD1   1 
ATOM   11428 C  CD2   . PHE B 1  354  ? -4.309  2.510   98.144  1.00 21.45 ? 352  PHE B CD2   1 
ATOM   11429 C  CE1   . PHE B 1  354  ? -2.739  0.673   96.797  1.00 21.18 ? 352  PHE B CE1   1 
ATOM   11430 C  CE2   . PHE B 1  354  ? -3.057  2.177   98.634  1.00 23.19 ? 352  PHE B CE2   1 
ATOM   11431 C  CZ    . PHE B 1  354  ? -2.275  1.258   97.959  1.00 24.33 ? 352  PHE B CZ    1 
ATOM   11432 N  N     . ILE B 1  355  ? -7.520  1.886   99.289  1.00 22.50 ? 353  ILE B N     1 
ATOM   11433 C  CA    . ILE B 1  355  ? -7.345  1.689   100.729 1.00 22.16 ? 353  ILE B CA    1 
ATOM   11434 C  C     . ILE B 1  355  ? -8.200  0.530   101.217 1.00 24.33 ? 353  ILE B C     1 
ATOM   11435 O  O     . ILE B 1  355  ? -7.749  -0.299  102.017 1.00 23.14 ? 353  ILE B O     1 
ATOM   11436 C  CB    . ILE B 1  355  ? -7.672  2.988   101.491 1.00 23.36 ? 353  ILE B CB    1 
ATOM   11437 C  CG1   . ILE B 1  355  ? -6.658  4.080   101.131 1.00 23.21 ? 353  ILE B CG1   1 
ATOM   11438 C  CG2   . ILE B 1  355  ? -7.753  2.725   103.016 1.00 24.10 ? 353  ILE B CG2   1 
ATOM   11439 C  CD1   . ILE B 1  355  ? -7.032  5.453   101.650 1.00 20.87 ? 353  ILE B CD1   1 
ATOM   11440 N  N     . ILE B 1  356  ? -9.442  0.442   100.737 1.00 22.29 ? 354  ILE B N     1 
ATOM   11441 C  CA    . ILE B 1  356  ? -10.316 -0.639  101.179 1.00 25.21 ? 354  ILE B CA    1 
ATOM   11442 C  C     . ILE B 1  356  ? -9.741  -1.980  100.756 1.00 25.03 ? 354  ILE B C     1 
ATOM   11443 O  O     . ILE B 1  356  ? -9.778  -2.957  101.514 1.00 26.69 ? 354  ILE B O     1 
ATOM   11444 C  CB    . ILE B 1  356  ? -11.743 -0.435  100.638 1.00 25.34 ? 354  ILE B CB    1 
ATOM   11445 C  CG1   . ILE B 1  356  ? -12.425 0.728   101.359 1.00 28.02 ? 354  ILE B CG1   1 
ATOM   11446 C  CG2   . ILE B 1  356  ? -12.563 -1.702  100.811 1.00 27.73 ? 354  ILE B CG2   1 
ATOM   11447 C  CD1   . ILE B 1  356  ? -13.654 1.259   100.650 1.00 24.36 ? 354  ILE B CD1   1 
ATOM   11448 N  N     . ASP B 1  357  ? -9.194  -2.049  99.543  1.00 25.49 ? 355  ASP B N     1 
ATOM   11449 C  CA    . ASP B 1  357  ? -8.565  -3.286  99.095  1.00 26.43 ? 355  ASP B CA    1 
ATOM   11450 C  C     . ASP B 1  357  ? -7.314  -3.593  99.909  1.00 24.06 ? 355  ASP B C     1 
ATOM   11451 O  O     . ASP B 1  357  ? -7.077  -4.750  100.279 1.00 23.46 ? 355  ASP B O     1 
ATOM   11452 C  CB    . ASP B 1  357  ? -8.221  -3.198  97.611  1.00 25.96 ? 355  ASP B CB    1 
ATOM   11453 C  CG    . ASP B 1  357  ? -7.388  -4.368  97.147  1.00 25.80 ? 355  ASP B CG    1 
ATOM   11454 O  OD1   . ASP B 1  357  ? -7.948  -5.484  97.016  1.00 27.47 ? 355  ASP B OD1   1 
ATOM   11455 O  OD2   . ASP B 1  357  ? -6.172  -4.177  96.943  1.00 25.27 ? 355  ASP B OD2   1 
ATOM   11456 N  N     . LEU B 1  358  ? -6.502  -2.570  100.196 1.00 24.52 ? 356  LEU B N     1 
ATOM   11457 C  CA    . LEU B 1  358  ? -5.315  -2.770  101.021 1.00 23.59 ? 356  LEU B CA    1 
ATOM   11458 C  C     . LEU B 1  358  ? -5.694  -3.288  102.399 1.00 23.86 ? 356  LEU B C     1 
ATOM   11459 O  O     . LEU B 1  358  ? -5.049  -4.200  102.926 1.00 23.87 ? 356  LEU B O     1 
ATOM   11460 C  CB    . LEU B 1  358  ? -4.523  -1.466  101.139 1.00 22.15 ? 356  LEU B CB    1 
ATOM   11461 C  CG    . LEU B 1  358  ? -3.295  -1.452  102.075 1.00 21.38 ? 356  LEU B CG    1 
ATOM   11462 C  CD1   . LEU B 1  358  ? -2.279  -2.500  101.663 1.00 23.93 ? 356  LEU B CD1   1 
ATOM   11463 C  CD2   . LEU B 1  358  ? -2.643  -0.065  102.071 1.00 20.04 ? 356  LEU B CD2   1 
ATOM   11464 N  N     . ALA B 1  359  ? -6.748  -2.724  102.993 1.00 22.57 ? 357  ALA B N     1 
ATOM   11465 C  CA    . ALA B 1  359  ? -7.205  -3.204  104.290 1.00 23.35 ? 357  ALA B CA    1 
ATOM   11466 C  C     . ALA B 1  359  ? -7.582  -4.674  104.218 1.00 26.36 ? 357  ALA B C     1 
ATOM   11467 O  O     . ALA B 1  359  ? -7.189  -5.474  105.074 1.00 25.48 ? 357  ALA B O     1 
ATOM   11468 C  CB    . ALA B 1  359  ? -8.395  -2.375  104.768 1.00 27.18 ? 357  ALA B CB    1 
ATOM   11469 N  N     . ARG B 1  360  ? -8.343  -5.044  103.182 1.00 25.15 ? 358  ARG B N     1 
ATOM   11470 C  CA    . ARG B 1  360  ? -8.800  -6.422  103.034 1.00 26.66 ? 358  ARG B CA    1 
ATOM   11471 C  C     . ARG B 1  360  ? -7.634  -7.391  102.923 1.00 23.41 ? 358  ARG B C     1 
ATOM   11472 O  O     . ARG B 1  360  ? -7.625  -8.443  103.571 1.00 26.69 ? 358  ARG B O     1 
ATOM   11473 C  CB    . ARG B 1  360  ? -9.696  -6.538  101.807 1.00 27.54 ? 358  ARG B CB    1 
ATOM   11474 C  CG    . ARG B 1  360  ? -11.097 -6.065  102.037 1.00 31.43 ? 358  ARG B CG    1 
ATOM   11475 C  CD    . ARG B 1  360  ? -11.996 -6.556  100.920 1.00 37.43 ? 358  ARG B CD    1 
ATOM   11476 N  NE    . ARG B 1  360  ? -13.287 -5.886  100.942 1.00 38.33 ? 358  ARG B NE    1 
ATOM   11477 C  CZ    . ARG B 1  360  ? -13.639 -4.929  100.095 1.00 39.09 ? 358  ARG B CZ    1 
ATOM   11478 N  NH1   . ARG B 1  360  ? -12.824 -4.522  99.134  1.00 44.99 ? 358  ARG B NH1   1 
ATOM   11479 N  NH2   . ARG B 1  360  ? -14.838 -4.369  100.213 1.00 46.64 ? 358  ARG B NH2   1 
ATOM   11480 N  N     . ARG B 1  361  ? -6.653  -7.071  102.085 1.00 26.88 ? 359  ARG B N     1 
ATOM   11481 C  CA    . ARG B 1  361  ? -5.614  -8.055  101.823 1.00 28.13 ? 359  ARG B CA    1 
ATOM   11482 C  C     . ARG B 1  361  ? -4.522  -8.055  102.883 1.00 24.72 ? 359  ARG B C     1 
ATOM   11483 O  O     . ARG B 1  361  ? -3.784  -9.036  102.983 1.00 26.05 ? 359  ARG B O     1 
ATOM   11484 C  CB    . ARG B 1  361  ? -5.019  -7.842  100.428 1.00 30.58 ? 359  ARG B CB    1 
ATOM   11485 C  CG    . ARG B 1  361  ? -4.271  -6.551  100.232 1.00 31.32 ? 359  ARG B CG    1 
ATOM   11486 C  CD    . ARG B 1  361  ? -3.918  -6.364  98.749  1.00 27.64 ? 359  ARG B CD    1 
ATOM   11487 N  NE    . ARG B 1  361  ? -3.740  -4.952  98.425  1.00 25.45 ? 359  ARG B NE    1 
ATOM   11488 C  CZ    . ARG B 1  361  ? -2.585  -4.302  98.470  1.00 26.08 ? 359  ARG B CZ    1 
ATOM   11489 N  NH1   . ARG B 1  361  ? -1.466  -4.901  98.832  1.00 26.06 ? 359  ARG B NH1   1 
ATOM   11490 N  NH2   . ARG B 1  361  ? -2.555  -3.010  98.144  1.00 24.06 ? 359  ARG B NH2   1 
ATOM   11491 N  N     . SER B 1  362  ? -4.422  -7.009  103.701 1.00 24.89 ? 360  SER B N     1 
ATOM   11492 C  CA    . SER B 1  362  ? -3.421  -6.982  104.760 1.00 25.14 ? 360  SER B CA    1 
ATOM   11493 C  C     . SER B 1  362  ? -3.971  -7.372  106.123 1.00 24.64 ? 360  SER B C     1 
ATOM   11494 O  O     . SER B 1  362  ? -3.189  -7.502  107.073 1.00 28.26 ? 360  SER B O     1 
ATOM   11495 C  CB    . SER B 1  362  ? -2.801  -5.586  104.859 1.00 27.29 ? 360  SER B CB    1 
ATOM   11496 O  OG    . SER B 1  362  ? -3.777  -4.658  105.285 1.00 23.77 ? 360  SER B OG    1 
ATOM   11497 N  N     . GLY B 1  363  ? -5.282  -7.507  106.266 1.00 23.99 ? 361  GLY B N     1 
ATOM   11498 C  CA    . GLY B 1  363  ? -5.832  -7.882  107.560 1.00 25.85 ? 361  GLY B CA    1 
ATOM   11499 C  C     . GLY B 1  363  ? -5.740  -6.767  108.579 1.00 27.45 ? 361  GLY B C     1 
ATOM   11500 O  O     . GLY B 1  363  ? -5.540  -7.034  109.770 1.00 26.83 ? 361  GLY B O     1 
ATOM   11501 N  N     . ARG B 1  364  ? -5.895  -5.525  108.134 1.00 27.80 ? 362  ARG B N     1 
ATOM   11502 C  CA    . ARG B 1  364  ? -5.843  -4.333  108.971 1.00 30.94 ? 362  ARG B CA    1 
ATOM   11503 C  C     . ARG B 1  364  ? -7.138  -3.565  108.770 1.00 28.33 ? 362  ARG B C     1 
ATOM   11504 O  O     . ARG B 1  364  ? -7.558  -3.356  107.631 1.00 30.22 ? 362  ARG B O     1 
ATOM   11505 C  CB    . ARG B 1  364  ? -4.670  -3.428  108.585 1.00 27.87 ? 362  ARG B CB    1 
ATOM   11506 C  CG    . ARG B 1  364  ? -3.292  -4.063  108.634 1.00 26.89 ? 362  ARG B CG    1 
ATOM   11507 C  CD    . ARG B 1  364  ? -2.726  -3.996  110.051 1.00 29.79 ? 362  ARG B CD    1 
ATOM   11508 N  NE    . ARG B 1  364  ? -1.482  -4.743  110.155 1.00 30.21 ? 362  ARG B NE    1 
ATOM   11509 C  CZ    . ARG B 1  364  ? -0.276  -4.226  109.966 1.00 29.18 ? 362  ARG B CZ    1 
ATOM   11510 N  NH1   . ARG B 1  364  ? -0.106  -2.939  109.695 1.00 28.18 ? 362  ARG B NH1   1 
ATOM   11511 N  NH2   . ARG B 1  364  ? 0.788   -5.021  110.050 1.00 31.29 ? 362  ARG B NH2   1 
ATOM   11512 N  N     . ARG B 1  365  ? -7.780  -3.153  109.852 1.00 27.24 ? 363  ARG B N     1 
ATOM   11513 C  CA    . ARG B 1  365  ? -8.832  -2.159  109.707 1.00 29.18 ? 363  ARG B CA    1 
ATOM   11514 C  C     . ARG B 1  365  ? -8.152  -0.802  109.687 1.00 24.04 ? 363  ARG B C     1 
ATOM   11515 O  O     . ARG B 1  365  ? -7.476  -0.436  110.646 1.00 25.55 ? 363  ARG B O     1 
ATOM   11516 C  CB    . ARG B 1  365  ? -9.862  -2.246  110.830 1.00 31.40 ? 363  ARG B CB    1 
ATOM   11517 C  CG    . ARG B 1  365  ? -11.074 -1.331  110.619 1.00 32.01 ? 363  ARG B CG    1 
ATOM   11518 C  CD    . ARG B 1  365  ? -12.220 -1.681  111.588 1.00 33.26 ? 363  ARG B CD    1 
ATOM   11519 N  NE    . ARG B 1  365  ? -13.476 -1.019  111.237 1.00 36.00 ? 363  ARG B NE    1 
ATOM   11520 C  CZ    . ARG B 1  365  ? -14.170 -0.235  112.054 1.00 35.16 ? 363  ARG B CZ    1 
ATOM   11521 N  NH1   . ARG B 1  365  ? -13.775 -0.009  113.298 1.00 34.60 ? 363  ARG B NH1   1 
ATOM   11522 N  NH2   . ARG B 1  365  ? -15.292 0.331   111.616 1.00 32.76 ? 363  ARG B NH2   1 
ATOM   11523 N  N     . ILE B 1  366  ? -8.272  -0.092  108.576 1.00 27.48 ? 364  ILE B N     1 
ATOM   11524 C  CA    . ILE B 1  366  ? -7.617  1.196   108.404 1.00 25.15 ? 364  ILE B CA    1 
ATOM   11525 C  C     . ILE B 1  366  ? -8.605  2.286   108.787 1.00 28.33 ? 364  ILE B C     1 
ATOM   11526 O  O     . ILE B 1  366  ? -9.755  2.280   108.333 1.00 26.01 ? 364  ILE B O     1 
ATOM   11527 C  CB    . ILE B 1  366  ? -7.120  1.370   106.957 1.00 22.56 ? 364  ILE B CB    1 
ATOM   11528 C  CG1   . ILE B 1  366  ? -6.124  0.266   106.601 1.00 22.84 ? 364  ILE B CG1   1 
ATOM   11529 C  CG2   . ILE B 1  366  ? -6.522  2.764   106.746 1.00 20.43 ? 364  ILE B CG2   1 
ATOM   11530 C  CD1   . ILE B 1  366  ? -5.631  0.312   105.163 1.00 26.02 ? 364  ILE B CD1   1 
ATOM   11531 N  N     . MET B 1  367  ? -8.169  3.213   109.640 1.00 24.93 ? 365  MET B N     1 
ATOM   11532 C  CA    . MET B 1  367  ? -8.989  4.370   109.967 1.00 24.52 ? 365  MET B CA    1 
ATOM   11533 C  C     . MET B 1  367  ? -8.871  5.384   108.843 1.00 23.99 ? 365  MET B C     1 
ATOM   11534 O  O     . MET B 1  367  ? -7.763  5.779   108.481 1.00 22.80 ? 365  MET B O     1 
ATOM   11535 C  CB    . MET B 1  367  ? -8.541  4.988   111.292 1.00 23.04 ? 365  MET B CB    1 
ATOM   11536 C  CG    . MET B 1  367  ? -8.324  3.960   112.370 1.00 23.76 ? 365  MET B CG    1 
ATOM   11537 S  SD    . MET B 1  367  ? -7.944  4.693   113.994 1.00 26.93 ? 365  MET B SD    1 
ATOM   11538 C  CE    . MET B 1  367  ? -7.093  6.205   113.538 1.00 30.71 ? 365  MET B CE    1 
ATOM   11539 N  N     . VAL B 1  368  ? -10.001 5.794   108.277 1.00 21.33 ? 366  VAL B N     1 
ATOM   11540 C  CA    . VAL B 1  368  ? -9.997  6.672   107.117 1.00 22.48 ? 366  VAL B CA    1 
ATOM   11541 C  C     . VAL B 1  368  ? -10.704 7.963   107.486 1.00 25.63 ? 366  VAL B C     1 
ATOM   11542 O  O     . VAL B 1  368  ? -11.933 7.983   107.660 1.00 23.58 ? 366  VAL B O     1 
ATOM   11543 C  CB    . VAL B 1  368  ? -10.659 6.023   105.897 1.00 24.50 ? 366  VAL B CB    1 
ATOM   11544 C  CG1   . VAL B 1  368  ? -10.574 6.962   104.718 1.00 26.93 ? 366  VAL B CG1   1 
ATOM   11545 C  CG2   . VAL B 1  368  ? -10.003 4.689   105.581 1.00 25.28 ? 366  VAL B CG2   1 
ATOM   11546 N  N     . ARG B 1  369  ? -9.940  9.047   107.591 1.00 21.57 ? 367  ARG B N     1 
ATOM   11547 C  CA    . ARG B 1  369  ? -10.512 10.356  107.869 1.00 22.59 ? 367  ARG B CA    1 
ATOM   11548 C  C     . ARG B 1  369  ? -10.859 11.010  106.541 1.00 24.35 ? 367  ARG B C     1 
ATOM   11549 O  O     . ARG B 1  369  ? -9.970  11.333  105.741 1.00 22.08 ? 367  ARG B O     1 
ATOM   11550 C  CB    . ARG B 1  369  ? -9.564  11.243  108.677 1.00 23.03 ? 367  ARG B CB    1 
ATOM   11551 C  CG    . ARG B 1  369  ? -10.183 12.611  108.960 1.00 24.21 ? 367  ARG B CG    1 
ATOM   11552 C  CD    . ARG B 1  369  ? -9.181  13.634  109.387 1.00 22.75 ? 367  ARG B CD    1 
ATOM   11553 N  NE    . ARG B 1  369  ? -8.529  13.240  110.625 1.00 25.05 ? 367  ARG B NE    1 
ATOM   11554 C  CZ    . ARG B 1  369  ? -7.286  13.569  110.930 1.00 26.13 ? 367  ARG B CZ    1 
ATOM   11555 N  NH1   . ARG B 1  369  ? -6.552  14.305  110.111 1.00 24.36 ? 367  ARG B NH1   1 
ATOM   11556 N  NH2   . ARG B 1  369  ? -6.762  13.125  112.069 1.00 24.09 ? 367  ARG B NH2   1 
ATOM   11557 N  N     . LEU B 1  370  ? -12.149 11.202  106.303 1.00 22.46 ? 368  LEU B N     1 
ATOM   11558 C  CA    . LEU B 1  370  ? -12.613 11.921  105.128 1.00 20.83 ? 368  LEU B CA    1 
ATOM   11559 C  C     . LEU B 1  370  ? -12.714 13.402  105.470 1.00 23.10 ? 368  LEU B C     1 
ATOM   11560 O  O     . LEU B 1  370  ? -13.472 13.797  106.364 1.00 25.87 ? 368  LEU B O     1 
ATOM   11561 C  CB    . LEU B 1  370  ? -13.957 11.360  104.653 1.00 23.90 ? 368  LEU B CB    1 
ATOM   11562 C  CG    . LEU B 1  370  ? -14.531 11.918  103.348 1.00 25.46 ? 368  LEU B CG    1 
ATOM   11563 C  CD1   . LEU B 1  370  ? -13.650 11.566  102.147 1.00 25.97 ? 368  LEU B CD1   1 
ATOM   11564 C  CD2   . LEU B 1  370  ? -15.963 11.418  103.134 1.00 25.32 ? 368  LEU B CD2   1 
ATOM   11565 N  N     . VAL B 1  371  ? -11.914 14.213  104.791 1.00 20.58 ? 369  VAL B N     1 
ATOM   11566 C  CA    . VAL B 1  371  ? -11.997 15.655  104.894 1.00 22.99 ? 369  VAL B CA    1 
ATOM   11567 C  C     . VAL B 1  371  ? -12.419 16.174  103.536 1.00 21.92 ? 369  VAL B C     1 
ATOM   11568 O  O     . VAL B 1  371  ? -12.405 15.450  102.544 1.00 23.70 ? 369  VAL B O     1 
ATOM   11569 C  CB    . VAL B 1  371  ? -10.664 16.284  105.315 1.00 22.03 ? 369  VAL B CB    1 
ATOM   11570 C  CG1   . VAL B 1  371  ? -10.157 15.661  106.597 1.00 22.69 ? 369  VAL B CG1   1 
ATOM   11571 C  CG2   . VAL B 1  371  ? -9.632  16.130  104.178 1.00 21.82 ? 369  VAL B CG2   1 
ATOM   11572 N  N     . LYS B 1  372  ? -12.761 17.456  103.483 1.00 21.48 ? 370  LYS B N     1 
ATOM   11573 C  CA    . LYS B 1  372  ? -12.969 18.030  102.161 1.00 21.31 ? 370  LYS B CA    1 
ATOM   11574 C  C     . LYS B 1  372  ? -11.639 18.437  101.532 1.00 20.82 ? 370  LYS B C     1 
ATOM   11575 O  O     . LYS B 1  372  ? -11.308 17.977  100.436 1.00 20.52 ? 370  LYS B O     1 
ATOM   11576 C  CB    . LYS B 1  372  ? -13.975 19.179  102.239 1.00 22.10 ? 370  LYS B CB    1 
ATOM   11577 C  CG    . LYS B 1  372  ? -15.358 18.622  102.609 1.00 23.56 ? 370  LYS B CG    1 
ATOM   11578 C  CD    . LYS B 1  372  ? -16.466 19.653  102.654 1.00 26.54 ? 370  LYS B CD    1 
ATOM   11579 C  CE    . LYS B 1  372  ? -17.736 19.004  103.191 1.00 28.79 ? 370  LYS B CE    1 
ATOM   11580 N  NZ    . LYS B 1  372  ? -18.884 19.957  103.246 1.00 29.25 ? 370  LYS B NZ    1 
ATOM   11581 N  N     . GLY B 1  373  ? -10.830 19.232  102.229 1.00 23.10 ? 371  GLY B N     1 
ATOM   11582 C  CA    . GLY B 1  373  ? -9.521  19.577  101.701 1.00 18.47 ? 371  GLY B CA    1 
ATOM   11583 C  C     . GLY B 1  373  ? -9.087  20.981  102.063 1.00 19.81 ? 371  GLY B C     1 
ATOM   11584 O  O     . GLY B 1  373  ? -9.883  21.915  101.970 1.00 23.53 ? 371  GLY B O     1 
ATOM   11585 N  N     . ALA B 1  374  ? -7.823  21.148  102.462 1.00 17.77 ? 372  ALA B N     1 
ATOM   11586 C  CA    . ALA B 1  374  ? -7.360  22.391  103.059 1.00 17.95 ? 372  ALA B CA    1 
ATOM   11587 C  C     . ALA B 1  374  ? -6.556  23.274  102.113 1.00 18.39 ? 372  ALA B C     1 
ATOM   11588 O  O     . ALA B 1  374  ? -6.244  24.412  102.480 1.00 21.35 ? 372  ALA B O     1 
ATOM   11589 C  CB    . ALA B 1  374  ? -6.501  22.099  104.293 1.00 18.93 ? 372  ALA B CB    1 
ATOM   11590 N  N     . TYR B 1  375  ? -6.224  22.795  100.911 1.00 18.31 ? 373  TYR B N     1 
ATOM   11591 C  CA    . TYR B 1  375  ? -5.277  23.475  100.040 1.00 17.77 ? 373  TYR B CA    1 
ATOM   11592 C  C     . TYR B 1  375  ? -5.931  23.997  98.765  1.00 17.63 ? 373  TYR B C     1 
ATOM   11593 O  O     . TYR B 1  375  ? -5.248  24.163  97.763  1.00 17.46 ? 373  TYR B O     1 
ATOM   11594 C  CB    . TYR B 1  375  ? -4.116  22.548  99.668  1.00 17.80 ? 373  TYR B CB    1 
ATOM   11595 C  CG    . TYR B 1  375  ? -3.379  21.966  100.857 1.00 18.24 ? 373  TYR B CG    1 
ATOM   11596 C  CD1   . TYR B 1  375  ? -3.896  20.883  101.557 1.00 19.05 ? 373  TYR B CD1   1 
ATOM   11597 C  CD2   . TYR B 1  375  ? -2.157  22.484  101.267 1.00 19.35 ? 373  TYR B CD2   1 
ATOM   11598 C  CE1   . TYR B 1  375  ? -3.230  20.348  102.636 1.00 18.40 ? 373  TYR B CE1   1 
ATOM   11599 C  CE2   . TYR B 1  375  ? -1.484  21.944  102.326 1.00 20.95 ? 373  TYR B CE2   1 
ATOM   11600 C  CZ    . TYR B 1  375  ? -2.025  20.878  103.012 1.00 19.04 ? 373  TYR B CZ    1 
ATOM   11601 O  OH    . TYR B 1  375  ? -1.338  20.349  104.081 1.00 20.31 ? 373  TYR B OH    1 
ATOM   11602 N  N     . TRP B 1  376  ? -7.240  24.276  98.793  1.00 17.81 ? 374  TRP B N     1 
ATOM   11603 C  CA    . TRP B 1  376  ? -7.957  24.527  97.543  1.00 18.41 ? 374  TRP B CA    1 
ATOM   11604 C  C     . TRP B 1  376  ? -7.338  25.673  96.746  1.00 18.99 ? 374  TRP B C     1 
ATOM   11605 O  O     . TRP B 1  376  ? -6.996  25.505  95.575  1.00 18.01 ? 374  TRP B O     1 
ATOM   11606 C  CB    . TRP B 1  376  ? -9.433  24.802  97.815  1.00 18.81 ? 374  TRP B CB    1 
ATOM   11607 C  CG    . TRP B 1  376  ? -10.192 24.942  96.535  1.00 19.00 ? 374  TRP B CG    1 
ATOM   11608 C  CD1   . TRP B 1  376  ? -10.639 23.930  95.730  1.00 19.44 ? 374  TRP B CD1   1 
ATOM   11609 C  CD2   . TRP B 1  376  ? -10.581 26.162  95.904  1.00 20.50 ? 374  TRP B CD2   1 
ATOM   11610 N  NE1   . TRP B 1  376  ? -11.296 24.450  94.646  1.00 20.27 ? 374  TRP B NE1   1 
ATOM   11611 C  CE2   . TRP B 1  376  ? -11.259 25.818  94.716  1.00 20.65 ? 374  TRP B CE2   1 
ATOM   11612 C  CE3   . TRP B 1  376  ? -10.421 27.515  96.224  1.00 25.07 ? 374  TRP B CE3   1 
ATOM   11613 C  CZ2   . TRP B 1  376  ? -11.784 26.773  93.854  1.00 20.37 ? 374  TRP B CZ2   1 
ATOM   11614 C  CZ3   . TRP B 1  376  ? -10.937 28.464  95.367  1.00 24.31 ? 374  TRP B CZ3   1 
ATOM   11615 C  CH2   . TRP B 1  376  ? -11.609 28.091  94.192  1.00 23.78 ? 374  TRP B CH2   1 
ATOM   11616 N  N     . ASP B 1  377  ? -7.188  26.850  97.358  1.00 17.01 ? 375  ASP B N     1 
ATOM   11617 C  CA    . ASP B 1  377  ? -6.658  27.990  96.614  1.00 19.66 ? 375  ASP B CA    1 
ATOM   11618 C  C     . ASP B 1  377  ? -5.278  27.690  96.054  1.00 18.81 ? 375  ASP B C     1 
ATOM   11619 O  O     . ASP B 1  377  ? -4.949  28.106  94.941  1.00 18.25 ? 375  ASP B O     1 
ATOM   11620 C  CB    . ASP B 1  377  ? -6.572  29.232  97.497  1.00 23.35 ? 375  ASP B CB    1 
ATOM   11621 C  CG    . ASP B 1  377  ? -7.899  29.892  97.702  1.00 29.23 ? 375  ASP B CG    1 
ATOM   11622 O  OD1   . ASP B 1  377  ? -8.448  30.437  96.725  1.00 38.18 ? 375  ASP B OD1   1 
ATOM   11623 O  OD2   . ASP B 1  377  ? -8.396  29.873  98.843  1.00 32.89 ? 375  ASP B OD2   1 
ATOM   11624 N  N     . ALA B 1  378  ? -4.448  26.990  96.825  1.00 18.08 ? 376  ALA B N     1 
ATOM   11625 C  CA    . ALA B 1  378  ? -3.099  26.699  96.353  1.00 16.39 ? 376  ALA B CA    1 
ATOM   11626 C  C     . ALA B 1  378  ? -3.116  25.717  95.196  1.00 17.36 ? 376  ALA B C     1 
ATOM   11627 O  O     . ALA B 1  378  ? -2.274  25.809  94.296  1.00 16.89 ? 376  ALA B O     1 
ATOM   11628 C  CB    . ALA B 1  378  ? -2.248  26.153  97.501  1.00 17.27 ? 376  ALA B CB    1 
ATOM   11629 N  N     . GLU B 1  379  ? -4.069  24.782  95.196  1.00 16.74 ? 377  GLU B N     1 
ATOM   11630 C  CA    . GLU B 1  379  ? -4.130  23.818  94.105  1.00 16.21 ? 377  GLU B CA    1 
ATOM   11631 C  C     . GLU B 1  379  ? -4.590  24.485  92.823  1.00 16.97 ? 377  GLU B C     1 
ATOM   11632 O  O     . GLU B 1  379  ? -4.118  24.134  91.739  1.00 16.19 ? 377  GLU B O     1 
ATOM   11633 C  CB    . GLU B 1  379  ? -5.053  22.645  94.457  1.00 17.23 ? 377  GLU B CB    1 
ATOM   11634 C  CG    . GLU B 1  379  ? -4.652  21.861  95.709  1.00 17.86 ? 377  GLU B CG    1 
ATOM   11635 C  CD    . GLU B 1  379  ? -3.401  21.008  95.546  1.00 18.10 ? 377  GLU B CD    1 
ATOM   11636 O  OE1   . GLU B 1  379  ? -2.782  21.013  94.453  1.00 19.22 ? 377  GLU B OE1   1 
ATOM   11637 O  OE2   . GLU B 1  379  ? -3.038  20.324  96.532  1.00 19.01 ? 377  GLU B OE2   1 
ATOM   11638 N  N     . ILE B 1  380  ? -5.517  25.444  92.913  1.00 17.88 ? 378  ILE B N     1 
ATOM   11639 C  CA    . ILE B 1  380  ? -5.923  26.165  91.704  1.00 15.60 ? 378  ILE B CA    1 
ATOM   11640 C  C     . ILE B 1  380  ? -4.738  26.929  91.133  1.00 16.42 ? 378  ILE B C     1 
ATOM   11641 O  O     . ILE B 1  380  ? -4.438  26.855  89.932  1.00 16.34 ? 378  ILE B O     1 
ATOM   11642 C  CB    . ILE B 1  380  ? -7.097  27.117  91.993  1.00 17.82 ? 378  ILE B CB    1 
ATOM   11643 C  CG1   . ILE B 1  380  ? -8.280  26.351  92.582  1.00 19.02 ? 378  ILE B CG1   1 
ATOM   11644 C  CG2   . ILE B 1  380  ? -7.505  27.839  90.712  1.00 17.39 ? 378  ILE B CG2   1 
ATOM   11645 C  CD1   . ILE B 1  380  ? -8.799  25.227  91.674  1.00 18.17 ? 378  ILE B CD1   1 
ATOM   11646 N  N     . LYS B 1  381  ? -4.047  27.678  91.992  1.00 14.81 ? 379  LYS B N     1 
ATOM   11647 C  CA    . LYS B 1  381  ? -2.915  28.453  91.522  1.00 15.63 ? 379  LYS B CA    1 
ATOM   11648 C  C     . LYS B 1  381  ? -1.850  27.550  90.918  1.00 16.39 ? 379  LYS B C     1 
ATOM   11649 O  O     . LYS B 1  381  ? -1.330  27.842  89.841  1.00 16.73 ? 379  LYS B O     1 
ATOM   11650 C  CB    . LYS B 1  381  ? -2.325  29.280  92.659  1.00 16.35 ? 379  LYS B CB    1 
ATOM   11651 C  CG    . LYS B 1  381  ? -1.072  30.050  92.235  1.00 15.20 ? 379  LYS B CG    1 
ATOM   11652 C  CD    . LYS B 1  381  ? -0.620  30.952  93.383  1.00 14.98 ? 379  LYS B CD    1 
ATOM   11653 C  CE    . LYS B 1  381  ? 0.528   31.861  92.947  1.00 17.14 ? 379  LYS B CE    1 
ATOM   11654 N  NZ    . LYS B 1  381  ? 1.013   32.724  94.094  1.00 16.60 ? 379  LYS B NZ    1 
ATOM   11655 N  N     . ARG B 1  382  ? -1.543  26.426  91.582  1.00 15.50 ? 380  ARG B N     1 
ATOM   11656 C  CA    . ARG B 1  382  ? -0.440  25.583  91.116  1.00 14.98 ? 380  ARG B CA    1 
ATOM   11657 C  C     . ARG B 1  382  ? -0.737  24.990  89.748  1.00 16.53 ? 380  ARG B C     1 
ATOM   11658 O  O     . ARG B 1  382  ? 0.136   24.974  88.867  1.00 16.48 ? 380  ARG B O     1 
ATOM   11659 C  CB    . ARG B 1  382  ? -0.167  24.468  92.125  1.00 18.23 ? 380  ARG B CB    1 
ATOM   11660 C  CG    . ARG B 1  382  ? 1.020   23.593  91.764  1.00 24.42 ? 380  ARG B CG    1 
ATOM   11661 C  CD    . ARG B 1  382  ? 2.319   24.398  91.674  1.00 24.95 ? 380  ARG B CD    1 
ATOM   11662 N  NE    . ARG B 1  382  ? 3.451   23.535  91.344  1.00 29.16 ? 380  ARG B NE    1 
ATOM   11663 C  CZ    . ARG B 1  382  ? 4.121   22.802  92.226  1.00 36.68 ? 380  ARG B CZ    1 
ATOM   11664 N  NH1   . ARG B 1  382  ? 3.807   22.807  93.514  1.00 35.67 ? 380  ARG B NH1   1 
ATOM   11665 N  NH2   . ARG B 1  382  ? 5.125   22.036  91.804  1.00 35.43 ? 380  ARG B NH2   1 
ATOM   11666 N  N     . ALA B 1  383  ? -1.958  24.503  89.548  1.00 16.06 ? 381  ALA B N     1 
ATOM   11667 C  CA    . ALA B 1  383  ? -2.311  23.921  88.257  1.00 14.64 ? 381  ALA B CA    1 
ATOM   11668 C  C     . ALA B 1  383  ? -2.249  24.967  87.153  1.00 16.96 ? 381  ALA B C     1 
ATOM   11669 O  O     . ALA B 1  383  ? -1.809  24.676  86.030  1.00 15.47 ? 381  ALA B O     1 
ATOM   11670 C  CB    . ALA B 1  383  ? -3.702  23.295  88.330  1.00 14.30 ? 381  ALA B CB    1 
ATOM   11671 N  N     . GLN B 1  384  ? -2.680  26.196  87.456  1.00 13.58 ? 382  GLN B N     1 
ATOM   11672 C  CA    . GLN B 1  384  ? -2.584  27.270  86.471  1.00 15.07 ? 382  GLN B CA    1 
ATOM   11673 C  C     . GLN B 1  384  ? -1.131  27.618  86.167  1.00 14.54 ? 382  GLN B C     1 
ATOM   11674 O  O     . GLN B 1  384  ? -0.761  27.770  84.998  1.00 16.88 ? 382  GLN B O     1 
ATOM   11675 C  CB    . GLN B 1  384  ? -3.335  28.507  86.954  1.00 16.19 ? 382  GLN B CB    1 
ATOM   11676 C  CG    . GLN B 1  384  ? -4.853  28.303  86.973  1.00 16.00 ? 382  GLN B CG    1 
ATOM   11677 C  CD    . GLN B 1  384  ? -5.590  29.566  87.370  1.00 18.39 ? 382  GLN B CD    1 
ATOM   11678 O  OE1   . GLN B 1  384  ? -5.014  30.453  87.982  1.00 20.07 ? 382  GLN B OE1   1 
ATOM   11679 N  NE2   . GLN B 1  384  ? -6.867  29.662  86.999  1.00 16.76 ? 382  GLN B NE2   1 
ATOM   11680 N  N     . LEU B 1  385  ? -0.309  27.795  87.209  1.00 16.41 ? 383  LEU B N     1 
ATOM   11681 C  CA    . LEU B 1  385  ? 1.104   28.105  86.998  1.00 15.84 ? 383  LEU B CA    1 
ATOM   11682 C  C     . LEU B 1  385  ? 1.778   27.051  86.139  1.00 16.87 ? 383  LEU B C     1 
ATOM   11683 O  O     . LEU B 1  385  ? 2.645   27.370  85.311  1.00 16.88 ? 383  LEU B O     1 
ATOM   11684 C  CB    . LEU B 1  385  ? 1.831   28.211  88.337  1.00 18.71 ? 383  LEU B CB    1 
ATOM   11685 C  CG    . LEU B 1  385  ? 1.529   29.456  89.165  1.00 18.84 ? 383  LEU B CG    1 
ATOM   11686 C  CD1   . LEU B 1  385  ? 2.326   29.384  90.437  1.00 21.15 ? 383  LEU B CD1   1 
ATOM   11687 C  CD2   . LEU B 1  385  ? 1.922   30.695  88.386  1.00 21.14 ? 383  LEU B CD2   1 
ATOM   11688 N  N     . ASP B 1  386  ? 1.424   25.785  86.343  1.00 18.22 ? 384  ASP B N     1 
ATOM   11689 C  CA    . ASP B 1  386  ? 2.139   24.697  85.686  1.00 16.71 ? 384  ASP B CA    1 
ATOM   11690 C  C     . ASP B 1  386  ? 1.536   24.331  84.341  1.00 18.88 ? 384  ASP B C     1 
ATOM   11691 O  O     . ASP B 1  386  ? 2.058   23.433  83.672  1.00 20.17 ? 384  ASP B O     1 
ATOM   11692 C  CB    . ASP B 1  386  ? 2.193   23.463  86.605  1.00 17.68 ? 384  ASP B CB    1 
ATOM   11693 C  CG    . ASP B 1  386  ? 3.110   23.655  87.816  1.00 22.63 ? 384  ASP B CG    1 
ATOM   11694 O  OD1   . ASP B 1  386  ? 3.828   24.674  87.902  1.00 20.17 ? 384  ASP B OD1   1 
ATOM   11695 O  OD2   . ASP B 1  386  ? 3.113   22.768  88.700  1.00 21.87 ? 384  ASP B OD2   1 
ATOM   11696 N  N     . GLY B 1  387  ? 0.476   25.023  83.924  1.00 17.33 ? 385  GLY B N     1 
ATOM   11697 C  CA    . GLY B 1  387  ? -0.172  24.772  82.653  1.00 16.17 ? 385  GLY B CA    1 
ATOM   11698 C  C     . GLY B 1  387  ? -0.633  23.342  82.482  1.00 19.48 ? 385  GLY B C     1 
ATOM   11699 O  O     . GLY B 1  387  ? -0.468  22.764  81.400  1.00 18.91 ? 385  GLY B O     1 
ATOM   11700 N  N     . LEU B 1  388  ? -1.214  22.754  83.520  1.00 16.82 ? 386  LEU B N     1 
ATOM   11701 C  CA    . LEU B 1  388  ? -1.581  21.351  83.429  1.00 18.79 ? 386  LEU B CA    1 
ATOM   11702 C  C     . LEU B 1  388  ? -2.988  21.202  82.858  1.00 18.03 ? 386  LEU B C     1 
ATOM   11703 O  O     . LEU B 1  388  ? -3.727  22.175  82.686  1.00 18.39 ? 386  LEU B O     1 
ATOM   11704 C  CB    . LEU B 1  388  ? -1.438  20.681  84.790  1.00 18.08 ? 386  LEU B CB    1 
ATOM   11705 C  CG    . LEU B 1  388  ? 0.032   20.720  85.222  1.00 15.86 ? 386  LEU B CG    1 
ATOM   11706 C  CD1   . LEU B 1  388  ? 0.279   20.023  86.565  1.00 21.01 ? 386  LEU B CD1   1 
ATOM   11707 C  CD2   . LEU B 1  388  ? 0.971   20.164  84.149  1.00 18.36 ? 386  LEU B CD2   1 
ATOM   11708 N  N     . ALA B 1  389  ? -3.359  19.956  82.544  1.00 18.55 ? 387  ALA B N     1 
ATOM   11709 C  CA    . ALA B 1  389  ? -4.553  19.736  81.732  1.00 17.40 ? 387  ALA B CA    1 
ATOM   11710 C  C     . ALA B 1  389  ? -5.818  20.187  82.454  1.00 18.11 ? 387  ALA B C     1 
ATOM   11711 O  O     . ALA B 1  389  ? -6.753  20.705  81.830  1.00 19.97 ? 387  ALA B O     1 
ATOM   11712 C  CB    . ALA B 1  389  ? -4.664  18.261  81.344  1.00 21.18 ? 387  ALA B CB    1 
ATOM   11713 N  N     . ASP B 1  390  ? -5.867  19.996  83.762  1.00 20.06 ? 388  ASP B N     1 
ATOM   11714 C  CA    . ASP B 1  390  ? -7.034  20.365  84.552  1.00 18.46 ? 388  ASP B CA    1 
ATOM   11715 C  C     . ASP B 1  390  ? -6.561  20.483  85.993  1.00 16.88 ? 388  ASP B C     1 
ATOM   11716 O  O     . ASP B 1  390  ? -5.378  20.289  86.299  1.00 18.66 ? 388  ASP B O     1 
ATOM   11717 C  CB    . ASP B 1  390  ? -8.150  19.326  84.399  1.00 18.47 ? 388  ASP B CB    1 
ATOM   11718 C  CG    . ASP B 1  390  ? -9.550  19.914  84.566  1.00 21.80 ? 388  ASP B CG    1 
ATOM   11719 O  OD1   . ASP B 1  390  ? -9.781  20.688  85.515  1.00 21.83 ? 388  ASP B OD1   1 
ATOM   11720 O  OD2   . ASP B 1  390  ? -10.423 19.592  83.732  1.00 21.29 ? 388  ASP B OD2   1 
ATOM   11721 N  N     . PHE B 1  391  ? -7.488  20.789  86.874  1.00 17.73 ? 389  PHE B N     1 
ATOM   11722 C  CA    . PHE B 1  391  ? -7.184  20.825  88.289  1.00 17.45 ? 389  PHE B CA    1 
ATOM   11723 C  C     . PHE B 1  391  ? -7.268  19.421  88.890  1.00 17.74 ? 389  PHE B C     1 
ATOM   11724 O  O     . PHE B 1  391  ? -7.987  18.555  88.379  1.00 17.54 ? 389  PHE B O     1 
ATOM   11725 C  CB    . PHE B 1  391  ? -8.153  21.768  88.998  1.00 18.71 ? 389  PHE B CB    1 
ATOM   11726 C  CG    . PHE B 1  391  ? -8.128  23.152  88.426  1.00 17.79 ? 389  PHE B CG    1 
ATOM   11727 C  CD1   . PHE B 1  391  ? -7.088  24.018  88.750  1.00 17.10 ? 389  PHE B CD1   1 
ATOM   11728 C  CD2   . PHE B 1  391  ? -9.104  23.572  87.533  1.00 18.67 ? 389  PHE B CD2   1 
ATOM   11729 C  CE1   . PHE B 1  391  ? -7.025  25.286  88.206  1.00 17.95 ? 389  PHE B CE1   1 
ATOM   11730 C  CE2   . PHE B 1  391  ? -9.050  24.854  86.989  1.00 17.31 ? 389  PHE B CE2   1 
ATOM   11731 C  CZ    . PHE B 1  391  ? -7.999  25.703  87.318  1.00 15.98 ? 389  PHE B CZ    1 
ATOM   11732 N  N     . PRO B 1  392  ? -6.519  19.165  89.960  1.00 16.18 ? 390  PRO B N     1 
ATOM   11733 C  CA    . PRO B 1  392  ? -6.661  17.908  90.703  1.00 15.04 ? 390  PRO B CA    1 
ATOM   11734 C  C     . PRO B 1  392  ? -7.746  17.958  91.764  1.00 17.03 ? 390  PRO B C     1 
ATOM   11735 O  O     . PRO B 1  392  ? -7.895  16.998  92.524  1.00 16.71 ? 390  PRO B O     1 
ATOM   11736 C  CB    . PRO B 1  392  ? -5.282  17.768  91.355  1.00 16.82 ? 390  PRO B CB    1 
ATOM   11737 C  CG    . PRO B 1  392  ? -4.919  19.196  91.703  1.00 16.53 ? 390  PRO B CG    1 
ATOM   11738 C  CD    . PRO B 1  392  ? -5.451  20.018  90.530  1.00 14.28 ? 390  PRO B CD    1 
ATOM   11739 N  N     . VAL B 1  393  ? -8.453  19.083  91.851  1.00 17.38 ? 391  VAL B N     1 
ATOM   11740 C  CA    . VAL B 1  393  ? -9.530  19.309  92.798  1.00 18.34 ? 391  VAL B CA    1 
ATOM   11741 C  C     . VAL B 1  393  ? -10.718 19.851  92.020  1.00 16.66 ? 391  VAL B C     1 
ATOM   11742 O  O     . VAL B 1  393  ? -10.579 20.341  90.900  1.00 17.17 ? 391  VAL B O     1 
ATOM   11743 C  CB    . VAL B 1  393  ? -9.126  20.286  93.924  1.00 18.35 ? 391  VAL B CB    1 
ATOM   11744 C  CG1   . VAL B 1  393  ? -7.943  19.726  94.696  1.00 17.34 ? 391  VAL B CG1   1 
ATOM   11745 C  CG2   . VAL B 1  393  ? -8.770  21.668  93.358  1.00 16.22 ? 391  VAL B CG2   1 
ATOM   11746 N  N     . PHE B 1  394  ? -11.892 19.786  92.641  1.00 19.66 ? 392  PHE B N     1 
ATOM   11747 C  CA    . PHE B 1  394  ? -13.068 20.396  92.037  1.00 18.23 ? 392  PHE B CA    1 
ATOM   11748 C  C     . PHE B 1  394  ? -12.966 21.917  92.108  1.00 18.73 ? 392  PHE B C     1 
ATOM   11749 O  O     . PHE B 1  394  ? -12.192 22.476  92.890  1.00 20.69 ? 392  PHE B O     1 
ATOM   11750 C  CB    . PHE B 1  394  ? -14.342 19.876  92.723  1.00 17.95 ? 392  PHE B CB    1 
ATOM   11751 C  CG    . PHE B 1  394  ? -14.482 18.395  92.601  1.00 19.31 ? 392  PHE B CG    1 
ATOM   11752 C  CD1   . PHE B 1  394  ? -14.711 17.823  91.358  1.00 21.70 ? 392  PHE B CD1   1 
ATOM   11753 C  CD2   . PHE B 1  394  ? -14.296 17.571  93.687  1.00 20.10 ? 392  PHE B CD2   1 
ATOM   11754 C  CE1   . PHE B 1  394  ? -14.797 16.454  91.209  1.00 20.18 ? 392  PHE B CE1   1 
ATOM   11755 C  CE2   . PHE B 1  394  ? -14.376 16.195  93.548  1.00 20.59 ? 392  PHE B CE2   1 
ATOM   11756 C  CZ    . PHE B 1  394  ? -14.624 15.638  92.293  1.00 19.26 ? 392  PHE B CZ    1 
ATOM   11757 N  N     . THR B 1  395  ? -13.766 22.592  91.273  1.00 19.76 ? 393  THR B N     1 
ATOM   11758 C  CA    . THR B 1  395  ? -13.757 24.047  91.236  1.00 20.23 ? 393  THR B CA    1 
ATOM   11759 C  C     . THR B 1  395  ? -15.050 24.680  91.733  1.00 19.46 ? 393  THR B C     1 
ATOM   11760 O  O     . THR B 1  395  ? -15.072 25.896  91.938  1.00 23.29 ? 393  THR B O     1 
ATOM   11761 C  CB    . THR B 1  395  ? -13.454 24.559  89.820  1.00 21.47 ? 393  THR B CB    1 
ATOM   11762 O  OG1   . THR B 1  395  ? -14.460 24.112  88.911  1.00 21.28 ? 393  THR B OG1   1 
ATOM   11763 C  CG2   . THR B 1  395  ? -12.089 24.059  89.341  1.00 20.66 ? 393  THR B CG2   1 
ATOM   11764 N  N     . ARG B 1  396  ? -16.114 23.905  91.926  1.00 20.14 ? 394  ARG B N     1 
ATOM   11765 C  CA    . ARG B 1  396  ? -17.322 24.376  92.592  1.00 22.46 ? 394  ARG B CA    1 
ATOM   11766 C  C     . ARG B 1  396  ? -17.418 23.704  93.948  1.00 23.51 ? 394  ARG B C     1 
ATOM   11767 O  O     . ARG B 1  396  ? -17.259 22.484  94.047  1.00 22.87 ? 394  ARG B O     1 
ATOM   11768 C  CB    . ARG B 1  396  ? -18.581 24.073  91.779  1.00 24.27 ? 394  ARG B CB    1 
ATOM   11769 C  CG    . ARG B 1  396  ? -18.601 24.749  90.428  1.00 25.76 ? 394  ARG B CG    1 
ATOM   11770 C  CD    . ARG B 1  396  ? -19.936 24.513  89.716  1.00 25.37 ? 394  ARG B CD    1 
ATOM   11771 N  NE    . ARG B 1  396  ? -19.841 24.988  88.342  1.00 27.26 ? 394  ARG B NE    1 
ATOM   11772 C  CZ    . ARG B 1  396  ? -20.678 25.853  87.783  1.00 30.28 ? 394  ARG B CZ    1 
ATOM   11773 N  NH1   . ARG B 1  396  ? -21.749 26.296  88.427  1.00 31.68 ? 394  ARG B NH1   1 
ATOM   11774 N  NH2   . ARG B 1  396  ? -20.437 26.278  86.547  1.00 29.68 ? 394  ARG B NH2   1 
ATOM   11775 N  N     . LYS B 1  397  ? -17.697 24.496  94.984  1.00 25.89 ? 395  LYS B N     1 
ATOM   11776 C  CA    . LYS B 1  397  ? -17.748 23.941  96.332  1.00 25.33 ? 395  LYS B CA    1 
ATOM   11777 C  C     . LYS B 1  397  ? -18.815 22.857  96.444  1.00 25.83 ? 395  LYS B C     1 
ATOM   11778 O  O     . LYS B 1  397  ? -18.623 21.850  97.134  1.00 24.06 ? 395  LYS B O     1 
ATOM   11779 C  CB    . LYS B 1  397  ? -17.976 25.070  97.335  1.00 27.45 ? 395  LYS B CB    1 
ATOM   11780 C  CG    . LYS B 1  397  ? -17.631 24.716  98.759  1.00 28.44 ? 395  LYS B CG    1 
ATOM   11781 C  CD    . LYS B 1  397  ? -18.865 24.232  99.474  1.00 32.89 ? 395  LYS B CD    1 
ATOM   11782 C  CE    . LYS B 1  397  ? -18.603 24.015  100.947 1.00 32.50 ? 395  LYS B CE    1 
ATOM   11783 N  NZ    . LYS B 1  397  ? -19.850 23.553  101.582 1.00 30.45 ? 395  LYS B NZ    1 
ATOM   11784 N  N     . ILE B 1  398  ? -19.940 23.027  95.747  1.00 24.78 ? 396  ILE B N     1 
ATOM   11785 C  CA    . ILE B 1  398  ? -20.989 22.015  95.804  1.00 27.30 ? 396  ILE B CA    1 
ATOM   11786 C  C     . ILE B 1  398  ? -20.499 20.676  95.264  1.00 24.42 ? 396  ILE B C     1 
ATOM   11787 O  O     . ILE B 1  398  ? -20.975 19.613  95.685  1.00 25.66 ? 396  ILE B O     1 
ATOM   11788 C  CB    . ILE B 1  398  ? -22.238 22.513  95.053  1.00 29.34 ? 396  ILE B CB    1 
ATOM   11789 C  CG1   . ILE B 1  398  ? -23.426 21.634  95.389  1.00 36.73 ? 396  ILE B CG1   1 
ATOM   11790 C  CG2   . ILE B 1  398  ? -21.989 22.528  93.547  1.00 28.95 ? 396  ILE B CG2   1 
ATOM   11791 C  CD1   . ILE B 1  398  ? -24.719 22.393  95.390  1.00 39.79 ? 396  ILE B CD1   1 
ATOM   11792 N  N     . HIS B 1  399  ? -19.519 20.696  94.356  1.00 23.83 ? 397  HIS B N     1 
ATOM   11793 C  CA    . HIS B 1  399  ? -18.988 19.442  93.828  1.00 22.68 ? 397  HIS B CA    1 
ATOM   11794 C  C     . HIS B 1  399  ? -18.200 18.690  94.888  1.00 21.37 ? 397  HIS B C     1 
ATOM   11795 O  O     . HIS B 1  399  ? -18.289 17.461  94.985  1.00 23.58 ? 397  HIS B O     1 
ATOM   11796 C  CB    . HIS B 1  399  ? -18.103 19.721  92.618  1.00 23.49 ? 397  HIS B CB    1 
ATOM   11797 C  CG    . HIS B 1  399  ? -18.855 20.256  91.441  1.00 25.07 ? 397  HIS B CG    1 
ATOM   11798 N  ND1   . HIS B 1  399  ? -18.226 20.754  90.322  1.00 24.95 ? 397  HIS B ND1   1 
ATOM   11799 C  CD2   . HIS B 1  399  ? -20.186 20.374  91.214  1.00 28.25 ? 397  HIS B CD2   1 
ATOM   11800 C  CE1   . HIS B 1  399  ? -19.139 21.147  89.448  1.00 25.36 ? 397  HIS B CE1   1 
ATOM   11801 N  NE2   . HIS B 1  399  ? -20.336 20.933  89.968  1.00 25.53 ? 397  HIS B NE2   1 
ATOM   11802 N  N     . THR B 1  400  ? -17.406 19.416  95.674  1.00 21.14 ? 398  THR B N     1 
ATOM   11803 C  CA    . THR B 1  400  ? -16.717 18.802  96.797  1.00 21.82 ? 398  THR B CA    1 
ATOM   11804 C  C     . THR B 1  400  ? -17.709 18.205  97.787  1.00 23.18 ? 398  THR B C     1 
ATOM   11805 O  O     . THR B 1  400  ? -17.486 17.107  98.308  1.00 25.32 ? 398  THR B O     1 
ATOM   11806 C  CB    . THR B 1  400  ? -15.819 19.838  97.470  1.00 19.50 ? 398  THR B CB    1 
ATOM   11807 O  OG1   . THR B 1  400  ? -14.726 20.154  96.593  1.00 20.64 ? 398  THR B OG1   1 
ATOM   11808 C  CG2   . THR B 1  400  ? -15.281 19.304  98.783  1.00 20.33 ? 398  THR B CG2   1 
ATOM   11809 N  N     . ASP B 1  401  ? -18.825 18.900  98.037  1.00 27.22 ? 399  ASP B N     1 
ATOM   11810 C  CA    . ASP B 1  401  ? -19.834 18.375  98.956  1.00 26.44 ? 399  ASP B CA    1 
ATOM   11811 C  C     . ASP B 1  401  ? -20.450 17.083  98.436  1.00 25.90 ? 399  ASP B C     1 
ATOM   11812 O  O     . ASP B 1  401  ? -20.644 16.133  99.199  1.00 25.55 ? 399  ASP B O     1 
ATOM   11813 C  CB    . ASP B 1  401  ? -20.927 19.420  99.200  1.00 26.75 ? 399  ASP B CB    1 
ATOM   11814 C  CG    . ASP B 1  401  ? -20.445 20.572  100.054 1.00 32.98 ? 399  ASP B CG    1 
ATOM   11815 O  OD1   . ASP B 1  401  ? -19.482 20.372  100.832 1.00 30.77 ? 399  ASP B OD1   1 
ATOM   11816 O  OD2   . ASP B 1  401  ? -21.015 21.679  99.947  1.00 29.44 ? 399  ASP B OD2   1 
ATOM   11817 N  N     . VAL B 1  402  ? -20.785 17.036  97.146  1.00 25.28 ? 400  VAL B N     1 
ATOM   11818 C  CA    . VAL B 1  402  ? -21.308 15.807  96.555  1.00 26.71 ? 400  VAL B CA    1 
ATOM   11819 C  C     . VAL B 1  402  ? -20.263 14.705  96.613  1.00 26.01 ? 400  VAL B C     1 
ATOM   11820 O  O     . VAL B 1  402  ? -20.567 13.550  96.947  1.00 28.01 ? 400  VAL B O     1 
ATOM   11821 C  CB    . VAL B 1  402  ? -21.769 16.072  95.110  1.00 28.13 ? 400  VAL B CB    1 
ATOM   11822 C  CG1   . VAL B 1  402  ? -22.097 14.764  94.395  1.00 29.29 ? 400  VAL B CG1   1 
ATOM   11823 C  CG2   . VAL B 1  402  ? -22.950 17.027  95.113  1.00 31.44 ? 400  VAL B CG2   1 
ATOM   11824 N  N     . SER B 1  403  ? -19.013 15.041  96.282  1.00 24.57 ? 401  SER B N     1 
ATOM   11825 C  CA    . SER B 1  403  ? -17.929 14.069  96.377  1.00 26.46 ? 401  SER B CA    1 
ATOM   11826 C  C     . SER B 1  403  ? -17.815 13.505  97.790  1.00 23.94 ? 401  SER B C     1 
ATOM   11827 O  O     . SER B 1  403  ? -17.668 12.292  97.975  1.00 24.33 ? 401  SER B O     1 
ATOM   11828 C  CB    . SER B 1  403  ? -16.617 14.725  95.946  1.00 22.64 ? 401  SER B CB    1 
ATOM   11829 O  OG    . SER B 1  403  ? -15.517 13.858  96.143  1.00 24.34 ? 401  SER B OG    1 
ATOM   11830 N  N     . TYR B 1  404  ? -17.913 14.371  98.797  1.00 25.82 ? 402  TYR B N     1 
ATOM   11831 C  CA    . TYR B 1  404  ? -17.841 13.924  100.184 1.00 26.78 ? 402  TYR B CA    1 
ATOM   11832 C  C     . TYR B 1  404  ? -18.943 12.918  100.488 1.00 26.58 ? 402  TYR B C     1 
ATOM   11833 O  O     . TYR B 1  404  ? -18.689 11.840  101.036 1.00 26.78 ? 402  TYR B O     1 
ATOM   11834 C  CB    . TYR B 1  404  ? -17.935 15.140  101.102 1.00 24.22 ? 402  TYR B CB    1 
ATOM   11835 C  CG    . TYR B 1  404  ? -17.534 14.893  102.538 1.00 24.42 ? 402  TYR B CG    1 
ATOM   11836 C  CD1   . TYR B 1  404  ? -18.398 14.271  103.428 1.00 26.48 ? 402  TYR B CD1   1 
ATOM   11837 C  CD2   . TYR B 1  404  ? -16.292 15.299  103.004 1.00 26.59 ? 402  TYR B CD2   1 
ATOM   11838 C  CE1   . TYR B 1  404  ? -18.032 14.055  104.741 1.00 28.03 ? 402  TYR B CE1   1 
ATOM   11839 C  CE2   . TYR B 1  404  ? -15.918 15.093  104.317 1.00 25.10 ? 402  TYR B CE2   1 
ATOM   11840 C  CZ    . TYR B 1  404  ? -16.793 14.472  105.181 1.00 27.69 ? 402  TYR B CZ    1 
ATOM   11841 O  OH    . TYR B 1  404  ? -16.423 14.262  106.489 1.00 29.86 ? 402  TYR B OH    1 
ATOM   11842 N  N     . ILE B 1  405  ? -20.179 13.241  100.101 1.00 27.62 ? 403  ILE B N     1 
ATOM   11843 C  CA    . ILE B 1  405  ? -21.305 12.365  100.410 1.00 27.66 ? 403  ILE B CA    1 
ATOM   11844 C  C     . ILE B 1  405  ? -21.187 11.042  99.656  1.00 27.63 ? 403  ILE B C     1 
ATOM   11845 O  O     . ILE B 1  405  ? -21.462 9.973   100.210 1.00 29.53 ? 403  ILE B O     1 
ATOM   11846 C  CB    . ILE B 1  405  ? -22.628 13.097  100.114 1.00 28.84 ? 403  ILE B CB    1 
ATOM   11847 C  CG1   . ILE B 1  405  ? -22.778 14.302  101.047 1.00 31.77 ? 403  ILE B CG1   1 
ATOM   11848 C  CG2   . ILE B 1  405  ? -23.801 12.178  100.289 1.00 28.61 ? 403  ILE B CG2   1 
ATOM   11849 C  CD1   . ILE B 1  405  ? -23.785 15.328  100.585 1.00 35.79 ? 403  ILE B CD1   1 
ATOM   11850 N  N     . ALA B 1  406  ? -20.763 11.088  98.384  1.00 28.42 ? 404  ALA B N     1 
ATOM   11851 C  CA    . ALA B 1  406  ? -20.535 9.859   97.624  1.00 27.38 ? 404  ALA B CA    1 
ATOM   11852 C  C     . ALA B 1  406  ? -19.460 8.994   98.270  1.00 27.42 ? 404  ALA B C     1 
ATOM   11853 O  O     . ALA B 1  406  ? -19.584 7.764   98.330  1.00 28.44 ? 404  ALA B O     1 
ATOM   11854 C  CB    . ALA B 1  406  ? -20.132 10.205  96.185  1.00 27.72 ? 404  ALA B CB    1 
ATOM   11855 N  N     . CYS B 1  407  ? -18.379 9.620   98.734  1.00 27.27 ? 405  CYS B N     1 
ATOM   11856 C  CA    . CYS B 1  407  ? -17.309 8.871   99.376  1.00 27.90 ? 405  CYS B CA    1 
ATOM   11857 C  C     . CYS B 1  407  ? -17.726 8.373   100.759 1.00 26.74 ? 405  CYS B C     1 
ATOM   11858 O  O     . CYS B 1  407  ? -17.318 7.280   101.172 1.00 26.90 ? 405  CYS B O     1 
ATOM   11859 C  CB    . CYS B 1  407  ? -16.053 9.744   99.433  1.00 24.60 ? 405  CYS B CB    1 
ATOM   11860 S  SG    . CYS B 1  407  ? -15.311 9.998   97.768  1.00 28.95 ? 405  CYS B SG    1 
ATOM   11861 N  N     . ALA B 1  408  ? -18.564 9.135   101.469 1.00 27.27 ? 406  ALA B N     1 
ATOM   11862 C  CA    . ALA B 1  408  ? -19.128 8.632   102.720 1.00 29.89 ? 406  ALA B CA    1 
ATOM   11863 C  C     . ALA B 1  408  ? -19.963 7.383   102.478 1.00 28.55 ? 406  ALA B C     1 
ATOM   11864 O  O     . ALA B 1  408  ? -19.910 6.432   103.263 1.00 31.54 ? 406  ALA B O     1 
ATOM   11865 C  CB    . ALA B 1  408  ? -19.973 9.711   103.398 1.00 29.73 ? 406  ALA B CB    1 
ATOM   11866 N  N     . ALA B 1  409  ? -20.720 7.354   101.377 1.00 28.85 ? 407  ALA B N     1 
ATOM   11867 C  CA    . ALA B 1  409  ? -21.505 6.167   101.065 1.00 31.83 ? 407  ALA B CA    1 
ATOM   11868 C  C     . ALA B 1  409  ? -20.603 4.961   100.846 1.00 31.90 ? 407  ALA B C     1 
ATOM   11869 O  O     . ALA B 1  409  ? -20.903 3.858   101.313 1.00 32.31 ? 407  ALA B O     1 
ATOM   11870 C  CB    . ALA B 1  409  ? -22.386 6.424   99.840  1.00 28.99 ? 407  ALA B CB    1 
ATOM   11871 N  N     . LYS B 1  410  ? -19.474 5.159   100.162 1.00 30.31 ? 408  LYS B N     1 
ATOM   11872 C  CA    . LYS B 1  410  ? -18.534 4.063   99.953  1.00 28.58 ? 408  LYS B CA    1 
ATOM   11873 C  C     . LYS B 1  410  ? -17.916 3.608   101.268 1.00 31.07 ? 408  LYS B C     1 
ATOM   11874 O  O     . LYS B 1  410  ? -17.781 2.404   101.517 1.00 31.62 ? 408  LYS B O     1 
ATOM   11875 C  CB    . LYS B 1  410  ? -17.449 4.499   98.970  1.00 27.20 ? 408  LYS B CB    1 
ATOM   11876 C  CG    . LYS B 1  410  ? -16.450 3.424   98.621  1.00 26.23 ? 408  LYS B CG    1 
ATOM   11877 C  CD    . LYS B 1  410  ? -15.266 4.014   97.878  1.00 27.63 ? 408  LYS B CD    1 
ATOM   11878 C  CE    . LYS B 1  410  ? -15.654 4.580   96.514  1.00 26.78 ? 408  LYS B CE    1 
ATOM   11879 N  NZ    . LYS B 1  410  ? -16.027 3.480   95.572  1.00 27.26 ? 408  LYS B NZ    1 
ATOM   11880 N  N     . LEU B 1  411  ? -17.526 4.559   102.117 1.00 29.63 ? 409  LEU B N     1 
ATOM   11881 C  CA    . LEU B 1  411  ? -16.931 4.212   103.403 1.00 29.83 ? 409  LEU B CA    1 
ATOM   11882 C  C     . LEU B 1  411  ? -17.922 3.461   104.278 1.00 31.66 ? 409  LEU B C     1 
ATOM   11883 O  O     . LEU B 1  411  ? -17.589 2.428   104.867 1.00 32.91 ? 409  LEU B O     1 
ATOM   11884 C  CB    . LEU B 1  411  ? -16.449 5.476   104.101 1.00 25.95 ? 409  LEU B CB    1 
ATOM   11885 C  CG    . LEU B 1  411  ? -15.112 5.993   103.572 1.00 30.26 ? 409  LEU B CG    1 
ATOM   11886 C  CD1   . LEU B 1  411  ? -14.841 7.372   104.126 1.00 28.68 ? 409  LEU B CD1   1 
ATOM   11887 C  CD2   . LEU B 1  411  ? -13.999 5.026   103.940 1.00 29.36 ? 409  LEU B CD2   1 
ATOM   11888 N  N     . LEU B 1  412  ? -19.155 3.963   104.362 1.00 34.38 ? 410  LEU B N     1 
ATOM   11889 C  CA    . LEU B 1  412  ? -20.153 3.342   105.225 1.00 34.09 ? 410  LEU B CA    1 
ATOM   11890 C  C     . LEU B 1  412  ? -20.525 1.940   104.763 1.00 34.83 ? 410  LEU B C     1 
ATOM   11891 O  O     . LEU B 1  412  ? -20.964 1.130   105.582 1.00 37.87 ? 410  LEU B O     1 
ATOM   11892 C  CB    . LEU B 1  412  ? -21.385 4.242   105.307 1.00 33.56 ? 410  LEU B CB    1 
ATOM   11893 C  CG    . LEU B 1  412  ? -21.164 5.459   106.214 1.00 37.01 ? 410  LEU B CG    1 
ATOM   11894 C  CD1   . LEU B 1  412  ? -22.199 6.541   105.982 1.00 38.31 ? 410  LEU B CD1   1 
ATOM   11895 C  CD2   . LEU B 1  412  ? -21.167 5.023   107.677 1.00 37.58 ? 410  LEU B CD2   1 
ATOM   11896 N  N     . ALA B 1  413  ? -20.348 1.629   103.480 1.00 36.17 ? 411  ALA B N     1 
ATOM   11897 C  CA    . ALA B 1  413  ? -20.575 0.275   102.994 1.00 36.93 ? 411  ALA B CA    1 
ATOM   11898 C  C     . ALA B 1  413  ? -19.395 -0.650  103.253 1.00 37.30 ? 411  ALA B C     1 
ATOM   11899 O  O     . ALA B 1  413  ? -19.498 -1.851  102.977 1.00 40.71 ? 411  ALA B O     1 
ATOM   11900 C  CB    . ALA B 1  413  ? -20.897 0.300   101.497 1.00 37.85 ? 411  ALA B CB    1 
ATOM   11901 N  N     . ALA B 1  414  ? -18.285 -0.130  103.788 1.00 36.36 ? 412  ALA B N     1 
ATOM   11902 C  CA    . ALA B 1  414  ? -17.099 -0.929  104.069 1.00 35.88 ? 412  ALA B CA    1 
ATOM   11903 C  C     . ALA B 1  414  ? -16.668 -0.824  105.531 1.00 37.47 ? 412  ALA B C     1 
ATOM   11904 O  O     . ALA B 1  414  ? -15.496 -1.060  105.845 1.00 37.44 ? 412  ALA B O     1 
ATOM   11905 C  CB    . ALA B 1  414  ? -15.948 -0.517  103.145 1.00 34.47 ? 412  ALA B CB    1 
ATOM   11906 N  N     . THR B 1  415  ? -17.594 -0.478  106.435 1.00 36.77 ? 413  THR B N     1 
ATOM   11907 C  CA    . THR B 1  415  ? -17.255 -0.342  107.851 1.00 34.76 ? 413  THR B CA    1 
ATOM   11908 C  C     . THR B 1  415  ? -16.700 -1.630  108.441 1.00 37.24 ? 413  THR B C     1 
ATOM   11909 O  O     . THR B 1  415  ? -16.095 -1.597  109.523 1.00 35.98 ? 413  THR B O     1 
ATOM   11910 C  CB    . THR B 1  415  ? -18.475 0.090   108.657 1.00 36.47 ? 413  THR B CB    1 
ATOM   11911 O  OG1   . THR B 1  415  ? -19.512 -0.880  108.495 1.00 38.71 ? 413  THR B OG1   1 
ATOM   11912 C  CG2   . THR B 1  415  ? -18.976 1.436   108.188 1.00 37.22 ? 413  THR B CG2   1 
ATOM   11913 N  N     . ASP B 1  416  ? -16.900 -2.762  107.765 1.00 38.28 ? 414  ASP B N     1 
ATOM   11914 C  CA    . ASP B 1  416  ? -16.292 -4.008  108.199 1.00 35.42 ? 414  ASP B CA    1 
ATOM   11915 C  C     . ASP B 1  416  ? -14.812 -4.063  107.859 1.00 33.56 ? 414  ASP B C     1 
ATOM   11916 O  O     . ASP B 1  416  ? -14.089 -4.878  108.440 1.00 40.07 ? 414  ASP B O     1 
ATOM   11917 C  CB    . ASP B 1  416  ? -17.022 -5.196  107.565 1.00 34.27 ? 414  ASP B CB    1 
ATOM   11918 N  N     . VAL B 1  417  ? -14.341 -3.216  106.940 1.00 36.54 ? 415  VAL B N     1 
ATOM   11919 C  CA    . VAL B 1  417  ? -12.949 -3.228  106.521 1.00 31.48 ? 415  VAL B CA    1 
ATOM   11920 C  C     . VAL B 1  417  ? -12.213 -1.949  106.903 1.00 28.86 ? 415  VAL B C     1 
ATOM   11921 O  O     . VAL B 1  417  ? -10.984 -1.971  107.006 1.00 32.67 ? 415  VAL B O     1 
ATOM   11922 C  CB    . VAL B 1  417  ? -12.832 -3.474  105.000 1.00 40.62 ? 415  VAL B CB    1 
ATOM   11923 N  N     . VAL B 1  418  ? -12.915 -0.831  107.063 1.00 32.16 ? 416  VAL B N     1 
ATOM   11924 C  CA    . VAL B 1  418  ? -12.291 0.446   107.382 1.00 29.37 ? 416  VAL B CA    1 
ATOM   11925 C  C     . VAL B 1  418  ? -13.142 1.151   108.424 1.00 33.16 ? 416  VAL B C     1 
ATOM   11926 O  O     . VAL B 1  418  ? -14.346 0.905   108.546 1.00 32.54 ? 416  VAL B O     1 
ATOM   11927 C  CB    . VAL B 1  418  ? -12.108 1.346   106.134 1.00 31.25 ? 416  VAL B CB    1 
ATOM   11928 C  CG1   . VAL B 1  418  ? -11.103 0.733   105.176 1.00 26.75 ? 416  VAL B CG1   1 
ATOM   11929 C  CG2   . VAL B 1  418  ? -13.453 1.586   105.432 1.00 30.23 ? 416  VAL B CG2   1 
ATOM   11930 N  N     . PHE B 1  419  ? -12.499 2.028   109.190 1.00 28.52 ? 417  PHE B N     1 
ATOM   11931 C  CA    . PHE B 1  419  ? -13.178 2.806   110.216 1.00 27.99 ? 417  PHE B CA    1 
ATOM   11932 C  C     . PHE B 1  419  ? -13.373 4.225   109.696 1.00 29.65 ? 417  PHE B C     1 
ATOM   11933 O  O     . PHE B 1  419  ? -12.416 5.019   109.693 1.00 26.00 ? 417  PHE B O     1 
ATOM   11934 C  CB    . PHE B 1  419  ? -12.366 2.807   111.517 1.00 29.35 ? 417  PHE B CB    1 
ATOM   11935 C  CG    . PHE B 1  419  ? -12.970 3.634   112.612 1.00 31.03 ? 417  PHE B CG    1 
ATOM   11936 C  CD1   . PHE B 1  419  ? -14.238 3.349   113.099 1.00 31.08 ? 417  PHE B CD1   1 
ATOM   11937 C  CD2   . PHE B 1  419  ? -12.264 4.684   113.174 1.00 26.70 ? 417  PHE B CD2   1 
ATOM   11938 C  CE1   . PHE B 1  419  ? -14.796 4.109   114.114 1.00 33.79 ? 417  PHE B CE1   1 
ATOM   11939 C  CE2   . PHE B 1  419  ? -12.811 5.448   114.192 1.00 26.45 ? 417  PHE B CE2   1 
ATOM   11940 C  CZ    . PHE B 1  419  ? -14.081 5.161   114.664 1.00 30.33 ? 417  PHE B CZ    1 
ATOM   11941 N  N     . PRO B 1  420  ? -14.561 4.586   109.217 1.00 27.77 ? 418  PRO B N     1 
ATOM   11942 C  CA    . PRO B 1  420  ? -14.744 5.909   108.615 1.00 25.19 ? 418  PRO B CA    1 
ATOM   11943 C  C     . PRO B 1  420  ? -14.823 6.999   109.670 1.00 29.06 ? 418  PRO B C     1 
ATOM   11944 O  O     . PRO B 1  420  ? -15.487 6.862   110.699 1.00 27.49 ? 418  PRO B O     1 
ATOM   11945 C  CB    . PRO B 1  420  ? -16.071 5.771   107.853 1.00 27.83 ? 418  PRO B CB    1 
ATOM   11946 C  CG    . PRO B 1  420  ? -16.303 4.292   107.738 1.00 28.21 ? 418  PRO B CG    1 
ATOM   11947 C  CD    . PRO B 1  420  ? -15.744 3.733   109.016 1.00 28.25 ? 418  PRO B CD    1 
ATOM   11948 N  N     . GLN B 1  421  ? -14.118 8.094   109.408 1.00 26.82 ? 419  GLN B N     1 
ATOM   11949 C  CA    . GLN B 1  421  ? -14.062 9.235   110.314 1.00 27.28 ? 419  GLN B CA    1 
ATOM   11950 C  C     . GLN B 1  421  ? -14.430 10.470  109.502 1.00 27.96 ? 419  GLN B C     1 
ATOM   11951 O  O     . GLN B 1  421  ? -13.663 10.901  108.635 1.00 24.08 ? 419  GLN B O     1 
ATOM   11952 C  CB    . GLN B 1  421  ? -12.667 9.358   110.947 1.00 25.00 ? 419  GLN B CB    1 
ATOM   11953 C  CG    . GLN B 1  421  ? -12.218 8.074   111.644 1.00 24.47 ? 419  GLN B CG    1 
ATOM   11954 C  CD    . GLN B 1  421  ? -10.722 8.032   111.932 1.00 25.21 ? 419  GLN B CD    1 
ATOM   11955 O  OE1   . GLN B 1  421  ? -10.303 7.798   113.069 1.00 25.52 ? 419  GLN B OE1   1 
ATOM   11956 N  NE2   . GLN B 1  421  ? -9.919  8.225   110.903 1.00 23.28 ? 419  GLN B NE2   1 
ATOM   11957 N  N     . PHE B 1  422  ? -15.609 11.030  109.755 1.00 27.73 ? 420  PHE B N     1 
ATOM   11958 C  CA    . PHE B 1  422  ? -16.154 12.086  108.902 1.00 25.29 ? 420  PHE B CA    1 
ATOM   11959 C  C     . PHE B 1  422  ? -15.847 13.441  109.524 1.00 27.29 ? 420  PHE B C     1 
ATOM   11960 O  O     . PHE B 1  422  ? -16.571 13.946  110.387 1.00 27.20 ? 420  PHE B O     1 
ATOM   11961 C  CB    . PHE B 1  422  ? -17.644 11.861  108.664 1.00 25.64 ? 420  PHE B CB    1 
ATOM   11962 C  CG    . PHE B 1  422  ? -17.927 10.558  107.989 1.00 28.68 ? 420  PHE B CG    1 
ATOM   11963 C  CD1   . PHE B 1  422  ? -17.551 10.362  106.672 1.00 29.19 ? 420  PHE B CD1   1 
ATOM   11964 C  CD2   . PHE B 1  422  ? -18.532 9.516   108.671 1.00 30.37 ? 420  PHE B CD2   1 
ATOM   11965 C  CE1   . PHE B 1  422  ? -17.786 9.156   106.045 1.00 29.92 ? 420  PHE B CE1   1 
ATOM   11966 C  CE2   . PHE B 1  422  ? -18.771 8.306   108.040 1.00 31.68 ? 420  PHE B CE2   1 
ATOM   11967 C  CZ    . PHE B 1  422  ? -18.399 8.135   106.719 1.00 28.59 ? 420  PHE B CZ    1 
ATOM   11968 N  N     . ALA B 1  423  ? -14.744 14.027  109.070 1.00 24.62 ? 421  ALA B N     1 
ATOM   11969 C  CA    . ALA B 1  423  ? -14.288 15.323  109.540 1.00 25.60 ? 421  ALA B CA    1 
ATOM   11970 C  C     . ALA B 1  423  ? -14.997 16.418  108.755 1.00 28.78 ? 421  ALA B C     1 
ATOM   11971 O  O     . ALA B 1  423  ? -14.687 16.647  107.583 1.00 28.05 ? 421  ALA B O     1 
ATOM   11972 C  CB    . ALA B 1  423  ? -12.774 15.427  109.376 1.00 23.86 ? 421  ALA B CB    1 
ATOM   11973 N  N     . THR B 1  424  ? -15.919 17.122  109.407 1.00 29.47 ? 422  THR B N     1 
ATOM   11974 C  CA    . THR B 1  424  ? -16.612 18.236  108.773 1.00 29.83 ? 422  THR B CA    1 
ATOM   11975 C  C     . THR B 1  424  ? -17.263 19.083  109.853 1.00 28.60 ? 422  THR B C     1 
ATOM   11976 O  O     . THR B 1  424  ? -17.663 18.574  110.899 1.00 30.75 ? 422  THR B O     1 
ATOM   11977 C  CB    . THR B 1  424  ? -17.675 17.757  107.767 1.00 31.38 ? 422  THR B CB    1 
ATOM   11978 O  OG1   . THR B 1  424  ? -18.247 18.892  107.109 1.00 30.12 ? 422  THR B OG1   1 
ATOM   11979 C  CG2   . THR B 1  424  ? -18.774 16.984  108.480 1.00 32.31 ? 422  THR B CG2   1 
ATOM   11980 N  N     . HIS B 1  425  ? -17.333 20.387  109.600 1.00 31.22 ? 423  HIS B N     1 
ATOM   11981 C  CA    . HIS B 1  425  ? -18.090 21.295  110.451 1.00 33.60 ? 423  HIS B CA    1 
ATOM   11982 C  C     . HIS B 1  425  ? -19.411 21.697  109.818 1.00 37.04 ? 423  HIS B C     1 
ATOM   11983 O  O     . HIS B 1  425  ? -20.092 22.591  110.332 1.00 36.52 ? 423  HIS B O     1 
ATOM   11984 C  CB    . HIS B 1  425  ? -17.262 22.535  110.762 1.00 31.13 ? 423  HIS B CB    1 
ATOM   11985 C  CG    . HIS B 1  425  ? -15.921 22.224  111.342 1.00 33.76 ? 423  HIS B CG    1 
ATOM   11986 N  ND1   . HIS B 1  425  ? -14.746 22.431  110.652 1.00 39.92 ? 423  HIS B ND1   1 
ATOM   11987 C  CD2   . HIS B 1  425  ? -15.568 21.694  112.537 1.00 35.13 ? 423  HIS B CD2   1 
ATOM   11988 C  CE1   . HIS B 1  425  ? -13.725 22.063  111.407 1.00 35.58 ? 423  HIS B CE1   1 
ATOM   11989 N  NE2   . HIS B 1  425  ? -14.197 21.614  112.555 1.00 31.30 ? 423  HIS B NE2   1 
ATOM   11990 N  N     . ASN B 1  426  ? -19.784 21.050  108.718 1.00 36.29 ? 424  ASN B N     1 
ATOM   11991 C  CA    . ASN B 1  426  ? -20.965 21.408  107.942 1.00 37.90 ? 424  ASN B CA    1 
ATOM   11992 C  C     . ASN B 1  426  ? -22.146 20.586  108.450 1.00 35.01 ? 424  ASN B C     1 
ATOM   11993 O  O     . ASN B 1  426  ? -22.165 19.357  108.310 1.00 33.05 ? 424  ASN B O     1 
ATOM   11994 C  CB    . ASN B 1  426  ? -20.685 21.163  106.459 1.00 34.20 ? 424  ASN B CB    1 
ATOM   11995 C  CG    . ASN B 1  426  ? -21.788 21.671  105.554 1.00 37.53 ? 424  ASN B CG    1 
ATOM   11996 O  OD1   . ASN B 1  426  ? -22.972 21.476  105.822 1.00 37.19 ? 424  ASN B OD1   1 
ATOM   11997 N  ND2   . ASN B 1  426  ? -21.396 22.320  104.459 1.00 34.85 ? 424  ASN B ND2   1 
ATOM   11998 N  N     . ALA B 1  427  ? -23.144 21.266  109.030 1.00 39.17 ? 425  ALA B N     1 
ATOM   11999 C  CA    . ALA B 1  427  ? -24.292 20.560  109.593 1.00 38.43 ? 425  ALA B CA    1 
ATOM   12000 C  C     . ALA B 1  427  ? -25.124 19.869  108.521 1.00 36.45 ? 425  ALA B C     1 
ATOM   12001 O  O     . ALA B 1  427  ? -25.744 18.833  108.795 1.00 37.02 ? 425  ALA B O     1 
ATOM   12002 C  CB    . ALA B 1  427  ? -25.170 21.518  110.396 1.00 42.58 ? 425  ALA B CB    1 
ATOM   12003 N  N     . GLN B 1  428  ? -25.160 20.420  107.305 1.00 35.56 ? 426  GLN B N     1 
ATOM   12004 C  CA    . GLN B 1  428  ? -25.843 19.724  106.222 1.00 37.76 ? 426  GLN B CA    1 
ATOM   12005 C  C     . GLN B 1  428  ? -25.103 18.442  105.861 1.00 35.59 ? 426  GLN B C     1 
ATOM   12006 O  O     . GLN B 1  428  ? -25.711 17.372  105.762 1.00 33.79 ? 426  GLN B O     1 
ATOM   12007 C  CB    . GLN B 1  428  ? -25.994 20.642  105.005 1.00 38.48 ? 426  GLN B CB    1 
ATOM   12008 C  CG    . GLN B 1  428  ? -27.002 20.138  103.965 1.00 42.56 ? 426  GLN B CG    1 
ATOM   12009 C  CD    . GLN B 1  428  ? -26.489 18.944  103.179 1.00 41.25 ? 426  GLN B CD    1 
ATOM   12010 O  OE1   . GLN B 1  428  ? -25.333 18.931  102.734 1.00 37.57 ? 426  GLN B OE1   1 
ATOM   12011 N  NE2   . GLN B 1  428  ? -27.328 17.925  103.026 1.00 39.52 ? 426  GLN B NE2   1 
ATOM   12012 N  N     . THR B 1  429  ? -23.780 18.529  105.675 1.00 37.77 ? 427  THR B N     1 
ATOM   12013 C  CA    . THR B 1  429  ? -22.996 17.327  105.410 1.00 35.27 ? 427  THR B CA    1 
ATOM   12014 C  C     . THR B 1  429  ? -23.160 16.307  106.530 1.00 34.07 ? 427  THR B C     1 
ATOM   12015 O  O     . THR B 1  429  ? -23.336 15.108  106.277 1.00 30.95 ? 427  THR B O     1 
ATOM   12016 C  CB    . THR B 1  429  ? -21.519 17.681  105.242 1.00 34.17 ? 427  THR B CB    1 
ATOM   12017 O  OG1   . THR B 1  429  ? -21.378 18.767  104.322 1.00 30.14 ? 427  THR B OG1   1 
ATOM   12018 C  CG2   . THR B 1  429  ? -20.761 16.480  104.735 1.00 32.92 ? 427  THR B CG2   1 
ATOM   12019 N  N     . LEU B 1  430  ? -23.087 16.768  107.783 1.00 35.22 ? 428  LEU B N     1 
ATOM   12020 C  CA    . LEU B 1  430  ? -23.221 15.867  108.923 1.00 35.31 ? 428  LEU B CA    1 
ATOM   12021 C  C     . LEU B 1  430  ? -24.589 15.200  108.932 1.00 34.99 ? 428  LEU B C     1 
ATOM   12022 O  O     . LEU B 1  430  ? -24.693 13.976  109.070 1.00 30.73 ? 428  LEU B O     1 
ATOM   12023 C  CB    . LEU B 1  430  ? -22.990 16.637  110.226 1.00 34.63 ? 428  LEU B CB    1 
ATOM   12024 C  CG    . LEU B 1  430  ? -22.844 15.907  111.573 1.00 35.04 ? 428  LEU B CG    1 
ATOM   12025 C  CD1   . LEU B 1  430  ? -22.350 16.907  112.596 1.00 34.52 ? 428  LEU B CD1   1 
ATOM   12026 C  CD2   . LEU B 1  430  ? -24.122 15.246  112.089 1.00 40.16 ? 428  LEU B CD2   1 
ATOM   12027 N  N     . ALA B 1  431  ? -25.653 15.996  108.807 1.00 37.71 ? 429  ALA B N     1 
ATOM   12028 C  CA    . ALA B 1  431  ? -27.001 15.434  108.844 1.00 36.66 ? 429  ALA B CA    1 
ATOM   12029 C  C     . ALA B 1  431  ? -27.184 14.383  107.758 1.00 35.26 ? 429  ALA B C     1 
ATOM   12030 O  O     . ALA B 1  431  ? -27.744 13.309  108.012 1.00 40.84 ? 429  ALA B O     1 
ATOM   12031 C  CB    . ALA B 1  431  ? -28.039 16.546  108.698 1.00 37.49 ? 429  ALA B CB    1 
ATOM   12032 N  N     . ALA B 1  432  ? -26.674 14.660  106.551 1.00 39.97 ? 430  ALA B N     1 
ATOM   12033 C  CA    . ALA B 1  432  ? -26.802 13.717  105.444 1.00 35.22 ? 430  ALA B CA    1 
ATOM   12034 C  C     . ALA B 1  432  ? -26.158 12.380  105.779 1.00 34.39 ? 430  ALA B C     1 
ATOM   12035 O  O     . ALA B 1  432  ? -26.736 11.320  105.525 1.00 37.68 ? 430  ALA B O     1 
ATOM   12036 C  CB    . ALA B 1  432  ? -26.185 14.314  104.178 1.00 35.95 ? 430  ALA B CB    1 
ATOM   12037 N  N     . ILE B 1  433  ? -24.953 12.408  106.351 1.00 36.84 ? 431  ILE B N     1 
ATOM   12038 C  CA    . ILE B 1  433  ? -24.264 11.163  106.673 1.00 34.78 ? 431  ILE B CA    1 
ATOM   12039 C  C     . ILE B 1  433  ? -24.857 10.510  107.913 1.00 35.51 ? 431  ILE B C     1 
ATOM   12040 O  O     . ILE B 1  433  ? -24.890 9.279   108.022 1.00 32.93 ? 431  ILE B O     1 
ATOM   12041 C  CB    . ILE B 1  433  ? -22.761 11.432  106.842 1.00 34.81 ? 431  ILE B CB    1 
ATOM   12042 C  CG1   . ILE B 1  433  ? -22.201 12.003  105.541 1.00 34.94 ? 431  ILE B CG1   1 
ATOM   12043 C  CG2   . ILE B 1  433  ? -22.028 10.159  107.264 1.00 36.10 ? 431  ILE B CG2   1 
ATOM   12044 C  CD1   . ILE B 1  433  ? -20.784 12.404  105.654 1.00 34.72 ? 431  ILE B CD1   1 
ATOM   12045 N  N     . TYR B 1  434  ? -25.294 11.320  108.880 1.00 36.77 ? 432  TYR B N     1 
ATOM   12046 C  CA    . TYR B 1  434  ? -25.973 10.792  110.059 1.00 37.30 ? 432  TYR B CA    1 
ATOM   12047 C  C     . TYR B 1  434  ? -27.150 9.911   109.656 1.00 38.30 ? 432  TYR B C     1 
ATOM   12048 O  O     . TYR B 1  434  ? -27.295 8.781   110.136 1.00 41.54 ? 432  TYR B O     1 
ATOM   12049 C  CB    . TYR B 1  434  ? -26.422 11.957  110.944 1.00 37.15 ? 432  TYR B CB    1 
ATOM   12050 C  CG    . TYR B 1  434  ? -27.343 11.605  112.094 1.00 39.81 ? 432  TYR B CG    1 
ATOM   12051 C  CD1   . TYR B 1  434  ? -26.866 10.944  113.221 1.00 38.11 ? 432  TYR B CD1   1 
ATOM   12052 C  CD2   . TYR B 1  434  ? -28.686 11.969  112.068 1.00 42.49 ? 432  TYR B CD2   1 
ATOM   12053 C  CE1   . TYR B 1  434  ? -27.706 10.636  114.287 1.00 37.88 ? 432  TYR B CE1   1 
ATOM   12054 C  CE2   . TYR B 1  434  ? -29.536 11.665  113.126 1.00 42.84 ? 432  TYR B CE2   1 
ATOM   12055 C  CZ    . TYR B 1  434  ? -29.039 10.998  114.231 1.00 43.38 ? 432  TYR B CZ    1 
ATOM   12056 O  OH    . TYR B 1  434  ? -29.872 10.695  115.284 1.00 38.92 ? 432  TYR B OH    1 
ATOM   12057 N  N     . HIS B 1  435  ? -27.974 10.392  108.726 1.00 40.07 ? 433  HIS B N     1 
ATOM   12058 C  CA    . HIS B 1  435  ? -29.118 9.595   108.298 1.00 41.00 ? 433  HIS B CA    1 
ATOM   12059 C  C     . HIS B 1  435  ? -28.719 8.543   107.270 1.00 39.66 ? 433  HIS B C     1 
ATOM   12060 O  O     . HIS B 1  435  ? -29.251 7.428   107.287 1.00 36.39 ? 433  HIS B O     1 
ATOM   12061 C  CB    . HIS B 1  435  ? -30.215 10.510  107.763 1.00 42.79 ? 433  HIS B CB    1 
ATOM   12062 C  CG    . HIS B 1  435  ? -30.860 11.341  108.827 1.00 43.56 ? 433  HIS B CG    1 
ATOM   12063 N  ND1   . HIS B 1  435  ? -31.699 10.803  109.778 1.00 43.82 ? 433  HIS B ND1   1 
ATOM   12064 C  CD2   . HIS B 1  435  ? -30.774 12.664  109.105 1.00 43.33 ? 433  HIS B CD2   1 
ATOM   12065 C  CE1   . HIS B 1  435  ? -32.110 11.759  110.591 1.00 45.78 ? 433  HIS B CE1   1 
ATOM   12066 N  NE2   . HIS B 1  435  ? -31.564 12.899  110.205 1.00 43.84 ? 433  HIS B NE2   1 
ATOM   12067 N  N     . MET B 1  436  ? -27.766 8.865   106.387 1.00 41.37 ? 434  MET B N     1 
ATOM   12068 C  CA    . MET B 1  436  ? -27.264 7.866   105.447 1.00 38.18 ? 434  MET B CA    1 
ATOM   12069 C  C     . MET B 1  436  ? -26.753 6.625   106.163 1.00 34.71 ? 434  MET B C     1 
ATOM   12070 O  O     . MET B 1  436  ? -26.841 5.514   105.627 1.00 39.79 ? 434  MET B O     1 
ATOM   12071 C  CB    . MET B 1  436  ? -26.156 8.470   104.581 1.00 37.14 ? 434  MET B CB    1 
ATOM   12072 C  CG    . MET B 1  436  ? -25.347 7.451   103.791 1.00 38.28 ? 434  MET B CG    1 
ATOM   12073 S  SD    . MET B 1  436  ? -23.945 8.200   102.924 1.00 42.19 ? 434  MET B SD    1 
ATOM   12074 C  CE    . MET B 1  436  ? -24.789 9.001   101.564 1.00 35.77 ? 434  MET B CE    1 
ATOM   12075 N  N     . ALA B 1  437  ? -26.227 6.787   107.370 1.00 36.24 ? 435  ALA B N     1 
ATOM   12076 C  CA    . ALA B 1  437  ? -25.723 5.658   108.132 1.00 34.76 ? 435  ALA B CA    1 
ATOM   12077 C  C     . ALA B 1  437  ? -26.870 4.885   108.777 1.00 38.35 ? 435  ALA B C     1 
ATOM   12078 O  O     . ALA B 1  437  ? -26.718 3.710   109.099 1.00 42.20 ? 435  ALA B O     1 
ATOM   12079 C  CB    . ALA B 1  437  ? -24.739 6.132   109.189 1.00 39.70 ? 435  ALA B CB    1 
ATOM   12080 N  N     . PHE B 1  441  ? -26.452 2.171   115.295 1.00 43.46 ? 439  PHE B N     1 
ATOM   12081 C  CA    . PHE B 1  441  ? -25.096 2.675   115.493 1.00 39.56 ? 439  PHE B CA    1 
ATOM   12082 C  C     . PHE B 1  441  ? -24.414 2.060   116.720 1.00 41.19 ? 439  PHE B C     1 
ATOM   12083 O  O     . PHE B 1  441  ? -25.073 1.612   117.659 1.00 39.49 ? 439  PHE B O     1 
ATOM   12084 C  CB    . PHE B 1  441  ? -25.106 4.202   115.629 1.00 37.04 ? 439  PHE B CB    1 
ATOM   12085 C  CG    . PHE B 1  441  ? -23.741 4.783   115.866 1.00 41.64 ? 439  PHE B CG    1 
ATOM   12086 C  CD1   . PHE B 1  441  ? -22.874 4.974   114.807 1.00 37.92 ? 439  PHE B CD1   1 
ATOM   12087 C  CD2   . PHE B 1  441  ? -23.311 5.095   117.148 1.00 39.60 ? 439  PHE B CD2   1 
ATOM   12088 C  CE1   . PHE B 1  441  ? -21.604 5.488   115.007 1.00 38.21 ? 439  PHE B CE1   1 
ATOM   12089 C  CE2   . PHE B 1  441  ? -22.041 5.606   117.361 1.00 40.76 ? 439  PHE B CE2   1 
ATOM   12090 C  CZ    . PHE B 1  441  ? -21.187 5.799   116.283 1.00 39.04 ? 439  PHE B CZ    1 
ATOM   12091 N  N     . HIS B 1  442  ? -23.084 2.039   116.703 1.00 40.40 ? 440  HIS B N     1 
ATOM   12092 C  CA    . HIS B 1  442  ? -22.307 1.674   117.878 1.00 41.57 ? 440  HIS B CA    1 
ATOM   12093 C  C     . HIS B 1  442  ? -20.945 2.341   117.777 1.00 38.23 ? 440  HIS B C     1 
ATOM   12094 O  O     . HIS B 1  442  ? -20.485 2.685   116.685 1.00 39.13 ? 440  HIS B O     1 
ATOM   12095 C  CB    . HIS B 1  442  ? -22.145 0.159   118.008 1.00 40.50 ? 440  HIS B CB    1 
ATOM   12096 C  CG    . HIS B 1  442  ? -21.368 -0.457  116.889 1.00 42.93 ? 440  HIS B CG    1 
ATOM   12097 N  ND1   . HIS B 1  442  ? -21.971 -1.019  115.783 1.00 42.75 ? 440  HIS B ND1   1 
ATOM   12098 C  CD2   . HIS B 1  442  ? -20.032 -0.582  116.695 1.00 43.44 ? 440  HIS B CD2   1 
ATOM   12099 C  CE1   . HIS B 1  442  ? -21.040 -1.473  114.961 1.00 44.74 ? 440  HIS B CE1   1 
ATOM   12100 N  NE2   . HIS B 1  442  ? -19.855 -1.221  115.491 1.00 45.65 ? 440  HIS B NE2   1 
ATOM   12101 N  N     . VAL B 1  443  ? -20.297 2.517   118.928 1.00 38.02 ? 441  VAL B N     1 
ATOM   12102 C  CA    . VAL B 1  443  ? -18.952 3.089   118.933 1.00 41.57 ? 441  VAL B CA    1 
ATOM   12103 C  C     . VAL B 1  443  ? -17.998 2.113   118.255 1.00 38.60 ? 441  VAL B C     1 
ATOM   12104 O  O     . VAL B 1  443  ? -17.900 0.945   118.645 1.00 40.20 ? 441  VAL B O     1 
ATOM   12105 C  CB    . VAL B 1  443  ? -18.494 3.415   120.360 1.00 40.76 ? 441  VAL B CB    1 
ATOM   12106 C  CG1   . VAL B 1  443  ? -17.024 3.827   120.355 1.00 37.01 ? 441  VAL B CG1   1 
ATOM   12107 C  CG2   . VAL B 1  443  ? -19.360 4.521   120.953 1.00 38.54 ? 441  VAL B CG2   1 
ATOM   12108 N  N     . GLY B 1  444  ? -17.299 2.584   117.223 1.00 38.68 ? 442  GLY B N     1 
ATOM   12109 C  CA    . GLY B 1  444  ? -16.417 1.751   116.434 1.00 35.55 ? 442  GLY B CA    1 
ATOM   12110 C  C     . GLY B 1  444  ? -16.908 1.489   115.025 1.00 37.17 ? 442  GLY B C     1 
ATOM   12111 O  O     . GLY B 1  444  ? -16.116 1.051   114.176 1.00 32.70 ? 442  GLY B O     1 
ATOM   12112 N  N     . LYS B 1  445  ? -18.188 1.741   114.751 1.00 37.02 ? 443  LYS B N     1 
ATOM   12113 C  CA    . LYS B 1  445  ? -18.676 1.667   113.379 1.00 37.99 ? 443  LYS B CA    1 
ATOM   12114 C  C     . LYS B 1  445  ? -18.109 2.811   112.553 1.00 35.43 ? 443  LYS B C     1 
ATOM   12115 O  O     . LYS B 1  445  ? -17.519 2.595   111.489 1.00 36.78 ? 443  LYS B O     1 
ATOM   12116 C  CB    . LYS B 1  445  ? -20.206 1.694   113.361 1.00 35.64 ? 443  LYS B CB    1 
ATOM   12117 N  N     . TYR B 1  446  ? -18.277 4.036   113.039 1.00 35.67 ? 444  TYR B N     1 
ATOM   12118 C  CA    . TYR B 1  446  ? -17.725 5.228   112.413 1.00 33.20 ? 444  TYR B CA    1 
ATOM   12119 C  C     . TYR B 1  446  ? -17.779 6.340   113.450 1.00 31.57 ? 444  TYR B C     1 
ATOM   12120 O  O     . TYR B 1  446  ? -18.389 6.190   114.511 1.00 33.45 ? 444  TYR B O     1 
ATOM   12121 C  CB    . TYR B 1  446  ? -18.495 5.607   111.141 1.00 32.32 ? 444  TYR B CB    1 
ATOM   12122 C  CG    . TYR B 1  446  ? -19.872 6.180   111.396 1.00 36.72 ? 444  TYR B CG    1 
ATOM   12123 C  CD1   . TYR B 1  446  ? -20.985 5.351   111.479 1.00 37.02 ? 444  TYR B CD1   1 
ATOM   12124 C  CD2   . TYR B 1  446  ? -20.060 7.552   111.542 1.00 32.56 ? 444  TYR B CD2   1 
ATOM   12125 C  CE1   . TYR B 1  446  ? -22.239 5.866   111.713 1.00 39.25 ? 444  TYR B CE1   1 
ATOM   12126 C  CE2   . TYR B 1  446  ? -21.314 8.076   111.782 1.00 38.38 ? 444  TYR B CE2   1 
ATOM   12127 C  CZ    . TYR B 1  446  ? -22.400 7.228   111.867 1.00 37.42 ? 444  TYR B CZ    1 
ATOM   12128 O  OH    . TYR B 1  446  ? -23.655 7.741   112.092 1.00 44.40 ? 444  TYR B OH    1 
ATOM   12129 N  N     . GLU B 1  447  ? -17.133 7.459   113.138 1.00 31.00 ? 445  GLU B N     1 
ATOM   12130 C  CA    . GLU B 1  447  ? -17.190 8.613   114.018 1.00 28.73 ? 445  GLU B CA    1 
ATOM   12131 C  C     . GLU B 1  447  ? -17.203 9.874   113.182 1.00 29.26 ? 445  GLU B C     1 
ATOM   12132 O  O     . GLU B 1  447  ? -16.911 9.859   111.985 1.00 28.77 ? 445  GLU B O     1 
ATOM   12133 C  CB    . GLU B 1  447  ? -16.009 8.637   114.997 1.00 26.58 ? 445  GLU B CB    1 
ATOM   12134 C  CG    . GLU B 1  447  ? -14.668 8.776   114.308 1.00 26.26 ? 445  GLU B CG    1 
ATOM   12135 C  CD    . GLU B 1  447  ? -13.507 8.746   115.287 1.00 26.00 ? 445  GLU B CD    1 
ATOM   12136 O  OE1   . GLU B 1  447  ? -13.726 8.358   116.456 1.00 27.06 ? 445  GLU B OE1   1 
ATOM   12137 O  OE2   . GLU B 1  447  ? -12.383 9.110   114.876 1.00 25.63 ? 445  GLU B OE2   1 
ATOM   12138 N  N     . PHE B 1  448  ? -17.552 10.976  113.823 1.00 24.97 ? 446  PHE B N     1 
ATOM   12139 C  CA    . PHE B 1  448  ? -17.310 12.290  113.256 1.00 28.87 ? 446  PHE B CA    1 
ATOM   12140 C  C     . PHE B 1  448  ? -16.005 12.855  113.819 1.00 27.11 ? 446  PHE B C     1 
ATOM   12141 O  O     . PHE B 1  448  ? -15.448 12.348  114.798 1.00 27.13 ? 446  PHE B O     1 
ATOM   12142 C  CB    . PHE B 1  448  ? -18.481 13.224  113.552 1.00 30.36 ? 446  PHE B CB    1 
ATOM   12143 C  CG    . PHE B 1  448  ? -19.759 12.832  112.862 1.00 30.51 ? 446  PHE B CG    1 
ATOM   12144 C  CD1   . PHE B 1  448  ? -19.952 13.116  111.521 1.00 29.65 ? 446  PHE B CD1   1 
ATOM   12145 C  CD2   . PHE B 1  448  ? -20.770 12.188  113.560 1.00 34.77 ? 446  PHE B CD2   1 
ATOM   12146 C  CE1   . PHE B 1  448  ? -21.125 12.753  110.875 1.00 32.85 ? 446  PHE B CE1   1 
ATOM   12147 C  CE2   . PHE B 1  448  ? -21.948 11.825  112.923 1.00 34.93 ? 446  PHE B CE2   1 
ATOM   12148 C  CZ    . PHE B 1  448  ? -22.126 12.111  111.579 1.00 32.40 ? 446  PHE B CZ    1 
ATOM   12149 N  N     . GLN B 1  449  ? -15.511 13.911  113.174 1.00 26.14 ? 447  GLN B N     1 
ATOM   12150 C  CA    . GLN B 1  449  ? -14.333 14.621  113.651 1.00 25.21 ? 447  GLN B CA    1 
ATOM   12151 C  C     . GLN B 1  449  ? -14.513 16.111  113.406 1.00 27.44 ? 447  GLN B C     1 
ATOM   12152 O  O     . GLN B 1  449  ? -15.227 16.526  112.490 1.00 26.03 ? 447  GLN B O     1 
ATOM   12153 C  CB    . GLN B 1  449  ? -13.046 14.116  112.965 1.00 24.72 ? 447  GLN B CB    1 
ATOM   12154 C  CG    . GLN B 1  449  ? -12.800 12.618  113.128 1.00 25.78 ? 447  GLN B CG    1 
ATOM   12155 C  CD    . GLN B 1  449  ? -11.335 12.246  112.981 1.00 23.57 ? 447  GLN B CD    1 
ATOM   12156 O  OE1   . GLN B 1  449  ? -10.537 13.050  112.507 1.00 24.20 ? 447  GLN B OE1   1 
ATOM   12157 N  NE2   . GLN B 1  449  ? -10.975 11.029  113.395 1.00 23.15 ? 447  GLN B NE2   1 
ATOM   12158 N  N     . CYS B 1  450  ? -13.841 16.915  114.226 1.00 25.27 ? 448  CYS B N     1 
ATOM   12159 C  CA    . CYS B 1  450  ? -13.891 18.360  114.100 1.00 28.41 ? 448  CYS B CA    1 
ATOM   12160 C  C     . CYS B 1  450  ? -12.568 18.925  114.585 1.00 26.74 ? 448  CYS B C     1 
ATOM   12161 O  O     . CYS B 1  450  ? -11.764 18.226  115.203 1.00 27.11 ? 448  CYS B O     1 
ATOM   12162 C  CB    . CYS B 1  450  ? -15.053 18.958  114.902 1.00 31.32 ? 448  CYS B CB    1 
ATOM   12163 S  SG    . CYS B 1  450  ? -14.787 18.914  116.700 1.00 29.74 ? 448  CYS B SG    1 
ATOM   12164 N  N     . LEU B 1  451  ? -12.352 20.206  114.308 1.00 27.81 ? 449  LEU B N     1 
ATOM   12165 C  CA    . LEU B 1  451  ? -11.204 20.914  114.854 1.00 29.84 ? 449  LEU B CA    1 
ATOM   12166 C  C     . LEU B 1  451  ? -11.525 21.443  116.244 1.00 31.81 ? 449  LEU B C     1 
ATOM   12167 O  O     . LEU B 1  451  ? -12.654 21.858  116.520 1.00 31.71 ? 449  LEU B O     1 
ATOM   12168 C  CB    . LEU B 1  451  ? -10.792 22.074  113.948 1.00 28.61 ? 449  LEU B CB    1 
ATOM   12169 C  CG    . LEU B 1  451  ? -10.440 21.647  112.529 1.00 32.09 ? 449  LEU B CG    1 
ATOM   12170 C  CD1   . LEU B 1  451  ? -10.009 22.847  111.713 1.00 39.44 ? 449  LEU B CD1   1 
ATOM   12171 C  CD2   . LEU B 1  451  ? -9.356  20.580  112.568 1.00 29.83 ? 449  LEU B CD2   1 
ATOM   12172 N  N     . HIS B 1  452  ? -10.524 21.410  117.119 1.00 28.28 ? 450  HIS B N     1 
ATOM   12173 C  CA    . HIS B 1  452  ? -10.624 22.054  118.422 1.00 34.69 ? 450  HIS B CA    1 
ATOM   12174 C  C     . HIS B 1  452  ? -11.073 23.504  118.282 1.00 34.91 ? 450  HIS B C     1 
ATOM   12175 O  O     . HIS B 1  452  ? -10.611 24.235  117.401 1.00 28.94 ? 450  HIS B O     1 
ATOM   12176 C  CB    . HIS B 1  452  ? -9.269  22.000  119.131 1.00 28.97 ? 450  HIS B CB    1 
ATOM   12177 C  CG    . HIS B 1  452  ? -9.211  22.822  120.381 1.00 32.87 ? 450  HIS B CG    1 
ATOM   12178 N  ND1   . HIS B 1  452  ? -9.593  22.333  121.613 1.00 36.31 ? 450  HIS B ND1   1 
ATOM   12179 C  CD2   . HIS B 1  452  ? -8.827  24.104  120.587 1.00 34.49 ? 450  HIS B CD2   1 
ATOM   12180 C  CE1   . HIS B 1  452  ? -9.436  23.276  122.526 1.00 34.64 ? 450  HIS B CE1   1 
ATOM   12181 N  NE2   . HIS B 1  452  ? -8.980  24.362  121.928 1.00 34.50 ? 450  HIS B NE2   1 
ATOM   12182 N  N     . GLY B 1  453  ? -11.983 23.915  119.164 1.00 35.62 ? 451  GLY B N     1 
ATOM   12183 C  CA    . GLY B 1  453  ? -12.471 25.279  119.181 1.00 37.10 ? 451  GLY B CA    1 
ATOM   12184 C  C     . GLY B 1  453  ? -13.585 25.513  118.185 1.00 40.87 ? 451  GLY B C     1 
ATOM   12185 O  O     . GLY B 1  453  ? -14.700 25.883  118.561 1.00 42.03 ? 451  GLY B O     1 
ATOM   12186 N  N     . MET B 1  454  ? -13.292 25.268  116.908 1.00 36.81 ? 452  MET B N     1 
ATOM   12187 C  CA    . MET B 1  454  ? -14.246 25.553  115.843 1.00 39.96 ? 452  MET B CA    1 
ATOM   12188 C  C     . MET B 1  454  ? -15.424 24.584  115.863 1.00 40.69 ? 452  MET B C     1 
ATOM   12189 O  O     . MET B 1  454  ? -16.567 24.986  115.619 1.00 45.35 ? 452  MET B O     1 
ATOM   12190 C  CB    . MET B 1  454  ? -13.525 25.505  114.493 1.00 42.69 ? 452  MET B CB    1 
ATOM   12191 C  CG    . MET B 1  454  ? -14.393 25.798  113.276 1.00 44.22 ? 452  MET B CG    1 
ATOM   12192 S  SD    . MET B 1  454  ? -13.472 25.604  111.728 1.00 60.94 ? 452  MET B SD    1 
ATOM   12193 C  CE    . MET B 1  454  ? -12.165 26.811  111.945 1.00 60.32 ? 452  MET B CE    1 
ATOM   12194 N  N     . GLY B 1  455  ? -15.176 23.310  116.159 1.00 38.53 ? 453  GLY B N     1 
ATOM   12195 C  CA    . GLY B 1  455  ? -16.188 22.288  115.968 1.00 38.03 ? 453  GLY B CA    1 
ATOM   12196 C  C     . GLY B 1  455  ? -17.097 21.992  117.146 1.00 41.15 ? 453  GLY B C     1 
ATOM   12197 O  O     . GLY B 1  455  ? -18.162 21.393  116.965 1.00 41.20 ? 453  GLY B O     1 
ATOM   12198 N  N     . GLU B 1  456  ? -16.694 22.383  118.355 1.00 40.30 ? 454  GLU B N     1 
ATOM   12199 C  CA    . GLU B 1  456  ? -17.480 22.025  119.534 1.00 41.35 ? 454  GLU B CA    1 
ATOM   12200 C  C     . GLU B 1  456  ? -18.913 22.549  119.499 1.00 38.56 ? 454  GLU B C     1 
ATOM   12201 O  O     . GLU B 1  456  ? -19.821 21.778  119.855 1.00 38.21 ? 454  GLU B O     1 
ATOM   12202 C  CB    . GLU B 1  456  ? -16.760 22.492  120.807 1.00 43.79 ? 454  GLU B CB    1 
ATOM   12203 C  CG    . GLU B 1  456  ? -15.527 21.671  121.172 1.00 45.39 ? 454  GLU B CG    1 
ATOM   12204 C  CD    . GLU B 1  456  ? -14.265 22.186  120.514 1.00 41.15 ? 454  GLU B CD    1 
ATOM   12205 O  OE1   . GLU B 1  456  ? -14.346 22.650  119.359 1.00 41.83 ? 454  GLU B OE1   1 
ATOM   12206 O  OE2   . GLU B 1  456  ? -13.190 22.143  121.157 1.00 40.00 ? 454  GLU B OE2   1 
ATOM   12207 N  N     . PRO B 1  457  ? -19.194 23.803  119.104 1.00 40.83 ? 455  PRO B N     1 
ATOM   12208 C  CA    . PRO B 1  457  ? -20.603 24.236  119.019 1.00 39.77 ? 455  PRO B CA    1 
ATOM   12209 C  C     . PRO B 1  457  ? -21.491 23.289  118.229 1.00 41.46 ? 455  PRO B C     1 
ATOM   12210 O  O     . PRO B 1  457  ? -22.611 22.986  118.661 1.00 42.21 ? 455  PRO B O     1 
ATOM   12211 C  CB    . PRO B 1  457  ? -20.498 25.607  118.339 1.00 41.01 ? 455  PRO B CB    1 
ATOM   12212 C  CG    . PRO B 1  457  ? -19.165 26.112  118.732 1.00 45.65 ? 455  PRO B CG    1 
ATOM   12213 C  CD    . PRO B 1  457  ? -18.271 24.908  118.777 1.00 43.71 ? 455  PRO B CD    1 
ATOM   12214 N  N     . LEU B 1  458  ? -21.020 22.805  117.081 1.00 40.42 ? 456  LEU B N     1 
ATOM   12215 C  CA    . LEU B 1  458  ? -21.816 21.863  116.302 1.00 41.22 ? 456  LEU B CA    1 
ATOM   12216 C  C     . LEU B 1  458  ? -21.900 20.512  116.999 1.00 38.76 ? 456  LEU B C     1 
ATOM   12217 O  O     . LEU B 1  458  ? -22.982 19.925  117.118 1.00 35.57 ? 456  LEU B O     1 
ATOM   12218 C  CB    . LEU B 1  458  ? -21.228 21.711  114.895 1.00 39.59 ? 456  LEU B CB    1 
ATOM   12219 C  CG    . LEU B 1  458  ? -21.838 20.614  114.018 1.00 40.19 ? 456  LEU B CG    1 
ATOM   12220 C  CD1   . LEU B 1  458  ? -23.335 20.823  113.821 1.00 39.53 ? 456  LEU B CD1   1 
ATOM   12221 C  CD2   . LEU B 1  458  ? -21.138 20.577  112.668 1.00 33.50 ? 456  LEU B CD2   1 
ATOM   12222 N  N     . TYR B 1  459  ? -20.765 19.999  117.473 1.00 38.52 ? 457  TYR B N     1 
ATOM   12223 C  CA    . TYR B 1  459  ? -20.751 18.633  117.976 1.00 36.24 ? 457  TYR B CA    1 
ATOM   12224 C  C     . TYR B 1  459  ? -21.216 18.523  119.426 1.00 35.67 ? 457  TYR B C     1 
ATOM   12225 O  O     . TYR B 1  459  ? -21.521 17.413  119.874 1.00 34.03 ? 457  TYR B O     1 
ATOM   12226 C  CB    . TYR B 1  459  ? -19.358 18.028  117.765 1.00 36.34 ? 457  TYR B CB    1 
ATOM   12227 C  CG    . TYR B 1  459  ? -19.180 17.637  116.311 1.00 33.79 ? 457  TYR B CG    1 
ATOM   12228 C  CD1   . TYR B 1  459  ? -19.719 16.456  115.833 1.00 33.31 ? 457  TYR B CD1   1 
ATOM   12229 C  CD2   . TYR B 1  459  ? -18.526 18.470  115.408 1.00 35.38 ? 457  TYR B CD2   1 
ATOM   12230 C  CE1   . TYR B 1  459  ? -19.602 16.099  114.509 1.00 32.28 ? 457  TYR B CE1   1 
ATOM   12231 C  CE2   . TYR B 1  459  ? -18.391 18.109  114.062 1.00 33.92 ? 457  TYR B CE2   1 
ATOM   12232 C  CZ    . TYR B 1  459  ? -18.933 16.913  113.626 1.00 31.39 ? 457  TYR B CZ    1 
ATOM   12233 O  OH    . TYR B 1  459  ? -18.835 16.523  112.302 1.00 31.94 ? 457  TYR B OH    1 
ATOM   12234 N  N     . GLU B 1  460  ? -21.323 19.642  120.148 1.00 36.48 ? 458  GLU B N     1 
ATOM   12235 C  CA    . GLU B 1  460  ? -22.064 19.622  121.406 1.00 38.66 ? 458  GLU B CA    1 
ATOM   12236 C  C     . GLU B 1  460  ? -23.530 19.290  121.170 1.00 44.56 ? 458  GLU B C     1 
ATOM   12237 O  O     . GLU B 1  460  ? -24.224 18.875  122.106 1.00 43.38 ? 458  GLU B O     1 
ATOM   12238 C  CB    . GLU B 1  460  ? -21.934 20.965  122.129 1.00 41.26 ? 458  GLU B CB    1 
ATOM   12239 N  N     . GLU B 1  461  ? -24.006 19.455  119.936 1.00 40.96 ? 459  GLU B N     1 
ATOM   12240 C  CA    . GLU B 1  461  ? -25.345 19.051  119.528 1.00 43.03 ? 459  GLU B CA    1 
ATOM   12241 C  C     . GLU B 1  461  ? -25.385 17.657  118.918 1.00 43.43 ? 459  GLU B C     1 
ATOM   12242 O  O     . GLU B 1  461  ? -26.415 17.276  118.349 1.00 40.99 ? 459  GLU B O     1 
ATOM   12243 C  CB    . GLU B 1  461  ? -25.916 20.059  118.528 1.00 39.86 ? 459  GLU B CB    1 
ATOM   12244 C  CG    . GLU B 1  461  ? -25.816 21.501  118.980 1.00 39.89 ? 459  GLU B CG    1 
ATOM   12245 C  CD    . GLU B 1  461  ? -26.506 21.735  120.313 1.00 47.79 ? 459  GLU B CD    1 
ATOM   12246 O  OE1   . GLU B 1  461  ? -27.436 20.971  120.646 1.00 46.92 ? 459  GLU B OE1   1 
ATOM   12247 O  OE2   . GLU B 1  461  ? -26.113 22.681  121.025 1.00 51.39 ? 459  GLU B OE2   1 
ATOM   12248 N  N     . VAL B 1  462  ? -24.299 16.887  119.031 1.00 41.44 ? 460  VAL B N     1 
ATOM   12249 C  CA    . VAL B 1  462  ? -24.188 15.606  118.340 1.00 39.85 ? 460  VAL B CA    1 
ATOM   12250 C  C     . VAL B 1  462  ? -23.859 14.483  119.314 1.00 39.45 ? 460  VAL B C     1 
ATOM   12251 O  O     . VAL B 1  462  ? -24.567 13.473  119.366 1.00 40.21 ? 460  VAL B O     1 
ATOM   12252 C  CB    . VAL B 1  462  ? -23.137 15.678  117.211 1.00 38.24 ? 460  VAL B CB    1 
ATOM   12253 C  CG1   . VAL B 1  462  ? -22.998 14.322  116.532 1.00 33.72 ? 460  VAL B CG1   1 
ATOM   12254 C  CG2   . VAL B 1  462  ? -23.515 16.752  116.198 1.00 39.47 ? 460  VAL B CG2   1 
ATOM   12255 N  N     . VAL B 1  463  ? -22.766 14.619  120.073 1.00 37.54 ? 461  VAL B N     1 
ATOM   12256 C  CA    . VAL B 1  463  ? -22.382 13.549  120.989 1.00 38.55 ? 461  VAL B CA    1 
ATOM   12257 C  C     . VAL B 1  463  ? -23.295 13.580  122.209 1.00 39.20 ? 461  VAL B C     1 
ATOM   12258 O  O     . VAL B 1  463  ? -23.793 14.637  122.621 1.00 42.20 ? 461  VAL B O     1 
ATOM   12259 C  CB    . VAL B 1  463  ? -20.893 13.643  121.389 1.00 39.34 ? 461  VAL B CB    1 
ATOM   12260 C  CG1   . VAL B 1  463  ? -20.024 14.107  120.207 1.00 31.71 ? 461  VAL B CG1   1 
ATOM   12261 C  CG2   . VAL B 1  463  ? -20.705 14.548  122.572 1.00 38.29 ? 461  VAL B CG2   1 
ATOM   12262 N  N     . GLY B 1  464  ? -23.528 12.413  122.781 1.00 40.15 ? 462  GLY B N     1 
ATOM   12263 C  CA    . GLY B 1  464  ? -24.322 12.306  123.992 1.00 42.23 ? 462  GLY B CA    1 
ATOM   12264 C  C     . GLY B 1  464  ? -25.751 11.867  123.721 1.00 46.47 ? 462  GLY B C     1 
ATOM   12265 O  O     . GLY B 1  464  ? -26.322 12.124  122.655 1.00 47.24 ? 462  GLY B O     1 
ATOM   12266 N  N     . ARG B 1  465  ? -26.350 11.208  124.720 1.00 53.25 ? 463  ARG B N     1 
ATOM   12267 C  CA    . ARG B 1  465  ? -27.707 10.682  124.570 1.00 49.01 ? 463  ARG B CA    1 
ATOM   12268 C  C     . ARG B 1  465  ? -28.719 11.796  124.324 1.00 50.34 ? 463  ARG B C     1 
ATOM   12269 O  O     . ARG B 1  465  ? -29.652 11.632  123.527 1.00 52.83 ? 463  ARG B O     1 
ATOM   12270 C  CB    . ARG B 1  465  ? -28.094 9.873   125.807 1.00 51.40 ? 463  ARG B CB    1 
ATOM   12271 N  N     . GLY B 1  466  ? -28.548 12.938  124.990 1.00 50.94 ? 464  GLY B N     1 
ATOM   12272 C  CA    . GLY B 1  466  ? -29.458 14.059  124.824 1.00 49.78 ? 464  GLY B CA    1 
ATOM   12273 C  C     . GLY B 1  466  ? -29.436 14.696  123.451 1.00 49.90 ? 464  GLY B C     1 
ATOM   12274 O  O     . GLY B 1  466  ? -30.312 15.517  123.157 1.00 48.00 ? 464  GLY B O     1 
ATOM   12275 N  N     . LYS B 1  467  ? -28.456 14.346  122.613 1.00 49.18 ? 465  LYS B N     1 
ATOM   12276 C  CA    . LYS B 1  467  ? -28.339 14.894  121.268 1.00 45.34 ? 465  LYS B CA    1 
ATOM   12277 C  C     . LYS B 1  467  ? -28.455 13.782  120.227 1.00 46.83 ? 465  LYS B C     1 
ATOM   12278 O  O     . LYS B 1  467  ? -29.402 12.990  120.270 1.00 44.91 ? 465  LYS B O     1 
ATOM   12279 C  CB    . LYS B 1  467  ? -27.022 15.657  121.125 1.00 43.66 ? 465  LYS B CB    1 
ATOM   12280 C  CG    . LYS B 1  467  ? -26.851 16.775  122.150 1.00 43.86 ? 465  LYS B CG    1 
ATOM   12281 C  CD    . LYS B 1  467  ? -28.090 17.668  122.191 1.00 50.25 ? 465  LYS B CD    1 
ATOM   12282 C  CE    . LYS B 1  467  ? -28.019 18.702  123.307 1.00 50.19 ? 465  LYS B CE    1 
ATOM   12283 N  NZ    . LYS B 1  467  ? -28.082 20.098  122.776 1.00 46.57 ? 465  LYS B NZ    1 
ATOM   12284 N  N     . LEU B 1  468  ? -27.514 13.709  119.281 1.00 43.93 ? 466  LEU B N     1 
ATOM   12285 C  CA    . LEU B 1  468  ? -27.582 12.675  118.251 1.00 41.58 ? 466  LEU B CA    1 
ATOM   12286 C  C     . LEU B 1  468  ? -26.928 11.368  118.676 1.00 37.15 ? 466  LEU B C     1 
ATOM   12287 O  O     . LEU B 1  468  ? -27.084 10.356  117.982 1.00 35.72 ? 466  LEU B O     1 
ATOM   12288 C  CB    . LEU B 1  468  ? -26.938 13.170  116.949 1.00 40.75 ? 466  LEU B CB    1 
ATOM   12289 C  CG    . LEU B 1  468  ? -27.469 14.496  116.396 1.00 43.61 ? 466  LEU B CG    1 
ATOM   12290 C  CD1   . LEU B 1  468  ? -26.932 14.770  114.990 1.00 42.81 ? 466  LEU B CD1   1 
ATOM   12291 C  CD2   . LEU B 1  468  ? -28.993 14.524  116.416 1.00 46.73 ? 466  LEU B CD2   1 
ATOM   12292 N  N     . ASP B 1  469  ? -26.199 11.375  119.789 1.00 40.37 ? 467  ASP B N     1 
ATOM   12293 C  CA    . ASP B 1  469  ? -25.518 10.193  120.322 1.00 43.03 ? 467  ASP B CA    1 
ATOM   12294 C  C     . ASP B 1  469  ? -24.505 9.620   119.333 1.00 37.99 ? 467  ASP B C     1 
ATOM   12295 O  O     . ASP B 1  469  ? -24.395 8.404   119.164 1.00 37.73 ? 467  ASP B O     1 
ATOM   12296 C  CB    . ASP B 1  469  ? -26.509 9.113   120.753 1.00 45.02 ? 467  ASP B CB    1 
ATOM   12297 C  CG    . ASP B 1  469  ? -25.916 8.179   121.772 1.00 44.38 ? 467  ASP B CG    1 
ATOM   12298 O  OD1   . ASP B 1  469  ? -25.028 8.638   122.521 1.00 44.07 ? 467  ASP B OD1   1 
ATOM   12299 O  OD2   . ASP B 1  469  ? -26.311 6.997   121.817 1.00 50.84 ? 467  ASP B OD2   1 
ATOM   12300 N  N     . ARG B 1  470  ? -23.753 10.503  118.681 1.00 37.80 ? 468  ARG B N     1 
ATOM   12301 C  CA    . ARG B 1  470  ? -22.676 10.054  117.817 1.00 36.62 ? 468  ARG B CA    1 
ATOM   12302 C  C     . ARG B 1  470  ? -21.351 10.613  118.317 1.00 36.04 ? 468  ARG B C     1 
ATOM   12303 O  O     . ARG B 1  470  ? -21.293 11.775  118.724 1.00 35.11 ? 468  ARG B O     1 
ATOM   12304 C  CB    . ARG B 1  470  ? -22.891 10.497  116.362 1.00 35.01 ? 468  ARG B CB    1 
ATOM   12305 C  CG    . ARG B 1  470  ? -24.077 9.828   115.681 1.00 36.81 ? 468  ARG B CG    1 
ATOM   12306 C  CD    . ARG B 1  470  ? -23.990 8.311   115.752 1.00 34.90 ? 468  ARG B CD    1 
ATOM   12307 N  NE    . ARG B 1  470  ? -25.190 7.689   115.202 1.00 42.77 ? 468  ARG B NE    1 
ATOM   12308 C  CZ    . ARG B 1  470  ? -26.278 7.405   115.908 1.00 41.13 ? 468  ARG B CZ    1 
ATOM   12309 N  NH1   . ARG B 1  470  ? -26.336 7.630   117.215 1.00 37.82 ? 468  ARG B NH1   1 
ATOM   12310 N  NH2   . ARG B 1  470  ? -27.333 6.883   115.289 1.00 43.17 ? 468  ARG B NH2   1 
ATOM   12311 N  N     . PRO B 1  471  ? -20.278 9.833   118.280 1.00 34.27 ? 469  PRO B N     1 
ATOM   12312 C  CA    . PRO B 1  471  ? -18.991 10.324  118.775 1.00 32.38 ? 469  PRO B CA    1 
ATOM   12313 C  C     . PRO B 1  471  ? -18.337 11.296  117.804 1.00 31.92 ? 469  PRO B C     1 
ATOM   12314 O  O     . PRO B 1  471  ? -18.604 11.312  116.601 1.00 27.85 ? 469  PRO B O     1 
ATOM   12315 C  CB    . PRO B 1  471  ? -18.159 9.045   118.922 1.00 32.51 ? 469  PRO B CB    1 
ATOM   12316 C  CG    . PRO B 1  471  ? -18.715 8.133   117.916 1.00 31.55 ? 469  PRO B CG    1 
ATOM   12317 C  CD    . PRO B 1  471  ? -20.194 8.435   117.843 1.00 30.62 ? 469  PRO B CD    1 
ATOM   12318 N  N     . CYS B 1  472  ? -17.471 12.132  118.372 1.00 28.89 ? 470  CYS B N     1 
ATOM   12319 C  CA    . CYS B 1  472  ? -16.687 13.092  117.620 1.00 29.59 ? 470  CYS B CA    1 
ATOM   12320 C  C     . CYS B 1  472  ? -15.278 13.088  118.190 1.00 30.38 ? 470  CYS B C     1 
ATOM   12321 O  O     . CYS B 1  472  ? -15.100 13.170  119.412 1.00 28.25 ? 470  CYS B O     1 
ATOM   12322 C  CB    . CYS B 1  472  ? -17.296 14.495  117.691 1.00 30.61 ? 470  CYS B CB    1 
ATOM   12323 S  SG    . CYS B 1  472  ? -16.398 15.746  116.749 1.00 32.04 ? 470  CYS B SG    1 
ATOM   12324 N  N     . ARG B 1  473  ? -14.290 12.950  117.307 1.00 28.36 ? 471  ARG B N     1 
ATOM   12325 C  CA    . ARG B 1  473  ? -12.883 13.035  117.683 1.00 27.67 ? 471  ARG B CA    1 
ATOM   12326 C  C     . ARG B 1  473  ? -12.387 14.439  117.374 1.00 26.68 ? 471  ARG B C     1 
ATOM   12327 O  O     . ARG B 1  473  ? -12.424 14.883  116.220 1.00 25.73 ? 471  ARG B O     1 
ATOM   12328 C  CB    . ARG B 1  473  ? -12.038 11.995  116.953 1.00 24.74 ? 471  ARG B CB    1 
ATOM   12329 C  CG    . ARG B 1  473  ? -10.562 12.009  117.392 1.00 24.50 ? 471  ARG B CG    1 
ATOM   12330 C  CD    . ARG B 1  473  ? -9.793  10.853  116.768 1.00 22.80 ? 471  ARG B CD    1 
ATOM   12331 N  NE    . ARG B 1  473  ? -10.499 9.587   116.915 1.00 26.71 ? 471  ARG B NE    1 
ATOM   12332 C  CZ    . ARG B 1  473  ? -10.417 8.792   117.973 1.00 26.69 ? 471  ARG B CZ    1 
ATOM   12333 N  NH1   . ARG B 1  473  ? -9.623  9.075   118.997 1.00 25.64 ? 471  ARG B NH1   1 
ATOM   12334 N  NH2   . ARG B 1  473  ? -11.146 7.682   118.004 1.00 26.39 ? 471  ARG B NH2   1 
ATOM   12335 N  N     . ILE B 1  474  ? -11.942 15.135  118.412 1.00 27.38 ? 472  ILE B N     1 
ATOM   12336 C  CA    . ILE B 1  474  ? -11.462 16.503  118.288 1.00 25.85 ? 472  ILE B CA    1 
ATOM   12337 C  C     . ILE B 1  474  ? -10.006 16.476  117.848 1.00 24.86 ? 472  ILE B C     1 
ATOM   12338 O  O     . ILE B 1  474  ? -9.151  15.899  118.528 1.00 25.81 ? 472  ILE B O     1 
ATOM   12339 C  CB    . ILE B 1  474  ? -11.618 17.252  119.618 1.00 26.82 ? 472  ILE B CB    1 
ATOM   12340 C  CG1   . ILE B 1  474  ? -13.095 17.334  119.994 1.00 28.22 ? 472  ILE B CG1   1 
ATOM   12341 C  CG2   . ILE B 1  474  ? -10.994 18.638  119.522 1.00 27.79 ? 472  ILE B CG2   1 
ATOM   12342 C  CD1   . ILE B 1  474  ? -13.315 17.808  121.397 1.00 30.74 ? 472  ILE B CD1   1 
ATOM   12343 N  N     . TYR B 1  475  ? -9.728  17.099  116.713 1.00 24.14 ? 473  TYR B N     1 
ATOM   12344 C  CA    . TYR B 1  475  ? -8.362  17.308  116.248 1.00 23.47 ? 473  TYR B CA    1 
ATOM   12345 C  C     . TYR B 1  475  ? -7.762  18.455  117.051 1.00 27.58 ? 473  TYR B C     1 
ATOM   12346 O  O     . TYR B 1  475  ? -8.199  19.604  116.930 1.00 24.95 ? 473  TYR B O     1 
ATOM   12347 C  CB    . TYR B 1  475  ? -8.372  17.610  114.754 1.00 25.14 ? 473  TYR B CB    1 
ATOM   12348 C  CG    . TYR B 1  475  ? -7.019  17.634  114.091 1.00 23.38 ? 473  TYR B CG    1 
ATOM   12349 C  CD1   . TYR B 1  475  ? -6.437  16.460  113.641 1.00 22.86 ? 473  TYR B CD1   1 
ATOM   12350 C  CD2   . TYR B 1  475  ? -6.340  18.829  113.897 1.00 22.51 ? 473  TYR B CD2   1 
ATOM   12351 C  CE1   . TYR B 1  475  ? -5.194  16.470  113.016 1.00 24.27 ? 473  TYR B CE1   1 
ATOM   12352 C  CE2   . TYR B 1  475  ? -5.094  18.851  113.271 1.00 23.66 ? 473  TYR B CE2   1 
ATOM   12353 C  CZ    . TYR B 1  475  ? -4.534  17.664  112.842 1.00 23.28 ? 473  TYR B CZ    1 
ATOM   12354 O  OH    . TYR B 1  475  ? -3.301  17.671  112.234 1.00 25.39 ? 473  TYR B OH    1 
ATOM   12355 N  N     . ALA B 1  476  ? -6.761  18.145  117.871 1.00 22.50 ? 474  ALA B N     1 
ATOM   12356 C  CA    . ALA B 1  476  ? -6.298  19.068  118.901 1.00 25.91 ? 474  ALA B CA    1 
ATOM   12357 C  C     . ALA B 1  476  ? -4.897  19.559  118.585 1.00 25.43 ? 474  ALA B C     1 
ATOM   12358 O  O     . ALA B 1  476  ? -3.926  18.803  118.746 1.00 24.57 ? 474  ALA B O     1 
ATOM   12359 C  CB    . ALA B 1  476  ? -6.331  18.381  120.266 1.00 25.47 ? 474  ALA B CB    1 
ATOM   12360 N  N     . PRO B 1  477  ? -4.735  20.797  118.122 1.00 22.92 ? 475  PRO B N     1 
ATOM   12361 C  CA    . PRO B 1  477  ? -3.386  21.343  117.954 1.00 25.34 ? 475  PRO B CA    1 
ATOM   12362 C  C     . PRO B 1  477  ? -2.718  21.522  119.304 1.00 25.16 ? 475  PRO B C     1 
ATOM   12363 O  O     . PRO B 1  477  ? -3.357  21.872  120.300 1.00 26.61 ? 475  PRO B O     1 
ATOM   12364 C  CB    . PRO B 1  477  ? -3.627  22.692  117.271 1.00 25.91 ? 475  PRO B CB    1 
ATOM   12365 C  CG    . PRO B 1  477  ? -4.976  22.562  116.637 1.00 24.50 ? 475  PRO B CG    1 
ATOM   12366 C  CD    . PRO B 1  477  ? -5.766  21.694  117.574 1.00 26.01 ? 475  PRO B CD    1 
ATOM   12367 N  N     . VAL B 1  478  ? -1.420  21.264  119.327 1.00 22.64 ? 476  VAL B N     1 
ATOM   12368 C  CA    . VAL B 1  478  ? -0.613  21.382  120.528 1.00 24.89 ? 476  VAL B CA    1 
ATOM   12369 C  C     . VAL B 1  478  ? 0.647   22.136  120.145 1.00 27.32 ? 476  VAL B C     1 
ATOM   12370 O  O     . VAL B 1  478  ? 1.400   21.688  119.279 1.00 25.69 ? 476  VAL B O     1 
ATOM   12371 C  CB    . VAL B 1  478  ? -0.265  20.012  121.131 1.00 24.20 ? 476  VAL B CB    1 
ATOM   12372 C  CG1   . VAL B 1  478  ? 0.535   20.208  122.409 1.00 26.61 ? 476  VAL B CG1   1 
ATOM   12373 C  CG2   . VAL B 1  478  ? -1.526  19.211  121.407 1.00 25.45 ? 476  VAL B CG2   1 
ATOM   12374 N  N     . GLY B 1  479  ? 0.866   23.280  120.768 1.00 28.84 ? 477  GLY B N     1 
ATOM   12375 C  CA    . GLY B 1  479  ? 2.060   24.045  120.487 1.00 32.38 ? 477  GLY B CA    1 
ATOM   12376 C  C     . GLY B 1  479  ? 2.022   25.355  121.239 1.00 33.18 ? 477  GLY B C     1 
ATOM   12377 O  O     . GLY B 1  479  ? 0.970   25.795  121.716 1.00 30.95 ? 477  GLY B O     1 
ATOM   12378 N  N     . THR B 1  480  ? 3.194   25.970  121.335 1.00 38.18 ? 478  THR B N     1 
ATOM   12379 C  CA    . THR B 1  480  ? 3.292   27.266  121.985 1.00 39.93 ? 478  THR B CA    1 
ATOM   12380 C  C     . THR B 1  480  ? 2.571   28.313  121.145 1.00 42.16 ? 478  THR B C     1 
ATOM   12381 O  O     . THR B 1  480  ? 2.471   28.195  119.919 1.00 41.93 ? 478  THR B O     1 
ATOM   12382 C  CB    . THR B 1  480  ? 4.756   27.660  122.183 1.00 40.95 ? 478  THR B CB    1 
ATOM   12383 O  OG1   . THR B 1  480  ? 5.374   27.850  120.908 1.00 40.59 ? 478  THR B OG1   1 
ATOM   12384 C  CG2   . THR B 1  480  ? 5.502   26.566  122.923 1.00 41.65 ? 478  THR B CG2   1 
ATOM   12385 N  N     . HIS B 1  481  ? 2.041   29.334  121.828 1.00 44.47 ? 479  HIS B N     1 
ATOM   12386 C  CA    . HIS B 1  481  ? 1.336   30.414  121.142 1.00 48.05 ? 479  HIS B CA    1 
ATOM   12387 C  C     . HIS B 1  481  ? 2.180   30.997  120.014 1.00 43.91 ? 479  HIS B C     1 
ATOM   12388 O  O     . HIS B 1  481  ? 1.680   31.226  118.907 1.00 47.94 ? 479  HIS B O     1 
ATOM   12389 C  CB    . HIS B 1  481  ? 0.944   31.499  122.150 1.00 45.55 ? 479  HIS B CB    1 
ATOM   12390 N  N     . GLU B 1  482  ? 3.474   31.212  120.269 1.00 46.46 ? 480  GLU B N     1 
ATOM   12391 C  CA    . GLU B 1  482  ? 4.379   31.674  119.220 1.00 46.52 ? 480  GLU B CA    1 
ATOM   12392 C  C     . GLU B 1  482  ? 4.391   30.708  118.040 1.00 46.84 ? 480  GLU B C     1 
ATOM   12393 O  O     . GLU B 1  482  ? 4.199   31.113  116.888 1.00 51.56 ? 480  GLU B O     1 
ATOM   12394 C  CB    . GLU B 1  482  ? 5.787   31.849  119.791 1.00 49.06 ? 480  GLU B CB    1 
ATOM   12395 N  N     . THR B 1  483  ? 4.613   29.419  118.311 1.00 48.47 ? 481  THR B N     1 
ATOM   12396 C  CA    . THR B 1  483  ? 4.573   28.411  117.253 1.00 49.77 ? 481  THR B CA    1 
ATOM   12397 C  C     . THR B 1  483  ? 3.214   28.388  116.562 1.00 46.63 ? 481  THR B C     1 
ATOM   12398 O  O     . THR B 1  483  ? 3.132   28.303  115.332 1.00 49.95 ? 481  THR B O     1 
ATOM   12399 C  CB    . THR B 1  483  ? 4.895   27.030  117.836 1.00 46.25 ? 481  THR B CB    1 
ATOM   12400 O  OG1   . THR B 1  483  ? 6.205   27.044  118.418 1.00 48.37 ? 481  THR B OG1   1 
ATOM   12401 C  CG2   . THR B 1  483  ? 4.818   25.946  116.764 1.00 43.50 ? 481  THR B CG2   1 
ATOM   12402 N  N     . LEU B 1  484  ? 2.137   28.481  117.345 1.00 48.09 ? 482  LEU B N     1 
ATOM   12403 C  CA    . LEU B 1  484  ? 0.791   28.324  116.807 1.00 51.02 ? 482  LEU B CA    1 
ATOM   12404 C  C     . LEU B 1  484  ? 0.455   29.380  115.761 1.00 54.56 ? 482  LEU B C     1 
ATOM   12405 O  O     . LEU B 1  484  ? -0.248  29.084  114.786 1.00 58.33 ? 482  LEU B O     1 
ATOM   12406 C  CB    . LEU B 1  484  ? -0.217  28.377  117.952 1.00 48.25 ? 482  LEU B CB    1 
ATOM   12407 C  CG    . LEU B 1  484  ? -1.544  29.066  117.657 1.00 46.84 ? 482  LEU B CG    1 
ATOM   12408 C  CD1   . LEU B 1  484  ? -2.476  28.116  116.911 1.00 44.29 ? 482  LEU B CD1   1 
ATOM   12409 C  CD2   . LEU B 1  484  ? -2.154  29.560  118.953 1.00 47.91 ? 482  LEU B CD2   1 
ATOM   12410 N  N     . LEU B 1  485  ? 0.952   30.605  115.930 1.00 61.80 ? 483  LEU B N     1 
ATOM   12411 C  CA    . LEU B 1  485  ? 0.586   31.714  115.053 1.00 63.88 ? 483  LEU B CA    1 
ATOM   12412 C  C     . LEU B 1  485  ? 1.018   31.480  113.606 1.00 67.55 ? 483  LEU B C     1 
ATOM   12413 O  O     . LEU B 1  485  ? 0.839   32.355  112.753 1.00 67.96 ? 483  LEU B O     1 
ATOM   12414 C  CB    . LEU B 1  485  ? 1.184   33.021  115.583 1.00 57.87 ? 483  LEU B CB    1 
ATOM   12415 N  N     . ALA B 1  486  ? 1.580   30.303  113.320 1.00 68.17 ? 484  ALA B N     1 
ATOM   12416 C  CA    . ALA B 1  486  ? 1.969   29.927  111.967 1.00 70.71 ? 484  ALA B CA    1 
ATOM   12417 C  C     . ALA B 1  486  ? 0.747   29.704  111.086 1.00 73.15 ? 484  ALA B C     1 
ATOM   12418 O  O     . ALA B 1  486  ? -0.036  30.632  110.849 1.00 73.94 ? 484  ALA B O     1 
ATOM   12419 C  CB    . ALA B 1  486  ? 2.840   28.672  111.994 1.00 66.87 ? 484  ALA B CB    1 
ATOM   12420 N  N     . TYR B 1  487  ? 0.559   28.471  110.613 1.00 73.00 ? 485  TYR B N     1 
ATOM   12421 C  CA    . TYR B 1  487  ? -0.491  28.172  109.642 1.00 78.73 ? 485  TYR B CA    1 
ATOM   12422 C  C     . TYR B 1  487  ? -1.889  28.244  110.246 1.00 80.63 ? 485  TYR B C     1 
ATOM   12423 O  O     . TYR B 1  487  ? -2.751  27.419  109.921 1.00 84.05 ? 485  TYR B O     1 
ATOM   12424 C  CB    . TYR B 1  487  ? -0.264  26.789  109.023 1.00 83.07 ? 485  TYR B CB    1 
ATOM   12425 N  N     . LEU B 1  488  ? -2.129  29.225  111.123 1.00 78.26 ? 486  LEU B N     1 
ATOM   12426 C  CA    . LEU B 1  488  ? -3.485  29.492  111.586 1.00 73.50 ? 486  LEU B CA    1 
ATOM   12427 C  C     . LEU B 1  488  ? -4.359  30.069  110.481 1.00 74.39 ? 486  LEU B C     1 
ATOM   12428 O  O     . LEU B 1  488  ? -5.586  29.937  110.546 1.00 75.08 ? 486  LEU B O     1 
ATOM   12429 C  CB    . LEU B 1  488  ? -3.452  30.447  112.780 1.00 64.13 ? 486  LEU B CB    1 
ATOM   12430 N  N     . VAL B 1  489  ? -3.751  30.683  109.462 1.00 74.88 ? 487  VAL B N     1 
ATOM   12431 C  CA    . VAL B 1  489  ? -4.525  31.284  108.379 1.00 72.94 ? 487  VAL B CA    1 
ATOM   12432 C  C     . VAL B 1  489  ? -5.106  30.209  107.468 1.00 75.64 ? 487  VAL B C     1 
ATOM   12433 O  O     . VAL B 1  489  ? -6.229  30.348  106.968 1.00 76.36 ? 487  VAL B O     1 
ATOM   12434 C  CB    . VAL B 1  489  ? -3.659  32.288  107.597 1.00 67.76 ? 487  VAL B CB    1 
ATOM   12435 C  CG1   . VAL B 1  489  ? -3.341  33.488  108.467 1.00 58.36 ? 487  VAL B CG1   1 
ATOM   12436 C  CG2   . VAL B 1  489  ? -2.377  31.627  107.109 1.00 72.93 ? 487  VAL B CG2   1 
ATOM   12437 N  N     . ARG B 1  490  ? -4.357  29.127  107.230 1.00 77.28 ? 488  ARG B N     1 
ATOM   12438 C  CA    . ARG B 1  490  ? -4.903  28.009  106.465 1.00 77.23 ? 488  ARG B CA    1 
ATOM   12439 C  C     . ARG B 1  490  ? -6.064  27.351  107.200 1.00 77.34 ? 488  ARG B C     1 
ATOM   12440 O  O     . ARG B 1  490  ? -7.018  26.882  106.567 1.00 76.56 ? 488  ARG B O     1 
ATOM   12441 C  CB    . ARG B 1  490  ? -3.805  26.985  106.170 1.00 76.88 ? 488  ARG B CB    1 
ATOM   12442 N  N     . ARG B 1  491  ? -6.008  27.321  108.533 1.00 76.96 ? 489  ARG B N     1 
ATOM   12443 C  CA    . ARG B 1  491  ? -7.099  26.780  109.333 1.00 76.98 ? 489  ARG B CA    1 
ATOM   12444 C  C     . ARG B 1  491  ? -8.280  27.735  109.445 1.00 78.07 ? 489  ARG B C     1 
ATOM   12445 O  O     . ARG B 1  491  ? -9.397  27.285  109.729 1.00 77.27 ? 489  ARG B O     1 
ATOM   12446 C  CB    . ARG B 1  491  ? -6.594  26.425  110.734 1.00 75.02 ? 489  ARG B CB    1 
ATOM   12447 N  N     . LEU B 1  492  ? -8.063  29.034  109.228 1.00 78.96 ? 490  LEU B N     1 
ATOM   12448 C  CA    . LEU B 1  492  ? -9.107  30.042  109.380 1.00 77.77 ? 490  LEU B CA    1 
ATOM   12449 C  C     . LEU B 1  492  ? -9.669  30.540  108.055 1.00 77.57 ? 490  LEU B C     1 
ATOM   12450 O  O     . LEU B 1  492  ? -10.843 30.925  108.004 1.00 77.90 ? 490  LEU B O     1 
ATOM   12451 C  CB    . LEU B 1  492  ? -8.578  31.240  110.179 1.00 73.57 ? 490  LEU B CB    1 
ATOM   12452 N  N     . LEU B 1  493  ? -8.865  30.559  106.987 1.00 74.11 ? 491  LEU B N     1 
ATOM   12453 C  CA    . LEU B 1  493  ? -9.398  30.927  105.680 1.00 69.93 ? 491  LEU B CA    1 
ATOM   12454 C  C     . LEU B 1  493  ? -10.473 29.945  105.239 1.00 72.91 ? 491  LEU B C     1 
ATOM   12455 O  O     . LEU B 1  493  ? -11.487 30.343  104.652 1.00 75.46 ? 491  LEU B O     1 
ATOM   12456 C  CB    . LEU B 1  493  ? -8.273  30.993  104.645 1.00 61.99 ? 491  LEU B CB    1 
ATOM   12457 N  N     . GLU B 1  494  ? -10.275 28.657  105.531 1.00 72.71 ? 492  GLU B N     1 
ATOM   12458 C  CA    . GLU B 1  494  ? -11.235 27.604  105.198 1.00 69.88 ? 492  GLU B CA    1 
ATOM   12459 C  C     . GLU B 1  494  ? -12.396 27.535  106.182 1.00 72.33 ? 492  GLU B C     1 
ATOM   12460 O  O     . GLU B 1  494  ? -12.857 26.447  106.536 1.00 65.34 ? 492  GLU B O     1 
ATOM   12461 C  CB    . GLU B 1  494  ? -10.507 26.264  105.122 1.00 63.81 ? 492  GLU B CB    1 
ATOM   12462 N  N     . ASN B 1  495  ? -12.876 28.693  106.636 1.00 75.33 ? 493  ASN B N     1 
ATOM   12463 C  CA    . ASN B 1  495  ? -13.937 28.782  107.630 1.00 75.95 ? 493  ASN B CA    1 
ATOM   12464 C  C     . ASN B 1  495  ? -14.706 30.085  107.450 1.00 78.91 ? 493  ASN B C     1 
ATOM   12465 O  O     . ASN B 1  495  ? -15.937 30.112  107.559 1.00 77.47 ? 493  ASN B O     1 
ATOM   12466 C  CB    . ASN B 1  495  ? -13.356 28.686  109.042 1.00 74.60 ? 493  ASN B CB    1 
ATOM   12467 N  N     . GLY B 1  496  ? -13.984 31.168  107.172 1.00 80.85 ? 494  GLY B N     1 
ATOM   12468 C  CA    . GLY B 1  496  ? -14.555 32.466  106.885 1.00 80.26 ? 494  GLY B CA    1 
ATOM   12469 C  C     . GLY B 1  496  ? -14.839 32.732  105.423 1.00 84.17 ? 494  GLY B C     1 
ATOM   12470 O  O     . GLY B 1  496  ? -15.164 33.871  105.068 1.00 87.75 ? 494  GLY B O     1 
ATOM   12471 N  N     . ALA B 1  497  ? -14.726 31.723  104.560 1.00 78.02 ? 495  ALA B N     1 
ATOM   12472 C  CA    . ALA B 1  497  ? -15.020 31.894  103.145 1.00 75.70 ? 495  ALA B CA    1 
ATOM   12473 C  C     . ALA B 1  497  ? -16.526 31.898  102.905 1.00 73.83 ? 495  ALA B C     1 
ATOM   12474 O  O     . ALA B 1  497  ? -17.299 31.291  103.654 1.00 72.72 ? 495  ALA B O     1 
ATOM   12475 C  CB    . ALA B 1  497  ? -14.361 30.789  102.320 1.00 70.64 ? 495  ALA B CB    1 
ATOM   12476 N  N     . ASN B 1  498  ? -16.937 32.595  101.842 1.00 72.78 ? 496  ASN B N     1 
ATOM   12477 C  CA    . ASN B 1  498  ? -18.361 32.739  101.548 1.00 73.37 ? 496  ASN B CA    1 
ATOM   12478 C  C     . ASN B 1  498  ? -19.030 31.379  101.384 1.00 68.34 ? 496  ASN B C     1 
ATOM   12479 O  O     . ASN B 1  498  ? -20.089 31.121  101.967 1.00 67.22 ? 496  ASN B O     1 
ATOM   12480 C  CB    . ASN B 1  498  ? -18.556 33.594  100.295 1.00 71.56 ? 496  ASN B CB    1 
ATOM   12481 N  N     . SER B 1  499  ? -18.417 30.491  100.598 1.00 65.64 ? 497  SER B N     1 
ATOM   12482 C  CA    . SER B 1  499  ? -18.947 29.146  100.406 1.00 59.93 ? 497  SER B CA    1 
ATOM   12483 C  C     . SER B 1  499  ? -18.826 28.274  101.651 1.00 55.63 ? 497  SER B C     1 
ATOM   12484 O  O     . SER B 1  499  ? -19.479 27.226  101.710 1.00 57.13 ? 497  SER B O     1 
ATOM   12485 C  CB    . SER B 1  499  ? -18.233 28.474  99.234  1.00 50.64 ? 497  SER B CB    1 
ATOM   12486 O  OG    . SER B 1  499  ? -16.826 28.507  99.418  1.00 52.84 ? 497  SER B OG    1 
ATOM   12487 N  N     . SER B 1  500  ? -18.027 28.681  102.638 1.00 57.53 ? 498  SER B N     1 
ATOM   12488 C  CA    . SER B 1  500  ? -17.798 27.853  103.816 1.00 59.37 ? 498  SER B CA    1 
ATOM   12489 C  C     . SER B 1  500  ? -19.009 27.879  104.740 1.00 58.69 ? 498  SER B C     1 
ATOM   12490 O  O     . SER B 1  500  ? -19.570 28.943  105.019 1.00 60.87 ? 498  SER B O     1 
ATOM   12491 C  CB    . SER B 1  500  ? -16.555 28.325  104.570 1.00 61.55 ? 498  SER B CB    1 
ATOM   12492 O  OG    . SER B 1  500  ? -15.380 28.081  103.820 1.00 66.26 ? 498  SER B OG    1 
ATOM   12493 N  N     . PHE B 1  501  ? -19.398 26.698  105.224 1.00 52.72 ? 499  PHE B N     1 
ATOM   12494 C  CA    . PHE B 1  501  ? -20.561 26.590  106.099 1.00 53.27 ? 499  PHE B CA    1 
ATOM   12495 C  C     . PHE B 1  501  ? -20.365 27.378  107.390 1.00 58.62 ? 499  PHE B C     1 
ATOM   12496 O  O     . PHE B 1  501  ? -21.322 27.953  107.923 1.00 59.66 ? 499  PHE B O     1 
ATOM   12497 C  CB    . PHE B 1  501  ? -20.842 25.119  106.405 1.00 47.35 ? 499  PHE B CB    1 
ATOM   12498 C  CG    . PHE B 1  501  ? -21.938 24.899  107.414 1.00 44.78 ? 499  PHE B CG    1 
ATOM   12499 C  CD1   . PHE B 1  501  ? -21.666 24.919  108.774 1.00 45.61 ? 499  PHE B CD1   1 
ATOM   12500 C  CD2   . PHE B 1  501  ? -23.234 24.647  106.999 1.00 45.82 ? 499  PHE B CD2   1 
ATOM   12501 C  CE1   . PHE B 1  501  ? -22.671 24.716  109.701 1.00 46.87 ? 499  PHE B CE1   1 
ATOM   12502 C  CE2   . PHE B 1  501  ? -24.237 24.435  107.915 1.00 46.49 ? 499  PHE B CE2   1 
ATOM   12503 C  CZ    . PHE B 1  501  ? -23.956 24.474  109.270 1.00 46.84 ? 499  PHE B CZ    1 
ATOM   12504 N  N     . VAL B 1  502  ? -19.138 27.400  107.917 1.00 58.46 ? 500  VAL B N     1 
ATOM   12505 C  CA    . VAL B 1  502  ? -18.881 28.072  109.190 1.00 64.58 ? 500  VAL B CA    1 
ATOM   12506 C  C     . VAL B 1  502  ? -19.242 29.550  109.096 1.00 68.40 ? 500  VAL B C     1 
ATOM   12507 O  O     . VAL B 1  502  ? -19.999 30.078  109.920 1.00 69.28 ? 500  VAL B O     1 
ATOM   12508 C  CB    . VAL B 1  502  ? -17.415 27.873  109.615 1.00 66.05 ? 500  VAL B CB    1 
ATOM   12509 N  N     . HIS B 1  503  ? -18.712 30.240  108.082 1.00 68.54 ? 501  HIS B N     1 
ATOM   12510 C  CA    . HIS B 1  503  ? -19.058 31.643  107.879 1.00 70.92 ? 501  HIS B CA    1 
ATOM   12511 C  C     . HIS B 1  503  ? -20.508 31.811  107.440 1.00 70.22 ? 501  HIS B C     1 
ATOM   12512 O  O     . HIS B 1  503  ? -21.145 32.815  107.779 1.00 69.64 ? 501  HIS B O     1 
ATOM   12513 C  CB    . HIS B 1  503  ? -18.117 32.271  106.852 1.00 75.89 ? 501  HIS B CB    1 
ATOM   12514 C  CG    . HIS B 1  503  ? -18.707 33.436  106.119 1.00 78.05 ? 501  HIS B CG    1 
ATOM   12515 N  ND1   . HIS B 1  503  ? -19.433 33.291  104.955 1.00 77.14 ? 501  HIS B ND1   1 
ATOM   12516 C  CD2   . HIS B 1  503  ? -18.675 34.765  106.379 1.00 78.14 ? 501  HIS B CD2   1 
ATOM   12517 C  CE1   . HIS B 1  503  ? -19.827 34.480  104.533 1.00 75.27 ? 501  HIS B CE1   1 
ATOM   12518 N  NE2   . HIS B 1  503  ? -19.379 35.391  105.378 1.00 77.09 ? 501  HIS B NE2   1 
ATOM   12519 N  N     . ARG B 1  504  ? -21.041 30.851  106.681 1.00 66.56 ? 502  ARG B N     1 
ATOM   12520 C  CA    . ARG B 1  504  ? -22.424 30.953  106.229 1.00 63.92 ? 502  ARG B CA    1 
ATOM   12521 C  C     . ARG B 1  504  ? -23.397 30.861  107.399 1.00 64.92 ? 502  ARG B C     1 
ATOM   12522 O  O     . ARG B 1  504  ? -24.443 31.521  107.396 1.00 65.14 ? 502  ARG B O     1 
ATOM   12523 C  CB    . ARG B 1  504  ? -22.716 29.870  105.191 1.00 61.42 ? 502  ARG B CB    1 
ATOM   12524 C  CG    . ARG B 1  504  ? -22.527 30.322  103.747 1.00 63.60 ? 502  ARG B CG    1 
ATOM   12525 C  CD    . ARG B 1  504  ? -22.429 29.146  102.776 1.00 56.80 ? 502  ARG B CD    1 
ATOM   12526 N  NE    . ARG B 1  504  ? -23.662 28.376  102.671 1.00 56.90 ? 502  ARG B NE    1 
ATOM   12527 C  CZ    . ARG B 1  504  ? -24.689 28.703  101.897 1.00 60.30 ? 502  ARG B CZ    1 
ATOM   12528 N  NH1   . ARG B 1  504  ? -24.683 29.809  101.170 1.00 64.64 ? 502  ARG B NH1   1 
ATOM   12529 N  NH2   . ARG B 1  504  ? -25.750 27.902  101.853 1.00 57.51 ? 502  ARG B NH2   1 
ATOM   12530 N  N     . ILE B 1  505  ? -23.065 30.059  108.414 1.00 61.96 ? 503  ILE B N     1 
ATOM   12531 C  CA    . ILE B 1  505  ? -23.944 29.915  109.569 1.00 63.87 ? 503  ILE B CA    1 
ATOM   12532 C  C     . ILE B 1  505  ? -24.005 31.192  110.395 1.00 63.37 ? 503  ILE B C     1 
ATOM   12533 O  O     . ILE B 1  505  ? -24.919 31.354  111.211 1.00 60.66 ? 503  ILE B O     1 
ATOM   12534 C  CB    . ILE B 1  505  ? -23.495 28.728  110.441 1.00 58.72 ? 503  ILE B CB    1 
ATOM   12535 N  N     . ASN B 1  506  ? -23.059 32.111  110.202 1.00 62.39 ? 504  ASN B N     1 
ATOM   12536 C  CA    . ASN B 1  506  ? -22.988 33.340  110.980 1.00 65.64 ? 504  ASN B CA    1 
ATOM   12537 C  C     . ASN B 1  506  ? -23.261 34.584  110.146 1.00 66.56 ? 504  ASN B C     1 
ATOM   12538 O  O     . ASN B 1  506  ? -23.039 35.699  110.628 1.00 67.33 ? 504  ASN B O     1 
ATOM   12539 C  CB    . ASN B 1  506  ? -21.624 33.458  111.661 1.00 69.55 ? 504  ASN B CB    1 
ATOM   12540 C  CG    . ASN B 1  506  ? -21.335 32.293  112.584 1.00 70.51 ? 504  ASN B CG    1 
ATOM   12541 O  OD1   . ASN B 1  506  ? -20.348 31.578  112.409 1.00 71.74 ? 504  ASN B OD1   1 
ATOM   12542 N  ND2   . ASN B 1  506  ? -22.200 32.092  113.573 1.00 65.88 ? 504  ASN B ND2   1 
ATOM   12543 N  N     . ASP B 1  507  ? -23.725 34.424  108.909 1.00 64.26 ? 505  ASP B N     1 
ATOM   12544 C  CA    . ASP B 1  507  ? -24.141 35.559  108.104 1.00 66.89 ? 505  ASP B CA    1 
ATOM   12545 C  C     . ASP B 1  507  ? -25.657 35.634  108.107 1.00 68.46 ? 505  ASP B C     1 
ATOM   12546 O  O     . ASP B 1  507  ? -26.314 34.694  107.631 1.00 67.24 ? 505  ASP B O     1 
ATOM   12547 C  CB    . ASP B 1  507  ? -23.619 35.435  106.679 1.00 67.31 ? 505  ASP B CB    1 
ATOM   12548 C  CG    . ASP B 1  507  ? -24.152 36.521  105.773 1.00 71.26 ? 505  ASP B CG    1 
ATOM   12549 O  OD1   . ASP B 1  507  ? -23.596 37.640  105.791 1.00 69.48 ? 505  ASP B OD1   1 
ATOM   12550 O  OD2   . ASP B 1  507  ? -25.137 36.256  105.051 1.00 72.36 ? 505  ASP B OD2   1 
ATOM   12551 N  N     . PRO B 1  508  ? -26.257 36.710  108.624 1.00 70.21 ? 506  PRO B N     1 
ATOM   12552 C  CA    . PRO B 1  508  ? -27.718 36.743  108.790 1.00 68.86 ? 506  PRO B CA    1 
ATOM   12553 C  C     . PRO B 1  508  ? -28.497 36.850  107.489 1.00 70.74 ? 506  PRO B C     1 
ATOM   12554 O  O     . PRO B 1  508  ? -29.731 36.921  107.536 1.00 70.56 ? 506  PRO B O     1 
ATOM   12555 C  CB    . PRO B 1  508  ? -27.943 37.987  109.667 1.00 73.84 ? 506  PRO B CB    1 
ATOM   12556 C  CG    . PRO B 1  508  ? -26.590 38.335  110.227 1.00 72.67 ? 506  PRO B CG    1 
ATOM   12557 C  CD    . PRO B 1  508  ? -25.610 37.903  109.191 1.00 68.86 ? 506  PRO B CD    1 
ATOM   12558 N  N     . LYS B 1  509  ? -27.833 36.870  106.335 1.00 70.33 ? 507  LYS B N     1 
ATOM   12559 C  CA    . LYS B 1  509  ? -28.527 36.886  105.056 1.00 69.71 ? 507  LYS B CA    1 
ATOM   12560 C  C     . LYS B 1  509  ? -28.750 35.491  104.487 1.00 71.46 ? 507  LYS B C     1 
ATOM   12561 O  O     . LYS B 1  509  ? -29.425 35.359  103.459 1.00 72.73 ? 507  LYS B O     1 
ATOM   12562 C  CB    . LYS B 1  509  ? -27.756 37.737  104.042 1.00 67.90 ? 507  LYS B CB    1 
ATOM   12563 N  N     . VAL B 1  510  ? -28.206 34.456  105.124 1.00 68.88 ? 508  VAL B N     1 
ATOM   12564 C  CA    . VAL B 1  510  ? -28.393 33.072  104.702 1.00 68.93 ? 508  VAL B CA    1 
ATOM   12565 C  C     . VAL B 1  510  ? -29.405 32.420  105.630 1.00 66.52 ? 508  VAL B C     1 
ATOM   12566 O  O     . VAL B 1  510  ? -29.324 32.570  106.855 1.00 68.33 ? 508  VAL B O     1 
ATOM   12567 C  CB    . VAL B 1  510  ? -27.059 32.300  104.707 1.00 67.60 ? 508  VAL B CB    1 
ATOM   12568 C  CG1   . VAL B 1  510  ? -27.220 30.959  104.007 1.00 64.29 ? 508  VAL B CG1   1 
ATOM   12569 C  CG2   . VAL B 1  510  ? -25.960 33.128  104.057 1.00 65.12 ? 508  VAL B CG2   1 
ATOM   12570 N  N     . SER B 1  511  ? -30.359 31.700  105.054 1.00 64.94 ? 509  SER B N     1 
ATOM   12571 C  CA    . SER B 1  511  ? -31.420 31.068  105.823 1.00 65.74 ? 509  SER B CA    1 
ATOM   12572 C  C     . SER B 1  511  ? -31.063 29.623  106.141 1.00 64.90 ? 509  SER B C     1 
ATOM   12573 O  O     . SER B 1  511  ? -30.182 29.023  105.519 1.00 64.89 ? 509  SER B O     1 
ATOM   12574 C  CB    . SER B 1  511  ? -32.747 31.112  105.063 1.00 67.08 ? 509  SER B CB    1 
ATOM   12575 O  OG    . SER B 1  511  ? -32.800 30.089  104.083 1.00 66.84 ? 509  SER B OG    1 
ATOM   12576 N  N     . ILE B 1  512  ? -31.769 29.067  107.128 1.00 63.02 ? 510  ILE B N     1 
ATOM   12577 C  CA    . ILE B 1  512  ? -31.634 27.643  107.419 1.00 62.78 ? 510  ILE B CA    1 
ATOM   12578 C  C     . ILE B 1  512  ? -31.949 26.823  106.174 1.00 62.99 ? 510  ILE B C     1 
ATOM   12579 O  O     . ILE B 1  512  ? -31.286 25.817  105.892 1.00 62.30 ? 510  ILE B O     1 
ATOM   12580 C  CB    . ILE B 1  512  ? -32.527 27.251  108.614 1.00 64.49 ? 510  ILE B CB    1 
ATOM   12581 C  CG1   . ILE B 1  512  ? -31.781 27.444  109.939 1.00 64.04 ? 510  ILE B CG1   1 
ATOM   12582 C  CG2   . ILE B 1  512  ? -33.019 25.812  108.494 1.00 62.66 ? 510  ILE B CG2   1 
ATOM   12583 C  CD1   . ILE B 1  512  ? -31.565 28.892  110.338 1.00 64.37 ? 510  ILE B CD1   1 
ATOM   12584 N  N     . ASP B 1  513  ? -32.934 27.266  105.385 1.00 63.49 ? 511  ASP B N     1 
ATOM   12585 C  CA    . ASP B 1  513  ? -33.297 26.554  104.162 1.00 61.18 ? 511  ASP B CA    1 
ATOM   12586 C  C     . ASP B 1  513  ? -32.126 26.488  103.187 1.00 59.59 ? 511  ASP B C     1 
ATOM   12587 O  O     . ASP B 1  513  ? -31.854 25.435  102.598 1.00 57.22 ? 511  ASP B O     1 
ATOM   12588 C  CB    . ASP B 1  513  ? -34.506 27.222  103.502 1.00 62.67 ? 511  ASP B CB    1 
ATOM   12589 C  CG    . ASP B 1  513  ? -35.819 26.856  104.172 1.00 63.81 ? 511  ASP B CG    1 
ATOM   12590 O  OD1   . ASP B 1  513  ? -35.903 25.774  104.793 1.00 62.25 ? 511  ASP B OD1   1 
ATOM   12591 O  OD2   . ASP B 1  513  ? -36.772 27.655  104.070 1.00 68.08 ? 511  ASP B OD2   1 
ATOM   12592 N  N     . GLU B 1  514  ? -31.429 27.612  102.991 1.00 57.62 ? 512  GLU B N     1 
ATOM   12593 C  CA    . GLU B 1  514  ? -30.268 27.618  102.105 1.00 59.96 ? 512  GLU B CA    1 
ATOM   12594 C  C     . GLU B 1  514  ? -29.190 26.667  102.610 1.00 59.38 ? 512  GLU B C     1 
ATOM   12595 O  O     . GLU B 1  514  ? -28.650 25.856  101.849 1.00 55.51 ? 512  GLU B O     1 
ATOM   12596 C  CB    . GLU B 1  514  ? -29.707 29.035  101.975 1.00 60.94 ? 512  GLU B CB    1 
ATOM   12597 C  CG    . GLU B 1  514  ? -30.720 30.090  101.567 1.00 67.86 ? 512  GLU B CG    1 
ATOM   12598 C  CD    . GLU B 1  514  ? -30.069 31.429  101.274 1.00 68.58 ? 512  GLU B CD    1 
ATOM   12599 O  OE1   . GLU B 1  514  ? -28.859 31.442  100.965 1.00 70.92 ? 512  GLU B OE1   1 
ATOM   12600 O  OE2   . GLU B 1  514  ? -30.761 32.467  101.357 1.00 69.12 ? 512  GLU B OE2   1 
ATOM   12601 N  N     . LEU B 1  515  ? -28.872 26.747  103.903 1.00 58.36 ? 513  LEU B N     1 
ATOM   12602 C  CA    . LEU B 1  515  ? -27.796 25.934  104.456 1.00 53.97 ? 513  LEU B CA    1 
ATOM   12603 C  C     . LEU B 1  515  ? -28.120 24.448  104.403 1.00 51.29 ? 513  LEU B C     1 
ATOM   12604 O  O     . LEU B 1  515  ? -27.205 23.619  104.367 1.00 49.74 ? 513  LEU B O     1 
ATOM   12605 C  CB    . LEU B 1  515  ? -27.511 26.366  105.893 1.00 54.75 ? 513  LEU B CB    1 
ATOM   12606 C  CG    . LEU B 1  515  ? -26.915 27.763  106.072 1.00 55.03 ? 513  LEU B CG    1 
ATOM   12607 C  CD1   . LEU B 1  515  ? -27.229 28.323  107.449 1.00 57.87 ? 513  LEU B CD1   1 
ATOM   12608 C  CD2   . LEU B 1  515  ? -25.417 27.724  105.857 1.00 55.15 ? 513  LEU B CD2   1 
ATOM   12609 N  N     . ILE B 1  516  ? -29.402 24.085  104.387 1.00 50.43 ? 514  ILE B N     1 
ATOM   12610 C  CA    . ILE B 1  516  ? -29.780 22.675  104.419 1.00 49.84 ? 514  ILE B CA    1 
ATOM   12611 C  C     . ILE B 1  516  ? -30.066 22.165  103.011 1.00 46.97 ? 514  ILE B C     1 
ATOM   12612 O  O     . ILE B 1  516  ? -30.492 21.017  102.831 1.00 46.83 ? 514  ILE B O     1 
ATOM   12613 C  CB    . ILE B 1  516  ? -30.992 22.429  105.339 1.00 52.15 ? 514  ILE B CB    1 
ATOM   12614 C  CG1   . ILE B 1  516  ? -32.255 23.065  104.749 1.00 52.98 ? 514  ILE B CG1   1 
ATOM   12615 C  CG2   . ILE B 1  516  ? -30.713 22.923  106.743 1.00 50.03 ? 514  ILE B CG2   1 
ATOM   12616 C  CD1   . ILE B 1  516  ? -33.508 22.809  105.562 1.00 54.76 ? 514  ILE B CD1   1 
ATOM   12617 N  N     . ALA B 1  517  ? -29.839 23.009  102.007 1.00 47.94 ? 515  ALA B N     1 
ATOM   12618 C  CA    . ALA B 1  517  ? -30.022 22.585  100.624 1.00 46.89 ? 515  ALA B CA    1 
ATOM   12619 C  C     . ALA B 1  517  ? -29.176 21.351  100.336 1.00 45.76 ? 515  ALA B C     1 
ATOM   12620 O  O     . ALA B 1  517  ? -28.020 21.260  100.755 1.00 43.68 ? 515  ALA B O     1 
ATOM   12621 C  CB    . ALA B 1  517  ? -29.654 23.716  99.665  1.00 45.02 ? 515  ALA B CB    1 
ATOM   12622 N  N     . ASP B 1  518  ? -29.776 20.376  99.656  1.00 42.98 ? 516  ASP B N     1 
ATOM   12623 C  CA    . ASP B 1  518  ? -29.062 19.151  99.335  1.00 39.88 ? 516  ASP B CA    1 
ATOM   12624 C  C     . ASP B 1  518  ? -28.111 19.441  98.182  1.00 38.62 ? 516  ASP B C     1 
ATOM   12625 O  O     . ASP B 1  518  ? -28.560 19.739  97.067  1.00 39.22 ? 516  ASP B O     1 
ATOM   12626 C  CB    . ASP B 1  518  ? -30.039 18.027  98.983  1.00 38.00 ? 516  ASP B CB    1 
ATOM   12627 C  CG    . ASP B 1  518  ? -29.361 16.670  98.860  1.00 42.60 ? 516  ASP B CG    1 
ATOM   12628 O  OD1   . ASP B 1  518  ? -28.114 16.613  98.813  1.00 39.82 ? 516  ASP B OD1   1 
ATOM   12629 O  OD2   . ASP B 1  518  ? -30.078 15.649  98.810  1.00 41.81 ? 516  ASP B OD2   1 
ATOM   12630 N  N     . PRO B 1  519  ? -26.797 19.378  98.409  1.00 38.27 ? 517  PRO B N     1 
ATOM   12631 C  CA    . PRO B 1  519  ? -25.864 19.617  97.300  1.00 35.63 ? 517  PRO B CA    1 
ATOM   12632 C  C     . PRO B 1  519  ? -26.066 18.645  96.163  1.00 36.34 ? 517  PRO B C     1 
ATOM   12633 O  O     . PRO B 1  519  ? -25.893 19.017  94.995  1.00 35.19 ? 517  PRO B O     1 
ATOM   12634 C  CB    . PRO B 1  519  ? -24.487 19.439  97.957  1.00 33.81 ? 517  PRO B CB    1 
ATOM   12635 C  CG    . PRO B 1  519  ? -24.737 18.546  99.118  1.00 36.53 ? 517  PRO B CG    1 
ATOM   12636 C  CD    . PRO B 1  519  ? -26.102 18.934  99.632  1.00 39.63 ? 517  PRO B CD    1 
ATOM   12637 N  N     . VAL B 1  520  ? -26.439 17.405  96.483  1.00 33.60 ? 518  VAL B N     1 
ATOM   12638 C  CA    . VAL B 1  520  ? -26.610 16.379  95.463  1.00 37.26 ? 518  VAL B CA    1 
ATOM   12639 C  C     . VAL B 1  520  ? -27.715 16.776  94.496  1.00 36.80 ? 518  VAL B C     1 
ATOM   12640 O  O     . VAL B 1  520  ? -27.549 16.711  93.273  1.00 33.79 ? 518  VAL B O     1 
ATOM   12641 C  CB    . VAL B 1  520  ? -26.898 15.020  96.122  1.00 36.73 ? 518  VAL B CB    1 
ATOM   12642 C  CG1   . VAL B 1  520  ? -26.918 13.909  95.076  1.00 39.13 ? 518  VAL B CG1   1 
ATOM   12643 C  CG2   . VAL B 1  520  ? -25.874 14.739  97.218  1.00 35.66 ? 518  VAL B CG2   1 
ATOM   12644 N  N     . GLU B 1  521  ? -28.859 17.206  95.029  1.00 36.89 ? 519  GLU B N     1 
ATOM   12645 C  CA    . GLU B 1  521  ? -29.976 17.545  94.154  1.00 36.04 ? 519  GLU B CA    1 
ATOM   12646 C  C     . GLU B 1  521  ? -29.739 18.848  93.404  1.00 36.09 ? 519  GLU B C     1 
ATOM   12647 O  O     . GLU B 1  521  ? -30.237 19.010  92.285  1.00 37.46 ? 519  GLU B O     1 
ATOM   12648 C  CB    . GLU B 1  521  ? -31.276 17.613  94.957  1.00 38.30 ? 519  GLU B CB    1 
ATOM   12649 C  CG    . GLU B 1  521  ? -31.648 16.297  95.615  1.00 38.53 ? 519  GLU B CG    1 
ATOM   12650 C  CD    . GLU B 1  521  ? -31.742 15.163  94.615  1.00 44.60 ? 519  GLU B CD    1 
ATOM   12651 O  OE1   . GLU B 1  521  ? -32.166 15.421  93.470  1.00 46.32 ? 519  GLU B OE1   1 
ATOM   12652 O  OE2   . GLU B 1  521  ? -31.391 14.015  94.968  1.00 47.94 ? 519  GLU B OE2   1 
ATOM   12653 N  N     . VAL B 1  522  ? -28.995 19.789  93.989  1.00 37.07 ? 520  VAL B N     1 
ATOM   12654 C  CA    . VAL B 1  522  ? -28.641 20.997  93.249  1.00 34.37 ? 520  VAL B CA    1 
ATOM   12655 C  C     . VAL B 1  522  ? -27.758 20.641  92.060  1.00 38.20 ? 520  VAL B C     1 
ATOM   12656 O  O     . VAL B 1  522  ? -27.983 21.106  90.937  1.00 38.20 ? 520  VAL B O     1 
ATOM   12657 C  CB    . VAL B 1  522  ? -27.961 22.026  94.168  1.00 36.63 ? 520  VAL B CB    1 
ATOM   12658 C  CG1   . VAL B 1  522  ? -27.508 23.242  93.365  1.00 37.54 ? 520  VAL B CG1   1 
ATOM   12659 C  CG2   . VAL B 1  522  ? -28.894 22.439  95.299  1.00 41.10 ? 520  VAL B CG2   1 
ATOM   12660 N  N     . VAL B 1  523  ? -26.748 19.796  92.287  1.00 34.09 ? 521  VAL B N     1 
ATOM   12661 C  CA    . VAL B 1  523  ? -25.878 19.368  91.192  1.00 33.80 ? 521  VAL B CA    1 
ATOM   12662 C  C     . VAL B 1  523  ? -26.677 18.607  90.142  1.00 34.85 ? 521  VAL B C     1 
ATOM   12663 O  O     . VAL B 1  523  ? -26.537 18.850  88.938  1.00 35.26 ? 521  VAL B O     1 
ATOM   12664 C  CB    . VAL B 1  523  ? -24.710 18.520  91.724  1.00 38.11 ? 521  VAL B CB    1 
ATOM   12665 C  CG1   . VAL B 1  523  ? -23.936 17.900  90.568  1.00 33.83 ? 521  VAL B CG1   1 
ATOM   12666 C  CG2   . VAL B 1  523  ? -23.788 19.378  92.567  1.00 34.04 ? 521  VAL B CG2   1 
ATOM   12667 N  N     . ARG B 1  524  ? -27.516 17.665  90.580  1.00 37.65 ? 522  ARG B N     1 
ATOM   12668 C  CA    . ARG B 1  524  ? -28.255 16.842  89.626  1.00 40.15 ? 522  ARG B CA    1 
ATOM   12669 C  C     . ARG B 1  524  ? -29.116 17.690  88.698  1.00 38.71 ? 522  ARG B C     1 
ATOM   12670 O  O     . ARG B 1  524  ? -29.416 17.269  87.576  1.00 42.41 ? 522  ARG B O     1 
ATOM   12671 C  CB    . ARG B 1  524  ? -29.126 15.826  90.366  1.00 39.76 ? 522  ARG B CB    1 
ATOM   12672 C  CG    . ARG B 1  524  ? -29.832 14.838  89.449  1.00 41.56 ? 522  ARG B CG    1 
ATOM   12673 C  CD    . ARG B 1  524  ? -31.078 14.276  90.101  1.00 45.17 ? 522  ARG B CD    1 
ATOM   12674 N  NE    . ARG B 1  524  ? -30.826 13.897  91.484  1.00 41.05 ? 522  ARG B NE    1 
ATOM   12675 C  CZ    . ARG B 1  524  ? -30.197 12.790  91.854  1.00 44.05 ? 522  ARG B CZ    1 
ATOM   12676 N  NH1   . ARG B 1  524  ? -29.734 11.925  90.964  1.00 41.51 ? 522  ARG B NH1   1 
ATOM   12677 N  NH2   . ARG B 1  524  ? -30.026 12.547  93.152  1.00 43.89 ? 522  ARG B NH2   1 
ATOM   12678 N  N     . ALA B 1  525  ? -29.497 18.888  89.131  1.00 39.04 ? 523  ALA B N     1 
ATOM   12679 C  CA    . ALA B 1  525  ? -30.435 19.716  88.385  1.00 42.60 ? 523  ALA B CA    1 
ATOM   12680 C  C     . ALA B 1  525  ? -29.750 20.718  87.470  1.00 45.02 ? 523  ALA B C     1 
ATOM   12681 O  O     . ALA B 1  525  ? -30.438 21.431  86.732  1.00 47.64 ? 523  ALA B O     1 
ATOM   12682 C  CB    . ALA B 1  525  ? -31.369 20.456  89.348  1.00 41.69 ? 523  ALA B CB    1 
ATOM   12683 N  N     . MET B 1  526  ? -28.424 20.796  87.503  1.00 43.60 ? 524  MET B N     1 
ATOM   12684 C  CA    . MET B 1  526  ? -27.716 21.737  86.656  1.00 44.75 ? 524  MET B CA    1 
ATOM   12685 C  C     . MET B 1  526  ? -27.897 21.364  85.186  1.00 41.06 ? 524  MET B C     1 
ATOM   12686 O  O     . MET B 1  526  ? -28.100 20.193  84.856  1.00 41.48 ? 524  MET B O     1 
ATOM   12687 C  CB    . MET B 1  526  ? -26.235 21.758  87.013  1.00 42.08 ? 524  MET B CB    1 
ATOM   12688 C  CG    . MET B 1  526  ? -25.978 22.229  88.425  1.00 46.70 ? 524  MET B CG    1 
ATOM   12689 S  SD    . MET B 1  526  ? -26.667 23.873  88.675  1.00 57.67 ? 524  MET B SD    1 
ATOM   12690 C  CE    . MET B 1  526  ? -25.489 24.876  87.770  1.00 46.73 ? 524  MET B CE    1 
ATOM   12691 N  N     . PRO B 1  527  ? -27.845 22.350  84.285  1.00 46.49 ? 525  PRO B N     1 
ATOM   12692 C  CA    . PRO B 1  527  ? -27.977 22.025  82.853  1.00 48.48 ? 525  PRO B CA    1 
ATOM   12693 C  C     . PRO B 1  527  ? -26.871 21.114  82.357  1.00 41.83 ? 525  PRO B C     1 
ATOM   12694 O  O     . PRO B 1  527  ? -27.125 20.226  81.536  1.00 39.22 ? 525  PRO B O     1 
ATOM   12695 C  CB    . PRO B 1  527  ? -27.938 23.404  82.178  1.00 47.18 ? 525  PRO B CB    1 
ATOM   12696 C  CG    . PRO B 1  527  ? -27.209 24.276  83.146  1.00 48.52 ? 525  PRO B CG    1 
ATOM   12697 C  CD    . PRO B 1  527  ? -27.611 23.788  84.507  1.00 47.96 ? 525  PRO B CD    1 
ATOM   12698 N  N     . VAL B 1  528  ? -25.647 21.300  82.844  1.00 39.98 ? 526  VAL B N     1 
ATOM   12699 C  CA    . VAL B 1  528  ? -24.546 20.389  82.566  1.00 36.61 ? 526  VAL B CA    1 
ATOM   12700 C  C     . VAL B 1  528  ? -23.995 19.935  83.910  1.00 33.06 ? 526  VAL B C     1 
ATOM   12701 O  O     . VAL B 1  528  ? -23.435 20.740  84.665  1.00 37.37 ? 526  VAL B O     1 
ATOM   12702 C  CB    . VAL B 1  528  ? -23.456 21.035  81.703  1.00 36.76 ? 526  VAL B CB    1 
ATOM   12703 C  CG1   . VAL B 1  528  ? -23.220 22.474  82.129  1.00 40.46 ? 526  VAL B CG1   1 
ATOM   12704 C  CG2   . VAL B 1  528  ? -22.164 20.224  81.780  1.00 35.55 ? 526  VAL B CG2   1 
ATOM   12705 N  N     . VAL B 1  529  ? -24.153 18.649  84.209  1.00 28.76 ? 527  VAL B N     1 
ATOM   12706 C  CA    . VAL B 1  529  ? -23.729 18.117  85.499  1.00 28.80 ? 527  VAL B CA    1 
ATOM   12707 C  C     . VAL B 1  529  ? -22.212 18.216  85.607  1.00 31.77 ? 527  VAL B C     1 
ATOM   12708 O  O     . VAL B 1  529  ? -21.477 17.685  84.764  1.00 30.57 ? 527  VAL B O     1 
ATOM   12709 C  CB    . VAL B 1  529  ? -24.205 16.671  85.680  1.00 31.63 ? 527  VAL B CB    1 
ATOM   12710 C  CG1   . VAL B 1  529  ? -23.582 16.069  86.925  1.00 30.07 ? 527  VAL B CG1   1 
ATOM   12711 C  CG2   . VAL B 1  529  ? -25.733 16.613  85.765  1.00 30.04 ? 527  VAL B CG2   1 
ATOM   12712 N  N     . GLY B 1  530  ? -21.740 18.909  86.642  1.00 28.62 ? 528  GLY B N     1 
ATOM   12713 C  CA    . GLY B 1  530  ? -20.320 18.973  86.925  1.00 26.78 ? 528  GLY B CA    1 
ATOM   12714 C  C     . GLY B 1  530  ? -19.531 19.983  86.123  1.00 26.00 ? 528  GLY B C     1 
ATOM   12715 O  O     . GLY B 1  530  ? -18.312 19.828  85.991  1.00 24.25 ? 528  GLY B O     1 
ATOM   12716 N  N     . ALA B 1  531  ? -20.173 21.018  85.582  1.00 23.65 ? 529  ALA B N     1 
ATOM   12717 C  CA    . ALA B 1  531  ? -19.423 22.037  84.855  1.00 24.68 ? 529  ALA B CA    1 
ATOM   12718 C  C     . ALA B 1  531  ? -18.436 22.748  85.768  1.00 24.94 ? 529  ALA B C     1 
ATOM   12719 O  O     . ALA B 1  531  ? -18.722 23.004  86.941  1.00 27.03 ? 529  ALA B O     1 
ATOM   12720 C  CB    . ALA B 1  531  ? -20.360 23.066  84.227  1.00 29.26 ? 529  ALA B CB    1 
ATOM   12721 N  N     . LYS B 1  532  ? -17.267 23.063  85.210  1.00 22.58 ? 530  LYS B N     1 
ATOM   12722 C  CA    . LYS B 1  532  ? -16.274 23.877  85.894  1.00 24.03 ? 530  LYS B CA    1 
ATOM   12723 C  C     . LYS B 1  532  ? -16.886 25.196  86.350  1.00 24.61 ? 530  LYS B C     1 
ATOM   12724 O  O     . LYS B 1  532  ? -17.795 25.738  85.710  1.00 22.29 ? 530  LYS B O     1 
ATOM   12725 C  CB    . LYS B 1  532  ? -15.098 24.144  84.945  1.00 23.15 ? 530  LYS B CB    1 
ATOM   12726 C  CG    . LYS B 1  532  ? -14.034 25.093  85.471  1.00 26.59 ? 530  LYS B CG    1 
ATOM   12727 C  CD    . LYS B 1  532  ? -12.975 25.377  84.402  1.00 22.46 ? 530  LYS B CD    1 
ATOM   12728 C  CE    . LYS B 1  532  ? -13.542 26.170  83.239  1.00 22.60 ? 530  LYS B CE    1 
ATOM   12729 N  NZ    . LYS B 1  532  ? -13.998 27.546  83.612  1.00 24.85 ? 530  LYS B NZ    1 
ATOM   12730 N  N     . HIS B 1  533  ? -16.378 25.717  87.467  1.00 23.26 ? 531  HIS B N     1 
ATOM   12731 C  CA    . HIS B 1  533  ? -16.749 27.052  87.911  1.00 23.19 ? 531  HIS B CA    1 
ATOM   12732 C  C     . HIS B 1  533  ? -16.569 28.057  86.780  1.00 22.67 ? 531  HIS B C     1 
ATOM   12733 O  O     . HIS B 1  533  ? -15.545 28.064  86.096  1.00 22.76 ? 531  HIS B O     1 
ATOM   12734 C  CB    . HIS B 1  533  ? -15.903 27.448  89.119  1.00 24.05 ? 531  HIS B CB    1 
ATOM   12735 C  CG    . HIS B 1  533  ? -16.454 28.606  89.893  1.00 26.02 ? 531  HIS B CG    1 
ATOM   12736 N  ND1   . HIS B 1  533  ? -16.524 29.881  89.377  1.00 26.15 ? 531  HIS B ND1   1 
ATOM   12737 C  CD2   . HIS B 1  533  ? -16.954 28.680  91.149  1.00 31.19 ? 531  HIS B CD2   1 
ATOM   12738 C  CE1   . HIS B 1  533  ? -17.049 30.691  90.280  1.00 30.72 ? 531  HIS B CE1   1 
ATOM   12739 N  NE2   . HIS B 1  533  ? -17.318 29.987  91.364  1.00 32.86 ? 531  HIS B NE2   1 
ATOM   12740 N  N     . ASP B 1  534  ? -17.585 28.899  86.574  1.00 25.66 ? 532  ASP B N     1 
ATOM   12741 C  CA    . ASP B 1  534  ? -17.555 29.831  85.451  1.00 27.30 ? 532  ASP B CA    1 
ATOM   12742 C  C     . ASP B 1  534  ? -16.466 30.884  85.584  1.00 22.53 ? 532  ASP B C     1 
ATOM   12743 O  O     . ASP B 1  534  ? -16.065 31.468  84.574  1.00 29.06 ? 532  ASP B O     1 
ATOM   12744 C  CB    . ASP B 1  534  ? -18.908 30.529  85.303  1.00 30.40 ? 532  ASP B CB    1 
ATOM   12745 C  CG    . ASP B 1  534  ? -19.991 29.597  84.821  1.00 38.63 ? 532  ASP B CG    1 
ATOM   12746 O  OD1   . ASP B 1  534  ? -19.674 28.694  84.013  1.00 40.57 ? 532  ASP B OD1   1 
ATOM   12747 O  OD2   . ASP B 1  534  ? -21.156 29.767  85.249  1.00 45.59 ? 532  ASP B OD2   1 
ATOM   12748 N  N     . ARG B 1  535  ? -15.975 31.136  86.796  1.00 24.37 ? 533  ARG B N     1 
ATOM   12749 C  CA    . ARG B 1  535  ? -15.039 32.224  87.045  1.00 22.01 ? 533  ARG B CA    1 
ATOM   12750 C  C     . ARG B 1  535  ? -13.634 31.723  87.352  1.00 23.35 ? 533  ARG B C     1 
ATOM   12751 O  O     . ARG B 1  535  ? -12.819 32.477  87.887  1.00 26.05 ? 533  ARG B O     1 
ATOM   12752 C  CB    . ARG B 1  535  ? -15.540 33.112  88.185  1.00 26.61 ? 533  ARG B CB    1 
ATOM   12753 C  CG    . ARG B 1  535  ? -16.816 33.898  87.854  1.00 31.73 ? 533  ARG B CG    1 
ATOM   12754 C  CD    . ARG B 1  535  ? -17.271 34.732  89.049  1.00 37.09 ? 533  ARG B CD    1 
ATOM   12755 N  N     . ILE B 1  536  ? -13.341 30.462  87.044  1.00 21.51 ? 534  ILE B N     1 
ATOM   12756 C  CA    . ILE B 1  536  ? -12.020 29.881  87.275  1.00 19.82 ? 534  ILE B CA    1 
ATOM   12757 C  C     . ILE B 1  536  ? -11.547 29.314  85.950  1.00 18.36 ? 534  ILE B C     1 
ATOM   12758 O  O     . ILE B 1  536  ? -12.207 28.439  85.373  1.00 23.27 ? 534  ILE B O     1 
ATOM   12759 C  CB    . ILE B 1  536  ? -12.033 28.784  88.351  1.00 19.63 ? 534  ILE B CB    1 
ATOM   12760 C  CG1   . ILE B 1  536  ? -12.520 29.348  89.685  1.00 22.89 ? 534  ILE B CG1   1 
ATOM   12761 C  CG2   . ILE B 1  536  ? -10.616 28.178  88.497  1.00 21.99 ? 534  ILE B CG2   1 
ATOM   12762 C  CD1   . ILE B 1  536  ? -12.566 28.323  90.791  1.00 27.10 ? 534  ILE B CD1   1 
ATOM   12763 N  N     . ALA B 1  537  ? -10.438 29.837  85.453  1.00 17.99 ? 535  ALA B N     1 
ATOM   12764 C  CA    . ALA B 1  537  ? -9.952  29.468  84.132  1.00 19.59 ? 535  ALA B CA    1 
ATOM   12765 C  C     . ALA B 1  537  ? -9.194  28.154  84.215  1.00 19.09 ? 535  ALA B C     1 
ATOM   12766 O  O     . ALA B 1  537  ? -8.349  27.975  85.096  1.00 18.09 ? 535  ALA B O     1 
ATOM   12767 C  CB    . ALA B 1  537  ? -9.038  30.561  83.576  1.00 19.60 ? 535  ALA B CB    1 
ATOM   12768 N  N     . LEU B 1  538  ? -9.495  27.238  83.305  1.00 18.41 ? 536  LEU B N     1 
ATOM   12769 C  CA    . LEU B 1  538  ? -8.568  26.136  83.105  1.00 19.52 ? 536  LEU B CA    1 
ATOM   12770 C  C     . LEU B 1  538  ? -7.187  26.707  82.816  1.00 19.33 ? 536  LEU B C     1 
ATOM   12771 O  O     . LEU B 1  538  ? -7.077  27.793  82.228  1.00 18.43 ? 536  LEU B O     1 
ATOM   12772 C  CB    . LEU B 1  538  ? -9.007  25.249  81.945  1.00 18.42 ? 536  LEU B CB    1 
ATOM   12773 C  CG    . LEU B 1  538  ? -10.196 24.334  82.187  1.00 22.17 ? 536  LEU B CG    1 
ATOM   12774 C  CD1   . LEU B 1  538  ? -10.543 23.649  80.878  1.00 25.85 ? 536  LEU B CD1   1 
ATOM   12775 C  CD2   . LEU B 1  538  ? -9.855  23.318  83.259  1.00 21.72 ? 536  LEU B CD2   1 
ATOM   12776 N  N     . PRO B 1  539  ? -6.117  26.013  83.199  1.00 16.74 ? 537  PRO B N     1 
ATOM   12777 C  CA    . PRO B 1  539  ? -4.775  26.523  82.876  1.00 17.77 ? 537  PRO B CA    1 
ATOM   12778 C  C     . PRO B 1  539  ? -4.621  26.892  81.409  1.00 16.56 ? 537  PRO B C     1 
ATOM   12779 O  O     . PRO B 1  539  ? -4.053  27.946  81.107  1.00 17.07 ? 537  PRO B O     1 
ATOM   12780 C  CB    . PRO B 1  539  ? -3.858  25.365  83.304  1.00 16.49 ? 537  PRO B CB    1 
ATOM   12781 C  CG    . PRO B 1  539  ? -4.631  24.706  84.454  1.00 15.50 ? 537  PRO B CG    1 
ATOM   12782 C  CD    . PRO B 1  539  ? -6.076  24.775  83.998  1.00 18.07 ? 537  PRO B CD    1 
ATOM   12783 N  N     . ALA B 1  540  ? -5.145  26.082  80.489  1.00 18.30 ? 538  ALA B N     1 
ATOM   12784 C  CA    . ALA B 1  540  ? -4.993  26.407  79.076  1.00 19.08 ? 538  ALA B CA    1 
ATOM   12785 C  C     . ALA B 1  540  ? -5.679  27.716  78.708  1.00 20.25 ? 538  ALA B C     1 
ATOM   12786 O  O     . ALA B 1  540  ? -5.323  28.329  77.696  1.00 18.73 ? 538  ALA B O     1 
ATOM   12787 C  CB    . ALA B 1  540  ? -5.546  25.273  78.210  1.00 20.10 ? 538  ALA B CB    1 
ATOM   12788 N  N     . GLU B 1  541  ? -6.648  28.167  79.509  1.00 19.73 ? 539  GLU B N     1 
ATOM   12789 C  CA    . GLU B 1  541  ? -7.512  29.278  79.122  1.00 18.51 ? 539  GLU B CA    1 
ATOM   12790 C  C     . GLU B 1  541  ? -7.207  30.549  79.918  1.00 19.93 ? 539  GLU B C     1 
ATOM   12791 O  O     . GLU B 1  541  ? -8.021  31.477  79.946  1.00 18.29 ? 539  GLU B O     1 
ATOM   12792 C  CB    . GLU B 1  541  ? -8.979  28.840  79.248  1.00 21.52 ? 539  GLU B CB    1 
ATOM   12793 C  CG    . GLU B 1  541  ? -9.252  27.604  78.335  1.00 25.18 ? 539  GLU B CG    1 
ATOM   12794 C  CD    . GLU B 1  541  ? -10.677 27.029  78.346  1.00 28.78 ? 539  GLU B CD    1 
ATOM   12795 O  OE1   . GLU B 1  541  ? -11.500 27.390  79.201  1.00 30.68 ? 539  GLU B OE1   1 
ATOM   12796 O  OE2   . GLU B 1  541  ? -10.964 26.181  77.476  1.00 32.54 ? 539  GLU B OE2   1 
ATOM   12797 N  N     . LEU B 1  542  ? -6.021  30.628  80.534  1.00 18.13 ? 540  LEU B N     1 
ATOM   12798 C  CA    . LEU B 1  542  ? -5.680  31.797  81.348  1.00 18.29 ? 540  LEU B CA    1 
ATOM   12799 C  C     . LEU B 1  542  ? -5.810  33.109  80.589  1.00 20.07 ? 540  LEU B C     1 
ATOM   12800 O  O     . LEU B 1  542  ? -6.102  34.151  81.190  1.00 20.75 ? 540  LEU B O     1 
ATOM   12801 C  CB    . LEU B 1  542  ? -4.240  31.703  81.859  1.00 19.56 ? 540  LEU B CB    1 
ATOM   12802 C  CG    . LEU B 1  542  ? -3.888  30.816  83.046  1.00 22.64 ? 540  LEU B CG    1 
ATOM   12803 C  CD1   . LEU B 1  542  ? -2.461  31.152  83.546  1.00 18.44 ? 540  LEU B CD1   1 
ATOM   12804 C  CD2   . LEU B 1  542  ? -4.913  30.919  84.178  1.00 21.01 ? 540  LEU B CD2   1 
ATOM   12805 N  N     . PHE B 1  543  ? -5.571  33.089  79.284  1.00 16.51 ? 541  PHE B N     1 
ATOM   12806 C  CA    . PHE B 1  543  ? -5.567  34.306  78.487  1.00 17.95 ? 541  PHE B CA    1 
ATOM   12807 C  C     . PHE B 1  543  ? -6.824  34.433  77.655  1.00 17.43 ? 541  PHE B C     1 
ATOM   12808 O  O     . PHE B 1  543  ? -6.917  35.335  76.821  1.00 19.49 ? 541  PHE B O     1 
ATOM   12809 C  CB    . PHE B 1  543  ? -4.310  34.352  77.618  1.00 16.76 ? 541  PHE B CB    1 
ATOM   12810 C  CG    . PHE B 1  543  ? -3.065  34.108  78.408  1.00 18.99 ? 541  PHE B CG    1 
ATOM   12811 C  CD1   . PHE B 1  543  ? -2.775  34.914  79.503  1.00 19.14 ? 541  PHE B CD1   1 
ATOM   12812 C  CD2   . PHE B 1  543  ? -2.223  33.052  78.109  1.00 18.15 ? 541  PHE B CD2   1 
ATOM   12813 C  CE1   . PHE B 1  543  ? -1.655  34.680  80.275  1.00 19.45 ? 541  PHE B CE1   1 
ATOM   12814 C  CE2   . PHE B 1  543  ? -1.094  32.815  78.882  1.00 19.16 ? 541  PHE B CE2   1 
ATOM   12815 C  CZ    . PHE B 1  543  ? -0.810  33.632  79.964  1.00 20.93 ? 541  PHE B CZ    1 
ATOM   12816 N  N     . GLY B 1  544  ? -7.808  33.572  77.897  1.00 19.42 ? 542  GLY B N     1 
ATOM   12817 C  CA    . GLY B 1  544  ? -9.091  33.716  77.230  1.00 19.92 ? 542  GLY B CA    1 
ATOM   12818 C  C     . GLY B 1  544  ? -8.966  33.608  75.724  1.00 21.23 ? 542  GLY B C     1 
ATOM   12819 O  O     . GLY B 1  544  ? -8.215  32.781  75.191  1.00 22.69 ? 542  GLY B O     1 
ATOM   12820 N  N     . ASP B 1  545  ? -9.703  34.469  75.017  1.00 23.88 ? 543  ASP B N     1 
ATOM   12821 C  CA    . ASP B 1  545  ? -9.732  34.401  73.561  1.00 26.40 ? 543  ASP B CA    1 
ATOM   12822 C  C     . ASP B 1  545  ? -8.436  34.868  72.909  1.00 24.88 ? 543  ASP B C     1 
ATOM   12823 O  O     . ASP B 1  545  ? -8.254  34.636  71.708  1.00 24.98 ? 543  ASP B O     1 
ATOM   12824 C  CB    . ASP B 1  545  ? -10.891 35.236  73.013  1.00 28.18 ? 543  ASP B CB    1 
ATOM   12825 C  CG    . ASP B 1  545  ? -12.246 34.742  73.488  1.00 38.02 ? 543  ASP B CG    1 
ATOM   12826 O  OD1   . ASP B 1  545  ? -12.383 33.526  73.750  1.00 38.54 ? 543  ASP B OD1   1 
ATOM   12827 O  OD2   . ASP B 1  545  ? -13.176 35.573  73.586  1.00 44.43 ? 543  ASP B OD2   1 
ATOM   12828 N  N     . ALA B 1  546  ? -7.540  35.511  73.663  1.00 20.30 ? 544  ALA B N     1 
ATOM   12829 C  CA    . ALA B 1  546  ? -6.336  36.091  73.070  1.00 20.22 ? 544  ALA B CA    1 
ATOM   12830 C  C     . ALA B 1  546  ? -5.391  35.020  72.532  1.00 19.78 ? 544  ALA B C     1 
ATOM   12831 O  O     . ALA B 1  546  ? -4.858  35.153  71.427  1.00 19.99 ? 544  ALA B O     1 
ATOM   12832 C  CB    . ALA B 1  546  ? -5.622  36.973  74.095  1.00 19.98 ? 544  ALA B CB    1 
ATOM   12833 N  N     . ARG B 1  547  ? -5.140  33.972  73.312  1.00 18.47 ? 545  ARG B N     1 
ATOM   12834 C  CA    . ARG B 1  547  ? -4.253  32.895  72.890  1.00 18.54 ? 545  ARG B CA    1 
ATOM   12835 C  C     . ARG B 1  547  ? -4.393  31.741  73.869  1.00 17.77 ? 545  ARG B C     1 
ATOM   12836 O  O     . ARG B 1  547  ? -4.956  31.888  74.960  1.00 18.91 ? 545  ARG B O     1 
ATOM   12837 C  CB    . ARG B 1  547  ? -2.785  33.345  72.811  1.00 19.43 ? 545  ARG B CB    1 
ATOM   12838 C  CG    . ARG B 1  547  ? -2.219  33.779  74.142  1.00 17.74 ? 545  ARG B CG    1 
ATOM   12839 C  CD    . ARG B 1  547  ? -0.814  34.377  73.952  1.00 17.25 ? 545  ARG B CD    1 
ATOM   12840 N  NE    . ARG B 1  547  ? -0.494  35.240  75.075  1.00 17.82 ? 545  ARG B NE    1 
ATOM   12841 C  CZ    . ARG B 1  547  ? 0.233   34.878  76.121  1.00 18.17 ? 545  ARG B CZ    1 
ATOM   12842 N  NH1   . ARG B 1  547  ? 0.830   33.697  76.175  1.00 16.71 ? 545  ARG B NH1   1 
ATOM   12843 N  NH2   . ARG B 1  547  ? 0.382   35.732  77.129  1.00 20.62 ? 545  ARG B NH2   1 
ATOM   12844 N  N     . THR B 1  548  ? -3.897  30.586  73.445  1.00 17.14 ? 546  THR B N     1 
ATOM   12845 C  CA    . THR B 1  548  ? -3.904  29.385  74.260  1.00 16.05 ? 546  THR B CA    1 
ATOM   12846 C  C     . THR B 1  548  ? -2.616  29.323  75.071  1.00 16.21 ? 546  THR B C     1 
ATOM   12847 O  O     . THR B 1  548  ? -1.521  29.463  74.521  1.00 15.90 ? 546  THR B O     1 
ATOM   12848 C  CB    . THR B 1  548  ? -4.034  28.149  73.374  1.00 18.83 ? 546  THR B CB    1 
ATOM   12849 O  OG1   . THR B 1  548  ? -5.240  28.245  72.601  1.00 20.40 ? 546  THR B OG1   1 
ATOM   12850 C  CG2   . THR B 1  548  ? -4.058  26.891  74.225  1.00 20.59 ? 546  THR B CG2   1 
ATOM   12851 N  N     . ASN B 1  549  ? -2.754  29.133  76.376  1.00 15.74 ? 547  ASN B N     1 
ATOM   12852 C  CA    . ASN B 1  549  ? -1.594  29.023  77.249  1.00 14.01 ? 547  ASN B CA    1 
ATOM   12853 C  C     . ASN B 1  549  ? -0.800  27.767  76.903  1.00 14.58 ? 547  ASN B C     1 
ATOM   12854 O  O     . ASN B 1  549  ? -1.375  26.726  76.576  1.00 16.82 ? 547  ASN B O     1 
ATOM   12855 C  CB    . ASN B 1  549  ? -2.078  28.991  78.702  1.00 15.91 ? 547  ASN B CB    1 
ATOM   12856 C  CG    . ASN B 1  549  ? -0.968  29.178  79.699  1.00 15.96 ? 547  ASN B CG    1 
ATOM   12857 O  OD1   . ASN B 1  549  ? 0.130   29.647  79.365  1.00 15.67 ? 547  ASN B OD1   1 
ATOM   12858 N  ND2   . ASN B 1  549  ? -1.260  28.842  80.950  1.00 16.13 ? 547  ASN B ND2   1 
ATOM   12859 N  N     . SER B 1  550  ? 0.528   27.876  76.926  1.00 14.69 ? 548  SER B N     1 
ATOM   12860 C  CA    . SER B 1  550  ? 1.348   26.675  76.805  1.00 16.17 ? 548  SER B CA    1 
ATOM   12861 C  C     . SER B 1  550  ? 1.005   25.701  77.928  1.00 17.11 ? 548  SER B C     1 
ATOM   12862 O  O     . SER B 1  550  ? 0.600   26.097  79.028  1.00 15.25 ? 548  SER B O     1 
ATOM   12863 C  CB    . SER B 1  550  ? 2.842   27.006  76.870  1.00 14.55 ? 548  SER B CB    1 
ATOM   12864 O  OG    . SER B 1  550  ? 3.172   27.546  78.137  1.00 15.34 ? 548  SER B OG    1 
ATOM   12865 N  N     . ALA B 1  551  ? 1.166   24.415  77.640  1.00 15.70 ? 549  ALA B N     1 
ATOM   12866 C  CA    . ALA B 1  551  ? 0.905   23.363  78.612  1.00 17.37 ? 549  ALA B CA    1 
ATOM   12867 C  C     . ALA B 1  551  ? 2.214   22.766  79.101  1.00 19.21 ? 549  ALA B C     1 
ATOM   12868 O  O     . ALA B 1  551  ? 3.168   22.618  78.332  1.00 18.12 ? 549  ALA B O     1 
ATOM   12869 C  CB    . ALA B 1  551  ? 0.032   22.261  78.011  1.00 18.79 ? 549  ALA B CB    1 
ATOM   12870 N  N     . GLY B 1  552  ? 2.249   22.414  80.380  1.00 19.24 ? 550  GLY B N     1 
ATOM   12871 C  CA    . GLY B 1  552  ? 3.373   21.729  80.969  1.00 19.05 ? 550  GLY B CA    1 
ATOM   12872 C  C     . GLY B 1  552  ? 3.157   20.230  81.035  1.00 15.23 ? 550  GLY B C     1 
ATOM   12873 O  O     . GLY B 1  552  ? 2.324   19.654  80.326  1.00 19.52 ? 550  GLY B O     1 
ATOM   12874 N  N     . LEU B 1  553  ? 3.933   19.585  81.901  1.00 17.89 ? 551  LEU B N     1 
ATOM   12875 C  CA    . LEU B 1  553  ? 3.823   18.153  82.140  1.00 19.42 ? 551  LEU B CA    1 
ATOM   12876 C  C     . LEU B 1  553  ? 3.852   17.927  83.639  1.00 16.29 ? 551  LEU B C     1 
ATOM   12877 O  O     . LEU B 1  553  ? 4.582   18.615  84.352  1.00 18.98 ? 551  LEU B O     1 
ATOM   12878 C  CB    . LEU B 1  553  ? 4.971   17.371  81.458  1.00 19.66 ? 551  LEU B CB    1 
ATOM   12879 C  CG    . LEU B 1  553  ? 4.975   17.352  79.925  1.00 20.04 ? 551  LEU B CG    1 
ATOM   12880 C  CD1   . LEU B 1  553  ? 6.300   16.805  79.390  1.00 22.16 ? 551  LEU B CD1   1 
ATOM   12881 C  CD2   . LEU B 1  553  ? 3.801   16.546  79.376  1.00 22.13 ? 551  LEU B CD2   1 
ATOM   12882 N  N     . ASP B 1  554  ? 3.046   16.979  84.117  1.00 17.69 ? 552  ASP B N     1 
ATOM   12883 C  CA    . ASP B 1  554  ? 2.917   16.734  85.554  1.00 17.53 ? 552  ASP B CA    1 
ATOM   12884 C  C     . ASP B 1  554  ? 3.943   15.683  85.962  1.00 16.35 ? 552  ASP B C     1 
ATOM   12885 O  O     . ASP B 1  554  ? 3.736   14.486  85.756  1.00 18.24 ? 552  ASP B O     1 
ATOM   12886 C  CB    . ASP B 1  554  ? 1.501   16.283  85.894  1.00 18.75 ? 552  ASP B CB    1 
ATOM   12887 C  CG    . ASP B 1  554  ? 1.287   16.106  87.391  1.00 17.98 ? 552  ASP B CG    1 
ATOM   12888 O  OD1   . ASP B 1  554  ? 2.250   16.285  88.175  1.00 19.63 ? 552  ASP B OD1   1 
ATOM   12889 O  OD2   . ASP B 1  554  ? 0.137   15.792  87.771  1.00 21.33 ? 552  ASP B OD2   1 
ATOM   12890 N  N     . LEU B 1  555  ? 5.040   16.123  86.566  1.00 18.34 ? 553  LEU B N     1 
ATOM   12891 C  CA    . LEU B 1  555  ? 6.071   15.179  86.961  1.00 19.88 ? 553  LEU B CA    1 
ATOM   12892 C  C     . LEU B 1  555  ? 5.739   14.467  88.263  1.00 20.89 ? 553  LEU B C     1 
ATOM   12893 O  O     . LEU B 1  555  ? 6.621   13.818  88.829  1.00 18.25 ? 553  LEU B O     1 
ATOM   12894 C  CB    . LEU B 1  555  ? 7.418   15.886  87.077  1.00 18.53 ? 553  LEU B CB    1 
ATOM   12895 C  CG    . LEU B 1  555  ? 7.883   16.577  85.794  1.00 19.68 ? 553  LEU B CG    1 
ATOM   12896 C  CD1   . LEU B 1  555  ? 9.260   17.145  86.048  1.00 19.85 ? 553  LEU B CD1   1 
ATOM   12897 C  CD2   . LEU B 1  555  ? 7.867   15.616  84.604  1.00 22.48 ? 553  LEU B CD2   1 
ATOM   12898 N  N     . SER B 1  556  ? 4.501   14.586  88.760  1.00 17.73 ? 554  SER B N     1 
ATOM   12899 C  CA    . SER B 1  556  ? 4.023   13.740  89.843  1.00 18.95 ? 554  SER B CA    1 
ATOM   12900 C  C     . SER B 1  556  ? 3.085   12.652  89.345  1.00 18.74 ? 554  SER B C     1 
ATOM   12901 O  O     . SER B 1  556  ? 2.660   11.805  90.134  1.00 19.64 ? 554  SER B O     1 
ATOM   12902 C  CB    . SER B 1  556  ? 3.322   14.583  90.926  1.00 19.30 ? 554  SER B CB    1 
ATOM   12903 O  OG    . SER B 1  556  ? 2.038   15.004  90.478  1.00 18.85 ? 554  SER B OG    1 
ATOM   12904 N  N     . ASN B 1  557  ? 2.778   12.642  88.051  1.00 17.18 ? 555  ASN B N     1 
ATOM   12905 C  CA    . ASN B 1  557  ? 1.864   11.682  87.458  1.00 18.61 ? 555  ASN B CA    1 
ATOM   12906 C  C     . ASN B 1  557  ? 2.667   10.506  86.904  1.00 19.92 ? 555  ASN B C     1 
ATOM   12907 O  O     . ASN B 1  557  ? 3.511   10.688  86.017  1.00 19.06 ? 555  ASN B O     1 
ATOM   12908 C  CB    . ASN B 1  557  ? 1.053   12.384  86.366  1.00 17.82 ? 555  ASN B CB    1 
ATOM   12909 C  CG    . ASN B 1  557  ? 0.039   11.467  85.699  1.00 21.45 ? 555  ASN B CG    1 
ATOM   12910 O  OD1   . ASN B 1  557  ? 0.375   10.367  85.257  1.00 21.28 ? 555  ASN B OD1   1 
ATOM   12911 N  ND2   . ASN B 1  557  ? -1.216  11.920  85.620  1.00 19.23 ? 555  ASN B ND2   1 
ATOM   12912 N  N     . GLU B 1  558  ? 2.408   9.302   87.424  1.00 19.46 ? 556  GLU B N     1 
ATOM   12913 C  CA    . GLU B 1  558  ? 3.229   8.155   87.037  1.00 21.53 ? 556  GLU B CA    1 
ATOM   12914 C  C     . GLU B 1  558  ? 3.074   7.815   85.569  1.00 21.19 ? 556  GLU B C     1 
ATOM   12915 O  O     . GLU B 1  558  ? 4.033   7.343   84.948  1.00 21.11 ? 556  GLU B O     1 
ATOM   12916 C  CB    . GLU B 1  558  ? 2.899   6.924   87.875  1.00 20.55 ? 556  GLU B CB    1 
ATOM   12917 C  CG    . GLU B 1  558  ? 3.305   7.031   89.310  1.00 20.22 ? 556  GLU B CG    1 
ATOM   12918 C  CD    . GLU B 1  558  ? 4.809   7.117   89.552  1.00 22.24 ? 556  GLU B CD    1 
ATOM   12919 O  OE1   . GLU B 1  558  ? 5.648   6.919   88.634  1.00 21.25 ? 556  GLU B OE1   1 
ATOM   12920 O  OE2   . GLU B 1  558  ? 5.149   7.408   90.708  1.00 19.90 ? 556  GLU B OE2   1 
ATOM   12921 N  N     . GLU B 1  559  ? 1.867   7.986   85.007  1.00 19.75 ? 557  GLU B N     1 
ATOM   12922 C  CA    . GLU B 1  559  ? 1.696   7.792   83.569  1.00 20.00 ? 557  GLU B CA    1 
ATOM   12923 C  C     . GLU B 1  559  ? 2.602   8.745   82.808  1.00 20.49 ? 557  GLU B C     1 
ATOM   12924 O  O     . GLU B 1  559  ? 3.291   8.354   81.860  1.00 20.84 ? 557  GLU B O     1 
ATOM   12925 C  CB    . GLU B 1  559  ? 0.244   8.028   83.135  1.00 24.63 ? 557  GLU B CB    1 
ATOM   12926 C  CG    . GLU B 1  559  ? -0.810  7.112   83.692  1.00 27.41 ? 557  GLU B CG    1 
ATOM   12927 C  CD    . GLU B 1  559  ? -2.194  7.442   83.133  1.00 33.43 ? 557  GLU B CD    1 
ATOM   12928 O  OE1   . GLU B 1  559  ? -2.274  7.979   82.006  1.00 34.93 ? 557  GLU B OE1   1 
ATOM   12929 O  OE2   . GLU B 1  559  ? -3.204  7.173   83.819  1.00 31.41 ? 557  GLU B OE2   1 
ATOM   12930 N  N     . THR B 1  560  ? 2.585   10.021  83.197  1.00 20.27 ? 558  THR B N     1 
ATOM   12931 C  CA    . THR B 1  560  ? 3.443   10.998  82.544  1.00 18.39 ? 558  THR B CA    1 
ATOM   12932 C  C     . THR B 1  560  ? 4.909   10.622  82.696  1.00 20.09 ? 558  THR B C     1 
ATOM   12933 O  O     . THR B 1  560  ? 5.682   10.693  81.733  1.00 19.83 ? 558  THR B O     1 
ATOM   12934 C  CB    . THR B 1  560  ? 3.186   12.390  83.122  1.00 18.24 ? 558  THR B CB    1 
ATOM   12935 O  OG1   . THR B 1  560  ? 1.793   12.712  82.970  1.00 19.88 ? 558  THR B OG1   1 
ATOM   12936 C  CG2   . THR B 1  560  ? 4.025   13.424  82.387  1.00 19.63 ? 558  THR B CG2   1 
ATOM   12937 N  N     . LEU B 1  561  ? 5.314   10.220  83.900  1.00 18.69 ? 559  LEU B N     1 
ATOM   12938 C  CA    . LEU B 1  561  ? 6.717   9.885   84.108  1.00 18.72 ? 559  LEU B CA    1 
ATOM   12939 C  C     . LEU B 1  561  ? 7.123   8.680   83.269  1.00 19.51 ? 559  LEU B C     1 
ATOM   12940 O  O     . LEU B 1  561  ? 8.236   8.642   82.734  1.00 19.88 ? 559  LEU B O     1 
ATOM   12941 C  CB    . LEU B 1  561  ? 6.982   9.639   85.592  1.00 19.47 ? 559  LEU B CB    1 
ATOM   12942 C  CG    . LEU B 1  561  ? 6.897   10.887  86.476  1.00 16.50 ? 559  LEU B CG    1 
ATOM   12943 C  CD1   . LEU B 1  561  ? 7.050   10.483  87.940  1.00 19.00 ? 559  LEU B CD1   1 
ATOM   12944 C  CD2   . LEU B 1  561  ? 7.977   11.877  86.061  1.00 17.82 ? 559  LEU B CD2   1 
ATOM   12945 N  N     . ALA B 1  562  ? 6.239   7.692   83.143  1.00 19.26 ? 560  ALA B N     1 
ATOM   12946 C  CA    . ALA B 1  562  ? 6.567   6.507   82.356  1.00 20.76 ? 560  ALA B CA    1 
ATOM   12947 C  C     . ALA B 1  562  ? 6.684   6.835   80.870  1.00 23.28 ? 560  ALA B C     1 
ATOM   12948 O  O     . ALA B 1  562  ? 7.610   6.367   80.197  1.00 22.76 ? 560  ALA B O     1 
ATOM   12949 C  CB    . ALA B 1  562  ? 5.514   5.422   82.586  1.00 19.76 ? 560  ALA B CB    1 
ATOM   12950 N  N     . SER B 1  563  ? 5.751   7.626   80.329  1.00 20.36 ? 561  SER B N     1 
ATOM   12951 C  CA    . SER B 1  563  ? 5.827   7.963   78.908  1.00 21.56 ? 561  SER B CA    1 
ATOM   12952 C  C     . SER B 1  563  ? 6.953   8.953   78.641  1.00 21.85 ? 561  SER B C     1 
ATOM   12953 O  O     . SER B 1  563  ? 7.619   8.882   77.600  1.00 23.10 ? 561  SER B O     1 
ATOM   12954 C  CB    . SER B 1  563  ? 4.490   8.524   78.417  1.00 23.92 ? 561  SER B CB    1 
ATOM   12955 O  OG    . SER B 1  563  ? 4.210   9.772   79.021  1.00 25.19 ? 561  SER B OG    1 
ATOM   12956 N  N     . LEU B 1  564  ? 7.175   9.888   79.568  1.00 20.56 ? 562  LEU B N     1 
ATOM   12957 C  CA    . LEU B 1  564  ? 8.295   10.804  79.422  1.00 19.17 ? 562  LEU B CA    1 
ATOM   12958 C  C     . LEU B 1  564  ? 9.624   10.053  79.446  1.00 19.21 ? 562  LEU B C     1 
ATOM   12959 O  O     . LEU B 1  564  ? 10.504  10.316  78.617  1.00 20.55 ? 562  LEU B O     1 
ATOM   12960 C  CB    . LEU B 1  564  ? 8.242   11.870  80.520  1.00 20.11 ? 562  LEU B CB    1 
ATOM   12961 C  CG    . LEU B 1  564  ? 9.305   12.951  80.444  1.00 22.78 ? 562  LEU B CG    1 
ATOM   12962 C  CD1   . LEU B 1  564  ? 9.202   13.677  79.099  1.00 23.41 ? 562  LEU B CD1   1 
ATOM   12963 C  CD2   . LEU B 1  564  ? 9.161   13.918  81.619  1.00 22.96 ? 562  LEU B CD2   1 
ATOM   12964 N  N     . THR B 1  565  ? 9.782   9.102   80.378  1.00 19.50 ? 563  THR B N     1 
ATOM   12965 C  CA    . THR B 1  565  ? 10.994  8.280   80.412  1.00 21.29 ? 563  THR B CA    1 
ATOM   12966 C  C     . THR B 1  565  ? 11.300  7.692   79.038  1.00 21.30 ? 563  THR B C     1 
ATOM   12967 O  O     . THR B 1  565  ? 12.435  7.758   78.553  1.00 20.88 ? 563  THR B O     1 
ATOM   12968 C  CB    . THR B 1  565  ? 10.848  7.151   81.433  1.00 21.68 ? 563  THR B CB    1 
ATOM   12969 O  OG1   . THR B 1  565  ? 10.765  7.699   82.754  1.00 21.15 ? 563  THR B OG1   1 
ATOM   12970 C  CG2   . THR B 1  565  ? 12.069  6.237   81.372  1.00 21.88 ? 563  THR B CG2   1 
ATOM   12971 N  N     . GLU B 1  566  ? 10.288  7.129   78.385  1.00 21.56 ? 564  GLU B N     1 
ATOM   12972 C  CA    . GLU B 1  566  ? 10.531  6.500   77.092  1.00 22.19 ? 564  GLU B CA    1 
ATOM   12973 C  C     . GLU B 1  566  ? 10.865  7.538   76.034  1.00 21.49 ? 564  GLU B C     1 
ATOM   12974 O  O     . GLU B 1  566  ? 11.755  7.320   75.204  1.00 20.76 ? 564  GLU B O     1 
ATOM   12975 C  CB    . GLU B 1  566  ? 9.321   5.664   76.680  1.00 24.68 ? 564  GLU B CB    1 
ATOM   12976 C  CG    . GLU B 1  566  ? 9.118   4.454   77.589  1.00 28.95 ? 564  GLU B CG    1 
ATOM   12977 C  CD    . GLU B 1  566  ? 10.431  3.776   77.962  1.00 33.62 ? 564  GLU B CD    1 
ATOM   12978 O  OE1   . GLU B 1  566  ? 11.226  3.444   77.050  1.00 37.13 ? 564  GLU B OE1   1 
ATOM   12979 O  OE2   . GLU B 1  566  ? 10.677  3.582   79.173  1.00 35.01 ? 564  GLU B OE2   1 
ATOM   12980 N  N     . ALA B 1  567  ? 10.167  8.677   76.056  1.00 20.02 ? 565  ALA B N     1 
ATOM   12981 C  CA    . ALA B 1  567  ? 10.445  9.747   75.104  1.00 21.25 ? 565  ALA B CA    1 
ATOM   12982 C  C     . ALA B 1  567  ? 11.842  10.312  75.301  1.00 20.18 ? 565  ALA B C     1 
ATOM   12983 O  O     . ALA B 1  567  ? 12.532  10.639  74.327  1.00 19.71 ? 565  ALA B O     1 
ATOM   12984 C  CB    . ALA B 1  567  ? 9.402   10.855  75.248  1.00 20.99 ? 565  ALA B CB    1 
ATOM   12985 N  N     . LEU B 1  568  ? 12.274  10.448  76.557  1.00 18.65 ? 566  LEU B N     1 
ATOM   12986 C  CA    . LEU B 1  568  ? 13.609  10.968  76.824  1.00 19.18 ? 566  LEU B CA    1 
ATOM   12987 C  C     . LEU B 1  568  ? 14.669  9.976   76.368  1.00 18.97 ? 566  LEU B C     1 
ATOM   12988 O  O     . LEU B 1  568  ? 15.658  10.357  75.733  1.00 19.60 ? 566  LEU B O     1 
ATOM   12989 C  CB    . LEU B 1  568  ? 13.766  11.288  78.315  1.00 18.70 ? 566  LEU B CB    1 
ATOM   12990 C  CG    . LEU B 1  568  ? 12.847  12.387  78.878  1.00 17.00 ? 566  LEU B CG    1 
ATOM   12991 C  CD1   . LEU B 1  568  ? 12.928  12.418  80.386  1.00 21.23 ? 566  LEU B CD1   1 
ATOM   12992 C  CD2   . LEU B 1  568  ? 13.188  13.755  78.312  1.00 19.87 ? 566  LEU B CD2   1 
ATOM   12993 N  N     . ARG B 1  569  ? 14.479  8.697   76.691  1.00 20.52 ? 567  ARG B N     1 
ATOM   12994 C  CA    . ARG B 1  569  ? 15.389  7.665   76.207  1.00 20.11 ? 567  ARG B CA    1 
ATOM   12995 C  C     . ARG B 1  569  ? 15.499  7.686   74.688  1.00 23.26 ? 567  ARG B C     1 
ATOM   12996 O  O     . ARG B 1  569  ? 16.606  7.650   74.137  1.00 22.74 ? 567  ARG B O     1 
ATOM   12997 C  CB    . ARG B 1  569  ? 14.924  6.293   76.694  1.00 21.33 ? 567  ARG B CB    1 
ATOM   12998 C  CG    . ARG B 1  569  ? 15.169  6.082   78.159  1.00 26.60 ? 567  ARG B CG    1 
ATOM   12999 C  CD    . ARG B 1  569  ? 14.628  4.742   78.662  1.00 28.95 ? 567  ARG B CD    1 
ATOM   13000 N  NE    . ARG B 1  569  ? 14.841  4.634   80.102  1.00 31.53 ? 567  ARG B NE    1 
ATOM   13001 C  CZ    . ARG B 1  569  ? 14.284  3.717   80.881  1.00 33.90 ? 567  ARG B CZ    1 
ATOM   13002 N  NH1   . ARG B 1  569  ? 13.452  2.811   80.394  1.00 34.71 ? 567  ARG B NH1   1 
ATOM   13003 N  NH2   . ARG B 1  569  ? 14.562  3.716   82.184  1.00 36.21 ? 567  ARG B NH2   1 
ATOM   13004 N  N     . GLU B 1  570  ? 14.355  7.755   73.998  1.00 21.59 ? 568  GLU B N     1 
ATOM   13005 C  CA    . GLU B 1  570  ? 14.363  7.757   72.539  1.00 22.28 ? 568  GLU B CA    1 
ATOM   13006 C  C     . GLU B 1  570  ? 15.042  9.001   71.986  1.00 21.96 ? 568  GLU B C     1 
ATOM   13007 O  O     . GLU B 1  570  ? 15.676  8.937   70.928  1.00 24.11 ? 568  GLU B O     1 
ATOM   13008 C  CB    . GLU B 1  570  ? 12.933  7.641   72.001  1.00 24.14 ? 568  GLU B CB    1 
ATOM   13009 C  CG    . GLU B 1  570  ? 12.311  6.274   72.251  1.00 25.27 ? 568  GLU B CG    1 
ATOM   13010 C  CD    . GLU B 1  570  ? 10.793  6.304   72.343  1.00 32.94 ? 568  GLU B CD    1 
ATOM   13011 O  OE1   . GLU B 1  570  ? 10.179  7.333   71.974  1.00 34.52 ? 568  GLU B OE1   1 
ATOM   13012 O  OE2   . GLU B 1  570  ? 10.216  5.291   72.802  1.00 35.27 ? 568  GLU B OE2   1 
ATOM   13013 N  N     . SER B 1  571  ? 14.925  10.135  72.686  1.00 22.02 ? 569  SER B N     1 
ATOM   13014 C  CA    . SER B 1  571  ? 15.555  11.364  72.218  1.00 20.77 ? 569  SER B CA    1 
ATOM   13015 C  C     . SER B 1  571  ? 17.070  11.236  72.215  1.00 23.05 ? 569  SER B C     1 
ATOM   13016 O  O     . SER B 1  571  ? 17.747  11.829  71.365  1.00 22.24 ? 569  SER B O     1 
ATOM   13017 C  CB    . SER B 1  571  ? 15.128  12.544  73.097  1.00 21.09 ? 569  SER B CB    1 
ATOM   13018 O  OG    . SER B 1  571  ? 15.860  12.578  74.328  1.00 22.50 ? 569  SER B OG    1 
ATOM   13019 N  N     . ALA B 1  572  ? 17.621  10.470  73.155  1.00 21.97 ? 570  ALA B N     1 
ATOM   13020 C  CA    . ALA B 1  572  ? 19.063  10.291  73.197  1.00 23.46 ? 570  ALA B CA    1 
ATOM   13021 C  C     . ALA B 1  572  ? 19.562  9.389   72.073  1.00 24.83 ? 570  ALA B C     1 
ATOM   13022 O  O     . ALA B 1  572  ? 20.749  9.446   71.728  1.00 26.85 ? 570  ALA B O     1 
ATOM   13023 C  CB    . ALA B 1  572  ? 19.478  9.738   74.557  1.00 24.77 ? 570  ALA B CB    1 
ATOM   13024 N  N     . ALA B 1  573  ? 18.688  8.572   71.482  1.00 23.52 ? 571  ALA B N     1 
ATOM   13025 C  CA    . ALA B 1  573  ? 19.095  7.715   70.377  1.00 25.68 ? 571  ALA B CA    1 
ATOM   13026 C  C     . ALA B 1  573  ? 19.054  8.421   69.026  1.00 25.51 ? 571  ALA B C     1 
ATOM   13027 O  O     . ALA B 1  573  ? 19.530  7.855   68.035  1.00 26.46 ? 571  ALA B O     1 
ATOM   13028 C  CB    . ALA B 1  573  ? 18.214  6.467   70.331  1.00 26.91 ? 571  ALA B CB    1 
ATOM   13029 N  N     . MET B 1  574  ? 18.498  9.627   68.957  1.00 25.47 ? 572  MET B N     1 
ATOM   13030 C  CA    . MET B 1  574  ? 18.416  10.353  67.698  1.00 22.88 ? 572  MET B CA    1 
ATOM   13031 C  C     . MET B 1  574  ? 19.759  10.980  67.344  1.00 23.01 ? 572  MET B C     1 
ATOM   13032 O  O     . MET B 1  574  ? 20.540  11.361  68.222  1.00 23.25 ? 572  MET B O     1 
ATOM   13033 C  CB    . MET B 1  574  ? 17.352  11.445  67.786  1.00 21.74 ? 572  MET B CB    1 
ATOM   13034 C  CG    . MET B 1  574  ? 15.942  10.894  67.913  1.00 24.24 ? 572  MET B CG    1 
ATOM   13035 S  SD    . MET B 1  574  ? 14.807  12.147  68.532  1.00 26.88 ? 572  MET B SD    1 
ATOM   13036 C  CE    . MET B 1  574  ? 13.289  11.190  68.545  1.00 25.20 ? 572  MET B CE    1 
ATOM   13037 N  N     . LYS B 1  575  ? 20.008  11.120  66.044  1.00 21.55 ? 573  LYS B N     1 
ATOM   13038 C  CA    . LYS B 1  575  ? 21.204  11.817  65.567  1.00 21.96 ? 573  LYS B CA    1 
ATOM   13039 C  C     . LYS B 1  575  ? 20.873  13.297  65.503  1.00 21.59 ? 573  LYS B C     1 
ATOM   13040 O  O     . LYS B 1  575  ? 20.188  13.751  64.581  1.00 21.84 ? 573  LYS B O     1 
ATOM   13041 C  CB    . LYS B 1  575  ? 21.656  11.307  64.205  1.00 20.69 ? 573  LYS B CB    1 
ATOM   13042 C  CG    . LYS B 1  575  ? 23.006  11.883  63.779  1.00 27.65 ? 573  LYS B CG    1 
ATOM   13043 C  CD    . LYS B 1  575  ? 23.142  11.956  62.255  1.00 33.28 ? 573  LYS B CD    1 
ATOM   13044 C  CE    . LYS B 1  575  ? 24.566  11.670  61.796  1.00 38.83 ? 573  LYS B CE    1 
ATOM   13045 N  NZ    . LYS B 1  575  ? 25.582  12.397  62.618  1.00 42.59 ? 573  LYS B NZ    1 
ATOM   13046 N  N     . TRP B 1  576  ? 21.349  14.044  66.495  1.00 20.56 ? 574  TRP B N     1 
ATOM   13047 C  CA    . TRP B 1  576  ? 21.136  15.478  66.575  1.00 18.93 ? 574  TRP B CA    1 
ATOM   13048 C  C     . TRP B 1  576  ? 22.279  16.212  65.899  1.00 19.21 ? 574  TRP B C     1 
ATOM   13049 O  O     . TRP B 1  576  ? 23.448  15.995  66.233  1.00 19.42 ? 574  TRP B O     1 
ATOM   13050 C  CB    . TRP B 1  576  ? 21.037  15.929  68.029  1.00 20.05 ? 574  TRP B CB    1 
ATOM   13051 C  CG    . TRP B 1  576  ? 19.841  15.383  68.756  1.00 18.04 ? 574  TRP B CG    1 
ATOM   13052 C  CD1   . TRP B 1  576  ? 19.839  14.409  69.718  1.00 21.21 ? 574  TRP B CD1   1 
ATOM   13053 C  CD2   . TRP B 1  576  ? 18.482  15.805  68.604  1.00 19.11 ? 574  TRP B CD2   1 
ATOM   13054 N  NE1   . TRP B 1  576  ? 18.555  14.194  70.170  1.00 19.74 ? 574  TRP B NE1   1 
ATOM   13055 C  CE2   . TRP B 1  576  ? 17.703  15.034  69.495  1.00 20.51 ? 574  TRP B CE2   1 
ATOM   13056 C  CE3   . TRP B 1  576  ? 17.847  16.747  67.792  1.00 18.40 ? 574  TRP B CE3   1 
ATOM   13057 C  CZ2   . TRP B 1  576  ? 16.321  15.191  69.607  1.00 21.71 ? 574  TRP B CZ2   1 
ATOM   13058 C  CZ3   . TRP B 1  576  ? 16.471  16.909  67.911  1.00 19.00 ? 574  TRP B CZ3   1 
ATOM   13059 C  CH2   . TRP B 1  576  ? 15.726  16.133  68.808  1.00 21.75 ? 574  TRP B CH2   1 
ATOM   13060 N  N     . THR B 1  577  ? 21.936  17.085  64.960  1.00 21.00 ? 575  THR B N     1 
ATOM   13061 C  CA    . THR B 1  577  ? 22.922  17.862  64.225  1.00 19.19 ? 575  THR B CA    1 
ATOM   13062 C  C     . THR B 1  577  ? 22.490  19.318  64.184  1.00 18.97 ? 575  THR B C     1 
ATOM   13063 O  O     . THR B 1  577  ? 21.318  19.654  64.379  1.00 18.08 ? 575  THR B O     1 
ATOM   13064 C  CB    . THR B 1  577  ? 23.097  17.357  62.792  1.00 21.72 ? 575  THR B CB    1 
ATOM   13065 O  OG1   . THR B 1  577  ? 21.881  17.563  62.067  1.00 22.46 ? 575  THR B OG1   1 
ATOM   13066 C  CG2   . THR B 1  577  ? 23.451  15.891  62.777  1.00 21.09 ? 575  THR B CG2   1 
ATOM   13067 N  N     . ALA B 1  578  ? 23.456  20.184  63.899  1.00 17.24 ? 576  ALA B N     1 
ATOM   13068 C  CA    . ALA B 1  578  ? 23.176  21.591  63.654  1.00 18.08 ? 576  ALA B CA    1 
ATOM   13069 C  C     . ALA B 1  578  ? 24.121  22.016  62.546  1.00 15.98 ? 576  ALA B C     1 
ATOM   13070 O  O     . ALA B 1  578  ? 25.329  21.818  62.668  1.00 19.36 ? 576  ALA B O     1 
ATOM   13071 C  CB    . ALA B 1  578  ? 23.370  22.447  64.915  1.00 16.77 ? 576  ALA B CB    1 
ATOM   13072 N  N     . LEU B 1  579  ? 23.573  22.559  61.469  1.00 17.48 ? 577  LEU B N     1 
ATOM   13073 C  CA    . LEU B 1  579  ? 24.312  22.893  60.265  1.00 17.45 ? 577  LEU B CA    1 
ATOM   13074 C  C     . LEU B 1  579  ? 24.075  24.348  59.913  1.00 16.72 ? 577  LEU B C     1 
ATOM   13075 O  O     . LEU B 1  579  ? 23.076  24.942  60.333  1.00 16.22 ? 577  LEU B O     1 
ATOM   13076 C  CB    . LEU B 1  579  ? 23.865  22.015  59.086  1.00 19.11 ? 577  LEU B CB    1 
ATOM   13077 C  CG    . LEU B 1  579  ? 23.691  20.533  59.379  1.00 23.51 ? 577  LEU B CG    1 
ATOM   13078 C  CD1   . LEU B 1  579  ? 23.151  19.787  58.153  1.00 24.25 ? 577  LEU B CD1   1 
ATOM   13079 C  CD2   . LEU B 1  579  ? 25.024  19.979  59.801  1.00 21.93 ? 577  LEU B CD2   1 
ATOM   13080 N  N     . PRO B 1  580  ? 24.965  24.947  59.122  1.00 16.48 ? 578  PRO B N     1 
ATOM   13081 C  CA    . PRO B 1  580  ? 24.639  26.235  58.507  1.00 16.20 ? 578  PRO B CA    1 
ATOM   13082 C  C     . PRO B 1  580  ? 23.541  26.014  57.483  1.00 17.06 ? 578  PRO B C     1 
ATOM   13083 O  O     . PRO B 1  580  ? 23.791  25.526  56.376  1.00 18.58 ? 578  PRO B O     1 
ATOM   13084 C  CB    . PRO B 1  580  ? 25.960  26.681  57.865  1.00 18.16 ? 578  PRO B CB    1 
ATOM   13085 C  CG    . PRO B 1  580  ? 27.012  25.797  58.516  1.00 18.23 ? 578  PRO B CG    1 
ATOM   13086 C  CD    . PRO B 1  580  ? 26.309  24.491  58.739  1.00 16.78 ? 578  PRO B CD    1 
ATOM   13087 N  N     . GLN B 1  581  ? 22.308  26.299  57.877  1.00 15.55 ? 579  GLN B N     1 
ATOM   13088 C  CA    . GLN B 1  581  ? 21.149  26.079  57.011  1.00 18.64 ? 579  GLN B CA    1 
ATOM   13089 C  C     . GLN B 1  581  ? 20.855  27.366  56.268  1.00 17.88 ? 579  GLN B C     1 
ATOM   13090 O  O     . GLN B 1  581  ? 20.145  28.245  56.763  1.00 17.12 ? 579  GLN B O     1 
ATOM   13091 C  CB    . GLN B 1  581  ? 19.948  25.635  57.825  1.00 19.28 ? 579  GLN B CB    1 
ATOM   13092 C  CG    . GLN B 1  581  ? 20.193  24.356  58.536  1.00 18.90 ? 579  GLN B CG    1 
ATOM   13093 C  CD    . GLN B 1  581  ? 20.133  23.145  57.631  1.00 23.63 ? 579  GLN B CD    1 
ATOM   13094 O  OE1   . GLN B 1  581  ? 19.925  23.251  56.410  1.00 23.81 ? 579  GLN B OE1   1 
ATOM   13095 N  NE2   . GLN B 1  581  ? 20.299  21.972  58.232  1.00 27.18 ? 579  GLN B NE2   1 
ATOM   13096 N  N     . LEU B 1  582  ? 21.421  27.485  55.074  1.00 19.03 ? 580  LEU B N     1 
ATOM   13097 C  CA    . LEU B 1  582  ? 21.158  28.644  54.240  1.00 17.32 ? 580  LEU B CA    1 
ATOM   13098 C  C     . LEU B 1  582  ? 19.899  28.402  53.400  1.00 18.36 ? 580  LEU B C     1 
ATOM   13099 O  O     . LEU B 1  582  ? 19.307  27.321  53.417  1.00 19.92 ? 580  LEU B O     1 
ATOM   13100 C  CB    . LEU B 1  582  ? 22.377  28.959  53.370  1.00 18.85 ? 580  LEU B CB    1 
ATOM   13101 C  CG    . LEU B 1  582  ? 23.481  29.788  54.067  1.00 23.05 ? 580  LEU B CG    1 
ATOM   13102 C  CD1   . LEU B 1  582  ? 24.119  29.055  55.256  1.00 22.17 ? 580  LEU B CD1   1 
ATOM   13103 C  CD2   . LEU B 1  582  ? 24.542  30.211  53.075  1.00 28.35 ? 580  LEU B CD2   1 
ATOM   13104 N  N     . ALA B 1  583  ? 19.459  29.446  52.693  1.00 17.22 ? 581  ALA B N     1 
ATOM   13105 C  CA    . ALA B 1  583  ? 18.248  29.302  51.890  1.00 19.83 ? 581  ALA B CA    1 
ATOM   13106 C  C     . ALA B 1  583  ? 18.407  28.215  50.836  1.00 26.05 ? 581  ALA B C     1 
ATOM   13107 O  O     . ALA B 1  583  ? 17.435  27.534  50.494  1.00 28.66 ? 581  ALA B O     1 
ATOM   13108 C  CB    . ALA B 1  583  ? 17.891  30.636  51.227  1.00 21.83 ? 581  ALA B CB    1 
ATOM   13109 N  N     . THR B 1  584  ? 19.616  28.038  50.317  1.00 20.30 ? 582  THR B N     1 
ATOM   13110 C  CA    . THR B 1  584  ? 19.886  27.076  49.259  1.00 24.17 ? 582  THR B CA    1 
ATOM   13111 C  C     . THR B 1  584  ? 20.222  25.686  49.785  1.00 21.64 ? 582  THR B C     1 
ATOM   13112 O  O     . THR B 1  584  ? 20.508  24.789  48.988  1.00 21.79 ? 582  THR B O     1 
ATOM   13113 C  CB    . THR B 1  584  ? 21.036  27.589  48.390  1.00 23.95 ? 582  THR B CB    1 
ATOM   13114 O  OG1   . THR B 1  584  ? 22.104  28.011  49.246  1.00 26.80 ? 582  THR B OG1   1 
ATOM   13115 C  CG2   . THR B 1  584  ? 20.588  28.769  47.579  1.00 28.80 ? 582  THR B CG2   1 
ATOM   13116 N  N     . GLY B 1  585  ? 20.205  25.481  51.099  1.00 21.17 ? 583  GLY B N     1 
ATOM   13117 C  CA    . GLY B 1  585  ? 20.567  24.202  51.654  1.00 19.56 ? 583  GLY B CA    1 
ATOM   13118 C  C     . GLY B 1  585  ? 21.677  24.345  52.673  1.00 21.40 ? 583  GLY B C     1 
ATOM   13119 O  O     . GLY B 1  585  ? 22.220  25.435  52.883  1.00 19.92 ? 583  GLY B O     1 
ATOM   13120 N  N     . PRO B 1  586  ? 22.015  23.247  53.344  1.00 19.41 ? 584  PRO B N     1 
ATOM   13121 C  CA    . PRO B 1  586  ? 23.076  23.303  54.354  1.00 18.28 ? 584  PRO B CA    1 
ATOM   13122 C  C     . PRO B 1  586  ? 24.431  23.469  53.703  1.00 22.60 ? 584  PRO B C     1 
ATOM   13123 O  O     . PRO B 1  586  ? 24.716  22.888  52.654  1.00 22.00 ? 584  PRO B O     1 
ATOM   13124 C  CB    . PRO B 1  586  ? 22.959  21.955  55.071  1.00 20.22 ? 584  PRO B CB    1 
ATOM   13125 C  CG    . PRO B 1  586  ? 22.390  21.050  54.026  1.00 22.65 ? 584  PRO B CG    1 
ATOM   13126 C  CD    . PRO B 1  586  ? 21.438  21.897  53.230  1.00 22.07 ? 584  PRO B CD    1 
ATOM   13127 N  N     . ALA B 1  587  ? 25.266  24.277  54.337  1.00 20.84 ? 585  ALA B N     1 
ATOM   13128 C  CA    . ALA B 1  587  ? 26.603  24.554  53.847  1.00 20.00 ? 585  ALA B CA    1 
ATOM   13129 C  C     . ALA B 1  587  ? 27.617  23.709  54.600  1.00 20.14 ? 585  ALA B C     1 
ATOM   13130 O  O     . ALA B 1  587  ? 27.384  23.265  55.729  1.00 19.49 ? 585  ALA B O     1 
ATOM   13131 C  CB    . ALA B 1  587  ? 26.941  26.043  53.994  1.00 21.50 ? 585  ALA B CB    1 
ATOM   13132 N  N     . ALA B 1  588  ? 28.746  23.476  53.941  1.00 20.68 ? 586  ALA B N     1 
ATOM   13133 C  CA    . ALA B 1  588  ? 29.870  22.810  54.577  1.00 20.37 ? 586  ALA B CA    1 
ATOM   13134 C  C     . ALA B 1  588  ? 30.532  23.738  55.586  1.00 20.02 ? 586  ALA B C     1 
ATOM   13135 O  O     . ALA B 1  588  ? 30.427  24.964  55.505  1.00 20.42 ? 586  ALA B O     1 
ATOM   13136 C  CB    . ALA B 1  588  ? 30.889  22.372  53.526  1.00 19.13 ? 586  ALA B CB    1 
ATOM   13137 N  N     . GLY B 1  589  ? 31.228  23.135  56.541  1.00 21.59 ? 587  GLY B N     1 
ATOM   13138 C  CA    . GLY B 1  589  ? 31.953  23.910  57.531  1.00 21.38 ? 587  GLY B CA    1 
ATOM   13139 C  C     . GLY B 1  589  ? 32.714  23.009  58.478  1.00 22.67 ? 587  GLY B C     1 
ATOM   13140 O  O     . GLY B 1  589  ? 32.758  21.789  58.308  1.00 23.89 ? 587  GLY B O     1 
ATOM   13141 N  N     . GLU B 1  590  ? 33.319  23.634  59.488  1.00 23.28 ? 588  GLU B N     1 
ATOM   13142 C  CA    . GLU B 1  590  ? 34.073  22.909  60.504  1.00 22.83 ? 588  GLU B CA    1 
ATOM   13143 C  C     . GLU B 1  590  ? 33.114  22.249  61.488  1.00 22.00 ? 588  GLU B C     1 
ATOM   13144 O  O     . GLU B 1  590  ? 32.256  22.913  62.068  1.00 21.57 ? 588  GLU B O     1 
ATOM   13145 C  CB    . GLU B 1  590  ? 35.011  23.861  61.246  1.00 26.21 ? 588  GLU B CB    1 
ATOM   13146 N  N     . THR B 1  591  ? 33.287  20.948  61.705  1.00 24.65 ? 589  THR B N     1 
ATOM   13147 C  CA    . THR B 1  591  ? 32.370  20.167  62.523  1.00 21.17 ? 589  THR B CA    1 
ATOM   13148 C  C     . THR B 1  591  ? 33.044  19.712  63.811  1.00 24.46 ? 589  THR B C     1 
ATOM   13149 O  O     . THR B 1  591  ? 34.219  19.328  63.810  1.00 25.30 ? 589  THR B O     1 
ATOM   13150 C  CB    . THR B 1  591  ? 31.871  18.954  61.741  1.00 22.71 ? 589  THR B CB    1 
ATOM   13151 O  OG1   . THR B 1  591  ? 31.251  19.404  60.529  1.00 26.04 ? 589  THR B OG1   1 
ATOM   13152 C  CG2   . THR B 1  591  ? 30.856  18.166  62.561  1.00 24.66 ? 589  THR B CG2   1 
ATOM   13153 N  N     . ARG B 1  592  ? 32.295  19.756  64.910  1.00 22.98 ? 590  ARG B N     1 
ATOM   13154 C  CA    . ARG B 1  592  ? 32.773  19.235  66.179  1.00 26.15 ? 590  ARG B CA    1 
ATOM   13155 C  C     . ARG B 1  592  ? 31.602  18.628  66.936  1.00 23.33 ? 590  ARG B C     1 
ATOM   13156 O  O     . ARG B 1  592  ? 30.436  18.842  66.590  1.00 22.78 ? 590  ARG B O     1 
ATOM   13157 C  CB    . ARG B 1  592  ? 33.442  20.327  67.014  1.00 25.66 ? 590  ARG B CB    1 
ATOM   13158 C  CG    . ARG B 1  592  ? 32.518  21.469  67.345  1.00 26.60 ? 590  ARG B CG    1 
ATOM   13159 C  CD    . ARG B 1  592  ? 33.030  22.261  68.513  1.00 30.55 ? 590  ARG B CD    1 
ATOM   13160 N  NE    . ARG B 1  592  ? 32.176  23.409  68.790  1.00 29.53 ? 590  ARG B NE    1 
ATOM   13161 C  CZ    . ARG B 1  592  ? 31.173  23.399  69.656  1.00 29.65 ? 590  ARG B CZ    1 
ATOM   13162 N  NH1   . ARG B 1  592  ? 30.859  22.308  70.336  1.00 27.10 ? 590  ARG B NH1   1 
ATOM   13163 N  NH2   . ARG B 1  592  ? 30.479  24.518  69.854  1.00 27.21 ? 590  ARG B NH2   1 
ATOM   13164 N  N     . THR B 1  593  ? 31.925  17.874  67.986  1.00 22.96 ? 591  THR B N     1 
ATOM   13165 C  CA    . THR B 1  593  ? 30.905  17.253  68.818  1.00 21.52 ? 591  THR B CA    1 
ATOM   13166 C  C     . THR B 1  593  ? 30.336  18.245  69.822  1.00 22.19 ? 591  THR B C     1 
ATOM   13167 O  O     . THR B 1  593  ? 30.985  19.212  70.228  1.00 22.76 ? 591  THR B O     1 
ATOM   13168 C  CB    . THR B 1  593  ? 31.467  16.043  69.566  1.00 23.51 ? 591  THR B CB    1 
ATOM   13169 O  OG1   . THR B 1  593  ? 32.552  16.465  70.403  1.00 26.66 ? 591  THR B OG1   1 
ATOM   13170 C  CG2   . THR B 1  593  ? 31.971  15.002  68.579  1.00 28.47 ? 591  THR B CG2   1 
ATOM   13171 N  N     . VAL B 1  594  ? 29.093  18.000  70.209  1.00 20.84 ? 592  VAL B N     1 
ATOM   13172 C  CA    . VAL B 1  594  ? 28.446  18.710  71.299  1.00 20.52 ? 592  VAL B CA    1 
ATOM   13173 C  C     . VAL B 1  594  ? 28.348  17.723  72.449  1.00 23.19 ? 592  VAL B C     1 
ATOM   13174 O  O     . VAL B 1  594  ? 27.799  16.627  72.284  1.00 22.17 ? 592  VAL B O     1 
ATOM   13175 C  CB    . VAL B 1  594  ? 27.070  19.246  70.877  1.00 20.03 ? 592  VAL B CB    1 
ATOM   13176 C  CG1   . VAL B 1  594  ? 26.410  19.992  72.033  1.00 20.49 ? 592  VAL B CG1   1 
ATOM   13177 C  CG2   . VAL B 1  594  ? 27.209  20.138  69.644  1.00 22.08 ? 592  VAL B CG2   1 
ATOM   13178 N  N     . LEU B 1  595  ? 28.932  18.083  73.589  1.00 21.93 ? 593  LEU B N     1 
ATOM   13179 C  CA    . LEU B 1  595  ? 29.054  17.190  74.731  1.00 21.74 ? 593  LEU B CA    1 
ATOM   13180 C  C     . LEU B 1  595  ? 28.154  17.657  75.865  1.00 19.21 ? 593  LEU B C     1 
ATOM   13181 O  O     . LEU B 1  595  ? 27.941  18.855  76.060  1.00 21.69 ? 593  LEU B O     1 
ATOM   13182 C  CB    . LEU B 1  595  ? 30.501  17.116  75.230  1.00 21.93 ? 593  LEU B CB    1 
ATOM   13183 C  CG    . LEU B 1  595  ? 31.543  16.681  74.211  1.00 22.31 ? 593  LEU B CG    1 
ATOM   13184 C  CD1   . LEU B 1  595  ? 32.908  16.665  74.874  1.00 24.94 ? 593  LEU B CD1   1 
ATOM   13185 C  CD2   . LEU B 1  595  ? 31.185  15.321  73.624  1.00 25.18 ? 593  LEU B CD2   1 
ATOM   13186 N  N     . ASN B 1  596  ? 27.613  16.696  76.594  1.00 18.58 ? 594  ASN B N     1 
ATOM   13187 C  CA    . ASN B 1  596  ? 26.788  16.996  77.761  1.00 20.96 ? 594  ASN B CA    1 
ATOM   13188 C  C     . ASN B 1  596  ? 27.628  17.738  78.798  1.00 17.69 ? 594  ASN B C     1 
ATOM   13189 O  O     . ASN B 1  596  ? 28.651  17.198  79.236  1.00 17.83 ? 594  ASN B O     1 
ATOM   13190 C  CB    . ASN B 1  596  ? 26.260  15.677  78.331  1.00 19.32 ? 594  ASN B CB    1 
ATOM   13191 C  CG    . ASN B 1  596  ? 25.219  15.869  79.391  1.00 20.62 ? 594  ASN B CG    1 
ATOM   13192 O  OD1   . ASN B 1  596  ? 25.236  16.854  80.138  1.00 19.55 ? 594  ASN B OD1   1 
ATOM   13193 N  ND2   . ASN B 1  596  ? 24.292  14.915  79.478  1.00 19.83 ? 594  ASN B ND2   1 
ATOM   13194 N  N     . PRO B 1  597  ? 27.260  18.961  79.205  1.00 17.47 ? 595  PRO B N     1 
ATOM   13195 C  CA    . PRO B 1  597  ? 28.080  19.670  80.207  1.00 19.17 ? 595  PRO B CA    1 
ATOM   13196 C  C     . PRO B 1  597  ? 28.163  18.952  81.538  1.00 18.39 ? 595  PRO B C     1 
ATOM   13197 O  O     . PRO B 1  597  ? 29.145  19.145  82.261  1.00 19.21 ? 595  PRO B O     1 
ATOM   13198 C  CB    . PRO B 1  597  ? 27.389  21.033  80.346  1.00 18.21 ? 595  PRO B CB    1 
ATOM   13199 C  CG    . PRO B 1  597  ? 25.943  20.787  79.841  1.00 16.37 ? 595  PRO B CG    1 
ATOM   13200 C  CD    . PRO B 1  597  ? 26.132  19.783  78.728  1.00 17.44 ? 595  PRO B CD    1 
ATOM   13201 N  N     . GLY B 1  598  ? 27.187  18.117  81.880  1.00 19.70 ? 596  GLY B N     1 
ATOM   13202 C  CA    . GLY B 1  598  ? 27.255  17.360  83.112  1.00 18.16 ? 596  GLY B CA    1 
ATOM   13203 C  C     . GLY B 1  598  ? 28.013  16.055  83.016  1.00 21.08 ? 596  GLY B C     1 
ATOM   13204 O  O     . GLY B 1  598  ? 28.230  15.398  84.038  1.00 22.30 ? 596  GLY B O     1 
ATOM   13205 N  N     . ASP B 1  599  ? 28.452  15.673  81.818  1.00 20.06 ? 597  ASP B N     1 
ATOM   13206 C  CA    . ASP B 1  599  ? 29.167  14.421  81.595  1.00 21.49 ? 597  ASP B CA    1 
ATOM   13207 C  C     . ASP B 1  599  ? 29.707  14.442  80.174  1.00 21.31 ? 597  ASP B C     1 
ATOM   13208 O  O     . ASP B 1  599  ? 28.990  14.127  79.222  1.00 19.98 ? 597  ASP B O     1 
ATOM   13209 C  CB    . ASP B 1  599  ? 28.260  13.209  81.822  1.00 21.07 ? 597  ASP B CB    1 
ATOM   13210 C  CG    . ASP B 1  599  ? 29.014  11.901  81.817  1.00 26.25 ? 597  ASP B CG    1 
ATOM   13211 O  OD1   . ASP B 1  599  ? 30.163  11.863  81.307  1.00 22.77 ? 597  ASP B OD1   1 
ATOM   13212 O  OD2   . ASP B 1  599  ? 28.451  10.906  82.328  1.00 25.71 ? 597  ASP B OD2   1 
ATOM   13213 N  N     . HIS B 1  600  ? 30.975  14.816  80.022  1.00 22.48 ? 598  HIS B N     1 
ATOM   13214 C  CA    . HIS B 1  600  ? 31.541  14.958  78.688  1.00 21.57 ? 598  HIS B CA    1 
ATOM   13215 C  C     . HIS B 1  600  ? 31.652  13.636  77.943  1.00 22.48 ? 598  HIS B C     1 
ATOM   13216 O  O     . HIS B 1  600  ? 31.923  13.651  76.742  1.00 24.52 ? 598  HIS B O     1 
ATOM   13217 C  CB    . HIS B 1  600  ? 32.903  15.651  78.770  1.00 21.56 ? 598  HIS B CB    1 
ATOM   13218 C  CG    . HIS B 1  600  ? 32.799  17.116  79.062  1.00 20.82 ? 598  HIS B CG    1 
ATOM   13219 N  ND1   . HIS B 1  600  ? 33.901  17.932  79.198  1.00 24.07 ? 598  HIS B ND1   1 
ATOM   13220 C  CD2   . HIS B 1  600  ? 31.718  17.904  79.277  1.00 21.62 ? 598  HIS B CD2   1 
ATOM   13221 C  CE1   . HIS B 1  600  ? 33.504  19.161  79.475  1.00 26.34 ? 598  HIS B CE1   1 
ATOM   13222 N  NE2   . HIS B 1  600  ? 32.182  19.172  79.530  1.00 24.32 ? 598  HIS B NE2   1 
ATOM   13223 N  N     . ARG B 1  601  ? 31.418  12.504  78.610  1.00 22.23 ? 599  ARG B N     1 
ATOM   13224 C  CA    . ARG B 1  601  ? 31.387  11.231  77.909  1.00 22.29 ? 599  ARG B CA    1 
ATOM   13225 C  C     . ARG B 1  601  ? 30.107  11.072  77.108  1.00 22.98 ? 599  ARG B C     1 
ATOM   13226 O  O     . ARG B 1  601  ? 30.031  10.193  76.244  1.00 23.76 ? 599  ARG B O     1 
ATOM   13227 C  CB    . ARG B 1  601  ? 31.519  10.080  78.904  1.00 25.84 ? 599  ARG B CB    1 
ATOM   13228 C  CG    . ARG B 1  601  ? 32.760  10.166  79.771  1.00 26.26 ? 599  ARG B CG    1 
ATOM   13229 C  CD    . ARG B 1  601  ? 32.710  9.155   80.903  1.00 30.05 ? 599  ARG B CD    1 
ATOM   13230 N  NE    . ARG B 1  601  ? 31.596  9.409   81.805  1.00 26.67 ? 599  ARG B NE    1 
ATOM   13231 C  CZ    . ARG B 1  601  ? 31.266  8.626   82.820  1.00 33.51 ? 599  ARG B CZ    1 
ATOM   13232 N  NH1   . ARG B 1  601  ? 31.966  7.537   83.108  1.00 32.78 ? 599  ARG B NH1   1 
ATOM   13233 N  NH2   . ARG B 1  601  ? 30.212  8.940   83.565  1.00 30.15 ? 599  ARG B NH2   1 
ATOM   13234 N  N     . ASP B 1  602  ? 29.101  11.897  77.393  1.00 21.56 ? 600  ASP B N     1 
ATOM   13235 C  CA    . ASP B 1  602  ? 27.797  11.817  76.749  1.00 20.27 ? 600  ASP B CA    1 
ATOM   13236 C  C     . ASP B 1  602  ? 27.805  12.763  75.558  1.00 22.07 ? 600  ASP B C     1 
ATOM   13237 O  O     . ASP B 1  602  ? 27.664  13.982  75.711  1.00 21.89 ? 600  ASP B O     1 
ATOM   13238 C  CB    . ASP B 1  602  ? 26.704  12.166  77.748  1.00 21.55 ? 600  ASP B CB    1 
ATOM   13239 C  CG    . ASP B 1  602  ? 25.325  12.038  77.169  1.00 24.48 ? 600  ASP B CG    1 
ATOM   13240 O  OD1   . ASP B 1  602  ? 25.170  11.314  76.164  1.00 25.60 ? 600  ASP B OD1   1 
ATOM   13241 O  OD2   . ASP B 1  602  ? 24.402  12.671  77.731  1.00 23.94 ? 600  ASP B OD2   1 
ATOM   13242 N  N     . VAL B 1  603  ? 27.983  12.198  74.368  1.00 23.60 ? 601  VAL B N     1 
ATOM   13243 C  CA    . VAL B 1  603  ? 27.977  12.977  73.136  1.00 21.27 ? 601  VAL B CA    1 
ATOM   13244 C  C     . VAL B 1  603  ? 26.527  13.219  72.737  1.00 23.69 ? 601  VAL B C     1 
ATOM   13245 O  O     . VAL B 1  603  ? 25.779  12.273  72.470  1.00 22.66 ? 601  VAL B O     1 
ATOM   13246 C  CB    . VAL B 1  603  ? 28.751  12.255  72.025  1.00 23.00 ? 601  VAL B CB    1 
ATOM   13247 C  CG1   . VAL B 1  603  ? 28.769  13.092  70.753  1.00 22.74 ? 601  VAL B CG1   1 
ATOM   13248 C  CG2   . VAL B 1  603  ? 30.186  11.947  72.491  1.00 23.10 ? 601  VAL B CG2   1 
ATOM   13249 N  N     . VAL B 1  604  ? 26.118  14.486  72.733  1.00 19.29 ? 602  VAL B N     1 
ATOM   13250 C  CA    . VAL B 1  604  ? 24.724  14.805  72.445  1.00 20.65 ? 602  VAL B CA    1 
ATOM   13251 C  C     . VAL B 1  604  ? 24.488  14.877  70.943  1.00 19.79 ? 602  VAL B C     1 
ATOM   13252 O  O     . VAL B 1  604  ? 23.435  14.451  70.451  1.00 20.16 ? 602  VAL B O     1 
ATOM   13253 C  CB    . VAL B 1  604  ? 24.319  16.111  73.149  1.00 19.31 ? 602  VAL B CB    1 
ATOM   13254 C  CG1   . VAL B 1  604  ? 22.835  16.387  72.947  1.00 16.73 ? 602  VAL B CG1   1 
ATOM   13255 C  CG2   . VAL B 1  604  ? 24.645  16.019  74.641  1.00 20.32 ? 602  VAL B CG2   1 
ATOM   13256 N  N     . GLY B 1  605  ? 25.447  15.412  70.198  1.00 18.96 ? 603  GLY B N     1 
ATOM   13257 C  CA    . GLY B 1  605  ? 25.252  15.598  68.772  1.00 18.32 ? 603  GLY B CA    1 
ATOM   13258 C  C     . GLY B 1  605  ? 26.475  16.218  68.138  1.00 20.84 ? 603  GLY B C     1 
ATOM   13259 O  O     . GLY B 1  605  ? 27.569  16.167  68.701  1.00 20.59 ? 603  GLY B O     1 
ATOM   13260 N  N     . SER B 1  606  ? 26.287  16.803  66.954  1.00 18.83 ? 604  SER B N     1 
ATOM   13261 C  CA    . SER B 1  606  ? 27.403  17.395  66.229  1.00 19.09 ? 604  SER B CA    1 
ATOM   13262 C  C     . SER B 1  606  ? 26.959  18.700  65.602  1.00 20.08 ? 604  SER B C     1 
ATOM   13263 O  O     . SER B 1  606  ? 25.815  18.828  65.151  1.00 21.80 ? 604  SER B O     1 
ATOM   13264 C  CB    . SER B 1  606  ? 27.953  16.457  65.145  1.00 24.92 ? 604  SER B CB    1 
ATOM   13265 O  OG    . SER B 1  606  ? 27.054  16.365  64.064  1.00 35.90 ? 604  SER B OG    1 
ATOM   13266 N  N     . VAL B 1  607  ? 27.859  19.677  65.595  1.00 18.39 ? 605  VAL B N     1 
ATOM   13267 C  CA    . VAL B 1  607  ? 27.567  20.988  65.035  1.00 16.26 ? 605  VAL B CA    1 
ATOM   13268 C  C     . VAL B 1  607  ? 28.579  21.289  63.943  1.00 20.65 ? 605  VAL B C     1 
ATOM   13269 O  O     . VAL B 1  607  ? 29.786  21.088  64.128  1.00 19.16 ? 605  VAL B O     1 
ATOM   13270 C  CB    . VAL B 1  607  ? 27.557  22.097  66.109  1.00 18.52 ? 605  VAL B CB    1 
ATOM   13271 C  CG1   . VAL B 1  607  ? 28.865  22.139  66.892  1.00 20.54 ? 605  VAL B CG1   1 
ATOM   13272 C  CG2   . VAL B 1  607  ? 27.270  23.442  65.469  1.00 18.65 ? 605  VAL B CG2   1 
ATOM   13273 N  N     . THR B 1  608  ? 28.079  21.760  62.809  1.00 18.62 ? 606  THR B N     1 
ATOM   13274 C  CA    . THR B 1  608  ? 28.899  22.262  61.720  1.00 18.47 ? 606  THR B CA    1 
ATOM   13275 C  C     . THR B 1  608  ? 28.770  23.778  61.737  1.00 19.21 ? 606  THR B C     1 
ATOM   13276 O  O     . THR B 1  608  ? 27.666  24.314  61.615  1.00 19.31 ? 606  THR B O     1 
ATOM   13277 C  CB    . THR B 1  608  ? 28.445  21.669  60.388  1.00 19.71 ? 606  THR B CB    1 
ATOM   13278 O  OG1   . THR B 1  608  ? 28.678  20.257  60.406  1.00 19.45 ? 606  THR B OG1   1 
ATOM   13279 C  CG2   . THR B 1  608  ? 29.199  22.289  59.225  1.00 20.63 ? 606  THR B CG2   1 
ATOM   13280 N  N     . GLU B 1  609  ? 29.882  24.465  61.942  1.00 18.68 ? 607  GLU B N     1 
ATOM   13281 C  CA    . GLU B 1  609  ? 29.805  25.895  62.175  1.00 21.46 ? 607  GLU B CA    1 
ATOM   13282 C  C     . GLU B 1  609  ? 30.024  26.661  60.874  1.00 19.17 ? 607  GLU B C     1 
ATOM   13283 O  O     . GLU B 1  609  ? 30.584  26.146  59.901  1.00 20.32 ? 607  GLU B O     1 
ATOM   13284 C  CB    . GLU B 1  609  ? 30.784  26.307  63.279  1.00 19.48 ? 607  GLU B CB    1 
ATOM   13285 C  CG    . GLU B 1  609  ? 30.284  25.763  64.624  1.00 22.78 ? 607  GLU B CG    1 
ATOM   13286 C  CD    . GLU B 1  609  ? 31.186  26.050  65.805  1.00 26.48 ? 607  GLU B CD    1 
ATOM   13287 O  OE1   . GLU B 1  609  ? 32.424  26.072  65.637  1.00 27.36 ? 607  GLU B OE1   1 
ATOM   13288 O  OE2   . GLU B 1  609  ? 30.642  26.248  66.911  1.00 25.39 ? 607  GLU B OE2   1 
ATOM   13289 N  N     . THR B 1  610  ? 29.522  27.891  60.865  1.00 19.17 ? 608  THR B N     1 
ATOM   13290 C  CA    . THR B 1  610  ? 29.366  28.689  59.654  1.00 17.66 ? 608  THR B CA    1 
ATOM   13291 C  C     . THR B 1  610  ? 30.643  29.464  59.367  1.00 19.48 ? 608  THR B C     1 
ATOM   13292 O  O     . THR B 1  610  ? 31.182  30.118  60.263  1.00 20.55 ? 608  THR B O     1 
ATOM   13293 C  CB    . THR B 1  610  ? 28.214  29.683  59.814  1.00 18.94 ? 608  THR B CB    1 
ATOM   13294 O  OG1   . THR B 1  610  ? 27.056  29.009  60.311  1.00 16.79 ? 608  THR B OG1   1 
ATOM   13295 C  CG2   . THR B 1  610  ? 27.886  30.328  58.482  1.00 19.28 ? 608  THR B CG2   1 
ATOM   13296 N  N     . SER B 1  611  ? 31.101  29.429  58.120  1.00 19.32 ? 609  SER B N     1 
ATOM   13297 C  CA    . SER B 1  611  ? 32.181  30.329  57.730  1.00 22.98 ? 609  SER B CA    1 
ATOM   13298 C  C     . SER B 1  611  ? 31.681  31.768  57.690  1.00 23.99 ? 609  SER B C     1 
ATOM   13299 O  O     . SER B 1  611  ? 30.495  32.038  57.468  1.00 20.04 ? 609  SER B O     1 
ATOM   13300 C  CB    . SER B 1  611  ? 32.746  29.942  56.361  1.00 22.78 ? 609  SER B CB    1 
ATOM   13301 O  OG    . SER B 1  611  ? 31.815  30.236  55.337  1.00 21.32 ? 609  SER B OG    1 
ATOM   13302 N  N     . GLU B 1  612  ? 32.599  32.712  57.902  1.00 21.07 ? 610  GLU B N     1 
ATOM   13303 C  CA    . GLU B 1  612  ? 32.197  34.110  57.790  1.00 23.14 ? 610  GLU B CA    1 
ATOM   13304 C  C     . GLU B 1  612  ? 31.698  34.430  56.384  1.00 23.32 ? 610  GLU B C     1 
ATOM   13305 O  O     . GLU B 1  612  ? 30.734  35.192  56.228  1.00 21.11 ? 610  GLU B O     1 
ATOM   13306 C  CB    . GLU B 1  612  ? 33.357  35.017  58.206  1.00 28.62 ? 610  GLU B CB    1 
ATOM   13307 C  CG    . GLU B 1  612  ? 33.768  34.766  59.655  1.00 29.12 ? 610  GLU B CG    1 
ATOM   13308 C  CD    . GLU B 1  612  ? 34.896  35.668  60.141  1.00 34.76 ? 610  GLU B CD    1 
ATOM   13309 O  OE1   . GLU B 1  612  ? 35.189  36.685  59.477  1.00 41.92 ? 610  GLU B OE1   1 
ATOM   13310 O  OE2   . GLU B 1  612  ? 35.485  35.351  61.197  1.00 34.29 ? 610  GLU B OE2   1 
ATOM   13311 N  N     . GLU B 1  613  ? 32.294  33.815  55.357  1.00 24.68 ? 611  GLU B N     1 
ATOM   13312 C  CA    . GLU B 1  613  ? 31.803  34.012  53.994  1.00 22.41 ? 611  GLU B CA    1 
ATOM   13313 C  C     . GLU B 1  613  ? 30.363  33.523  53.851  1.00 22.94 ? 611  GLU B C     1 
ATOM   13314 O  O     . GLU B 1  613  ? 29.544  34.174  53.198  1.00 23.99 ? 611  GLU B O     1 
ATOM   13315 C  CB    . GLU B 1  613  ? 32.718  33.306  52.986  1.00 26.16 ? 611  GLU B CB    1 
ATOM   13316 N  N     . ASP B 1  614  ? 30.033  32.377  54.454  1.00 21.81 ? 612  ASP B N     1 
ATOM   13317 C  CA    . ASP B 1  614  ? 28.665  31.881  54.335  1.00 20.79 ? 612  ASP B CA    1 
ATOM   13318 C  C     . ASP B 1  614  ? 27.696  32.699  55.176  1.00 21.43 ? 612  ASP B C     1 
ATOM   13319 O  O     . ASP B 1  614  ? 26.513  32.807  54.827  1.00 20.54 ? 612  ASP B O     1 
ATOM   13320 C  CB    . ASP B 1  614  ? 28.596  30.408  54.724  1.00 21.88 ? 612  ASP B CB    1 
ATOM   13321 C  CG    . ASP B 1  614  ? 29.048  29.489  53.595  1.00 23.51 ? 612  ASP B CG    1 
ATOM   13322 O  OD1   . ASP B 1  614  ? 28.926  29.888  52.418  1.00 24.48 ? 612  ASP B OD1   1 
ATOM   13323 O  OD2   . ASP B 1  614  ? 29.519  28.370  53.883  1.00 23.53 ? 612  ASP B OD2   1 
ATOM   13324 N  N     . ALA B 1  615  ? 28.166  33.271  56.287  1.00 19.77 ? 613  ALA B N     1 
ATOM   13325 C  CA    . ALA B 1  615  ? 27.322  34.193  57.042  1.00 19.32 ? 613  ALA B CA    1 
ATOM   13326 C  C     . ALA B 1  615  ? 26.921  35.375  56.172  1.00 20.70 ? 613  ALA B C     1 
ATOM   13327 O  O     . ALA B 1  615  ? 25.744  35.744  56.108  1.00 19.18 ? 613  ALA B O     1 
ATOM   13328 C  CB    . ALA B 1  615  ? 28.052  34.667  58.301  1.00 20.00 ? 613  ALA B CB    1 
ATOM   13329 N  N     . ARG B 1  616  ? 27.889  35.964  55.465  1.00 21.45 ? 614  ARG B N     1 
ATOM   13330 C  CA    . ARG B 1  616  ? 27.558  37.055  54.556  1.00 21.65 ? 614  ARG B CA    1 
ATOM   13331 C  C     . ARG B 1  616  ? 26.650  36.581  53.428  1.00 21.89 ? 614  ARG B C     1 
ATOM   13332 O  O     . ARG B 1  616  ? 25.718  37.294  53.032  1.00 21.26 ? 614  ARG B O     1 
ATOM   13333 C  CB    . ARG B 1  616  ? 28.841  37.682  54.015  1.00 23.52 ? 614  ARG B CB    1 
ATOM   13334 C  CG    . ARG B 1  616  ? 29.495  38.605  55.040  1.00 25.33 ? 614  ARG B CG    1 
ATOM   13335 C  CD    . ARG B 1  616  ? 30.674  39.346  54.446  1.00 31.67 ? 614  ARG B CD    1 
ATOM   13336 N  NE    . ARG B 1  616  ? 31.797  38.444  54.240  1.00 31.53 ? 614  ARG B NE    1 
ATOM   13337 C  CZ    . ARG B 1  616  ? 32.639  38.076  55.194  1.00 32.04 ? 614  ARG B CZ    1 
ATOM   13338 N  NH1   . ARG B 1  616  ? 32.513  38.519  56.436  1.00 30.60 ? 614  ARG B NH1   1 
ATOM   13339 N  NH2   . ARG B 1  616  ? 33.627  37.239  54.898  1.00 30.94 ? 614  ARG B NH2   1 
ATOM   13340 N  N     . ARG B 1  617  ? 26.895  35.379  52.900  1.00 20.73 ? 615  ARG B N     1 
ATOM   13341 C  CA    . ARG B 1  617  ? 26.027  34.863  51.846  1.00 22.28 ? 615  ARG B CA    1 
ATOM   13342 C  C     . ARG B 1  617  ? 24.597  34.719  52.340  1.00 20.45 ? 615  ARG B C     1 
ATOM   13343 O  O     . ARG B 1  617  ? 23.647  35.030  51.613  1.00 19.17 ? 615  ARG B O     1 
ATOM   13344 C  CB    . ARG B 1  617  ? 26.546  33.519  51.332  1.00 22.69 ? 615  ARG B CB    1 
ATOM   13345 C  CG    . ARG B 1  617  ? 25.704  32.940  50.201  1.00 26.58 ? 615  ARG B CG    1 
ATOM   13346 C  CD    . ARG B 1  617  ? 26.501  31.935  49.359  1.00 31.21 ? 615  ARG B CD    1 
ATOM   13347 N  NE    . ARG B 1  617  ? 26.721  30.676  50.059  1.00 33.39 ? 615  ARG B NE    1 
ATOM   13348 C  CZ    . ARG B 1  617  ? 25.871  29.656  50.046  1.00 37.58 ? 615  ARG B CZ    1 
ATOM   13349 N  NH1   . ARG B 1  617  ? 24.727  29.716  49.380  1.00 36.67 ? 615  ARG B NH1   1 
ATOM   13350 N  NH2   . ARG B 1  617  ? 26.175  28.548  50.718  1.00 38.52 ? 615  ARG B NH2   1 
ATOM   13351 N  N     . ALA B 1  618  ? 24.421  34.255  53.576  1.00 20.65 ? 616  ALA B N     1 
ATOM   13352 C  CA    . ALA B 1  618  ? 23.069  34.124  54.121  1.00 19.92 ? 616  ALA B CA    1 
ATOM   13353 C  C     . ALA B 1  618  ? 22.356  35.471  54.168  1.00 19.61 ? 616  ALA B C     1 
ATOM   13354 O  O     . ALA B 1  618  ? 21.148  35.567  53.886  1.00 18.34 ? 616  ALA B O     1 
ATOM   13355 C  CB    . ALA B 1  618  ? 23.135  33.510  55.520  1.00 18.02 ? 616  ALA B CB    1 
ATOM   13356 N  N     . VAL B 1  619  ? 23.076  36.523  54.555  1.00 20.01 ? 617  VAL B N     1 
ATOM   13357 C  CA    . VAL B 1  619  ? 22.428  37.821  54.670  1.00 18.97 ? 617  VAL B CA    1 
ATOM   13358 C  C     . VAL B 1  619  ? 21.988  38.299  53.297  1.00 19.45 ? 617  VAL B C     1 
ATOM   13359 O  O     . VAL B 1  619  ? 20.906  38.873  53.147  1.00 21.07 ? 617  VAL B O     1 
ATOM   13360 C  CB    . VAL B 1  619  ? 23.351  38.834  55.376  1.00 19.13 ? 617  VAL B CB    1 
ATOM   13361 C  CG1   . VAL B 1  619  ? 22.699  40.207  55.425  1.00 20.18 ? 617  VAL B CG1   1 
ATOM   13362 C  CG2   . VAL B 1  619  ? 23.647  38.365  56.798  1.00 18.96 ? 617  VAL B CG2   1 
ATOM   13363 N  N     . ARG B 1  620  ? 22.801  38.038  52.266  1.00 21.55 ? 618  ARG B N     1 
ATOM   13364 C  CA    . ARG B 1  620  ? 22.392  38.391  50.909  1.00 21.63 ? 618  ARG B CA    1 
ATOM   13365 C  C     . ARG B 1  620  ? 21.175  37.586  50.474  1.00 21.00 ? 618  ARG B C     1 
ATOM   13366 O  O     . ARG B 1  620  ? 20.266  38.126  49.830  1.00 21.27 ? 618  ARG B O     1 
ATOM   13367 C  CB    . ARG B 1  620  ? 23.556  38.189  49.933  1.00 23.64 ? 618  ARG B CB    1 
ATOM   13368 C  CG    . ARG B 1  620  ? 24.741  39.105  50.225  1.00 27.62 ? 618  ARG B CG    1 
ATOM   13369 C  CD    . ARG B 1  620  ? 25.771  39.117  49.091  1.00 35.23 ? 618  ARG B CD    1 
ATOM   13370 N  NE    . ARG B 1  620  ? 26.248  37.778  48.771  1.00 37.72 ? 618  ARG B NE    1 
ATOM   13371 C  CZ    . ARG B 1  620  ? 27.368  37.243  49.238  1.00 34.20 ? 618  ARG B CZ    1 
ATOM   13372 N  NH1   . ARG B 1  620  ? 28.184  37.920  50.030  1.00 35.72 ? 618  ARG B NH1   1 
ATOM   13373 N  NH2   . ARG B 1  620  ? 27.681  35.996  48.894  1.00 38.76 ? 618  ARG B NH2   1 
ATOM   13374 N  N     . LEU B 1  621  ? 21.140  36.293  50.804  1.00 18.99 ? 619  LEU B N     1 
ATOM   13375 C  CA    . LEU B 1  621  ? 19.966  35.485  50.482  1.00 19.65 ? 619  LEU B CA    1 
ATOM   13376 C  C     . LEU B 1  621  ? 18.735  35.989  51.225  1.00 21.07 ? 619  LEU B C     1 
ATOM   13377 O  O     . LEU B 1  621  ? 17.622  36.003  50.675  1.00 20.57 ? 619  LEU B O     1 
ATOM   13378 C  CB    . LEU B 1  621  ? 20.228  34.016  50.819  1.00 20.88 ? 619  LEU B CB    1 
ATOM   13379 C  CG    . LEU B 1  621  ? 21.262  33.290  49.947  1.00 23.21 ? 619  LEU B CG    1 
ATOM   13380 C  CD1   . LEU B 1  621  ? 21.722  31.998  50.613  1.00 22.43 ? 619  LEU B CD1   1 
ATOM   13381 C  CD2   . LEU B 1  621  ? 20.701  32.990  48.560  1.00 25.23 ? 619  LEU B CD2   1 
ATOM   13382 N  N     . ALA B 1  622  ? 18.912  36.409  52.477  1.00 18.97 ? 620  ALA B N     1 
ATOM   13383 C  CA    . ALA B 1  622  ? 17.793  36.978  53.217  1.00 20.22 ? 620  ALA B CA    1 
ATOM   13384 C  C     . ALA B 1  622  ? 17.312  38.265  52.558  1.00 19.28 ? 620  ALA B C     1 
ATOM   13385 O  O     . ALA B 1  622  ? 16.103  38.488  52.425  1.00 18.45 ? 620  ALA B O     1 
ATOM   13386 C  CB    . ALA B 1  622  ? 18.187  37.227  54.676  1.00 17.68 ? 620  ALA B CB    1 
ATOM   13387 N  N     . ALA B 1  623  ? 18.247  39.111  52.119  1.00 18.91 ? 621  ALA B N     1 
ATOM   13388 C  CA    . ALA B 1  623  ? 17.868  40.355  51.456  1.00 19.60 ? 621  ALA B CA    1 
ATOM   13389 C  C     . ALA B 1  623  ? 17.100  40.075  50.171  1.00 20.80 ? 621  ALA B C     1 
ATOM   13390 O  O     . ALA B 1  623  ? 16.066  40.707  49.905  1.00 19.83 ? 621  ALA B O     1 
ATOM   13391 C  CB    . ALA B 1  623  ? 19.119  41.194  51.177  1.00 20.07 ? 621  ALA B CB    1 
ATOM   13392 N  N     . ASP B 1  624  ? 17.555  39.082  49.399  1.00 22.03 ? 622  ASP B N     1 
ATOM   13393 C  CA    . ASP B 1  624  ? 16.877  38.720  48.156  1.00 22.53 ? 622  ASP B CA    1 
ATOM   13394 C  C     . ASP B 1  624  ? 15.424  38.344  48.401  1.00 23.01 ? 622  ASP B C     1 
ATOM   13395 O  O     . ASP B 1  624  ? 14.539  38.714  47.621  1.00 29.63 ? 622  ASP B O     1 
ATOM   13396 C  CB    . ASP B 1  624  ? 17.602  37.553  47.480  1.00 26.45 ? 622  ASP B CB    1 
ATOM   13397 C  CG    . ASP B 1  624  ? 18.960  37.929  46.949  1.00 32.98 ? 622  ASP B CG    1 
ATOM   13398 O  OD1   . ASP B 1  624  ? 19.273  39.141  46.869  1.00 36.48 ? 622  ASP B OD1   1 
ATOM   13399 O  OD2   . ASP B 1  624  ? 19.720  36.994  46.605  1.00 34.15 ? 622  ASP B OD2   1 
ATOM   13400 N  N     . ALA B 1  625  ? 15.159  37.601  49.468  1.00 22.52 ? 623  ALA B N     1 
ATOM   13401 C  CA    . ALA B 1  625  ? 13.821  37.091  49.723  1.00 26.20 ? 623  ALA B CA    1 
ATOM   13402 C  C     . ALA B 1  625  ? 13.003  37.991  50.629  1.00 23.36 ? 623  ALA B C     1 
ATOM   13403 O  O     . ALA B 1  625  ? 11.853  37.655  50.941  1.00 23.39 ? 623  ALA B O     1 
ATOM   13404 C  CB    . ALA B 1  625  ? 13.896  35.696  50.333  1.00 29.19 ? 623  ALA B CB    1 
ATOM   13405 N  N     . ALA B 1  626  ? 13.560  39.114  51.075  1.00 21.25 ? 624  ALA B N     1 
ATOM   13406 C  CA    . ALA B 1  626  ? 12.820  39.970  51.999  1.00 20.53 ? 624  ALA B CA    1 
ATOM   13407 C  C     . ALA B 1  626  ? 11.476  40.426  51.439  1.00 21.05 ? 624  ALA B C     1 
ATOM   13408 O  O     . ALA B 1  626  ? 10.470  40.327  52.163  1.00 22.25 ? 624  ALA B O     1 
ATOM   13409 C  CB    . ALA B 1  626  ? 13.703  41.150  52.421  1.00 18.79 ? 624  ALA B CB    1 
ATOM   13410 N  N     . PRO B 1  627  ? 11.359  40.879  50.183  1.00 22.70 ? 625  PRO B N     1 
ATOM   13411 C  CA    . PRO B 1  627  ? 10.030  41.299  49.704  1.00 22.73 ? 625  PRO B CA    1 
ATOM   13412 C  C     . PRO B 1  627  ? 9.007   40.176  49.691  1.00 24.48 ? 625  PRO B C     1 
ATOM   13413 O  O     . PRO B 1  627  ? 7.829   40.418  49.996  1.00 21.12 ? 625  PRO B O     1 
ATOM   13414 C  CB    . PRO B 1  627  ? 10.316  41.810  48.281  1.00 24.23 ? 625  PRO B CB    1 
ATOM   13415 C  CG    . PRO B 1  627  ? 11.772  42.118  48.264  1.00 26.72 ? 625  PRO B CG    1 
ATOM   13416 C  CD    . PRO B 1  627  ? 12.400  41.108  49.164  1.00 23.60 ? 625  PRO B CD    1 
ATOM   13417 N  N     . ASP B 1  628  ? 9.416   38.954  49.325  1.00 21.64 ? 626  ASP B N     1 
ATOM   13418 C  CA    . ASP B 1  628  ? 8.470   37.843  49.300  1.00 24.82 ? 626  ASP B CA    1 
ATOM   13419 C  C     . ASP B 1  628  ? 7.911   37.559  50.691  1.00 24.10 ? 626  ASP B C     1 
ATOM   13420 O  O     . ASP B 1  628  ? 6.718   37.267  50.845  1.00 23.13 ? 626  ASP B O     1 
ATOM   13421 C  CB    . ASP B 1  628  ? 9.135   36.589  48.737  1.00 24.11 ? 626  ASP B CB    1 
ATOM   13422 C  CG    . ASP B 1  628  ? 9.452   36.696  47.255  1.00 31.36 ? 626  ASP B CG    1 
ATOM   13423 O  OD1   . ASP B 1  628  ? 9.110   37.717  46.621  1.00 32.12 ? 626  ASP B OD1   1 
ATOM   13424 O  OD2   . ASP B 1  628  ? 10.043  35.739  46.723  1.00 36.09 ? 626  ASP B OD2   1 
ATOM   13425 N  N     . TRP B 1  629  ? 8.755   37.627  51.720  1.00 19.10 ? 627  TRP B N     1 
ATOM   13426 C  CA    . TRP B 1  629  ? 8.251   37.312  53.047  1.00 18.17 ? 627  TRP B CA    1 
ATOM   13427 C  C     . TRP B 1  629  ? 7.404   38.451  53.598  1.00 18.65 ? 627  TRP B C     1 
ATOM   13428 O  O     . TRP B 1  629  ? 6.383   38.211  54.253  1.00 18.54 ? 627  TRP B O     1 
ATOM   13429 C  CB    . TRP B 1  629  ? 9.413   36.981  53.988  1.00 17.68 ? 627  TRP B CB    1 
ATOM   13430 C  CG    . TRP B 1  629  ? 8.974   36.717  55.390  1.00 18.36 ? 627  TRP B CG    1 
ATOM   13431 C  CD1   . TRP B 1  629  ? 9.338   37.419  56.514  1.00 16.17 ? 627  TRP B CD1   1 
ATOM   13432 C  CD2   . TRP B 1  629  ? 8.079   35.689  55.835  1.00 18.48 ? 627  TRP B CD2   1 
ATOM   13433 N  NE1   . TRP B 1  629  ? 8.735   36.881  57.622  1.00 16.54 ? 627  TRP B NE1   1 
ATOM   13434 C  CE2   . TRP B 1  629  ? 7.949   35.826  57.237  1.00 16.51 ? 627  TRP B CE2   1 
ATOM   13435 C  CE3   . TRP B 1  629  ? 7.377   34.662  55.191  1.00 18.61 ? 627  TRP B CE3   1 
ATOM   13436 C  CZ2   . TRP B 1  629  ? 7.146   34.979  58.001  1.00 15.55 ? 627  TRP B CZ2   1 
ATOM   13437 C  CZ3   . TRP B 1  629  ? 6.567   33.833  55.955  1.00 19.13 ? 627  TRP B CZ3   1 
ATOM   13438 C  CH2   . TRP B 1  629  ? 6.459   33.996  57.340  1.00 19.17 ? 627  TRP B CH2   1 
ATOM   13439 N  N     . ALA B 1  630  ? 7.799   39.691  53.327  1.00 18.72 ? 628  ALA B N     1 
ATOM   13440 C  CA    . ALA B 1  630  ? 7.002   40.820  53.782  1.00 19.53 ? 628  ALA B CA    1 
ATOM   13441 C  C     . ALA B 1  630  ? 5.612   40.783  53.170  1.00 21.90 ? 628  ALA B C     1 
ATOM   13442 O  O     . ALA B 1  630  ? 4.651   41.256  53.785  1.00 21.50 ? 628  ALA B O     1 
ATOM   13443 C  CB    . ALA B 1  630  ? 7.703   42.131  53.436  1.00 21.84 ? 628  ALA B CB    1 
ATOM   13444 N  N     . ALA B 1  631  ? 5.489   40.197  51.979  1.00 20.73 ? 629  ALA B N     1 
ATOM   13445 C  CA    . ALA B 1  631  ? 4.218   40.128  51.266  1.00 20.54 ? 629  ALA B CA    1 
ATOM   13446 C  C     . ALA B 1  631  ? 3.282   39.049  51.799  1.00 21.48 ? 629  ALA B C     1 
ATOM   13447 O  O     . ALA B 1  631  ? 2.107   39.024  51.417  1.00 21.14 ? 629  ALA B O     1 
ATOM   13448 C  CB    . ALA B 1  631  ? 4.484   39.902  49.776  1.00 22.60 ? 629  ALA B CB    1 
ATOM   13449 N  N     . VAL B 1  632  ? 3.758   38.161  52.665  1.00 18.07 ? 630  VAL B N     1 
ATOM   13450 C  CA    . VAL B 1  632  ? 2.881   37.203  53.329  1.00 20.53 ? 630  VAL B CA    1 
ATOM   13451 C  C     . VAL B 1  632  ? 2.079   37.997  54.351  1.00 21.13 ? 630  VAL B C     1 
ATOM   13452 O  O     . VAL B 1  632  ? 2.684   38.676  55.196  1.00 19.24 ? 630  VAL B O     1 
ATOM   13453 C  CB    . VAL B 1  632  ? 3.684   36.073  53.989  1.00 21.14 ? 630  VAL B CB    1 
ATOM   13454 C  CG1   . VAL B 1  632  ? 2.753   35.138  54.760  1.00 19.49 ? 630  VAL B CG1   1 
ATOM   13455 C  CG2   . VAL B 1  632  ? 4.491   35.305  52.932  1.00 20.18 ? 630  VAL B CG2   1 
ATOM   13456 N  N     . PRO B 1  633  ? 0.748   37.956  54.314  1.00 17.91 ? 631  PRO B N     1 
ATOM   13457 C  CA    . PRO B 1  633  ? -0.031  38.811  55.200  1.00 16.87 ? 631  PRO B CA    1 
ATOM   13458 C  C     . PRO B 1  633  ? 0.302   38.534  56.651  1.00 20.04 ? 631  PRO B C     1 
ATOM   13459 O  O     . PRO B 1  633  ? 0.578   37.383  57.034  1.00 18.59 ? 631  PRO B O     1 
ATOM   13460 C  CB    . PRO B 1  633  ? -1.481  38.426  54.881  1.00 18.64 ? 631  PRO B CB    1 
ATOM   13461 C  CG    . PRO B 1  633  ? -1.443  37.964  53.468  1.00 21.12 ? 631  PRO B CG    1 
ATOM   13462 C  CD    . PRO B 1  633  ? -0.100  37.266  53.322  1.00 19.38 ? 631  PRO B CD    1 
ATOM   13463 N  N     . PRO B 1  634  ? 0.266   39.562  57.503  1.00 19.97 ? 632  PRO B N     1 
ATOM   13464 C  CA    . PRO B 1  634  ? 0.570   39.361  58.930  1.00 20.07 ? 632  PRO B CA    1 
ATOM   13465 C  C     . PRO B 1  634  ? -0.194  38.222  59.575  1.00 18.15 ? 632  PRO B C     1 
ATOM   13466 O  O     . PRO B 1  634  ? 0.395   37.456  60.347  1.00 17.56 ? 632  PRO B O     1 
ATOM   13467 C  CB    . PRO B 1  634  ? 0.190   40.715  59.552  1.00 20.06 ? 632  PRO B CB    1 
ATOM   13468 C  CG    . PRO B 1  634  ? 0.392   41.695  58.448  1.00 23.27 ? 632  PRO B CG    1 
ATOM   13469 C  CD    . PRO B 1  634  ? 0.002   40.978  57.179  1.00 20.28 ? 632  PRO B CD    1 
ATOM   13470 N  N     . SER B 1  635  ? -1.494  38.087  59.298  1.00 18.67 ? 633  SER B N     1 
ATOM   13471 C  CA    . SER B 1  635  ? -2.246  36.996  59.913  1.00 18.38 ? 633  SER B CA    1 
ATOM   13472 C  C     . SER B 1  635  ? -1.709  35.634  59.491  1.00 17.17 ? 633  SER B C     1 
ATOM   13473 O  O     . SER B 1  635  ? -1.757  34.682  60.279  1.00 18.23 ? 633  SER B O     1 
ATOM   13474 C  CB    . SER B 1  635  ? -3.737  37.099  59.567  1.00 19.83 ? 633  SER B CB    1 
ATOM   13475 O  OG    . SER B 1  635  ? -3.927  37.061  58.164  1.00 29.05 ? 633  SER B OG    1 
ATOM   13476 N  N     . GLU B 1  636  ? -1.201  35.513  58.260  1.00 17.51 ? 634  GLU B N     1 
ATOM   13477 C  CA    . GLU B 1  636  ? -0.638  34.238  57.826  1.00 18.37 ? 634  GLU B CA    1 
ATOM   13478 C  C     . GLU B 1  636  ? 0.749   34.012  58.416  1.00 18.37 ? 634  GLU B C     1 
ATOM   13479 O  O     . GLU B 1  636  ? 1.111   32.877  58.746  1.00 17.52 ? 634  GLU B O     1 
ATOM   13480 C  CB    . GLU B 1  636  ? -0.578  34.175  56.300  1.00 19.04 ? 634  GLU B CB    1 
ATOM   13481 C  CG    . GLU B 1  636  ? 0.086   32.890  55.767  1.00 27.97 ? 634  GLU B CG    1 
ATOM   13482 C  CD    . GLU B 1  636  ? -0.522  31.597  56.342  1.00 32.23 ? 634  GLU B CD    1 
ATOM   13483 O  OE1   . GLU B 1  636  ? -1.772  31.498  56.477  1.00 27.73 ? 634  GLU B OE1   1 
ATOM   13484 O  OE2   . GLU B 1  636  ? 0.263   30.671  56.661  1.00 27.96 ? 634  GLU B OE2   1 
ATOM   13485 N  N     . ARG B 1  637  ? 1.546   35.073  58.543  1.00 16.87 ? 635  ARG B N     1 
ATOM   13486 C  CA    . ARG B 1  637  ? 2.803   34.920  59.264  1.00 15.43 ? 635  ARG B CA    1 
ATOM   13487 C  C     . ARG B 1  637  ? 2.537   34.496  60.701  1.00 15.76 ? 635  ARG B C     1 
ATOM   13488 O  O     . ARG B 1  637  ? 3.216   33.606  61.228  1.00 16.49 ? 635  ARG B O     1 
ATOM   13489 C  CB    . ARG B 1  637  ? 3.615   36.210  59.218  1.00 16.48 ? 635  ARG B CB    1 
ATOM   13490 C  CG    . ARG B 1  637  ? 3.855   36.722  57.805  1.00 16.23 ? 635  ARG B CG    1 
ATOM   13491 C  CD    . ARG B 1  637  ? 4.905   37.827  57.770  1.00 14.74 ? 635  ARG B CD    1 
ATOM   13492 N  NE    . ARG B 1  637  ? 4.532   38.978  58.587  1.00 17.18 ? 635  ARG B NE    1 
ATOM   13493 C  CZ    . ARG B 1  637  ? 4.273   40.186  58.107  1.00 21.80 ? 635  ARG B CZ    1 
ATOM   13494 N  NH1   . ARG B 1  637  ? 4.175   40.407  56.806  1.00 22.70 ? 635  ARG B NH1   1 
ATOM   13495 N  NH2   . ARG B 1  637  ? 4.140   41.205  58.952  1.00 18.55 ? 635  ARG B NH2   1 
ATOM   13496 N  N     . ALA B 1  638  ? 1.530   35.102  61.338  1.00 15.32 ? 636  ALA B N     1 
ATOM   13497 C  CA    . ALA B 1  638  ? 1.167   34.696  62.687  1.00 15.36 ? 636  ALA B CA    1 
ATOM   13498 C  C     . ALA B 1  638  ? 0.674   33.251  62.715  1.00 16.48 ? 636  ALA B C     1 
ATOM   13499 O  O     . ALA B 1  638  ? 0.938   32.524  63.674  1.00 15.32 ? 636  ALA B O     1 
ATOM   13500 C  CB    . ALA B 1  638  ? 0.120   35.664  63.258  1.00 17.14 ? 636  ALA B CB    1 
ATOM   13501 N  N     . ALA B 1  639  ? -0.046  32.812  61.673  1.00 14.33 ? 637  ALA B N     1 
ATOM   13502 C  CA    . ALA B 1  639  ? -0.468  31.412  61.619  1.00 16.20 ? 637  ALA B CA    1 
ATOM   13503 C  C     . ALA B 1  639  ? 0.731   30.464  61.628  1.00 15.17 ? 637  ALA B C     1 
ATOM   13504 O  O     . ALA B 1  639  ? 0.654   29.369  62.201  1.00 14.71 ? 637  ALA B O     1 
ATOM   13505 C  CB    . ALA B 1  639  ? -1.342  31.159  60.382  1.00 16.26 ? 637  ALA B CB    1 
ATOM   13506 N  N     . CYS B 1  640  ? 1.836   30.852  60.974  1.00 14.75 ? 638  CYS B N     1 
ATOM   13507 C  CA    . CYS B 1  640  ? 3.042   30.029  61.016  1.00 15.31 ? 638  CYS B CA    1 
ATOM   13508 C  C     . CYS B 1  640  ? 3.555   29.907  62.438  1.00 12.97 ? 638  CYS B C     1 
ATOM   13509 O  O     . CYS B 1  640  ? 3.964   28.818  62.869  1.00 14.44 ? 638  CYS B O     1 
ATOM   13510 C  CB    . CYS B 1  640  ? 4.148   30.624  60.135  1.00 15.86 ? 638  CYS B CB    1 
ATOM   13511 S  SG    . CYS B 1  640  ? 3.854   30.593  58.372  1.00 17.00 ? 638  CYS B SG    1 
ATOM   13512 N  N     . LEU B 1  641  ? 3.553   31.017  63.175  1.00 13.51 ? 639  LEU B N     1 
ATOM   13513 C  CA    . LEU B 1  641  ? 3.990   30.967  64.567  1.00 13.70 ? 639  LEU B CA    1 
ATOM   13514 C  C     . LEU B 1  641  ? 3.092   30.052  65.381  1.00 13.13 ? 639  LEU B C     1 
ATOM   13515 O  O     . LEU B 1  641  ? 3.584   29.265  66.199  1.00 14.76 ? 639  LEU B O     1 
ATOM   13516 C  CB    . LEU B 1  641  ? 3.997   32.366  65.186  1.00 13.72 ? 639  LEU B CB    1 
ATOM   13517 C  CG    . LEU B 1  641  ? 5.279   33.175  65.010  1.00 14.59 ? 639  LEU B CG    1 
ATOM   13518 C  CD1   . LEU B 1  641  ? 5.640   33.386  63.542  1.00 17.64 ? 639  LEU B CD1   1 
ATOM   13519 C  CD2   . LEU B 1  641  ? 5.146   34.515  65.746  1.00 14.69 ? 639  LEU B CD2   1 
ATOM   13520 N  N     . ASP B 1  642  ? 1.769   30.156  65.192  1.00 14.50 ? 640  ASP B N     1 
ATOM   13521 C  CA    . ASP B 1  642  ? 0.870   29.302  65.961  1.00 12.73 ? 640  ASP B CA    1 
ATOM   13522 C  C     . ASP B 1  642  ? 1.070   27.833  65.612  1.00 15.20 ? 640  ASP B C     1 
ATOM   13523 O  O     . ASP B 1  642  ? 1.018   26.971  66.494  1.00 14.94 ? 640  ASP B O     1 
ATOM   13524 C  CB    . ASP B 1  642  ? -0.595  29.691  65.731  1.00 15.40 ? 640  ASP B CB    1 
ATOM   13525 C  CG    . ASP B 1  642  ? -1.006  30.930  66.488  1.00 16.27 ? 640  ASP B CG    1 
ATOM   13526 O  OD1   . ASP B 1  642  ? -0.360  31.278  67.496  1.00 16.21 ? 640  ASP B OD1   1 
ATOM   13527 O  OD2   . ASP B 1  642  ? -2.022  31.541  66.084  1.00 17.02 ? 640  ASP B OD2   1 
ATOM   13528 N  N     . ARG B 1  643  ? 1.303   27.525  64.329  1.00 15.86 ? 641  ARG B N     1 
ATOM   13529 C  CA    . ARG B 1  643  ? 1.585   26.139  63.960  1.00 16.61 ? 641  ARG B CA    1 
ATOM   13530 C  C     . ARG B 1  643  ? 2.871   25.648  64.612  1.00 15.73 ? 641  ARG B C     1 
ATOM   13531 O  O     . ARG B 1  643  ? 2.937   24.508  65.096  1.00 16.05 ? 641  ARG B O     1 
ATOM   13532 C  CB    . ARG B 1  643  ? 1.662   25.995  62.443  1.00 16.72 ? 641  ARG B CB    1 
ATOM   13533 C  CG    . ARG B 1  643  ? 0.295   25.959  61.773  1.00 18.12 ? 641  ARG B CG    1 
ATOM   13534 C  CD    . ARG B 1  643  ? 0.402   25.555  60.300  1.00 20.28 ? 641  ARG B CD    1 
ATOM   13535 N  NE    . ARG B 1  643  ? 1.061   26.581  59.495  1.00 20.35 ? 641  ARG B NE    1 
ATOM   13536 C  CZ    . ARG B 1  643  ? 0.435   27.593  58.912  1.00 24.12 ? 641  ARG B CZ    1 
ATOM   13537 N  NH1   . ARG B 1  643  ? -0.880  27.732  58.997  1.00 19.65 ? 641  ARG B NH1   1 
ATOM   13538 N  NH2   . ARG B 1  643  ? 1.145   28.486  58.227  1.00 22.09 ? 641  ARG B NH2   1 
ATOM   13539 N  N     . ALA B 1  644  ? 3.902   26.491  64.628  1.00 14.97 ? 642  ALA B N     1 
ATOM   13540 C  CA    . ALA B 1  644  ? 5.148   26.096  65.273  1.00 15.34 ? 642  ALA B CA    1 
ATOM   13541 C  C     . ALA B 1  644  ? 4.925   25.816  66.749  1.00 15.76 ? 642  ALA B C     1 
ATOM   13542 O  O     . ALA B 1  644  ? 5.504   24.872  67.306  1.00 15.80 ? 642  ALA B O     1 
ATOM   13543 C  CB    . ALA B 1  644  ? 6.207   27.183  65.078  1.00 13.73 ? 642  ALA B CB    1 
ATOM   13544 N  N     . ALA B 1  645  ? 4.091   26.631  67.408  1.00 15.12 ? 643  ALA B N     1 
ATOM   13545 C  CA    . ALA B 1  645  ? 3.805   26.391  68.815  1.00 13.06 ? 643  ALA B CA    1 
ATOM   13546 C  C     . ALA B 1  645  ? 3.109   25.051  69.011  1.00 15.02 ? 643  ALA B C     1 
ATOM   13547 O  O     . ALA B 1  645  ? 3.402   24.336  69.977  1.00 15.76 ? 643  ALA B O     1 
ATOM   13548 C  CB    . ALA B 1  645  ? 2.966   27.538  69.400  1.00 14.75 ? 643  ALA B CB    1 
ATOM   13549 N  N     . GLU B 1  646  ? 2.188   24.691  68.106  1.00 15.75 ? 644  GLU B N     1 
ATOM   13550 C  CA    . GLU B 1  646  ? 1.530   23.387  68.193  1.00 18.33 ? 644  GLU B CA    1 
ATOM   13551 C  C     . GLU B 1  646  ? 2.544   22.263  68.079  1.00 17.55 ? 644  GLU B C     1 
ATOM   13552 O  O     . GLU B 1  646  ? 2.463   21.260  68.801  1.00 16.83 ? 644  GLU B O     1 
ATOM   13553 C  CB    . GLU B 1  646  ? 0.474   23.239  67.091  1.00 17.45 ? 644  GLU B CB    1 
ATOM   13554 C  CG    . GLU B 1  646  ? -0.741  24.137  67.258  1.00 20.56 ? 644  GLU B CG    1 
ATOM   13555 C  CD    . GLU B 1  646  ? -1.455  23.914  68.580  1.00 25.90 ? 644  GLU B CD    1 
ATOM   13556 O  OE1   . GLU B 1  646  ? -1.745  22.748  68.918  1.00 30.74 ? 644  GLU B OE1   1 
ATOM   13557 O  OE2   . GLU B 1  646  ? -1.710  24.911  69.292  1.00 27.95 ? 644  GLU B OE2   1 
ATOM   13558 N  N     . LEU B 1  647  ? 3.527   22.431  67.195  1.00 15.05 ? 645  LEU B N     1 
ATOM   13559 C  CA    . LEU B 1  647  ? 4.536   21.395  67.015  1.00 16.69 ? 645  LEU B CA    1 
ATOM   13560 C  C     . LEU B 1  647  ? 5.441   21.293  68.234  1.00 17.27 ? 645  LEU B C     1 
ATOM   13561 O  O     . LEU B 1  647  ? 5.759   20.189  68.687  1.00 17.06 ? 645  LEU B O     1 
ATOM   13562 C  CB    . LEU B 1  647  ? 5.356   21.678  65.758  1.00 16.26 ? 645  LEU B CB    1 
ATOM   13563 C  CG    . LEU B 1  647  ? 4.571   21.589  64.454  1.00 17.39 ? 645  LEU B CG    1 
ATOM   13564 C  CD1   . LEU B 1  647  ? 5.485   21.923  63.287  1.00 17.75 ? 645  LEU B CD1   1 
ATOM   13565 C  CD2   . LEU B 1  647  ? 3.936   20.201  64.266  1.00 19.88 ? 645  LEU B CD2   1 
ATOM   13566 N  N     . MET B 1  648  ? 5.869   22.429  68.783  1.00 14.22 ? 646  MET B N     1 
ATOM   13567 C  CA    . MET B 1  648  ? 6.692   22.371  69.987  1.00 15.90 ? 646  MET B CA    1 
ATOM   13568 C  C     . MET B 1  648  ? 5.925   21.761  71.150  1.00 15.37 ? 646  MET B C     1 
ATOM   13569 O  O     . MET B 1  648  ? 6.503   21.051  71.982  1.00 16.63 ? 646  MET B O     1 
ATOM   13570 C  CB    . MET B 1  648  ? 7.182   23.758  70.364  1.00 15.11 ? 646  MET B CB    1 
ATOM   13571 C  CG    . MET B 1  648  ? 8.205   24.289  69.415  1.00 16.59 ? 646  MET B CG    1 
ATOM   13572 S  SD    . MET B 1  648  ? 9.051   25.678  70.184  1.00 16.46 ? 646  MET B SD    1 
ATOM   13573 C  CE    . MET B 1  648  ? 10.133  26.105  68.841  1.00 17.67 ? 646  MET B CE    1 
ATOM   13574 N  N     . GLN B 1  649  ? 4.628   22.063  71.251  1.00 15.26 ? 647  GLN B N     1 
ATOM   13575 C  CA    . GLN B 1  649  ? 3.828   21.488  72.326  1.00 15.96 ? 647  GLN B CA    1 
ATOM   13576 C  C     . GLN B 1  649  ? 3.748   19.975  72.187  1.00 16.74 ? 647  GLN B C     1 
ATOM   13577 O  O     . GLN B 1  649  ? 3.958   19.234  73.160  1.00 17.01 ? 647  GLN B O     1 
ATOM   13578 C  CB    . GLN B 1  649  ? 2.426   22.100  72.320  1.00 16.32 ? 647  GLN B CB    1 
ATOM   13579 C  CG    . GLN B 1  649  ? 1.567   21.647  73.493  1.00 18.19 ? 647  GLN B CG    1 
ATOM   13580 C  CD    . GLN B 1  649  ? 2.013   22.280  74.792  1.00 17.88 ? 647  GLN B CD    1 
ATOM   13581 O  OE1   . GLN B 1  649  ? 1.737   23.463  75.043  1.00 18.23 ? 647  GLN B OE1   1 
ATOM   13582 N  NE2   . GLN B 1  649  ? 2.747   21.519  75.611  1.00 17.88 ? 647  GLN B NE2   1 
ATOM   13583 N  N     . ALA B 1  650  ? 3.431   19.506  70.978  1.00 16.60 ? 648  ALA B N     1 
ATOM   13584 C  CA    . ALA B 1  650  ? 3.319   18.075  70.718  1.00 18.69 ? 648  ALA B CA    1 
ATOM   13585 C  C     . ALA B 1  650  ? 4.642   17.356  70.933  1.00 19.79 ? 648  ALA B C     1 
ATOM   13586 O  O     . ALA B 1  650  ? 4.653   16.195  71.359  1.00 22.03 ? 648  ALA B O     1 
ATOM   13587 C  CB    . ALA B 1  650  ? 2.824   17.842  69.292  1.00 20.63 ? 648  ALA B CB    1 
ATOM   13588 N  N     . ARG B 1  651  ? 5.758   18.020  70.640  1.00 18.69 ? 649  ARG B N     1 
ATOM   13589 C  CA    . ARG B 1  651  ? 7.071   17.402  70.687  1.00 18.62 ? 649  ARG B CA    1 
ATOM   13590 C  C     . ARG B 1  651  ? 7.840   17.765  71.939  1.00 18.00 ? 649  ARG B C     1 
ATOM   13591 O  O     . ARG B 1  651  ? 9.030   17.454  72.036  1.00 19.23 ? 649  ARG B O     1 
ATOM   13592 C  CB    . ARG B 1  651  ? 7.862   17.785  69.436  1.00 18.18 ? 649  ARG B CB    1 
ATOM   13593 C  CG    . ARG B 1  651  ? 7.112   17.311  68.205  1.00 18.62 ? 649  ARG B CG    1 
ATOM   13594 C  CD    . ARG B 1  651  ? 7.748   17.793  66.927  1.00 19.58 ? 649  ARG B CD    1 
ATOM   13595 N  NE    . ARG B 1  651  ? 6.889   17.455  65.799  1.00 21.33 ? 649  ARG B NE    1 
ATOM   13596 C  CZ    . ARG B 1  651  ? 7.094   17.883  64.564  1.00 23.33 ? 649  ARG B CZ    1 
ATOM   13597 N  NH1   . ARG B 1  651  ? 8.152   18.622  64.260  1.00 19.30 ? 649  ARG B NH1   1 
ATOM   13598 N  NH2   . ARG B 1  651  ? 6.215   17.565  63.612  1.00 21.34 ? 649  ARG B NH2   1 
ATOM   13599 N  N     . MET B 1  652  ? 7.175   18.372  72.920  1.00 17.02 ? 650  MET B N     1 
ATOM   13600 C  CA    . MET B 1  652  ? 7.865   18.783  74.135  1.00 16.94 ? 650  MET B CA    1 
ATOM   13601 C  C     . MET B 1  652  ? 8.669   17.665  74.796  1.00 16.87 ? 650  MET B C     1 
ATOM   13602 O  O     . MET B 1  652  ? 9.801   17.942  75.220  1.00 18.67 ? 650  MET B O     1 
ATOM   13603 C  CB    . MET B 1  652  ? 6.851   19.393  75.119  1.00 15.26 ? 650  MET B CB    1 
ATOM   13604 C  CG    . MET B 1  652  ? 7.463   19.716  76.470  1.00 17.19 ? 650  MET B CG    1 
ATOM   13605 S  SD    . MET B 1  652  ? 6.269   20.487  77.596  1.00 19.77 ? 650  MET B SD    1 
ATOM   13606 C  CE    . MET B 1  652  ? 6.032   22.074  76.817  1.00 17.35 ? 650  MET B CE    1 
ATOM   13607 N  N     . PRO B 1  653  ? 8.198   16.410  74.890  1.00 17.12 ? 651  PRO B N     1 
ATOM   13608 C  CA    . PRO B 1  653  ? 9.029   15.395  75.561  1.00 20.37 ? 651  PRO B CA    1 
ATOM   13609 C  C     . PRO B 1  653  ? 10.379  15.216  74.897  1.00 17.23 ? 651  PRO B C     1 
ATOM   13610 O  O     . PRO B 1  653  ? 11.392  15.124  75.588  1.00 18.72 ? 651  PRO B O     1 
ATOM   13611 C  CB    . PRO B 1  653  ? 8.171   14.125  75.469  1.00 19.77 ? 651  PRO B CB    1 
ATOM   13612 C  CG    . PRO B 1  653  ? 6.776   14.637  75.505  1.00 22.21 ? 651  PRO B CG    1 
ATOM   13613 C  CD    . PRO B 1  653  ? 6.830   15.905  74.652  1.00 19.53 ? 651  PRO B CD    1 
ATOM   13614 N  N     . THR B 1  654  ? 10.406  15.191  73.565  1.00 17.76 ? 652  THR B N     1 
ATOM   13615 C  CA    . THR B 1  654  ? 11.666  15.059  72.840  1.00 18.76 ? 652  THR B CA    1 
ATOM   13616 C  C     . THR B 1  654  ? 12.534  16.300  73.013  1.00 19.25 ? 652  THR B C     1 
ATOM   13617 O  O     . THR B 1  654  ? 13.750  16.198  73.246  1.00 20.23 ? 652  THR B O     1 
ATOM   13618 C  CB    . THR B 1  654  ? 11.368  14.816  71.365  1.00 21.20 ? 652  THR B CB    1 
ATOM   13619 O  OG1   . THR B 1  654  ? 10.541  13.651  71.235  1.00 21.89 ? 652  THR B OG1   1 
ATOM   13620 C  CG2   . THR B 1  654  ? 12.657  14.629  70.581  1.00 19.63 ? 652  THR B CG2   1 
ATOM   13621 N  N     . LEU B 1  655  ? 11.933  17.482  72.884  1.00 17.68 ? 653  LEU B N     1 
ATOM   13622 C  CA    . LEU B 1  655  ? 12.679  18.714  73.094  1.00 16.58 ? 653  LEU B CA    1 
ATOM   13623 C  C     . LEU B 1  655  ? 13.273  18.761  74.493  1.00 19.49 ? 653  LEU B C     1 
ATOM   13624 O  O     . LEU B 1  655  ? 14.402  19.234  74.676  1.00 17.00 ? 653  LEU B O     1 
ATOM   13625 C  CB    . LEU B 1  655  ? 11.779  19.924  72.861  1.00 17.59 ? 653  LEU B CB    1 
ATOM   13626 C  CG    . LEU B 1  655  ? 11.112  20.010  71.489  1.00 18.20 ? 653  LEU B CG    1 
ATOM   13627 C  CD1   . LEU B 1  655  ? 10.266  21.270  71.365  1.00 18.04 ? 653  LEU B CD1   1 
ATOM   13628 C  CD2   . LEU B 1  655  ? 12.141  19.944  70.386  1.00 22.65 ? 653  LEU B CD2   1 
ATOM   13629 N  N     . LEU B 1  656  ? 12.518  18.292  75.495  1.00 17.76 ? 654  LEU B N     1 
ATOM   13630 C  CA    . LEU B 1  656  ? 13.041  18.246  76.864  1.00 19.23 ? 654  LEU B CA    1 
ATOM   13631 C  C     . LEU B 1  656  ? 14.327  17.444  76.927  1.00 18.84 ? 654  LEU B C     1 
ATOM   13632 O  O     . LEU B 1  656  ? 15.306  17.861  77.558  1.00 20.31 ? 654  LEU B O     1 
ATOM   13633 C  CB    . LEU B 1  656  ? 12.023  17.605  77.812  1.00 21.40 ? 654  LEU B CB    1 
ATOM   13634 C  CG    . LEU B 1  656  ? 10.657  18.213  78.020  1.00 23.62 ? 654  LEU B CG    1 
ATOM   13635 C  CD1   . LEU B 1  656  ? 9.940   17.534  79.186  1.00 22.28 ? 654  LEU B CD1   1 
ATOM   13636 C  CD2   . LEU B 1  656  ? 10.785  19.704  78.209  1.00 21.48 ? 654  LEU B CD2   1 
ATOM   13637 N  N     . GLY B 1  657  ? 14.321  16.263  76.310  1.00 20.52 ? 655  GLY B N     1 
ATOM   13638 C  CA    . GLY B 1  657  ? 15.489  15.406  76.344  1.00 19.51 ? 655  GLY B CA    1 
ATOM   13639 C  C     . GLY B 1  657  ? 16.721  16.093  75.800  1.00 22.36 ? 655  GLY B C     1 
ATOM   13640 O  O     . GLY B 1  657  ? 17.799  16.006  76.388  1.00 20.21 ? 655  GLY B O     1 
ATOM   13641 N  N     . LEU B 1  658  ? 16.572  16.804  74.682  1.00 19.24 ? 656  LEU B N     1 
ATOM   13642 C  CA    . LEU B 1  658  ? 17.715  17.501  74.109  1.00 15.96 ? 656  LEU B CA    1 
ATOM   13643 C  C     . LEU B 1  658  ? 18.174  18.642  75.013  1.00 18.26 ? 656  LEU B C     1 
ATOM   13644 O  O     . LEU B 1  658  ? 19.375  18.799  75.265  1.00 17.87 ? 656  LEU B O     1 
ATOM   13645 C  CB    . LEU B 1  658  ? 17.350  18.010  72.719  1.00 17.48 ? 656  LEU B CB    1 
ATOM   13646 C  CG    . LEU B 1  658  ? 18.461  18.722  71.957  1.00 17.95 ? 656  LEU B CG    1 
ATOM   13647 C  CD1   . LEU B 1  658  ? 19.687  17.832  71.823  1.00 15.78 ? 656  LEU B CD1   1 
ATOM   13648 C  CD2   . LEU B 1  658  ? 17.950  19.114  70.578  1.00 16.88 ? 656  LEU B CD2   1 
ATOM   13649 N  N     . ILE B 1  659  ? 17.235  19.424  75.547  1.00 15.85 ? 657  ILE B N     1 
ATOM   13650 C  CA    . ILE B 1  659  ? 17.606  20.563  76.388  1.00 12.99 ? 657  ILE B CA    1 
ATOM   13651 C  C     . ILE B 1  659  ? 18.289  20.085  77.659  1.00 15.93 ? 657  ILE B C     1 
ATOM   13652 O  O     . ILE B 1  659  ? 19.271  20.683  78.118  1.00 17.12 ? 657  ILE B O     1 
ATOM   13653 C  CB    . ILE B 1  659  ? 16.356  21.408  76.696  1.00 14.62 ? 657  ILE B CB    1 
ATOM   13654 C  CG1   . ILE B 1  659  ? 15.874  22.089  75.413  1.00 15.90 ? 657  ILE B CG1   1 
ATOM   13655 C  CG2   . ILE B 1  659  ? 16.634  22.423  77.797  1.00 18.57 ? 657  ILE B CG2   1 
ATOM   13656 C  CD1   . ILE B 1  659  ? 14.461  22.650  75.516  1.00 17.76 ? 657  ILE B CD1   1 
ATOM   13657 N  N     . ILE B 1  660  ? 17.771  19.004  78.253  1.00 15.87 ? 658  ILE B N     1 
ATOM   13658 C  CA    . ILE B 1  660  ? 18.364  18.462  79.470  1.00 15.50 ? 658  ILE B CA    1 
ATOM   13659 C  C     . ILE B 1  660  ? 19.819  18.098  79.231  1.00 17.59 ? 658  ILE B C     1 
ATOM   13660 O  O     . ILE B 1  660  ? 20.698  18.387  80.058  1.00 18.01 ? 658  ILE B O     1 
ATOM   13661 C  CB    . ILE B 1  660  ? 17.554  17.240  79.940  1.00 17.03 ? 658  ILE B CB    1 
ATOM   13662 C  CG1   . ILE B 1  660  ? 16.242  17.687  80.585  1.00 15.87 ? 658  ILE B CG1   1 
ATOM   13663 C  CG2   . ILE B 1  660  ? 18.368  16.390  80.904  1.00 17.95 ? 658  ILE B CG2   1 
ATOM   13664 C  CD1   . ILE B 1  660  ? 15.315  16.525  80.860  1.00 20.63 ? 658  ILE B CD1   1 
ATOM   13665 N  N     . ARG B 1  661  ? 20.095  17.452  78.106  1.00 16.77 ? 659  ARG B N     1 
ATOM   13666 C  CA    . ARG B 1  661  ? 21.431  16.934  77.846  1.00 17.45 ? 659  ARG B CA    1 
ATOM   13667 C  C     . ARG B 1  661  ? 22.369  17.965  77.232  1.00 19.11 ? 659  ARG B C     1 
ATOM   13668 O  O     . ARG B 1  661  ? 23.568  17.933  77.521  1.00 18.40 ? 659  ARG B O     1 
ATOM   13669 C  CB    . ARG B 1  661  ? 21.339  15.690  76.963  1.00 17.73 ? 659  ARG B CB    1 
ATOM   13670 C  CG    . ARG B 1  661  ? 20.880  14.494  77.762  1.00 20.28 ? 659  ARG B CG    1 
ATOM   13671 C  CD    . ARG B 1  661  ? 20.697  13.257  76.908  1.00 20.84 ? 659  ARG B CD    1 
ATOM   13672 N  NE    . ARG B 1  661  ? 21.934  12.824  76.257  1.00 22.13 ? 659  ARG B NE    1 
ATOM   13673 C  CZ    . ARG B 1  661  ? 22.091  12.741  74.944  1.00 24.81 ? 659  ARG B CZ    1 
ATOM   13674 N  NH1   . ARG B 1  661  ? 21.108  13.037  74.108  1.00 24.11 ? 659  ARG B NH1   1 
ATOM   13675 N  NH2   . ARG B 1  661  ? 23.256  12.317  74.453  1.00 24.11 ? 659  ARG B NH2   1 
ATOM   13676 N  N     . GLU B 1  662  ? 21.861  18.898  76.425  1.00 16.37 ? 660  GLU B N     1 
ATOM   13677 C  CA    . GLU B 1  662  ? 22.746  19.874  75.798  1.00 15.46 ? 660  GLU B CA    1 
ATOM   13678 C  C     . GLU B 1  662  ? 23.074  21.041  76.723  1.00 18.32 ? 660  GLU B C     1 
ATOM   13679 O  O     . GLU B 1  662  ? 24.190  21.575  76.680  1.00 17.90 ? 660  GLU B O     1 
ATOM   13680 C  CB    . GLU B 1  662  ? 22.116  20.409  74.508  1.00 18.74 ? 660  GLU B CB    1 
ATOM   13681 C  CG    . GLU B 1  662  ? 23.043  21.376  73.758  1.00 18.10 ? 660  GLU B CG    1 
ATOM   13682 C  CD    . GLU B 1  662  ? 22.458  21.890  72.436  1.00 15.82 ? 660  GLU B CD    1 
ATOM   13683 O  OE1   . GLU B 1  662  ? 21.227  22.049  72.324  1.00 17.29 ? 660  GLU B OE1   1 
ATOM   13684 O  OE2   . GLU B 1  662  ? 23.256  22.152  71.523  1.00 16.34 ? 660  GLU B OE2   1 
ATOM   13685 N  N     . ALA B 1  663  ? 22.116  21.472  77.535  1.00 15.28 ? 661  ALA B N     1 
ATOM   13686 C  CA    . ALA B 1  663  ? 22.232  22.748  78.228  1.00 14.84 ? 661  ALA B CA    1 
ATOM   13687 C  C     . ALA B 1  663  ? 22.240  22.612  79.746  1.00 16.96 ? 661  ALA B C     1 
ATOM   13688 O  O     . ALA B 1  663  ? 22.113  23.627  80.442  1.00 20.59 ? 661  ALA B O     1 
ATOM   13689 C  CB    . ALA B 1  663  ? 21.101  23.684  77.783  1.00 16.12 ? 661  ALA B CB    1 
ATOM   13690 N  N     . GLY B 1  664  ? 22.355  21.396  80.278  1.00 18.02 ? 662  GLY B N     1 
ATOM   13691 C  CA    . GLY B 1  664  ? 22.455  21.248  81.722  1.00 19.41 ? 662  GLY B CA    1 
ATOM   13692 C  C     . GLY B 1  664  ? 21.186  21.515  82.491  1.00 19.49 ? 662  GLY B C     1 
ATOM   13693 O  O     . GLY B 1  664  ? 21.246  21.797  83.686  1.00 18.32 ? 662  GLY B O     1 
ATOM   13694 N  N     . LYS B 1  665  ? 20.030  21.423  81.848  1.00 16.92 ? 663  LYS B N     1 
ATOM   13695 C  CA    . LYS B 1  665  ? 18.777  21.768  82.499  1.00 18.73 ? 663  LYS B CA    1 
ATOM   13696 C  C     . LYS B 1  665  ? 18.142  20.555  83.162  1.00 16.55 ? 663  LYS B C     1 
ATOM   13697 O  O     . LYS B 1  665  ? 18.211  19.435  82.650  1.00 16.15 ? 663  LYS B O     1 
ATOM   13698 C  CB    . LYS B 1  665  ? 17.786  22.346  81.489  1.00 15.57 ? 663  LYS B CB    1 
ATOM   13699 C  CG    . LYS B 1  665  ? 18.302  23.548  80.733  1.00 17.47 ? 663  LYS B CG    1 
ATOM   13700 C  CD    . LYS B 1  665  ? 18.559  24.720  81.642  1.00 21.62 ? 663  LYS B CD    1 
ATOM   13701 C  CE    . LYS B 1  665  ? 19.170  25.887  80.860  1.00 20.03 ? 663  LYS B CE    1 
ATOM   13702 N  NZ    . LYS B 1  665  ? 19.651  26.991  81.762  1.00 20.42 ? 663  LYS B NZ    1 
ATOM   13703 N  N     . SER B 1  666  ? 17.480  20.796  84.290  1.00 17.81 ? 664  SER B N     1 
ATOM   13704 C  CA    . SER B 1  666  ? 16.624  19.778  84.865  1.00 18.14 ? 664  SER B CA    1 
ATOM   13705 C  C     . SER B 1  666  ? 15.349  19.647  84.038  1.00 18.93 ? 664  SER B C     1 
ATOM   13706 O  O     . SER B 1  666  ? 15.022  20.508  83.223  1.00 17.85 ? 664  SER B O     1 
ATOM   13707 C  CB    . SER B 1  666  ? 16.246  20.139  86.292  1.00 20.94 ? 664  SER B CB    1 
ATOM   13708 O  OG    . SER B 1  666  ? 15.341  21.230  86.261  1.00 21.94 ? 664  SER B OG    1 
ATOM   13709 N  N     . ALA B 1  667  ? 14.610  18.562  84.290  1.00 18.11 ? 665  ALA B N     1 
ATOM   13710 C  CA    . ALA B 1  667  ? 13.346  18.338  83.586  1.00 16.97 ? 665  ALA B CA    1 
ATOM   13711 C  C     . ALA B 1  667  ? 12.389  19.510  83.764  1.00 19.65 ? 665  ALA B C     1 
ATOM   13712 O  O     . ALA B 1  667  ? 11.766  19.962  82.794  1.00 17.55 ? 665  ALA B O     1 
ATOM   13713 C  CB    . ALA B 1  667  ? 12.697  17.048  84.085  1.00 19.88 ? 665  ALA B CB    1 
ATOM   13714 N  N     . LEU B 1  668  ? 12.227  19.990  85.005  1.00 18.45 ? 666  LEU B N     1 
ATOM   13715 C  CA    . LEU B 1  668  ? 11.303  21.097  85.246  1.00 21.86 ? 666  LEU B CA    1 
ATOM   13716 C  C     . LEU B 1  668  ? 11.750  22.347  84.506  1.00 19.51 ? 666  LEU B C     1 
ATOM   13717 O  O     . LEU B 1  668  ? 10.928  23.079  83.941  1.00 18.45 ? 666  LEU B O     1 
ATOM   13718 C  CB    . LEU B 1  668  ? 11.182  21.391  86.743  1.00 23.25 ? 666  LEU B CB    1 
ATOM   13719 C  CG    . LEU B 1  668  ? 10.161  20.551  87.509  1.00 25.68 ? 666  LEU B CG    1 
ATOM   13720 C  CD1   . LEU B 1  668  ? 10.199  20.904  88.992  1.00 29.13 ? 666  LEU B CD1   1 
ATOM   13721 C  CD2   . LEU B 1  668  ? 8.744   20.717  86.928  1.00 25.29 ? 666  LEU B CD2   1 
ATOM   13722 N  N     . ASN B 1  669  ? 13.052  22.602  84.480  1.00 17.40 ? 667  ASN B N     1 
ATOM   13723 C  CA    . ASN B 1  669  ? 13.495  23.803  83.790  1.00 19.48 ? 667  ASN B CA    1 
ATOM   13724 C  C     . ASN B 1  669  ? 13.441  23.643  82.282  1.00 20.00 ? 667  ASN B C     1 
ATOM   13725 O  O     . ASN B 1  669  ? 13.245  24.636  81.571  1.00 19.43 ? 667  ASN B O     1 
ATOM   13726 C  CB    . ASN B 1  669  ? 14.886  24.189  84.271  1.00 24.93 ? 667  ASN B CB    1 
ATOM   13727 C  CG    . ASN B 1  669  ? 14.860  24.707  85.703  1.00 27.62 ? 667  ASN B CG    1 
ATOM   13728 O  OD1   . ASN B 1  669  ? 15.766  24.453  86.483  1.00 32.18 ? 667  ASN B OD1   1 
ATOM   13729 N  ND2   . ASN B 1  669  ? 13.783  25.419  86.055  1.00 28.38 ? 667  ASN B ND2   1 
ATOM   13730 N  N     . ALA B 1  670  ? 13.570  22.416  81.779  1.00 16.80 ? 668  ALA B N     1 
ATOM   13731 C  CA    . ALA B 1  670  ? 13.416  22.201  80.348  1.00 16.85 ? 668  ALA B CA    1 
ATOM   13732 C  C     . ALA B 1  670  ? 11.959  22.344  79.934  1.00 15.43 ? 668  ALA B C     1 
ATOM   13733 O  O     . ALA B 1  670  ? 11.662  22.837  78.838  1.00 15.17 ? 668  ALA B O     1 
ATOM   13734 C  CB    . ALA B 1  670  ? 13.959  20.828  79.956  1.00 16.15 ? 668  ALA B CB    1 
ATOM   13735 N  N     . ILE B 1  671  ? 11.031  21.888  80.782  1.00 17.34 ? 669  ILE B N     1 
ATOM   13736 C  CA    . ILE B 1  671  ? 9.615   22.147  80.527  1.00 15.58 ? 669  ILE B CA    1 
ATOM   13737 C  C     . ILE B 1  671  ? 9.357   23.648  80.452  1.00 17.16 ? 669  ILE B C     1 
ATOM   13738 O  O     . ILE B 1  671  ? 8.691   24.136  79.530  1.00 17.81 ? 669  ILE B O     1 
ATOM   13739 C  CB    . ILE B 1  671  ? 8.747   21.481  81.608  1.00 17.10 ? 669  ILE B CB    1 
ATOM   13740 C  CG1   . ILE B 1  671  ? 8.773   19.956  81.454  1.00 17.97 ? 669  ILE B CG1   1 
ATOM   13741 C  CG2   . ILE B 1  671  ? 7.307   22.033  81.553  1.00 17.00 ? 669  ILE B CG2   1 
ATOM   13742 C  CD1   . ILE B 1  671  ? 8.182   19.214  82.654  1.00 20.02 ? 669  ILE B CD1   1 
ATOM   13743 N  N     . ALA B 1  672  ? 9.879   24.402  81.419  1.00 16.06 ? 670  ALA B N     1 
ATOM   13744 C  CA    . ALA B 1  672  ? 9.659   25.844  81.413  1.00 17.86 ? 670  ALA B CA    1 
ATOM   13745 C  C     . ALA B 1  672  ? 10.266  26.474  80.169  1.00 16.99 ? 670  ALA B C     1 
ATOM   13746 O  O     . ALA B 1  672  ? 9.707   27.422  79.599  1.00 17.00 ? 670  ALA B O     1 
ATOM   13747 C  CB    . ALA B 1  672  ? 10.251  26.467  82.680  1.00 19.73 ? 670  ALA B CB    1 
ATOM   13748 N  N     . GLU B 1  673  ? 11.407  25.947  79.729  1.00 15.42 ? 671  GLU B N     1 
ATOM   13749 C  CA    . GLU B 1  673  ? 12.059  26.437  78.524  1.00 16.16 ? 671  GLU B CA    1 
ATOM   13750 C  C     . GLU B 1  673  ? 11.175  26.259  77.295  1.00 16.38 ? 671  GLU B C     1 
ATOM   13751 O  O     . GLU B 1  673  ? 10.963  27.206  76.527  1.00 15.22 ? 671  GLU B O     1 
ATOM   13752 C  CB    . GLU B 1  673  ? 13.385  25.701  78.341  1.00 16.56 ? 671  GLU B CB    1 
ATOM   13753 C  CG    . GLU B 1  673  ? 14.211  26.199  77.183  1.00 18.56 ? 671  GLU B CG    1 
ATOM   13754 C  CD    . GLU B 1  673  ? 14.969  27.485  77.481  1.00 19.17 ? 671  GLU B CD    1 
ATOM   13755 O  OE1   . GLU B 1  673  ? 15.162  27.848  78.673  1.00 19.08 ? 671  GLU B OE1   1 
ATOM   13756 O  OE2   . GLU B 1  673  ? 15.404  28.123  76.502  1.00 15.43 ? 671  GLU B OE2   1 
ATOM   13757 N  N     . VAL B 1  674  ? 10.662  25.046  77.082  1.00 13.15 ? 672  VAL B N     1 
ATOM   13758 C  CA    . VAL B 1  674  ? 9.809   24.806  75.918  1.00 13.07 ? 672  VAL B CA    1 
ATOM   13759 C  C     . VAL B 1  674  ? 8.496   25.576  76.034  1.00 14.09 ? 672  VAL B C     1 
ATOM   13760 O  O     . VAL B 1  674  ? 7.991   26.120  75.040  1.00 14.83 ? 672  VAL B O     1 
ATOM   13761 C  CB    . VAL B 1  674  ? 9.571   23.294  75.732  1.00 14.26 ? 672  VAL B CB    1 
ATOM   13762 C  CG1   . VAL B 1  674  ? 8.693   23.044  74.508  1.00 15.34 ? 672  VAL B CG1   1 
ATOM   13763 C  CG2   . VAL B 1  674  ? 10.898  22.559  75.583  1.00 15.41 ? 672  VAL B CG2   1 
ATOM   13764 N  N     . ARG B 1  675  ? 7.907   25.625  77.235  1.00 14.61 ? 673  ARG B N     1 
ATOM   13765 C  CA    . ARG B 1  675  ? 6.675   26.392  77.398  1.00 14.62 ? 673  ARG B CA    1 
ATOM   13766 C  C     . ARG B 1  675  ? 6.877   27.846  77.012  1.00 13.39 ? 673  ARG B C     1 
ATOM   13767 O  O     . ARG B 1  675  ? 6.017   28.453  76.365  1.00 15.71 ? 673  ARG B O     1 
ATOM   13768 C  CB    . ARG B 1  675  ? 6.175   26.325  78.835  1.00 16.51 ? 673  ARG B CB    1 
ATOM   13769 C  CG    . ARG B 1  675  ? 5.562   24.994  79.232  1.00 14.19 ? 673  ARG B CG    1 
ATOM   13770 C  CD    . ARG B 1  675  ? 4.905   25.138  80.600  1.00 17.61 ? 673  ARG B CD    1 
ATOM   13771 N  NE    . ARG B 1  675  ? 3.771   26.051  80.515  1.00 17.08 ? 673  ARG B NE    1 
ATOM   13772 C  CZ    . ARG B 1  675  ? 3.158   26.573  81.566  1.00 16.37 ? 673  ARG B CZ    1 
ATOM   13773 N  NH1   . ARG B 1  675  ? 3.591   26.352  82.797  1.00 17.82 ? 673  ARG B NH1   1 
ATOM   13774 N  NH2   . ARG B 1  675  ? 2.083   27.333  81.376  1.00 16.16 ? 673  ARG B NH2   1 
ATOM   13775 N  N     . GLU B 1  676  ? 7.998   28.424  77.426  1.00 13.67 ? 674  GLU B N     1 
ATOM   13776 C  CA    A GLU B 1  676  ? 8.254   29.827  77.121  0.47 14.14 ? 674  GLU B CA    1 
ATOM   13777 C  CA    B GLU B 1  676  ? 8.263   29.825  77.121  0.53 13.87 ? 674  GLU B CA    1 
ATOM   13778 C  C     . GLU B 1  676  ? 8.382   30.050  75.620  1.00 13.79 ? 674  GLU B C     1 
ATOM   13779 O  O     . GLU B 1  676  ? 7.903   31.059  75.099  1.00 14.09 ? 674  GLU B O     1 
ATOM   13780 C  CB    A GLU B 1  676  ? 9.512   30.300  77.852  0.47 16.00 ? 674  GLU B CB    1 
ATOM   13781 C  CB    B GLU B 1  676  ? 9.539   30.276  77.832  0.53 15.99 ? 674  GLU B CB    1 
ATOM   13782 C  CG    A GLU B 1  676  ? 9.728   31.807  77.794  0.47 16.24 ? 674  GLU B CG    1 
ATOM   13783 C  CG    B GLU B 1  676  ? 9.827   31.760  77.701  0.53 16.23 ? 674  GLU B CG    1 
ATOM   13784 C  CD    A GLU B 1  676  ? 10.832  32.277  78.722  0.47 19.08 ? 674  GLU B CD    1 
ATOM   13785 C  CD    B GLU B 1  676  ? 9.216   32.577  78.816  0.53 18.91 ? 674  GLU B CD    1 
ATOM   13786 O  OE1   A GLU B 1  676  ? 10.833  31.871  79.905  0.47 21.39 ? 674  GLU B OE1   1 
ATOM   13787 O  OE1   B GLU B 1  676  ? 8.361   32.055  79.563  0.53 20.01 ? 674  GLU B OE1   1 
ATOM   13788 O  OE2   A GLU B 1  676  ? 11.695  33.052  78.267  0.47 23.40 ? 674  GLU B OE2   1 
ATOM   13789 O  OE2   B GLU B 1  676  ? 9.603   33.754  78.948  0.53 18.25 ? 674  GLU B OE2   1 
ATOM   13790 N  N     . ALA B 1  677  ? 9.039   29.127  74.910  1.00 12.06 ? 675  ALA B N     1 
ATOM   13791 C  CA    . ALA B 1  677  ? 9.115   29.240  73.454  1.00 13.28 ? 675  ALA B CA    1 
ATOM   13792 C  C     . ALA B 1  677  ? 7.723   29.229  72.839  1.00 13.74 ? 675  ALA B C     1 
ATOM   13793 O  O     . ALA B 1  677  ? 7.412   30.037  71.955  1.00 13.45 ? 675  ALA B O     1 
ATOM   13794 C  CB    . ALA B 1  677  ? 9.959   28.102  72.863  1.00 13.47 ? 675  ALA B CB    1 
ATOM   13795 N  N     . ILE B 1  678  ? 6.881   28.298  73.292  1.00 13.57 ? 676  ILE B N     1 
ATOM   13796 C  CA    . ILE B 1  678  ? 5.498   28.222  72.821  1.00 12.03 ? 676  ILE B CA    1 
ATOM   13797 C  C     . ILE B 1  678  ? 4.768   29.523  73.108  1.00 12.56 ? 676  ILE B C     1 
ATOM   13798 O  O     . ILE B 1  678  ? 4.014   30.027  72.268  1.00 15.32 ? 676  ILE B O     1 
ATOM   13799 C  CB    . ILE B 1  678  ? 4.787   27.030  73.483  1.00 14.19 ? 676  ILE B CB    1 
ATOM   13800 C  CG1   . ILE B 1  678  ? 5.376   25.709  72.970  1.00 15.86 ? 676  ILE B CG1   1 
ATOM   13801 C  CG2   . ILE B 1  678  ? 3.258   27.119  73.283  1.00 13.96 ? 676  ILE B CG2   1 
ATOM   13802 C  CD1   . ILE B 1  678  ? 5.125   24.545  73.934  1.00 14.65 ? 676  ILE B CD1   1 
ATOM   13803 N  N     . ASP B 1  679  ? 4.942   30.062  74.314  1.00 13.33 ? 677  ASP B N     1 
ATOM   13804 C  CA    . ASP B 1  679  ? 4.237   31.293  74.669  1.00 13.79 ? 677  ASP B CA    1 
ATOM   13805 C  C     . ASP B 1  679  ? 4.726   32.477  73.845  1.00 12.72 ? 677  ASP B C     1 
ATOM   13806 O  O     . ASP B 1  679  ? 3.919   33.314  73.436  1.00 14.23 ? 677  ASP B O     1 
ATOM   13807 C  CB    . ASP B 1  679  ? 4.377   31.582  76.164  1.00 15.05 ? 677  ASP B CB    1 
ATOM   13808 C  CG    . ASP B 1  679  ? 3.623   30.585  77.032  1.00 16.99 ? 677  ASP B CG    1 
ATOM   13809 O  OD1   . ASP B 1  679  ? 2.561   30.079  76.613  1.00 16.56 ? 677  ASP B OD1   1 
ATOM   13810 O  OD2   . ASP B 1  679  ? 4.096   30.317  78.145  1.00 15.31 ? 677  ASP B OD2   1 
ATOM   13811 N  N     . PHE B 1  680  ? 6.038   32.575  73.585  1.00 12.23 ? 678  PHE B N     1 
ATOM   13812 C  CA    . PHE B 1  680  ? 6.516   33.624  72.684  1.00 13.67 ? 678  PHE B CA    1 
ATOM   13813 C  C     . PHE B 1  680  ? 5.840   33.510  71.329  1.00 14.06 ? 678  PHE B C     1 
ATOM   13814 O  O     . PHE B 1  680  ? 5.387   34.508  70.752  1.00 14.63 ? 678  PHE B O     1 
ATOM   13815 C  CB    . PHE B 1  680  ? 8.034   33.539  72.492  1.00 12.73 ? 678  PHE B CB    1 
ATOM   13816 C  CG    . PHE B 1  680  ? 8.841   34.196  73.572  1.00 13.64 ? 678  PHE B CG    1 
ATOM   13817 C  CD1   . PHE B 1  680  ? 8.587   35.492  73.986  1.00 12.58 ? 678  PHE B CD1   1 
ATOM   13818 C  CD2   . PHE B 1  680  ? 9.903   33.502  74.146  1.00 13.51 ? 678  PHE B CD2   1 
ATOM   13819 C  CE1   . PHE B 1  680  ? 9.379   36.087  74.992  1.00 14.53 ? 678  PHE B CE1   1 
ATOM   13820 C  CE2   . PHE B 1  680  ? 10.692  34.075  75.140  1.00 15.16 ? 678  PHE B CE2   1 
ATOM   13821 C  CZ    . PHE B 1  680  ? 10.441  35.373  75.555  1.00 14.57 ? 678  PHE B CZ    1 
ATOM   13822 N  N     . LEU B 1  681  ? 5.803   32.296  70.781  1.00 11.59 ? 679  LEU B N     1 
ATOM   13823 C  CA    . LEU B 1  681  ? 5.206   32.112  69.462  1.00 13.50 ? 679  LEU B CA    1 
ATOM   13824 C  C     . LEU B 1  681  ? 3.762   32.585  69.457  1.00 14.23 ? 679  LEU B C     1 
ATOM   13825 O  O     . LEU B 1  681  ? 3.355   33.376  68.594  1.00 14.10 ? 679  LEU B O     1 
ATOM   13826 C  CB    . LEU B 1  681  ? 5.290   30.642  69.047  1.00 12.46 ? 679  LEU B CB    1 
ATOM   13827 C  CG    . LEU B 1  681  ? 6.717   30.156  68.736  1.00 13.13 ? 679  LEU B CG    1 
ATOM   13828 C  CD1   . LEU B 1  681  ? 6.765   28.637  68.786  1.00 13.38 ? 679  LEU B CD1   1 
ATOM   13829 C  CD2   . LEU B 1  681  ? 7.173   30.662  67.377  1.00 14.26 ? 679  LEU B CD2   1 
ATOM   13830 N  N     . ARG B 1  682  ? 2.975   32.114  70.423  1.00 13.48 ? 680  ARG B N     1 
ATOM   13831 C  CA    . ARG B 1  682  ? 1.560   32.458  70.430  1.00 13.48 ? 680  ARG B CA    1 
ATOM   13832 C  C     . ARG B 1  682  ? 1.326   33.910  70.806  1.00 13.55 ? 680  ARG B C     1 
ATOM   13833 O  O     . ARG B 1  682  ? 0.357   34.517  70.332  1.00 14.86 ? 680  ARG B O     1 
ATOM   13834 C  CB    . ARG B 1  682  ? 0.804   31.539  71.382  1.00 11.85 ? 680  ARG B CB    1 
ATOM   13835 C  CG    . ARG B 1  682  ? 0.739   30.107  70.863  1.00 13.16 ? 680  ARG B CG    1 
ATOM   13836 C  CD    . ARG B 1  682  ? 0.092   29.239  71.883  1.00 14.82 ? 680  ARG B CD    1 
ATOM   13837 N  NE    . ARG B 1  682  ? -0.125  27.885  71.389  1.00 13.37 ? 680  ARG B NE    1 
ATOM   13838 C  CZ    . ARG B 1  682  ? -0.326  26.839  72.175  1.00 14.89 ? 680  ARG B CZ    1 
ATOM   13839 N  NH1   . ARG B 1  682  ? -0.315  26.951  73.493  1.00 15.82 ? 680  ARG B NH1   1 
ATOM   13840 N  NH2   . ARG B 1  682  ? -0.498  25.640  71.623  1.00 17.58 ? 680  ARG B NH2   1 
ATOM   13841 N  N     . TYR B 1  683  ? 2.173   34.468  71.663  1.00 14.63 ? 681  TYR B N     1 
ATOM   13842 C  CA    . TYR B 1  683  ? 2.000   35.862  72.051  1.00 15.79 ? 681  TYR B CA    1 
ATOM   13843 C  C     . TYR B 1  683  ? 2.317   36.798  70.892  1.00 14.44 ? 681  TYR B C     1 
ATOM   13844 O  O     . TYR B 1  683  ? 1.543   37.719  70.596  1.00 13.44 ? 681  TYR B O     1 
ATOM   13845 C  CB    . TYR B 1  683  ? 2.874   36.179  73.262  1.00 12.91 ? 681  TYR B CB    1 
ATOM   13846 C  CG    . TYR B 1  683  ? 2.838   37.624  73.681  1.00 13.88 ? 681  TYR B CG    1 
ATOM   13847 C  CD1   . TYR B 1  683  ? 1.792   38.103  74.450  1.00 15.22 ? 681  TYR B CD1   1 
ATOM   13848 C  CD2   . TYR B 1  683  ? 3.865   38.496  73.332  1.00 13.58 ? 681  TYR B CD2   1 
ATOM   13849 C  CE1   . TYR B 1  683  ? 1.752   39.433  74.850  1.00 13.47 ? 681  TYR B CE1   1 
ATOM   13850 C  CE2   . TYR B 1  683  ? 3.835   39.838  73.716  1.00 13.06 ? 681  TYR B CE2   1 
ATOM   13851 C  CZ    . TYR B 1  683  ? 2.771   40.290  74.478  1.00 13.61 ? 681  TYR B CZ    1 
ATOM   13852 O  OH    . TYR B 1  683  ? 2.706   41.609  74.877  1.00 14.99 ? 681  TYR B OH    1 
ATOM   13853 N  N     . TYR B 1  684  ? 3.458   36.594  70.229  1.00 12.72 ? 682  TYR B N     1 
ATOM   13854 C  CA    . TYR B 1  684  ? 3.767   37.480  69.109  1.00 12.77 ? 682  TYR B CA    1 
ATOM   13855 C  C     . TYR B 1  684  ? 2.785   37.265  67.963  1.00 13.70 ? 682  TYR B C     1 
ATOM   13856 O  O     . TYR B 1  684  ? 2.478   38.209  67.235  1.00 14.70 ? 682  TYR B O     1 
ATOM   13857 C  CB    . TYR B 1  684  ? 5.216   37.289  68.645  1.00 13.81 ? 682  TYR B CB    1 
ATOM   13858 C  CG    . TYR B 1  684  ? 6.229   37.667  69.698  1.00 14.16 ? 682  TYR B CG    1 
ATOM   13859 C  CD1   . TYR B 1  684  ? 6.070   38.809  70.463  1.00 14.13 ? 682  TYR B CD1   1 
ATOM   13860 C  CD2   . TYR B 1  684  ? 7.342   36.885  69.916  1.00 12.85 ? 682  TYR B CD2   1 
ATOM   13861 C  CE1   . TYR B 1  684  ? 6.985   39.149  71.439  1.00 13.42 ? 682  TYR B CE1   1 
ATOM   13862 C  CE2   . TYR B 1  684  ? 8.275   37.215  70.897  1.00 11.97 ? 682  TYR B CE2   1 
ATOM   13863 C  CZ    . TYR B 1  684  ? 8.094   38.348  71.650  1.00 14.04 ? 682  TYR B CZ    1 
ATOM   13864 O  OH    . TYR B 1  684  ? 9.011   38.676  72.632  1.00 13.07 ? 682  TYR B OH    1 
ATOM   13865 N  N     . ALA B 1  685  ? 2.256   36.046  67.810  1.00 14.86 ? 683  ALA B N     1 
ATOM   13866 C  CA    . ALA B 1  685  ? 1.205   35.825  66.821  1.00 13.87 ? 683  ALA B CA    1 
ATOM   13867 C  C     . ALA B 1  685  ? -0.015  36.682  67.132  1.00 14.79 ? 683  ALA B C     1 
ATOM   13868 O  O     . ALA B 1  685  ? -0.533  37.386  66.253  1.00 13.71 ? 683  ALA B O     1 
ATOM   13869 C  CB    . ALA B 1  685  ? 0.838   34.342  66.769  1.00 13.99 ? 683  ALA B CB    1 
ATOM   13870 N  N     . GLU B 1  686  ? -0.484  36.642  68.381  1.00 14.30 ? 684  GLU B N     1 
ATOM   13871 C  CA    . GLU B 1  686  ? -1.655  37.433  68.751  1.00 17.07 ? 684  GLU B CA    1 
ATOM   13872 C  C     . GLU B 1  686  ? -1.365  38.922  68.659  1.00 16.68 ? 684  GLU B C     1 
ATOM   13873 O  O     . GLU B 1  686  ? -2.174  39.684  68.130  1.00 14.68 ? 684  GLU B O     1 
ATOM   13874 C  CB    . GLU B 1  686  ? -2.128  37.075  70.154  1.00 17.50 ? 684  GLU B CB    1 
ATOM   13875 C  CG    . GLU B 1  686  ? -3.278  37.983  70.671  1.00 16.33 ? 684  GLU B CG    1 
ATOM   13876 C  CD    . GLU B 1  686  ? -4.550  37.914  69.835  1.00 18.95 ? 684  GLU B CD    1 
ATOM   13877 O  OE1   . GLU B 1  686  ? -4.676  37.043  68.948  1.00 19.52 ? 684  GLU B OE1   1 
ATOM   13878 O  OE2   . GLU B 1  686  ? -5.459  38.735  70.094  1.00 18.95 ? 684  GLU B OE2   1 
ATOM   13879 N  N     . GLN B 1  687  ? -0.215  39.360  69.171  1.00 15.03 ? 685  GLN B N     1 
ATOM   13880 C  CA    . GLN B 1  687  ? 0.098   40.785  69.095  1.00 14.48 ? 685  GLN B CA    1 
ATOM   13881 C  C     . GLN B 1  687  ? 0.135   41.260  67.650  1.00 16.86 ? 685  GLN B C     1 
ATOM   13882 O  O     . GLN B 1  687  ? -0.294  42.382  67.346  1.00 16.25 ? 685  GLN B O     1 
ATOM   13883 C  CB    . GLN B 1  687  ? 1.426   41.087  69.783  1.00 14.86 ? 685  GLN B CB    1 
ATOM   13884 C  CG    . GLN B 1  687  ? 1.364   40.898  71.293  1.00 14.69 ? 685  GLN B CG    1 
ATOM   13885 C  CD    . GLN B 1  687  ? 0.327   41.795  71.933  1.00 15.59 ? 685  GLN B CD    1 
ATOM   13886 O  OE1   . GLN B 1  687  ? 0.348   43.009  71.743  1.00 16.61 ? 685  GLN B OE1   1 
ATOM   13887 N  NE2   . GLN B 1  687  ? -0.596  41.201  72.683  1.00 19.11 ? 685  GLN B NE2   1 
ATOM   13888 N  N     . THR B 1  688  ? 0.632   40.411  66.742  1.00 14.92 ? 686  THR B N     1 
ATOM   13889 C  CA    . THR B 1  688  ? 0.573   40.735  65.319  1.00 14.73 ? 686  THR B CA    1 
ATOM   13890 C  C     . THR B 1  688  ? -0.866  40.886  64.845  1.00 14.69 ? 686  THR B C     1 
ATOM   13891 O  O     . THR B 1  688  ? -1.211  41.865  64.175  1.00 15.72 ? 686  THR B O     1 
ATOM   13892 C  CB    . THR B 1  688  ? 1.275   39.652  64.508  1.00 13.16 ? 686  THR B CB    1 
ATOM   13893 O  OG1   . THR B 1  688  ? 2.676   39.689  64.787  1.00 15.40 ? 686  THR B OG1   1 
ATOM   13894 C  CG2   . THR B 1  688  ? 1.049   39.896  63.022  1.00 15.90 ? 686  THR B CG2   1 
ATOM   13895 N  N     . ARG B 1  689  ? -1.721  39.921  65.182  1.00 13.17 ? 687  ARG B N     1 
ATOM   13896 C  CA    . ARG B 1  689  ? -3.122  40.002  64.770  1.00 15.86 ? 687  ARG B CA    1 
ATOM   13897 C  C     . ARG B 1  689  ? -3.810  41.244  65.322  1.00 15.74 ? 687  ARG B C     1 
ATOM   13898 O  O     . ARG B 1  689  ? -4.773  41.731  64.728  1.00 17.41 ? 687  ARG B O     1 
ATOM   13899 C  CB    . ARG B 1  689  ? -3.865  38.752  65.226  1.00 16.53 ? 687  ARG B CB    1 
ATOM   13900 C  CG    . ARG B 1  689  ? -3.567  37.519  64.379  1.00 17.04 ? 687  ARG B CG    1 
ATOM   13901 C  CD    . ARG B 1  689  ? -4.470  36.384  64.796  1.00 14.88 ? 687  ARG B CD    1 
ATOM   13902 N  NE    . ARG B 1  689  ? -4.256  35.982  66.176  1.00 18.19 ? 687  ARG B NE    1 
ATOM   13903 C  CZ    . ARG B 1  689  ? -3.497  34.967  66.563  1.00 18.11 ? 687  ARG B CZ    1 
ATOM   13904 N  NH1   . ARG B 1  689  ? -2.835  34.219  65.689  1.00 16.42 ? 687  ARG B NH1   1 
ATOM   13905 N  NH2   . ARG B 1  689  ? -3.411  34.682  67.858  1.00 16.45 ? 687  ARG B NH2   1 
ATOM   13906 N  N     . ARG B 1  690  ? -3.328  41.773  66.451  1.00 14.63 ? 688  ARG B N     1 
ATOM   13907 C  CA    . ARG B 1  690  ? -3.905  42.980  67.032  1.00 14.84 ? 688  ARG B CA    1 
ATOM   13908 C  C     . ARG B 1  690  ? -3.386  44.271  66.411  1.00 16.95 ? 688  ARG B C     1 
ATOM   13909 O  O     . ARG B 1  690  ? -4.013  45.321  66.601  1.00 17.37 ? 688  ARG B O     1 
ATOM   13910 C  CB    . ARG B 1  690  ? -3.628  43.024  68.541  1.00 16.27 ? 688  ARG B CB    1 
ATOM   13911 C  CG    . ARG B 1  690  ? -4.311  41.909  69.346  1.00 18.57 ? 688  ARG B CG    1 
ATOM   13912 C  CD    . ARG B 1  690  ? -5.818  42.145  69.524  1.00 21.45 ? 688  ARG B CD    1 
ATOM   13913 N  NE    . ARG B 1  690  ? -6.080  43.390  70.239  1.00 24.59 ? 688  ARG B NE    1 
ATOM   13914 C  CZ    . ARG B 1  690  ? -6.618  44.470  69.690  1.00 25.97 ? 688  ARG B CZ    1 
ATOM   13915 N  NH1   . ARG B 1  690  ? -7.014  44.481  68.424  1.00 26.26 ? 688  ARG B NH1   1 
ATOM   13916 N  NH2   . ARG B 1  690  ? -6.787  45.561  70.435  1.00 22.24 ? 688  ARG B NH2   1 
ATOM   13917 N  N     . THR B 1  691  ? -2.252  44.242  65.705  1.00 14.59 ? 689  THR B N     1 
ATOM   13918 C  CA    . THR B 1  691  ? -1.618  45.503  65.340  1.00 17.42 ? 689  THR B CA    1 
ATOM   13919 C  C     . THR B 1  691  ? -1.219  45.678  63.879  1.00 17.23 ? 689  THR B C     1 
ATOM   13920 O  O     . THR B 1  691  ? -1.457  46.750  63.324  1.00 21.73 ? 689  THR B O     1 
ATOM   13921 C  CB    . THR B 1  691  ? -0.368  45.733  66.186  1.00 15.19 ? 689  THR B CB    1 
ATOM   13922 O  OG1   . THR B 1  691  ? 0.531   44.621  66.047  1.00 15.25 ? 689  THR B OG1   1 
ATOM   13923 C  CG2   . THR B 1  691  ? -0.754  45.901  67.641  1.00 17.21 ? 689  THR B CG2   1 
ATOM   13924 N  N     . LEU B 1  692  ? -0.583  44.687  63.254  1.00 16.46 ? 690  LEU B N     1 
ATOM   13925 C  CA    . LEU B 1  692  ? 0.180   44.983  62.045  1.00 18.57 ? 690  LEU B CA    1 
ATOM   13926 C  C     . LEU B 1  692  ? -0.716  45.106  60.816  1.00 18.45 ? 690  LEU B C     1 
ATOM   13927 O  O     . LEU B 1  692  ? -1.526  44.222  60.523  1.00 19.63 ? 690  LEU B O     1 
ATOM   13928 C  CB    . LEU B 1  692  ? 1.261   43.930  61.802  1.00 16.76 ? 690  LEU B CB    1 
ATOM   13929 C  CG    . LEU B 1  692  ? 2.318   43.898  62.914  1.00 15.88 ? 690  LEU B CG    1 
ATOM   13930 C  CD1   . LEU B 1  692  ? 3.452   42.946  62.545  1.00 18.22 ? 690  LEU B CD1   1 
ATOM   13931 C  CD2   . LEU B 1  692  ? 2.879   45.286  63.234  1.00 16.68 ? 690  LEU B CD2   1 
ATOM   13932 N  N     . GLY B 1  693  ? -0.544  46.209  60.102  1.00 19.71 ? 691  GLY B N     1 
ATOM   13933 C  CA    . GLY B 1  693  ? -1.234  46.474  58.867  1.00 19.66 ? 691  GLY B CA    1 
ATOM   13934 C  C     . GLY B 1  693  ? -0.246  46.913  57.809  1.00 21.99 ? 691  GLY B C     1 
ATOM   13935 O  O     . GLY B 1  693  ? 0.970   46.908  58.023  1.00 21.38 ? 691  GLY B O     1 
ATOM   13936 N  N     . PRO B 1  694  ? -0.751  47.339  56.651  1.00 23.91 ? 692  PRO B N     1 
ATOM   13937 C  CA    . PRO B 1  694  ? 0.146   47.545  55.501  1.00 22.61 ? 692  PRO B CA    1 
ATOM   13938 C  C     . PRO B 1  694  ? 1.172   48.647  55.700  1.00 25.04 ? 692  PRO B C     1 
ATOM   13939 O  O     . PRO B 1  694  ? 2.257   48.586  55.106  1.00 25.53 ? 692  PRO B O     1 
ATOM   13940 C  CB    . PRO B 1  694  ? -0.828  47.868  54.354  1.00 24.49 ? 692  PRO B CB    1 
ATOM   13941 C  CG    . PRO B 1  694  ? -2.114  48.236  55.006  1.00 27.50 ? 692  PRO B CG    1 
ATOM   13942 C  CD    . PRO B 1  694  ? -2.173  47.492  56.299  1.00 25.89 ? 692  PRO B CD    1 
ATOM   13943 N  N     . GLY B 1  695  ? 0.877   49.653  56.517  1.00 23.27 ? 693  GLY B N     1 
ATOM   13944 C  CA    . GLY B 1  695  ? 1.816   50.722  56.763  1.00 23.82 ? 693  GLY B CA    1 
ATOM   13945 C  C     . GLY B 1  695  ? 2.918   50.409  57.751  1.00 24.92 ? 693  GLY B C     1 
ATOM   13946 O  O     . GLY B 1  695  ? 3.759   51.271  58.019  1.00 24.51 ? 693  GLY B O     1 
ATOM   13947 N  N     . HIS B 1  696  ? 2.936   49.205  58.324  1.00 22.63 ? 694  HIS B N     1 
ATOM   13948 C  CA    . HIS B 1  696  ? 3.971   48.828  59.285  1.00 21.57 ? 694  HIS B CA    1 
ATOM   13949 C  C     . HIS B 1  696  ? 4.989   47.960  58.550  1.00 21.95 ? 694  HIS B C     1 
ATOM   13950 O  O     . HIS B 1  696  ? 5.024   46.736  58.668  1.00 23.84 ? 694  HIS B O     1 
ATOM   13951 C  CB    . HIS B 1  696  ? 3.346   48.129  60.492  1.00 19.68 ? 694  HIS B CB    1 
ATOM   13952 C  CG    . HIS B 1  696  ? 2.240   48.918  61.125  1.00 19.59 ? 694  HIS B CG    1 
ATOM   13953 N  ND1   . HIS B 1  696  ? 0.942   48.462  61.191  1.00 20.65 ? 694  HIS B ND1   1 
ATOM   13954 C  CD2   . HIS B 1  696  ? 2.233   50.149  61.684  1.00 19.00 ? 694  HIS B CD2   1 
ATOM   13955 C  CE1   . HIS B 1  696  ? 0.185   49.375  61.770  1.00 19.36 ? 694  HIS B CE1   1 
ATOM   13956 N  NE2   . HIS B 1  696  ? 0.943   50.409  62.078  1.00 18.59 ? 694  HIS B NE2   1 
ATOM   13957 N  N     . GLY B 1  697  ? 5.832   48.624  57.772  1.00 23.99 ? 695  GLY B N     1 
ATOM   13958 C  CA    . GLY B 1  697  ? 6.773   47.944  56.917  1.00 22.94 ? 695  GLY B CA    1 
ATOM   13959 C  C     . GLY B 1  697  ? 7.892   47.283  57.687  1.00 20.60 ? 695  GLY B C     1 
ATOM   13960 O  O     . GLY B 1  697  ? 8.386   47.814  58.682  1.00 21.84 ? 695  GLY B O     1 
ATOM   13961 N  N     . PRO B 1  698  ? 8.340   46.119  57.224  1.00 21.16 ? 696  PRO B N     1 
ATOM   13962 C  CA    . PRO B 1  698  ? 9.467   45.454  57.885  1.00 19.96 ? 696  PRO B CA    1 
ATOM   13963 C  C     . PRO B 1  698  ? 10.758  46.236  57.716  1.00 19.14 ? 696  PRO B C     1 
ATOM   13964 O  O     . PRO B 1  698  ? 10.923  47.049  56.805  1.00 20.39 ? 696  PRO B O     1 
ATOM   13965 C  CB    . PRO B 1  698  ? 9.556   44.105  57.165  1.00 22.09 ? 696  PRO B CB    1 
ATOM   13966 C  CG    . PRO B 1  698  ? 9.015   44.399  55.804  1.00 26.70 ? 696  PRO B CG    1 
ATOM   13967 C  CD    . PRO B 1  698  ? 7.884   45.374  56.039  1.00 23.33 ? 696  PRO B CD    1 
ATOM   13968 N  N     . LEU B 1  699  ? 11.691  45.966  58.625  1.00 17.76 ? 697  LEU B N     1 
ATOM   13969 C  CA    . LEU B 1  699  ? 13.026  46.529  58.489  1.00 17.92 ? 697  LEU B CA    1 
ATOM   13970 C  C     . LEU B 1  699  ? 13.775  45.896  57.327  1.00 17.54 ? 697  LEU B C     1 
ATOM   13971 O  O     . LEU B 1  699  ? 14.472  46.588  56.583  1.00 19.91 ? 697  LEU B O     1 
ATOM   13972 C  CB    . LEU B 1  699  ? 13.819  46.314  59.774  1.00 16.88 ? 697  LEU B CB    1 
ATOM   13973 C  CG    . LEU B 1  699  ? 13.220  46.898  61.049  1.00 18.46 ? 697  LEU B CG    1 
ATOM   13974 C  CD1   . LEU B 1  699  ? 14.103  46.488  62.213  1.00 19.05 ? 697  LEU B CD1   1 
ATOM   13975 C  CD2   . LEU B 1  699  ? 13.114  48.417  60.943  1.00 20.34 ? 697  LEU B CD2   1 
ATOM   13976 N  N     . GLY B 1  700  ? 13.672  44.578  57.180  1.00 18.70 ? 698  GLY B N     1 
ATOM   13977 C  CA    . GLY B 1  700  ? 14.564  43.838  56.314  1.00 18.61 ? 698  GLY B CA    1 
ATOM   13978 C  C     . GLY B 1  700  ? 15.233  42.718  57.087  1.00 15.22 ? 698  GLY B C     1 
ATOM   13979 O  O     . GLY B 1  700  ? 14.785  42.353  58.178  1.00 17.01 ? 698  GLY B O     1 
ATOM   13980 N  N     . PRO B 1  701  ? 16.306  42.150  56.548  1.00 15.98 ? 699  PRO B N     1 
ATOM   13981 C  CA    . PRO B 1  701  ? 16.977  41.041  57.239  1.00 14.70 ? 699  PRO B CA    1 
ATOM   13982 C  C     . PRO B 1  701  ? 17.358  41.422  58.659  1.00 16.21 ? 699  PRO B C     1 
ATOM   13983 O  O     . PRO B 1  701  ? 17.998  42.445  58.900  1.00 17.02 ? 699  PRO B O     1 
ATOM   13984 C  CB    . PRO B 1  701  ? 18.218  40.784  56.375  1.00 16.62 ? 699  PRO B CB    1 
ATOM   13985 C  CG    . PRO B 1  701  ? 17.818  41.264  55.006  1.00 17.56 ? 699  PRO B CG    1 
ATOM   13986 C  CD    . PRO B 1  701  ? 16.992  42.503  55.291  1.00 18.69 ? 699  PRO B CD    1 
ATOM   13987 N  N     . ILE B 1  702  ? 16.939  40.597  59.611  1.00 15.80 ? 700  ILE B N     1 
ATOM   13988 C  CA    . ILE B 1  702  ? 17.255  40.807  61.015  1.00 14.22 ? 700  ILE B CA    1 
ATOM   13989 C  C     . ILE B 1  702  ? 18.159  39.680  61.484  1.00 15.73 ? 700  ILE B C     1 
ATOM   13990 O  O     . ILE B 1  702  ? 17.878  38.492  61.256  1.00 14.29 ? 700  ILE B O     1 
ATOM   13991 C  CB    . ILE B 1  702  ? 15.984  40.900  61.877  1.00 14.63 ? 700  ILE B CB    1 
ATOM   13992 C  CG1   . ILE B 1  702  ? 15.264  42.210  61.580  1.00 15.10 ? 700  ILE B CG1   1 
ATOM   13993 C  CG2   . ILE B 1  702  ? 16.338  40.805  63.390  1.00 15.16 ? 700  ILE B CG2   1 
ATOM   13994 C  CD1   . ILE B 1  702  ? 14.038  42.424  62.467  1.00 19.56 ? 700  ILE B CD1   1 
ATOM   13995 N  N     . VAL B 1  703  ? 19.246  40.063  62.134  1.00 15.34 ? 701  VAL B N     1 
ATOM   13996 C  CA    . VAL B 1  703  ? 20.186  39.132  62.731  1.00 14.13 ? 701  VAL B CA    1 
ATOM   13997 C  C     . VAL B 1  703  ? 19.754  38.914  64.174  1.00 14.88 ? 701  VAL B C     1 
ATOM   13998 O  O     . VAL B 1  703  ? 19.664  39.874  64.945  1.00 13.60 ? 701  VAL B O     1 
ATOM   13999 C  CB    . VAL B 1  703  ? 21.610  39.695  62.654  1.00 15.40 ? 701  VAL B CB    1 
ATOM   14000 C  CG1   . VAL B 1  703  ? 22.558  38.885  63.520  1.00 14.85 ? 701  VAL B CG1   1 
ATOM   14001 C  CG2   . VAL B 1  703  ? 22.076  39.741  61.203  1.00 14.92 ? 701  VAL B CG2   1 
ATOM   14002 N  N     . CYS B 1  704  ? 19.480  37.664  64.535  1.00 14.18 ? 702  CYS B N     1 
ATOM   14003 C  CA    . CYS B 1  704  ? 19.059  37.303  65.886  1.00 14.38 ? 702  CYS B CA    1 
ATOM   14004 C  C     . CYS B 1  704  ? 20.185  36.515  66.529  1.00 13.65 ? 702  CYS B C     1 
ATOM   14005 O  O     . CYS B 1  704  ? 20.491  35.403  66.090  1.00 13.50 ? 702  CYS B O     1 
ATOM   14006 C  CB    . CYS B 1  704  ? 17.778  36.479  65.865  1.00 13.11 ? 702  CYS B CB    1 
ATOM   14007 S  SG    . CYS B 1  704  ? 16.374  37.362  65.159  1.00 15.42 ? 702  CYS B SG    1 
ATOM   14008 N  N     . ILE B 1  705  ? 20.768  37.082  67.585  1.00 12.86 ? 703  ILE B N     1 
ATOM   14009 C  CA    . ILE B 1  705  ? 21.905  36.497  68.291  1.00 14.08 ? 703  ILE B CA    1 
ATOM   14010 C  C     . ILE B 1  705  ? 21.456  36.223  69.719  1.00 13.04 ? 703  ILE B C     1 
ATOM   14011 O  O     . ILE B 1  705  ? 20.913  37.114  70.381  1.00 14.03 ? 703  ILE B O     1 
ATOM   14012 C  CB    . ILE B 1  705  ? 23.127  37.433  68.255  1.00 13.42 ? 703  ILE B CB    1 
ATOM   14013 C  CG1   . ILE B 1  705  ? 23.693  37.503  66.831  1.00 15.37 ? 703  ILE B CG1   1 
ATOM   14014 C  CG2   . ILE B 1  705  ? 24.168  36.954  69.229  1.00 14.79 ? 703  ILE B CG2   1 
ATOM   14015 C  CD1   . ILE B 1  705  ? 24.651  38.690  66.611  1.00 15.34 ? 703  ILE B CD1   1 
ATOM   14016 N  N     . SER B 1  706  ? 21.616  34.985  70.166  1.00 14.23 ? 704  SER B N     1 
ATOM   14017 C  CA    . SER B 1  706  ? 20.959  34.514  71.374  1.00 16.78 ? 704  SER B CA    1 
ATOM   14018 C  C     . SER B 1  706  ? 21.966  33.890  72.328  1.00 13.75 ? 704  SER B C     1 
ATOM   14019 O  O     . SER B 1  706  ? 23.063  33.477  71.919  1.00 15.06 ? 704  SER B O     1 
ATOM   14020 C  CB    . SER B 1  706  ? 19.850  33.511  71.017  1.00 14.98 ? 704  SER B CB    1 
ATOM   14021 O  OG    . SER B 1  706  ? 20.360  32.479  70.196  1.00 14.04 ? 704  SER B OG    1 
ATOM   14022 N  N     . PRO B 1  707  ? 21.637  33.853  73.620  1.00 14.44 ? 705  PRO B N     1 
ATOM   14023 C  CA    . PRO B 1  707  ? 22.548  33.315  74.632  1.00 15.19 ? 705  PRO B CA    1 
ATOM   14024 C  C     . PRO B 1  707  ? 22.356  31.810  74.767  1.00 16.16 ? 705  PRO B C     1 
ATOM   14025 O  O     . PRO B 1  707  ? 21.381  31.235  74.276  1.00 16.48 ? 705  PRO B O     1 
ATOM   14026 C  CB    . PRO B 1  707  ? 22.095  34.051  75.905  1.00 15.48 ? 705  PRO B CB    1 
ATOM   14027 C  CG    . PRO B 1  707  ? 20.611  34.151  75.729  1.00 15.18 ? 705  PRO B CG    1 
ATOM   14028 C  CD    . PRO B 1  707  ? 20.426  34.434  74.235  1.00 15.92 ? 705  PRO B CD    1 
ATOM   14029 N  N     . TRP B 1  708  ? 23.329  31.168  75.423  1.00 14.63 ? 706  TRP B N     1 
ATOM   14030 C  CA    . TRP B 1  708  ? 23.212  29.725  75.615  1.00 15.71 ? 706  TRP B CA    1 
ATOM   14031 C  C     . TRP B 1  708  ? 22.204  29.359  76.696  1.00 15.82 ? 706  TRP B C     1 
ATOM   14032 O  O     . TRP B 1  708  ? 21.682  28.243  76.678  1.00 15.09 ? 706  TRP B O     1 
ATOM   14033 C  CB    . TRP B 1  708  ? 24.572  29.092  75.979  1.00 14.59 ? 706  TRP B CB    1 
ATOM   14034 C  CG    . TRP B 1  708  ? 24.954  29.346  77.406  1.00 16.67 ? 706  TRP B CG    1 
ATOM   14035 C  CD1   . TRP B 1  708  ? 25.717  30.376  77.888  1.00 16.28 ? 706  TRP B CD1   1 
ATOM   14036 C  CD2   . TRP B 1  708  ? 24.539  28.587  78.548  1.00 16.80 ? 706  TRP B CD2   1 
ATOM   14037 N  NE1   . TRP B 1  708  ? 25.794  30.304  79.254  1.00 17.76 ? 706  TRP B NE1   1 
ATOM   14038 C  CE2   . TRP B 1  708  ? 25.078  29.217  79.685  1.00 17.30 ? 706  TRP B CE2   1 
ATOM   14039 C  CE3   . TRP B 1  708  ? 23.773  27.436  78.716  1.00 14.99 ? 706  TRP B CE3   1 
ATOM   14040 C  CZ2   . TRP B 1  708  ? 24.870  28.733  80.975  1.00 17.11 ? 706  TRP B CZ2   1 
ATOM   14041 C  CZ3   . TRP B 1  708  ? 23.552  26.959  80.004  1.00 17.58 ? 706  TRP B CZ3   1 
ATOM   14042 C  CH2   . TRP B 1  708  ? 24.105  27.602  81.116  1.00 17.10 ? 706  TRP B CH2   1 
ATOM   14043 N  N     . ASN B 1  709  ? 21.934  30.252  77.651  1.00 15.13 ? 707  ASN B N     1 
ATOM   14044 C  CA    . ASN B 1  709  ? 21.368  29.778  78.909  1.00 16.52 ? 707  ASN B CA    1 
ATOM   14045 C  C     . ASN B 1  709  ? 19.872  29.550  78.843  1.00 17.38 ? 707  ASN B C     1 
ATOM   14046 O  O     . ASN B 1  709  ? 19.345  28.795  79.666  1.00 17.18 ? 707  ASN B O     1 
ATOM   14047 C  CB    . ASN B 1  709  ? 21.691  30.757  80.041  1.00 15.00 ? 707  ASN B CB    1 
ATOM   14048 C  CG    . ASN B 1  709  ? 20.917  32.044  79.922  1.00 16.82 ? 707  ASN B CG    1 
ATOM   14049 O  OD1   . ASN B 1  709  ? 21.170  32.846  79.044  1.00 17.95 ? 707  ASN B OD1   1 
ATOM   14050 N  ND2   . ASN B 1  709  ? 19.939  32.234  80.800  1.00 16.16 ? 707  ASN B ND2   1 
ATOM   14051 N  N     . PHE B 1  710  ? 19.180  30.201  77.909  1.00 16.18 ? 708  PHE B N     1 
ATOM   14052 C  CA    . PHE B 1  710  ? 17.794  29.896  77.573  1.00 15.30 ? 708  PHE B CA    1 
ATOM   14053 C  C     . PHE B 1  710  ? 17.810  29.510  76.098  1.00 14.00 ? 708  PHE B C     1 
ATOM   14054 O  O     . PHE B 1  710  ? 17.382  30.282  75.229  1.00 14.01 ? 708  PHE B O     1 
ATOM   14055 C  CB    . PHE B 1  710  ? 16.859  31.074  77.846  1.00 15.07 ? 708  PHE B CB    1 
ATOM   14056 C  CG    . PHE B 1  710  ? 16.791  31.495  79.297  1.00 18.16 ? 708  PHE B CG    1 
ATOM   14057 C  CD1   . PHE B 1  710  ? 16.718  30.555  80.321  1.00 18.31 ? 708  PHE B CD1   1 
ATOM   14058 C  CD2   . PHE B 1  710  ? 16.774  32.840  79.632  1.00 17.68 ? 708  PHE B CD2   1 
ATOM   14059 C  CE1   . PHE B 1  710  ? 16.635  30.952  81.652  1.00 19.65 ? 708  PHE B CE1   1 
ATOM   14060 C  CE2   . PHE B 1  710  ? 16.694  33.253  80.963  1.00 18.83 ? 708  PHE B CE2   1 
ATOM   14061 C  CZ    . PHE B 1  710  ? 16.630  32.311  81.975  1.00 18.36 ? 708  PHE B CZ    1 
ATOM   14062 N  N     . PRO B 1  711  ? 18.307  28.304  75.788  1.00 16.55 ? 709  PRO B N     1 
ATOM   14063 C  CA    . PRO B 1  711  ? 18.736  28.009  74.413  1.00 15.58 ? 709  PRO B CA    1 
ATOM   14064 C  C     . PRO B 1  711  ? 17.605  27.785  73.432  1.00 15.63 ? 709  PRO B C     1 
ATOM   14065 O  O     . PRO B 1  711  ? 17.866  27.802  72.223  1.00 15.53 ? 709  PRO B O     1 
ATOM   14066 C  CB    . PRO B 1  711  ? 19.574  26.734  74.581  1.00 16.43 ? 709  PRO B CB    1 
ATOM   14067 C  CG    . PRO B 1  711  ? 18.945  26.061  75.771  1.00 16.62 ? 709  PRO B CG    1 
ATOM   14068 C  CD    . PRO B 1  711  ? 18.608  27.188  76.705  1.00 14.47 ? 709  PRO B CD    1 
ATOM   14069 N  N     . LEU B 1  712  ? 16.380  27.546  73.901  1.00 14.84 ? 710  LEU B N     1 
ATOM   14070 C  CA    . LEU B 1  712  ? 15.222  27.497  73.015  1.00 14.86 ? 710  LEU B CA    1 
ATOM   14071 C  C     . LEU B 1  712  ? 14.295  28.689  73.182  1.00 14.71 ? 710  LEU B C     1 
ATOM   14072 O  O     . LEU B 1  712  ? 13.784  29.205  72.188  1.00 15.27 ? 710  LEU B O     1 
ATOM   14073 C  CB    . LEU B 1  712  ? 14.421  26.200  73.231  1.00 13.41 ? 710  LEU B CB    1 
ATOM   14074 C  CG    . LEU B 1  712  ? 13.243  26.009  72.250  1.00 12.51 ? 710  LEU B CG    1 
ATOM   14075 C  CD1   . LEU B 1  712  ? 13.702  25.934  70.795  1.00 13.20 ? 710  LEU B CD1   1 
ATOM   14076 C  CD2   . LEU B 1  712  ? 12.466  24.753  72.622  1.00 16.95 ? 710  LEU B CD2   1 
ATOM   14077 N  N     . ALA B 1  713  ? 14.098  29.167  74.413  1.00 13.73 ? 711  ALA B N     1 
ATOM   14078 C  CA    . ALA B 1  713  ? 13.078  30.186  74.657  1.00 14.85 ? 711  ALA B CA    1 
ATOM   14079 C  C     . ALA B 1  713  ? 13.467  31.528  74.047  1.00 14.49 ? 711  ALA B C     1 
ATOM   14080 O  O     . ALA B 1  713  ? 12.727  32.091  73.235  1.00 14.38 ? 711  ALA B O     1 
ATOM   14081 C  CB    . ALA B 1  713  ? 12.834  30.335  76.160  1.00 14.96 ? 711  ALA B CB    1 
ATOM   14082 N  N     . ILE B 1  714  ? 14.617  32.083  74.444  1.00 15.11 ? 712  ILE B N     1 
ATOM   14083 C  CA    . ILE B 1  714  ? 14.989  33.386  73.895  1.00 13.93 ? 712  ILE B CA    1 
ATOM   14084 C  C     . ILE B 1  714  ? 15.341  33.255  72.416  1.00 15.62 ? 712  ILE B C     1 
ATOM   14085 O  O     . ILE B 1  714  ? 15.010  34.128  71.598  1.00 13.51 ? 712  ILE B O     1 
ATOM   14086 C  CB    . ILE B 1  714  ? 16.140  33.997  74.709  1.00 16.36 ? 712  ILE B CB    1 
ATOM   14087 C  CG1   . ILE B 1  714  ? 15.595  34.407  76.076  1.00 16.37 ? 712  ILE B CG1   1 
ATOM   14088 C  CG2   . ILE B 1  714  ? 16.745  35.175  73.947  1.00 14.87 ? 712  ILE B CG2   1 
ATOM   14089 C  CD1   . ILE B 1  714  ? 16.524  35.291  76.885  1.00 18.78 ? 712  ILE B CD1   1 
ATOM   14090 N  N     . PHE B 1  715  ? 16.016  32.165  72.051  1.00 15.06 ? 713  PHE B N     1 
ATOM   14091 C  CA    . PHE B 1  715  ? 16.265  31.867  70.644  1.00 12.84 ? 713  PHE B CA    1 
ATOM   14092 C  C     . PHE B 1  715  ? 14.985  31.983  69.827  1.00 13.14 ? 713  PHE B C     1 
ATOM   14093 O  O     . PHE B 1  715  ? 14.936  32.709  68.823  1.00 13.41 ? 713  PHE B O     1 
ATOM   14094 C  CB    . PHE B 1  715  ? 16.848  30.462  70.519  1.00 13.37 ? 713  PHE B CB    1 
ATOM   14095 C  CG    . PHE B 1  715  ? 17.082  30.043  69.099  1.00 14.02 ? 713  PHE B CG    1 
ATOM   14096 C  CD1   . PHE B 1  715  ? 18.206  30.485  68.410  1.00 13.91 ? 713  PHE B CD1   1 
ATOM   14097 C  CD2   . PHE B 1  715  ? 16.171  29.226  68.447  1.00 14.56 ? 713  PHE B CD2   1 
ATOM   14098 C  CE1   . PHE B 1  715  ? 18.430  30.108  67.105  1.00 14.82 ? 713  PHE B CE1   1 
ATOM   14099 C  CE2   . PHE B 1  715  ? 16.383  28.850  67.116  1.00 13.96 ? 713  PHE B CE2   1 
ATOM   14100 C  CZ    . PHE B 1  715  ? 17.516  29.293  66.454  1.00 14.08 ? 713  PHE B CZ    1 
ATOM   14101 N  N     . THR B 1  716  ? 13.923  31.301  70.276  1.00 12.52 ? 714  THR B N     1 
ATOM   14102 C  CA    . THR B 1  716  ? 12.659  31.285  69.538  1.00 13.78 ? 714  THR B CA    1 
ATOM   14103 C  C     . THR B 1  716  ? 11.953  32.630  69.604  1.00 13.75 ? 714  THR B C     1 
ATOM   14104 O  O     . THR B 1  716  ? 11.385  33.080  68.603  1.00 14.19 ? 714  THR B O     1 
ATOM   14105 C  CB    . THR B 1  716  ? 11.739  30.187  70.081  1.00 13.45 ? 714  THR B CB    1 
ATOM   14106 O  OG1   . THR B 1  716  ? 12.373  28.912  69.906  1.00 14.16 ? 714  THR B OG1   1 
ATOM   14107 C  CG2   . THR B 1  716  ? 10.395  30.193  69.328  1.00 14.04 ? 714  THR B CG2   1 
ATOM   14108 N  N     . GLY B 1  717  ? 11.954  33.270  70.777  1.00 13.52 ? 715  GLY B N     1 
ATOM   14109 C  CA    . GLY B 1  717  ? 11.256  34.542  70.920  1.00 13.53 ? 715  GLY B CA    1 
ATOM   14110 C  C     . GLY B 1  717  ? 11.765  35.604  69.965  1.00 12.46 ? 715  GLY B C     1 
ATOM   14111 O  O     . GLY B 1  717  ? 10.982  36.258  69.275  1.00 14.03 ? 715  GLY B O     1 
ATOM   14112 N  N     . GLN B 1  718  ? 13.084  35.798  69.912  1.00 12.91 ? 716  GLN B N     1 
ATOM   14113 C  CA    . GLN B 1  718  ? 13.611  36.840  69.037  1.00 13.20 ? 716  GLN B CA    1 
ATOM   14114 C  C     . GLN B 1  718  ? 13.284  36.528  67.585  1.00 13.03 ? 716  GLN B C     1 
ATOM   14115 O  O     . GLN B 1  718  ? 12.851  37.408  66.837  1.00 12.66 ? 716  GLN B O     1 
ATOM   14116 C  CB    . GLN B 1  718  ? 15.130  36.976  69.199  1.00 13.03 ? 716  GLN B CB    1 
ATOM   14117 C  CG    . GLN B 1  718  ? 15.572  37.339  70.622  1.00 13.84 ? 716  GLN B CG    1 
ATOM   14118 C  CD    . GLN B 1  718  ? 17.060  37.641  70.722  1.00 14.71 ? 716  GLN B CD    1 
ATOM   14119 O  OE1   . GLN B 1  718  ? 17.456  38.632  71.336  1.00 16.67 ? 716  GLN B OE1   1 
ATOM   14120 N  NE2   . GLN B 1  718  ? 17.889  36.797  70.110  1.00 13.90 ? 716  GLN B NE2   1 
ATOM   14121 N  N     . ILE B 1  719  ? 13.466  35.268  67.185  1.00 13.02 ? 717  ILE B N     1 
ATOM   14122 C  CA    . ILE B 1  719  ? 13.242  34.882  65.797  1.00 14.46 ? 717  ILE B CA    1 
ATOM   14123 C  C     . ILE B 1  719  ? 11.783  35.028  65.430  1.00 14.00 ? 717  ILE B C     1 
ATOM   14124 O  O     . ILE B 1  719  ? 11.441  35.537  64.355  1.00 14.14 ? 717  ILE B O     1 
ATOM   14125 C  CB    . ILE B 1  719  ? 13.733  33.445  65.575  1.00 13.17 ? 717  ILE B CB    1 
ATOM   14126 C  CG1   . ILE B 1  719  ? 15.256  33.428  65.623  1.00 13.95 ? 717  ILE B CG1   1 
ATOM   14127 C  CG2   . ILE B 1  719  ? 13.262  32.909  64.259  1.00 18.03 ? 717  ILE B CG2   1 
ATOM   14128 C  CD1   . ILE B 1  719  ? 15.776  32.028  65.663  1.00 20.78 ? 717  ILE B CD1   1 
ATOM   14129 N  N     . ALA B 1  720  ? 10.900  34.579  66.314  1.00 13.70 ? 718  ALA B N     1 
ATOM   14130 C  CA    . ALA B 1  720  ? 9.477   34.618  66.019  1.00 13.42 ? 718  ALA B CA    1 
ATOM   14131 C  C     . ALA B 1  720  ? 9.005   36.052  65.830  1.00 14.37 ? 718  ALA B C     1 
ATOM   14132 O  O     . ALA B 1  720  ? 8.220   36.351  64.912  1.00 14.53 ? 718  ALA B O     1 
ATOM   14133 C  CB    . ALA B 1  720  ? 8.708   33.931  67.151  1.00 14.49 ? 718  ALA B CB    1 
ATOM   14134 N  N     . ALA B 1  721  ? 9.461   36.949  66.702  1.00 13.11 ? 719  ALA B N     1 
ATOM   14135 C  CA    . ALA B 1  721  ? 9.049   38.343  66.618  1.00 14.66 ? 719  ALA B CA    1 
ATOM   14136 C  C     . ALA B 1  721  ? 9.535   38.969  65.324  1.00 12.86 ? 719  ALA B C     1 
ATOM   14137 O  O     . ALA B 1  721  ? 8.769   39.631  64.620  1.00 14.20 ? 719  ALA B O     1 
ATOM   14138 C  CB    . ALA B 1  721  ? 9.568   39.119  67.829  1.00 14.30 ? 719  ALA B CB    1 
ATOM   14139 N  N     . ALA B 1  722  ? 10.810  38.768  64.986  1.00 13.38 ? 720  ALA B N     1 
ATOM   14140 C  CA    . ALA B 1  722  ? 11.318  39.334  63.744  1.00 12.07 ? 720  ALA B CA    1 
ATOM   14141 C  C     . ALA B 1  722  ? 10.554  38.784  62.541  1.00 14.53 ? 720  ALA B C     1 
ATOM   14142 O  O     . ALA B 1  722  ? 10.148  39.543  61.654  1.00 14.22 ? 720  ALA B O     1 
ATOM   14143 C  CB    . ALA B 1  722  ? 12.822  39.054  63.623  1.00 13.09 ? 720  ALA B CB    1 
ATOM   14144 N  N     . LEU B 1  723  ? 10.333  37.469  62.514  1.00 14.53 ? 721  LEU B N     1 
ATOM   14145 C  CA    . LEU B 1  723  ? 9.613   36.851  61.404  1.00 14.13 ? 721  LEU B CA    1 
ATOM   14146 C  C     . LEU B 1  723  ? 8.199   37.386  61.282  1.00 13.29 ? 721  LEU B C     1 
ATOM   14147 O  O     . LEU B 1  723  ? 7.741   37.698  60.172  1.00 16.33 ? 721  LEU B O     1 
ATOM   14148 C  CB    . LEU B 1  723  ? 9.559   35.337  61.585  1.00 14.09 ? 721  LEU B CB    1 
ATOM   14149 C  CG    . LEU B 1  723  ? 10.865  34.585  61.351  1.00 15.13 ? 721  LEU B CG    1 
ATOM   14150 C  CD1   . LEU B 1  723  ? 10.683  33.149  61.816  1.00 14.56 ? 721  LEU B CD1   1 
ATOM   14151 C  CD2   . LEU B 1  723  ? 11.205  34.620  59.887  1.00 14.84 ? 721  LEU B CD2   1 
ATOM   14152 N  N     . VAL B 1  724  ? 7.455   37.420  62.392  1.00 13.54 ? 722  VAL B N     1 
ATOM   14153 C  CA    . VAL B 1  724  ? 6.042   37.760  62.270  1.00 13.07 ? 722  VAL B CA    1 
ATOM   14154 C  C     . VAL B 1  724  ? 5.876   39.236  61.927  1.00 15.27 ? 722  VAL B C     1 
ATOM   14155 O  O     . VAL B 1  724  ? 4.887   39.629  61.293  1.00 16.91 ? 722  VAL B O     1 
ATOM   14156 C  CB    . VAL B 1  724  ? 5.278   37.348  63.547  1.00 13.70 ? 722  VAL B CB    1 
ATOM   14157 C  CG1   . VAL B 1  724  ? 5.494   38.354  64.692  1.00 16.56 ? 722  VAL B CG1   1 
ATOM   14158 C  CG2   . VAL B 1  724  ? 3.789   37.149  63.242  1.00 13.84 ? 722  VAL B CG2   1 
ATOM   14159 N  N     . ALA B 1  725  ? 6.852   40.063  62.289  1.00 15.58 ? 723  ALA B N     1 
ATOM   14160 C  CA    . ALA B 1  725  ? 6.873   41.453  61.857  1.00 15.50 ? 723  ALA B CA    1 
ATOM   14161 C  C     . ALA B 1  725  ? 7.222   41.606  60.378  1.00 17.48 ? 723  ALA B C     1 
ATOM   14162 O  O     . ALA B 1  725  ? 7.219   42.734  59.875  1.00 18.54 ? 723  ALA B O     1 
ATOM   14163 C  CB    . ALA B 1  725  ? 7.859   42.237  62.730  1.00 14.52 ? 723  ALA B CB    1 
ATOM   14164 N  N     . GLY B 1  726  ? 7.524   40.521  59.671  1.00 15.81 ? 724  GLY B N     1 
ATOM   14165 C  CA    . GLY B 1  726  ? 7.732   40.590  58.240  1.00 15.33 ? 724  GLY B CA    1 
ATOM   14166 C  C     . GLY B 1  726  ? 9.174   40.584  57.805  1.00 17.25 ? 724  GLY B C     1 
ATOM   14167 O  O     . GLY B 1  726  ? 9.452   40.898  56.638  1.00 18.44 ? 724  GLY B O     1 
ATOM   14168 N  N     . ASN B 1  727  ? 10.101  40.221  58.699  1.00 14.95 ? 725  ASN B N     1 
ATOM   14169 C  CA    . ASN B 1  727  ? 11.532  40.282  58.448  1.00 15.34 ? 725  ASN B CA    1 
ATOM   14170 C  C     . ASN B 1  727  ? 12.091  38.882  58.290  1.00 15.29 ? 725  ASN B C     1 
ATOM   14171 O  O     . ASN B 1  727  ? 11.810  38.021  59.135  1.00 15.83 ? 725  ASN B O     1 
ATOM   14172 C  CB    . ASN B 1  727  ? 12.257  40.977  59.605  1.00 15.20 ? 725  ASN B CB    1 
ATOM   14173 C  CG    . ASN B 1  727  ? 11.666  42.341  59.939  1.00 14.24 ? 725  ASN B CG    1 
ATOM   14174 O  OD1   . ASN B 1  727  ? 11.961  43.338  59.273  1.00 16.26 ? 725  ASN B OD1   1 
ATOM   14175 N  ND2   . ASN B 1  727  ? 10.860  42.396  61.001  1.00 14.49 ? 725  ASN B ND2   1 
ATOM   14176 N  N     . PRO B 1  728  ? 12.880  38.617  57.247  1.00 15.43 ? 726  PRO B N     1 
ATOM   14177 C  CA    . PRO B 1  728  ? 13.636  37.369  57.214  1.00 15.33 ? 726  PRO B CA    1 
ATOM   14178 C  C     . PRO B 1  728  ? 14.716  37.423  58.279  1.00 15.51 ? 726  PRO B C     1 
ATOM   14179 O  O     . PRO B 1  728  ? 15.210  38.496  58.639  1.00 16.54 ? 726  PRO B O     1 
ATOM   14180 C  CB    . PRO B 1  728  ? 14.234  37.345  55.804  1.00 17.44 ? 726  PRO B CB    1 
ATOM   14181 C  CG    . PRO B 1  728  ? 14.378  38.786  55.446  1.00 18.27 ? 726  PRO B CG    1 
ATOM   14182 C  CD    . PRO B 1  728  ? 13.209  39.494  56.108  1.00 16.83 ? 726  PRO B CD    1 
ATOM   14183 N  N     . VAL B 1  729  ? 15.072  36.253  58.790  1.00 14.05 ? 727  VAL B N     1 
ATOM   14184 C  CA    . VAL B 1  729  ? 15.906  36.153  59.980  1.00 15.12 ? 727  VAL B CA    1 
ATOM   14185 C  C     . VAL B 1  729  ? 17.160  35.343  59.693  1.00 16.81 ? 727  VAL B C     1 
ATOM   14186 O  O     . VAL B 1  729  ? 17.104  34.265  59.083  1.00 14.93 ? 727  VAL B O     1 
ATOM   14187 C  CB    . VAL B 1  729  ? 15.122  35.518  61.138  1.00 13.90 ? 727  VAL B CB    1 
ATOM   14188 C  CG1   . VAL B 1  729  ? 16.080  35.099  62.273  1.00 14.95 ? 727  VAL B CG1   1 
ATOM   14189 C  CG2   . VAL B 1  729  ? 14.080  36.495  61.639  1.00 14.27 ? 727  VAL B CG2   1 
ATOM   14190 N  N     . LEU B 1  730  ? 18.291  35.851  60.178  1.00 15.04 ? 728  LEU B N     1 
ATOM   14191 C  CA    . LEU B 1  730  ? 19.532  35.100  60.280  1.00 16.22 ? 728  LEU B CA    1 
ATOM   14192 C  C     . LEU B 1  730  ? 19.691  34.734  61.750  1.00 13.73 ? 728  LEU B C     1 
ATOM   14193 O  O     . LEU B 1  730  ? 19.908  35.610  62.588  1.00 16.61 ? 728  LEU B O     1 
ATOM   14194 C  CB    . LEU B 1  730  ? 20.726  35.924  59.797  1.00 14.93 ? 728  LEU B CB    1 
ATOM   14195 C  CG    . LEU B 1  730  ? 20.760  36.420  58.350  1.00 17.01 ? 728  LEU B CG    1 
ATOM   14196 C  CD1   . LEU B 1  730  ? 20.347  35.293  57.394  1.00 15.91 ? 728  LEU B CD1   1 
ATOM   14197 C  CD2   . LEU B 1  730  ? 19.867  37.652  58.153  1.00 17.39 ? 728  LEU B CD2   1 
ATOM   14198 N  N     . ALA B 1  731  ? 19.600  33.453  62.065  1.00 12.97 ? 729  ALA B N     1 
ATOM   14199 C  CA    . ALA B 1  731  ? 19.567  33.007  63.453  1.00 12.76 ? 729  ALA B CA    1 
ATOM   14200 C  C     . ALA B 1  731  ? 20.935  32.456  63.836  1.00 15.07 ? 729  ALA B C     1 
ATOM   14201 O  O     . ALA B 1  731  ? 21.376  31.438  63.295  1.00 14.41 ? 729  ALA B O     1 
ATOM   14202 C  CB    . ALA B 1  731  ? 18.475  31.957  63.637  1.00 14.89 ? 729  ALA B CB    1 
ATOM   14203 N  N     . LYS B 1  732  ? 21.602  33.136  64.773  1.00 13.46 ? 730  LYS B N     1 
ATOM   14204 C  CA    . LYS B 1  732  ? 22.933  32.767  65.242  1.00 14.61 ? 730  LYS B CA    1 
ATOM   14205 C  C     . LYS B 1  732  ? 22.843  32.331  66.698  1.00 13.98 ? 730  LYS B C     1 
ATOM   14206 O  O     . LYS B 1  732  ? 22.896  33.167  67.614  1.00 14.86 ? 730  LYS B O     1 
ATOM   14207 C  CB    . LYS B 1  732  ? 23.906  33.930  65.077  1.00 14.47 ? 730  LYS B CB    1 
ATOM   14208 C  CG    . LYS B 1  732  ? 25.335  33.493  64.733  1.00 14.80 ? 730  LYS B CG    1 
ATOM   14209 C  CD    . LYS B 1  732  ? 25.975  32.633  65.814  1.00 16.48 ? 730  LYS B CD    1 
ATOM   14210 C  CE    . LYS B 1  732  ? 26.296  33.423  67.060  1.00 14.08 ? 730  LYS B CE    1 
ATOM   14211 N  NZ    . LYS B 1  732  ? 26.924  32.510  68.068  1.00 15.94 ? 730  LYS B NZ    1 
ATOM   14212 N  N     . PRO B 1  733  ? 22.710  31.041  66.960  1.00 15.01 ? 731  PRO B N     1 
ATOM   14213 C  CA    . PRO B 1  733  ? 22.613  30.568  68.339  1.00 14.84 ? 731  PRO B CA    1 
ATOM   14214 C  C     . PRO B 1  733  ? 23.976  30.589  69.000  1.00 15.15 ? 731  PRO B C     1 
ATOM   14215 O  O     . PRO B 1  733  ? 25.022  30.602  68.343  1.00 14.97 ? 731  PRO B O     1 
ATOM   14216 C  CB    . PRO B 1  733  ? 22.122  29.131  68.173  1.00 14.49 ? 731  PRO B CB    1 
ATOM   14217 C  CG    . PRO B 1  733  ? 22.814  28.686  66.881  1.00 14.92 ? 731  PRO B CG    1 
ATOM   14218 C  CD    . PRO B 1  733  ? 22.724  29.932  65.989  1.00 16.59 ? 731  PRO B CD    1 
ATOM   14219 N  N     . ALA B 1  734  ? 23.945  30.587  70.323  1.00 14.56 ? 732  ALA B N     1 
ATOM   14220 C  CA    . ALA B 1  734  ? 25.181  30.499  71.089  1.00 14.71 ? 732  ALA B CA    1 
ATOM   14221 C  C     . ALA B 1  734  ? 25.965  29.251  70.701  1.00 17.51 ? 732  ALA B C     1 
ATOM   14222 O  O     . ALA B 1  734  ? 25.394  28.203  70.391  1.00 17.34 ? 732  ALA B O     1 
ATOM   14223 C  CB    . ALA B 1  734  ? 24.868  30.462  72.582  1.00 15.13 ? 732  ALA B CB    1 
ATOM   14224 N  N     . GLU B 1  735  ? 27.296  29.358  70.760  1.00 14.14 ? 733  GLU B N     1 
ATOM   14225 C  CA    . GLU B 1  735  ? 28.120  28.232  70.336  1.00 16.91 ? 733  GLU B CA    1 
ATOM   14226 C  C     . GLU B 1  735  ? 27.959  27.027  71.252  1.00 16.14 ? 733  GLU B C     1 
ATOM   14227 O  O     . GLU B 1  735  ? 28.175  25.900  70.806  1.00 14.42 ? 733  GLU B O     1 
ATOM   14228 C  CB    . GLU B 1  735  ? 29.590  28.656  70.247  1.00 20.02 ? 733  GLU B CB    1 
ATOM   14229 C  CG    . GLU B 1  735  ? 30.154  29.284  71.514  1.00 21.23 ? 733  GLU B CG    1 
ATOM   14230 C  CD    . GLU B 1  735  ? 30.029  30.804  71.554  1.00 23.65 ? 733  GLU B CD    1 
ATOM   14231 O  OE1   . GLU B 1  735  ? 29.056  31.360  70.992  1.00 19.59 ? 733  GLU B OE1   1 
ATOM   14232 O  OE2   . GLU B 1  735  ? 30.912  31.449  72.166  1.00 25.12 ? 733  GLU B OE2   1 
ATOM   14233 N  N     . GLU B 1  736  ? 27.540  27.242  72.504  1.00 16.01 ? 734  GLU B N     1 
ATOM   14234 C  CA    . GLU B 1  736  ? 27.379  26.138  73.443  1.00 16.02 ? 734  GLU B CA    1 
ATOM   14235 C  C     . GLU B 1  736  ? 26.153  25.271  73.146  1.00 17.79 ? 734  GLU B C     1 
ATOM   14236 O  O     . GLU B 1  736  ? 26.130  24.090  73.513  1.00 17.56 ? 734  GLU B O     1 
ATOM   14237 C  CB    . GLU B 1  736  ? 27.280  26.681  74.867  1.00 16.83 ? 734  GLU B CB    1 
ATOM   14238 C  CG    . GLU B 1  736  ? 28.525  27.364  75.387  1.00 17.26 ? 734  GLU B CG    1 
ATOM   14239 C  CD    . GLU B 1  736  ? 28.534  28.873  75.162  1.00 18.35 ? 734  GLU B CD    1 
ATOM   14240 O  OE1   . GLU B 1  736  ? 27.726  29.386  74.358  1.00 16.99 ? 734  GLU B OE1   1 
ATOM   14241 O  OE2   . GLU B 1  736  ? 29.366  29.546  75.809  1.00 23.70 ? 734  GLU B OE2   1 
ATOM   14242 N  N     . THR B 1  737  ? 25.107  25.830  72.537  1.00 15.43 ? 735  THR B N     1 
ATOM   14243 C  CA    . THR B 1  737  ? 23.804  25.161  72.469  1.00 16.75 ? 735  THR B CA    1 
ATOM   14244 C  C     . THR B 1  737  ? 23.219  25.234  71.066  1.00 14.73 ? 735  THR B C     1 
ATOM   14245 O  O     . THR B 1  737  ? 22.081  25.673  70.874  1.00 16.07 ? 735  THR B O     1 
ATOM   14246 C  CB    . THR B 1  737  ? 22.838  25.766  73.487  1.00 15.96 ? 735  THR B CB    1 
ATOM   14247 O  OG1   . THR B 1  737  ? 22.793  27.186  73.311  1.00 14.71 ? 735  THR B OG1   1 
ATOM   14248 C  CG2   . THR B 1  737  ? 23.307  25.458  74.907  1.00 15.86 ? 735  THR B CG2   1 
ATOM   14249 N  N     . PRO B 1  738  ? 23.952  24.758  70.055  1.00 16.00 ? 736  PRO B N     1 
ATOM   14250 C  CA    . PRO B 1  738  ? 23.415  24.829  68.686  1.00 14.47 ? 736  PRO B CA    1 
ATOM   14251 C  C     . PRO B 1  738  ? 22.333  23.807  68.389  1.00 15.66 ? 736  PRO B C     1 
ATOM   14252 O  O     . PRO B 1  738  ? 21.541  24.038  67.464  1.00 15.67 ? 736  PRO B O     1 
ATOM   14253 C  CB    . PRO B 1  738  ? 24.651  24.573  67.820  1.00 13.79 ? 736  PRO B CB    1 
ATOM   14254 C  CG    . PRO B 1  738  ? 25.465  23.619  68.655  1.00 16.61 ? 736  PRO B CG    1 
ATOM   14255 C  CD    . PRO B 1  738  ? 25.279  24.104  70.082  1.00 16.58 ? 736  PRO B CD    1 
ATOM   14256 N  N     . LEU B 1  739  ? 22.292  22.677  69.103  1.00 14.85 ? 737  LEU B N     1 
ATOM   14257 C  CA    . LEU B 1  739  ? 21.412  21.589  68.677  1.00 16.15 ? 737  LEU B CA    1 
ATOM   14258 C  C     . LEU B 1  739  ? 19.945  21.943  68.879  1.00 17.11 ? 737  LEU B C     1 
ATOM   14259 O  O     . LEU B 1  739  ? 19.119  21.719  67.983  1.00 15.70 ? 737  LEU B O     1 
ATOM   14260 C  CB    . LEU B 1  739  ? 21.764  20.300  69.422  1.00 15.06 ? 737  LEU B CB    1 
ATOM   14261 C  CG    . LEU B 1  739  ? 23.204  19.841  69.200  1.00 15.64 ? 737  LEU B CG    1 
ATOM   14262 C  CD1   . LEU B 1  739  ? 23.465  18.608  70.044  1.00 16.48 ? 737  LEU B CD1   1 
ATOM   14263 C  CD2   . LEU B 1  739  ? 23.468  19.551  67.721  1.00 15.73 ? 737  LEU B CD2   1 
ATOM   14264 N  N     . ILE B 1  740  ? 19.586  22.457  70.058  1.00 15.61 ? 738  ILE B N     1 
ATOM   14265 C  CA    . ILE B 1  740  ? 18.180  22.795  70.275  1.00 13.31 ? 738  ILE B CA    1 
ATOM   14266 C  C     . ILE B 1  740  ? 17.784  23.962  69.383  1.00 14.97 ? 738  ILE B C     1 
ATOM   14267 O  O     . ILE B 1  740  ? 16.636  24.046  68.938  1.00 15.64 ? 738  ILE B O     1 
ATOM   14268 C  CB    . ILE B 1  740  ? 17.904  23.077  71.768  1.00 17.52 ? 738  ILE B CB    1 
ATOM   14269 C  CG1   . ILE B 1  740  ? 16.397  23.277  72.021  1.00 15.72 ? 738  ILE B CG1   1 
ATOM   14270 C  CG2   . ILE B 1  740  ? 18.710  24.271  72.248  1.00 16.96 ? 738  ILE B CG2   1 
ATOM   14271 C  CD1   . ILE B 1  740  ? 15.560  22.009  71.780  1.00 18.28 ? 738  ILE B CD1   1 
ATOM   14272 N  N     . ALA B 1  741  ? 18.730  24.856  69.075  1.00 15.25 ? 739  ALA B N     1 
ATOM   14273 C  CA    . ALA B 1  741  ? 18.451  25.949  68.145  1.00 15.02 ? 739  ALA B CA    1 
ATOM   14274 C  C     . ALA B 1  741  ? 18.131  25.406  66.760  1.00 16.13 ? 739  ALA B C     1 
ATOM   14275 O  O     . ALA B 1  741  ? 17.153  25.832  66.128  1.00 15.44 ? 739  ALA B O     1 
ATOM   14276 C  CB    . ALA B 1  741  ? 19.645  26.911  68.085  1.00 13.82 ? 739  ALA B CB    1 
ATOM   14277 N  N     . ALA B 1  742  ? 18.944  24.454  66.275  1.00 15.92 ? 740  ALA B N     1 
ATOM   14278 C  CA    . ALA B 1  742  ? 18.672  23.823  64.985  1.00 17.21 ? 740  ALA B CA    1 
ATOM   14279 C  C     . ALA B 1  742  ? 17.282  23.200  64.969  1.00 16.10 ? 740  ALA B C     1 
ATOM   14280 O  O     . ALA B 1  742  ? 16.570  23.271  63.959  1.00 15.58 ? 740  ALA B O     1 
ATOM   14281 C  CB    . ALA B 1  742  ? 19.728  22.759  64.675  1.00 16.34 ? 740  ALA B CB    1 
ATOM   14282 N  N     . GLU B 1  743  ? 16.883  22.588  66.083  1.00 16.91 ? 741  GLU B N     1 
ATOM   14283 C  CA    . GLU B 1  743  ? 15.568  21.962  66.151  1.00 16.53 ? 741  GLU B CA    1 
ATOM   14284 C  C     . GLU B 1  743  ? 14.471  23.011  66.123  1.00 14.04 ? 741  GLU B C     1 
ATOM   14285 O  O     . GLU B 1  743  ? 13.441  22.823  65.460  1.00 16.72 ? 741  GLU B O     1 
ATOM   14286 C  CB    . GLU B 1  743  ? 15.476  21.094  67.408  1.00 18.81 ? 741  GLU B CB    1 
ATOM   14287 C  CG    . GLU B 1  743  ? 14.134  20.403  67.579  1.00 16.91 ? 741  GLU B CG    1 
ATOM   14288 C  CD    . GLU B 1  743  ? 13.875  19.312  66.549  1.00 20.43 ? 741  GLU B CD    1 
ATOM   14289 O  OE1   . GLU B 1  743  ? 14.773  18.982  65.741  1.00 18.41 ? 741  GLU B OE1   1 
ATOM   14290 O  OE2   . GLU B 1  743  ? 12.754  18.775  66.555  1.00 21.07 ? 741  GLU B OE2   1 
ATOM   14291 N  N     . GLY B 1  744  ? 14.689  24.137  66.809  1.00 15.33 ? 742  GLY B N     1 
ATOM   14292 C  CA    . GLY B 1  744  ? 13.753  25.246  66.714  1.00 15.39 ? 742  GLY B CA    1 
ATOM   14293 C  C     . GLY B 1  744  ? 13.559  25.704  65.280  1.00 15.45 ? 742  GLY B C     1 
ATOM   14294 O  O     . GLY B 1  744  ? 12.437  25.960  64.845  1.00 15.05 ? 742  GLY B O     1 
ATOM   14295 N  N     . VAL B 1  745  ? 14.653  25.800  64.525  1.00 14.95 ? 743  VAL B N     1 
ATOM   14296 C  CA    . VAL B 1  745  ? 14.552  26.222  63.133  1.00 14.55 ? 743  VAL B CA    1 
ATOM   14297 C  C     . VAL B 1  745  ? 13.849  25.158  62.300  1.00 16.02 ? 743  VAL B C     1 
ATOM   14298 O  O     . VAL B 1  745  ? 13.036  25.486  61.421  1.00 17.21 ? 743  VAL B O     1 
ATOM   14299 C  CB    . VAL B 1  745  ? 15.942  26.575  62.578  1.00 15.62 ? 743  VAL B CB    1 
ATOM   14300 C  CG1   . VAL B 1  745  ? 15.916  26.678  61.054  1.00 14.23 ? 743  VAL B CG1   1 
ATOM   14301 C  CG2   . VAL B 1  745  ? 16.399  27.913  63.182  1.00 15.59 ? 743  VAL B CG2   1 
ATOM   14302 N  N     . ARG B 1  746  ? 14.128  23.874  62.563  1.00 15.48 ? 744  ARG B N     1 
ATOM   14303 C  CA    . ARG B 1  746  ? 13.385  22.823  61.862  1.00 15.06 ? 744  ARG B CA    1 
ATOM   14304 C  C     . ARG B 1  746  ? 11.886  23.006  62.063  1.00 14.57 ? 744  ARG B C     1 
ATOM   14305 O  O     . ARG B 1  746  ? 11.100  22.887  61.114  1.00 16.15 ? 744  ARG B O     1 
ATOM   14306 C  CB    . ARG B 1  746  ? 13.774  21.434  62.369  1.00 16.13 ? 744  ARG B CB    1 
ATOM   14307 C  CG    . ARG B 1  746  ? 15.156  20.962  61.984  1.00 18.05 ? 744  ARG B CG    1 
ATOM   14308 C  CD    . ARG B 1  746  ? 15.396  19.527  62.509  1.00 16.70 ? 744  ARG B CD    1 
ATOM   14309 N  NE    . ARG B 1  746  ? 16.796  19.161  62.353  1.00 19.39 ? 744  ARG B NE    1 
ATOM   14310 C  CZ    . ARG B 1  746  ? 17.703  19.260  63.316  1.00 15.77 ? 744  ARG B CZ    1 
ATOM   14311 N  NH1   . ARG B 1  746  ? 17.351  19.499  64.571  1.00 17.17 ? 744  ARG B NH1   1 
ATOM   14312 N  NH2   . ARG B 1  746  ? 18.992  19.118  63.009  1.00 17.85 ? 744  ARG B NH2   1 
ATOM   14313 N  N     . ILE B 1  747  ? 11.477  23.278  63.302  1.00 14.91 ? 745  ILE B N     1 
ATOM   14314 C  CA    . ILE B 1  747  ? 10.053  23.336  63.608  1.00 13.67 ? 745  ILE B CA    1 
ATOM   14315 C  C     . ILE B 1  747  ? 9.411   24.562  62.964  1.00 14.88 ? 745  ILE B C     1 
ATOM   14316 O  O     . ILE B 1  747  ? 8.294   24.494  62.424  1.00 15.22 ? 745  ILE B O     1 
ATOM   14317 C  CB    . ILE B 1  747  ? 9.865   23.311  65.137  1.00 15.23 ? 745  ILE B CB    1 
ATOM   14318 C  CG1   . ILE B 1  747  ? 10.150  21.897  65.652  1.00 16.72 ? 745  ILE B CG1   1 
ATOM   14319 C  CG2   . ILE B 1  747  ? 8.449   23.791  65.511  1.00 15.93 ? 745  ILE B CG2   1 
ATOM   14320 C  CD1   . ILE B 1  747  ? 10.143  21.788  67.160  1.00 16.93 ? 745  ILE B CD1   1 
ATOM   14321 N  N     . LEU B 1  748  ? 10.092  25.703  63.019  1.00 14.94 ? 746  LEU B N     1 
ATOM   14322 C  CA    . LEU B 1  748  ? 9.555   26.898  62.380  1.00 14.14 ? 746  LEU B CA    1 
ATOM   14323 C  C     . LEU B 1  748  ? 9.444   26.710  60.876  1.00 15.22 ? 746  LEU B C     1 
ATOM   14324 O  O     . LEU B 1  748  ? 8.456   27.125  60.268  1.00 14.59 ? 746  LEU B O     1 
ATOM   14325 C  CB    . LEU B 1  748  ? 10.414  28.117  62.706  1.00 15.63 ? 746  LEU B CB    1 
ATOM   14326 C  CG    . LEU B 1  748  ? 10.117  28.776  64.054  1.00 19.09 ? 746  LEU B CG    1 
ATOM   14327 C  CD1   . LEU B 1  748  ? 11.277  29.669  64.517  1.00 15.11 ? 746  LEU B CD1   1 
ATOM   14328 C  CD2   . LEU B 1  748  ? 8.857   29.577  63.930  1.00 20.44 ? 746  LEU B CD2   1 
ATOM   14329 N  N     . ARG B 1  749  ? 10.453  26.093  60.251  1.00 14.64 ? 747  ARG B N     1 
ATOM   14330 C  CA    . ARG B 1  749  ? 10.329  25.821  58.823  1.00 15.47 ? 747  ARG B CA    1 
ATOM   14331 C  C     . ARG B 1  749  ? 9.186   24.853  58.551  1.00 16.29 ? 747  ARG B C     1 
ATOM   14332 O  O     . ARG B 1  749  ? 8.421   25.036  57.593  1.00 15.50 ? 747  ARG B O     1 
ATOM   14333 C  CB    . ARG B 1  749  ? 11.643  25.268  58.279  1.00 15.84 ? 747  ARG B CB    1 
ATOM   14334 C  CG    . ARG B 1  749  ? 12.714  26.319  58.113  1.00 15.88 ? 747  ARG B CG    1 
ATOM   14335 C  CD    . ARG B 1  749  ? 13.900  25.732  57.366  1.00 17.06 ? 747  ARG B CD    1 
ATOM   14336 N  NE    . ARG B 1  749  ? 14.902  26.732  57.032  1.00 16.51 ? 747  ARG B NE    1 
ATOM   14337 C  CZ    . ARG B 1  749  ? 15.919  26.486  56.215  1.00 21.73 ? 747  ARG B CZ    1 
ATOM   14338 N  NH1   . ARG B 1  749  ? 16.045  25.316  55.605  1.00 24.91 ? 747  ARG B NH1   1 
ATOM   14339 N  NH2   . ARG B 1  749  ? 16.841  27.425  56.019  1.00 22.13 ? 747  ARG B NH2   1 
ATOM   14340 N  N     . GLU B 1  750  ? 9.056   23.810  59.379  1.00 15.76 ? 748  GLU B N     1 
ATOM   14341 C  CA    . GLU B 1  750  ? 7.972   22.857  59.175  1.00 17.45 ? 748  GLU B CA    1 
ATOM   14342 C  C     . GLU B 1  750  ? 6.624   23.544  59.299  1.00 15.20 ? 748  GLU B C     1 
ATOM   14343 O  O     . GLU B 1  750  ? 5.684   23.211  58.565  1.00 16.75 ? 748  GLU B O     1 
ATOM   14344 C  CB    . GLU B 1  750  ? 8.077   21.713  60.186  1.00 16.42 ? 748  GLU B CB    1 
ATOM   14345 C  CG    . GLU B 1  750  ? 7.041   20.643  59.983  1.00 18.19 ? 748  GLU B CG    1 
ATOM   14346 C  CD    . GLU B 1  750  ? 7.217   19.486  60.935  1.00 20.00 ? 748  GLU B CD    1 
ATOM   14347 O  OE1   . GLU B 1  750  ? 8.292   19.408  61.573  1.00 20.85 ? 748  GLU B OE1   1 
ATOM   14348 O  OE2   . GLU B 1  750  ? 6.281   18.670  61.037  1.00 21.01 ? 748  GLU B OE2   1 
ATOM   14349 N  N     . ALA B 1  751  ? 6.536   24.541  60.180  1.00 17.03 ? 749  ALA B N     1 
ATOM   14350 C  CA    . ALA B 1  751  ? 5.293   25.270  60.394  1.00 17.70 ? 749  ALA B CA    1 
ATOM   14351 C  C     . ALA B 1  751  ? 4.973   26.256  59.277  1.00 16.94 ? 749  ALA B C     1 
ATOM   14352 O  O     . ALA B 1  751  ? 3.903   26.872  59.318  1.00 17.17 ? 749  ALA B O     1 
ATOM   14353 C  CB    . ALA B 1  751  ? 5.360   26.024  61.721  1.00 16.12 ? 749  ALA B CB    1 
ATOM   14354 N  N     . GLY B 1  752  ? 5.870   26.455  58.314  1.00 15.87 ? 750  GLY B N     1 
ATOM   14355 C  CA    . GLY B 1  752  ? 5.554   27.309  57.185  1.00 17.78 ? 750  GLY B CA    1 
ATOM   14356 C  C     . GLY B 1  752  ? 6.520   28.444  56.909  1.00 17.96 ? 750  GLY B C     1 
ATOM   14357 O  O     . GLY B 1  752  ? 6.364   29.150  55.907  1.00 18.07 ? 750  GLY B O     1 
ATOM   14358 N  N     . ILE B 1  753  ? 7.522   28.647  57.767  1.00 16.01 ? 751  ILE B N     1 
ATOM   14359 C  CA    . ILE B 1  753  ? 8.475   29.725  57.515  1.00 15.24 ? 751  ILE B CA    1 
ATOM   14360 C  C     . ILE B 1  753  ? 9.373   29.285  56.362  1.00 17.85 ? 751  ILE B C     1 
ATOM   14361 O  O     . ILE B 1  753  ? 10.027  28.240  56.465  1.00 18.77 ? 751  ILE B O     1 
ATOM   14362 C  CB    . ILE B 1  753  ? 9.321   30.048  58.755  1.00 12.40 ? 751  ILE B CB    1 
ATOM   14363 C  CG1   . ILE B 1  753  ? 8.430   30.382  59.967  1.00 15.37 ? 751  ILE B CG1   1 
ATOM   14364 C  CG2   . ILE B 1  753  ? 10.256  31.194  58.427  1.00 15.09 ? 751  ILE B CG2   1 
ATOM   14365 C  CD1   . ILE B 1  753  ? 7.587   31.653  59.793  1.00 15.85 ? 751  ILE B CD1   1 
ATOM   14366 N  N     . PRO B 1  754  ? 9.437   30.037  55.263  1.00 16.38 ? 752  PRO B N     1 
ATOM   14367 C  CA    . PRO B 1  754  ? 10.252  29.612  54.119  1.00 16.55 ? 752  PRO B CA    1 
ATOM   14368 C  C     . PRO B 1  754  ? 11.725  29.532  54.490  1.00 17.39 ? 752  PRO B C     1 
ATOM   14369 O  O     . PRO B 1  754  ? 12.202  30.243  55.373  1.00 17.84 ? 752  PRO B O     1 
ATOM   14370 C  CB    . PRO B 1  754  ? 10.004  30.706  53.072  1.00 19.07 ? 752  PRO B CB    1 
ATOM   14371 C  CG    . PRO B 1  754  ? 8.733   31.391  53.511  1.00 22.81 ? 752  PRO B CG    1 
ATOM   14372 C  CD    . PRO B 1  754  ? 8.677   31.271  55.001  1.00 16.77 ? 752  PRO B CD    1 
ATOM   14373 N  N     . ALA B 1  755  ? 12.448  28.657  53.785  1.00 19.58 ? 753  ALA B N     1 
ATOM   14374 C  CA    . ALA B 1  755  ? 13.881  28.519  54.034  1.00 22.93 ? 753  ALA B CA    1 
ATOM   14375 C  C     . ALA B 1  755  ? 14.609  29.847  53.850  1.00 19.24 ? 753  ALA B C     1 
ATOM   14376 O  O     . ALA B 1  755  ? 15.528  30.171  54.609  1.00 19.77 ? 753  ALA B O     1 
ATOM   14377 C  CB    . ALA B 1  755  ? 14.471  27.449  53.116  1.00 22.85 ? 753  ALA B CB    1 
ATOM   14378 N  N     . SER B 1  756  ? 14.203  30.647  52.865  1.00 17.92 ? 754  SER B N     1 
ATOM   14379 C  CA    . SER B 1  756  ? 14.883  31.926  52.685  1.00 18.30 ? 754  SER B CA    1 
ATOM   14380 C  C     . SER B 1  756  ? 14.537  32.924  53.778  1.00 17.55 ? 754  SER B C     1 
ATOM   14381 O  O     . SER B 1  756  ? 15.273  33.897  53.966  1.00 19.57 ? 754  SER B O     1 
ATOM   14382 C  CB    . SER B 1  756  ? 14.544  32.524  51.329  1.00 19.12 ? 754  SER B CB    1 
ATOM   14383 O  OG    . SER B 1  756  ? 13.138  32.685  51.232  1.00 24.35 ? 754  SER B OG    1 
ATOM   14384 N  N     . ALA B 1  757  ? 13.434  32.721  54.487  1.00 14.81 ? 755  ALA B N     1 
ATOM   14385 C  CA    . ALA B 1  757  ? 13.078  33.621  55.571  1.00 15.22 ? 755  ALA B CA    1 
ATOM   14386 C  C     . ALA B 1  757  ? 13.736  33.263  56.898  1.00 15.79 ? 755  ALA B C     1 
ATOM   14387 O  O     . ALA B 1  757  ? 13.720  34.087  57.818  1.00 16.66 ? 755  ALA B O     1 
ATOM   14388 C  CB    . ALA B 1  757  ? 11.559  33.660  55.754  1.00 16.30 ? 755  ALA B CB    1 
ATOM   14389 N  N     . LEU B 1  758  ? 14.286  32.060  57.039  1.00 15.77 ? 756  LEU B N     1 
ATOM   14390 C  CA    . LEU B 1  758  ? 14.858  31.655  58.324  1.00 16.05 ? 756  LEU B CA    1 
ATOM   14391 C  C     . LEU B 1  758  ? 16.049  30.750  58.069  1.00 15.27 ? 756  LEU B C     1 
ATOM   14392 O  O     . LEU B 1  758  ? 15.899  29.584  57.685  1.00 16.03 ? 756  LEU B O     1 
ATOM   14393 C  CB    . LEU B 1  758  ? 13.826  30.960  59.200  1.00 14.53 ? 756  LEU B CB    1 
ATOM   14394 C  CG    . LEU B 1  758  ? 14.345  30.420  60.530  1.00 16.54 ? 756  LEU B CG    1 
ATOM   14395 C  CD1   . LEU B 1  758  ? 14.992  31.520  61.394  1.00 14.99 ? 756  LEU B CD1   1 
ATOM   14396 C  CD2   . LEU B 1  758  ? 13.202  29.741  61.301  1.00 17.34 ? 756  LEU B CD2   1 
ATOM   14397 N  N     . GLN B 1  759  ? 17.229  31.298  58.290  1.00 15.54 ? 757  GLN B N     1 
ATOM   14398 C  CA    . GLN B 1  759  ? 18.480  30.595  58.078  1.00 15.02 ? 757  GLN B CA    1 
ATOM   14399 C  C     . GLN B 1  759  ? 19.179  30.478  59.417  1.00 15.85 ? 757  GLN B C     1 
ATOM   14400 O  O     . GLN B 1  759  ? 19.135  31.415  60.219  1.00 17.31 ? 757  GLN B O     1 
ATOM   14401 C  CB    . GLN B 1  759  ? 19.353  31.337  57.071  1.00 14.67 ? 757  GLN B CB    1 
ATOM   14402 C  CG    . GLN B 1  759  ? 18.752  31.321  55.661  1.00 16.02 ? 757  GLN B CG    1 
ATOM   14403 C  CD    . GLN B 1  759  ? 19.496  32.209  54.706  1.00 16.21 ? 757  GLN B CD    1 
ATOM   14404 O  OE1   . GLN B 1  759  ? 20.327  31.737  53.945  1.00 19.72 ? 757  GLN B OE1   1 
ATOM   14405 N  NE2   . GLN B 1  759  ? 19.203  33.503  54.736  1.00 16.37 ? 757  GLN B NE2   1 
ATOM   14406 N  N     . LEU B 1  760  ? 19.789  29.319  59.663  1.00 14.38 ? 758  LEU B N     1 
ATOM   14407 C  CA    . LEU B 1  760  ? 20.513  29.047  60.904  1.00 14.09 ? 758  LEU B CA    1 
ATOM   14408 C  C     . LEU B 1  760  ? 22.010  29.090  60.640  1.00 16.07 ? 758  LEU B C     1 
ATOM   14409 O  O     . LEU B 1  760  ? 22.502  28.374  59.767  1.00 15.85 ? 758  LEU B O     1 
ATOM   14410 C  CB    . LEU B 1  760  ? 20.143  27.675  61.475  1.00 15.11 ? 758  LEU B CB    1 
ATOM   14411 C  CG    . LEU B 1  760  ? 20.848  27.334  62.791  1.00 14.78 ? 758  LEU B CG    1 
ATOM   14412 C  CD1   . LEU B 1  760  ? 20.087  27.936  63.986  1.00 15.31 ? 758  LEU B CD1   1 
ATOM   14413 C  CD2   . LEU B 1  760  ? 21.009  25.801  62.922  1.00 15.48 ? 758  LEU B CD2   1 
ATOM   14414 N  N     . LEU B 1  761  ? 22.739  29.897  61.413  1.00 15.63 ? 759  LEU B N     1 
ATOM   14415 C  CA    . LEU B 1  761  ? 24.188  30.038  61.246  1.00 14.54 ? 759  LEU B CA    1 
ATOM   14416 C  C     . LEU B 1  761  ? 24.851  29.682  62.567  1.00 16.28 ? 759  LEU B C     1 
ATOM   14417 O  O     . LEU B 1  761  ? 25.132  30.568  63.386  1.00 16.88 ? 759  LEU B O     1 
ATOM   14418 C  CB    . LEU B 1  761  ? 24.573  31.450  60.809  1.00 15.41 ? 759  LEU B CB    1 
ATOM   14419 C  CG    . LEU B 1  761  ? 24.058  31.990  59.471  1.00 16.87 ? 759  LEU B CG    1 
ATOM   14420 C  CD1   . LEU B 1  761  ? 24.179  30.933  58.350  1.00 18.19 ? 759  LEU B CD1   1 
ATOM   14421 C  CD2   . LEU B 1  761  ? 22.630  32.546  59.573  1.00 17.72 ? 759  LEU B CD2   1 
ATOM   14422 N  N     . PRO B 1  762  ? 25.107  28.403  62.826  1.00 14.41 ? 760  PRO B N     1 
ATOM   14423 C  CA    . PRO B 1  762  ? 25.819  28.037  64.056  1.00 16.42 ? 760  PRO B CA    1 
ATOM   14424 C  C     . PRO B 1  762  ? 27.242  28.560  64.026  1.00 15.64 ? 760  PRO B C     1 
ATOM   14425 O  O     . PRO B 1  762  ? 27.837  28.762  62.966  1.00 17.42 ? 760  PRO B O     1 
ATOM   14426 C  CB    . PRO B 1  762  ? 25.807  26.499  64.053  1.00 15.65 ? 760  PRO B CB    1 
ATOM   14427 C  CG    . PRO B 1  762  ? 24.759  26.114  63.024  1.00 16.08 ? 760  PRO B CG    1 
ATOM   14428 C  CD    . PRO B 1  762  ? 24.790  27.228  62.001  1.00 14.55 ? 760  PRO B CD    1 
ATOM   14429 N  N     . GLY B 1  763  ? 27.796  28.745  65.217  1.00 15.80 ? 761  GLY B N     1 
ATOM   14430 C  CA    . GLY B 1  763  ? 29.183  29.132  65.367  1.00 16.94 ? 761  GLY B CA    1 
ATOM   14431 C  C     . GLY B 1  763  ? 29.361  30.074  66.540  1.00 16.42 ? 761  GLY B C     1 
ATOM   14432 O  O     . GLY B 1  763  ? 28.457  30.287  67.348  1.00 15.99 ? 761  GLY B O     1 
ATOM   14433 N  N     . ASP B 1  764  ? 30.561  30.634  66.650  1.00 18.58 ? 762  ASP B N     1 
ATOM   14434 C  CA    . ASP B 1  764  ? 30.874  31.421  67.822  1.00 17.07 ? 762  ASP B CA    1 
ATOM   14435 C  C     . ASP B 1  764  ? 30.638  32.903  67.526  1.00 18.60 ? 762  ASP B C     1 
ATOM   14436 O  O     . ASP B 1  764  ? 29.919  33.263  66.580  1.00 18.00 ? 762  ASP B O     1 
ATOM   14437 C  CB    . ASP B 1  764  ? 32.307  31.103  68.291  1.00 20.12 ? 762  ASP B CB    1 
ATOM   14438 C  CG    . ASP B 1  764  ? 33.377  31.511  67.294  1.00 23.27 ? 762  ASP B CG    1 
ATOM   14439 O  OD1   . ASP B 1  764  ? 33.131  32.324  66.376  1.00 20.84 ? 762  ASP B OD1   1 
ATOM   14440 O  OD2   . ASP B 1  764  ? 34.509  30.996  67.429  1.00 31.25 ? 762  ASP B OD2   1 
ATOM   14441 N  N     . GLY B 1  765  ? 31.219  33.775  68.350  1.00 18.94 ? 763  GLY B N     1 
ATOM   14442 C  CA    . GLY B 1  765  ? 30.966  35.197  68.215  1.00 18.66 ? 763  GLY B CA    1 
ATOM   14443 C  C     . GLY B 1  765  ? 31.465  35.794  66.918  1.00 17.23 ? 763  GLY B C     1 
ATOM   14444 O  O     . GLY B 1  765  ? 30.959  36.840  66.507  1.00 19.59 ? 763  GLY B O     1 
ATOM   14445 N  N     . ARG B 1  766  ? 32.458  35.167  66.278  1.00 18.68 ? 764  ARG B N     1 
ATOM   14446 C  CA    . ARG B 1  766  ? 32.894  35.615  64.957  1.00 21.28 ? 764  ARG B CA    1 
ATOM   14447 C  C     . ARG B 1  766  ? 31.769  35.501  63.937  1.00 18.95 ? 764  ARG B C     1 
ATOM   14448 O  O     . ARG B 1  766  ? 31.658  36.331  63.025  1.00 19.73 ? 764  ARG B O     1 
ATOM   14449 C  CB    . ARG B 1  766  ? 34.099  34.801  64.483  1.00 21.75 ? 764  ARG B CB    1 
ATOM   14450 C  CG    . ARG B 1  766  ? 35.342  34.897  65.356  1.00 29.27 ? 764  ARG B CG    1 
ATOM   14451 C  CD    . ARG B 1  766  ? 36.355  33.817  64.959  1.00 28.60 ? 764  ARG B CD    1 
ATOM   14452 N  NE    . ARG B 1  766  ? 35.783  32.484  65.129  1.00 34.13 ? 764  ARG B NE    1 
ATOM   14453 C  CZ    . ARG B 1  766  ? 36.378  31.351  64.775  1.00 37.22 ? 764  ARG B CZ    1 
ATOM   14454 N  NH1   . ARG B 1  766  ? 37.579  31.343  64.217  1.00 34.79 ? 764  ARG B NH1   1 
ATOM   14455 N  NH2   . ARG B 1  766  ? 35.752  30.195  64.988  1.00 36.39 ? 764  ARG B NH2   1 
ATOM   14456 N  N     . VAL B 1  767  ? 30.934  34.468  64.060  1.00 17.95 ? 765  VAL B N     1 
ATOM   14457 C  CA    . VAL B 1  767  ? 29.806  34.343  63.141  1.00 16.71 ? 765  VAL B CA    1 
ATOM   14458 C  C     . VAL B 1  767  ? 28.764  35.421  63.427  1.00 16.33 ? 765  VAL B C     1 
ATOM   14459 O  O     . VAL B 1  767  ? 28.227  36.054  62.502  1.00 17.28 ? 765  VAL B O     1 
ATOM   14460 C  CB    . VAL B 1  767  ? 29.215  32.925  63.219  1.00 15.37 ? 765  VAL B CB    1 
ATOM   14461 C  CG1   . VAL B 1  767  ? 28.021  32.800  62.269  1.00 17.36 ? 765  VAL B CG1   1 
ATOM   14462 C  CG2   . VAL B 1  767  ? 30.274  31.909  62.848  1.00 18.28 ? 765  VAL B CG2   1 
ATOM   14463 N  N     . GLY B 1  768  ? 28.464  35.659  64.705  1.00 15.51 ? 766  GLY B N     1 
ATOM   14464 C  CA    . GLY B 1  768  ? 27.588  36.772  65.040  1.00 16.87 ? 766  GLY B CA    1 
ATOM   14465 C  C     . GLY B 1  768  ? 28.114  38.089  64.498  1.00 17.63 ? 766  GLY B C     1 
ATOM   14466 O  O     . GLY B 1  768  ? 27.372  38.877  63.905  1.00 16.69 ? 766  GLY B O     1 
ATOM   14467 N  N     . ALA B 1  769  ? 29.415  38.337  64.667  1.00 17.27 ? 767  ALA B N     1 
ATOM   14468 C  CA    . ALA B 1  769  ? 29.961  39.619  64.226  1.00 17.01 ? 767  ALA B CA    1 
ATOM   14469 C  C     . ALA B 1  769  ? 29.875  39.761  62.710  1.00 19.11 ? 767  ALA B C     1 
ATOM   14470 O  O     . ALA B 1  769  ? 29.566  40.844  62.201  1.00 17.32 ? 767  ALA B O     1 
ATOM   14471 C  CB    . ALA B 1  769  ? 31.408  39.770  64.706  1.00 18.01 ? 767  ALA B CB    1 
ATOM   14472 N  N     . ALA B 1  770  ? 30.149  38.678  61.971  1.00 17.56 ? 768  ALA B N     1 
ATOM   14473 C  CA    . ALA B 1  770  ? 30.069  38.737  60.515  1.00 17.14 ? 768  ALA B CA    1 
ATOM   14474 C  C     . ALA B 1  770  ? 28.647  39.032  60.059  1.00 17.74 ? 768  ALA B C     1 
ATOM   14475 O  O     . ALA B 1  770  ? 28.432  39.768  59.088  1.00 20.89 ? 768  ALA B O     1 
ATOM   14476 C  CB    . ALA B 1  770  ? 30.561  37.422  59.907  1.00 19.32 ? 768  ALA B CB    1 
ATOM   14477 N  N     . LEU B 1  771  ? 27.661  38.463  60.747  1.00 15.82 ? 769  LEU B N     1 
ATOM   14478 C  CA    . LEU B 1  771  ? 26.272  38.737  60.398  1.00 17.69 ? 769  LEU B CA    1 
ATOM   14479 C  C     . LEU B 1  771  ? 25.926  40.198  60.662  1.00 17.25 ? 769  LEU B C     1 
ATOM   14480 O  O     . LEU B 1  771  ? 25.286  40.861  59.834  1.00 19.48 ? 769  LEU B O     1 
ATOM   14481 C  CB    . LEU B 1  771  ? 25.347  37.814  61.194  1.00 17.53 ? 769  LEU B CB    1 
ATOM   14482 C  CG    . LEU B 1  771  ? 25.378  36.336  60.778  1.00 17.04 ? 769  LEU B CG    1 
ATOM   14483 C  CD1   . LEU B 1  771  ? 24.568  35.513  61.766  1.00 17.83 ? 769  LEU B CD1   1 
ATOM   14484 C  CD2   . LEU B 1  771  ? 24.837  36.152  59.352  1.00 16.83 ? 769  LEU B CD2   1 
ATOM   14485 N  N     . VAL B 1  772  ? 26.332  40.706  61.828  1.00 16.31 ? 770  VAL B N     1 
ATOM   14486 C  CA    . VAL B 1  772  ? 26.019  42.080  62.207  1.00 17.10 ? 770  VAL B CA    1 
ATOM   14487 C  C     . VAL B 1  772  ? 26.623  43.063  61.209  1.00 19.30 ? 770  VAL B C     1 
ATOM   14488 O  O     . VAL B 1  772  ? 25.995  44.069  60.846  1.00 20.90 ? 770  VAL B O     1 
ATOM   14489 C  CB    . VAL B 1  772  ? 26.516  42.348  63.644  1.00 16.64 ? 770  VAL B CB    1 
ATOM   14490 C  CG1   . VAL B 1  772  ? 26.574  43.844  63.940  1.00 19.01 ? 770  VAL B CG1   1 
ATOM   14491 C  CG2   . VAL B 1  772  ? 25.645  41.613  64.675  1.00 17.37 ? 770  VAL B CG2   1 
ATOM   14492 N  N     . ALA B 1  773  ? 27.848  42.791  60.753  1.00 19.03 ? 771  ALA B N     1 
ATOM   14493 C  CA    . ALA B 1  773  ? 28.544  43.726  59.872  1.00 20.37 ? 771  ALA B CA    1 
ATOM   14494 C  C     . ALA B 1  773  ? 28.089  43.646  58.423  1.00 23.83 ? 771  ALA B C     1 
ATOM   14495 O  O     . ALA B 1  773  ? 28.499  44.493  57.618  1.00 24.24 ? 771  ALA B O     1 
ATOM   14496 C  CB    . ALA B 1  773  ? 30.050  43.486  59.932  1.00 20.63 ? 771  ALA B CB    1 
ATOM   14497 N  N     . ALA B 1  774  ? 27.284  42.651  58.064  1.00 20.91 ? 772  ALA B N     1 
ATOM   14498 C  CA    . ALA B 1  774  ? 26.907  42.457  56.669  1.00 23.05 ? 772  ALA B CA    1 
ATOM   14499 C  C     . ALA B 1  774  ? 26.090  43.635  56.150  1.00 22.44 ? 772  ALA B C     1 
ATOM   14500 O  O     . ALA B 1  774  ? 25.276  44.222  56.863  1.00 23.07 ? 772  ALA B O     1 
ATOM   14501 C  CB    . ALA B 1  774  ? 26.124  41.154  56.498  1.00 22.75 ? 772  ALA B CB    1 
ATOM   14502 N  N     . ALA B 1  775  ? 26.304  43.952  54.869  1.00 25.98 ? 773  ALA B N     1 
ATOM   14503 C  CA    . ALA B 1  775  ? 25.758  45.172  54.284  1.00 25.88 ? 773  ALA B CA    1 
ATOM   14504 C  C     . ALA B 1  775  ? 24.234  45.231  54.377  1.00 21.67 ? 773  ALA B C     1 
ATOM   14505 O  O     . ALA B 1  775  ? 23.665  46.296  54.637  1.00 24.18 ? 773  ALA B O     1 
ATOM   14506 C  CB    . ALA B 1  775  ? 26.205  45.286  52.826  1.00 26.23 ? 773  ALA B CB    1 
ATOM   14507 N  N     . GLU B 1  776  ? 23.557  44.103  54.181  1.00 21.10 ? 774  GLU B N     1 
ATOM   14508 C  CA    . GLU B 1  776  ? 22.101  44.107  54.094  1.00 18.88 ? 774  GLU B CA    1 
ATOM   14509 C  C     . GLU B 1  776  ? 21.415  43.928  55.448  1.00 18.49 ? 774  GLU B C     1 
ATOM   14510 O  O     . GLU B 1  776  ? 20.185  43.935  55.507  1.00 18.39 ? 774  GLU B O     1 
ATOM   14511 C  CB    . GLU B 1  776  ? 21.627  43.020  53.122  1.00 20.80 ? 774  GLU B CB    1 
ATOM   14512 C  CG    . GLU B 1  776  ? 22.219  43.145  51.701  1.00 25.47 ? 774  GLU B CG    1 
ATOM   14513 C  CD    . GLU B 1  776  ? 23.590  42.479  51.545  1.00 27.74 ? 774  GLU B CD    1 
ATOM   14514 O  OE1   . GLU B 1  776  ? 24.104  41.874  52.517  1.00 27.49 ? 774  GLU B OE1   1 
ATOM   14515 O  OE2   . GLU B 1  776  ? 24.167  42.567  50.438  1.00 32.95 ? 774  GLU B OE2   1 
ATOM   14516 N  N     . THR B 1  777  ? 22.167  43.767  56.530  1.00 18.16 ? 775  THR B N     1 
ATOM   14517 C  CA    . THR B 1  777  ? 21.548  43.611  57.840  1.00 18.61 ? 775  THR B CA    1 
ATOM   14518 C  C     . THR B 1  777  ? 20.800  44.890  58.204  1.00 17.78 ? 775  THR B C     1 
ATOM   14519 O  O     . THR B 1  777  ? 21.380  45.984  58.193  1.00 18.72 ? 775  THR B O     1 
ATOM   14520 C  CB    . THR B 1  777  ? 22.613  43.272  58.882  1.00 17.51 ? 775  THR B CB    1 
ATOM   14521 O  OG1   . THR B 1  777  ? 23.090  41.945  58.633  1.00 20.17 ? 775  THR B OG1   1 
ATOM   14522 C  CG2   . THR B 1  777  ? 22.051  43.335  60.291  1.00 16.23 ? 775  THR B CG2   1 
ATOM   14523 N  N     . ALA B 1  778  ? 19.504  44.750  58.497  1.00 15.85 ? 776  ALA B N     1 
ATOM   14524 C  CA    . ALA B 1  778  ? 18.630  45.890  58.727  1.00 15.99 ? 776  ALA B CA    1 
ATOM   14525 C  C     . ALA B 1  778  ? 18.217  46.043  60.182  1.00 16.59 ? 776  ALA B C     1 
ATOM   14526 O  O     . ALA B 1  778  ? 17.568  47.036  60.523  1.00 17.22 ? 776  ALA B O     1 
ATOM   14527 C  CB    . ALA B 1  778  ? 17.374  45.779  57.847  1.00 16.81 ? 776  ALA B CB    1 
ATOM   14528 N  N     . GLY B 1  779  ? 18.589  45.101  61.042  1.00 15.28 ? 777  GLY B N     1 
ATOM   14529 C  CA    . GLY B 1  779  ? 18.306  45.199  62.461  1.00 17.73 ? 777  GLY B CA    1 
ATOM   14530 C  C     . GLY B 1  779  ? 18.932  44.024  63.168  1.00 16.89 ? 777  GLY B C     1 
ATOM   14531 O  O     . GLY B 1  779  ? 19.200  42.984  62.561  1.00 17.34 ? 777  GLY B O     1 
ATOM   14532 N  N     . VAL B 1  780  ? 19.191  44.207  64.458  1.00 15.53 ? 778  VAL B N     1 
ATOM   14533 C  CA    . VAL B 1  780  ? 19.819  43.169  65.257  1.00 14.90 ? 778  VAL B CA    1 
ATOM   14534 C  C     . VAL B 1  780  ? 19.044  43.005  66.552  1.00 15.05 ? 778  VAL B C     1 
ATOM   14535 O  O     . VAL B 1  780  ? 18.746  43.994  67.236  1.00 14.92 ? 778  VAL B O     1 
ATOM   14536 C  CB    . VAL B 1  780  ? 21.298  43.486  65.552  1.00 15.33 ? 778  VAL B CB    1 
ATOM   14537 C  CG1   . VAL B 1  780  ? 21.921  42.356  66.382  1.00 16.24 ? 778  VAL B CG1   1 
ATOM   14538 C  CG2   . VAL B 1  780  ? 22.077  43.680  64.263  1.00 17.35 ? 778  VAL B CG2   1 
ATOM   14539 N  N     . MET B 1  781  ? 18.731  41.759  66.892  1.00 14.30 ? 779  MET B N     1 
ATOM   14540 C  CA    . MET B 1  781  ? 18.151  41.417  68.185  1.00 13.49 ? 779  MET B CA    1 
ATOM   14541 C  C     . MET B 1  781  ? 19.191  40.594  68.921  1.00 13.08 ? 779  MET B C     1 
ATOM   14542 O  O     . MET B 1  781  ? 19.553  39.503  68.471  1.00 15.02 ? 779  MET B O     1 
ATOM   14543 C  CB    . MET B 1  781  ? 16.847  40.641  68.025  1.00 13.75 ? 779  MET B CB    1 
ATOM   14544 C  CG    . MET B 1  781  ? 15.884  41.367  67.100  1.00 15.81 ? 779  MET B CG    1 
ATOM   14545 S  SD    . MET B 1  781  ? 14.421  40.398  66.745  1.00 14.94 ? 779  MET B SD    1 
ATOM   14546 C  CE    . MET B 1  781  ? 13.549  40.452  68.302  1.00 13.50 ? 779  MET B CE    1 
ATOM   14547 N  N     . PHE B 1  782  ? 19.716  41.146  70.008  1.00 13.79 ? 780  PHE B N     1 
ATOM   14548 C  CA    . PHE B 1  782  ? 20.782  40.530  70.775  1.00 14.06 ? 780  PHE B CA    1 
ATOM   14549 C  C     . PHE B 1  782  ? 20.329  40.306  72.204  1.00 14.56 ? 780  PHE B C     1 
ATOM   14550 O  O     . PHE B 1  782  ? 19.752  41.201  72.819  1.00 16.05 ? 780  PHE B O     1 
ATOM   14551 C  CB    . PHE B 1  782  ? 22.020  41.421  70.808  1.00 12.55 ? 780  PHE B CB    1 
ATOM   14552 C  CG    . PHE B 1  782  ? 23.093  40.897  71.709  1.00 13.87 ? 780  PHE B CG    1 
ATOM   14553 C  CD1   . PHE B 1  782  ? 23.903  39.858  71.280  1.00 14.86 ? 780  PHE B CD1   1 
ATOM   14554 C  CD2   . PHE B 1  782  ? 23.272  41.410  72.983  1.00 15.24 ? 780  PHE B CD2   1 
ATOM   14555 C  CE1   . PHE B 1  782  ? 24.892  39.351  72.088  1.00 18.12 ? 780  PHE B CE1   1 
ATOM   14556 C  CE2   . PHE B 1  782  ? 24.272  40.896  73.803  1.00 13.73 ? 780  PHE B CE2   1 
ATOM   14557 C  CZ    . PHE B 1  782  ? 25.080  39.879  73.348  1.00 17.10 ? 780  PHE B CZ    1 
ATOM   14558 N  N     . THR B 1  783  ? 20.608  39.123  72.728  1.00 13.17 ? 781  THR B N     1 
ATOM   14559 C  CA    . THR B 1  783  ? 20.471  38.848  74.148  1.00 15.33 ? 781  THR B CA    1 
ATOM   14560 C  C     . THR B 1  783  ? 21.740  38.132  74.569  1.00 15.98 ? 781  THR B C     1 
ATOM   14561 O  O     . THR B 1  783  ? 22.142  37.151  73.932  1.00 15.62 ? 781  THR B O     1 
ATOM   14562 C  CB    . THR B 1  783  ? 19.240  38.002  74.462  1.00 14.47 ? 781  THR B CB    1 
ATOM   14563 O  OG1   . THR B 1  783  ? 18.064  38.675  73.991  1.00 13.81 ? 781  THR B OG1   1 
ATOM   14564 C  CG2   . THR B 1  783  ? 19.107  37.836  75.968  1.00 14.80 ? 781  THR B CG2   1 
ATOM   14565 N  N     . GLY B 1  784  ? 22.390  38.645  75.608  1.00 15.46 ? 782  GLY B N     1 
ATOM   14566 C  CA    . GLY B 1  784  ? 23.701  38.152  75.974  1.00 15.21 ? 782  GLY B CA    1 
ATOM   14567 C  C     . GLY B 1  784  ? 24.357  39.118  76.938  1.00 16.53 ? 782  GLY B C     1 
ATOM   14568 O  O     . GLY B 1  784  ? 23.681  39.926  77.573  1.00 16.06 ? 782  GLY B O     1 
ATOM   14569 N  N     . SER B 1  785  ? 25.673  39.027  77.030  1.00 17.54 ? 783  SER B N     1 
ATOM   14570 C  CA    . SER B 1  785  ? 26.404  39.872  77.964  1.00 18.66 ? 783  SER B CA    1 
ATOM   14571 C  C     . SER B 1  785  ? 26.434  41.325  77.490  1.00 20.22 ? 783  SER B C     1 
ATOM   14572 O  O     . SER B 1  785  ? 26.417  41.623  76.292  1.00 18.72 ? 783  SER B O     1 
ATOM   14573 C  CB    . SER B 1  785  ? 27.826  39.344  78.155  1.00 18.61 ? 783  SER B CB    1 
ATOM   14574 O  OG    . SER B 1  785  ? 28.589  39.367  76.958  1.00 17.77 ? 783  SER B OG    1 
ATOM   14575 N  N     . THR B 1  786  ? 26.485  42.243  78.459  1.00 20.48 ? 784  THR B N     1 
ATOM   14576 C  CA    . THR B 1  786  ? 26.603  43.660  78.120  1.00 18.79 ? 784  THR B CA    1 
ATOM   14577 C  C     . THR B 1  786  ? 27.865  43.925  77.309  1.00 18.68 ? 784  THR B C     1 
ATOM   14578 O  O     . THR B 1  786  ? 27.853  44.743  76.384  1.00 20.64 ? 784  THR B O     1 
ATOM   14579 C  CB    . THR B 1  786  ? 26.589  44.508  79.404  1.00 20.03 ? 784  THR B CB    1 
ATOM   14580 O  OG1   . THR B 1  786  ? 25.446  44.160  80.192  1.00 22.95 ? 784  THR B OG1   1 
ATOM   14581 C  CG2   . THR B 1  786  ? 26.524  45.986  79.072  1.00 24.60 ? 784  THR B CG2   1 
ATOM   14582 N  N     . GLU B 1  787  ? 28.962  43.228  77.628  1.00 21.36 ? 785  GLU B N     1 
ATOM   14583 C  CA    . GLU B 1  787  ? 30.221  43.456  76.928  1.00 19.46 ? 785  GLU B CA    1 
ATOM   14584 C  C     . GLU B 1  787  ? 30.085  43.177  75.435  1.00 21.57 ? 785  GLU B C     1 
ATOM   14585 O  O     . GLU B 1  787  ? 30.576  43.946  74.598  1.00 19.87 ? 785  GLU B O     1 
ATOM   14586 C  CB    . GLU B 1  787  ? 31.324  42.577  77.529  1.00 25.13 ? 785  GLU B CB    1 
ATOM   14587 C  CG    . GLU B 1  787  ? 32.682  42.758  76.875  1.00 35.24 ? 785  GLU B CG    1 
ATOM   14588 C  CD    . GLU B 1  787  ? 33.748  41.880  77.503  1.00 41.42 ? 785  GLU B CD    1 
ATOM   14589 O  OE1   . GLU B 1  787  ? 33.400  41.102  78.421  1.00 46.49 ? 785  GLU B OE1   1 
ATOM   14590 O  OE2   . GLU B 1  787  ? 34.928  41.973  77.087  1.00 42.92 ? 785  GLU B OE2   1 
ATOM   14591 N  N     . VAL B 1  788  ? 29.435  42.062  75.085  1.00 18.97 ? 786  VAL B N     1 
ATOM   14592 C  CA    . VAL B 1  788  ? 29.266  41.713  73.679  1.00 20.27 ? 786  VAL B CA    1 
ATOM   14593 C  C     . VAL B 1  788  ? 28.308  42.686  73.007  1.00 17.17 ? 786  VAL B C     1 
ATOM   14594 O  O     . VAL B 1  788  ? 28.534  43.114  71.869  1.00 18.35 ? 786  VAL B O     1 
ATOM   14595 C  CB    . VAL B 1  788  ? 28.792  40.253  73.552  1.00 17.06 ? 786  VAL B CB    1 
ATOM   14596 C  CG1   . VAL B 1  788  ? 28.310  39.965  72.126  1.00 17.59 ? 786  VAL B CG1   1 
ATOM   14597 C  CG2   . VAL B 1  788  ? 29.917  39.286  73.965  1.00 18.70 ? 786  VAL B CG2   1 
ATOM   14598 N  N     . ALA B 1  789  ? 27.236  43.075  73.712  1.00 17.45 ? 787  ALA B N     1 
ATOM   14599 C  CA    . ALA B 1  789  ? 26.287  44.018  73.133  1.00 15.40 ? 787  ALA B CA    1 
ATOM   14600 C  C     . ALA B 1  789  ? 26.990  45.302  72.731  1.00 17.42 ? 787  ALA B C     1 
ATOM   14601 O  O     . ALA B 1  789  ? 26.663  45.909  71.706  1.00 17.50 ? 787  ALA B O     1 
ATOM   14602 C  CB    . ALA B 1  789  ? 25.156  44.333  74.122  1.00 14.74 ? 787  ALA B CB    1 
ATOM   14603 N  N     . ARG B 1  790  ? 27.956  45.739  73.544  1.00 17.54 ? 788  ARG B N     1 
ATOM   14604 C  CA    . ARG B 1  790  ? 28.656  46.980  73.240  1.00 17.57 ? 788  ARG B CA    1 
ATOM   14605 C  C     . ARG B 1  790  ? 29.446  46.851  71.948  1.00 21.19 ? 788  ARG B C     1 
ATOM   14606 O  O     . ARG B 1  790  ? 29.528  47.799  71.159  1.00 22.15 ? 788  ARG B O     1 
ATOM   14607 C  CB    . ARG B 1  790  ? 29.568  47.349  74.414  1.00 22.53 ? 788  ARG B CB    1 
ATOM   14608 C  CG    . ARG B 1  790  ? 29.826  48.823  74.577  1.00 32.74 ? 788  ARG B CG    1 
ATOM   14609 C  CD    . ARG B 1  790  ? 30.655  49.103  75.838  1.00 30.13 ? 788  ARG B CD    1 
ATOM   14610 N  NE    . ARG B 1  790  ? 29.920  48.824  77.067  1.00 28.82 ? 788  ARG B NE    1 
ATOM   14611 C  CZ    . ARG B 1  790  ? 28.997  49.629  77.581  1.00 32.54 ? 788  ARG B CZ    1 
ATOM   14612 N  NH1   . ARG B 1  790  ? 28.641  50.753  76.974  1.00 29.44 ? 788  ARG B NH1   1 
ATOM   14613 N  NH2   . ARG B 1  790  ? 28.405  49.292  78.727  1.00 34.77 ? 788  ARG B NH2   1 
ATOM   14614 N  N     . LEU B 1  791  ? 30.023  45.676  71.701  1.00 19.69 ? 789  LEU B N     1 
ATOM   14615 C  CA    . LEU B 1  791  ? 30.741  45.466  70.447  1.00 19.69 ? 789  LEU B CA    1 
ATOM   14616 C  C     . LEU B 1  791  ? 29.792  45.514  69.257  1.00 20.84 ? 789  LEU B C     1 
ATOM   14617 O  O     . LEU B 1  791  ? 30.116  46.088  68.212  1.00 20.63 ? 789  LEU B O     1 
ATOM   14618 C  CB    . LEU B 1  791  ? 31.463  44.125  70.489  1.00 20.69 ? 789  LEU B CB    1 
ATOM   14619 C  CG    . LEU B 1  791  ? 32.519  43.980  71.573  1.00 22.69 ? 789  LEU B CG    1 
ATOM   14620 C  CD1   . LEU B 1  791  ? 33.079  42.578  71.469  1.00 22.31 ? 789  LEU B CD1   1 
ATOM   14621 C  CD2   . LEU B 1  791  ? 33.620  45.048  71.400  1.00 22.36 ? 789  LEU B CD2   1 
ATOM   14622 N  N     . ILE B 1  792  ? 28.616  44.901  69.398  1.00 19.27 ? 790  ILE B N     1 
ATOM   14623 C  CA    . ILE B 1  792  ? 27.635  44.911  68.320  1.00 17.78 ? 790  ILE B CA    1 
ATOM   14624 C  C     . ILE B 1  792  ? 27.156  46.322  68.054  1.00 17.33 ? 790  ILE B C     1 
ATOM   14625 O  O     . ILE B 1  792  ? 27.015  46.745  66.899  1.00 20.72 ? 790  ILE B O     1 
ATOM   14626 C  CB    . ILE B 1  792  ? 26.476  43.977  68.691  1.00 17.24 ? 790  ILE B CB    1 
ATOM   14627 C  CG1   . ILE B 1  792  ? 26.958  42.532  68.636  1.00 16.28 ? 790  ILE B CG1   1 
ATOM   14628 C  CG2   . ILE B 1  792  ? 25.257  44.242  67.807  1.00 18.27 ? 790  ILE B CG2   1 
ATOM   14629 C  CD1   . ILE B 1  792  ? 25.971  41.554  69.231  1.00 18.42 ? 790  ILE B CD1   1 
ATOM   14630 N  N     . GLN B 1  793  ? 26.883  47.062  69.126  1.00 17.51 ? 791  GLN B N     1 
ATOM   14631 C  CA    . GLN B 1  793  ? 26.454  48.445  69.009  1.00 18.15 ? 791  GLN B CA    1 
ATOM   14632 C  C     . GLN B 1  793  ? 27.479  49.279  68.252  1.00 18.99 ? 791  GLN B C     1 
ATOM   14633 O  O     . GLN B 1  793  ? 27.120  50.079  67.380  1.00 19.94 ? 791  GLN B O     1 
ATOM   14634 C  CB    . GLN B 1  793  ? 26.221  49.003  70.410  1.00 20.96 ? 791  GLN B CB    1 
ATOM   14635 C  CG    . GLN B 1  793  ? 25.835  50.460  70.469  1.00 20.75 ? 791  GLN B CG    1 
ATOM   14636 C  CD    . GLN B 1  793  ? 26.131  51.057  71.822  1.00 24.54 ? 791  GLN B CD    1 
ATOM   14637 O  OE1   . GLN B 1  793  ? 27.209  50.839  72.386  1.00 26.62 ? 791  GLN B OE1   1 
ATOM   14638 N  NE2   . GLN B 1  793  ? 25.174  51.797  72.365  1.00 24.95 ? 791  GLN B NE2   1 
ATOM   14639 N  N     . ALA B 1  794  ? 28.763  49.091  68.552  1.00 20.11 ? 792  ALA B N     1 
ATOM   14640 C  CA    . ALA B 1  794  ? 29.797  49.830  67.831  1.00 23.02 ? 792  ALA B CA    1 
ATOM   14641 C  C     . ALA B 1  794  ? 29.788  49.500  66.341  1.00 24.54 ? 792  ALA B C     1 
ATOM   14642 O  O     . ALA B 1  794  ? 29.913  50.399  65.495  1.00 24.72 ? 792  ALA B O     1 
ATOM   14643 C  CB    . ALA B 1  794  ? 31.173  49.532  68.430  1.00 23.40 ? 792  ALA B CB    1 
ATOM   14644 N  N     . GLN B 1  795  ? 29.657  48.216  65.997  1.00 20.71 ? 793  GLN B N     1 
ATOM   14645 C  CA    . GLN B 1  795  ? 29.682  47.846  64.587  1.00 21.04 ? 793  GLN B CA    1 
ATOM   14646 C  C     . GLN B 1  795  ? 28.508  48.471  63.846  1.00 20.58 ? 793  GLN B C     1 
ATOM   14647 O  O     . GLN B 1  795  ? 28.665  48.972  62.724  1.00 22.10 ? 793  GLN B O     1 
ATOM   14648 C  CB    . GLN B 1  795  ? 29.673  46.323  64.434  1.00 24.88 ? 793  GLN B CB    1 
ATOM   14649 N  N     . LEU B 1  796  ? 27.322  48.474  64.471  1.00 18.46 ? 794  LEU B N     1 
ATOM   14650 C  CA    . LEU B 1  796  ? 26.134  48.997  63.797  1.00 18.22 ? 794  LEU B CA    1 
ATOM   14651 C  C     . LEU B 1  796  ? 26.203  50.505  63.615  1.00 22.48 ? 794  LEU B C     1 
ATOM   14652 O  O     . LEU B 1  796  ? 25.662  51.038  62.638  1.00 25.00 ? 794  LEU B O     1 
ATOM   14653 C  CB    . LEU B 1  796  ? 24.880  48.635  64.591  1.00 17.27 ? 794  LEU B CB    1 
ATOM   14654 C  CG    . LEU B 1  796  ? 24.475  47.169  64.567  1.00 20.06 ? 794  LEU B CG    1 
ATOM   14655 C  CD1   . LEU B 1  796  ? 23.210  46.994  65.400  1.00 19.13 ? 794  LEU B CD1   1 
ATOM   14656 C  CD2   . LEU B 1  796  ? 24.243  46.738  63.130  1.00 19.41 ? 794  LEU B CD2   1 
ATOM   14657 N  N     . ALA B 1  797  ? 26.848  51.206  64.545  1.00 21.45 ? 795  ALA B N     1 
ATOM   14658 C  CA    . ALA B 1  797  ? 26.933  52.656  64.471  1.00 24.65 ? 795  ALA B CA    1 
ATOM   14659 C  C     . ALA B 1  797  ? 27.748  53.123  63.276  1.00 28.00 ? 795  ALA B C     1 
ATOM   14660 O  O     . ALA B 1  797  ? 27.616  54.276  62.866  1.00 27.40 ? 795  ALA B O     1 
ATOM   14661 C  CB    . ALA B 1  797  ? 27.538  53.208  65.760  1.00 27.53 ? 795  ALA B CB    1 
ATOM   14662 N  N     . ASP B 1  798  ? 28.578  52.255  62.703  1.00 27.44 ? 796  ASP B N     1 
ATOM   14663 C  CA    . ASP B 1  798  ? 29.293  52.630  61.495  1.00 30.13 ? 796  ASP B CA    1 
ATOM   14664 C  C     . ASP B 1  798  ? 28.388  52.692  60.274  1.00 29.55 ? 796  ASP B C     1 
ATOM   14665 O  O     . ASP B 1  798  ? 28.798  53.246  59.250  1.00 31.29 ? 796  ASP B O     1 
ATOM   14666 C  CB    . ASP B 1  798  ? 30.431  51.645  61.237  1.00 29.92 ? 796  ASP B CB    1 
ATOM   14667 C  CG    . ASP B 1  798  ? 31.538  52.247  60.393  1.00 41.10 ? 796  ASP B CG    1 
ATOM   14668 O  OD1   . ASP B 1  798  ? 32.125  53.259  60.828  1.00 44.30 ? 796  ASP B OD1   1 
ATOM   14669 O  OD2   . ASP B 1  798  ? 31.822  51.712  59.299  1.00 44.06 ? 796  ASP B OD2   1 
ATOM   14670 N  N     . ARG B 1  799  ? 27.174  52.159  60.357  1.00 26.85 ? 797  ARG B N     1 
ATOM   14671 C  CA    . ARG B 1  799  ? 26.341  51.963  59.185  1.00 30.08 ? 797  ARG B CA    1 
ATOM   14672 C  C     . ARG B 1  799  ? 24.999  52.665  59.348  1.00 26.00 ? 797  ARG B C     1 
ATOM   14673 O  O     . ARG B 1  799  ? 24.617  53.102  60.436  1.00 25.43 ? 797  ARG B O     1 
ATOM   14674 C  CB    . ARG B 1  799  ? 26.132  50.468  58.923  1.00 30.17 ? 797  ARG B CB    1 
ATOM   14675 C  CG    . ARG B 1  799  ? 27.412  49.639  59.080  1.00 35.33 ? 797  ARG B CG    1 
ATOM   14676 C  CD    . ARG B 1  799  ? 27.401  48.467  58.122  1.00 35.81 ? 797  ARG B CD    1 
ATOM   14677 N  NE    . ARG B 1  799  ? 26.020  48.091  57.859  1.00 37.79 ? 797  ARG B NE    1 
ATOM   14678 C  CZ    . ARG B 1  799  ? 25.337  47.216  58.582  1.00 34.14 ? 797  ARG B CZ    1 
ATOM   14679 N  NH1   . ARG B 1  799  ? 25.919  46.511  59.538  1.00 32.91 ? 797  ARG B NH1   1 
ATOM   14680 N  NH2   . ARG B 1  799  ? 24.033  47.065  58.353  1.00 27.73 ? 797  ARG B NH2   1 
ATOM   14681 N  N     . LEU B 1  800  ? 24.289  52.761  58.227  1.00 25.43 ? 798  LEU B N     1 
ATOM   14682 C  CA    . LEU B 1  800  ? 22.961  53.341  58.150  1.00 27.35 ? 798  LEU B CA    1 
ATOM   14683 C  C     . LEU B 1  800  ? 22.106  52.465  57.251  1.00 28.87 ? 798  LEU B C     1 
ATOM   14684 O  O     . LEU B 1  800  ? 22.620  51.759  56.379  1.00 30.84 ? 798  LEU B O     1 
ATOM   14685 C  CB    . LEU B 1  800  ? 22.983  54.766  57.586  1.00 28.64 ? 798  LEU B CB    1 
ATOM   14686 C  CG    . LEU B 1  800  ? 23.581  55.878  58.442  1.00 28.70 ? 798  LEU B CG    1 
ATOM   14687 C  CD1   . LEU B 1  800  ? 23.604  57.164  57.636  1.00 30.10 ? 798  LEU B CD1   1 
ATOM   14688 C  CD2   . LEU B 1  800  ? 22.765  56.044  59.709  1.00 24.98 ? 798  LEU B CD2   1 
ATOM   14689 N  N     . SER B 1  801  ? 20.798  52.513  57.474  1.00 26.62 ? 799  SER B N     1 
ATOM   14690 C  CA    . SER B 1  801  ? 19.872  51.858  56.577  1.00 32.48 ? 799  SER B CA    1 
ATOM   14691 C  C     . SER B 1  801  ? 19.908  52.543  55.217  1.00 35.18 ? 799  SER B C     1 
ATOM   14692 O  O     . SER B 1  801  ? 20.405  53.664  55.094  1.00 33.64 ? 799  SER B O     1 
ATOM   14693 C  CB    . SER B 1  801  ? 18.462  51.911  57.147  1.00 31.68 ? 799  SER B CB    1 
ATOM   14694 O  OG    . SER B 1  801  ? 17.961  53.232  57.060  1.00 32.72 ? 799  SER B OG    1 
ATOM   14695 N  N     . PRO B 1  802  ? 19.397  51.881  54.172  1.00 39.12 ? 800  PRO B N     1 
ATOM   14696 C  CA    . PRO B 1  802  ? 19.257  52.562  52.870  1.00 37.43 ? 800  PRO B CA    1 
ATOM   14697 C  C     . PRO B 1  802  ? 18.508  53.883  52.950  1.00 36.51 ? 800  PRO B C     1 
ATOM   14698 O  O     . PRO B 1  802  ? 18.728  54.765  52.109  1.00 38.97 ? 800  PRO B O     1 
ATOM   14699 C  CB    . PRO B 1  802  ? 18.498  51.528  52.029  1.00 38.09 ? 800  PRO B CB    1 
ATOM   14700 C  CG    . PRO B 1  802  ? 18.943  50.213  52.599  1.00 41.03 ? 800  PRO B CG    1 
ATOM   14701 C  CD    . PRO B 1  802  ? 19.080  50.442  54.082  1.00 36.98 ? 800  PRO B CD    1 
ATOM   14702 N  N     . ALA B 1  803  ? 17.639  54.051  53.944  1.00 35.07 ? 801  ALA B N     1 
ATOM   14703 C  CA    . ALA B 1  803  ? 16.935  55.303  54.186  1.00 32.97 ? 801  ALA B CA    1 
ATOM   14704 C  C     . ALA B 1  803  ? 17.729  56.264  55.063  1.00 35.11 ? 801  ALA B C     1 
ATOM   14705 O  O     . ALA B 1  803  ? 17.188  57.294  55.479  1.00 39.30 ? 801  ALA B O     1 
ATOM   14706 C  CB    . ALA B 1  803  ? 15.575  55.025  54.828  1.00 33.36 ? 801  ALA B CB    1 
ATOM   14707 N  N     . GLY B 1  804  ? 18.981  55.944  55.368  1.00 31.89 ? 802  GLY B N     1 
ATOM   14708 C  CA    . GLY B 1  804  ? 19.827  56.846  56.127  1.00 34.91 ? 802  GLY B CA    1 
ATOM   14709 C  C     . GLY B 1  804  ? 19.489  56.960  57.597  1.00 30.54 ? 802  GLY B C     1 
ATOM   14710 O  O     . GLY B 1  804  ? 19.661  58.033  58.184  1.00 27.70 ? 802  GLY B O     1 
ATOM   14711 N  N     . ARG B 1  805  ? 19.024  55.884  58.218  1.00 29.35 ? 803  ARG B N     1 
ATOM   14712 C  CA    . ARG B 1  805  ? 18.663  55.910  59.623  1.00 25.47 ? 803  ARG B CA    1 
ATOM   14713 C  C     . ARG B 1  805  ? 19.427  54.836  60.387  1.00 23.63 ? 803  ARG B C     1 
ATOM   14714 O  O     . ARG B 1  805  ? 19.908  53.863  59.792  1.00 25.38 ? 803  ARG B O     1 
ATOM   14715 C  CB    . ARG B 1  805  ? 17.154  55.700  59.806  1.00 28.00 ? 803  ARG B CB    1 
ATOM   14716 C  CG    . ARG B 1  805  ? 16.308  56.808  59.210  1.00 33.31 ? 803  ARG B CG    1 
ATOM   14717 C  CD    . ARG B 1  805  ? 16.532  58.119  59.948  1.00 31.85 ? 803  ARG B CD    1 
ATOM   14718 N  NE    . ARG B 1  805  ? 15.668  59.171  59.425  1.00 35.88 ? 803  ARG B NE    1 
ATOM   14719 C  CZ    . ARG B 1  805  ? 16.036  60.058  58.510  1.00 32.70 ? 803  ARG B CZ    1 
ATOM   14720 N  NH1   . ARG B 1  805  ? 17.256  60.059  57.996  1.00 34.59 ? 803  ARG B NH1   1 
ATOM   14721 N  NH2   . ARG B 1  805  ? 15.154  60.966  58.100  1.00 38.30 ? 803  ARG B NH2   1 
ATOM   14722 N  N     . PRO B 1  806  ? 19.582  54.994  61.703  1.00 22.12 ? 804  PRO B N     1 
ATOM   14723 C  CA    . PRO B 1  806  ? 20.315  53.988  62.480  1.00 21.13 ? 804  PRO B CA    1 
ATOM   14724 C  C     . PRO B 1  806  ? 19.672  52.609  62.379  1.00 23.06 ? 804  PRO B C     1 
ATOM   14725 O  O     . PRO B 1  806  ? 18.444  52.465  62.356  1.00 20.31 ? 804  PRO B O     1 
ATOM   14726 C  CB    . PRO B 1  806  ? 20.254  54.533  63.912  1.00 23.45 ? 804  PRO B CB    1 
ATOM   14727 C  CG    . PRO B 1  806  ? 20.014  56.004  63.747  1.00 23.39 ? 804  PRO B CG    1 
ATOM   14728 C  CD    . PRO B 1  806  ? 19.125  56.108  62.551  1.00 21.85 ? 804  PRO B CD    1 
ATOM   14729 N  N     . ILE B 1  807  ? 20.524  51.590  62.328  1.00 20.59 ? 805  ILE B N     1 
ATOM   14730 C  CA    . ILE B 1  807  ? 20.069  50.202  62.335  1.00 19.34 ? 805  ILE B CA    1 
ATOM   14731 C  C     . ILE B 1  807  ? 19.563  49.865  63.734  1.00 19.79 ? 805  ILE B C     1 
ATOM   14732 O  O     . ILE B 1  807  ? 20.336  49.981  64.700  1.00 18.91 ? 805  ILE B O     1 
ATOM   14733 C  CB    . ILE B 1  807  ? 21.201  49.246  61.937  1.00 19.57 ? 805  ILE B CB    1 
ATOM   14734 C  CG1   . ILE B 1  807  ? 21.816  49.634  60.586  1.00 23.11 ? 805  ILE B CG1   1 
ATOM   14735 C  CG2   . ILE B 1  807  ? 20.687  47.807  61.972  1.00 18.32 ? 805  ILE B CG2   1 
ATOM   14736 C  CD1   . ILE B 1  807  ? 20.876  49.514  59.413  1.00 26.45 ? 805  ILE B CD1   1 
ATOM   14737 N  N     . PRO B 1  808  ? 18.308  49.436  63.899  1.00 17.35 ? 806  PRO B N     1 
ATOM   14738 C  CA    . PRO B 1  808  ? 17.792  49.183  65.250  1.00 18.51 ? 806  PRO B CA    1 
ATOM   14739 C  C     . PRO B 1  808  ? 18.504  48.023  65.919  1.00 18.51 ? 806  PRO B C     1 
ATOM   14740 O  O     . PRO B 1  808  ? 18.800  46.998  65.295  1.00 16.77 ? 806  PRO B O     1 
ATOM   14741 C  CB    . PRO B 1  808  ? 16.311  48.857  65.017  1.00 17.28 ? 806  PRO B CB    1 
ATOM   14742 C  CG    . PRO B 1  808  ? 15.983  49.473  63.697  1.00 21.46 ? 806  PRO B CG    1 
ATOM   14743 C  CD    . PRO B 1  808  ? 17.247  49.344  62.881  1.00 17.98 ? 806  PRO B CD    1 
ATOM   14744 N  N     . LEU B 1  809  ? 18.799  48.202  67.198  1.00 15.49 ? 807  LEU B N     1 
ATOM   14745 C  CA    . LEU B 1  809  ? 19.384  47.149  68.013  1.00 15.53 ? 807  LEU B CA    1 
ATOM   14746 C  C     . LEU B 1  809  ? 18.533  46.984  69.260  1.00 15.13 ? 807  LEU B C     1 
ATOM   14747 O  O     . LEU B 1  809  ? 18.336  47.948  70.003  1.00 16.69 ? 807  LEU B O     1 
ATOM   14748 C  CB    . LEU B 1  809  ? 20.822  47.496  68.392  1.00 16.41 ? 807  LEU B CB    1 
ATOM   14749 C  CG    . LEU B 1  809  ? 21.495  46.627  69.447  1.00 16.62 ? 807  LEU B CG    1 
ATOM   14750 C  CD1   . LEU B 1  809  ? 21.713  45.193  68.926  1.00 16.57 ? 807  LEU B CD1   1 
ATOM   14751 C  CD2   . LEU B 1  809  ? 22.819  47.298  69.838  1.00 16.65 ? 807  LEU B CD2   1 
ATOM   14752 N  N     . ILE B 1  810  ? 18.028  45.773  69.494  1.00 14.91 ? 808  ILE B N     1 
ATOM   14753 C  CA    . ILE B 1  810  ? 17.496  45.413  70.802  1.00 16.02 ? 808  ILE B CA    1 
ATOM   14754 C  C     . ILE B 1  810  ? 18.607  44.652  71.488  1.00 16.47 ? 808  ILE B C     1 
ATOM   14755 O  O     . ILE B 1  810  ? 19.096  43.649  70.952  1.00 15.73 ? 808  ILE B O     1 
ATOM   14756 C  CB    . ILE B 1  810  ? 16.224  44.556  70.715  1.00 13.08 ? 808  ILE B CB    1 
ATOM   14757 C  CG1   . ILE B 1  810  ? 15.177  45.215  69.829  1.00 15.95 ? 808  ILE B CG1   1 
ATOM   14758 C  CG2   . ILE B 1  810  ? 15.663  44.315  72.134  1.00 17.82 ? 808  ILE B CG2   1 
ATOM   14759 C  CD1   . ILE B 1  810  ? 13.850  44.443  69.827  1.00 16.28 ? 808  ILE B CD1   1 
ATOM   14760 N  N     . ALA B 1  811  ? 19.052  45.143  72.641  1.00 15.44 ? 809  ALA B N     1 
ATOM   14761 C  CA    . ALA B 1  811  ? 20.184  44.525  73.332  1.00 15.29 ? 809  ALA B CA    1 
ATOM   14762 C  C     . ALA B 1  811  ? 19.766  44.304  74.779  1.00 16.06 ? 809  ALA B C     1 
ATOM   14763 O  O     . ALA B 1  811  ? 19.756  45.243  75.587  1.00 16.53 ? 809  ALA B O     1 
ATOM   14764 C  CB    . ALA B 1  811  ? 21.446  45.380  73.236  1.00 15.36 ? 809  ALA B CB    1 
ATOM   14765 N  N     . GLU B 1  812  ? 19.421  43.063  75.089  1.00 14.36 ? 810  GLU B N     1 
ATOM   14766 C  CA    . GLU B 1  812  ? 18.912  42.681  76.393  1.00 16.46 ? 810  GLU B CA    1 
ATOM   14767 C  C     . GLU B 1  812  ? 20.033  41.932  77.088  1.00 17.39 ? 810  GLU B C     1 
ATOM   14768 O  O     . GLU B 1  812  ? 20.487  40.889  76.603  1.00 16.28 ? 810  GLU B O     1 
ATOM   14769 C  CB    . GLU B 1  812  ? 17.639  41.850  76.237  1.00 14.87 ? 810  GLU B CB    1 
ATOM   14770 C  CG    . GLU B 1  812  ? 16.566  42.650  75.496  1.00 16.11 ? 810  GLU B CG    1 
ATOM   14771 C  CD    . GLU B 1  812  ? 16.186  43.901  76.273  1.00 17.94 ? 810  GLU B CD    1 
ATOM   14772 O  OE1   . GLU B 1  812  ? 15.471  43.773  77.279  1.00 17.00 ? 810  GLU B OE1   1 
ATOM   14773 O  OE2   . GLU B 1  812  ? 16.607  45.010  75.890  1.00 16.42 ? 810  GLU B OE2   1 
ATOM   14774 N  N     . THR B 1  813  ? 20.531  42.509  78.177  1.00 15.70 ? 811  THR B N     1 
ATOM   14775 C  CA    . THR B 1  813  ? 21.843  42.118  78.668  1.00 13.65 ? 811  THR B CA    1 
ATOM   14776 C  C     . THR B 1  813  ? 21.822  41.693  80.135  1.00 15.80 ? 811  THR B C     1 
ATOM   14777 O  O     . THR B 1  813  ? 20.813  41.177  80.620  1.00 15.38 ? 811  THR B O     1 
ATOM   14778 C  CB    . THR B 1  813  ? 22.830  43.255  78.375  1.00 15.84 ? 811  THR B CB    1 
ATOM   14779 O  OG1   . THR B 1  813  ? 22.272  44.513  78.780  1.00 16.06 ? 811  THR B OG1   1 
ATOM   14780 C  CG2   . THR B 1  813  ? 23.065  43.324  76.853  1.00 18.18 ? 811  THR B CG2   1 
ATOM   14781 N  N     . GLY B 1  814  ? 22.928  41.869  80.848  1.00 15.10 ? 812  GLY B N     1 
ATOM   14782 C  CA    . GLY B 1  814  ? 23.101  41.194  82.120  1.00 17.04 ? 812  GLY B CA    1 
ATOM   14783 C  C     . GLY B 1  814  ? 22.347  41.845  83.268  1.00 18.67 ? 812  GLY B C     1 
ATOM   14784 O  O     . GLY B 1  814  ? 21.656  42.849  83.116  1.00 18.33 ? 812  GLY B O     1 
ATOM   14785 N  N     . GLY B 1  815  ? 22.486  41.235  84.448  1.00 15.79 ? 813  GLY B N     1 
ATOM   14786 C  CA    . GLY B 1  815  ? 21.880  41.770  85.655  1.00 15.60 ? 813  GLY B CA    1 
ATOM   14787 C  C     . GLY B 1  815  ? 22.803  41.564  86.840  1.00 15.09 ? 813  GLY B C     1 
ATOM   14788 O  O     . GLY B 1  815  ? 23.736  40.760  86.793  1.00 17.43 ? 813  GLY B O     1 
ATOM   14789 N  N     . GLN B 1  816  ? 22.541  42.336  87.902  1.00 14.00 ? 814  GLN B N     1 
ATOM   14790 C  CA    . GLN B 1  816  ? 23.183  42.162  89.207  1.00 14.93 ? 814  GLN B CA    1 
ATOM   14791 C  C     . GLN B 1  816  ? 22.063  42.179  90.245  1.00 14.21 ? 814  GLN B C     1 
ATOM   14792 O  O     . GLN B 1  816  ? 21.889  43.149  90.981  1.00 16.86 ? 814  GLN B O     1 
ATOM   14793 C  CB    . GLN B 1  816  ? 24.217  43.250  89.479  1.00 15.57 ? 814  GLN B CB    1 
ATOM   14794 C  CG    . GLN B 1  816  ? 25.129  42.930  90.648  1.00 16.38 ? 814  GLN B CG    1 
ATOM   14795 C  CD    . GLN B 1  816  ? 25.976  41.710  90.361  1.00 17.69 ? 814  GLN B CD    1 
ATOM   14796 O  OE1   . GLN B 1  816  ? 25.498  40.579  90.475  1.00 15.85 ? 814  GLN B OE1   1 
ATOM   14797 N  NE2   . GLN B 1  816  ? 27.244  41.926  89.973  1.00 16.99 ? 814  GLN B NE2   1 
ATOM   14798 N  N     . ASN B 1  817  ? 21.284  41.107  90.276  1.00 13.30 ? 815  ASN B N     1 
ATOM   14799 C  CA    . ASN B 1  817  ? 19.929  41.156  90.812  1.00 14.29 ? 815  ASN B CA    1 
ATOM   14800 C  C     . ASN B 1  817  ? 19.914  40.936  92.317  1.00 16.26 ? 815  ASN B C     1 
ATOM   14801 O  O     . ASN B 1  817  ? 20.513  39.980  92.820  1.00 16.63 ? 815  ASN B O     1 
ATOM   14802 C  CB    . ASN B 1  817  ? 19.053  40.117  90.115  1.00 13.77 ? 815  ASN B CB    1 
ATOM   14803 C  CG    . ASN B 1  817  ? 19.185  40.172  88.603  1.00 14.42 ? 815  ASN B CG    1 
ATOM   14804 O  OD1   . ASN B 1  817  ? 19.015  41.234  87.991  1.00 13.91 ? 815  ASN B OD1   1 
ATOM   14805 N  ND2   . ASN B 1  817  ? 19.500  39.030  87.994  1.00 13.87 ? 815  ASN B ND2   1 
ATOM   14806 N  N     . ALA B 1  818  ? 19.198  41.801  93.022  1.00 14.74 ? 816  ALA B N     1 
ATOM   14807 C  CA    . ALA B 1  818  ? 19.110  41.753  94.473  1.00 15.29 ? 816  ALA B CA    1 
ATOM   14808 C  C     . ALA B 1  818  ? 17.733  41.304  94.928  1.00 15.52 ? 816  ALA B C     1 
ATOM   14809 O  O     . ALA B 1  818  ? 16.736  41.475  94.222  1.00 15.67 ? 816  ALA B O     1 
ATOM   14810 C  CB    . ALA B 1  818  ? 19.394  43.126  95.087  1.00 13.43 ? 816  ALA B CB    1 
ATOM   14811 N  N     . MET B 1  819  ? 17.690  40.732  96.125  1.00 13.24 ? 817  MET B N     1 
ATOM   14812 C  CA    . MET B 1  819  ? 16.443  40.513  96.839  1.00 13.89 ? 817  MET B CA    1 
ATOM   14813 C  C     . MET B 1  819  ? 16.625  41.108  98.219  1.00 15.53 ? 817  MET B C     1 
ATOM   14814 O  O     . MET B 1  819  ? 17.615  40.807  98.898  1.00 16.17 ? 817  MET B O     1 
ATOM   14815 C  CB    . MET B 1  819  ? 16.072  39.032  96.944  1.00 14.84 ? 817  MET B CB    1 
ATOM   14816 C  CG    . MET B 1  819  ? 14.865  38.784  97.870  1.00 13.76 ? 817  MET B CG    1 
ATOM   14817 S  SD    . MET B 1  819  ? 14.555  37.025  98.144  1.00 16.93 ? 817  MET B SD    1 
ATOM   14818 C  CE    . MET B 1  819  ? 13.981  36.534  96.514  1.00 17.96 ? 817  MET B CE    1 
ATOM   14819 N  N     . ILE B 1  820  ? 15.694  41.972  98.611  1.00 16.01 ? 818  ILE B N     1 
ATOM   14820 C  CA    . ILE B 1  820  ? 15.696  42.568  99.941  1.00 15.15 ? 818  ILE B CA    1 
ATOM   14821 C  C     . ILE B 1  820  ? 14.671  41.845  100.799 1.00 15.58 ? 818  ILE B C     1 
ATOM   14822 O  O     . ILE B 1  820  ? 13.524  41.658  100.386 1.00 15.54 ? 818  ILE B O     1 
ATOM   14823 C  CB    . ILE B 1  820  ? 15.410  44.076  99.879  1.00 14.86 ? 818  ILE B CB    1 
ATOM   14824 C  CG1   . ILE B 1  820  ? 16.501  44.782  99.074  1.00 17.06 ? 818  ILE B CG1   1 
ATOM   14825 C  CG2   . ILE B 1  820  ? 15.353  44.649  101.291 1.00 16.15 ? 818  ILE B CG2   1 
ATOM   14826 C  CD1   . ILE B 1  820  ? 16.330  46.274  99.024  1.00 16.75 ? 818  ILE B CD1   1 
ATOM   14827 N  N     . VAL B 1  821  ? 15.089  41.440  101.997 1.00 15.70 ? 819  VAL B N     1 
ATOM   14828 C  CA    . VAL B 1  821  ? 14.273  40.672  102.934 1.00 14.39 ? 819  VAL B CA    1 
ATOM   14829 C  C     . VAL B 1  821  ? 14.296  41.408  104.269 1.00 16.77 ? 819  VAL B C     1 
ATOM   14830 O  O     . VAL B 1  821  ? 15.375  41.616  104.833 1.00 17.78 ? 819  VAL B O     1 
ATOM   14831 C  CB    . VAL B 1  821  ? 14.828  39.249  103.120 1.00 16.05 ? 819  VAL B CB    1 
ATOM   14832 C  CG1   . VAL B 1  821  ? 13.969  38.448  104.078 1.00 17.68 ? 819  VAL B CG1   1 
ATOM   14833 C  CG2   . VAL B 1  821  ? 14.962  38.541  101.769 1.00 16.65 ? 819  VAL B CG2   1 
ATOM   14834 N  N     . ASP B 1  822  ? 13.124  41.787  104.785 1.00 17.36 ? 820  ASP B N     1 
ATOM   14835 C  CA    . ASP B 1  822  ? 13.090  42.432  106.093 1.00 16.80 ? 820  ASP B CA    1 
ATOM   14836 C  C     . ASP B 1  822  ? 12.626  41.435  107.157 1.00 19.36 ? 820  ASP B C     1 
ATOM   14837 O  O     . ASP B 1  822  ? 12.377  40.262  106.884 1.00 19.41 ? 820  ASP B O     1 
ATOM   14838 C  CB    . ASP B 1  822  ? 12.251  43.721  106.058 1.00 17.24 ? 820  ASP B CB    1 
ATOM   14839 C  CG    . ASP B 1  822  ? 10.733  43.491  105.970 1.00 20.79 ? 820  ASP B CG    1 
ATOM   14840 O  OD1   . ASP B 1  822  ? 10.214  42.377  106.198 1.00 17.84 ? 820  ASP B OD1   1 
ATOM   14841 O  OD2   . ASP B 1  822  ? 10.042  44.495  105.683 1.00 20.16 ? 820  ASP B OD2   1 
ATOM   14842 N  N     . SER B 1  823  ? 12.548  41.902  108.401 1.00 19.94 ? 821  SER B N     1 
ATOM   14843 C  CA    . SER B 1  823  ? 12.252  40.986  109.498 1.00 22.28 ? 821  SER B CA    1 
ATOM   14844 C  C     . SER B 1  823  ? 10.794  40.541  109.544 1.00 22.83 ? 821  SER B C     1 
ATOM   14845 O  O     . SER B 1  823  ? 10.437  39.726  110.406 1.00 22.85 ? 821  SER B O     1 
ATOM   14846 C  CB    . SER B 1  823  ? 12.636  41.632  110.827 1.00 22.20 ? 821  SER B CB    1 
ATOM   14847 O  OG    . SER B 1  823  ? 11.950  42.856  111.003 1.00 24.83 ? 821  SER B OG    1 
ATOM   14848 N  N     . SER B 1  824  ? 9.934   41.038  108.659 1.00 18.77 ? 822  SER B N     1 
ATOM   14849 C  CA    . SER B 1  824  ? 8.561   40.562  108.619 1.00 19.20 ? 822  SER B CA    1 
ATOM   14850 C  C     . SER B 1  824  ? 8.381   39.384  107.671 1.00 21.23 ? 822  SER B C     1 
ATOM   14851 O  O     . SER B 1  824  ? 7.329   38.741  107.691 1.00 22.68 ? 822  SER B O     1 
ATOM   14852 C  CB    . SER B 1  824  ? 7.614   41.702  108.212 1.00 20.88 ? 822  SER B CB    1 
ATOM   14853 O  OG    . SER B 1  824  ? 7.670   41.932  106.811 1.00 18.39 ? 822  SER B OG    1 
ATOM   14854 N  N     . ALA B 1  825  ? 9.375   39.092  106.840 1.00 18.49 ? 823  ALA B N     1 
ATOM   14855 C  CA    . ALA B 1  825  ? 9.239   38.019  105.870 1.00 18.87 ? 823  ALA B CA    1 
ATOM   14856 C  C     . ALA B 1  825  ? 9.180   36.668  106.577 1.00 21.84 ? 823  ALA B C     1 
ATOM   14857 O  O     . ALA B 1  825  ? 9.713   36.498  107.675 1.00 22.43 ? 823  ALA B O     1 
ATOM   14858 C  CB    . ALA B 1  825  ? 10.416  38.057  104.890 1.00 18.15 ? 823  ALA B CB    1 
ATOM   14859 N  N     . LEU B 1  826  ? 8.543   35.697  105.930 1.00 22.18 ? 824  LEU B N     1 
ATOM   14860 C  CA    . LEU B 1  826  ? 8.500   34.331  106.444 1.00 22.69 ? 824  LEU B CA    1 
ATOM   14861 C  C     . LEU B 1  826  ? 9.745   33.580  105.975 1.00 21.08 ? 824  LEU B C     1 
ATOM   14862 O  O     . LEU B 1  826  ? 9.932   33.376  104.772 1.00 19.78 ? 824  LEU B O     1 
ATOM   14863 C  CB    . LEU B 1  826  ? 7.237   33.617  105.977 1.00 25.27 ? 824  LEU B CB    1 
ATOM   14864 C  CG    . LEU B 1  826  ? 7.003   32.219  106.558 1.00 28.71 ? 824  LEU B CG    1 
ATOM   14865 C  CD1   . LEU B 1  826  ? 6.993   32.224  108.085 1.00 32.39 ? 824  LEU B CD1   1 
ATOM   14866 C  CD2   . LEU B 1  826  ? 5.701   31.646  106.022 1.00 37.01 ? 824  LEU B CD2   1 
ATOM   14867 N  N     . ALA B 1  827  ? 10.582  33.151  106.929 1.00 20.73 ? 825  ALA B N     1 
ATOM   14868 C  CA    . ALA B 1  827  ? 11.904  32.634  106.578 1.00 17.90 ? 825  ALA B CA    1 
ATOM   14869 C  C     . ALA B 1  827  ? 11.813  31.443  105.626 1.00 20.75 ? 825  ALA B C     1 
ATOM   14870 O  O     . ALA B 1  827  ? 12.581  31.360  104.657 1.00 19.55 ? 825  ALA B O     1 
ATOM   14871 C  CB    . ALA B 1  827  ? 12.670  32.254  107.844 1.00 19.16 ? 825  ALA B CB    1 
ATOM   14872 N  N     . GLU B 1  828  ? 10.874  30.519  105.878 1.00 19.68 ? 826  GLU B N     1 
ATOM   14873 C  CA    . GLU B 1  828  ? 10.727  29.355  105.006 1.00 21.33 ? 826  GLU B CA    1 
ATOM   14874 C  C     . GLU B 1  828  ? 10.444  29.777  103.574 1.00 22.32 ? 826  GLU B C     1 
ATOM   14875 O  O     . GLU B 1  828  ? 10.975  29.185  102.625 1.00 19.60 ? 826  GLU B O     1 
ATOM   14876 C  CB    . GLU B 1  828  ? 9.606   28.445  105.512 1.00 22.40 ? 826  GLU B CB    1 
ATOM   14877 C  CG    . GLU B 1  828  ? 9.947   27.643  106.762 1.00 26.75 ? 826  GLU B CG    1 
ATOM   14878 C  CD    . GLU B 1  828  ? 9.888   28.462  108.042 1.00 27.54 ? 826  GLU B CD    1 
ATOM   14879 O  OE1   . GLU B 1  828  ? 9.497   29.650  107.993 1.00 26.03 ? 826  GLU B OE1   1 
ATOM   14880 O  OE2   . GLU B 1  828  ? 10.247  27.911  109.105 1.00 30.36 ? 826  GLU B OE2   1 
ATOM   14881 N  N     . GLN B 1  829  ? 9.606   30.803  103.401 1.00 19.72 ? 827  GLN B N     1 
ATOM   14882 C  CA    . GLN B 1  829  ? 9.273   31.276  102.062 1.00 20.30 ? 827  GLN B CA    1 
ATOM   14883 C  C     . GLN B 1  829  ? 10.479  31.907  101.397 1.00 18.45 ? 827  GLN B C     1 
ATOM   14884 O  O     . GLN B 1  829  ? 10.744  31.671  100.214 1.00 17.76 ? 827  GLN B O     1 
ATOM   14885 C  CB    . GLN B 1  829  ? 8.131   32.289  102.127 1.00 24.09 ? 827  GLN B CB    1 
ATOM   14886 C  CG    . GLN B 1  829  ? 6.775   31.714  102.476 1.00 29.47 ? 827  GLN B CG    1 
ATOM   14887 C  CD    . GLN B 1  829  ? 5.659   32.701  102.148 1.00 36.27 ? 827  GLN B CD    1 
ATOM   14888 O  OE1   . GLN B 1  829  ? 5.874   33.920  102.144 1.00 31.14 ? 827  GLN B OE1   1 
ATOM   14889 N  NE2   . GLN B 1  829  ? 4.473   32.182  101.858 1.00 39.34 ? 827  GLN B NE2   1 
ATOM   14890 N  N     . VAL B 1  830  ? 11.196  32.751  102.138 1.00 17.98 ? 828  VAL B N     1 
ATOM   14891 C  CA    . VAL B 1  830  ? 12.410  33.376  101.624 1.00 16.77 ? 828  VAL B CA    1 
ATOM   14892 C  C     . VAL B 1  830  ? 13.381  32.313  101.146 1.00 17.68 ? 828  VAL B C     1 
ATOM   14893 O  O     . VAL B 1  830  ? 13.934  32.397  100.047 1.00 17.54 ? 828  VAL B O     1 
ATOM   14894 C  CB    . VAL B 1  830  ? 13.063  34.249  102.709 1.00 17.65 ? 828  VAL B CB    1 
ATOM   14895 C  CG1   . VAL B 1  830  ? 14.447  34.733  102.250 1.00 15.65 ? 828  VAL B CG1   1 
ATOM   14896 C  CG2   . VAL B 1  830  ? 12.157  35.389  103.099 1.00 18.76 ? 828  VAL B CG2   1 
ATOM   14897 N  N     . VAL B 1  831  ? 13.618  31.305  101.986 1.00 18.10 ? 829  VAL B N     1 
ATOM   14898 C  CA    . VAL B 1  831  ? 14.633  30.313  101.667 1.00 17.49 ? 829  VAL B CA    1 
ATOM   14899 C  C     . VAL B 1  831  ? 14.263  29.563  100.394 1.00 17.30 ? 829  VAL B C     1 
ATOM   14900 O  O     . VAL B 1  831  ? 15.106  29.367  99.514  1.00 18.16 ? 829  VAL B O     1 
ATOM   14901 C  CB    . VAL B 1  831  ? 14.849  29.379  102.867 1.00 18.30 ? 829  VAL B CB    1 
ATOM   14902 C  CG1   . VAL B 1  831  ? 15.661  28.164  102.457 1.00 16.90 ? 829  VAL B CG1   1 
ATOM   14903 C  CG2   . VAL B 1  831  ? 15.574  30.152  103.964 1.00 17.57 ? 829  VAL B CG2   1 
ATOM   14904 N  N     . GLY B 1  832  ? 12.996  29.172  100.250 1.00 16.20 ? 830  GLY B N     1 
ATOM   14905 C  CA    . GLY B 1  832  ? 12.593  28.498  99.029  1.00 18.35 ? 830  GLY B CA    1 
ATOM   14906 C  C     . GLY B 1  832  ? 12.793  29.373  97.809  1.00 18.60 ? 830  GLY B C     1 
ATOM   14907 O  O     . GLY B 1  832  ? 13.266  28.911  96.767  1.00 18.17 ? 830  GLY B O     1 
ATOM   14908 N  N     . ASP B 1  833  ? 12.465  30.660  97.933  1.00 15.30 ? 831  ASP B N     1 
ATOM   14909 C  CA    . ASP B 1  833  ? 12.598  31.559  96.793  1.00 15.51 ? 831  ASP B CA    1 
ATOM   14910 C  C     . ASP B 1  833  ? 14.052  31.910  96.514  1.00 15.07 ? 831  ASP B C     1 
ATOM   14911 O  O     . ASP B 1  833  ? 14.410  32.169  95.361  1.00 15.99 ? 831  ASP B O     1 
ATOM   14912 C  CB    . ASP B 1  833  ? 11.774  32.819  97.032  1.00 14.75 ? 831  ASP B CB    1 
ATOM   14913 C  CG    . ASP B 1  833  ? 10.291  32.529  97.032  1.00 17.13 ? 831  ASP B CG    1 
ATOM   14914 O  OD1   . ASP B 1  833  ? 9.903   31.417  96.587  1.00 18.41 ? 831  ASP B OD1   1 
ATOM   14915 O  OD2   . ASP B 1  833  ? 9.503   33.379  97.476  1.00 17.65 ? 831  ASP B OD2   1 
ATOM   14916 N  N     . VAL B 1  834  ? 14.898  31.913  97.545  1.00 15.27 ? 832  VAL B N     1 
ATOM   14917 C  CA    . VAL B 1  834  ? 16.319  32.151  97.322  1.00 15.12 ? 832  VAL B CA    1 
ATOM   14918 C  C     . VAL B 1  834  ? 16.941  30.963  96.609  1.00 16.57 ? 832  VAL B C     1 
ATOM   14919 O  O     . VAL B 1  834  ? 17.733  31.122  95.671  1.00 16.78 ? 832  VAL B O     1 
ATOM   14920 C  CB    . VAL B 1  834  ? 17.028  32.439  98.656  1.00 15.70 ? 832  VAL B CB    1 
ATOM   14921 C  CG1   . VAL B 1  834  ? 18.529  32.338  98.495  1.00 17.07 ? 832  VAL B CG1   1 
ATOM   14922 C  CG2   . VAL B 1  834  ? 16.638  33.816  99.185  1.00 18.45 ? 832  VAL B CG2   1 
ATOM   14923 N  N     . ILE B 1  835  ? 16.614  29.753  97.052  1.00 16.41 ? 833  ILE B N     1 
ATOM   14924 C  CA    . ILE B 1  835  ? 17.198  28.575  96.424  1.00 19.38 ? 833  ILE B CA    1 
ATOM   14925 C  C     . ILE B 1  835  ? 16.795  28.504  94.965  1.00 19.55 ? 833  ILE B C     1 
ATOM   14926 O  O     . ILE B 1  835  ? 17.630  28.265  94.083  1.00 21.77 ? 833  ILE B O     1 
ATOM   14927 C  CB    . ILE B 1  835  ? 16.801  27.305  97.188  1.00 20.61 ? 833  ILE B CB    1 
ATOM   14928 C  CG1   . ILE B 1  835  ? 17.560  27.269  98.506  1.00 22.60 ? 833  ILE B CG1   1 
ATOM   14929 C  CG2   . ILE B 1  835  ? 17.088  26.063  96.348  1.00 23.61 ? 833  ILE B CG2   1 
ATOM   14930 C  CD1   . ILE B 1  835  ? 17.345  26.031  99.253  1.00 23.28 ? 833  ILE B CD1   1 
ATOM   14931 N  N     . THR B 1  836  ? 15.519  28.751  94.685  1.00 16.74 ? 834  THR B N     1 
ATOM   14932 C  CA    . THR B 1  836  ? 15.049  28.800  93.307  1.00 19.07 ? 834  THR B CA    1 
ATOM   14933 C  C     . THR B 1  836  ? 15.765  29.898  92.534  1.00 19.15 ? 834  THR B C     1 
ATOM   14934 O  O     . THR B 1  836  ? 16.317  29.664  91.456  1.00 20.69 ? 834  THR B O     1 
ATOM   14935 C  CB    . THR B 1  836  ? 13.535  29.040  93.291  1.00 19.00 ? 834  THR B CB    1 
ATOM   14936 O  OG1   . THR B 1  836  ? 12.842  27.897  93.823  1.00 23.63 ? 834  THR B OG1   1 
ATOM   14937 C  CG2   . THR B 1  836  ? 13.043  29.320  91.858  1.00 20.69 ? 834  THR B CG2   1 
ATOM   14938 N  N     . SER B 1  837  ? 15.783  31.108  93.080  1.00 16.45 ? 835  SER B N     1 
ATOM   14939 C  CA    . SER B 1  837  ? 16.269  32.231  92.288  1.00 16.50 ? 835  SER B CA    1 
ATOM   14940 C  C     . SER B 1  837  ? 17.774  32.182  92.113  1.00 15.73 ? 835  SER B C     1 
ATOM   14941 O  O     . SER B 1  837  ? 18.292  32.565  91.059  1.00 17.53 ? 835  SER B O     1 
ATOM   14942 C  CB    . SER B 1  837  ? 15.870  33.549  92.938  1.00 14.66 ? 835  SER B CB    1 
ATOM   14943 O  OG    . SER B 1  837  ? 14.469  33.579  93.112  1.00 15.86 ? 835  SER B OG    1 
ATOM   14944 N  N     . ALA B 1  838  ? 18.497  31.759  93.144  1.00 15.61 ? 836  ALA B N     1 
ATOM   14945 C  CA    . ALA B 1  838  ? 19.951  31.831  93.089  1.00 13.78 ? 836  ALA B CA    1 
ATOM   14946 C  C     . ALA B 1  838  ? 20.600  30.594  92.491  1.00 16.07 ? 836  ALA B C     1 
ATOM   14947 O  O     . ALA B 1  838  ? 21.635  30.714  91.828  1.00 17.96 ? 836  ALA B O     1 
ATOM   14948 C  CB    . ALA B 1  838  ? 20.532  32.045  94.494  1.00 15.78 ? 836  ALA B CB    1 
ATOM   14949 N  N     . PHE B 1  839  ? 20.039  29.410  92.719  1.00 17.64 ? 837  PHE B N     1 
ATOM   14950 C  CA    . PHE B 1  839  ? 20.766  28.183  92.436  1.00 19.23 ? 837  PHE B CA    1 
ATOM   14951 C  C     . PHE B 1  839  ? 20.093  27.264  91.432  1.00 19.92 ? 837  PHE B C     1 
ATOM   14952 O  O     . PHE B 1  839  ? 20.775  26.384  90.888  1.00 19.57 ? 837  PHE B O     1 
ATOM   14953 C  CB    . PHE B 1  839  ? 21.031  27.415  93.735  1.00 18.40 ? 837  PHE B CB    1 
ATOM   14954 C  CG    . PHE B 1  839  ? 21.752  28.230  94.773  1.00 18.24 ? 837  PHE B CG    1 
ATOM   14955 C  CD1   . PHE B 1  839  ? 23.028  28.743  94.519  1.00 16.96 ? 837  PHE B CD1   1 
ATOM   14956 C  CD2   . PHE B 1  839  ? 21.163  28.498  95.999  1.00 18.01 ? 837  PHE B CD2   1 
ATOM   14957 C  CE1   . PHE B 1  839  ? 23.695  29.497  95.464  1.00 16.89 ? 837  PHE B CE1   1 
ATOM   14958 C  CE2   . PHE B 1  839  ? 21.836  29.253  96.964  1.00 19.50 ? 837  PHE B CE2   1 
ATOM   14959 C  CZ    . PHE B 1  839  ? 23.102  29.752  96.698  1.00 21.25 ? 837  PHE B CZ    1 
ATOM   14960 N  N     . ASP B 1  840  ? 18.800  27.432  91.168  1.00 20.73 ? 838  ASP B N     1 
ATOM   14961 C  CA    . ASP B 1  840  ? 18.174  26.761  90.035  1.00 21.70 ? 838  ASP B CA    1 
ATOM   14962 C  C     . ASP B 1  840  ? 18.980  27.036  88.774  1.00 22.03 ? 838  ASP B C     1 
ATOM   14963 O  O     . ASP B 1  840  ? 19.449  28.157  88.549  1.00 17.73 ? 838  ASP B O     1 
ATOM   14964 C  CB    . ASP B 1  840  ? 16.731  27.252  89.870  1.00 27.13 ? 838  ASP B CB    1 
ATOM   14965 C  CG    . ASP B 1  840  ? 16.021  26.669  88.655  1.00 32.25 ? 838  ASP B CG    1 
ATOM   14966 O  OD1   . ASP B 1  840  ? 16.322  27.062  87.500  1.00 30.43 ? 838  ASP B OD1   1 
ATOM   14967 O  OD2   . ASP B 1  840  ? 15.123  25.838  88.866  1.00 32.69 ? 838  ASP B OD2   1 
ATOM   14968 N  N     . SER B 1  841  ? 19.161  25.998  87.961  1.00 19.31 ? 839  SER B N     1 
ATOM   14969 C  CA    . SER B 1  841  ? 19.956  26.102  86.741  1.00 17.84 ? 839  SER B CA    1 
ATOM   14970 C  C     . SER B 1  841  ? 21.376  26.539  87.046  1.00 16.92 ? 839  SER B C     1 
ATOM   14971 O  O     . SER B 1  841  ? 22.033  27.173  86.215  1.00 16.62 ? 839  SER B O     1 
ATOM   14972 C  CB    . SER B 1  841  ? 19.309  27.055  85.726  1.00 19.47 ? 839  SER B CB    1 
ATOM   14973 O  OG    . SER B 1  841  ? 17.979  26.639  85.440  1.00 22.80 ? 839  SER B OG    1 
ATOM   14974 N  N     . ALA B 1  842  ? 21.852  26.209  88.251  1.00 15.24 ? 840  ALA B N     1 
ATOM   14975 C  CA    . ALA B 1  842  ? 23.169  26.628  88.737  1.00 15.00 ? 840  ALA B CA    1 
ATOM   14976 C  C     . ALA B 1  842  ? 23.375  28.128  88.549  1.00 14.37 ? 840  ALA B C     1 
ATOM   14977 O  O     . ALA B 1  842  ? 24.457  28.587  88.191  1.00 15.31 ? 840  ALA B O     1 
ATOM   14978 C  CB    . ALA B 1  842  ? 24.290  25.821  88.069  1.00 16.79 ? 840  ALA B CB    1 
ATOM   14979 N  N     . GLY B 1  843  ? 22.316  28.897  88.799  1.00 14.52 ? 841  GLY B N     1 
ATOM   14980 C  CA    . GLY B 1  843  ? 22.408  30.341  88.717  1.00 16.23 ? 841  GLY B CA    1 
ATOM   14981 C  C     . GLY B 1  843  ? 22.611  30.858  87.315  1.00 16.22 ? 841  GLY B C     1 
ATOM   14982 O  O     . GLY B 1  843  ? 22.986  32.022  87.139  1.00 15.68 ? 841  GLY B O     1 
ATOM   14983 N  N     . GLN B 1  844  ? 22.388  30.020  86.314  1.00 14.65 ? 842  GLN B N     1 
ATOM   14984 C  CA    . GLN B 1  844  ? 22.639  30.418  84.929  1.00 14.10 ? 842  GLN B CA    1 
ATOM   14985 C  C     . GLN B 1  844  ? 21.371  30.952  84.283  1.00 16.32 ? 842  GLN B C     1 
ATOM   14986 O  O     . GLN B 1  844  ? 20.921  30.510  83.233  1.00 15.19 ? 842  GLN B O     1 
ATOM   14987 C  CB    . GLN B 1  844  ? 23.241  29.256  84.156  1.00 13.89 ? 842  GLN B CB    1 
ATOM   14988 C  CG    . GLN B 1  844  ? 24.637  28.947  84.717  1.00 15.48 ? 842  GLN B CG    1 
ATOM   14989 C  CD    . GLN B 1  844  ? 25.197  27.634  84.238  1.00 15.76 ? 842  GLN B CD    1 
ATOM   14990 O  OE1   . GLN B 1  844  ? 26.256  27.600  83.615  1.00 16.11 ? 842  GLN B OE1   1 
ATOM   14991 N  NE2   . GLN B 1  844  ? 24.519  26.544  84.564  1.00 15.27 ? 842  GLN B NE2   1 
ATOM   14992 N  N     . ARG B 1  845  ? 20.782  31.927  84.969  1.00 15.27 ? 843  ARG B N     1 
ATOM   14993 C  CA    . ARG B 1  845  ? 19.680  32.728  84.458  1.00 13.89 ? 843  ARG B CA    1 
ATOM   14994 C  C     . ARG B 1  845  ? 20.078  34.190  84.559  1.00 14.73 ? 843  ARG B C     1 
ATOM   14995 O  O     . ARG B 1  845  ? 20.653  34.615  85.560  1.00 13.66 ? 843  ARG B O     1 
ATOM   14996 C  CB    . ARG B 1  845  ? 18.393  32.510  85.267  1.00 14.52 ? 843  ARG B CB    1 
ATOM   14997 C  CG    . ARG B 1  845  ? 17.826  31.087  85.231  1.00 16.88 ? 843  ARG B CG    1 
ATOM   14998 C  CD    . ARG B 1  845  ? 16.476  31.048  85.974  1.00 20.54 ? 843  ARG B CD    1 
ATOM   14999 N  NE    . ARG B 1  845  ? 15.809  29.756  85.865  1.00 22.04 ? 843  ARG B NE    1 
ATOM   15000 C  CZ    . ARG B 1  845  ? 14.907  29.442  84.942  1.00 31.97 ? 843  ARG B CZ    1 
ATOM   15001 N  NH1   . ARG B 1  845  ? 14.460  30.338  84.072  1.00 30.79 ? 843  ARG B NH1   1 
ATOM   15002 N  NH2   . ARG B 1  845  ? 14.442  28.197  84.886  1.00 35.07 ? 843  ARG B NH2   1 
ATOM   15003 N  N     . CYS B 1  846  ? 19.757  34.978  83.539  1.00 15.21 ? 844  CYS B N     1 
ATOM   15004 C  CA    . CYS B 1  846  ? 20.016  36.410  83.657  1.00 16.80 ? 844  CYS B CA    1 
ATOM   15005 C  C     . CYS B 1  846  ? 19.251  37.011  84.826  1.00 13.54 ? 844  CYS B C     1 
ATOM   15006 O  O     . CYS B 1  846  ? 19.704  37.990  85.426  1.00 15.14 ? 844  CYS B O     1 
ATOM   15007 C  CB    . CYS B 1  846  ? 19.632  37.118  82.371  1.00 16.46 ? 844  CYS B CB    1 
ATOM   15008 S  SG    . CYS B 1  846  ? 17.959  36.757  81.843  1.00 15.93 ? 844  CYS B SG    1 
ATOM   15009 N  N     . SER B 1  847  ? 18.096  36.439  85.145  1.00 13.54 ? 845  SER B N     1 
ATOM   15010 C  CA    . SER B 1  847  ? 17.241  36.860  86.246  1.00 14.45 ? 845  SER B CA    1 
ATOM   15011 C  C     . SER B 1  847  ? 17.721  36.382  87.610  1.00 15.13 ? 845  SER B C     1 
ATOM   15012 O  O     . SER B 1  847  ? 17.117  36.761  88.622  1.00 14.44 ? 845  SER B O     1 
ATOM   15013 C  CB    . SER B 1  847  ? 15.845  36.308  86.012  1.00 16.16 ? 845  SER B CB    1 
ATOM   15014 O  OG    . SER B 1  847  ? 15.974  34.918  85.767  1.00 15.03 ? 845  SER B OG    1 
ATOM   15015 N  N     . ALA B 1  848  ? 18.765  35.553  87.665  1.00 15.06 ? 846  ALA B N     1 
ATOM   15016 C  CA    . ALA B 1  848  ? 19.121  34.863  88.901  1.00 14.69 ? 846  ALA B CA    1 
ATOM   15017 C  C     . ALA B 1  848  ? 19.438  35.842  90.028  1.00 15.74 ? 846  ALA B C     1 
ATOM   15018 O  O     . ALA B 1  848  ? 20.002  36.920  89.817  1.00 14.44 ? 846  ALA B O     1 
ATOM   15019 C  CB    . ALA B 1  848  ? 20.322  33.931  88.663  1.00 14.27 ? 846  ALA B CB    1 
ATOM   15020 N  N     . LEU B 1  849  ? 19.084  35.440  91.249  1.00 14.19 ? 847  LEU B N     1 
ATOM   15021 C  CA    . LEU B 1  849  ? 19.419  36.217  92.438  1.00 15.68 ? 847  LEU B CA    1 
ATOM   15022 C  C     . LEU B 1  849  ? 20.923  36.199  92.692  1.00 15.91 ? 847  LEU B C     1 
ATOM   15023 O  O     . LEU B 1  849  ? 21.505  35.131  92.896  1.00 16.05 ? 847  LEU B O     1 
ATOM   15024 C  CB    . LEU B 1  849  ? 18.670  35.648  93.637  1.00 16.29 ? 847  LEU B CB    1 
ATOM   15025 C  CG    . LEU B 1  849  ? 19.028  36.258  94.989  1.00 16.35 ? 847  LEU B CG    1 
ATOM   15026 C  CD1   . LEU B 1  849  ? 18.768  37.763  94.953  1.00 17.42 ? 847  LEU B CD1   1 
ATOM   15027 C  CD2   . LEU B 1  849  ? 18.201  35.577  96.074  1.00 17.22 ? 847  LEU B CD2   1 
ATOM   15028 N  N     . ARG B 1  850  ? 21.553  37.384  92.687  1.00 14.21 ? 848  ARG B N     1 
ATOM   15029 C  CA    . ARG B 1  850  ? 22.989  37.529  92.906  1.00 15.39 ? 848  ARG B CA    1 
ATOM   15030 C  C     . ARG B 1  850  ? 23.336  38.098  94.272  1.00 16.42 ? 848  ARG B C     1 
ATOM   15031 O  O     . ARG B 1  850  ? 24.422  37.821  94.787  1.00 16.51 ? 848  ARG B O     1 
ATOM   15032 C  CB    . ARG B 1  850  ? 23.618  38.446  91.843  1.00 14.87 ? 848  ARG B CB    1 
ATOM   15033 C  CG    . ARG B 1  850  ? 23.286  38.082  90.403  1.00 15.04 ? 848  ARG B CG    1 
ATOM   15034 C  CD    . ARG B 1  850  ? 23.682  36.650  90.112  1.00 14.70 ? 848  ARG B CD    1 
ATOM   15035 N  NE    . ARG B 1  850  ? 23.489  36.317  88.704  1.00 15.97 ? 848  ARG B NE    1 
ATOM   15036 C  CZ    . ARG B 1  850  ? 23.583  35.092  88.206  1.00 17.00 ? 848  ARG B CZ    1 
ATOM   15037 N  NH1   . ARG B 1  850  ? 23.821  34.049  88.985  1.00 15.45 ? 848  ARG B NH1   1 
ATOM   15038 N  NH2   . ARG B 1  850  ? 23.404  34.907  86.896  1.00 15.61 ? 848  ARG B NH2   1 
ATOM   15039 N  N     . VAL B 1  851  ? 22.468  38.925  94.849  1.00 16.26 ? 849  VAL B N     1 
ATOM   15040 C  CA    . VAL B 1  851  ? 22.763  39.600  96.112  1.00 15.88 ? 849  VAL B CA    1 
ATOM   15041 C  C     . VAL B 1  851  ? 21.536  39.505  97.007  1.00 17.44 ? 849  VAL B C     1 
ATOM   15042 O  O     . VAL B 1  851  ? 20.521  40.158  96.739  1.00 17.16 ? 849  VAL B O     1 
ATOM   15043 C  CB    . VAL B 1  851  ? 23.154  41.073  95.930  1.00 17.91 ? 849  VAL B CB    1 
ATOM   15044 C  CG1   . VAL B 1  851  ? 23.592  41.631  97.270  1.00 19.79 ? 849  VAL B CG1   1 
ATOM   15045 C  CG2   . VAL B 1  851  ? 24.253  41.242  94.899  1.00 18.36 ? 849  VAL B CG2   1 
ATOM   15046 N  N     . LEU B 1  852  ? 21.636  38.719  98.078  1.00 15.78 ? 850  LEU B N     1 
ATOM   15047 C  CA    . LEU B 1  852  ? 20.566  38.584  99.058  1.00 14.94 ? 850  LEU B CA    1 
ATOM   15048 C  C     . LEU B 1  852  ? 20.834  39.559  100.192 1.00 15.38 ? 850  LEU B C     1 
ATOM   15049 O  O     . LEU B 1  852  ? 21.873  39.466  100.850 1.00 16.87 ? 850  LEU B O     1 
ATOM   15050 C  CB    . LEU B 1  852  ? 20.511  37.156  99.592  1.00 15.18 ? 850  LEU B CB    1 
ATOM   15051 C  CG    . LEU B 1  852  ? 19.518  36.899  100.726 1.00 15.70 ? 850  LEU B CG    1 
ATOM   15052 C  CD1   . LEU B 1  852  ? 18.090  37.183  100.243 1.00 14.50 ? 850  LEU B CD1   1 
ATOM   15053 C  CD2   . LEU B 1  852  ? 19.640  35.448  101.176 1.00 17.51 ? 850  LEU B CD2   1 
ATOM   15054 N  N     . CYS B 1  853  ? 19.905  40.491  100.416 1.00 15.28 ? 851  CYS B N     1 
ATOM   15055 C  CA    . CYS B 1  853  ? 20.047  41.527  101.431 1.00 14.22 ? 851  CYS B CA    1 
ATOM   15056 C  C     . CYS B 1  853  ? 19.108  41.212  102.588 1.00 14.04 ? 851  CYS B C     1 
ATOM   15057 O  O     . CYS B 1  853  ? 17.882  41.271  102.437 1.00 16.41 ? 851  CYS B O     1 
ATOM   15058 C  CB    . CYS B 1  853  ? 19.751  42.900  100.844 1.00 15.31 ? 851  CYS B CB    1 
ATOM   15059 S  SG    . CYS B 1  853  ? 20.734  43.258  99.379  1.00 18.69 ? 851  CYS B SG    1 
ATOM   15060 N  N     . LEU B 1  854  ? 19.684  40.895  103.749 1.00 15.87 ? 852  LEU B N     1 
ATOM   15061 C  CA    . LEU B 1  854  ? 18.921  40.418  104.896 1.00 15.63 ? 852  LEU B CA    1 
ATOM   15062 C  C     . LEU B 1  854  ? 18.960  41.457  106.002 1.00 15.56 ? 852  LEU B C     1 
ATOM   15063 O  O     . LEU B 1  854  ? 20.045  41.905  106.391 1.00 18.02 ? 852  LEU B O     1 
ATOM   15064 C  CB    . LEU B 1  854  ? 19.495  39.103  105.430 1.00 15.40 ? 852  LEU B CB    1 
ATOM   15065 C  CG    . LEU B 1  854  ? 19.509  37.915  104.474 1.00 16.18 ? 852  LEU B CG    1 
ATOM   15066 C  CD1   . LEU B 1  854  ? 20.239  36.741  105.111 1.00 14.89 ? 852  LEU B CD1   1 
ATOM   15067 C  CD2   . LEU B 1  854  ? 18.093  37.532  104.091 1.00 16.85 ? 852  LEU B CD2   1 
ATOM   15068 N  N     . GLN B 1  855  ? 17.790  41.809  106.530 1.00 16.62 ? 853  GLN B N     1 
ATOM   15069 C  CA    . GLN B 1  855  ? 17.771  42.692  107.687 1.00 16.40 ? 853  GLN B CA    1 
ATOM   15070 C  C     . GLN B 1  855  ? 18.569  42.043  108.810 1.00 19.71 ? 853  GLN B C     1 
ATOM   15071 O  O     . GLN B 1  855  ? 18.498  40.826  109.012 1.00 17.82 ? 853  GLN B O     1 
ATOM   15072 C  CB    . GLN B 1  855  ? 16.341  42.975  108.139 1.00 16.90 ? 853  GLN B CB    1 
ATOM   15073 C  CG    . GLN B 1  855  ? 16.291  44.103  109.171 1.00 19.32 ? 853  GLN B CG    1 
ATOM   15074 C  CD    . GLN B 1  855  ? 14.882  44.438  109.609 1.00 23.81 ? 853  GLN B CD    1 
ATOM   15075 O  OE1   . GLN B 1  855  ? 13.963  44.517  108.793 1.00 24.43 ? 853  GLN B OE1   1 
ATOM   15076 N  NE2   . GLN B 1  855  ? 14.707  44.662  110.908 1.00 25.45 ? 853  GLN B NE2   1 
ATOM   15077 N  N     . GLU B 1  856  ? 19.366  42.859  109.508 1.00 18.43 ? 854  GLU B N     1 
ATOM   15078 C  CA    . GLU B 1  856  ? 20.393  42.327  110.413 1.00 19.07 ? 854  GLU B CA    1 
ATOM   15079 C  C     . GLU B 1  856  ? 19.800  41.370  111.440 1.00 21.79 ? 854  GLU B C     1 
ATOM   15080 O  O     . GLU B 1  856  ? 20.419  40.354  111.790 1.00 23.11 ? 854  GLU B O     1 
ATOM   15081 C  CB    . GLU B 1  856  ? 21.113  43.486  111.112 1.00 24.01 ? 854  GLU B CB    1 
ATOM   15082 N  N     . ASP B 1  857  ? 18.588  41.669  111.918 1.00 22.92 ? 855  ASP B N     1 
ATOM   15083 C  CA    . ASP B 1  857  ? 17.986  40.938  113.029 1.00 21.44 ? 855  ASP B CA    1 
ATOM   15084 C  C     . ASP B 1  857  ? 17.553  39.528  112.658 1.00 22.71 ? 855  ASP B C     1 
ATOM   15085 O  O     . ASP B 1  857  ? 17.441  38.678  113.546 1.00 25.02 ? 855  ASP B O     1 
ATOM   15086 C  CB    . ASP B 1  857  ? 16.784  41.715  113.572 1.00 27.32 ? 855  ASP B CB    1 
ATOM   15087 N  N     . VAL B 1  858  ? 17.285  39.258  111.381 1.00 19.53 ? 856  VAL B N     1 
ATOM   15088 C  CA    . VAL B 1  858  ? 16.876  37.929  110.944 1.00 19.71 ? 856  VAL B CA    1 
ATOM   15089 C  C     . VAL B 1  858  ? 17.941  37.241  110.111 1.00 19.02 ? 856  VAL B C     1 
ATOM   15090 O  O     . VAL B 1  858  ? 17.724  36.100  109.682 1.00 18.91 ? 856  VAL B O     1 
ATOM   15091 C  CB    . VAL B 1  858  ? 15.552  37.972  110.159 1.00 18.95 ? 856  VAL B CB    1 
ATOM   15092 C  CG1   . VAL B 1  858  ? 14.423  38.461  111.038 1.00 21.91 ? 856  VAL B CG1   1 
ATOM   15093 C  CG2   . VAL B 1  858  ? 15.714  38.848  108.928 1.00 18.56 ? 856  VAL B CG2   1 
ATOM   15094 N  N     . ALA B 1  859  ? 19.085  37.887  109.869 1.00 19.21 ? 857  ALA B N     1 
ATOM   15095 C  CA    . ALA B 1  859  ? 20.041  37.352  108.899 1.00 17.89 ? 857  ALA B CA    1 
ATOM   15096 C  C     . ALA B 1  859  ? 20.560  35.979  109.317 1.00 18.73 ? 857  ALA B C     1 
ATOM   15097 O  O     . ALA B 1  859  ? 20.572  35.039  108.512 1.00 18.63 ? 857  ALA B O     1 
ATOM   15098 C  CB    . ALA B 1  859  ? 21.190  38.339  108.688 1.00 18.43 ? 857  ALA B CB    1 
ATOM   15099 N  N     . ASP B 1  860  ? 20.969  35.834  110.584 1.00 20.58 ? 858  ASP B N     1 
ATOM   15100 C  CA    . ASP B 1  860  ? 21.545  34.566  111.032 1.00 20.83 ? 858  ASP B CA    1 
ATOM   15101 C  C     . ASP B 1  860  ? 20.553  33.420  110.920 1.00 18.40 ? 858  ASP B C     1 
ATOM   15102 O  O     . ASP B 1  860  ? 20.909  32.332  110.449 1.00 18.73 ? 858  ASP B O     1 
ATOM   15103 C  CB    . ASP B 1  860  ? 22.044  34.686  112.473 1.00 19.74 ? 858  ASP B CB    1 
ATOM   15104 C  CG    . ASP B 1  860  ? 23.268  35.551  112.585 1.00 24.54 ? 858  ASP B CG    1 
ATOM   15105 O  OD1   . ASP B 1  860  ? 24.026  35.642  111.598 1.00 26.42 ? 858  ASP B OD1   1 
ATOM   15106 O  OD2   . ASP B 1  860  ? 23.472  36.137  113.662 1.00 29.05 ? 858  ASP B OD2   1 
ATOM   15107 N  N     . ARG B 1  861  ? 19.302  33.635  111.342 1.00 18.88 ? 859  ARG B N     1 
ATOM   15108 C  CA    . ARG B 1  861  ? 18.327  32.551  111.286 1.00 19.91 ? 859  ARG B CA    1 
ATOM   15109 C  C     . ARG B 1  861  ? 18.013  32.154  109.849 1.00 19.08 ? 859  ARG B C     1 
ATOM   15110 O  O     . ARG B 1  861  ? 17.936  30.961  109.531 1.00 18.87 ? 859  ARG B O     1 
ATOM   15111 C  CB    . ARG B 1  861  ? 17.050  32.945  112.024 1.00 23.87 ? 859  ARG B CB    1 
ATOM   15112 C  CG    . ARG B 1  861  ? 15.948  31.921  111.876 1.00 31.32 ? 859  ARG B CG    1 
ATOM   15113 C  CD    . ARG B 1  861  ? 14.910  32.017  112.979 1.00 38.27 ? 859  ARG B CD    1 
ATOM   15114 N  NE    . ARG B 1  861  ? 13.854  31.037  112.758 1.00 42.40 ? 859  ARG B NE    1 
ATOM   15115 C  CZ    . ARG B 1  861  ? 12.772  31.263  112.025 1.00 39.27 ? 859  ARG B CZ    1 
ATOM   15116 N  NH1   . ARG B 1  861  ? 12.548  32.445  111.471 1.00 37.75 ? 859  ARG B NH1   1 
ATOM   15117 N  NH2   . ARG B 1  861  ? 11.895  30.279  111.842 1.00 39.62 ? 859  ARG B NH2   1 
ATOM   15118 N  N     . ILE B 1  862  ? 17.866  33.136  108.960 1.00 17.15 ? 860  ILE B N     1 
ATOM   15119 C  CA    . ILE B 1  862  ? 17.622  32.831  107.554 1.00 16.05 ? 860  ILE B CA    1 
ATOM   15120 C  C     . ILE B 1  862  ? 18.820  32.114  106.930 1.00 14.83 ? 860  ILE B C     1 
ATOM   15121 O  O     . ILE B 1  862  ? 18.649  31.162  106.153 1.00 17.25 ? 860  ILE B O     1 
ATOM   15122 C  CB    . ILE B 1  862  ? 17.255  34.121  106.805 1.00 16.94 ? 860  ILE B CB    1 
ATOM   15123 C  CG1   . ILE B 1  862  ? 15.854  34.575  107.244 1.00 20.07 ? 860  ILE B CG1   1 
ATOM   15124 C  CG2   . ILE B 1  862  ? 17.335  33.914  105.294 1.00 17.13 ? 860  ILE B CG2   1 
ATOM   15125 C  CD1   . ILE B 1  862  ? 15.455  35.962  106.736 1.00 21.31 ? 860  ILE B CD1   1 
ATOM   15126 N  N     . LEU B 1  863  ? 20.041  32.549  107.246 1.00 17.50 ? 861  LEU B N     1 
ATOM   15127 C  CA    . LEU B 1  863  ? 21.215  31.897  106.663 1.00 18.70 ? 861  LEU B CA    1 
ATOM   15128 C  C     . LEU B 1  863  ? 21.357  30.461  107.156 1.00 20.58 ? 861  LEU B C     1 
ATOM   15129 O  O     . LEU B 1  863  ? 21.731  29.568  106.386 1.00 18.40 ? 861  LEU B O     1 
ATOM   15130 C  CB    . LEU B 1  863  ? 22.481  32.691  106.977 1.00 19.58 ? 861  LEU B CB    1 
ATOM   15131 C  CG    . LEU B 1  863  ? 22.590  34.015  106.233 1.00 19.13 ? 861  LEU B CG    1 
ATOM   15132 C  CD1   . LEU B 1  863  ? 23.724  34.863  106.812 1.00 22.01 ? 861  LEU B CD1   1 
ATOM   15133 C  CD2   . LEU B 1  863  ? 22.794  33.761  104.734 1.00 23.27 ? 861  LEU B CD2   1 
ATOM   15134 N  N     . THR B 1  864  ? 21.080  30.216  108.437 1.00 19.68 ? 862  THR B N     1 
ATOM   15135 C  CA    . THR B 1  864  ? 21.129  28.839  108.925 1.00 18.84 ? 862  THR B CA    1 
ATOM   15136 C  C     . THR B 1  864  ? 20.126  27.967  108.184 1.00 21.11 ? 862  THR B C     1 
ATOM   15137 O  O     . THR B 1  864  ? 20.436  26.838  107.787 1.00 19.68 ? 862  THR B O     1 
ATOM   15138 C  CB    . THR B 1  864  ? 20.876  28.804  110.435 1.00 22.07 ? 862  THR B CB    1 
ATOM   15139 O  OG1   . THR B 1  864  ? 21.970  29.431  111.105 1.00 23.98 ? 862  THR B OG1   1 
ATOM   15140 C  CG2   . THR B 1  864  ? 20.738  27.354  110.938 1.00 24.43 ? 862  THR B CG2   1 
ATOM   15141 N  N     . MET B 1  865  ? 18.926  28.493  107.955 1.00 18.95 ? 863  MET B N     1 
ATOM   15142 C  CA    . MET B 1  865  ? 17.899  27.720  107.274 1.00 16.97 ? 863  MET B CA    1 
ATOM   15143 C  C     . MET B 1  865  ? 18.266  27.510  105.807 1.00 17.14 ? 863  MET B C     1 
ATOM   15144 O  O     . MET B 1  865  ? 18.085  26.417  105.259 1.00 16.83 ? 863  MET B O     1 
ATOM   15145 C  CB    . MET B 1  865  ? 16.562  28.439  107.411 1.00 19.07 ? 863  MET B CB    1 
ATOM   15146 C  CG    . MET B 1  865  ? 15.401  27.703  106.813 1.00 19.06 ? 863  MET B CG    1 
ATOM   15147 S  SD    . MET B 1  865  ? 13.860  28.610  107.017 1.00 23.45 ? 863  MET B SD    1 
ATOM   15148 C  CE    . MET B 1  865  ? 13.871  28.923  108.774 1.00 23.62 ? 863  MET B CE    1 
ATOM   15149 N  N     . LEU B 1  866  ? 18.803  28.549  105.168 1.00 16.88 ? 864  LEU B N     1 
ATOM   15150 C  CA    . LEU B 1  866  ? 19.232  28.428  103.780 1.00 15.81 ? 864  LEU B CA    1 
ATOM   15151 C  C     . LEU B 1  866  ? 20.319  27.367  103.634 1.00 17.34 ? 864  LEU B C     1 
ATOM   15152 O  O     . LEU B 1  866  ? 20.265  26.521  102.734 1.00 16.81 ? 864  LEU B O     1 
ATOM   15153 C  CB    . LEU B 1  866  ? 19.732  29.784  103.289 1.00 16.97 ? 864  LEU B CB    1 
ATOM   15154 C  CG    . LEU B 1  866  ? 20.371  29.803  101.906 1.00 16.96 ? 864  LEU B CG    1 
ATOM   15155 C  CD1   . LEU B 1  866  ? 19.359  29.342  100.869 1.00 19.62 ? 864  LEU B CD1   1 
ATOM   15156 C  CD2   . LEU B 1  866  ? 20.866  31.221  101.604 1.00 18.76 ? 864  LEU B CD2   1 
ATOM   15157 N  N     . LYS B 1  867  ? 21.313  27.393  104.523 1.00 17.85 ? 865  LYS B N     1 
ATOM   15158 C  CA    . LYS B 1  867  ? 22.388  26.415  104.429 1.00 17.96 ? 865  LYS B CA    1 
ATOM   15159 C  C     . LYS B 1  867  ? 21.866  25.007  104.677 1.00 19.20 ? 865  LYS B C     1 
ATOM   15160 O  O     . LYS B 1  867  ? 22.269  24.066  103.992 1.00 17.78 ? 865  LYS B O     1 
ATOM   15161 C  CB    . LYS B 1  867  ? 23.512  26.777  105.409 1.00 16.91 ? 865  LYS B CB    1 
ATOM   15162 C  CG    . LYS B 1  867  ? 24.244  28.037  104.962 1.00 21.90 ? 865  LYS B CG    1 
ATOM   15163 C  CD    . LYS B 1  867  ? 25.041  28.678  106.072 1.00 25.10 ? 865  LYS B CD    1 
ATOM   15164 C  CE    . LYS B 1  867  ? 25.627  30.004  105.599 1.00 28.23 ? 865  LYS B CE    1 
ATOM   15165 N  NZ    . LYS B 1  867  ? 26.511  30.633  106.631 1.00 31.88 ? 865  LYS B NZ    1 
ATOM   15166 N  N     . GLY B 1  868  ? 20.945  24.847  105.630 1.00 18.62 ? 866  GLY B N     1 
ATOM   15167 C  CA    . GLY B 1  868  ? 20.343  23.536  105.826 1.00 18.46 ? 866  GLY B CA    1 
ATOM   15168 C  C     . GLY B 1  868  ? 19.579  23.062  104.603 1.00 18.54 ? 866  GLY B C     1 
ATOM   15169 O  O     . GLY B 1  868  ? 19.664  21.895  104.215 1.00 19.39 ? 866  GLY B O     1 
ATOM   15170 N  N     . ALA B 1  869  ? 18.827  23.964  103.973 1.00 18.47 ? 867  ALA B N     1 
ATOM   15171 C  CA    . ALA B 1  869  ? 18.097  23.598  102.766 1.00 18.90 ? 867  ALA B CA    1 
ATOM   15172 C  C     . ALA B 1  869  ? 19.051  23.273  101.623 1.00 17.73 ? 867  ALA B C     1 
ATOM   15173 O  O     . ALA B 1  869  ? 18.792  22.360  100.832 1.00 18.93 ? 867  ALA B O     1 
ATOM   15174 C  CB    . ALA B 1  869  ? 17.147  24.731  102.373 1.00 17.75 ? 867  ALA B CB    1 
ATOM   15175 N  N     . LEU B 1  870  ? 20.159  24.010  101.517 1.00 16.56 ? 868  LEU B N     1 
ATOM   15176 C  CA    . LEU B 1  870  ? 21.131  23.719  100.461 1.00 18.74 ? 868  LEU B CA    1 
ATOM   15177 C  C     . LEU B 1  870  ? 21.737  22.329  100.614 1.00 18.26 ? 868  LEU B C     1 
ATOM   15178 O  O     . LEU B 1  870  ? 22.104  21.700  99.614  1.00 18.50 ? 868  LEU B O     1 
ATOM   15179 C  CB    . LEU B 1  870  ? 22.246  24.770  100.450 1.00 19.41 ? 868  LEU B CB    1 
ATOM   15180 C  CG    . LEU B 1  870  ? 21.908  26.117  99.816  1.00 22.14 ? 868  LEU B CG    1 
ATOM   15181 C  CD1   . LEU B 1  870  ? 23.085  27.063  99.951  1.00 21.83 ? 868  LEU B CD1   1 
ATOM   15182 C  CD2   . LEU B 1  870  ? 21.542  25.917  98.344  1.00 19.46 ? 868  LEU B CD2   1 
ATOM   15183 N  N     . HIS B 1  871  ? 21.856  21.832  101.846 1.00 17.08 ? 869  HIS B N     1 
ATOM   15184 C  CA    . HIS B 1  871  ? 22.423  20.506  102.041 1.00 19.85 ? 869  HIS B CA    1 
ATOM   15185 C  C     . HIS B 1  871  ? 21.507  19.405  101.543 1.00 21.09 ? 869  HIS B C     1 
ATOM   15186 O  O     . HIS B 1  871  ? 21.958  18.265  101.394 1.00 21.30 ? 869  HIS B O     1 
ATOM   15187 C  CB    . HIS B 1  871  ? 22.767  20.278  103.516 1.00 23.20 ? 869  HIS B CB    1 
ATOM   15188 C  CG    . HIS B 1  871  ? 24.132  20.772  103.895 1.00 30.73 ? 869  HIS B CG    1 
ATOM   15189 N  ND1   . HIS B 1  871  ? 24.335  21.920  104.634 1.00 29.66 ? 869  HIS B ND1   1 
ATOM   15190 C  CD2   . HIS B 1  871  ? 25.365  20.283  103.613 1.00 33.11 ? 869  HIS B CD2   1 
ATOM   15191 C  CE1   . HIS B 1  871  ? 25.633  22.107  104.806 1.00 32.26 ? 869  HIS B CE1   1 
ATOM   15192 N  NE2   . HIS B 1  871  ? 26.280  21.133  104.188 1.00 33.68 ? 869  HIS B NE2   1 
ATOM   15193 N  N     . GLU B 1  872  ? 20.249  19.714  101.262 1.00 16.85 ? 870  GLU B N     1 
ATOM   15194 C  CA    . GLU B 1  872  ? 19.329  18.714  100.757 1.00 17.57 ? 870  GLU B CA    1 
ATOM   15195 C  C     . GLU B 1  872  ? 19.265  18.673  99.242  1.00 18.13 ? 870  GLU B C     1 
ATOM   15196 O  O     . GLU B 1  872  ? 18.504  17.872  98.693  1.00 18.65 ? 870  GLU B O     1 
ATOM   15197 C  CB    . GLU B 1  872  ? 17.939  18.960  101.337 1.00 19.78 ? 870  GLU B CB    1 
ATOM   15198 C  CG    . GLU B 1  872  ? 17.959  18.959  102.847 1.00 19.79 ? 870  GLU B CG    1 
ATOM   15199 C  CD    . GLU B 1  872  ? 18.285  17.597  103.412 1.00 17.58 ? 870  GLU B CD    1 
ATOM   15200 O  OE1   . GLU B 1  872  ? 18.004  16.590  102.735 1.00 21.29 ? 870  GLU B OE1   1 
ATOM   15201 O  OE2   . GLU B 1  872  ? 18.823  17.527  104.532 1.00 20.85 ? 870  GLU B OE2   1 
ATOM   15202 N  N     . LEU B 1  873  ? 20.043  19.498  98.551  1.00 17.73 ? 871  LEU B N     1 
ATOM   15203 C  CA    . LEU B 1  873  ? 19.969  19.542  97.098  1.00 18.55 ? 871  LEU B CA    1 
ATOM   15204 C  C     . LEU B 1  873  ? 20.862  18.477  96.485  1.00 18.40 ? 871  LEU B C     1 
ATOM   15205 O  O     . LEU B 1  873  ? 21.926  18.158  97.009  1.00 19.13 ? 871  LEU B O     1 
ATOM   15206 C  CB    . LEU B 1  873  ? 20.392  20.910  96.568  1.00 18.79 ? 871  LEU B CB    1 
ATOM   15207 C  CG    . LEU B 1  873  ? 19.518  22.097  96.938  1.00 20.79 ? 871  LEU B CG    1 
ATOM   15208 C  CD1   . LEU B 1  873  ? 20.006  23.309  96.164  1.00 21.96 ? 871  LEU B CD1   1 
ATOM   15209 C  CD2   . LEU B 1  873  ? 18.040  21.812  96.633  1.00 18.63 ? 871  LEU B CD2   1 
ATOM   15210 N  N     . HIS B 1  874  ? 20.436  17.962  95.340  1.00 18.89 ? 872  HIS B N     1 
ATOM   15211 C  CA    . HIS B 1  874  ? 21.181  16.953  94.598  1.00 20.11 ? 872  HIS B CA    1 
ATOM   15212 C  C     . HIS B 1  874  ? 21.781  17.627  93.364  1.00 18.40 ? 872  HIS B C     1 
ATOM   15213 O  O     . HIS B 1  874  ? 21.042  18.099  92.491  1.00 18.71 ? 872  HIS B O     1 
ATOM   15214 C  CB    . HIS B 1  874  ? 20.243  15.800  94.240  1.00 17.96 ? 872  HIS B CB    1 
ATOM   15215 C  CG    . HIS B 1  874  ? 20.876  14.685  93.472  1.00 20.13 ? 872  HIS B CG    1 
ATOM   15216 N  ND1   . HIS B 1  874  ? 22.211  14.662  93.128  1.00 25.66 ? 872  HIS B ND1   1 
ATOM   15217 C  CD2   . HIS B 1  874  ? 20.338  13.553  92.964  1.00 21.64 ? 872  HIS B CD2   1 
ATOM   15218 C  CE1   . HIS B 1  874  ? 22.469  13.561  92.444  1.00 23.22 ? 872  HIS B CE1   1 
ATOM   15219 N  NE2   . HIS B 1  874  ? 21.347  12.876  92.321  1.00 25.84 ? 872  HIS B NE2   1 
ATOM   15220 N  N     . ILE B 1  875  ? 23.114  17.692  93.307  1.00 17.26 ? 873  ILE B N     1 
ATOM   15221 C  CA    . ILE B 1  875  ? 23.839  18.278  92.181  1.00 19.70 ? 873  ILE B CA    1 
ATOM   15222 C  C     . ILE B 1  875  ? 24.370  17.148  91.312  1.00 17.71 ? 873  ILE B C     1 
ATOM   15223 O  O     . ILE B 1  875  ? 25.041  16.243  91.820  1.00 21.00 ? 873  ILE B O     1 
ATOM   15224 C  CB    . ILE B 1  875  ? 25.008  19.151  92.657  1.00 23.52 ? 873  ILE B CB    1 
ATOM   15225 C  CG1   . ILE B 1  875  ? 24.526  20.243  93.614  1.00 24.44 ? 873  ILE B CG1   1 
ATOM   15226 C  CG2   . ILE B 1  875  ? 25.762  19.740  91.451  1.00 22.11 ? 873  ILE B CG2   1 
ATOM   15227 C  CD1   . ILE B 1  875  ? 25.579  20.606  94.646  1.00 31.88 ? 873  ILE B CD1   1 
ATOM   15228 N  N     . GLY B 1  876  ? 24.100  17.202  90.011  1.00 17.62 ? 874  GLY B N     1 
ATOM   15229 C  CA    . GLY B 1  876  ? 24.634  16.170  89.145  1.00 19.45 ? 874  GLY B CA    1 
ATOM   15230 C  C     . GLY B 1  876  ? 24.072  16.248  87.740  1.00 18.35 ? 874  GLY B C     1 
ATOM   15231 O  O     . GLY B 1  876  ? 23.448  17.233  87.348  1.00 17.39 ? 874  GLY B O     1 
ATOM   15232 N  N     . ARG B 1  877  ? 24.336  15.180  86.983  1.00 18.07 ? 875  ARG B N     1 
ATOM   15233 C  CA    . ARG B 1  877  ? 23.852  15.099  85.616  1.00 17.43 ? 875  ARG B CA    1 
ATOM   15234 C  C     . ARG B 1  877  ? 22.329  15.104  85.627  1.00 20.19 ? 875  ARG B C     1 
ATOM   15235 O  O     . ARG B 1  877  ? 21.705  14.389  86.411  1.00 20.57 ? 875  ARG B O     1 
ATOM   15236 C  CB    . ARG B 1  877  ? 24.390  13.838  84.940  1.00 20.02 ? 875  ARG B CB    1 
ATOM   15237 C  CG    . ARG B 1  877  ? 24.352  13.919  83.420  1.00 23.33 ? 875  ARG B CG    1 
ATOM   15238 C  CD    . ARG B 1  877  ? 24.984  12.696  82.776  1.00 29.33 ? 875  ARG B CD    1 
ATOM   15239 N  NE    . ARG B 1  877  ? 24.073  11.565  82.679  1.00 26.26 ? 875  ARG B NE    1 
ATOM   15240 C  CZ    . ARG B 1  877  ? 24.391  10.404  82.122  1.00 34.42 ? 875  ARG B CZ    1 
ATOM   15241 N  NH1   . ARG B 1  877  ? 25.612  10.172  81.657  1.00 28.75 ? 875  ARG B NH1   1 
ATOM   15242 N  NH2   . ARG B 1  877  ? 23.466  9.449   82.033  1.00 32.84 ? 875  ARG B NH2   1 
ATOM   15243 N  N     . THR B 1  878  ? 21.729  15.911  84.751  1.00 15.62 ? 876  THR B N     1 
ATOM   15244 C  CA    . THR B 1  878  ? 20.337  16.319  84.908  1.00 18.88 ? 876  THR B CA    1 
ATOM   15245 C  C     . THR B 1  878  ? 19.332  15.334  84.311  1.00 16.95 ? 876  THR B C     1 
ATOM   15246 O  O     . THR B 1  878  ? 18.129  15.627  84.283  1.00 17.36 ? 876  THR B O     1 
ATOM   15247 C  CB    . THR B 1  878  ? 20.142  17.708  84.300  1.00 17.12 ? 876  THR B CB    1 
ATOM   15248 O  OG1   . THR B 1  878  ? 20.700  17.747  82.976  1.00 20.80 ? 876  THR B OG1   1 
ATOM   15249 C  CG2   . THR B 1  878  ? 20.827  18.753  85.145  1.00 19.24 ? 876  THR B CG2   1 
ATOM   15250 N  N     . ASP B 1  879  ? 19.777  14.169  83.844  1.00 18.66 ? 877  ASP B N     1 
ATOM   15251 C  CA    . ASP B 1  879  ? 18.855  13.186  83.284  1.00 19.85 ? 877  ASP B CA    1 
ATOM   15252 C  C     . ASP B 1  879  ? 18.273  12.260  84.352  1.00 18.89 ? 877  ASP B C     1 
ATOM   15253 O  O     . ASP B 1  879  ? 17.936  11.110  84.066  1.00 18.98 ? 877  ASP B O     1 
ATOM   15254 C  CB    . ASP B 1  879  ? 19.534  12.396  82.162  1.00 19.88 ? 877  ASP B CB    1 
ATOM   15255 C  CG    . ASP B 1  879  ? 20.731  11.580  82.632  1.00 24.50 ? 877  ASP B CG    1 
ATOM   15256 O  OD1   . ASP B 1  879  ? 21.475  12.007  83.550  1.00 27.19 ? 877  ASP B OD1   1 
ATOM   15257 O  OD2   . ASP B 1  879  ? 20.927  10.492  82.061  1.00 26.07 ? 877  ASP B OD2   1 
ATOM   15258 N  N     . ARG B 1  880  ? 18.158  12.750  85.584  1.00 21.42 ? 878  ARG B N     1 
ATOM   15259 C  CA    . ARG B 1  880  ? 17.482  12.081  86.688  1.00 21.66 ? 878  ARG B CA    1 
ATOM   15260 C  C     . ARG B 1  880  ? 16.527  13.080  87.315  1.00 19.67 ? 878  ARG B C     1 
ATOM   15261 O  O     . ARG B 1  880  ? 16.917  14.219  87.592  1.00 18.32 ? 878  ARG B O     1 
ATOM   15262 C  CB    . ARG B 1  880  ? 18.471  11.589  87.755  1.00 20.87 ? 878  ARG B CB    1 
ATOM   15263 C  CG    . ARG B 1  880  ? 19.206  10.328  87.378  1.00 26.71 ? 878  ARG B CG    1 
ATOM   15264 C  CD    . ARG B 1  880  ? 20.122  9.834   88.488  1.00 31.24 ? 878  ARG B CD    1 
ATOM   15265 N  NE    . ARG B 1  880  ? 20.923  8.726   87.982  1.00 44.73 ? 878  ARG B NE    1 
ATOM   15266 C  CZ    . ARG B 1  880  ? 21.907  8.135   88.643  1.00 49.66 ? 878  ARG B CZ    1 
ATOM   15267 N  NH1   . ARG B 1  880  ? 22.240  8.507   89.868  1.00 60.96 ? 878  ARG B NH1   1 
ATOM   15268 N  NH2   . ARG B 1  880  ? 22.577  7.146   88.057  1.00 49.47 ? 878  ARG B NH2   1 
ATOM   15269 N  N     . LEU B 1  881  ? 15.289  12.649  87.561  1.00 17.68 ? 879  LEU B N     1 
ATOM   15270 C  CA    . LEU B 1  881  ? 14.314  13.543  88.173  1.00 17.17 ? 879  LEU B CA    1 
ATOM   15271 C  C     . LEU B 1  881  ? 14.780  14.033  89.539  1.00 17.99 ? 879  LEU B C     1 
ATOM   15272 O  O     . LEU B 1  881  ? 14.465  15.164  89.936  1.00 18.19 ? 879  LEU B O     1 
ATOM   15273 C  CB    . LEU B 1  881  ? 12.975  12.827  88.291  1.00 19.55 ? 879  LEU B CB    1 
ATOM   15274 C  CG    . LEU B 1  881  ? 11.809  13.615  88.884  1.00 20.44 ? 879  LEU B CG    1 
ATOM   15275 C  CD1   . LEU B 1  881  ? 11.394  14.737  87.935  1.00 21.27 ? 879  LEU B CD1   1 
ATOM   15276 C  CD2   . LEU B 1  881  ? 10.665  12.668  89.136  1.00 20.08 ? 879  LEU B CD2   1 
ATOM   15277 N  N     . SER B 1  882  ? 15.562  13.221  90.256  1.00 17.13 ? 880  SER B N     1 
ATOM   15278 C  CA    . SER B 1  882  ? 16.026  13.596  91.583  1.00 17.84 ? 880  SER B CA    1 
ATOM   15279 C  C     . SER B 1  882  ? 17.089  14.690  91.573  1.00 19.43 ? 880  SER B C     1 
ATOM   15280 O  O     . SER B 1  882  ? 17.471  15.151  92.651  1.00 19.09 ? 880  SER B O     1 
ATOM   15281 C  CB    . SER B 1  882  ? 16.581  12.368  92.306  1.00 19.73 ? 880  SER B CB    1 
ATOM   15282 O  OG    . SER B 1  882  ? 17.769  11.919  91.662  1.00 22.11 ? 880  SER B OG    1 
ATOM   15283 N  N     . VAL B 1  883  ? 17.594  15.108  90.415  1.00 18.11 ? 881  VAL B N     1 
ATOM   15284 C  CA    . VAL B 1  883  ? 18.658  16.108  90.381  1.00 18.80 ? 881  VAL B CA    1 
ATOM   15285 C  C     . VAL B 1  883  ? 18.044  17.498  90.424  1.00 17.24 ? 881  VAL B C     1 
ATOM   15286 O  O     . VAL B 1  883  ? 17.114  17.806  89.668  1.00 20.73 ? 881  VAL B O     1 
ATOM   15287 C  CB    . VAL B 1  883  ? 19.558  15.931  89.148  1.00 19.61 ? 881  VAL B CB    1 
ATOM   15288 C  CG1   . VAL B 1  883  ? 20.520  17.114  89.017  1.00 18.97 ? 881  VAL B CG1   1 
ATOM   15289 C  CG2   . VAL B 1  883  ? 20.329  14.640  89.273  1.00 19.63 ? 881  VAL B CG2   1 
ATOM   15290 N  N     . ASP B 1  884  ? 18.560  18.328  91.323  1.00 18.66 ? 882  ASP B N     1 
ATOM   15291 C  CA    . ASP B 1  884  ? 18.089  19.682  91.571  1.00 17.09 ? 882  ASP B CA    1 
ATOM   15292 C  C     . ASP B 1  884  ? 18.904  20.742  90.848  1.00 20.04 ? 882  ASP B C     1 
ATOM   15293 O  O     . ASP B 1  884  ? 18.329  21.689  90.313  1.00 23.08 ? 882  ASP B O     1 
ATOM   15294 C  CB    . ASP B 1  884  ? 18.133  19.973  93.071  1.00 17.64 ? 882  ASP B CB    1 
ATOM   15295 C  CG    . ASP B 1  884  ? 17.238  19.033  93.861  1.00 19.30 ? 882  ASP B CG    1 
ATOM   15296 O  OD1   . ASP B 1  884  ? 16.054  18.917  93.489  1.00 19.17 ? 882  ASP B OD1   1 
ATOM   15297 O  OD2   . ASP B 1  884  ? 17.724  18.396  94.820  1.00 18.73 ? 882  ASP B OD2   1 
ATOM   15298 N  N     . VAL B 1  885  ? 20.230  20.613  90.855  1.00 19.02 ? 883  VAL B N     1 
ATOM   15299 C  CA    . VAL B 1  885  ? 21.147  21.615  90.316  1.00 17.19 ? 883  VAL B CA    1 
ATOM   15300 C  C     . VAL B 1  885  ? 22.042  20.917  89.304  1.00 19.65 ? 883  VAL B C     1 
ATOM   15301 O  O     . VAL B 1  885  ? 22.682  19.910  89.627  1.00 18.68 ? 883  VAL B O     1 
ATOM   15302 C  CB    . VAL B 1  885  ? 21.993  22.278  91.423  1.00 20.08 ? 883  VAL B CB    1 
ATOM   15303 C  CG1   . VAL B 1  885  ? 23.071  23.215  90.825  1.00 19.54 ? 883  VAL B CG1   1 
ATOM   15304 C  CG2   . VAL B 1  885  ? 21.108  23.034  92.395  1.00 21.20 ? 883  VAL B CG2   1 
ATOM   15305 N  N     . GLY B 1  886  ? 22.076  21.447  88.089  1.00 18.96 ? 884  GLY B N     1 
ATOM   15306 C  CA    . GLY B 1  886  ? 22.869  20.878  87.031  1.00 18.78 ? 884  GLY B CA    1 
ATOM   15307 C  C     . GLY B 1  886  ? 24.238  21.513  86.922  1.00 16.46 ? 884  GLY B C     1 
ATOM   15308 O  O     . GLY B 1  886  ? 24.676  22.273  87.792  1.00 16.72 ? 884  GLY B O     1 
ATOM   15309 N  N     . PRO B 1  887  ? 24.942  21.195  85.842  1.00 15.98 ? 885  PRO B N     1 
ATOM   15310 C  CA    . PRO B 1  887  ? 26.298  21.709  85.643  1.00 14.74 ? 885  PRO B CA    1 
ATOM   15311 C  C     . PRO B 1  887  ? 26.307  23.149  85.145  1.00 15.60 ? 885  PRO B C     1 
ATOM   15312 O  O     . PRO B 1  887  ? 25.315  23.689  84.654  1.00 14.87 ? 885  PRO B O     1 
ATOM   15313 C  CB    . PRO B 1  887  ? 26.857  20.771  84.569  1.00 15.97 ? 885  PRO B CB    1 
ATOM   15314 C  CG    . PRO B 1  887  ? 25.622  20.434  83.758  1.00 15.30 ? 885  PRO B CG    1 
ATOM   15315 C  CD    . PRO B 1  887  ? 24.535  20.267  84.771  1.00 15.59 ? 885  PRO B CD    1 
ATOM   15316 N  N     . VAL B 1  888  ? 27.485  23.753  85.234  1.00 16.88 ? 886  VAL B N     1 
ATOM   15317 C  CA    . VAL B 1  888  ? 27.742  24.960  84.464  1.00 14.97 ? 886  VAL B CA    1 
ATOM   15318 C  C     . VAL B 1  888  ? 28.130  24.565  83.040  1.00 16.39 ? 886  VAL B C     1 
ATOM   15319 O  O     . VAL B 1  888  ? 28.580  23.446  82.772  1.00 16.88 ? 886  VAL B O     1 
ATOM   15320 C  CB    . VAL B 1  888  ? 28.817  25.838  85.138  1.00 19.43 ? 886  VAL B CB    1 
ATOM   15321 C  CG1   . VAL B 1  888  ? 28.340  26.301  86.538  1.00 17.78 ? 886  VAL B CG1   1 
ATOM   15322 C  CG2   . VAL B 1  888  ? 30.137  25.120  85.222  1.00 22.07 ? 886  VAL B CG2   1 
ATOM   15323 N  N     . ILE B 1  889  ? 27.920  25.492  82.106  1.00 16.63 ? 887  ILE B N     1 
ATOM   15324 C  CA    . ILE B 1  889  ? 27.830  25.093  80.702  1.00 16.26 ? 887  ILE B CA    1 
ATOM   15325 C  C     . ILE B 1  889  ? 29.180  24.644  80.139  1.00 16.59 ? 887  ILE B C     1 
ATOM   15326 O  O     . ILE B 1  889  ? 29.228  23.763  79.272  1.00 15.66 ? 887  ILE B O     1 
ATOM   15327 C  CB    . ILE B 1  889  ? 27.223  26.244  79.881  1.00 16.39 ? 887  ILE B CB    1 
ATOM   15328 C  CG1   . ILE B 1  889  ? 26.937  25.799  78.441  1.00 15.52 ? 887  ILE B CG1   1 
ATOM   15329 C  CG2   . ILE B 1  889  ? 28.134  27.473  79.912  1.00 18.51 ? 887  ILE B CG2   1 
ATOM   15330 C  CD1   . ILE B 1  889  ? 25.967  24.635  78.344  1.00 16.70 ? 887  ILE B CD1   1 
ATOM   15331 N  N     . THR B 1  890  ? 30.289  25.237  80.589  1.00 16.09 ? 888  THR B N     1 
ATOM   15332 C  CA    . THR B 1  890  ? 31.600  24.926  80.027  1.00 17.07 ? 888  THR B CA    1 
ATOM   15333 C  C     . THR B 1  890  ? 32.663  25.008  81.105  1.00 16.61 ? 888  THR B C     1 
ATOM   15334 O  O     . THR B 1  890  ? 32.463  25.601  82.164  1.00 17.42 ? 888  THR B O     1 
ATOM   15335 C  CB    . THR B 1  890  ? 32.024  25.900  78.913  1.00 17.08 ? 888  THR B CB    1 
ATOM   15336 O  OG1   . THR B 1  890  ? 32.053  27.239  79.439  1.00 18.49 ? 888  THR B OG1   1 
ATOM   15337 C  CG2   . THR B 1  890  ? 31.069  25.830  77.712  1.00 17.49 ? 888  THR B CG2   1 
ATOM   15338 N  N     . SER B 1  891  ? 33.828  24.449  80.784  1.00 17.43 ? 889  SER B N     1 
ATOM   15339 C  CA    A SER B 1  891  ? 34.994  24.602  81.651  0.47 17.99 ? 889  SER B CA    1 
ATOM   15340 C  CA    B SER B 1  891  ? 34.966  24.606  81.680  0.53 17.98 ? 889  SER B CA    1 
ATOM   15341 C  C     . SER B 1  891  ? 35.387  26.064  81.776  1.00 19.20 ? 889  SER B C     1 
ATOM   15342 O  O     . SER B 1  891  ? 35.827  26.511  82.841  1.00 20.55 ? 889  SER B O     1 
ATOM   15343 C  CB    A SER B 1  891  ? 36.170  23.789  81.105  0.47 20.70 ? 889  SER B CB    1 
ATOM   15344 C  CB    B SER B 1  891  ? 36.132  23.739  81.209  0.53 20.71 ? 889  SER B CB    1 
ATOM   15345 O  OG    A SER B 1  891  ? 35.946  22.398  81.218  0.47 21.04 ? 889  SER B OG    1 
ATOM   15346 O  OG    B SER B 1  891  ? 36.663  24.234  79.998  0.53 22.74 ? 889  SER B OG    1 
ATOM   15347 N  N     . GLU B 1  892  ? 35.260  26.816  80.681  1.00 17.06 ? 890  GLU B N     1 
ATOM   15348 C  CA    . GLU B 1  892  ? 35.599  28.234  80.708  1.00 18.85 ? 890  GLU B CA    1 
ATOM   15349 C  C     . GLU B 1  892  ? 34.698  28.986  81.676  1.00 21.37 ? 890  GLU B C     1 
ATOM   15350 O  O     . GLU B 1  892  ? 35.169  29.812  82.468  1.00 19.09 ? 890  GLU B O     1 
ATOM   15351 C  CB    . GLU B 1  892  ? 35.490  28.825  79.300  1.00 24.52 ? 890  GLU B CB    1 
ATOM   15352 C  CG    . GLU B 1  892  ? 36.619  28.406  78.356  1.00 30.10 ? 890  GLU B CG    1 
ATOM   15353 C  CD    . GLU B 1  892  ? 36.445  27.032  77.677  1.00 34.41 ? 890  GLU B CD    1 
ATOM   15354 O  OE1   . GLU B 1  892  ? 35.448  26.294  77.917  1.00 28.95 ? 890  GLU B OE1   1 
ATOM   15355 O  OE2   . GLU B 1  892  ? 37.342  26.693  76.871  1.00 41.42 ? 890  GLU B OE2   1 
ATOM   15356 N  N     . ALA B 1  893  ? 33.391  28.718  81.613  1.00 18.16 ? 891  ALA B N     1 
ATOM   15357 C  CA    . ALA B 1  893  ? 32.461  29.329  82.555  1.00 17.87 ? 891  ALA B CA    1 
ATOM   15358 C  C     . ALA B 1  893  ? 32.822  28.957  83.984  1.00 18.97 ? 891  ALA B C     1 
ATOM   15359 O  O     . ALA B 1  893  ? 32.880  29.819  84.866  1.00 19.40 ? 891  ALA B O     1 
ATOM   15360 C  CB    . ALA B 1  893  ? 31.032  28.898  82.228  1.00 18.70 ? 891  ALA B CB    1 
ATOM   15361 N  N     . LYS B 1  894  ? 33.092  27.671  84.218  1.00 17.50 ? 892  LYS B N     1 
ATOM   15362 C  CA    . LYS B 1  894  ? 33.486  27.216  85.548  1.00 17.41 ? 892  LYS B CA    1 
ATOM   15363 C  C     . LYS B 1  894  ? 34.713  27.972  86.045  1.00 19.39 ? 892  LYS B C     1 
ATOM   15364 O  O     . LYS B 1  894  ? 34.747  28.441  87.186  1.00 20.24 ? 892  LYS B O     1 
ATOM   15365 C  CB    . LYS B 1  894  ? 33.758  25.714  85.514  1.00 18.56 ? 892  LYS B CB    1 
ATOM   15366 C  CG    . LYS B 1  894  ? 34.253  25.111  86.806  1.00 20.19 ? 892  LYS B CG    1 
ATOM   15367 C  CD    . LYS B 1  894  ? 34.269  23.592  86.679  1.00 20.49 ? 892  LYS B CD    1 
ATOM   15368 C  CE    . LYS B 1  894  ? 34.783  22.937  87.955  1.00 25.57 ? 892  LYS B CE    1 
ATOM   15369 N  NZ    . LYS B 1  894  ? 36.151  23.403  88.253  1.00 35.55 ? 892  LYS B NZ    1 
ATOM   15370 N  N     . ASP B 1  895  ? 35.727  28.110  85.190  1.00 20.35 ? 893  ASP B N     1 
ATOM   15371 C  CA    . ASP B 1  895  ? 36.933  28.833  85.582  1.00 20.24 ? 893  ASP B CA    1 
ATOM   15372 C  C     . ASP B 1  895  ? 36.625  30.288  85.919  1.00 19.19 ? 893  ASP B C     1 
ATOM   15373 O  O     . ASP B 1  895  ? 37.226  30.867  86.834  1.00 21.19 ? 893  ASP B O     1 
ATOM   15374 C  CB    . ASP B 1  895  ? 37.970  28.773  84.461  1.00 22.57 ? 893  ASP B CB    1 
ATOM   15375 C  CG    . ASP B 1  895  ? 38.547  27.388  84.257  1.00 22.94 ? 893  ASP B CG    1 
ATOM   15376 O  OD1   . ASP B 1  895  ? 38.437  26.533  85.163  1.00 24.94 ? 893  ASP B OD1   1 
ATOM   15377 O  OD2   . ASP B 1  895  ? 39.137  27.165  83.183  1.00 27.49 ? 893  ASP B OD2   1 
ATOM   15378 N  N     . ASN B 1  896  ? 35.728  30.902  85.150  1.00 19.25 ? 894  ASN B N     1 
ATOM   15379 C  CA    . ASN B 1  896  ? 35.363  32.296  85.364  1.00 17.91 ? 894  ASN B CA    1 
ATOM   15380 C  C     . ASN B 1  896  ? 34.697  32.466  86.729  1.00 19.23 ? 894  ASN B C     1 
ATOM   15381 O  O     . ASN B 1  896  ? 35.064  33.344  87.523  1.00 18.26 ? 894  ASN B O     1 
ATOM   15382 C  CB    . ASN B 1  896  ? 34.450  32.721  84.202  1.00 20.21 ? 894  ASN B CB    1 
ATOM   15383 C  CG    . ASN B 1  896  ? 33.943  34.147  84.308  1.00 27.76 ? 894  ASN B CG    1 
ATOM   15384 O  OD1   . ASN B 1  896  ? 33.377  34.560  85.320  1.00 29.08 ? 894  ASN B OD1   1 
ATOM   15385 N  ND2   . ASN B 1  896  ? 34.086  34.892  83.215  1.00 31.18 ? 894  ASN B ND2   1 
ATOM   15386 N  N     . ILE B 1  897  ? 33.733  31.598  87.027  1.00 17.57 ? 895  ILE B N     1 
ATOM   15387 C  CA    . ILE B 1  897  ? 33.046  31.631  88.311  1.00 18.21 ? 895  ILE B CA    1 
ATOM   15388 C  C     . ILE B 1  897  ? 34.034  31.398  89.448  1.00 19.05 ? 895  ILE B C     1 
ATOM   15389 O  O     . ILE B 1  897  ? 34.042  32.126  90.444  1.00 18.95 ? 895  ILE B O     1 
ATOM   15390 C  CB    . ILE B 1  897  ? 31.923  30.583  88.322  1.00 17.65 ? 895  ILE B CB    1 
ATOM   15391 C  CG1   . ILE B 1  897  ? 30.892  30.933  87.256  1.00 16.05 ? 895  ILE B CG1   1 
ATOM   15392 C  CG2   . ILE B 1  897  ? 31.287  30.470  89.712  1.00 17.99 ? 895  ILE B CG2   1 
ATOM   15393 C  CD1   . ILE B 1  897  ? 30.086  29.734  86.829  1.00 17.27 ? 895  ILE B CD1   1 
ATOM   15394 N  N     . GLU B 1  898  ? 34.871  30.371  89.319  1.00 18.66 ? 896  GLU B N     1 
ATOM   15395 C  CA    . GLU B 1  898  ? 35.802  30.042  90.394  1.00 18.03 ? 896  GLU B CA    1 
ATOM   15396 C  C     . GLU B 1  898  ? 36.834  31.139  90.595  1.00 19.46 ? 896  GLU B C     1 
ATOM   15397 O  O     . GLU B 1  898  ? 37.280  31.362  91.725  1.00 19.11 ? 896  GLU B O     1 
ATOM   15398 C  CB    . GLU B 1  898  ? 36.479  28.700  90.111  1.00 19.04 ? 896  GLU B CB    1 
ATOM   15399 C  CG    . GLU B 1  898  ? 35.482  27.542  90.213  1.00 21.86 ? 896  GLU B CG    1 
ATOM   15400 C  CD    . GLU B 1  898  ? 36.103  26.183  89.976  1.00 26.92 ? 896  GLU B CD    1 
ATOM   15401 O  OE1   . GLU B 1  898  ? 37.189  26.110  89.359  1.00 25.86 ? 896  GLU B OE1   1 
ATOM   15402 O  OE2   . GLU B 1  898  ? 35.494  25.185  90.416  1.00 32.84 ? 896  GLU B OE2   1 
ATOM   15403 N  N     . LYS B 1  899  ? 37.220  31.839  89.525  1.00 19.62 ? 897  LYS B N     1 
ATOM   15404 C  CA    . LYS B 1  899  ? 38.144  32.961  89.691  1.00 20.41 ? 897  LYS B CA    1 
ATOM   15405 C  C     . LYS B 1  899  ? 37.544  34.020  90.605  1.00 20.09 ? 897  LYS B C     1 
ATOM   15406 O  O     . LYS B 1  899  ? 38.239  34.579  91.468  1.00 21.21 ? 897  LYS B O     1 
ATOM   15407 C  CB    . LYS B 1  899  ? 38.496  33.564  88.330  1.00 21.68 ? 897  LYS B CB    1 
ATOM   15408 C  CG    . LYS B 1  899  ? 39.375  34.805  88.437  1.00 24.55 ? 897  LYS B CG    1 
ATOM   15409 C  CD    . LYS B 1  899  ? 39.999  35.188  87.102  1.00 27.11 ? 897  LYS B CD    1 
ATOM   15410 C  CE    . LYS B 1  899  ? 39.073  36.012  86.236  1.00 32.54 ? 897  LYS B CE    1 
ATOM   15411 N  NZ    . LYS B 1  899  ? 39.859  36.859  85.275  1.00 29.62 ? 897  LYS B NZ    1 
ATOM   15412 N  N     . HIS B 1  900  ? 36.247  34.291  90.446  1.00 18.13 ? 898  HIS B N     1 
ATOM   15413 C  CA    . HIS B 1  900  ? 35.571  35.244  91.317  1.00 18.03 ? 898  HIS B CA    1 
ATOM   15414 C  C     . HIS B 1  900  ? 35.529  34.736  92.748  1.00 19.76 ? 898  HIS B C     1 
ATOM   15415 O  O     . HIS B 1  900  ? 35.825  35.476  93.697  1.00 19.78 ? 898  HIS B O     1 
ATOM   15416 C  CB    . HIS B 1  900  ? 34.151  35.485  90.820  1.00 16.90 ? 898  HIS B CB    1 
ATOM   15417 C  CG    . HIS B 1  900  ? 33.309  36.236  91.792  1.00 17.79 ? 898  HIS B CG    1 
ATOM   15418 N  ND1   . HIS B 1  900  ? 33.491  37.577  92.044  1.00 20.61 ? 898  HIS B ND1   1 
ATOM   15419 C  CD2   . HIS B 1  900  ? 32.300  35.831  92.599  1.00 18.96 ? 898  HIS B CD2   1 
ATOM   15420 C  CE1   . HIS B 1  900  ? 32.597  37.977  92.932  1.00 21.50 ? 898  HIS B CE1   1 
ATOM   15421 N  NE2   . HIS B 1  900  ? 31.873  36.935  93.296  1.00 18.39 ? 898  HIS B NE2   1 
ATOM   15422 N  N     . ILE B 1  901  ? 35.136  33.476  92.918  1.00 18.06 ? 899  ILE B N     1 
ATOM   15423 C  CA    . ILE B 1  901  ? 35.052  32.890  94.250  1.00 16.94 ? 899  ILE B CA    1 
ATOM   15424 C  C     . ILE B 1  901  ? 36.398  32.990  94.954  1.00 19.76 ? 899  ILE B C     1 
ATOM   15425 O  O     . ILE B 1  901  ? 36.484  33.446  96.100  1.00 21.10 ? 899  ILE B O     1 
ATOM   15426 C  CB    . ILE B 1  901  ? 34.553  31.436  94.165  1.00 18.05 ? 899  ILE B CB    1 
ATOM   15427 C  CG1   . ILE B 1  901  ? 33.090  31.408  93.701  1.00 16.21 ? 899  ILE B CG1   1 
ATOM   15428 C  CG2   . ILE B 1  901  ? 34.715  30.737  95.515  1.00 19.51 ? 899  ILE B CG2   1 
ATOM   15429 C  CD1   . ILE B 1  901  ? 32.597  29.997  93.336  1.00 19.62 ? 899  ILE B CD1   1 
ATOM   15430 N  N     . GLU B 1  902  ? 37.473  32.606  94.261  1.00 18.62 ? 900  GLU B N     1 
ATOM   15431 C  CA    . GLU B 1  902  ? 38.794  32.635  94.882  1.00 21.49 ? 900  GLU B CA    1 
ATOM   15432 C  C     . GLU B 1  902  ? 39.266  34.061  95.123  1.00 22.23 ? 900  GLU B C     1 
ATOM   15433 O  O     . GLU B 1  902  ? 39.999  34.313  96.086  1.00 22.92 ? 900  GLU B O     1 
ATOM   15434 C  CB    . GLU B 1  902  ? 39.798  31.871  94.015  1.00 23.33 ? 900  GLU B CB    1 
ATOM   15435 C  CG    . GLU B 1  902  ? 39.565  30.366  94.035  1.00 27.37 ? 900  GLU B CG    1 
ATOM   15436 C  CD    . GLU B 1  902  ? 39.323  29.842  95.446  1.00 31.49 ? 900  GLU B CD    1 
ATOM   15437 O  OE1   . GLU B 1  902  ? 40.168  30.106  96.331  1.00 30.83 ? 900  GLU B OE1   1 
ATOM   15438 O  OE2   . GLU B 1  902  ? 38.282  29.184  95.670  1.00 34.91 ? 900  GLU B OE2   1 
ATOM   15439 N  N     . ARG B 1  903  ? 38.861  35.004  94.278  1.00 22.42 ? 901  ARG B N     1 
ATOM   15440 C  CA    . ARG B 1  903  ? 39.216  36.392  94.538  1.00 23.13 ? 901  ARG B CA    1 
ATOM   15441 C  C     . ARG B 1  903  ? 38.533  36.897  95.799  1.00 25.44 ? 901  ARG B C     1 
ATOM   15442 O  O     . ARG B 1  903  ? 39.151  37.596  96.612  1.00 24.38 ? 901  ARG B O     1 
ATOM   15443 C  CB    . ARG B 1  903  ? 38.842  37.260  93.347  1.00 24.95 ? 901  ARG B CB    1 
ATOM   15444 C  CG    . ARG B 1  903  ? 39.192  38.704  93.570  1.00 30.58 ? 901  ARG B CG    1 
ATOM   15445 C  CD    . ARG B 1  903  ? 38.989  39.536  92.321  1.00 33.94 ? 901  ARG B CD    1 
ATOM   15446 N  NE    . ARG B 1  903  ? 39.395  40.902  92.606  1.00 41.87 ? 901  ARG B NE    1 
ATOM   15447 C  CZ    . ARG B 1  903  ? 38.597  41.809  93.149  1.00 42.38 ? 901  ARG B CZ    1 
ATOM   15448 N  NH1   . ARG B 1  903  ? 37.316  41.556  93.372  1.00 36.43 ? 901  ARG B NH1   1 
ATOM   15449 N  NH2   . ARG B 1  903  ? 39.098  42.997  93.479  1.00 39.57 ? 901  ARG B NH2   1 
ATOM   15450 N  N     . MET B 1  904  ? 37.259  36.545  95.981  1.00 21.76 ? 902  MET B N     1 
ATOM   15451 C  CA    . MET B 1  904  ? 36.571  36.902  97.218  1.00 21.91 ? 902  MET B CA    1 
ATOM   15452 C  C     . MET B 1  904  ? 37.230  36.234  98.416  1.00 24.57 ? 902  MET B C     1 
ATOM   15453 O  O     . MET B 1  904  ? 37.449  36.874  99.450  1.00 23.40 ? 902  MET B O     1 
ATOM   15454 C  CB    . MET B 1  904  ? 35.096  36.516  97.128  1.00 22.91 ? 902  MET B CB    1 
ATOM   15455 C  CG    . MET B 1  904  ? 34.348  37.235  96.017  1.00 21.62 ? 902  MET B CG    1 
ATOM   15456 S  SD    . MET B 1  904  ? 34.181  39.013  96.331  1.00 29.66 ? 902  MET B SD    1 
ATOM   15457 C  CE    . MET B 1  904  ? 35.338  39.672  95.142  1.00 28.03 ? 902  MET B CE    1 
ATOM   15458 N  N     . ARG B 1  905  ? 37.565  34.952  98.294  1.00 21.84 ? 903  ARG B N     1 
ATOM   15459 C  CA    . ARG B 1  905  ? 38.187  34.266  99.419  1.00 25.19 ? 903  ARG B CA    1 
ATOM   15460 C  C     . ARG B 1  905  ? 39.522  34.907  99.766  1.00 24.96 ? 903  ARG B C     1 
ATOM   15461 O  O     . ARG B 1  905  ? 39.839  35.101  100.946 1.00 25.69 ? 903  ARG B O     1 
ATOM   15462 C  CB    . ARG B 1  905  ? 38.363  32.781  99.100  1.00 24.97 ? 903  ARG B CB    1 
ATOM   15463 C  CG    . ARG B 1  905  ? 38.581  31.914  100.332 1.00 27.55 ? 903  ARG B CG    1 
ATOM   15464 C  CD    . ARG B 1  905  ? 39.103  30.548  99.932  1.00 31.20 ? 903  ARG B CD    1 
ATOM   15465 N  NE    . ARG B 1  905  ? 38.308  29.940  98.868  1.00 30.06 ? 903  ARG B NE    1 
ATOM   15466 C  CZ    . ARG B 1  905  ? 37.199  29.242  99.065  1.00 28.09 ? 903  ARG B CZ    1 
ATOM   15467 N  NH1   . ARG B 1  905  ? 36.666  29.114  100.270 1.00 28.56 ? 903  ARG B NH1   1 
ATOM   15468 N  NH2   . ARG B 1  905  ? 36.614  28.650  98.028  1.00 29.70 ? 903  ARG B NH2   1 
ATOM   15469 N  N     . GLY B 1  906  ? 40.297  35.287  98.747  1.00 22.89 ? 904  GLY B N     1 
ATOM   15470 C  CA    . GLY B 1  906  ? 41.615  35.853  98.996  1.00 26.81 ? 904  GLY B CA    1 
ATOM   15471 C  C     . GLY B 1  906  ? 41.574  37.231  99.624  1.00 27.33 ? 904  GLY B C     1 
ATOM   15472 O  O     . GLY B 1  906  ? 42.525  37.636  100.303 1.00 31.73 ? 904  GLY B O     1 
ATOM   15473 N  N     . LEU B 1  907  ? 40.491  37.973  99.407  1.00 27.74 ? 905  LEU B N     1 
ATOM   15474 C  CA    . LEU B 1  907  ? 40.288  39.254  100.070 1.00 30.30 ? 905  LEU B CA    1 
ATOM   15475 C  C     . LEU B 1  907  ? 39.690  39.106  101.462 1.00 27.18 ? 905  LEU B C     1 
ATOM   15476 O  O     . LEU B 1  907  ? 39.375  40.122  102.090 1.00 29.19 ? 905  LEU B O     1 
ATOM   15477 C  CB    . LEU B 1  907  ? 39.393  40.155  99.217  1.00 30.53 ? 905  LEU B CB    1 
ATOM   15478 C  CG    . LEU B 1  907  ? 40.004  40.639  97.900  1.00 31.65 ? 905  LEU B CG    1 
ATOM   15479 C  CD1   . LEU B 1  907  ? 39.010  41.495  97.135  1.00 36.22 ? 905  LEU B CD1   1 
ATOM   15480 C  CD2   . LEU B 1  907  ? 41.293  41.403  98.143  1.00 31.90 ? 905  LEU B CD2   1 
ATOM   15481 N  N     . GLY B 1  908  ? 39.518  37.878  101.945 1.00 26.64 ? 906  GLY B N     1 
ATOM   15482 C  CA    . GLY B 1  908  ? 39.080  37.627  103.298 1.00 28.34 ? 906  GLY B CA    1 
ATOM   15483 C  C     . GLY B 1  908  ? 37.586  37.522  103.503 1.00 30.72 ? 906  GLY B C     1 
ATOM   15484 O  O     . GLY B 1  908  ? 37.150  37.413  104.655 1.00 29.97 ? 906  GLY B O     1 
ATOM   15485 N  N     . ARG B 1  909  ? 36.785  37.562  102.438 1.00 24.91 ? 907  ARG B N     1 
ATOM   15486 C  CA    . ARG B 1  909  ? 35.344  37.421  102.598 1.00 22.95 ? 907  ARG B CA    1 
ATOM   15487 C  C     . ARG B 1  909  ? 34.991  35.982  102.954 1.00 26.27 ? 907  ARG B C     1 
ATOM   15488 O  O     . ARG B 1  909  ? 35.628  35.029  102.498 1.00 25.97 ? 907  ARG B O     1 
ATOM   15489 C  CB    . ARG B 1  909  ? 34.606  37.822  101.316 1.00 23.47 ? 907  ARG B CB    1 
ATOM   15490 C  CG    . ARG B 1  909  ? 34.948  39.207  100.783 1.00 28.90 ? 907  ARG B CG    1 
ATOM   15491 C  CD    . ARG B 1  909  ? 34.368  40.307  101.672 1.00 36.82 ? 907  ARG B CD    1 
ATOM   15492 N  NE    . ARG B 1  909  ? 34.665  41.643  101.159 1.00 41.06 ? 907  ARG B NE    1 
ATOM   15493 C  CZ    . ARG B 1  909  ? 35.663  42.408  101.583 1.00 45.39 ? 907  ARG B CZ    1 
ATOM   15494 N  NH1   . ARG B 1  909  ? 36.493  42.002  102.533 1.00 44.55 ? 907  ARG B NH1   1 
ATOM   15495 N  NH2   . ARG B 1  909  ? 35.829  43.614  101.045 1.00 47.87 ? 907  ARG B NH2   1 
ATOM   15496 N  N     . LYS B 1  910  ? 33.947  35.827  103.762 1.00 20.93 ? 908  LYS B N     1 
ATOM   15497 C  CA    . LYS B 1  910  ? 33.495  34.494  104.130 1.00 22.00 ? 908  LYS B CA    1 
ATOM   15498 C  C     . LYS B 1  910  ? 32.852  33.820  102.923 1.00 23.10 ? 908  LYS B C     1 
ATOM   15499 O  O     . LYS B 1  910  ? 31.874  34.330  102.363 1.00 22.45 ? 908  LYS B O     1 
ATOM   15500 C  CB    . LYS B 1  910  ? 32.513  34.552  105.296 1.00 25.57 ? 908  LYS B CB    1 
ATOM   15501 C  CG    . LYS B 1  910  ? 32.008  33.159  105.682 1.00 29.18 ? 908  LYS B CG    1 
ATOM   15502 C  CD    . LYS B 1  910  ? 31.126  33.169  106.924 1.00 32.35 ? 908  LYS B CD    1 
ATOM   15503 C  CE    . LYS B 1  910  ? 30.911  31.741  107.432 1.00 38.00 ? 908  LYS B CE    1 
ATOM   15504 N  NZ    . LYS B 1  910  ? 29.791  31.624  108.414 1.00 39.51 ? 908  LYS B NZ    1 
ATOM   15505 N  N     . VAL B 1  911  ? 33.414  32.682  102.523 1.00 22.32 ? 909  VAL B N     1 
ATOM   15506 C  CA    . VAL B 1  911  ? 32.944  31.897  101.386 1.00 21.31 ? 909  VAL B CA    1 
ATOM   15507 C  C     . VAL B 1  911  ? 32.582  30.506  101.891 1.00 23.88 ? 909  VAL B C     1 
ATOM   15508 O  O     . VAL B 1  911  ? 33.388  29.861  102.572 1.00 22.37 ? 909  VAL B O     1 
ATOM   15509 C  CB    . VAL B 1  911  ? 34.017  31.800  100.284 1.00 21.01 ? 909  VAL B CB    1 
ATOM   15510 C  CG1   . VAL B 1  911  ? 33.550  30.870  99.156  1.00 19.52 ? 909  VAL B CG1   1 
ATOM   15511 C  CG2   . VAL B 1  911  ? 34.396  33.197  99.764  1.00 20.82 ? 909  VAL B CG2   1 
ATOM   15512 N  N     . GLU B 1  912  ? 31.378  30.048  101.563 1.00 19.79 ? 910  GLU B N     1 
ATOM   15513 C  CA    . GLU B 1  912  ? 30.920  28.718  101.950 1.00 21.32 ? 910  GLU B CA    1 
ATOM   15514 C  C     . GLU B 1  912  ? 30.342  28.011  100.737 1.00 24.20 ? 910  GLU B C     1 
ATOM   15515 O  O     . GLU B 1  912  ? 29.538  28.594  100.005 1.00 21.07 ? 910  GLU B O     1 
ATOM   15516 C  CB    . GLU B 1  912  ? 29.862  28.782  103.046 1.00 24.93 ? 910  GLU B CB    1 
ATOM   15517 C  CG    . GLU B 1  912  ? 30.316  29.494  104.299 1.00 27.96 ? 910  GLU B CG    1 
ATOM   15518 C  CD    . GLU B 1  912  ? 29.180  29.652  105.283 1.00 35.68 ? 910  GLU B CD    1 
ATOM   15519 O  OE1   . GLU B 1  912  ? 28.747  28.631  105.851 1.00 38.15 ? 910  GLU B OE1   1 
ATOM   15520 O  OE2   . GLU B 1  912  ? 28.700  30.791  105.457 1.00 43.52 ? 910  GLU B OE2   1 
ATOM   15521 N  N     . GLN B 1  913  ? 30.739  26.754  100.534 1.00 22.60 ? 911  GLN B N     1 
ATOM   15522 C  CA    . GLN B 1  913  ? 30.179  25.941  99.463  1.00 23.72 ? 911  GLN B CA    1 
ATOM   15523 C  C     . GLN B 1  913  ? 29.676  24.620  100.019 1.00 29.27 ? 911  GLN B C     1 
ATOM   15524 O  O     . GLN B 1  913  ? 30.211  24.098  100.999 1.00 25.92 ? 911  GLN B O     1 
ATOM   15525 C  CB    . GLN B 1  913  ? 31.210  25.653  98.365  1.00 23.63 ? 911  GLN B CB    1 
ATOM   15526 C  CG    . GLN B 1  913  ? 31.825  26.908  97.800  1.00 23.82 ? 911  GLN B CG    1 
ATOM   15527 C  CD    . GLN B 1  913  ? 32.863  26.613  96.746  1.00 27.65 ? 911  GLN B CD    1 
ATOM   15528 O  OE1   . GLN B 1  913  ? 33.904  26.032  97.038  1.00 32.30 ? 911  GLN B OE1   1 
ATOM   15529 N  NE2   . GLN B 1  913  ? 32.583  27.009  95.511  1.00 23.55 ? 911  GLN B NE2   1 
ATOM   15530 N  N     . ILE B 1  914  ? 28.659  24.061  99.372  1.00 27.85 ? 912  ILE B N     1 
ATOM   15531 C  CA    . ILE B 1  914  ? 28.287  22.688  99.696  1.00 37.27 ? 912  ILE B CA    1 
ATOM   15532 C  C     . ILE B 1  914  ? 29.154  21.709  98.905  1.00 41.11 ? 912  ILE B C     1 
ATOM   15533 O  O     . ILE B 1  914  ? 29.944  22.109  98.040  1.00 37.58 ? 912  ILE B O     1 
ATOM   15534 C  CB    . ILE B 1  914  ? 26.791  22.441  99.452  1.00 36.41 ? 912  ILE B CB    1 
ATOM   15535 C  CG1   . ILE B 1  914  ? 26.412  22.739  98.003  1.00 24.48 ? 912  ILE B CG1   1 
ATOM   15536 C  CG2   . ILE B 1  914  ? 25.952  23.276  100.440 1.00 30.94 ? 912  ILE B CG2   1 
ATOM   15537 C  CD1   . ILE B 1  914  ? 24.961  22.332  97.683  1.00 33.15 ? 912  ILE B CD1   1 
ATOM   15538 N  N     . GLY B 1  915  ? 29.028  20.415  99.211  1.00 50.66 ? 913  GLY B N     1 
ATOM   15539 C  CA    . GLY B 1  915  ? 29.862  19.423  98.571  1.00 49.50 ? 913  GLY B CA    1 
ATOM   15540 C  C     . GLY B 1  915  ? 29.320  18.970  97.227  1.00 50.10 ? 913  GLY B C     1 
ATOM   15541 O  O     . GLY B 1  915  ? 28.156  19.181  96.886  1.00 45.42 ? 913  GLY B O     1 
ATOM   15542 N  N     . LEU B 1  916  ? 30.198  18.335  96.454  1.00 46.76 ? 914  LEU B N     1 
ATOM   15543 C  CA    . LEU B 1  916  ? 29.864  17.777  95.150  1.00 43.77 ? 914  LEU B CA    1 
ATOM   15544 C  C     . LEU B 1  916  ? 30.145  16.283  95.149  1.00 44.76 ? 914  LEU B C     1 
ATOM   15545 O  O     . LEU B 1  916  ? 31.168  15.837  95.677  1.00 42.64 ? 914  LEU B O     1 
ATOM   15546 C  CB    . LEU B 1  916  ? 30.680  18.431  94.027  1.00 43.13 ? 914  LEU B CB    1 
ATOM   15547 C  CG    . LEU B 1  916  ? 30.417  19.882  93.627  1.00 38.17 ? 914  LEU B CG    1 
ATOM   15548 C  CD1   . LEU B 1  916  ? 31.312  20.262  92.443  1.00 32.98 ? 914  LEU B CD1   1 
ATOM   15549 C  CD2   . LEU B 1  916  ? 28.945  20.099  93.309  1.00 32.42 ? 914  LEU B CD2   1 
ATOM   15550 N  N     . ALA B 1  917  ? 29.240  15.516  94.547  1.00 42.08 ? 915  ALA B N     1 
ATOM   15551 C  CA    . ALA B 1  917  ? 29.471  14.091  94.362  1.00 47.95 ? 915  ALA B CA    1 
ATOM   15552 C  C     . ALA B 1  917  ? 30.634  13.861  93.401  1.00 47.08 ? 915  ALA B C     1 
ATOM   15553 O  O     . ALA B 1  917  ? 30.906  14.676  92.516  1.00 42.97 ? 915  ALA B O     1 
ATOM   15554 C  CB    . ALA B 1  917  ? 28.212  13.408  93.827  1.00 42.84 ? 915  ALA B CB    1 
ATOM   15555 N  N     . SER B 1  918  ? 31.328  12.733  93.584  1.00 46.60 ? 916  SER B N     1 
ATOM   15556 C  CA    . SER B 1  918  ? 32.427  12.393  92.683  1.00 46.37 ? 916  SER B CA    1 
ATOM   15557 C  C     . SER B 1  918  ? 31.950  12.268  91.240  1.00 44.27 ? 916  SER B C     1 
ATOM   15558 O  O     . SER B 1  918  ? 32.697  12.590  90.308  1.00 40.87 ? 916  SER B O     1 
ATOM   15559 C  CB    . SER B 1  918  ? 33.098  11.097  93.137  1.00 48.20 ? 916  SER B CB    1 
ATOM   15560 O  OG    . SER B 1  918  ? 32.202  10.005  93.037  1.00 49.32 ? 916  SER B OG    1 
ATOM   15561 N  N     . GLU B 1  919  ? 30.700  11.833  91.041  1.00 44.70 ? 917  GLU B N     1 
ATOM   15562 C  CA    . GLU B 1  919  ? 30.134  11.706  89.701  1.00 41.78 ? 917  GLU B CA    1 
ATOM   15563 C  C     . GLU B 1  919  ? 30.131  13.026  88.938  1.00 39.11 ? 917  GLU B C     1 
ATOM   15564 O  O     . GLU B 1  919  ? 29.957  13.018  87.715  1.00 39.73 ? 917  GLU B O     1 
ATOM   15565 C  CB    . GLU B 1  919  ? 28.708  11.154  89.783  1.00 37.51 ? 917  GLU B CB    1 
ATOM   15566 N  N     . THR B 1  920  ? 30.314  14.156  89.624  1.00 37.70 ? 918  THR B N     1 
ATOM   15567 C  CA    . THR B 1  920  ? 30.402  15.435  88.930  1.00 34.20 ? 918  THR B CA    1 
ATOM   15568 C  C     . THR B 1  920  ? 31.735  15.612  88.199  1.00 33.22 ? 918  THR B C     1 
ATOM   15569 O  O     . THR B 1  920  ? 31.835  16.497  87.344  1.00 31.92 ? 918  THR B O     1 
ATOM   15570 C  CB    . THR B 1  920  ? 30.177  16.601  89.914  1.00 32.53 ? 918  THR B CB    1 
ATOM   15571 O  OG1   . THR B 1  920  ? 31.215  16.625  90.906  1.00 35.11 ? 918  THR B OG1   1 
ATOM   15572 C  CG2   . THR B 1  920  ? 28.823  16.491  90.605  1.00 29.64 ? 918  THR B CG2   1 
ATOM   15573 N  N     . GLY B 1  921  ? 32.749  14.785  88.501  1.00 32.88 ? 919  GLY B N     1 
ATOM   15574 C  CA    . GLY B 1  921  ? 34.072  14.981  87.919  1.00 31.02 ? 919  GLY B CA    1 
ATOM   15575 C  C     . GLY B 1  921  ? 34.113  14.859  86.406  1.00 29.99 ? 919  GLY B C     1 
ATOM   15576 O  O     . GLY B 1  921  ? 35.001  15.418  85.754  1.00 31.13 ? 919  GLY B O     1 
ATOM   15577 N  N     . VAL B 1  922  ? 33.167  14.122  85.826  1.00 25.06 ? 920  VAL B N     1 
ATOM   15578 C  CA    . VAL B 1  922  ? 33.137  13.937  84.377  1.00 24.01 ? 920  VAL B CA    1 
ATOM   15579 C  C     . VAL B 1  922  ? 32.498  15.107  83.646  1.00 22.95 ? 920  VAL B C     1 
ATOM   15580 O  O     . VAL B 1  922  ? 32.578  15.176  82.408  1.00 21.57 ? 920  VAL B O     1 
ATOM   15581 C  CB    . VAL B 1  922  ? 32.398  12.632  84.037  1.00 26.36 ? 920  VAL B CB    1 
ATOM   15582 C  CG1   . VAL B 1  922  ? 33.182  11.437  84.566  1.00 26.34 ? 920  VAL B CG1   1 
ATOM   15583 C  CG2   . VAL B 1  922  ? 30.994  12.651  84.636  1.00 26.91 ? 920  VAL B CG2   1 
ATOM   15584 N  N     . GLY B 1  923  ? 31.870  16.027  84.375  1.00 21.52 ? 921  GLY B N     1 
ATOM   15585 C  CA    . GLY B 1  923  ? 31.308  17.229  83.789  1.00 19.77 ? 921  GLY B CA    1 
ATOM   15586 C  C     . GLY B 1  923  ? 31.868  18.471  84.450  1.00 20.30 ? 921  GLY B C     1 
ATOM   15587 O  O     . GLY B 1  923  ? 32.852  18.384  85.195  1.00 20.77 ? 921  GLY B O     1 
ATOM   15588 N  N     . THR B 1  924  ? 31.252  19.629  84.219  1.00 18.06 ? 922  THR B N     1 
ATOM   15589 C  CA    . THR B 1  924  ? 31.737  20.895  84.771  1.00 17.30 ? 922  THR B CA    1 
ATOM   15590 C  C     . THR B 1  924  ? 30.692  21.423  85.746  1.00 16.91 ? 922  THR B C     1 
ATOM   15591 O  O     . THR B 1  924  ? 29.650  21.927  85.332  1.00 18.93 ? 922  THR B O     1 
ATOM   15592 C  CB    . THR B 1  924  ? 32.032  21.903  83.663  1.00 17.00 ? 922  THR B CB    1 
ATOM   15593 O  OG1   . THR B 1  924  ? 30.912  22.003  82.775  1.00 17.76 ? 922  THR B OG1   1 
ATOM   15594 C  CG2   . THR B 1  924  ? 33.230  21.448  82.848  1.00 19.68 ? 922  THR B CG2   1 
ATOM   15595 N  N     . PHE B 1  925  ? 30.975  21.299  87.039  1.00 18.13 ? 923  PHE B N     1 
ATOM   15596 C  CA    . PHE B 1  925  ? 30.046  21.697  88.086  1.00 19.71 ? 923  PHE B CA    1 
ATOM   15597 C  C     . PHE B 1  925  ? 30.706  22.688  89.031  1.00 19.23 ? 923  PHE B C     1 
ATOM   15598 O  O     . PHE B 1  925  ? 31.909  22.611  89.311  1.00 19.49 ? 923  PHE B O     1 
ATOM   15599 C  CB    . PHE B 1  925  ? 29.559  20.489  88.906  1.00 18.39 ? 923  PHE B CB    1 
ATOM   15600 C  CG    . PHE B 1  925  ? 28.683  19.532  88.137  1.00 19.62 ? 923  PHE B CG    1 
ATOM   15601 C  CD1   . PHE B 1  925  ? 29.244  18.561  87.322  1.00 19.34 ? 923  PHE B CD1   1 
ATOM   15602 C  CD2   . PHE B 1  925  ? 27.299  19.592  88.246  1.00 18.53 ? 923  PHE B CD2   1 
ATOM   15603 C  CE1   . PHE B 1  925  ? 28.452  17.660  86.623  1.00 17.65 ? 923  PHE B CE1   1 
ATOM   15604 C  CE2   . PHE B 1  925  ? 26.494  18.698  87.543  1.00 17.35 ? 923  PHE B CE2   1 
ATOM   15605 C  CZ    . PHE B 1  925  ? 27.073  17.728  86.737  1.00 18.67 ? 923  PHE B CZ    1 
ATOM   15606 N  N     . VAL B 1  926  ? 29.893  23.614  89.525  1.00 17.60 ? 924  VAL B N     1 
ATOM   15607 C  CA    . VAL B 1  926  ? 30.234  24.497  90.629  1.00 17.67 ? 924  VAL B CA    1 
ATOM   15608 C  C     . VAL B 1  926  ? 29.116  24.319  91.647  1.00 18.74 ? 924  VAL B C     1 
ATOM   15609 O  O     . VAL B 1  926  ? 27.942  24.417  91.272  1.00 17.61 ? 924  VAL B O     1 
ATOM   15610 C  CB    . VAL B 1  926  ? 30.336  25.958  90.165  1.00 17.91 ? 924  VAL B CB    1 
ATOM   15611 C  CG1   . VAL B 1  926  ? 30.622  26.881  91.354  1.00 18.84 ? 924  VAL B CG1   1 
ATOM   15612 C  CG2   . VAL B 1  926  ? 31.392  26.101  89.058  1.00 18.64 ? 924  VAL B CG2   1 
ATOM   15613 N  N     . PRO B 1  927  ? 29.412  24.059  92.914  1.00 20.04 ? 925  PRO B N     1 
ATOM   15614 C  CA    . PRO B 1  927  ? 28.348  23.893  93.897  1.00 19.15 ? 925  PRO B CA    1 
ATOM   15615 C  C     . PRO B 1  927  ? 27.780  25.238  94.299  1.00 17.65 ? 925  PRO B C     1 
ATOM   15616 O  O     . PRO B 1  927  ? 28.456  26.269  94.172  1.00 19.37 ? 925  PRO B O     1 
ATOM   15617 C  CB    . PRO B 1  927  ? 29.062  23.226  95.079  1.00 23.56 ? 925  PRO B CB    1 
ATOM   15618 C  CG    . PRO B 1  927  ? 30.443  23.779  95.004  1.00 22.59 ? 925  PRO B CG    1 
ATOM   15619 C  CD    . PRO B 1  927  ? 30.747  23.940  93.523  1.00 21.36 ? 925  PRO B CD    1 
ATOM   15620 N  N     . PRO B 1  928  ? 26.545  25.265  94.791  1.00 18.61 ? 926  PRO B N     1 
ATOM   15621 C  CA    . PRO B 1  928  ? 26.012  26.485  95.402  1.00 17.42 ? 926  PRO B CA    1 
ATOM   15622 C  C     . PRO B 1  928  ? 26.990  27.097  96.390  1.00 18.86 ? 926  PRO B C     1 
ATOM   15623 O  O     . PRO B 1  928  ? 27.527  26.420  97.278  1.00 19.91 ? 926  PRO B O     1 
ATOM   15624 C  CB    . PRO B 1  928  ? 24.738  25.995  96.096  1.00 19.92 ? 926  PRO B CB    1 
ATOM   15625 C  CG    . PRO B 1  928  ? 24.261  24.893  95.187  1.00 19.76 ? 926  PRO B CG    1 
ATOM   15626 C  CD    . PRO B 1  928  ? 25.528  24.205  94.693  1.00 20.67 ? 926  PRO B CD    1 
ATOM   15627 N  N     . THR B 1  929  ? 27.230  28.389  96.217  1.00 18.66 ? 927  THR B N     1 
ATOM   15628 C  CA    . THR B 1  929  ? 28.258  29.120  96.936  1.00 18.42 ? 927  THR B CA    1 
ATOM   15629 C  C     . THR B 1  929  ? 27.639  30.363  97.550  1.00 18.45 ? 927  THR B C     1 
ATOM   15630 O  O     . THR B 1  929  ? 26.869  31.070  96.895  1.00 19.42 ? 927  THR B O     1 
ATOM   15631 C  CB    . THR B 1  929  ? 29.398  29.499  95.985  1.00 18.00 ? 927  THR B CB    1 
ATOM   15632 O  OG1   . THR B 1  929  ? 29.968  28.302  95.442  1.00 18.20 ? 927  THR B OG1   1 
ATOM   15633 C  CG2   . THR B 1  929  ? 30.474  30.313  96.692  1.00 18.53 ? 927  THR B CG2   1 
ATOM   15634 N  N     . ILE B 1  930  ? 27.981  30.628  98.807  1.00 18.41 ? 928  ILE B N     1 
ATOM   15635 C  CA    . ILE B 1  930  ? 27.493  31.797  99.525  1.00 17.19 ? 928  ILE B CA    1 
ATOM   15636 C  C     . ILE B 1  930  ? 28.705  32.612  99.951  1.00 19.66 ? 928  ILE B C     1 
ATOM   15637 O  O     . ILE B 1  930  ? 29.619  32.091  100.611 1.00 19.81 ? 928  ILE B O     1 
ATOM   15638 C  CB    . ILE B 1  930  ? 26.625  31.409  100.732 1.00 19.64 ? 928  ILE B CB    1 
ATOM   15639 C  CG1   . ILE B 1  930  ? 25.421  30.579  100.275 1.00 17.59 ? 928  ILE B CG1   1 
ATOM   15640 C  CG2   . ILE B 1  930  ? 26.168  32.666  101.486 1.00 19.62 ? 928  ILE B CG2   1 
ATOM   15641 C  CD1   . ILE B 1  930  ? 24.551  30.067  101.408 1.00 24.33 ? 928  ILE B CD1   1 
ATOM   15642 N  N     . ILE B 1  931  ? 28.726  33.879  99.559  1.00 19.31 ? 929  ILE B N     1 
ATOM   15643 C  CA    . ILE B 1  931  ? 29.827  34.788  99.853  1.00 20.61 ? 929  ILE B CA    1 
ATOM   15644 C  C     . ILE B 1  931  ? 29.253  35.974  100.605 1.00 21.68 ? 929  ILE B C     1 
ATOM   15645 O  O     . ILE B 1  931  ? 28.327  36.630  100.116 1.00 18.60 ? 929  ILE B O     1 
ATOM   15646 C  CB    . ILE B 1  931  ? 30.541  35.246  98.576  1.00 17.86 ? 929  ILE B CB    1 
ATOM   15647 C  CG1   . ILE B 1  931  ? 31.006  34.029  97.776  1.00 18.64 ? 929  ILE B CG1   1 
ATOM   15648 C  CG2   . ILE B 1  931  ? 31.750  36.154  98.904  1.00 16.96 ? 929  ILE B CG2   1 
ATOM   15649 C  CD1   . ILE B 1  931  ? 31.880  34.395  96.584  1.00 19.95 ? 929  ILE B CD1   1 
ATOM   15650 N  N     . GLU B 1  932  ? 29.783  36.245  101.795 1.00 20.28 ? 930  GLU B N     1 
ATOM   15651 C  CA    . GLU B 1  932  ? 29.328  37.388  102.572 1.00 20.42 ? 930  GLU B CA    1 
ATOM   15652 C  C     . GLU B 1  932  ? 30.103  38.631  102.164 1.00 21.28 ? 930  GLU B C     1 
ATOM   15653 O  O     . GLU B 1  932  ? 31.339  38.626  102.153 1.00 21.35 ? 930  GLU B O     1 
ATOM   15654 C  CB    . GLU B 1  932  ? 29.491  37.119  104.065 1.00 23.78 ? 930  GLU B CB    1 
ATOM   15655 C  CG    . GLU B 1  932  ? 28.498  36.107  104.559 1.00 24.92 ? 930  GLU B CG    1 
ATOM   15656 C  CD    . GLU B 1  932  ? 28.496  35.967  106.062 1.00 32.85 ? 930  GLU B CD    1 
ATOM   15657 O  OE1   . GLU B 1  932  ? 29.433  36.495  106.715 1.00 34.91 ? 930  GLU B OE1   1 
ATOM   15658 O  OE2   . GLU B 1  932  ? 27.562  35.318  106.581 1.00 30.79 ? 930  GLU B OE2   1 
ATOM   15659 N  N     . LEU B 1  933  ? 29.382  39.691  101.823 1.00 19.71 ? 931  LEU B N     1 
ATOM   15660 C  CA    . LEU B 1  933  ? 30.011  40.940  101.430 1.00 21.80 ? 931  LEU B CA    1 
ATOM   15661 C  C     . LEU B 1  933  ? 29.858  41.985  102.529 1.00 23.87 ? 931  LEU B C     1 
ATOM   15662 O  O     . LEU B 1  933  ? 28.874  41.989  103.271 1.00 27.88 ? 931  LEU B O     1 
ATOM   15663 C  CB    . LEU B 1  933  ? 29.398  41.490  100.141 1.00 21.96 ? 931  LEU B CB    1 
ATOM   15664 C  CG    . LEU B 1  933  ? 29.493  40.612  98.896  1.00 22.16 ? 931  LEU B CG    1 
ATOM   15665 C  CD1   . LEU B 1  933  ? 28.823  41.336  97.736  1.00 23.29 ? 931  LEU B CD1   1 
ATOM   15666 C  CD2   . LEU B 1  933  ? 30.952  40.280  98.588  1.00 27.45 ? 931  LEU B CD2   1 
ATOM   15667 N  N     . GLU B 1  934  ? 30.833  42.887  102.601 1.00 27.07 ? 932  GLU B N     1 
ATOM   15668 C  CA    . GLU B 1  934  ? 30.687  44.063  103.450 1.00 26.11 ? 932  GLU B CA    1 
ATOM   15669 C  C     . GLU B 1  934  ? 29.820  45.113  102.777 1.00 27.98 ? 932  GLU B C     1 
ATOM   15670 O  O     . GLU B 1  934  ? 29.012  45.776  103.433 1.00 30.70 ? 932  GLU B O     1 
ATOM   15671 C  CB    . GLU B 1  934  ? 32.059  44.655  103.780 1.00 26.96 ? 932  GLU B CB    1 
ATOM   15672 N  N     . LYS B 1  935  ? 29.979  45.277  101.470 1.00 25.65 ? 933  LYS B N     1 
ATOM   15673 C  CA    . LYS B 1  935  ? 29.259  46.293  100.725 1.00 26.64 ? 933  LYS B CA    1 
ATOM   15674 C  C     . LYS B 1  935  ? 28.956  45.743  99.342  1.00 25.93 ? 933  LYS B C     1 
ATOM   15675 O  O     . LYS B 1  935  ? 29.722  44.947  98.796  1.00 24.85 ? 933  LYS B O     1 
ATOM   15676 C  CB    . LYS B 1  935  ? 30.070  47.588  100.621 1.00 28.51 ? 933  LYS B CB    1 
ATOM   15677 N  N     . LEU B 1  936  ? 27.821  46.161  98.783  1.00 23.69 ? 934  LEU B N     1 
ATOM   15678 C  CA    . LEU B 1  936  ? 27.480  45.705  97.442  1.00 24.74 ? 934  LEU B CA    1 
ATOM   15679 C  C     . LEU B 1  936  ? 28.560  46.093  96.437  1.00 25.65 ? 934  LEU B C     1 
ATOM   15680 O  O     . LEU B 1  936  ? 28.828  45.343  95.492  1.00 25.50 ? 934  LEU B O     1 
ATOM   15681 C  CB    . LEU B 1  936  ? 26.117  46.266  97.032  1.00 24.93 ? 934  LEU B CB    1 
ATOM   15682 C  CG    . LEU B 1  936  ? 25.215  45.295  96.271  1.00 26.12 ? 934  LEU B CG    1 
ATOM   15683 C  CD1   . LEU B 1  936  ? 23.765  45.758  96.323  1.00 24.90 ? 934  LEU B CD1   1 
ATOM   15684 C  CD2   . LEU B 1  936  ? 25.675  45.159  94.847  1.00 25.58 ? 934  LEU B CD2   1 
ATOM   15685 N  N     . SER B 1  937  ? 29.224  47.231  96.647  1.00 25.55 ? 935  SER B N     1 
ATOM   15686 C  CA    . SER B 1  937  ? 30.268  47.639  95.714  1.00 26.40 ? 935  SER B CA    1 
ATOM   15687 C  C     . SER B 1  937  ? 31.468  46.701  95.724  1.00 26.01 ? 935  SER B C     1 
ATOM   15688 O  O     . SER B 1  937  ? 32.341  46.844  94.856  1.00 24.66 ? 935  SER B O     1 
ATOM   15689 C  CB    . SER B 1  937  ? 30.724  49.068  96.018  1.00 25.92 ? 935  SER B CB    1 
ATOM   15690 O  OG    . SER B 1  937  ? 31.222  49.172  97.337  1.00 27.60 ? 935  SER B OG    1 
ATOM   15691 N  N     . ASP B 1  938  ? 31.548  45.767  96.685  1.00 23.57 ? 936  ASP B N     1 
ATOM   15692 C  CA    . ASP B 1  938  ? 32.541  44.697  96.605  1.00 27.74 ? 936  ASP B CA    1 
ATOM   15693 C  C     . ASP B 1  938  ? 32.369  43.865  95.345  1.00 24.16 ? 936  ASP B C     1 
ATOM   15694 O  O     . ASP B 1  938  ? 33.317  43.209  94.909  1.00 25.18 ? 936  ASP B O     1 
ATOM   15695 C  CB    . ASP B 1  938  ? 32.449  43.741  97.801  1.00 28.36 ? 936  ASP B CB    1 
ATOM   15696 C  CG    . ASP B 1  938  ? 32.804  44.397  99.127  1.00 32.17 ? 936  ASP B CG    1 
ATOM   15697 O  OD1   . ASP B 1  938  ? 33.349  45.517  99.129  1.00 31.94 ? 936  ASP B OD1   1 
ATOM   15698 O  OD2   . ASP B 1  938  ? 32.517  43.774  100.173 1.00 38.18 ? 936  ASP B OD2   1 
ATOM   15699 N  N     . LEU B 1  939  ? 31.172  43.851  94.782  1.00 22.58 ? 937  LEU B N     1 
ATOM   15700 C  CA    . LEU B 1  939  ? 30.854  43.047  93.614  1.00 24.35 ? 937  LEU B CA    1 
ATOM   15701 C  C     . LEU B 1  939  ? 30.901  43.953  92.390  1.00 25.70 ? 937  LEU B C     1 
ATOM   15702 O  O     . LEU B 1  939  ? 30.163  44.946  92.323  1.00 29.15 ? 937  LEU B O     1 
ATOM   15703 C  CB    . LEU B 1  939  ? 29.473  42.417  93.788  1.00 21.87 ? 937  LEU B CB    1 
ATOM   15704 C  CG    . LEU B 1  939  ? 28.975  41.386  92.783  1.00 27.54 ? 937  LEU B CG    1 
ATOM   15705 C  CD1   . LEU B 1  939  ? 29.925  40.209  92.695  1.00 27.59 ? 937  LEU B CD1   1 
ATOM   15706 C  CD2   . LEU B 1  939  ? 27.598  40.940  93.220  1.00 23.58 ? 937  LEU B CD2   1 
ATOM   15707 N  N     . GLN B 1  940  ? 31.758  43.606  91.426  1.00 22.85 ? 938  GLN B N     1 
ATOM   15708 C  CA    . GLN B 1  940  ? 32.069  44.481  90.302  1.00 25.22 ? 938  GLN B CA    1 
ATOM   15709 C  C     . GLN B 1  940  ? 31.610  43.952  88.948  1.00 23.91 ? 938  GLN B C     1 
ATOM   15710 O  O     . GLN B 1  940  ? 31.673  44.696  87.959  1.00 24.22 ? 938  GLN B O     1 
ATOM   15711 C  CB    . GLN B 1  940  ? 33.582  44.746  90.244  1.00 29.66 ? 938  GLN B CB    1 
ATOM   15712 N  N     . ARG B 1  941  ? 31.157  42.702  88.864  1.00 19.65 ? 939  ARG B N     1 
ATOM   15713 C  CA    . ARG B 1  941  ? 30.764  42.143  87.580  1.00 23.05 ? 939  ARG B CA    1 
ATOM   15714 C  C     . ARG B 1  941  ? 29.681  41.103  87.814  1.00 18.84 ? 939  ARG B C     1 
ATOM   15715 O  O     . ARG B 1  941  ? 29.546  40.559  88.913  1.00 18.09 ? 939  ARG B O     1 
ATOM   15716 C  CB    . ARG B 1  941  ? 31.960  41.525  86.837  1.00 22.53 ? 939  ARG B CB    1 
ATOM   15717 C  CG    . ARG B 1  941  ? 32.571  40.291  87.507  1.00 21.83 ? 939  ARG B CG    1 
ATOM   15718 C  CD    . ARG B 1  941  ? 33.909  39.912  86.845  1.00 27.21 ? 939  ARG B CD    1 
ATOM   15719 N  NE    . ARG B 1  941  ? 34.499  38.686  87.377  1.00 23.72 ? 939  ARG B NE    1 
ATOM   15720 C  CZ    . ARG B 1  941  ? 34.261  37.468  86.903  1.00 25.71 ? 939  ARG B CZ    1 
ATOM   15721 N  NH1   . ARG B 1  941  ? 33.381  37.264  85.931  1.00 24.50 ? 939  ARG B NH1   1 
ATOM   15722 N  NH2   . ARG B 1  941  ? 34.932  36.431  87.405  1.00 22.61 ? 939  ARG B NH2   1 
ATOM   15723 N  N     . GLU B 1  942  ? 28.892  40.855  86.767  1.00 19.84 ? 940  GLU B N     1 
ATOM   15724 C  CA    . GLU B 1  942  ? 27.925  39.764  86.792  1.00 18.58 ? 940  GLU B CA    1 
ATOM   15725 C  C     . GLU B 1  942  ? 28.666  38.435  86.753  1.00 20.00 ? 940  GLU B C     1 
ATOM   15726 O  O     . GLU B 1  942  ? 29.387  38.152  85.792  1.00 21.34 ? 940  GLU B O     1 
ATOM   15727 C  CB    . GLU B 1  942  ? 26.972  39.872  85.602  1.00 19.81 ? 940  GLU B CB    1 
ATOM   15728 C  CG    . GLU B 1  942  ? 25.977  38.716  85.510  1.00 17.00 ? 940  GLU B CG    1 
ATOM   15729 C  CD    . GLU B 1  942  ? 25.273  38.678  84.168  1.00 19.11 ? 940  GLU B CD    1 
ATOM   15730 O  OE1   . GLU B 1  942  ? 25.955  38.891  83.139  1.00 21.32 ? 940  GLU B OE1   1 
ATOM   15731 O  OE2   . GLU B 1  942  ? 24.052  38.428  84.144  1.00 16.46 ? 940  GLU B OE2   1 
ATOM   15732 N  N     . VAL B 1  943  ? 28.499  37.628  87.793  1.00 17.28 ? 941  VAL B N     1 
ATOM   15733 C  CA    . VAL B 1  943  ? 29.118  36.312  87.880  1.00 18.09 ? 941  VAL B CA    1 
ATOM   15734 C  C     . VAL B 1  943  ? 28.022  35.295  87.607  1.00 17.61 ? 941  VAL B C     1 
ATOM   15735 O  O     . VAL B 1  943  ? 27.116  35.106  88.428  1.00 16.33 ? 941  VAL B O     1 
ATOM   15736 C  CB    . VAL B 1  943  ? 29.785  36.090  89.241  1.00 19.58 ? 941  VAL B CB    1 
ATOM   15737 C  CG1   . VAL B 1  943  ? 30.416  34.709  89.298  1.00 19.40 ? 941  VAL B CG1   1 
ATOM   15738 C  CG2   . VAL B 1  943  ? 30.842  37.162  89.470  1.00 20.95 ? 941  VAL B CG2   1 
ATOM   15739 N  N     . PHE B 1  944  ? 28.093  34.660  86.434  1.00 16.84 ? 942  PHE B N     1 
ATOM   15740 C  CA    . PHE B 1  944  ? 26.971  33.905  85.879  1.00 15.63 ? 942  PHE B CA    1 
ATOM   15741 C  C     . PHE B 1  944  ? 27.092  32.443  86.313  1.00 15.90 ? 942  PHE B C     1 
ATOM   15742 O  O     . PHE B 1  944  ? 27.452  31.545  85.553  1.00 16.54 ? 942  PHE B O     1 
ATOM   15743 C  CB    . PHE B 1  944  ? 26.948  34.054  84.359  1.00 14.86 ? 942  PHE B CB    1 
ATOM   15744 C  CG    . PHE B 1  944  ? 25.616  33.781  83.737  1.00 17.03 ? 942  PHE B CG    1 
ATOM   15745 C  CD1   . PHE B 1  944  ? 24.578  34.687  83.882  1.00 16.05 ? 942  PHE B CD1   1 
ATOM   15746 C  CD2   . PHE B 1  944  ? 25.407  32.638  82.975  1.00 15.84 ? 942  PHE B CD2   1 
ATOM   15747 C  CE1   . PHE B 1  944  ? 23.336  34.456  83.296  1.00 16.04 ? 942  PHE B CE1   1 
ATOM   15748 C  CE2   . PHE B 1  944  ? 24.152  32.405  82.377  1.00 17.15 ? 942  PHE B CE2   1 
ATOM   15749 C  CZ    . PHE B 1  944  ? 23.121  33.312  82.554  1.00 16.43 ? 942  PHE B CZ    1 
ATOM   15750 N  N     . GLY B 1  945  ? 26.779  32.220  87.585  1.00 15.74 ? 943  GLY B N     1 
ATOM   15751 C  CA    . GLY B 1  945  ? 26.913  30.916  88.167  1.00 16.39 ? 943  GLY B CA    1 
ATOM   15752 C  C     . GLY B 1  945  ? 26.204  30.855  89.496  1.00 17.29 ? 943  GLY B C     1 
ATOM   15753 O  O     . GLY B 1  945  ? 25.524  31.798  89.907  1.00 16.92 ? 943  GLY B O     1 
ATOM   15754 N  N     . PRO B 1  946  ? 26.361  29.746  90.208  1.00 17.08 ? 944  PRO B N     1 
ATOM   15755 C  CA    . PRO B 1  946  ? 25.575  29.541  91.439  1.00 17.39 ? 944  PRO B CA    1 
ATOM   15756 C  C     . PRO B 1  946  ? 26.231  30.207  92.639  1.00 15.41 ? 944  PRO B C     1 
ATOM   15757 O  O     . PRO B 1  946  ? 26.613  29.561  93.612  1.00 17.96 ? 944  PRO B O     1 
ATOM   15758 C  CB    . PRO B 1  946  ? 25.545  28.012  91.553  1.00 16.10 ? 944  PRO B CB    1 
ATOM   15759 C  CG    . PRO B 1  946  ? 26.921  27.603  90.991  1.00 17.00 ? 944  PRO B CG    1 
ATOM   15760 C  CD    . PRO B 1  946  ? 27.160  28.564  89.841  1.00 15.75 ? 944  PRO B CD    1 
ATOM   15761 N  N     . VAL B 1  947  ? 26.397  31.521  92.557  1.00 15.15 ? 945  VAL B N     1 
ATOM   15762 C  CA    . VAL B 1  947  ? 27.173  32.257  93.547  1.00 16.19 ? 945  VAL B CA    1 
ATOM   15763 C  C     . VAL B 1  947  ? 26.277  33.347  94.112  1.00 19.38 ? 945  VAL B C     1 
ATOM   15764 O  O     . VAL B 1  947  ? 25.989  34.346  93.434  1.00 17.90 ? 945  VAL B O     1 
ATOM   15765 C  CB    . VAL B 1  947  ? 28.466  32.839  92.965  1.00 16.59 ? 945  VAL B CB    1 
ATOM   15766 C  CG1   . VAL B 1  947  ? 29.259  33.549  94.057  1.00 18.49 ? 945  VAL B CG1   1 
ATOM   15767 C  CG2   . VAL B 1  947  ? 29.310  31.742  92.332  1.00 17.34 ? 945  VAL B CG2   1 
ATOM   15768 N  N     . LEU B 1  948  ? 25.835  33.156  95.353  1.00 16.28 ? 946  LEU B N     1 
ATOM   15769 C  CA    . LEU B 1  948  ? 24.959  34.095  96.038  1.00 17.28 ? 946  LEU B CA    1 
ATOM   15770 C  C     . LEU B 1  948  ? 25.773  34.958  96.980  1.00 17.23 ? 946  LEU B C     1 
ATOM   15771 O  O     . LEU B 1  948  ? 26.516  34.441  97.816  1.00 17.75 ? 946  LEU B O     1 
ATOM   15772 C  CB    . LEU B 1  948  ? 23.886  33.357  96.831  1.00 15.95 ? 946  LEU B CB    1 
ATOM   15773 C  CG    . LEU B 1  948  ? 22.956  34.276  97.615  1.00 16.51 ? 946  LEU B CG    1 
ATOM   15774 C  CD1   . LEU B 1  948  ? 22.149  35.140  96.644  1.00 17.18 ? 946  LEU B CD1   1 
ATOM   15775 C  CD2   . LEU B 1  948  ? 22.042  33.416  98.471  1.00 19.63 ? 946  LEU B CD2   1 
ATOM   15776 N  N     . HIS B 1  949  ? 25.629  36.263  96.854  1.00 15.78 ? 947  HIS B N     1 
ATOM   15777 C  CA    . HIS B 1  949  ? 26.305  37.187  97.747  1.00 16.05 ? 947  HIS B CA    1 
ATOM   15778 C  C     . HIS B 1  949  ? 25.321  37.657  98.803  1.00 19.32 ? 947  HIS B C     1 
ATOM   15779 O  O     . HIS B 1  949  ? 24.134  37.832  98.518  1.00 20.20 ? 947  HIS B O     1 
ATOM   15780 C  CB    . HIS B 1  949  ? 26.877  38.352  96.948  1.00 18.13 ? 947  HIS B CB    1 
ATOM   15781 C  CG    . HIS B 1  949  ? 27.772  37.893  95.842  1.00 16.83 ? 947  HIS B CG    1 
ATOM   15782 N  ND1   . HIS B 1  949  ? 27.293  37.535  94.600  1.00 16.96 ? 947  HIS B ND1   1 
ATOM   15783 C  CD2   . HIS B 1  949  ? 29.106  37.653  95.817  1.00 17.23 ? 947  HIS B CD2   1 
ATOM   15784 C  CE1   . HIS B 1  949  ? 28.299  37.130  93.844  1.00 16.68 ? 947  HIS B CE1   1 
ATOM   15785 N  NE2   . HIS B 1  949  ? 29.407  37.183  94.562  1.00 16.74 ? 947  HIS B NE2   1 
ATOM   15786 N  N     . VAL B 1  950  ? 25.797  37.807  100.037 1.00 17.81 ? 948  VAL B N     1 
ATOM   15787 C  CA    . VAL B 1  950  ? 24.924  38.164  101.148 1.00 20.17 ? 948  VAL B CA    1 
ATOM   15788 C  C     . VAL B 1  950  ? 25.372  39.481  101.753 1.00 19.53 ? 948  VAL B C     1 
ATOM   15789 O  O     . VAL B 1  950  ? 26.555  39.664  102.072 1.00 20.31 ? 948  VAL B O     1 
ATOM   15790 C  CB    . VAL B 1  950  ? 24.873  37.070  102.225 1.00 19.52 ? 948  VAL B CB    1 
ATOM   15791 C  CG1   . VAL B 1  950  ? 24.049  37.576  103.398 1.00 19.44 ? 948  VAL B CG1   1 
ATOM   15792 C  CG2   . VAL B 1  950  ? 24.247  35.805  101.634 1.00 19.99 ? 948  VAL B CG2   1 
ATOM   15793 N  N     . ILE B 1  951  ? 24.407  40.371  101.946 1.00 18.10 ? 949  ILE B N     1 
ATOM   15794 C  CA    . ILE B 1  951  ? 24.589  41.666  102.578 1.00 19.02 ? 949  ILE B CA    1 
ATOM   15795 C  C     . ILE B 1  951  ? 23.627  41.729  103.754 1.00 18.16 ? 949  ILE B C     1 
ATOM   15796 O  O     . ILE B 1  951  ? 22.457  41.358  103.611 1.00 19.02 ? 949  ILE B O     1 
ATOM   15797 C  CB    . ILE B 1  951  ? 24.290  42.809  101.590 1.00 21.82 ? 949  ILE B CB    1 
ATOM   15798 C  CG1   . ILE B 1  951  ? 25.326  42.845  100.476 1.00 25.31 ? 949  ILE B CG1   1 
ATOM   15799 C  CG2   . ILE B 1  951  ? 24.214  44.159  102.310 1.00 26.00 ? 949  ILE B CG2   1 
ATOM   15800 C  CD1   . ILE B 1  951  ? 25.107  43.996  99.545  1.00 28.84 ? 949  ILE B CD1   1 
ATOM   15801 N  N     . ARG B 1  952  ? 24.115  42.178  104.909 1.00 17.32 ? 950  ARG B N     1 
ATOM   15802 C  CA    A ARG B 1  952  ? 23.264  42.447  106.059 0.52 19.50 ? 950  ARG B CA    1 
ATOM   15803 C  CA    B ARG B 1  952  ? 23.272  42.449  106.065 0.48 19.50 ? 950  ARG B CA    1 
ATOM   15804 C  C     . ARG B 1  952  ? 23.055  43.951  106.171 1.00 19.51 ? 950  ARG B C     1 
ATOM   15805 O  O     . ARG B 1  952  ? 23.981  44.733  105.943 1.00 22.92 ? 950  ARG B O     1 
ATOM   15806 C  CB    A ARG B 1  952  ? 23.886  41.891  107.345 0.52 19.79 ? 950  ARG B CB    1 
ATOM   15807 C  CB    B ARG B 1  952  ? 23.917  41.924  107.347 0.48 19.78 ? 950  ARG B CB    1 
ATOM   15808 C  CG    A ARG B 1  952  ? 24.092  40.379  107.319 0.52 20.51 ? 950  ARG B CG    1 
ATOM   15809 C  CG    B ARG B 1  952  ? 24.504  40.538  107.201 0.48 21.08 ? 950  ARG B CG    1 
ATOM   15810 C  CD    A ARG B 1  952  ? 25.093  39.953  108.385 0.52 22.51 ? 950  ARG B CD    1 
ATOM   15811 C  CD    B ARG B 1  952  ? 25.431  40.235  108.367 0.48 21.95 ? 950  ARG B CD    1 
ATOM   15812 N  NE    A ARG B 1  952  ? 25.621  38.613  108.152 0.52 24.86 ? 950  ARG B NE    1 
ATOM   15813 N  NE    B ARG B 1  952  ? 24.690  40.154  109.619 0.48 21.89 ? 950  ARG B NE    1 
ATOM   15814 C  CZ    A ARG B 1  952  ? 25.338  37.555  108.901 0.52 22.70 ? 950  ARG B CZ    1 
ATOM   15815 C  CZ    B ARG B 1  952  ? 24.374  39.019  110.226 0.48 22.82 ? 950  ARG B CZ    1 
ATOM   15816 N  NH1   A ARG B 1  952  ? 24.496  37.633  109.917 0.52 23.76 ? 950  ARG B NH1   1 
ATOM   15817 N  NH1   B ARG B 1  952  ? 24.717  37.846  109.719 0.48 23.46 ? 950  ARG B NH1   1 
ATOM   15818 N  NH2   A ARG B 1  952  ? 25.927  36.394  108.630 0.52 22.42 ? 950  ARG B NH2   1 
ATOM   15819 N  NH2   B ARG B 1  952  ? 23.690  39.063  111.369 0.48 21.83 ? 950  ARG B NH2   1 
ATOM   15820 N  N     . TYR B 1  953  ? 21.830  44.362  106.514 1.00 18.40 ? 951  TYR B N     1 
ATOM   15821 C  CA    . TYR B 1  953  ? 21.551  45.793  106.597 1.00 18.78 ? 951  TYR B CA    1 
ATOM   15822 C  C     . TYR B 1  953  ? 20.680  46.110  107.803 1.00 19.05 ? 951  TYR B C     1 
ATOM   15823 O  O     . TYR B 1  953  ? 19.888  45.281  108.254 1.00 19.30 ? 951  TYR B O     1 
ATOM   15824 C  CB    . TYR B 1  953  ? 20.863  46.314  105.319 1.00 19.80 ? 951  TYR B CB    1 
ATOM   15825 C  CG    . TYR B 1  953  ? 19.422  45.876  105.174 1.00 17.03 ? 951  TYR B CG    1 
ATOM   15826 C  CD1   . TYR B 1  953  ? 19.094  44.635  104.620 1.00 16.01 ? 951  TYR B CD1   1 
ATOM   15827 C  CD2   . TYR B 1  953  ? 18.384  46.703  105.582 1.00 17.94 ? 951  TYR B CD2   1 
ATOM   15828 C  CE1   . TYR B 1  953  ? 17.771  44.242  104.494 1.00 17.40 ? 951  TYR B CE1   1 
ATOM   15829 C  CE2   . TYR B 1  953  ? 17.059  46.313  105.455 1.00 19.90 ? 951  TYR B CE2   1 
ATOM   15830 C  CZ    . TYR B 1  953  ? 16.759  45.084  104.908 1.00 18.02 ? 951  TYR B CZ    1 
ATOM   15831 O  OH    . TYR B 1  953  ? 15.434  44.711  104.799 1.00 18.83 ? 951  TYR B OH    1 
ATOM   15832 N  N     . ARG B 1  954  ? 20.856  47.321  108.338 1.00 20.39 ? 952  ARG B N     1 
ATOM   15833 C  CA    . ARG B 1  954  ? 19.966  47.840  109.369 1.00 24.07 ? 952  ARG B CA    1 
ATOM   15834 C  C     . ARG B 1  954  ? 18.756  48.478  108.703 1.00 23.64 ? 952  ARG B C     1 
ATOM   15835 O  O     . ARG B 1  954  ? 18.889  49.137  107.669 1.00 22.53 ? 952  ARG B O     1 
ATOM   15836 C  CB    . ARG B 1  954  ? 20.694  48.871  110.241 1.00 25.60 ? 952  ARG B CB    1 
ATOM   15837 N  N     . ARG B 1  955  ? 17.569  48.292  109.301 1.00 22.92 ? 953  ARG B N     1 
ATOM   15838 C  CA    . ARG B 1  955  ? 16.349  48.776  108.657 1.00 26.21 ? 953  ARG B CA    1 
ATOM   15839 C  C     . ARG B 1  955  ? 16.392  50.284  108.424 1.00 25.40 ? 953  ARG B C     1 
ATOM   15840 O  O     . ARG B 1  955  ? 15.822  50.773  107.438 1.00 24.59 ? 953  ARG B O     1 
ATOM   15841 C  CB    . ARG B 1  955  ? 15.118  48.389  109.487 1.00 26.90 ? 953  ARG B CB    1 
ATOM   15842 C  CG    . ARG B 1  955  ? 13.771  48.820  108.894 1.00 34.78 ? 953  ARG B CG    1 
ATOM   15843 C  CD    . ARG B 1  955  ? 13.603  48.409  107.413 1.00 31.48 ? 953  ARG B CD    1 
ATOM   15844 N  NE    . ARG B 1  955  ? 12.318  48.831  106.853 1.00 31.20 ? 953  ARG B NE    1 
ATOM   15845 C  CZ    . ARG B 1  955  ? 12.006  50.082  106.531 1.00 36.32 ? 953  ARG B CZ    1 
ATOM   15846 N  NH1   . ARG B 1  955  ? 12.858  51.079  106.714 1.00 33.12 ? 953  ARG B NH1   1 
ATOM   15847 N  NH2   . ARG B 1  955  ? 10.804  50.341  106.016 1.00 37.47 ? 953  ARG B NH2   1 
ATOM   15848 N  N     . ASP B 1  956  ? 17.067  51.030  109.305 1.00 24.38 ? 954  ASP B N     1 
ATOM   15849 C  CA    . ASP B 1  956  ? 17.259  52.464  109.105 1.00 24.71 ? 954  ASP B CA    1 
ATOM   15850 C  C     . ASP B 1  956  ? 18.049  52.778  107.845 1.00 25.93 ? 954  ASP B C     1 
ATOM   15851 O  O     . ASP B 1  956  ? 17.981  53.912  107.352 1.00 29.15 ? 954  ASP B O     1 
ATOM   15852 C  CB    . ASP B 1  956  ? 17.983  53.083  110.300 1.00 28.54 ? 954  ASP B CB    1 
ATOM   15853 C  CG    . ASP B 1  956  ? 17.104  53.188  111.515 1.00 38.13 ? 954  ASP B CG    1 
ATOM   15854 O  OD1   . ASP B 1  956  ? 15.874  53.013  111.366 1.00 39.39 ? 954  ASP B OD1   1 
ATOM   15855 O  OD2   . ASP B 1  956  ? 17.644  53.445  112.616 1.00 44.42 ? 954  ASP B OD2   1 
ATOM   15856 N  N     . ASP B 1  957  ? 18.806  51.815  107.327 1.00 22.73 ? 955  ASP B N     1 
ATOM   15857 C  CA    . ASP B 1  957  ? 19.622  52.015  106.142 1.00 24.56 ? 955  ASP B CA    1 
ATOM   15858 C  C     . ASP B 1  957  ? 18.952  51.503  104.875 1.00 21.21 ? 955  ASP B C     1 
ATOM   15859 O  O     . ASP B 1  957  ? 19.619  51.403  103.848 1.00 21.67 ? 955  ASP B O     1 
ATOM   15860 C  CB    . ASP B 1  957  ? 20.977  51.325  106.299 1.00 24.19 ? 955  ASP B CB    1 
ATOM   15861 C  CG    . ASP B 1  957  ? 21.887  52.033  107.275 1.00 30.93 ? 955  ASP B CG    1 
ATOM   15862 O  OD1   . ASP B 1  957  ? 21.743  53.264  107.438 1.00 31.89 ? 955  ASP B OD1   1 
ATOM   15863 O  OD2   . ASP B 1  957  ? 22.752  51.355  107.874 1.00 32.80 ? 955  ASP B OD2   1 
ATOM   15864 N  N     . LEU B 1  958  ? 17.652  51.188  104.927 1.00 21.17 ? 956  LEU B N     1 
ATOM   15865 C  CA    . LEU B 1  958  ? 16.981  50.585  103.775 1.00 20.60 ? 956  LEU B CA    1 
ATOM   15866 C  C     . LEU B 1  958  ? 17.095  51.464  102.530 1.00 20.55 ? 956  LEU B C     1 
ATOM   15867 O  O     . LEU B 1  958  ? 17.387  50.970  101.431 1.00 20.30 ? 956  LEU B O     1 
ATOM   15868 C  CB    . LEU B 1  958  ? 15.514  50.322  104.105 1.00 21.24 ? 956  LEU B CB    1 
ATOM   15869 C  CG    . LEU B 1  958  ? 14.692  49.714  102.966 1.00 20.71 ? 956  LEU B CG    1 
ATOM   15870 C  CD1   . LEU B 1  958  ? 15.290  48.385  102.481 1.00 19.62 ? 956  LEU B CD1   1 
ATOM   15871 C  CD2   . LEU B 1  958  ? 13.250  49.545  103.412 1.00 21.53 ? 956  LEU B CD2   1 
ATOM   15872 N  N     . ASP B 1  959  ? 16.865  52.771  102.679 1.00 19.25 ? 957  ASP B N     1 
ATOM   15873 C  CA    . ASP B 1  959  ? 16.912  53.643  101.509 1.00 19.54 ? 957  ASP B CA    1 
ATOM   15874 C  C     . ASP B 1  959  ? 18.303  53.654  100.884 1.00 18.46 ? 957  ASP B C     1 
ATOM   15875 O  O     . ASP B 1  959  ? 18.437  53.642  99.656  1.00 20.33 ? 957  ASP B O     1 
ATOM   15876 C  CB    . ASP B 1  959  ? 16.479  55.059  101.884 1.00 19.50 ? 957  ASP B CB    1 
ATOM   15877 C  CG    . ASP B 1  959  ? 15.999  55.842  100.691 1.00 19.51 ? 957  ASP B CG    1 
ATOM   15878 O  OD1   . ASP B 1  959  ? 15.275  55.263  99.854  1.00 19.43 ? 957  ASP B OD1   1 
ATOM   15879 O  OD2   . ASP B 1  959  ? 16.329  57.040  100.582 1.00 21.86 ? 957  ASP B OD2   1 
ATOM   15880 N  N     . ARG B 1  960  ? 19.349  53.681  101.716 1.00 18.51 ? 958  ARG B N     1 
ATOM   15881 C  CA    . ARG B 1  960  ? 20.714  53.637  101.204 1.00 18.12 ? 958  ARG B CA    1 
ATOM   15882 C  C     . ARG B 1  960  ? 21.011  52.294  100.551 1.00 18.77 ? 958  ARG B C     1 
ATOM   15883 O  O     . ARG B 1  960  ? 21.739  52.230  99.557  1.00 18.58 ? 958  ARG B O     1 
ATOM   15884 C  CB    . ARG B 1  960  ? 21.702  53.915  102.342 1.00 21.19 ? 958  ARG B CB    1 
ATOM   15885 N  N     . LEU B 1  961  ? 20.482  51.208  101.113 1.00 16.89 ? 959  LEU B N     1 
ATOM   15886 C  CA    . LEU B 1  961  ? 20.637  49.900  100.486 1.00 17.71 ? 959  LEU B CA    1 
ATOM   15887 C  C     . LEU B 1  961  ? 20.032  49.888  99.085  1.00 17.82 ? 959  LEU B C     1 
ATOM   15888 O  O     . LEU B 1  961  ? 20.627  49.339  98.148  1.00 16.80 ? 959  LEU B O     1 
ATOM   15889 C  CB    . LEU B 1  961  ? 19.989  48.822  101.356 1.00 18.26 ? 959  LEU B CB    1 
ATOM   15890 C  CG    . LEU B 1  961  ? 20.008  47.412  100.757 1.00 19.09 ? 959  LEU B CG    1 
ATOM   15891 C  CD1   . LEU B 1  961  ? 21.440  46.911  100.629 1.00 21.08 ? 959  LEU B CD1   1 
ATOM   15892 C  CD2   . LEU B 1  961  ? 19.150  46.455  101.571 1.00 20.21 ? 959  LEU B CD2   1 
ATOM   15893 N  N     . VAL B 1  962  ? 18.852  50.486  98.919  1.00 16.05 ? 960  VAL B N     1 
ATOM   15894 C  CA    . VAL B 1  962  ? 18.264  50.542  97.585  1.00 16.58 ? 960  VAL B CA    1 
ATOM   15895 C  C     . VAL B 1  962  ? 19.187  51.294  96.632  1.00 18.97 ? 960  VAL B C     1 
ATOM   15896 O  O     . VAL B 1  962  ? 19.393  50.869  95.488  1.00 18.38 ? 960  VAL B O     1 
ATOM   15897 C  CB    . VAL B 1  962  ? 16.861  51.169  97.646  1.00 15.91 ? 960  VAL B CB    1 
ATOM   15898 C  CG1   . VAL B 1  962  ? 16.367  51.498  96.252  1.00 19.96 ? 960  VAL B CG1   1 
ATOM   15899 C  CG2   . VAL B 1  962  ? 15.882  50.214  98.343  1.00 17.78 ? 960  VAL B CG2   1 
ATOM   15900 N  N     . ASP B 1  963  ? 19.769  52.413  97.091  1.00 17.15 ? 961  ASP B N     1 
ATOM   15901 C  CA    . ASP B 1  963  ? 20.782  53.106  96.292  1.00 19.42 ? 961  ASP B CA    1 
ATOM   15902 C  C     . ASP B 1  963  ? 21.911  52.165  95.909  1.00 17.82 ? 961  ASP B C     1 
ATOM   15903 O  O     . ASP B 1  963  ? 22.356  52.150  94.753  1.00 19.41 ? 961  ASP B O     1 
ATOM   15904 C  CB    . ASP B 1  963  ? 21.371  54.293  97.054  1.00 19.26 ? 961  ASP B CB    1 
ATOM   15905 C  CG    . ASP B 1  963  ? 20.423  55.441  97.185  1.00 22.20 ? 961  ASP B CG    1 
ATOM   15906 O  OD1   . ASP B 1  963  ? 19.451  55.500  96.405  1.00 23.53 ? 961  ASP B OD1   1 
ATOM   15907 O  OD2   . ASP B 1  963  ? 20.680  56.302  98.069  1.00 23.47 ? 961  ASP B OD2   1 
ATOM   15908 N  N     . ASP B 1  964  ? 22.409  51.389  96.881  1.00 18.51 ? 962  ASP B N     1 
ATOM   15909 C  CA    . ASP B 1  964  ? 23.528  50.495  96.608  1.00 18.98 ? 962  ASP B CA    1 
ATOM   15910 C  C     . ASP B 1  964  ? 23.164  49.480  95.535  1.00 19.19 ? 962  ASP B C     1 
ATOM   15911 O  O     . ASP B 1  964  ? 23.987  49.166  94.670  1.00 17.77 ? 962  ASP B O     1 
ATOM   15912 C  CB    . ASP B 1  964  ? 23.971  49.781  97.884  1.00 19.74 ? 962  ASP B CB    1 
ATOM   15913 C  CG    . ASP B 1  964  ? 24.624  50.720  98.887  1.00 20.48 ? 962  ASP B CG    1 
ATOM   15914 O  OD1   . ASP B 1  964  ? 24.931  51.877  98.527  1.00 22.50 ? 962  ASP B OD1   1 
ATOM   15915 O  OD2   . ASP B 1  964  ? 24.823  50.294  100.045 1.00 26.79 ? 962  ASP B OD2   1 
ATOM   15916 N  N     . VAL B 1  965  ? 21.928  48.974  95.560  1.00 16.13 ? 963  VAL B N     1 
ATOM   15917 C  CA    . VAL B 1  965  ? 21.484  48.049  94.519  1.00 14.30 ? 963  VAL B CA    1 
ATOM   15918 C  C     . VAL B 1  965  ? 21.452  48.750  93.165  1.00 16.29 ? 963  VAL B C     1 
ATOM   15919 O  O     . VAL B 1  965  ? 21.957  48.225  92.164  1.00 17.60 ? 963  VAL B O     1 
ATOM   15920 C  CB    . VAL B 1  965  ? 20.108  47.451  94.872  1.00 16.80 ? 963  VAL B CB    1 
ATOM   15921 C  CG1   . VAL B 1  965  ? 19.577  46.626  93.676  1.00 15.62 ? 963  VAL B CG1   1 
ATOM   15922 C  CG2   . VAL B 1  965  ? 20.209  46.583  96.123  1.00 19.74 ? 963  VAL B CG2   1 
ATOM   15923 N  N     . ASN B 1  966  ? 20.881  49.960  93.117  1.00 16.09 ? 964  ASN B N     1 
ATOM   15924 C  CA    . ASN B 1  966  ? 20.808  50.702  91.854  1.00 16.53 ? 964  ASN B CA    1 
ATOM   15925 C  C     . ASN B 1  966  ? 22.192  51.106  91.364  1.00 18.19 ? 964  ASN B C     1 
ATOM   15926 O  O     . ASN B 1  966  ? 22.399  51.278  90.158  1.00 18.79 ? 964  ASN B O     1 
ATOM   15927 C  CB    . ASN B 1  966  ? 19.962  51.965  92.004  1.00 17.10 ? 964  ASN B CB    1 
ATOM   15928 C  CG    . ASN B 1  966  ? 18.481  51.680  92.222  1.00 16.30 ? 964  ASN B CG    1 
ATOM   15929 O  OD1   . ASN B 1  966  ? 17.954  50.657  91.776  1.00 16.50 ? 964  ASN B OD1   1 
ATOM   15930 N  ND2   . ASN B 1  966  ? 17.801  52.601  92.899  1.00 15.96 ? 964  ASN B ND2   1 
ATOM   15931 N  N     . ALA B 1  967  ? 23.142  51.263  92.284  1.00 16.53 ? 965  ALA B N     1 
ATOM   15932 C  CA    . ALA B 1  967  ? 24.435  51.838  91.942  1.00 18.36 ? 965  ALA B CA    1 
ATOM   15933 C  C     . ALA B 1  967  ? 25.286  50.925  91.075  1.00 18.80 ? 965  ALA B C     1 
ATOM   15934 O  O     . ALA B 1  967  ? 26.298  51.391  90.541  1.00 18.38 ? 965  ALA B O     1 
ATOM   15935 C  CB    . ALA B 1  967  ? 25.211  52.181  93.218  1.00 20.85 ? 965  ALA B CB    1 
ATOM   15936 N  N     . THR B 1  968  ? 24.937  49.641  90.950  1.00 17.85 ? 966  THR B N     1 
ATOM   15937 C  CA    . THR B 1  968  ? 25.692  48.771  90.054  1.00 15.73 ? 966  THR B CA    1 
ATOM   15938 C  C     . THR B 1  968  ? 25.543  49.189  88.595  1.00 17.81 ? 966  THR B C     1 
ATOM   15939 O  O     . THR B 1  968  ? 26.374  48.799  87.767  1.00 18.51 ? 966  THR B O     1 
ATOM   15940 C  CB    . THR B 1  968  ? 25.242  47.316  90.174  1.00 15.27 ? 966  THR B CB    1 
ATOM   15941 O  OG1   . THR B 1  968  ? 23.961  47.184  89.535  1.00 16.69 ? 966  THR B OG1   1 
ATOM   15942 C  CG2   . THR B 1  968  ? 25.131  46.879  91.632  1.00 18.71 ? 966  THR B CG2   1 
ATOM   15943 N  N     . GLY B 1  969  ? 24.502  49.958  88.263  1.00 17.64 ? 967  GLY B N     1 
ATOM   15944 C  CA    . GLY B 1  969  ? 24.198  50.288  86.890  1.00 16.80 ? 967  GLY B CA    1 
ATOM   15945 C  C     . GLY B 1  969  ? 23.290  49.297  86.197  1.00 17.39 ? 967  GLY B C     1 
ATOM   15946 O  O     . GLY B 1  969  ? 22.777  49.604  85.118  1.00 17.31 ? 967  GLY B O     1 
ATOM   15947 N  N     . TYR B 1  970  ? 23.082  48.124  86.782  1.00 16.96 ? 968  TYR B N     1 
ATOM   15948 C  CA    . TYR B 1  970  ? 22.167  47.131  86.250  1.00 15.01 ? 968  TYR B CA    1 
ATOM   15949 C  C     . TYR B 1  970  ? 20.756  47.429  86.742  1.00 16.75 ? 968  TYR B C     1 
ATOM   15950 O  O     . TYR B 1  970  ? 20.545  48.255  87.630  1.00 17.72 ? 968  TYR B O     1 
ATOM   15951 C  CB    . TYR B 1  970  ? 22.615  45.734  86.686  1.00 13.92 ? 968  TYR B CB    1 
ATOM   15952 C  CG    . TYR B 1  970  ? 23.829  45.212  85.949  1.00 17.58 ? 968  TYR B CG    1 
ATOM   15953 C  CD1   . TYR B 1  970  ? 23.688  44.692  84.677  1.00 19.89 ? 968  TYR B CD1   1 
ATOM   15954 C  CD2   . TYR B 1  970  ? 25.100  45.213  86.534  1.00 18.04 ? 968  TYR B CD2   1 
ATOM   15955 C  CE1   . TYR B 1  970  ? 24.771  44.183  83.964  1.00 21.77 ? 968  TYR B CE1   1 
ATOM   15956 C  CE2   . TYR B 1  970  ? 26.214  44.695  85.815  1.00 22.96 ? 968  TYR B CE2   1 
ATOM   15957 C  CZ    . TYR B 1  970  ? 26.016  44.187  84.533  1.00 23.29 ? 968  TYR B CZ    1 
ATOM   15958 O  OH    . TYR B 1  970  ? 27.059  43.664  83.784  1.00 27.77 ? 968  TYR B OH    1 
ATOM   15959 N  N     . GLY B 1  971  ? 19.780  46.743  86.157  1.00 13.89 ? 969  GLY B N     1 
ATOM   15960 C  CA    . GLY B 1  971  ? 18.402  46.931  86.570  1.00 15.05 ? 969  GLY B CA    1 
ATOM   15961 C  C     . GLY B 1  971  ? 17.497  45.935  85.889  1.00 15.18 ? 969  GLY B C     1 
ATOM   15962 O  O     . GLY B 1  971  ? 16.567  46.319  85.167  1.00 15.39 ? 969  GLY B O     1 
ATOM   15963 N  N     . LEU B 1  972  ? 17.752  44.651  86.132  1.00 14.85 ? 970  LEU B N     1 
ATOM   15964 C  CA    . LEU B 1  972  ? 16.992  43.594  85.481  1.00 14.65 ? 970  LEU B CA    1 
ATOM   15965 C  C     . LEU B 1  972  ? 15.903  43.090  86.422  1.00 12.61 ? 970  LEU B C     1 
ATOM   15966 O  O     . LEU B 1  972  ? 14.772  43.584  86.362  1.00 15.16 ? 970  LEU B O     1 
ATOM   15967 C  CB    . LEU B 1  972  ? 17.920  42.471  85.015  1.00 14.68 ? 970  LEU B CB    1 
ATOM   15968 C  CG    . LEU B 1  972  ? 17.299  41.387  84.132  1.00 15.04 ? 970  LEU B CG    1 
ATOM   15969 C  CD1   . LEU B 1  972  ? 16.496  41.966  82.962  1.00 14.90 ? 970  LEU B CD1   1 
ATOM   15970 C  CD2   . LEU B 1  972  ? 18.411  40.480  83.606  1.00 16.50 ? 970  LEU B CD2   1 
ATOM   15971 N  N     . THR B 1  973  ? 16.207  42.120  87.290  1.00 13.88 ? 971  THR B N     1 
ATOM   15972 C  CA    . THR B 1  973  ? 15.199  41.645  88.227  1.00 12.61 ? 971  THR B CA    1 
ATOM   15973 C  C     . THR B 1  973  ? 15.513  42.121  89.638  1.00 14.37 ? 971  THR B C     1 
ATOM   15974 O  O     . THR B 1  973  ? 16.655  42.446  89.983  1.00 15.23 ? 971  THR B O     1 
ATOM   15975 C  CB    . THR B 1  973  ? 15.082  40.116  88.215  1.00 13.30 ? 971  THR B CB    1 
ATOM   15976 O  OG1   . THR B 1  973  ? 16.338  39.537  88.573  1.00 13.98 ? 971  THR B OG1   1 
ATOM   15977 C  CG2   . THR B 1  973  ? 14.661  39.642  86.837  1.00 15.38 ? 971  THR B CG2   1 
ATOM   15978 N  N     . PHE B 1  974  ? 14.465  42.161  90.452  1.00 14.58 ? 972  PHE B N     1 
ATOM   15979 C  CA    . PHE B 1  974  ? 14.605  42.601  91.828  1.00 14.10 ? 972  PHE B CA    1 
ATOM   15980 C  C     . PHE B 1  974  ? 13.492  41.972  92.645  1.00 12.68 ? 972  PHE B C     1 
ATOM   15981 O  O     . PHE B 1  974  ? 12.340  41.964  92.214  1.00 13.67 ? 972  PHE B O     1 
ATOM   15982 C  CB    . PHE B 1  974  ? 14.530  44.125  91.954  1.00 13.97 ? 972  PHE B CB    1 
ATOM   15983 C  CG    . PHE B 1  974  ? 14.442  44.589  93.375  1.00 13.31 ? 972  PHE B CG    1 
ATOM   15984 C  CD1   . PHE B 1  974  ? 15.594  44.684  94.139  1.00 15.05 ? 972  PHE B CD1   1 
ATOM   15985 C  CD2   . PHE B 1  974  ? 13.224  44.877  93.955  1.00 14.23 ? 972  PHE B CD2   1 
ATOM   15986 C  CE1   . PHE B 1  974  ? 15.542  45.077  95.448  1.00 16.63 ? 972  PHE B CE1   1 
ATOM   15987 C  CE2   . PHE B 1  974  ? 13.155  45.275  95.293  1.00 14.20 ? 972  PHE B CE2   1 
ATOM   15988 C  CZ    . PHE B 1  974  ? 14.316  45.363  96.034  1.00 14.35 ? 972  PHE B CZ    1 
ATOM   15989 N  N     . GLY B 1  975  ? 13.829  41.482  93.833  1.00 13.08 ? 973  GLY B N     1 
ATOM   15990 C  CA    . GLY B 1  975  ? 12.849  40.874  94.715  1.00 15.51 ? 973  GLY B CA    1 
ATOM   15991 C  C     . GLY B 1  975  ? 12.757  41.577  96.055  1.00 15.39 ? 973  GLY B C     1 
ATOM   15992 O  O     . GLY B 1  975  ? 13.746  42.081  96.575  1.00 14.37 ? 973  GLY B O     1 
ATOM   15993 N  N     . LEU B 1  976  ? 11.554  41.578  96.621  1.00 13.72 ? 974  LEU B N     1 
ATOM   15994 C  CA    . LEU B 1  976  ? 11.332  42.127  97.952  1.00 13.75 ? 974  LEU B CA    1 
ATOM   15995 C  C     . LEU B 1  976  ? 10.447  41.158  98.717  1.00 15.30 ? 974  LEU B C     1 
ATOM   15996 O  O     . LEU B 1  976  ? 9.376   40.788  98.232  1.00 16.38 ? 974  LEU B O     1 
ATOM   15997 C  CB    . LEU B 1  976  ? 10.671  43.506  97.879  1.00 14.62 ? 974  LEU B CB    1 
ATOM   15998 C  CG    . LEU B 1  976  ? 10.232  44.111  99.218  1.00 16.60 ? 974  LEU B CG    1 
ATOM   15999 C  CD1   . LEU B 1  976  ? 11.435  44.443  100.125 1.00 17.94 ? 974  LEU B CD1   1 
ATOM   16000 C  CD2   . LEU B 1  976  ? 9.348   45.338  98.969  1.00 17.11 ? 974  LEU B CD2   1 
ATOM   16001 N  N     . HIS B 1  977  ? 10.903  40.731  99.892  1.00 14.29 ? 975  HIS B N     1 
ATOM   16002 C  CA    . HIS B 1  977  ? 10.110  39.898  100.789 1.00 16.15 ? 975  HIS B CA    1 
ATOM   16003 C  C     . HIS B 1  977  ? 9.810   40.724  102.027 1.00 15.59 ? 975  HIS B C     1 
ATOM   16004 O  O     . HIS B 1  977  ? 10.711  41.022  102.819 1.00 15.93 ? 975  HIS B O     1 
ATOM   16005 C  CB    . HIS B 1  977  ? 10.842  38.614  101.170 1.00 16.95 ? 975  HIS B CB    1 
ATOM   16006 C  CG    . HIS B 1  977  ? 10.444  37.422  100.363 1.00 17.21 ? 975  HIS B CG    1 
ATOM   16007 N  ND1   . HIS B 1  977  ? 9.568   36.469  100.831 1.00 22.87 ? 975  HIS B ND1   1 
ATOM   16008 C  CD2   . HIS B 1  977  ? 10.824  37.014  99.129  1.00 20.71 ? 975  HIS B CD2   1 
ATOM   16009 C  CE1   . HIS B 1  977  ? 9.421   35.525  99.919  1.00 21.11 ? 975  HIS B CE1   1 
ATOM   16010 N  NE2   . HIS B 1  977  ? 10.183  35.825  98.884  1.00 17.52 ? 975  HIS B NE2   1 
ATOM   16011 N  N     . THR B 1  978  ? 8.550   41.097  102.176 1.00 15.45 ? 976  THR B N     1 
ATOM   16012 C  CA    . THR B 1  978  ? 8.062   41.841  103.324 1.00 16.30 ? 976  THR B CA    1 
ATOM   16013 C  C     . THR B 1  978  ? 6.558   41.672  103.374 1.00 18.02 ? 976  THR B C     1 
ATOM   16014 O  O     . THR B 1  978  ? 5.909   41.449  102.350 1.00 18.41 ? 976  THR B O     1 
ATOM   16015 C  CB    . THR B 1  978  ? 8.408   43.329  103.244 1.00 16.26 ? 976  THR B CB    1 
ATOM   16016 O  OG1   . THR B 1  978  ? 7.871   43.997  104.390 1.00 15.59 ? 976  THR B OG1   1 
ATOM   16017 C  CG2   . THR B 1  978  ? 7.794   43.958  102.002 1.00 17.16 ? 976  THR B CG2   1 
ATOM   16018 N  N     . ARG B 1  979  ? 6.008   41.769  104.571 1.00 18.90 ? 977  ARG B N     1 
ATOM   16019 C  CA    . ARG B 1  979  ? 4.563   41.793  104.692 1.00 19.79 ? 977  ARG B CA    1 
ATOM   16020 C  C     . ARG B 1  979  ? 4.031   43.202  104.906 1.00 19.11 ? 977  ARG B C     1 
ATOM   16021 O  O     . ARG B 1  979  ? 2.826   43.370  105.110 1.00 19.35 ? 977  ARG B O     1 
ATOM   16022 C  CB    . ARG B 1  979  ? 4.122   40.852  105.813 1.00 22.18 ? 977  ARG B CB    1 
ATOM   16023 C  CG    . ARG B 1  979  ? 4.056   39.396  105.335 1.00 26.46 ? 977  ARG B CG    1 
ATOM   16024 C  CD    . ARG B 1  979  ? 3.606   38.461  106.439 1.00 32.79 ? 977  ARG B CD    1 
ATOM   16025 N  NE    . ARG B 1  979  ? 4.734   37.966  107.218 1.00 33.80 ? 977  ARG B NE    1 
ATOM   16026 C  CZ    . ARG B 1  979  ? 4.634   37.371  108.401 1.00 34.69 ? 977  ARG B CZ    1 
ATOM   16027 N  NH1   . ARG B 1  979  ? 3.465   37.229  109.011 1.00 32.85 ? 977  ARG B NH1   1 
ATOM   16028 N  NH2   . ARG B 1  979  ? 5.736   36.897  108.984 1.00 37.38 ? 977  ARG B NH2   1 
ATOM   16029 N  N     . LEU B 1  980  ? 4.888   44.218  104.821 1.00 17.57 ? 978  LEU B N     1 
ATOM   16030 C  CA    . LEU B 1  980  ? 4.555   45.567  105.270 1.00 15.38 ? 978  LEU B CA    1 
ATOM   16031 C  C     . LEU B 1  980  ? 4.357   46.487  104.073 1.00 16.22 ? 978  LEU B C     1 
ATOM   16032 O  O     . LEU B 1  980  ? 5.294   46.714  103.296 1.00 16.43 ? 978  LEU B O     1 
ATOM   16033 C  CB    . LEU B 1  980  ? 5.642   46.116  106.192 1.00 17.32 ? 978  LEU B CB    1 
ATOM   16034 C  CG    . LEU B 1  980  ? 5.982   45.183  107.351 1.00 18.55 ? 978  LEU B CG    1 
ATOM   16035 C  CD1   . LEU B 1  980  ? 7.134   45.763  108.142 1.00 20.43 ? 978  LEU B CD1   1 
ATOM   16036 C  CD2   . LEU B 1  980  ? 4.765   45.007  108.223 1.00 19.38 ? 978  LEU B CD2   1 
ATOM   16037 N  N     . ASP B 1  981  ? 3.142   47.031  103.942 1.00 17.63 ? 979  ASP B N     1 
ATOM   16038 C  CA    . ASP B 1  981  ? 2.822   47.855  102.780 1.00 17.50 ? 979  ASP B CA    1 
ATOM   16039 C  C     . ASP B 1  981  ? 3.724   49.073  102.673 1.00 17.39 ? 979  ASP B C     1 
ATOM   16040 O  O     . ASP B 1  981  ? 4.050   49.503  101.561 1.00 17.97 ? 979  ASP B O     1 
ATOM   16041 C  CB    . ASP B 1  981  ? 1.369   48.319  102.838 1.00 18.26 ? 979  ASP B CB    1 
ATOM   16042 C  CG    . ASP B 1  981  ? 0.394   47.226  102.503 1.00 21.81 ? 979  ASP B CG    1 
ATOM   16043 O  OD1   . ASP B 1  981  ? 0.820   46.213  101.924 1.00 21.19 ? 979  ASP B OD1   1 
ATOM   16044 O  OD2   . ASP B 1  981  ? -0.807  47.407  102.817 1.00 22.39 ? 979  ASP B OD2   1 
ATOM   16045 N  N     . GLU B 1  982  ? 4.091   49.681  103.808 1.00 17.62 ? 980  GLU B N     1 
ATOM   16046 C  CA    . GLU B 1  982  ? 4.962   50.849  103.738 1.00 18.08 ? 980  GLU B CA    1 
ATOM   16047 C  C     . GLU B 1  982  ? 6.296   50.482  103.117 1.00 17.49 ? 980  GLU B C     1 
ATOM   16048 O  O     . GLU B 1  982  ? 6.832   51.228  102.295 1.00 18.05 ? 980  GLU B O     1 
ATOM   16049 C  CB    . GLU B 1  982  ? 5.190   51.460  105.118 1.00 19.35 ? 980  GLU B CB    1 
ATOM   16050 C  CG    . GLU B 1  982  ? 6.170   52.618  105.060 1.00 22.14 ? 980  GLU B CG    1 
ATOM   16051 C  CD    . GLU B 1  982  ? 6.660   53.052  106.418 1.00 26.94 ? 980  GLU B CD    1 
ATOM   16052 O  OE1   . GLU B 1  982  ? 7.030   52.172  107.230 1.00 32.34 ? 980  GLU B OE1   1 
ATOM   16053 O  OE2   . GLU B 1  982  ? 6.669   54.271  106.673 1.00 24.72 ? 980  GLU B OE2   1 
ATOM   16054 N  N     . THR B 1  983  ? 6.832   49.317  103.484 1.00 14.98 ? 981  THR B N     1 
ATOM   16055 C  CA    . THR B 1  983  ? 8.107   48.881  102.924 1.00 16.00 ? 981  THR B CA    1 
ATOM   16056 C  C     . THR B 1  983  ? 7.969   48.572  101.439 1.00 15.34 ? 981  THR B C     1 
ATOM   16057 O  O     . THR B 1  983  ? 8.862   48.898  100.644 1.00 15.58 ? 981  THR B O     1 
ATOM   16058 C  CB    . THR B 1  983  ? 8.622   47.671  103.709 1.00 17.28 ? 981  THR B CB    1 
ATOM   16059 O  OG1   . THR B 1  983  ? 8.899   48.085  105.054 1.00 19.01 ? 981  THR B OG1   1 
ATOM   16060 C  CG2   . THR B 1  983  ? 9.896   47.098  103.080 1.00 17.19 ? 981  THR B CG2   1 
ATOM   16061 N  N     . ILE B 1  984  ? 6.839   47.979  101.038 1.00 14.09 ? 982  ILE B N     1 
ATOM   16062 C  CA    . ILE B 1  984  ? 6.606   47.724  99.618  1.00 15.95 ? 982  ILE B CA    1 
ATOM   16063 C  C     . ILE B 1  984  ? 6.577   49.032  98.840  1.00 16.07 ? 982  ILE B C     1 
ATOM   16064 O  O     . ILE B 1  984  ? 7.221   49.164  97.792  1.00 17.49 ? 982  ILE B O     1 
ATOM   16065 C  CB    . ILE B 1  984  ? 5.305   46.934  99.418  1.00 14.19 ? 982  ILE B CB    1 
ATOM   16066 C  CG1   . ILE B 1  984  ? 5.435   45.535  100.016 1.00 18.30 ? 982  ILE B CG1   1 
ATOM   16067 C  CG2   . ILE B 1  984  ? 4.962   46.853  97.928  1.00 17.65 ? 982  ILE B CG2   1 
ATOM   16068 C  CD1   . ILE B 1  984  ? 4.120   44.810  100.083 1.00 18.39 ? 982  ILE B CD1   1 
ATOM   16069 N  N     . ALA B 1  985  ? 5.834   50.019  99.341  1.00 16.02 ? 983  ALA B N     1 
ATOM   16070 C  CA    . ALA B 1  985  ? 5.726   51.297  98.636  1.00 18.19 ? 983  ALA B CA    1 
ATOM   16071 C  C     . ALA B 1  985  ? 7.081   51.984  98.550  1.00 17.43 ? 983  ALA B C     1 
ATOM   16072 O  O     . ALA B 1  985  ? 7.473   52.489  97.491  1.00 16.54 ? 983  ALA B O     1 
ATOM   16073 C  CB    . ALA B 1  985  ? 4.714   52.202  99.337  1.00 18.31 ? 983  ALA B CB    1 
ATOM   16074 N  N     . HIS B 1  986  ? 7.809   52.009  99.665  1.00 16.29 ? 984  HIS B N     1 
ATOM   16075 C  CA    . HIS B 1  986  ? 9.120   52.648  99.687  1.00 18.38 ? 984  HIS B CA    1 
ATOM   16076 C  C     . HIS B 1  986  ? 10.039  51.996  98.666  1.00 16.83 ? 984  HIS B C     1 
ATOM   16077 O  O     . HIS B 1  986  ? 10.565  52.659  97.763  1.00 18.66 ? 984  HIS B O     1 
ATOM   16078 C  CB    . HIS B 1  986  ? 9.704   52.550  101.098 1.00 15.54 ? 984  HIS B CB    1 
ATOM   16079 C  CG    . HIS B 1  986  ? 11.093  53.102  101.241 1.00 19.41 ? 984  HIS B CG    1 
ATOM   16080 N  ND1   . HIS B 1  986  ? 11.707  53.225  102.467 1.00 24.19 ? 984  HIS B ND1   1 
ATOM   16081 C  CD2   . HIS B 1  986  ? 11.989  53.546  100.328 1.00 22.07 ? 984  HIS B CD2   1 
ATOM   16082 C  CE1   . HIS B 1  986  ? 12.916  53.736  102.308 1.00 25.20 ? 984  HIS B CE1   1 
ATOM   16083 N  NE2   . HIS B 1  986  ? 13.116  53.935  101.018 1.00 22.03 ? 984  HIS B NE2   1 
ATOM   16084 N  N     . VAL B 1  987  ? 10.219  50.684  98.781  1.00 15.29 ? 985  VAL B N     1 
ATOM   16085 C  CA    . VAL B 1  987  ? 11.231  50.003  97.978  1.00 15.70 ? 985  VAL B CA    1 
ATOM   16086 C  C     . VAL B 1  987  ? 10.854  50.014  96.508  1.00 17.36 ? 985  VAL B C     1 
ATOM   16087 O  O     . VAL B 1  987  ? 11.701  50.281  95.648  1.00 17.31 ? 985  VAL B O     1 
ATOM   16088 C  CB    . VAL B 1  987  ? 11.447  48.577  98.502  1.00 16.46 ? 985  VAL B CB    1 
ATOM   16089 C  CG1   . VAL B 1  987  ? 12.290  47.770  97.513  1.00 18.29 ? 985  VAL B CG1   1 
ATOM   16090 C  CG2   . VAL B 1  987  ? 12.115  48.635  99.882  1.00 16.78 ? 985  VAL B CG2   1 
ATOM   16091 N  N     . THR B 1  988  ? 9.586   49.754  96.186  1.00 17.02 ? 986  THR B N     1 
ATOM   16092 C  CA    . THR B 1  988  ? 9.224   49.709  94.775  1.00 15.83 ? 986  THR B CA    1 
ATOM   16093 C  C     . THR B 1  988  ? 9.243   51.096  94.150  1.00 17.69 ? 986  THR B C     1 
ATOM   16094 O  O     . THR B 1  988  ? 9.456   51.216  92.940  1.00 23.12 ? 986  THR B O     1 
ATOM   16095 C  CB    . THR B 1  988  ? 7.855   49.046  94.564  1.00 18.74 ? 986  THR B CB    1 
ATOM   16096 O  OG1   . THR B 1  988  ? 6.835   49.778  95.238  1.00 21.32 ? 986  THR B OG1   1 
ATOM   16097 C  CG2   . THR B 1  988  ? 7.882   47.595  95.051  1.00 21.40 ? 986  THR B CG2   1 
ATOM   16098 N  N     . SER B 1  989  ? 9.059   52.151  94.942  1.00 18.17 ? 987  SER B N     1 
ATOM   16099 C  CA    . SER B 1  989  ? 9.153   53.500  94.391  1.00 20.05 ? 987  SER B CA    1 
ATOM   16100 C  C     . SER B 1  989  ? 10.592  53.945  94.144  1.00 23.52 ? 987  SER B C     1 
ATOM   16101 O  O     . SER B 1  989  ? 10.809  54.887  93.373  1.00 24.57 ? 987  SER B O     1 
ATOM   16102 C  CB    . SER B 1  989  ? 8.462   54.515  95.309  1.00 20.28 ? 987  SER B CB    1 
ATOM   16103 O  OG    . SER B 1  989  ? 9.190   54.735  96.499  1.00 26.86 ? 987  SER B OG    1 
ATOM   16104 N  N     . ARG B 1  990  ? 11.576  53.297  94.769  1.00 17.34 ? 988  ARG B N     1 
ATOM   16105 C  CA    . ARG B 1  990  ? 12.961  53.752  94.707  1.00 18.66 ? 988  ARG B CA    1 
ATOM   16106 C  C     . ARG B 1  990  ? 13.873  52.829  93.912  1.00 19.09 ? 988  ARG B C     1 
ATOM   16107 O  O     . ARG B 1  990  ? 14.891  53.292  93.387  1.00 19.72 ? 988  ARG B O     1 
ATOM   16108 C  CB    . ARG B 1  990  ? 13.530  53.907  96.122  1.00 20.45 ? 988  ARG B CB    1 
ATOM   16109 C  CG    . ARG B 1  990  ? 12.682  54.779  97.021  1.00 26.18 ? 988  ARG B CG    1 
ATOM   16110 C  CD    . ARG B 1  990  ? 12.929  56.236  96.760  1.00 25.27 ? 988  ARG B CD    1 
ATOM   16111 N  NE    . ARG B 1  990  ? 14.017  56.751  97.587  1.00 22.17 ? 988  ARG B NE    1 
ATOM   16112 C  CZ    . ARG B 1  990  ? 14.437  58.008  97.551  1.00 21.25 ? 988  ARG B CZ    1 
ATOM   16113 N  NH1   . ARG B 1  990  ? 13.895  58.891  96.729  1.00 25.29 ? 988  ARG B NH1   1 
ATOM   16114 N  NH2   . ARG B 1  990  ? 15.430  58.384  98.350  1.00 21.71 ? 988  ARG B NH2   1 
ATOM   16115 N  N     . ILE B 1  991  ? 13.539  51.539  93.819  1.00 17.22 ? 989  ILE B N     1 
ATOM   16116 C  CA    . ILE B 1  991  ? 14.332  50.613  93.024  1.00 17.12 ? 989  ILE B CA    1 
ATOM   16117 C  C     . ILE B 1  991  ? 14.169  50.952  91.548  1.00 18.02 ? 989  ILE B C     1 
ATOM   16118 O  O     . ILE B 1  991  ? 13.123  51.448  91.105  1.00 19.09 ? 989  ILE B O     1 
ATOM   16119 C  CB    . ILE B 1  991  ? 13.917  49.157  93.313  1.00 15.60 ? 989  ILE B CB    1 
ATOM   16120 C  CG1   . ILE B 1  991  ? 14.980  48.171  92.834  1.00 19.57 ? 989  ILE B CG1   1 
ATOM   16121 C  CG2   . ILE B 1  991  ? 12.569  48.837  92.673  1.00 19.32 ? 989  ILE B CG2   1 
ATOM   16122 C  CD1   . ILE B 1  991  ? 16.270  48.265  93.648  1.00 19.49 ? 989  ILE B CD1   1 
ATOM   16123 N  N     . LYS B 1  992  ? 15.221  50.716  90.780  1.00 16.38 ? 990  LYS B N     1 
ATOM   16124 C  CA    . LYS B 1  992  ? 15.207  50.991  89.343  1.00 17.84 ? 990  LYS B CA    1 
ATOM   16125 C  C     . LYS B 1  992  ? 15.522  49.694  88.611  1.00 17.74 ? 990  LYS B C     1 
ATOM   16126 O  O     . LYS B 1  992  ? 16.660  49.450  88.204  1.00 17.84 ? 990  LYS B O     1 
ATOM   16127 C  CB    . LYS B 1  992  ? 16.187  52.074  89.018  1.00 17.42 ? 990  LYS B CB    1 
ATOM   16128 C  CG    . LYS B 1  992  ? 15.808  53.410  89.642  1.00 20.03 ? 990  LYS B CG    1 
ATOM   16129 C  CD    . LYS B 1  992  ? 16.903  54.439  89.382  1.00 25.27 ? 990  LYS B CD    1 
ATOM   16130 C  CE    . LYS B 1  992  ? 17.186  54.581  87.890  1.00 31.51 ? 990  LYS B CE    1 
ATOM   16131 N  NZ    . LYS B 1  992  ? 18.391  55.434  87.632  1.00 34.66 ? 990  LYS B NZ    1 
ATOM   16132 N  N     . ALA B 1  993  ? 14.506  48.854  88.444  1.00 16.61 ? 991  ALA B N     1 
ATOM   16133 C  CA    . ALA B 1  993  ? 14.676  47.586  87.752  1.00 14.06 ? 991  ALA B CA    1 
ATOM   16134 C  C     . ALA B 1  993  ? 13.436  47.296  86.924  1.00 15.02 ? 991  ALA B C     1 
ATOM   16135 O  O     . ALA B 1  993  ? 12.332  47.749  87.251  1.00 15.14 ? 991  ALA B O     1 
ATOM   16136 C  CB    . ALA B 1  993  ? 14.931  46.429  88.723  1.00 16.39 ? 991  ALA B CB    1 
ATOM   16137 N  N     . GLY B 1  994  ? 13.625  46.519  85.852  1.00 14.36 ? 992  GLY B N     1 
ATOM   16138 C  CA    . GLY B 1  994  ? 12.523  46.297  84.929  1.00 14.61 ? 992  GLY B CA    1 
ATOM   16139 C  C     . GLY B 1  994  ? 11.528  45.244  85.364  1.00 13.71 ? 992  GLY B C     1 
ATOM   16140 O  O     . GLY B 1  994  ? 10.384  45.267  84.906  1.00 12.57 ? 992  GLY B O     1 
ATOM   16141 N  N     . ASN B 1  995  ? 11.937  44.312  86.211  1.00 13.53 ? 993  ASN B N     1 
ATOM   16142 C  CA    . ASN B 1  995  ? 11.081  43.219  86.667  1.00 13.94 ? 993  ASN B CA    1 
ATOM   16143 C  C     . ASN B 1  995  ? 11.191  43.128  88.178  1.00 12.72 ? 993  ASN B C     1 
ATOM   16144 O  O     . ASN B 1  995  ? 12.257  42.775  88.703  1.00 13.37 ? 993  ASN B O     1 
ATOM   16145 C  CB    . ASN B 1  995  ? 11.473  41.893  86.011  1.00 13.51 ? 993  ASN B CB    1 
ATOM   16146 C  CG    . ASN B 1  995  ? 10.923  41.774  84.602  1.00 12.98 ? 993  ASN B CG    1 
ATOM   16147 O  OD1   . ASN B 1  995  ? 11.533  42.245  83.647  1.00 12.06 ? 993  ASN B OD1   1 
ATOM   16148 N  ND2   . ASN B 1  995  ? 9.740   41.186  84.479  1.00 14.51 ? 993  ASN B ND2   1 
ATOM   16149 N  N     . LEU B 1  996  ? 10.097  43.449  88.861  1.00 14.17 ? 994  LEU B N     1 
ATOM   16150 C  CA    . LEU B 1  996  ? 10.015  43.437  90.312  1.00 13.50 ? 994  LEU B CA    1 
ATOM   16151 C  C     . LEU B 1  996  ? 9.162   42.259  90.734  1.00 15.00 ? 994  LEU B C     1 
ATOM   16152 O  O     . LEU B 1  996  ? 8.212   41.890  90.042  1.00 13.46 ? 994  LEU B O     1 
ATOM   16153 C  CB    . LEU B 1  996  ? 9.395   44.720  90.851  1.00 14.20 ? 994  LEU B CB    1 
ATOM   16154 C  CG    . LEU B 1  996  ? 9.924   46.014  90.248  1.00 14.66 ? 994  LEU B CG    1 
ATOM   16155 C  CD1   . LEU B 1  996  ? 9.149   47.198  90.879  1.00 15.68 ? 994  LEU B CD1   1 
ATOM   16156 C  CD2   . LEU B 1  996  ? 11.427  46.129  90.459  1.00 14.01 ? 994  LEU B CD2   1 
ATOM   16157 N  N     . TYR B 1  997  ? 9.513   41.670  91.875  1.00 15.18 ? 995  TYR B N     1 
ATOM   16158 C  CA    . TYR B 1  997  ? 8.801   40.506  92.379  1.00 16.55 ? 995  TYR B CA    1 
ATOM   16159 C  C     . TYR B 1  997  ? 8.640   40.657  93.874  1.00 14.59 ? 995  TYR B C     1 
ATOM   16160 O  O     . TYR B 1  997  ? 9.627   40.869  94.586  1.00 15.43 ? 995  TYR B O     1 
ATOM   16161 C  CB    . TYR B 1  997  ? 9.550   39.208  92.069  1.00 14.05 ? 995  TYR B CB    1 
ATOM   16162 C  CG    . TYR B 1  997  ? 9.906   39.045  90.619  1.00 13.33 ? 995  TYR B CG    1 
ATOM   16163 C  CD1   . TYR B 1  997  ? 11.064  39.615  90.111  1.00 14.67 ? 995  TYR B CD1   1 
ATOM   16164 C  CD2   . TYR B 1  997  ? 9.090   38.323  89.754  1.00 17.29 ? 995  TYR B CD2   1 
ATOM   16165 C  CE1   . TYR B 1  997  ? 11.410  39.475  88.789  1.00 18.44 ? 995  TYR B CE1   1 
ATOM   16166 C  CE2   . TYR B 1  997  ? 9.441   38.171  88.412  1.00 16.63 ? 995  TYR B CE2   1 
ATOM   16167 C  CZ    . TYR B 1  997  ? 10.606  38.755  87.951  1.00 17.32 ? 995  TYR B CZ    1 
ATOM   16168 O  OH    . TYR B 1  997  ? 10.984  38.643  86.632  1.00 21.12 ? 995  TYR B OH    1 
ATOM   16169 N  N     . ILE B 1  998  ? 7.405   40.540  94.346  1.00 14.61 ? 996  ILE B N     1 
ATOM   16170 C  CA    . ILE B 1  998  ? 7.088   40.772  95.751  1.00 13.64 ? 996  ILE B CA    1 
ATOM   16171 C  C     . ILE B 1  998  ? 6.655   39.444  96.366  1.00 15.53 ? 996  ILE B C     1 
ATOM   16172 O  O     . ILE B 1  998  ? 5.647   38.862  95.950  1.00 15.04 ? 996  ILE B O     1 
ATOM   16173 C  CB    . ILE B 1  998  ? 5.982   41.822  95.922  1.00 17.20 ? 996  ILE B CB    1 
ATOM   16174 C  CG1   . ILE B 1  998  ? 6.347   43.155  95.241  1.00 18.47 ? 996  ILE B CG1   1 
ATOM   16175 C  CG2   . ILE B 1  998  ? 5.655   41.995  97.395  1.00 17.04 ? 996  ILE B CG2   1 
ATOM   16176 C  CD1   . ILE B 1  998  ? 7.613   43.787  95.731  1.00 20.23 ? 996  ILE B CD1   1 
ATOM   16177 N  N     . ASN B 1  999  ? 7.424   38.963  97.344  1.00 14.11 ? 997  ASN B N     1 
ATOM   16178 C  CA    . ASN B 1  999  ? 7.054   37.767  98.112  1.00 14.79 ? 997  ASN B CA    1 
ATOM   16179 C  C     . ASN B 1  999  ? 6.996   36.510  97.244  1.00 15.13 ? 997  ASN B C     1 
ATOM   16180 O  O     . ASN B 1  999  ? 6.169   35.619  97.462  1.00 15.79 ? 997  ASN B O     1 
ATOM   16181 C  CB    . ASN B 1  999  ? 5.734   37.981  98.856  1.00 16.73 ? 997  ASN B CB    1 
ATOM   16182 C  CG    . ASN B 1  999  ? 5.868   39.008  99.949  1.00 15.83 ? 997  ASN B CG    1 
ATOM   16183 O  OD1   . ASN B 1  999  ? 6.940   39.131  100.547 1.00 16.28 ? 997  ASN B OD1   1 
ATOM   16184 N  ND2   . ASN B 1  999  ? 4.785   39.736  100.242 1.00 15.40 ? 997  ASN B ND2   1 
ATOM   16185 N  N     . ARG B 1  1000 ? 7.908   36.423  96.281  1.00 14.59 ? 998  ARG B N     1 
ATOM   16186 C  CA    . ARG B 1  1000 ? 8.036   35.255  95.415  1.00 13.43 ? 998  ARG B CA    1 
ATOM   16187 C  C     . ARG B 1  1000 ? 9.467   35.224  94.886  1.00 14.49 ? 998  ARG B C     1 
ATOM   16188 O  O     . ARG B 1  1000 ? 10.277  36.097  95.201  1.00 16.39 ? 998  ARG B O     1 
ATOM   16189 C  CB    . ARG B 1  1000 ? 7.023   35.298  94.266  1.00 13.73 ? 998  ARG B CB    1 
ATOM   16190 C  CG    . ARG B 1  1000 ? 7.021   36.638  93.546  1.00 14.83 ? 998  ARG B CG    1 
ATOM   16191 C  CD    . ARG B 1  1000 ? 6.535   36.516  92.106  1.00 16.19 ? 998  ARG B CD    1 
ATOM   16192 N  NE    . ARG B 1  1000 ? 7.453   35.704  91.316  1.00 13.08 ? 998  ARG B NE    1 
ATOM   16193 C  CZ    . ARG B 1  1000 ? 7.184   35.266  90.094  1.00 15.67 ? 998  ARG B CZ    1 
ATOM   16194 N  NH1   . ARG B 1  1000 ? 6.068   35.603  89.476  1.00 14.78 ? 998  ARG B NH1   1 
ATOM   16195 N  NH2   . ARG B 1  1000 ? 8.053   34.465  89.480  1.00 16.79 ? 998  ARG B NH2   1 
ATOM   16196 N  N     . ASN B 1  1001 ? 9.770   34.216  94.066  1.00 13.20 ? 999  ASN B N     1 
ATOM   16197 C  CA    . ASN B 1  1001 ? 11.092  34.173  93.453  1.00 15.33 ? 999  ASN B CA    1 
ATOM   16198 C  C     . ASN B 1  1001 ? 11.201  35.283  92.408  1.00 15.27 ? 999  ASN B C     1 
ATOM   16199 O  O     . ASN B 1  1001 ? 10.208  35.925  92.059  1.00 14.81 ? 999  ASN B O     1 
ATOM   16200 C  CB    . ASN B 1  1001 ? 11.357  32.788  92.851  1.00 14.91 ? 999  ASN B CB    1 
ATOM   16201 C  CG    . ASN B 1  1001 ? 10.481  32.483  91.638  1.00 17.64 ? 999  ASN B CG    1 
ATOM   16202 O  OD1   . ASN B 1  1001 ? 10.376  33.275  90.705  1.00 18.37 ? 999  ASN B OD1   1 
ATOM   16203 N  ND2   . ASN B 1  1001 ? 9.844   31.323  91.657  1.00 25.23 ? 999  ASN B ND2   1 
ATOM   16204 N  N     . ILE B 1  1002 ? 12.415  35.525  91.912  1.00 14.63 ? 1000 ILE B N     1 
ATOM   16205 C  CA    . ILE B 1  1002 ? 12.638  36.642  90.994  1.00 13.25 ? 1000 ILE B CA    1 
ATOM   16206 C  C     . ILE B 1  1002 ? 12.970  36.166  89.582  1.00 16.39 ? 1000 ILE B C     1 
ATOM   16207 O  O     . ILE B 1  1002 ? 13.592  36.905  88.817  1.00 17.25 ? 1000 ILE B O     1 
ATOM   16208 C  CB    . ILE B 1  1002 ? 13.723  37.602  91.512  1.00 16.07 ? 1000 ILE B CB    1 
ATOM   16209 C  CG1   . ILE B 1  1002 ? 15.101  36.934  91.558  1.00 14.08 ? 1000 ILE B CG1   1 
ATOM   16210 C  CG2   . ILE B 1  1002 ? 13.325  38.141  92.871  1.00 15.15 ? 1000 ILE B CG2   1 
ATOM   16211 C  CD1   . ILE B 1  1002 ? 16.249  37.943  91.687  1.00 14.41 ? 1000 ILE B CD1   1 
ATOM   16212 N  N     . ILE B 1  1003 ? 12.567  34.956  89.207  1.00 16.75 ? 1001 ILE B N     1 
ATOM   16213 C  CA    . ILE B 1  1003 ? 12.939  34.447  87.893  1.00 17.95 ? 1001 ILE B CA    1 
ATOM   16214 C  C     . ILE B 1  1003 ? 11.728  34.323  86.974  1.00 22.56 ? 1001 ILE B C     1 
ATOM   16215 O  O     . ILE B 1  1003 ? 11.829  33.726  85.894  1.00 23.26 ? 1001 ILE B O     1 
ATOM   16216 C  CB    . ILE B 1  1003 ? 13.723  33.129  88.005  1.00 18.48 ? 1001 ILE B CB    1 
ATOM   16217 C  CG1   . ILE B 1  1003 ? 12.947  32.061  88.758  1.00 21.56 ? 1001 ILE B CG1   1 
ATOM   16218 C  CG2   . ILE B 1  1003 ? 15.048  33.370  88.737  1.00 17.31 ? 1001 ILE B CG2   1 
ATOM   16219 C  CD1   . ILE B 1  1003 ? 13.690  30.724  88.753  1.00 26.44 ? 1001 ILE B CD1   1 
ATOM   16220 N  N     . GLY B 1  1004 ? 10.601  34.924  87.353  1.00 19.18 ? 1002 GLY B N     1 
ATOM   16221 C  CA    . GLY B 1  1004 ? 9.416   34.896  86.506  1.00 20.84 ? 1002 GLY B CA    1 
ATOM   16222 C  C     . GLY B 1  1004 ? 9.586   35.730  85.245  1.00 23.06 ? 1002 GLY B C     1 
ATOM   16223 O  O     . GLY B 1  1004 ? 9.897   36.926  85.302  1.00 22.95 ? 1002 GLY B O     1 
ATOM   16224 N  N     . ALA B 1  1005 ? 9.356   35.104  84.100  1.00 18.36 ? 1003 ALA B N     1 
ATOM   16225 C  CA    . ALA B 1  1005 ? 9.337   35.813  82.834  1.00 19.61 ? 1003 ALA B CA    1 
ATOM   16226 C  C     . ALA B 1  1005 ? 8.188   35.317  81.988  1.00 19.28 ? 1003 ALA B C     1 
ATOM   16227 O  O     . ALA B 1  1005 ? 8.314   35.176  80.765  1.00 19.03 ? 1003 ALA B O     1 
ATOM   16228 C  CB    . ALA B 1  1005 ? 10.660  35.655  82.086  1.00 20.27 ? 1003 ALA B CB    1 
ATOM   16229 N  N     . VAL B 1  1006 ? 7.031   35.073  82.614  1.00 14.72 ? 1004 VAL B N     1 
ATOM   16230 C  CA    . VAL B 1  1006 ? 5.932   34.499  81.848  1.00 16.35 ? 1004 VAL B CA    1 
ATOM   16231 C  C     . VAL B 1  1006 ? 5.523   35.497  80.778  1.00 15.60 ? 1004 VAL B C     1 
ATOM   16232 O  O     . VAL B 1  1006 ? 5.222   36.661  81.067  1.00 14.47 ? 1004 VAL B O     1 
ATOM   16233 C  CB    . VAL B 1  1006 ? 4.761   34.117  82.758  1.00 14.90 ? 1004 VAL B CB    1 
ATOM   16234 C  CG1   . VAL B 1  1006 ? 3.576   33.627  81.908  1.00 17.41 ? 1004 VAL B CG1   1 
ATOM   16235 C  CG2   . VAL B 1  1006 ? 5.186   33.024  83.733  1.00 16.29 ? 1004 VAL B CG2   1 
ATOM   16236 N  N     . VAL B 1  1007 ? 5.535   35.042  79.528  1.00 14.47 ? 1005 VAL B N     1 
ATOM   16237 C  CA    . VAL B 1  1007 ? 5.265   35.909  78.389  1.00 15.00 ? 1005 VAL B CA    1 
ATOM   16238 C  C     . VAL B 1  1007 ? 3.898   36.572  78.540  1.00 14.11 ? 1005 VAL B C     1 
ATOM   16239 O  O     . VAL B 1  1007 ? 2.895   35.916  78.850  1.00 16.07 ? 1005 VAL B O     1 
ATOM   16240 C  CB    . VAL B 1  1007 ? 5.365   35.077  77.103  1.00 14.26 ? 1005 VAL B CB    1 
ATOM   16241 C  CG1   . VAL B 1  1007 ? 5.024   35.921  75.927  1.00 16.40 ? 1005 VAL B CG1   1 
ATOM   16242 C  CG2   . VAL B 1  1007 ? 6.771   34.520  76.953  1.00 14.43 ? 1005 VAL B CG2   1 
ATOM   16243 N  N     . GLY B 1  1008 ? 3.852   37.891  78.332  1.00 13.76 ? 1006 GLY B N     1 
ATOM   16244 C  CA    . GLY B 1  1008 ? 2.605   38.634  78.416  1.00 16.46 ? 1006 GLY B CA    1 
ATOM   16245 C  C     . GLY B 1  1008 ? 2.024   38.753  79.809  1.00 17.22 ? 1006 GLY B C     1 
ATOM   16246 O  O     . GLY B 1  1008 ? 0.932   39.331  79.974  1.00 18.69 ? 1006 GLY B O     1 
ATOM   16247 N  N     . VAL B 1  1009 ? 2.706   38.212  80.810  1.00 15.67 ? 1007 VAL B N     1 
ATOM   16248 C  CA    . VAL B 1  1009 ? 2.291   38.292  82.204  1.00 14.61 ? 1007 VAL B CA    1 
ATOM   16249 C  C     . VAL B 1  1009 ? 3.333   39.025  83.036  1.00 15.52 ? 1007 VAL B C     1 
ATOM   16250 O  O     . VAL B 1  1009 ? 3.016   39.970  83.759  1.00 14.99 ? 1007 VAL B O     1 
ATOM   16251 C  CB    . VAL B 1  1009 ? 2.022   36.890  82.783  1.00 14.64 ? 1007 VAL B CB    1 
ATOM   16252 C  CG1   . VAL B 1  1009 ? 1.504   36.986  84.231  1.00 15.39 ? 1007 VAL B CG1   1 
ATOM   16253 C  CG2   . VAL B 1  1009 ? 1.012   36.164  81.887  1.00 16.65 ? 1007 VAL B CG2   1 
ATOM   16254 N  N     . GLN B 1  1010 ? 4.592   38.607  82.932  1.00 14.23 ? 1008 GLN B N     1 
ATOM   16255 C  CA    . GLN B 1  1010 ? 5.730   39.437  83.326  1.00 13.78 ? 1008 GLN B CA    1 
ATOM   16256 C  C     . GLN B 1  1010 ? 6.560   39.739  82.083  1.00 13.93 ? 1008 GLN B C     1 
ATOM   16257 O  O     . GLN B 1  1010 ? 7.593   39.097  81.852  1.00 16.53 ? 1008 GLN B O     1 
ATOM   16258 C  CB    . GLN B 1  1010 ? 6.611   38.778  84.390  1.00 15.29 ? 1008 GLN B CB    1 
ATOM   16259 C  CG    . GLN B 1  1010 ? 5.897   38.440  85.680  1.00 16.03 ? 1008 GLN B CG    1 
ATOM   16260 C  CD    . GLN B 1  1010 ? 5.456   36.991  85.723  1.00 16.55 ? 1008 GLN B CD    1 
ATOM   16261 O  OE1   . GLN B 1  1010 ? 6.134   36.111  85.194  1.00 16.98 ? 1008 GLN B OE1   1 
ATOM   16262 N  NE2   . GLN B 1  1010 ? 4.313   36.737  86.359  1.00 14.31 ? 1008 GLN B NE2   1 
ATOM   16263 N  N     . PRO B 1  1011 ? 6.139   40.703  81.259  1.00 13.44 ? 1009 PRO B N     1 
ATOM   16264 C  CA    . PRO B 1  1011 ? 7.013   41.184  80.183  1.00 13.13 ? 1009 PRO B CA    1 
ATOM   16265 C  C     . PRO B 1  1011 ? 8.393   41.428  80.766  1.00 13.69 ? 1009 PRO B C     1 
ATOM   16266 O  O     . PRO B 1  1011 ? 8.537   42.053  81.820  1.00 14.18 ? 1009 PRO B O     1 
ATOM   16267 C  CB    . PRO B 1  1011 ? 6.340   42.488  79.736  1.00 14.12 ? 1009 PRO B CB    1 
ATOM   16268 C  CG    . PRO B 1  1011 ? 4.882   42.235  80.006  1.00 14.49 ? 1009 PRO B CG    1 
ATOM   16269 C  CD    . PRO B 1  1011 ? 4.897   41.484  81.345  1.00 14.77 ? 1009 PRO B CD    1 
ATOM   16270 N  N     . PHE B 1  1012 ? 9.405   40.872  80.122  1.00 13.71 ? 1010 PHE B N     1 
ATOM   16271 C  CA    . PHE B 1  1012 ? 10.699  40.713  80.760  1.00 12.53 ? 1010 PHE B CA    1 
ATOM   16272 C  C     . PHE B 1  1012 ? 11.757  41.578  80.084  1.00 15.08 ? 1010 PHE B C     1 
ATOM   16273 O  O     . PHE B 1  1012 ? 11.890  41.578  78.856  1.00 14.80 ? 1010 PHE B O     1 
ATOM   16274 C  CB    . PHE B 1  1012 ? 11.131  39.249  80.751  1.00 12.36 ? 1010 PHE B CB    1 
ATOM   16275 C  CG    . PHE B 1  1012 ? 12.377  39.016  81.532  1.00 13.11 ? 1010 PHE B CG    1 
ATOM   16276 C  CD1   . PHE B 1  1012 ? 12.320  38.855  82.908  1.00 16.28 ? 1010 PHE B CD1   1 
ATOM   16277 C  CD2   . PHE B 1  1012 ? 13.609  38.994  80.900  1.00 15.20 ? 1010 PHE B CD2   1 
ATOM   16278 C  CE1   . PHE B 1  1012 ? 13.490  38.656  83.647  1.00 15.09 ? 1010 PHE B CE1   1 
ATOM   16279 C  CE2   . PHE B 1  1012 ? 14.789  38.798  81.631  1.00 17.96 ? 1010 PHE B CE2   1 
ATOM   16280 C  CZ    . PHE B 1  1012 ? 14.727  38.630  83.006  1.00 15.63 ? 1010 PHE B CZ    1 
ATOM   16281 N  N     . GLY B 1  1013 ? 12.521  42.288  80.890  1.00 13.56 ? 1011 GLY B N     1 
ATOM   16282 C  CA    . GLY B 1  1013 ? 13.633  43.073  80.390  1.00 14.45 ? 1011 GLY B CA    1 
ATOM   16283 C  C     . GLY B 1  1013 ? 13.862  44.253  81.302  1.00 14.92 ? 1011 GLY B C     1 
ATOM   16284 O  O     . GLY B 1  1013 ? 12.951  44.753  81.959  1.00 13.70 ? 1011 GLY B O     1 
ATOM   16285 N  N     . GLY B 1  1014 ? 15.115  44.697  81.342  1.00 14.96 ? 1012 GLY B N     1 
ATOM   16286 C  CA    . GLY B 1  1014 ? 15.512  45.759  82.238  1.00 16.18 ? 1012 GLY B CA    1 
ATOM   16287 C  C     . GLY B 1  1014 ? 16.089  46.996  81.591  1.00 17.26 ? 1012 GLY B C     1 
ATOM   16288 O  O     . GLY B 1  1014 ? 16.018  47.180  80.376  1.00 17.42 ? 1012 GLY B O     1 
ATOM   16289 N  N     . ARG B 1  1015 ? 16.683  47.842  82.423  1.00 14.84 ? 1013 ARG B N     1 
ATOM   16290 C  CA    . ARG B 1  1015 ? 17.178  49.157  82.063  1.00 17.07 ? 1013 ARG B CA    1 
ATOM   16291 C  C     . ARG B 1  1015 ? 18.650  49.258  82.419  1.00 16.93 ? 1013 ARG B C     1 
ATOM   16292 O  O     . ARG B 1  1015 ? 19.238  48.339  82.986  1.00 15.42 ? 1013 ARG B O     1 
ATOM   16293 C  CB    . ARG B 1  1015 ? 16.391  50.251  82.794  1.00 16.74 ? 1013 ARG B CB    1 
ATOM   16294 C  CG    . ARG B 1  1015 ? 16.411  50.110  84.327  1.00 18.71 ? 1013 ARG B CG    1 
ATOM   16295 C  CD    . ARG B 1  1015 ? 16.319  51.467  85.045  1.00 21.02 ? 1013 ARG B CD    1 
ATOM   16296 N  NE    . ARG B 1  1015 ? 17.622  52.137  85.060  1.00 24.95 ? 1013 ARG B NE    1 
ATOM   16297 C  CZ    . ARG B 1  1015 ? 18.642  51.786  85.836  1.00 24.46 ? 1013 ARG B CZ    1 
ATOM   16298 N  NH1   . ARG B 1  1015 ? 18.543  50.799  86.716  1.00 20.32 ? 1013 ARG B NH1   1 
ATOM   16299 N  NH2   . ARG B 1  1015 ? 19.802  52.427  85.711  1.00 24.22 ? 1013 ARG B NH2   1 
ATOM   16300 N  N     . GLY B 1  1016 ? 19.236  50.410  82.115  1.00 16.62 ? 1014 GLY B N     1 
ATOM   16301 C  CA    . GLY B 1  1016 ? 20.634  50.585  82.454  1.00 16.23 ? 1014 GLY B CA    1 
ATOM   16302 C  C     . GLY B 1  1016 ? 21.500  49.604  81.692  1.00 16.83 ? 1014 GLY B C     1 
ATOM   16303 O  O     . GLY B 1  1016 ? 21.285  49.343  80.501  1.00 17.20 ? 1014 GLY B O     1 
ATOM   16304 N  N     . LEU B 1  1017 ? 22.465  49.014  82.400  1.00 16.54 ? 1015 LEU B N     1 
ATOM   16305 C  CA    . LEU B 1  1017 ? 23.328  47.995  81.820  1.00 16.28 ? 1015 LEU B CA    1 
ATOM   16306 C  C     . LEU B 1  1017 ? 22.589  46.712  81.472  1.00 15.76 ? 1015 LEU B C     1 
ATOM   16307 O  O     . LEU B 1  1017 ? 23.200  45.819  80.877  1.00 16.74 ? 1015 LEU B O     1 
ATOM   16308 C  CB    . LEU B 1  1017 ? 24.473  47.667  82.784  1.00 17.56 ? 1015 LEU B CB    1 
ATOM   16309 C  CG    . LEU B 1  1017 ? 25.396  48.857  83.038  1.00 19.20 ? 1015 LEU B CG    1 
ATOM   16310 C  CD1   . LEU B 1  1017 ? 26.419  48.504  84.110  1.00 20.32 ? 1015 LEU B CD1   1 
ATOM   16311 C  CD2   . LEU B 1  1017 ? 26.095  49.268  81.745  1.00 20.10 ? 1015 LEU B CD2   1 
ATOM   16312 N  N     . SER B 1  1018 ? 21.302  46.601  81.828  1.00 14.33 ? 1016 SER B N     1 
ATOM   16313 C  CA    . SER B 1  1018 ? 20.529  45.395  81.609  1.00 15.02 ? 1016 SER B CA    1 
ATOM   16314 C  C     . SER B 1  1018 ? 19.729  45.403  80.314  1.00 13.17 ? 1016 SER B C     1 
ATOM   16315 O  O     . SER B 1  1018 ? 19.225  44.352  79.925  1.00 15.45 ? 1016 SER B O     1 
ATOM   16316 C  CB    . SER B 1  1018 ? 19.565  45.167  82.784  1.00 15.08 ? 1016 SER B CB    1 
ATOM   16317 O  OG    . SER B 1  1018 ? 20.315  44.985  83.975  1.00 16.25 ? 1016 SER B OG    1 
ATOM   16318 N  N     . GLY B 1  1019 ? 19.577  46.536  79.646  1.00 14.03 ? 1017 GLY B N     1 
ATOM   16319 C  CA    . GLY B 1  1019 ? 18.810  46.457  78.422  1.00 15.46 ? 1017 GLY B CA    1 
ATOM   16320 C  C     . GLY B 1  1019 ? 18.541  47.779  77.747  1.00 15.38 ? 1017 GLY B C     1 
ATOM   16321 O  O     . GLY B 1  1019 ? 18.560  48.836  78.381  1.00 16.45 ? 1017 GLY B O     1 
ATOM   16322 N  N     . THR B 1  1020 ? 18.274  47.711  76.443  1.00 15.35 ? 1018 THR B N     1 
ATOM   16323 C  CA    . THR B 1  1020 ? 17.727  48.826  75.690  1.00 15.24 ? 1018 THR B CA    1 
ATOM   16324 C  C     . THR B 1  1020 ? 16.215  48.850  75.749  1.00 14.97 ? 1018 THR B C     1 
ATOM   16325 O  O     . THR B 1  1020 ? 15.606  49.911  75.581  1.00 16.50 ? 1018 THR B O     1 
ATOM   16326 C  CB    . THR B 1  1020 ? 18.135  48.720  74.220  1.00 15.32 ? 1018 THR B CB    1 
ATOM   16327 O  OG1   . THR B 1  1020 ? 17.684  47.457  73.707  1.00 14.81 ? 1018 THR B OG1   1 
ATOM   16328 C  CG2   . THR B 1  1020 ? 19.662  48.792  74.078  1.00 16.29 ? 1018 THR B CG2   1 
ATOM   16329 N  N     . GLY B 1  1021 ? 15.607  47.694  75.954  1.00 14.86 ? 1019 GLY B N     1 
ATOM   16330 C  CA    . GLY B 1  1021 ? 14.203  47.541  75.680  1.00 15.22 ? 1019 GLY B CA    1 
ATOM   16331 C  C     . GLY B 1  1021 ? 13.987  47.559  74.181  1.00 13.93 ? 1019 GLY B C     1 
ATOM   16332 O  O     . GLY B 1  1021 ? 14.937  47.687  73.397  1.00 14.22 ? 1019 GLY B O     1 
ATOM   16333 N  N     . PRO B 1  1022 ? 12.735  47.422  73.748  1.00 13.93 ? 1020 PRO B N     1 
ATOM   16334 C  CA    . PRO B 1  1022 ? 11.543  47.162  74.563  1.00 12.98 ? 1020 PRO B CA    1 
ATOM   16335 C  C     . PRO B 1  1022 ? 11.573  45.735  75.125  1.00 14.94 ? 1020 PRO B C     1 
ATOM   16336 O  O     . PRO B 1  1022 ? 12.348  44.886  74.678  1.00 15.59 ? 1020 PRO B O     1 
ATOM   16337 C  CB    . PRO B 1  1022 ? 10.395  47.375  73.561  1.00 14.76 ? 1020 PRO B CB    1 
ATOM   16338 C  CG    . PRO B 1  1022 ? 10.988  46.957  72.241  1.00 14.39 ? 1020 PRO B CG    1 
ATOM   16339 C  CD    . PRO B 1  1022 ? 12.408  47.498  72.310  1.00 14.97 ? 1020 PRO B CD    1 
ATOM   16340 N  N     . LYS B 1  1023 ? 10.720  45.449  76.106  1.00 14.62 ? 1021 LYS B N     1 
ATOM   16341 C  CA    . LYS B 1  1023 ? 10.716  44.135  76.741  1.00 14.26 ? 1021 LYS B CA    1 
ATOM   16342 C  C     . LYS B 1  1023 ? 10.271  43.042  75.783  1.00 13.69 ? 1021 LYS B C     1 
ATOM   16343 O  O     . LYS B 1  1023 ? 9.224   43.159  75.133  1.00 13.58 ? 1021 LYS B O     1 
ATOM   16344 C  CB    . LYS B 1  1023 ? 9.773   44.131  77.937  1.00 12.23 ? 1021 LYS B CB    1 
ATOM   16345 C  CG    . LYS B 1  1023 ? 10.222  44.947  79.144  1.00 12.86 ? 1021 LYS B CG    1 
ATOM   16346 C  CD    . LYS B 1  1023 ? 9.069   44.957  80.138  1.00 11.97 ? 1021 LYS B CD    1 
ATOM   16347 C  CE    . LYS B 1  1023 ? 9.481   45.419  81.541  1.00 13.70 ? 1021 LYS B CE    1 
ATOM   16348 N  NZ    . LYS B 1  1023 ? 10.272  44.367  82.258  1.00 12.66 ? 1021 LYS B NZ    1 
ATOM   16349 N  N     . ALA B 1  1024 ? 11.045  41.960  75.734  1.00 15.09 ? 1022 ALA B N     1 
ATOM   16350 C  CA    . ALA B 1  1024 ? 10.540  40.707  75.187  1.00 15.47 ? 1022 ALA B CA    1 
ATOM   16351 C  C     . ALA B 1  1024 ? 9.283   40.266  75.939  1.00 14.21 ? 1022 ALA B C     1 
ATOM   16352 O  O     . ALA B 1  1024 ? 9.129   40.498  77.144  1.00 14.74 ? 1022 ALA B O     1 
ATOM   16353 C  CB    . ALA B 1  1024 ? 11.625  39.626  75.267  1.00 16.43 ? 1022 ALA B CB    1 
ATOM   16354 N  N     . GLY B 1  1025 ? 8.351   39.655  75.210  1.00 12.58 ? 1023 GLY B N     1 
ATOM   16355 C  CA    . GLY B 1  1025 ? 7.138   39.179  75.849  1.00 13.33 ? 1023 GLY B CA    1 
ATOM   16356 C  C     . GLY B 1  1025 ? 6.226   40.288  76.307  1.00 12.89 ? 1023 GLY B C     1 
ATOM   16357 O  O     . GLY B 1  1025 ? 5.342   40.063  77.141  1.00 13.56 ? 1023 GLY B O     1 
ATOM   16358 N  N     . GLY B 1  1026 ? 6.416   41.486  75.769  1.00 13.74 ? 1024 GLY B N     1 
ATOM   16359 C  CA    . GLY B 1  1026 ? 5.587   42.624  76.080  1.00 13.53 ? 1024 GLY B CA    1 
ATOM   16360 C  C     . GLY B 1  1026 ? 5.076   43.263  74.805  1.00 13.40 ? 1024 GLY B C     1 
ATOM   16361 O  O     . GLY B 1  1026 ? 5.495   42.928  73.697  1.00 13.66 ? 1024 GLY B O     1 
ATOM   16362 N  N     . PRO B 1  1027 ? 4.178   44.234  74.957  1.00 15.60 ? 1025 PRO B N     1 
ATOM   16363 C  CA    . PRO B 1  1027 ? 3.427   44.759  73.804  1.00 12.77 ? 1025 PRO B CA    1 
ATOM   16364 C  C     . PRO B 1  1027 ? 4.156   45.810  72.983  1.00 15.00 ? 1025 PRO B C     1 
ATOM   16365 O  O     . PRO B 1  1027 ? 3.650   46.177  71.922  1.00 14.56 ? 1025 PRO B O     1 
ATOM   16366 C  CB    . PRO B 1  1027 ? 2.183   45.360  74.465  1.00 14.10 ? 1025 PRO B CB    1 
ATOM   16367 C  CG    . PRO B 1  1027 ? 2.669   45.741  75.853  1.00 15.64 ? 1025 PRO B CG    1 
ATOM   16368 C  CD    . PRO B 1  1027 ? 3.598   44.649  76.248  1.00 15.38 ? 1025 PRO B CD    1 
ATOM   16369 N  N     . LEU B 1  1028 ? 5.300   46.317  73.432  1.00 13.96 ? 1026 LEU B N     1 
ATOM   16370 C  CA    . LEU B 1  1028 ? 6.083   47.259  72.638  1.00 15.23 ? 1026 LEU B CA    1 
ATOM   16371 C  C     . LEU B 1  1028 ? 7.073   46.570  71.721  1.00 15.26 ? 1026 LEU B C     1 
ATOM   16372 O  O     . LEU B 1  1028 ? 7.677   47.241  70.875  1.00 16.06 ? 1026 LEU B O     1 
ATOM   16373 C  CB    . LEU B 1  1028 ? 6.849   48.214  73.556  1.00 14.13 ? 1026 LEU B CB    1 
ATOM   16374 C  CG    . LEU B 1  1028 ? 5.947   49.051  74.458  1.00 18.05 ? 1026 LEU B CG    1 
ATOM   16375 C  CD1   . LEU B 1  1028 ? 6.811   49.966  75.304  1.00 20.10 ? 1026 LEU B CD1   1 
ATOM   16376 C  CD2   . LEU B 1  1028 ? 5.013   49.850  73.620  1.00 22.00 ? 1026 LEU B CD2   1 
ATOM   16377 N  N     . TYR B 1  1029 ? 7.232   45.255  71.858  1.00 13.21 ? 1027 TYR B N     1 
ATOM   16378 C  CA    . TYR B 1  1029 ? 8.363   44.568  71.247  1.00 14.05 ? 1027 TYR B CA    1 
ATOM   16379 C  C     . TYR B 1  1029 ? 8.279   44.590  69.729  1.00 12.75 ? 1027 TYR B C     1 
ATOM   16380 O  O     . TYR B 1  1029 ? 9.256   44.931  69.056  1.00 13.64 ? 1027 TYR B O     1 
ATOM   16381 C  CB    . TYR B 1  1029 ? 8.396   43.135  71.752  1.00 14.11 ? 1027 TYR B CB    1 
ATOM   16382 C  CG    . TYR B 1  1029 ? 9.662   42.352  71.586  1.00 14.67 ? 1027 TYR B CG    1 
ATOM   16383 C  CD1   . TYR B 1  1029 ? 10.803  42.668  72.324  1.00 13.13 ? 1027 TYR B CD1   1 
ATOM   16384 C  CD2   . TYR B 1  1029 ? 9.686   41.212  70.795  1.00 16.70 ? 1027 TYR B CD2   1 
ATOM   16385 C  CE1   . TYR B 1  1029 ? 11.962  41.895  72.221  1.00 14.06 ? 1027 TYR B CE1   1 
ATOM   16386 C  CE2   . TYR B 1  1029 ? 10.827  40.437  70.692  1.00 16.09 ? 1027 TYR B CE2   1 
ATOM   16387 C  CZ    . TYR B 1  1029 ? 11.949  40.774  71.412  1.00 15.71 ? 1027 TYR B CZ    1 
ATOM   16388 O  OH    . TYR B 1  1029 ? 13.064  39.989  71.320  1.00 15.44 ? 1027 TYR B OH    1 
ATOM   16389 N  N     . LEU B 1  1030 ? 7.138   44.162  69.168  1.00 14.04 ? 1028 LEU B N     1 
ATOM   16390 C  CA    . LEU B 1  1030 ? 7.049   44.014  67.713  1.00 16.09 ? 1028 LEU B CA    1 
ATOM   16391 C  C     . LEU B 1  1030 ? 7.233   45.347  67.006  1.00 16.87 ? 1028 LEU B C     1 
ATOM   16392 O  O     . LEU B 1  1030 ? 7.789   45.399  65.899  1.00 15.48 ? 1028 LEU B O     1 
ATOM   16393 C  CB    . LEU B 1  1030 ? 5.706   43.394  67.318  1.00 14.85 ? 1028 LEU B CB    1 
ATOM   16394 C  CG    . LEU B 1  1030 ? 5.461   41.940  67.722  1.00 16.09 ? 1028 LEU B CG    1 
ATOM   16395 C  CD1   . LEU B 1  1030 ? 4.129   41.477  67.170  1.00 19.07 ? 1028 LEU B CD1   1 
ATOM   16396 C  CD2   . LEU B 1  1030 ? 6.603   41.060  67.191  1.00 16.90 ? 1028 LEU B CD2   1 
ATOM   16397 N  N     . GLY B 1  1031 ? 6.799   46.435  67.637  1.00 16.44 ? 1029 GLY B N     1 
ATOM   16398 C  CA    . GLY B 1  1031 ? 6.887   47.744  67.012  1.00 17.21 ? 1029 GLY B CA    1 
ATOM   16399 C  C     . GLY B 1  1031 ? 8.305   48.212  66.746  1.00 15.65 ? 1029 GLY B C     1 
ATOM   16400 O  O     . GLY B 1  1031 ? 8.510   49.131  65.942  1.00 17.36 ? 1029 GLY B O     1 
ATOM   16401 N  N     . ARG B 1  1032 ? 9.288   47.616  67.413  1.00 14.95 ? 1030 ARG B N     1 
ATOM   16402 C  CA    . ARG B 1  1032 ? 10.686  47.931  67.140  1.00 14.74 ? 1030 ARG B CA    1 
ATOM   16403 C  C     . ARG B 1  1032 ? 11.192  47.274  65.868  1.00 15.69 ? 1030 ARG B C     1 
ATOM   16404 O  O     . ARG B 1  1032 ? 12.265  47.639  65.367  1.00 16.50 ? 1030 ARG B O     1 
ATOM   16405 C  CB    . ARG B 1  1032 ? 11.538  47.486  68.334  1.00 15.66 ? 1030 ARG B CB    1 
ATOM   16406 C  CG    . ARG B 1  1032 ? 12.965  47.970  68.307  1.00 15.90 ? 1030 ARG B CG    1 
ATOM   16407 C  CD    . ARG B 1  1032 ? 13.025  49.475  68.606  1.00 17.13 ? 1030 ARG B CD    1 
ATOM   16408 N  NE    . ARG B 1  1032 ? 14.396  49.930  68.788  1.00 18.28 ? 1030 ARG B NE    1 
ATOM   16409 C  CZ    . ARG B 1  1032 ? 14.987  50.893  68.091  1.00 18.03 ? 1030 ARG B CZ    1 
ATOM   16410 N  NH1   . ARG B 1  1032 ? 14.350  51.547  67.130  1.00 19.50 ? 1030 ARG B NH1   1 
ATOM   16411 N  NH2   . ARG B 1  1032 ? 16.245  51.218  68.380  1.00 19.87 ? 1030 ARG B NH2   1 
ATOM   16412 N  N     . LEU B 1  1033 ? 10.459  46.295  65.347  1.00 15.27 ? 1031 LEU B N     1 
ATOM   16413 C  CA    . LEU B 1  1033 ? 10.927  45.475  64.238  1.00 15.65 ? 1031 LEU B CA    1 
ATOM   16414 C  C     . LEU B 1  1033 ? 10.252  45.852  62.925  1.00 17.37 ? 1031 LEU B C     1 
ATOM   16415 O  O     . LEU B 1  1033 ? 10.272  45.069  61.970  1.00 17.42 ? 1031 LEU B O     1 
ATOM   16416 C  CB    . LEU B 1  1033 ? 10.687  44.004  64.572  1.00 14.99 ? 1031 LEU B CB    1 
ATOM   16417 C  CG    . LEU B 1  1033 ? 11.223  43.630  65.960  1.00 13.80 ? 1031 LEU B CG    1 
ATOM   16418 C  CD1   . LEU B 1  1033 ? 10.854  42.177  66.326  1.00 16.06 ? 1031 LEU B CD1   1 
ATOM   16419 C  CD2   . LEU B 1  1033 ? 12.740  43.855  66.068  1.00 16.15 ? 1031 LEU B CD2   1 
ATOM   16420 N  N     . VAL B 1  1034 ? 9.619   47.026  62.886  1.00 16.43 ? 1032 VAL B N     1 
ATOM   16421 C  CA    . VAL B 1  1034 ? 9.012   47.592  61.688  1.00 18.66 ? 1032 VAL B CA    1 
ATOM   16422 C  C     . VAL B 1  1034 ? 9.459   49.046  61.599  1.00 20.91 ? 1032 VAL B C     1 
ATOM   16423 O  O     . VAL B 1  1034 ? 9.941   49.625  62.571  1.00 19.09 ? 1032 VAL B O     1 
ATOM   16424 C  CB    . VAL B 1  1034 ? 7.473   47.500  61.699  1.00 16.74 ? 1032 VAL B CB    1 
ATOM   16425 C  CG1   . VAL B 1  1034 ? 7.003   46.048  61.556  1.00 17.60 ? 1032 VAL B CG1   1 
ATOM   16426 C  CG2   . VAL B 1  1034 ? 6.926   48.128  62.967  1.00 17.01 ? 1032 VAL B CG2   1 
ATOM   16427 N  N     . THR B 1  1035 ? 9.333   49.630  60.400  1.00 19.55 ? 1033 THR B N     1 
ATOM   16428 C  CA    . THR B 1  1035 ? 9.825   50.991  60.215  1.00 20.29 ? 1033 THR B CA    1 
ATOM   16429 C  C     . THR B 1  1035 ? 8.870   52.039  60.760  1.00 22.14 ? 1033 THR B C     1 
ATOM   16430 O  O     . THR B 1  1035 ? 9.304   53.159  61.053  1.00 23.58 ? 1033 THR B O     1 
ATOM   16431 C  CB    . THR B 1  1035 ? 10.115  51.264  58.737  1.00 25.09 ? 1033 THR B CB    1 
ATOM   16432 O  OG1   . THR B 1  1035 ? 8.986   50.884  57.945  1.00 30.67 ? 1033 THR B OG1   1 
ATOM   16433 C  CG2   . THR B 1  1035 ? 11.347  50.467  58.283  1.00 26.02 ? 1033 THR B CG2   1 
ATOM   16434 N  N     . THR B 1  1036 ? 7.593   51.702  60.917  1.00 20.04 ? 1034 THR B N     1 
ATOM   16435 C  CA    . THR B 1  1036 ? 6.623   52.568  61.572  1.00 20.71 ? 1034 THR B CA    1 
ATOM   16436 C  C     . THR B 1  1036 ? 5.935   51.748  62.649  1.00 21.63 ? 1034 THR B C     1 
ATOM   16437 O  O     . THR B 1  1036 ? 5.294   50.739  62.343  1.00 18.83 ? 1034 THR B O     1 
ATOM   16438 C  CB    . THR B 1  1036 ? 5.597   53.129  60.584  1.00 25.41 ? 1034 THR B CB    1 
ATOM   16439 O  OG1   . THR B 1  1036 ? 6.286   53.782  59.513  1.00 30.92 ? 1034 THR B OG1   1 
ATOM   16440 C  CG2   . THR B 1  1036 ? 4.684   54.138  61.278  1.00 27.38 ? 1034 THR B CG2   1 
ATOM   16441 N  N     . ALA B 1  1037 ? 6.081   52.174  63.903  1.00 20.27 ? 1035 ALA B N     1 
ATOM   16442 C  CA    . ALA B 1  1037 ? 5.545   51.376  65.001  1.00 18.85 ? 1035 ALA B CA    1 
ATOM   16443 C  C     . ALA B 1  1037 ? 4.025   51.511  65.074  1.00 19.82 ? 1035 ALA B C     1 
ATOM   16444 O  O     . ALA B 1  1037 ? 3.483   52.610  64.913  1.00 20.41 ? 1035 ALA B O     1 
ATOM   16445 C  CB    . ALA B 1  1037 ? 6.167   51.798  66.333  1.00 20.71 ? 1035 ALA B CB    1 
ATOM   16446 N  N     . PRO B 1  1038 ? 3.323   50.418  65.319  1.00 15.65 ? 1036 PRO B N     1 
ATOM   16447 C  CA    . PRO B 1  1038 ? 1.884   50.498  65.575  1.00 16.59 ? 1036 PRO B CA    1 
ATOM   16448 C  C     . PRO B 1  1038 ? 1.614   50.951  67.003  1.00 17.53 ? 1036 PRO B C     1 
ATOM   16449 O  O     . PRO B 1  1038 ? 2.501   51.021  67.852  1.00 18.24 ? 1036 PRO B O     1 
ATOM   16450 C  CB    . PRO B 1  1038 ? 1.415   49.056  65.358  1.00 17.73 ? 1036 PRO B CB    1 
ATOM   16451 C  CG    . PRO B 1  1038 ? 2.577   48.246  65.856  1.00 18.19 ? 1036 PRO B CG    1 
ATOM   16452 C  CD    . PRO B 1  1038 ? 3.823   49.033  65.424  1.00 16.63 ? 1036 PRO B CD    1 
ATOM   16453 N  N     . VAL B 1  1039 ? 0.348   51.258  67.251  1.00 19.04 ? 1037 VAL B N     1 
ATOM   16454 C  CA    . VAL B 1  1039 ? -0.150  51.517  68.597  1.00 17.42 ? 1037 VAL B CA    1 
ATOM   16455 C  C     . VAL B 1  1039 ? -0.448  50.166  69.236  1.00 17.49 ? 1037 VAL B C     1 
ATOM   16456 O  O     . VAL B 1  1039 ? -1.366  49.466  68.794  1.00 16.77 ? 1037 VAL B O     1 
ATOM   16457 C  CB    . VAL B 1  1039 ? -1.401  52.404  68.552  1.00 18.95 ? 1037 VAL B CB    1 
ATOM   16458 C  CG1   . VAL B 1  1039 ? -1.850  52.727  69.968  1.00 20.11 ? 1037 VAL B CG1   1 
ATOM   16459 C  CG2   . VAL B 1  1039 ? -1.108  53.674  67.772  1.00 19.48 ? 1037 VAL B CG2   1 
ATOM   16460 N  N     . PRO B 1  1040 ? 0.299   49.750  70.251  1.00 17.07 ? 1038 PRO B N     1 
ATOM   16461 C  CA    . PRO B 1  1040 ? 0.069   48.430  70.840  1.00 16.59 ? 1038 PRO B CA    1 
ATOM   16462 C  C     . PRO B 1  1040 ? -1.278  48.363  71.537  1.00 16.64 ? 1038 PRO B C     1 
ATOM   16463 O  O     . PRO B 1  1040 ? -1.859  49.398  71.904  1.00 16.90 ? 1038 PRO B O     1 
ATOM   16464 C  CB    . PRO B 1  1040 ? 1.224   48.286  71.847  1.00 17.87 ? 1038 PRO B CB    1 
ATOM   16465 C  CG    . PRO B 1  1040 ? 2.270   49.268  71.367  1.00 18.52 ? 1038 PRO B CG    1 
ATOM   16466 C  CD    . PRO B 1  1040 ? 1.476   50.422  70.829  1.00 18.65 ? 1038 PRO B CD    1 
ATOM   16467 N  N     . PRO B 1  1041 ? -1.801  47.157  71.746  1.00 16.16 ? 1039 PRO B N     1 
ATOM   16468 C  CA    . PRO B 1  1041 ? -3.026  47.002  72.537  1.00 16.47 ? 1039 PRO B CA    1 
ATOM   16469 C  C     . PRO B 1  1041 ? -2.882  47.639  73.910  1.00 18.77 ? 1039 PRO B C     1 
ATOM   16470 O  O     . PRO B 1  1041 ? -1.823  47.556  74.546  1.00 18.36 ? 1039 PRO B O     1 
ATOM   16471 C  CB    . PRO B 1  1041 ? -3.189  45.481  72.647  1.00 19.80 ? 1039 PRO B CB    1 
ATOM   16472 C  CG    . PRO B 1  1041 ? -2.367  44.928  71.512  1.00 18.43 ? 1039 PRO B CG    1 
ATOM   16473 C  CD    . PRO B 1  1041 ? -1.219  45.864  71.346  1.00 19.09 ? 1039 PRO B CD    1 
ATOM   16474 N  N     . GLN B 1  1042 ? -3.951  48.294  74.348  1.00 17.85 ? 1040 GLN B N     1 
ATOM   16475 C  CA    . GLN B 1  1042 ? -4.055  48.939  75.655  1.00 19.45 ? 1040 GLN B CA    1 
ATOM   16476 C  C     . GLN B 1  1042 ? -3.037  50.058  75.873  1.00 17.01 ? 1040 GLN B C     1 
ATOM   16477 O  O     . GLN B 1  1042 ? -2.868  50.515  77.013  1.00 17.19 ? 1040 GLN B O     1 
ATOM   16478 C  CB    . GLN B 1  1042 ? -3.923  47.909  76.787  1.00 21.95 ? 1040 GLN B CB    1 
ATOM   16479 C  CG    . GLN B 1  1042 ? -4.974  46.806  76.758  1.00 23.35 ? 1040 GLN B CG    1 
ATOM   16480 C  CD    . GLN B 1  1042 ? -4.706  45.744  77.816  1.00 27.98 ? 1040 GLN B CD    1 
ATOM   16481 O  OE1   . GLN B 1  1042 ? -3.554  45.411  78.105  1.00 34.86 ? 1040 GLN B OE1   1 
ATOM   16482 N  NE2   . GLN B 1  1042 ? -5.763  45.224  78.403  1.00 34.86 ? 1040 GLN B NE2   1 
ATOM   16483 N  N     . HIS B 1  1043 ? -2.339  50.516  74.828  1.00 16.92 ? 1041 HIS B N     1 
ATOM   16484 C  CA    . HIS B 1  1043 ? -1.224  51.455  75.008  1.00 16.21 ? 1041 HIS B CA    1 
ATOM   16485 C  C     . HIS B 1  1043 ? -1.755  52.884  74.952  1.00 17.81 ? 1041 HIS B C     1 
ATOM   16486 O  O     . HIS B 1  1043 ? -1.796  53.515  73.894  1.00 19.26 ? 1041 HIS B O     1 
ATOM   16487 C  CB    . HIS B 1  1043 ? -0.151  51.204  73.953  1.00 16.14 ? 1041 HIS B CB    1 
ATOM   16488 C  CG    . HIS B 1  1043 ? 1.052   52.097  74.060  1.00 15.94 ? 1041 HIS B CG    1 
ATOM   16489 N  ND1   . HIS B 1  1043 ? 2.141   51.804  74.857  1.00 16.33 ? 1041 HIS B ND1   1 
ATOM   16490 C  CD2   . HIS B 1  1043 ? 1.346   53.267  73.440  1.00 18.65 ? 1041 HIS B CD2   1 
ATOM   16491 C  CE1   . HIS B 1  1043 ? 3.044   52.762  74.735  1.00 18.64 ? 1041 HIS B CE1   1 
ATOM   16492 N  NE2   . HIS B 1  1043 ? 2.598   53.650  73.864  1.00 17.53 ? 1041 HIS B NE2   1 
ATOM   16493 N  N     . SER B 1  1044 ? -2.151  53.410  76.109  1.00 15.24 ? 1042 SER B N     1 
ATOM   16494 C  CA    . SER B 1  1044 ? -2.593  54.793  76.209  1.00 15.25 ? 1042 SER B CA    1 
ATOM   16495 C  C     . SER B 1  1044 ? -2.526  55.209  77.667  1.00 16.00 ? 1042 SER B C     1 
ATOM   16496 O  O     . SER B 1  1044 ? -2.356  54.382  78.561  1.00 17.31 ? 1042 SER B O     1 
ATOM   16497 C  CB    . SER B 1  1044 ? -4.006  54.963  75.658  1.00 16.20 ? 1042 SER B CB    1 
ATOM   16498 O  OG    . SER B 1  1044 ? -4.947  54.374  76.542  1.00 17.52 ? 1042 SER B OG    1 
ATOM   16499 N  N     . SER B 1  1045 ? -2.692  56.505  77.897  1.00 16.94 ? 1043 SER B N     1 
ATOM   16500 C  CA    . SER B 1  1045 ? -2.709  57.045  79.247  1.00 16.80 ? 1043 SER B CA    1 
ATOM   16501 C  C     . SER B 1  1045 ? -3.580  58.285  79.253  1.00 16.16 ? 1043 SER B C     1 
ATOM   16502 O  O     . SER B 1  1045 ? -3.532  59.077  78.312  1.00 16.93 ? 1043 SER B O     1 
ATOM   16503 C  CB    . SER B 1  1045 ? -1.291  57.401  79.722  1.00 15.85 ? 1043 SER B CB    1 
ATOM   16504 O  OG    . SER B 1  1045 ? -1.340  57.989  81.009  1.00 16.60 ? 1043 SER B OG    1 
ATOM   16505 N  N     . VAL B 1  1046 ? -4.390  58.450  80.306  1.00 17.30 ? 1044 VAL B N     1 
ATOM   16506 C  CA    . VAL B 1  1046 ? -5.188  59.664  80.434  1.00 18.05 ? 1044 VAL B CA    1 
ATOM   16507 C  C     . VAL B 1  1046 ? -4.411  60.792  81.091  1.00 18.45 ? 1044 VAL B C     1 
ATOM   16508 O  O     . VAL B 1  1046 ? -4.933  61.908  81.216  1.00 18.28 ? 1044 VAL B O     1 
ATOM   16509 C  CB    . VAL B 1  1046 ? -6.489  59.420  81.227  1.00 19.22 ? 1044 VAL B CB    1 
ATOM   16510 C  CG1   . VAL B 1  1046 ? -7.291  58.294  80.571  1.00 21.17 ? 1044 VAL B CG1   1 
ATOM   16511 C  CG2   . VAL B 1  1046 ? -6.180  59.105  82.674  1.00 18.94 ? 1044 VAL B CG2   1 
ATOM   16512 N  N     . HIS B 1  1047 ? -3.172  60.546  81.492  1.00 18.88 ? 1045 HIS B N     1 
ATOM   16513 C  CA    . HIS B 1  1047 ? -2.392  61.542  82.198  1.00 19.43 ? 1045 HIS B CA    1 
ATOM   16514 C  C     . HIS B 1  1047 ? -1.544  62.330  81.215  1.00 18.10 ? 1045 HIS B C     1 
ATOM   16515 O  O     . HIS B 1  1047 ? -1.064  61.789  80.218  1.00 19.13 ? 1045 HIS B O     1 
ATOM   16516 C  CB    . HIS B 1  1047 ? -1.545  60.849  83.258  1.00 22.85 ? 1045 HIS B CB    1 
ATOM   16517 C  CG    . HIS B 1  1047 ? -2.376  60.011  84.179  1.00 25.31 ? 1045 HIS B CG    1 
ATOM   16518 N  ND1   . HIS B 1  1047 ? -3.349  60.554  84.993  1.00 26.46 ? 1045 HIS B ND1   1 
ATOM   16519 C  CD2   . HIS B 1  1047 ? -2.443  58.667  84.353  1.00 26.39 ? 1045 HIS B CD2   1 
ATOM   16520 C  CE1   . HIS B 1  1047 ? -3.947  59.585  85.664  1.00 28.78 ? 1045 HIS B CE1   1 
ATOM   16521 N  NE2   . HIS B 1  1047 ? -3.419  58.430  85.290  1.00 24.55 ? 1045 HIS B NE2   1 
ATOM   16522 N  N     . THR B 1  1048 ? -1.411  63.623  81.478  1.00 17.18 ? 1046 THR B N     1 
ATOM   16523 C  CA    . THR B 1  1048 ? -0.619  64.513  80.647  1.00 18.03 ? 1046 THR B CA    1 
ATOM   16524 C  C     . THR B 1  1048 ? 0.501   65.080  81.501  1.00 16.77 ? 1046 THR B C     1 
ATOM   16525 O  O     . THR B 1  1048 ? 0.253   65.601  82.594  1.00 18.55 ? 1046 THR B O     1 
ATOM   16526 C  CB    . THR B 1  1048 ? -1.457  65.655  80.068  1.00 21.79 ? 1046 THR B CB    1 
ATOM   16527 O  OG1   . THR B 1  1048 ? -2.624  65.129  79.426  1.00 20.37 ? 1046 THR B OG1   1 
ATOM   16528 C  CG2   . THR B 1  1048 ? -0.639  66.421  79.036  1.00 21.33 ? 1046 THR B CG2   1 
ATOM   16529 N  N     . ASP B 1  1049 ? 1.716   64.968  81.008  1.00 17.35 ? 1047 ASP B N     1 
ATOM   16530 C  CA    . ASP B 1  1049 ? 2.845   65.457  81.768  1.00 17.89 ? 1047 ASP B CA    1 
ATOM   16531 C  C     . ASP B 1  1049 ? 2.686   66.955  82.005  1.00 16.91 ? 1047 ASP B C     1 
ATOM   16532 O  O     . ASP B 1  1049 ? 2.402   67.705  81.059  1.00 20.02 ? 1047 ASP B O     1 
ATOM   16533 C  CB    . ASP B 1  1049 ? 4.144   65.145  81.026  1.00 17.48 ? 1047 ASP B CB    1 
ATOM   16534 C  CG    . ASP B 1  1049 ? 5.355   65.568  81.805  1.00 16.89 ? 1047 ASP B CG    1 
ATOM   16535 O  OD1   . ASP B 1  1049 ? 5.692   66.758  81.721  1.00 19.27 ? 1047 ASP B OD1   1 
ATOM   16536 O  OD2   . ASP B 1  1049 ? 5.928   64.714  82.507  1.00 17.56 ? 1047 ASP B OD2   1 
ATOM   16537 N  N     . PRO B 1  1050 ? 2.817   67.427  83.247  1.00 18.59 ? 1048 PRO B N     1 
ATOM   16538 C  CA    . PRO B 1  1050 ? 2.576   68.848  83.506  1.00 20.64 ? 1048 PRO B CA    1 
ATOM   16539 C  C     . PRO B 1  1050 ? 3.644   69.740  82.914  1.00 20.88 ? 1048 PRO B C     1 
ATOM   16540 O  O     . PRO B 1  1050 ? 3.349   70.885  82.552  1.00 21.06 ? 1048 PRO B O     1 
ATOM   16541 C  CB    . PRO B 1  1050 ? 2.554   68.922  85.040  1.00 21.72 ? 1048 PRO B CB    1 
ATOM   16542 C  CG    . PRO B 1  1050 ? 3.383   67.783  85.474  1.00 23.11 ? 1048 PRO B CG    1 
ATOM   16543 C  CD    . PRO B 1  1050 ? 3.177   66.690  84.464  1.00 20.17 ? 1048 PRO B CD    1 
ATOM   16544 N  N     . VAL B 1  1051 ? 4.880   69.255  82.820  1.00 19.79 ? 1049 VAL B N     1 
ATOM   16545 C  CA    . VAL B 1  1051 ? 5.933   70.071  82.231  1.00 21.19 ? 1049 VAL B CA    1 
ATOM   16546 C  C     . VAL B 1  1051 ? 5.729   70.185  80.730  1.00 19.60 ? 1049 VAL B C     1 
ATOM   16547 O  O     . VAL B 1  1051 ? 5.926   71.254  80.142  1.00 19.64 ? 1049 VAL B O     1 
ATOM   16548 C  CB    . VAL B 1  1051 ? 7.314   69.500  82.584  1.00 22.76 ? 1049 VAL B CB    1 
ATOM   16549 C  CG1   . VAL B 1  1051 ? 8.401   70.353  81.928  1.00 23.38 ? 1049 VAL B CG1   1 
ATOM   16550 C  CG2   . VAL B 1  1051 ? 7.487   69.480  84.108  1.00 20.57 ? 1049 VAL B CG2   1 
ATOM   16551 N  N     . LEU B 1  1052 ? 5.285   69.101  80.090  1.00 18.50 ? 1050 LEU B N     1 
ATOM   16552 C  CA    . LEU B 1  1052 ? 4.853   69.204  78.702  1.00 18.07 ? 1050 LEU B CA    1 
ATOM   16553 C  C     . LEU B 1  1052 ? 3.811   70.309  78.543  1.00 20.52 ? 1050 LEU B C     1 
ATOM   16554 O  O     . LEU B 1  1052 ? 3.902   71.135  77.632  1.00 19.45 ? 1050 LEU B O     1 
ATOM   16555 C  CB    . LEU B 1  1052 ? 4.312   67.850  78.222  1.00 16.59 ? 1050 LEU B CB    1 
ATOM   16556 C  CG    . LEU B 1  1052 ? 3.823   67.700  76.769  1.00 17.32 ? 1050 LEU B CG    1 
ATOM   16557 C  CD1   . LEU B 1  1052 ? 2.423   68.284  76.542  1.00 19.70 ? 1050 LEU B CD1   1 
ATOM   16558 C  CD2   . LEU B 1  1052 ? 4.821   68.301  75.781  1.00 18.51 ? 1050 LEU B CD2   1 
ATOM   16559 N  N     . LEU B 1  1053 ? 2.820   70.352  79.440  1.00 19.54 ? 1051 LEU B N     1 
ATOM   16560 C  CA    . LEU B 1  1053 ? 1.774   71.362  79.322  1.00 22.47 ? 1051 LEU B CA    1 
ATOM   16561 C  C     . LEU B 1  1053 ? 2.352   72.766  79.432  1.00 21.11 ? 1051 LEU B C     1 
ATOM   16562 O  O     . LEU B 1  1053 ? 1.975   73.666  78.668  1.00 23.66 ? 1051 LEU B O     1 
ATOM   16563 C  CB    . LEU B 1  1053 ? 0.701   71.144  80.391  1.00 23.80 ? 1051 LEU B CB    1 
ATOM   16564 C  CG    . LEU B 1  1053 ? -0.193  69.907  80.232  1.00 24.60 ? 1051 LEU B CG    1 
ATOM   16565 C  CD1   . LEU B 1  1053 ? -0.964  69.673  81.524  1.00 22.81 ? 1051 LEU B CD1   1 
ATOM   16566 C  CD2   . LEU B 1  1053 ? -1.145  70.091  79.071  1.00 25.39 ? 1051 LEU B CD2   1 
ATOM   16567 N  N     . ASP B 1  1054 ? 3.278   72.971  80.368  1.00 22.85 ? 1052 ASP B N     1 
ATOM   16568 C  CA    . ASP B 1  1054 ? 3.901   74.284  80.492  1.00 24.05 ? 1052 ASP B CA    1 
ATOM   16569 C  C     . ASP B 1  1054 ? 4.727   74.623  79.262  1.00 22.30 ? 1052 ASP B C     1 
ATOM   16570 O  O     . ASP B 1  1054 ? 4.787   75.789  78.860  1.00 24.47 ? 1052 ASP B O     1 
ATOM   16571 C  CB    . ASP B 1  1054 ? 4.770   74.327  81.745  1.00 23.23 ? 1052 ASP B CB    1 
ATOM   16572 C  CG    . ASP B 1  1054 ? 3.950   74.331  83.015  1.00 25.93 ? 1052 ASP B CG    1 
ATOM   16573 O  OD1   . ASP B 1  1054 ? 2.716   74.514  82.918  1.00 26.48 ? 1052 ASP B OD1   1 
ATOM   16574 O  OD2   . ASP B 1  1054 ? 4.534   74.151  84.106  1.00 31.03 ? 1052 ASP B OD2   1 
ATOM   16575 N  N     . PHE B 1  1055 ? 5.361   73.618  78.655  1.00 22.76 ? 1053 PHE B N     1 
ATOM   16576 C  CA    . PHE B 1  1055 ? 6.151   73.850  77.454  1.00 20.75 ? 1053 PHE B CA    1 
ATOM   16577 C  C     . PHE B 1  1055 ? 5.257   74.249  76.286  1.00 24.79 ? 1053 PHE B C     1 
ATOM   16578 O  O     . PHE B 1  1055 ? 5.599   75.152  75.514  1.00 22.53 ? 1053 PHE B O     1 
ATOM   16579 C  CB    . PHE B 1  1055 ? 6.973   72.595  77.134  1.00 21.36 ? 1053 PHE B CB    1 
ATOM   16580 C  CG    . PHE B 1  1055 ? 7.868   72.738  75.938  1.00 22.02 ? 1053 PHE B CG    1 
ATOM   16581 C  CD1   . PHE B 1  1055 ? 8.826   73.739  75.892  1.00 23.70 ? 1053 PHE B CD1   1 
ATOM   16582 C  CD2   . PHE B 1  1055 ? 7.761   71.862  74.868  1.00 21.01 ? 1053 PHE B CD2   1 
ATOM   16583 C  CE1   . PHE B 1  1055 ? 9.663   73.863  74.791  1.00 21.91 ? 1053 PHE B CE1   1 
ATOM   16584 C  CE2   . PHE B 1  1055 ? 8.588   71.989  73.759  1.00 22.13 ? 1053 PHE B CE2   1 
ATOM   16585 C  CZ    . PHE B 1  1055 ? 9.534   72.994  73.722  1.00 21.45 ? 1053 PHE B CZ    1 
ATOM   16586 N  N     . ALA B 1  1056 ? 4.095   73.601  76.156  1.00 21.82 ? 1054 ALA B N     1 
ATOM   16587 C  CA    . ALA B 1  1056 ? 3.164   73.964  75.092  1.00 23.40 ? 1054 ALA B CA    1 
ATOM   16588 C  C     . ALA B 1  1056 ? 2.713   75.413  75.229  1.00 24.49 ? 1054 ALA B C     1 
ATOM   16589 O  O     . ALA B 1  1056 ? 2.650   76.147  74.236  1.00 27.24 ? 1054 ALA B O     1 
ATOM   16590 C  CB    . ALA B 1  1056 ? 1.954   73.025  75.100  1.00 24.85 ? 1054 ALA B CB    1 
ATOM   16591 N  N     . LYS B 1  1057 ? 2.397   75.843  76.452  1.00 25.10 ? 1055 LYS B N     1 
ATOM   16592 C  CA    . LYS B 1  1057 ? 1.958   77.221  76.655  1.00 23.65 ? 1055 LYS B CA    1 
ATOM   16593 C  C     . LYS B 1  1057 ? 3.068   78.200  76.305  1.00 30.45 ? 1055 LYS B C     1 
ATOM   16594 O  O     . LYS B 1  1057 ? 2.818   79.242  75.684  1.00 31.26 ? 1055 LYS B O     1 
ATOM   16595 C  CB    . LYS B 1  1057 ? 1.514   77.425  78.101  1.00 28.49 ? 1055 LYS B CB    1 
ATOM   16596 C  CG    . LYS B 1  1057 ? 0.267   76.639  78.476  1.00 32.11 ? 1055 LYS B CG    1 
ATOM   16597 C  CD    . LYS B 1  1057 ? -0.222  77.005  79.861  1.00 25.36 ? 1055 LYS B CD    1 
ATOM   16598 C  CE    . LYS B 1  1057 ? 0.808   76.660  80.918  1.00 27.78 ? 1055 LYS B CE    1 
ATOM   16599 N  NZ    . LYS B 1  1057 ? 0.169   76.622  82.264  1.00 27.32 ? 1055 LYS B NZ    1 
ATOM   16600 N  N     . TRP B 1  1058 ? 4.301   77.880  76.705  1.00 28.61 ? 1056 TRP B N     1 
ATOM   16601 C  CA    . TRP B 1  1058 ? 5.447   78.708  76.347  1.00 28.25 ? 1056 TRP B CA    1 
ATOM   16602 C  C     . TRP B 1  1058 ? 5.582   78.819  74.835  1.00 28.42 ? 1056 TRP B C     1 
ATOM   16603 O  O     . TRP B 1  1058 ? 5.780   79.916  74.300  1.00 30.31 ? 1056 TRP B O     1 
ATOM   16604 C  CB    . TRP B 1  1058 ? 6.713   78.130  76.982  1.00 29.03 ? 1056 TRP B CB    1 
ATOM   16605 C  CG    . TRP B 1  1058 ? 7.973   78.871  76.652  1.00 31.53 ? 1056 TRP B CG    1 
ATOM   16606 C  CD1   . TRP B 1  1058 ? 8.399   80.051  77.193  1.00 33.71 ? 1056 TRP B CD1   1 
ATOM   16607 C  CD2   . TRP B 1  1058 ? 8.978   78.473  75.715  1.00 29.30 ? 1056 TRP B CD2   1 
ATOM   16608 N  NE1   . TRP B 1  1058 ? 9.604   80.415  76.642  1.00 32.68 ? 1056 TRP B NE1   1 
ATOM   16609 C  CE2   . TRP B 1  1058 ? 9.984   79.464  75.734  1.00 33.03 ? 1056 TRP B CE2   1 
ATOM   16610 C  CE3   . TRP B 1  1058 ? 9.129   77.375  74.858  1.00 29.17 ? 1056 TRP B CE3   1 
ATOM   16611 C  CZ2   . TRP B 1  1058 ? 11.129  79.386  74.935  1.00 33.65 ? 1056 TRP B CZ2   1 
ATOM   16612 C  CZ3   . TRP B 1  1058 ? 10.266  77.302  74.056  1.00 33.07 ? 1056 TRP B CZ3   1 
ATOM   16613 C  CH2   . TRP B 1  1058 ? 11.249  78.306  74.104  1.00 30.92 ? 1056 TRP B CH2   1 
ATOM   16614 N  N     . LEU B 1  1059 ? 5.458   77.692  74.126  1.00 26.66 ? 1057 LEU B N     1 
ATOM   16615 C  CA    . LEU B 1  1059 ? 5.482   77.728  72.664  1.00 28.55 ? 1057 LEU B CA    1 
ATOM   16616 C  C     . LEU B 1  1059 ? 4.348   78.580  72.107  1.00 33.70 ? 1057 LEU B C     1 
ATOM   16617 O  O     . LEU B 1  1059 ? 4.542   79.316  71.132  1.00 32.72 ? 1057 LEU B O     1 
ATOM   16618 C  CB    . LEU B 1  1059 ? 5.399   76.313  72.093  1.00 25.53 ? 1057 LEU B CB    1 
ATOM   16619 C  CG    . LEU B 1  1059 ? 6.618   75.422  72.336  1.00 27.28 ? 1057 LEU B CG    1 
ATOM   16620 C  CD1   . LEU B 1  1059 ? 6.330   74.012  71.863  1.00 25.42 ? 1057 LEU B CD1   1 
ATOM   16621 C  CD2   . LEU B 1  1059 ? 7.841   75.989  71.623  1.00 30.38 ? 1057 LEU B CD2   1 
ATOM   16622 N  N     . ASP B 1  1060 ? 3.149   78.466  72.691  1.00 30.76 ? 1058 ASP B N     1 
ATOM   16623 C  CA    . ASP B 1  1060 ? 2.028   79.315  72.283  1.00 30.96 ? 1058 ASP B CA    1 
ATOM   16624 C  C     . ASP B 1  1060 ? 2.402   80.791  72.372  1.00 33.68 ? 1058 ASP B C     1 
ATOM   16625 O  O     . ASP B 1  1060 ? 2.168   81.562  71.434  1.00 36.08 ? 1058 ASP B O     1 
ATOM   16626 C  CB    . ASP B 1  1060 ? 0.794   79.051  73.162  1.00 35.22 ? 1058 ASP B CB    1 
ATOM   16627 C  CG    . ASP B 1  1060 ? 0.039   77.761  72.805  1.00 36.12 ? 1058 ASP B CG    1 
ATOM   16628 O  OD1   . ASP B 1  1060 ? 0.058   77.318  71.637  1.00 32.99 ? 1058 ASP B OD1   1 
ATOM   16629 O  OD2   . ASP B 1  1060 ? -0.617  77.205  73.723  1.00 37.23 ? 1058 ASP B OD2   1 
ATOM   16630 N  N     . GLY B 1  1061 ? 2.969   81.205  73.509  1.00 33.60 ? 1059 GLY B N     1 
ATOM   16631 C  CA    . GLY B 1  1061 ? 3.301   82.607  73.697  1.00 37.94 ? 1059 GLY B CA    1 
ATOM   16632 C  C     . GLY B 1  1061 ? 4.318   83.121  72.698  1.00 37.48 ? 1059 GLY B C     1 
ATOM   16633 O  O     . GLY B 1  1061 ? 4.313   84.305  72.361  1.00 39.08 ? 1059 GLY B O     1 
ATOM   16634 N  N     . LYS B 1  1062 ? 5.199   82.245  72.211  1.00 35.37 ? 1060 LYS B N     1 
ATOM   16635 C  CA    . LYS B 1  1062 ? 6.193   82.607  71.207  1.00 37.57 ? 1060 LYS B CA    1 
ATOM   16636 C  C     . LYS B 1  1062 ? 5.654   82.584  69.787  1.00 39.18 ? 1060 LYS B C     1 
ATOM   16637 O  O     . LYS B 1  1062 ? 6.397   82.929  68.862  1.00 39.80 ? 1060 LYS B O     1 
ATOM   16638 C  CB    . LYS B 1  1062 ? 7.382   81.652  71.264  1.00 36.04 ? 1060 LYS B CB    1 
ATOM   16639 C  CG    . LYS B 1  1062 ? 8.179   81.711  72.521  1.00 36.52 ? 1060 LYS B CG    1 
ATOM   16640 C  CD    . LYS B 1  1062 ? 9.177   80.578  72.504  1.00 32.30 ? 1060 LYS B CD    1 
ATOM   16641 C  CE    . LYS B 1  1062 ? 9.982   80.567  71.211  1.00 34.95 ? 1060 LYS B CE    1 
ATOM   16642 N  NZ    . LYS B 1  1062 ? 11.325  81.177  71.377  1.00 36.57 ? 1060 LYS B NZ    1 
ATOM   16643 N  N     . GLY B 1  1063 ? 4.409   82.160  69.587  1.00 36.83 ? 1061 GLY B N     1 
ATOM   16644 C  CA    . GLY B 1  1063 ? 3.886   82.001  68.250  1.00 38.42 ? 1061 GLY B CA    1 
ATOM   16645 C  C     . GLY B 1  1063 ? 4.394   80.793  67.501  1.00 38.64 ? 1061 GLY B C     1 
ATOM   16646 O  O     . GLY B 1  1063 ? 4.198   80.715  66.282  1.00 37.83 ? 1061 GLY B O     1 
ATOM   16647 N  N     . ALA B 1  1064 ? 5.040   79.845  68.186  1.00 33.88 ? 1062 ALA B N     1 
ATOM   16648 C  CA    . ALA B 1  1064 ? 5.523   78.620  67.549  1.00 32.86 ? 1062 ALA B CA    1 
ATOM   16649 C  C     . ALA B 1  1064 ? 4.355   77.639  67.440  1.00 34.79 ? 1062 ALA B C     1 
ATOM   16650 O  O     . ALA B 1  1064 ? 4.269   76.636  68.152  1.00 30.09 ? 1062 ALA B O     1 
ATOM   16651 C  CB    . ALA B 1  1064 ? 6.687   78.030  68.335  1.00 32.15 ? 1062 ALA B CB    1 
ATOM   16652 N  N     . ARG B 1  1065 ? 3.450   77.946  66.502  1.00 33.20 ? 1063 ARG B N     1 
ATOM   16653 C  CA    . ARG B 1  1065 ? 2.129   77.313  66.499  1.00 31.92 ? 1063 ARG B CA    1 
ATOM   16654 C  C     . ARG B 1  1065 ? 2.201   75.851  66.077  1.00 30.45 ? 1063 ARG B C     1 
ATOM   16655 O  O     . ARG B 1  1065 ? 1.541   74.993  66.680  1.00 30.84 ? 1063 ARG B O     1 
ATOM   16656 C  CB    . ARG B 1  1065 ? 1.170   78.093  65.593  1.00 31.93 ? 1063 ARG B CB    1 
ATOM   16657 N  N     . ALA B 1  1066 ? 2.993   75.537  65.051  1.00 28.99 ? 1064 ALA B N     1 
ATOM   16658 C  CA    . ALA B 1  1066 ? 3.155   74.138  64.679  1.00 30.08 ? 1064 ALA B CA    1 
ATOM   16659 C  C     . ALA B 1  1066 ? 3.776   73.342  65.820  1.00 28.12 ? 1064 ALA B C     1 
ATOM   16660 O  O     . ALA B 1  1066 ? 3.339   72.224  66.117  1.00 28.57 ? 1064 ALA B O     1 
ATOM   16661 C  CB    . ALA B 1  1066 ? 4.004   74.015  63.413  1.00 31.95 ? 1064 ALA B CB    1 
ATOM   16662 N  N     . GLU B 1  1067 ? 4.777   73.914  66.492  1.00 27.12 ? 1065 GLU B N     1 
ATOM   16663 C  CA    . GLU B 1  1067 ? 5.459   73.181  67.554  1.00 26.85 ? 1065 GLU B CA    1 
ATOM   16664 C  C     . GLU B 1  1067 ? 4.552   72.973  68.759  1.00 24.05 ? 1065 GLU B C     1 
ATOM   16665 O  O     . GLU B 1  1067 ? 4.527   71.881  69.339  1.00 25.71 ? 1065 GLU B O     1 
ATOM   16666 C  CB    . GLU B 1  1067 ? 6.734   73.917  67.964  1.00 28.62 ? 1065 GLU B CB    1 
ATOM   16667 C  CG    . GLU B 1  1067 ? 7.844   73.830  66.923  1.00 26.60 ? 1065 GLU B CG    1 
ATOM   16668 C  CD    . GLU B 1  1067 ? 7.684   74.839  65.817  1.00 30.89 ? 1065 GLU B CD    1 
ATOM   16669 O  OE1   . GLU B 1  1067 ? 6.802   75.718  65.933  1.00 31.00 ? 1065 GLU B OE1   1 
ATOM   16670 O  OE2   . GLU B 1  1067 ? 8.439   74.753  64.822  1.00 30.17 ? 1065 GLU B OE2   1 
ATOM   16671 N  N     . ALA B 1  1068 ? 3.808   74.010  69.150  1.00 27.98 ? 1066 ALA B N     1 
ATOM   16672 C  CA    . ALA B 1  1068 ? 2.876   73.879  70.267  1.00 29.47 ? 1066 ALA B CA    1 
ATOM   16673 C  C     . ALA B 1  1068 ? 1.833   72.808  69.985  1.00 28.07 ? 1066 ALA B C     1 
ATOM   16674 O  O     . ALA B 1  1068 ? 1.465   72.034  70.879  1.00 24.96 ? 1066 ALA B O     1 
ATOM   16675 C  CB    . ALA B 1  1068 ? 2.202   75.221  70.547  1.00 24.76 ? 1066 ALA B CB    1 
ATOM   16676 N  N     . GLU B 1  1069 ? 1.351   72.745  68.741  1.00 25.14 ? 1067 GLU B N     1 
ATOM   16677 C  CA    . GLU B 1  1069 ? 0.421   71.689  68.360  1.00 28.04 ? 1067 GLU B CA    1 
ATOM   16678 C  C     . GLU B 1  1069 ? 1.088   70.324  68.437  1.00 27.91 ? 1067 GLU B C     1 
ATOM   16679 O  O     . GLU B 1  1069 ? 0.480   69.350  68.903  1.00 26.99 ? 1067 GLU B O     1 
ATOM   16680 C  CB    . GLU B 1  1069 ? -0.120  71.951  66.953  1.00 31.18 ? 1067 GLU B CB    1 
ATOM   16681 C  CG    . GLU B 1  1069 ? -0.978  70.834  66.372  1.00 31.57 ? 1067 GLU B CG    1 
ATOM   16682 C  CD    . GLU B 1  1069 ? -2.370  70.766  66.987  1.00 37.10 ? 1067 GLU B CD    1 
ATOM   16683 O  OE1   . GLU B 1  1069 ? -2.698  71.607  67.854  1.00 37.12 ? 1067 GLU B OE1   1 
ATOM   16684 O  OE2   . GLU B 1  1069 ? -3.143  69.862  66.598  1.00 43.17 ? 1067 GLU B OE2   1 
ATOM   16685 N  N     . ALA B 1  1070 ? 2.339   70.228  67.984  1.00 24.94 ? 1068 ALA B N     1 
ATOM   16686 C  CA    . ALA B 1  1070 ? 3.054   68.968  68.112  1.00 26.10 ? 1068 ALA B CA    1 
ATOM   16687 C  C     . ALA B 1  1070 ? 3.226   68.601  69.578  1.00 23.34 ? 1068 ALA B C     1 
ATOM   16688 O  O     . ALA B 1  1070 ? 3.087   67.433  69.951  1.00 23.97 ? 1068 ALA B O     1 
ATOM   16689 C  CB    . ALA B 1  1070 ? 4.411   69.053  67.409  1.00 26.78 ? 1068 ALA B CB    1 
ATOM   16690 N  N     . ALA B 1  1071 ? 3.486   69.595  70.431  1.00 21.98 ? 1069 ALA B N     1 
ATOM   16691 C  CA    . ALA B 1  1071 ? 3.655   69.315  71.852  1.00 21.43 ? 1069 ALA B CA    1 
ATOM   16692 C  C     . ALA B 1  1071 ? 2.353   68.821  72.475  1.00 21.26 ? 1069 ALA B C     1 
ATOM   16693 O  O     . ALA B 1  1071 ? 2.354   67.851  73.240  1.00 21.58 ? 1069 ALA B O     1 
ATOM   16694 C  CB    . ALA B 1  1071 ? 4.168   70.556  72.580  1.00 21.53 ? 1069 ALA B CB    1 
ATOM   16695 N  N     . ARG B 1  1072 ? 1.232   69.482  72.175  1.00 22.46 ? 1070 ARG B N     1 
ATOM   16696 C  CA    . ARG B 1  1072 ? -0.039  69.006  72.716  1.00 22.79 ? 1070 ARG B CA    1 
ATOM   16697 C  C     . ARG B 1  1072 ? -0.342  67.595  72.233  1.00 21.80 ? 1070 ARG B C     1 
ATOM   16698 O  O     . ARG B 1  1072 ? -0.800  66.748  73.011  1.00 21.76 ? 1070 ARG B O     1 
ATOM   16699 C  CB    . ARG B 1  1072 ? -1.171  69.960  72.338  1.00 23.17 ? 1070 ARG B CB    1 
ATOM   16700 C  CG    . ARG B 1  1072 ? -1.180  71.264  73.127  1.00 26.29 ? 1070 ARG B CG    1 
ATOM   16701 C  CD    . ARG B 1  1072 ? -2.432  72.099  72.816  1.00 27.51 ? 1070 ARG B CD    1 
ATOM   16702 N  NE    . ARG B 1  1072 ? -2.445  72.530  71.424  1.00 33.76 ? 1070 ARG B NE    1 
ATOM   16703 C  CZ    . ARG B 1  1072 ? -1.949  73.684  70.991  1.00 35.88 ? 1070 ARG B CZ    1 
ATOM   16704 N  NH1   . ARG B 1  1072 ? -1.475  74.595  71.830  1.00 31.94 ? 1070 ARG B NH1   1 
ATOM   16705 N  NH2   . ARG B 1  1072 ? -1.910  73.922  69.682  1.00 29.08 ? 1070 ARG B NH2   1 
ATOM   16706 N  N     . ASN B 1  1073 ? -0.082  67.320  70.953  1.00 21.17 ? 1071 ASN B N     1 
ATOM   16707 C  CA    . ASN B 1  1073 ? -0.323  65.979  70.421  1.00 22.32 ? 1071 ASN B CA    1 
ATOM   16708 C  C     . ASN B 1  1073 ? 0.561   64.942  71.098  1.00 22.46 ? 1071 ASN B C     1 
ATOM   16709 O  O     . ASN B 1  1073 ? 0.112   63.825  71.379  1.00 21.61 ? 1071 ASN B O     1 
ATOM   16710 C  CB    . ASN B 1  1073 ? -0.111  65.966  68.911  1.00 24.99 ? 1071 ASN B CB    1 
ATOM   16711 C  CG    . ASN B 1  1073 ? -1.208  66.698  68.174  1.00 28.57 ? 1071 ASN B CG    1 
ATOM   16712 O  OD1   . ASN B 1  1073 ? -2.324  66.833  68.682  1.00 33.37 ? 1071 ASN B OD1   1 
ATOM   16713 N  ND2   . ASN B 1  1073 ? -0.900  67.191  66.980  1.00 30.12 ? 1071 ASN B ND2   1 
ATOM   16714 N  N     . ALA B 1  1074 ? 1.825   65.284  71.357  1.00 20.42 ? 1072 ALA B N     1 
ATOM   16715 C  CA    . ALA B 1  1074 ? 2.697   64.364  72.077  1.00 21.93 ? 1072 ALA B CA    1 
ATOM   16716 C  C     . ALA B 1  1074 ? 2.199   64.135  73.499  1.00 17.04 ? 1072 ALA B C     1 
ATOM   16717 O  O     . ALA B 1  1074 ? 2.233   63.003  74.001  1.00 17.73 ? 1072 ALA B O     1 
ATOM   16718 C  CB    . ALA B 1  1074 ? 4.126   64.903  72.089  1.00 21.01 ? 1072 ALA B CB    1 
ATOM   16719 N  N     . GLY B 1  1075 ? 1.752   65.201  74.168  1.00 18.00 ? 1073 GLY B N     1 
ATOM   16720 C  CA    . GLY B 1  1075 ? 1.223   65.050  75.514  1.00 20.90 ? 1073 GLY B CA    1 
ATOM   16721 C  C     . GLY B 1  1075 ? 0.070   64.065  75.576  1.00 22.51 ? 1073 GLY B C     1 
ATOM   16722 O  O     . GLY B 1  1075 ? -0.033  63.267  76.514  1.00 21.45 ? 1073 GLY B O     1 
ATOM   16723 N  N     . SER B 1  1076 ? -0.794  64.088  74.564  1.00 21.80 ? 1074 SER B N     1 
ATOM   16724 C  CA    . SER B 1  1076 ? -1.953  63.207  74.569  1.00 19.67 ? 1074 SER B CA    1 
ATOM   16725 C  C     . SER B 1  1076 ? -1.589  61.786  74.169  1.00 20.94 ? 1074 SER B C     1 
ATOM   16726 O  O     . SER B 1  1076 ? -2.074  60.828  74.777  1.00 23.32 ? 1074 SER B O     1 
ATOM   16727 C  CB    . SER B 1  1076 ? -3.027  63.755  73.628  1.00 21.69 ? 1074 SER B CB    1 
ATOM   16728 O  OG    . SER B 1  1076 ? -3.670  64.879  74.204  1.00 25.09 ? 1074 SER B OG    1 
ATOM   16729 N  N     . SER B 1  1077 ? -0.742  61.615  73.159  1.00 19.76 ? 1075 SER B N     1 
ATOM   16730 C  CA    . SER B 1  1077 ? -0.498  60.264  72.674  1.00 21.34 ? 1075 SER B CA    1 
ATOM   16731 C  C     . SER B 1  1077 ? 0.544   59.525  73.505  1.00 19.83 ? 1075 SER B C     1 
ATOM   16732 O  O     . SER B 1  1077 ? 0.626   58.293  73.418  1.00 23.94 ? 1075 SER B O     1 
ATOM   16733 C  CB    . SER B 1  1077 ? -0.080  60.291  71.206  1.00 25.13 ? 1075 SER B CB    1 
ATOM   16734 O  OG    . SER B 1  1077 ? 1.229   60.777  71.076  1.00 24.60 ? 1075 SER B OG    1 
ATOM   16735 N  N     . SER B 1  1078 ? 1.324   60.250  74.309  1.00 16.42 ? 1076 SER B N     1 
ATOM   16736 C  CA    . SER B 1  1078 ? 2.201   59.613  75.285  1.00 17.99 ? 1076 SER B CA    1 
ATOM   16737 C  C     . SER B 1  1078 ? 1.415   58.632  76.140  1.00 17.30 ? 1076 SER B C     1 
ATOM   16738 O  O     . SER B 1  1078 ? 0.297   58.926  76.583  1.00 16.88 ? 1076 SER B O     1 
ATOM   16739 C  CB    . SER B 1  1078 ? 2.833   60.669  76.188  1.00 15.84 ? 1076 SER B CB    1 
ATOM   16740 O  OG    . SER B 1  1078 ? 3.542   60.050  77.260  1.00 16.22 ? 1076 SER B OG    1 
ATOM   16741 N  N     . ALA B 1  1079 ? 2.000   57.459  76.375  1.00 15.39 ? 1077 ALA B N     1 
ATOM   16742 C  CA    . ALA B 1  1079 ? 1.384   56.500  77.281  1.00 16.39 ? 1077 ALA B CA    1 
ATOM   16743 C  C     . ALA B 1  1079 ? 2.051   56.505  78.644  1.00 16.09 ? 1077 ALA B C     1 
ATOM   16744 O  O     . ALA B 1  1079 ? 1.850   55.574  79.427  1.00 14.72 ? 1077 ALA B O     1 
ATOM   16745 C  CB    . ALA B 1  1079 ? 1.389   55.092  76.688  1.00 17.66 ? 1077 ALA B CB    1 
ATOM   16746 N  N     . LEU B 1  1080 ? 2.830   57.544  78.944  1.00 15.46 ? 1078 LEU B N     1 
ATOM   16747 C  CA    . LEU B 1  1080 ? 3.377   57.702  80.288  1.00 13.87 ? 1078 LEU B CA    1 
ATOM   16748 C  C     . LEU B 1  1080 ? 2.248   57.668  81.314  1.00 14.41 ? 1078 LEU B C     1 
ATOM   16749 O  O     . LEU B 1  1080 ? 1.256   58.381  81.175  1.00 16.36 ? 1078 LEU B O     1 
ATOM   16750 C  CB    . LEU B 1  1080 ? 4.117   59.031  80.385  1.00 15.09 ? 1078 LEU B CB    1 
ATOM   16751 C  CG    . LEU B 1  1080 ? 4.553   59.444  81.778  1.00 16.33 ? 1078 LEU B CG    1 
ATOM   16752 C  CD1   . LEU B 1  1080 ? 5.752   58.632  82.207  1.00 15.91 ? 1078 LEU B CD1   1 
ATOM   16753 C  CD2   . LEU B 1  1080 ? 4.843   60.942  81.774  1.00 17.69 ? 1078 LEU B CD2   1 
ATOM   16754 N  N     . GLY B 1  1081 ? 2.408   56.847  82.354  1.00 15.13 ? 1079 GLY B N     1 
ATOM   16755 C  CA    . GLY B 1  1081 ? 1.383   56.715  83.375  1.00 17.45 ? 1079 GLY B CA    1 
ATOM   16756 C  C     . GLY B 1  1081 ? 0.464   55.521  83.188  1.00 18.63 ? 1079 GLY B C     1 
ATOM   16757 O  O     . GLY B 1  1081 ? -0.384  55.259  84.064  1.00 18.67 ? 1079 GLY B O     1 
ATOM   16758 N  N     . LEU B 1  1082 ? 0.585   54.816  82.064  1.00 16.09 ? 1080 LEU B N     1 
ATOM   16759 C  CA    A LEU B 1  1082 ? -0.132  53.562  81.884  0.49 17.08 ? 1080 LEU B CA    1 
ATOM   16760 C  CA    B LEU B 1  1082 ? -0.122  53.556  81.879  0.51 17.08 ? 1080 LEU B CA    1 
ATOM   16761 C  C     . LEU B 1  1082 ? 0.120   52.651  83.075  1.00 17.27 ? 1080 LEU B C     1 
ATOM   16762 O  O     . LEU B 1  1082 ? 1.248   52.518  83.547  1.00 16.68 ? 1080 LEU B O     1 
ATOM   16763 C  CB    A LEU B 1  1082 ? 0.313   52.882  80.587  0.49 16.19 ? 1080 LEU B CB    1 
ATOM   16764 C  CB    B LEU B 1  1082 ? 0.350   52.878  80.590  0.51 16.19 ? 1080 LEU B CB    1 
ATOM   16765 C  CG    A LEU B 1  1082 ? -0.343  51.552  80.210  0.49 15.92 ? 1080 LEU B CG    1 
ATOM   16766 C  CG    B LEU B 1  1082 ? -0.232  51.520  80.186  0.51 15.92 ? 1080 LEU B CG    1 
ATOM   16767 C  CD1   A LEU B 1  1082 ? -1.859  51.688  80.174  0.49 17.47 ? 1080 LEU B CD1   1 
ATOM   16768 C  CD1   B LEU B 1  1082 ? -0.149  51.358  78.668  0.51 16.57 ? 1080 LEU B CD1   1 
ATOM   16769 C  CD2   A LEU B 1  1082 ? 0.188   51.047  78.862  0.49 16.86 ? 1080 LEU B CD2   1 
ATOM   16770 C  CD2   B LEU B 1  1082 ? 0.485   50.360  80.880  0.51 16.78 ? 1080 LEU B CD2   1 
ATOM   16771 N  N     . ASP B 1  1083 ? -0.947  52.025  83.565  1.00 16.94 ? 1081 ASP B N     1 
ATOM   16772 C  CA    . ASP B 1  1083 ? -0.832  51.237  84.786  1.00 20.28 ? 1081 ASP B CA    1 
ATOM   16773 C  C     . ASP B 1  1083 ? -1.899  50.152  84.703  1.00 21.00 ? 1081 ASP B C     1 
ATOM   16774 O  O     . ASP B 1  1083 ? -3.066  50.406  85.012  1.00 23.80 ? 1081 ASP B O     1 
ATOM   16775 C  CB    . ASP B 1  1083 ? -1.004  52.135  86.003  1.00 23.67 ? 1081 ASP B CB    1 
ATOM   16776 C  CG    . ASP B 1  1083 ? -0.838  51.399  87.317  1.00 29.78 ? 1081 ASP B CG    1 
ATOM   16777 O  OD1   . ASP B 1  1083 ? -0.273  50.289  87.329  1.00 31.86 ? 1081 ASP B OD1   1 
ATOM   16778 O  OD2   . ASP B 1  1083 ? -1.284  51.949  88.347  1.00 35.96 ? 1081 ASP B OD2   1 
ATOM   16779 N  N     . LEU B 1  1084 ? -1.491  48.964  84.271  1.00 20.01 ? 1082 LEU B N     1 
ATOM   16780 C  CA    . LEU B 1  1084 ? -2.401  47.884  83.922  1.00 18.87 ? 1082 LEU B CA    1 
ATOM   16781 C  C     . LEU B 1  1084 ? -2.128  46.666  84.788  1.00 18.11 ? 1082 LEU B C     1 
ATOM   16782 O  O     . LEU B 1  1084 ? -0.989  46.415  85.192  1.00 17.67 ? 1082 LEU B O     1 
ATOM   16783 C  CB    . LEU B 1  1084 ? -2.244  47.461  82.461  1.00 21.16 ? 1082 LEU B CB    1 
ATOM   16784 C  CG    . LEU B 1  1084 ? -2.622  48.490  81.404  1.00 22.85 ? 1082 LEU B CG    1 
ATOM   16785 C  CD1   . LEU B 1  1084 ? -2.211  47.974  80.047  1.00 23.65 ? 1082 LEU B CD1   1 
ATOM   16786 C  CD2   . LEU B 1  1084 ? -4.111  48.793  81.460  1.00 26.88 ? 1082 LEU B CD2   1 
ATOM   16787 N  N     . GLU B 1  1085 ? -3.184  45.907  85.057  1.00 17.53 ? 1083 GLU B N     1 
ATOM   16788 C  CA    . GLU B 1  1085 ? -3.046  44.550  85.556  1.00 17.17 ? 1083 GLU B CA    1 
ATOM   16789 C  C     . GLU B 1  1085 ? -3.213  43.579  84.394  1.00 16.66 ? 1083 GLU B C     1 
ATOM   16790 O  O     . GLU B 1  1085 ? -4.225  43.625  83.675  1.00 18.00 ? 1083 GLU B O     1 
ATOM   16791 C  CB    . GLU B 1  1085 ? -4.064  44.234  86.652  1.00 17.31 ? 1083 GLU B CB    1 
ATOM   16792 C  CG    . GLU B 1  1085 ? -3.726  42.885  87.274  1.00 19.19 ? 1083 GLU B CG    1 
ATOM   16793 C  CD    . GLU B 1  1085 ? -4.567  42.494  88.469  1.00 22.38 ? 1083 GLU B CD    1 
ATOM   16794 O  OE1   . GLU B 1  1085 ? -5.224  43.367  89.080  1.00 24.90 ? 1083 GLU B OE1   1 
ATOM   16795 O  OE2   . GLU B 1  1085 ? -4.539  41.288  88.801  1.00 23.99 ? 1083 GLU B OE2   1 
ATOM   16796 N  N     . LEU B 1  1086 ? -2.233  42.716  84.212  1.00 16.80 ? 1084 LEU B N     1 
ATOM   16797 C  CA    . LEU B 1  1086 ? -2.237  41.747  83.125  1.00 16.50 ? 1084 LEU B CA    1 
ATOM   16798 C  C     . LEU B 1  1086 ? -2.918  40.451  83.563  1.00 18.81 ? 1084 LEU B C     1 
ATOM   16799 O  O     . LEU B 1  1086 ? -2.802  40.048  84.721  1.00 19.68 ? 1084 LEU B O     1 
ATOM   16800 C  CB    . LEU B 1  1086 ? -0.820  41.447  82.672  1.00 17.89 ? 1084 LEU B CB    1 
ATOM   16801 C  CG    . LEU B 1  1086 ? -0.072  42.682  82.174  1.00 18.30 ? 1084 LEU B CG    1 
ATOM   16802 C  CD1   . LEU B 1  1086 ? 1.306   42.293  81.649  1.00 16.96 ? 1084 LEU B CD1   1 
ATOM   16803 C  CD2   . LEU B 1  1086 ? -0.895  43.371  81.097  1.00 20.16 ? 1084 LEU B CD2   1 
ATOM   16804 N  N     . PRO B 1  1087 ? -3.632  39.791  82.657  1.00 18.64 ? 1085 PRO B N     1 
ATOM   16805 C  CA    . PRO B 1  1087 ? -4.244  38.503  83.004  1.00 19.57 ? 1085 PRO B CA    1 
ATOM   16806 C  C     . PRO B 1  1087 ? -3.177  37.472  83.323  1.00 19.13 ? 1085 PRO B C     1 
ATOM   16807 O  O     . PRO B 1  1087 ? -2.139  37.404  82.664  1.00 21.39 ? 1085 PRO B O     1 
ATOM   16808 C  CB    . PRO B 1  1087 ? -5.026  38.125  81.739  1.00 22.05 ? 1085 PRO B CB    1 
ATOM   16809 C  CG    . PRO B 1  1087 ? -5.273  39.417  81.039  1.00 24.46 ? 1085 PRO B CG    1 
ATOM   16810 C  CD    . PRO B 1  1087 ? -4.107  40.309  81.356  1.00 22.03 ? 1085 PRO B CD    1 
ATOM   16811 N  N     . GLY B 1  1088 ? -3.440  36.674  84.353  1.00 19.43 ? 1086 GLY B N     1 
ATOM   16812 C  CA    . GLY B 1  1088 ? -2.532  35.627  84.746  1.00 18.63 ? 1086 GLY B CA    1 
ATOM   16813 C  C     . GLY B 1  1088 ? -3.165  34.681  85.744  1.00 17.72 ? 1086 GLY B C     1 
ATOM   16814 O  O     . GLY B 1  1088 ? -4.391  34.613  85.883  1.00 17.77 ? 1086 GLY B O     1 
ATOM   16815 N  N     . PRO B 1  1089 ? -2.333  33.943  86.472  1.00 18.04 ? 1087 PRO B N     1 
ATOM   16816 C  CA    . PRO B 1  1089 ? -2.856  32.964  87.433  1.00 18.08 ? 1087 PRO B CA    1 
ATOM   16817 C  C     . PRO B 1  1089 ? -3.490  33.629  88.647  1.00 19.16 ? 1087 PRO B C     1 
ATOM   16818 O  O     . PRO B 1  1089 ? -3.154  34.756  89.019  1.00 19.14 ? 1087 PRO B O     1 
ATOM   16819 C  CB    . PRO B 1  1089 ? -1.605  32.178  87.842  1.00 20.71 ? 1087 PRO B CB    1 
ATOM   16820 C  CG    . PRO B 1  1089 ? -0.505  33.195  87.705  1.00 21.14 ? 1087 PRO B CG    1 
ATOM   16821 C  CD    . PRO B 1  1089 ? -0.862  33.993  86.477  1.00 19.22 ? 1087 PRO B CD    1 
ATOM   16822 N  N     . VAL B 1  1090 ? -4.416  32.901  89.279  1.00 16.51 ? 1088 VAL B N     1 
ATOM   16823 C  CA    . VAL B 1  1090 ? -4.924  33.347  90.567  1.00 15.51 ? 1088 VAL B CA    1 
ATOM   16824 C  C     . VAL B 1  1090 ? -3.785  33.363  91.584  1.00 18.06 ? 1088 VAL B C     1 
ATOM   16825 O  O     . VAL B 1  1090 ? -2.747  32.718  91.407  1.00 18.31 ? 1088 VAL B O     1 
ATOM   16826 C  CB    . VAL B 1  1090 ? -6.067  32.453  91.063  1.00 18.08 ? 1088 VAL B CB    1 
ATOM   16827 C  CG1   . VAL B 1  1090 ? -7.190  32.423  90.039  1.00 19.20 ? 1088 VAL B CG1   1 
ATOM   16828 C  CG2   . VAL B 1  1090 ? -5.546  31.036  91.355  1.00 19.09 ? 1088 VAL B CG2   1 
ATOM   16829 N  N     . GLY B 1  1091 ? -4.000  34.107  92.669  1.00 17.54 ? 1089 GLY B N     1 
ATOM   16830 C  CA    . GLY B 1  1091 ? -3.003  34.202  93.723  1.00 15.57 ? 1089 GLY B CA    1 
ATOM   16831 C  C     . GLY B 1  1091 ? -1.796  35.028  93.365  1.00 17.03 ? 1089 GLY B C     1 
ATOM   16832 O  O     . GLY B 1  1091 ? -0.778  34.961  94.064  1.00 16.98 ? 1089 GLY B O     1 
ATOM   16833 N  N     . GLU B 1  1092 ? -1.885  35.797  92.286  1.00 15.03 ? 1090 GLU B N     1 
ATOM   16834 C  CA    . GLU B 1  1092 ? -0.804  36.636  91.815  1.00 15.37 ? 1090 GLU B CA    1 
ATOM   16835 C  C     . GLU B 1  1092 ? -1.441  37.867  91.197  1.00 17.61 ? 1090 GLU B C     1 
ATOM   16836 O  O     . GLU B 1  1092 ? -2.511  37.770  90.585  1.00 17.89 ? 1090 GLU B O     1 
ATOM   16837 C  CB    . GLU B 1  1092 ? 0.037   35.897  90.769  1.00 19.35 ? 1090 GLU B CB    1 
ATOM   16838 C  CG    . GLU B 1  1092 ? 1.496   35.980  90.958  1.00 21.40 ? 1090 GLU B CG    1 
ATOM   16839 C  CD    . GLU B 1  1092 ? 2.253   35.154  89.930  1.00 19.54 ? 1090 GLU B CD    1 
ATOM   16840 O  OE1   . GLU B 1  1092 ? 2.026   35.358  88.722  1.00 18.58 ? 1090 GLU B OE1   1 
ATOM   16841 O  OE2   . GLU B 1  1092 ? 3.059   34.295  90.341  1.00 22.33 ? 1090 GLU B OE2   1 
ATOM   16842 N  N     . ARG B 1  1093 ? -0.804  39.019  91.376  1.00 15.53 ? 1091 ARG B N     1 
ATOM   16843 C  CA    . ARG B 1  1093 ? -1.179  40.239  90.669  1.00 15.02 ? 1091 ARG B CA    1 
ATOM   16844 C  C     . ARG B 1  1093 ? 0.018   40.662  89.847  1.00 16.49 ? 1091 ARG B C     1 
ATOM   16845 O  O     . ARG B 1  1093 ? 1.113   40.849  90.388  1.00 15.83 ? 1091 ARG B O     1 
ATOM   16846 C  CB    . ARG B 1  1093 ? -1.583  41.379  91.615  1.00 20.05 ? 1091 ARG B CB    1 
ATOM   16847 C  CG    . ARG B 1  1093 ? -2.867  41.187  92.386  1.00 26.95 ? 1091 ARG B CG    1 
ATOM   16848 C  CD    . ARG B 1  1093 ? -3.178  42.440  93.261  1.00 30.11 ? 1091 ARG B CD    1 
ATOM   16849 N  NE    . ARG B 1  1093 ? -3.306  43.670  92.480  1.00 38.39 ? 1091 ARG B NE    1 
ATOM   16850 C  CZ    . ARG B 1  1093 ? -2.633  44.793  92.709  1.00 42.80 ? 1091 ARG B CZ    1 
ATOM   16851 N  NH1   . ARG B 1  1093 ? -1.752  44.885  93.693  1.00 42.99 ? 1091 ARG B NH1   1 
ATOM   16852 N  NH2   . ARG B 1  1093 ? -2.861  45.856  91.940  1.00 41.29 ? 1091 ARG B NH2   1 
ATOM   16853 N  N     . ASN B 1  1094 ? -0.198  40.823  88.551  1.00 14.92 ? 1092 ASN B N     1 
ATOM   16854 C  CA    . ASN B 1  1094 ? 0.880   41.043  87.604  1.00 15.26 ? 1092 ASN B CA    1 
ATOM   16855 C  C     . ASN B 1  1094 ? 0.607   42.379  86.945  1.00 17.04 ? 1092 ASN B C     1 
ATOM   16856 O  O     . ASN B 1  1094 ? -0.398  42.543  86.237  1.00 16.81 ? 1092 ASN B O     1 
ATOM   16857 C  CB    . ASN B 1  1094 ? 0.968   39.882  86.618  1.00 14.37 ? 1092 ASN B CB    1 
ATOM   16858 C  CG    . ASN B 1  1094 ? 1.578   38.659  87.267  1.00 14.30 ? 1092 ASN B CG    1 
ATOM   16859 O  OD1   . ASN B 1  1094 ? 2.763   38.673  87.620  1.00 15.38 ? 1092 ASN B OD1   1 
ATOM   16860 N  ND2   . ASN B 1  1094 ? 0.770   37.632  87.500  1.00 16.55 ? 1092 ASN B ND2   1 
ATOM   16861 N  N     . LEU B 1  1095 ? 1.470   43.341  87.244  1.00 15.06 ? 1093 LEU B N     1 
ATOM   16862 C  CA    . LEU B 1  1095 ? 1.248   44.734  86.921  1.00 14.52 ? 1093 LEU B CA    1 
ATOM   16863 C  C     . LEU B 1  1095 ? 2.241   45.175  85.862  1.00 12.85 ? 1093 LEU B C     1 
ATOM   16864 O  O     . LEU B 1  1095 ? 3.372   44.687  85.803  1.00 15.33 ? 1093 LEU B O     1 
ATOM   16865 C  CB    . LEU B 1  1095 ? 1.391   45.610  88.160  1.00 15.80 ? 1093 LEU B CB    1 
ATOM   16866 C  CG    . LEU B 1  1095 ? 0.495   45.166  89.326  1.00 20.60 ? 1093 LEU B CG    1 
ATOM   16867 C  CD1   . LEU B 1  1095 ? 0.753   46.050  90.557  1.00 23.90 ? 1093 LEU B CD1   1 
ATOM   16868 C  CD2   . LEU B 1  1095 ? -0.974  45.164  88.907  1.00 20.15 ? 1093 LEU B CD2   1 
ATOM   16869 N  N     . TYR B 1  1096 ? 1.802   46.101  85.014  1.00 13.49 ? 1094 TYR B N     1 
ATOM   16870 C  CA    . TYR B 1  1096 ? 2.641   46.577  83.922  1.00 14.25 ? 1094 TYR B CA    1 
ATOM   16871 C  C     . TYR B 1  1096 ? 2.449   48.079  83.838  1.00 14.58 ? 1094 TYR B C     1 
ATOM   16872 O  O     . TYR B 1  1096 ? 1.315   48.550  83.739  1.00 15.90 ? 1094 TYR B O     1 
ATOM   16873 C  CB    . TYR B 1  1096 ? 2.257   45.889  82.610  1.00 14.49 ? 1094 TYR B CB    1 
ATOM   16874 C  CG    . TYR B 1  1096 ? 2.932   46.414  81.368  1.00 12.73 ? 1094 TYR B CG    1 
ATOM   16875 C  CD1   . TYR B 1  1096 ? 4.184   45.947  80.964  1.00 15.04 ? 1094 TYR B CD1   1 
ATOM   16876 C  CD2   . TYR B 1  1096 ? 2.295   47.343  80.575  1.00 15.84 ? 1094 TYR B CD2   1 
ATOM   16877 C  CE1   . TYR B 1  1096 ? 4.774   46.422  79.799  1.00 14.51 ? 1094 TYR B CE1   1 
ATOM   16878 C  CE2   . TYR B 1  1096 ? 2.862   47.806  79.405  1.00 15.58 ? 1094 TYR B CE2   1 
ATOM   16879 C  CZ    . TYR B 1  1096 ? 4.098   47.356  79.030  1.00 13.77 ? 1094 TYR B CZ    1 
ATOM   16880 O  OH    . TYR B 1  1096 ? 4.652   47.833  77.873  1.00 15.28 ? 1094 TYR B OH    1 
ATOM   16881 N  N     . THR B 1  1097 ? 3.542   48.831  83.945  1.00 14.22 ? 1095 THR B N     1 
ATOM   16882 C  CA    . THR B 1  1097 ? 3.429   50.279  84.086  1.00 12.53 ? 1095 THR B CA    1 
ATOM   16883 C  C     . THR B 1  1097 ? 4.457   50.953  83.193  1.00 14.13 ? 1095 THR B C     1 
ATOM   16884 O  O     . THR B 1  1097 ? 5.529   50.406  82.958  1.00 15.46 ? 1095 THR B O     1 
ATOM   16885 C  CB    . THR B 1  1097 ? 3.648   50.734  85.530  1.00 17.57 ? 1095 THR B CB    1 
ATOM   16886 O  OG1   . THR B 1  1097 ? 4.966   50.375  85.940  1.00 20.59 ? 1095 THR B OG1   1 
ATOM   16887 C  CG2   . THR B 1  1097 ? 2.672   50.063  86.467  1.00 18.60 ? 1095 THR B CG2   1 
ATOM   16888 N  N     . LEU B 1  1098 ? 4.117   52.141  82.690  1.00 14.26 ? 1096 LEU B N     1 
ATOM   16889 C  CA    . LEU B 1  1098 ? 5.019   52.908  81.841  1.00 14.42 ? 1096 LEU B CA    1 
ATOM   16890 C  C     . LEU B 1  1098 ? 5.463   54.155  82.588  1.00 16.34 ? 1096 LEU B C     1 
ATOM   16891 O  O     . LEU B 1  1098 ? 4.636   54.987  82.972  1.00 14.21 ? 1096 LEU B O     1 
ATOM   16892 C  CB    . LEU B 1  1098 ? 4.366   53.292  80.515  1.00 15.20 ? 1096 LEU B CB    1 
ATOM   16893 C  CG    . LEU B 1  1098 ? 4.060   52.097  79.611  1.00 13.29 ? 1096 LEU B CG    1 
ATOM   16894 C  CD1   . LEU B 1  1098 ? 3.486   52.596  78.287  1.00 14.92 ? 1096 LEU B CD1   1 
ATOM   16895 C  CD2   . LEU B 1  1098 ? 5.312   51.212  79.394  1.00 13.17 ? 1096 LEU B CD2   1 
ATOM   16896 N  N     . HIS B 1  1099 ? 6.773   54.286  82.762  1.00 16.02 ? 1097 HIS B N     1 
ATOM   16897 C  CA    . HIS B 1  1099 ? 7.406   55.380  83.479  1.00 15.85 ? 1097 HIS B CA    1 
ATOM   16898 C  C     . HIS B 1  1099 ? 8.258   56.183  82.507  1.00 15.36 ? 1097 HIS B C     1 
ATOM   16899 O  O     . HIS B 1  1099 ? 8.509   55.762  81.377  1.00 15.08 ? 1097 HIS B O     1 
ATOM   16900 C  CB    . HIS B 1  1099 ? 8.295   54.839  84.605  1.00 17.01 ? 1097 HIS B CB    1 
ATOM   16901 C  CG    . HIS B 1  1099 ? 7.561   53.994  85.599  1.00 22.00 ? 1097 HIS B CG    1 
ATOM   16902 N  ND1   . HIS B 1  1099 ? 7.199   54.462  86.845  1.00 21.12 ? 1097 HIS B ND1   1 
ATOM   16903 C  CD2   . HIS B 1  1099 ? 7.101   52.720  85.524  1.00 21.10 ? 1097 HIS B CD2   1 
ATOM   16904 C  CE1   . HIS B 1  1099 ? 6.568   53.503  87.504  1.00 23.44 ? 1097 HIS B CE1   1 
ATOM   16905 N  NE2   . HIS B 1  1099 ? 6.489   52.439  86.721  1.00 21.16 ? 1097 HIS B NE2   1 
ATOM   16906 N  N     . ALA B 1  1100 ? 8.747   57.331  82.964  1.00 15.06 ? 1098 ALA B N     1 
ATOM   16907 C  CA    . ALA B 1  1100 ? 9.729   58.047  82.161  1.00 16.69 ? 1098 ALA B CA    1 
ATOM   16908 C  C     . ALA B 1  1100 ? 10.987  57.201  82.034  1.00 17.53 ? 1098 ALA B C     1 
ATOM   16909 O  O     . ALA B 1  1100 ? 11.282  56.369  82.895  1.00 18.19 ? 1098 ALA B O     1 
ATOM   16910 C  CB    . ALA B 1  1100 ? 10.052  59.398  82.790  1.00 16.92 ? 1098 ALA B CB    1 
ATOM   16911 N  N     . ARG B 1  1101 ? 11.715  57.383  80.925  1.00 16.45 ? 1099 ARG B N     1 
ATOM   16912 C  CA    . ARG B 1  1101 ? 12.993  56.684  80.777  1.00 17.00 ? 1099 ARG B CA    1 
ATOM   16913 C  C     . ARG B 1  1101 ? 14.064  57.271  81.692  1.00 16.35 ? 1099 ARG B C     1 
ATOM   16914 O  O     . ARG B 1  1101 ? 14.907  56.534  82.229  1.00 17.25 ? 1099 ARG B O     1 
ATOM   16915 C  CB    . ARG B 1  1101 ? 13.467  56.725  79.324  1.00 18.72 ? 1099 ARG B CB    1 
ATOM   16916 C  CG    . ARG B 1  1101 ? 12.835  55.663  78.408  1.00 19.43 ? 1099 ARG B CG    1 
ATOM   16917 C  CD    . ARG B 1  1101 ? 13.745  54.453  78.245  1.00 21.87 ? 1099 ARG B CD    1 
ATOM   16918 N  NE    . ARG B 1  1101 ? 13.134  53.422  77.406  1.00 20.24 ? 1099 ARG B NE    1 
ATOM   16919 C  CZ    . ARG B 1  1101 ? 13.816  52.515  76.720  1.00 19.86 ? 1099 ARG B CZ    1 
ATOM   16920 N  NH1   . ARG B 1  1101 ? 15.138  52.453  76.774  1.00 19.58 ? 1099 ARG B NH1   1 
ATOM   16921 N  NH2   . ARG B 1  1101 ? 13.155  51.654  75.951  1.00 24.17 ? 1099 ARG B NH2   1 
ATOM   16922 N  N     . GLY B 1  1102 ? 14.058  58.587  81.874  1.00 16.25 ? 1100 GLY B N     1 
ATOM   16923 C  CA    . GLY B 1  1102 ? 15.113  59.245  82.617  1.00 19.59 ? 1100 GLY B CA    1 
ATOM   16924 C  C     . GLY B 1  1102 ? 15.547  60.531  81.940  1.00 19.87 ? 1100 GLY B C     1 
ATOM   16925 O  O     . GLY B 1  1102 ? 14.718  61.394  81.641  1.00 18.32 ? 1100 GLY B O     1 
ATOM   16926 N  N     . ARG B 1  1103 ? 16.842  60.686  81.686  1.00 18.10 ? 1101 ARG B N     1 
ATOM   16927 C  CA    . ARG B 1  1103 ? 17.335  61.864  80.988  1.00 18.20 ? 1101 ARG B CA    1 
ATOM   16928 C  C     . ARG B 1  1103 ? 17.680  61.468  79.561  1.00 17.96 ? 1101 ARG B C     1 
ATOM   16929 O  O     . ARG B 1  1103 ? 18.426  60.508  79.341  1.00 18.58 ? 1101 ARG B O     1 
ATOM   16930 C  CB    . ARG B 1  1103 ? 18.562  62.474  81.683  1.00 20.02 ? 1101 ARG B CB    1 
ATOM   16931 C  CG    . ARG B 1  1103 ? 18.958  63.839  81.074  1.00 21.90 ? 1101 ARG B CG    1 
ATOM   16932 C  CD    . ARG B 1  1103 ? 19.981  64.627  81.917  1.00 25.34 ? 1101 ARG B CD    1 
ATOM   16933 N  NE    . ARG B 1  1103 ? 19.553  64.857  83.295  1.00 30.84 ? 1101 ARG B NE    1 
ATOM   16934 C  CZ    . ARG B 1  1103 ? 18.981  65.967  83.747  1.00 33.31 ? 1101 ARG B CZ    1 
ATOM   16935 N  NH1   . ARG B 1  1103 ? 18.699  66.992  82.940  1.00 25.64 ? 1101 ARG B NH1   1 
ATOM   16936 N  NH2   . ARG B 1  1103 ? 18.683  66.055  85.043  1.00 30.21 ? 1101 ARG B NH2   1 
ATOM   16937 N  N     . ILE B 1  1104 ? 17.112  62.185  78.594  1.00 16.12 ? 1102 ILE B N     1 
ATOM   16938 C  CA    . ILE B 1  1104 ? 17.295  61.870  77.183  1.00 15.59 ? 1102 ILE B CA    1 
ATOM   16939 C  C     . ILE B 1  1104 ? 18.312  62.837  76.600  1.00 17.05 ? 1102 ILE B C     1 
ATOM   16940 O  O     . ILE B 1  1104 ? 18.189  64.055  76.767  1.00 17.85 ? 1102 ILE B O     1 
ATOM   16941 C  CB    . ILE B 1  1104 ? 15.966  61.954  76.416  1.00 16.44 ? 1102 ILE B CB    1 
ATOM   16942 C  CG1   . ILE B 1  1104 ? 14.883  61.114  77.112  1.00 14.88 ? 1102 ILE B CG1   1 
ATOM   16943 C  CG2   . ILE B 1  1104 ? 16.166  61.521  74.950  1.00 15.13 ? 1102 ILE B CG2   1 
ATOM   16944 C  CD1   . ILE B 1  1104 ? 15.207  59.638  77.160  1.00 16.66 ? 1102 ILE B CD1   1 
ATOM   16945 N  N     . LEU B 1  1105 ? 19.316  62.299  75.921  1.00 15.81 ? 1103 LEU B N     1 
ATOM   16946 C  CA    . LEU B 1  1105 ? 20.254  63.137  75.184  1.00 18.87 ? 1103 LEU B CA    1 
ATOM   16947 C  C     . LEU B 1  1105 ? 19.577  63.691  73.934  1.00 17.88 ? 1103 LEU B C     1 
ATOM   16948 O  O     . LEU B 1  1105 ? 19.084  62.931  73.101  1.00 15.75 ? 1103 LEU B O     1 
ATOM   16949 C  CB    . LEU B 1  1105 ? 21.484  62.318  74.805  1.00 16.83 ? 1103 LEU B CB    1 
ATOM   16950 C  CG    . LEU B 1  1105 ? 22.506  63.031  73.925  1.00 19.55 ? 1103 LEU B CG    1 
ATOM   16951 C  CD1   . LEU B 1  1105 ? 23.136  64.204  74.692  1.00 17.40 ? 1103 LEU B CD1   1 
ATOM   16952 C  CD2   . LEU B 1  1105 ? 23.554  62.016  73.482  1.00 19.41 ? 1103 LEU B CD2   1 
ATOM   16953 N  N     . LEU B 1  1106 ? 19.566  65.009  73.791  1.00 16.64 ? 1104 LEU B N     1 
ATOM   16954 C  CA    . LEU B 1  1106 ? 18.970  65.663  72.636  1.00 17.17 ? 1104 LEU B CA    1 
ATOM   16955 C  C     . LEU B 1  1106 ? 20.097  66.208  71.776  1.00 17.33 ? 1104 LEU B C     1 
ATOM   16956 O  O     . LEU B 1  1106 ? 20.931  66.972  72.265  1.00 18.52 ? 1104 LEU B O     1 
ATOM   16957 C  CB    . LEU B 1  1106 ? 18.029  66.789  73.057  1.00 17.29 ? 1104 LEU B CB    1 
ATOM   16958 C  CG    . LEU B 1  1106 ? 16.551  66.414  73.102  1.00 21.60 ? 1104 LEU B CG    1 
ATOM   16959 C  CD1   . LEU B 1  1106 ? 16.326  65.057  73.742  1.00 21.89 ? 1104 LEU B CD1   1 
ATOM   16960 C  CD2   . LEU B 1  1106 ? 15.752  67.516  73.789  1.00 18.04 ? 1104 LEU B CD2   1 
ATOM   16961 N  N     . VAL B 1  1107 ? 20.117  65.807  70.510  1.00 16.57 ? 1105 VAL B N     1 
ATOM   16962 C  CA    . VAL B 1  1107 ? 21.107  66.296  69.553  1.00 18.36 ? 1105 VAL B CA    1 
ATOM   16963 C  C     . VAL B 1  1107 ? 20.355  66.991  68.424  1.00 17.46 ? 1105 VAL B C     1 
ATOM   16964 O  O     . VAL B 1  1107 ? 20.150  66.399  67.353  1.00 18.35 ? 1105 VAL B O     1 
ATOM   16965 C  CB    . VAL B 1  1107 ? 21.997  65.152  69.038  1.00 17.66 ? 1105 VAL B CB    1 
ATOM   16966 C  CG1   . VAL B 1  1107 ? 23.175  65.714  68.230  1.00 20.11 ? 1105 VAL B CG1   1 
ATOM   16967 C  CG2   . VAL B 1  1107 ? 22.506  64.296  70.202  1.00 17.49 ? 1105 VAL B CG2   1 
ATOM   16968 N  N     . PRO B 1  1108 ? 19.919  68.235  68.616  1.00 17.81 ? 1106 PRO B N     1 
ATOM   16969 C  CA    . PRO B 1  1108 ? 19.185  68.934  67.563  1.00 21.43 ? 1106 PRO B CA    1 
ATOM   16970 C  C     . PRO B 1  1108 ? 20.125  69.569  66.551  1.00 20.88 ? 1106 PRO B C     1 
ATOM   16971 O  O     . PRO B 1  1108 ? 21.317  69.752  66.792  1.00 23.09 ? 1106 PRO B O     1 
ATOM   16972 C  CB    . PRO B 1  1108 ? 18.433  70.020  68.337  1.00 18.18 ? 1106 PRO B CB    1 
ATOM   16973 C  CG    . PRO B 1  1108 ? 19.392  70.356  69.449  1.00 18.33 ? 1106 PRO B CG    1 
ATOM   16974 C  CD    . PRO B 1  1108 ? 19.972  69.027  69.858  1.00 17.65 ? 1106 PRO B CD    1 
ATOM   16975 N  N     . ALA B 1  1109 ? 19.551  69.925  65.411  1.00 21.35 ? 1107 ALA B N     1 
ATOM   16976 C  CA    . ALA B 1  1109 ? 20.232  70.753  64.426  1.00 25.02 ? 1107 ALA B CA    1 
ATOM   16977 C  C     . ALA B 1  1109 ? 19.584  72.117  64.264  1.00 23.35 ? 1107 ALA B C     1 
ATOM   16978 O  O     . ALA B 1  1109 ? 20.283  73.115  64.058  1.00 23.51 ? 1107 ALA B O     1 
ATOM   16979 C  CB    . ALA B 1  1109 ? 20.267  70.034  63.070  1.00 22.93 ? 1107 ALA B CB    1 
ATOM   16980 N  N     . THR B 1  1110 ? 18.258  72.185  64.373  1.00 22.37 ? 1108 THR B N     1 
ATOM   16981 C  CA    . THR B 1  1110 ? 17.504  73.413  64.179  1.00 23.43 ? 1108 THR B CA    1 
ATOM   16982 C  C     . THR B 1  1110 ? 16.653  73.718  65.406  1.00 24.05 ? 1108 THR B C     1 
ATOM   16983 O  O     . THR B 1  1110 ? 16.381  72.848  66.239  1.00 21.32 ? 1108 THR B O     1 
ATOM   16984 C  CB    . THR B 1  1110 ? 16.583  73.320  62.957  1.00 25.95 ? 1108 THR B CB    1 
ATOM   16985 O  OG1   . THR B 1  1110 ? 15.597  72.299  63.175  1.00 24.11 ? 1108 THR B OG1   1 
ATOM   16986 C  CG2   . THR B 1  1110 ? 17.376  73.002  61.694  1.00 26.76 ? 1108 THR B CG2   1 
ATOM   16987 N  N     . GLU B 1  1111 ? 16.213  74.974  65.488  1.00 24.11 ? 1109 GLU B N     1 
ATOM   16988 C  CA    . GLU B 1  1111 ? 15.354  75.385  66.596  1.00 23.55 ? 1109 GLU B CA    1 
ATOM   16989 C  C     . GLU B 1  1111 ? 14.052  74.590  66.612  1.00 22.51 ? 1109 GLU B C     1 
ATOM   16990 O  O     . GLU B 1  1111 ? 13.642  74.069  67.659  1.00 23.08 ? 1109 GLU B O     1 
ATOM   16991 C  CB    . GLU B 1  1111 ? 15.073  76.882  66.503  1.00 25.12 ? 1109 GLU B CB    1 
ATOM   16992 C  CG    . GLU B 1  1111 ? 13.971  77.357  67.439  1.00 26.61 ? 1109 GLU B CG    1 
ATOM   16993 C  CD    . GLU B 1  1111 ? 13.813  78.866  67.429  1.00 25.54 ? 1109 GLU B CD    1 
ATOM   16994 O  OE1   . GLU B 1  1111 ? 14.653  79.553  68.047  1.00 26.84 ? 1109 GLU B OE1   1 
ATOM   16995 O  OE2   . GLU B 1  1111 ? 12.852  79.355  66.807  1.00 29.99 ? 1109 GLU B OE2   1 
ATOM   16996 N  N     . SER B 1  1112 ? 13.386  74.484  65.457  1.00 23.28 ? 1110 SER B N     1 
ATOM   16997 C  CA    . SER B 1  1112 ? 12.144  73.717  65.397  1.00 23.92 ? 1110 SER B CA    1 
ATOM   16998 C  C     . SER B 1  1112 ? 12.379  72.259  65.764  1.00 24.71 ? 1110 SER B C     1 
ATOM   16999 O  O     . SER B 1  1112 ? 11.569  71.649  66.474  1.00 23.05 ? 1110 SER B O     1 
ATOM   17000 C  CB    . SER B 1  1112 ? 11.518  73.815  64.008  1.00 27.96 ? 1110 SER B CB    1 
ATOM   17001 O  OG    . SER B 1  1112 ? 10.297  73.089  63.964  1.00 27.32 ? 1110 SER B OG    1 
ATOM   17002 N  N     . GLY B 1  1113 ? 13.483  71.681  65.284  1.00 21.12 ? 1111 GLY B N     1 
ATOM   17003 C  CA    . GLY B 1  1113 ? 13.811  70.317  65.658  1.00 22.01 ? 1111 GLY B CA    1 
ATOM   17004 C  C     . GLY B 1  1113 ? 13.982  70.161  67.156  1.00 18.58 ? 1111 GLY B C     1 
ATOM   17005 O  O     . GLY B 1  1113 ? 13.522  69.178  67.743  1.00 20.07 ? 1111 GLY B O     1 
ATOM   17006 N  N     . LEU B 1  1114 ? 14.636  71.134  67.797  1.00 20.00 ? 1112 LEU B N     1 
ATOM   17007 C  CA    . LEU B 1  1114 ? 14.807  71.077  69.246  1.00 20.78 ? 1112 LEU B CA    1 
ATOM   17008 C  C     . LEU B 1  1114 ? 13.463  71.130  69.961  1.00 20.65 ? 1112 LEU B C     1 
ATOM   17009 O  O     . LEU B 1  1114 ? 13.234  70.385  70.920  1.00 18.57 ? 1112 LEU B O     1 
ATOM   17010 C  CB    . LEU B 1  1114 ? 15.702  72.222  69.727  1.00 20.81 ? 1112 LEU B CB    1 
ATOM   17011 C  CG    . LEU B 1  1114 ? 15.795  72.405  71.247  1.00 20.90 ? 1112 LEU B CG    1 
ATOM   17012 C  CD1   . LEU B 1  1114 ? 16.328  71.138  71.934  1.00 18.51 ? 1112 LEU B CD1   1 
ATOM   17013 C  CD2   . LEU B 1  1114 ? 16.637  73.632  71.624  1.00 24.90 ? 1112 LEU B CD2   1 
ATOM   17014 N  N     . TYR B 1  1115 ? 12.576  72.022  69.523  1.00 21.35 ? 1113 TYR B N     1 
ATOM   17015 C  CA    . TYR B 1  1115 ? 11.250  72.095  70.132  1.00 20.79 ? 1113 TYR B CA    1 
ATOM   17016 C  C     . TYR B 1  1115 ? 10.508  70.772  69.995  1.00 19.84 ? 1113 TYR B C     1 
ATOM   17017 O  O     . TYR B 1  1115 ? 9.861   70.317  70.946  1.00 20.69 ? 1113 TYR B O     1 
ATOM   17018 C  CB    . TYR B 1  1115 ? 10.425  73.216  69.499  1.00 21.86 ? 1113 TYR B CB    1 
ATOM   17019 C  CG    . TYR B 1  1115 ? 10.932  74.622  69.754  1.00 22.81 ? 1113 TYR B CG    1 
ATOM   17020 C  CD1   . TYR B 1  1115 ? 11.887  74.883  70.734  1.00 23.13 ? 1113 TYR B CD1   1 
ATOM   17021 C  CD2   . TYR B 1  1115 ? 10.441  75.689  69.021  1.00 25.24 ? 1113 TYR B CD2   1 
ATOM   17022 C  CE1   . TYR B 1  1115 ? 12.340  76.177  70.961  1.00 26.40 ? 1113 TYR B CE1   1 
ATOM   17023 C  CE2   . TYR B 1  1115 ? 10.878  76.976  69.249  1.00 24.67 ? 1113 TYR B CE2   1 
ATOM   17024 C  CZ    . TYR B 1  1115 ? 11.830  77.216  70.215  1.00 30.02 ? 1113 TYR B CZ    1 
ATOM   17025 O  OH    . TYR B 1  1115 ? 12.277  78.507  70.423  1.00 30.00 ? 1113 TYR B OH    1 
ATOM   17026 N  N     . HIS B 1  1116 ? 10.576  70.151  68.815  1.00 18.30 ? 1114 HIS B N     1 
ATOM   17027 C  CA    . HIS B 1  1116 ? 9.929   68.855  68.623  1.00 19.11 ? 1114 HIS B CA    1 
ATOM   17028 C  C     . HIS B 1  1116 ? 10.574  67.784  69.490  1.00 20.74 ? 1114 HIS B C     1 
ATOM   17029 O  O     . HIS B 1  1116 ? 9.871   66.941  70.060  1.00 20.34 ? 1114 HIS B O     1 
ATOM   17030 C  CB    . HIS B 1  1116 ? 9.970   68.439  67.153  1.00 18.73 ? 1114 HIS B CB    1 
ATOM   17031 C  CG    . HIS B 1  1116 ? 8.904   69.073  66.306  1.00 22.67 ? 1114 HIS B CG    1 
ATOM   17032 N  ND1   . HIS B 1  1116 ? 9.057   70.308  65.711  1.00 24.43 ? 1114 HIS B ND1   1 
ATOM   17033 C  CD2   . HIS B 1  1116 ? 7.676   68.631  65.943  1.00 24.65 ? 1114 HIS B CD2   1 
ATOM   17034 C  CE1   . HIS B 1  1116 ? 7.965   70.603  65.025  1.00 25.52 ? 1114 HIS B CE1   1 
ATOM   17035 N  NE2   . HIS B 1  1116 ? 7.114   69.601  65.146  1.00 24.82 ? 1114 HIS B NE2   1 
ATOM   17036 N  N     . GLN B 1  1117 ? 11.913  67.786  69.596  1.00 17.11 ? 1115 GLN B N     1 
ATOM   17037 C  CA    . GLN B 1  1117 ? 12.568  66.816  70.472  1.00 15.43 ? 1115 GLN B CA    1 
ATOM   17038 C  C     . GLN B 1  1117 ? 12.152  67.018  71.918  1.00 17.17 ? 1115 GLN B C     1 
ATOM   17039 O  O     . GLN B 1  1117 ? 11.875  66.046  72.637  1.00 17.54 ? 1115 GLN B O     1 
ATOM   17040 C  CB    . GLN B 1  1117 ? 14.090  66.918  70.345  1.00 17.29 ? 1115 GLN B CB    1 
ATOM   17041 C  CG    . GLN B 1  1117 ? 14.623  66.421  69.018  1.00 17.58 ? 1115 GLN B CG    1 
ATOM   17042 C  CD    . GLN B 1  1117 ? 16.125  66.606  68.905  1.00 16.68 ? 1115 GLN B CD    1 
ATOM   17043 O  OE1   . GLN B 1  1117 ? 16.722  67.318  69.710  1.00 18.56 ? 1115 GLN B OE1   1 
ATOM   17044 N  NE2   . GLN B 1  1117 ? 16.740  65.958  67.917  1.00 17.94 ? 1115 GLN B NE2   1 
ATOM   17045 N  N     . LEU B 1  1118 ? 12.130  68.275  72.369  1.00 15.86 ? 1116 LEU B N     1 
ATOM   17046 C  CA    . LEU B 1  1118 ? 11.718  68.579  73.734  1.00 17.18 ? 1116 LEU B CA    1 
ATOM   17047 C  C     . LEU B 1  1118 ? 10.290  68.127  73.983  1.00 17.76 ? 1116 LEU B C     1 
ATOM   17048 O  O     . LEU B 1  1118 ? 9.993   67.541  75.027  1.00 18.57 ? 1116 LEU B O     1 
ATOM   17049 C  CB    . LEU B 1  1118 ? 11.838  70.078  74.007  1.00 18.48 ? 1116 LEU B CB    1 
ATOM   17050 C  CG    . LEU B 1  1118 ? 13.240  70.607  74.258  1.00 25.06 ? 1116 LEU B CG    1 
ATOM   17051 C  CD1   . LEU B 1  1118 ? 13.209  72.133  74.271  1.00 24.05 ? 1116 LEU B CD1   1 
ATOM   17052 C  CD2   . LEU B 1  1118 ? 13.771  70.051  75.577  1.00 23.63 ? 1116 LEU B CD2   1 
ATOM   17053 N  N     . ALA B 1  1119 ? 9.398   68.374  73.024  1.00 19.10 ? 1117 ALA B N     1 
ATOM   17054 C  CA    . ALA B 1  1119 ? 8.009   67.950  73.190  1.00 16.84 ? 1117 ALA B CA    1 
ATOM   17055 C  C     . ALA B 1  1119 ? 7.928   66.445  73.404  1.00 18.87 ? 1117 ALA B C     1 
ATOM   17056 O  O     . ALA B 1  1119 ? 7.261   65.977  74.335  1.00 19.12 ? 1117 ALA B O     1 
ATOM   17057 C  CB    . ALA B 1  1119 ? 7.175   68.357  71.976  1.00 18.07 ? 1117 ALA B CB    1 
ATOM   17058 N  N     . ALA B 1  1120 ? 8.611   65.674  72.552  1.00 18.25 ? 1118 ALA B N     1 
ATOM   17059 C  CA    . ALA B 1  1120 ? 8.579   64.218  72.668  1.00 15.14 ? 1118 ALA B CA    1 
ATOM   17060 C  C     . ALA B 1  1120 ? 9.126   63.759  74.014  1.00 18.31 ? 1118 ALA B C     1 
ATOM   17061 O  O     . ALA B 1  1120 ? 8.524   62.914  74.689  1.00 16.47 ? 1118 ALA B O     1 
ATOM   17062 C  CB    . ALA B 1  1120 ? 9.378   63.577  71.531  1.00 19.84 ? 1118 ALA B CB    1 
ATOM   17063 N  N     . ALA B 1  1121 ? 10.267  64.318  74.430  1.00 16.10 ? 1119 ALA B N     1 
ATOM   17064 C  CA    . ALA B 1  1121 ? 10.881  63.904  75.687  1.00 15.90 ? 1119 ALA B CA    1 
ATOM   17065 C  C     . ALA B 1  1121 ? 10.068  64.348  76.902  1.00 14.97 ? 1119 ALA B C     1 
ATOM   17066 O  O     . ALA B 1  1121 ? 9.933   63.590  77.872  1.00 16.75 ? 1119 ALA B O     1 
ATOM   17067 C  CB    . ALA B 1  1121 ? 12.296  64.465  75.771  1.00 17.29 ? 1119 ALA B CB    1 
ATOM   17068 N  N     . LEU B 1  1122 ? 9.570   65.583  76.897  1.00 15.78 ? 1120 LEU B N     1 
ATOM   17069 C  CA    . LEU B 1  1122 ? 8.811   66.055  78.049  1.00 17.82 ? 1120 LEU B CA    1 
ATOM   17070 C  C     . LEU B 1  1122 ? 7.491   65.309  78.170  1.00 16.82 ? 1120 LEU B C     1 
ATOM   17071 O  O     . LEU B 1  1122 ? 7.063   64.979  79.281  1.00 15.72 ? 1120 LEU B O     1 
ATOM   17072 C  CB    . LEU B 1  1122 ? 8.564   67.559  77.953  1.00 18.41 ? 1120 LEU B CB    1 
ATOM   17073 C  CG    . LEU B 1  1122 ? 9.799   68.458  78.042  1.00 20.25 ? 1120 LEU B CG    1 
ATOM   17074 C  CD1   . LEU B 1  1122 ? 9.403   69.908  77.832  1.00 21.24 ? 1120 LEU B CD1   1 
ATOM   17075 C  CD2   . LEU B 1  1122 ? 10.525  68.273  79.380  1.00 19.53 ? 1120 LEU B CD2   1 
ATOM   17076 N  N     . ALA B 1  1123 ? 6.847   65.027  77.035  1.00 16.73 ? 1121 ALA B N     1 
ATOM   17077 C  CA    . ALA B 1  1123 ? 5.544   64.362  77.048  1.00 17.13 ? 1121 ALA B CA    1 
ATOM   17078 C  C     . ALA B 1  1123 ? 5.622   62.979  77.676  1.00 18.58 ? 1121 ALA B C     1 
ATOM   17079 O  O     . ALA B 1  1123 ? 4.617   62.465  78.198  1.00 16.18 ? 1121 ALA B O     1 
ATOM   17080 C  CB    . ALA B 1  1123 ? 5.009   64.250  75.622  1.00 16.30 ? 1121 ALA B CB    1 
ATOM   17081 N  N     . THR B 1  1124 ? 6.797   62.358  77.622  1.00 15.85 ? 1122 THR B N     1 
ATOM   17082 C  CA    . THR B 1  1124 ? 7.025   61.046  78.189  1.00 14.75 ? 1122 THR B CA    1 
ATOM   17083 C  C     . THR B 1  1124 ? 7.712   61.125  79.552  1.00 14.52 ? 1122 THR B C     1 
ATOM   17084 O  O     . THR B 1  1124 ? 8.218   60.116  80.041  1.00 16.20 ? 1122 THR B O     1 
ATOM   17085 C  CB    . THR B 1  1124 ? 7.824   60.187  77.196  1.00 14.86 ? 1122 THR B CB    1 
ATOM   17086 O  OG1   . THR B 1  1124 ? 8.875   60.973  76.604  1.00 15.44 ? 1122 THR B OG1   1 
ATOM   17087 C  CG2   . THR B 1  1124 ? 6.906   59.694  76.068  1.00 15.84 ? 1122 THR B CG2   1 
ATOM   17088 N  N     . GLY B 1  1125 ? 7.718   62.303  80.175  1.00 15.18 ? 1123 GLY B N     1 
ATOM   17089 C  CA    . GLY B 1  1125 ? 8.134   62.458  81.562  1.00 14.09 ? 1123 GLY B CA    1 
ATOM   17090 C  C     . GLY B 1  1125 ? 9.615   62.624  81.780  1.00 14.59 ? 1123 GLY B C     1 
ATOM   17091 O  O     . GLY B 1  1125 ? 10.054  62.651  82.937  1.00 16.02 ? 1123 GLY B O     1 
ATOM   17092 N  N     . ASN B 1  1126 ? 10.392  62.759  80.715  1.00 15.62 ? 1124 ASN B N     1 
ATOM   17093 C  CA    . ASN B 1  1126 ? 11.842  62.738  80.812  1.00 14.13 ? 1124 ASN B CA    1 
ATOM   17094 C  C     . ASN B 1  1126 ? 12.401  64.130  81.060  1.00 15.72 ? 1124 ASN B C     1 
ATOM   17095 O  O     . ASN B 1  1126 ? 11.770  65.145  80.767  1.00 17.69 ? 1124 ASN B O     1 
ATOM   17096 C  CB    . ASN B 1  1126 ? 12.448  62.180  79.528  1.00 16.12 ? 1124 ASN B CB    1 
ATOM   17097 C  CG    . ASN B 1  1126 ? 11.979  60.775  79.233  1.00 13.60 ? 1124 ASN B CG    1 
ATOM   17098 O  OD1   . ASN B 1  1126 ? 12.337  59.833  79.936  1.00 16.33 ? 1124 ASN B OD1   1 
ATOM   17099 N  ND2   . ASN B 1  1126 ? 11.195  60.622  78.171  1.00 14.37 ? 1124 ASN B ND2   1 
ATOM   17100 N  N     . SER B 1  1127 ? 13.616  64.158  81.609  1.00 17.09 ? 1125 SER B N     1 
ATOM   17101 C  CA    . SER B 1  1127 ? 14.453  65.341  81.519  1.00 16.76 ? 1125 SER B CA    1 
ATOM   17102 C  C     . SER B 1  1127 ? 15.335  65.204  80.280  1.00 18.17 ? 1125 SER B C     1 
ATOM   17103 O  O     . SER B 1  1127 ? 15.359  64.162  79.627  1.00 17.94 ? 1125 SER B O     1 
ATOM   17104 C  CB    . SER B 1  1127 ? 15.303  65.499  82.778  1.00 18.62 ? 1125 SER B CB    1 
ATOM   17105 O  OG    . SER B 1  1127 ? 16.071  64.333  83.005  1.00 22.19 ? 1125 SER B OG    1 
ATOM   17106 N  N     . VAL B 1  1128 ? 16.067  66.266  79.952  1.00 18.16 ? 1126 VAL B N     1 
ATOM   17107 C  CA    . VAL B 1  1128 ? 16.878  66.242  78.742  1.00 17.76 ? 1126 VAL B CA    1 
ATOM   17108 C  C     . VAL B 1  1128 ? 18.244  66.846  79.012  1.00 19.12 ? 1126 VAL B C     1 
ATOM   17109 O  O     . VAL B 1  1128 ? 18.412  67.712  79.879  1.00 20.65 ? 1126 VAL B O     1 
ATOM   17110 C  CB    . VAL B 1  1128 ? 16.203  66.982  77.564  1.00 17.72 ? 1126 VAL B CB    1 
ATOM   17111 C  CG1   . VAL B 1  1128 ? 14.857  66.341  77.213  1.00 16.55 ? 1126 VAL B CG1   1 
ATOM   17112 C  CG2   . VAL B 1  1128 ? 16.029  68.463  77.879  1.00 19.57 ? 1126 VAL B CG2   1 
ATOM   17113 N  N     . ALA B 1  1129 ? 19.227  66.366  78.255  1.00 17.98 ? 1127 ALA B N     1 
ATOM   17114 C  CA    . ALA B 1  1129 ? 20.508  67.039  78.103  1.00 18.44 ? 1127 ALA B CA    1 
ATOM   17115 C  C     . ALA B 1  1129 ? 20.646  67.401  76.633  1.00 18.16 ? 1127 ALA B C     1 
ATOM   17116 O  O     . ALA B 1  1129 ? 20.612  66.514  75.771  1.00 18.46 ? 1127 ALA B O     1 
ATOM   17117 C  CB    . ALA B 1  1129 ? 21.656  66.143  78.564  1.00 18.47 ? 1127 ALA B CB    1 
ATOM   17118 N  N     . ILE B 1  1130 ? 20.742  68.694  76.344  1.00 17.93 ? 1128 ILE B N     1 
ATOM   17119 C  CA    . ILE B 1  1130 ? 20.785  69.188  74.976  1.00 17.38 ? 1128 ILE B CA    1 
ATOM   17120 C  C     . ILE B 1  1130 ? 22.237  69.414  74.597  1.00 18.27 ? 1128 ILE B C     1 
ATOM   17121 O  O     . ILE B 1  1130 ? 23.000  70.024  75.359  1.00 18.38 ? 1128 ILE B O     1 
ATOM   17122 C  CB    . ILE B 1  1130 ? 19.984  70.486  74.800  1.00 19.18 ? 1128 ILE B CB    1 
ATOM   17123 C  CG1   . ILE B 1  1130 ? 18.569  70.357  75.390  1.00 21.59 ? 1128 ILE B CG1   1 
ATOM   17124 C  CG2   . ILE B 1  1130 ? 19.902  70.829  73.320  1.00 18.53 ? 1128 ILE B CG2   1 
ATOM   17125 C  CD1   . ILE B 1  1130 ? 17.847  71.694  75.489  1.00 19.38 ? 1128 ILE B CD1   1 
ATOM   17126 N  N     . ASP B 1  1131 ? 22.609  68.940  73.415  1.00 17.07 ? 1129 ASP B N     1 
ATOM   17127 C  CA    . ASP B 1  1131 ? 23.962  69.119  72.899  1.00 17.23 ? 1129 ASP B CA    1 
ATOM   17128 C  C     . ASP B 1  1131 ? 24.297  70.597  72.745  1.00 18.51 ? 1129 ASP B C     1 
ATOM   17129 O  O     . ASP B 1  1131 ? 23.709  71.291  71.907  1.00 21.12 ? 1129 ASP B O     1 
ATOM   17130 C  CB    . ASP B 1  1131 ? 24.092  68.397  71.563  1.00 18.59 ? 1129 ASP B CB    1 
ATOM   17131 C  CG    . ASP B 1  1131 ? 25.441  68.603  70.917  1.00 19.43 ? 1129 ASP B CG    1 
ATOM   17132 O  OD1   . ASP B 1  1131 ? 26.443  68.702  71.662  1.00 18.73 ? 1129 ASP B OD1   1 
ATOM   17133 O  OD2   . ASP B 1  1131 ? 25.471  68.683  69.672  1.00 20.65 ? 1129 ASP B OD2   1 
ATOM   17134 N  N     . ALA B 1  1132 ? 25.242  71.086  73.553  1.00 20.61 ? 1130 ALA B N     1 
ATOM   17135 C  CA    . ALA B 1  1132 ? 25.614  72.496  73.481  1.00 19.39 ? 1130 ALA B CA    1 
ATOM   17136 C  C     . ALA B 1  1132 ? 26.198  72.857  72.123  1.00 22.52 ? 1130 ALA B C     1 
ATOM   17137 O  O     . ALA B 1  1132 ? 26.062  74.003  71.677  1.00 23.10 ? 1130 ALA B O     1 
ATOM   17138 C  CB    . ALA B 1  1132 ? 26.603  72.839  74.596  1.00 20.54 ? 1130 ALA B CB    1 
ATOM   17139 N  N     . ALA B 1  1133 ? 26.822  71.897  71.436  1.00 22.22 ? 1131 ALA B N     1 
ATOM   17140 C  CA    . ALA B 1  1133 ? 27.422  72.199  70.141  1.00 24.61 ? 1131 ALA B CA    1 
ATOM   17141 C  C     . ALA B 1  1133 ? 26.381  72.520  69.080  1.00 25.32 ? 1131 ALA B C     1 
ATOM   17142 O  O     . ALA B 1  1133 ? 26.747  72.984  67.997  1.00 26.71 ? 1131 ALA B O     1 
ATOM   17143 C  CB    . ALA B 1  1133 ? 28.303  71.037  69.672  1.00 24.40 ? 1131 ALA B CB    1 
ATOM   17144 N  N     . SER B 1  1134 ? 25.095  72.286  69.366  1.00 21.40 ? 1132 SER B N     1 
ATOM   17145 C  CA    . SER B 1  1134 ? 24.048  72.692  68.437  1.00 23.10 ? 1132 SER B CA    1 
ATOM   17146 C  C     . SER B 1  1134 ? 24.001  74.203  68.291  1.00 21.05 ? 1132 SER B C     1 
ATOM   17147 O  O     . SER B 1  1134 ? 23.512  74.709  67.278  1.00 23.26 ? 1132 SER B O     1 
ATOM   17148 C  CB    . SER B 1  1134 ? 22.689  72.182  68.914  1.00 20.43 ? 1132 SER B CB    1 
ATOM   17149 O  OG    . SER B 1  1134 ? 22.328  72.856  70.110  1.00 20.64 ? 1132 SER B OG    1 
ATOM   17150 N  N     . GLY B 1  1135 ? 24.467  74.931  69.303  1.00 22.06 ? 1133 GLY B N     1 
ATOM   17151 C  CA    . GLY B 1  1135 ? 24.443  76.380  69.262  1.00 23.82 ? 1133 GLY B CA    1 
ATOM   17152 C  C     . GLY B 1  1135 ? 23.064  76.991  69.377  1.00 24.64 ? 1133 GLY B C     1 
ATOM   17153 O  O     . GLY B 1  1135 ? 22.875  78.150  69.001  1.00 25.90 ? 1133 GLY B O     1 
ATOM   17154 N  N     . LEU B 1  1136 ? 22.094  76.248  69.912  1.00 24.27 ? 1134 LEU B N     1 
ATOM   17155 C  CA    . LEU B 1  1136 ? 20.706  76.690  69.951  1.00 25.74 ? 1134 LEU B CA    1 
ATOM   17156 C  C     . LEU B 1  1136 ? 20.297  77.240  71.318  1.00 26.59 ? 1134 LEU B C     1 
ATOM   17157 O  O     . LEU B 1  1136 ? 19.098  77.327  71.605  1.00 26.91 ? 1134 LEU B O     1 
ATOM   17158 C  CB    . LEU B 1  1136 ? 19.785  75.538  69.541  1.00 24.06 ? 1134 LEU B CB    1 
ATOM   17159 C  CG    . LEU B 1  1136 ? 19.994  74.976  68.128  1.00 24.05 ? 1134 LEU B CG    1 
ATOM   17160 C  CD1   . LEU B 1  1136 ? 19.180  73.708  67.893  1.00 23.61 ? 1134 LEU B CD1   1 
ATOM   17161 C  CD2   . LEU B 1  1136 ? 19.656  76.020  67.070  1.00 26.26 ? 1134 LEU B CD2   1 
ATOM   17162 N  N     . GLN B 1  1137 ? 21.263  77.625  72.159  1.00 24.92 ? 1135 GLN B N     1 
ATOM   17163 C  CA    . GLN B 1  1137 ? 20.944  78.063  73.518  1.00 25.74 ? 1135 GLN B CA    1 
ATOM   17164 C  C     . GLN B 1  1137 ? 19.935  79.209  73.523  1.00 29.96 ? 1135 GLN B C     1 
ATOM   17165 O  O     . GLN B 1  1137 ? 19.044  79.258  74.382  1.00 28.50 ? 1135 GLN B O     1 
ATOM   17166 C  CB    . GLN B 1  1137 ? 22.217  78.485  74.256  1.00 28.00 ? 1135 GLN B CB    1 
ATOM   17167 C  CG    . GLN B 1  1137 ? 23.120  77.334  74.688  1.00 26.92 ? 1135 GLN B CG    1 
ATOM   17168 C  CD    . GLN B 1  1137 ? 24.021  76.833  73.573  1.00 25.11 ? 1135 GLN B CD    1 
ATOM   17169 O  OE1   . GLN B 1  1137 ? 23.853  77.191  72.408  1.00 25.25 ? 1135 GLN B OE1   1 
ATOM   17170 N  NE2   . GLN B 1  1137 ? 24.986  75.989  73.931  1.00 27.54 ? 1135 GLN B NE2   1 
ATOM   17171 N  N     . ALA B 1  1138 ? 20.039  80.125  72.560  1.00 25.92 ? 1136 ALA B N     1 
ATOM   17172 C  CA    . ALA B 1  1138 ? 19.160  81.287  72.547  1.00 28.32 ? 1136 ALA B CA    1 
ATOM   17173 C  C     . ALA B 1  1138 ? 17.714  80.927  72.240  1.00 31.98 ? 1136 ALA B C     1 
ATOM   17174 O  O     . ALA B 1  1138 ? 16.832  81.773  72.423  1.00 35.01 ? 1136 ALA B O     1 
ATOM   17175 C  CB    . ALA B 1  1138 ? 19.664  82.317  71.537  1.00 26.30 ? 1136 ALA B CB    1 
ATOM   17176 N  N     . SER B 1  1139 ? 17.447  79.698  71.792  1.00 31.01 ? 1137 SER B N     1 
ATOM   17177 C  CA    . SER B 1  1139 ? 16.094  79.272  71.453  1.00 29.33 ? 1137 SER B CA    1 
ATOM   17178 C  C     . SER B 1  1139 ? 15.234  78.985  72.678  1.00 32.67 ? 1137 SER B C     1 
ATOM   17179 O  O     . SER B 1  1139 ? 14.009  78.877  72.539  1.00 30.63 ? 1137 SER B O     1 
ATOM   17180 C  CB    . SER B 1  1139 ? 16.146  78.024  70.567  1.00 27.69 ? 1137 SER B CB    1 
ATOM   17181 O  OG    . SER B 1  1139 ? 16.675  78.332  69.289  1.00 28.75 ? 1137 SER B OG    1 
ATOM   17182 N  N     . LEU B 1  1140 ? 15.842  78.838  73.856  1.00 29.43 ? 1138 LEU B N     1 
ATOM   17183 C  CA    . LEU B 1  1140 ? 15.129  78.566  75.098  1.00 33.25 ? 1138 LEU B CA    1 
ATOM   17184 C  C     . LEU B 1  1140 ? 15.129  79.774  76.031  1.00 35.01 ? 1138 LEU B C     1 
ATOM   17185 O  O     . LEU B 1  1140 ? 15.018  79.625  77.250  1.00 34.66 ? 1138 LEU B O     1 
ATOM   17186 C  CB    . LEU B 1  1140 ? 15.718  77.346  75.805  1.00 31.31 ? 1138 LEU B CB    1 
ATOM   17187 C  CG    . LEU B 1  1140 ? 15.718  76.051  74.994  1.00 30.18 ? 1138 LEU B CG    1 
ATOM   17188 C  CD1   . LEU B 1  1140 ? 16.171  74.860  75.835  1.00 30.49 ? 1138 LEU B CD1   1 
ATOM   17189 C  CD2   . LEU B 1  1140 ? 14.352  75.781  74.356  1.00 32.03 ? 1138 LEU B CD2   1 
ATOM   17190 N  N     . LYS B 1  1141 ? 15.253  80.975  75.477  1.00 37.21 ? 1139 LYS B N     1 
ATOM   17191 C  CA    . LYS B 1  1141 ? 15.177  82.173  76.301  1.00 38.17 ? 1139 LYS B CA    1 
ATOM   17192 C  C     . LYS B 1  1141 ? 13.770  82.315  76.874  1.00 36.35 ? 1139 LYS B C     1 
ATOM   17193 O  O     . LYS B 1  1141 ? 12.775  82.049  76.191  1.00 38.66 ? 1139 LYS B O     1 
ATOM   17194 C  CB    . LYS B 1  1141 ? 15.554  83.413  75.485  1.00 35.43 ? 1139 LYS B CB    1 
ATOM   17195 N  N     . ASN B 1  1142 ? 13.699  82.705  78.149  1.00 39.57 ? 1140 ASN B N     1 
ATOM   17196 C  CA    . ASN B 1  1142 ? 12.452  82.919  78.882  1.00 35.84 ? 1140 ASN B CA    1 
ATOM   17197 C  C     . ASN B 1  1142 ? 11.679  81.627  79.131  1.00 37.49 ? 1140 ASN B C     1 
ATOM   17198 O  O     . ASN B 1  1142 ? 10.460  81.663  79.334  1.00 37.12 ? 1140 ASN B O     1 
ATOM   17199 C  CB    . ASN B 1  1142 ? 11.549  83.935  78.174  1.00 40.17 ? 1140 ASN B CB    1 
ATOM   17200 N  N     . LEU B 1  1143 ? 12.359  80.484  79.125  1.00 38.03 ? 1141 LEU B N     1 
ATOM   17201 C  CA    . LEU B 1  1143 ? 11.690  79.223  79.399  1.00 35.75 ? 1141 LEU B CA    1 
ATOM   17202 C  C     . LEU B 1  1143 ? 11.118  79.240  80.816  1.00 32.88 ? 1141 LEU B C     1 
ATOM   17203 O  O     . LEU B 1  1143 ? 11.772  79.729  81.740  1.00 35.23 ? 1141 LEU B O     1 
ATOM   17204 C  CB    . LEU B 1  1143 ? 12.675  78.061  79.236  1.00 32.37 ? 1141 LEU B CB    1 
ATOM   17205 C  CG    . LEU B 1  1143 ? 12.149  76.635  79.125  1.00 32.36 ? 1141 LEU B CG    1 
ATOM   17206 C  CD1   . LEU B 1  1143 ? 11.471  76.411  77.788  1.00 30.63 ? 1141 LEU B CD1   1 
ATOM   17207 C  CD2   . LEU B 1  1143 ? 13.279  75.632  79.340  1.00 27.65 ? 1141 LEU B CD2   1 
ATOM   17208 N  N     . PRO B 1  1144 ? 9.905   78.730  81.026  1.00 33.44 ? 1142 PRO B N     1 
ATOM   17209 C  CA    . PRO B 1  1144 ? 9.373   78.657  82.394  1.00 34.67 ? 1142 PRO B CA    1 
ATOM   17210 C  C     . PRO B 1  1144 ? 10.243  77.762  83.262  1.00 31.44 ? 1142 PRO B C     1 
ATOM   17211 O  O     . PRO B 1  1144 ? 10.776  76.752  82.798  1.00 30.06 ? 1142 PRO B O     1 
ATOM   17212 C  CB    . PRO B 1  1144 ? 7.971   78.061  82.205  1.00 35.93 ? 1142 PRO B CB    1 
ATOM   17213 C  CG    . PRO B 1  1144 ? 7.654   78.249  80.749  1.00 34.43 ? 1142 PRO B CG    1 
ATOM   17214 C  CD    . PRO B 1  1144 ? 8.965   78.190  80.031  1.00 31.14 ? 1142 PRO B CD    1 
ATOM   17215 N  N     . GLN B 1  1145 ? 10.382  78.140  84.539  1.00 34.19 ? 1143 GLN B N     1 
ATOM   17216 C  CA    . GLN B 1  1145 ? 11.225  77.372  85.451  1.00 32.16 ? 1143 GLN B CA    1 
ATOM   17217 C  C     . GLN B 1  1145 ? 10.810  75.912  85.509  1.00 32.33 ? 1143 GLN B C     1 
ATOM   17218 O  O     . GLN B 1  1145 ? 11.664  75.033  85.647  1.00 28.36 ? 1143 GLN B O     1 
ATOM   17219 C  CB    . GLN B 1  1145 ? 11.193  77.974  86.857  1.00 31.61 ? 1143 GLN B CB    1 
ATOM   17220 N  N     . THR B 1  1146 ? 9.510   75.631  85.394  1.00 31.45 ? 1144 THR B N     1 
ATOM   17221 C  CA    . THR B 1  1146 ? 9.059   74.244  85.415  1.00 30.52 ? 1144 THR B CA    1 
ATOM   17222 C  C     . THR B 1  1146 ? 9.712   73.443  84.299  1.00 29.80 ? 1144 THR B C     1 
ATOM   17223 O  O     . THR B 1  1146 ? 10.120  72.293  84.506  1.00 32.38 ? 1144 THR B O     1 
ATOM   17224 C  CB    . THR B 1  1146 ? 7.538   74.179  85.288  1.00 28.73 ? 1144 THR B CB    1 
ATOM   17225 O  OG1   . THR B 1  1146 ? 7.126   74.979  84.175  1.00 33.54 ? 1144 THR B OG1   1 
ATOM   17226 C  CG2   . THR B 1  1146 ? 6.880   74.704  86.553  1.00 37.55 ? 1144 THR B CG2   1 
ATOM   17227 N  N     . VAL B 1  1147 ? 9.824   74.034  83.109  1.00 26.58 ? 1145 VAL B N     1 
ATOM   17228 C  CA    . VAL B 1  1147 ? 10.499  73.338  82.020  1.00 27.21 ? 1145 VAL B CA    1 
ATOM   17229 C  C     . VAL B 1  1147 ? 12.010  73.418  82.197  1.00 27.38 ? 1145 VAL B C     1 
ATOM   17230 O  O     . VAL B 1  1147 ? 12.725  72.435  81.974  1.00 26.08 ? 1145 VAL B O     1 
ATOM   17231 C  CB    . VAL B 1  1147 ? 10.061  73.896  80.654  1.00 24.05 ? 1145 VAL B CB    1 
ATOM   17232 C  CG1   . VAL B 1  1147 ? 10.595  73.016  79.531  1.00 27.35 ? 1145 VAL B CG1   1 
ATOM   17233 C  CG2   . VAL B 1  1147 ? 8.545   74.004  80.572  1.00 25.16 ? 1145 VAL B CG2   1 
ATOM   17234 N  N     . GLY B 1  1148 ? 12.516  74.578  82.622  1.00 28.06 ? 1146 GLY B N     1 
ATOM   17235 C  CA    . GLY B 1  1148 ? 13.952  74.733  82.775  1.00 28.34 ? 1146 GLY B CA    1 
ATOM   17236 C  C     . GLY B 1  1148 ? 14.570  73.717  83.711  1.00 28.45 ? 1146 GLY B C     1 
ATOM   17237 O  O     . GLY B 1  1148 ? 15.704  73.278  83.494  1.00 27.73 ? 1146 GLY B O     1 
ATOM   17238 N  N     . LEU B 1  1149 ? 13.831  73.313  84.750  1.00 26.84 ? 1147 LEU B N     1 
ATOM   17239 C  CA    . LEU B 1  1149 ? 14.344  72.357  85.722  1.00 28.39 ? 1147 LEU B CA    1 
ATOM   17240 C  C     . LEU B 1  1149 ? 14.593  70.992  85.113  1.00 28.86 ? 1147 LEU B C     1 
ATOM   17241 O  O     . LEU B 1  1149 ? 15.378  70.218  85.672  1.00 27.13 ? 1147 LEU B O     1 
ATOM   17242 C  CB    . LEU B 1  1149 ? 13.375  72.223  86.899  1.00 31.93 ? 1147 LEU B CB    1 
ATOM   17243 C  CG    . LEU B 1  1149 ? 13.297  73.480  87.765  1.00 36.61 ? 1147 LEU B CG    1 
ATOM   17244 C  CD1   . LEU B 1  1149 ? 12.395  73.266  88.975  1.00 36.10 ? 1147 LEU B CD1   1 
ATOM   17245 C  CD2   . LEU B 1  1149 ? 14.697  73.927  88.175  1.00 39.50 ? 1147 LEU B CD2   1 
ATOM   17246 N  N     . ARG B 1  1150 ? 13.950  70.686  83.988  1.00 25.43 ? 1148 ARG B N     1 
ATOM   17247 C  CA    . ARG B 1  1150 ? 14.151  69.431  83.275  1.00 26.21 ? 1148 ARG B CA    1 
ATOM   17248 C  C     . ARG B 1  1150 ? 15.228  69.522  82.209  1.00 21.69 ? 1148 ARG B C     1 
ATOM   17249 O  O     . ARG B 1  1150 ? 15.530  68.508  81.574  1.00 20.64 ? 1148 ARG B O     1 
ATOM   17250 C  CB    . ARG B 1  1150 ? 12.859  68.986  82.596  1.00 22.51 ? 1148 ARG B CB    1 
ATOM   17251 C  CG    . ARG B 1  1150 ? 11.754  68.550  83.527  1.00 23.25 ? 1148 ARG B CG    1 
ATOM   17252 C  CD    . ARG B 1  1150 ? 11.362  67.102  83.227  1.00 24.92 ? 1148 ARG B CD    1 
ATOM   17253 N  NE    . ARG B 1  1150 ? 10.112  66.743  83.884  1.00 20.93 ? 1148 ARG B NE    1 
ATOM   17254 C  CZ    . ARG B 1  1150 ? 9.037   66.291  83.254  1.00 22.06 ? 1148 ARG B CZ    1 
ATOM   17255 N  NH1   . ARG B 1  1150 ? 9.033   66.095  81.940  1.00 18.97 ? 1148 ARG B NH1   1 
ATOM   17256 N  NH2   . ARG B 1  1150 ? 7.947   66.011  83.964  1.00 21.48 ? 1148 ARG B NH2   1 
ATOM   17257 N  N     . VAL B 1  1151 ? 15.777  70.709  81.973  1.00 22.86 ? 1149 VAL B N     1 
ATOM   17258 C  CA    . VAL B 1  1151 ? 16.636  70.974  80.826  1.00 20.47 ? 1149 VAL B CA    1 
ATOM   17259 C  C     . VAL B 1  1151 ? 18.042  71.252  81.322  1.00 25.08 ? 1149 VAL B C     1 
ATOM   17260 O  O     . VAL B 1  1151 ? 18.243  72.107  82.190  1.00 25.70 ? 1149 VAL B O     1 
ATOM   17261 C  CB    . VAL B 1  1151 ? 16.120  72.161  79.996  1.00 24.20 ? 1149 VAL B CB    1 
ATOM   17262 C  CG1   . VAL B 1  1151 ? 17.182  72.605  78.978  1.00 26.88 ? 1149 VAL B CG1   1 
ATOM   17263 C  CG2   . VAL B 1  1151 ? 14.830  71.796  79.288  1.00 23.84 ? 1149 VAL B CG2   1 
ATOM   17264 N  N     . SER B 1  1152 ? 19.014  70.547  80.758  1.00 22.58 ? 1150 SER B N     1 
ATOM   17265 C  CA    . SER B 1  1152 ? 20.410  70.907  80.928  1.00 24.13 ? 1150 SER B CA    1 
ATOM   17266 C  C     . SER B 1  1152 ? 21.056  70.944  79.553  1.00 21.16 ? 1150 SER B C     1 
ATOM   17267 O  O     . SER B 1  1152 ? 20.518  70.416  78.576  1.00 23.02 ? 1150 SER B O     1 
ATOM   17268 C  CB    . SER B 1  1152 ? 21.148  69.937  81.864  1.00 24.30 ? 1150 SER B CB    1 
ATOM   17269 O  OG    . SER B 1  1152 ? 21.174  68.629  81.320  1.00 28.20 ? 1150 SER B OG    1 
ATOM   17270 N  N     . TRP B 1  1153 ? 22.207  71.598  79.481  1.00 21.84 ? 1151 TRP B N     1 
ATOM   17271 C  CA    . TRP B 1  1153 ? 22.975  71.689  78.253  1.00 19.94 ? 1151 TRP B CA    1 
ATOM   17272 C  C     . TRP B 1  1153 ? 24.293  70.969  78.473  1.00 22.37 ? 1151 TRP B C     1 
ATOM   17273 O  O     . TRP B 1  1153 ? 24.928  71.153  79.516  1.00 23.64 ? 1151 TRP B O     1 
ATOM   17274 C  CB    . TRP B 1  1153 ? 23.219  73.146  77.876  1.00 23.09 ? 1151 TRP B CB    1 
ATOM   17275 C  CG    . TRP B 1  1153 ? 21.986  73.829  77.400  1.00 22.50 ? 1151 TRP B CG    1 
ATOM   17276 C  CD1   . TRP B 1  1153 ? 21.035  74.460  78.162  1.00 26.18 ? 1151 TRP B CD1   1 
ATOM   17277 C  CD2   . TRP B 1  1153 ? 21.570  73.960  76.044  1.00 21.41 ? 1151 TRP B CD2   1 
ATOM   17278 N  NE1   . TRP B 1  1153 ? 20.053  74.981  77.345  1.00 23.35 ? 1151 TRP B NE1   1 
ATOM   17279 C  CE2   . TRP B 1  1153 ? 20.359  74.682  76.042  1.00 22.65 ? 1151 TRP B CE2   1 
ATOM   17280 C  CE3   . TRP B 1  1153 ? 22.105  73.538  74.820  1.00 20.42 ? 1151 TRP B CE3   1 
ATOM   17281 C  CZ2   . TRP B 1  1153 ? 19.683  74.989  74.867  1.00 25.32 ? 1151 TRP B CZ2   1 
ATOM   17282 C  CZ3   . TRP B 1  1153 ? 21.433  73.840  73.663  1.00 21.59 ? 1151 TRP B CZ3   1 
ATOM   17283 C  CH2   . TRP B 1  1153 ? 20.233  74.558  73.692  1.00 24.88 ? 1151 TRP B CH2   1 
ATOM   17284 N  N     . SER B 1  1154 ? 24.691  70.137  77.510  1.00 19.50 ? 1152 SER B N     1 
ATOM   17285 C  CA    . SER B 1  1154 ? 25.860  69.281  77.686  1.00 19.95 ? 1152 SER B CA    1 
ATOM   17286 C  C     . SER B 1  1154 ? 26.926  69.611  76.654  1.00 18.51 ? 1152 SER B C     1 
ATOM   17287 O  O     . SER B 1  1154 ? 26.671  69.551  75.447  1.00 21.05 ? 1152 SER B O     1 
ATOM   17288 C  CB    . SER B 1  1154 ? 25.493  67.805  77.580  1.00 21.46 ? 1152 SER B CB    1 
ATOM   17289 O  OG    . SER B 1  1154 ? 26.668  67.026  77.741  1.00 19.74 ? 1152 SER B OG    1 
ATOM   17290 N  N     . LYS B 1  1155 ? 28.125  69.925  77.142  1.00 18.46 ? 1153 LYS B N     1 
ATOM   17291 C  CA    . LYS B 1  1155 ? 29.317  70.066  76.319  1.00 21.12 ? 1153 LYS B CA    1 
ATOM   17292 C  C     . LYS B 1  1155 ? 30.190  68.825  76.394  1.00 21.30 ? 1153 LYS B C     1 
ATOM   17293 O  O     . LYS B 1  1155 ? 31.309  68.820  75.868  1.00 24.06 ? 1153 LYS B O     1 
ATOM   17294 C  CB    . LYS B 1  1155 ? 30.120  71.291  76.761  1.00 22.21 ? 1153 LYS B CB    1 
ATOM   17295 N  N     . ASP B 1  1156 ? 29.708  67.782  77.055  1.00 17.77 ? 1154 ASP B N     1 
ATOM   17296 C  CA    . ASP B 1  1156 ? 30.516  66.592  77.315  1.00 17.18 ? 1154 ASP B CA    1 
ATOM   17297 C  C     . ASP B 1  1156 ? 29.517  65.457  77.558  1.00 18.28 ? 1154 ASP B C     1 
ATOM   17298 O  O     . ASP B 1  1156 ? 29.122  65.212  78.697  1.00 18.95 ? 1154 ASP B O     1 
ATOM   17299 C  CB    . ASP B 1  1156 ? 31.428  66.805  78.509  1.00 18.11 ? 1154 ASP B CB    1 
ATOM   17300 C  CG    . ASP B 1  1156 ? 32.423  65.679  78.694  1.00 18.65 ? 1154 ASP B CG    1 
ATOM   17301 O  OD1   . ASP B 1  1156 ? 32.105  64.537  78.327  1.00 18.38 ? 1154 ASP B OD1   1 
ATOM   17302 O  OD2   . ASP B 1  1156 ? 33.525  65.948  79.201  1.00 18.93 ? 1154 ASP B OD2   1 
ATOM   17303 N  N     . TRP B 1  1157 ? 29.108  64.787  76.475  1.00 17.70 ? 1155 TRP B N     1 
ATOM   17304 C  CA    . TRP B 1  1157 ? 28.025  63.813  76.609  1.00 18.90 ? 1155 TRP B CA    1 
ATOM   17305 C  C     . TRP B 1  1157 ? 28.423  62.670  77.524  1.00 21.19 ? 1155 TRP B C     1 
ATOM   17306 O  O     . TRP B 1  1157 ? 27.617  62.205  78.332  1.00 19.31 ? 1155 TRP B O     1 
ATOM   17307 C  CB    . TRP B 1  1157 ? 27.615  63.250  75.256  1.00 19.34 ? 1155 TRP B CB    1 
ATOM   17308 C  CG    . TRP B 1  1157 ? 27.192  64.243  74.240  1.00 17.24 ? 1155 TRP B CG    1 
ATOM   17309 C  CD1   . TRP B 1  1157 ? 26.966  65.583  74.413  1.00 17.87 ? 1155 TRP B CD1   1 
ATOM   17310 C  CD2   . TRP B 1  1157 ? 26.936  63.965  72.865  1.00 17.64 ? 1155 TRP B CD2   1 
ATOM   17311 N  NE1   . TRP B 1  1157 ? 26.597  66.148  73.223  1.00 18.07 ? 1155 TRP B NE1   1 
ATOM   17312 C  CE2   . TRP B 1  1157 ? 26.573  65.177  72.254  1.00 17.36 ? 1155 TRP B CE2   1 
ATOM   17313 C  CE3   . TRP B 1  1157 ? 26.995  62.803  72.086  1.00 19.64 ? 1155 TRP B CE3   1 
ATOM   17314 C  CZ2   . TRP B 1  1157 ? 26.252  65.262  70.905  1.00 20.41 ? 1155 TRP B CZ2   1 
ATOM   17315 C  CZ3   . TRP B 1  1157 ? 26.682  62.885  70.750  1.00 19.82 ? 1155 TRP B CZ3   1 
ATOM   17316 C  CH2   . TRP B 1  1157 ? 26.321  64.110  70.167  1.00 21.37 ? 1155 TRP B CH2   1 
ATOM   17317 N  N     . ALA B 1  1158 ? 29.666  62.203  77.420  1.00 17.14 ? 1156 ALA B N     1 
ATOM   17318 C  CA    . ALA B 1  1158 ? 30.052  61.043  78.215  1.00 20.60 ? 1156 ALA B CA    1 
ATOM   17319 C  C     . ALA B 1  1158 ? 30.143  61.379  79.696  1.00 20.39 ? 1156 ALA B C     1 
ATOM   17320 O  O     . ALA B 1  1158 ? 29.877  60.516  80.538  1.00 21.36 ? 1156 ALA B O     1 
ATOM   17321 C  CB    . ALA B 1  1158 ? 31.377  60.469  77.714  1.00 16.53 ? 1156 ALA B CB    1 
ATOM   17322 N  N     . ALA B 1  1159 ? 30.515  62.612  80.036  1.00 17.71 ? 1157 ALA B N     1 
ATOM   17323 C  CA    . ALA B 1  1159 ? 30.622  62.998  81.435  1.00 19.77 ? 1157 ALA B CA    1 
ATOM   17324 C  C     . ALA B 1  1159 ? 29.267  63.287  82.067  1.00 21.34 ? 1157 ALA B C     1 
ATOM   17325 O  O     . ALA B 1  1159 ? 29.139  63.187  83.287  1.00 20.29 ? 1157 ALA B O     1 
ATOM   17326 C  CB    . ALA B 1  1159 ? 31.516  64.227  81.582  1.00 20.47 ? 1157 ALA B CB    1 
ATOM   17327 N  N     . ASP B 1  1160 ? 28.262  63.628  81.265  1.00 20.01 ? 1158 ASP B N     1 
ATOM   17328 C  CA    . ASP B 1  1160 ? 26.980  64.109  81.771  1.00 21.98 ? 1158 ASP B CA    1 
ATOM   17329 C  C     . ASP B 1  1160 ? 25.898  63.039  81.801  1.00 23.31 ? 1158 ASP B C     1 
ATOM   17330 O  O     . ASP B 1  1160 ? 24.754  63.342  82.172  1.00 23.26 ? 1158 ASP B O     1 
ATOM   17331 C  CB    . ASP B 1  1160 ? 26.508  65.295  80.930  1.00 19.59 ? 1158 ASP B CB    1 
ATOM   17332 C  CG    . ASP B 1  1160 ? 27.392  66.511  81.115  1.00 23.01 ? 1158 ASP B CG    1 
ATOM   17333 O  OD1   . ASP B 1  1160 ? 28.174  66.532  82.101  1.00 24.03 ? 1158 ASP B OD1   1 
ATOM   17334 O  OD2   . ASP B 1  1160 ? 27.336  67.431  80.269  1.00 22.94 ? 1158 ASP B OD2   1 
ATOM   17335 N  N     . GLY B 1  1161 ? 26.219  61.817  81.395  1.00 18.10 ? 1159 GLY B N     1 
ATOM   17336 C  CA    . GLY B 1  1161 ? 25.313  60.703  81.488  1.00 21.18 ? 1159 GLY B CA    1 
ATOM   17337 C  C     . GLY B 1  1161 ? 25.274  60.125  82.891  1.00 26.61 ? 1159 GLY B C     1 
ATOM   17338 O  O     . GLY B 1  1161 ? 25.836  60.687  83.838  1.00 26.47 ? 1159 GLY B O     1 
ATOM   17339 N  N     . PRO B 1  1162 ? 24.631  58.965  83.049  1.00 26.28 ? 1160 PRO B N     1 
ATOM   17340 C  CA    . PRO B 1  1162 ? 24.064  58.128  81.991  1.00 22.23 ? 1160 PRO B CA    1 
ATOM   17341 C  C     . PRO B 1  1162 ? 22.748  58.691  81.492  1.00 22.43 ? 1160 PRO B C     1 
ATOM   17342 O  O     . PRO B 1  1162 ? 21.939  59.257  82.230  1.00 25.03 ? 1160 PRO B O     1 
ATOM   17343 C  CB    . PRO B 1  1162 ? 23.883  56.776  82.695  1.00 26.84 ? 1160 PRO B CB    1 
ATOM   17344 C  CG    . PRO B 1  1162 ? 23.487  57.181  84.106  1.00 27.92 ? 1160 PRO B CG    1 
ATOM   17345 C  CD    . PRO B 1  1162 ? 24.324  58.423  84.391  1.00 27.49 ? 1160 PRO B CD    1 
ATOM   17346 N  N     . PHE B 1  1163 ? 22.519  58.544  80.200  1.00 18.41 ? 1161 PHE B N     1 
ATOM   17347 C  CA    . PHE B 1  1163 ? 21.233  58.869  79.608  1.00 18.92 ? 1161 PHE B CA    1 
ATOM   17348 C  C     . PHE B 1  1163 ? 20.423  57.593  79.456  1.00 16.66 ? 1161 PHE B C     1 
ATOM   17349 O  O     . PHE B 1  1163 ? 20.898  56.488  79.739  1.00 18.65 ? 1161 PHE B O     1 
ATOM   17350 C  CB    . PHE B 1  1163 ? 21.441  59.586  78.273  1.00 17.37 ? 1161 PHE B CB    1 
ATOM   17351 C  CG    . PHE B 1  1163 ? 22.321  60.800  78.388  1.00 18.17 ? 1161 PHE B CG    1 
ATOM   17352 C  CD1   . PHE B 1  1163 ? 21.950  61.859  79.196  1.00 21.49 ? 1161 PHE B CD1   1 
ATOM   17353 C  CD2   . PHE B 1  1163 ? 23.529  60.875  77.709  1.00 17.75 ? 1161 PHE B CD2   1 
ATOM   17354 C  CE1   . PHE B 1  1163 ? 22.751  62.968  79.327  1.00 22.20 ? 1161 PHE B CE1   1 
ATOM   17355 C  CE2   . PHE B 1  1163 ? 24.332  61.999  77.826  1.00 19.76 ? 1161 PHE B CE2   1 
ATOM   17356 C  CZ    . PHE B 1  1163 ? 23.948  63.041  78.638  1.00 18.48 ? 1161 PHE B CZ    1 
ATOM   17357 N  N     . ALA B 1  1164 ? 19.162  57.755  79.040  1.00 17.25 ? 1162 ALA B N     1 
ATOM   17358 C  CA    . ALA B 1  1164 ? 18.280  56.614  78.841  1.00 19.05 ? 1162 ALA B CA    1 
ATOM   17359 C  C     . ALA B 1  1164 ? 17.682  56.583  77.439  1.00 19.66 ? 1162 ALA B C     1 
ATOM   17360 O  O     . ALA B 1  1164 ? 16.717  55.840  77.197  1.00 21.10 ? 1162 ALA B O     1 
ATOM   17361 C  CB    . ALA B 1  1164 ? 17.174  56.623  79.903  1.00 18.72 ? 1162 ALA B CB    1 
ATOM   17362 N  N     . GLY B 1  1165 ? 18.227  57.369  76.520  1.00 15.94 ? 1163 GLY B N     1 
ATOM   17363 C  CA    . GLY B 1  1165 ? 17.808  57.373  75.136  1.00 16.56 ? 1163 GLY B CA    1 
ATOM   17364 C  C     . GLY B 1  1165 ? 18.393  58.611  74.496  1.00 16.58 ? 1163 GLY B C     1 
ATOM   17365 O  O     . GLY B 1  1165 ? 19.006  59.436  75.165  1.00 15.29 ? 1163 GLY B O     1 
ATOM   17366 N  N     . ALA B 1  1166 ? 18.182  58.734  73.192  1.00 16.72 ? 1164 ALA B N     1 
ATOM   17367 C  CA    . ALA B 1  1166 ? 18.701  59.889  72.482  1.00 16.91 ? 1164 ALA B CA    1 
ATOM   17368 C  C     . ALA B 1  1166 ? 17.810  60.203  71.299  1.00 18.04 ? 1164 ALA B C     1 
ATOM   17369 O  O     . ALA B 1  1166 ? 17.335  59.295  70.616  1.00 18.22 ? 1164 ALA B O     1 
ATOM   17370 C  CB    . ALA B 1  1166 ? 20.140  59.652  72.000  1.00 16.55 ? 1164 ALA B CB    1 
ATOM   17371 N  N     . LEU B 1  1167 ? 17.597  61.494  71.062  1.00 15.34 ? 1165 LEU B N     1 
ATOM   17372 C  CA    . LEU B 1  1167 ? 16.910  61.978  69.873  1.00 17.95 ? 1165 LEU B CA    1 
ATOM   17373 C  C     . LEU B 1  1167 ? 17.905  62.805  69.075  1.00 18.82 ? 1165 LEU B C     1 
ATOM   17374 O  O     . LEU B 1  1167 ? 18.577  63.681  69.635  1.00 17.43 ? 1165 LEU B O     1 
ATOM   17375 C  CB    . LEU B 1  1167 ? 15.687  62.821  70.233  1.00 19.08 ? 1165 LEU B CB    1 
ATOM   17376 C  CG    . LEU B 1  1167 ? 14.678  62.142  71.156  1.00 18.47 ? 1165 LEU B CG    1 
ATOM   17377 C  CD1   . LEU B 1  1167 ? 13.581  63.148  71.510  1.00 19.53 ? 1165 LEU B CD1   1 
ATOM   17378 C  CD2   . LEU B 1  1167 ? 14.084  60.890  70.494  1.00 18.77 ? 1165 LEU B CD2   1 
ATOM   17379 N  N     . VAL B 1  1168 ? 18.001  62.516  67.778  1.00 16.51 ? 1166 VAL B N     1 
ATOM   17380 C  CA    . VAL B 1  1168 ? 18.997  63.115  66.904  1.00 18.16 ? 1166 VAL B CA    1 
ATOM   17381 C  C     . VAL B 1  1168 ? 18.291  63.715  65.698  1.00 19.74 ? 1166 VAL B C     1 
ATOM   17382 O  O     . VAL B 1  1168 ? 17.392  63.092  65.116  1.00 18.95 ? 1166 VAL B O     1 
ATOM   17383 C  CB    . VAL B 1  1168 ? 20.044  62.075  66.460  1.00 17.43 ? 1166 VAL B CB    1 
ATOM   17384 C  CG1   . VAL B 1  1168 ? 21.114  62.717  65.569  1.00 18.60 ? 1166 VAL B CG1   1 
ATOM   17385 C  CG2   . VAL B 1  1168 ? 20.674  61.397  67.679  1.00 16.65 ? 1166 VAL B CG2   1 
ATOM   17386 N  N     . GLU B 1  1169 ? 18.695  64.929  65.330  1.00 17.94 ? 1167 GLU B N     1 
ATOM   17387 C  CA    . GLU B 1  1169 ? 18.239  65.607  64.123  1.00 18.44 ? 1167 GLU B CA    1 
ATOM   17388 C  C     . GLU B 1  1169 ? 19.446  65.867  63.232  1.00 20.54 ? 1167 GLU B C     1 
ATOM   17389 O  O     . GLU B 1  1169 ? 20.474  66.335  63.717  1.00 21.94 ? 1167 GLU B O     1 
ATOM   17390 C  CB    . GLU B 1  1169 ? 17.565  66.933  64.458  1.00 19.94 ? 1167 GLU B CB    1 
ATOM   17391 C  CG    . GLU B 1  1169 ? 17.093  67.699  63.236  1.00 20.72 ? 1167 GLU B CG    1 
ATOM   17392 C  CD    . GLU B 1  1169 ? 16.691  69.120  63.571  1.00 21.15 ? 1167 GLU B CD    1 
ATOM   17393 O  OE1   . GLU B 1  1169 ? 16.956  69.569  64.705  1.00 21.87 ? 1167 GLU B OE1   1 
ATOM   17394 O  OE2   . GLU B 1  1169 ? 16.109  69.791  62.699  1.00 23.97 ? 1167 GLU B OE2   1 
ATOM   17395 N  N     . GLY B 1  1170 ? 19.328  65.562  61.948  1.00 19.89 ? 1168 GLY B N     1 
ATOM   17396 C  CA    . GLY B 1  1170 ? 20.410  65.871  61.031  1.00 22.20 ? 1168 GLY B CA    1 
ATOM   17397 C  C     . GLY B 1  1170 ? 20.298  65.089  59.745  1.00 25.74 ? 1168 GLY B C     1 
ATOM   17398 O  O     . GLY B 1  1170 ? 19.445  64.218  59.586  1.00 24.31 ? 1168 GLY B O     1 
ATOM   17399 N  N     . ASP B 1  1171 ? 21.183  65.424  58.803  1.00 25.23 ? 1169 ASP B N     1 
ATOM   17400 C  CA    . ASP B 1  1171 ? 21.202  64.652  57.572  1.00 24.04 ? 1169 ASP B CA    1 
ATOM   17401 C  C     . ASP B 1  1171 ? 21.890  63.316  57.823  1.00 24.15 ? 1169 ASP B C     1 
ATOM   17402 O  O     . ASP B 1  1171 ? 22.344  63.020  58.931  1.00 25.21 ? 1169 ASP B O     1 
ATOM   17403 C  CB    . ASP B 1  1171 ? 21.852  65.434  56.426  1.00 25.81 ? 1169 ASP B CB    1 
ATOM   17404 C  CG    . ASP B 1  1171 ? 23.300  65.810  56.681  1.00 24.89 ? 1169 ASP B CG    1 
ATOM   17405 O  OD1   . ASP B 1  1171 ? 23.953  65.285  57.609  1.00 25.01 ? 1169 ASP B OD1   1 
ATOM   17406 O  OD2   . ASP B 1  1171 ? 23.798  66.676  55.923  1.00 31.60 ? 1169 ASP B OD2   1 
ATOM   17407 N  N     . ALA B 1  1172 ? 21.951  62.492  56.776  1.00 25.43 ? 1170 ALA B N     1 
ATOM   17408 C  CA    . ALA B 1  1172 ? 22.445  61.128  56.934  1.00 26.43 ? 1170 ALA B CA    1 
ATOM   17409 C  C     . ALA B 1  1172 ? 23.837  61.107  57.557  1.00 25.41 ? 1170 ALA B C     1 
ATOM   17410 O  O     . ALA B 1  1172 ? 24.098  60.340  58.489  1.00 26.43 ? 1170 ALA B O     1 
ATOM   17411 C  CB    . ALA B 1  1172 ? 22.445  60.410  55.584  1.00 27.49 ? 1170 ALA B CB    1 
ATOM   17412 N  N     . GLU B 1  1173 ? 24.749  61.948  57.070  1.00 25.40 ? 1171 GLU B N     1 
ATOM   17413 C  CA    . GLU B 1  1173 ? 26.105  61.863  57.603  1.00 24.15 ? 1171 GLU B CA    1 
ATOM   17414 C  C     . GLU B 1  1173 ? 26.195  62.436  59.016  1.00 22.85 ? 1171 GLU B C     1 
ATOM   17415 O  O     . GLU B 1  1173 ? 26.998  61.959  59.825  1.00 25.30 ? 1171 GLU B O     1 
ATOM   17416 C  CB    . GLU B 1  1173 ? 27.095  62.538  56.654  1.00 31.38 ? 1171 GLU B CB    1 
ATOM   17417 C  CG    . GLU B 1  1173 ? 27.402  61.697  55.401  1.00 34.15 ? 1171 GLU B CG    1 
ATOM   17418 C  CD    . GLU B 1  1173 ? 27.704  60.220  55.699  1.00 37.15 ? 1171 GLU B CD    1 
ATOM   17419 O  OE1   . GLU B 1  1173 ? 28.589  59.918  56.534  1.00 35.48 ? 1171 GLU B OE1   1 
ATOM   17420 O  OE2   . GLU B 1  1173 ? 27.048  59.349  55.087  1.00 40.53 ? 1171 GLU B OE2   1 
ATOM   17421 N  N     . ARG B 1  1174 ? 25.367  63.430  59.342  1.00 22.25 ? 1172 ARG B N     1 
ATOM   17422 C  CA    . ARG B 1  1174 ? 25.277  63.886  60.727  1.00 22.42 ? 1172 ARG B CA    1 
ATOM   17423 C  C     . ARG B 1  1174 ? 24.772  62.770  61.629  1.00 21.62 ? 1172 ARG B C     1 
ATOM   17424 O  O     . ARG B 1  1174 ? 25.326  62.530  62.707  1.00 21.69 ? 1172 ARG B O     1 
ATOM   17425 C  CB    . ARG B 1  1174 ? 24.358  65.103  60.821  1.00 22.67 ? 1172 ARG B CB    1 
ATOM   17426 C  CG    . ARG B 1  1174 ? 24.118  65.592  62.243  1.00 20.85 ? 1172 ARG B CG    1 
ATOM   17427 C  CD    . ARG B 1  1174 ? 25.413  66.045  62.886  1.00 22.78 ? 1172 ARG B CD    1 
ATOM   17428 N  NE    . ARG B 1  1174 ? 25.180  66.583  64.219  1.00 23.59 ? 1172 ARG B NE    1 
ATOM   17429 C  CZ    . ARG B 1  1174 ? 26.107  66.675  65.161  1.00 22.72 ? 1172 ARG B CZ    1 
ATOM   17430 N  NH1   . ARG B 1  1174 ? 27.361  66.305  64.939  1.00 22.82 ? 1172 ARG B NH1   1 
ATOM   17431 N  NH2   . ARG B 1  1174 ? 25.767  67.137  66.361  1.00 23.21 ? 1172 ARG B NH2   1 
ATOM   17432 N  N     . ILE B 1  1175 ? 23.732  62.064  61.189  1.00 22.99 ? 1173 ILE B N     1 
ATOM   17433 C  CA    . ILE B 1  1175 ? 23.185  60.968  61.984  1.00 21.64 ? 1173 ILE B CA    1 
ATOM   17434 C  C     . ILE B 1  1175 ? 24.247  59.905  62.236  1.00 22.16 ? 1173 ILE B C     1 
ATOM   17435 O  O     . ILE B 1  1175 ? 24.443  59.460  63.371  1.00 21.01 ? 1173 ILE B O     1 
ATOM   17436 C  CB    . ILE B 1  1175 ? 21.942  60.383  61.294  1.00 21.11 ? 1173 ILE B CB    1 
ATOM   17437 C  CG1   . ILE B 1  1175 ? 20.792  61.387  61.379  1.00 21.90 ? 1173 ILE B CG1   1 
ATOM   17438 C  CG2   . ILE B 1  1175 ? 21.561  59.073  61.921  1.00 21.91 ? 1173 ILE B CG2   1 
ATOM   17439 C  CD1   . ILE B 1  1175 ? 19.638  61.063  60.474  1.00 21.99 ? 1173 ILE B CD1   1 
ATOM   17440 N  N     . ARG B 1  1176 ? 24.967  59.495  61.186  1.00 25.48 ? 1174 ARG B N     1 
ATOM   17441 C  CA    . ARG B 1  1176 ? 26.012  58.486  61.370  1.00 22.78 ? 1174 ARG B CA    1 
ATOM   17442 C  C     . ARG B 1  1176 ? 27.053  58.951  62.383  1.00 20.85 ? 1174 ARG B C     1 
ATOM   17443 O  O     . ARG B 1  1176 ? 27.465  58.192  63.267  1.00 20.06 ? 1174 ARG B O     1 
ATOM   17444 C  CB    . ARG B 1  1176 ? 26.688  58.162  60.030  1.00 24.09 ? 1174 ARG B CB    1 
ATOM   17445 C  CG    . ARG B 1  1176 ? 27.574  56.916  60.091  1.00 26.94 ? 1174 ARG B CG    1 
ATOM   17446 C  CD    . ARG B 1  1176 ? 28.549  56.819  58.907  1.00 30.06 ? 1174 ARG B CD    1 
ATOM   17447 N  NE    . ARG B 1  1176 ? 27.881  57.013  57.625  1.00 34.39 ? 1174 ARG B NE    1 
ATOM   17448 C  CZ    . ARG B 1  1176 ? 27.270  56.053  56.941  1.00 37.20 ? 1174 ARG B CZ    1 
ATOM   17449 N  NH1   . ARG B 1  1176 ? 27.241  54.804  57.376  1.00 34.74 ? 1174 ARG B NH1   1 
ATOM   17450 N  NH2   . ARG B 1  1176 ? 26.675  56.352  55.788  1.00 39.57 ? 1174 ARG B NH2   1 
ATOM   17451 N  N     . ALA B 1  1177 ? 27.503  60.202  62.257  1.00 22.33 ? 1175 ALA B N     1 
ATOM   17452 C  CA    . ALA B 1  1177 ? 28.537  60.706  63.148  1.00 22.68 ? 1175 ALA B CA    1 
ATOM   17453 C  C     . ALA B 1  1177 ? 28.044  60.734  64.588  1.00 19.91 ? 1175 ALA B C     1 
ATOM   17454 O  O     . ALA B 1  1177 ? 28.779  60.378  65.518  1.00 20.44 ? 1175 ALA B O     1 
ATOM   17455 C  CB    . ALA B 1  1177 ? 28.975  62.102  62.694  1.00 24.38 ? 1175 ALA B CB    1 
ATOM   17456 N  N     . VAL B 1  1178 ? 26.788  61.130  64.784  1.00 22.25 ? 1176 VAL B N     1 
ATOM   17457 C  CA    . VAL B 1  1178 ? 26.240  61.204  66.131  1.00 19.82 ? 1176 VAL B CA    1 
ATOM   17458 C  C     . VAL B 1  1178 ? 26.033  59.803  66.688  1.00 20.30 ? 1176 VAL B C     1 
ATOM   17459 O  O     . VAL B 1  1178 ? 26.320  59.534  67.859  1.00 20.25 ? 1176 VAL B O     1 
ATOM   17460 C  CB    . VAL B 1  1178 ? 24.940  62.026  66.118  1.00 18.94 ? 1176 VAL B CB    1 
ATOM   17461 C  CG1   . VAL B 1  1178 ? 24.266  61.987  67.483  1.00 20.27 ? 1176 VAL B CG1   1 
ATOM   17462 C  CG2   . VAL B 1  1178 ? 25.240  63.468  65.758  1.00 20.99 ? 1176 VAL B CG2   1 
ATOM   17463 N  N     . ASN B 1  1179 ? 25.563  58.884  65.845  1.00 20.51 ? 1177 ASN B N     1 
ATOM   17464 C  CA    . ASN B 1  1179 ? 25.311  57.519  66.293  1.00 21.34 ? 1177 ASN B CA    1 
ATOM   17465 C  C     . ASN B 1  1179 ? 26.613  56.838  66.695  1.00 20.83 ? 1177 ASN B C     1 
ATOM   17466 O  O     . ASN B 1  1179 ? 26.665  56.122  67.703  1.00 21.83 ? 1177 ASN B O     1 
ATOM   17467 C  CB    . ASN B 1  1179 ? 24.587  56.756  65.179  1.00 20.42 ? 1177 ASN B CB    1 
ATOM   17468 C  CG    . ASN B 1  1179 ? 23.898  55.502  65.673  1.00 26.20 ? 1177 ASN B CG    1 
ATOM   17469 O  OD1   . ASN B 1  1179 ? 23.457  55.429  66.816  1.00 24.35 ? 1177 ASN B OD1   1 
ATOM   17470 N  ND2   . ASN B 1  1179 ? 23.795  54.506  64.800  1.00 23.72 ? 1177 ASN B ND2   1 
ATOM   17471 N  N     . LYS B 1  1180 ? 27.689  57.084  65.942  1.00 22.18 ? 1178 LYS B N     1 
ATOM   17472 C  CA    . LYS B 1  1180 ? 28.995  56.570  66.339  1.00 20.32 ? 1178 LYS B CA    1 
ATOM   17473 C  C     . LYS B 1  1180 ? 29.424  57.138  67.685  1.00 19.91 ? 1178 LYS B C     1 
ATOM   17474 O  O     . LYS B 1  1180 ? 29.931  56.403  68.539  1.00 21.47 ? 1178 LYS B O     1 
ATOM   17475 C  CB    . LYS B 1  1180 ? 30.049  56.888  65.275  1.00 23.62 ? 1178 LYS B CB    1 
ATOM   17476 C  CG    . LYS B 1  1180 ? 29.816  56.233  63.931  1.00 28.66 ? 1178 LYS B CG    1 
ATOM   17477 C  CD    . LYS B 1  1180 ? 31.013  56.474  63.000  1.00 31.38 ? 1178 LYS B CD    1 
ATOM   17478 C  CE    . LYS B 1  1180 ? 32.192  55.603  63.384  1.00 35.05 ? 1178 LYS B CE    1 
ATOM   17479 N  NZ    . LYS B 1  1180 ? 31.873  54.142  63.262  1.00 34.29 ? 1178 LYS B NZ    1 
ATOM   17480 N  N     . ALA B 1  1181 ? 29.229  58.445  67.893  1.00 20.06 ? 1179 ALA B N     1 
ATOM   17481 C  CA    . ALA B 1  1181 ? 29.610  59.042  69.168  1.00 18.88 ? 1179 ALA B CA    1 
ATOM   17482 C  C     . ALA B 1  1181 ? 28.786  58.467  70.313  1.00 19.14 ? 1179 ALA B C     1 
ATOM   17483 O  O     . ALA B 1  1181 ? 29.317  58.224  71.404  1.00 20.83 ? 1179 ALA B O     1 
ATOM   17484 C  CB    . ALA B 1  1181 ? 29.462  60.563  69.117  1.00 20.51 ? 1179 ALA B CB    1 
ATOM   17485 N  N     . ILE B 1  1182 ? 27.490  58.231  70.079  1.00 18.99 ? 1180 ILE B N     1 
ATOM   17486 C  CA    . ILE B 1  1182 ? 26.638  57.688  71.133  1.00 20.26 ? 1180 ILE B CA    1 
ATOM   17487 C  C     . ILE B 1  1182 ? 27.042  56.259  71.464  1.00 19.89 ? 1180 ILE B C     1 
ATOM   17488 O  O     . ILE B 1  1182 ? 27.092  55.870  72.636  1.00 20.11 ? 1180 ILE B O     1 
ATOM   17489 C  CB    . ILE B 1  1182 ? 25.155  57.783  70.722  1.00 19.36 ? 1180 ILE B CB    1 
ATOM   17490 C  CG1   . ILE B 1  1182 ? 24.715  59.252  70.743  1.00 20.37 ? 1180 ILE B CG1   1 
ATOM   17491 C  CG2   . ILE B 1  1182 ? 24.295  56.935  71.640  1.00 22.82 ? 1180 ILE B CG2   1 
ATOM   17492 C  CD1   . ILE B 1  1182 ? 23.308  59.498  70.164  1.00 19.21 ? 1180 ILE B CD1   1 
ATOM   17493 N  N     . ALA B 1  1183 ? 27.361  55.458  70.444  1.00 23.16 ? 1181 ALA B N     1 
ATOM   17494 C  CA    . ALA B 1  1183 ? 27.802  54.094  70.710  1.00 21.78 ? 1181 ALA B CA    1 
ATOM   17495 C  C     . ALA B 1  1183 ? 29.086  54.053  71.526  1.00 22.88 ? 1181 ALA B C     1 
ATOM   17496 O  O     . ALA B 1  1183 ? 29.333  53.063  72.221  1.00 25.43 ? 1181 ALA B O     1 
ATOM   17497 C  CB    . ALA B 1  1183 ? 27.985  53.323  69.400  1.00 22.35 ? 1181 ALA B CB    1 
ATOM   17498 N  N     . ALA B 1  1184 ? 29.889  55.113  71.494  1.00 20.85 ? 1182 ALA B N     1 
ATOM   17499 C  CA    . ALA B 1  1184 ? 31.116  55.159  72.277  1.00 21.80 ? 1182 ALA B CA    1 
ATOM   17500 C  C     . ALA B 1  1184 ? 30.903  55.688  73.686  1.00 22.14 ? 1182 ALA B C     1 
ATOM   17501 O  O     . ALA B 1  1184 ? 31.869  55.775  74.449  1.00 21.31 ? 1182 ALA B O     1 
ATOM   17502 C  CB    . ALA B 1  1184 ? 32.176  56.018  71.571  1.00 22.27 ? 1182 ALA B CB    1 
ATOM   17503 N  N     . LEU B 1  1185 ? 29.685  56.072  74.049  1.00 19.02 ? 1183 LEU B N     1 
ATOM   17504 C  CA    . LEU B 1  1185 ? 29.465  56.556  75.404  1.00 22.31 ? 1183 LEU B CA    1 
ATOM   17505 C  C     . LEU B 1  1185 ? 29.584  55.402  76.395  1.00 22.49 ? 1183 LEU B C     1 
ATOM   17506 O  O     . LEU B 1  1185 ? 29.141  54.284  76.108  1.00 22.90 ? 1183 LEU B O     1 
ATOM   17507 C  CB    . LEU B 1  1185 ? 28.087  57.201  75.541  1.00 20.28 ? 1183 LEU B CB    1 
ATOM   17508 C  CG    . LEU B 1  1185 ? 27.832  58.432  74.671  1.00 19.42 ? 1183 LEU B CG    1 
ATOM   17509 C  CD1   . LEU B 1  1185 ? 26.391  58.867  74.835  1.00 18.32 ? 1183 LEU B CD1   1 
ATOM   17510 C  CD2   . LEU B 1  1185 ? 28.807  59.563  75.022  1.00 19.98 ? 1183 LEU B CD2   1 
ATOM   17511 N  N     . PRO B 1  1186 ? 30.158  55.639  77.568  1.00 22.61 ? 1184 PRO B N     1 
ATOM   17512 C  CA    . PRO B 1  1186 ? 30.196  54.592  78.590  1.00 22.31 ? 1184 PRO B CA    1 
ATOM   17513 C  C     . PRO B 1  1186 ? 28.810  54.366  79.166  1.00 19.06 ? 1184 PRO B C     1 
ATOM   17514 O  O     . PRO B 1  1186 ? 27.901  55.183  79.009  1.00 24.33 ? 1184 PRO B O     1 
ATOM   17515 C  CB    . PRO B 1  1186 ? 31.141  55.168  79.648  1.00 26.69 ? 1184 PRO B CB    1 
ATOM   17516 C  CG    . PRO B 1  1186 ? 30.882  56.655  79.557  1.00 28.02 ? 1184 PRO B CG    1 
ATOM   17517 C  CD    . PRO B 1  1186 ? 30.643  56.933  78.083  1.00 24.20 ? 1184 PRO B CD    1 
ATOM   17518 N  N     . GLY B 1  1187 ? 28.656  53.235  79.840  1.00 20.67 ? 1185 GLY B N     1 
ATOM   17519 C  CA    . GLY B 1  1187 ? 27.419  52.968  80.537  1.00 21.27 ? 1185 GLY B CA    1 
ATOM   17520 C  C     . GLY B 1  1187 ? 26.388  52.280  79.671  1.00 21.43 ? 1185 GLY B C     1 
ATOM   17521 O  O     . GLY B 1  1187 ? 26.710  51.418  78.849  1.00 22.13 ? 1185 GLY B O     1 
ATOM   17522 N  N     . PRO B 1  1188 ? 25.119  52.629  79.851  1.00 18.32 ? 1186 PRO B N     1 
ATOM   17523 C  CA    . PRO B 1  1188 ? 24.064  51.899  79.140  1.00 17.20 ? 1186 PRO B CA    1 
ATOM   17524 C  C     . PRO B 1  1188 ? 24.106  52.142  77.641  1.00 18.45 ? 1186 PRO B C     1 
ATOM   17525 O  O     . PRO B 1  1188 ? 24.536  53.198  77.160  1.00 19.72 ? 1186 PRO B O     1 
ATOM   17526 C  CB    . PRO B 1  1188 ? 22.768  52.439  79.754  1.00 20.20 ? 1186 PRO B CB    1 
ATOM   17527 C  CG    . PRO B 1  1188 ? 23.140  53.743  80.404  1.00 23.35 ? 1186 PRO B CG    1 
ATOM   17528 C  CD    . PRO B 1  1188 ? 24.596  53.656  80.771  1.00 18.03 ? 1186 PRO B CD    1 
ATOM   17529 N  N     . LEU B 1  1189 ? 23.623  51.145  76.902  1.00 18.25 ? 1187 LEU B N     1 
ATOM   17530 C  CA    . LEU B 1  1189 ? 23.432  51.275  75.461  1.00 17.38 ? 1187 LEU B CA    1 
ATOM   17531 C  C     . LEU B 1  1189 ? 22.190  52.111  75.206  1.00 17.50 ? 1187 LEU B C     1 
ATOM   17532 O  O     . LEU B 1  1189 ? 21.093  51.733  75.636  1.00 18.68 ? 1187 LEU B O     1 
ATOM   17533 C  CB    . LEU B 1  1189 ? 23.278  49.902  74.812  1.00 15.86 ? 1187 LEU B CB    1 
ATOM   17534 C  CG    . LEU B 1  1189 ? 24.577  49.145  74.541  1.00 17.77 ? 1187 LEU B CG    1 
ATOM   17535 C  CD1   . LEU B 1  1189 ? 25.157  48.591  75.836  1.00 22.73 ? 1187 LEU B CD1   1 
ATOM   17536 C  CD2   . LEU B 1  1189 ? 24.294  48.029  73.543  1.00 18.29 ? 1187 LEU B CD2   1 
ATOM   17537 N  N     . LEU B 1  1190 ? 22.342  53.238  74.515  1.00 16.62 ? 1188 LEU B N     1 
ATOM   17538 C  CA    . LEU B 1  1190 ? 21.224  54.161  74.341  1.00 18.06 ? 1188 LEU B CA    1 
ATOM   17539 C  C     . LEU B 1  1190 ? 20.363  53.763  73.148  1.00 19.09 ? 1188 LEU B C     1 
ATOM   17540 O  O     . LEU B 1  1190 ? 20.873  53.431  72.071  1.00 18.57 ? 1188 LEU B O     1 
ATOM   17541 C  CB    . LEU B 1  1190 ? 21.703  55.602  74.156  1.00 18.89 ? 1188 LEU B CB    1 
ATOM   17542 C  CG    . LEU B 1  1190 ? 22.518  56.213  75.298  1.00 16.59 ? 1188 LEU B CG    1 
ATOM   17543 C  CD1   . LEU B 1  1190 ? 22.609  57.719  75.093  1.00 17.64 ? 1188 LEU B CD1   1 
ATOM   17544 C  CD2   . LEU B 1  1190 ? 21.885  55.866  76.648  1.00 18.87 ? 1188 LEU B CD2   1 
ATOM   17545 N  N     . LEU B 1  1191 ? 19.052  53.814  73.350  1.00 18.05 ? 1189 LEU B N     1 
ATOM   17546 C  CA    . LEU B 1  1191 ? 18.100  53.663  72.255  1.00 16.08 ? 1189 LEU B CA    1 
ATOM   17547 C  C     . LEU B 1  1191 ? 18.019  54.998  71.520  1.00 16.26 ? 1189 LEU B C     1 
ATOM   17548 O  O     . LEU B 1  1191 ? 17.456  55.972  72.041  1.00 19.08 ? 1189 LEU B O     1 
ATOM   17549 C  CB    . LEU B 1  1191 ? 16.743  53.226  72.796  1.00 15.86 ? 1189 LEU B CB    1 
ATOM   17550 C  CG    . LEU B 1  1191 ? 15.765  52.566  71.819  1.00 17.83 ? 1189 LEU B CG    1 
ATOM   17551 C  CD1   . LEU B 1  1191 ? 14.635  51.933  72.617  1.00 15.97 ? 1189 LEU B CD1   1 
ATOM   17552 C  CD2   . LEU B 1  1191 ? 15.219  53.579  70.824  1.00 15.99 ? 1189 LEU B CD2   1 
ATOM   17553 N  N     . VAL B 1  1192 ? 18.589  55.040  70.317  1.00 15.71 ? 1190 VAL B N     1 
ATOM   17554 C  CA    . VAL B 1  1192 ? 18.739  56.260  69.525  1.00 16.68 ? 1190 VAL B CA    1 
ATOM   17555 C  C     . VAL B 1  1192 ? 17.615  56.335  68.503  1.00 17.52 ? 1190 VAL B C     1 
ATOM   17556 O  O     . VAL B 1  1192 ? 17.332  55.354  67.806  1.00 20.21 ? 1190 VAL B O     1 
ATOM   17557 C  CB    . VAL B 1  1192 ? 20.108  56.292  68.822  1.00 17.42 ? 1190 VAL B CB    1 
ATOM   17558 C  CG1   . VAL B 1  1192 ? 20.221  57.500  67.921  1.00 19.47 ? 1190 VAL B CG1   1 
ATOM   17559 C  CG2   . VAL B 1  1192 ? 21.264  56.256  69.855  1.00 17.47 ? 1190 VAL B CG2   1 
ATOM   17560 N  N     . GLN B 1  1193 ? 16.982  57.498  68.407  1.00 18.04 ? 1191 GLN B N     1 
ATOM   17561 C  CA    . GLN B 1  1193 ? 16.025  57.789  67.348  1.00 16.93 ? 1191 GLN B CA    1 
ATOM   17562 C  C     . GLN B 1  1193 ? 16.529  58.981  66.560  1.00 18.91 ? 1191 GLN B C     1 
ATOM   17563 O  O     . GLN B 1  1193 ? 16.864  60.010  67.152  1.00 18.25 ? 1191 GLN B O     1 
ATOM   17564 C  CB    . GLN B 1  1193 ? 14.649  58.114  67.909  1.00 19.90 ? 1191 GLN B CB    1 
ATOM   17565 C  CG    . GLN B 1  1193 ? 14.107  57.051  68.812  1.00 18.24 ? 1191 GLN B CG    1 
ATOM   17566 C  CD    . GLN B 1  1193 ? 12.636  57.238  69.028  1.00 18.66 ? 1191 GLN B CD    1 
ATOM   17567 O  OE1   . GLN B 1  1193 ? 11.857  57.152  68.086  1.00 18.84 ? 1191 GLN B OE1   1 
ATOM   17568 N  NE2   . GLN B 1  1193 ? 12.248  57.534  70.260  1.00 17.73 ? 1191 GLN B NE2   1 
ATOM   17569 N  N     . ALA B 1  1194 ? 16.551  58.860  65.236  1.00 17.87 ? 1192 ALA B N     1 
ATOM   17570 C  CA    . ALA B 1  1194 ? 17.061  59.939  64.403  1.00 19.64 ? 1192 ALA B CA    1 
ATOM   17571 C  C     . ALA B 1  1194 ? 16.046  60.302  63.337  1.00 22.97 ? 1192 ALA B C     1 
ATOM   17572 O  O     . ALA B 1  1194 ? 15.237  59.470  62.909  1.00 22.57 ? 1192 ALA B O     1 
ATOM   17573 C  CB    . ALA B 1  1194 ? 18.385  59.567  63.747  1.00 19.95 ? 1192 ALA B CB    1 
ATOM   17574 N  N     . ALA B 1  1195 ? 16.096  61.564  62.922  1.00 19.55 ? 1193 ALA B N     1 
ATOM   17575 C  CA    . ALA B 1  1195 ? 15.238  62.040  61.853  1.00 22.39 ? 1193 ALA B CA    1 
ATOM   17576 C  C     . ALA B 1  1195 ? 15.901  63.250  61.217  1.00 25.17 ? 1193 ALA B C     1 
ATOM   17577 O  O     . ALA B 1  1195 ? 16.671  63.964  61.864  1.00 21.97 ? 1193 ALA B O     1 
ATOM   17578 C  CB    . ALA B 1  1195 ? 13.844  62.401  62.376  1.00 24.75 ? 1193 ALA B CB    1 
ATOM   17579 N  N     . SER B 1  1196 ? 15.603  63.464  59.940  1.00 25.37 ? 1194 SER B N     1 
ATOM   17580 C  CA    . SER B 1  1196 ? 16.036  64.688  59.287  1.00 25.82 ? 1194 SER B CA    1 
ATOM   17581 C  C     . SER B 1  1196 ? 15.130  65.848  59.683  1.00 25.44 ? 1194 SER B C     1 
ATOM   17582 O  O     . SER B 1  1196 ? 14.010  65.661  60.172  1.00 24.13 ? 1194 SER B O     1 
ATOM   17583 C  CB    . SER B 1  1196 ? 16.008  64.528  57.774  1.00 28.73 ? 1194 SER B CB    1 
ATOM   17584 O  OG    . SER B 1  1196 ? 14.667  64.483  57.333  1.00 28.27 ? 1194 SER B OG    1 
ATOM   17585 N  N     . SER B 1  1197 ? 15.624  67.067  59.449  1.00 25.71 ? 1195 SER B N     1 
ATOM   17586 C  CA    . SER B 1  1197 ? 14.801  68.249  59.685  1.00 25.91 ? 1195 SER B CA    1 
ATOM   17587 C  C     . SER B 1  1197 ? 13.517  68.198  58.871  1.00 26.82 ? 1195 SER B C     1 
ATOM   17588 O  O     . SER B 1  1197 ? 12.449  68.581  59.358  1.00 24.64 ? 1195 SER B O     1 
ATOM   17589 C  CB    . SER B 1  1197 ? 15.583  69.517  59.348  1.00 24.73 ? 1195 SER B CB    1 
ATOM   17590 O  OG    . SER B 1  1197 ? 16.724  69.646  60.173  1.00 23.34 ? 1195 SER B OG    1 
ATOM   17591 N  N     . GLY B 1  1198 ? 13.601  67.736  57.625  1.00 26.56 ? 1196 GLY B N     1 
ATOM   17592 C  CA    . GLY B 1  1198 ? 12.404  67.638  56.812  1.00 32.46 ? 1196 GLY B CA    1 
ATOM   17593 C  C     . GLY B 1  1198 ? 11.454  66.567  57.297  1.00 32.21 ? 1196 GLY B C     1 
ATOM   17594 O  O     . GLY B 1  1198 ? 10.233  66.721  57.190  1.00 30.22 ? 1196 GLY B O     1 
ATOM   17595 N  N     . GLU B 1  1199 ? 11.995  65.474  57.841  1.00 30.07 ? 1197 GLU B N     1 
ATOM   17596 C  CA    . GLU B 1  1199 ? 11.142  64.433  58.397  1.00 29.18 ? 1197 GLU B CA    1 
ATOM   17597 C  C     . GLU B 1  1199 ? 10.391  64.944  59.619  1.00 29.44 ? 1197 GLU B C     1 
ATOM   17598 O  O     . GLU B 1  1199 ? 9.200   64.660  59.785  1.00 29.43 ? 1197 GLU B O     1 
ATOM   17599 C  CB    . GLU B 1  1199 ? 11.976  63.196  58.744  1.00 29.22 ? 1197 GLU B CB    1 
ATOM   17600 C  CG    . GLU B 1  1199 ? 11.126  62.015  59.163  1.00 35.45 ? 1197 GLU B CG    1 
ATOM   17601 C  CD    . GLU B 1  1199 ? 11.934  60.752  59.399  1.00 40.36 ? 1197 GLU B CD    1 
ATOM   17602 O  OE1   . GLU B 1  1199 ? 13.174  60.786  59.224  1.00 40.04 ? 1197 GLU B OE1   1 
ATOM   17603 O  OE2   . GLU B 1  1199 ? 11.322  59.726  59.763  1.00 44.42 ? 1197 GLU B OE2   1 
ATOM   17604 N  N     . ILE B 1  1200 ? 11.064  65.721  60.474  1.00 25.58 ? 1198 ILE B N     1 
ATOM   17605 C  CA    . ILE B 1  1200 ? 10.398  66.284  61.644  1.00 24.60 ? 1198 ILE B CA    1 
ATOM   17606 C  C     . ILE B 1  1200 ? 9.236   67.173  61.226  1.00 29.55 ? 1198 ILE B C     1 
ATOM   17607 O  O     . ILE B 1  1200 ? 8.159   67.138  61.833  1.00 26.34 ? 1198 ILE B O     1 
ATOM   17608 C  CB    . ILE B 1  1200 ? 11.414  67.046  62.513  1.00 23.37 ? 1198 ILE B CB    1 
ATOM   17609 C  CG1   . ILE B 1  1200 ? 12.431  66.066  63.113  1.00 23.69 ? 1198 ILE B CG1   1 
ATOM   17610 C  CG2   . ILE B 1  1200 ? 10.689  67.853  63.591  1.00 24.02 ? 1198 ILE B CG2   1 
ATOM   17611 C  CD1   . ILE B 1  1200 ? 13.535  66.744  63.917  1.00 23.10 ? 1198 ILE B CD1   1 
ATOM   17612 N  N     . ALA B 1  1201 ? 9.426   67.972  60.177  1.00 27.93 ? 1199 ALA B N     1 
ATOM   17613 C  CA    . ALA B 1  1201 ? 8.372   68.888  59.755  1.00 26.89 ? 1199 ALA B CA    1 
ATOM   17614 C  C     . ALA B 1  1201 ? 7.197   68.159  59.112  1.00 29.64 ? 1199 ALA B C     1 
ATOM   17615 O  O     . ALA B 1  1201 ? 6.049   68.590  59.264  1.00 32.38 ? 1199 ALA B O     1 
ATOM   17616 C  CB    . ALA B 1  1201 ? 8.940   69.930  58.790  1.00 31.93 ? 1199 ALA B CB    1 
ATOM   17617 N  N     . ARG B 1  1202 ? 7.453   67.059  58.404  1.00 31.08 ? 1200 ARG B N     1 
ATOM   17618 C  CA    . ARG B 1  1202 ? 6.412   66.411  57.613  1.00 32.20 ? 1200 ARG B CA    1 
ATOM   17619 C  C     . ARG B 1  1202 ? 5.727   65.257  58.332  1.00 33.92 ? 1200 ARG B C     1 
ATOM   17620 O  O     . ARG B 1  1202 ? 4.564   64.964  58.032  1.00 36.17 ? 1200 ARG B O     1 
ATOM   17621 C  CB    . ARG B 1  1202 ? 6.993   65.899  56.290  1.00 36.42 ? 1200 ARG B CB    1 
ATOM   17622 C  CG    . ARG B 1  1202 ? 7.707   64.562  56.380  1.00 36.60 ? 1200 ARG B CG    1 
ATOM   17623 C  CD    . ARG B 1  1202 ? 8.173   64.083  55.007  1.00 43.87 ? 1200 ARG B CD    1 
ATOM   17624 N  NE    . ARG B 1  1202 ? 9.282   64.884  54.500  1.00 41.67 ? 1200 ARG B NE    1 
ATOM   17625 C  CZ    . ARG B 1  1202 ? 10.555  64.514  54.541  1.00 42.22 ? 1200 ARG B CZ    1 
ATOM   17626 N  NH1   . ARG B 1  1202 ? 10.921  63.338  55.033  1.00 40.24 ? 1200 ARG B NH1   1 
ATOM   17627 N  NH2   . ARG B 1  1202 ? 11.485  65.344  54.075  1.00 44.55 ? 1200 ARG B NH2   1 
ATOM   17628 N  N     . ASN B 1  1203 ? 6.401   64.608  59.275  1.00 29.73 ? 1201 ASN B N     1 
ATOM   17629 C  CA    . ASN B 1  1203 ? 5.899   63.388  59.911  1.00 30.62 ? 1201 ASN B CA    1 
ATOM   17630 C  C     . ASN B 1  1203 ? 5.708   63.623  61.401  1.00 31.80 ? 1201 ASN B C     1 
ATOM   17631 O  O     . ASN B 1  1203 ? 6.706   63.706  62.143  1.00 28.79 ? 1201 ASN B O     1 
ATOM   17632 C  CB    . ASN B 1  1203 ? 6.873   62.236  59.660  1.00 32.05 ? 1201 ASN B CB    1 
ATOM   17633 C  CG    . ASN B 1  1203 ? 6.448   60.932  60.319  1.00 32.35 ? 1201 ASN B CG    1 
ATOM   17634 O  OD1   . ASN B 1  1203 ? 5.333   60.802  60.838  1.00 32.20 ? 1201 ASN B OD1   1 
ATOM   17635 N  ND2   . ASN B 1  1203 ? 7.348   59.954  60.300  1.00 31.30 ? 1201 ASN B ND2   1 
ATOM   17636 N  N     . PRO B 1  1204 ? 4.471   63.728  61.894  1.00 31.22 ? 1202 PRO B N     1 
ATOM   17637 C  CA    . PRO B 1  1204 ? 4.275   63.939  63.338  1.00 30.90 ? 1202 PRO B CA    1 
ATOM   17638 C  C     . PRO B 1  1204 ? 4.854   62.831  64.203  1.00 27.11 ? 1202 PRO B C     1 
ATOM   17639 O  O     . PRO B 1  1204 ? 5.154   63.081  65.375  1.00 30.45 ? 1202 PRO B O     1 
ATOM   17640 C  CB    . PRO B 1  1204 ? 2.747   64.027  63.482  1.00 34.97 ? 1202 PRO B CB    1 
ATOM   17641 C  CG    . PRO B 1  1204 ? 2.189   63.451  62.211  1.00 34.20 ? 1202 PRO B CG    1 
ATOM   17642 C  CD    . PRO B 1  1204 ? 3.199   63.758  61.148  1.00 32.39 ? 1202 PRO B CD    1 
ATOM   17643 N  N     . ASP B 1  1205 ? 5.033   61.622  63.669  1.00 26.26 ? 1203 ASP B N     1 
ATOM   17644 C  CA    . ASP B 1  1205 ? 5.609   60.518  64.423  1.00 29.08 ? 1203 ASP B CA    1 
ATOM   17645 C  C     . ASP B 1  1205 ? 7.079   60.288  64.093  1.00 29.64 ? 1203 ASP B C     1 
ATOM   17646 O  O     . ASP B 1  1205 ? 7.575   59.170  64.274  1.00 27.21 ? 1203 ASP B O     1 
ATOM   17647 C  CB    . ASP B 1  1205 ? 4.819   59.230  64.179  1.00 31.20 ? 1203 ASP B CB    1 
ATOM   17648 C  CG    . ASP B 1  1205 ? 3.409   59.290  64.744  1.00 32.76 ? 1203 ASP B CG    1 
ATOM   17649 O  OD1   . ASP B 1  1205 ? 3.172   60.053  65.706  1.00 32.17 ? 1203 ASP B OD1   1 
ATOM   17650 O  OD2   . ASP B 1  1205 ? 2.539   58.560  64.229  1.00 35.68 ? 1203 ASP B OD2   1 
ATOM   17651 N  N     . ALA B 1  1206 ? 7.782   61.318  63.611  1.00 26.83 ? 1204 ALA B N     1 
ATOM   17652 C  CA    . ALA B 1  1206 ? 9.202   61.168  63.291  1.00 29.17 ? 1204 ALA B CA    1 
ATOM   17653 C  C     . ALA B 1  1206 ? 9.986   60.607  64.475  1.00 23.31 ? 1204 ALA B C     1 
ATOM   17654 O  O     . ALA B 1  1206 ? 10.893  59.782  64.297  1.00 24.57 ? 1204 ALA B O     1 
ATOM   17655 C  CB    . ALA B 1  1206 ? 9.781   62.513  62.847  1.00 28.81 ? 1204 ALA B CB    1 
ATOM   17656 N  N     . TYR B 1  1207 ? 9.658   61.048  65.690  1.00 22.94 ? 1205 TYR B N     1 
ATOM   17657 C  CA    . TYR B 1  1207 ? 10.154  60.429  66.911  1.00 22.58 ? 1205 TYR B CA    1 
ATOM   17658 C  C     . TYR B 1  1207 ? 9.021   59.647  67.556  1.00 22.75 ? 1205 TYR B C     1 
ATOM   17659 O  O     . TYR B 1  1207 ? 7.911   60.166  67.706  1.00 26.78 ? 1205 TYR B O     1 
ATOM   17660 C  CB    . TYR B 1  1207 ? 10.706  61.468  67.885  1.00 20.85 ? 1205 TYR B CB    1 
ATOM   17661 C  CG    . TYR B 1  1207 ? 11.881  62.229  67.332  1.00 19.64 ? 1205 TYR B CG    1 
ATOM   17662 C  CD1   . TYR B 1  1207 ? 13.040  61.566  66.956  1.00 20.36 ? 1205 TYR B CD1   1 
ATOM   17663 C  CD2   . TYR B 1  1207 ? 11.831  63.609  67.179  1.00 21.20 ? 1205 TYR B CD2   1 
ATOM   17664 C  CE1   . TYR B 1  1207 ? 14.124  62.259  66.453  1.00 19.11 ? 1205 TYR B CE1   1 
ATOM   17665 C  CE2   . TYR B 1  1207 ? 12.912  64.314  66.674  1.00 19.77 ? 1205 TYR B CE2   1 
ATOM   17666 C  CZ    . TYR B 1  1207 ? 14.056  63.631  66.314  1.00 20.83 ? 1205 TYR B CZ    1 
ATOM   17667 O  OH    . TYR B 1  1207 ? 15.133  64.318  65.809  1.00 20.20 ? 1205 TYR B OH    1 
ATOM   17668 N  N     . CYS B 1  1208 ? 9.299   58.404  67.913  1.00 17.95 ? 1206 CYS B N     1 
ATOM   17669 C  CA    . CYS B 1  1208 ? 8.290   57.481  68.421  1.00 18.27 ? 1206 CYS B CA    1 
ATOM   17670 C  C     . CYS B 1  1208 ? 8.287   57.511  69.946  1.00 16.61 ? 1206 CYS B C     1 
ATOM   17671 O  O     . CYS B 1  1208 ? 9.311   57.235  70.575  1.00 17.41 ? 1206 CYS B O     1 
ATOM   17672 C  CB    . CYS B 1  1208 ? 8.568   56.073  67.906  1.00 22.02 ? 1206 CYS B CB    1 
ATOM   17673 S  SG    . CYS B 1  1208 ? 7.353   54.882  68.477  1.00 22.02 ? 1206 CYS B SG    1 
ATOM   17674 N  N     . LEU B 1  1209 ? 7.133   57.834  70.543  1.00 17.08 ? 1207 LEU B N     1 
ATOM   17675 C  CA    . LEU B 1  1209 ? 7.071   57.916  72.000  1.00 18.61 ? 1207 LEU B CA    1 
ATOM   17676 C  C     . LEU B 1  1209 ? 7.110   56.548  72.664  1.00 17.37 ? 1207 LEU B C     1 
ATOM   17677 O  O     . LEU B 1  1209 ? 7.323   56.478  73.879  1.00 15.81 ? 1207 LEU B O     1 
ATOM   17678 C  CB    . LEU B 1  1209 ? 5.814   58.668  72.442  1.00 14.91 ? 1207 LEU B CB    1 
ATOM   17679 C  CG    . LEU B 1  1209 ? 5.610   60.037  71.783  1.00 19.68 ? 1207 LEU B CG    1 
ATOM   17680 C  CD1   . LEU B 1  1209 ? 4.433   60.771  72.429  1.00 19.55 ? 1207 LEU B CD1   1 
ATOM   17681 C  CD2   . LEU B 1  1209 ? 6.881   60.873  71.842  1.00 20.79 ? 1207 LEU B CD2   1 
ATOM   17682 N  N     . ASN B 1  1210 ? 6.910   55.466  71.905  1.00 17.32 ? 1208 ASN B N     1 
ATOM   17683 C  CA    . ASN B 1  1210 ? 6.992   54.136  72.496  1.00 18.59 ? 1208 ASN B CA    1 
ATOM   17684 C  C     . ASN B 1  1210 ? 8.344   53.906  73.152  1.00 17.92 ? 1208 ASN B C     1 
ATOM   17685 O  O     . ASN B 1  1210 ? 8.430   53.213  74.172  1.00 19.37 ? 1208 ASN B O     1 
ATOM   17686 C  CB    . ASN B 1  1210 ? 6.751   53.042  71.440  1.00 20.50 ? 1208 ASN B CB    1 
ATOM   17687 C  CG    . ASN B 1  1210 ? 5.347   53.097  70.816  1.00 20.76 ? 1208 ASN B CG    1 
ATOM   17688 O  OD1   . ASN B 1  1210 ? 4.654   54.108  70.890  1.00 22.72 ? 1208 ASN B OD1   1 
ATOM   17689 N  ND2   . ASN B 1  1210 ? 4.948   52.010  70.171  1.00 26.68 ? 1208 ASN B ND2   1 
ATOM   17690 N  N     . TRP B 1  1211 ? 9.405   54.490  72.600  1.00 15.07 ? 1209 TRP B N     1 
ATOM   17691 C  CA    . TRP B 1  1211 ? 10.753  54.200  73.071  1.00 15.14 ? 1209 TRP B CA    1 
ATOM   17692 C  C     . TRP B 1  1211 ? 11.240  55.203  74.097  1.00 18.11 ? 1209 TRP B C     1 
ATOM   17693 O  O     . TRP B 1  1211 ? 12.374  55.074  74.575  1.00 18.47 ? 1209 TRP B O     1 
ATOM   17694 C  CB    . TRP B 1  1211 ? 11.735  54.149  71.886  1.00 18.53 ? 1209 TRP B CB    1 
ATOM   17695 C  CG    . TRP B 1  1211 ? 11.144  53.514  70.677  1.00 18.21 ? 1209 TRP B CG    1 
ATOM   17696 C  CD1   . TRP B 1  1211 ? 11.063  54.053  69.415  1.00 19.44 ? 1209 TRP B CD1   1 
ATOM   17697 C  CD2   . TRP B 1  1211 ? 10.504  52.241  70.610  1.00 18.94 ? 1209 TRP B CD2   1 
ATOM   17698 N  NE1   . TRP B 1  1211 ? 10.419  53.182  68.572  1.00 20.46 ? 1209 TRP B NE1   1 
ATOM   17699 C  CE2   . TRP B 1  1211 ? 10.072  52.060  69.279  1.00 20.55 ? 1209 TRP B CE2   1 
ATOM   17700 C  CE3   . TRP B 1  1211 ? 10.241  51.233  71.550  1.00 19.07 ? 1209 TRP B CE3   1 
ATOM   17701 C  CZ2   . TRP B 1  1211 ? 9.393   50.910  68.865  1.00 22.93 ? 1209 TRP B CZ2   1 
ATOM   17702 C  CZ3   . TRP B 1  1211 ? 9.575   50.089  71.132  1.00 19.10 ? 1209 TRP B CZ3   1 
ATOM   17703 C  CH2   . TRP B 1  1211 ? 9.154   49.939  69.806  1.00 18.49 ? 1209 TRP B CH2   1 
ATOM   17704 N  N     . LEU B 1  1212 ? 10.415  56.188  74.445  1.00 15.92 ? 1210 LEU B N     1 
ATOM   17705 C  CA    . LEU B 1  1212 ? 10.786  57.227  75.395  1.00 14.53 ? 1210 LEU B CA    1 
ATOM   17706 C  C     . LEU B 1  1212 ? 10.179  56.993  76.767  1.00 15.28 ? 1210 LEU B C     1 
ATOM   17707 O  O     . LEU B 1  1212 ? 10.335  57.832  77.655  1.00 16.00 ? 1210 LEU B O     1 
ATOM   17708 C  CB    . LEU B 1  1212 ? 10.382  58.601  74.853  1.00 15.45 ? 1210 LEU B CB    1 
ATOM   17709 C  CG    . LEU B 1  1212 ? 11.336  59.049  73.735  1.00 15.40 ? 1210 LEU B CG    1 
ATOM   17710 C  CD1   . LEU B 1  1212 ? 10.748  60.182  72.930  1.00 17.70 ? 1210 LEU B CD1   1 
ATOM   17711 C  CD2   . LEU B 1  1212 ? 12.687  59.433  74.349  1.00 15.79 ? 1210 LEU B CD2   1 
ATOM   17712 N  N     . VAL B 1  1213 ? 9.504   55.863  76.959  1.00 14.93 ? 1211 VAL B N     1 
ATOM   17713 C  CA    . VAL B 1  1213 ? 9.044   55.450  78.271  1.00 14.38 ? 1211 VAL B CA    1 
ATOM   17714 C  C     . VAL B 1  1213 ? 9.764   54.161  78.630  1.00 15.28 ? 1211 VAL B C     1 
ATOM   17715 O  O     . VAL B 1  1213 ? 10.261  53.438  77.765  1.00 17.39 ? 1211 VAL B O     1 
ATOM   17716 C  CB    . VAL B 1  1213 ? 7.515   55.254  78.321  1.00 15.41 ? 1211 VAL B CB    1 
ATOM   17717 C  CG1   . VAL B 1  1213 ? 6.808   56.613  78.210  1.00 16.83 ? 1211 VAL B CG1   1 
ATOM   17718 C  CG2   . VAL B 1  1213 ? 7.089   54.305  77.203  1.00 16.05 ? 1211 VAL B CG2   1 
ATOM   17719 N  N     . GLU B 1  1214 ? 9.846   53.893  79.928  1.00 16.66 ? 1212 GLU B N     1 
ATOM   17720 C  CA    . GLU B 1  1214 ? 10.428  52.660  80.440  1.00 16.23 ? 1212 GLU B CA    1 
ATOM   17721 C  C     . GLU B 1  1214 ? 9.310   51.759  80.941  1.00 13.58 ? 1212 GLU B C     1 
ATOM   17722 O  O     . GLU B 1  1214 ? 8.474   52.190  81.738  1.00 14.72 ? 1212 GLU B O     1 
ATOM   17723 C  CB    . GLU B 1  1214 ? 11.419  52.918  81.585  1.00 17.51 ? 1212 GLU B CB    1 
ATOM   17724 C  CG    . GLU B 1  1214 ? 12.018  51.611  82.123  1.00 19.61 ? 1212 GLU B CG    1 
ATOM   17725 C  CD    . GLU B 1  1214 ? 12.901  51.773  83.357  1.00 22.89 ? 1212 GLU B CD    1 
ATOM   17726 O  OE1   . GLU B 1  1214 ? 13.406  52.887  83.606  1.00 23.70 ? 1212 GLU B OE1   1 
ATOM   17727 O  OE2   . GLU B 1  1214 ? 13.086  50.764  84.082  1.00 25.82 ? 1212 GLU B OE2   1 
ATOM   17728 N  N     . GLU B 1  1215 ? 9.315   50.511  80.484  1.00 16.00 ? 1213 GLU B N     1 
ATOM   17729 C  CA    . GLU B 1  1215 ? 8.377   49.508  80.976  1.00 14.63 ? 1213 GLU B CA    1 
ATOM   17730 C  C     . GLU B 1  1215 ? 8.836   48.920  82.302  1.00 13.00 ? 1213 GLU B C     1 
ATOM   17731 O  O     . GLU B 1  1215 ? 10.006  48.558  82.461  1.00 14.77 ? 1213 GLU B O     1 
ATOM   17732 C  CB    . GLU B 1  1215 ? 8.266   48.372  79.966  1.00 14.73 ? 1213 GLU B CB    1 
ATOM   17733 C  CG    . GLU B 1  1215 ? 7.785   48.784  78.607  1.00 15.88 ? 1213 GLU B CG    1 
ATOM   17734 C  CD    . GLU B 1  1215 ? 7.996   47.670  77.625  1.00 14.73 ? 1213 GLU B CD    1 
ATOM   17735 O  OE1   . GLU B 1  1215 ? 9.146   47.525  77.166  1.00 14.48 ? 1213 GLU B OE1   1 
ATOM   17736 O  OE2   . GLU B 1  1215 ? 7.037   46.918  77.355  1.00 15.35 ? 1213 GLU B OE2   1 
ATOM   17737 N  N     . VAL B 1  1216 ? 7.903   48.774  83.241  1.00 14.27 ? 1214 VAL B N     1 
ATOM   17738 C  CA    . VAL B 1  1216 ? 8.194   48.089  84.494  1.00 13.54 ? 1214 VAL B CA    1 
ATOM   17739 C  C     . VAL B 1  1216 ? 7.125   47.045  84.746  1.00 14.83 ? 1214 VAL B C     1 
ATOM   17740 O  O     . VAL B 1  1216 ? 5.924   47.351  84.734  1.00 14.78 ? 1214 VAL B O     1 
ATOM   17741 C  CB    . VAL B 1  1216 ? 8.289   49.051  85.690  1.00 14.18 ? 1214 VAL B CB    1 
ATOM   17742 C  CG1   . VAL B 1  1216 ? 8.503   48.234  86.995  1.00 16.11 ? 1214 VAL B CG1   1 
ATOM   17743 C  CG2   . VAL B 1  1216 ? 9.435   50.042  85.465  1.00 15.36 ? 1214 VAL B CG2   1 
ATOM   17744 N  N     . SER B 1  1217 ? 7.568   45.818  84.988  1.00 13.47 ? 1215 SER B N     1 
ATOM   17745 C  CA    . SER B 1  1217 ? 6.702   44.714  85.363  1.00 11.86 ? 1215 SER B CA    1 
ATOM   17746 C  C     . SER B 1  1217 ? 6.865   44.447  86.852  1.00 12.76 ? 1215 SER B C     1 
ATOM   17747 O  O     . SER B 1  1217 ? 7.982   44.449  87.366  1.00 13.70 ? 1215 SER B O     1 
ATOM   17748 C  CB    . SER B 1  1217 ? 7.077   43.474  84.548  1.00 15.57 ? 1215 SER B CB    1 
ATOM   17749 O  OG    . SER B 1  1217 ? 6.570   42.286  85.119  1.00 16.25 ? 1215 SER B OG    1 
ATOM   17750 N  N     . ALA B 1  1218 ? 5.746   44.249  87.547  1.00 12.34 ? 1216 ALA B N     1 
ATOM   17751 C  CA    . ALA B 1  1218 ? 5.777   43.876  88.953  1.00 13.99 ? 1216 ALA B CA    1 
ATOM   17752 C  C     . ALA B 1  1218 ? 4.848   42.693  89.171  1.00 15.19 ? 1216 ALA B C     1 
ATOM   17753 O  O     . ALA B 1  1218 ? 3.669   42.748  88.805  1.00 15.91 ? 1216 ALA B O     1 
ATOM   17754 C  CB    . ALA B 1  1218 ? 5.376   45.049  89.847  1.00 14.57 ? 1216 ALA B CB    1 
ATOM   17755 N  N     . SER B 1  1219 ? 5.368   41.635  89.784  1.00 15.01 ? 1217 SER B N     1 
ATOM   17756 C  CA    . SER B 1  1219 ? 4.586   40.439  90.069  1.00 14.59 ? 1217 SER B CA    1 
ATOM   17757 C  C     . SER B 1  1219 ? 4.502   40.271  91.575  1.00 13.81 ? 1217 SER B C     1 
ATOM   17758 O  O     . SER B 1  1219 ? 5.526   40.069  92.227  1.00 13.72 ? 1217 SER B O     1 
ATOM   17759 C  CB    . SER B 1  1219 ? 5.215   39.206  89.417  1.00 17.84 ? 1217 SER B CB    1 
ATOM   17760 O  OG    . SER B 1  1219 ? 4.413   38.049  89.632  1.00 16.24 ? 1217 SER B OG    1 
ATOM   17761 N  N     . ILE B 1  1220 ? 3.287   40.330  92.119  1.00 14.83 ? 1218 ILE B N     1 
ATOM   17762 C  CA    . ILE B 1  1220 ? 3.054   40.212  93.557  1.00 16.51 ? 1218 ILE B CA    1 
ATOM   17763 C  C     . ILE B 1  1220 ? 2.361   38.886  93.834  1.00 17.51 ? 1218 ILE B C     1 
ATOM   17764 O  O     . ILE B 1  1220 ? 1.296   38.608  93.275  1.00 17.07 ? 1218 ILE B O     1 
ATOM   17765 C  CB    . ILE B 1  1220 ? 2.195   41.374  94.083  1.00 19.55 ? 1218 ILE B CB    1 
ATOM   17766 C  CG1   . ILE B 1  1220 ? 2.780   42.711  93.617  1.00 19.57 ? 1218 ILE B CG1   1 
ATOM   17767 C  CG2   . ILE B 1  1220 ? 2.031   41.259  95.619  1.00 17.97 ? 1218 ILE B CG2   1 
ATOM   17768 C  CD1   . ILE B 1  1220 ? 1.807   43.864  93.722  1.00 28.72 ? 1218 ILE B CD1   1 
ATOM   17769 N  N     . ASN B 1  1221 ? 2.943   38.088  94.720  1.00 14.59 ? 1219 ASN B N     1 
ATOM   17770 C  CA    . ASN B 1  1221 ? 2.332   36.838  95.166  1.00 15.87 ? 1219 ASN B CA    1 
ATOM   17771 C  C     . ASN B 1  1221 ? 1.322   37.181  96.250  1.00 18.40 ? 1219 ASN B C     1 
ATOM   17772 O  O     . ASN B 1  1221 ? 1.699   37.474  97.387  1.00 21.69 ? 1219 ASN B O     1 
ATOM   17773 C  CB    . ASN B 1  1221 ? 3.414   35.898  95.684  1.00 16.94 ? 1219 ASN B CB    1 
ATOM   17774 C  CG    . ASN B 1  1221 ? 2.856   34.645  96.329  1.00 18.99 ? 1219 ASN B CG    1 
ATOM   17775 O  OD1   . ASN B 1  1221 ? 1.666   34.352  96.238  1.00 19.18 ? 1219 ASN B OD1   1 
ATOM   17776 N  ND2   . ASN B 1  1221 ? 3.736   33.885  96.979  1.00 21.40 ? 1219 ASN B ND2   1 
ATOM   17777 N  N     . THR B 1  1222 ? 0.037   37.161  95.908  1.00 15.62 ? 1220 THR B N     1 
ATOM   17778 C  CA    . THR B 1  1222 ? -1.011  37.534  96.852  1.00 19.98 ? 1220 THR B CA    1 
ATOM   17779 C  C     . THR B 1  1222 ? -1.524  36.352  97.650  1.00 24.46 ? 1220 THR B C     1 
ATOM   17780 O  O     . THR B 1  1222 ? -2.422  36.520  98.484  1.00 24.93 ? 1220 THR B O     1 
ATOM   17781 C  CB    . THR B 1  1222 ? -2.168  38.200  96.119  1.00 21.02 ? 1220 THR B CB    1 
ATOM   17782 O  OG1   . THR B 1  1222 ? -2.669  37.312  95.108  1.00 20.98 ? 1220 THR B OG1   1 
ATOM   17783 C  CG2   . THR B 1  1222 ? -1.686  39.481  95.454  1.00 21.55 ? 1220 THR B CG2   1 
ATOM   17784 N  N     . ALA B 1  1223 ? -0.974  35.169  97.423  1.00 24.36 ? 1221 ALA B N     1 
ATOM   17785 C  CA    . ALA B 1  1223 ? -1.236  34.025  98.279  1.00 28.60 ? 1221 ALA B CA    1 
ATOM   17786 C  C     . ALA B 1  1223 ? -0.216  33.887  99.404  1.00 30.84 ? 1221 ALA B C     1 
ATOM   17787 O  O     . ALA B 1  1223 ? -0.326  32.954  100.205 1.00 34.48 ? 1221 ALA B O     1 
ATOM   17788 C  CB    . ALA B 1  1223 ? -1.254  32.751  97.441  1.00 26.14 ? 1221 ALA B CB    1 
ATOM   17789 N  N     . ALA B 1  1224 ? 0.763   34.788  99.483  1.00 30.72 ? 1222 ALA B N     1 
ATOM   17790 C  CA    . ALA B 1  1224 ? 1.889   34.626  100.408 1.00 36.28 ? 1222 ALA B CA    1 
ATOM   17791 C  C     . ALA B 1  1224 ? 1.468   34.818  101.861 1.00 43.13 ? 1222 ALA B C     1 
ATOM   17792 O  O     . ALA B 1  1224 ? 2.133   34.323  102.773 1.00 44.09 ? 1222 ALA B O     1 
ATOM   17793 C  CB    . ALA B 1  1224 ? 3.017   35.598  100.054 1.00 29.83 ? 1222 ALA B CB    1 
HETATM 17794 P  PA    . P5F C 2  .    ? -38.479 43.683  82.920  1.00 21.99 ? 1301 P5F A PA    1 
HETATM 17795 O  O1A   . P5F C 2  .    ? -39.503 42.553  83.234  1.00 22.14 ? 1301 P5F A O1A   1 
HETATM 17796 O  O2A   . P5F C 2  .    ? -37.071 43.365  82.747  1.00 24.41 ? 1301 P5F A O2A   1 
HETATM 17797 O  O5B   . P5F C 2  .    ? -38.404 44.740  83.949  1.00 19.95 ? 1301 P5F A O5B   1 
HETATM 17798 C  C5B   . P5F C 2  .    ? -37.409 45.743  84.078  1.00 20.68 ? 1301 P5F A C5B   1 
HETATM 17799 C  C4B   . P5F C 2  .    ? -37.951 46.784  85.055  1.00 20.98 ? 1301 P5F A C4B   1 
HETATM 17800 O  O4B   . P5F C 2  .    ? -37.980 46.327  86.383  1.00 19.69 ? 1301 P5F A O4B   1 
HETATM 17801 C  C3B   . P5F C 2  .    ? -37.185 48.071  85.124  1.00 20.13 ? 1301 P5F A C3B   1 
HETATM 17802 O  O3B   . P5F C 2  .    ? -37.432 48.897  84.045  1.00 19.86 ? 1301 P5F A O3B   1 
HETATM 17803 C  C2B   . P5F C 2  .    ? -37.639 48.635  86.406  1.00 20.01 ? 1301 P5F A C2B   1 
HETATM 17804 O  O2B   . P5F C 2  .    ? -38.861 49.292  86.280  1.00 19.61 ? 1301 P5F A O2B   1 
HETATM 17805 C  C1B   . P5F C 2  .    ? -37.817 47.415  87.242  1.00 20.00 ? 1301 P5F A C1B   1 
HETATM 17806 N  N9A   . P5F C 2  .    ? -36.709 47.137  88.133  1.00 21.35 ? 1301 P5F A N9A   1 
HETATM 17807 C  C8A   . P5F C 2  .    ? -35.406 46.780  87.814  1.00 22.07 ? 1301 P5F A C8A   1 
HETATM 17808 N  N7A   . P5F C 2  .    ? -34.717 46.608  88.952  1.00 19.40 ? 1301 P5F A N7A   1 
HETATM 17809 C  C5A   . P5F C 2  .    ? -35.545 46.857  90.048  1.00 19.13 ? 1301 P5F A C5A   1 
HETATM 17810 C  C6A   . P5F C 2  .    ? -35.389 46.829  91.425  1.00 20.55 ? 1301 P5F A C6A   1 
HETATM 17811 N  N6A   . P5F C 2  .    ? -34.123 46.488  92.015  1.00 19.05 ? 1301 P5F A N6A   1 
HETATM 17812 N  N1A   . P5F C 2  .    ? -36.423 47.130  92.225  1.00 20.10 ? 1301 P5F A N1A   1 
HETATM 17813 C  C2A   . P5F C 2  .    ? -37.638 47.452  91.723  1.00 19.23 ? 1301 P5F A C2A   1 
HETATM 17814 N  N3A   . P5F C 2  .    ? -37.840 47.485  90.379  1.00 19.47 ? 1301 P5F A N3A   1 
HETATM 17815 C  C4A   . P5F C 2  .    ? -36.833 47.197  89.532  1.00 19.98 ? 1301 P5F A C4A   1 
HETATM 17816 N  N1    . P5F C 2  .    ? -41.210 54.078  81.654  1.00 19.12 ? 1301 P5F A N1    1 
HETATM 17817 C  C2    . P5F C 2  .    ? -41.731 55.131  82.466  1.00 17.30 ? 1301 P5F A C2    1 
HETATM 17818 O  O2    . P5F C 2  .    ? -41.322 55.235  83.739  1.00 16.33 ? 1301 P5F A O2    1 
HETATM 17819 N  N3    . P5F C 2  .    ? -42.662 56.055  81.978  1.00 17.61 ? 1301 P5F A N3    1 
HETATM 17820 C  C4    . P5F C 2  .    ? -43.089 55.936  80.663  1.00 19.07 ? 1301 P5F A C4    1 
HETATM 17821 O  O4    . P5F C 2  .    ? -43.985 56.829  80.184  1.00 16.96 ? 1301 P5F A O4    1 
HETATM 17822 C  C4X   . P5F C 2  .    ? -42.549 54.861  79.789  1.00 16.71 ? 1301 P5F A C4X   1 
HETATM 17823 N  N5    . P5F C 2  .    ? -42.840 54.822  78.381  1.00 17.10 ? 1301 P5F A N5    1 
HETATM 17824 C  C5X   . P5F C 2  .    ? -42.815 53.471  77.838  1.00 15.47 ? 1301 P5F A C5X   1 
HETATM 17825 C  C6    . P5F C 2  .    ? -43.706 53.113  76.704  1.00 18.24 ? 1301 P5F A C6    1 
HETATM 17826 C  C7    . P5F C 2  .    ? -43.681 51.789  76.223  1.00 19.09 ? 1301 P5F A C7    1 
HETATM 17827 C  C7M   . P5F C 2  .    ? -44.589 51.416  75.079  1.00 20.24 ? 1301 P5F A C7M   1 
HETATM 17828 C  C8    . P5F C 2  .    ? -42.830 50.805  76.793  1.00 19.88 ? 1301 P5F A C8    1 
HETATM 17829 C  C8M   . P5F C 2  .    ? -42.804 49.391  76.265  1.00 21.79 ? 1301 P5F A C8M   1 
HETATM 17830 C  C9    . P5F C 2  .    ? -41.979 51.146  77.868  1.00 18.75 ? 1301 P5F A C9    1 
HETATM 17831 C  C9A   . P5F C 2  .    ? -41.998 52.524  78.379  1.00 18.43 ? 1301 P5F A C9A   1 
HETATM 17832 N  N10   . P5F C 2  .    ? -41.193 52.851  79.527  1.00 18.54 ? 1301 P5F A N10   1 
HETATM 17833 C  C10   . P5F C 2  .    ? -41.639 53.967  80.294  1.00 17.51 ? 1301 P5F A C10   1 
HETATM 17834 C  "C1'" . P5F C 2  .    ? -40.139 51.953  80.054  1.00 19.17 ? 1301 P5F A "C1'" 1 
HETATM 17835 C  "C2'" . P5F C 2  .    ? -40.686 50.930  81.047  1.00 19.42 ? 1301 P5F A "C2'" 1 
HETATM 17836 O  "O2'" . P5F C 2  .    ? -40.986 51.552  82.235  1.00 20.23 ? 1301 P5F A "O2'" 1 
HETATM 17837 C  "C3'" . P5F C 2  .    ? -39.707 49.810  81.403  1.00 23.75 ? 1301 P5F A "C3'" 1 
HETATM 17838 O  "O3'" . P5F C 2  .    ? -38.528 50.363  81.895  1.00 27.63 ? 1301 P5F A "O3'" 1 
HETATM 17839 C  "C4'" . P5F C 2  .    ? -39.370 48.830  80.292  1.00 27.52 ? 1301 P5F A "C4'" 1 
HETATM 17840 O  "O4'" . P5F C 2  .    ? -40.477 48.583  79.480  1.00 30.19 ? 1301 P5F A "O4'" 1 
HETATM 17841 C  "C5'" . P5F C 2  .    ? -38.800 47.520  80.853  1.00 23.55 ? 1301 P5F A "C5'" 1 
HETATM 17842 O  "O5'" . P5F C 2  .    ? -39.721 46.705  81.542  1.00 23.32 ? 1301 P5F A "O5'" 1 
HETATM 17843 P  P     . P5F C 2  .    ? -39.986 45.231  80.963  1.00 22.60 ? 1301 P5F A P     1 
HETATM 17844 O  O1P   . P5F C 2  .    ? -40.133 45.103  79.405  1.00 24.20 ? 1301 P5F A O1P   1 
HETATM 17845 O  O2P   . P5F C 2  .    ? -41.200 44.779  81.848  1.00 25.56 ? 1301 P5F A O2P   1 
HETATM 17846 O  O3P   . P5F C 2  .    ? -38.692 44.465  81.659  1.00 23.29 ? 1301 P5F A O3P   1 
HETATM 17847 C  C21   . P5F C 2  .    ? -41.819 57.133  78.168  1.00 19.11 ? 1301 P5F A C21   1 
HETATM 17848 C  C22   . P5F C 2  .    ? -42.278 55.896  77.628  1.00 17.34 ? 1301 P5F A C22   1 
HETATM 17849 C  C23   . P5F C 2  .    ? -41.510 58.138  77.256  1.00 20.67 ? 1301 P5F A C23   1 
HETATM 17850 P  PA    . NAD D 3  .    ? -18.546 88.857  107.463 1.00 24.85 ? 1302 NAD A PA    1 
HETATM 17851 O  O1A   . NAD D 3  .    ? -17.070 88.831  107.186 1.00 24.49 ? 1302 NAD A O1A   1 
HETATM 17852 O  O2A   . NAD D 3  .    ? -19.151 90.146  106.973 1.00 22.84 ? 1302 NAD A O2A   1 
HETATM 17853 O  O5B   . NAD D 3  .    ? -18.916 88.591  109.056 1.00 25.00 ? 1302 NAD A O5B   1 
HETATM 17854 C  C5B   . NAD D 3  .    ? -18.759 87.279  109.603 1.00 23.56 ? 1302 NAD A C5B   1 
HETATM 17855 C  C4B   . NAD D 3  .    ? -18.779 87.406  111.168 1.00 23.65 ? 1302 NAD A C4B   1 
HETATM 17856 O  O4B   . NAD D 3  .    ? -17.508 88.288  111.602 1.00 23.83 ? 1302 NAD A O4B   1 
HETATM 17857 C  C3B   . NAD D 3  .    ? -19.843 88.020  111.636 1.00 19.90 ? 1302 NAD A C3B   1 
HETATM 17858 O  O3B   . NAD D 3  .    ? -20.335 87.301  112.859 1.00 20.26 ? 1302 NAD A O3B   1 
HETATM 17859 C  C2B   . NAD D 3  .    ? -19.384 89.458  112.010 1.00 23.85 ? 1302 NAD A C2B   1 
HETATM 17860 O  O2B   . NAD D 3  .    ? -20.165 90.008  113.004 1.00 24.62 ? 1302 NAD A O2B   1 
HETATM 17861 C  C1B   . NAD D 3  .    ? -17.946 89.216  112.456 1.00 23.60 ? 1302 NAD A C1B   1 
HETATM 17862 N  N9A   . NAD D 3  .    ? -17.140 90.407  112.246 1.00 21.56 ? 1302 NAD A N9A   1 
HETATM 17863 C  C8A   . NAD D 3  .    ? -17.151 91.468  111.453 1.00 24.68 ? 1302 NAD A C8A   1 
HETATM 17864 N  N7A   . NAD D 3  .    ? -16.056 92.192  111.766 1.00 23.37 ? 1302 NAD A N7A   1 
HETATM 17865 C  C5A   . NAD D 3  .    ? -15.385 91.561  112.746 1.00 24.42 ? 1302 NAD A C5A   1 
HETATM 17866 C  C6A   . NAD D 3  .    ? -14.211 91.891  113.425 1.00 25.18 ? 1302 NAD A C6A   1 
HETATM 17867 N  N6A   . NAD D 3  .    ? -13.487 93.133  113.067 1.00 26.54 ? 1302 NAD A N6A   1 
HETATM 17868 N  N1A   . NAD D 3  .    ? -13.744 91.085  114.364 1.00 24.27 ? 1302 NAD A N1A   1 
HETATM 17869 C  C2A   . NAD D 3  .    ? -14.416 89.921  114.689 1.00 25.73 ? 1302 NAD A C2A   1 
HETATM 17870 N  N3A   . NAD D 3  .    ? -15.564 89.608  114.041 1.00 23.22 ? 1302 NAD A N3A   1 
HETATM 17871 C  C4A   . NAD D 3  .    ? -16.039 90.440  113.055 1.00 25.65 ? 1302 NAD A C4A   1 
HETATM 17872 O  O3    . NAD D 3  .    ? -19.202 87.600  106.648 1.00 22.95 ? 1302 NAD A O3    1 
HETATM 17873 P  PN    . NAD D 3  .    ? -20.830 87.339  106.322 1.00 23.11 ? 1302 NAD A PN    1 
HETATM 17874 O  O1N   . NAD D 3  .    ? -21.350 88.481  105.431 1.00 25.06 ? 1302 NAD A O1N   1 
HETATM 17875 O  O2N   . NAD D 3  .    ? -21.620 87.150  107.585 1.00 23.31 ? 1302 NAD A O2N   1 
HETATM 17876 O  O5D   . NAD D 3  .    ? -20.765 85.960  105.426 1.00 22.69 ? 1302 NAD A O5D   1 
HETATM 17877 C  C5D   . NAD D 3  .    ? -20.368 86.102  104.068 1.00 24.32 ? 1302 NAD A C5D   1 
HETATM 17878 C  C4D   . NAD D 3  .    ? -18.915 85.704  103.795 1.00 22.01 ? 1302 NAD A C4D   1 
HETATM 17879 O  O4D   . NAD D 3  .    ? -18.626 84.328  104.551 1.00 19.54 ? 1302 NAD A O4D   1 
HETATM 17880 C  C3D   . NAD D 3  .    ? -18.681 85.469  102.503 1.00 21.27 ? 1302 NAD A C3D   1 
HETATM 17881 O  O3D   . NAD D 3  .    ? -17.338 86.069  102.123 1.00 22.74 ? 1302 NAD A O3D   1 
HETATM 17882 C  C2D   . NAD D 3  .    ? -18.612 83.973  102.331 1.00 19.22 ? 1302 NAD A C2D   1 
HETATM 17883 O  O2D   . NAD D 3  .    ? -17.829 83.553  101.238 1.00 19.76 ? 1302 NAD A O2D   1 
HETATM 17884 C  C1D   . NAD D 3  .    ? -17.976 83.609  103.706 1.00 20.56 ? 1302 NAD A C1D   1 
HETATM 17885 N  N1N   . NAD D 3  .    ? -18.283 82.188  103.981 1.00 19.46 ? 1302 NAD A N1N   1 
HETATM 17886 C  C2N   . NAD D 3  .    ? -17.289 81.235  103.925 1.00 19.26 ? 1302 NAD A C2N   1 
HETATM 17887 C  C3N   . NAD D 3  .    ? -17.662 79.924  104.181 1.00 21.73 ? 1302 NAD A C3N   1 
HETATM 17888 C  C7N   . NAD D 3  .    ? -16.613 78.771  104.125 1.00 17.55 ? 1302 NAD A C7N   1 
HETATM 17889 O  O7N   . NAD D 3  .    ? -16.911 77.679  104.490 1.00 20.73 ? 1302 NAD A O7N   1 
HETATM 17890 N  N7N   . NAD D 3  .    ? -15.277 79.034  103.569 1.00 17.94 ? 1302 NAD A N7N   1 
HETATM 17891 C  C4N   . NAD D 3  .    ? -18.970 79.615  104.509 1.00 27.70 ? 1302 NAD A C4N   1 
HETATM 17892 C  C5N   . NAD D 3  .    ? -19.953 80.572  104.524 1.00 23.70 ? 1302 NAD A C5N   1 
HETATM 17893 C  C6N   . NAD D 3  .    ? -19.582 81.883  104.265 1.00 20.60 ? 1302 NAD A C6N   1 
HETATM 17894 S  S     . SO4 E 4  .    ? -9.594  53.225  111.300 1.00 20.67 ? 1303 SO4 A S     1 
HETATM 17895 O  O1    . SO4 E 4  .    ? -8.493  53.491  110.333 1.00 21.87 ? 1303 SO4 A O1    1 
HETATM 17896 O  O2    . SO4 E 4  .    ? -10.633 52.381  110.636 1.00 22.92 ? 1303 SO4 A O2    1 
HETATM 17897 O  O3    . SO4 E 4  .    ? -9.072  52.513  112.507 1.00 19.73 ? 1303 SO4 A O3    1 
HETATM 17898 O  O4    . SO4 E 4  .    ? -10.135 54.561  111.709 1.00 23.18 ? 1303 SO4 A O4    1 
HETATM 17899 S  S     . SO4 F 4  .    ? -12.858 75.578  70.297  0.67 31.19 ? 1304 SO4 A S     1 
HETATM 17900 O  O1    . SO4 F 4  .    ? -11.618 75.815  71.090  0.67 31.37 ? 1304 SO4 A O1    1 
HETATM 17901 O  O2    . SO4 F 4  .    ? -13.118 76.731  69.377  0.67 36.00 ? 1304 SO4 A O2    1 
HETATM 17902 O  O3    . SO4 F 4  .    ? -12.631 74.341  69.486  0.67 36.18 ? 1304 SO4 A O3    1 
HETATM 17903 O  O4    . SO4 F 4  .    ? -14.052 75.388  71.180  0.67 27.73 ? 1304 SO4 A O4    1 
HETATM 17904 S  S     . SO4 G 4  .    ? 12.037  75.607  126.314 0.74 34.56 ? 1305 SO4 A S     1 
HETATM 17905 O  O1    . SO4 G 4  .    ? 12.991  76.205  125.326 0.74 37.32 ? 1305 SO4 A O1    1 
HETATM 17906 O  O2    . SO4 G 4  .    ? 10.769  75.177  125.645 0.74 31.93 ? 1305 SO4 A O2    1 
HETATM 17907 O  O3    . SO4 G 4  .    ? 12.710  74.407  126.907 0.74 36.33 ? 1305 SO4 A O3    1 
HETATM 17908 O  O4    . SO4 G 4  .    ? 11.708  76.606  127.379 0.74 41.75 ? 1305 SO4 A O4    1 
HETATM 17909 S  S     . SO4 H 4  .    ? -34.666 24.901  80.150  0.74 44.77 ? 1306 SO4 A S     1 
HETATM 17910 O  O1    . SO4 H 4  .    ? -33.673 25.915  79.665  0.74 43.05 ? 1306 SO4 A O1    1 
HETATM 17911 O  O2    . SO4 H 4  .    ? -35.604 24.574  79.031  0.74 41.94 ? 1306 SO4 A O2    1 
HETATM 17912 O  O3    . SO4 H 4  .    ? -33.956 23.651  80.569  0.74 53.31 ? 1306 SO4 A O3    1 
HETATM 17913 O  O4    . SO4 H 4  .    ? -35.410 25.437  81.338  0.74 42.83 ? 1306 SO4 A O4    1 
HETATM 17914 S  S     . SO4 I 4  .    ? -39.556 66.481  56.023  0.54 31.91 ? 1307 SO4 A S     1 
HETATM 17915 O  O1    . SO4 I 4  .    ? -38.202 66.592  55.385  0.54 38.01 ? 1307 SO4 A O1    1 
HETATM 17916 O  O2    . SO4 I 4  .    ? -40.589 66.922  55.038  0.54 25.18 ? 1307 SO4 A O2    1 
HETATM 17917 O  O3    . SO4 I 4  .    ? -39.793 65.051  56.402  0.54 27.95 ? 1307 SO4 A O3    1 
HETATM 17918 O  O4    . SO4 I 4  .    ? -39.605 67.302  57.279  0.54 30.18 ? 1307 SO4 A O4    1 
HETATM 17919 MG MG    . MG  J 5  .    ? -20.357 91.751  107.370 1.00 26.05 ? 1308 MG  A MG    1 
HETATM 17920 C  C     . FMT K 6  .    ? -40.872 61.688  103.072 1.00 25.89 ? 1309 FMT A C     1 
HETATM 17921 O  O1    . FMT K 6  .    ? -40.063 61.325  103.949 1.00 30.82 ? 1309 FMT A O1    1 
HETATM 17922 O  O2    . FMT K 6  .    ? -42.116 61.852  103.142 1.00 32.20 ? 1309 FMT A O2    1 
HETATM 17923 C  C1    . PEG L 7  .    ? 2.064   60.739  96.257  1.00 35.86 ? 1310 PEG A C1    1 
HETATM 17924 O  O1    . PEG L 7  .    ? 2.184   59.795  95.208  1.00 44.11 ? 1310 PEG A O1    1 
HETATM 17925 C  C2    . PEG L 7  .    ? 1.155   61.874  95.844  1.00 32.86 ? 1310 PEG A C2    1 
HETATM 17926 O  O2    . PEG L 7  .    ? 0.836   62.677  96.957  1.00 32.41 ? 1310 PEG A O2    1 
HETATM 17927 C  C3    . PEG L 7  .    ? -0.461  63.224  96.905  1.00 26.83 ? 1310 PEG A C3    1 
HETATM 17928 C  C4    . PEG L 7  .    ? -1.479  62.118  96.806  1.00 21.37 ? 1310 PEG A C4    1 
HETATM 17929 O  O4    . PEG L 7  .    ? -2.766  62.645  96.581  1.00 34.49 ? 1310 PEG A O4    1 
HETATM 17930 C  C1    . PEG M 7  .    ? -52.222 76.871  73.899  1.00 30.81 ? 1311 PEG A C1    1 
HETATM 17931 O  O1    . PEG M 7  .    ? -52.361 78.098  74.587  1.00 38.79 ? 1311 PEG A O1    1 
HETATM 17932 C  C2    . PEG M 7  .    ? -51.293 77.014  72.717  1.00 30.28 ? 1311 PEG A C2    1 
HETATM 17933 O  O2    . PEG M 7  .    ? -49.945 76.951  73.128  1.00 34.39 ? 1311 PEG A O2    1 
HETATM 17934 C  C3    . PEG M 7  .    ? -49.030 77.044  72.057  1.00 30.16 ? 1311 PEG A C3    1 
HETATM 17935 C  C4    . PEG M 7  .    ? -47.651 76.620  72.501  1.00 30.45 ? 1311 PEG A C4    1 
HETATM 17936 O  O4    . PEG M 7  .    ? -47.206 77.391  73.597  1.00 36.91 ? 1311 PEG A O4    1 
HETATM 17937 P  PA    . P5F N 2  .    ? -17.464 23.262  104.269 1.00 29.38 ? 1301 P5F B PA    1 
HETATM 17938 O  O1A   . P5F N 2  .    ? -18.773 22.437  104.112 1.00 31.09 ? 1301 P5F B O1A   1 
HETATM 17939 O  O2A   . P5F N 2  .    ? -17.534 24.687  104.327 1.00 27.47 ? 1301 P5F B O2A   1 
HETATM 17940 O  O5B   . P5F N 2  .    ? -16.466 23.131  103.139 1.00 26.81 ? 1301 P5F B O5B   1 
HETATM 17941 C  C5B   . P5F N 2  .    ? -15.284 23.896  103.000 1.00 27.91 ? 1301 P5F B C5B   1 
HETATM 17942 C  C4B   . P5F N 2  .    ? -14.389 23.218  101.956 1.00 22.64 ? 1301 P5F B C4B   1 
HETATM 17943 O  O4B   . P5F N 2  .    ? -14.964 23.173  100.665 1.00 24.41 ? 1301 P5F B O4B   1 
HETATM 17944 C  C3B   . P5F N 2  .    ? -13.061 23.867  101.730 1.00 22.71 ? 1301 P5F B C3B   1 
HETATM 17945 O  O3B   . P5F N 2  .    ? -12.185 23.609  102.758 1.00 22.29 ? 1301 P5F B O3B   1 
HETATM 17946 C  C2B   . P5F N 2  .    ? -12.654 23.232  100.463 1.00 20.47 ? 1301 P5F B C2B   1 
HETATM 17947 O  O2B   . P5F N 2  .    ? -12.213 21.941  100.679 1.00 22.02 ? 1301 P5F B O2B   1 
HETATM 17948 C  C1B   . P5F N 2  .    ? -13.933 23.166  99.711  1.00 22.84 ? 1301 P5F B C1B   1 
HETATM 17949 N  N9A   . P5F N 2  .    ? -14.120 24.257  98.771  1.00 21.70 ? 1301 P5F B N9A   1 
HETATM 17950 C  C8A   . P5F N 2  .    ? -14.238 25.615  99.001  1.00 24.45 ? 1301 P5F B C8A   1 
HETATM 17951 N  N7A   . P5F N 2  .    ? -14.422 26.256  97.841  1.00 24.31 ? 1301 P5F B N7A   1 
HETATM 17952 C  C5A   . P5F N 2  .    ? -14.423 25.326  96.804  1.00 20.12 ? 1301 P5F B C5A   1 
HETATM 17953 C  C6A   . P5F N 2  .    ? -14.573 25.398  95.427  1.00 21.57 ? 1301 P5F B C6A   1 
HETATM 17954 N  N6A   . P5F N 2  .    ? -14.775 26.661  94.775  1.00 21.54 ? 1301 P5F B N6A   1 
HETATM 17955 N  N1A   . P5F N 2  .    ? -14.515 24.273  94.697  1.00 20.17 ? 1301 P5F B N1A   1 
HETATM 17956 C  C2A   . P5F N 2  .    ? -14.338 23.059  95.260  1.00 19.43 ? 1301 P5F B C2A   1 
HETATM 17957 N  N3A   . P5F N 2  .    ? -14.198 22.941  96.615  1.00 20.87 ? 1301 P5F B N3A   1 
HETATM 17958 C  C4A   . P5F N 2  .    ? -14.236 24.038  97.385  1.00 20.73 ? 1301 P5F B C4A   1 
HETATM 17959 N  N1    . P5F N 2  .    ? -7.524  19.175  105.287 1.00 19.30 ? 1301 P5F B N1    1 
HETATM 17960 C  C2    . P5F N 2  .    ? -6.631  18.420  104.446 1.00 19.88 ? 1301 P5F B C2    1 
HETATM 17961 O  O2    . P5F N 2  .    ? -6.550  18.733  103.130 1.00 19.08 ? 1301 P5F B O2    1 
HETATM 17962 N  N3    . P5F N 2  .    ? -5.844  17.372  104.943 1.00 20.23 ? 1301 P5F B N3    1 
HETATM 17963 C  C4    . P5F N 2  .    ? -5.908  17.033  106.295 1.00 19.98 ? 1301 P5F B C4    1 
HETATM 17964 O  O4    . P5F N 2  .    ? -5.146  16.010  106.774 1.00 19.44 ? 1301 P5F B O4    1 
HETATM 17965 C  C4X   . P5F N 2  .    ? -6.816  17.809  107.189 1.00 20.62 ? 1301 P5F B C4X   1 
HETATM 17966 N  N5    . P5F N 2  .    ? -6.779  17.616  108.618 1.00 22.06 ? 1301 P5F B N5    1 
HETATM 17967 C  C5X   . P5F N 2  .    ? -8.078  17.853  109.229 1.00 23.11 ? 1301 P5F B C5X   1 
HETATM 17968 C  C6    . P5F N 2  .    ? -8.481  17.016  110.389 1.00 23.55 ? 1301 P5F B C6    1 
HETATM 17969 C  C7    . P5F N 2  .    ? -9.761  17.217  110.946 1.00 23.70 ? 1301 P5F B C7    1 
HETATM 17970 C  C7M   . P5F N 2  .    ? -10.190 16.380  112.122 1.00 24.95 ? 1301 P5F B C7M   1 
HETATM 17971 C  C8    . P5F N 2  .    ? -10.653 18.197  110.406 1.00 25.46 ? 1301 P5F B C8    1 
HETATM 17972 C  C8M   . P5F N 2  .    ? -12.023 18.422  110.999 1.00 25.46 ? 1301 P5F B C8M   1 
HETATM 17973 C  C9    . P5F N 2  .    ? -10.267 18.985  109.303 1.00 24.73 ? 1301 P5F B C9    1 
HETATM 17974 C  C9A   . P5F N 2  .    ? -8.929  18.785  108.715 1.00 22.81 ? 1301 P5F B C9A   1 
HETATM 17975 N  N10   . P5F N 2  .    ? -8.583  19.482  107.493 1.00 24.71 ? 1301 P5F B N10   1 
HETATM 17976 C  C10   . P5F N 2  .    ? -7.588  18.832  106.688 1.00 23.73 ? 1301 P5F B C10   1 
HETATM 17977 C  "C1'" . P5F N 2  .    ? -9.371  20.600  106.930 1.00 21.67 ? 1301 P5F B "C1'" 1 
HETATM 17978 C  "C2'" . P5F N 2  .    ? -10.505 20.117  106.031 1.00 24.68 ? 1301 P5F B "C2'" 1 
HETATM 17979 O  "O2'" . P5F N 2  .    ? -10.012 19.676  104.812 1.00 24.37 ? 1301 P5F B "O2'" 1 
HETATM 17980 C  "C3'" . P5F N 2  .    ? -11.532 21.184  105.686 1.00 28.27 ? 1301 P5F B "C3'" 1 
HETATM 17981 O  "O3'" . P5F N 2  .    ? -10.902 22.235  105.040 1.00 29.92 ? 1301 P5F B "O3'" 1 
HETATM 17982 C  "C4'" . P5F N 2  .    ? -12.403 21.739  106.807 1.00 31.07 ? 1301 P5F B "C4'" 1 
HETATM 17983 O  "O4'" . P5F N 2  .    ? -12.881 20.732  107.640 1.00 33.36 ? 1301 P5F B "O4'" 1 
HETATM 17984 C  "C5'" . P5F N 2  .    ? -13.561 22.534  106.206 1.00 29.71 ? 1301 P5F B "C5'" 1 
HETATM 17985 O  "O5'" . P5F N 2  .    ? -14.585 21.740  105.641 1.00 29.08 ? 1301 P5F B "O5'" 1 
HETATM 17986 P  P     . P5F N 2  .    ? -16.043 21.871  106.294 1.00 30.71 ? 1301 P5F B P     1 
HETATM 17987 O  O1P   . P5F N 2  .    ? -16.052 21.940  107.872 1.00 30.46 ? 1301 P5F B O1P   1 
HETATM 17988 O  O2P   . P5F N 2  .    ? -16.739 20.629  105.633 1.00 30.65 ? 1301 P5F B O2P   1 
HETATM 17989 O  O3P   . P5F N 2  .    ? -16.620 23.165  105.490 1.00 30.20 ? 1301 P5F B O3P   1 
HETATM 17990 C  C21   . P5F N 2  .    ? -4.327  18.351  108.601 1.00 21.09 ? 1301 P5F B C21   1 
HETATM 17991 C  C22   . P5F N 2  .    ? -5.579  18.060  109.229 1.00 20.18 ? 1301 P5F B C22   1 
HETATM 17992 C  C23   . P5F N 2  .    ? -3.276  18.642  109.456 1.00 21.91 ? 1301 P5F B C23   1 
HETATM 17993 P  PA    . NAD O 3  .    ? 27.430  35.968  75.463  1.00 16.89 ? 1302 NAD B PA    1 
HETATM 17994 O  O1A   . NAD O 3  .    ? 27.480  37.481  75.475  1.00 15.88 ? 1302 NAD B O1A   1 
HETATM 17995 O  O2A   . NAD O 3  .    ? 28.738  35.310  75.812  1.00 16.73 ? 1302 NAD B O2A   1 
HETATM 17996 O  O5B   . NAD O 3  .    ? 27.024  35.396  73.980  1.00 16.90 ? 1302 NAD B O5B   1 
HETATM 17997 C  C5B   . NAD O 3  .    ? 25.695  35.660  73.554  1.00 16.90 ? 1302 NAD B C5B   1 
HETATM 17998 C  C4B   . NAD O 3  .    ? 25.701  35.442  72.005  1.00 16.34 ? 1302 NAD B C4B   1 
HETATM 17999 O  O4B   . NAD O 3  .    ? 26.577  36.601  71.348  1.00 17.40 ? 1302 NAD B O4B   1 
HETATM 18000 C  C3B   . NAD O 3  .    ? 26.237  34.299  71.639  1.00 16.13 ? 1302 NAD B C3B   1 
HETATM 18001 O  O3B   . NAD O 3  .    ? 25.473  33.797  70.455  1.00 14.28 ? 1302 NAD B O3B   1 
HETATM 18002 C  C2B   . NAD O 3  .    ? 27.653  34.652  71.112  1.00 16.40 ? 1302 NAD B C2B   1 
HETATM 18003 O  O2B   . NAD O 3  .    ? 28.137  33.735  70.199  1.00 16.66 ? 1302 NAD B O2B   1 
HETATM 18004 C  C1B   . NAD O 3  .    ? 27.404  36.005  70.484  1.00 17.00 ? 1302 NAD B C1B   1 
HETATM 18005 N  N9A   . NAD O 3  .    ? 28.674  36.707  70.494  1.00 16.83 ? 1302 NAD B N9A   1 
HETATM 18006 C  C8A   . NAD O 3  .    ? 29.775  36.640  71.246  1.00 17.90 ? 1302 NAD B C8A   1 
HETATM 18007 N  N7A   . NAD O 3  .    ? 30.616  37.594  70.780  1.00 18.97 ? 1302 NAD B N7A   1 
HETATM 18008 C  C5A   . NAD O 3  .    ? 30.027  38.224  69.738  1.00 18.05 ? 1302 NAD B C5A   1 
HETATM 18009 C  C6A   . NAD O 3  .    ? 30.449  39.278  68.911  1.00 17.76 ? 1302 NAD B C6A   1 
HETATM 18010 N  N6A   . NAD O 3  .    ? 31.803  39.883  69.101  1.00 21.16 ? 1302 NAD B N6A   1 
HETATM 18011 N  N1A   . NAD O 3  .    ? 29.666  39.745  67.956  1.00 18.49 ? 1302 NAD B N1A   1 
HETATM 18012 C  C2A   . NAD O 3  .    ? 28.417  39.184  67.772  1.00 18.48 ? 1302 NAD B C2A   1 
HETATM 18013 N  N3A   . NAD O 3  .    ? 28.011  38.170  68.564  1.00 16.56 ? 1302 NAD B N3A   1 
HETATM 18014 C  C4A   . NAD O 3  .    ? 28.806  37.683  69.555  1.00 15.43 ? 1302 NAD B C4A   1 
HETATM 18015 O  O3    . NAD O 3  .    ? 26.247  35.519  76.459  1.00 15.23 ? 1302 NAD B O3    1 
HETATM 18016 P  PN    . NAD O 3  .    ? 25.932  33.974  76.991  1.00 17.55 ? 1302 NAD B PN    1 
HETATM 18017 O  O1N   . NAD O 3  .    ? 27.075  33.475  77.877  1.00 17.09 ? 1302 NAD B O1N   1 
HETATM 18018 O  O2N   . NAD O 3  .    ? 25.612  33.046  75.839  1.00 17.02 ? 1302 NAD B O2N   1 
HETATM 18019 O  O5D   . NAD O 3  .    ? 24.601  34.213  77.908  1.00 16.90 ? 1302 NAD B O5D   1 
HETATM 18020 C  C5D   . NAD O 3  .    ? 24.696  34.704  79.252  1.00 17.34 ? 1302 NAD B C5D   1 
HETATM 18021 C  C4D   . NAD O 3  .    ? 24.595  36.235  79.340  1.00 16.16 ? 1302 NAD B C4D   1 
HETATM 18022 O  O4D   . NAD O 3  .    ? 23.234  36.683  78.649  1.00 17.48 ? 1302 NAD B O4D   1 
HETATM 18023 C  C3D   . NAD O 3  .    ? 24.538  36.716  80.593  1.00 16.42 ? 1302 NAD B C3D   1 
HETATM 18024 O  O3D   . NAD O 3  .    ? 25.215  38.081  80.640  1.00 17.76 ? 1302 NAD B O3D   1 
HETATM 18025 C  C2D   . NAD O 3  .    ? 23.071  36.921  80.850  1.00 16.63 ? 1302 NAD B C2D   1 
HETATM 18026 O  O2D   . NAD O 3  .    ? 22.785  37.851  81.860  1.00 17.33 ? 1302 NAD B O2D   1 
HETATM 18027 C  C1D   . NAD O 3  .    ? 22.657  37.486  79.461  1.00 16.94 ? 1302 NAD B C1D   1 
HETATM 18028 N  N1N   . NAD O 3  .    ? 21.202  37.269  79.341  1.00 16.31 ? 1302 NAD B N1N   1 
HETATM 18029 C  C2N   . NAD O 3  .    ? 20.329  38.337  79.336  1.00 15.98 ? 1302 NAD B C2N   1 
HETATM 18030 C  C3N   . NAD O 3  .    ? 18.982  38.048  79.261  1.00 16.74 ? 1302 NAD B C3N   1 
HETATM 18031 C  C7N   . NAD O 3  .    ? 17.896  39.170  79.252  1.00 15.62 ? 1302 NAD B C7N   1 
HETATM 18032 O  O7N   . NAD O 3  .    ? 16.771  38.876  78.958  1.00 17.47 ? 1302 NAD B O7N   1 
HETATM 18033 N  N7N   . NAD O 3  .    ? 18.260  40.551  79.626  1.00 15.45 ? 1302 NAD B N7N   1 
HETATM 18034 C  C4N   . NAD O 3  .    ? 18.562  36.741  79.122  1.00 23.06 ? 1302 NAD B C4N   1 
HETATM 18035 C  C5N   . NAD O 3  .    ? 19.441  35.687  79.175  1.00 18.53 ? 1302 NAD B C5N   1 
HETATM 18036 C  C6N   . NAD O 3  .    ? 20.793  35.978  79.244  1.00 14.65 ? 1302 NAD B C6N   1 
HETATM 18037 S  S     . SO4 P 4  .    ? -7.439  47.781  73.293  1.00 19.49 ? 1303 SO4 B S     1 
HETATM 18038 O  O1    . SO4 P 4  .    ? -6.242  47.045  72.791  1.00 22.50 ? 1303 SO4 B O1    1 
HETATM 18039 O  O2    . SO4 P 4  .    ? -8.240  48.267  72.122  1.00 17.57 ? 1303 SO4 B O2    1 
HETATM 18040 O  O3    . SO4 P 4  .    ? -8.286  46.890  74.120  1.00 19.94 ? 1303 SO4 B O3    1 
HETATM 18041 O  O4    . SO4 P 4  .    ? -6.960  48.933  74.100  1.00 20.85 ? 1303 SO4 B O4    1 
HETATM 18042 S  S     . SO4 Q 4  .    ? -0.110  20.365  136.502 0.76 45.38 ? 1304 SO4 B S     1 
HETATM 18043 O  O1    . SO4 Q 4  .    ? -0.391  19.005  135.942 0.76 44.92 ? 1304 SO4 B O1    1 
HETATM 18044 O  O2    . SO4 Q 4  .    ? -1.195  21.300  136.064 0.76 45.33 ? 1304 SO4 B O2    1 
HETATM 18045 O  O3    . SO4 Q 4  .    ? -0.068  20.285  137.998 0.76 44.86 ? 1304 SO4 B O3    1 
HETATM 18046 O  O4    . SO4 Q 4  .    ? 1.211   20.880  136.008 0.76 44.16 ? 1304 SO4 B O4    1 
HETATM 18047 MG MG    . MG  R 5  .    ? 29.999  33.652  75.581  1.00 27.64 ? 1305 MG  B MG    1 
HETATM 18048 C  C     . FMT S 6  .    ? -1.255  17.090  83.325  1.00 15.66 ? 1306 FMT B C     1 
HETATM 18049 O  O1    . FMT S 6  .    ? -1.409  15.849  83.366  1.00 31.15 ? 1306 FMT B O1    1 
HETATM 18050 O  O2    . FMT S 6  .    ? -1.513  17.862  82.399  1.00 28.11 ? 1306 FMT B O2    1 
HETATM 18051 C  C1    . PEG T 7  .    ? 14.781  67.277  54.439  1.00 39.46 ? 1307 PEG B C1    1 
HETATM 18052 O  O1    . PEG T 7  .    ? 15.748  67.292  55.475  1.00 34.60 ? 1307 PEG B O1    1 
HETATM 18053 C  C2    . PEG T 7  .    ? 14.884  66.062  53.546  1.00 37.60 ? 1307 PEG B C2    1 
HETATM 18054 O  O2    . PEG T 7  .    ? 14.542  64.871  54.216  1.00 46.76 ? 1307 PEG B O2    1 
HETATM 18055 C  C3    . PEG T 7  .    ? 15.170  63.753  53.632  1.00 44.35 ? 1307 PEG B C3    1 
HETATM 18056 C  C4    . PEG T 7  .    ? 14.917  62.508  54.439  1.00 38.24 ? 1307 PEG B C4    1 
HETATM 18057 O  O4    . PEG T 7  .    ? 16.125  62.096  55.031  1.00 43.35 ? 1307 PEG B O4    1 
HETATM 18058 O  O1    . PG4 U 8  .    ? 0.850   55.401  90.420  1.00 49.89 ? 1308 PG4 B O1    1 
HETATM 18059 C  C1    . PG4 U 8  .    ? 0.375   54.441  89.504  1.00 43.47 ? 1308 PG4 B C1    1 
HETATM 18060 C  C2    . PG4 U 8  .    ? 1.515   53.925  88.662  1.00 39.36 ? 1308 PG4 B C2    1 
HETATM 18061 O  O2    . PG4 U 8  .    ? 2.039   54.947  87.850  1.00 39.77 ? 1308 PG4 B O2    1 
HETATM 18062 C  C3    . PG4 U 8  .    ? 2.564   54.450  86.643  1.00 34.00 ? 1308 PG4 B C3    1 
HETATM 18063 C  C4    . PG4 U 8  .    ? 3.687   55.335  86.161  1.00 29.42 ? 1308 PG4 B C4    1 
HETATM 18064 O  O3    . PG4 U 8  .    ? 3.267   56.672  86.178  1.00 31.80 ? 1308 PG4 B O3    1 
HETATM 18065 C  C5    . PG4 U 8  .    ? 4.260   57.554  85.729  1.00 29.35 ? 1308 PG4 B C5    1 
HETATM 18066 C  C6    . PG4 U 8  .    ? 3.653   58.924  85.595  1.00 29.08 ? 1308 PG4 B C6    1 
HETATM 18067 O  O4    . PG4 U 8  .    ? 2.942   59.222  86.768  1.00 38.41 ? 1308 PG4 B O4    1 
HETATM 18068 C  C7    . PG4 U 8  .    ? 2.291   60.468  86.731  1.00 37.56 ? 1308 PG4 B C7    1 
HETATM 18069 C  C8    . PG4 U 8  .    ? 0.865   60.292  86.269  1.00 36.59 ? 1308 PG4 B C8    1 
HETATM 18070 O  O5    . PG4 U 8  .    ? 0.021   60.143  87.391  1.00 39.47 ? 1308 PG4 B O5    1 
HETATM 18071 C  C1    . PGE V 9  .    ? 36.567  37.047  83.514  1.00 36.34 ? 1309 PGE B C1    1 
HETATM 18072 O  O1    . PGE V 9  .    ? 37.835  36.642  83.036  1.00 38.47 ? 1309 PGE B O1    1 
HETATM 18073 C  C2    . PGE V 9  .    ? 36.603  38.477  84.002  1.00 32.91 ? 1309 PGE B C2    1 
HETATM 18074 O  O2    . PGE V 9  .    ? 37.442  38.590  85.135  1.00 34.85 ? 1309 PGE B O2    1 
HETATM 18075 C  C3    . PGE V 9  .    ? 37.589  39.892  85.668  1.00 32.88 ? 1309 PGE B C3    1 
HETATM 18076 C  C4    . PGE V 9  .    ? 38.908  40.566  85.348  1.00 32.90 ? 1309 PGE B C4    1 
HETATM 18077 O  O4    . PGE V 9  .    ? 42.125  38.479  86.129  1.00 31.57 ? 1309 PGE B O4    1 
HETATM 18078 C  C6    . PGE V 9  .    ? 42.170  39.744  86.757  1.00 30.01 ? 1309 PGE B C6    1 
HETATM 18079 C  C5    . PGE V 9  .    ? 41.137  40.618  86.080  1.00 31.07 ? 1309 PGE B C5    1 
HETATM 18080 O  O3    . PGE V 9  .    ? 39.990  39.832  85.865  1.00 32.75 ? 1309 PGE B O3    1 
HETATM 18081 O  O     . HOH W 10 .    ? -1.535  89.103  105.800 1.00 19.84 ? 1401 HOH A O     1 
HETATM 18082 O  O     . HOH W 10 .    ? -51.740 74.121  68.511  1.00 33.31 ? 1402 HOH A O     1 
HETATM 18083 O  O     . HOH W 10 .    ? -32.752 56.255  86.452  1.00 25.52 ? 1403 HOH A O     1 
HETATM 18084 O  O     . HOH W 10 .    ? -34.274 73.524  76.804  1.00 28.27 ? 1404 HOH A O     1 
HETATM 18085 O  O     . HOH W 10 .    ? -57.902 67.619  61.854  1.00 27.68 ? 1405 HOH A O     1 
HETATM 18086 O  O     . HOH W 10 .    ? -36.431 85.800  104.596 1.00 26.92 ? 1406 HOH A O     1 
HETATM 18087 O  O     . HOH W 10 .    ? -45.917 89.525  106.485 1.00 35.15 ? 1407 HOH A O     1 
HETATM 18088 O  O     . HOH W 10 .    ? -55.399 33.866  71.483  1.00 32.61 ? 1408 HOH A O     1 
HETATM 18089 O  O     . HOH W 10 .    ? -12.669 88.056  99.309  1.00 33.08 ? 1409 HOH A O     1 
HETATM 18090 O  O     . HOH W 10 .    ? -19.926 73.101  97.988  1.00 23.37 ? 1410 HOH A O     1 
HETATM 18091 O  O     . HOH W 10 .    ? -25.792 61.010  128.277 1.00 37.27 ? 1411 HOH A O     1 
HETATM 18092 O  O     . HOH W 10 .    ? -53.068 61.531  102.167 1.00 27.77 ? 1412 HOH A O     1 
HETATM 18093 O  O     . HOH W 10 .    ? 21.385  68.243  116.781 1.00 28.39 ? 1413 HOH A O     1 
HETATM 18094 O  O     . HOH W 10 .    ? -24.694 93.187  127.274 1.00 31.82 ? 1414 HOH A O     1 
HETATM 18095 O  O     . HOH W 10 .    ? -5.233  70.535  76.654  1.00 34.73 ? 1415 HOH A O     1 
HETATM 18096 O  O     . HOH W 10 .    ? -62.529 57.814  63.938  1.00 29.15 ? 1416 HOH A O     1 
HETATM 18097 O  O     . HOH W 10 .    ? 14.409  55.430  111.117 1.00 32.36 ? 1417 HOH A O     1 
HETATM 18098 O  O     . HOH W 10 .    ? -43.715 80.809  90.124  1.00 27.99 ? 1418 HOH A O     1 
HETATM 18099 O  O     . HOH W 10 .    ? -21.374 55.327  116.256 1.00 33.17 ? 1419 HOH A O     1 
HETATM 18100 O  O     . HOH W 10 .    ? -38.326 62.534  81.947  1.00 25.79 ? 1420 HOH A O     1 
HETATM 18101 O  O     . HOH W 10 .    ? -45.248 30.412  96.624  1.00 38.16 ? 1421 HOH A O     1 
HETATM 18102 O  O     . HOH W 10 .    ? -58.888 72.355  80.283  1.00 29.76 ? 1422 HOH A O     1 
HETATM 18103 O  O     . HOH W 10 .    ? -39.412 77.873  97.524  1.00 21.82 ? 1423 HOH A O     1 
HETATM 18104 O  O     . HOH W 10 .    ? -13.616 55.756  81.636  1.00 26.84 ? 1424 HOH A O     1 
HETATM 18105 O  O     . HOH W 10 .    ? -7.015  58.737  120.399 1.00 21.31 ? 1425 HOH A O     1 
HETATM 18106 O  O     . HOH W 10 .    ? -12.152 68.991  76.855  1.00 24.37 ? 1426 HOH A O     1 
HETATM 18107 O  O     . HOH W 10 .    ? 0.216   85.446  112.017 1.00 31.51 ? 1427 HOH A O     1 
HETATM 18108 O  O     . HOH W 10 .    ? -32.276 87.150  76.964  1.00 34.30 ? 1428 HOH A O     1 
HETATM 18109 O  O     . HOH W 10 .    ? -25.325 65.410  95.135  1.00 29.72 ? 1429 HOH A O     1 
HETATM 18110 O  O     . HOH W 10 .    ? -48.643 81.875  85.109  1.00 31.39 ? 1430 HOH A O     1 
HETATM 18111 O  O     . HOH W 10 .    ? -34.972 76.987  96.564  1.00 28.06 ? 1431 HOH A O     1 
HETATM 18112 O  O     . HOH W 10 .    ? -19.786 92.214  105.618 1.00 28.10 ? 1432 HOH A O     1 
HETATM 18113 O  O     . HOH W 10 .    ? -64.538 52.912  89.900  1.00 31.34 ? 1433 HOH A O     1 
HETATM 18114 O  O     . HOH W 10 .    ? 20.618  57.652  105.500 1.00 32.14 ? 1434 HOH A O     1 
HETATM 18115 O  O     . HOH W 10 .    ? 20.295  58.613  111.374 1.00 31.48 ? 1435 HOH A O     1 
HETATM 18116 O  O     . HOH W 10 .    ? -43.956 75.807  114.457 1.00 28.53 ? 1436 HOH A O     1 
HETATM 18117 O  O     . HOH W 10 .    ? -43.029 38.969  85.317  1.00 28.55 ? 1437 HOH A O     1 
HETATM 18118 O  O     . HOH W 10 .    ? -1.483  78.152  115.009 1.00 24.18 ? 1438 HOH A O     1 
HETATM 18119 O  O     . HOH W 10 .    ? -21.943 90.663  106.650 1.00 27.75 ? 1439 HOH A O     1 
HETATM 18120 O  O     . HOH W 10 .    ? -0.808  63.955  110.182 1.00 21.07 ? 1440 HOH A O     1 
HETATM 18121 O  O     . HOH W 10 .    ? -10.908 49.838  110.333 1.00 23.26 ? 1441 HOH A O     1 
HETATM 18122 O  O     . HOH W 10 .    ? -37.112 63.629  96.386  1.00 22.74 ? 1442 HOH A O     1 
HETATM 18123 O  O     . HOH W 10 .    ? -6.067  53.803  111.151 1.00 17.02 ? 1443 HOH A O     1 
HETATM 18124 O  O     . HOH W 10 .    ? -67.103 67.973  72.140  1.00 28.14 ? 1444 HOH A O     1 
HETATM 18125 O  O     . HOH W 10 .    ? -47.381 59.934  102.371 1.00 22.68 ? 1445 HOH A O     1 
HETATM 18126 O  O     . HOH W 10 .    ? -1.378  50.603  58.006  1.00 26.66 ? 1446 HOH A O     1 
HETATM 18127 O  O     . HOH W 10 .    ? -18.048 72.986  111.688 1.00 19.09 ? 1447 HOH A O     1 
HETATM 18128 O  O     . HOH W 10 .    ? -56.852 34.788  86.664  1.00 26.57 ? 1448 HOH A O     1 
HETATM 18129 O  O     . HOH W 10 .    ? -4.394  79.424  104.233 1.00 20.16 ? 1449 HOH A O     1 
HETATM 18130 O  O     . HOH W 10 .    ? -29.624 57.821  115.996 1.00 32.06 ? 1450 HOH A O     1 
HETATM 18131 O  O     . HOH W 10 .    ? -10.650 81.407  91.491  1.00 22.15 ? 1451 HOH A O     1 
HETATM 18132 O  O     . HOH W 10 .    ? -59.076 38.463  76.425  1.00 34.87 ? 1452 HOH A O     1 
HETATM 18133 O  O     . HOH W 10 .    ? -14.667 61.688  107.983 1.00 23.47 ? 1453 HOH A O     1 
HETATM 18134 O  O     . HOH W 10 .    ? -4.027  70.595  117.911 1.00 23.35 ? 1454 HOH A O     1 
HETATM 18135 O  O     . HOH W 10 .    ? -50.802 32.799  92.009  1.00 36.71 ? 1455 HOH A O     1 
HETATM 18136 O  O     . HOH W 10 .    ? -19.301 59.296  104.733 1.00 24.97 ? 1456 HOH A O     1 
HETATM 18137 O  O     . HOH W 10 .    ? -1.183  58.463  110.754 1.00 28.26 ? 1457 HOH A O     1 
HETATM 18138 O  O     . HOH W 10 .    ? -61.050 59.987  90.730  1.00 20.16 ? 1458 HOH A O     1 
HETATM 18139 O  O     . HOH W 10 .    ? 5.374   63.351  97.611  1.00 19.74 ? 1459 HOH A O     1 
HETATM 18140 O  O     . HOH W 10 .    ? -18.341 82.946  97.004  1.00 20.17 ? 1460 HOH A O     1 
HETATM 18141 O  O     . HOH W 10 .    ? -67.436 72.711  75.538  1.00 27.50 ? 1461 HOH A O     1 
HETATM 18142 O  O     . HOH W 10 .    ? -6.664  68.791  92.765  1.00 25.82 ? 1462 HOH A O     1 
HETATM 18143 O  O     . HOH W 10 .    ? 6.583   54.313  101.791 1.00 18.96 ? 1463 HOH A O     1 
HETATM 18144 O  O     . HOH W 10 .    ? -39.406 49.775  102.919 1.00 28.22 ? 1464 HOH A O     1 
HETATM 18145 O  O     . HOH W 10 .    ? 3.099   59.635  114.227 1.00 35.58 ? 1465 HOH A O     1 
HETATM 18146 O  O     . HOH W 10 .    ? -15.143 64.290  99.703  1.00 22.10 ? 1466 HOH A O     1 
HETATM 18147 O  O     . HOH W 10 .    ? -25.449 67.184  86.509  1.00 26.63 ? 1467 HOH A O     1 
HETATM 18148 O  O     . HOH W 10 .    ? -14.758 76.093  110.244 1.00 20.55 ? 1468 HOH A O     1 
HETATM 18149 O  O     . HOH W 10 .    ? -51.051 52.310  64.123  1.00 22.06 ? 1469 HOH A O     1 
HETATM 18150 O  O     . HOH W 10 .    ? -12.715 79.590  94.834  1.00 16.34 ? 1470 HOH A O     1 
HETATM 18151 O  O     . HOH W 10 .    ? 8.023   90.141  120.530 1.00 27.61 ? 1471 HOH A O     1 
HETATM 18152 O  O     . HOH W 10 .    ? -42.057 64.329  103.963 1.00 23.18 ? 1472 HOH A O     1 
HETATM 18153 O  O     . HOH W 10 .    ? -44.473 62.450  70.430  1.00 23.33 ? 1473 HOH A O     1 
HETATM 18154 O  O     . HOH W 10 .    ? -29.119 77.625  103.741 1.00 29.64 ? 1474 HOH A O     1 
HETATM 18155 O  O     . HOH W 10 .    ? 17.697  59.305  95.939  1.00 31.25 ? 1475 HOH A O     1 
HETATM 18156 O  O     . HOH W 10 .    ? -4.462  79.679  111.357 1.00 27.29 ? 1476 HOH A O     1 
HETATM 18157 O  O     . HOH W 10 .    ? -7.434  50.706  76.884  1.00 25.80 ? 1477 HOH A O     1 
HETATM 18158 O  O     . HOH W 10 .    ? -52.306 47.585  69.191  1.00 28.23 ? 1478 HOH A O     1 
HETATM 18159 O  O     . HOH W 10 .    ? -60.955 61.759  92.979  1.00 23.83 ? 1479 HOH A O     1 
HETATM 18160 O  O     . HOH W 10 .    ? -23.764 64.057  98.258  1.00 17.94 ? 1480 HOH A O     1 
HETATM 18161 O  O     . HOH W 10 .    ? -24.710 60.013  122.014 1.00 34.05 ? 1481 HOH A O     1 
HETATM 18162 O  O     . HOH W 10 .    ? -20.455 59.424  76.258  1.00 24.36 ? 1482 HOH A O     1 
HETATM 18163 O  O     . HOH W 10 .    ? -23.353 80.916  110.564 1.00 27.05 ? 1483 HOH A O     1 
HETATM 18164 O  O     . HOH W 10 .    ? -37.433 80.888  79.340  1.00 20.44 ? 1484 HOH A O     1 
HETATM 18165 O  O     . HOH W 10 .    ? -26.536 51.077  105.853 1.00 30.92 ? 1485 HOH A O     1 
HETATM 18166 O  O     . HOH W 10 .    ? -29.290 75.439  102.143 1.00 29.92 ? 1486 HOH A O     1 
HETATM 18167 O  O     . HOH W 10 .    ? -32.787 79.417  96.583  1.00 28.51 ? 1487 HOH A O     1 
HETATM 18168 O  O     . HOH W 10 .    ? -37.244 64.251  67.600  1.00 30.05 ? 1488 HOH A O     1 
HETATM 18169 O  O     . HOH W 10 .    ? -41.295 49.372  64.229  1.00 27.83 ? 1489 HOH A O     1 
HETATM 18170 O  O     . HOH W 10 .    ? -13.823 78.225  111.491 1.00 19.21 ? 1490 HOH A O     1 
HETATM 18171 O  O     . HOH W 10 .    ? -27.378 89.710  77.955  1.00 25.63 ? 1491 HOH A O     1 
HETATM 18172 O  O     . HOH W 10 .    ? -4.519  76.512  125.098 1.00 25.66 ? 1492 HOH A O     1 
HETATM 18173 O  O     . HOH W 10 .    ? -26.733 56.815  108.450 1.00 22.33 ? 1493 HOH A O     1 
HETATM 18174 O  O     . HOH W 10 .    ? 14.130  61.404  94.917  1.00 29.32 ? 1494 HOH A O     1 
HETATM 18175 O  O     . HOH W 10 .    ? 7.540   91.718  113.950 1.00 30.43 ? 1495 HOH A O     1 
HETATM 18176 O  O     . HOH W 10 .    ? -49.798 66.965  94.291  1.00 19.83 ? 1496 HOH A O     1 
HETATM 18177 O  O     . HOH W 10 .    ? 13.995  87.132  110.647 1.00 30.64 ? 1497 HOH A O     1 
HETATM 18178 O  O     . HOH W 10 .    ? -51.959 55.436  76.029  1.00 19.23 ? 1498 HOH A O     1 
HETATM 18179 O  O     . HOH W 10 .    ? 13.507  87.378  99.034  1.00 33.88 ? 1499 HOH A O     1 
HETATM 18180 O  O     . HOH W 10 .    ? -43.312 48.515  60.356  1.00 30.35 ? 1500 HOH A O     1 
HETATM 18181 O  O     . HOH W 10 .    ? -27.721 83.100  130.101 1.00 34.05 ? 1501 HOH A O     1 
HETATM 18182 O  O     . HOH W 10 .    ? -42.027 79.972  80.454  1.00 26.39 ? 1502 HOH A O     1 
HETATM 18183 O  O     . HOH W 10 .    ? -65.890 48.127  85.720  1.00 34.09 ? 1503 HOH A O     1 
HETATM 18184 O  O     . HOH W 10 .    ? -55.439 56.755  65.007  1.00 18.99 ? 1504 HOH A O     1 
HETATM 18185 O  O     . HOH W 10 .    ? -46.194 76.416  94.623  1.00 24.91 ? 1505 HOH A O     1 
HETATM 18186 O  O     . HOH W 10 .    ? -52.705 49.119  63.015  1.00 31.60 ? 1506 HOH A O     1 
HETATM 18187 O  O     . HOH W 10 .    ? -23.792 64.066  106.578 1.00 17.29 ? 1507 HOH A O     1 
HETATM 18188 O  O     . HOH W 10 .    ? -35.878 76.455  92.783  1.00 31.11 ? 1508 HOH A O     1 
HETATM 18189 O  O     . HOH W 10 .    ? -11.951 63.484  113.617 1.00 18.09 ? 1509 HOH A O     1 
HETATM 18190 O  O     . HOH W 10 .    ? -24.337 63.740  92.039  1.00 20.32 ? 1510 HOH A O     1 
HETATM 18191 O  O     . HOH W 10 .    ? -2.533  78.361  75.988  1.00 28.87 ? 1511 HOH A O     1 
HETATM 18192 O  O     . HOH W 10 .    ? -47.515 35.320  87.345  1.00 32.28 ? 1512 HOH A O     1 
HETATM 18193 O  O     . HOH W 10 .    ? -9.903  65.268  76.681  1.00 20.60 ? 1513 HOH A O     1 
HETATM 18194 O  O     . HOH W 10 .    ? -23.557 60.719  116.268 1.00 20.90 ? 1514 HOH A O     1 
HETATM 18195 O  O     . HOH W 10 .    ? -48.721 83.148  111.715 1.00 31.25 ? 1515 HOH A O     1 
HETATM 18196 O  O     . HOH W 10 .    ? -5.435  54.691  108.593 1.00 18.81 ? 1516 HOH A O     1 
HETATM 18197 O  O     . HOH W 10 .    ? -52.111 73.314  105.986 1.00 31.58 ? 1517 HOH A O     1 
HETATM 18198 O  O     . HOH W 10 .    ? -26.741 83.007  112.910 1.00 23.91 ? 1518 HOH A O     1 
HETATM 18199 O  O     . HOH W 10 .    ? -43.420 85.644  97.747  1.00 27.83 ? 1519 HOH A O     1 
HETATM 18200 O  O     . HOH W 10 .    ? -40.478 57.493  88.410  1.00 17.00 ? 1520 HOH A O     1 
HETATM 18201 O  O     . HOH W 10 .    ? -58.714 35.118  84.429  1.00 27.39 ? 1521 HOH A O     1 
HETATM 18202 O  O     . HOH W 10 .    ? -19.213 59.894  69.942  1.00 23.08 ? 1522 HOH A O     1 
HETATM 18203 O  O     . HOH W 10 .    ? -4.077  58.044  73.098  1.00 22.66 ? 1523 HOH A O     1 
HETATM 18204 O  O     . HOH W 10 .    ? -17.076 56.085  112.748 1.00 28.26 ? 1524 HOH A O     1 
HETATM 18205 O  O     . HOH W 10 .    ? -58.855 65.636  94.609  1.00 29.79 ? 1525 HOH A O     1 
HETATM 18206 O  O     . HOH W 10 .    ? -32.200 82.728  75.616  1.00 22.25 ? 1526 HOH A O     1 
HETATM 18207 O  O     . HOH W 10 .    ? -39.206 65.301  96.605  1.00 26.96 ? 1527 HOH A O     1 
HETATM 18208 O  O     . HOH W 10 .    ? 0.099   85.723  103.356 1.00 22.06 ? 1528 HOH A O     1 
HETATM 18209 O  O     . HOH W 10 .    ? -1.929  77.124  88.041  1.00 27.33 ? 1529 HOH A O     1 
HETATM 18210 O  O     . HOH W 10 .    ? 22.796  65.969  115.204 1.00 28.92 ? 1530 HOH A O     1 
HETATM 18211 O  O     . HOH W 10 .    ? -36.913 95.472  94.261  1.00 34.99 ? 1531 HOH A O     1 
HETATM 18212 O  O     . HOH W 10 .    ? -31.730 84.600  99.605  1.00 21.53 ? 1532 HOH A O     1 
HETATM 18213 O  O     . HOH W 10 .    ? -12.744 77.344  103.476 1.00 18.65 ? 1533 HOH A O     1 
HETATM 18214 O  O     . HOH W 10 .    ? -47.825 60.560  85.498  1.00 17.06 ? 1534 HOH A O     1 
HETATM 18215 O  O     . HOH W 10 .    ? -62.304 58.417  70.281  1.00 20.34 ? 1535 HOH A O     1 
HETATM 18216 O  O     . HOH W 10 .    ? -15.134 49.078  75.948  1.00 28.70 ? 1536 HOH A O     1 
HETATM 18217 O  O     . HOH W 10 .    ? -48.729 54.872  61.457  1.00 24.80 ? 1537 HOH A O     1 
HETATM 18218 O  O     . HOH W 10 .    ? -4.501  73.402  117.323 1.00 23.52 ? 1538 HOH A O     1 
HETATM 18219 O  O     . HOH W 10 .    ? -45.186 63.648  81.741  1.00 16.61 ? 1539 HOH A O     1 
HETATM 18220 O  O     . HOH W 10 .    ? -44.965 41.767  104.642 1.00 32.76 ? 1540 HOH A O     1 
HETATM 18221 O  O     . HOH W 10 .    ? -41.812 86.079  114.169 1.00 29.19 ? 1541 HOH A O     1 
HETATM 18222 O  O     . HOH W 10 .    ? -35.124 80.771  120.793 1.00 26.44 ? 1542 HOH A O     1 
HETATM 18223 O  O     . HOH W 10 .    ? -32.722 93.396  104.144 1.00 27.40 ? 1543 HOH A O     1 
HETATM 18224 O  O     . HOH W 10 .    ? -26.350 64.040  105.192 1.00 20.37 ? 1544 HOH A O     1 
HETATM 18225 O  O     . HOH W 10 .    ? 4.729   55.248  97.190  1.00 26.09 ? 1545 HOH A O     1 
HETATM 18226 O  O     . HOH W 10 .    ? -48.483 66.382  58.110  1.00 25.02 ? 1546 HOH A O     1 
HETATM 18227 O  O     . HOH W 10 .    ? -7.438  80.792  128.417 1.00 29.22 ? 1547 HOH A O     1 
HETATM 18228 O  O     . HOH W 10 .    ? -9.322  45.285  56.013  1.00 31.25 ? 1548 HOH A O     1 
HETATM 18229 O  O     . HOH W 10 .    ? -6.697  83.024  103.584 1.00 20.37 ? 1549 HOH A O     1 
HETATM 18230 O  O     . HOH W 10 .    ? -10.926 69.521  134.006 1.00 32.50 ? 1550 HOH A O     1 
HETATM 18231 O  O     . HOH W 10 .    ? -59.981 54.471  74.891  1.00 21.31 ? 1551 HOH A O     1 
HETATM 18232 O  O     . HOH W 10 .    ? -36.020 51.909  85.750  1.00 18.25 ? 1552 HOH A O     1 
HETATM 18233 O  O     . HOH W 10 .    ? -33.534 92.581  107.404 1.00 33.65 ? 1553 HOH A O     1 
HETATM 18234 O  O     . HOH W 10 .    ? -12.007 59.996  84.785  1.00 27.18 ? 1554 HOH A O     1 
HETATM 18235 O  O     . HOH W 10 .    ? -16.425 91.892  104.856 1.00 32.50 ? 1555 HOH A O     1 
HETATM 18236 O  O     . HOH W 10 .    ? -4.320  78.594  122.961 1.00 24.28 ? 1556 HOH A O     1 
HETATM 18237 O  O     . HOH W 10 .    ? -14.247 74.640  106.456 1.00 17.56 ? 1557 HOH A O     1 
HETATM 18238 O  O     . HOH W 10 .    ? -7.786  42.713  62.240  1.00 28.18 ? 1558 HOH A O     1 
HETATM 18239 O  O     . HOH W 10 .    ? 4.547   67.408  96.428  1.00 24.57 ? 1559 HOH A O     1 
HETATM 18240 O  O     . HOH W 10 .    ? -29.267 55.172  112.212 1.00 34.19 ? 1560 HOH A O     1 
HETATM 18241 O  O     . HOH W 10 .    ? -70.112 65.197  74.033  1.00 26.18 ? 1561 HOH A O     1 
HETATM 18242 O  O     . HOH W 10 .    ? -11.984 88.873  129.405 1.00 37.01 ? 1562 HOH A O     1 
HETATM 18243 O  O     . HOH W 10 .    ? 1.141   73.496  116.260 1.00 29.87 ? 1563 HOH A O     1 
HETATM 18244 O  O     . HOH W 10 .    ? -16.734 75.771  106.377 1.00 21.21 ? 1564 HOH A O     1 
HETATM 18245 O  O     . HOH W 10 .    ? -21.395 54.857  91.153  1.00 31.23 ? 1565 HOH A O     1 
HETATM 18246 O  O     . HOH W 10 .    ? -63.487 44.282  82.590  1.00 32.58 ? 1566 HOH A O     1 
HETATM 18247 O  O     . HOH W 10 .    ? -27.720 65.033  100.482 1.00 23.45 ? 1567 HOH A O     1 
HETATM 18248 O  O     . HOH W 10 .    ? -45.376 63.769  84.625  1.00 17.33 ? 1568 HOH A O     1 
HETATM 18249 O  O     . HOH W 10 .    ? -51.568 70.223  94.262  1.00 19.10 ? 1569 HOH A O     1 
HETATM 18250 O  O     . HOH W 10 .    ? -22.316 89.217  109.337 1.00 25.14 ? 1570 HOH A O     1 
HETATM 18251 O  O     . HOH W 10 .    ? -3.452  90.249  109.029 1.00 24.48 ? 1571 HOH A O     1 
HETATM 18252 O  O     . HOH W 10 .    ? -56.801 56.106  95.259  1.00 21.11 ? 1572 HOH A O     1 
HETATM 18253 O  O     . HOH W 10 .    ? -53.583 64.000  98.670  1.00 20.83 ? 1573 HOH A O     1 
HETATM 18254 O  O     . HOH W 10 .    ? -19.488 61.694  85.636  1.00 22.38 ? 1574 HOH A O     1 
HETATM 18255 O  O     . HOH W 10 .    ? -61.675 55.746  67.684  1.00 19.09 ? 1575 HOH A O     1 
HETATM 18256 O  O     . HOH W 10 .    ? -18.140 59.460  86.541  1.00 29.18 ? 1576 HOH A O     1 
HETATM 18257 O  O     . HOH W 10 .    ? -57.197 46.140  71.328  1.00 22.07 ? 1577 HOH A O     1 
HETATM 18258 O  O     . HOH W 10 .    ? -28.168 79.087  101.670 1.00 25.08 ? 1578 HOH A O     1 
HETATM 18259 O  O     . HOH W 10 .    ? -69.230 56.763  82.867  1.00 29.20 ? 1579 HOH A O     1 
HETATM 18260 O  O     . HOH W 10 .    ? -66.010 69.407  69.386  1.00 30.58 ? 1580 HOH A O     1 
HETATM 18261 O  O     . HOH W 10 .    ? -16.971 76.765  108.872 1.00 17.69 ? 1581 HOH A O     1 
HETATM 18262 O  O     . HOH W 10 .    ? -66.298 59.129  76.017  1.00 20.63 ? 1582 HOH A O     1 
HETATM 18263 O  O     . HOH W 10 .    ? -51.172 70.009  100.704 1.00 21.94 ? 1583 HOH A O     1 
HETATM 18264 O  O     . HOH W 10 .    ? -22.702 67.655  81.525  1.00 24.69 ? 1584 HOH A O     1 
HETATM 18265 O  O     . HOH W 10 .    ? -47.056 54.439  89.962  1.00 17.45 ? 1585 HOH A O     1 
HETATM 18266 O  O     . HOH W 10 .    ? -42.971 66.618  63.793  1.00 32.54 ? 1586 HOH A O     1 
HETATM 18267 O  O     . HOH W 10 .    ? -23.062 75.212  99.959  1.00 22.30 ? 1587 HOH A O     1 
HETATM 18268 O  O     . HOH W 10 .    ? -42.760 47.762  81.382  1.00 23.39 ? 1588 HOH A O     1 
HETATM 18269 O  O     . HOH W 10 .    ? -25.198 88.578  79.528  1.00 24.11 ? 1589 HOH A O     1 
HETATM 18270 O  O     . HOH W 10 .    ? -18.594 61.019  66.819  1.00 27.87 ? 1590 HOH A O     1 
HETATM 18271 O  O     . HOH W 10 .    ? -52.816 78.511  87.842  1.00 27.61 ? 1591 HOH A O     1 
HETATM 18272 O  O     . HOH W 10 .    ? -28.643 62.285  102.537 1.00 19.12 ? 1592 HOH A O     1 
HETATM 18273 O  O     . HOH W 10 .    ? -44.748 74.031  75.256  1.00 23.50 ? 1593 HOH A O     1 
HETATM 18274 O  O     . HOH W 10 .    ? -58.783 46.040  92.440  1.00 36.71 ? 1594 HOH A O     1 
HETATM 18275 O  O     . HOH W 10 .    ? -0.782  77.597  117.574 1.00 25.02 ? 1595 HOH A O     1 
HETATM 18276 O  O     . HOH W 10 .    ? -2.710  53.991  104.907 1.00 26.74 ? 1596 HOH A O     1 
HETATM 18277 O  O     . HOH W 10 .    ? 8.778   55.470  105.194 1.00 27.80 ? 1597 HOH A O     1 
HETATM 18278 O  O     . HOH W 10 .    ? -51.750 65.158  95.051  1.00 18.62 ? 1598 HOH A O     1 
HETATM 18279 O  O     . HOH W 10 .    ? 0.712   74.952  107.638 1.00 25.64 ? 1599 HOH A O     1 
HETATM 18280 O  O     . HOH W 10 .    ? 10.442  57.644  106.161 1.00 25.18 ? 1600 HOH A O     1 
HETATM 18281 O  O     . HOH W 10 .    ? 8.880   57.149  97.892  1.00 25.60 ? 1601 HOH A O     1 
HETATM 18282 O  O     . HOH W 10 .    ? -37.045 59.118  94.610  1.00 18.19 ? 1602 HOH A O     1 
HETATM 18283 O  O     . HOH W 10 .    ? -40.992 59.112  80.668  1.00 20.49 ? 1603 HOH A O     1 
HETATM 18284 O  O     . HOH W 10 .    ? -13.671 59.550  122.886 1.00 26.86 ? 1604 HOH A O     1 
HETATM 18285 O  O     . HOH W 10 .    ? -24.191 83.455  112.323 1.00 22.84 ? 1605 HOH A O     1 
HETATM 18286 O  O     . HOH W 10 .    ? 3.665   58.161  105.153 1.00 20.26 ? 1606 HOH A O     1 
HETATM 18287 O  O     . HOH W 10 .    ? -48.544 57.971  86.583  1.00 15.47 ? 1607 HOH A O     1 
HETATM 18288 O  O     . HOH W 10 .    ? -60.023 38.633  83.013  1.00 32.40 ? 1608 HOH A O     1 
HETATM 18289 O  O     . HOH W 10 .    ? -18.565 57.620  97.632  1.00 17.37 ? 1609 HOH A O     1 
HETATM 18290 O  O     . HOH W 10 .    ? -32.236 89.287  109.042 1.00 28.25 ? 1610 HOH A O     1 
HETATM 18291 O  O     . HOH W 10 .    ? -28.988 62.195  117.220 1.00 23.38 ? 1611 HOH A O     1 
HETATM 18292 O  O     . HOH W 10 .    ? -0.591  93.333  105.048 1.00 27.11 ? 1612 HOH A O     1 
HETATM 18293 O  O     . HOH W 10 .    ? -42.920 78.095  76.107  1.00 27.29 ? 1613 HOH A O     1 
HETATM 18294 O  O     . HOH W 10 .    ? -33.046 82.439  98.317  1.00 25.97 ? 1614 HOH A O     1 
HETATM 18295 O  O     . HOH W 10 .    ? 5.912   91.221  106.995 1.00 27.94 ? 1615 HOH A O     1 
HETATM 18296 O  O     . HOH W 10 .    ? -9.090  65.362  114.290 1.00 17.97 ? 1616 HOH A O     1 
HETATM 18297 O  O     . HOH W 10 .    ? -31.864 58.784  115.880 1.00 37.83 ? 1617 HOH A O     1 
HETATM 18298 O  O     . HOH W 10 .    ? -2.033  78.099  121.643 1.00 26.78 ? 1618 HOH A O     1 
HETATM 18299 O  O     . HOH W 10 .    ? 16.678  69.369  118.257 1.00 21.87 ? 1619 HOH A O     1 
HETATM 18300 O  O     . HOH W 10 .    ? -10.154 74.654  104.500 1.00 18.69 ? 1620 HOH A O     1 
HETATM 18301 O  O     . HOH W 10 .    ? -18.776 79.755  127.705 1.00 28.24 ? 1621 HOH A O     1 
HETATM 18302 O  O     . HOH W 10 .    ? -8.523  60.257  94.451  1.00 34.40 ? 1622 HOH A O     1 
HETATM 18303 O  O     . HOH W 10 .    ? -20.163 55.124  107.486 1.00 27.56 ? 1623 HOH A O     1 
HETATM 18304 O  O     . HOH W 10 .    ? -52.714 72.954  64.574  1.00 29.62 ? 1624 HOH A O     1 
HETATM 18305 O  O     . HOH W 10 .    ? -60.268 61.058  76.106  1.00 16.80 ? 1625 HOH A O     1 
HETATM 18306 O  O     . HOH W 10 .    ? -38.645 65.706  88.596  1.00 27.47 ? 1626 HOH A O     1 
HETATM 18307 O  O     . HOH W 10 .    ? -41.932 71.850  64.528  1.00 25.63 ? 1627 HOH A O     1 
HETATM 18308 O  O     . HOH W 10 .    ? 25.352  80.014  107.909 1.00 33.81 ? 1628 HOH A O     1 
HETATM 18309 O  O     . HOH W 10 .    ? -45.731 64.019  105.799 1.00 33.31 ? 1629 HOH A O     1 
HETATM 18310 O  O     . HOH W 10 .    ? -1.102  70.545  96.406  1.00 32.44 ? 1630 HOH A O     1 
HETATM 18311 O  O     . HOH W 10 .    ? -53.169 54.309  100.593 1.00 28.77 ? 1631 HOH A O     1 
HETATM 18312 O  O     . HOH W 10 .    ? -38.442 41.121  71.979  1.00 28.59 ? 1632 HOH A O     1 
HETATM 18313 O  O     . HOH W 10 .    ? -35.783 76.405  83.467  1.00 29.95 ? 1633 HOH A O     1 
HETATM 18314 O  O     . HOH W 10 .    ? -6.187  65.413  114.558 1.00 21.94 ? 1634 HOH A O     1 
HETATM 18315 O  O     . HOH W 10 .    ? -41.525 90.904  99.089  1.00 27.17 ? 1635 HOH A O     1 
HETATM 18316 O  O     . HOH W 10 .    ? -62.509 62.094  68.311  1.00 24.47 ? 1636 HOH A O     1 
HETATM 18317 O  O     . HOH W 10 .    ? -31.671 71.816  83.264  1.00 29.92 ? 1637 HOH A O     1 
HETATM 18318 O  O     . HOH W 10 .    ? -9.358  78.274  132.078 1.00 35.07 ? 1638 HOH A O     1 
HETATM 18319 O  O     . HOH W 10 .    ? -46.871 67.751  59.927  1.00 25.29 ? 1639 HOH A O     1 
HETATM 18320 O  O     . HOH W 10 .    ? -39.530 89.174  91.139  1.00 34.12 ? 1640 HOH A O     1 
HETATM 18321 O  O     . HOH W 10 .    ? -49.951 78.478  77.824  1.00 28.27 ? 1641 HOH A O     1 
HETATM 18322 O  O     . HOH W 10 .    ? -0.825  66.313  94.755  1.00 32.91 ? 1642 HOH A O     1 
HETATM 18323 O  O     . HOH W 10 .    ? -2.307  85.786  113.477 1.00 27.63 ? 1643 HOH A O     1 
HETATM 18324 O  O     . HOH W 10 .    ? -19.308 70.393  87.990  1.00 24.51 ? 1644 HOH A O     1 
HETATM 18325 O  O     . HOH W 10 .    ? -25.881 62.854  110.456 1.00 21.16 ? 1645 HOH A O     1 
HETATM 18326 O  O     . HOH W 10 .    ? -34.068 84.203  123.688 1.00 29.63 ? 1646 HOH A O     1 
HETATM 18327 O  O     . HOH W 10 .    ? 16.291  58.074  103.192 1.00 21.06 ? 1647 HOH A O     1 
HETATM 18328 O  O     . HOH W 10 .    ? -23.341 67.389  97.762  1.00 17.87 ? 1648 HOH A O     1 
HETATM 18329 O  O     . HOH W 10 .    ? -11.999 73.482  128.900 1.00 28.37 ? 1649 HOH A O     1 
HETATM 18330 O  O     . HOH W 10 .    ? -8.924  80.816  74.942  1.00 29.44 ? 1650 HOH A O     1 
HETATM 18331 O  O     . HOH W 10 .    ? -1.547  84.094  118.276 1.00 27.35 ? 1651 HOH A O     1 
HETATM 18332 O  O     . HOH W 10 .    ? -43.336 61.458  100.510 1.00 23.24 ? 1652 HOH A O     1 
HETATM 18333 O  O     . HOH W 10 .    ? -44.328 89.509  113.651 1.00 36.41 ? 1653 HOH A O     1 
HETATM 18334 O  O     . HOH W 10 .    ? -3.309  62.775  77.793  1.00 23.15 ? 1654 HOH A O     1 
HETATM 18335 O  O     . HOH W 10 .    ? -19.715 91.258  77.291  1.00 30.12 ? 1655 HOH A O     1 
HETATM 18336 O  O     . HOH W 10 .    ? -59.671 52.183  66.195  1.00 22.35 ? 1656 HOH A O     1 
HETATM 18337 O  O     . HOH W 10 .    ? -20.356 89.237  75.410  1.00 31.93 ? 1657 HOH A O     1 
HETATM 18338 O  O     . HOH W 10 .    ? -48.977 78.649  75.262  1.00 30.44 ? 1658 HOH A O     1 
HETATM 18339 O  O     . HOH W 10 .    ? -9.181  60.364  107.464 1.00 19.87 ? 1659 HOH A O     1 
HETATM 18340 O  O     . HOH W 10 .    ? -67.346 68.291  80.681  1.00 20.77 ? 1660 HOH A O     1 
HETATM 18341 O  O     . HOH W 10 .    ? -64.242 71.221  71.082  1.00 26.67 ? 1661 HOH A O     1 
HETATM 18342 O  O     . HOH W 10 .    ? 13.617  82.423  114.579 1.00 24.63 ? 1662 HOH A O     1 
HETATM 18343 O  O     . HOH W 10 .    ? -12.912 77.552  91.326  1.00 16.68 ? 1663 HOH A O     1 
HETATM 18344 O  O     . HOH W 10 .    ? -44.732 56.034  95.444  1.00 16.78 ? 1664 HOH A O     1 
HETATM 18345 O  O     . HOH W 10 .    ? -50.560 56.973  71.864  1.00 24.66 ? 1665 HOH A O     1 
HETATM 18346 O  O     . HOH W 10 .    ? -37.382 60.667  96.770  1.00 18.26 ? 1666 HOH A O     1 
HETATM 18347 O  O     . HOH W 10 .    ? -45.906 62.858  92.928  1.00 15.53 ? 1667 HOH A O     1 
HETATM 18348 O  O     . HOH W 10 .    ? -11.136 68.106  108.448 1.00 16.33 ? 1668 HOH A O     1 
HETATM 18349 O  O     . HOH W 10 .    ? -46.864 30.772  85.848  1.00 30.52 ? 1669 HOH A O     1 
HETATM 18350 O  O     . HOH W 10 .    ? -50.397 49.304  100.161 1.00 24.30 ? 1670 HOH A O     1 
HETATM 18351 O  O     . HOH W 10 .    ? -60.772 47.349  88.924  1.00 26.35 ? 1671 HOH A O     1 
HETATM 18352 O  O     . HOH W 10 .    ? -63.594 54.227  72.417  1.00 25.14 ? 1672 HOH A O     1 
HETATM 18353 O  O     . HOH W 10 .    ? -34.632 82.857  118.917 1.00 25.69 ? 1673 HOH A O     1 
HETATM 18354 O  O     . HOH W 10 .    ? -65.100 45.092  78.351  1.00 32.01 ? 1674 HOH A O     1 
HETATM 18355 O  O     . HOH W 10 .    ? 16.452  71.647  119.595 1.00 22.30 ? 1675 HOH A O     1 
HETATM 18356 O  O     . HOH W 10 .    ? -5.826  77.954  95.278  1.00 21.85 ? 1676 HOH A O     1 
HETATM 18357 O  O     . HOH W 10 .    ? 20.279  62.289  99.373  1.00 24.20 ? 1677 HOH A O     1 
HETATM 18358 O  O     . HOH W 10 .    ? -54.046 72.566  68.479  1.00 23.67 ? 1678 HOH A O     1 
HETATM 18359 O  O     . HOH W 10 .    ? -68.033 60.448  70.073  1.00 29.12 ? 1679 HOH A O     1 
HETATM 18360 O  O     . HOH W 10 .    ? -3.080  56.184  100.063 1.00 26.75 ? 1680 HOH A O     1 
HETATM 18361 O  O     . HOH W 10 .    ? -35.808 73.586  83.941  1.00 23.53 ? 1681 HOH A O     1 
HETATM 18362 O  O     . HOH W 10 .    ? -46.237 65.536  92.194  1.00 17.70 ? 1682 HOH A O     1 
HETATM 18363 O  O     . HOH W 10 .    ? -15.205 67.526  73.355  1.00 24.26 ? 1683 HOH A O     1 
HETATM 18364 O  O     . HOH W 10 .    ? -23.809 86.919  74.033  1.00 30.59 ? 1684 HOH A O     1 
HETATM 18365 O  O     . HOH W 10 .    ? -28.153 71.164  90.181  1.00 24.52 ? 1685 HOH A O     1 
HETATM 18366 O  O     . HOH W 10 .    ? 14.974  83.360  111.555 1.00 24.29 ? 1686 HOH A O     1 
HETATM 18367 O  O     . HOH W 10 .    ? -21.839 59.677  122.973 1.00 27.79 ? 1687 HOH A O     1 
HETATM 18368 O  O     . HOH W 10 .    ? -20.456 78.983  70.379  1.00 24.18 ? 1688 HOH A O     1 
HETATM 18369 O  O     . HOH W 10 .    ? -68.351 37.354  75.820  1.00 36.46 ? 1689 HOH A O     1 
HETATM 18370 O  O     . HOH W 10 .    ? -48.822 75.448  95.911  1.00 21.02 ? 1690 HOH A O     1 
HETATM 18371 O  O     . HOH W 10 .    ? -20.041 85.345  75.901  1.00 30.61 ? 1691 HOH A O     1 
HETATM 18372 O  O     . HOH W 10 .    ? -66.817 61.849  75.862  1.00 19.14 ? 1692 HOH A O     1 
HETATM 18373 O  O     . HOH W 10 .    ? 3.704   60.664  101.381 1.00 22.86 ? 1693 HOH A O     1 
HETATM 18374 O  O     . HOH W 10 .    ? -16.411 68.317  97.023  1.00 15.95 ? 1694 HOH A O     1 
HETATM 18375 O  O     . HOH W 10 .    ? -4.582  70.500  107.261 1.00 25.92 ? 1695 HOH A O     1 
HETATM 18376 O  O     . HOH W 10 .    ? -36.356 39.535  85.361  1.00 34.30 ? 1696 HOH A O     1 
HETATM 18377 O  O     . HOH W 10 .    ? -1.307  73.588  89.002  1.00 29.93 ? 1697 HOH A O     1 
HETATM 18378 O  O     . HOH W 10 .    ? -62.163 70.626  83.230  1.00 20.40 ? 1698 HOH A O     1 
HETATM 18379 O  O     . HOH W 10 .    ? -31.599 61.181  90.900  1.00 21.83 ? 1699 HOH A O     1 
HETATM 18380 O  O     . HOH W 10 .    ? -58.237 58.215  101.498 1.00 27.03 ? 1700 HOH A O     1 
HETATM 18381 O  O     . HOH W 10 .    ? 10.586  67.871  116.981 1.00 23.53 ? 1701 HOH A O     1 
HETATM 18382 O  O     . HOH W 10 .    ? -40.022 78.545  100.336 1.00 22.04 ? 1702 HOH A O     1 
HETATM 18383 O  O     . HOH W 10 .    ? -32.926 59.967  110.043 1.00 29.51 ? 1703 HOH A O     1 
HETATM 18384 O  O     . HOH W 10 .    ? -48.356 59.408  83.050  1.00 15.47 ? 1704 HOH A O     1 
HETATM 18385 O  O     . HOH W 10 .    ? -56.244 36.942  76.427  1.00 31.77 ? 1705 HOH A O     1 
HETATM 18386 O  O     . HOH W 10 .    ? -24.491 67.513  105.575 1.00 19.94 ? 1706 HOH A O     1 
HETATM 18387 O  O     . HOH W 10 .    ? -23.922 54.713  101.735 1.00 24.34 ? 1707 HOH A O     1 
HETATM 18388 O  O     . HOH W 10 .    ? 8.469   65.232  94.742  1.00 26.44 ? 1708 HOH A O     1 
HETATM 18389 O  O     . HOH W 10 .    ? -4.946  59.511  118.699 1.00 22.13 ? 1709 HOH A O     1 
HETATM 18390 O  O     . HOH W 10 .    ? -47.138 66.865  94.192  1.00 17.62 ? 1710 HOH A O     1 
HETATM 18391 O  O     . HOH W 10 .    ? -16.884 60.437  106.835 1.00 21.14 ? 1711 HOH A O     1 
HETATM 18392 O  O     . HOH W 10 .    ? -46.322 72.875  64.413  1.00 17.98 ? 1712 HOH A O     1 
HETATM 18393 O  O     . HOH W 10 .    ? -38.880 61.707  92.214  1.00 17.41 ? 1713 HOH A O     1 
HETATM 18394 O  O     . HOH W 10 .    ? 9.051   68.225  94.315  1.00 30.93 ? 1714 HOH A O     1 
HETATM 18395 O  O     . HOH W 10 .    ? 15.603  62.031  116.524 1.00 33.20 ? 1715 HOH A O     1 
HETATM 18396 O  O     . HOH W 10 .    ? -35.165 66.812  101.967 1.00 22.50 ? 1716 HOH A O     1 
HETATM 18397 O  O     . HOH W 10 .    ? 13.391  86.998  121.127 1.00 31.68 ? 1717 HOH A O     1 
HETATM 18398 O  O     . HOH W 10 .    ? -42.397 68.153  91.450  1.00 18.77 ? 1718 HOH A O     1 
HETATM 18399 O  O     . HOH W 10 .    ? -47.591 49.153  93.522  1.00 18.33 ? 1719 HOH A O     1 
HETATM 18400 O  O     . HOH W 10 .    ? -7.119  93.912  113.612 1.00 31.18 ? 1720 HOH A O     1 
HETATM 18401 O  O     . HOH W 10 .    ? 2.533   65.259  113.526 1.00 28.01 ? 1721 HOH A O     1 
HETATM 18402 O  O     . HOH W 10 .    ? 9.848   63.327  113.366 1.00 28.83 ? 1722 HOH A O     1 
HETATM 18403 O  O     . HOH W 10 .    ? -6.229  76.409  111.441 1.00 17.87 ? 1723 HOH A O     1 
HETATM 18404 O  O     . HOH W 10 .    ? -62.110 36.943  78.539  1.00 40.41 ? 1724 HOH A O     1 
HETATM 18405 O  O     . HOH W 10 .    ? -7.226  70.798  94.450  1.00 23.25 ? 1725 HOH A O     1 
HETATM 18406 O  O     . HOH W 10 .    ? -29.456 76.913  73.160  1.00 28.86 ? 1726 HOH A O     1 
HETATM 18407 O  O     . HOH W 10 .    ? -54.823 47.729  67.501  1.00 27.29 ? 1727 HOH A O     1 
HETATM 18408 O  O     . HOH W 10 .    ? -17.735 87.071  92.476  1.00 24.50 ? 1728 HOH A O     1 
HETATM 18409 O  O     . HOH W 10 .    ? -46.656 24.540  82.784  1.00 35.25 ? 1729 HOH A O     1 
HETATM 18410 O  O     . HOH W 10 .    ? -32.604 62.081  111.991 1.00 25.22 ? 1730 HOH A O     1 
HETATM 18411 O  O     . HOH W 10 .    ? -2.832  74.771  84.596  1.00 28.89 ? 1731 HOH A O     1 
HETATM 18412 O  O     . HOH W 10 .    ? -42.841 56.951  89.815  1.00 17.01 ? 1732 HOH A O     1 
HETATM 18413 O  O     . HOH W 10 .    ? -20.399 52.573  78.247  1.00 31.35 ? 1733 HOH A O     1 
HETATM 18414 O  O     . HOH W 10 .    ? 0.997   62.526  111.605 1.00 26.48 ? 1734 HOH A O     1 
HETATM 18415 O  O     . HOH W 10 .    ? -20.734 66.164  81.361  1.00 22.81 ? 1735 HOH A O     1 
HETATM 18416 O  O     . HOH W 10 .    ? -23.163 83.661  91.850  1.00 18.09 ? 1736 HOH A O     1 
HETATM 18417 O  O     . HOH W 10 .    ? -47.278 82.629  101.833 1.00 25.80 ? 1737 HOH A O     1 
HETATM 18418 O  O     . HOH W 10 .    ? -1.861  79.601  100.250 1.00 22.66 ? 1738 HOH A O     1 
HETATM 18419 O  O     . HOH W 10 .    ? -52.927 62.283  94.987  1.00 19.29 ? 1739 HOH A O     1 
HETATM 18420 O  O     . HOH W 10 .    ? -32.668 75.332  126.776 1.00 29.83 ? 1740 HOH A O     1 
HETATM 18421 O  O     . HOH W 10 .    ? -1.927  58.423  96.867  1.00 29.01 ? 1741 HOH A O     1 
HETATM 18422 O  O     . HOH W 10 .    ? -46.813 56.256  87.744  1.00 15.94 ? 1742 HOH A O     1 
HETATM 18423 O  O     . HOH W 10 .    ? -54.220 55.737  68.629  1.00 18.61 ? 1743 HOH A O     1 
HETATM 18424 O  O     . HOH W 10 .    ? -46.714 32.156  70.585  1.00 32.50 ? 1744 HOH A O     1 
HETATM 18425 O  O     . HOH W 10 .    ? -57.566 60.475  61.190  1.00 20.54 ? 1745 HOH A O     1 
HETATM 18426 O  O     . HOH W 10 .    ? -61.895 53.227  91.343  1.00 24.91 ? 1746 HOH A O     1 
HETATM 18427 O  O     . HOH W 10 .    ? 19.064  82.261  113.732 1.00 28.84 ? 1747 HOH A O     1 
HETATM 18428 O  O     . HOH W 10 .    ? -55.603 26.777  92.000  1.00 37.17 ? 1748 HOH A O     1 
HETATM 18429 O  O     . HOH W 10 .    ? -59.563 42.893  89.599  1.00 29.70 ? 1749 HOH A O     1 
HETATM 18430 O  O     . HOH W 10 .    ? -65.141 43.274  86.495  1.00 31.11 ? 1750 HOH A O     1 
HETATM 18431 O  O     . HOH W 10 .    ? -14.237 42.093  71.267  1.00 31.42 ? 1751 HOH A O     1 
HETATM 18432 O  O     . HOH W 10 .    ? -32.285 88.915  95.582  1.00 22.45 ? 1752 HOH A O     1 
HETATM 18433 O  O     . HOH W 10 .    ? 3.845   74.071  116.696 1.00 28.89 ? 1753 HOH A O     1 
HETATM 18434 O  O     . HOH W 10 .    ? -19.945 91.065  97.911  1.00 35.11 ? 1754 HOH A O     1 
HETATM 18435 O  O     . HOH W 10 .    ? -38.366 69.630  123.772 1.00 34.09 ? 1755 HOH A O     1 
HETATM 18436 O  O     . HOH W 10 .    ? -33.631 78.566  74.433  1.00 26.79 ? 1756 HOH A O     1 
HETATM 18437 O  O     . HOH W 10 .    ? -38.966 50.680  98.944  1.00 25.15 ? 1757 HOH A O     1 
HETATM 18438 O  O     . HOH W 10 .    ? -31.950 60.324  105.862 1.00 24.63 ? 1758 HOH A O     1 
HETATM 18439 O  O     . HOH W 10 .    ? -30.668 81.566  123.372 1.00 29.86 ? 1759 HOH A O     1 
HETATM 18440 O  O     . HOH W 10 .    ? -41.626 71.897  114.702 1.00 26.59 ? 1760 HOH A O     1 
HETATM 18441 O  O     . HOH W 10 .    ? -20.988 81.796  116.129 1.00 21.14 ? 1761 HOH A O     1 
HETATM 18442 O  O     . HOH W 10 .    ? 1.970   85.979  118.362 1.00 29.18 ? 1762 HOH A O     1 
HETATM 18443 O  O     . HOH W 10 .    ? -21.709 55.274  95.316  1.00 26.13 ? 1763 HOH A O     1 
HETATM 18444 O  O     . HOH W 10 .    ? -16.435 54.070  101.032 1.00 29.33 ? 1764 HOH A O     1 
HETATM 18445 O  O     . HOH W 10 .    ? -48.358 64.571  97.148  1.00 21.30 ? 1765 HOH A O     1 
HETATM 18446 O  O     . HOH W 10 .    ? 22.872  63.188  115.794 1.00 23.56 ? 1766 HOH A O     1 
HETATM 18447 O  O     . HOH W 10 .    ? -55.588 47.778  70.044  1.00 23.93 ? 1767 HOH A O     1 
HETATM 18448 O  O     . HOH W 10 .    ? -21.168 71.107  75.923  1.00 21.10 ? 1768 HOH A O     1 
HETATM 18449 O  O     . HOH W 10 .    ? -27.619 54.167  110.130 1.00 28.83 ? 1769 HOH A O     1 
HETATM 18450 O  O     . HOH W 10 .    ? -7.795  50.999  53.107  1.00 27.99 ? 1770 HOH A O     1 
HETATM 18451 O  O     . HOH W 10 .    ? -42.061 89.148  97.205  1.00 28.92 ? 1771 HOH A O     1 
HETATM 18452 O  O     . HOH W 10 .    ? -44.837 31.780  84.320  1.00 29.98 ? 1772 HOH A O     1 
HETATM 18453 O  O     . HOH W 10 .    ? -58.150 65.041  91.343  1.00 28.11 ? 1773 HOH A O     1 
HETATM 18454 O  O     . HOH W 10 .    ? -55.051 37.628  89.440  1.00 29.15 ? 1774 HOH A O     1 
HETATM 18455 O  O     . HOH W 10 .    ? -49.835 47.864  97.643  1.00 24.57 ? 1775 HOH A O     1 
HETATM 18456 O  O     . HOH W 10 .    ? -8.776  82.258  105.291 1.00 21.58 ? 1776 HOH A O     1 
HETATM 18457 O  O     . HOH W 10 .    ? 6.428   61.321  103.576 1.00 17.04 ? 1777 HOH A O     1 
HETATM 18458 O  O     . HOH W 10 .    ? -31.162 91.363  107.515 1.00 26.54 ? 1778 HOH A O     1 
HETATM 18459 O  O     . HOH W 10 .    ? -20.340 86.985  91.867  1.00 21.59 ? 1779 HOH A O     1 
HETATM 18460 O  O     . HOH W 10 .    ? -46.217 78.507  96.393  1.00 22.02 ? 1780 HOH A O     1 
HETATM 18461 O  O     . HOH W 10 .    ? -8.310  75.400  70.669  1.00 31.10 ? 1781 HOH A O     1 
HETATM 18462 O  O     . HOH W 10 .    ? -0.899  84.070  110.035 1.00 26.11 ? 1782 HOH A O     1 
HETATM 18463 O  O     . HOH W 10 .    ? 2.221   84.380  101.941 1.00 23.77 ? 1783 HOH A O     1 
HETATM 18464 O  O     . HOH W 10 .    ? -38.957 73.473  90.562  1.00 30.92 ? 1784 HOH A O     1 
HETATM 18465 O  O     . HOH W 10 .    ? -1.762  84.091  115.663 1.00 31.26 ? 1785 HOH A O     1 
HETATM 18466 O  O     . HOH W 10 .    ? -40.184 61.894  94.925  1.00 19.95 ? 1786 HOH A O     1 
HETATM 18467 O  O     . HOH W 10 .    ? -34.049 45.939  85.007  1.00 32.94 ? 1787 HOH A O     1 
HETATM 18468 O  O     . HOH W 10 .    ? -30.115 83.780  101.739 1.00 24.17 ? 1788 HOH A O     1 
HETATM 18469 O  O     . HOH W 10 .    ? -49.862 54.527  59.423  1.00 32.32 ? 1789 HOH A O     1 
HETATM 18470 O  O     . HOH W 10 .    ? -9.848  56.216  82.840  1.00 26.72 ? 1790 HOH A O     1 
HETATM 18471 O  O     . HOH W 10 .    ? -7.113  42.136  66.419  1.00 26.96 ? 1791 HOH A O     1 
HETATM 18472 O  O     . HOH W 10 .    ? -41.061 82.156  111.080 1.00 29.66 ? 1792 HOH A O     1 
HETATM 18473 O  O     . HOH W 10 .    ? -42.238 71.038  95.533  1.00 21.79 ? 1793 HOH A O     1 
HETATM 18474 O  O     . HOH W 10 .    ? -39.785 76.861  93.543  1.00 23.13 ? 1794 HOH A O     1 
HETATM 18475 O  O     . HOH W 10 .    ? 10.053  81.678  125.647 1.00 29.56 ? 1795 HOH A O     1 
HETATM 18476 O  O     . HOH W 10 .    ? -3.806  82.771  97.827  1.00 23.88 ? 1796 HOH A O     1 
HETATM 18477 O  O     . HOH W 10 .    ? -47.843 71.049  111.672 1.00 34.68 ? 1797 HOH A O     1 
HETATM 18478 O  O     . HOH W 10 .    ? -25.844 88.753  116.619 1.00 24.64 ? 1798 HOH A O     1 
HETATM 18479 O  O     . HOH W 10 .    ? -28.621 69.652  86.212  1.00 26.33 ? 1799 HOH A O     1 
HETATM 18480 O  O     . HOH W 10 .    ? -31.838 41.509  98.834  1.00 33.29 ? 1800 HOH A O     1 
HETATM 18481 O  O     . HOH W 10 .    ? 10.278  67.349  112.316 1.00 29.81 ? 1801 HOH A O     1 
HETATM 18482 O  O     . HOH W 10 .    ? 17.167  80.578  97.245  1.00 32.69 ? 1802 HOH A O     1 
HETATM 18483 O  O     . HOH W 10 .    ? -50.158 76.152  101.838 1.00 23.90 ? 1803 HOH A O     1 
HETATM 18484 O  O     . HOH W 10 .    ? -41.815 27.938  70.511  1.00 36.28 ? 1804 HOH A O     1 
HETATM 18485 O  O     . HOH W 10 .    ? -5.659  68.264  78.049  1.00 28.43 ? 1805 HOH A O     1 
HETATM 18486 O  O     . HOH W 10 .    ? -38.558 67.849  98.488  1.00 24.44 ? 1806 HOH A O     1 
HETATM 18487 O  O     . HOH W 10 .    ? -10.542 82.496  78.601  1.00 34.83 ? 1807 HOH A O     1 
HETATM 18488 O  O     . HOH W 10 .    ? -66.015 71.792  80.678  1.00 25.12 ? 1808 HOH A O     1 
HETATM 18489 O  O     . HOH W 10 .    ? -27.432 52.116  99.152  1.00 23.12 ? 1809 HOH A O     1 
HETATM 18490 O  O     . HOH W 10 .    ? -26.799 50.506  97.054  1.00 27.63 ? 1810 HOH A O     1 
HETATM 18491 O  O     . HOH W 10 .    ? -57.753 53.702  96.450  1.00 22.66 ? 1811 HOH A O     1 
HETATM 18492 O  O     . HOH W 10 .    ? -26.158 94.360  78.529  1.00 32.60 ? 1812 HOH A O     1 
HETATM 18493 O  O     . HOH W 10 .    ? -49.064 61.903  57.024  1.00 23.90 ? 1813 HOH A O     1 
HETATM 18494 O  O     . HOH W 10 .    ? -38.671 70.593  82.021  1.00 22.29 ? 1814 HOH A O     1 
HETATM 18495 O  O     . HOH W 10 .    ? -2.233  78.190  105.637 1.00 20.06 ? 1815 HOH A O     1 
HETATM 18496 O  O     . HOH W 10 .    ? -22.422 54.620  86.474  1.00 32.39 ? 1816 HOH A O     1 
HETATM 18497 O  O     . HOH W 10 .    ? 18.365  73.424  118.596 1.00 23.88 ? 1817 HOH A O     1 
HETATM 18498 O  O     . HOH W 10 .    ? -0.425  52.958  63.211  1.00 26.36 ? 1818 HOH A O     1 
HETATM 18499 O  O     . HOH W 10 .    ? -23.119 54.234  93.184  1.00 25.23 ? 1819 HOH A O     1 
HETATM 18500 O  O     . HOH W 10 .    ? -25.093 89.243  100.241 1.00 22.10 ? 1820 HOH A O     1 
HETATM 18501 O  O     . HOH W 10 .    ? -43.061 77.860  78.695  1.00 23.64 ? 1821 HOH A O     1 
HETATM 18502 O  O     . HOH W 10 .    ? -44.452 59.708  87.945  1.00 15.41 ? 1822 HOH A O     1 
HETATM 18503 O  O     . HOH W 10 .    ? -6.947  71.243  104.450 1.00 24.00 ? 1823 HOH A O     1 
HETATM 18504 O  O     . HOH W 10 .    ? 13.968  78.673  121.161 1.00 29.81 ? 1824 HOH A O     1 
HETATM 18505 O  O     . HOH W 10 .    ? -8.600  77.454  92.302  1.00 19.37 ? 1825 HOH A O     1 
HETATM 18506 O  O     . HOH W 10 .    ? -37.090 69.640  119.677 1.00 29.34 ? 1826 HOH A O     1 
HETATM 18507 O  O     . HOH W 10 .    ? -0.567  74.435  96.466  1.00 32.63 ? 1827 HOH A O     1 
HETATM 18508 O  O     . HOH W 10 .    ? -8.241  72.732  100.819 1.00 24.39 ? 1828 HOH A O     1 
HETATM 18509 O  O     . HOH W 10 .    ? -35.375 95.337  96.636  1.00 28.00 ? 1829 HOH A O     1 
HETATM 18510 O  O     . HOH W 10 .    ? -28.952 95.372  89.394  1.00 30.29 ? 1830 HOH A O     1 
HETATM 18511 O  O     . HOH W 10 .    ? -18.756 92.682  108.220 1.00 30.55 ? 1831 HOH A O     1 
HETATM 18512 O  O     . HOH W 10 .    ? 12.355  67.604  93.576  1.00 32.92 ? 1832 HOH A O     1 
HETATM 18513 O  O     . HOH W 10 .    ? 25.362  64.550  102.990 1.00 27.77 ? 1833 HOH A O     1 
HETATM 18514 O  O     . HOH W 10 .    ? -48.582 72.543  113.374 1.00 37.84 ? 1834 HOH A O     1 
HETATM 18515 O  O     . HOH W 10 .    ? -45.303 61.327  85.843  1.00 16.38 ? 1835 HOH A O     1 
HETATM 18516 O  O     . HOH W 10 .    ? 22.353  76.399  115.420 1.00 26.15 ? 1836 HOH A O     1 
HETATM 18517 O  O     . HOH W 10 .    ? -4.549  73.246  77.347  1.00 26.34 ? 1837 HOH A O     1 
HETATM 18518 O  O     . HOH W 10 .    ? -20.668 91.277  109.410 1.00 28.71 ? 1838 HOH A O     1 
HETATM 18519 O  O     . HOH W 10 .    ? -8.346  88.014  93.928  1.00 37.60 ? 1839 HOH A O     1 
HETATM 18520 O  O     . HOH W 10 .    ? -3.544  78.080  101.796 1.00 23.89 ? 1840 HOH A O     1 
HETATM 18521 O  O     . HOH W 10 .    ? -3.505  57.661  68.467  1.00 30.26 ? 1841 HOH A O     1 
HETATM 18522 O  O     . HOH W 10 .    ? -7.636  62.661  107.471 1.00 18.07 ? 1842 HOH A O     1 
HETATM 18523 O  O     . HOH W 10 .    ? -27.636 90.828  116.069 1.00 25.22 ? 1843 HOH A O     1 
HETATM 18524 O  O     . HOH W 10 .    ? -41.116 80.463  88.036  1.00 19.62 ? 1844 HOH A O     1 
HETATM 18525 O  O     . HOH W 10 .    ? -28.296 56.162  90.911  1.00 27.25 ? 1845 HOH A O     1 
HETATM 18526 O  O     . HOH W 10 .    ? -38.432 73.156  87.760  1.00 29.43 ? 1846 HOH A O     1 
HETATM 18527 O  O     . HOH W 10 .    ? -13.103 53.823  110.874 1.00 29.05 ? 1847 HOH A O     1 
HETATM 18528 O  O     . HOH W 10 .    ? -61.417 68.932  68.799  1.00 21.66 ? 1848 HOH A O     1 
HETATM 18529 O  O     . HOH W 10 .    ? -23.615 89.414  102.450 1.00 25.89 ? 1849 HOH A O     1 
HETATM 18530 O  O     . HOH W 10 .    ? -58.560 58.161  63.205  1.00 21.17 ? 1850 HOH A O     1 
HETATM 18531 O  O     . HOH W 10 .    ? -4.772  82.721  125.373 1.00 33.79 ? 1851 HOH A O     1 
HETATM 18532 O  O     . HOH W 10 .    ? -37.214 68.688  83.546  1.00 27.59 ? 1852 HOH A O     1 
HETATM 18533 O  O     . HOH W 10 .    ? -13.085 66.159  113.135 1.00 17.97 ? 1853 HOH A O     1 
HETATM 18534 O  O     . HOH W 10 .    ? -1.815  80.671  112.305 1.00 27.94 ? 1854 HOH A O     1 
HETATM 18535 O  O     . HOH W 10 .    ? 17.974  57.636  105.424 1.00 28.53 ? 1855 HOH A O     1 
HETATM 18536 O  O     . HOH W 10 .    ? -26.739 84.708  74.363  1.00 29.14 ? 1856 HOH A O     1 
HETATM 18537 O  O     . HOH W 10 .    ? -14.428 85.368  77.403  1.00 29.31 ? 1857 HOH A O     1 
HETATM 18538 O  O     . HOH W 10 .    ? -39.229 71.374  84.507  1.00 24.92 ? 1858 HOH A O     1 
HETATM 18539 O  O     . HOH W 10 .    ? -47.553 77.376  92.440  1.00 25.39 ? 1859 HOH A O     1 
HETATM 18540 O  O     . HOH W 10 .    ? 0.845   66.708  96.905  1.00 22.87 ? 1860 HOH A O     1 
HETATM 18541 O  O     . HOH W 10 .    ? 11.941  65.555  119.014 1.00 25.53 ? 1861 HOH A O     1 
HETATM 18542 O  O     . HOH W 10 .    ? -34.675 56.741  105.845 1.00 23.73 ? 1862 HOH A O     1 
HETATM 18543 O  O     . HOH W 10 .    ? -3.616  88.012  105.198 1.00 25.12 ? 1863 HOH A O     1 
HETATM 18544 O  O     . HOH W 10 .    ? -17.555 53.472  76.451  1.00 30.29 ? 1864 HOH A O     1 
HETATM 18545 O  O     . HOH W 10 .    ? -25.507 79.483  95.428  1.00 19.35 ? 1865 HOH A O     1 
HETATM 18546 O  O     . HOH W 10 .    ? -50.844 66.604  106.738 1.00 28.17 ? 1866 HOH A O     1 
HETATM 18547 O  O     . HOH W 10 .    ? -36.655 81.065  76.146  1.00 25.82 ? 1867 HOH A O     1 
HETATM 18548 O  O     . HOH W 10 .    ? -38.440 40.401  74.694  1.00 31.21 ? 1868 HOH A O     1 
HETATM 18549 O  O     . HOH W 10 .    ? -59.653 58.687  77.084  1.00 17.11 ? 1869 HOH A O     1 
HETATM 18550 O  O     . HOH W 10 .    ? -0.558  86.830  106.016 1.00 24.54 ? 1870 HOH A O     1 
HETATM 18551 O  O     . HOH W 10 .    ? -1.595  70.447  116.719 1.00 23.83 ? 1871 HOH A O     1 
HETATM 18552 O  O     . HOH W 10 .    ? -50.424 72.714  101.566 1.00 23.50 ? 1872 HOH A O     1 
HETATM 18553 O  O     . HOH W 10 .    ? -40.005 85.112  104.195 1.00 26.98 ? 1873 HOH A O     1 
HETATM 18554 O  O     . HOH W 10 .    ? 5.422   58.965  97.638  1.00 28.69 ? 1874 HOH A O     1 
HETATM 18555 O  O     . HOH W 10 .    ? -34.502 91.054  122.545 1.00 34.73 ? 1875 HOH A O     1 
HETATM 18556 O  O     . HOH W 10 .    ? -31.039 50.462  105.207 1.00 27.96 ? 1876 HOH A O     1 
HETATM 18557 O  O     . HOH W 10 .    ? -14.680 58.386  110.450 1.00 29.74 ? 1877 HOH A O     1 
HETATM 18558 O  O     . HOH W 10 .    ? -31.511 91.773  80.785  1.00 30.07 ? 1878 HOH A O     1 
HETATM 18559 O  O     . HOH W 10 .    ? -48.211 49.273  96.187  1.00 21.57 ? 1879 HOH A O     1 
HETATM 18560 O  O     . HOH W 10 .    ? -45.771 57.846  102.545 1.00 28.05 ? 1880 HOH A O     1 
HETATM 18561 O  O     . HOH W 10 .    ? 2.382   74.628  109.811 1.00 21.61 ? 1881 HOH A O     1 
HETATM 18562 O  O     . HOH W 10 .    ? -15.305 59.540  127.049 1.00 29.50 ? 1882 HOH A O     1 
HETATM 18563 O  O     . HOH W 10 .    ? -21.335 58.473  97.701  1.00 18.86 ? 1883 HOH A O     1 
HETATM 18564 O  O     . HOH W 10 .    ? -11.708 43.738  74.264  1.00 27.38 ? 1884 HOH A O     1 
HETATM 18565 O  O     . HOH W 10 .    ? -25.846 59.674  114.859 1.00 25.71 ? 1885 HOH A O     1 
HETATM 18566 O  O     . HOH W 10 .    ? -10.020 64.170  96.529  1.00 20.55 ? 1886 HOH A O     1 
HETATM 18567 O  O     . HOH W 10 .    ? 2.004   76.701  117.339 1.00 23.97 ? 1887 HOH A O     1 
HETATM 18568 O  O     . HOH W 10 .    ? -7.512  64.989  94.736  1.00 31.14 ? 1888 HOH A O     1 
HETATM 18569 O  O     . HOH W 10 .    ? -50.308 68.874  92.302  1.00 19.45 ? 1889 HOH A O     1 
HETATM 18570 O  O     . HOH W 10 .    ? -18.866 69.072  104.958 1.00 19.49 ? 1890 HOH A O     1 
HETATM 18571 O  O     . HOH W 10 .    ? -25.364 69.577  74.737  1.00 27.94 ? 1891 HOH A O     1 
HETATM 18572 O  O     . HOH W 10 .    ? 24.812  77.639  109.921 1.00 31.71 ? 1892 HOH A O     1 
HETATM 18573 O  O     . HOH W 10 .    ? -25.899 68.352  90.995  1.00 24.46 ? 1893 HOH A O     1 
HETATM 18574 O  O     . HOH W 10 .    ? -39.766 86.705  89.707  1.00 27.49 ? 1894 HOH A O     1 
HETATM 18575 O  O     . HOH W 10 .    ? -34.726 77.733  85.367  1.00 24.33 ? 1895 HOH A O     1 
HETATM 18576 O  O     . HOH W 10 .    ? -54.090 69.183  93.745  1.00 23.04 ? 1896 HOH A O     1 
HETATM 18577 O  O     . HOH W 10 .    ? -39.539 66.952  94.752  1.00 25.91 ? 1897 HOH A O     1 
HETATM 18578 O  O     . HOH W 10 .    ? -37.247 51.877  61.084  1.00 35.04 ? 1898 HOH A O     1 
HETATM 18579 O  O     . HOH W 10 .    ? -11.525 54.232  100.640 1.00 21.60 ? 1899 HOH A O     1 
HETATM 18580 O  O     . HOH W 10 .    ? -62.984 67.852  66.501  1.00 29.25 ? 1900 HOH A O     1 
HETATM 18581 O  O     . HOH W 10 .    ? -9.556  60.780  84.536  1.00 23.10 ? 1901 HOH A O     1 
HETATM 18582 O  O     . HOH W 10 .    ? -27.828 62.164  89.428  1.00 19.69 ? 1902 HOH A O     1 
HETATM 18583 O  O     . HOH W 10 .    ? -13.776 54.365  77.512  1.00 23.97 ? 1903 HOH A O     1 
HETATM 18584 O  O     . HOH W 10 .    ? -14.188 86.955  101.099 1.00 23.44 ? 1904 HOH A O     1 
HETATM 18585 O  O     . HOH W 10 .    ? -58.794 38.151  96.064  1.00 29.15 ? 1905 HOH A O     1 
HETATM 18586 O  O     . HOH W 10 .    ? -50.028 54.581  74.217  1.00 23.98 ? 1906 HOH A O     1 
HETATM 18587 O  O     . HOH W 10 .    ? -37.789 45.689  104.730 1.00 32.56 ? 1907 HOH A O     1 
HETATM 18588 O  O     . HOH W 10 .    ? -22.662 77.198  70.474  1.00 22.94 ? 1908 HOH A O     1 
HETATM 18589 O  O     . HOH W 10 .    ? -34.141 70.994  76.168  1.00 32.56 ? 1909 HOH A O     1 
HETATM 18590 O  O     . HOH W 10 .    ? -38.748 61.868  74.301  1.00 31.24 ? 1910 HOH A O     1 
HETATM 18591 O  O     . HOH W 10 .    ? 2.259   78.177  98.506  1.00 21.45 ? 1911 HOH A O     1 
HETATM 18592 O  O     . HOH W 10 .    ? -1.956  54.590  102.142 1.00 22.46 ? 1912 HOH A O     1 
HETATM 18593 O  O     . HOH W 10 .    ? -31.113 96.422  105.311 1.00 30.48 ? 1913 HOH A O     1 
HETATM 18594 O  O     . HOH W 10 .    ? -40.837 65.215  62.275  1.00 31.26 ? 1914 HOH A O     1 
HETATM 18595 O  O     . HOH W 10 .    ? 10.765  61.356  115.587 1.00 31.96 ? 1915 HOH A O     1 
HETATM 18596 O  O     . HOH W 10 .    ? -5.479  55.986  101.594 1.00 27.19 ? 1916 HOH A O     1 
HETATM 18597 O  O     . HOH W 10 .    ? -55.649 41.938  97.219  1.00 33.05 ? 1917 HOH A O     1 
HETATM 18598 O  O     . HOH W 10 .    ? -3.916  82.484  110.352 1.00 27.88 ? 1918 HOH A O     1 
HETATM 18599 O  O     . HOH W 10 .    ? -57.106 73.794  96.798  1.00 32.93 ? 1919 HOH A O     1 
HETATM 18600 O  O     . HOH W 10 .    ? -44.039 91.021  100.445 1.00 33.64 ? 1920 HOH A O     1 
HETATM 18601 O  O     . HOH W 10 .    ? -18.004 85.829  77.764  1.00 27.46 ? 1921 HOH A O     1 
HETATM 18602 O  O     . HOH W 10 .    ? 21.179  72.887  116.516 1.00 27.81 ? 1922 HOH A O     1 
HETATM 18603 O  O     . HOH W 10 .    ? 16.087  65.408  120.316 1.00 25.69 ? 1923 HOH A O     1 
HETATM 18604 O  O     . HOH W 10 .    ? -62.265 67.319  60.763  1.00 34.09 ? 1924 HOH A O     1 
HETATM 18605 O  O     . HOH W 10 .    ? -11.323 67.177  127.904 1.00 34.78 ? 1925 HOH A O     1 
HETATM 18606 O  O     . HOH W 10 .    ? -40.560 38.203  85.523  1.00 28.19 ? 1926 HOH A O     1 
HETATM 18607 O  O     . HOH W 10 .    ? -20.272 79.412  115.238 1.00 20.34 ? 1927 HOH A O     1 
HETATM 18608 O  O     . HOH W 10 .    ? -2.597  62.896  113.770 1.00 32.45 ? 1928 HOH A O     1 
HETATM 18609 O  O     . HOH W 10 .    ? -10.721 63.961  115.978 1.00 19.74 ? 1929 HOH A O     1 
HETATM 18610 O  O     . HOH W 10 .    ? 0.148   64.477  107.621 1.00 17.43 ? 1930 HOH A O     1 
HETATM 18611 O  O     . HOH W 10 .    ? -25.512 83.151  72.900  1.00 29.54 ? 1931 HOH A O     1 
HETATM 18612 O  O     . HOH W 10 .    ? -50.197 73.240  63.070  1.00 21.22 ? 1932 HOH A O     1 
HETATM 18613 O  O     . HOH W 10 .    ? 10.781  85.470  125.056 1.00 26.33 ? 1933 HOH A O     1 
HETATM 18614 O  O     . HOH W 10 .    ? -36.998 83.091  121.310 1.00 31.12 ? 1934 HOH A O     1 
HETATM 18615 O  O     . HOH W 10 .    ? -54.748 79.616  81.818  1.00 34.40 ? 1935 HOH A O     1 
HETATM 18616 O  O     . HOH W 10 .    ? -31.471 84.276  123.756 1.00 28.03 ? 1936 HOH A O     1 
HETATM 18617 O  O     . HOH W 10 .    ? -22.457 52.845  104.716 1.00 34.77 ? 1937 HOH A O     1 
HETATM 18618 O  O     . HOH W 10 .    ? -31.578 74.707  88.058  1.00 26.67 ? 1938 HOH A O     1 
HETATM 18619 O  O     . HOH W 10 .    ? -27.319 63.186  86.767  1.00 21.51 ? 1939 HOH A O     1 
HETATM 18620 O  O     . HOH W 10 .    ? -11.056 87.266  91.852  1.00 31.39 ? 1940 HOH A O     1 
HETATM 18621 O  O     . HOH W 10 .    ? -60.038 63.135  77.730  1.00 20.69 ? 1941 HOH A O     1 
HETATM 18622 O  O     . HOH W 10 .    ? 18.440  62.484  94.821  1.00 31.01 ? 1942 HOH A O     1 
HETATM 18623 O  O     . HOH W 10 .    ? -0.543  68.051  118.055 1.00 26.11 ? 1943 HOH A O     1 
HETATM 18624 O  O     . HOH W 10 .    ? 12.706  89.134  116.617 1.00 32.01 ? 1944 HOH A O     1 
HETATM 18625 O  O     . HOH W 10 .    ? -46.136 55.265  92.483  1.00 17.33 ? 1945 HOH A O     1 
HETATM 18626 O  O     . HOH W 10 .    ? -23.321 95.001  118.575 1.00 31.77 ? 1946 HOH A O     1 
HETATM 18627 O  O     . HOH W 10 .    ? -65.321 59.555  99.870  1.00 42.04 ? 1947 HOH A O     1 
HETATM 18628 O  O     . HOH W 10 .    ? 6.777   55.462  99.106  1.00 18.50 ? 1948 HOH A O     1 
HETATM 18629 O  O     . HOH W 10 .    ? -37.334 45.447  78.454  1.00 32.18 ? 1949 HOH A O     1 
HETATM 18630 O  O     . HOH W 10 .    ? -31.962 76.934  74.681  1.00 33.25 ? 1950 HOH A O     1 
HETATM 18631 O  O     . HOH W 10 .    ? -2.381  91.266  105.998 1.00 26.66 ? 1951 HOH A O     1 
HETATM 18632 O  O     . HOH W 10 .    ? -37.964 86.558  102.215 1.00 26.54 ? 1952 HOH A O     1 
HETATM 18633 O  O     . HOH W 10 .    ? 0.931   57.440  107.982 1.00 19.13 ? 1953 HOH A O     1 
HETATM 18634 O  O     . HOH W 10 .    ? -15.356 53.411  75.719  1.00 30.29 ? 1954 HOH A O     1 
HETATM 18635 O  O     . HOH W 10 .    ? -56.951 40.552  67.959  1.00 34.57 ? 1955 HOH A O     1 
HETATM 18636 O  O     . HOH W 10 .    ? -22.263 67.673  73.835  1.00 32.90 ? 1956 HOH A O     1 
HETATM 18637 O  O     . HOH W 10 .    ? -9.215  41.106  69.355  1.00 34.14 ? 1957 HOH A O     1 
HETATM 18638 O  O     . HOH W 10 .    ? -3.167  76.265  77.627  1.00 22.36 ? 1958 HOH A O     1 
HETATM 18639 O  O     . HOH W 10 .    ? 22.799  73.277  98.676  1.00 37.40 ? 1959 HOH A O     1 
HETATM 18640 O  O     . HOH W 10 .    ? -31.912 94.756  127.528 1.00 36.04 ? 1960 HOH A O     1 
HETATM 18641 O  O     . HOH W 10 .    ? -3.992  79.121  93.723  1.00 30.35 ? 1961 HOH A O     1 
HETATM 18642 O  O     . HOH W 10 .    ? -26.360 69.890  96.098  1.00 27.78 ? 1962 HOH A O     1 
HETATM 18643 O  O     . HOH W 10 .    ? -63.658 62.728  98.315  1.00 31.44 ? 1963 HOH A O     1 
HETATM 18644 O  O     . HOH W 10 .    ? -66.790 69.032  84.213  1.00 28.34 ? 1964 HOH A O     1 
HETATM 18645 O  O     . HOH W 10 .    ? -43.606 56.571  92.446  1.00 17.60 ? 1965 HOH A O     1 
HETATM 18646 O  O     . HOH W 10 .    ? -22.868 54.634  97.645  1.00 25.63 ? 1966 HOH A O     1 
HETATM 18647 O  O     . HOH W 10 .    ? -37.420 49.993  101.163 1.00 25.82 ? 1967 HOH A O     1 
HETATM 18648 O  O     . HOH W 10 .    ? -62.581 60.296  96.109  1.00 24.60 ? 1968 HOH A O     1 
HETATM 18649 O  O     . HOH W 10 .    ? -49.083 65.672  54.413  1.00 31.48 ? 1969 HOH A O     1 
HETATM 18650 O  O     . HOH W 10 .    ? -9.223  52.064  107.766 1.00 28.33 ? 1970 HOH A O     1 
HETATM 18651 O  O     . HOH W 10 .    ? -19.252 60.051  108.627 1.00 30.25 ? 1971 HOH A O     1 
HETATM 18652 O  O     . HOH W 10 .    ? -1.252  75.090  117.266 1.00 31.05 ? 1972 HOH A O     1 
HETATM 18653 O  O     . HOH W 10 .    ? -65.302 55.493  80.861  1.00 26.51 ? 1973 HOH A O     1 
HETATM 18654 O  O     . HOH W 10 .    ? -35.732 40.594  92.355  1.00 23.42 ? 1974 HOH A O     1 
HETATM 18655 O  O     . HOH W 10 .    ? -41.810 64.834  58.664  1.00 26.20 ? 1975 HOH A O     1 
HETATM 18656 O  O     . HOH W 10 .    ? 12.494  63.808  121.059 1.00 31.60 ? 1976 HOH A O     1 
HETATM 18657 O  O     . HOH W 10 .    ? -3.684  75.516  102.291 1.00 25.88 ? 1977 HOH A O     1 
HETATM 18658 O  O     . HOH W 10 .    ? -33.851 42.745  92.900  1.00 23.08 ? 1978 HOH A O     1 
HETATM 18659 O  O     . HOH W 10 .    ? -37.832 75.720  97.958  1.00 26.59 ? 1979 HOH A O     1 
HETATM 18660 O  O     . HOH W 10 .    ? 4.119   86.362  101.263 1.00 27.78 ? 1980 HOH A O     1 
HETATM 18661 O  O     . HOH W 10 .    ? 0.839   69.945  87.830  1.00 31.11 ? 1981 HOH A O     1 
HETATM 18662 O  O     . HOH W 10 .    ? -68.221 64.644  85.585  1.00 31.07 ? 1982 HOH A O     1 
HETATM 18663 O  O     . HOH W 10 .    ? -20.809 54.892  99.432  1.00 30.14 ? 1983 HOH A O     1 
HETATM 18664 O  O     . HOH W 10 .    ? -2.210  80.279  97.726  1.00 26.49 ? 1984 HOH A O     1 
HETATM 18665 O  O     . HOH W 10 .    ? -18.409 54.152  99.055  1.00 31.95 ? 1985 HOH A O     1 
HETATM 18666 O  O     . HOH W 10 .    ? -66.583 64.690  88.278  1.00 28.81 ? 1986 HOH A O     1 
HETATM 18667 O  O     . HOH W 10 .    ? -6.119  75.480  103.417 1.00 25.51 ? 1987 HOH A O     1 
HETATM 18668 O  O     . HOH W 10 .    ? -53.859 49.482  60.634  1.00 30.32 ? 1988 HOH A O     1 
HETATM 18669 O  O     . HOH W 10 .    ? -46.675 52.051  72.302  1.00 23.34 ? 1989 HOH A O     1 
HETATM 18670 O  O     . HOH W 10 .    ? -54.759 45.491  92.395  1.00 29.29 ? 1990 HOH A O     1 
HETATM 18671 O  O     . HOH W 10 .    ? 14.626  82.928  119.738 1.00 28.10 ? 1991 HOH A O     1 
HETATM 18672 O  O     . HOH W 10 .    ? -35.257 65.296  66.134  1.00 31.91 ? 1992 HOH A O     1 
HETATM 18673 O  O     . HOH W 10 .    ? -42.025 89.233  94.051  1.00 34.46 ? 1993 HOH A O     1 
HETATM 18674 O  O     . HOH W 10 .    ? -0.399  67.427  86.634  1.00 32.17 ? 1994 HOH A O     1 
HETATM 18675 O  O     . HOH W 10 .    ? -28.982 57.627  88.964  1.00 29.25 ? 1995 HOH A O     1 
HETATM 18676 O  O     . HOH W 10 .    ? -32.165 68.090  101.618 1.00 30.41 ? 1996 HOH A O     1 
HETATM 18677 O  O     . HOH W 10 .    ? -57.525 32.531  88.068  1.00 28.09 ? 1997 HOH A O     1 
HETATM 18678 O  O     . HOH W 10 .    ? -40.139 47.420  104.441 1.00 30.70 ? 1998 HOH A O     1 
HETATM 18679 O  O     . HOH W 10 .    ? -23.763 76.267  133.928 1.00 33.71 ? 1999 HOH A O     1 
HETATM 18680 O  O     . HOH W 10 .    ? -46.283 78.559  90.359  1.00 20.58 ? 2000 HOH A O     1 
HETATM 18681 O  O     . HOH W 10 .    ? -47.915 64.272  56.312  1.00 29.27 ? 2001 HOH A O     1 
HETATM 18682 O  O     . HOH W 10 .    ? -51.112 54.990  105.269 1.00 36.45 ? 2002 HOH A O     1 
HETATM 18683 O  O     . HOH W 10 .    ? -53.244 57.269  73.997  1.00 26.65 ? 2003 HOH A O     1 
HETATM 18684 O  O     . HOH W 10 .    ? -53.453 66.682  102.295 1.00 33.45 ? 2004 HOH A O     1 
HETATM 18685 O  O     . HOH W 10 .    ? -34.608 59.497  106.764 1.00 27.24 ? 2005 HOH A O     1 
HETATM 18686 O  O     . HOH W 10 .    ? -42.208 80.406  70.408  1.00 33.29 ? 2006 HOH A O     1 
HETATM 18687 O  O     . HOH W 10 .    ? -31.579 78.415  91.401  1.00 26.03 ? 2007 HOH A O     1 
HETATM 18688 O  O     . HOH W 10 .    ? -40.410 68.131  89.256  1.00 26.97 ? 2008 HOH A O     1 
HETATM 18689 O  O     . HOH W 10 .    ? -52.278 55.446  70.638  1.00 23.38 ? 2009 HOH A O     1 
HETATM 18690 O  O     . HOH W 10 .    ? -27.528 92.477  77.113  1.00 35.63 ? 2010 HOH A O     1 
HETATM 18691 O  O     . HOH W 10 .    ? -28.030 51.434  110.122 1.00 33.73 ? 2011 HOH A O     1 
HETATM 18692 O  O     . HOH W 10 .    ? 16.087  65.051  117.510 1.00 32.47 ? 2012 HOH A O     1 
HETATM 18693 O  O     . HOH W 10 .    ? -39.765 35.775  89.109  1.00 32.42 ? 2013 HOH A O     1 
HETATM 18694 O  O     . HOH W 10 .    ? -26.403 74.895  133.297 1.00 35.29 ? 2014 HOH A O     1 
HETATM 18695 O  O     . HOH W 10 .    ? -19.109 59.874  111.385 1.00 24.87 ? 2015 HOH A O     1 
HETATM 18696 O  O     . HOH W 10 .    ? -23.083 74.533  69.966  1.00 29.60 ? 2016 HOH A O     1 
HETATM 18697 O  O     . HOH W 10 .    ? -64.556 51.486  73.491  1.00 30.20 ? 2017 HOH A O     1 
HETATM 18698 O  O     . HOH W 10 .    ? -1.967  92.347  109.485 1.00 34.08 ? 2018 HOH A O     1 
HETATM 18699 O  O     . HOH W 10 .    ? -8.003  73.198  103.889 1.00 30.07 ? 2019 HOH A O     1 
HETATM 18700 O  O     . HOH W 10 .    ? -27.331 65.716  103.071 1.00 26.35 ? 2020 HOH A O     1 
HETATM 18701 O  O     . HOH W 10 .    ? 7.417   62.801  112.861 1.00 31.75 ? 2021 HOH A O     1 
HETATM 18702 O  O     . HOH W 10 .    ? -60.424 64.470  92.528  1.00 31.35 ? 2022 HOH A O     1 
HETATM 18703 O  O     . HOH W 10 .    ? -59.224 30.859  87.018  1.00 31.59 ? 2023 HOH A O     1 
HETATM 18704 O  O     . HOH W 10 .    ? -26.407 67.770  94.408  1.00 32.85 ? 2024 HOH A O     1 
HETATM 18705 O  O     . HOH W 10 .    ? -33.330 84.656  77.270  1.00 24.66 ? 2025 HOH A O     1 
HETATM 18706 O  O     . HOH W 10 .    ? -55.807 57.856  102.621 1.00 26.86 ? 2026 HOH A O     1 
HETATM 18707 O  O     . HOH W 10 .    ? -35.182 76.651  87.730  1.00 25.67 ? 2027 HOH A O     1 
HETATM 18708 O  O     . HOH W 10 .    ? -64.785 63.560  68.573  1.00 30.31 ? 2028 HOH A O     1 
HETATM 18709 O  O     . HOH W 10 .    ? -28.204 63.934  90.966  1.00 30.83 ? 2029 HOH A O     1 
HETATM 18710 O  O     . HOH W 10 .    ? -64.387 65.611  66.703  1.00 32.30 ? 2030 HOH A O     1 
HETATM 18711 O  O     . HOH W 10 .    ? -15.678 58.157  106.557 1.00 29.35 ? 2031 HOH A O     1 
HETATM 18712 O  O     . HOH W 10 .    ? 15.712  83.609  116.814 1.00 32.08 ? 2032 HOH A O     1 
HETATM 18713 O  O     . HOH W 10 .    ? -35.671 74.011  87.115  1.00 29.37 ? 2033 HOH A O     1 
HETATM 18714 O  O     . HOH W 10 .    ? -21.694 93.401  107.501 1.00 30.79 ? 2034 HOH A O     1 
HETATM 18715 O  O     . HOH W 10 .    ? 3.434   65.171  96.644  1.00 25.92 ? 2035 HOH A O     1 
HETATM 18716 O  O     . HOH W 10 .    ? -66.195 54.551  78.870  1.00 31.68 ? 2036 HOH A O     1 
HETATM 18717 O  O     . HOH W 10 .    ? -53.122 64.514  101.158 1.00 29.58 ? 2037 HOH A O     1 
HETATM 18718 O  O     . HOH W 10 .    ? -52.653 74.397  62.206  1.00 21.93 ? 2038 HOH A O     1 
HETATM 18719 O  O     . HOH W 10 .    ? -36.601 63.450  90.831  1.00 28.33 ? 2039 HOH A O     1 
HETATM 18720 O  O     . HOH W 10 .    ? 4.511   60.840  98.644  1.00 23.82 ? 2040 HOH A O     1 
HETATM 18721 O  O     . HOH W 10 .    ? -2.905  57.234  70.875  1.00 27.70 ? 2041 HOH A O     1 
HETATM 18722 O  O     . HOH W 10 .    ? -24.448 77.848  68.690  1.00 35.41 ? 2042 HOH A O     1 
HETATM 18723 O  O     . HOH W 10 .    ? -10.929 78.923  92.695  1.00 19.64 ? 2043 HOH A O     1 
HETATM 18724 O  O     . HOH W 10 .    ? -11.907 59.947  106.955 1.00 30.70 ? 2044 HOH A O     1 
HETATM 18725 O  O     . HOH W 10 .    ? -23.373 71.638  74.468  1.00 30.52 ? 2045 HOH A O     1 
HETATM 18726 O  O     . HOH W 10 .    ? -7.154  55.419  82.956  1.00 28.60 ? 2046 HOH A O     1 
HETATM 18727 O  O     . HOH W 10 .    ? -42.465 64.174  106.565 1.00 31.44 ? 2047 HOH A O     1 
HETATM 18728 O  O     . HOH W 10 .    ? -10.128 67.622  132.781 1.00 35.05 ? 2048 HOH A O     1 
HETATM 18729 O  O     . HOH W 10 .    ? -34.041 81.157  74.985  1.00 28.21 ? 2049 HOH A O     1 
HETATM 18730 O  O     . HOH W 10 .    ? -9.835  73.959  129.627 1.00 34.43 ? 2050 HOH A O     1 
HETATM 18731 O  O     . HOH W 10 .    ? -58.494 32.579  90.463  1.00 26.92 ? 2051 HOH A O     1 
HETATM 18732 O  O     . HOH W 10 .    ? -67.493 66.377  83.478  1.00 23.11 ? 2052 HOH A O     1 
HETATM 18733 O  O     . HOH W 10 .    ? -56.939 75.071  79.589  1.00 28.85 ? 2053 HOH A O     1 
HETATM 18734 O  O     . HOH W 10 .    ? -30.704 79.732  126.041 1.00 33.70 ? 2054 HOH A O     1 
HETATM 18735 O  O     . HOH W 10 .    ? -53.858 45.792  94.979  1.00 34.33 ? 2055 HOH A O     1 
HETATM 18736 O  O     . HOH W 10 .    ? -32.666 73.928  84.058  1.00 33.16 ? 2056 HOH A O     1 
HETATM 18737 O  O     . HOH W 10 .    ? -26.186 83.728  70.218  1.00 37.72 ? 2057 HOH A O     1 
HETATM 18738 O  O     . HOH W 10 .    ? -27.634 59.734  116.809 1.00 33.69 ? 2058 HOH A O     1 
HETATM 18739 O  O     . HOH W 10 .    ? -34.116 81.450  122.930 1.00 32.80 ? 2059 HOH A O     1 
HETATM 18740 O  O     . HOH W 10 .    ? -57.174 44.349  92.563  1.00 35.92 ? 2060 HOH A O     1 
HETATM 18741 O  O     . HOH W 10 .    ? -25.935 62.357  102.640 1.00 27.14 ? 2061 HOH A O     1 
HETATM 18742 O  O     . HOH W 10 .    ? -45.372 82.881  89.113  1.00 36.57 ? 2062 HOH A O     1 
HETATM 18743 O  O     . HOH W 10 .    ? -23.159 91.793  104.026 1.00 31.73 ? 2063 HOH A O     1 
HETATM 18744 O  O     . HOH W 10 .    ? -18.951 74.823  109.664 1.00 19.74 ? 2064 HOH A O     1 
HETATM 18745 O  O     . HOH W 10 .    ? 1.764   75.301  120.143 1.00 36.53 ? 2065 HOH A O     1 
HETATM 18746 O  O     . HOH W 10 .    ? -53.672 69.224  101.261 1.00 29.55 ? 2066 HOH A O     1 
HETATM 18747 O  O     . HOH W 10 .    ? -49.487 77.708  94.253  1.00 33.69 ? 2067 HOH A O     1 
HETATM 18748 O  O     . HOH W 10 .    ? 20.260  61.934  96.710  1.00 32.33 ? 2068 HOH A O     1 
HETATM 18749 O  O     . HOH W 10 .    ? -9.183  57.812  84.557  1.00 32.33 ? 2069 HOH A O     1 
HETATM 18750 O  O     . HOH W 10 .    ? -62.915 54.067  65.972  1.00 31.76 ? 2070 HOH A O     1 
HETATM 18751 O  O     . HOH W 10 .    ? -2.550  74.103  119.064 1.00 31.86 ? 2071 HOH A O     1 
HETATM 18752 O  O     . HOH W 10 .    ? -20.757 75.203  102.001 1.00 29.45 ? 2072 HOH A O     1 
HETATM 18753 O  O     . HOH W 10 .    ? -52.506 73.486  103.075 1.00 27.95 ? 2073 HOH A O     1 
HETATM 18754 O  O     . HOH W 10 .    ? -32.443 75.677  85.555  1.00 26.64 ? 2074 HOH A O     1 
HETATM 18755 O  O     . HOH W 10 .    ? -4.365  80.303  125.388 1.00 31.90 ? 2075 HOH A O     1 
HETATM 18756 O  O     . HOH W 10 .    ? -47.145 81.177  90.203  1.00 31.40 ? 2076 HOH A O     1 
HETATM 18757 O  O     . HOH W 10 .    ? -1.088  61.092  112.838 1.00 32.84 ? 2077 HOH A O     1 
HETATM 18758 O  O     . HOH W 10 .    ? -37.333 82.898  77.647  1.00 35.18 ? 2078 HOH A O     1 
HETATM 18759 O  O     . HOH W 10 .    ? 22.799  70.374  116.223 1.00 26.44 ? 2079 HOH A O     1 
HETATM 18760 O  O     . HOH W 10 .    ? -29.044 78.054  70.601  1.00 32.60 ? 2080 HOH A O     1 
HETATM 18761 O  O     . HOH W 10 .    ? -16.866 93.783  106.514 1.00 28.79 ? 2081 HOH A O     1 
HETATM 18762 O  O     . HOH W 10 .    ? 6.399   62.996  95.095  1.00 27.17 ? 2082 HOH A O     1 
HETATM 18763 O  O     . HOH W 10 .    ? 3.232   69.797  88.670  1.00 29.84 ? 2083 HOH A O     1 
HETATM 18764 O  O     . HOH W 10 .    ? -33.653 58.751  114.001 1.00 35.93 ? 2084 HOH A O     1 
HETATM 18765 O  O     . HOH W 10 .    ? -9.912  62.532  94.490  1.00 30.83 ? 2085 HOH A O     1 
HETATM 18766 O  O     . HOH W 10 .    ? -1.367  80.421  77.034  1.00 38.49 ? 2086 HOH A O     1 
HETATM 18767 O  O     . HOH W 10 .    ? -24.998 52.423  100.489 1.00 28.03 ? 2087 HOH A O     1 
HETATM 18768 O  O     . HOH W 10 .    ? -19.757 57.927  107.076 1.00 29.20 ? 2088 HOH A O     1 
HETATM 18769 O  O     . HOH W 10 .    ? -19.001 74.354  106.585 1.00 22.02 ? 2089 HOH A O     1 
HETATM 18770 O  O     . HOH W 10 .    ? -8.917  77.166  129.931 1.00 35.00 ? 2090 HOH A O     1 
HETATM 18771 O  O     . HOH W 10 .    ? -29.791 60.284  89.007  1.00 21.16 ? 2091 HOH A O     1 
HETATM 18772 O  O     . HOH W 10 .    ? -2.420  92.211  98.397  1.00 31.23 ? 2092 HOH A O     1 
HETATM 18773 O  O     . HOH W 10 .    ? -29.722 93.031  109.323 1.00 29.00 ? 2093 HOH A O     1 
HETATM 18774 O  O     . HOH W 10 .    ? -30.448 60.421  86.394  1.00 30.79 ? 2094 HOH A O     1 
HETATM 18775 O  O     . HOH W 10 .    ? -21.251 53.001  101.610 1.00 34.23 ? 2095 HOH A O     1 
HETATM 18776 O  O     . HOH W 10 .    ? 6.583   60.353  94.363  1.00 31.78 ? 2096 HOH A O     1 
HETATM 18777 O  O     . HOH W 10 .    ? -57.133 76.695  76.867  1.00 30.26 ? 2097 HOH A O     1 
HETATM 18778 O  O     . HOH W 10 .    ? -3.692  83.715  112.664 1.00 29.05 ? 2098 HOH A O     1 
HETATM 18779 O  O     . HOH W 10 .    ? 12.336  62.942  93.554  1.00 31.65 ? 2099 HOH A O     1 
HETATM 18780 O  O     . HOH W 10 .    ? -63.084 55.663  70.011  1.00 28.41 ? 2100 HOH A O     1 
HETATM 18781 O  O     . HOH W 10 .    ? -64.033 57.835  96.814  1.00 36.34 ? 2101 HOH A O     1 
HETATM 18782 O  O     . HOH W 10 .    ? -52.459 47.420  97.020  1.00 27.89 ? 2102 HOH A O     1 
HETATM 18783 O  O     . HOH W 10 .    ? -61.959 70.993  85.951  1.00 31.09 ? 2103 HOH A O     1 
HETATM 18784 O  O     . HOH W 10 .    ? -24.551 50.645  95.852  1.00 29.81 ? 2104 HOH A O     1 
HETATM 18785 O  O     . HOH W 10 .    ? -23.441 52.395  97.866  1.00 35.24 ? 2105 HOH A O     1 
HETATM 18786 O  O     . HOH W 10 .    ? -2.878  85.169  96.892  1.00 30.13 ? 2106 HOH A O     1 
HETATM 18787 O  O     . HOH W 10 .    ? -57.446 52.851  99.012  1.00 29.50 ? 2107 HOH A O     1 
HETATM 18788 O  O     . HOH W 10 .    ? -55.696 53.138  100.735 1.00 32.87 ? 2108 HOH A O     1 
HETATM 18789 O  O     . HOH W 10 .    ? -67.123 47.722  73.895  1.00 30.21 ? 2109 HOH A O     1 
HETATM 18790 O  O     . HOH W 10 .    ? -46.783 39.288  104.917 1.00 32.97 ? 2110 HOH A O     1 
HETATM 18791 O  O     . HOH W 10 .    ? -62.490 53.330  94.358  1.00 38.05 ? 2111 HOH A O     1 
HETATM 18792 O  O     . HOH W 10 .    ? -25.467 63.160  100.183 1.00 28.10 ? 2112 HOH A O     1 
HETATM 18793 O  O     . HOH W 10 .    ? 11.026  64.845  93.603  1.00 34.53 ? 2113 HOH A O     1 
HETATM 18794 O  O     . HOH W 10 .    ? -0.412  57.276  67.993  1.00 29.19 ? 2114 HOH A O     1 
HETATM 18795 O  O     . HOH W 10 .    ? -33.556 57.707  111.502 1.00 35.53 ? 2115 HOH A O     1 
HETATM 18796 O  O     . HOH W 10 .    ? -37.613 34.541  90.324  1.00 34.32 ? 2116 HOH A O     1 
HETATM 18797 O  O     . HOH W 10 .    ? -56.396 79.130  77.501  1.00 32.50 ? 2117 HOH A O     1 
HETATM 18798 O  O     . HOH W 10 .    ? -37.069 32.272  91.100  1.00 39.17 ? 2118 HOH A O     1 
HETATM 18799 O  O     . HOH W 10 .    ? -48.421 37.945  103.310 1.00 38.83 ? 2119 HOH A O     1 
HETATM 18800 O  O     . HOH X 10 .    ? -11.470 27.813  81.260  1.00 26.39 ? 1401 HOH B O     1 
HETATM 18801 O  O     . HOH X 10 .    ? 4.757   22.889  123.094 1.00 32.03 ? 1402 HOH B O     1 
HETATM 18802 O  O     . HOH X 10 .    ? -0.303  18.856  80.658  1.00 24.57 ? 1403 HOH B O     1 
HETATM 18803 O  O     . HOH X 10 .    ? 3.088   21.122  137.391 1.00 37.00 ? 1404 HOH B O     1 
HETATM 18804 O  O     . HOH X 10 .    ? 6.765   51.592  57.601  1.00 29.77 ? 1405 HOH B O     1 
HETATM 18805 O  O     . HOH X 10 .    ? 11.864  70.656  60.474  1.00 31.35 ? 1406 HOH B O     1 
HETATM 18806 O  O     . HOH X 10 .    ? 5.939   32.151  79.362  1.00 21.05 ? 1407 HOH B O     1 
HETATM 18807 O  O     . HOH X 10 .    ? 22.565  35.139  115.699 1.00 29.26 ? 1408 HOH B O     1 
HETATM 18808 O  O     . HOH X 10 .    ? -2.599  29.469  57.558  1.00 31.80 ? 1409 HOH B O     1 
HETATM 18809 O  O     . HOH X 10 .    ? 9.419   26.174  55.298  1.00 22.07 ? 1410 HOH B O     1 
HETATM 18810 O  O     . HOH X 10 .    ? 33.034  18.091  90.136  1.00 36.25 ? 1411 HOH B O     1 
HETATM 18811 O  O     . HOH X 10 .    ? 17.616  12.946  117.558 1.00 24.62 ? 1412 HOH B O     1 
HETATM 18812 O  O     . HOH X 10 .    ? 15.382  62.623  84.640  1.00 33.18 ? 1413 HOH B O     1 
HETATM 18813 O  O     . HOH X 10 .    ? 18.338  38.654  115.845 1.00 31.67 ? 1414 HOH B O     1 
HETATM 18814 O  O     . HOH X 10 .    ? 30.694  26.335  53.121  1.00 32.84 ? 1415 HOH B O     1 
HETATM 18815 O  O     . HOH X 10 .    ? 15.404  21.882  88.659  1.00 33.77 ? 1416 HOH B O     1 
HETATM 18816 O  O     . HOH X 10 .    ? 28.153  13.616  86.100  1.00 26.76 ? 1417 HOH B O     1 
HETATM 18817 O  O     . HOH X 10 .    ? -7.940  -0.805  120.265 1.00 30.58 ? 1418 HOH B O     1 
HETATM 18818 O  O     . HOH X 10 .    ? 18.798  25.134  54.530  1.00 26.15 ? 1419 HOH B O     1 
HETATM 18819 O  O     . HOH X 10 .    ? 11.747  45.542  109.363 1.00 36.12 ? 1420 HOH B O     1 
HETATM 18820 O  O     . HOH X 10 .    ? -10.504 11.427  130.044 1.00 34.43 ? 1421 HOH B O     1 
HETATM 18821 O  O     . HOH X 10 .    ? 1.269   20.690  104.043 1.00 27.35 ? 1422 HOH B O     1 
HETATM 18822 O  O     . HOH X 10 .    ? -1.328  -8.831  102.413 1.00 27.74 ? 1423 HOH B O     1 
HETATM 18823 O  O     . HOH X 10 .    ? 7.965   8.037   72.975  1.00 35.23 ? 1424 HOH B O     1 
HETATM 18824 O  O     . HOH X 10 .    ? 1.372   57.621  87.943  1.00 35.14 ? 1425 HOH B O     1 
HETATM 18825 O  O     . HOH X 10 .    ? -2.772  5.110   85.226  1.00 28.67 ? 1426 HOH B O     1 
HETATM 18826 O  O     . HOH X 10 .    ? 22.898  48.876  107.359 1.00 33.44 ? 1427 HOH B O     1 
HETATM 18827 O  O     . HOH X 10 .    ? 32.968  29.995  62.060  1.00 24.15 ? 1428 HOH B O     1 
HETATM 18828 O  O     . HOH X 10 .    ? 13.722  41.732  77.107  1.00 15.63 ? 1429 HOH B O     1 
HETATM 18829 O  O     . HOH X 10 .    ? 7.833   -0.745  107.520 1.00 32.44 ? 1430 HOH B O     1 
HETATM 18830 O  O     . HOH X 10 .    ? 5.573   -5.521  117.128 1.00 36.47 ? 1431 HOH B O     1 
HETATM 18831 O  O     . HOH X 10 .    ? 29.285  42.602  84.431  1.00 26.58 ? 1432 HOH B O     1 
HETATM 18832 O  O     . HOH X 10 .    ? -25.359 10.545  87.884  1.00 33.28 ? 1433 HOH B O     1 
HETATM 18833 O  O     . HOH X 10 .    ? 29.777  27.571  56.293  1.00 21.96 ? 1434 HOH B O     1 
HETATM 18834 O  O     . HOH X 10 .    ? 13.270  34.891  79.075  1.00 26.37 ? 1435 HOH B O     1 
HETATM 18835 O  O     . HOH X 10 .    ? -12.890 20.162  84.073  1.00 22.12 ? 1436 HOH B O     1 
HETATM 18836 O  O     . HOH X 10 .    ? 18.513  13.264  95.628  1.00 25.23 ? 1437 HOH B O     1 
HETATM 18837 O  O     . HOH X 10 .    ? 4.549   49.761  68.729  1.00 23.24 ? 1438 HOH B O     1 
HETATM 18838 O  O     . HOH X 10 .    ? 39.059  27.069  87.896  1.00 31.27 ? 1439 HOH B O     1 
HETATM 18839 O  O     . HOH X 10 .    ? -6.757  12.497  125.671 1.00 29.86 ? 1440 HOH B O     1 
HETATM 18840 O  O     . HOH X 10 .    ? -5.586  40.060  72.285  1.00 22.41 ? 1441 HOH B O     1 
HETATM 18841 O  O     . HOH X 10 .    ? -7.365  8.664   111.300 1.00 26.91 ? 1442 HOH B O     1 
HETATM 18842 O  O     . HOH X 10 .    ? 15.507  55.750  92.981  1.00 26.43 ? 1443 HOH B O     1 
HETATM 18843 O  O     . HOH X 10 .    ? -6.096  37.586  77.745  1.00 25.99 ? 1444 HOH B O     1 
HETATM 18844 O  O     . HOH X 10 .    ? -13.217 9.244   124.594 1.00 33.89 ? 1445 HOH B O     1 
HETATM 18845 O  O     . HOH X 10 .    ? 15.545  53.050  57.936  1.00 31.27 ? 1446 HOH B O     1 
HETATM 18846 O  O     . HOH X 10 .    ? -1.515  38.618  80.352  1.00 21.68 ? 1447 HOH B O     1 
HETATM 18847 O  O     . HOH X 10 .    ? 9.763   50.873  90.404  1.00 25.67 ? 1448 HOH B O     1 
HETATM 18848 O  O     . HOH X 10 .    ? -15.686 47.515  114.329 1.00 32.71 ? 1449 HOH B O     1 
HETATM 18849 O  O     . HOH X 10 .    ? -9.077  45.365  109.192 1.00 32.49 ? 1450 HOH B O     1 
HETATM 18850 O  O     . HOH X 10 .    ? 14.811  39.139  77.294  1.00 16.17 ? 1451 HOH B O     1 
HETATM 18851 O  O     . HOH X 10 .    ? 23.807  19.280  98.383  1.00 30.07 ? 1452 HOH B O     1 
HETATM 18852 O  O     . HOH X 10 .    ? 28.742  69.589  80.037  1.00 20.60 ? 1453 HOH B O     1 
HETATM 18853 O  O     . HOH X 10 .    ? -4.986  27.173  70.261  1.00 27.60 ? 1454 HOH B O     1 
HETATM 18854 O  O     . HOH X 10 .    ? 14.697  56.184  74.837  1.00 24.44 ? 1455 HOH B O     1 
HETATM 18855 O  O     . HOH X 10 .    ? 10.912  18.435  64.763  1.00 24.09 ? 1456 HOH B O     1 
HETATM 18856 O  O     . HOH X 10 .    ? -6.612  51.326  73.161  1.00 15.30 ? 1457 HOH B O     1 
HETATM 18857 O  O     . HOH X 10 .    ? -21.558 15.864  82.917  1.00 31.23 ? 1458 HOH B O     1 
HETATM 18858 O  O     . HOH X 10 .    ? 8.218   36.038  103.007 1.00 27.44 ? 1459 HOH B O     1 
HETATM 18859 O  O     . HOH X 10 .    ? -12.091 18.675  126.948 1.00 31.30 ? 1460 HOH B O     1 
HETATM 18860 O  O     . HOH X 10 .    ? 14.831  40.629  73.116  1.00 17.11 ? 1461 HOH B O     1 
HETATM 18861 O  O     . HOH X 10 .    ? -1.622  14.766  86.155  1.00 21.78 ? 1462 HOH B O     1 
HETATM 18862 O  O     . HOH X 10 .    ? 0.586   -10.129 111.219 1.00 31.11 ? 1463 HOH B O     1 
HETATM 18863 O  O     . HOH X 10 .    ? 7.126   32.845  98.389  1.00 25.73 ? 1464 HOH B O     1 
HETATM 18864 O  O     . HOH X 10 .    ? 38.077  34.262  102.926 1.00 30.57 ? 1465 HOH B O     1 
HETATM 18865 O  O     . HOH X 10 .    ? 34.062  62.823  78.417  1.00 18.56 ? 1466 HOH B O     1 
HETATM 18866 O  O     . HOH X 10 .    ? 9.486   30.956  110.247 1.00 34.37 ? 1467 HOH B O     1 
HETATM 18867 O  O     . HOH X 10 .    ? 6.008   5.935   86.247  1.00 19.10 ? 1468 HOH B O     1 
HETATM 18868 O  O     . HOH X 10 .    ? 5.370   44.151  58.694  1.00 28.10 ? 1469 HOH B O     1 
HETATM 18869 O  O     . HOH X 10 .    ? 7.451   65.847  63.986  1.00 29.36 ? 1470 HOH B O     1 
HETATM 18870 O  O     . HOH X 10 .    ? 23.249  18.601  80.560  1.00 23.40 ? 1471 HOH B O     1 
HETATM 18871 O  O     . HOH X 10 .    ? 13.422  58.623  64.583  1.00 27.52 ? 1472 HOH B O     1 
HETATM 18872 O  O     . HOH X 10 .    ? 32.568  19.186  58.245  1.00 27.91 ? 1473 HOH B O     1 
HETATM 18873 O  O     . HOH X 10 .    ? 18.608  62.632  57.686  1.00 34.05 ? 1474 HOH B O     1 
HETATM 18874 O  O     . HOH X 10 .    ? 21.207  50.773  87.873  1.00 22.36 ? 1475 HOH B O     1 
HETATM 18875 O  O     . HOH X 10 .    ? -2.653  24.446  76.657  1.00 25.22 ? 1476 HOH B O     1 
HETATM 18876 O  O     . HOH X 10 .    ? 6.335   5.984   92.558  1.00 21.41 ? 1477 HOH B O     1 
HETATM 18877 O  O     . HOH X 10 .    ? 0.785   42.498  76.420  1.00 25.30 ? 1478 HOH B O     1 
HETATM 18878 O  O     . HOH X 10 .    ? -0.567  56.295  86.464  1.00 30.89 ? 1479 HOH B O     1 
HETATM 18879 O  O     . HOH X 10 .    ? 1.342   13.377  102.098 1.00 18.75 ? 1480 HOH B O     1 
HETATM 18880 O  O     . HOH X 10 .    ? 29.260  32.511  76.796  1.00 23.37 ? 1481 HOH B O     1 
HETATM 18881 O  O     . HOH X 10 .    ? -4.449  18.948  98.261  1.00 15.94 ? 1482 HOH B O     1 
HETATM 18882 O  O     . HOH X 10 .    ? -4.611  64.510  81.208  1.00 16.82 ? 1483 HOH B O     1 
HETATM 18883 O  O     . HOH X 10 .    ? 18.564  50.540  70.335  1.00 25.12 ? 1484 HOH B O     1 
HETATM 18884 O  O     . HOH X 10 .    ? -1.649  32.853  69.154  1.00 15.53 ? 1485 HOH B O     1 
HETATM 18885 O  O     . HOH X 10 .    ? 26.563  20.803  56.133  1.00 27.32 ? 1486 HOH B O     1 
HETATM 18886 O  O     . HOH X 10 .    ? 3.950   42.451  84.549  1.00 20.23 ? 1487 HOH B O     1 
HETATM 18887 O  O     . HOH X 10 .    ? -8.435  12.825  97.355  1.00 20.26 ? 1488 HOH B O     1 
HETATM 18888 O  O     . HOH X 10 .    ? 3.093   33.993  86.743  1.00 19.70 ? 1489 HOH B O     1 
HETATM 18889 O  O     . HOH X 10 .    ? 31.409  60.430  65.491  1.00 25.74 ? 1490 HOH B O     1 
HETATM 18890 O  O     . HOH X 10 .    ? 19.421  5.650   77.093  1.00 27.63 ? 1491 HOH B O     1 
HETATM 18891 O  O     . HOH X 10 .    ? -5.034  37.236  90.054  1.00 27.41 ? 1492 HOH B O     1 
HETATM 18892 O  O     . HOH X 10 .    ? -10.595 31.901  80.311  1.00 28.43 ? 1493 HOH B O     1 
HETATM 18893 O  O     . HOH X 10 .    ? 19.421  51.343  77.634  1.00 19.61 ? 1494 HOH B O     1 
HETATM 18894 O  O     . HOH X 10 .    ? 3.092   -4.485  98.457  1.00 37.46 ? 1495 HOH B O     1 
HETATM 18895 O  O     . HOH X 10 .    ? 5.705   25.757  86.401  1.00 29.84 ? 1496 HOH B O     1 
HETATM 18896 O  O     . HOH X 10 .    ? -5.487  51.958  75.636  1.00 18.77 ? 1497 HOH B O     1 
HETATM 18897 O  O     . HOH X 10 .    ? -6.283  -7.192  115.929 1.00 36.39 ? 1498 HOH B O     1 
HETATM 18898 O  O     . HOH X 10 .    ? 33.614  12.573  75.027  1.00 32.57 ? 1499 HOH B O     1 
HETATM 18899 O  O     . HOH X 10 .    ? 2.895   18.602  89.263  1.00 27.27 ? 1500 HOH B O     1 
HETATM 18900 O  O     . HOH X 10 .    ? 15.169  53.928  81.889  1.00 21.96 ? 1501 HOH B O     1 
HETATM 18901 O  O     . HOH X 10 .    ? 31.105  29.160  77.759  1.00 28.59 ? 1502 HOH B O     1 
HETATM 18902 O  O     . HOH X 10 .    ? -3.823  10.812  84.631  1.00 23.82 ? 1503 HOH B O     1 
HETATM 18903 O  O     . HOH X 10 .    ? -10.491 32.707  89.116  1.00 23.76 ? 1504 HOH B O     1 
HETATM 18904 O  O     . HOH X 10 .    ? 27.697  67.930  68.462  1.00 28.15 ? 1505 HOH B O     1 
HETATM 18905 O  O     . HOH X 10 .    ? 18.721  45.537  53.998  1.00 27.55 ? 1506 HOH B O     1 
HETATM 18906 O  O     . HOH X 10 .    ? 4.972   36.316  49.103  1.00 29.56 ? 1507 HOH B O     1 
HETATM 18907 O  O     . HOH X 10 .    ? 25.612  55.560  77.661  1.00 22.77 ? 1508 HOH B O     1 
HETATM 18908 O  O     . HOH X 10 .    ? 19.214  55.101  93.802  1.00 21.75 ? 1509 HOH B O     1 
HETATM 18909 O  O     . HOH X 10 .    ? -2.648  39.779  87.347  1.00 17.75 ? 1510 HOH B O     1 
HETATM 18910 O  O     . HOH X 10 .    ? 18.008  23.643  85.338  1.00 22.65 ? 1511 HOH B O     1 
HETATM 18911 O  O     . HOH X 10 .    ? 10.946  49.430  76.808  1.00 27.21 ? 1512 HOH B O     1 
HETATM 18912 O  O     . HOH X 10 .    ? 12.763  56.194  65.792  1.00 25.65 ? 1513 HOH B O     1 
HETATM 18913 O  O     . HOH X 10 .    ? 22.231  12.384  71.582  1.00 24.80 ? 1514 HOH B O     1 
HETATM 18914 O  O     . HOH X 10 .    ? 22.094  45.829  90.832  1.00 15.87 ? 1515 HOH B O     1 
HETATM 18915 O  O     . HOH X 10 .    ? 14.736  21.105  92.796  1.00 28.09 ? 1516 HOH B O     1 
HETATM 18916 O  O     . HOH X 10 .    ? 10.322  24.790  103.849 1.00 30.44 ? 1517 HOH B O     1 
HETATM 18917 O  O     . HOH X 10 .    ? 8.871   4.126   81.030  1.00 24.01 ? 1518 HOH B O     1 
HETATM 18918 O  O     . HOH X 10 .    ? 15.006  4.181   98.672  1.00 28.94 ? 1519 HOH B O     1 
HETATM 18919 O  O     . HOH X 10 .    ? -4.864  60.216  125.893 1.00 30.38 ? 1520 HOH B O     1 
HETATM 18920 O  O     . HOH X 10 .    ? 15.086  17.028  88.153  1.00 20.61 ? 1521 HOH B O     1 
HETATM 18921 O  O     . HOH X 10 .    ? 2.303   53.904  69.688  1.00 29.56 ? 1522 HOH B O     1 
HETATM 18922 O  O     . HOH X 10 .    ? 9.953   51.058  64.799  1.00 21.81 ? 1523 HOH B O     1 
HETATM 18923 O  O     . HOH X 10 .    ? 13.255  10.639  91.558  1.00 22.67 ? 1524 HOH B O     1 
HETATM 18924 O  O     . HOH X 10 .    ? 12.900  51.394  86.649  1.00 26.12 ? 1525 HOH B O     1 
HETATM 18925 O  O     . HOH X 10 .    ? 2.339   44.272  70.532  1.00 15.96 ? 1526 HOH B O     1 
HETATM 18926 O  O     . HOH X 10 .    ? 10.189  51.788  75.552  1.00 23.14 ? 1527 HOH B O     1 
HETATM 18927 O  O     . HOH X 10 .    ? -3.311  -2.130  94.826  1.00 26.08 ? 1528 HOH B O     1 
HETATM 18928 O  O     . HOH X 10 .    ? -2.497  49.154  63.748  1.00 19.37 ? 1529 HOH B O     1 
HETATM 18929 O  O     . HOH X 10 .    ? 18.952  79.569  68.718  1.00 30.29 ? 1530 HOH B O     1 
HETATM 18930 O  O     . HOH X 10 .    ? 2.104   41.880  54.194  1.00 27.60 ? 1531 HOH B O     1 
HETATM 18931 O  O     . HOH X 10 .    ? 18.768  31.685  73.452  1.00 20.61 ? 1532 HOH B O     1 
HETATM 18932 O  O     . HOH X 10 .    ? -5.188  30.987  77.447  1.00 18.90 ? 1533 HOH B O     1 
HETATM 18933 O  O     . HOH X 10 .    ? 17.764  23.926  110.820 1.00 23.98 ? 1534 HOH B O     1 
HETATM 18934 O  O     . HOH X 10 .    ? 10.723  46.717  107.057 1.00 28.58 ? 1535 HOH B O     1 
HETATM 18935 O  O     . HOH X 10 .    ? 29.944  50.372  71.674  1.00 28.35 ? 1536 HOH B O     1 
HETATM 18936 O  O     . HOH X 10 .    ? -6.037  5.487   122.468 1.00 25.04 ? 1537 HOH B O     1 
HETATM 18937 O  O     . HOH X 10 .    ? 10.835  6.072   122.089 1.00 28.35 ? 1538 HOH B O     1 
HETATM 18938 O  O     . HOH X 10 .    ? -5.850  55.381  78.833  1.00 24.23 ? 1539 HOH B O     1 
HETATM 18939 O  O     . HOH X 10 .    ? 3.851   -8.554  104.541 1.00 33.16 ? 1540 HOH B O     1 
HETATM 18940 O  O     . HOH X 10 .    ? 1.388   13.809  104.938 1.00 19.39 ? 1541 HOH B O     1 
HETATM 18941 O  O     . HOH X 10 .    ? 10.956  19.442  61.661  1.00 25.22 ? 1542 HOH B O     1 
HETATM 18942 O  O     . HOH X 10 .    ? -6.742  0.533   86.484  1.00 26.79 ? 1543 HOH B O     1 
HETATM 18943 O  O     . HOH X 10 .    ? 0.710   39.034  108.594 1.00 30.97 ? 1544 HOH B O     1 
HETATM 18944 O  O     . HOH X 10 .    ? -5.100  -1.747  97.190  1.00 24.17 ? 1545 HOH B O     1 
HETATM 18945 O  O     . HOH X 10 .    ? -10.907 46.711  74.589  1.00 19.48 ? 1546 HOH B O     1 
HETATM 18946 O  O     . HOH X 10 .    ? -1.360  22.528  71.550  1.00 28.28 ? 1547 HOH B O     1 
HETATM 18947 O  O     . HOH X 10 .    ? 11.444  37.593  72.451  1.00 14.07 ? 1548 HOH B O     1 
HETATM 18948 O  O     . HOH X 10 .    ? 7.952   13.954  71.810  1.00 22.39 ? 1549 HOH B O     1 
HETATM 18949 O  O     . HOH X 10 .    ? 22.651  48.886  78.253  1.00 18.77 ? 1550 HOH B O     1 
HETATM 18950 O  O     . HOH X 10 .    ? -8.627  -8.642  106.040 1.00 24.70 ? 1551 HOH B O     1 
HETATM 18951 O  O     . HOH X 10 .    ? 3.749   55.801  72.749  1.00 25.70 ? 1552 HOH B O     1 
HETATM 18952 O  O     . HOH X 10 .    ? -2.505  42.059  61.750  1.00 24.18 ? 1553 HOH B O     1 
HETATM 18953 O  O     . HOH X 10 .    ? -10.667 -2.399  116.108 1.00 36.91 ? 1554 HOH B O     1 
HETATM 18954 O  O     . HOH X 10 .    ? -0.684  27.293  68.643  1.00 17.44 ? 1555 HOH B O     1 
HETATM 18955 O  O     . HOH X 10 .    ? 17.873  52.941  66.789  1.00 22.27 ? 1556 HOH B O     1 
HETATM 18956 O  O     . HOH X 10 .    ? -8.139  24.557  116.433 1.00 34.05 ? 1557 HOH B O     1 
HETATM 18957 O  O     . HOH X 10 .    ? 31.366  54.202  68.036  1.00 26.36 ? 1558 HOH B O     1 
HETATM 18958 O  O     . HOH X 10 .    ? -2.978  60.318  120.367 1.00 27.91 ? 1559 HOH B O     1 
HETATM 18959 O  O     . HOH X 10 .    ? -11.222 20.484  122.982 1.00 32.71 ? 1560 HOH B O     1 
HETATM 18960 O  O     . HOH X 10 .    ? -9.026  24.364  77.142  1.00 33.04 ? 1561 HOH B O     1 
HETATM 18961 O  O     . HOH X 10 .    ? 28.767  23.038  76.736  1.00 20.44 ? 1562 HOH B O     1 
HETATM 18962 O  O     . HOH X 10 .    ? 7.248   49.423  106.913 1.00 21.13 ? 1563 HOH B O     1 
HETATM 18963 O  O     . HOH X 10 .    ? 14.046  25.834  110.541 1.00 32.56 ? 1564 HOH B O     1 
HETATM 18964 O  O     . HOH X 10 .    ? 23.733  26.287  50.841  1.00 27.83 ? 1565 HOH B O     1 
HETATM 18965 O  O     . HOH X 10 .    ? 30.944  21.661  80.116  1.00 18.77 ? 1566 HOH B O     1 
HETATM 18966 O  O     . HOH X 10 .    ? 21.605  53.572  67.381  1.00 25.72 ? 1567 HOH B O     1 
HETATM 18967 O  O     . HOH X 10 .    ? 7.015   38.080  103.017 1.00 25.58 ? 1568 HOH B O     1 
HETATM 18968 O  O     . HOH X 10 .    ? -6.948  52.690  107.369 1.00 25.61 ? 1569 HOH B O     1 
HETATM 18969 O  O     . HOH X 10 .    ? 31.587  38.778  84.384  1.00 26.87 ? 1570 HOH B O     1 
HETATM 18970 O  O     . HOH X 10 .    ? 17.429  27.782  83.072  1.00 22.10 ? 1571 HOH B O     1 
HETATM 18971 O  O     . HOH X 10 .    ? 13.867  72.651  61.147  1.00 27.92 ? 1572 HOH B O     1 
HETATM 18972 O  O     . HOH X 10 .    ? -2.794  45.597  102.892 1.00 28.93 ? 1573 HOH B O     1 
HETATM 18973 O  O     . HOH X 10 .    ? -1.320  55.789  72.540  1.00 26.15 ? 1574 HOH B O     1 
HETATM 18974 O  O     . HOH X 10 .    ? 19.772  43.813  88.077  1.00 13.95 ? 1575 HOH B O     1 
HETATM 18975 O  O     . HOH X 10 .    ? 26.504  22.277  75.503  1.00 20.98 ? 1576 HOH B O     1 
HETATM 18976 O  O     . HOH X 10 .    ? 29.364  60.677  58.996  1.00 30.60 ? 1577 HOH B O     1 
HETATM 18977 O  O     . HOH X 10 .    ? 5.513   15.389  94.898  1.00 17.23 ? 1578 HOH B O     1 
HETATM 18978 O  O     . HOH X 10 .    ? 32.738  46.405  67.691  1.00 31.61 ? 1579 HOH B O     1 
HETATM 18979 O  O     . HOH X 10 .    ? 22.653  23.984  84.943  1.00 18.54 ? 1580 HOH B O     1 
HETATM 18980 O  O     . HOH X 10 .    ? -8.059  30.231  76.055  1.00 23.17 ? 1581 HOH B O     1 
HETATM 18981 O  O     . HOH X 10 .    ? 18.316  13.661  74.596  1.00 24.69 ? 1582 HOH B O     1 
HETATM 18982 O  O     . HOH X 10 .    ? 7.314   45.214  75.282  1.00 14.21 ? 1583 HOH B O     1 
HETATM 18983 O  O     . HOH X 10 .    ? 0.186   20.390  69.960  1.00 23.81 ? 1584 HOH B O     1 
HETATM 18984 O  O     . HOH X 10 .    ? 11.057  41.613  54.589  1.00 20.42 ? 1585 HOH B O     1 
HETATM 18985 O  O     . HOH X 10 .    ? 7.564   57.025  87.611  1.00 31.36 ? 1586 HOH B O     1 
HETATM 18986 O  O     . HOH X 10 .    ? 14.058  33.836  84.202  1.00 21.89 ? 1587 HOH B O     1 
HETATM 18987 O  O     . HOH X 10 .    ? 25.832  47.796  100.267 1.00 28.16 ? 1588 HOH B O     1 
HETATM 18988 O  O     . HOH X 10 .    ? 2.862   41.289  117.656 1.00 32.75 ? 1589 HOH B O     1 
HETATM 18989 O  O     . HOH X 10 .    ? 11.818  11.323  71.748  1.00 25.09 ? 1590 HOH B O     1 
HETATM 18990 O  O     . HOH X 10 .    ? -8.485  2.636   92.668  1.00 22.18 ? 1591 HOH B O     1 
HETATM 18991 O  O     . HOH X 10 .    ? 1.823   40.755  114.857 1.00 30.31 ? 1592 HOH B O     1 
HETATM 18992 O  O     . HOH X 10 .    ? 21.381  30.432  71.692  1.00 15.82 ? 1593 HOH B O     1 
HETATM 18993 O  O     . HOH X 10 .    ? 11.707  12.082  121.650 1.00 25.87 ? 1594 HOH B O     1 
HETATM 18994 O  O     . HOH X 10 .    ? -4.993  2.258   124.328 1.00 29.43 ? 1595 HOH B O     1 
HETATM 18995 O  O     . HOH X 10 .    ? 21.892  24.774  108.761 1.00 27.26 ? 1596 HOH B O     1 
HETATM 18996 O  O     . HOH X 10 .    ? 25.068  13.974  65.437  1.00 27.99 ? 1597 HOH B O     1 
HETATM 18997 O  O     . HOH X 10 .    ? 25.145  55.214  62.261  1.00 23.52 ? 1598 HOH B O     1 
HETATM 18998 O  O     . HOH X 10 .    ? -11.469 2.038   121.958 1.00 27.67 ? 1599 HOH B O     1 
HETATM 18999 O  O     . HOH X 10 .    ? -0.207  12.560  93.948  1.00 15.91 ? 1600 HOH B O     1 
HETATM 19000 O  O     . HOH X 10 .    ? 16.839  43.106  79.524  1.00 14.89 ? 1601 HOH B O     1 
HETATM 19001 O  O     . HOH X 10 .    ? 3.280   8.138   92.534  1.00 20.68 ? 1602 HOH B O     1 
HETATM 19002 O  O     . HOH X 10 .    ? 6.466   -8.088  107.824 1.00 32.42 ? 1603 HOH B O     1 
HETATM 19003 O  O     . HOH X 10 .    ? 33.621  48.051  97.928  1.00 36.55 ? 1604 HOH B O     1 
HETATM 19004 O  O     . HOH X 10 .    ? 4.610   63.272  84.391  1.00 20.13 ? 1605 HOH B O     1 
HETATM 19005 O  O     . HOH X 10 .    ? 19.561  19.741  105.920 1.00 17.93 ? 1606 HOH B O     1 
HETATM 19006 O  O     . HOH X 10 .    ? -7.105  11.535  128.094 1.00 32.61 ? 1607 HOH B O     1 
HETATM 19007 O  O     . HOH X 10 .    ? -2.271  2.772   126.099 1.00 28.39 ? 1608 HOH B O     1 
HETATM 19008 O  O     . HOH X 10 .    ? 2.266   39.547  99.048  1.00 21.58 ? 1609 HOH B O     1 
HETATM 19009 O  O     . HOH X 10 .    ? 16.957  41.282  71.663  1.00 17.10 ? 1610 HOH B O     1 
HETATM 19010 O  O     . HOH X 10 .    ? -3.093  55.158  83.886  1.00 29.56 ? 1611 HOH B O     1 
HETATM 19011 O  O     . HOH X 10 .    ? 16.660  53.316  64.221  1.00 25.22 ? 1612 HOH B O     1 
HETATM 19012 O  O     . HOH X 10 .    ? 16.529  14.618  109.691 1.00 25.55 ? 1613 HOH B O     1 
HETATM 19013 O  O     . HOH X 10 .    ? 6.349   16.613  121.838 1.00 26.31 ? 1614 HOH B O     1 
HETATM 19014 O  O     . HOH X 10 .    ? 22.582  67.750  64.688  1.00 22.03 ? 1615 HOH B O     1 
HETATM 19015 O  O     . HOH X 10 .    ? 23.153  52.242  62.562  1.00 21.91 ? 1616 HOH B O     1 
HETATM 19016 O  O     . HOH X 10 .    ? 0.733   29.071  83.134  1.00 16.55 ? 1617 HOH B O     1 
HETATM 19017 O  O     . HOH X 10 .    ? -15.247 6.563   117.822 1.00 29.27 ? 1618 HOH B O     1 
HETATM 19018 O  O     . HOH X 10 .    ? 16.946  55.339  97.456  1.00 25.20 ? 1619 HOH B O     1 
HETATM 19019 O  O     . HOH X 10 .    ? 15.277  10.287  89.726  1.00 20.85 ? 1620 HOH B O     1 
HETATM 19020 O  O     . HOH X 10 .    ? 10.690  20.384  121.071 1.00 30.25 ? 1621 HOH B O     1 
HETATM 19021 O  O     . HOH X 10 .    ? -0.652  73.644  77.957  1.00 26.83 ? 1622 HOH B O     1 
HETATM 19022 O  O     . HOH X 10 .    ? -17.268 5.285   116.885 1.00 31.77 ? 1623 HOH B O     1 
HETATM 19023 O  O     . HOH X 10 .    ? 9.579   2.586   117.593 1.00 26.60 ? 1624 HOH B O     1 
HETATM 19024 O  O     . HOH X 10 .    ? -3.630  -10.935 101.038 1.00 25.25 ? 1625 HOH B O     1 
HETATM 19025 O  O     . HOH X 10 .    ? 12.181  2.510   92.333  1.00 34.45 ? 1626 HOH B O     1 
HETATM 19026 O  O     . HOH X 10 .    ? 11.635  49.966  88.670  1.00 18.69 ? 1627 HOH B O     1 
HETATM 19027 O  O     . HOH X 10 .    ? 19.617  33.306  67.593  1.00 15.21 ? 1628 HOH B O     1 
HETATM 19028 O  O     . HOH X 10 .    ? -10.076 6.164   87.296  1.00 28.02 ? 1629 HOH B O     1 
HETATM 19029 O  O     . HOH X 10 .    ? 22.817  73.189  65.057  1.00 31.60 ? 1630 HOH B O     1 
HETATM 19030 O  O     . HOH X 10 .    ? -6.193  39.489  107.147 1.00 34.29 ? 1631 HOH B O     1 
HETATM 19031 O  O     . HOH X 10 .    ? 32.968  58.258  74.216  1.00 27.52 ? 1632 HOH B O     1 
HETATM 19032 O  O     . HOH X 10 .    ? -4.778  -0.131  110.882 1.00 24.00 ? 1633 HOH B O     1 
HETATM 19033 O  O     . HOH X 10 .    ? 8.163   15.121  90.660  1.00 22.89 ? 1634 HOH B O     1 
HETATM 19034 O  O     . HOH X 10 .    ? -3.007  63.178  85.646  1.00 24.33 ? 1635 HOH B O     1 
HETATM 19035 O  O     . HOH X 10 .    ? 2.381   30.934  80.208  1.00 18.01 ? 1636 HOH B O     1 
HETATM 19036 O  O     . HOH X 10 .    ? 0.832   -0.716  92.990  1.00 27.64 ? 1637 HOH B O     1 
HETATM 19037 O  O     . HOH X 10 .    ? -0.786  24.209  74.326  1.00 18.51 ? 1638 HOH B O     1 
HETATM 19038 O  O     . HOH X 10 .    ? 10.597  53.213  104.958 1.00 28.81 ? 1639 HOH B O     1 
HETATM 19039 O  O     . HOH X 10 .    ? 6.586   8.247   75.157  1.00 27.28 ? 1640 HOH B O     1 
HETATM 19040 O  O     . HOH X 10 .    ? 23.922  69.218  67.491  1.00 21.84 ? 1641 HOH B O     1 
HETATM 19041 O  O     . HOH X 10 .    ? 27.529  32.103  74.142  1.00 19.15 ? 1642 HOH B O     1 
HETATM 19042 O  O     . HOH X 10 .    ? 18.000  44.059  91.726  1.00 13.85 ? 1643 HOH B O     1 
HETATM 19043 O  O     . HOH X 10 .    ? 31.465  59.672  72.265  1.00 22.68 ? 1644 HOH B O     1 
HETATM 19044 O  O     . HOH X 10 .    ? 19.947  24.617  46.322  1.00 22.23 ? 1645 HOH B O     1 
HETATM 19045 O  O     . HOH X 10 .    ? 11.929  21.707  101.834 1.00 27.31 ? 1646 HOH B O     1 
HETATM 19046 O  O     . HOH X 10 .    ? 15.482  26.943  81.229  1.00 24.31 ? 1647 HOH B O     1 
HETATM 19047 O  O     . HOH X 10 .    ? 15.758  48.839  70.889  1.00 14.65 ? 1648 HOH B O     1 
HETATM 19048 O  O     . HOH X 10 .    ? -0.397  4.377   88.730  1.00 22.44 ? 1649 HOH B O     1 
HETATM 19049 O  O     . HOH X 10 .    ? -5.831  12.874  84.644  1.00 25.28 ? 1650 HOH B O     1 
HETATM 19050 O  O     . HOH X 10 .    ? 12.144  2.146   111.626 1.00 25.57 ? 1651 HOH B O     1 
HETATM 19051 O  O     . HOH X 10 .    ? 26.716  49.268  94.755  1.00 26.67 ? 1652 HOH B O     1 
HETATM 19052 O  O     . HOH X 10 .    ? 30.088  35.531  50.889  1.00 30.13 ? 1653 HOH B O     1 
HETATM 19053 O  O     . HOH X 10 .    ? 17.072  49.340  59.139  1.00 21.80 ? 1654 HOH B O     1 
HETATM 19054 O  O     . HOH X 10 .    ? 2.426   33.237  78.571  1.00 15.29 ? 1655 HOH B O     1 
HETATM 19055 O  O     . HOH X 10 .    ? -9.161  24.345  100.945 1.00 21.95 ? 1656 HOH B O     1 
HETATM 19056 O  O     . HOH X 10 .    ? 20.994  5.558   68.286  1.00 34.35 ? 1657 HOH B O     1 
HETATM 19057 O  O     . HOH X 10 .    ? 18.195  67.152  58.517  1.00 26.94 ? 1658 HOH B O     1 
HETATM 19058 O  O     . HOH X 10 .    ? -9.713  10.263  123.313 1.00 26.51 ? 1659 HOH B O     1 
HETATM 19059 O  O     . HOH X 10 .    ? 1.258   6.337   92.011  1.00 19.03 ? 1660 HOH B O     1 
HETATM 19060 O  O     . HOH X 10 .    ? -4.916  10.989  100.629 1.00 17.97 ? 1661 HOH B O     1 
HETATM 19061 O  O     . HOH X 10 .    ? 22.519  37.587  86.250  1.00 15.54 ? 1662 HOH B O     1 
HETATM 19062 O  O     . HOH X 10 .    ? 3.358   33.900  93.034  1.00 20.33 ? 1663 HOH B O     1 
HETATM 19063 O  O     . HOH X 10 .    ? 26.538  66.169  57.795  1.00 32.65 ? 1664 HOH B O     1 
HETATM 19064 O  O     . HOH X 10 .    ? 20.497  27.853  71.462  1.00 14.98 ? 1665 HOH B O     1 
HETATM 19065 O  O     . HOH X 10 .    ? 9.690   71.566  61.769  1.00 27.29 ? 1666 HOH B O     1 
HETATM 19066 O  O     . HOH X 10 .    ? 19.519  19.432  66.528  1.00 15.67 ? 1667 HOH B O     1 
HETATM 19067 O  O     . HOH X 10 .    ? 2.373   6.184   80.460  1.00 27.62 ? 1668 HOH B O     1 
HETATM 19068 O  O     . HOH X 10 .    ? -2.237  11.408  101.571 1.00 17.08 ? 1669 HOH B O     1 
HETATM 19069 O  O     . HOH X 10 .    ? 12.533  50.343  64.999  1.00 22.13 ? 1670 HOH B O     1 
HETATM 19070 O  O     . HOH X 10 .    ? 6.765   42.925  49.677  1.00 26.60 ? 1671 HOH B O     1 
HETATM 19071 O  O     . HOH X 10 .    ? 29.840  20.556  77.070  1.00 25.68 ? 1672 HOH B O     1 
HETATM 19072 O  O     . HOH X 10 .    ? -13.963 12.063  91.424  1.00 20.30 ? 1673 HOH B O     1 
HETATM 19073 O  O     . HOH X 10 .    ? -6.580  12.973  99.432  1.00 18.63 ? 1674 HOH B O     1 
HETATM 19074 O  O     . HOH X 10 .    ? -11.661 20.607  88.252  1.00 22.95 ? 1675 HOH B O     1 
HETATM 19075 O  O     . HOH X 10 .    ? 4.561   30.866  54.747  1.00 30.40 ? 1676 HOH B O     1 
HETATM 19076 O  O     . HOH X 10 .    ? 0.654   31.099  74.889  1.00 17.53 ? 1677 HOH B O     1 
HETATM 19077 O  O     . HOH X 10 .    ? 33.227  26.639  59.339  1.00 25.16 ? 1678 HOH B O     1 
HETATM 19078 O  O     . HOH X 10 .    ? 14.357  22.709  102.056 1.00 23.81 ? 1679 HOH B O     1 
HETATM 19079 O  O     . HOH X 10 .    ? -3.151  31.276  63.593  1.00 23.34 ? 1680 HOH B O     1 
HETATM 19080 O  O     . HOH X 10 .    ? 15.082  54.294  66.634  1.00 26.17 ? 1681 HOH B O     1 
HETATM 19081 O  O     . HOH X 10 .    ? 24.625  16.549  95.300  1.00 23.67 ? 1682 HOH B O     1 
HETATM 19082 O  O     . HOH X 10 .    ? 39.489  29.922  88.079  1.00 23.14 ? 1683 HOH B O     1 
HETATM 19083 O  O     . HOH X 10 .    ? -0.463  -7.104  107.366 1.00 29.81 ? 1684 HOH B O     1 
HETATM 19084 O  O     . HOH X 10 .    ? 5.259   7.381   94.470  1.00 19.06 ? 1685 HOH B O     1 
HETATM 19085 O  O     . HOH X 10 .    ? 16.895  34.458  56.118  1.00 16.63 ? 1686 HOH B O     1 
HETATM 19086 O  O     . HOH X 10 .    ? 19.907  51.005  67.219  1.00 23.80 ? 1687 HOH B O     1 
HETATM 19087 O  O     . HOH X 10 .    ? 5.352   55.991  104.974 1.00 22.35 ? 1688 HOH B O     1 
HETATM 19088 O  O     . HOH X 10 .    ? -2.899  21.665  91.744  1.00 15.65 ? 1689 HOH B O     1 
HETATM 19089 O  O     . HOH X 10 .    ? -1.519  60.826  77.624  1.00 23.02 ? 1690 HOH B O     1 
HETATM 19090 O  O     . HOH X 10 .    ? 23.284  52.933  70.712  1.00 28.80 ? 1691 HOH B O     1 
HETATM 19091 O  O     . HOH X 10 .    ? -7.037  14.515  91.687  1.00 17.92 ? 1692 HOH B O     1 
HETATM 19092 O  O     . HOH X 10 .    ? 23.263  33.315  91.794  1.00 17.50 ? 1693 HOH B O     1 
HETATM 19093 O  O     . HOH X 10 .    ? 1.433   20.824  89.704  1.00 20.65 ? 1694 HOH B O     1 
HETATM 19094 O  O     . HOH X 10 .    ? 26.843  35.720  91.197  1.00 17.13 ? 1695 HOH B O     1 
HETATM 19095 O  O     . HOH X 10 .    ? 0.056   27.143  94.942  1.00 22.83 ? 1696 HOH B O     1 
HETATM 19096 O  O     . HOH X 10 .    ? 2.372   11.892  94.627  1.00 17.66 ? 1697 HOH B O     1 
HETATM 19097 O  O     . HOH X 10 .    ? -1.410  67.119  84.194  1.00 27.04 ? 1698 HOH B O     1 
HETATM 19098 O  O     . HOH X 10 .    ? -2.505  18.582  105.978 1.00 23.24 ? 1699 HOH B O     1 
HETATM 19099 O  O     . HOH X 10 .    ? 1.075   15.160  116.426 1.00 26.43 ? 1700 HOH B O     1 
HETATM 19100 O  O     . HOH X 10 .    ? -6.073  35.660  87.809  1.00 26.86 ? 1701 HOH B O     1 
HETATM 19101 O  O     . HOH X 10 .    ? 27.856  29.931  83.346  1.00 15.99 ? 1702 HOH B O     1 
HETATM 19102 O  O     . HOH X 10 .    ? 3.573   10.750  92.520  1.00 17.87 ? 1703 HOH B O     1 
HETATM 19103 O  O     . HOH X 10 .    ? 6.329   33.952  86.909  1.00 18.32 ? 1704 HOH B O     1 
HETATM 19104 O  O     . HOH X 10 .    ? 1.166   15.370  82.482  1.00 20.75 ? 1705 HOH B O     1 
HETATM 19105 O  O     . HOH X 10 .    ? 29.194  32.794  103.615 1.00 25.80 ? 1706 HOH B O     1 
HETATM 19106 O  O     . HOH X 10 .    ? 12.139  13.050  110.740 1.00 22.66 ? 1707 HOH B O     1 
HETATM 19107 O  O     . HOH X 10 .    ? -7.055  6.620   118.924 1.00 22.98 ? 1708 HOH B O     1 
HETATM 19108 O  O     . HOH X 10 .    ? 0.639   55.871  110.861 1.00 23.97 ? 1709 HOH B O     1 
HETATM 19109 O  O     . HOH X 10 .    ? 4.079   19.454  97.586  1.00 30.85 ? 1710 HOH B O     1 
HETATM 19110 O  O     . HOH X 10 .    ? 34.738  65.095  81.539  1.00 19.98 ? 1711 HOH B O     1 
HETATM 19111 O  O     . HOH X 10 .    ? 17.122  28.864  111.146 1.00 25.95 ? 1712 HOH B O     1 
HETATM 19112 O  O     . HOH X 10 .    ? 20.122  52.808  69.479  1.00 19.98 ? 1713 HOH B O     1 
HETATM 19113 O  O     . HOH X 10 .    ? 16.838  34.245  48.682  1.00 29.18 ? 1714 HOH B O     1 
HETATM 19114 O  O     . HOH X 10 .    ? 5.920   50.309  88.541  1.00 31.51 ? 1715 HOH B O     1 
HETATM 19115 O  O     . HOH X 10 .    ? 4.253   77.981  80.470  1.00 30.84 ? 1716 HOH B O     1 
HETATM 19116 O  O     . HOH X 10 .    ? -0.532  40.401  77.877  1.00 22.36 ? 1717 HOH B O     1 
HETATM 19117 O  O     . HOH X 10 .    ? 18.823  6.035   74.540  1.00 28.55 ? 1718 HOH B O     1 
HETATM 19118 O  O     . HOH X 10 .    ? 18.822  8.489   84.251  1.00 24.49 ? 1719 HOH B O     1 
HETATM 19119 O  O     . HOH X 10 .    ? -0.051  48.011  76.630  1.00 18.67 ? 1720 HOH B O     1 
HETATM 19120 O  O     . HOH X 10 .    ? 31.128  52.879  65.752  1.00 28.40 ? 1721 HOH B O     1 
HETATM 19121 O  O     . HOH X 10 .    ? 33.682  38.063  62.247  1.00 23.55 ? 1722 HOH B O     1 
HETATM 19122 O  O     . HOH X 10 .    ? 15.690  16.312  85.504  1.00 19.94 ? 1723 HOH B O     1 
HETATM 19123 O  O     . HOH X 10 .    ? -1.547  67.488  75.581  1.00 29.96 ? 1724 HOH B O     1 
HETATM 19124 O  O     . HOH X 10 .    ? 26.930  42.799  105.081 1.00 28.85 ? 1725 HOH B O     1 
HETATM 19125 O  O     . HOH X 10 .    ? 6.055   -3.998  104.729 1.00 30.34 ? 1726 HOH B O     1 
HETATM 19126 O  O     . HOH X 10 .    ? -13.938 12.857  94.089  1.00 20.80 ? 1727 HOH B O     1 
HETATM 19127 O  O     . HOH X 10 .    ? -6.982  35.543  69.336  1.00 32.12 ? 1728 HOH B O     1 
HETATM 19128 O  O     . HOH X 10 .    ? 14.665  7.121   69.083  1.00 29.84 ? 1729 HOH B O     1 
HETATM 19129 O  O     . HOH X 10 .    ? 8.150   40.952  86.976  1.00 16.19 ? 1730 HOH B O     1 
HETATM 19130 O  O     . HOH X 10 .    ? -13.903 18.778  105.948 1.00 27.99 ? 1731 HOH B O     1 
HETATM 19131 O  O     . HOH X 10 .    ? 17.821  23.561  88.322  1.00 30.02 ? 1732 HOH B O     1 
HETATM 19132 O  O     . HOH X 10 .    ? 14.287  45.979  78.487  1.00 16.09 ? 1733 HOH B O     1 
HETATM 19133 O  O     . HOH X 10 .    ? 0.911   9.668   89.813  1.00 21.39 ? 1734 HOH B O     1 
HETATM 19134 O  O     . HOH X 10 .    ? 15.401  38.480  74.768  1.00 15.51 ? 1735 HOH B O     1 
HETATM 19135 O  O     . HOH X 10 .    ? 9.065   19.340  104.067 1.00 24.83 ? 1736 HOH B O     1 
HETATM 19136 O  O     . HOH X 10 .    ? 27.732  10.931  85.015  1.00 30.51 ? 1737 HOH B O     1 
HETATM 19137 O  O     . HOH X 10 .    ? 20.209  22.876  86.602  1.00 29.30 ? 1738 HOH B O     1 
HETATM 19138 O  O     . HOH X 10 .    ? 23.058  12.723  68.250  1.00 24.97 ? 1739 HOH B O     1 
HETATM 19139 O  O     . HOH X 10 .    ? 4.441   46.923  69.360  1.00 16.07 ? 1740 HOH B O     1 
HETATM 19140 O  O     . HOH X 10 .    ? 23.417  22.889  107.077 1.00 35.80 ? 1741 HOH B O     1 
HETATM 19141 O  O     . HOH X 10 .    ? 26.732  52.927  75.470  1.00 27.79 ? 1742 HOH B O     1 
HETATM 19142 O  O     . HOH X 10 .    ? 20.730  37.771  112.792 1.00 23.15 ? 1743 HOH B O     1 
HETATM 19143 O  O     . HOH X 10 .    ? 32.769  45.576  75.161  1.00 24.82 ? 1744 HOH B O     1 
HETATM 19144 O  O     . HOH X 10 .    ? 32.325  29.454  64.839  1.00 22.21 ? 1745 HOH B O     1 
HETATM 19145 O  O     . HOH X 10 .    ? 32.769  25.843  102.220 1.00 28.79 ? 1746 HOH B O     1 
HETATM 19146 O  O     . HOH X 10 .    ? 27.078  38.303  90.127  1.00 18.69 ? 1747 HOH B O     1 
HETATM 19147 O  O     . HOH X 10 .    ? 37.309  31.482  81.810  1.00 28.59 ? 1748 HOH B O     1 
HETATM 19148 O  O     . HOH X 10 .    ? 10.708  9.334   70.098  1.00 29.18 ? 1749 HOH B O     1 
HETATM 19149 O  O     . HOH X 10 .    ? 4.989   3.637   93.277  1.00 23.86 ? 1750 HOH B O     1 
HETATM 19150 O  O     . HOH X 10 .    ? 7.661   65.883  68.718  1.00 30.63 ? 1751 HOH B O     1 
HETATM 19151 O  O     . HOH X 10 .    ? -1.352  51.270  65.034  1.00 17.62 ? 1752 HOH B O     1 
HETATM 19152 O  O     . HOH X 10 .    ? 8.692   6.262   85.255  1.00 20.41 ? 1753 HOH B O     1 
HETATM 19153 O  O     . HOH X 10 .    ? 25.268  54.104  73.939  1.00 21.12 ? 1754 HOH B O     1 
HETATM 19154 O  O     . HOH X 10 .    ? 11.536  16.636  67.880  1.00 33.11 ? 1755 HOH B O     1 
HETATM 19155 O  O     . HOH X 10 .    ? 41.015  34.886  91.577  1.00 25.13 ? 1756 HOH B O     1 
HETATM 19156 O  O     . HOH X 10 .    ? -14.918 7.500   120.582 1.00 28.42 ? 1757 HOH B O     1 
HETATM 19157 O  O     . HOH X 10 .    ? -3.709  66.721  77.399  1.00 27.09 ? 1758 HOH B O     1 
HETATM 19158 O  O     . HOH X 10 .    ? 27.056  23.267  88.874  1.00 18.01 ? 1759 HOH B O     1 
HETATM 19159 O  O     . HOH X 10 .    ? 15.044  49.203  57.395  1.00 24.71 ? 1760 HOH B O     1 
HETATM 19160 O  O     . HOH X 10 .    ? 30.559  40.608  57.476  1.00 23.27 ? 1761 HOH B O     1 
HETATM 19161 O  O     . HOH X 10 .    ? -0.676  18.099  91.635  1.00 21.40 ? 1762 HOH B O     1 
HETATM 19162 O  O     . HOH X 10 .    ? -13.772 54.296  122.905 1.00 29.92 ? 1763 HOH B O     1 
HETATM 19163 O  O     . HOH X 10 .    ? -6.587  34.773  83.876  1.00 26.22 ? 1764 HOH B O     1 
HETATM 19164 O  O     . HOH X 10 .    ? 0.377   -7.781  109.819 1.00 32.39 ? 1765 HOH B O     1 
HETATM 19165 O  O     . HOH X 10 .    ? 31.384  35.444  74.906  1.00 32.71 ? 1766 HOH B O     1 
HETATM 19166 O  O     . HOH X 10 .    ? 26.195  40.054  53.078  1.00 26.61 ? 1767 HOH B O     1 
HETATM 19167 O  O     . HOH X 10 .    ? -1.751  5.624   92.362  1.00 19.60 ? 1768 HOH B O     1 
HETATM 19168 O  O     . HOH X 10 .    ? 19.879  54.469  81.395  1.00 22.61 ? 1769 HOH B O     1 
HETATM 19169 O  O     . HOH X 10 .    ? 18.051  15.282  97.720  1.00 24.48 ? 1770 HOH B O     1 
HETATM 19170 O  O     . HOH X 10 .    ? 14.490  16.963  92.224  1.00 20.93 ? 1771 HOH B O     1 
HETATM 19171 O  O     . HOH X 10 .    ? -1.140  38.058  76.756  1.00 27.20 ? 1772 HOH B O     1 
HETATM 19172 O  O     . HOH X 10 .    ? -3.289  11.109  104.059 1.00 17.36 ? 1773 HOH B O     1 
HETATM 19173 O  O     . HOH X 10 .    ? 29.030  24.389  51.303  1.00 30.90 ? 1774 HOH B O     1 
HETATM 19174 O  O     . HOH X 10 .    ? 29.864  33.643  73.568  1.00 25.83 ? 1775 HOH B O     1 
HETATM 19175 O  O     . HOH X 10 .    ? 3.476   14.251  73.007  1.00 32.42 ? 1776 HOH B O     1 
HETATM 19176 O  O     . HOH X 10 .    ? -1.955  25.662  80.108  1.00 21.53 ? 1777 HOH B O     1 
HETATM 19177 O  O     . HOH X 10 .    ? -1.140  56.176  122.027 1.00 31.89 ? 1778 HOH B O     1 
HETATM 19178 O  O     . HOH X 10 .    ? 17.633  54.145  83.097  1.00 23.93 ? 1779 HOH B O     1 
HETATM 19179 O  O     . HOH X 10 .    ? 3.710   29.917  84.793  1.00 21.02 ? 1780 HOH B O     1 
HETATM 19180 O  O     . HOH X 10 .    ? 10.281  23.457  109.733 1.00 32.44 ? 1781 HOH B O     1 
HETATM 19181 O  O     . HOH X 10 .    ? 9.425   43.936  110.410 1.00 29.59 ? 1782 HOH B O     1 
HETATM 19182 O  O     . HOH X 10 .    ? 11.882  8.082   90.643  1.00 21.58 ? 1783 HOH B O     1 
HETATM 19183 O  O     . HOH X 10 .    ? 13.131  26.145  96.288  1.00 28.82 ? 1784 HOH B O     1 
HETATM 19184 O  O     . HOH X 10 .    ? -5.505  9.911   115.300 1.00 24.99 ? 1785 HOH B O     1 
HETATM 19185 O  O     . HOH X 10 .    ? 2.042   63.551  78.498  1.00 17.58 ? 1786 HOH B O     1 
HETATM 19186 O  O     . HOH X 10 .    ? 22.314  54.530  93.257  1.00 24.81 ? 1787 HOH B O     1 
HETATM 19187 O  O     . HOH X 10 .    ? 36.913  28.282  93.385  1.00 27.90 ? 1788 HOH B O     1 
HETATM 19188 O  O     . HOH X 10 .    ? 16.128  21.878  100.069 1.00 21.05 ? 1789 HOH B O     1 
HETATM 19189 O  O     . HOH X 10 .    ? 2.545   44.631  58.521  1.00 27.49 ? 1790 HOH B O     1 
HETATM 19190 O  O     . HOH X 10 .    ? 36.315  20.931  78.846  1.00 35.50 ? 1791 HOH B O     1 
HETATM 19191 O  O     . HOH X 10 .    ? 12.186  6.264   84.713  1.00 22.31 ? 1792 HOH B O     1 
HETATM 19192 O  O     . HOH X 10 .    ? 11.913  21.161  59.043  1.00 17.20 ? 1793 HOH B O     1 
HETATM 19193 O  O     . HOH X 10 .    ? 11.596  49.813  78.985  1.00 26.45 ? 1794 HOH B O     1 
HETATM 19194 O  O     . HOH X 10 .    ? 34.049  22.860  78.467  1.00 24.73 ? 1795 HOH B O     1 
HETATM 19195 O  O     . HOH X 10 .    ? 18.784  52.374  80.145  1.00 21.04 ? 1796 HOH B O     1 
HETATM 19196 O  O     . HOH X 10 .    ? 10.515  29.660  94.470  1.00 24.11 ? 1797 HOH B O     1 
HETATM 19197 O  O     . HOH X 10 .    ? -5.767  -2.064  117.422 1.00 32.03 ? 1798 HOH B O     1 
HETATM 19198 O  O     . HOH X 10 .    ? 18.641  30.850  88.756  1.00 18.62 ? 1799 HOH B O     1 
HETATM 19199 O  O     . HOH X 10 .    ? 30.904  51.564  80.171  1.00 31.27 ? 1800 HOH B O     1 
HETATM 19200 O  O     . HOH X 10 .    ? -3.256  33.996  62.568  1.00 21.03 ? 1801 HOH B O     1 
HETATM 19201 O  O     . HOH X 10 .    ? 11.352  25.323  108.726 1.00 31.44 ? 1802 HOH B O     1 
HETATM 19202 O  O     . HOH X 10 .    ? 0.758   10.785  129.838 1.00 25.30 ? 1803 HOH B O     1 
HETATM 19203 O  O     . HOH X 10 .    ? 9.184   29.509  98.544  1.00 29.44 ? 1804 HOH B O     1 
HETATM 19204 O  O     . HOH X 10 .    ? 22.811  54.483  53.855  1.00 37.23 ? 1805 HOH B O     1 
HETATM 19205 O  O     . HOH X 10 .    ? 28.014  25.829  67.867  1.00 19.66 ? 1806 HOH B O     1 
HETATM 19206 O  O     . HOH X 10 .    ? 21.845  46.660  76.862  1.00 17.03 ? 1807 HOH B O     1 
HETATM 19207 O  O     . HOH X 10 .    ? -11.760 -1.865  96.760  1.00 26.85 ? 1808 HOH B O     1 
HETATM 19208 O  O     . HOH X 10 .    ? 11.464  26.435  102.177 1.00 27.42 ? 1809 HOH B O     1 
HETATM 19209 O  O     . HOH X 10 .    ? 43.470  37.112  88.210  1.00 27.55 ? 1810 HOH B O     1 
HETATM 19210 O  O     . HOH X 10 .    ? 18.060  23.575  61.572  1.00 21.38 ? 1811 HOH B O     1 
HETATM 19211 O  O     . HOH X 10 .    ? 1.410   9.951   79.398  1.00 30.12 ? 1812 HOH B O     1 
HETATM 19212 O  O     . HOH X 10 .    ? 9.803   22.388  103.077 1.00 34.29 ? 1813 HOH B O     1 
HETATM 19213 O  O     . HOH X 10 .    ? -8.023  27.329  100.030 1.00 31.09 ? 1814 HOH B O     1 
HETATM 19214 O  O     . HOH X 10 .    ? 0.406   0.274   96.455  1.00 24.03 ? 1815 HOH B O     1 
HETATM 19215 O  O     . HOH X 10 .    ? 35.753  31.813  103.871 1.00 30.83 ? 1816 HOH B O     1 
HETATM 19216 O  O     . HOH X 10 .    ? 24.695  57.749  78.564  1.00 21.59 ? 1817 HOH B O     1 
HETATM 19217 O  O     . HOH X 10 .    ? 4.554   22.112  83.934  1.00 23.20 ? 1818 HOH B O     1 
HETATM 19218 O  O     . HOH X 10 .    ? 11.479  18.494  95.304  1.00 31.13 ? 1819 HOH B O     1 
HETATM 19219 O  O     . HOH X 10 .    ? 19.309  16.344  63.839  1.00 19.36 ? 1820 HOH B O     1 
HETATM 19220 O  O     . HOH X 10 .    ? -2.846  14.714  98.939  1.00 16.28 ? 1821 HOH B O     1 
HETATM 19221 O  O     . HOH X 10 .    ? -1.413  20.968  89.697  1.00 17.57 ? 1822 HOH B O     1 
HETATM 19222 O  O     . HOH X 10 .    ? 26.814  59.505  78.692  1.00 18.98 ? 1823 HOH B O     1 
HETATM 19223 O  O     . HOH X 10 .    ? 10.884  16.462  122.307 1.00 28.46 ? 1824 HOH B O     1 
HETATM 19224 O  O     . HOH X 10 .    ? 35.661  39.038  90.933  1.00 33.96 ? 1825 HOH B O     1 
HETATM 19225 O  O     . HOH X 10 .    ? 28.918  65.637  62.657  1.00 28.64 ? 1826 HOH B O     1 
HETATM 19226 O  O     . HOH X 10 .    ? 23.715  31.911  110.619 1.00 25.18 ? 1827 HOH B O     1 
HETATM 19227 O  O     . HOH X 10 .    ? -6.528  42.028  84.151  1.00 30.08 ? 1828 HOH B O     1 
HETATM 19228 O  O     . HOH X 10 .    ? 4.579   47.759  87.205  1.00 18.18 ? 1829 HOH B O     1 
HETATM 19229 O  O     . HOH X 10 .    ? -4.936  44.868  109.041 1.00 31.34 ? 1830 HOH B O     1 
HETATM 19230 O  O     . HOH X 10 .    ? 23.292  52.223  84.138  1.00 26.13 ? 1831 HOH B O     1 
HETATM 19231 O  O     . HOH X 10 .    ? 27.154  18.553  62.097  1.00 23.54 ? 1832 HOH B O     1 
HETATM 19232 O  O     . HOH X 10 .    ? 1.238   22.725  63.672  1.00 23.77 ? 1833 HOH B O     1 
HETATM 19233 O  O     . HOH X 10 .    ? 28.408  46.833  88.073  1.00 24.24 ? 1834 HOH B O     1 
HETATM 19234 O  O     . HOH X 10 .    ? -5.768  23.316  80.733  1.00 21.25 ? 1835 HOH B O     1 
HETATM 19235 O  O     . HOH X 10 .    ? 8.814   62.238  85.466  1.00 22.99 ? 1836 HOH B O     1 
HETATM 19236 O  O     . HOH X 10 .    ? 2.869   23.471  58.901  1.00 29.74 ? 1837 HOH B O     1 
HETATM 19237 O  O     . HOH X 10 .    ? 2.709   35.701  121.575 1.00 37.23 ? 1838 HOH B O     1 
HETATM 19238 O  O     . HOH X 10 .    ? 23.169  56.334  99.451  1.00 26.31 ? 1839 HOH B O     1 
HETATM 19239 O  O     . HOH X 10 .    ? 32.785  38.252  104.700 1.00 30.07 ? 1840 HOH B O     1 
HETATM 19240 O  O     . HOH X 10 .    ? 2.249   29.974  54.741  1.00 30.97 ? 1841 HOH B O     1 
HETATM 19241 O  O     . HOH X 10 .    ? 12.289  37.630  108.122 1.00 21.28 ? 1842 HOH B O     1 
HETATM 19242 O  O     . HOH X 10 .    ? 18.173  48.234  90.293  1.00 18.78 ? 1843 HOH B O     1 
HETATM 19243 O  O     . HOH X 10 .    ? -2.015  49.603  101.460 1.00 27.77 ? 1844 HOH B O     1 
HETATM 19244 O  O     . HOH X 10 .    ? 21.086  54.091  83.786  1.00 24.62 ? 1845 HOH B O     1 
HETATM 19245 O  O     . HOH X 10 .    ? -15.718 10.516  90.072  1.00 24.73 ? 1846 HOH B O     1 
HETATM 19246 O  O     . HOH X 10 .    ? -20.728 25.599  94.800  1.00 29.63 ? 1847 HOH B O     1 
HETATM 19247 O  O     . HOH X 10 .    ? 18.224  53.617  76.237  1.00 17.74 ? 1848 HOH B O     1 
HETATM 19248 O  O     . HOH X 10 .    ? -4.813  56.051  81.791  1.00 28.52 ? 1849 HOH B O     1 
HETATM 19249 O  O     . HOH X 10 .    ? 18.393  66.277  55.812  1.00 32.39 ? 1850 HOH B O     1 
HETATM 19250 O  O     . HOH X 10 .    ? -7.431  28.054  74.419  1.00 27.86 ? 1851 HOH B O     1 
HETATM 19251 O  O     . HOH X 10 .    ? 8.074   63.352  66.264  1.00 31.84 ? 1852 HOH B O     1 
HETATM 19252 O  O     . HOH X 10 .    ? -14.531 9.665   87.609  1.00 22.74 ? 1853 HOH B O     1 
HETATM 19253 O  O     . HOH X 10 .    ? 22.426  11.986  87.774  1.00 28.01 ? 1854 HOH B O     1 
HETATM 19254 O  O     . HOH X 10 .    ? 33.170  19.640  87.805  1.00 23.88 ? 1855 HOH B O     1 
HETATM 19255 O  O     . HOH X 10 .    ? 8.082   37.722  79.395  1.00 16.15 ? 1856 HOH B O     1 
HETATM 19256 O  O     . HOH X 10 .    ? 5.373   12.176  78.001  1.00 31.22 ? 1857 HOH B O     1 
HETATM 19257 O  O     . HOH X 10 .    ? 4.950   43.017  70.891  1.00 14.10 ? 1858 HOH B O     1 
HETATM 19258 O  O     . HOH X 10 .    ? -7.071  44.315  73.845  1.00 30.84 ? 1859 HOH B O     1 
HETATM 19259 O  O     . HOH X 10 .    ? 24.497  51.218  67.249  1.00 23.08 ? 1860 HOH B O     1 
HETATM 19260 O  O     . HOH X 10 .    ? -5.397  16.578  97.064  1.00 18.57 ? 1861 HOH B O     1 
HETATM 19261 O  O     . HOH X 10 .    ? 10.362  33.794  109.711 1.00 26.85 ? 1862 HOH B O     1 
HETATM 19262 O  O     . HOH X 10 .    ? 29.476  41.922  80.133  1.00 26.34 ? 1863 HOH B O     1 
HETATM 19263 O  O     . HOH X 10 .    ? 32.536  33.456  70.882  1.00 28.66 ? 1864 HOH B O     1 
HETATM 19264 O  O     . HOH X 10 .    ? -1.600  74.443  74.698  1.00 31.09 ? 1865 HOH B O     1 
HETATM 19265 O  O     . HOH X 10 .    ? 4.678   58.080  69.066  1.00 22.15 ? 1866 HOH B O     1 
HETATM 19266 O  O     . HOH X 10 .    ? -12.263 22.121  85.756  1.00 24.65 ? 1867 HOH B O     1 
HETATM 19267 O  O     . HOH X 10 .    ? 1.687   30.829  96.153  1.00 20.54 ? 1868 HOH B O     1 
HETATM 19268 O  O     . HOH X 10 .    ? 1.184   46.852  99.140  1.00 27.16 ? 1869 HOH B O     1 
HETATM 19269 O  O     . HOH X 10 .    ? -2.357  58.010  75.303  1.00 17.09 ? 1870 HOH B O     1 
HETATM 19270 O  O     . HOH X 10 .    ? -9.621  33.610  69.389  1.00 40.94 ? 1871 HOH B O     1 
HETATM 19271 O  O     . HOH X 10 .    ? 16.155  54.175  105.139 1.00 28.96 ? 1872 HOH B O     1 
HETATM 19272 O  O     . HOH X 10 .    ? 21.843  25.428  82.794  1.00 18.77 ? 1873 HOH B O     1 
HETATM 19273 O  O     . HOH X 10 .    ? 27.901  9.337   74.019  1.00 31.94 ? 1874 HOH B O     1 
HETATM 19274 O  O     . HOH X 10 .    ? 5.407   18.807  87.554  1.00 23.17 ? 1875 HOH B O     1 
HETATM 19275 O  O     . HOH X 10 .    ? 4.549   18.972  124.332 1.00 26.27 ? 1876 HOH B O     1 
HETATM 19276 O  O     . HOH X 10 .    ? 12.884  48.422  82.304  1.00 19.30 ? 1877 HOH B O     1 
HETATM 19277 O  O     . HOH X 10 .    ? -16.725 22.177  82.512  1.00 27.18 ? 1878 HOH B O     1 
HETATM 19278 O  O     . HOH X 10 .    ? 26.143  27.706  67.350  1.00 14.75 ? 1879 HOH B O     1 
HETATM 19279 O  O     . HOH X 10 .    ? 34.970  32.720  55.294  1.00 28.95 ? 1880 HOH B O     1 
HETATM 19280 O  O     . HOH X 10 .    ? 2.970   31.535  98.481  1.00 26.14 ? 1881 HOH B O     1 
HETATM 19281 O  O     . HOH X 10 .    ? -0.205  19.732  94.157  1.00 20.55 ? 1882 HOH B O     1 
HETATM 19282 O  O     . HOH X 10 .    ? 5.265   24.223  120.319 1.00 35.90 ? 1883 HOH B O     1 
HETATM 19283 O  O     . HOH X 10 .    ? 28.051  44.705  89.957  1.00 23.15 ? 1884 HOH B O     1 
HETATM 19284 O  O     . HOH X 10 .    ? 9.541   18.589  101.493 1.00 22.48 ? 1885 HOH B O     1 
HETATM 19285 O  O     . HOH X 10 .    ? 17.654  76.857  63.819  1.00 29.54 ? 1886 HOH B O     1 
HETATM 19286 O  O     . HOH X 10 .    ? 30.450  34.647  84.745  1.00 26.33 ? 1887 HOH B O     1 
HETATM 19287 O  O     . HOH X 10 .    ? -3.647  52.752  82.783  1.00 26.26 ? 1888 HOH B O     1 
HETATM 19288 O  O     . HOH X 10 .    ? -1.215  13.720  100.866 1.00 17.22 ? 1889 HOH B O     1 
HETATM 19289 O  O     . HOH X 10 .    ? -2.075  37.048  87.506  1.00 18.46 ? 1890 HOH B O     1 
HETATM 19290 O  O     . HOH X 10 .    ? 2.341   49.296  76.308  1.00 17.47 ? 1891 HOH B O     1 
HETATM 19291 O  O     . HOH X 10 .    ? -10.959 2.000   91.556  1.00 26.13 ? 1892 HOH B O     1 
HETATM 19292 O  O     . HOH X 10 .    ? 18.907  58.814  82.507  1.00 23.28 ? 1893 HOH B O     1 
HETATM 19293 O  O     . HOH X 10 .    ? 26.203  13.283  88.152  1.00 28.87 ? 1894 HOH B O     1 
HETATM 19294 O  O     . HOH X 10 .    ? 12.407  62.381  84.626  1.00 31.23 ? 1895 HOH B O     1 
HETATM 19295 O  O     . HOH X 10 .    ? 31.460  62.687  75.181  1.00 21.73 ? 1896 HOH B O     1 
HETATM 19296 O  O     . HOH X 10 .    ? 20.565  22.334  61.109  1.00 18.24 ? 1897 HOH B O     1 
HETATM 19297 O  O     . HOH X 10 .    ? -12.508 8.521   127.315 1.00 32.79 ? 1898 HOH B O     1 
HETATM 19298 O  O     . HOH X 10 .    ? 4.168   0.299   86.892  1.00 35.44 ? 1899 HOH B O     1 
HETATM 19299 O  O     . HOH X 10 .    ? 7.371   20.925  102.448 1.00 26.36 ? 1900 HOH B O     1 
HETATM 19300 O  O     . HOH X 10 .    ? 17.318  34.370  68.574  1.00 13.09 ? 1901 HOH B O     1 
HETATM 19301 O  O     . HOH X 10 .    ? -3.847  46.177  107.058 1.00 25.59 ? 1902 HOH B O     1 
HETATM 19302 O  O     . HOH X 10 .    ? 31.102  34.711  77.411  1.00 32.85 ? 1903 HOH B O     1 
HETATM 19303 O  O     . HOH X 10 .    ? 27.907  49.418  98.060  1.00 31.69 ? 1904 HOH B O     1 
HETATM 19304 O  O     . HOH X 10 .    ? 18.612  35.768  113.210 1.00 20.98 ? 1905 HOH B O     1 
HETATM 19305 O  O     . HOH X 10 .    ? 3.717   17.723  75.646  1.00 28.62 ? 1906 HOH B O     1 
HETATM 19306 O  O     . HOH X 10 .    ? -2.787  30.718  70.747  1.00 18.39 ? 1907 HOH B O     1 
HETATM 19307 O  O     . HOH X 10 .    ? 28.103  31.101  80.855  1.00 23.09 ? 1908 HOH B O     1 
HETATM 19308 O  O     . HOH X 10 .    ? 15.623  10.533  95.767  1.00 21.63 ? 1909 HOH B O     1 
HETATM 19309 O  O     . HOH X 10 .    ? -3.056  64.887  83.534  1.00 17.96 ? 1910 HOH B O     1 
HETATM 19310 O  O     . HOH X 10 .    ? 15.866  56.335  63.930  1.00 22.95 ? 1911 HOH B O     1 
HETATM 19311 O  O     . HOH X 10 .    ? 0.109   11.347  81.002  1.00 30.07 ? 1912 HOH B O     1 
HETATM 19312 O  O     . HOH X 10 .    ? -1.026  -7.599  99.882  1.00 27.84 ? 1913 HOH B O     1 
HETATM 19313 O  O     . HOH X 10 .    ? 30.839  67.653  82.570  1.00 28.97 ? 1914 HOH B O     1 
HETATM 19314 O  O     . HOH X 10 .    ? 7.557   54.612  64.591  1.00 26.44 ? 1915 HOH B O     1 
HETATM 19315 O  O     . HOH X 10 .    ? 7.018   66.795  86.634  1.00 31.65 ? 1916 HOH B O     1 
HETATM 19316 O  O     . HOH X 10 .    ? 4.593   18.120  91.337  1.00 21.59 ? 1917 HOH B O     1 
HETATM 19317 O  O     . HOH X 10 .    ? 2.762   54.629  66.919  1.00 29.90 ? 1918 HOH B O     1 
HETATM 19318 O  O     . HOH X 10 .    ? 7.892   31.971  94.298  1.00 23.76 ? 1919 HOH B O     1 
HETATM 19319 O  O     . HOH X 10 .    ? 20.488  55.967  85.647  1.00 32.30 ? 1920 HOH B O     1 
HETATM 19320 O  O     . HOH X 10 .    ? 17.538  50.083  112.045 1.00 31.12 ? 1921 HOH B O     1 
HETATM 19321 O  O     . HOH X 10 .    ? -8.910  31.822  86.993  1.00 18.48 ? 1922 HOH B O     1 
HETATM 19322 O  O     . HOH X 10 .    ? 12.053  77.736  64.484  1.00 34.22 ? 1923 HOH B O     1 
HETATM 19323 O  O     . HOH X 10 .    ? 7.747   58.519  85.464  1.00 22.34 ? 1924 HOH B O     1 
HETATM 19324 O  O     . HOH X 10 .    ? 12.569  29.686  50.610  1.00 25.60 ? 1925 HOH B O     1 
HETATM 19325 O  O     . HOH X 10 .    ? -4.413  31.004  94.922  1.00 25.79 ? 1926 HOH B O     1 
HETATM 19326 O  O     . HOH X 10 .    ? 22.749  51.586  65.241  1.00 20.46 ? 1927 HOH B O     1 
HETATM 19327 O  O     . HOH X 10 .    ? 11.939  0.771   94.351  1.00 41.23 ? 1928 HOH B O     1 
HETATM 19328 O  O     . HOH X 10 .    ? -2.110  28.638  62.931  1.00 26.90 ? 1929 HOH B O     1 
HETATM 19329 O  O     . HOH X 10 .    ? -7.894  10.700  113.313 1.00 25.75 ? 1930 HOH B O     1 
HETATM 19330 O  O     . HOH X 10 .    ? -3.165  40.101  57.932  1.00 23.15 ? 1931 HOH B O     1 
HETATM 19331 O  O     . HOH X 10 .    ? -13.981 49.161  110.795 1.00 30.61 ? 1932 HOH B O     1 
HETATM 19332 O  O     . HOH X 10 .    ? 9.739   53.552  65.716  1.00 24.49 ? 1933 HOH B O     1 
HETATM 19333 O  O     . HOH X 10 .    ? -19.878 29.090  88.437  1.00 31.81 ? 1934 HOH B O     1 
HETATM 19334 O  O     . HOH X 10 .    ? 20.116  19.250  60.272  1.00 23.21 ? 1935 HOH B O     1 
HETATM 19335 O  O     . HOH X 10 .    ? 14.215  9.258   93.780  1.00 19.64 ? 1936 HOH B O     1 
HETATM 19336 O  O     . HOH X 10 .    ? 21.917  15.232  81.221  1.00 22.23 ? 1937 HOH B O     1 
HETATM 19337 O  O     . HOH X 10 .    ? 10.331  37.868  77.795  1.00 20.06 ? 1938 HOH B O     1 
HETATM 19338 O  O     . HOH X 10 .    ? 20.049  20.606  109.449 1.00 20.89 ? 1939 HOH B O     1 
HETATM 19339 O  O     . HOH X 10 .    ? 3.544   19.677  60.492  1.00 29.52 ? 1940 HOH B O     1 
HETATM 19340 O  O     . HOH X 10 .    ? -5.875  46.909  84.308  1.00 21.79 ? 1941 HOH B O     1 
HETATM 19341 O  O     . HOH X 10 .    ? -9.737  14.434  115.009 1.00 28.23 ? 1942 HOH B O     1 
HETATM 19342 O  O     . HOH X 10 .    ? -9.922  0.917   112.751 1.00 29.69 ? 1943 HOH B O     1 
HETATM 19343 O  O     . HOH X 10 .    ? 24.794  53.564  68.704  1.00 24.39 ? 1944 HOH B O     1 
HETATM 19344 O  O     . HOH X 10 .    ? 28.814  22.892  72.414  1.00 29.13 ? 1945 HOH B O     1 
HETATM 19345 O  O     . HOH X 10 .    ? -7.725  13.445  94.745  1.00 18.66 ? 1946 HOH B O     1 
HETATM 19346 O  O     . HOH X 10 .    ? 34.757  16.989  67.742  1.00 31.56 ? 1947 HOH B O     1 
HETATM 19347 O  O     . HOH X 10 .    ? 13.242  30.122  79.945  1.00 27.34 ? 1948 HOH B O     1 
HETATM 19348 O  O     . HOH X 10 .    ? -4.590  26.803  99.800  1.00 26.68 ? 1949 HOH B O     1 
HETATM 19349 O  O     . HOH X 10 .    ? 2.697   45.327  67.981  1.00 16.36 ? 1950 HOH B O     1 
HETATM 19350 O  O     . HOH X 10 .    ? 4.544   56.516  75.119  1.00 19.10 ? 1951 HOH B O     1 
HETATM 19351 O  O     . HOH X 10 .    ? -2.663  -7.418  110.793 1.00 26.84 ? 1952 HOH B O     1 
HETATM 19352 O  O     . HOH X 10 .    ? -6.988  39.130  67.549  1.00 27.54 ? 1953 HOH B O     1 
HETATM 19353 O  O     . HOH X 10 .    ? -6.292  36.038  92.617  1.00 25.47 ? 1954 HOH B O     1 
HETATM 19354 O  O     . HOH X 10 .    ? 18.994  54.878  104.447 1.00 25.34 ? 1955 HOH B O     1 
HETATM 19355 O  O     . HOH X 10 .    ? 0.280   63.477  84.717  1.00 28.64 ? 1956 HOH B O     1 
HETATM 19356 O  O     . HOH X 10 .    ? 1.489   20.340  92.433  1.00 31.12 ? 1957 HOH B O     1 
HETATM 19357 O  O     . HOH X 10 .    ? 30.853  20.152  56.415  1.00 26.87 ? 1958 HOH B O     1 
HETATM 19358 O  O     . HOH X 10 .    ? 4.537   61.171  68.149  1.00 35.73 ? 1959 HOH B O     1 
HETATM 19359 O  O     . HOH X 10 .    ? 2.182   49.266  99.208  1.00 24.32 ? 1960 HOH B O     1 
HETATM 19360 O  O     . HOH X 10 .    ? 14.764  57.307  72.305  1.00 23.73 ? 1961 HOH B O     1 
HETATM 19361 O  O     . HOH X 10 .    ? -5.268  -3.730  91.996  1.00 29.13 ? 1962 HOH B O     1 
HETATM 19362 O  O     . HOH X 10 .    ? 26.229  20.385  53.434  1.00 29.13 ? 1963 HOH B O     1 
HETATM 19363 O  O     . HOH X 10 .    ? -6.086  15.759  94.611  1.00 18.24 ? 1964 HOH B O     1 
HETATM 19364 O  O     . HOH X 10 .    ? 36.610  21.928  84.137  1.00 32.13 ? 1965 HOH B O     1 
HETATM 19365 O  O     . HOH X 10 .    ? 13.837  76.096  62.931  1.00 27.84 ? 1966 HOH B O     1 
HETATM 19366 O  O     . HOH X 10 .    ? 7.596   28.896  81.200  1.00 28.10 ? 1967 HOH B O     1 
HETATM 19367 O  O     . HOH X 10 .    ? 15.102  49.845  79.256  1.00 25.06 ? 1968 HOH B O     1 
HETATM 19368 O  O     . HOH X 10 .    ? 32.784  28.492  53.052  1.00 30.93 ? 1969 HOH B O     1 
HETATM 19369 O  O     . HOH X 10 .    ? 2.183   19.050  77.352  1.00 28.93 ? 1970 HOH B O     1 
HETATM 19370 O  O     . HOH X 10 .    ? 23.716  17.367  82.911  1.00 22.77 ? 1971 HOH B O     1 
HETATM 19371 O  O     . HOH X 10 .    ? 2.183   4.097   84.920  1.00 29.53 ? 1972 HOH B O     1 
HETATM 19372 O  O     . HOH X 10 .    ? 25.532  75.687  76.910  1.00 28.29 ? 1973 HOH B O     1 
HETATM 19373 O  O     . HOH X 10 .    ? 13.165  18.953  87.709  1.00 24.22 ? 1974 HOH B O     1 
HETATM 19374 O  O     . HOH X 10 .    ? -15.387 19.646  82.786  1.00 27.00 ? 1975 HOH B O     1 
HETATM 19375 O  O     . HOH X 10 .    ? 20.456  63.065  54.185  1.00 36.39 ? 1976 HOH B O     1 
HETATM 19376 O  O     . HOH X 10 .    ? 36.972  37.852  89.172  1.00 21.03 ? 1977 HOH B O     1 
HETATM 19377 O  O     . HOH X 10 .    ? 16.488  51.647  60.159  1.00 27.73 ? 1978 HOH B O     1 
HETATM 19378 O  O     . HOH X 10 .    ? 35.404  31.688  58.556  1.00 28.32 ? 1979 HOH B O     1 
HETATM 19379 O  O     . HOH X 10 .    ? -0.536  45.432  77.581  1.00 31.29 ? 1980 HOH B O     1 
HETATM 19380 O  O     . HOH X 10 .    ? 4.850   43.455  55.912  1.00 26.87 ? 1981 HOH B O     1 
HETATM 19381 O  O     . HOH X 10 .    ? 26.444  41.520  81.466  1.00 24.92 ? 1982 HOH B O     1 
HETATM 19382 O  O     . HOH X 10 .    ? -2.640  60.642  124.242 1.00 34.86 ? 1983 HOH B O     1 
HETATM 19383 O  O     . HOH X 10 .    ? 16.024  52.365  79.786  1.00 23.03 ? 1984 HOH B O     1 
HETATM 19384 O  O     . HOH X 10 .    ? -4.383  54.549  131.171 1.00 37.56 ? 1985 HOH B O     1 
HETATM 19385 O  O     . HOH X 10 .    ? 15.130  29.314  49.306  1.00 30.93 ? 1986 HOH B O     1 
HETATM 19386 O  O     . HOH X 10 .    ? 10.364  10.323  123.478 1.00 29.13 ? 1987 HOH B O     1 
HETATM 19387 O  O     . HOH X 10 .    ? 35.345  20.239  85.774  1.00 32.94 ? 1988 HOH B O     1 
HETATM 19388 O  O     . HOH X 10 .    ? 22.761  68.011  59.715  1.00 26.70 ? 1989 HOH B O     1 
HETATM 19389 O  O     . HOH X 10 .    ? -18.397 27.494  94.172  1.00 25.97 ? 1990 HOH B O     1 
HETATM 19390 O  O     . HOH X 10 .    ? 6.270   24.987  83.868  1.00 25.65 ? 1991 HOH B O     1 
HETATM 19391 O  O     . HOH X 10 .    ? 16.905  25.079  52.475  1.00 25.80 ? 1992 HOH B O     1 
HETATM 19392 O  O     . HOH X 10 .    ? 11.902  58.256  94.307  1.00 30.37 ? 1993 HOH B O     1 
HETATM 19393 O  O     . HOH X 10 .    ? 2.547   57.683  70.916  1.00 26.03 ? 1994 HOH B O     1 
HETATM 19394 O  O     . HOH X 10 .    ? 15.977  14.304  107.073 1.00 26.39 ? 1995 HOH B O     1 
HETATM 19395 O  O     . HOH X 10 .    ? -3.091  23.114  79.568  1.00 22.79 ? 1996 HOH B O     1 
HETATM 19396 O  O     . HOH X 10 .    ? 0.849   56.286  65.782  1.00 29.85 ? 1997 HOH B O     1 
HETATM 19397 O  O     . HOH X 10 .    ? -2.303  62.704  69.541  1.00 30.40 ? 1998 HOH B O     1 
HETATM 19398 O  O     . HOH X 10 .    ? 11.219  43.916  51.294  1.00 34.78 ? 1999 HOH B O     1 
HETATM 19399 O  O     . HOH X 10 .    ? -2.808  -5.457  89.896  1.00 32.97 ? 2000 HOH B O     1 
HETATM 19400 O  O     . HOH X 10 .    ? -5.931  37.780  86.104  1.00 29.82 ? 2001 HOH B O     1 
HETATM 19401 O  O     . HOH X 10 .    ? 23.522  24.813  47.782  1.00 31.77 ? 2002 HOH B O     1 
HETATM 19402 O  O     . HOH X 10 .    ? -1.274  44.474  75.721  1.00 28.41 ? 2003 HOH B O     1 
HETATM 19403 O  O     . HOH X 10 .    ? 34.580  16.357  62.317  1.00 34.59 ? 2004 HOH B O     1 
HETATM 19404 O  O     . HOH X 10 .    ? -1.713  38.042  73.703  1.00 18.63 ? 2005 HOH B O     1 
HETATM 19405 O  O     . HOH X 10 .    ? 27.286  13.389  66.848  1.00 28.60 ? 2006 HOH B O     1 
HETATM 19406 O  O     . HOH X 10 .    ? 4.170   29.867  82.066  1.00 25.61 ? 2007 HOH B O     1 
HETATM 19407 O  O     . HOH X 10 .    ? -6.334  39.984  86.279  1.00 30.23 ? 2008 HOH B O     1 
HETATM 19408 O  O     . HOH X 10 .    ? 16.359  56.701  95.179  1.00 30.64 ? 2009 HOH B O     1 
HETATM 19409 O  O     . HOH X 10 .    ? -8.098  12.366  82.927  1.00 33.95 ? 2010 HOH B O     1 
HETATM 19410 O  O     . HOH X 10 .    ? 7.181   33.980  51.486  1.00 30.02 ? 2011 HOH B O     1 
HETATM 19411 O  O     . HOH X 10 .    ? -0.498  -1.945  95.024  1.00 28.06 ? 2012 HOH B O     1 
HETATM 19412 O  O     . HOH X 10 .    ? 28.369  41.662  53.419  1.00 31.12 ? 2013 HOH B O     1 
HETATM 19413 O  O     . HOH X 10 .    ? 5.953   17.689  96.726  1.00 25.92 ? 2014 HOH B O     1 
HETATM 19414 O  O     . HOH X 10 .    ? 39.639  38.609  89.053  1.00 30.69 ? 2015 HOH B O     1 
HETATM 19415 O  O     . HOH X 10 .    ? 33.079  40.477  61.610  1.00 35.65 ? 2016 HOH B O     1 
HETATM 19416 O  O     . HOH X 10 .    ? -7.153  8.380   116.633 1.00 26.17 ? 2017 HOH B O     1 
HETATM 19417 O  O     . HOH X 10 .    ? 38.339  32.975  84.052  1.00 29.64 ? 2018 HOH B O     1 
HETATM 19418 O  O     . HOH X 10 .    ? 24.430  70.612  65.369  1.00 32.69 ? 2019 HOH B O     1 
HETATM 19419 O  O     . HOH X 10 .    ? 23.517  69.067  62.334  1.00 27.76 ? 2020 HOH B O     1 
HETATM 19420 O  O     . HOH X 10 .    ? 15.720  35.593  113.720 1.00 32.14 ? 2021 HOH B O     1 
HETATM 19421 O  O     . HOH X 10 .    ? 20.557  68.898  58.510  1.00 35.66 ? 2022 HOH B O     1 
HETATM 19422 O  O     . HOH X 10 .    ? 32.549  21.067  76.556  1.00 30.78 ? 2023 HOH B O     1 
HETATM 19423 O  O     . HOH X 10 .    ? 40.527  30.547  90.553  1.00 26.16 ? 2024 HOH B O     1 
HETATM 19424 O  O     . HOH X 10 .    ? 5.070   44.780  53.811  1.00 31.11 ? 2025 HOH B O     1 
HETATM 19425 O  O     . HOH X 10 .    ? 32.685  59.078  67.390  1.00 29.10 ? 2026 HOH B O     1 
HETATM 19426 O  O     . HOH X 10 .    ? 2.021   62.548  83.602  1.00 22.52 ? 2027 HOH B O     1 
HETATM 19427 O  O     . HOH X 10 .    ? -2.737  30.114  96.993  1.00 30.71 ? 2028 HOH B O     1 
HETATM 19428 O  O     . HOH X 10 .    ? 13.956  52.206  63.601  1.00 28.59 ? 2029 HOH B O     1 
HETATM 19429 O  O     . HOH X 10 .    ? 4.494   43.732  51.154  1.00 27.69 ? 2030 HOH B O     1 
HETATM 19430 O  O     . HOH X 10 .    ? 19.399  45.780  90.007  1.00 15.83 ? 2031 HOH B O     1 
HETATM 19431 O  O     . HOH X 10 .    ? 0.119   4.903   86.127  1.00 30.55 ? 2032 HOH B O     1 
HETATM 19432 O  O     . HOH X 10 .    ? -2.864  52.086  101.239 1.00 26.08 ? 2033 HOH B O     1 
HETATM 19433 O  O     . HOH X 10 .    ? 8.712   23.659  122.625 1.00 29.35 ? 2034 HOH B O     1 
HETATM 19434 O  O     . HOH X 10 .    ? 31.804  32.797  75.472  1.00 32.55 ? 2035 HOH B O     1 
HETATM 19435 O  O     . HOH X 10 .    ? 3.660   30.157  94.350  1.00 31.51 ? 2036 HOH B O     1 
HETATM 19436 O  O     . HOH X 10 .    ? 30.746  59.180  60.804  1.00 32.16 ? 2037 HOH B O     1 
HETATM 19437 O  O     . HOH X 10 .    ? 11.742  17.673  89.731  1.00 32.75 ? 2038 HOH B O     1 
HETATM 19438 O  O     . HOH X 10 .    ? -7.543  22.579  78.700  1.00 26.62 ? 2039 HOH B O     1 
HETATM 19439 O  O     . HOH X 10 .    ? 16.649  26.419  110.126 1.00 26.14 ? 2040 HOH B O     1 
HETATM 19440 O  O     . HOH X 10 .    ? -2.949  28.576  68.990  1.00 24.82 ? 2041 HOH B O     1 
HETATM 19441 O  O     . HOH X 10 .    ? 11.996  21.465  98.845  1.00 30.21 ? 2042 HOH B O     1 
HETATM 19442 O  O     . HOH X 10 .    ? -0.079  18.393  71.836  1.00 33.52 ? 2043 HOH B O     1 
HETATM 19443 O  O     . HOH X 10 .    ? -10.905 30.308  76.246  1.00 31.80 ? 2044 HOH B O     1 
HETATM 19444 O  O     . HOH X 10 .    ? 5.509   11.115  75.348  1.00 31.27 ? 2045 HOH B O     1 
HETATM 19445 O  O     . HOH X 10 .    ? 6.699   2.673   79.946  1.00 34.27 ? 2046 HOH B O     1 
HETATM 19446 O  O     . HOH X 10 .    ? 31.023  15.424  65.002  1.00 34.21 ? 2047 HOH B O     1 
HETATM 19447 O  O     . HOH X 10 .    ? 30.190  30.967  79.253  1.00 28.52 ? 2048 HOH B O     1 
HETATM 19448 O  O     . HOH X 10 .    ? -2.857  41.659  78.223  1.00 31.48 ? 2049 HOH B O     1 
HETATM 19449 O  O     . HOH X 10 .    ? 14.671  51.592  56.027  1.00 34.82 ? 2050 HOH B O     1 
HETATM 19450 O  O     . HOH X 10 .    ? 23.976  32.920  115.668 1.00 35.10 ? 2051 HOH B O     1 
HETATM 19451 O  O     . HOH X 10 .    ? 6.718   19.023  90.068  1.00 29.06 ? 2052 HOH B O     1 
HETATM 19452 O  O     . HOH X 10 .    ? 1.006   14.790  79.817  1.00 28.71 ? 2053 HOH B O     1 
HETATM 19453 O  O     . HOH X 10 .    ? -4.241  40.479  60.616  1.00 29.08 ? 2054 HOH B O     1 
HETATM 19454 O  O     . HOH X 10 .    ? 33.203  15.754  64.941  1.00 35.62 ? 2055 HOH B O     1 
HETATM 19455 O  O     . HOH X 10 .    ? 8.457   -3.238  105.890 1.00 35.25 ? 2056 HOH B O     1 
HETATM 19456 O  O     . HOH X 10 .    ? 40.062  45.392  90.558  1.00 30.74 ? 2057 HOH B O     1 
HETATM 19457 O  O     . HOH X 10 .    ? 14.533  22.317  97.938  1.00 24.60 ? 2058 HOH B O     1 
HETATM 19458 O  O     . HOH X 10 .    ? 20.300  23.265  110.191 1.00 31.78 ? 2059 HOH B O     1 
HETATM 19459 O  O     . HOH X 10 .    ? 12.403  18.463  91.978  1.00 31.42 ? 2060 HOH B O     1 
HETATM 19460 O  O     . HOH X 10 .    ? 13.785  25.325  100.957 1.00 23.62 ? 2061 HOH B O     1 
HETATM 19461 O  O     . HOH X 10 .    ? 7.033   28.191  83.646  1.00 34.16 ? 2062 HOH B O     1 
HETATM 19462 O  O     . HOH X 10 .    ? 23.129  71.774  61.593  1.00 35.99 ? 2063 HOH B O     1 
HETATM 19463 O  O     . HOH X 10 .    ? 0.880   31.795  82.668  1.00 25.74 ? 2064 HOH B O     1 
HETATM 19464 O  O     . HOH X 10 .    ? 10.184  0.886   107.453 1.00 28.68 ? 2065 HOH B O     1 
HETATM 19465 O  O     . HOH X 10 .    ? 19.781  34.418  115.276 1.00 24.82 ? 2066 HOH B O     1 
HETATM 19466 O  O     . HOH X 10 .    ? 2.884   13.377  77.767  1.00 33.12 ? 2067 HOH B O     1 
HETATM 19467 O  O     . HOH X 10 .    ? 6.600   23.924  124.871 1.00 28.15 ? 2068 HOH B O     1 
HETATM 19468 O  O     . HOH X 10 .    ? -8.817  -2.193  117.902 1.00 36.83 ? 2069 HOH B O     1 
HETATM 19469 O  O     . HOH X 10 .    ? 15.949  77.187  62.088  1.00 36.50 ? 2070 HOH B O     1 
HETATM 19470 O  O     . HOH X 10 .    ? 30.553  61.874  72.715  1.00 27.71 ? 2071 HOH B O     1 
HETATM 19471 O  O     . HOH X 10 .    ? 34.529  26.560  56.888  1.00 28.06 ? 2072 HOH B O     1 
HETATM 19472 O  O     . HOH X 10 .    ? 6.109   16.031  92.244  1.00 25.58 ? 2073 HOH B O     1 
HETATM 19473 O  O     . HOH X 10 .    ? 5.023   31.962  93.082  1.00 33.56 ? 2074 HOH B O     1 
HETATM 19474 O  O     . HOH X 10 .    ? 5.569   20.699  122.769 1.00 34.46 ? 2075 HOH B O     1 
HETATM 19475 O  O     . HOH X 10 .    ? 13.301  36.709  74.344  1.00 17.26 ? 2076 HOH B O     1 
HETATM 19476 O  O     . HOH X 10 .    ? 12.283  55.646  105.791 1.00 32.28 ? 2077 HOH B O     1 
HETATM 19477 O  O     . HOH X 10 .    ? 14.553  44.504  52.983  1.00 31.94 ? 2078 HOH B O     1 
HETATM 19478 O  O     . HOH X 10 .    ? 11.797  44.076  53.492  1.00 27.23 ? 2079 HOH B O     1 
HETATM 19479 O  O     . HOH X 10 .    ? 34.482  27.874  61.481  1.00 26.47 ? 2080 HOH B O     1 
HETATM 19480 O  O     . HOH X 10 .    ? 9.032   4.071   83.942  1.00 26.41 ? 2081 HOH B O     1 
HETATM 19481 O  O     . HOH X 10 .    ? 6.350   61.216  85.333  1.00 23.94 ? 2082 HOH B O     1 
HETATM 19482 O  O     . HOH X 10 .    ? 41.708  37.307  90.145  1.00 31.29 ? 2083 HOH B O     1 
HETATM 19483 O  O     . HOH X 10 .    ? 4.940   3.360   86.059  1.00 29.83 ? 2084 HOH B O     1 
HETATM 19484 O  O     . HOH X 10 .    ? 12.278  0.715   109.405 1.00 34.17 ? 2085 HOH B O     1 
HETATM 19485 O  O     . HOH X 10 .    ? -25.555 13.075  86.920  1.00 33.82 ? 2086 HOH B O     1 
HETATM 19486 O  O     . HOH X 10 .    ? 12.932  37.024  77.426  1.00 18.02 ? 2087 HOH B O     1 
HETATM 19487 O  O     . HOH X 10 .    ? 4.586   56.165  67.074  1.00 33.14 ? 2088 HOH B O     1 
HETATM 19488 O  O     . HOH X 10 .    ? 18.085  9.296   95.920  1.00 31.12 ? 2089 HOH B O     1 
HETATM 19489 O  O     . HOH X 10 .    ? 8.560   20.140  123.524 1.00 28.68 ? 2090 HOH B O     1 
HETATM 19490 O  O     . HOH X 10 .    ? 21.600  19.854  107.426 1.00 26.73 ? 2091 HOH B O     1 
HETATM 19491 O  O     . HOH X 10 .    ? 31.495  69.961  80.314  1.00 28.94 ? 2092 HOH B O     1 
HETATM 19492 O  O     . HOH X 10 .    ? 30.312  24.148  74.565  1.00 22.84 ? 2093 HOH B O     1 
HETATM 19493 O  O     . HOH X 10 .    ? 14.232  35.643  81.868  1.00 23.84 ? 2094 HOH B O     1 
HETATM 19494 O  O     . HOH X 10 .    ? 13.583  24.873  98.344  1.00 29.39 ? 2095 HOH B O     1 
HETATM 19495 O  O     . HOH X 10 .    ? -8.341  35.672  87.497  1.00 33.17 ? 2096 HOH B O     1 
HETATM 19496 O  O     . HOH X 10 .    ? -7.368  25.284  75.111  1.00 27.19 ? 2097 HOH B O     1 
HETATM 19497 O  O     . HOH X 10 .    ? 14.794  56.148  104.629 1.00 31.33 ? 2098 HOH B O     1 
HETATM 19498 O  O     . HOH X 10 .    ? 5.250   30.614  86.816  1.00 31.63 ? 2099 HOH B O     1 
HETATM 19499 O  O     . HOH X 10 .    ? 2.303   21.983  61.147  1.00 32.61 ? 2100 HOH B O     1 
HETATM 19500 O  O     . HOH X 10 .    ? -8.746  33.953  85.415  1.00 29.70 ? 2101 HOH B O     1 
HETATM 19501 O  O     . HOH X 10 .    ? -13.083 -0.163  122.047 1.00 38.64 ? 2102 HOH B O     1 
HETATM 19502 O  O     . HOH X 10 .    ? -11.328 47.520  77.312  1.00 35.00 ? 2103 HOH B O     1 
HETATM 19503 O  O     . HOH X 10 .    ? 32.358  60.267  62.851  1.00 30.14 ? 2104 HOH B O     1 
HETATM 19504 O  O     . HOH X 10 .    ? 26.079  52.824  84.221  1.00 34.33 ? 2105 HOH B O     1 
HETATM 19505 O  O     . HOH X 10 .    ? -11.341 3.966   87.088  1.00 32.48 ? 2106 HOH B O     1 
HETATM 19506 O  O     . HOH X 10 .    ? 22.283  50.671  68.803  1.00 24.77 ? 2107 HOH B O     1 
HETATM 19507 O  O     . HOH X 10 .    ? 9.132   17.328  90.122  1.00 27.53 ? 2108 HOH B O     1 
HETATM 19508 O  O     . HOH X 10 .    ? -0.323  29.067  96.740  1.00 24.23 ? 2109 HOH B O     1 
HETATM 19509 O  O     . HOH X 10 .    ? -3.343  38.128  78.050  1.00 27.56 ? 2110 HOH B O     1 
HETATM 19510 O  O     . HOH X 10 .    ? 6.122   -4.620  102.221 1.00 34.05 ? 2111 HOH B O     1 
HETATM 19511 O  O     . HOH X 10 .    ? 19.813  11.078  96.589  1.00 30.10 ? 2112 HOH B O     1 
HETATM 19512 O  O     . HOH X 10 .    ? -7.981  37.186  84.009  1.00 33.42 ? 2113 HOH B O     1 
HETATM 19513 O  O     . HOH X 10 .    ? 6.035   12.271  73.214  1.00 33.37 ? 2114 HOH B O     1 
HETATM 19514 O  O     . HOH X 10 .    ? 5.433   31.751  52.252  1.00 31.62 ? 2115 HOH B O     1 
HETATM 19515 O  O     . HOH X 10 .    ? 3.110   15.199  75.572  1.00 30.97 ? 2116 HOH B O     1 
HETATM 19516 O  O     . HOH X 10 .    ? 4.195   64.439  86.760  1.00 34.05 ? 2117 HOH B O     1 
HETATM 19517 O  O     . HOH X 10 .    ? -1.412  23.355  64.061  1.00 28.72 ? 2118 HOH B O     1 
HETATM 19518 O  O     . HOH X 10 .    ? -11.765 1.882   89.159  1.00 32.66 ? 2119 HOH B O     1 
HETATM 19519 O  O     . HOH X 10 .    ? -23.696 14.237  82.538  1.00 34.27 ? 2120 HOH B O     1 
HETATM 19520 O  O     . HOH X 10 .    ? 30.256  64.147  71.092  1.00 32.09 ? 2121 HOH B O     1 
HETATM 19521 O  O     . HOH X 10 .    ? 1.934   32.046  85.150  1.00 22.22 ? 2122 HOH B O     1 
HETATM 19522 O  O     . HOH X 10 .    ? -5.138  23.768  75.166  1.00 27.53 ? 2123 HOH B O     1 
HETATM 19523 O  O     . HOH X 10 .    ? -25.251 13.174  84.306  1.00 36.24 ? 2124 HOH B O     1 
HETATM 19524 O  O     . HOH X 10 .    ? 6.969   2.113   84.544  1.00 34.99 ? 2125 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   ? 0.5541 0.5841 0.6413 0.1116  -0.0325 -0.1330 14   ALA A N   
2     C CA  . ALA A 16   ? 0.5493 0.5812 0.6280 0.1101  -0.0297 -0.1312 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5430 0.5847 0.6127 0.1104  -0.0232 -0.1268 14   ALA A C   
4     O O   . ALA A 16   ? 0.5675 0.6230 0.6336 0.1130  -0.0204 -0.1295 14   ALA A O   
5     C CB  . ALA A 16   ? 0.5791 0.6178 0.6564 0.1120  -0.0315 -0.1385 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5093 0.5441 0.5743 0.1051  -0.0209 -0.1173 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4436 0.4863 0.4998 0.1026  -0.0150 -0.1099 15   PRO A CA  
8     C C   . PRO A 17   ? 0.4771 0.5323 0.5252 0.1040  -0.0116 -0.1120 15   PRO A C   
9     O O   . PRO A 17   ? 0.4719 0.5256 0.5180 0.1039  -0.0129 -0.1148 15   PRO A O   
10    C CB  . PRO A 17   ? 0.5215 0.5523 0.5751 0.0958  -0.0144 -0.0998 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.5163 0.5336 0.5787 0.0951  -0.0199 -0.1011 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.4694 0.4888 0.5371 0.1001  -0.0238 -0.1118 15   PRO A CD  
13    N N   . ALA A 18   ? 0.4499 0.5182 0.4935 0.1053  -0.0073 -0.1104 16   ALA A N   
14    C CA  . ALA A 18   ? 0.3825 0.4639 0.4181 0.1063  -0.0037 -0.1111 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3809 0.4568 0.4094 0.1006  -0.0015 -0.1024 16   ALA A C   
16    O O   . ALA A 18   ? 0.3437 0.4114 0.3713 0.0958  -0.0003 -0.0940 16   ALA A O   
17    C CB  . ALA A 18   ? 0.3950 0.4917 0.4280 0.1085  0.0004  -0.1100 16   ALA A CB  
18    N N   . PRO A 19   ? 0.3621 0.4424 0.3856 0.1009  -0.0010 -0.1045 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3270 0.4015 0.3445 0.0956  0.0007  -0.0969 17   PRO A CA  
20    C C   . PRO A 19   ? 0.3182 0.3980 0.3300 0.0923  0.0055  -0.0876 17   PRO A C   
21    O O   . PRO A 19   ? 0.3105 0.4043 0.3195 0.0944  0.0085  -0.0877 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3551 0.4370 0.3687 0.0979  0.0003  -0.1022 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.3488 0.4342 0.3687 0.1038  -0.0033 -0.1136 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3358 0.4258 0.3599 0.1063  -0.0026 -0.1146 17   PRO A CD  
25    N N   . PHE A 20   ? 0.2999 0.3685 0.3106 0.0869  0.0059  -0.0795 18   PHE A N   
26    C CA  . PHE A 20   ? 0.3157 0.3865 0.3217 0.0829  0.0099  -0.0703 18   PHE A CA  
27    C C   . PHE A 20   ? 0.3071 0.3835 0.3153 0.0837  0.0118  -0.0681 18   PHE A C   
28    O O   . PHE A 20   ? 0.3333 0.4138 0.3380 0.0810  0.0151  -0.0609 18   PHE A O   
29    C CB  . PHE A 20   ? 0.2925 0.3741 0.2915 0.0827  0.0129  -0.0681 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2870 0.3635 0.2834 0.0815  0.0115  -0.0693 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2742 0.3391 0.2691 0.0765  0.0113  -0.0632 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.3110 0.3948 0.3063 0.0853  0.0103  -0.0766 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.3053 0.3658 0.2978 0.0754  0.0099  -0.0641 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.2842 0.3635 0.2772 0.0841  0.0088  -0.0776 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.3220 0.3895 0.3136 0.0791  0.0087  -0.0712 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3392 0.4156 0.3535 0.0873  0.0095  -0.0739 19   ALA A N   
37    C CA  . ALA A 21   ? 0.3320 0.4138 0.3488 0.0882  0.0111  -0.0721 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3613 0.4329 0.3788 0.0833  0.0116  -0.0639 19   ALA A C   
39    O O   . ALA A 21   ? 0.3750 0.4516 0.3934 0.0829  0.0137  -0.0603 19   ALA A O   
40    C CB  . ALA A 21   ? 0.3687 0.4517 0.3927 0.0934  0.0080  -0.0807 19   ALA A CB  
41    N N   . ASP A 22   ? 0.3036 0.3621 0.3211 0.0795  0.0098  -0.0609 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3520 0.4012 0.3699 0.0748  0.0101  -0.0535 20   ASP A CA  
43    C C   . ASP A 22   ? 0.2831 0.3262 0.2959 0.0702  0.0110  -0.0480 20   ASP A C   
44    O O   . ASP A 22   ? 0.3009 0.3328 0.3147 0.0667  0.0096  -0.0445 20   ASP A O   
45    C CB  . ASP A 22   ? 0.3987 0.4371 0.4234 0.0749  0.0062  -0.0554 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.4778 0.5087 0.5032 0.0705  0.0066  -0.0481 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.5286 0.5652 0.5533 0.0699  0.0092  -0.0444 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.5312 0.5510 0.5580 0.0676  0.0043  -0.0460 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2534 0.3044 0.2609 0.0704  0.0134  -0.0473 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2406 0.2860 0.2438 0.0668  0.0138  -0.0436 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2349 0.2739 0.2369 0.0618  0.0152  -0.0355 21   PHE A C   
52    O O   . PHE A 23   ? 0.2474 0.2761 0.2493 0.0587  0.0138  -0.0333 21   PHE A O   
53    C CB  . PHE A 23   ? 0.2509 0.3070 0.2489 0.0680  0.0161  -0.0438 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2434 0.2949 0.2371 0.0642  0.0169  -0.0391 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2687 0.3110 0.2625 0.0633  0.0144  -0.0413 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.2524 0.3085 0.2425 0.0615  0.0200  -0.0324 21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2423 0.2804 0.2324 0.0598  0.0151  -0.0371 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.2752 0.3267 0.2619 0.0582  0.0205  -0.0282 21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.2517 0.2943 0.2382 0.0574  0.0181  -0.0307 21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2377 0.2832 0.2389 0.0610  0.0179  -0.0311 22   ALA A N   
61    C CA  . ALA A 24   ? 0.2577 0.2980 0.2579 0.0564  0.0192  -0.0238 22   ALA A CA  
62    C C   . ALA A 24   ? 0.2334 0.2804 0.2350 0.0563  0.0213  -0.0203 22   ALA A C   
63    O O   . ALA A 24   ? 0.2368 0.2880 0.2361 0.0540  0.0237  -0.0149 22   ALA A O   
64    C CB  . ALA A 24   ? 0.2726 0.3133 0.2680 0.0537  0.0208  -0.0198 22   ALA A CB  
65    N N   . PRO A 25   ? 0.2605 0.3085 0.2663 0.0585  0.0203  -0.0231 23   PRO A N   
66    C CA  . PRO A 25   ? 0.2669 0.3214 0.2744 0.0583  0.0223  -0.0197 23   PRO A CA  
67    C C   . PRO A 25   ? 0.2434 0.2912 0.2508 0.0535  0.0228  -0.0129 23   PRO A C   
68    O O   . PRO A 25   ? 0.2463 0.2833 0.2545 0.0513  0.0209  -0.0122 23   PRO A O   
69    C CB  . PRO A 25   ? 0.2992 0.3533 0.3120 0.0616  0.0203  -0.0246 23   PRO A CB  
70    C CG  . PRO A 25   ? 0.2983 0.3405 0.3127 0.0611  0.0169  -0.0273 23   PRO A CG  
71    C CD  . PRO A 25   ? 0.2903 0.3319 0.3005 0.0608  0.0170  -0.0286 23   PRO A CD  
72    N N   . PRO A 26   ? 0.2557 0.3100 0.2623 0.0518  0.0253  -0.0077 24   PRO A N   
73    C CA  . PRO A 26   ? 0.2317 0.2799 0.2387 0.0474  0.0256  -0.0017 24   PRO A CA  
74    C C   . PRO A 26   ? 0.2487 0.2918 0.2598 0.0471  0.0241  -0.0019 24   PRO A C   
75    O O   . PRO A 26   ? 0.2487 0.2954 0.2629 0.0503  0.0235  -0.0055 24   PRO A O   
76    C CB  . PRO A 26   ? 0.2445 0.3025 0.2509 0.0464  0.0284  0.0033  24   PRO A CB  
77    C CG  . PRO A 26   ? 0.2909 0.3610 0.2979 0.0508  0.0295  -0.0003 24   PRO A CG  
78    C CD  . PRO A 26   ? 0.2636 0.3317 0.2693 0.0540  0.0279  -0.0071 24   PRO A CD  
79    N N   . VAL A 27   ? 0.2633 0.2982 0.2745 0.0432  0.0234  0.0020  25   VAL A N   
80    C CA  . VAL A 27   ? 0.2672 0.2973 0.2820 0.0422  0.0220  0.0028  25   VAL A CA  
81    C C   . VAL A 27   ? 0.2750 0.3136 0.2928 0.0437  0.0233  0.0037  25   VAL A C   
82    O O   . VAL A 27   ? 0.2800 0.3181 0.3015 0.0455  0.0220  0.0016  25   VAL A O   
83    C CB  . VAL A 27   ? 0.2656 0.2884 0.2795 0.0377  0.0217  0.0074  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2693 0.2894 0.2868 0.0364  0.0206  0.0090  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2438 0.2580 0.2555 0.0363  0.0201  0.0061  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.2888 0.3355 0.3057 0.0431  0.0258  0.0072  26   ARG A N   
87    C CA  . ARG A 28   ? 0.2864 0.3423 0.3061 0.0442  0.0273  0.0087  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3330 0.4001 0.3508 0.0451  0.0299  0.0104  26   ARG A C   
89    O O   . ARG A 28   ? 0.2722 0.3386 0.2867 0.0438  0.0305  0.0119  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3373 0.3900 0.3593 0.0405  0.0272  0.0138  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.3386 0.3916 0.3591 0.0368  0.0286  0.0192  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.3562 0.4056 0.3795 0.0333  0.0281  0.0235  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.3967 0.4349 0.4193 0.0311  0.0260  0.0229  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.3919 0.4251 0.4162 0.0315  0.0242  0.0209  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.3989 0.4364 0.4262 0.0340  0.0240  0.0192  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.3794 0.4035 0.4026 0.0294  0.0224  0.0207  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.2799 0.3581 0.2998 0.0473  0.0314  0.0105  27   PRO A N   
98    C CA  . PRO A 29   ? 0.3059 0.3961 0.3243 0.0476  0.0340  0.0134  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2558 0.3440 0.2739 0.0429  0.0348  0.0206  27   PRO A C   
100   O O   . PRO A 29   ? 0.3057 0.3882 0.3264 0.0400  0.0341  0.0239  27   PRO A O   
101   C CB  . PRO A 29   ? 0.3121 0.4138 0.3338 0.0503  0.0352  0.0128  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3171 0.4135 0.3412 0.0532  0.0331  0.0068  27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3194 0.4007 0.3434 0.0499  0.0308  0.0078  27   PRO A CD  
104   N N   . GLN A 30   ? 0.2821 0.3750 0.2975 0.0423  0.0361  0.0229  28   GLN A N   
105   C CA  . GLN A 30   ? 0.2969 0.3870 0.3124 0.0380  0.0364  0.0295  28   GLN A CA  
106   C C   . GLN A 30   ? 0.2868 0.3869 0.3059 0.0366  0.0381  0.0354  28   GLN A C   
107   O O   . GLN A 30   ? 0.3042 0.4173 0.3230 0.0385  0.0399  0.0364  28   GLN A O   
108   C CB  . GLN A 30   ? 0.2788 0.3699 0.2904 0.0378  0.0369  0.0300  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2460 0.3280 0.2543 0.0392  0.0352  0.0242  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2698 0.3377 0.2787 0.0363  0.0332  0.0243  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2697 0.3324 0.2781 0.0332  0.0329  0.0277  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.2575 0.3197 0.2678 0.0374  0.0317  0.0205  28   GLN A NE2 
113   N N   . SER A 31   ? 0.2975 0.3920 0.3201 0.0332  0.0373  0.0392  29   SER A N   
114   C CA  . SER A 31   ? 0.2783 0.3811 0.3050 0.0312  0.0385  0.0454  29   SER A CA  
115   C C   . SER A 31   ? 0.2925 0.4006 0.3191 0.0290  0.0395  0.0513  29   SER A C   
116   O O   . SER A 31   ? 0.2585 0.3622 0.2819 0.0286  0.0391  0.0508  29   SER A O   
117   C CB  . SER A 31   ? 0.2744 0.3690 0.3052 0.0280  0.0370  0.0478  29   SER A CB  
118   O OG  . SER A 31   ? 0.2378 0.3220 0.2680 0.0247  0.0355  0.0495  29   SER A OG  
119   N N   . THR A 32   ? 0.2441 0.3622 0.2746 0.0276  0.0407  0.0574  30   THR A N   
120   C CA  . THR A 32   ? 0.2405 0.3635 0.2723 0.0248  0.0413  0.0643  30   THR A CA  
121   C C   . THR A 32   ? 0.2209 0.3308 0.2536 0.0212  0.0393  0.0662  30   THR A C   
122   O O   . THR A 32   ? 0.2555 0.3645 0.2864 0.0202  0.0392  0.0682  30   THR A O   
123   C CB  . THR A 32   ? 0.2878 0.4217 0.3252 0.0231  0.0424  0.0711  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3569 0.5046 0.3933 0.0267  0.0445  0.0693  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.2801 0.4184 0.3199 0.0198  0.0426  0.0790  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2618 0.3617 0.2972 0.0193  0.0376  0.0654  31   LEU A N   
127   C CA  . LEU A 33   ? 0.2329 0.3208 0.2694 0.0160  0.0356  0.0665  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2574 0.3368 0.2883 0.0174  0.0349  0.0611  31   LEU A C   
129   O O   . LEU A 33   ? 0.2215 0.2955 0.2520 0.0156  0.0340  0.0626  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2428 0.3234 0.2832 0.0139  0.0339  0.0662  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2387 0.3255 0.2859 0.0113  0.0340  0.0727  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.2236 0.3042 0.2741 0.0099  0.0324  0.0713  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.2808 0.3666 0.3317 0.0079  0.0331  0.0786  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.2205 0.2984 0.2477 0.0206  0.0350  0.0548  32   ARG A N   
135   C CA  . ARG A 34   ? 0.2439 0.3144 0.2661 0.0220  0.0343  0.0499  32   ARG A CA  
136   C C   . ARG A 34   ? 0.2188 0.2955 0.2379 0.0231  0.0355  0.0509  32   ARG A C   
137   O O   . ARG A 34   ? 0.2240 0.2946 0.2408 0.0224  0.0347  0.0501  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2496 0.3181 0.2694 0.0252  0.0340  0.0434  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2645 0.3240 0.2863 0.0240  0.0323  0.0416  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2539 0.3016 0.2742 0.0217  0.0305  0.0406  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2478 0.2908 0.2636 0.0236  0.0300  0.0358  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.2678 0.3058 0.2824 0.0252  0.0288  0.0312  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.2761 0.3134 0.2934 0.0254  0.0282  0.0306  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.2488 0.2826 0.2600 0.0266  0.0282  0.0274  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2348 0.3245 0.2540 0.0251  0.0373  0.0525  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2345 0.3319 0.2507 0.0263  0.0385  0.0536  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2580 0.3545 0.2763 0.0228  0.0381  0.0602  33   ARG A C   
148   O O   . ARG A 35   ? 0.2322 0.3288 0.2475 0.0230  0.0381  0.0603  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2541 0.3672 0.2702 0.0290  0.0406  0.0542  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.2752 0.3897 0.2887 0.0333  0.0408  0.0465  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.3694 0.5001 0.3832 0.0364  0.0429  0.0464  33   ARG A CD  
152   N NE  . ARG A 35   ? 0.4373 0.5682 0.4487 0.0408  0.0426  0.0380  33   ARG A NE  
153   C CZ  . ARG A 35   ? 0.4926 0.6253 0.4998 0.0438  0.0426  0.0329  33   ARG A CZ  
154   N NH1 . ARG A 35   ? 0.4998 0.6357 0.5042 0.0430  0.0431  0.0353  33   ARG A NH1 
155   N NH2 . ARG A 35   ? 0.5299 0.6609 0.5361 0.0476  0.0417  0.0250  33   ARG A NH2 
156   N N   . ALA A 36   ? 0.2217 0.3173 0.2456 0.0195  0.0376  0.0658  34   ALA A N   
157   C CA  . ALA A 36   ? 0.2373 0.3313 0.2644 0.0161  0.0367  0.0721  34   ALA A CA  
158   C C   . ALA A 36   ? 0.2463 0.3265 0.2720 0.0147  0.0348  0.0693  34   ALA A C   
159   O O   . ALA A 36   ? 0.2592 0.3381 0.2854 0.0132  0.0342  0.0725  34   ALA A O   
160   C CB  . ALA A 36   ? 0.2279 0.3240 0.2622 0.0129  0.0362  0.0784  34   ALA A CB  
161   N N   . ILE A 37   ? 0.2149 0.2854 0.2391 0.0153  0.0337  0.0637  35   ILE A N   
162   C CA  . ILE A 37   ? 0.1907 0.2495 0.2127 0.0145  0.0321  0.0603  35   ILE A CA  
163   C C   . ILE A 37   ? 0.1998 0.2600 0.2163 0.0168  0.0328  0.0575  35   ILE A C   
164   O O   . ILE A 37   ? 0.1985 0.2553 0.2145 0.0157  0.0321  0.0588  35   ILE A O   
165   C CB  . ILE A 37   ? 0.1877 0.2379 0.2088 0.0149  0.0311  0.0550  35   ILE A CB  
166   C CG1 . ILE A 37   ? 0.2207 0.2691 0.2474 0.0124  0.0302  0.0579  35   ILE A CG1 
167   C CG2 . ILE A 37   ? 0.1897 0.2291 0.2078 0.0145  0.0296  0.0512  35   ILE A CG2 
168   C CD1 . ILE A 37   ? 0.1834 0.2258 0.2094 0.0130  0.0293  0.0533  35   ILE A CD1 
169   N N   . THR A 38   ? 0.2164 0.2815 0.2290 0.0202  0.0339  0.0531  36   THR A N   
170   C CA  . THR A 38   ? 0.2222 0.2884 0.2297 0.0226  0.0342  0.0495  36   THR A CA  
171   C C   . THR A 38   ? 0.2285 0.3028 0.2358 0.0221  0.0351  0.0544  36   THR A C   
172   O O   . THR A 38   ? 0.2257 0.2973 0.2302 0.0223  0.0347  0.0534  36   THR A O   
173   C CB  . THR A 38   ? 0.2345 0.3060 0.2392 0.0264  0.0351  0.0441  36   THR A CB  
174   O OG1 . THR A 38   ? 0.2206 0.2850 0.2265 0.0265  0.0341  0.0407  36   THR A OG1 
175   C CG2 . THR A 38   ? 0.2286 0.2992 0.2284 0.0288  0.0349  0.0392  36   THR A CG2 
176   N N   . ALA A 39   ? 0.2135 0.2980 0.2241 0.0213  0.0363  0.0601  37   ALA A N   
177   C CA  . ALA A 39   ? 0.2591 0.3526 0.2700 0.0207  0.0370  0.0657  37   ALA A CA  
178   C C   . ALA A 39   ? 0.2474 0.3334 0.2608 0.0175  0.0354  0.0696  37   ALA A C   
179   O O   . ALA A 39   ? 0.2518 0.3424 0.2640 0.0174  0.0356  0.0725  37   ALA A O   
180   C CB  . ALA A 39   ? 0.2421 0.3483 0.2570 0.0200  0.0384  0.0718  37   ALA A CB  
181   N N   . ALA A 40   ? 0.2239 0.2987 0.2408 0.0151  0.0337  0.0695  38   ALA A N   
182   C CA  . ALA A 40   ? 0.2267 0.2943 0.2469 0.0122  0.0320  0.0729  38   ALA A CA  
183   C C   . ALA A 40   ? 0.2324 0.2897 0.2487 0.0128  0.0309  0.0675  38   ALA A C   
184   O O   . ALA A 40   ? 0.2466 0.2977 0.2654 0.0108  0.0293  0.0694  38   ALA A O   
185   C CB  . ALA A 40   ? 0.2287 0.2905 0.2555 0.0092  0.0305  0.0756  38   ALA A CB  
186   N N   . TYR A 41   ? 0.2383 0.2940 0.2489 0.0156  0.0315  0.0609  39   TYR A N   
187   C CA  . TYR A 41   ? 0.2395 0.2850 0.2468 0.0160  0.0303  0.0555  39   TYR A CA  
188   C C   . TYR A 41   ? 0.2351 0.2782 0.2421 0.0150  0.0295  0.0574  39   TYR A C   
189   O O   . TYR A 41   ? 0.2414 0.2754 0.2499 0.0134  0.0280  0.0564  39   TYR A O   
190   C CB  . TYR A 41   ? 0.2462 0.2934 0.2480 0.0194  0.0311  0.0492  39   TYR A CB  
191   C CG  . TYR A 41   ? 0.2205 0.2573 0.2196 0.0199  0.0299  0.0431  39   TYR A CG  
192   C CD1 . TYR A 41   ? 0.2001 0.2282 0.1993 0.0182  0.0286  0.0426  39   TYR A CD1 
193   C CD2 . TYR A 41   ? 0.2203 0.2568 0.2170 0.0223  0.0301  0.0380  39   TYR A CD2 
194   C CE1 . TYR A 41   ? 0.1922 0.2121 0.1889 0.0186  0.0275  0.0375  39   TYR A CE1 
195   C CE2 . TYR A 41   ? 0.2181 0.2459 0.2128 0.0226  0.0288  0.0331  39   TYR A CE2 
196   C CZ  . TYR A 41   ? 0.1837 0.2035 0.1782 0.0207  0.0277  0.0330  39   TYR A CZ  
197   O OH  . TYR A 41   ? 0.2023 0.2144 0.1949 0.0209  0.0265  0.0286  39   TYR A OH  
198   N N   . ARG A 42   ? 0.2582 0.3102 0.2635 0.0161  0.0305  0.0599  40   ARG A N   
199   C CA  . ARG A 42   ? 0.2564 0.3072 0.2615 0.0154  0.0297  0.0621  40   ARG A CA  
200   C C   . ARG A 42   ? 0.2595 0.3194 0.2684 0.0139  0.0301  0.0701  40   ARG A C   
201   O O   . ARG A 42   ? 0.2641 0.3286 0.2715 0.0143  0.0302  0.0724  40   ARG A O   
202   C CB  . ARG A 42   ? 0.2800 0.3317 0.2786 0.0181  0.0302  0.0570  40   ARG A CB  
203   C CG  . ARG A 42   ? 0.2680 0.3087 0.2641 0.0186  0.0292  0.0502  40   ARG A CG  
204   C CD  . ARG A 42   ? 0.2830 0.3246 0.2734 0.0214  0.0295  0.0445  40   ARG A CD  
205   N NE  . ARG A 42   ? 0.2733 0.3071 0.2623 0.0220  0.0289  0.0388  40   ARG A NE  
206   C CZ  . ARG A 42   ? 0.2467 0.2705 0.2355 0.0209  0.0275  0.0363  40   ARG A CZ  
207   N NH1 . ARG A 42   ? 0.2330 0.2530 0.2227 0.0193  0.0267  0.0382  40   ARG A NH1 
208   N NH2 . ARG A 42   ? 0.2427 0.2608 0.2308 0.0213  0.0270  0.0321  40   ARG A NH2 
209   N N   . ARG A 43   ? 0.2535 0.3158 0.2679 0.0120  0.0300  0.0747  41   ARG A N   
210   C CA  . ARG A 43   ? 0.2268 0.2981 0.2460 0.0103  0.0301  0.0832  41   ARG A CA  
211   C C   . ARG A 43   ? 0.2591 0.3259 0.2817 0.0083  0.0282  0.0870  41   ARG A C   
212   O O   . ARG A 43   ? 0.2541 0.3095 0.2788 0.0071  0.0265  0.0845  41   ARG A O   
213   C CB  . ARG A 43   ? 0.2353 0.3075 0.2608 0.0082  0.0298  0.0871  41   ARG A CB  
214   C CG  . ARG A 43   ? 0.2686 0.3494 0.3006 0.0058  0.0295  0.0967  41   ARG A CG  
215   C CD  . ARG A 43   ? 0.3028 0.3864 0.3399 0.0043  0.0297  0.0996  41   ARG A CD  
216   N NE  . ARG A 43   ? 0.2730 0.3649 0.3052 0.0071  0.0321  0.0963  41   ARG A NE  
217   C CZ  . ARG A 43   ? 0.2422 0.3341 0.2761 0.0070  0.0326  0.0949  41   ARG A CZ  
218   N NH1 . ARG A 43   ? 0.2861 0.3697 0.3258 0.0045  0.0308  0.0960  41   ARG A NH1 
219   N NH2 . ARG A 43   ? 0.2818 0.3823 0.3116 0.0098  0.0347  0.0921  41   ARG A NH2 
220   N N   . PRO A 44   ? 0.2760 0.3520 0.2996 0.0079  0.0285  0.0931  42   PRO A N   
221   C CA  . PRO A 44   ? 0.2946 0.3664 0.3222 0.0060  0.0265  0.0972  42   PRO A CA  
222   C C   . PRO A 44   ? 0.2487 0.3118 0.2850 0.0029  0.0241  0.1001  42   PRO A C   
223   O O   . PRO A 44   ? 0.2626 0.3281 0.3038 0.0014  0.0240  0.1035  42   PRO A O   
224   C CB  . PRO A 44   ? 0.3085 0.3942 0.3370 0.0058  0.0273  0.1049  42   PRO A CB  
225   C CG  . PRO A 44   ? 0.3221 0.4182 0.3434 0.0089  0.0300  0.1015  42   PRO A CG  
226   C CD  . PRO A 44   ? 0.3150 0.4061 0.3357 0.0095  0.0306  0.0963  42   PRO A CD  
227   N N   . GLU A 45   ? 0.2905 0.3437 0.3288 0.0021  0.0220  0.0984  43   GLU A N   
228   C CA  . GLU A 45   ? 0.2687 0.3126 0.3152 -0.0004 0.0195  0.0995  43   GLU A CA  
229   C C   . GLU A 45   ? 0.2819 0.3312 0.3377 -0.0032 0.0181  0.1090  43   GLU A C   
230   O O   . GLU A 45   ? 0.3063 0.3519 0.3689 -0.0052 0.0166  0.1105  43   GLU A O   
231   C CB  . GLU A 45   ? 0.3013 0.3352 0.3481 -0.0003 0.0176  0.0958  43   GLU A CB  
232   C CG  . GLU A 45   ? 0.3204 0.3432 0.3724 -0.0017 0.0153  0.0924  43   GLU A CG  
233   C CD  . GLU A 45   ? 0.2763 0.2898 0.3250 -0.0006 0.0145  0.0854  43   GLU A CD  
234   O OE1 . GLU A 45   ? 0.2713 0.2861 0.3133 0.0013  0.0157  0.0828  43   GLU A OE1 
235   O OE2 . GLU A 45   ? 0.2564 0.2616 0.3095 -0.0016 0.0126  0.0825  43   GLU A OE2 
236   N N   . THR A 46   ? 0.3003 0.3589 0.3568 -0.0035 0.0183  0.1157  44   THR A N   
237   C CA  . THR A 46   ? 0.2993 0.3643 0.3649 -0.0063 0.0170  0.1257  44   THR A CA  
238   C C   . THR A 46   ? 0.3146 0.3878 0.3813 -0.0069 0.0186  0.1286  44   THR A C   
239   O O   . THR A 46   ? 0.3087 0.3843 0.3845 -0.0097 0.0170  0.1359  44   THR A O   
240   C CB  . THR A 46   ? 0.2747 0.3495 0.3398 -0.0063 0.0172  0.1324  44   THR A CB  
241   O OG1 . THR A 46   ? 0.3048 0.3890 0.3598 -0.0034 0.0204  0.1294  44   THR A OG1 
242   C CG2 . THR A 46   ? 0.3228 0.3892 0.3898 -0.0065 0.0149  0.1314  44   THR A CG2 
243   N N   . GLU A 47   ? 0.3085 0.3860 0.3669 -0.0043 0.0215  0.1232  45   GLU A N   
244   C CA  . GLU A 47   ? 0.3119 0.3970 0.3714 -0.0046 0.0230  0.1252  45   GLU A CA  
245   C C   . GLU A 47   ? 0.2633 0.3383 0.3256 -0.0054 0.0220  0.1206  45   GLU A C   
246   O O   . GLU A 47   ? 0.2804 0.3593 0.3479 -0.0070 0.0219  0.1244  45   GLU A O   
247   C CB  . GLU A 47   ? 0.3379 0.4330 0.3879 -0.0012 0.0264  0.1214  45   GLU A CB  
248   C CG  . GLU A 47   ? 0.4094 0.5161 0.4561 -0.0002 0.0275  0.1256  45   GLU A CG  
249   C CD  . GLU A 47   ? 0.4350 0.5524 0.4729 0.0033  0.0306  0.1214  45   GLU A CD  
250   O OE1 . GLU A 47   ? 0.4121 0.5291 0.4478 0.0046  0.0319  0.1166  45   GLU A OE1 
251   O OE2 . GLU A 47   ? 0.5071 0.6333 0.5406 0.0048  0.0316  0.1227  45   GLU A OE2 
252   N N   . CYS A 48   ? 0.2745 0.3374 0.3339 -0.0044 0.0211  0.1128  46   CYS A N   
253   C CA  . CYS A 48   ? 0.2748 0.3288 0.3363 -0.0051 0.0201  0.1080  46   CYS A CA  
254   C C   . CYS A 48   ? 0.2691 0.3177 0.3417 -0.0085 0.0169  0.1126  46   CYS A C   
255   O O   . CYS A 48   ? 0.2472 0.2937 0.3240 -0.0097 0.0163  0.1124  46   CYS A O   
256   C CB  . CYS A 48   ? 0.2546 0.2981 0.3101 -0.0032 0.0200  0.0988  46   CYS A CB  
257   S SG  . CYS A 48   ? 0.2790 0.3269 0.3226 0.0007  0.0232  0.0923  46   CYS A SG  
258   N N   . LEU A 49   ? 0.2691 0.3149 0.3470 -0.0099 0.0147  0.1164  47   LEU A N   
259   C CA  . LEU A 49   ? 0.2784 0.3157 0.3666 -0.0126 0.0111  0.1181  47   LEU A CA  
260   C C   . LEU A 49   ? 0.2702 0.3128 0.3685 -0.0156 0.0097  0.1264  47   LEU A C   
261   O O   . LEU A 49   ? 0.2785 0.3148 0.3832 -0.0172 0.0075  0.1251  47   LEU A O   
262   C CB  . LEU A 49   ? 0.2991 0.3309 0.3907 -0.0130 0.0087  0.1190  47   LEU A CB  
263   C CG  . LEU A 49   ? 0.3077 0.3279 0.3958 -0.0115 0.0078  0.1098  47   LEU A CG  
264   C CD1 . LEU A 49   ? 0.2999 0.3114 0.3947 -0.0129 0.0053  0.1063  47   LEU A CD1 
265   C CD2 . LEU A 49   ? 0.2685 0.2894 0.3444 -0.0085 0.0110  0.1025  47   LEU A CD2 
266   N N   . PRO A 50   ? 0.2967 0.3511 0.3969 -0.0165 0.0106  0.1351  48   PRO A N   
267   C CA  . PRO A 50   ? 0.2791 0.3383 0.3904 -0.0199 0.0087  0.1441  48   PRO A CA  
268   C C   . PRO A 50   ? 0.2726 0.3314 0.3856 -0.0205 0.0091  0.1420  48   PRO A C   
269   O O   . PRO A 50   ? 0.3068 0.3608 0.4301 -0.0232 0.0061  0.1446  48   PRO A O   
270   C CB  . PRO A 50   ? 0.3060 0.3803 0.4156 -0.0199 0.0109  0.1526  48   PRO A CB  
271   C CG  . PRO A 50   ? 0.3131 0.3867 0.4158 -0.0178 0.0116  0.1500  48   PRO A CG  
272   C CD  . PRO A 50   ? 0.3034 0.3671 0.3973 -0.0149 0.0128  0.1380  48   PRO A CD  
273   N N   . PRO A 51   ? 0.2707 0.3341 0.3746 -0.0181 0.0125  0.1373  49   PRO A N   
274   C CA  . PRO A 51   ? 0.3028 0.3649 0.4089 -0.0188 0.0126  0.1351  49   PRO A CA  
275   C C   . PRO A 51   ? 0.2792 0.3273 0.3877 -0.0192 0.0100  0.1279  49   PRO A C   
276   O O   . PRO A 51   ? 0.2686 0.3141 0.3837 -0.0211 0.0083  0.1284  49   PRO A O   
277   C CB  . PRO A 51   ? 0.2893 0.3587 0.3847 -0.0156 0.0166  0.1307  49   PRO A CB  
278   C CG  . PRO A 51   ? 0.3014 0.3710 0.3881 -0.0130 0.0182  0.1272  49   PRO A CG  
279   C CD  . PRO A 51   ? 0.2846 0.3555 0.3770 -0.0148 0.0163  0.1342  49   PRO A CD  
280   N N   . LEU A 52   ? 0.2854 0.3249 0.3888 -0.0174 0.0097  0.1211  50   LEU A N   
281   C CA  . LEU A 52   ? 0.2770 0.3042 0.3826 -0.0177 0.0072  0.1141  50   LEU A CA  
282   C C   . LEU A 52   ? 0.2554 0.2772 0.3736 -0.0206 0.0030  0.1181  50   LEU A C   
283   O O   . LEU A 52   ? 0.2740 0.2895 0.3982 -0.0220 0.0005  0.1154  50   LEU A O   
284   C CB  . LEU A 52   ? 0.2705 0.2913 0.3674 -0.0150 0.0081  0.1063  50   LEU A CB  
285   C CG  . LEU A 52   ? 0.2829 0.3077 0.3678 -0.0120 0.0118  0.1015  50   LEU A CG  
286   C CD1 . LEU A 52   ? 0.3055 0.3240 0.3833 -0.0098 0.0122  0.0949  50   LEU A CD1 
287   C CD2 . LEU A 52   ? 0.3225 0.3468 0.4054 -0.0116 0.0127  0.0976  50   LEU A CD2 
288   N N   . VAL A 53   ? 0.2654 0.2897 0.3881 -0.0216 0.0018  0.1245  51   VAL A N   
289   C CA  . VAL A 53   ? 0.2855 0.3054 0.4215 -0.0246 -0.0026 0.1294  51   VAL A CA  
290   C C   . VAL A 53   ? 0.2896 0.3133 0.4348 -0.0274 -0.0040 0.1350  51   VAL A C   
291   O O   . VAL A 53   ? 0.2808 0.2973 0.4354 -0.0293 -0.0076 0.1338  51   VAL A O   
292   C CB  . VAL A 53   ? 0.2547 0.2787 0.3939 -0.0252 -0.0034 0.1367  51   VAL A CB  
293   C CG1 . VAL A 53   ? 0.3184 0.3395 0.4724 -0.0284 -0.0081 0.1428  51   VAL A CG1 
294   C CG2 . VAL A 53   ? 0.2753 0.2939 0.4071 -0.0226 -0.0027 0.1306  51   VAL A CG2 
295   N N   . GLU A 54   ? 0.2658 0.3010 0.4082 -0.0276 -0.0011 0.1407  52   GLU A N   
296   C CA  . GLU A 54   ? 0.2992 0.3389 0.4504 -0.0304 -0.0023 0.1466  52   GLU A CA  
297   C C   . GLU A 54   ? 0.2673 0.3007 0.4179 -0.0301 -0.0028 0.1391  52   GLU A C   
298   O O   . GLU A 54   ? 0.2962 0.3253 0.4573 -0.0327 -0.0062 0.1404  52   GLU A O   
299   C CB  . GLU A 54   ? 0.3228 0.3776 0.4703 -0.0302 0.0010  0.1532  52   GLU A CB  
300   C CG  . GLU A 54   ? 0.3257 0.3865 0.4808 -0.0323 -0.0003 0.1574  52   GLU A CG  
301   C CD  . GLU A 54   ? 0.3668 0.4252 0.5353 -0.0349 -0.0057 0.1612  52   GLU A CD  
302   O OE1 . GLU A 54   ? 0.3972 0.4558 0.5689 -0.0350 -0.0076 0.1640  52   GLU A OE1 
303   O OE2 . GLU A 54   ? 0.3729 0.4296 0.5491 -0.0367 -0.0080 0.1615  52   GLU A OE2 
304   N N   . ALA A 55   ? 0.2585 0.2911 0.3973 -0.0271 0.0004  0.1311  53   ALA A N   
305   C CA  . ALA A 55   ? 0.2861 0.3138 0.4237 -0.0267 0.0001  0.1245  53   ALA A CA  
306   C C   . ALA A 55   ? 0.2877 0.3031 0.4306 -0.0274 -0.0037 0.1184  53   ALA A C   
307   O O   . ALA A 55   ? 0.2802 0.2918 0.4273 -0.0284 -0.0054 0.1153  53   ALA A O   
308   C CB  . ALA A 55   ? 0.3178 0.3472 0.4419 -0.0233 0.0041  0.1177  53   ALA A CB  
309   N N   . ALA A 56   ? 0.2713 0.2810 0.4144 -0.0267 -0.0051 0.1165  54   ALA A N   
310   C CA  . ALA A 56   ? 0.2701 0.2687 0.4175 -0.0268 -0.0086 0.1099  54   ALA A CA  
311   C C   . ALA A 56   ? 0.3206 0.3157 0.4831 -0.0299 -0.0134 0.1149  54   ALA A C   
312   O O   . ALA A 56   ? 0.3122 0.2984 0.4800 -0.0300 -0.0168 0.1095  54   ALA A O   
313   C CB  . ALA A 56   ? 0.2888 0.2831 0.4288 -0.0244 -0.0076 0.1048  54   ALA A CB  
314   N N   . THR A 57   ? 0.2928 0.2950 0.4627 -0.0323 -0.0139 0.1250  55   THR A N   
315   C CA  . THR A 57   ? 0.2888 0.2885 0.4730 -0.0349 -0.0188 0.1298  55   THR A CA  
316   C C   . THR A 57   ? 0.3314 0.3270 0.5240 -0.0366 -0.0221 0.1269  55   THR A C   
317   O O   . THR A 57   ? 0.3218 0.3213 0.5125 -0.0373 -0.0202 0.1278  55   THR A O   
318   C CB  . THR A 57   ? 0.3118 0.3231 0.4988 -0.0359 -0.0184 0.1392  55   THR A CB  
319   O OG1 . THR A 57   ? 0.3322 0.3467 0.5124 -0.0343 -0.0162 0.1413  55   THR A OG1 
320   C CG2 . THR A 57   ? 0.3513 0.3620 0.5523 -0.0379 -0.0238 0.1425  55   THR A CG2 
321   N N   . GLN A 58   ? 0.3198 0.3078 0.5219 -0.0371 -0.0270 0.1231  56   GLN A N   
322   C CA  . GLN A 58   ? 0.3181 0.3022 0.5293 -0.0386 -0.0307 0.1201  56   GLN A CA  
323   C C   . GLN A 58   ? 0.3322 0.3166 0.5567 -0.0399 -0.0359 0.1237  56   GLN A C   
324   O O   . GLN A 58   ? 0.3464 0.3319 0.5730 -0.0395 -0.0369 0.1268  56   GLN A O   
325   C CB  . GLN A 58   ? 0.3246 0.2984 0.5345 -0.0375 -0.0319 0.1096  56   GLN A CB  
326   C CG  . GLN A 58   ? 0.2879 0.2628 0.4828 -0.0352 -0.0270 0.1042  56   GLN A CG  
327   C CD  . GLN A 58   ? 0.3180 0.2862 0.5103 -0.0337 -0.0283 0.0930  56   GLN A CD  
328   O OE1 . GLN A 58   ? 0.3036 0.2719 0.4990 -0.0348 -0.0294 0.0910  56   GLN A OE1 
329   N NE2 . GLN A 58   ? 0.3077 0.2708 0.4943 -0.0313 -0.0281 0.0857  56   GLN A NE2 
330   N N   . SER A 59   ? 0.3450 0.3284 0.5789 -0.0415 -0.0394 0.1232  57   SER A N   
331   C CA  . SER A 59   ? 0.3293 0.3133 0.5768 -0.0429 -0.0446 0.1269  57   SER A CA  
332   C C   . SER A 59   ? 0.3972 0.3728 0.6500 -0.0416 -0.0484 0.1210  57   SER A C   
333   O O   . SER A 59   ? 0.3544 0.3225 0.6021 -0.0399 -0.0478 0.1124  57   SER A O   
334   C CB  . SER A 59   ? 0.3313 0.3150 0.5875 -0.0446 -0.0477 0.1263  57   SER A CB  
335   O OG  . SER A 59   ? 0.3613 0.3359 0.6181 -0.0437 -0.0496 0.1162  57   SER A OG  
336   N N   . LYS A 60   ? 0.3538 0.3310 0.6174 -0.0424 -0.0524 0.1258  58   LYS A N   
337   C CA  . LYS A 60   ? 0.3677 0.3375 0.6382 -0.0413 -0.0565 0.1205  58   LYS A CA  
338   C C   . LYS A 60   ? 0.3686 0.3301 0.6438 -0.0406 -0.0598 0.1106  58   LYS A C   
339   O O   . LYS A 60   ? 0.3983 0.3527 0.6721 -0.0386 -0.0609 0.1022  58   LYS A O   
340   C CB  . LYS A 60   ? 0.4258 0.3993 0.7091 -0.0426 -0.0609 0.1278  58   LYS A CB  
341   N N   . GLU A 61   ? 0.3633 0.3261 0.6439 -0.0421 -0.0615 0.1111  59   GLU A N   
342   C CA  . GLU A 61   ? 0.3713 0.3272 0.6559 -0.0415 -0.0645 0.1015  59   GLU A CA  
343   C C   . GLU A 61   ? 0.3839 0.3352 0.6561 -0.0397 -0.0609 0.0929  59   GLU A C   
344   O O   . GLU A 61   ? 0.3930 0.3376 0.6664 -0.0380 -0.0630 0.0834  59   GLU A O   
345   C CB  . GLU A 61   ? 0.3636 0.3226 0.6542 -0.0435 -0.0661 0.1043  59   GLU A CB  
346   N N   . ILE A 62   ? 0.3649 0.3204 0.6255 -0.0400 -0.0553 0.0962  60   ILE A N   
347   C CA  . ILE A 62   ? 0.3534 0.3049 0.6025 -0.0385 -0.0519 0.0887  60   ILE A CA  
348   C C   . ILE A 62   ? 0.3740 0.3212 0.6183 -0.0362 -0.0511 0.0847  60   ILE A C   
349   O O   . ILE A 62   ? 0.3745 0.3157 0.6154 -0.0345 -0.0514 0.0753  60   ILE A O   
350   C CB  . ILE A 62   ? 0.3313 0.2888 0.5699 -0.0392 -0.0463 0.0937  60   ILE A CB  
351   C CG1 . ILE A 62   ? 0.3586 0.3185 0.6012 -0.0411 -0.0472 0.0942  60   ILE A CG1 
352   C CG2 . ILE A 62   ? 0.3392 0.2933 0.5653 -0.0374 -0.0423 0.0879  60   ILE A CG2 
353   C CD1 . ILE A 62   ? 0.3623 0.3278 0.5952 -0.0416 -0.0421 0.0977  60   ILE A CD1 
354   N N   . ARG A 63   ? 0.3625 0.3132 0.6063 -0.0361 -0.0501 0.0915  61   ARG A N   
355   C CA  . ARG A 63   ? 0.3497 0.2966 0.5893 -0.0340 -0.0494 0.0880  61   ARG A CA  
356   C C   . ARG A 63   ? 0.3599 0.2999 0.6082 -0.0327 -0.0545 0.0798  61   ARG A C   
357   O O   . ARG A 63   ? 0.3336 0.2684 0.5772 -0.0305 -0.0541 0.0719  61   ARG A O   
358   C CB  . ARG A 63   ? 0.3693 0.3218 0.6083 -0.0343 -0.0481 0.0971  61   ARG A CB  
359   C CG  . ARG A 63   ? 0.4030 0.3636 0.6331 -0.0352 -0.0430 0.1050  61   ARG A CG  
360   C CD  . ARG A 63   ? 0.4777 0.4435 0.7048 -0.0349 -0.0413 0.1119  61   ARG A CD  
361   N NE  . ARG A 63   ? 0.4671 0.4354 0.7061 -0.0361 -0.0455 0.1174  61   ARG A NE  
362   C CZ  . ARG A 63   ? 0.5183 0.4950 0.7623 -0.0381 -0.0459 0.1265  61   ARG A CZ  
363   N NH1 . ARG A 63   ? 0.5291 0.5127 0.7671 -0.0390 -0.0423 0.1308  61   ARG A NH1 
364   N NH2 . ARG A 63   ? 0.5551 0.5337 0.8107 -0.0392 -0.0501 0.1312  61   ARG A NH2 
365   N N   . ASP A 64   ? 0.3617 0.3021 0.6233 -0.0338 -0.0595 0.0816  62   ASP A N   
366   C CA  . ASP A 64   ? 0.3735 0.3081 0.6445 -0.0324 -0.0647 0.0735  62   ASP A CA  
367   C C   . ASP A 64   ? 0.3738 0.3037 0.6418 -0.0312 -0.0650 0.0626  62   ASP A C   
368   O O   . ASP A 64   ? 0.3425 0.2676 0.6100 -0.0289 -0.0664 0.0535  62   ASP A O   
369   C CB  . ASP A 64   ? 0.3805 0.3169 0.6667 -0.0340 -0.0700 0.0781  62   ASP A CB  
370   C CG  . ASP A 64   ? 0.3928 0.3332 0.6839 -0.0348 -0.0708 0.0874  62   ASP A CG  
371   O OD1 . ASP A 64   ? 0.3985 0.3396 0.6817 -0.0339 -0.0676 0.0891  62   ASP A OD1 
372   O OD2 . ASP A 64   ? 0.4531 0.3961 0.7564 -0.0364 -0.0748 0.0929  62   ASP A OD2 
373   N N   . ALA A 65   ? 0.3443 0.2761 0.6103 -0.0327 -0.0639 0.0633  63   ALA A N   
374   C CA  . ALA A 65   ? 0.3521 0.2804 0.6153 -0.0318 -0.0643 0.0531  63   ALA A CA  
375   C C   . ALA A 65   ? 0.3669 0.2929 0.6171 -0.0300 -0.0601 0.0476  63   ALA A C   
376   O O   . ALA A 65   ? 0.3837 0.3059 0.6325 -0.0281 -0.0613 0.0372  63   ALA A O   
377   C CB  . ALA A 65   ? 0.3558 0.2872 0.6194 -0.0340 -0.0636 0.0559  63   ALA A CB  
378   N N   . ALA A 66   ? 0.3372 0.2661 0.5778 -0.0304 -0.0551 0.0543  64   ALA A N   
379   C CA  . ALA A 66   ? 0.3739 0.3013 0.6016 -0.0285 -0.0510 0.0496  64   ALA A CA  
380   C C   . ALA A 66   ? 0.3839 0.3068 0.6128 -0.0261 -0.0526 0.0441  64   ALA A C   
381   O O   . ALA A 66   ? 0.3410 0.2631 0.5616 -0.0235 -0.0513 0.0348  64   ALA A O   
382   C CB  . ALA A 66   ? 0.3469 0.2807 0.5634 -0.0287 -0.0453 0.0578  64   ALA A CB  
383   N N   . ALA A 67   ? 0.3265 0.2501 0.5624 -0.0262 -0.0547 0.0490  65   ALA A N   
384   C CA  . ALA A 67   ? 0.3885 0.3086 0.6258 -0.0238 -0.0564 0.0438  65   ALA A CA  
385   C C   . ALA A 67   ? 0.3609 0.2772 0.6044 -0.0221 -0.0606 0.0325  65   ALA A C   
386   O O   . ALA A 67   ? 0.4075 0.3210 0.6472 -0.0196 -0.0604 0.0244  65   ALA A O   
387   C CB  . ALA A 67   ? 0.3893 0.3114 0.6344 -0.0244 -0.0584 0.0516  65   ALA A CB  
388   N N   . SER A 68   ? 0.3736 0.2904 0.6268 -0.0233 -0.0644 0.0317  66   SER A N   
389   C CA  . SER A 68   ? 0.4016 0.3157 0.6609 -0.0216 -0.0685 0.0207  66   SER A CA  
390   C C   . SER A 68   ? 0.4058 0.3190 0.6554 -0.0204 -0.0661 0.0117  66   SER A C   
391   O O   . SER A 68   ? 0.3818 0.2934 0.6306 -0.0179 -0.0674 0.0015  66   SER A O   
392   C CB  . SER A 68   ? 0.4020 0.3171 0.6738 -0.0231 -0.0731 0.0223  66   SER A CB  
393   O OG  . SER A 68   ? 0.4569 0.3703 0.7331 -0.0214 -0.0766 0.0112  66   SER A OG  
394   N N   . THR A 69   ? 0.3613 0.2763 0.6037 -0.0223 -0.0627 0.0154  67   THR A N   
395   C CA  . THR A 69   ? 0.3573 0.2743 0.5878 -0.0209 -0.0596 0.0077  67   THR A CA  
396   C C   . THR A 69   ? 0.3663 0.2845 0.5844 -0.0181 -0.0557 0.0044  67   THR A C   
397   O O   . THR A 69   ? 0.3653 0.2845 0.5777 -0.0157 -0.0554 -0.0053 67   THR A O   
398   C CB  . THR A 69   ? 0.3450 0.2671 0.5674 -0.0226 -0.0557 0.0135  67   THR A CB  
399   O OG1 . THR A 69   ? 0.3492 0.2704 0.5832 -0.0252 -0.0595 0.0156  67   THR A OG1 
400   C CG2 . THR A 69   ? 0.3436 0.2698 0.5513 -0.0207 -0.0519 0.0065  67   THR A CG2 
401   N N   . ALA A 70   ? 0.3568 0.2758 0.5705 -0.0184 -0.0527 0.0124  68   ALA A N   
402   C CA  . ALA A 70   ? 0.3651 0.2850 0.5677 -0.0159 -0.0493 0.0097  68   ALA A CA  
403   C C   . ALA A 70   ? 0.4099 0.3259 0.6194 -0.0137 -0.0529 0.0017  68   ALA A C   
404   O O   . ALA A 70   ? 0.3784 0.2959 0.5797 -0.0112 -0.0513 -0.0062 68   ALA A O   
405   C CB  . ALA A 70   ? 0.3630 0.2844 0.5615 -0.0167 -0.0461 0.0199  68   ALA A CB  
406   N N   . ARG A 71   ? 0.4103 0.3214 0.6353 -0.0146 -0.0580 0.0037  69   ARG A N   
407   C CA  . ARG A 71   ? 0.3899 0.2984 0.6218 -0.0122 -0.0617 -0.0041 69   ARG A CA  
408   C C   . ARG A 71   ? 0.4240 0.3328 0.6561 -0.0105 -0.0637 -0.0164 69   ARG A C   
409   O O   . ARG A 71   ? 0.4293 0.3383 0.6591 -0.0077 -0.0640 -0.0250 69   ARG A O   
410   C CB  . ARG A 71   ? 0.4095 0.3179 0.6549 -0.0129 -0.0662 0.0006  69   ARG A CB  
411   C CG  . ARG A 71   ? 0.4677 0.3752 0.7218 -0.0103 -0.0709 -0.0086 69   ARG A CG  
412   C CD  . ARG A 71   ? 0.4316 0.3389 0.6995 -0.0110 -0.0754 -0.0033 69   ARG A CD  
413   N NE  . ARG A 71   ? 0.4171 0.3243 0.6834 -0.0114 -0.0737 0.0046  69   ARG A NE  
414   C CZ  . ARG A 71   ? 0.4858 0.3919 0.7494 -0.0091 -0.0731 0.0010  69   ARG A CZ  
415   N NH1 . ARG A 71   ? 0.4596 0.3652 0.7221 -0.0061 -0.0741 -0.0104 69   ARG A NH1 
416   N NH2 . ARG A 71   ? 0.4672 0.3737 0.7293 -0.0097 -0.0715 0.0090  69   ARG A NH2 
417   N N   . LYS A 72   ? 0.3885 0.2985 0.6233 -0.0120 -0.0650 -0.0174 70   LYS A N   
418   C CA  . LYS A 72   ? 0.4058 0.3173 0.6406 -0.0105 -0.0669 -0.0290 70   LYS A CA  
419   C C   . LYS A 72   ? 0.4330 0.3501 0.6508 -0.0086 -0.0618 -0.0341 70   LYS A C   
420   O O   . LYS A 72   ? 0.3968 0.3157 0.6128 -0.0060 -0.0627 -0.0444 70   LYS A O   
421   C CB  . LYS A 72   ? 0.3808 0.2934 0.6210 -0.0127 -0.0690 -0.0278 70   LYS A CB  
422   C CG  . LYS A 72   ? 0.4191 0.3345 0.6565 -0.0115 -0.0700 -0.0389 70   LYS A CG  
423   C CD  . LYS A 72   ? 0.4549 0.3711 0.7008 -0.0133 -0.0735 -0.0388 70   LYS A CD  
424   C CE  . LYS A 72   ? 0.5163 0.4359 0.7607 -0.0116 -0.0752 -0.0509 70   LYS A CE  
425   N NZ  . LYS A 72   ? 0.6299 0.5504 0.8847 -0.0124 -0.0796 -0.0523 70   LYS A NZ  
426   N N   . LEU A 73   ? 0.4044 0.3248 0.6098 -0.0097 -0.0565 -0.0271 71   LEU A N   
427   C CA  . LEU A 73   ? 0.4104 0.3360 0.5998 -0.0080 -0.0516 -0.0308 71   LEU A CA  
428   C C   . LEU A 73   ? 0.4005 0.3259 0.5860 -0.0055 -0.0505 -0.0342 71   LEU A C   
429   O O   . LEU A 73   ? 0.4066 0.3357 0.5853 -0.0033 -0.0494 -0.0423 71   LEU A O   
430   C CB  . LEU A 73   ? 0.3842 0.3127 0.5626 -0.0096 -0.0465 -0.0221 71   LEU A CB  
431   C CG  . LEU A 73   ? 0.3621 0.2923 0.5419 -0.0119 -0.0466 -0.0182 71   LEU A CG  
432   C CD1 . LEU A 73   ? 0.3810 0.3138 0.5507 -0.0131 -0.0415 -0.0092 71   LEU A CD1 
433   C CD2 . LEU A 73   ? 0.3667 0.3006 0.5427 -0.0112 -0.0471 -0.0265 71   LEU A CD2 
434   N N   . ILE A 74   ? 0.3636 0.2852 0.5535 -0.0058 -0.0507 -0.0279 72   ILE A N   
435   C CA  . ILE A 74   ? 0.4320 0.3533 0.6182 -0.0035 -0.0495 -0.0302 72   ILE A CA  
436   C C   . ILE A 74   ? 0.4284 0.3482 0.6235 -0.0012 -0.0540 -0.0406 72   ILE A C   
437   O O   . ILE A 74   ? 0.4385 0.3609 0.6276 0.0013  -0.0526 -0.0469 72   ILE A O   
438   C CB  . ILE A 74   ? 0.3869 0.3049 0.5761 -0.0046 -0.0490 -0.0204 72   ILE A CB  
439   C CG1 . ILE A 74   ? 0.3999 0.3211 0.5775 -0.0061 -0.0438 -0.0118 72   ILE A CG1 
440   C CG2 . ILE A 74   ? 0.4162 0.3330 0.6049 -0.0022 -0.0489 -0.0233 72   ILE A CG2 
441   C CD1 . ILE A 74   ? 0.4273 0.3466 0.6079 -0.0075 -0.0432 -0.0014 72   ILE A CD1 
442   N N   . GLU A 75   ? 0.4260 0.3419 0.6359 -0.0018 -0.0594 -0.0426 73   GLU A N   
443   C CA  . GLU A 75   ? 0.4442 0.3590 0.6633 0.0006  -0.0640 -0.0535 73   GLU A CA  
444   C C   . GLU A 75   ? 0.4545 0.3758 0.6653 0.0024  -0.0628 -0.0637 73   GLU A C   
445   O O   . GLU A 75   ? 0.4544 0.3783 0.6640 0.0053  -0.0634 -0.0726 73   GLU A O   
446   C CB  . GLU A 75   ? 0.4195 0.3329 0.6532 -0.0002 -0.0693 -0.0521 73   GLU A CB  
447   C CG  . GLU A 75   ? 0.4141 0.3248 0.6561 -0.0006 -0.0711 -0.0444 73   GLU A CG  
448   C CD  . GLU A 75   ? 0.4817 0.3913 0.7371 -0.0023 -0.0756 -0.0399 73   GLU A CD  
449   O OE1 . GLU A 75   ? 0.4713 0.3820 0.7297 -0.0032 -0.0773 -0.0425 73   GLU A OE1 
450   O OE2 . GLU A 75   ? 0.5285 0.4366 0.7916 -0.0028 -0.0775 -0.0335 73   GLU A OE2 
451   N N   . ALA A 76   ? 0.4624 0.3871 0.6670 0.0007  -0.0610 -0.0623 74   ALA A N   
452   C CA  . ALA A 76   ? 0.4410 0.3728 0.6364 0.0022  -0.0593 -0.0708 74   ALA A CA  
453   C C   . ALA A 76   ? 0.4642 0.4009 0.6450 0.0037  -0.0542 -0.0712 74   ALA A C   
454   O O   . ALA A 76   ? 0.5120 0.4541 0.6886 0.0060  -0.0540 -0.0802 74   ALA A O   
455   C CB  . ALA A 76   ? 0.4354 0.3697 0.6270 -0.0002 -0.0582 -0.0678 74   ALA A CB  
456   N N   . LEU A 77   ? 0.4560 0.3914 0.6291 0.0024  -0.0501 -0.0617 75   LEU A N   
457   C CA  . LEU A 77   ? 0.4532 0.3928 0.6130 0.0037  -0.0453 -0.0615 75   LEU A CA  
458   C C   . LEU A 77   ? 0.4934 0.4327 0.6562 0.0064  -0.0467 -0.0676 75   LEU A C   
459   O O   . LEU A 77   ? 0.5259 0.4710 0.6811 0.0083  -0.0449 -0.0739 75   LEU A O   
460   C CB  . LEU A 77   ? 0.4185 0.3559 0.5715 0.0019  -0.0414 -0.0504 75   LEU A CB  
461   C CG  . LEU A 77   ? 0.4391 0.3791 0.5833 -0.0001 -0.0380 -0.0447 75   LEU A CG  
462   C CD1 . LEU A 77   ? 0.4390 0.3773 0.5774 -0.0012 -0.0344 -0.0349 75   LEU A CD1 
463   C CD2 . LEU A 77   ? 0.4391 0.3860 0.5720 0.0008  -0.0354 -0.0502 75   LEU A CD2 
464   N N   . ARG A 78   ? 0.4930 0.4261 0.6673 0.0066  -0.0499 -0.0654 76   ARG A N   
465   C CA  . ARG A 78   ? 0.4933 0.4259 0.6714 0.0092  -0.0513 -0.0707 76   ARG A CA  
466   C C   . ARG A 78   ? 0.4820 0.4175 0.6669 0.0117  -0.0553 -0.0831 76   ARG A C   
467   O O   . ARG A 78   ? 0.5728 0.5112 0.7565 0.0144  -0.0553 -0.0897 76   ARG A O   
468   C CB  . ARG A 78   ? 0.4734 0.3984 0.6622 0.0086  -0.0539 -0.0643 76   ARG A CB  
469   C CG  . ARG A 78   ? 0.4712 0.3951 0.6519 0.0070  -0.0496 -0.0533 76   ARG A CG  
470   C CD  . ARG A 78   ? 0.4540 0.3718 0.6448 0.0065  -0.0520 -0.0469 76   ARG A CD  
471   N NE  . ARG A 78   ? 0.4678 0.3862 0.6491 0.0061  -0.0478 -0.0393 76   ARG A NE  
472   C CZ  . ARG A 78   ? 0.4710 0.3855 0.6578 0.0056  -0.0487 -0.0325 76   ARG A CZ  
473   N NH1 . ARG A 78   ? 0.4758 0.3851 0.6779 0.0053  -0.0538 -0.0314 76   ARG A NH1 
474   N NH2 . ARG A 78   ? 0.5323 0.4484 0.7094 0.0054  -0.0446 -0.0265 76   ARG A NH2 
475   N N   . GLY A 79   ? 0.4973 0.4325 0.6891 0.0109  -0.0585 -0.0867 77   GLY A N   
476   C CA  . GLY A 79   ? 0.5589 0.4978 0.7567 0.0134  -0.0623 -0.0991 77   GLY A CA  
477   C C   . GLY A 79   ? 0.5938 0.5428 0.7792 0.0147  -0.0592 -0.1060 77   GLY A C   
478   O O   . GLY A 79   ? 0.5684 0.5221 0.7576 0.0169  -0.0620 -0.1168 77   GLY A O   
479   N N   . LYS A 80   ? 0.5879 0.5405 0.7588 0.0134  -0.0537 -0.0999 78   LYS A N   
480   C CA  . LYS A 80   ? 0.5993 0.5617 0.7582 0.0142  -0.0506 -0.1048 78   LYS A CA  
481   C C   . LYS A 80   ? 0.5970 0.5617 0.7426 0.0139  -0.0451 -0.0989 78   LYS A C   
482   O O   . LYS A 80   ? 0.6624 0.6322 0.8035 0.0160  -0.0438 -0.1036 78   LYS A O   
483   C CB  . LYS A 80   ? 0.6169 0.5819 0.7725 0.0121  -0.0503 -0.1037 78   LYS A CB  
484   C CG  . LYS A 80   ? 0.5737 0.5351 0.7227 0.0091  -0.0467 -0.0918 78   LYS A CG  
485   C CD  . LYS A 80   ? 0.5188 0.4818 0.6669 0.0071  -0.0471 -0.0905 78   LYS A CD  
486   C CE  . LYS A 80   ? 0.5193 0.4795 0.6605 0.0044  -0.0434 -0.0790 78   LYS A CE  
487   N NZ  . LYS A 80   ? 0.4029 0.3647 0.5433 0.0024  -0.0436 -0.0770 78   LYS A NZ  
488   N N   . GLY A 85   ? 0.5116 0.5317 0.5752 0.0184  -0.0164 -0.0984 83   GLY A N   
489   C CA  . GLY A 85   ? 0.4394 0.4699 0.4932 0.0177  -0.0136 -0.0979 83   GLY A CA  
490   C C   . GLY A 85   ? 0.4110 0.4440 0.4604 0.0182  -0.0113 -0.0962 83   GLY A C   
491   O O   . GLY A 85   ? 0.4057 0.4475 0.4552 0.0201  -0.0114 -0.1024 83   GLY A O   
492   N N   . VAL A 86   ? 0.4351 0.4610 0.4807 0.0166  -0.0092 -0.0878 84   VAL A N   
493   C CA  . VAL A 86   ? 0.4167 0.4435 0.4591 0.0170  -0.0073 -0.0857 84   VAL A CA  
494   C C   . VAL A 86   ? 0.4217 0.4460 0.4723 0.0197  -0.0094 -0.0910 84   VAL A C   
495   O O   . VAL A 86   ? 0.3919 0.4221 0.4416 0.0212  -0.0087 -0.0943 84   VAL A O   
496   C CB  . VAL A 86   ? 0.4541 0.4729 0.4920 0.0149  -0.0051 -0.0761 84   VAL A CB  
497   C CG1 . VAL A 86   ? 0.4086 0.4265 0.4449 0.0156  -0.0037 -0.0742 84   VAL A CG1 
498   C CG2 . VAL A 86   ? 0.4491 0.4717 0.4787 0.0126  -0.0030 -0.0713 84   VAL A CG2 
499   N N   . GLU A 87   ? 0.4370 0.4528 0.4962 0.0203  -0.0121 -0.0918 85   GLU A N   
500   C CA  . GLU A 87   ? 0.4609 0.4734 0.5292 0.0229  -0.0147 -0.0967 85   GLU A CA  
501   C C   . GLU A 87   ? 0.4275 0.4500 0.4989 0.0255  -0.0162 -0.1071 85   GLU A C   
502   O O   . GLU A 87   ? 0.4463 0.4711 0.5206 0.0277  -0.0167 -0.1111 85   GLU A O   
503   C CB  . GLU A 87   ? 0.5340 0.5363 0.6117 0.0227  -0.0177 -0.0955 85   GLU A CB  
504   N N   . GLY A 88   ? 0.4014 0.4306 0.4721 0.0255  -0.0171 -0.1119 86   GLY A N   
505   C CA  . GLY A 88   ? 0.3777 0.4177 0.4511 0.0282  -0.0186 -0.1224 86   GLY A CA  
506   C C   . GLY A 88   ? 0.3899 0.4414 0.4552 0.0286  -0.0156 -0.1232 86   GLY A C   
507   O O   . GLY A 88   ? 0.3596 0.4188 0.4279 0.0314  -0.0165 -0.1310 86   GLY A O   
508   N N   . LEU A 89   ? 0.3725 0.4257 0.4280 0.0259  -0.0122 -0.1153 87   LEU A N   
509   C CA  . LEU A 89   ? 0.3559 0.4192 0.4038 0.0257  -0.0093 -0.1144 87   LEU A CA  
510   C C   . LEU A 89   ? 0.3397 0.3996 0.3897 0.0269  -0.0088 -0.1135 87   LEU A C   
511   O O   . LEU A 89   ? 0.3237 0.3926 0.3737 0.0289  -0.0085 -0.1187 87   LEU A O   
512   C CB  . LEU A 89   ? 0.3669 0.4308 0.4051 0.0222  -0.0064 -0.1055 87   LEU A CB  
513   C CG  . LEU A 89   ? 0.4041 0.4770 0.4341 0.0210  -0.0033 -0.1018 87   LEU A CG  
514   C CD1 . LEU A 89   ? 0.4032 0.4920 0.4309 0.0220  -0.0032 -0.1083 87   LEU A CD1 
515   C CD2 . LEU A 89   ? 0.4249 0.4936 0.4477 0.0176  -0.0011 -0.0920 87   LEU A CD2 
516   N N   . VAL A 90   ? 0.3803 0.4275 0.4320 0.0259  -0.0087 -0.1069 88   VAL A N   
517   C CA  . VAL A 90   ? 0.3314 0.3743 0.3860 0.0271  -0.0086 -0.1059 88   VAL A CA  
518   C C   . VAL A 90   ? 0.3568 0.4021 0.4207 0.0308  -0.0116 -0.1153 88   VAL A C   
519   O O   . VAL A 90   ? 0.3508 0.4007 0.4153 0.0325  -0.0111 -0.1182 88   VAL A O   
520   C CB  . VAL A 90   ? 0.3001 0.3291 0.3563 0.0256  -0.0087 -0.0979 88   VAL A CB  
521   C CG1 . VAL A 90   ? 0.3446 0.3687 0.4056 0.0272  -0.0094 -0.0976 88   VAL A CG1 
522   C CG2 . VAL A 90   ? 0.3399 0.3676 0.3866 0.0225  -0.0056 -0.0891 88   VAL A CG2 
523   N N   . GLN A 91   ? 0.3711 0.4134 0.4428 0.0320  -0.0148 -0.1206 89   GLN A N   
524   C CA  . GLN A 91   ? 0.3706 0.4145 0.4525 0.0356  -0.0182 -0.1302 89   GLN A CA  
525   C C   . GLN A 91   ? 0.3567 0.4160 0.4363 0.0378  -0.0177 -0.1389 89   GLN A C   
526   O O   . GLN A 91   ? 0.3753 0.4389 0.4590 0.0406  -0.0184 -0.1444 89   GLN A O   
527   C CB  . GLN A 91   ? 0.3681 0.4051 0.4594 0.0361  -0.0221 -0.1336 89   GLN A CB  
528   N N   . GLU A 92   ? 0.3589 0.4275 0.4321 0.0366  -0.0164 -0.1400 90   GLU A N   
529   C CA  . GLU A 92   ? 0.3725 0.4572 0.4439 0.0387  -0.0162 -0.1487 90   GLU A CA  
530   C C   . GLU A 92   ? 0.3448 0.4377 0.4106 0.0391  -0.0132 -0.1473 90   GLU A C   
531   O O   . GLU A 92   ? 0.3347 0.4379 0.4033 0.0421  -0.0139 -0.1555 90   GLU A O   
532   C CB  . GLU A 92   ? 0.3535 0.4466 0.4181 0.0368  -0.0151 -0.1484 90   GLU A CB  
533   C CG  . GLU A 92   ? 0.3528 0.4645 0.4132 0.0384  -0.0141 -0.1554 90   GLU A CG  
534   C CD  . GLU A 92   ? 0.4303 0.5505 0.4854 0.0368  -0.0137 -0.1559 90   GLU A CD  
535   O OE1 . GLU A 92   ? 0.4125 0.5240 0.4659 0.0341  -0.0137 -0.1496 90   GLU A OE1 
536   O OE2 . GLU A 92   ? 0.4118 0.5480 0.4645 0.0383  -0.0134 -0.1626 90   GLU A OE2 
537   N N   . TYR A 93   ? 0.3228 0.4117 0.3811 0.0360  -0.0102 -0.1371 91   TYR A N   
538   C CA  . TYR A 93   ? 0.3263 0.4229 0.3791 0.0358  -0.0074 -0.1348 91   TYR A CA  
539   C C   . TYR A 93   ? 0.3331 0.4199 0.3893 0.0364  -0.0073 -0.1312 91   TYR A C   
540   O O   . TYR A 93   ? 0.3023 0.3932 0.3535 0.0356  -0.0049 -0.1275 91   TYR A O   
541   C CB  . TYR A 93   ? 0.2887 0.3899 0.3306 0.0321  -0.0040 -0.1264 91   TYR A CB  
542   C CG  . TYR A 93   ? 0.3015 0.4166 0.3395 0.0319  -0.0037 -0.1305 91   TYR A CG  
543   C CD1 . TYR A 93   ? 0.2755 0.4074 0.3109 0.0332  -0.0026 -0.1355 91   TYR A CD1 
544   C CD2 . TYR A 93   ? 0.3438 0.4561 0.3810 0.0304  -0.0046 -0.1296 91   TYR A CD2 
545   C CE1 . TYR A 93   ? 0.3070 0.4528 0.3387 0.0331  -0.0023 -0.1393 91   TYR A CE1 
546   C CE2 . TYR A 93   ? 0.3389 0.4645 0.3726 0.0303  -0.0045 -0.1334 91   TYR A CE2 
547   C CZ  . TYR A 93   ? 0.3257 0.4681 0.3566 0.0316  -0.0033 -0.1381 91   TYR A CZ  
548   O OH  . TYR A 93   ? 0.3512 0.5079 0.3784 0.0314  -0.0032 -0.1418 91   TYR A OH  
549   N N   . SER A 94   ? 0.3153 0.3896 0.3799 0.0375  -0.0101 -0.1319 92   SER A N   
550   C CA  . SER A 94   ? 0.3125 0.3777 0.3815 0.0383  -0.0106 -0.1289 92   SER A CA  
551   C C   . SER A 94   ? 0.2764 0.3369 0.3373 0.0351  -0.0075 -0.1182 92   SER A C   
552   O O   . SER A 94   ? 0.2923 0.3531 0.3525 0.0356  -0.0064 -0.1163 92   SER A O   
553   C CB  . SER A 94   ? 0.3179 0.3911 0.3918 0.0419  -0.0115 -0.1368 92   SER A CB  
554   O OG  . SER A 94   ? 0.3677 0.4466 0.4489 0.0450  -0.0144 -0.1476 92   SER A OG  
555   N N   . LEU A 95   ? 0.2711 0.3273 0.3263 0.0320  -0.0062 -0.1115 93   LEU A N   
556   C CA  . LEU A 95   ? 0.2799 0.3324 0.3273 0.0291  -0.0033 -0.1019 93   LEU A CA  
557   C C   . LEU A 95   ? 0.2724 0.3115 0.3233 0.0287  -0.0041 -0.0964 93   LEU A C   
558   O O   . LEU A 95   ? 0.2918 0.3223 0.3492 0.0293  -0.0064 -0.0967 93   LEU A O   
559   C CB  . LEU A 95   ? 0.2544 0.3073 0.2949 0.0261  -0.0019 -0.0970 93   LEU A CB  
560   C CG  . LEU A 95   ? 0.2494 0.3161 0.2856 0.0259  -0.0010 -0.1010 93   LEU A CG  
561   C CD1 . LEU A 95   ? 0.2981 0.3637 0.3276 0.0227  0.0004  -0.0947 93   LEU A CD1 
562   C CD2 . LEU A 95   ? 0.2593 0.3376 0.2915 0.0263  0.0009  -0.1022 93   LEU A CD2 
563   N N   . SER A 96   ? 0.2199 0.2579 0.2667 0.0278  -0.0021 -0.0911 94   SER A N   
564   C CA  . SER A 96   ? 0.2548 0.2811 0.3024 0.0267  -0.0022 -0.0842 94   SER A CA  
565   C C   . SER A 96   ? 0.2391 0.2603 0.2813 0.0238  -0.0010 -0.0775 94   SER A C   
566   O O   . SER A 96   ? 0.2430 0.2699 0.2802 0.0224  0.0001  -0.0776 94   SER A O   
567   C CB  . SER A 96   ? 0.2662 0.2935 0.3103 0.0264  -0.0005 -0.0806 94   SER A CB  
568   O OG  . SER A 96   ? 0.2445 0.2772 0.2797 0.0240  0.0023  -0.0765 94   SER A OG  
569   N N   . SER A 97   ? 0.2418 0.2527 0.2851 0.0229  -0.0013 -0.0715 95   SER A N   
570   C CA  . SER A 97   ? 0.2759 0.2820 0.3142 0.0203  -0.0001 -0.0652 95   SER A CA  
571   C C   . SER A 97   ? 0.2434 0.2545 0.2726 0.0183  0.0027  -0.0612 95   SER A C   
572   O O   . SER A 97   ? 0.2343 0.2476 0.2590 0.0166  0.0036  -0.0596 95   SER A O   
573   C CB  . SER A 97   ? 0.3036 0.2994 0.3445 0.0199  -0.0007 -0.0595 95   SER A CB  
574   O OG  . SER A 97   ? 0.3490 0.3398 0.3984 0.0210  -0.0034 -0.0618 95   SER A OG  
575   N N   . GLN A 98   ? 0.2190 0.2320 0.2458 0.0184  0.0039  -0.0596 96   GLN A N   
576   C CA  . GLN A 98   ? 0.2227 0.2402 0.2417 0.0163  0.0062  -0.0557 96   GLN A CA  
577   C C   . GLN A 98   ? 0.2137 0.2422 0.2300 0.0159  0.0068  -0.0593 96   GLN A C   
578   O O   . GLN A 98   ? 0.2144 0.2457 0.2250 0.0137  0.0081  -0.0557 96   GLN A O   
579   C CB  . GLN A 98   ? 0.2159 0.2337 0.2337 0.0165  0.0070  -0.0538 96   GLN A CB  
580   C CG  . GLN A 98   ? 0.2379 0.2458 0.2558 0.0161  0.0069  -0.0482 96   GLN A CG  
581   C CD  . GLN A 98   ? 0.2289 0.2330 0.2414 0.0137  0.0081  -0.0423 96   GLN A CD  
582   O OE1 . GLN A 98   ? 0.2558 0.2561 0.2689 0.0132  0.0077  -0.0413 96   GLN A OE1 
583   N NE2 . GLN A 98   ? 0.2477 0.2526 0.2553 0.0123  0.0095  -0.0384 96   GLN A NE2 
584   N N   . GLU A 99   ? 0.2022 0.2374 0.2226 0.0181  0.0057  -0.0665 97   GLU A N   
585   C CA  . GLU A 99   ? 0.1737 0.2206 0.1916 0.0179  0.0062  -0.0703 97   GLU A CA  
586   C C   . GLU A 99   ? 0.2115 0.2575 0.2283 0.0168  0.0057  -0.0700 97   GLU A C   
587   O O   . GLU A 99   ? 0.2145 0.2673 0.2261 0.0150  0.0069  -0.0682 97   GLU A O   
588   C CB  . GLU A 99   ? 0.1886 0.2430 0.2117 0.0209  0.0050  -0.0789 97   GLU A CB  
589   C CG  . GLU A 99   ? 0.2016 0.2600 0.2248 0.0218  0.0058  -0.0792 97   GLU A CG  
590   C CD  . GLU A 99   ? 0.2212 0.2856 0.2508 0.0253  0.0043  -0.0879 97   GLU A CD  
591   O OE1 . GLU A 99   ? 0.2107 0.2746 0.2457 0.0271  0.0022  -0.0938 97   GLU A OE1 
592   O OE2 . GLU A 99   ? 0.2049 0.2744 0.2347 0.0262  0.0050  -0.0891 97   GLU A OE2 
593   N N   . GLY A 100  ? 0.2127 0.2506 0.2349 0.0177  0.0039  -0.0715 98   GLY A N   
594   C CA  . GLY A 100  ? 0.1989 0.2353 0.2202 0.0166  0.0034  -0.0708 98   GLY A CA  
595   C C   . GLY A 100  ? 0.2242 0.2576 0.2389 0.0137  0.0052  -0.0629 98   GLY A C   
596   O O   . GLY A 100  ? 0.2152 0.2534 0.2261 0.0122  0.0057  -0.0619 98   GLY A O   
597   N N   . VAL A 101  ? 0.2172 0.2427 0.2307 0.0129  0.0059  -0.0573 99   VAL A N   
598   C CA  . VAL A 101  ? 0.2161 0.2382 0.2239 0.0105  0.0074  -0.0502 99   VAL A CA  
599   C C   . VAL A 101  ? 0.2506 0.2818 0.2527 0.0089  0.0089  -0.0486 99   VAL A C   
600   O O   . VAL A 101  ? 0.2173 0.2507 0.2156 0.0070  0.0095  -0.0454 99   VAL A O   
601   C CB  . VAL A 101  ? 0.2123 0.2254 0.2202 0.0103  0.0078  -0.0454 99   VAL A CB  
602   C CG1 . VAL A 101  ? 0.2161 0.2267 0.2184 0.0081  0.0092  -0.0389 99   VAL A CG1 
603   C CG2 . VAL A 101  ? 0.2488 0.2535 0.2625 0.0115  0.0062  -0.0459 99   VAL A CG2 
604   N N   . ALA A 102  ? 0.2185 0.2555 0.2204 0.0096  0.0095  -0.0504 100  ALA A N   
605   C CA  . ALA A 102  ? 0.1909 0.2372 0.1880 0.0080  0.0108  -0.0484 100  ALA A CA  
606   C C   . ALA A 102  ? 0.1924 0.2487 0.1881 0.0075  0.0107  -0.0512 100  ALA A C   
607   O O   . ALA A 102  ? 0.2118 0.2733 0.2032 0.0053  0.0116  -0.0472 100  ALA A O   
608   C CB  . ALA A 102  ? 0.2169 0.2686 0.2148 0.0090  0.0113  -0.0505 100  ALA A CB  
609   N N   . LEU A 103  ? 0.1965 0.2563 0.1963 0.0097  0.0095  -0.0582 101  LEU A N   
610   C CA  . LEU A 103  ? 0.1826 0.2523 0.1813 0.0095  0.0091  -0.0617 101  LEU A CA  
611   C C   . LEU A 103  ? 0.2242 0.2901 0.2204 0.0075  0.0091  -0.0573 101  LEU A C   
612   O O   . LEU A 103  ? 0.2461 0.3202 0.2384 0.0058  0.0097  -0.0554 101  LEU A O   
613   C CB  . LEU A 103  ? 0.2058 0.2778 0.2103 0.0125  0.0074  -0.0704 101  LEU A CB  
614   C CG  . LEU A 103  ? 0.2252 0.3078 0.2292 0.0128  0.0067  -0.0752 101  LEU A CG  
615   C CD1 . LEU A 103  ? 0.2050 0.3027 0.2044 0.0119  0.0081  -0.0753 101  LEU A CD1 
616   C CD2 . LEU A 103  ? 0.2254 0.3083 0.2363 0.0159  0.0045  -0.0842 101  LEU A CD2 
617   N N   . MET A 104  ? 0.2345 0.2884 0.2330 0.0076  0.0083  -0.0554 102  MET A N   
618   C CA  . MET A 104  ? 0.2205 0.2708 0.2170 0.0059  0.0082  -0.0515 102  MET A CA  
619   C C   . MET A 104  ? 0.2314 0.2812 0.2226 0.0033  0.0097  -0.0440 102  MET A C   
620   O O   . MET A 104  ? 0.2687 0.3213 0.2571 0.0016  0.0098  -0.0411 102  MET A O   
621   C CB  . MET A 104  ? 0.2556 0.2941 0.2563 0.0066  0.0071  -0.0512 102  MET A CB  
622   C CG  . MET A 104  ? 0.2345 0.2730 0.2416 0.0090  0.0052  -0.0585 102  MET A CG  
623   S SD  . MET A 104  ? 0.3628 0.4130 0.3701 0.0095  0.0041  -0.0649 102  MET A SD  
624   C CE  . MET A 104  ? 0.3699 0.4150 0.3753 0.0074  0.0039  -0.0601 102  MET A CE  
625   N N   . CYS A 105  ? 0.2261 0.2725 0.2162 0.0030  0.0105  -0.0408 103  CYS A N   
626   C CA  . CYS A 105  ? 0.2366 0.2831 0.2224 0.0006  0.0116  -0.0341 103  CYS A CA  
627   C C   . CYS A 105  ? 0.2856 0.3450 0.2685 -0.0008 0.0120  -0.0336 103  CYS A C   
628   O O   . CYS A 105  ? 0.2845 0.3458 0.2645 -0.0031 0.0122  -0.0286 103  CYS A O   
629   C CB  . CYS A 105  ? 0.2463 0.2875 0.2321 0.0008  0.0122  -0.0316 103  CYS A CB  
630   S SG  . CYS A 105  ? 0.2492 0.2761 0.2375 0.0019  0.0118  -0.0301 103  CYS A SG  
631   N N   . LEU A 106  ? 0.2579 0.3265 0.2417 0.0004  0.0122  -0.0385 104  LEU A N   
632   C CA  . LEU A 106  ? 0.2534 0.3361 0.2345 -0.0009 0.0127  -0.0383 104  LEU A CA  
633   C C   . LEU A 106  ? 0.3025 0.3901 0.2826 -0.0015 0.0120  -0.0391 104  LEU A C   
634   O O   . LEU A 106  ? 0.2989 0.3934 0.2758 -0.0038 0.0123  -0.0347 104  LEU A O   
635   C CB  . LEU A 106  ? 0.2723 0.3646 0.2550 0.0011  0.0129  -0.0445 104  LEU A CB  
636   C CG  . LEU A 106  ? 0.2832 0.3922 0.2633 0.0001  0.0134  -0.0453 104  LEU A CG  
637   C CD1 . LEU A 106  ? 0.3410 0.4546 0.3176 -0.0030 0.0144  -0.0376 104  LEU A CD1 
638   C CD2 . LEU A 106  ? 0.2922 0.4111 0.2746 0.0027  0.0134  -0.0531 104  LEU A CD2 
639   N N   . ALA A 107  ? 0.2458 0.3302 0.2289 0.0005  0.0110  -0.0447 105  ALA A N   
640   C CA  . ALA A 107  ? 0.2819 0.3709 0.2643 0.0000  0.0102  -0.0460 105  ALA A CA  
641   C C   . ALA A 107  ? 0.3564 0.4394 0.3365 -0.0025 0.0103  -0.0386 105  ALA A C   
642   O O   . ALA A 107  ? 0.3394 0.4298 0.3168 -0.0042 0.0102  -0.0362 105  ALA A O   
643   C CB  . ALA A 107  ? 0.2603 0.3449 0.2475 0.0024  0.0087  -0.0529 105  ALA A CB  
644   N N   . GLU A 108  ? 0.3109 0.3807 0.2919 -0.0026 0.0104  -0.0352 106  GLU A N   
645   C CA  . GLU A 108  ? 0.3352 0.3988 0.3143 -0.0046 0.0104  -0.0284 106  GLU A CA  
646   C C   . GLU A 108  ? 0.4035 0.4744 0.3791 -0.0071 0.0110  -0.0226 106  GLU A C   
647   O O   . GLU A 108  ? 0.3994 0.4728 0.3734 -0.0090 0.0106  -0.0187 106  GLU A O   
648   C CB  . GLU A 108  ? 0.3411 0.3913 0.3216 -0.0040 0.0106  -0.0260 106  GLU A CB  
649   C CG  . GLU A 108  ? 0.3445 0.3879 0.3235 -0.0057 0.0107  -0.0195 106  GLU A CG  
650   C CD  . GLU A 108  ? 0.3907 0.4240 0.3702 -0.0053 0.0111  -0.0168 106  GLU A CD  
651   O OE1 . GLU A 108  ? 0.3468 0.3762 0.3285 -0.0035 0.0112  -0.0200 106  GLU A OE1 
652   O OE2 . GLU A 108  ? 0.3989 0.4285 0.3769 -0.0067 0.0112  -0.0116 106  GLU A OE2 
653   N N   . ALA A 109  ? 0.3308 0.4054 0.3058 -0.0073 0.0117  -0.0220 107  ALA A N   
654   C CA  . ALA A 109  ? 0.4026 0.4840 0.3751 -0.0099 0.0121  -0.0161 107  ALA A CA  
655   C C   . ALA A 109  ? 0.4453 0.5414 0.4161 -0.0110 0.0119  -0.0165 107  ALA A C   
656   O O   . ALA A 109  ? 0.4669 0.5670 0.4359 -0.0135 0.0116  -0.0106 107  ALA A O   
657   C CB  . ALA A 109  ? 0.3863 0.4690 0.3590 -0.0098 0.0128  -0.0157 107  ALA A CB  
658   N N   . LEU A 110  ? 0.3999 0.5043 0.3712 -0.0091 0.0121  -0.0235 108  LEU A N   
659   C CA  . LEU A 110  ? 0.4083 0.5279 0.3778 -0.0099 0.0119  -0.0247 108  LEU A CA  
660   C C   . LEU A 110  ? 0.4738 0.5926 0.4427 -0.0108 0.0110  -0.0231 108  LEU A C   
661   O O   . LEU A 110  ? 0.4852 0.6146 0.4517 -0.0127 0.0107  -0.0199 108  LEU A O   
662   C CB  . LEU A 110  ? 0.3579 0.4857 0.3288 -0.0071 0.0120  -0.0338 108  LEU A CB  
663   C CG  . LEU A 110  ? 0.3824 0.5154 0.3536 -0.0064 0.0130  -0.0353 108  LEU A CG  
664   C CD1 . LEU A 110  ? 0.3194 0.4575 0.2933 -0.0030 0.0128  -0.0451 108  LEU A CD1 
665   C CD2 . LEU A 110  ? 0.4037 0.5510 0.3719 -0.0090 0.0137  -0.0300 108  LEU A CD2 
666   N N   . LEU A 111  ? 0.4315 0.5381 0.4024 -0.0095 0.0103  -0.0250 109  LEU A N   
667   C CA  . LEU A 111  ? 0.4667 0.5718 0.4372 -0.0104 0.0094  -0.0233 109  LEU A CA  
668   C C   . LEU A 111  ? 0.5139 0.6150 0.4829 -0.0131 0.0092  -0.0144 109  LEU A C   
669   O O   . LEU A 111  ? 0.5617 0.6648 0.5300 -0.0144 0.0085  -0.0118 109  LEU A O   
670   C CB  . LEU A 111  ? 0.4145 0.5081 0.3880 -0.0083 0.0087  -0.0276 109  LEU A CB  
671   C CG  . LEU A 111  ? 0.4172 0.5161 0.3931 -0.0058 0.0082  -0.0367 109  LEU A CG  
672   C CD1 . LEU A 111  ? 0.3872 0.4743 0.3672 -0.0039 0.0073  -0.0405 109  LEU A CD1 
673   C CD2 . LEU A 111  ? 0.4354 0.5483 0.4096 -0.0062 0.0075  -0.0392 109  LEU A CD2 
674   N N   . ARG A 112  ? 0.5039 0.5995 0.4728 -0.0141 0.0098  -0.0098 110  ARG A N   
675   C CA  . ARG A 112  ? 0.5443 0.6377 0.5125 -0.0167 0.0093  -0.0016 110  ARG A CA  
676   C C   . ARG A 112  ? 0.5921 0.6998 0.5584 -0.0192 0.0091  0.0026  110  ARG A C   
677   O O   . ARG A 112  ? 0.6040 0.7113 0.5703 -0.0216 0.0083  0.0098  110  ARG A O   
678   C CB  . ARG A 112  ? 0.5349 0.6187 0.5041 -0.0169 0.0097  0.0016  110  ARG A CB  
679   C CG  . ARG A 112  ? 0.5188 0.5879 0.4897 -0.0152 0.0097  0.0001  110  ARG A CG  
680   C CD  . ARG A 112  ? 0.5884 0.6488 0.5599 -0.0159 0.0096  0.0047  110  ARG A CD  
681   N NE  . ARG A 112  ? 0.5808 0.6429 0.5524 -0.0155 0.0104  0.0035  110  ARG A NE  
682   C CZ  . ARG A 112  ? 0.6430 0.6993 0.6156 -0.0133 0.0110  -0.0010 110  ARG A CZ  
683   N NH1 . ARG A 112  ? 0.6417 0.6906 0.6154 -0.0113 0.0110  -0.0045 110  ARG A NH1 
684   N NH2 . ARG A 112  ? 0.6026 0.6610 0.5753 -0.0131 0.0116  -0.0017 110  ARG A NH2 
685   N N   . ILE A 113  ? 0.6005 0.7213 0.5656 -0.0186 0.0097  -0.0016 111  ILE A N   
686   C CA  . ILE A 113  ? 0.5930 0.7298 0.5561 -0.0208 0.0095  0.0019  111  ILE A CA  
687   C C   . ILE A 113  ? 0.6443 0.7856 0.6065 -0.0209 0.0086  0.0007  111  ILE A C   
688   O O   . ILE A 113  ? 0.6197 0.7632 0.5820 -0.0186 0.0086  -0.0069 111  ILE A O   
689   C CB  . ILE A 113  ? 0.5579 0.7079 0.5199 -0.0199 0.0105  -0.0026 111  ILE A CB  
690   C CG1 . ILE A 113  ? 0.5570 0.7038 0.5200 -0.0205 0.0113  0.0001  111  ILE A CG1 
691   C CG2 . ILE A 113  ? 0.5996 0.7682 0.5594 -0.0218 0.0104  -0.0002 111  ILE A CG2 
692   C CD1 . ILE A 113  ? 0.4605 0.6196 0.4229 -0.0194 0.0124  -0.0044 111  ILE A CD1 
693   N N   . PRO A 114  ? 0.6845 0.8270 0.6463 -0.0235 0.0076  0.0079  112  PRO A N   
694   C CA  . PRO A 114  ? 0.6795 0.8244 0.6408 -0.0235 0.0065  0.0072  112  PRO A CA  
695   C C   . PRO A 114  ? 0.6788 0.8410 0.6379 -0.0231 0.0066  0.0028  112  PRO A C   
696   O O   . PRO A 114  ? 0.7125 0.8752 0.6718 -0.0212 0.0062  -0.0037 112  PRO A O   
697   C CB  . PRO A 114  ? 0.7133 0.8565 0.6751 -0.0266 0.0053  0.0169  112  PRO A CB  
698   C CG  . PRO A 114  ? 0.7025 0.8365 0.6660 -0.0274 0.0056  0.0214  112  PRO A CG  
699   C CD  . PRO A 114  ? 0.6763 0.8163 0.6390 -0.0263 0.0070  0.0172  112  PRO A CD  
700   N N   . ASP A 115  ? 0.6774 0.8543 0.6348 -0.0250 0.0070  0.0062  113  ASP A N   
701   C CA  . ASP A 115  ? 0.6824 0.8777 0.6375 -0.0247 0.0070  0.0022  113  ASP A CA  
702   C C   . ASP A 115  ? 0.6384 0.8366 0.5937 -0.0212 0.0080  -0.0084 113  ASP A C   
703   O O   . ASP A 115  ? 0.6450 0.8417 0.6009 -0.0205 0.0090  -0.0098 113  ASP A O   
704   C CB  . ASP A 115  ? 0.6452 0.8565 0.5985 -0.0277 0.0072  0.0094  113  ASP A CB  
705   C CG  . ASP A 115  ? 0.6693 0.9014 0.6199 -0.0271 0.0075  0.0048  113  ASP A CG  
706   O OD1 . ASP A 115  ? 0.6610 0.8973 0.6106 -0.0265 0.0065  0.0018  113  ASP A OD1 
707   O OD2 . ASP A 115  ? 0.6365 0.8810 0.5859 -0.0272 0.0086  0.0039  113  ASP A OD2 
708   N N   . THR A 116  ? 0.6475 0.8501 0.6026 -0.0192 0.0073  -0.0159 114  THR A N   
709   C CA  . THR A 116  ? 0.6236 0.8288 0.5799 -0.0157 0.0077  -0.0267 114  THR A CA  
710   C C   . THR A 116  ? 0.6273 0.8500 0.5817 -0.0155 0.0088  -0.0287 114  THR A C   
711   O O   . THR A 116  ? 0.6365 0.8581 0.5924 -0.0133 0.0097  -0.0341 114  THR A O   
712   C CB  . THR A 116  ? 0.6098 0.8172 0.5668 -0.0138 0.0064  -0.0341 114  THR A CB  
713   O OG1 . THR A 116  ? 0.6701 0.8606 0.6293 -0.0138 0.0055  -0.0325 114  THR A OG1 
714   C CG2 . THR A 116  ? 0.6378 0.8484 0.5969 -0.0101 0.0064  -0.0457 114  THR A CG2 
715   N N   . ALA A 117  ? 0.5988 0.8387 0.5503 -0.0178 0.0088  -0.0241 115  ALA A N   
716   C CA  . ALA A 117  ? 0.6002 0.8586 0.5498 -0.0177 0.0099  -0.0257 115  ALA A CA  
717   C C   . ALA A 117  ? 0.5733 0.8280 0.5236 -0.0191 0.0112  -0.0201 115  ALA A C   
718   O O   . ALA A 117  ? 0.5609 0.8228 0.5114 -0.0175 0.0123  -0.0247 115  ALA A O   
719   C CB  . ALA A 117  ? 0.5965 0.8747 0.5427 -0.0202 0.0096  -0.0209 115  ALA A CB  
720   N N   . THR A 118  ? 0.5763 0.8198 0.5272 -0.0220 0.0109  -0.0103 116  THR A N   
721   C CA  . THR A 118  ? 0.5944 0.8327 0.5465 -0.0233 0.0117  -0.0051 116  THR A CA  
722   C C   . THR A 118  ? 0.5429 0.7685 0.4973 -0.0201 0.0124  -0.0125 116  THR A C   
723   O O   . THR A 118  ? 0.5529 0.7820 0.5078 -0.0196 0.0135  -0.0135 116  THR A O   
724   C CB  . THR A 118  ? 0.6065 0.8330 0.5597 -0.0266 0.0108  0.0055  116  THR A CB  
725   O OG1 . THR A 118  ? 0.6747 0.9125 0.6263 -0.0296 0.0098  0.0126  116  THR A OG1 
726   C CG2 . THR A 118  ? 0.5197 0.7427 0.4743 -0.0282 0.0114  0.0112  116  THR A CG2 
727   N N   . ARG A 119  ? 0.5752 0.7863 0.5313 -0.0179 0.0117  -0.0174 117  ARG A N   
728   C CA  . ARG A 119  ? 0.5656 0.7643 0.5243 -0.0148 0.0121  -0.0241 117  ARG A CA  
729   C C   . ARG A 119  ? 0.5495 0.7601 0.5087 -0.0119 0.0127  -0.0335 117  ARG A C   
730   O O   . ARG A 119  ? 0.5143 0.7227 0.4750 -0.0105 0.0136  -0.0360 117  ARG A O   
731   C CB  . ARG A 119  ? 0.5089 0.6923 0.4696 -0.0133 0.0110  -0.0273 117  ARG A CB  
732   C CG  . ARG A 119  ? 0.4809 0.6493 0.4448 -0.0107 0.0112  -0.0321 117  ARG A CG  
733   C CD  . ARG A 119  ? 0.4861 0.6430 0.4523 -0.0091 0.0100  -0.0361 117  ARG A CD  
734   N NE  . ARG A 119  ? 0.5389 0.6896 0.5040 -0.0114 0.0094  -0.0292 117  ARG A NE  
735   C CZ  . ARG A 119  ? 0.5548 0.7078 0.5196 -0.0115 0.0083  -0.0304 117  ARG A CZ  
736   N NH1 . ARG A 119  ? 0.5138 0.6746 0.4794 -0.0095 0.0076  -0.0385 117  ARG A NH1 
737   N NH2 . ARG A 119  ? 0.6225 0.7699 0.5865 -0.0137 0.0077  -0.0235 117  ARG A NH2 
738   N N   . ASP A 120  ? 0.5322 0.7556 0.4903 -0.0107 0.0122  -0.0392 118  ASP A N   
739   C CA  . ASP A 120  ? 0.5166 0.7516 0.4757 -0.0075 0.0125  -0.0493 118  ASP A CA  
740   C C   . ASP A 120  ? 0.5204 0.7704 0.4777 -0.0084 0.0140  -0.0470 118  ASP A C   
741   O O   . ASP A 120  ? 0.5123 0.7658 0.4714 -0.0058 0.0146  -0.0536 118  ASP A O   
742   C CB  . ASP A 120  ? 0.5142 0.7609 0.4723 -0.0062 0.0114  -0.0556 118  ASP A CB  
743   C CG  . ASP A 120  ? 0.5548 0.7868 0.5153 -0.0051 0.0098  -0.0585 118  ASP A CG  
744   O OD1 . ASP A 120  ? 0.5076 0.7211 0.4703 -0.0052 0.0097  -0.0558 118  ASP A OD1 
745   O OD2 . ASP A 120  ? 0.5500 0.7894 0.5101 -0.0042 0.0086  -0.0635 118  ASP A OD2 
746   N N   . ALA A 121  ? 0.5239 0.7830 0.4783 -0.0122 0.0144  -0.0373 119  ALA A N   
747   C CA  . ALA A 121  ? 0.5535 0.8268 0.5066 -0.0135 0.0158  -0.0338 119  ALA A CA  
748   C C   . ALA A 121  ? 0.5316 0.7922 0.4871 -0.0135 0.0166  -0.0314 119  ALA A C   
749   O O   . ALA A 121  ? 0.5373 0.8055 0.4934 -0.0122 0.0177  -0.0348 119  ALA A O   
750   C CB  . ALA A 121  ? 0.5742 0.8588 0.5245 -0.0180 0.0158  -0.0229 119  ALA A CB  
751   N N   . LEU A 122  ? 0.5441 0.7856 0.5008 -0.0149 0.0160  -0.0259 120  LEU A N   
752   C CA  . LEU A 122  ? 0.5211 0.7500 0.4799 -0.0148 0.0165  -0.0240 120  LEU A CA  
753   C C   . LEU A 122  ? 0.5081 0.7317 0.4695 -0.0106 0.0168  -0.0343 120  LEU A C   
754   O O   . LEU A 122  ? 0.5340 0.7587 0.4967 -0.0097 0.0176  -0.0355 120  LEU A O   
755   C CB  . LEU A 122  ? 0.5468 0.7565 0.5065 -0.0166 0.0156  -0.0173 120  LEU A CB  
756   C CG  . LEU A 122  ? 0.5169 0.7156 0.4785 -0.0172 0.0160  -0.0135 120  LEU A CG  
757   C CD1 . LEU A 122  ? 0.5885 0.7996 0.5492 -0.0204 0.0166  -0.0062 120  LEU A CD1 
758   C CD2 . LEU A 122  ? 0.5131 0.6928 0.4758 -0.0183 0.0151  -0.0087 120  LEU A CD2 
759   N N   . ILE A 123  ? 0.5080 0.7260 0.4708 -0.0079 0.0158  -0.0417 121  ILE A N   
760   C CA  . ILE A 123  ? 0.5072 0.7205 0.4734 -0.0038 0.0156  -0.0517 121  ILE A CA  
761   C C   . ILE A 123  ? 0.5189 0.7506 0.4851 -0.0019 0.0164  -0.0579 121  ILE A C   
762   O O   . ILE A 123  ? 0.4563 0.6869 0.4247 -0.0001 0.0171  -0.0611 121  ILE A O   
763   C CB  . ILE A 123  ? 0.4847 0.6906 0.4528 -0.0016 0.0141  -0.0582 121  ILE A CB  
764   C CG1 . ILE A 123  ? 0.4659 0.6526 0.4346 -0.0030 0.0134  -0.0526 121  ILE A CG1 
765   C CG2 . ILE A 123  ? 0.4061 0.6104 0.3786 0.0027  0.0135  -0.0692 121  ILE A CG2 
766   C CD1 . ILE A 123  ? 0.4124 0.5932 0.3827 -0.0017 0.0119  -0.0570 121  ILE A CD1 
767   N N   . ARG A 124  ? 0.5158 0.7655 0.4795 -0.0022 0.0165  -0.0596 122  ARG A N   
768   C CA  . ARG A 124  ? 0.4948 0.7631 0.4585 0.0002  0.0172  -0.0671 122  ARG A CA  
769   C C   . ARG A 124  ? 0.5482 0.8263 0.5107 -0.0016 0.0189  -0.0618 122  ARG A C   
770   O O   . ARG A 124  ? 0.5571 0.8408 0.5217 0.0010  0.0195  -0.0678 122  ARG A O   
771   C CB  . ARG A 124  ? 0.4845 0.7705 0.4456 0.0001  0.0167  -0.0699 122  ARG A CB  
772   N N   . ASP A 125  ? 0.5657 0.8459 0.5255 -0.0060 0.0194  -0.0504 123  ASP A N   
773   C CA  . ASP A 125  ? 0.5720 0.8649 0.5306 -0.0081 0.0208  -0.0447 123  ASP A CA  
774   C C   . ASP A 125  ? 0.5843 0.8626 0.5449 -0.0093 0.0212  -0.0395 123  ASP A C   
775   O O   . ASP A 125  ? 0.6483 0.9353 0.6094 -0.0097 0.0223  -0.0381 123  ASP A O   
776   C CB  . ASP A 125  ? 0.6148 0.9185 0.5713 -0.0125 0.0204  -0.0345 123  ASP A CB  
777   C CG  . ASP A 125  ? 0.6590 0.9731 0.6157 -0.0117 0.0189  -0.0380 123  ASP A CG  
778   O OD1 . ASP A 125  ? 0.6302 0.9509 0.5894 -0.0080 0.0182  -0.0480 123  ASP A OD1 
779   O OD2 . ASP A 125  ? 0.7062 1.0218 0.6608 -0.0148 0.0182  -0.0307 123  ASP A OD2 
780   N N   . LYS A 126  ? 0.5882 0.8453 0.5501 -0.0097 0.0203  -0.0368 124  LYS A N   
781   C CA  . LYS A 126  ? 0.5860 0.8297 0.5496 -0.0112 0.0204  -0.0309 124  LYS A CA  
782   C C   . LYS A 126  ? 0.5849 0.8106 0.5516 -0.0080 0.0200  -0.0369 124  LYS A C   
783   O O   . LYS A 126  ? 0.6133 0.8367 0.5819 -0.0069 0.0206  -0.0385 124  LYS A O   
784   C CB  . LYS A 126  ? 0.6020 0.8373 0.5643 -0.0153 0.0197  -0.0200 124  LYS A CB  
785   N N   . ILE A 127  ? 0.5569 0.7702 0.5244 -0.0066 0.0189  -0.0400 125  ILE A N   
786   C CA  . ILE A 127  ? 0.5216 0.7174 0.4923 -0.0040 0.0183  -0.0444 125  ILE A CA  
787   C C   . ILE A 127  ? 0.5491 0.7503 0.5227 0.0001  0.0184  -0.0545 125  ILE A C   
788   O O   . ILE A 127  ? 0.5496 0.7448 0.5256 0.0014  0.0187  -0.0560 125  ILE A O   
789   C CB  . ILE A 127  ? 0.4597 0.6425 0.4308 -0.0036 0.0170  -0.0452 125  ILE A CB  
790   C CG1 . ILE A 127  ? 0.5385 0.7181 0.5069 -0.0074 0.0168  -0.0357 125  ILE A CG1 
791   C CG2 . ILE A 127  ? 0.4645 0.6292 0.4390 -0.0015 0.0164  -0.0478 125  ILE A CG2 
792   C CD1 . ILE A 127  ? 0.5360 0.7062 0.5044 -0.0098 0.0170  -0.0276 125  ILE A CD1 
793   N N   . ALA A 128  ? 0.5515 0.7645 0.5253 0.0021  0.0180  -0.0619 126  ALA A N   
794   C CA  . ALA A 128  ? 0.5323 0.7492 0.5098 0.0065  0.0177  -0.0727 126  ALA A CA  
795   C C   . ALA A 128  ? 0.6311 0.8599 0.6089 0.0070  0.0190  -0.0734 126  ALA A C   
796   O O   . ALA A 128  ? 0.5557 0.7811 0.5373 0.0100  0.0188  -0.0795 126  ALA A O   
797   C CB  . ALA A 128  ? 0.4700 0.6983 0.4476 0.0085  0.0168  -0.0805 126  ALA A CB  
798   N N   . ASP A 129  ? 0.9048 1.1477 0.8788 0.0040  0.0203  -0.0671 127  ASP A N   
799   C CA  . ASP A 129  ? 0.9435 1.2010 0.9178 0.0044  0.0217  -0.0679 127  ASP A CA  
800   C C   . ASP A 129  ? 0.9477 1.1943 0.9237 0.0036  0.0222  -0.0636 127  ASP A C   
801   O O   . ASP A 129  ? 0.9928 1.2473 0.9706 0.0053  0.0230  -0.0670 127  ASP A O   
802   C CB  . ASP A 129  ? 0.8893 1.1658 0.8593 0.0010  0.0228  -0.0614 127  ASP A CB  
803   N N   . GLY A 130  ? 0.7756 1.0049 0.7513 0.0014  0.0217  -0.0566 128  GLY A N   
804   C CA  . GLY A 130  ? 0.8076 1.0268 0.7849 0.0007  0.0220  -0.0528 128  GLY A CA  
805   C C   . GLY A 130  ? 0.7843 0.9843 0.7613 -0.0014 0.0212  -0.0459 128  GLY A C   
806   O O   . GLY A 130  ? 0.7140 0.9002 0.6923 0.0002  0.0202  -0.0487 128  GLY A O   
807   N N   . ASN A 131  ? 0.8403 1.0397 0.8158 -0.0050 0.0216  -0.0368 129  ASN A N   
808   C CA  . ASN A 131  ? 0.8333 1.0150 0.8089 -0.0069 0.0208  -0.0305 129  ASN A CA  
809   C C   . ASN A 131  ? 0.7478 0.9223 0.7218 -0.0081 0.0199  -0.0281 129  ASN A C   
810   O O   . ASN A 131  ? 0.7832 0.9656 0.7550 -0.0109 0.0199  -0.0228 129  ASN A O   
811   C CB  . ASN A 131  ? 0.8305 1.0151 0.8056 -0.0105 0.0211  -0.0218 129  ASN A CB  
812   N N   . TRP A 132  ? 0.6382 0.7981 0.6137 -0.0059 0.0191  -0.0317 130  TRP A N   
813   C CA  . TRP A 132  ? 0.5975 0.7479 0.5717 -0.0072 0.0183  -0.0284 130  TRP A CA  
814   C C   . TRP A 132  ? 0.5797 0.7202 0.5532 -0.0102 0.0179  -0.0198 130  TRP A C   
815   O O   . TRP A 132  ? 0.6037 0.7408 0.5758 -0.0122 0.0172  -0.0149 130  TRP A O   
816   C CB  . TRP A 132  ? 0.4994 0.6376 0.4758 -0.0041 0.0175  -0.0346 130  TRP A CB  
817   C CG  . TRP A 132  ? 0.4501 0.5762 0.4290 -0.0025 0.0174  -0.0357 130  TRP A CG  
818   C CD1 . TRP A 132  ? 0.3914 0.5191 0.3731 0.0003  0.0175  -0.0418 130  TRP A CD1 
819   C CD2 . TRP A 132  ? 0.3719 0.4831 0.3508 -0.0035 0.0170  -0.0307 130  TRP A CD2 
820   N NE1 . TRP A 132  ? 0.3745 0.4893 0.3579 0.0010  0.0173  -0.0404 130  TRP A NE1 
821   C CE2 . TRP A 132  ? 0.3640 0.4689 0.3456 -0.0013 0.0170  -0.0338 130  TRP A CE2 
822   C CE3 . TRP A 132  ? 0.4127 0.5159 0.3900 -0.0060 0.0165  -0.0241 130  TRP A CE3 
823   C CZ2 . TRP A 132  ? 0.3342 0.4256 0.3164 -0.0016 0.0166  -0.0305 130  TRP A CZ2 
824   C CZ3 . TRP A 132  ? 0.3270 0.4168 0.3050 -0.0060 0.0162  -0.0213 130  TRP A CZ3 
825   C CH2 . TRP A 132  ? 0.3388 0.4231 0.3191 -0.0039 0.0163  -0.0244 130  TRP A CH2 
826   N N   . LYS A 133  ? 0.5765 0.7121 0.5513 -0.0103 0.0181  -0.0180 131  LYS A N   
827   C CA  . LYS A 133  ? 0.6289 0.7542 0.6037 -0.0128 0.0174  -0.0107 131  LYS A CA  
828   C C   . LYS A 133  ? 0.7234 0.8576 0.6971 -0.0167 0.0172  -0.0030 131  LYS A C   
829   O O   . LYS A 133  ? 0.7467 0.8735 0.7202 -0.0188 0.0161  0.0028  131  LYS A O   
830   C CB  . LYS A 133  ? 0.5437 0.6634 0.5203 -0.0119 0.0176  -0.0111 131  LYS A CB  
831   N N   . SER A 134  ? 0.7533 0.9038 0.7265 -0.0176 0.0179  -0.0028 132  SER A N   
832   C CA  . SER A 134  ? 0.7777 0.9379 0.7503 -0.0215 0.0176  0.0053  132  SER A CA  
833   C C   . SER A 134  ? 0.8019 0.9636 0.7730 -0.0232 0.0168  0.0086  132  SER A C   
834   O O   . SER A 134  ? 0.8363 1.0017 0.8076 -0.0267 0.0159  0.0166  132  SER A O   
835   C CB  . SER A 134  ? 0.7771 0.9563 0.7494 -0.0219 0.0188  0.0043  132  SER A CB  
836   N N   . HIS A 135  ? 0.7861 0.9445 0.7561 -0.0208 0.0169  0.0030  133  HIS A N   
837   C CA  . HIS A 135  ? 0.8015 0.9625 0.7699 -0.0221 0.0162  0.0055  133  HIS A CA  
838   C C   . HIS A 135  ? 0.8164 0.9610 0.7851 -0.0213 0.0152  0.0054  133  HIS A C   
839   O O   . HIS A 135  ? 0.8362 0.9812 0.8042 -0.0230 0.0144  0.0092  133  HIS A O   
840   C CB  . HIS A 135  ? 0.7729 0.9478 0.7396 -0.0203 0.0169  -0.0008 133  HIS A CB  
841   C CG  . HIS A 135  ? 0.8128 1.0058 0.7790 -0.0206 0.0180  -0.0017 133  HIS A CG  
842   N ND1 . HIS A 135  ? 0.7770 0.9724 0.7445 -0.0180 0.0190  -0.0079 133  HIS A ND1 
843   C CD2 . HIS A 135  ? 0.8095 1.0197 0.7744 -0.0233 0.0183  0.0030  133  HIS A CD2 
844   C CE1 . HIS A 135  ? 0.8085 1.0219 0.7753 -0.0189 0.0199  -0.0073 133  HIS A CE1 
845   N NE2 . HIS A 135  ? 0.8312 1.0541 0.7963 -0.0222 0.0195  -0.0006 133  HIS A NE2 
846   N N   . LEU A 136  ? 0.8140 0.9452 0.7840 -0.0189 0.0153  0.0014  134  LEU A N   
847   C CA  . LEU A 136  ? 0.8276 0.9441 0.7980 -0.0180 0.0145  0.0011  134  LEU A CA  
848   C C   . LEU A 136  ? 0.8485 0.9507 0.8204 -0.0175 0.0142  0.0024  134  LEU A C   
849   O O   . LEU A 136  ? 0.8549 0.9452 0.8272 -0.0174 0.0135  0.0040  134  LEU A O   
850   C CB  . LEU A 136  ? 0.7890 0.9044 0.7592 -0.0149 0.0148  -0.0067 134  LEU A CB  
851   C CG  . LEU A 136  ? 0.7448 0.8714 0.7135 -0.0152 0.0147  -0.0084 134  LEU A CG  
852   C CD1 . LEU A 136  ? 0.6348 0.7602 0.6045 -0.0118 0.0147  -0.0172 134  LEU A CD1 
853   C CD2 . LEU A 136  ? 0.7127 0.8355 0.6806 -0.0174 0.0137  -0.0024 134  LEU A CD2 
854   N N   . SER A 139  ? 0.6406 0.7017 0.6192 -0.0249 0.0081  0.0271  137  SER A N   
855   C CA  . SER A 139  ? 0.5764 0.6250 0.5568 -0.0247 0.0067  0.0289  137  SER A CA  
856   C C   . SER A 139  ? 0.5776 0.6167 0.5566 -0.0215 0.0076  0.0237  137  SER A C   
857   O O   . SER A 139  ? 0.5475 0.5764 0.5275 -0.0206 0.0068  0.0238  137  SER A O   
858   C CB  . SER A 139  ? 0.5944 0.6429 0.5765 -0.0270 0.0049  0.0347  137  SER A CB  
859   O OG  . SER A 139  ? 0.7541 0.8093 0.7386 -0.0302 0.0036  0.0407  137  SER A OG  
860   N N   . ARG A 140  ? 0.4806 0.5236 0.4576 -0.0198 0.0091  0.0190  138  ARG A N   
861   C CA  . ARG A 140  ? 0.4191 0.4543 0.3954 -0.0169 0.0098  0.0142  138  ARG A CA  
862   C C   . ARG A 140  ? 0.4166 0.4560 0.3921 -0.0150 0.0112  0.0087  138  ARG A C   
863   O O   . ARG A 140  ? 0.4250 0.4745 0.3998 -0.0154 0.0118  0.0072  138  ARG A O   
864   C CB  . ARG A 140  ? 0.4196 0.4534 0.3953 -0.0168 0.0096  0.0143  138  ARG A CB  
865   N N   . SER A 141  ? 0.3965 0.4287 0.3725 -0.0129 0.0117  0.0057  139  SER A N   
866   C CA  . SER A 141  ? 0.3288 0.3635 0.3049 -0.0108 0.0127  0.0003  139  SER A CA  
867   C C   . SER A 141  ? 0.3425 0.3812 0.3184 -0.0098 0.0130  -0.0032 139  SER A C   
868   O O   . SER A 141  ? 0.3159 0.3504 0.2916 -0.0098 0.0126  -0.0025 139  SER A O   
869   C CB  . SER A 141  ? 0.3364 0.3613 0.3134 -0.0087 0.0128  -0.0017 139  SER A CB  
870   O OG  . SER A 141  ? 0.3019 0.3285 0.2799 -0.0065 0.0134  -0.0068 139  SER A OG  
871   N N   . LEU A 142  ? 0.3240 0.3713 0.3001 -0.0090 0.0136  -0.0072 140  LEU A N   
872   C CA  . LEU A 142  ? 0.2770 0.3274 0.2535 -0.0075 0.0137  -0.0119 140  LEU A CA  
873   C C   . LEU A 142  ? 0.2616 0.3015 0.2398 -0.0054 0.0134  -0.0145 140  LEU A C   
874   O O   . LEU A 142  ? 0.2653 0.3049 0.2441 -0.0047 0.0131  -0.0169 140  LEU A O   
875   C CB  . LEU A 142  ? 0.2606 0.3209 0.2379 -0.0063 0.0142  -0.0168 140  LEU A CB  
876   C CG  . LEU A 142  ? 0.3075 0.3784 0.2840 -0.0064 0.0142  -0.0195 140  LEU A CG  
877   C CD1 . LEU A 142  ? 0.4099 0.4894 0.3841 -0.0094 0.0142  -0.0139 140  LEU A CD1 
878   C CD2 . LEU A 142  ? 0.3289 0.4081 0.3070 -0.0043 0.0146  -0.0261 140  LEU A CD2 
879   N N   . PHE A 143  ? 0.2318 0.2635 0.2109 -0.0045 0.0135  -0.0139 141  PHE A N   
880   C CA  . PHE A 143  ? 0.2574 0.2809 0.2385 -0.0024 0.0133  -0.0166 141  PHE A CA  
881   C C   . PHE A 143  ? 0.2860 0.3000 0.2666 -0.0027 0.0131  -0.0130 141  PHE A C   
882   O O   . PHE A 143  ? 0.2893 0.2962 0.2715 -0.0012 0.0130  -0.0138 141  PHE A O   
883   C CB  . PHE A 143  ? 0.2421 0.2646 0.2249 -0.0009 0.0135  -0.0189 141  PHE A CB  
884   C CG  . PHE A 143  ? 0.2368 0.2695 0.2202 -0.0005 0.0138  -0.0224 141  PHE A CG  
885   C CD1 . PHE A 143  ? 0.2243 0.2624 0.2093 0.0008  0.0135  -0.0275 141  PHE A CD1 
886   C CD2 . PHE A 143  ? 0.2546 0.2919 0.2371 -0.0013 0.0142  -0.0210 141  PHE A CD2 
887   C CE1 . PHE A 143  ? 0.2357 0.2842 0.2213 0.0014  0.0138  -0.0313 141  PHE A CE1 
888   C CE2 . PHE A 143  ? 0.2480 0.2959 0.2311 -0.0009 0.0146  -0.0243 141  PHE A CE2 
889   C CZ  . PHE A 143  ? 0.2154 0.2690 0.1999 0.0006  0.0144  -0.0296 141  PHE A CZ  
890   N N   . VAL A 144  ? 0.2653 0.2796 0.2441 -0.0046 0.0129  -0.0090 142  VAL A N   
891   C CA  A VAL A 144  ? 0.2989 0.3048 0.2774 -0.0047 0.0126  -0.0059 142  VAL A CA  
892   C CA  B VAL A 144  ? 0.2988 0.3048 0.2773 -0.0047 0.0126  -0.0059 142  VAL A CA  
893   C C   . VAL A 144  ? 0.2880 0.2890 0.2680 -0.0032 0.0125  -0.0079 142  VAL A C   
894   O O   . VAL A 144  ? 0.3019 0.2958 0.2824 -0.0023 0.0125  -0.0068 142  VAL A O   
895   C CB  A VAL A 144  ? 0.2938 0.3014 0.2709 -0.0068 0.0120  -0.0016 142  VAL A CB  
896   C CB  B VAL A 144  ? 0.2936 0.3017 0.2707 -0.0069 0.0120  -0.0017 142  VAL A CB  
897   C CG1 A VAL A 144  ? 0.3205 0.3309 0.2970 -0.0084 0.0118  0.0014  142  VAL A CG1 
898   C CG1 B VAL A 144  ? 0.3067 0.3073 0.2839 -0.0066 0.0117  0.0005  142  VAL A CG1 
899   C CG2 A VAL A 144  ? 0.2835 0.2983 0.2602 -0.0076 0.0119  -0.0024 142  VAL A CG2 
900   C CG2 B VAL A 144  ? 0.3206 0.3316 0.2971 -0.0085 0.0117  0.0014  142  VAL A CG2 
901   N N   . ASN A 145  ? 0.2891 0.2943 0.2701 -0.0028 0.0124  -0.0110 143  ASN A N   
902   C CA  . ASN A 145  ? 0.2873 0.2882 0.2705 -0.0017 0.0121  -0.0128 143  ASN A CA  
903   C C   . ASN A 145  ? 0.3184 0.3188 0.3048 0.0002  0.0118  -0.0172 143  ASN A C   
904   O O   . ASN A 145  ? 0.2839 0.2828 0.2730 0.0010  0.0112  -0.0196 143  ASN A O   
905   C CB  . ASN A 145  ? 0.3181 0.3231 0.3009 -0.0026 0.0117  -0.0131 143  ASN A CB  
906   C CG  . ASN A 145  ? 0.3365 0.3400 0.3173 -0.0041 0.0116  -0.0084 143  ASN A CG  
907   O OD1 . ASN A 145  ? 0.3998 0.3964 0.3806 -0.0039 0.0117  -0.0058 143  ASN A OD1 
908   N ND2 . ASN A 145  ? 0.3475 0.3577 0.3267 -0.0057 0.0113  -0.0071 143  ASN A ND2 
909   N N   . ALA A 146  ? 0.2650 0.2664 0.2518 0.0009  0.0121  -0.0184 144  ALA A N   
910   C CA  . ALA A 146  ? 0.2762 0.2776 0.2667 0.0028  0.0116  -0.0227 144  ALA A CA  
911   C C   . ALA A 146  ? 0.2738 0.2671 0.2673 0.0040  0.0111  -0.0223 144  ALA A C   
912   O O   . ALA A 146  ? 0.3151 0.3079 0.3129 0.0053  0.0102  -0.0259 144  ALA A O   
913   C CB  . ALA A 146  ? 0.2615 0.2654 0.2516 0.0032  0.0120  -0.0235 144  ALA A CB  
914   N N   . ALA A 147  ? 0.3097 0.2972 0.3017 0.0035  0.0115  -0.0181 145  ALA A N   
915   C CA  . ALA A 147  ? 0.3276 0.3087 0.3225 0.0045  0.0111  -0.0172 145  ALA A CA  
916   C C   . ALA A 147  ? 0.3332 0.3141 0.3310 0.0045  0.0102  -0.0188 145  ALA A C   
917   O O   . ALA A 147  ? 0.3174 0.2954 0.3198 0.0055  0.0093  -0.0202 145  ALA A O   
918   C CB  . ALA A 147  ? 0.3756 0.3521 0.3680 0.0040  0.0117  -0.0127 145  ALA A CB  
919   N N   . THR A 148  ? 0.3183 0.3025 0.3139 0.0033  0.0104  -0.0185 146  THR A N   
920   C CA  . THR A 148  ? 0.3192 0.3040 0.3173 0.0032  0.0095  -0.0204 146  THR A CA  
921   C C   . THR A 148  ? 0.3128 0.3017 0.3146 0.0043  0.0084  -0.0260 146  THR A C   
922   O O   . THR A 148  ? 0.3136 0.3001 0.3204 0.0051  0.0071  -0.0282 146  THR A O   
923   C CB  . THR A 148  ? 0.3493 0.3374 0.3439 0.0017  0.0099  -0.0187 146  THR A CB  
924   O OG1 . THR A 148  ? 0.3459 0.3299 0.3380 0.0011  0.0107  -0.0140 146  THR A OG1 
925   C CG2 . THR A 148  ? 0.3746 0.3637 0.3718 0.0016  0.0089  -0.0207 146  THR A CG2 
926   N N   . TRP A 149  ? 0.2858 0.2813 0.2857 0.0043  0.0087  -0.0285 147  TRP A N   
927   C CA  . TRP A 149  ? 0.2946 0.2949 0.2981 0.0056  0.0076  -0.0345 147  TRP A CA  
928   C C   . TRP A 149  ? 0.2697 0.2656 0.2782 0.0073  0.0067  -0.0364 147  TRP A C   
929   O O   . TRP A 149  ? 0.3058 0.3023 0.3197 0.0087  0.0052  -0.0411 147  TRP A O   
930   C CB  . TRP A 149  ? 0.2692 0.2787 0.2694 0.0052  0.0084  -0.0364 147  TRP A CB  
931   C CG  . TRP A 149  ? 0.2518 0.2668 0.2481 0.0035  0.0088  -0.0348 147  TRP A CG  
932   C CD1 . TRP A 149  ? 0.3065 0.3247 0.2979 0.0018  0.0099  -0.0307 147  TRP A CD1 
933   C CD2 . TRP A 149  ? 0.2837 0.3019 0.2810 0.0033  0.0079  -0.0372 147  TRP A CD2 
934   N NE1 . TRP A 149  ? 0.3168 0.3402 0.3062 0.0005  0.0098  -0.0300 147  TRP A NE1 
935   C CE2 . TRP A 149  ? 0.3058 0.3294 0.2985 0.0014  0.0086  -0.0341 147  TRP A CE2 
936   C CE3 . TRP A 149  ? 0.2736 0.2907 0.2758 0.0045  0.0063  -0.0417 147  TRP A CE3 
937   C CZ2 . TRP A 149  ? 0.3355 0.3637 0.3278 0.0007  0.0080  -0.0352 147  TRP A CZ2 
938   C CZ3 . TRP A 149  ? 0.3566 0.3781 0.3583 0.0038  0.0057  -0.0431 147  TRP A CZ3 
939   C CH2 . TRP A 149  ? 0.3713 0.3985 0.3680 0.0020  0.0066  -0.0399 147  TRP A CH2 
940   N N   . GLY A 150  ? 0.2754 0.2668 0.2828 0.0074  0.0075  -0.0329 148  GLY A N   
941   C CA  . GLY A 150  ? 0.2819 0.2687 0.2943 0.0089  0.0065  -0.0337 148  GLY A CA  
942   C C   . GLY A 150  ? 0.3081 0.2893 0.3257 0.0092  0.0051  -0.0332 148  GLY A C   
943   O O   . GLY A 150  ? 0.3263 0.3056 0.3503 0.0106  0.0034  -0.0361 148  GLY A O   
944   N N   . LEU A 151  ? 0.3008 0.2792 0.3163 0.0079  0.0057  -0.0294 149  LEU A N   
945   C CA  . LEU A 151  ? 0.3481 0.3221 0.3687 0.0080  0.0043  -0.0286 149  LEU A CA  
946   C C   . LEU A 151  ? 0.3352 0.3123 0.3603 0.0085  0.0025  -0.0341 149  LEU A C   
947   O O   . LEU A 151  ? 0.3436 0.3176 0.3758 0.0093  0.0005  -0.0359 149  LEU A O   
948   C CB  . LEU A 151  ? 0.3513 0.3229 0.3684 0.0065  0.0054  -0.0236 149  LEU A CB  
949   C CG  . LEU A 151  ? 0.4132 0.3799 0.4296 0.0065  0.0062  -0.0184 149  LEU A CG  
950   C CD1 . LEU A 151  ? 0.4827 0.4486 0.4946 0.0053  0.0075  -0.0143 149  LEU A CD1 
951   C CD2 . LEU A 151  ? 0.4151 0.3776 0.4386 0.0070  0.0046  -0.0176 149  LEU A CD2 
952   N N   . VAL A 152  ? 0.3550 0.3384 0.3764 0.0080  0.0031  -0.0369 150  VAL A N   
953   C CA  . VAL A 152  ? 0.2965 0.2841 0.3216 0.0086  0.0014  -0.0427 150  VAL A CA  
954   C C   . VAL A 152  ? 0.3426 0.3315 0.3735 0.0106  -0.0003 -0.0484 150  VAL A C   
955   O O   . VAL A 152  ? 0.3485 0.3363 0.3864 0.0116  -0.0027 -0.0525 150  VAL A O   
956   C CB  . VAL A 152  ? 0.3323 0.3280 0.3517 0.0077  0.0024  -0.0441 150  VAL A CB  
957   C CG1 . VAL A 152  ? 0.3566 0.3582 0.3796 0.0086  0.0006  -0.0510 150  VAL A CG1 
958   C CG2 . VAL A 152  ? 0.3503 0.3443 0.3653 0.0058  0.0035  -0.0389 150  VAL A CG2 
959   N N   . VAL A 153  ? 0.3229 0.3141 0.3517 0.0114  0.0007  -0.0489 151  VAL A N   
960   C CA  . VAL A 153  ? 0.3324 0.3261 0.3663 0.0135  -0.0008 -0.0548 151  VAL A CA  
961   C C   . VAL A 153  ? 0.3051 0.2911 0.3460 0.0145  -0.0025 -0.0536 151  VAL A C   
962   O O   . VAL A 153  ? 0.3453 0.3306 0.3941 0.0162  -0.0050 -0.0585 151  VAL A O   
963   C CB  . VAL A 153  ? 0.2949 0.2953 0.3239 0.0138  0.0009  -0.0558 151  VAL A CB  
964   C CG1 . VAL A 153  ? 0.3115 0.3137 0.3462 0.0162  -0.0006 -0.0614 151  VAL A CG1 
965   C CG2 . VAL A 153  ? 0.2835 0.2931 0.3071 0.0129  0.0020  -0.0577 151  VAL A CG2 
966   N N   . THR A 154  ? 0.3113 0.2920 0.3500 0.0137  -0.0012 -0.0472 152  THR A N   
967   C CA  . THR A 154  ? 0.3290 0.3034 0.3735 0.0146  -0.0026 -0.0452 152  THR A CA  
968   C C   . THR A 154  ? 0.3600 0.3277 0.4077 0.0135  -0.0033 -0.0401 152  THR A C   
969   O O   . THR A 154  ? 0.3659 0.3289 0.4201 0.0141  -0.0050 -0.0385 152  THR A O   
970   C CB  . THR A 154  ? 0.3536 0.3277 0.3937 0.0146  -0.0008 -0.0418 152  THR A CB  
971   O OG1 . THR A 154  ? 0.3636 0.3358 0.3972 0.0129  0.0012  -0.0356 152  THR A OG1 
972   C CG2 . THR A 154  ? 0.3313 0.3128 0.3678 0.0153  0.0002  -0.0460 152  THR A CG2 
973   N N   . GLY A 155  ? 0.3545 0.3221 0.3982 0.0119  -0.0022 -0.0372 153  GLY A N   
974   C CA  . GLY A 155  ? 0.3654 0.3276 0.4114 0.0108  -0.0025 -0.0317 153  GLY A CA  
975   C C   . GLY A 155  ? 0.4178 0.3770 0.4601 0.0103  -0.0009 -0.0253 153  GLY A C   
976   O O   . GLY A 155  ? 0.4307 0.3862 0.4751 0.0096  -0.0011 -0.0205 153  GLY A O   
977   N N   . LYS A 156  ? 0.3632 0.3245 0.4005 0.0107  0.0006  -0.0252 154  LYS A N   
978   C CA  . LYS A 156  ? 0.3946 0.3537 0.4283 0.0105  0.0020  -0.0200 154  LYS A CA  
979   C C   . LYS A 156  ? 0.3927 0.3545 0.4176 0.0096  0.0045  -0.0186 154  LYS A C   
980   O O   . LYS A 156  ? 0.3625 0.3286 0.3843 0.0095  0.0050  -0.0220 154  LYS A O   
981   C CB  . LYS A 156  ? 0.4408 0.3993 0.4774 0.0118  0.0013  -0.0209 154  LYS A CB  
982   N N   . LEU A 157  ? 0.3614 0.3211 0.3828 0.0090  0.0057  -0.0135 155  LEU A N   
983   C CA  . LEU A 157  ? 0.3850 0.3464 0.3990 0.0082  0.0077  -0.0118 155  LEU A CA  
984   C C   . LEU A 157  ? 0.4431 0.4046 0.4544 0.0088  0.0084  -0.0107 155  LEU A C   
985   O O   . LEU A 157  ? 0.4168 0.3759 0.4300 0.0094  0.0081  -0.0081 155  LEU A O   
986   C CB  . LEU A 157  ? 0.4014 0.3608 0.4133 0.0074  0.0085  -0.0075 155  LEU A CB  
987   C CG  . LEU A 157  ? 0.4726 0.4331 0.4777 0.0068  0.0101  -0.0057 155  LEU A CG  
988   C CD1 . LEU A 157  ? 0.4082 0.3721 0.4106 0.0060  0.0104  -0.0083 155  LEU A CD1 
989   C CD2 . LEU A 157  ? 0.4587 0.4174 0.4627 0.0065  0.0108  -0.0017 155  LEU A CD2 
990   N N   . THR A 158  ? 0.4326 0.3974 0.4396 0.0085  0.0092  -0.0125 156  THR A N   
991   C CA  . THR A 158  ? 0.4116 0.3769 0.4151 0.0087  0.0100  -0.0112 156  THR A CA  
992   C C   . THR A 158  ? 0.4409 0.4069 0.4387 0.0075  0.0113  -0.0092 156  THR A C   
993   O O   . THR A 158  ? 0.4838 0.4525 0.4798 0.0066  0.0115  -0.0105 156  THR A O   
994   C CB  . THR A 158  ? 0.4580 0.4268 0.4622 0.0092  0.0097  -0.0149 156  THR A CB  
995   O OG1 . THR A 158  ? 0.4991 0.4675 0.5095 0.0104  0.0083  -0.0178 156  THR A OG1 
996   C CG2 . THR A 158  ? 0.4779 0.4466 0.4798 0.0095  0.0102  -0.0134 156  THR A CG2 
997   N N   . SER A 159  ? 0.3758 0.3397 0.3712 0.0076  0.0118  -0.0060 157  SER A N   
998   C CA  . SER A 159  ? 0.3673 0.3310 0.3584 0.0068  0.0126  -0.0041 157  SER A CA  
999   C C   . SER A 159  ? 0.3440 0.3106 0.3320 0.0059  0.0129  -0.0051 157  SER A C   
1000  O O   . SER A 159  ? 0.3897 0.3570 0.3754 0.0049  0.0131  -0.0042 157  SER A O   
1001  C CB  . SER A 159  ? 0.4281 0.3895 0.4177 0.0074  0.0130  -0.0012 157  SER A CB  
1002  O OG  . SER A 159  ? 0.4701 0.4316 0.4600 0.0082  0.0128  -0.0013 157  SER A OG  
1003  N N   . THR A 160  ? 0.3490 0.3175 0.3373 0.0062  0.0127  -0.0067 158  THR A N   
1004  C CA  . THR A 160  ? 0.2917 0.2638 0.2778 0.0051  0.0129  -0.0074 158  THR A CA  
1005  C C   . THR A 160  ? 0.2934 0.2698 0.2816 0.0053  0.0126  -0.0107 158  THR A C   
1006  O O   . THR A 160  ? 0.3190 0.2948 0.3107 0.0065  0.0121  -0.0127 158  THR A O   
1007  C CB  . THR A 160  ? 0.3012 0.2725 0.2854 0.0052  0.0129  -0.0060 158  THR A CB  
1008  O OG1 . THR A 160  ? 0.3139 0.2844 0.3002 0.0065  0.0127  -0.0069 158  THR A OG1 
1009  C CG2 . THR A 160  ? 0.3455 0.3133 0.3276 0.0052  0.0130  -0.0034 158  THR A CG2 
1010  N N   . VAL A 161  ? 0.2198 0.2011 0.2063 0.0042  0.0128  -0.0113 159  VAL A N   
1011  C CA  . VAL A 161  ? 0.2373 0.2245 0.2251 0.0042  0.0128  -0.0147 159  VAL A CA  
1012  C C   . VAL A 161  ? 0.2221 0.2122 0.2102 0.0046  0.0128  -0.0156 159  VAL A C   
1013  O O   . VAL A 161  ? 0.2361 0.2269 0.2218 0.0035  0.0131  -0.0133 159  VAL A O   
1014  C CB  . VAL A 161  ? 0.2445 0.2367 0.2301 0.0025  0.0130  -0.0142 159  VAL A CB  
1015  C CG1 . VAL A 161  ? 0.2808 0.2807 0.2673 0.0026  0.0130  -0.0176 159  VAL A CG1 
1016  C CG2 . VAL A 161  ? 0.2888 0.2784 0.2744 0.0022  0.0129  -0.0132 159  VAL A CG2 
1017  N N   . ASN A 162  ? 0.2060 0.1980 0.1973 0.0061  0.0125  -0.0191 160  ASN A N   
1018  C CA  . ASN A 162  ? 0.2113 0.2074 0.2029 0.0064  0.0126  -0.0204 160  ASN A CA  
1019  C C   . ASN A 162  ? 0.2053 0.2099 0.1958 0.0054  0.0130  -0.0221 160  ASN A C   
1020  O O   . ASN A 162  ? 0.2104 0.2199 0.2032 0.0064  0.0128  -0.0262 160  ASN A O   
1021  C CB  . ASN A 162  ? 0.2075 0.2023 0.2035 0.0085  0.0119  -0.0233 160  ASN A CB  
1022  C CG  . ASN A 162  ? 0.2560 0.2550 0.2523 0.0089  0.0120  -0.0245 160  ASN A CG  
1023  O OD1 . ASN A 162  ? 0.2290 0.2336 0.2228 0.0076  0.0126  -0.0240 160  ASN A OD1 
1024  N ND2 . ASN A 162  ? 0.2652 0.2616 0.2649 0.0107  0.0113  -0.0256 160  ASN A ND2 
1025  N N   . ASP A 163  ? 0.1910 0.1978 0.1782 0.0033  0.0134  -0.0188 161  ASP A N   
1026  C CA  . ASP A 163  ? 0.1939 0.2092 0.1797 0.0019  0.0138  -0.0193 161  ASP A CA  
1027  C C   . ASP A 163  ? 0.2119 0.2351 0.1988 0.0023  0.0141  -0.0217 161  ASP A C   
1028  O O   . ASP A 163  ? 0.2037 0.2355 0.1905 0.0020  0.0144  -0.0238 161  ASP A O   
1029  C CB  . ASP A 163  ? 0.2074 0.2228 0.1903 -0.0006 0.0139  -0.0145 161  ASP A CB  
1030  C CG  . ASP A 163  ? 0.2609 0.2722 0.2429 -0.0013 0.0136  -0.0112 161  ASP A CG  
1031  O OD1 . ASP A 163  ? 0.2372 0.2423 0.2200 0.0001  0.0134  -0.0115 161  ASP A OD1 
1032  O OD2 . ASP A 163  ? 0.2613 0.2758 0.2420 -0.0034 0.0134  -0.0080 161  ASP A OD2 
1033  N N   . ARG A 164  ? 0.2064 0.2275 0.1943 0.0031  0.0140  -0.0217 162  ARG A N   
1034  C CA  A ARG A 164  ? 0.1965 0.2254 0.1858 0.0038  0.0143  -0.0244 162  ARG A CA  
1035  C CA  B ARG A 164  ? 0.1970 0.2258 0.1864 0.0038  0.0143  -0.0244 162  ARG A CA  
1036  C C   . ARG A 164  ? 0.1933 0.2242 0.1863 0.0064  0.0139  -0.0303 162  ARG A C   
1037  O O   . ARG A 164  ? 0.2112 0.2513 0.2053 0.0070  0.0142  -0.0338 162  ARG A O   
1038  C CB  A ARG A 164  ? 0.2192 0.2455 0.2088 0.0038  0.0142  -0.0226 162  ARG A CB  
1039  C CB  B ARG A 164  ? 0.2197 0.2456 0.2093 0.0039  0.0141  -0.0226 162  ARG A CB  
1040  C CG  A ARG A 164  ? 0.2337 0.2588 0.2205 0.0012  0.0142  -0.0174 162  ARG A CG  
1041  C CG  B ARG A 164  ? 0.2340 0.2586 0.2208 0.0013  0.0141  -0.0175 162  ARG A CG  
1042  C CD  A ARG A 164  ? 0.2691 0.3024 0.2542 -0.0011 0.0145  -0.0155 162  ARG A CD  
1043  C CD  B ARG A 164  ? 0.2389 0.2736 0.2247 -0.0008 0.0146  -0.0161 162  ARG A CD  
1044  N NE  A ARG A 164  ? 0.2493 0.2935 0.2354 -0.0008 0.0151  -0.0184 162  ARG A NE  
1045  N NE  B ARG A 164  ? 0.2876 0.3253 0.2718 -0.0023 0.0147  -0.0146 162  ARG A NE  
1046  C CZ  A ARG A 164  ? 0.2937 0.3472 0.2788 -0.0023 0.0156  -0.0180 162  ARG A CZ  
1047  C CZ  B ARG A 164  ? 0.2814 0.3282 0.2655 -0.0024 0.0152  -0.0168 162  ARG A CZ  
1048  N NH1 A ARG A 164  ? 0.2999 0.3528 0.2830 -0.0042 0.0154  -0.0147 162  ARG A NH1 
1049  N NH1 B ARG A 164  ? 0.2927 0.3471 0.2785 -0.0009 0.0157  -0.0210 162  ARG A NH1 
1050  N NH2 A ARG A 164  ? 0.2471 0.3113 0.2331 -0.0017 0.0162  -0.0210 162  ARG A NH2 
1051  N NH2 B ARG A 164  ? 0.2945 0.3434 0.2769 -0.0039 0.0152  -0.0149 162  ARG A NH2 
1052  N N   . SER A 165  ? 0.1885 0.2115 0.1839 0.0079  0.0132  -0.0314 163  SER A N   
1053  C CA  . SER A 165  ? 0.1811 0.2053 0.1810 0.0103  0.0124  -0.0369 163  SER A CA  
1054  C C   . SER A 165  ? 0.1810 0.2114 0.1805 0.0101  0.0125  -0.0397 163  SER A C   
1055  O O   . SER A 165  ? 0.1662 0.2035 0.1685 0.0116  0.0121  -0.0451 163  SER A O   
1056  C CB  . SER A 165  ? 0.1886 0.2029 0.1915 0.0116  0.0114  -0.0364 163  SER A CB  
1057  O OG  . SER A 165  ? 0.2134 0.2281 0.2213 0.0136  0.0102  -0.0414 163  SER A OG  
1058  N N   . LEU A 166  ? 0.1778 0.2060 0.1741 0.0082  0.0128  -0.0363 164  LEU A N   
1059  C CA  . LEU A 166  ? 0.1968 0.2310 0.1925 0.0078  0.0128  -0.0385 164  LEU A CA  
1060  C C   . LEU A 166  ? 0.1875 0.2338 0.1810 0.0068  0.0136  -0.0394 164  LEU A C   
1061  O O   . LEU A 166  ? 0.1840 0.2384 0.1784 0.0076  0.0135  -0.0438 164  LEU A O   
1062  C CB  . LEU A 166  ? 0.2022 0.2311 0.1950 0.0060  0.0129  -0.0341 164  LEU A CB  
1063  C CG  . LEU A 166  ? 0.2079 0.2268 0.2033 0.0070  0.0120  -0.0339 164  LEU A CG  
1064  C CD1 . LEU A 166  ? 0.2183 0.2329 0.2108 0.0053  0.0123  -0.0296 164  LEU A CD1 
1065  C CD2 . LEU A 166  ? 0.2036 0.2237 0.2036 0.0090  0.0109  -0.0397 164  LEU A CD2 
1066  N N   . ALA A 167  ? 0.1969 0.2452 0.1876 0.0050  0.0144  -0.0351 165  ALA A N   
1067  C CA  . ALA A 167  ? 0.1837 0.2443 0.1727 0.0038  0.0151  -0.0351 165  ALA A CA  
1068  C C   . ALA A 167  ? 0.1892 0.2573 0.1813 0.0062  0.0152  -0.0412 165  ALA A C   
1069  O O   . ALA A 167  ? 0.1850 0.2644 0.1769 0.0065  0.0155  -0.0445 165  ALA A O   
1070  C CB  . ALA A 167  ? 0.2071 0.2674 0.1937 0.0014  0.0156  -0.0291 165  ALA A CB  
1071  N N   . ALA A 168  ? 0.1795 0.2418 0.1746 0.0080  0.0147  -0.0427 166  ALA A N   
1072  C CA  . ALA A 168  ? 0.1881 0.2568 0.1869 0.0107  0.0145  -0.0489 166  ALA A CA  
1073  C C   . ALA A 168  ? 0.1751 0.2462 0.1771 0.0129  0.0136  -0.0554 166  ALA A C   
1074  O O   . ALA A 168  ? 0.1792 0.2614 0.1826 0.0142  0.0137  -0.0607 166  ALA A O   
1075  C CB  . ALA A 168  ? 0.1867 0.2475 0.1887 0.0122  0.0139  -0.0490 166  ALA A CB  
1076  N N   . ALA A 169  ? 0.1845 0.2461 0.1878 0.0132  0.0126  -0.0552 167  ALA A N   
1077  C CA  . ALA A 169  ? 0.1714 0.2343 0.1785 0.0152  0.0113  -0.0613 167  ALA A CA  
1078  C C   . ALA A 169  ? 0.1713 0.2451 0.1755 0.0143  0.0119  -0.0631 167  ALA A C   
1079  O O   . ALA A 169  ? 0.1755 0.2565 0.1826 0.0163  0.0111  -0.0699 167  ALA A O   
1080  C CB  . ALA A 169  ? 0.1774 0.2278 0.1865 0.0153  0.0102  -0.0595 167  ALA A CB  
1081  N N   . LEU A 170  ? 0.1673 0.2427 0.1662 0.0113  0.0130  -0.0571 168  LEU A N   
1082  C CA  . LEU A 170  ? 0.1699 0.2561 0.1658 0.0101  0.0134  -0.0578 168  LEU A CA  
1083  C C   . LEU A 170  ? 0.1906 0.2917 0.1860 0.0106  0.0143  -0.0609 168  LEU A C   
1084  O O   . LEU A 170  ? 0.1945 0.3061 0.1905 0.0118  0.0141  -0.0664 168  LEU A O   
1085  C CB  . LEU A 170  ? 0.2127 0.2963 0.2038 0.0067  0.0142  -0.0500 168  LEU A CB  
1086  C CG  . LEU A 170  ? 0.2442 0.3381 0.2323 0.0051  0.0145  -0.0496 168  LEU A CG  
1087  C CD1 . LEU A 170  ? 0.2314 0.3249 0.2221 0.0070  0.0133  -0.0555 168  LEU A CD1 
1088  C CD2 . LEU A 170  ? 0.2542 0.3440 0.2384 0.0019  0.0149  -0.0415 168  LEU A CD2 
1089  N N   . THR A 171  ? 0.1930 0.2958 0.1874 0.0097  0.0152  -0.0577 169  THR A N   
1090  C CA  . THR A 171  ? 0.1783 0.2955 0.1727 0.0103  0.0161  -0.0606 169  THR A CA  
1091  C C   . THR A 171  ? 0.1839 0.3050 0.1834 0.0143  0.0151  -0.0700 169  THR A C   
1092  O O   . THR A 171  ? 0.1956 0.3304 0.1953 0.0154  0.0154  -0.0752 169  THR A O   
1093  C CB  . THR A 171  ? 0.2000 0.3164 0.1937 0.0091  0.0169  -0.0559 169  THR A CB  
1094  O OG1 . THR A 171  ? 0.2367 0.3498 0.2263 0.0054  0.0174  -0.0475 169  THR A OG1 
1095  C CG2 . THR A 171  ? 0.2347 0.3667 0.2287 0.0097  0.0178  -0.0589 169  THR A CG2 
1096  N N   . ARG A 172  ? 0.1673 0.2768 0.1713 0.0164  0.0139  -0.0724 170  ARG A N   
1097  C CA  . ARG A 172  ? 0.1757 0.2876 0.1858 0.0203  0.0125  -0.0812 170  ARG A CA  
1098  C C   . ARG A 172  ? 0.1865 0.3032 0.1981 0.0217  0.0114  -0.0874 170  ARG A C   
1099  O O   . ARG A 172  ? 0.2003 0.3284 0.2146 0.0242  0.0110  -0.0950 170  ARG A O   
1100  C CB  . ARG A 172  ? 0.1964 0.2937 0.2114 0.0219  0.0111  -0.0812 170  ARG A CB  
1101  C CG  . ARG A 172  ? 0.1903 0.2895 0.2126 0.0259  0.0095  -0.0895 170  ARG A CG  
1102  C CD  . ARG A 172  ? 0.2036 0.2876 0.2312 0.0273  0.0077  -0.0889 170  ARG A CD  
1103  N NE  . ARG A 172  ? 0.1899 0.2654 0.2146 0.0252  0.0086  -0.0810 170  ARG A NE  
1104  C CZ  . ARG A 172  ? 0.1831 0.2480 0.2052 0.0230  0.0087  -0.0747 170  ARG A CZ  
1105  N NH1 . ARG A 172  ? 0.1818 0.2425 0.2041 0.0226  0.0079  -0.0750 170  ARG A NH1 
1106  N NH2 . ARG A 172  ? 0.2013 0.2600 0.2207 0.0214  0.0095  -0.0684 170  ARG A NH2 
1107  N N   . LEU A 173  ? 0.1797 0.2886 0.1899 0.0203  0.0109  -0.0846 171  LEU A N   
1108  C CA  . LEU A 173  ? 0.1760 0.2882 0.1887 0.0218  0.0095  -0.0908 171  LEU A CA  
1109  C C   . LEU A 173  ? 0.1842 0.3129 0.1925 0.0209  0.0106  -0.0923 171  LEU A C   
1110  O O   . LEU A 173  ? 0.1986 0.3363 0.2095 0.0232  0.0096  -0.1003 171  LEU A O   
1111  C CB  . LEU A 173  ? 0.2052 0.3045 0.2179 0.0204  0.0085  -0.0871 171  LEU A CB  
1112  C CG  . LEU A 173  ? 0.2121 0.3097 0.2184 0.0168  0.0097  -0.0794 171  LEU A CG  
1113  C CD1 . LEU A 173  ? 0.2414 0.3490 0.2456 0.0164  0.0096  -0.0822 171  LEU A CD1 
1114  C CD2 . LEU A 173  ? 0.2228 0.3045 0.2300 0.0159  0.0091  -0.0745 171  LEU A CD2 
1115  N N   . ILE A 174  ? 0.2088 0.3421 0.2109 0.0175  0.0124  -0.0848 172  ILE A N   
1116  C CA  . ILE A 174  ? 0.1814 0.3314 0.1794 0.0164  0.0135  -0.0852 172  ILE A CA  
1117  C C   . ILE A 174  ? 0.1924 0.3570 0.1920 0.0186  0.0141  -0.0912 172  ILE A C   
1118  O O   . ILE A 174  ? 0.2005 0.3791 0.2002 0.0201  0.0139  -0.0974 172  ILE A O   
1119  C CB  . ILE A 174  ? 0.2064 0.3572 0.1984 0.0121  0.0151  -0.0750 172  ILE A CB  
1120  C CG1 . ILE A 174  ? 0.2562 0.3957 0.2465 0.0102  0.0144  -0.0704 172  ILE A CG1 
1121  C CG2 . ILE A 174  ? 0.2525 0.4224 0.2407 0.0107  0.0163  -0.0744 172  ILE A CG2 
1122  C CD1 . ILE A 174  ? 0.2551 0.3921 0.2408 0.0062  0.0154  -0.0603 172  ILE A CD1 
1123  N N   . SER A 175  ? 0.1924 0.3546 0.1933 0.0190  0.0147  -0.0897 173  SER A N   
1124  C CA  . SER A 175  ? 0.1755 0.3517 0.1782 0.0212  0.0153  -0.0953 173  SER A CA  
1125  C C   . SER A 175  ? 0.2047 0.3824 0.2139 0.0258  0.0134  -0.1065 173  SER A C   
1126  O O   . SER A 175  ? 0.2183 0.4115 0.2287 0.0281  0.0137  -0.1134 173  SER A O   
1127  C CB  . SER A 175  ? 0.1947 0.3669 0.1979 0.0207  0.0162  -0.0911 173  SER A CB  
1128  O OG  . SER A 175  ? 0.2472 0.4200 0.2451 0.0165  0.0177  -0.0813 173  SER A OG  
1129  N N   . ARG A 176  ? 0.1978 0.3604 0.2116 0.0273  0.0114  -0.1087 174  ARG A N   
1130  C CA  . ARG A 176  ? 0.2006 0.3634 0.2217 0.0316  0.0091  -0.1193 174  ARG A CA  
1131  C C   . ARG A 176  ? 0.2249 0.3952 0.2459 0.0324  0.0081  -0.1250 174  ARG A C   
1132  O O   . ARG A 176  ? 0.2335 0.4150 0.2581 0.0357  0.0070  -0.1346 174  ARG A O   
1133  C CB  . ARG A 176  ? 0.2547 0.3985 0.2816 0.0327  0.0071  -0.1188 174  ARG A CB  
1134  C CG  . ARG A 176  ? 0.2302 0.3725 0.2664 0.0372  0.0043  -0.1292 174  ARG A CG  
1135  C CD  . ARG A 176  ? 0.2199 0.3438 0.2620 0.0379  0.0024  -0.1270 174  ARG A CD  
1136  N NE  . ARG A 176  ? 0.2258 0.3382 0.2676 0.0360  0.0014  -0.1232 174  ARG A NE  
1137  C CZ  . ARG A 176  ? 0.2595 0.3603 0.2976 0.0330  0.0023  -0.1139 174  ARG A CZ  
1138  N NH1 . ARG A 176  ? 0.2160 0.3137 0.2506 0.0313  0.0041  -0.1072 174  ARG A NH1 
1139  N NH2 . ARG A 176  ? 0.2824 0.3747 0.3205 0.0316  0.0013  -0.1116 174  ARG A NH2 
1140  N N   . CYS A 177  ? 0.2213 0.3863 0.2383 0.0295  0.0082  -0.1194 175  CYS A N   
1141  C CA  . CYS A 177  ? 0.2527 0.4214 0.2705 0.0303  0.0068  -0.1246 175  CYS A CA  
1142  C C   . CYS A 177  ? 0.2705 0.4519 0.2809 0.0275  0.0084  -0.1209 175  CYS A C   
1143  O O   . CYS A 177  ? 0.2922 0.4807 0.3030 0.0284  0.0072  -0.1264 175  CYS A O   
1144  C CB  . CYS A 177  ? 0.2483 0.3991 0.2693 0.0298  0.0049  -0.1227 175  CYS A CB  
1145  S SG  . CYS A 177  ? 0.2833 0.4188 0.3137 0.0328  0.0025  -0.1263 175  CYS A SG  
1146  N N   . GLY A 178  ? 0.2580 0.4421 0.2622 0.0240  0.0107  -0.1117 176  GLY A N   
1147  C CA  . GLY A 178  ? 0.2460 0.4453 0.2440 0.0216  0.0121  -0.1085 176  GLY A CA  
1148  C C   . GLY A 178  ? 0.2337 0.4293 0.2291 0.0196  0.0114  -0.1055 176  GLY A C   
1149  O O   . GLY A 178  ? 0.2598 0.4395 0.2569 0.0189  0.0104  -0.1030 176  GLY A O   
1150  N N   . GLU A 179  ? 0.2760 0.4880 0.2672 0.0185  0.0121  -0.1058 177  GLU A N   
1151  C CA  . GLU A 179  ? 0.2471 0.4583 0.2353 0.0164  0.0115  -0.1026 177  GLU A CA  
1152  C C   . GLU A 179  ? 0.2245 0.4251 0.2175 0.0185  0.0091  -0.1089 177  GLU A C   
1153  O O   . GLU A 179  ? 0.2785 0.4683 0.2703 0.0164  0.0086  -0.1036 177  GLU A O   
1154  C CB  . GLU A 179  ? 0.2434 0.4765 0.2272 0.0156  0.0124  -0.1037 177  GLU A CB  
1155  N N   . PRO A 180  ? 0.2517 0.4546 0.2505 0.0226  0.0073  -0.1199 178  PRO A N   
1156  C CA  . PRO A 180  ? 0.2474 0.4400 0.2513 0.0242  0.0047  -0.1252 178  PRO A CA  
1157  C C   . PRO A 180  ? 0.2508 0.4219 0.2570 0.0229  0.0041  -0.1192 178  PRO A C   
1158  O O   . PRO A 180  ? 0.2708 0.4342 0.2775 0.0219  0.0029  -0.1178 178  PRO A O   
1159  C CB  . PRO A 180  ? 0.2630 0.4608 0.2739 0.0289  0.0028  -0.1376 178  PRO A CB  
1160  C CG  . PRO A 180  ? 0.2770 0.4943 0.2849 0.0294  0.0044  -0.1393 178  PRO A CG  
1161  C CD  . PRO A 180  ? 0.2894 0.5064 0.2907 0.0259  0.0074  -0.1286 178  PRO A CD  
1162  N N   . VAL A 181  ? 0.2270 0.3888 0.2346 0.0229  0.0048  -0.1157 179  VAL A N   
1163  C CA  . VAL A 181  ? 0.2439 0.3864 0.2535 0.0218  0.0043  -0.1100 179  VAL A CA  
1164  C C   . VAL A 181  ? 0.2436 0.3820 0.2467 0.0177  0.0059  -0.0995 179  VAL A C   
1165  O O   . VAL A 181  ? 0.2515 0.3771 0.2556 0.0166  0.0051  -0.0957 179  VAL A O   
1166  C CB  . VAL A 181  ? 0.2561 0.3901 0.2692 0.0230  0.0045  -0.1092 179  VAL A CB  
1167  C CG1 . VAL A 181  ? 0.2289 0.3671 0.2362 0.0207  0.0072  -0.1018 179  VAL A CG1 
1168  C CG2 . VAL A 181  ? 0.2792 0.3945 0.2962 0.0227  0.0032  -0.1059 179  VAL A CG2 
1169  N N   . ILE A 182  ? 0.2482 0.3976 0.2453 0.0154  0.0079  -0.0945 180  ILE A N   
1170  C CA  . ILE A 182  ? 0.2153 0.3611 0.2069 0.0117  0.0090  -0.0847 180  ILE A CA  
1171  C C   . ILE A 182  ? 0.2924 0.4403 0.2831 0.0109  0.0080  -0.0856 180  ILE A C   
1172  O O   . ILE A 182  ? 0.2659 0.4032 0.2556 0.0091  0.0077  -0.0801 180  ILE A O   
1173  C CB  . ILE A 182  ? 0.2406 0.3985 0.2269 0.0093  0.0111  -0.0790 180  ILE A CB  
1174  C CG1 . ILE A 182  ? 0.2507 0.4061 0.2381 0.0099  0.0121  -0.0778 180  ILE A CG1 
1175  C CG2 . ILE A 182  ? 0.2743 0.4282 0.2560 0.0055  0.0118  -0.0691 180  ILE A CG2 
1176  C CD1 . ILE A 182  ? 0.2876 0.4575 0.2710 0.0081  0.0138  -0.0740 180  ILE A CD1 
1177  N N   . ARG A 183  ? 0.2489 0.4110 0.2398 0.0125  0.0073  -0.0927 181  ARG A N   
1178  C CA  . ARG A 183  ? 0.2893 0.4546 0.2795 0.0120  0.0060  -0.0945 181  ARG A CA  
1179  C C   . ARG A 183  ? 0.3360 0.4857 0.3315 0.0131  0.0040  -0.0968 181  ARG A C   
1180  O O   . ARG A 183  ? 0.3236 0.4672 0.3177 0.0113  0.0036  -0.0925 181  ARG A O   
1181  C CB  . ARG A 183  ? 0.3177 0.5013 0.3082 0.0142  0.0054  -0.1035 181  ARG A CB  
1182  C CG  . ARG A 183  ? 0.3769 0.5650 0.3682 0.0147  0.0035  -0.1083 181  ARG A CG  
1183  C CD  . ARG A 183  ? 0.4456 0.6315 0.4320 0.0111  0.0040  -0.0993 181  ARG A CD  
1184  N NE  . ARG A 183  ? 0.4603 0.6570 0.4403 0.0082  0.0062  -0.0916 181  ARG A NE  
1185  C CZ  . ARG A 183  ? 0.4353 0.6270 0.4116 0.0047  0.0070  -0.0813 181  ARG A CZ  
1186  N NH1 . ARG A 183  ? 0.4029 0.5792 0.3804 0.0037  0.0063  -0.0776 181  ARG A NH1 
1187  N NH2 . ARG A 183  ? 0.4925 0.6951 0.4640 0.0022  0.0086  -0.0746 181  ARG A NH2 
1188  N N   . ARG A 184  ? 0.2902 0.4332 0.2920 0.0161  0.0026  -0.1032 182  ARG A N   
1189  C CA  . ARG A 184  ? 0.3087 0.4374 0.3165 0.0171  0.0005  -0.1053 182  ARG A CA  
1190  C C   . ARG A 184  ? 0.3108 0.4242 0.3173 0.0147  0.0014  -0.0958 182  ARG A C   
1191  O O   . ARG A 184  ? 0.3065 0.4105 0.3148 0.0139  0.0003  -0.0940 182  ARG A O   
1192  C CB  . ARG A 184  ? 0.3018 0.4275 0.3173 0.0207  -0.0013 -0.1137 182  ARG A CB  
1193  C CG  . ARG A 184  ? 0.3593 0.4971 0.3785 0.0236  -0.0033 -0.1249 182  ARG A CG  
1194  C CD  . ARG A 184  ? 0.3534 0.4836 0.3786 0.0245  -0.0063 -0.1293 182  ARG A CD  
1195  N NE  . ARG A 184  ? 0.4191 0.5371 0.4534 0.0268  -0.0086 -0.1332 182  ARG A NE  
1196  C CZ  . ARG A 184  ? 0.4085 0.5108 0.4466 0.0258  -0.0097 -0.1287 182  ARG A CZ  
1197  N NH1 . ARG A 184  ? 0.4403 0.5364 0.4741 0.0227  -0.0086 -0.1206 182  ARG A NH1 
1198  N NH2 . ARG A 184  ? 0.3788 0.4716 0.4256 0.0280  -0.0119 -0.1324 182  ARG A NH2 
1199  N N   . GLY A 185  ? 0.2741 0.3850 0.2774 0.0135  0.0034  -0.0899 183  GLY A N   
1200  C CA  . GLY A 185  ? 0.2773 0.3749 0.2791 0.0114  0.0042  -0.0812 183  GLY A CA  
1201  C C   . GLY A 185  ? 0.3113 0.4099 0.3078 0.0084  0.0050  -0.0746 183  GLY A C   
1202  O O   . GLY A 185  ? 0.3090 0.3966 0.3059 0.0072  0.0047  -0.0702 183  GLY A O   
1203  N N   . VAL A 186  ? 0.2816 0.3938 0.2735 0.0071  0.0059  -0.0736 184  VAL A N   
1204  C CA  . VAL A 186  ? 0.3512 0.4655 0.3385 0.0043  0.0064  -0.0672 184  VAL A CA  
1205  C C   . VAL A 186  ? 0.3317 0.4431 0.3213 0.0047  0.0047  -0.0702 184  VAL A C   
1206  O O   . VAL A 186  ? 0.3323 0.4352 0.3211 0.0030  0.0046  -0.0648 184  VAL A O   
1207  C CB  . VAL A 186  ? 0.3173 0.4485 0.2999 0.0029  0.0075  -0.0659 184  VAL A CB  
1208  C CG1 . VAL A 186  ? 0.3452 0.4809 0.3243 0.0006  0.0072  -0.0615 184  VAL A CG1 
1209  C CG2 . VAL A 186  ? 0.3312 0.4628 0.3110 0.0014  0.0092  -0.0597 184  VAL A CG2 
1210  N N   . ASP A 187  ? 0.3222 0.4406 0.3151 0.0070  0.0031  -0.0790 185  ASP A N   
1211  C CA  . ASP A 187  ? 0.3617 0.4781 0.3572 0.0073  0.0012  -0.0823 185  ASP A CA  
1212  C C   . ASP A 187  ? 0.3943 0.4939 0.3948 0.0077  0.0001  -0.0812 185  ASP A C   
1213  O O   . ASP A 187  ? 0.3879 0.4820 0.3889 0.0066  -0.0006 -0.0787 185  ASP A O   
1214  C CB  . ASP A 187  ? 0.3702 0.4978 0.3689 0.0100  -0.0005 -0.0929 185  ASP A CB  
1215  C CG  . ASP A 187  ? 0.3797 0.5260 0.3732 0.0094  0.0005  -0.0939 185  ASP A CG  
1216  O OD1 . ASP A 187  ? 0.4302 0.5805 0.4179 0.0066  0.0020  -0.0860 185  ASP A OD1 
1217  O OD2 . ASP A 187  ? 0.3692 0.5264 0.3646 0.0119  -0.0003 -0.1025 185  ASP A OD2 
1218  N N   . MET A 188  ? 0.3554 0.4472 0.3597 0.0093  0.0001  -0.0826 186  MET A N   
1219  C CA  . MET A 188  ? 0.3634 0.4398 0.3723 0.0095  -0.0008 -0.0805 186  MET A CA  
1220  C C   . MET A 188  ? 0.3828 0.4511 0.3877 0.0069  0.0008  -0.0708 186  MET A C   
1221  O O   . MET A 188  ? 0.3983 0.4586 0.4049 0.0061  0.0000  -0.0683 186  MET A O   
1222  C CB  . MET A 188  ? 0.4073 0.4784 0.4208 0.0116  -0.0011 -0.0832 186  MET A CB  
1223  C CG  . MET A 188  ? 0.4554 0.5117 0.4742 0.0118  -0.0022 -0.0810 186  MET A CG  
1224  S SD  . MET A 188  ? 0.5750 0.6285 0.6019 0.0132  -0.0056 -0.0876 186  MET A SD  
1225  C CE  . MET A 188  ? 0.4183 0.4826 0.4495 0.0164  -0.0073 -0.0989 186  MET A CE  
1226  N N   . ALA A 189  ? 0.3728 0.4431 0.3726 0.0056  0.0028  -0.0654 187  ALA A N   
1227  C CA  . ALA A 189  ? 0.3646 0.4275 0.3609 0.0033  0.0041  -0.0568 187  ALA A CA  
1228  C C   . ALA A 189  ? 0.4010 0.4669 0.3947 0.0015  0.0038  -0.0539 187  ALA A C   
1229  O O   . ALA A 189  ? 0.3712 0.4285 0.3649 0.0004  0.0039  -0.0491 187  ALA A O   
1230  C CB  . ALA A 189  ? 0.3888 0.4546 0.3806 0.0022  0.0060  -0.0521 187  ALA A CB  
1231  N N   . MET A 190  ? 0.3521 0.4307 0.3435 0.0012  0.0036  -0.0567 188  MET A N   
1232  C CA  . MET A 190  ? 0.3999 0.4824 0.3889 -0.0005 0.0032  -0.0539 188  MET A CA  
1233  C C   . MET A 190  ? 0.3737 0.4490 0.3669 0.0001  0.0015  -0.0564 188  MET A C   
1234  O O   . MET A 190  ? 0.4110 0.4817 0.4033 -0.0014 0.0015  -0.0515 188  MET A O   
1235  C CB  . MET A 190  ? 0.3829 0.4817 0.3691 -0.0007 0.0030  -0.0573 188  MET A CB  
1236  C CG  . MET A 190  ? 0.4377 0.5423 0.4206 -0.0028 0.0027  -0.0533 188  MET A CG  
1237  S SD  . MET A 190  ? 0.5588 0.6840 0.5387 -0.0028 0.0024  -0.0578 188  MET A SD  
1238  C CE  . MET A 190  ? 0.4493 0.5822 0.4271 -0.0025 0.0041  -0.0577 188  MET A CE  
1239  N N   . ARG A 191  ? 0.3872 0.4616 0.3858 0.0023  -0.0001 -0.0639 189  ARG A N   
1240  C CA  . ARG A 191  ? 0.4120 0.4794 0.4158 0.0029  -0.0020 -0.0663 189  ARG A CA  
1241  C C   . ARG A 191  ? 0.4383 0.4915 0.4440 0.0023  -0.0015 -0.0606 189  ARG A C   
1242  O O   . ARG A 191  ? 0.4312 0.4792 0.4379 0.0013  -0.0021 -0.0578 189  ARG A O   
1243  C CB  . ARG A 191  ? 0.3994 0.4687 0.4095 0.0055  -0.0041 -0.0756 189  ARG A CB  
1244  N N   . MET A 192  ? 0.4276 0.4750 0.4337 0.0029  -0.0005 -0.0590 190  MET A N   
1245  C CA  . MET A 192  ? 0.4021 0.4372 0.4100 0.0025  -0.0001 -0.0538 190  MET A CA  
1246  C C   . MET A 192  ? 0.4274 0.4602 0.4302 0.0004  0.0015  -0.0461 190  MET A C   
1247  O O   . MET A 192  ? 0.4583 0.4839 0.4626 -0.0002 0.0013  -0.0426 190  MET A O   
1248  C CB  . MET A 192  ? 0.4202 0.4509 0.4293 0.0037  0.0007  -0.0537 190  MET A CB  
1249  C CG  . MET A 192  ? 0.4071 0.4395 0.4219 0.0060  -0.0010 -0.0613 190  MET A CG  
1250  S SD  . MET A 192  ? 0.5400 0.5661 0.5568 0.0072  -0.0003 -0.0603 190  MET A SD  
1251  C CE  . MET A 192  ? 0.3844 0.3974 0.4031 0.0062  -0.0002 -0.0535 190  MET A CE  
1252  N N   . MET A 193  ? 0.4245 0.4636 0.4219 -0.0007 0.0029  -0.0432 191  MET A N   
1253  C CA  . MET A 193  ? 0.4121 0.4486 0.4055 -0.0026 0.0041  -0.0358 191  MET A CA  
1254  C C   . MET A 193  ? 0.4313 0.4716 0.4233 -0.0039 0.0034  -0.0343 191  MET A C   
1255  O O   . MET A 193  ? 0.4613 0.4970 0.4518 -0.0051 0.0039  -0.0288 191  MET A O   
1256  C CB  . MET A 193  ? 0.4053 0.4466 0.3942 -0.0035 0.0055  -0.0328 191  MET A CB  
1257  C CG  . MET A 193  ? 0.3675 0.4036 0.3571 -0.0025 0.0063  -0.0327 191  MET A CG  
1258  S SD  . MET A 193  ? 0.5057 0.5444 0.4905 -0.0040 0.0078  -0.0270 191  MET A SD  
1259  C CE  . MET A 193  ? 0.4107 0.4648 0.3931 -0.0046 0.0078  -0.0298 191  MET A CE  
1260  N N   . GLY A 194  ? 0.4122 0.4612 0.4049 -0.0036 0.0022  -0.0393 192  GLY A N   
1261  C CA  . GLY A 194  ? 0.4241 0.4780 0.4153 -0.0048 0.0015  -0.0381 192  GLY A CA  
1262  C C   . GLY A 194  ? 0.4303 0.4799 0.4262 -0.0042 -0.0002 -0.0410 192  GLY A C   
1263  O O   . GLY A 194  ? 0.4579 0.5081 0.4532 -0.0054 -0.0007 -0.0385 192  GLY A O   
1264  N N   . GLU A 195  ? 0.4126 0.4578 0.4136 -0.0025 -0.0012 -0.0462 193  GLU A N   
1265  C CA  . GLU A 195  ? 0.4218 0.4640 0.4282 -0.0019 -0.0032 -0.0498 193  GLU A CA  
1266  C C   . GLU A 195  ? 0.4004 0.4311 0.4124 -0.0011 -0.0037 -0.0494 193  GLU A C   
1267  O O   . GLU A 195  ? 0.3404 0.3672 0.3568 -0.0013 -0.0051 -0.0497 193  GLU A O   
1268  C CB  . GLU A 195  ? 0.4588 0.5098 0.4679 -0.0006 -0.0051 -0.0584 193  GLU A CB  
1269  C CG  . GLU A 195  ? 0.5331 0.5974 0.5369 -0.0012 -0.0048 -0.0595 193  GLU A CG  
1270  C CD  . GLU A 195  ? 0.5897 0.6634 0.5961 0.0005  -0.0065 -0.0687 193  GLU A CD  
1271  O OE1 . GLU A 195  ? 0.5871 0.6561 0.6002 0.0021  -0.0085 -0.0743 193  GLU A OE1 
1272  O OE2 . GLU A 195  ? 0.6717 0.7579 0.6739 0.0004  -0.0061 -0.0703 193  GLU A OE2 
1273  N N   . GLN A 196  ? 0.4274 0.4534 0.4399 -0.0003 -0.0027 -0.0484 194  GLN A N   
1274  C CA  . GLN A 196  ? 0.4192 0.4353 0.4373 0.0005  -0.0033 -0.0479 194  GLN A CA  
1275  C C   . GLN A 196  ? 0.4531 0.4616 0.4688 -0.0004 -0.0015 -0.0404 194  GLN A C   
1276  O O   . GLN A 196  ? 0.4661 0.4678 0.4853 -0.0007 -0.0019 -0.0378 194  GLN A O   
1277  C CB  . GLN A 196  ? 0.4764 0.4926 0.4977 0.0023  -0.0040 -0.0528 194  GLN A CB  
1278  N N   . PHE A 197  ? 0.4295 0.4394 0.4396 -0.0009 0.0004  -0.0370 195  PHE A N   
1279  C CA  . PHE A 197  ? 0.4358 0.4392 0.4436 -0.0015 0.0020  -0.0305 195  PHE A CA  
1280  C C   . PHE A 197  ? 0.3991 0.4027 0.4046 -0.0029 0.0024  -0.0264 195  PHE A C   
1281  O O   . PHE A 197  ? 0.4337 0.4312 0.4393 -0.0032 0.0031  -0.0219 195  PHE A O   
1282  C CB  . PHE A 197  ? 0.4547 0.4594 0.4579 -0.0016 0.0037  -0.0285 195  PHE A CB  
1283  C CG  . PHE A 197  ? 0.4973 0.5006 0.5027 -0.0002 0.0036  -0.0315 195  PHE A CG  
1284  C CD1 . PHE A 197  ? 0.4986 0.4959 0.5098 0.0009  0.0025  -0.0330 195  PHE A CD1 
1285  C CD2 . PHE A 197  ? 0.4724 0.4805 0.4746 0.0000  0.0045  -0.0324 195  PHE A CD2 
1286  C CE1 . PHE A 197  ? 0.5175 0.5134 0.5312 0.0023  0.0023  -0.0355 195  PHE A CE1 
1287  C CE2 . PHE A 197  ? 0.5073 0.5143 0.5119 0.0014  0.0043  -0.0353 195  PHE A CE2 
1288  C CZ  . PHE A 197  ? 0.4839 0.4846 0.4943 0.0026  0.0032  -0.0368 195  PHE A CZ  
1289  N N   . VAL A 198  ? 0.3710 0.3818 0.3745 -0.0037 0.0018  -0.0278 196  VAL A N   
1290  C CA  . VAL A 198  ? 0.3537 0.3653 0.3555 -0.0050 0.0018  -0.0242 196  VAL A CA  
1291  C C   . VAL A 198  ? 0.3504 0.3671 0.3547 -0.0051 -0.0001 -0.0284 196  VAL A C   
1292  O O   . VAL A 198  ? 0.3770 0.3994 0.3825 -0.0044 -0.0011 -0.0340 196  VAL A O   
1293  C CB  . VAL A 198  ? 0.3248 0.3409 0.3209 -0.0062 0.0028  -0.0202 196  VAL A CB  
1294  C CG1 . VAL A 198  ? 0.3850 0.3956 0.3791 -0.0060 0.0044  -0.0162 196  VAL A CG1 
1295  C CG2 . VAL A 198  ? 0.3364 0.3626 0.3302 -0.0064 0.0025  -0.0236 196  VAL A CG2 
1296  N N   . THR A 199  ? 0.2962 0.3111 0.3017 -0.0059 -0.0006 -0.0260 197  THR A N   
1297  C CA  . THR A 199  ? 0.3188 0.3393 0.3260 -0.0063 -0.0023 -0.0294 197  THR A CA  
1298  C C   . THR A 199  ? 0.3377 0.3680 0.3400 -0.0072 -0.0022 -0.0294 197  THR A C   
1299  O O   . THR A 199  ? 0.3617 0.3997 0.3646 -0.0070 -0.0036 -0.0343 197  THR A O   
1300  C CB  . THR A 199  ? 0.3044 0.3204 0.3143 -0.0069 -0.0029 -0.0264 197  THR A CB  
1301  O OG1 . THR A 199  ? 0.3112 0.3188 0.3257 -0.0063 -0.0029 -0.0258 197  THR A OG1 
1302  C CG2 . THR A 199  ? 0.3199 0.3412 0.3323 -0.0073 -0.0049 -0.0303 197  THR A CG2 
1303  N N   . GLY A 200  ? 0.2991 0.3298 0.2969 -0.0081 -0.0008 -0.0239 198  GLY A N   
1304  C CA  . GLY A 200  ? 0.3148 0.3551 0.3081 -0.0091 -0.0006 -0.0229 198  GLY A CA  
1305  C C   . GLY A 200  ? 0.3117 0.3501 0.3014 -0.0099 0.0009  -0.0170 198  GLY A C   
1306  O O   . GLY A 200  ? 0.2887 0.3184 0.2791 -0.0097 0.0017  -0.0136 198  GLY A O   
1307  N N   . GLU A 201  ? 0.3245 0.3714 0.3105 -0.0109 0.0011  -0.0159 199  GLU A N   
1308  C CA  . GLU A 201  ? 0.3112 0.3568 0.2944 -0.0119 0.0021  -0.0101 199  GLU A CA  
1309  C C   . GLU A 201  ? 0.3215 0.3645 0.3044 -0.0131 0.0018  -0.0042 199  GLU A C   
1310  O O   . GLU A 201  ? 0.3192 0.3565 0.3016 -0.0134 0.0024  0.0003  199  GLU A O   
1311  C CB  . GLU A 201  ? 0.3557 0.4119 0.3357 -0.0128 0.0023  -0.0101 199  GLU A CB  
1312  N N   . THR A 202  ? 0.2935 0.3408 0.2770 -0.0137 0.0006  -0.0045 200  THR A N   
1313  C CA  . THR A 202  ? 0.2980 0.3434 0.2817 -0.0147 0.0000  0.0007  200  THR A CA  
1314  C C   . THR A 202  ? 0.2667 0.3083 0.2535 -0.0140 -0.0007 -0.0014 200  THR A C   
1315  O O   . THR A 202  ? 0.2651 0.3081 0.2538 -0.0132 -0.0012 -0.0069 200  THR A O   
1316  C CB  . THR A 202  ? 0.2878 0.3436 0.2692 -0.0165 -0.0009 0.0036  200  THR A CB  
1317  O OG1 . THR A 202  ? 0.3104 0.3746 0.2917 -0.0164 -0.0018 -0.0015 200  THR A OG1 
1318  C CG2 . THR A 202  ? 0.3037 0.3644 0.2824 -0.0175 -0.0003 0.0062  200  THR A CG2 
1319  N N   . ILE A 203  ? 0.2605 0.2978 0.2484 -0.0144 -0.0010 0.0028  201  ILE A N   
1320  C CA  . ILE A 203  ? 0.2644 0.2987 0.2555 -0.0139 -0.0017 0.0012  201  ILE A CA  
1321  C C   . ILE A 203  ? 0.2825 0.3258 0.2737 -0.0145 -0.0032 -0.0022 201  ILE A C   
1322  O O   . ILE A 203  ? 0.2716 0.3140 0.2657 -0.0139 -0.0039 -0.0065 201  ILE A O   
1323  C CB  . ILE A 203  ? 0.2463 0.2753 0.2386 -0.0141 -0.0017 0.0064  201  ILE A CB  
1324  C CG1 . ILE A 203  ? 0.2370 0.2624 0.2330 -0.0135 -0.0021 0.0048  201  ILE A CG1 
1325  C CG2 . ILE A 203  ? 0.2760 0.3112 0.2667 -0.0156 -0.0027 0.0108  201  ILE A CG2 
1326  C CD1 . ILE A 203  ? 0.2511 0.2702 0.2497 -0.0122 -0.0014 0.0015  201  ILE A CD1 
1327  N N   . ARG A 204  ? 0.2605 0.3129 0.2488 -0.0159 -0.0038 -0.0003 202  ARG A N   
1328  C CA  . ARG A 204  ? 0.2931 0.3554 0.2810 -0.0164 -0.0052 -0.0037 202  ARG A CA  
1329  C C   . ARG A 204  ? 0.2734 0.3390 0.2620 -0.0152 -0.0054 -0.0112 202  ARG A C   
1330  O O   . ARG A 204  ? 0.3016 0.3698 0.2925 -0.0148 -0.0067 -0.0160 202  ARG A O   
1331  C CB  . ARG A 204  ? 0.3398 0.4122 0.3242 -0.0181 -0.0058 0.0003  202  ARG A CB  
1332  C CG  . ARG A 204  ? 0.3768 0.4490 0.3619 -0.0192 -0.0067 0.0060  202  ARG A CG  
1333  C CD  . ARG A 204  ? 0.4222 0.5010 0.4046 -0.0210 -0.0071 0.0122  202  ARG A CD  
1334  N NE  . ARG A 204  ? 0.4045 0.4820 0.3884 -0.0219 -0.0082 0.0177  202  ARG A NE  
1335  C CZ  . ARG A 204  ? 0.4133 0.4807 0.3995 -0.0214 -0.0079 0.0213  202  ARG A CZ  
1336  N NH1 . ARG A 204  ? 0.3472 0.4052 0.3342 -0.0201 -0.0064 0.0204  202  ARG A NH1 
1337  N NH2 . ARG A 204  ? 0.3769 0.4441 0.3648 -0.0221 -0.0091 0.0258  202  ARG A NH2 
1338  N N   . GLU A 205  ? 0.2753 0.3410 0.2623 -0.0147 -0.0042 -0.0124 203  GLU A N   
1339  C CA  . GLU A 205  ? 0.2997 0.3680 0.2879 -0.0133 -0.0045 -0.0197 203  GLU A CA  
1340  C C   . GLU A 205  ? 0.3032 0.3617 0.2964 -0.0120 -0.0048 -0.0231 203  GLU A C   
1341  O O   . GLU A 205  ? 0.3083 0.3690 0.3044 -0.0110 -0.0061 -0.0295 203  GLU A O   
1342  C CB  . GLU A 205  ? 0.3101 0.3800 0.2957 -0.0131 -0.0031 -0.0196 203  GLU A CB  
1343  C CG  . GLU A 205  ? 0.3366 0.4111 0.3233 -0.0116 -0.0034 -0.0272 203  GLU A CG  
1344  C CD  . GLU A 205  ? 0.4273 0.5052 0.4112 -0.0114 -0.0021 -0.0268 203  GLU A CD  
1345  O OE1 . GLU A 205  ? 0.4015 0.4706 0.3859 -0.0110 -0.0008 -0.0247 203  GLU A OE1 
1346  O OE2 . GLU A 205  ? 0.4585 0.5485 0.4398 -0.0118 -0.0022 -0.0286 203  GLU A OE2 
1347  N N   . ALA A 206  ? 0.2751 0.3231 0.2695 -0.0118 -0.0037 -0.0190 204  ALA A N   
1348  C CA  . ALA A 206  ? 0.2940 0.3333 0.2933 -0.0107 -0.0040 -0.0213 204  ALA A CA  
1349  C C   . ALA A 206  ? 0.2867 0.3267 0.2894 -0.0110 -0.0057 -0.0229 204  ALA A C   
1350  O O   . ALA A 206  ? 0.2983 0.3364 0.3057 -0.0102 -0.0070 -0.0278 204  ALA A O   
1351  C CB  . ALA A 206  ? 0.2566 0.2861 0.2560 -0.0105 -0.0025 -0.0161 204  ALA A CB  
1352  N N   . LEU A 207  ? 0.2659 0.3087 0.2670 -0.0122 -0.0060 -0.0189 205  LEU A N   
1353  C CA  . LEU A 207  ? 0.2811 0.3254 0.2853 -0.0126 -0.0078 -0.0203 205  LEU A CA  
1354  C C   . LEU A 207  ? 0.3166 0.3697 0.3217 -0.0124 -0.0096 -0.0271 205  LEU A C   
1355  O O   . LEU A 207  ? 0.3246 0.3769 0.3343 -0.0121 -0.0114 -0.0310 205  LEU A O   
1356  C CB  . LEU A 207  ? 0.3079 0.3546 0.3099 -0.0139 -0.0078 -0.0145 205  LEU A CB  
1357  C CG  . LEU A 207  ? 0.3004 0.3383 0.3031 -0.0139 -0.0065 -0.0087 205  LEU A CG  
1358  C CD1 . LEU A 207  ? 0.2710 0.3119 0.2715 -0.0150 -0.0067 -0.0031 205  LEU A CD1 
1359  C CD2 . LEU A 207  ? 0.2588 0.2899 0.2668 -0.0133 -0.0069 -0.0097 205  LEU A CD2 
1360  N N   . LYS A 208  ? 0.2896 0.3517 0.2906 -0.0125 -0.0094 -0.0288 206  LYS A N   
1361  C CA  . LYS A 208  ? 0.3534 0.4251 0.3550 -0.0120 -0.0111 -0.0359 206  LYS A CA  
1362  C C   . LYS A 208  ? 0.3012 0.3684 0.3078 -0.0103 -0.0120 -0.0427 206  LYS A C   
1363  O O   . LYS A 208  ? 0.3882 0.4577 0.3991 -0.0097 -0.0142 -0.0486 206  LYS A O   
1364  C CB  . LYS A 208  ? 0.3194 0.4022 0.3154 -0.0123 -0.0105 -0.0359 206  LYS A CB  
1365  N N   . ARG A 209  ? 0.3321 0.3928 0.3390 -0.0095 -0.0105 -0.0420 207  ARG A N   
1366  C CA  . ARG A 209  ? 0.3294 0.3857 0.3414 -0.0079 -0.0114 -0.0480 207  ARG A CA  
1367  C C   . ARG A 209  ? 0.3508 0.3970 0.3694 -0.0078 -0.0125 -0.0475 207  ARG A C   
1368  O O   . ARG A 209  ? 0.3982 0.4408 0.4224 -0.0066 -0.0139 -0.0524 207  ARG A O   
1369  C CB  . ARG A 209  ? 0.3304 0.3837 0.3402 -0.0071 -0.0095 -0.0468 207  ARG A CB  
1370  C CG  . ARG A 209  ? 0.3824 0.4468 0.3868 -0.0071 -0.0088 -0.0481 207  ARG A CG  
1371  C CD  . ARG A 209  ? 0.4033 0.4645 0.4049 -0.0069 -0.0067 -0.0452 207  ARG A CD  
1372  N NE  . ARG A 209  ? 0.4752 0.5474 0.4725 -0.0068 -0.0061 -0.0471 207  ARG A NE  
1373  C CZ  . ARG A 209  ? 0.5230 0.5950 0.5180 -0.0065 -0.0045 -0.0458 207  ARG A CZ  
1374  N NH1 . ARG A 209  ? 0.4524 0.5137 0.4486 -0.0062 -0.0033 -0.0427 207  ARG A NH1 
1375  N NH2 . ARG A 209  ? 0.5670 0.6503 0.5584 -0.0065 -0.0040 -0.0476 207  ARG A NH2 
1376  N N   . SER A 210  ? 0.3603 0.4023 0.3786 -0.0090 -0.0120 -0.0416 208  SER A N   
1377  C CA  . SER A 210  ? 0.3396 0.3730 0.3642 -0.0091 -0.0129 -0.0405 208  SER A CA  
1378  C C   . SER A 210  ? 0.3554 0.3919 0.3851 -0.0093 -0.0157 -0.0451 208  SER A C   
1379  O O   . SER A 210  ? 0.3183 0.3483 0.3547 -0.0093 -0.0171 -0.0457 208  SER A O   
1380  C CB  . SER A 210  ? 0.3175 0.3456 0.3401 -0.0100 -0.0111 -0.0326 208  SER A CB  
1381  O OG  . SER A 210  ? 0.3357 0.3602 0.3545 -0.0097 -0.0087 -0.0288 208  SER A OG  
1382  N N   . LYS A 211  ? 0.3617 0.4081 0.3886 -0.0096 -0.0168 -0.0483 209  LYS A N   
1383  C CA  . LYS A 211  ? 0.3500 0.3998 0.3814 -0.0099 -0.0196 -0.0524 209  LYS A CA  
1384  C C   . LYS A 211  ? 0.3598 0.4069 0.3991 -0.0087 -0.0222 -0.0597 209  LYS A C   
1385  O O   . LYS A 211  ? 0.3592 0.4028 0.4051 -0.0091 -0.0244 -0.0611 209  LYS A O   
1386  C CB  . LYS A 211  ? 0.3794 0.4417 0.4059 -0.0103 -0.0203 -0.0547 209  LYS A CB  
1387  N N   . GLU A 212  ? 0.3819 0.4303 0.4211 -0.0072 -0.0221 -0.0644 210  GLU A N   
1388  C CA  . GLU A 212  ? 0.3818 0.4286 0.4289 -0.0058 -0.0250 -0.0722 210  GLU A CA  
1389  C C   . GLU A 212  ? 0.3717 0.4069 0.4269 -0.0062 -0.0260 -0.0697 210  GLU A C   
1390  O O   . GLU A 212  ? 0.3603 0.3938 0.4233 -0.0062 -0.0291 -0.0735 210  GLU A O   
1391  C CB  . GLU A 212  ? 0.4120 0.4617 0.4574 -0.0040 -0.0244 -0.0768 210  GLU A CB  
1392  C CG  . GLU A 212  ? 0.4729 0.5209 0.5270 -0.0023 -0.0275 -0.0853 210  GLU A CG  
1393  C CD  . GLU A 212  ? 0.5619 0.6131 0.6146 -0.0003 -0.0268 -0.0898 210  GLU A CD  
1394  O OE1 . GLU A 212  ? 0.5934 0.6482 0.6382 -0.0006 -0.0238 -0.0860 210  GLU A OE1 
1395  O OE2 . GLU A 212  ? 0.6484 0.6985 0.7084 0.0014  -0.0295 -0.0972 210  GLU A OE2 
1396  N N   . LEU A 213  ? 0.3626 0.3901 0.4162 -0.0065 -0.0234 -0.0630 211  LEU A N   
1397  C CA  . LEU A 213  ? 0.3569 0.3743 0.4179 -0.0069 -0.0242 -0.0599 211  LEU A CA  
1398  C C   . LEU A 213  ? 0.3597 0.3744 0.4222 -0.0086 -0.0242 -0.0544 211  LEU A C   
1399  O O   . LEU A 213  ? 0.3455 0.3542 0.4158 -0.0092 -0.0259 -0.0533 211  LEU A O   
1400  C CB  . LEU A 213  ? 0.3409 0.3520 0.3998 -0.0065 -0.0216 -0.0553 211  LEU A CB  
1401  C CG  . LEU A 213  ? 0.3749 0.3866 0.4350 -0.0046 -0.0222 -0.0609 211  LEU A CG  
1402  C CD1 . LEU A 213  ? 0.3514 0.3570 0.4096 -0.0043 -0.0197 -0.0561 211  LEU A CD1 
1403  C CD2 . LEU A 213  ? 0.3879 0.3976 0.4585 -0.0039 -0.0261 -0.0675 211  LEU A CD2 
1404  N N   . GLU A 214  ? 0.3367 0.3561 0.3922 -0.0095 -0.0225 -0.0506 212  GLU A N   
1405  C CA  . GLU A 214  ? 0.3582 0.3761 0.4157 -0.0110 -0.0228 -0.0463 212  GLU A CA  
1406  C C   . GLU A 214  ? 0.3660 0.3867 0.4304 -0.0113 -0.0266 -0.0518 212  GLU A C   
1407  O O   . GLU A 214  ? 0.3568 0.3733 0.4272 -0.0124 -0.0278 -0.0494 212  GLU A O   
1408  C CB  . GLU A 214  ? 0.3566 0.3795 0.4058 -0.0117 -0.0207 -0.0417 212  GLU A CB  
1409  C CG  . GLU A 214  ? 0.3001 0.3185 0.3443 -0.0117 -0.0173 -0.0347 212  GLU A CG  
1410  C CD  . GLU A 214  ? 0.3437 0.3662 0.3811 -0.0124 -0.0157 -0.0301 212  GLU A CD  
1411  O OE1 . GLU A 214  ? 0.3660 0.3961 0.4016 -0.0129 -0.0170 -0.0325 212  GLU A OE1 
1412  O OE2 . GLU A 214  ? 0.3367 0.3552 0.3711 -0.0125 -0.0134 -0.0242 212  GLU A OE2 
1413  N N   . GLU A 215  ? 0.3582 0.3863 0.4219 -0.0104 -0.0284 -0.0594 213  GLU A N   
1414  C CA  . GLU A 215  ? 0.3722 0.4033 0.4428 -0.0105 -0.0323 -0.0659 213  GLU A CA  
1415  C C   . GLU A 215  ? 0.4284 0.4519 0.5099 -0.0102 -0.0350 -0.0688 213  GLU A C   
1416  O O   . GLU A 215  ? 0.4123 0.4357 0.5015 -0.0107 -0.0384 -0.0724 213  GLU A O   
1417  C CB  . GLU A 215  ? 0.4043 0.4461 0.4715 -0.0093 -0.0335 -0.0740 213  GLU A CB  
1418  N N   . LYS A 216  ? 0.3867 0.4038 0.4694 -0.0094 -0.0338 -0.0670 214  LYS A N   
1419  C CA  . LYS A 216  ? 0.3799 0.3893 0.4733 -0.0093 -0.0363 -0.0684 214  LYS A CA  
1420  C C   . LYS A 216  ? 0.4169 0.4183 0.5140 -0.0109 -0.0353 -0.0598 214  LYS A C   
1421  O O   . LYS A 216  ? 0.4434 0.4385 0.5501 -0.0112 -0.0376 -0.0597 214  LYS A O   
1422  C CB  . LYS A 216  ? 0.3652 0.3725 0.4584 -0.0075 -0.0357 -0.0713 214  LYS A CB  
1423  N N   . GLY A 217  ? 0.3870 0.3889 0.4773 -0.0119 -0.0322 -0.0526 215  GLY A N   
1424  C CA  . GLY A 217  ? 0.3391 0.3349 0.4322 -0.0133 -0.0310 -0.0446 215  GLY A CA  
1425  C C   . GLY A 217  ? 0.3569 0.3494 0.4439 -0.0130 -0.0271 -0.0380 215  GLY A C   
1426  O O   . GLY A 217  ? 0.3491 0.3376 0.4378 -0.0140 -0.0258 -0.0312 215  GLY A O   
1427  N N   . PHE A 218  ? 0.3333 0.3277 0.4134 -0.0117 -0.0252 -0.0398 216  PHE A N   
1428  C CA  . PHE A 218  ? 0.2933 0.2850 0.3670 -0.0114 -0.0215 -0.0337 216  PHE A CA  
1429  C C   . PHE A 218  ? 0.3056 0.3008 0.3714 -0.0119 -0.0190 -0.0293 216  PHE A C   
1430  O O   . PHE A 218  ? 0.2906 0.2914 0.3543 -0.0123 -0.0199 -0.0316 216  PHE A O   
1431  C CB  . PHE A 218  ? 0.2907 0.2833 0.3600 -0.0098 -0.0204 -0.0370 216  PHE A CB  
1432  C CG  . PHE A 218  ? 0.3267 0.3149 0.4033 -0.0090 -0.0224 -0.0403 216  PHE A CG  
1433  C CD1 . PHE A 218  ? 0.3395 0.3295 0.4227 -0.0084 -0.0260 -0.0480 216  PHE A CD1 
1434  C CD2 . PHE A 218  ? 0.3179 0.3006 0.3949 -0.0087 -0.0208 -0.0361 216  PHE A CD2 
1435  C CE1 . PHE A 218  ? 0.3343 0.3200 0.4249 -0.0075 -0.0280 -0.0511 216  PHE A CE1 
1436  C CE2 . PHE A 218  ? 0.3332 0.3119 0.4173 -0.0079 -0.0228 -0.0388 216  PHE A CE2 
1437  C CZ  . PHE A 218  ? 0.2849 0.2649 0.3760 -0.0073 -0.0264 -0.0463 216  PHE A CZ  
1438  N N   . SER A 219  ? 0.2529 0.2451 0.3146 -0.0119 -0.0161 -0.0232 217  SER A N   
1439  C CA  . SER A 219  ? 0.2601 0.2550 0.3142 -0.0120 -0.0136 -0.0191 217  SER A CA  
1440  C C   . SER A 219  ? 0.2480 0.2416 0.2957 -0.0110 -0.0110 -0.0174 217  SER A C   
1441  O O   . SER A 219  ? 0.2392 0.2300 0.2884 -0.0102 -0.0110 -0.0192 217  SER A O   
1442  C CB  . SER A 219  ? 0.2622 0.2548 0.3182 -0.0129 -0.0127 -0.0130 217  SER A CB  
1443  O OG  . SER A 219  ? 0.2861 0.2734 0.3452 -0.0127 -0.0117 -0.0094 217  SER A OG  
1444  N N   . TYR A 220  ? 0.2352 0.2309 0.2763 -0.0110 -0.0089 -0.0139 218  TYR A N   
1445  C CA  . TYR A 220  ? 0.2482 0.2434 0.2831 -0.0102 -0.0067 -0.0125 218  TYR A CA  
1446  C C   . TYR A 220  ? 0.2520 0.2448 0.2837 -0.0101 -0.0045 -0.0064 218  TYR A C   
1447  O O   . TYR A 220  ? 0.2410 0.2347 0.2731 -0.0106 -0.0044 -0.0036 218  TYR A O   
1448  C CB  . TYR A 220  ? 0.2523 0.2539 0.2818 -0.0102 -0.0069 -0.0155 218  TYR A CB  
1449  C CG  . TYR A 220  ? 0.2563 0.2603 0.2876 -0.0096 -0.0085 -0.0219 218  TYR A CG  
1450  C CD1 . TYR A 220  ? 0.2846 0.2917 0.3207 -0.0099 -0.0111 -0.0269 218  TYR A CD1 
1451  C CD2 . TYR A 220  ? 0.2725 0.2759 0.3013 -0.0087 -0.0074 -0.0232 218  TYR A CD2 
1452  C CE1 . TYR A 220  ? 0.2907 0.3002 0.3289 -0.0090 -0.0127 -0.0335 218  TYR A CE1 
1453  C CE2 . TYR A 220  ? 0.2901 0.2960 0.3208 -0.0079 -0.0088 -0.0293 218  TYR A CE2 
1454  C CZ  . TYR A 220  ? 0.3046 0.3136 0.3401 -0.0080 -0.0115 -0.0346 218  TYR A CZ  
1455  O OH  . TYR A 220  ? 0.2985 0.3103 0.3364 -0.0069 -0.0130 -0.0413 218  TYR A OH  
1456  N N   . SER A 221  ? 0.2372 0.2270 0.2659 -0.0092 -0.0027 -0.0047 219  SER A N   
1457  C CA  . SER A 221  ? 0.2315 0.2198 0.2560 -0.0088 -0.0006 -0.0001 219  SER A CA  
1458  C C   . SER A 221  ? 0.2358 0.2250 0.2549 -0.0083 0.0004  -0.0009 219  SER A C   
1459  O O   . SER A 221  ? 0.2678 0.2553 0.2871 -0.0077 0.0006  -0.0029 219  SER A O   
1460  C CB  . SER A 221  ? 0.2500 0.2337 0.2769 -0.0082 0.0007  0.0034  219  SER A CB  
1461  O OG  . SER A 221  ? 0.2520 0.2350 0.2752 -0.0075 0.0025  0.0071  219  SER A OG  
1462  N N   . TYR A 222  ? 0.1945 0.1865 0.2092 -0.0085 0.0009  0.0008  220  TYR A N   
1463  C CA  . TYR A 222  ? 0.2301 0.2241 0.2402 -0.0084 0.0015  0.0002  220  TYR A CA  
1464  C C   . TYR A 222  ? 0.2262 0.2162 0.2337 -0.0076 0.0032  0.0036  220  TYR A C   
1465  O O   . TYR A 222  ? 0.2425 0.2307 0.2500 -0.0073 0.0038  0.0069  220  TYR A O   
1466  C CB  . TYR A 222  ? 0.2278 0.2279 0.2350 -0.0094 0.0007  0.0003  220  TYR A CB  
1467  C CG  . TYR A 222  ? 0.2130 0.2178 0.2223 -0.0100 -0.0011 -0.0038 220  TYR A CG  
1468  C CD1 . TYR A 222  ? 0.2295 0.2379 0.2384 -0.0099 -0.0017 -0.0084 220  TYR A CD1 
1469  C CD2 . TYR A 222  ? 0.2284 0.2343 0.2407 -0.0106 -0.0022 -0.0034 220  TYR A CD2 
1470  C CE1 . TYR A 222  ? 0.2320 0.2450 0.2431 -0.0102 -0.0036 -0.0129 220  TYR A CE1 
1471  C CE2 . TYR A 222  ? 0.2458 0.2562 0.2604 -0.0111 -0.0041 -0.0077 220  TYR A CE2 
1472  C CZ  . TYR A 222  ? 0.2392 0.2532 0.2533 -0.0108 -0.0048 -0.0125 220  TYR A CZ  
1473  O OH  . TYR A 222  ? 0.2698 0.2885 0.2864 -0.0111 -0.0068 -0.0174 220  TYR A OH  
1474  N N   . ASP A 223  ? 0.2381 0.2274 0.2435 -0.0071 0.0039  0.0023  221  ASP A N   
1475  C CA  . ASP A 223  ? 0.2609 0.2466 0.2639 -0.0063 0.0053  0.0047  221  ASP A CA  
1476  C C   . ASP A 223  ? 0.2776 0.2664 0.2765 -0.0068 0.0053  0.0048  221  ASP A C   
1477  O O   . ASP A 223  ? 0.2972 0.2886 0.2951 -0.0070 0.0051  0.0021  221  ASP A O   
1478  C CB  . ASP A 223  ? 0.2694 0.2516 0.2740 -0.0054 0.0059  0.0033  221  ASP A CB  
1479  C CG  . ASP A 223  ? 0.3450 0.3243 0.3467 -0.0046 0.0073  0.0049  221  ASP A CG  
1480  O OD1 . ASP A 223  ? 0.3678 0.3468 0.3672 -0.0045 0.0077  0.0075  221  ASP A OD1 
1481  O OD2 . ASP A 223  ? 0.3984 0.3759 0.4008 -0.0040 0.0076  0.0035  221  ASP A OD2 
1482  N N   . MET A 224  ? 0.2972 0.2862 0.2943 -0.0071 0.0054  0.0081  222  MET A N   
1483  C CA  . MET A 224  ? 0.2886 0.2803 0.2826 -0.0078 0.0053  0.0093  222  MET A CA  
1484  C C   . MET A 224  ? 0.3248 0.3127 0.3174 -0.0069 0.0063  0.0093  222  MET A C   
1485  O O   . MET A 224  ? 0.3774 0.3612 0.3701 -0.0060 0.0069  0.0115  222  MET A O   
1486  C CB  . MET A 224  ? 0.3056 0.2982 0.2992 -0.0083 0.0046  0.0130  222  MET A CB  
1487  C CG  . MET A 224  ? 0.3433 0.3396 0.3384 -0.0091 0.0035  0.0132  222  MET A CG  
1488  S SD  . MET A 224  ? 0.3533 0.3576 0.3473 -0.0104 0.0025  0.0098  222  MET A SD  
1489  C CE  . MET A 224  ? 0.3826 0.3919 0.3734 -0.0118 0.0020  0.0128  222  MET A CE  
1490  N N   . LEU A 225  ? 0.3365 0.3261 0.3282 -0.0070 0.0065  0.0066  223  LEU A N   
1491  C CA  . LEU A 225  ? 0.3626 0.3488 0.3533 -0.0061 0.0075  0.0063  223  LEU A CA  
1492  C C   . LEU A 225  ? 0.4016 0.3868 0.3903 -0.0063 0.0076  0.0094  223  LEU A C   
1493  O O   . LEU A 225  ? 0.4263 0.4152 0.4138 -0.0075 0.0068  0.0111  223  LEU A O   
1494  C CB  . LEU A 225  ? 0.3750 0.3644 0.3652 -0.0063 0.0075  0.0029  223  LEU A CB  
1495  C CG  . LEU A 225  ? 0.3886 0.3778 0.3818 -0.0056 0.0072  -0.0008 223  LEU A CG  
1496  C CD1 . LEU A 225  ? 0.4128 0.4061 0.4052 -0.0057 0.0069  -0.0045 223  LEU A CD1 
1497  C CD2 . LEU A 225  ? 0.3567 0.3396 0.3520 -0.0044 0.0079  -0.0002 223  LEU A CD2 
1498  N N   . GLY A 226  ? 0.4234 0.4038 0.4120 -0.0051 0.0084  0.0101  224  GLY A N   
1499  C CA  . GLY A 226  ? 0.4604 0.4394 0.4476 -0.0052 0.0083  0.0123  224  GLY A CA  
1500  C C   . GLY A 226  ? 0.4673 0.4414 0.4545 -0.0036 0.0092  0.0121  224  GLY A C   
1501  O O   . GLY A 226  ? 0.4949 0.4669 0.4833 -0.0026 0.0100  0.0109  224  GLY A O   
1502  N N   . GLU A 227  ? 0.4783 0.4509 0.4646 -0.0035 0.0089  0.0134  225  GLU A N   
1503  C CA  . GLU A 227  ? 0.5083 0.4767 0.4945 -0.0019 0.0096  0.0132  225  GLU A CA  
1504  C C   . GLU A 227  ? 0.4117 0.3779 0.3994 -0.0007 0.0094  0.0145  225  GLU A C   
1505  O O   . GLU A 227  ? 0.4341 0.4013 0.4228 -0.0013 0.0085  0.0160  225  GLU A O   
1506  C CB  . GLU A 227  ? 0.4722 0.4400 0.4572 -0.0022 0.0091  0.0136  225  GLU A CB  
1507  C CG  . GLU A 227  ? 0.5431 0.5129 0.5267 -0.0029 0.0096  0.0120  225  GLU A CG  
1508  C CD  . GLU A 227  ? 0.6303 0.5982 0.6141 -0.0015 0.0107  0.0100  225  GLU A CD  
1509  O OE1 . GLU A 227  ? 0.6179 0.5827 0.6017 -0.0001 0.0112  0.0102  225  GLU A OE1 
1510  O OE2 . GLU A 227  ? 0.7999 0.7698 0.7839 -0.0018 0.0111  0.0082  225  GLU A OE2 
1511  N N   . ALA A 228  ? 0.3862 0.3498 0.3739 0.0010  0.0102  0.0139  226  ALA A N   
1512  C CA  . ALA A 228  ? 0.3887 0.3507 0.3777 0.0025  0.0100  0.0146  226  ALA A CA  
1513  C C   . ALA A 228  ? 0.3430 0.3039 0.3325 0.0023  0.0085  0.0156  226  ALA A C   
1514  O O   . ALA A 228  ? 0.3464 0.3069 0.3350 0.0015  0.0079  0.0156  226  ALA A O   
1515  C CB  . ALA A 228  ? 0.3093 0.2700 0.2979 0.0045  0.0112  0.0136  226  ALA A CB  
1516  N N   . ALA A 229  ? 0.2737 0.2340 0.2652 0.0031  0.0076  0.0165  227  ALA A N   
1517  C CA  . ALA A 229  ? 0.2610 0.2202 0.2542 0.0026  0.0056  0.0179  227  ALA A CA  
1518  C C   . ALA A 229  ? 0.2779 0.2343 0.2713 0.0041  0.0051  0.0165  227  ALA A C   
1519  O O   . ALA A 229  ? 0.2605 0.2160 0.2537 0.0063  0.0060  0.0146  227  ALA A O   
1520  C CB  . ALA A 229  ? 0.2844 0.2437 0.2804 0.0031  0.0046  0.0191  227  ALA A CB  
1521  N N   . THR A 230  ? 0.2603 0.2158 0.2541 0.0028  0.0037  0.0174  228  THR A N   
1522  C CA  . THR A 230  ? 0.2665 0.2192 0.2613 0.0040  0.0026  0.0161  228  THR A CA  
1523  C C   . THR A 230  ? 0.2395 0.1901 0.2385 0.0043  0.0000  0.0172  228  THR A C   
1524  O O   . THR A 230  ? 0.2366 0.1847 0.2374 0.0061  -0.0011 0.0154  228  THR A O   
1525  C CB  . THR A 230  ? 0.3144 0.2675 0.3076 0.0023  0.0025  0.0164  228  THR A CB  
1526  O OG1 . THR A 230  ? 0.3796 0.3345 0.3695 0.0023  0.0048  0.0152  228  THR A OG1 
1527  C CG2 . THR A 230  ? 0.3891 0.3394 0.3833 0.0034  0.0013  0.0150  228  THR A CG2 
1528  N N   . THR A 231  ? 0.2632 0.2151 0.2641 0.0027  -0.0012 0.0201  229  THR A N   
1529  C CA  . THR A 231  ? 0.2173 0.1672 0.2230 0.0026  -0.0041 0.0218  229  THR A CA  
1530  C C   . THR A 231  ? 0.2215 0.1728 0.2290 0.0028  -0.0044 0.0232  229  THR A C   
1531  O O   . THR A 231  ? 0.2351 0.1893 0.2400 0.0022  -0.0025 0.0235  229  THR A O   
1532  C CB  . THR A 231  ? 0.2583 0.2088 0.2656 -0.0003 -0.0061 0.0252  229  THR A CB  
1533  O OG1 . THR A 231  ? 0.2667 0.2216 0.2722 -0.0026 -0.0055 0.0280  229  THR A OG1 
1534  C CG2 . THR A 231  ? 0.2492 0.1992 0.2543 -0.0008 -0.0056 0.0240  229  THR A CG2 
1535  N N   . ALA A 232  ? 0.2334 0.1825 0.2458 0.0037  -0.0068 0.0239  230  ALA A N   
1536  C CA  . ALA A 232  ? 0.2444 0.1948 0.2593 0.0036  -0.0076 0.0258  230  ALA A CA  
1537  C C   . ALA A 232  ? 0.2729 0.2270 0.2866 0.0004  -0.0078 0.0299  230  ALA A C   
1538  O O   . ALA A 232  ? 0.2752 0.2321 0.2877 0.0000  -0.0068 0.0306  230  ALA A O   
1539  C CB  . ALA A 232  ? 0.2918 0.2389 0.3130 0.0049  -0.0108 0.0262  230  ALA A CB  
1540  N N   . ALA A 233  ? 0.2889 0.2436 0.3031 -0.0020 -0.0093 0.0325  231  ALA A N   
1541  C CA  . ALA A 233  ? 0.2743 0.2337 0.2874 -0.0051 -0.0096 0.0365  231  ALA A CA  
1542  C C   . ALA A 233  ? 0.2844 0.2478 0.2920 -0.0057 -0.0066 0.0348  231  ALA A C   
1543  O O   . ALA A 233  ? 0.2933 0.2609 0.2999 -0.0070 -0.0064 0.0365  231  ALA A O   
1544  C CB  . ALA A 233  ? 0.3304 0.2905 0.3451 -0.0076 -0.0116 0.0397  231  ALA A CB  
1545  N N   . ASP A 234  ? 0.2522 0.2143 0.2566 -0.0046 -0.0046 0.0314  232  ASP A N   
1546  C CA  . ASP A 234  ? 0.2693 0.2347 0.2694 -0.0050 -0.0021 0.0297  232  ASP A CA  
1547  C C   . ASP A 234  ? 0.2774 0.2429 0.2773 -0.0035 -0.0008 0.0281  232  ASP A C   
1548  O O   . ASP A 234  ? 0.2736 0.2426 0.2716 -0.0045 0.0002  0.0280  232  ASP A O   
1549  C CB  . ASP A 234  ? 0.3463 0.3103 0.3436 -0.0044 -0.0005 0.0270  232  ASP A CB  
1550  C CG  . ASP A 234  ? 0.3622 0.3278 0.3592 -0.0064 -0.0014 0.0287  232  ASP A CG  
1551  O OD1 . ASP A 234  ? 0.3992 0.3678 0.3976 -0.0086 -0.0031 0.0322  232  ASP A OD1 
1552  O OD2 . ASP A 234  ? 0.4285 0.3925 0.4239 -0.0058 -0.0006 0.0267  232  ASP A OD2 
1553  N N   . ALA A 235  ? 0.2494 0.2115 0.2514 -0.0011 -0.0009 0.0268  233  ALA A N   
1554  C CA  . ALA A 235  ? 0.2295 0.1922 0.2318 0.0002  0.0002  0.0258  233  ALA A CA  
1555  C C   . ALA A 235  ? 0.2493 0.2148 0.2536 -0.0012 -0.0012 0.0287  233  ALA A C   
1556  O O   . ALA A 235  ? 0.2580 0.2260 0.2614 -0.0015 -0.0002 0.0284  233  ALA A O   
1557  C CB  . ALA A 235  ? 0.2402 0.1999 0.2446 0.0031  0.0002  0.0239  233  ALA A CB  
1558  N N   . GLU A 236  ? 0.2541 0.2190 0.2614 -0.0021 -0.0037 0.0315  234  GLU A N   
1559  C CA  . GLU A 236  ? 0.2602 0.2282 0.2695 -0.0036 -0.0052 0.0347  234  GLU A CA  
1560  C C   . GLU A 236  ? 0.2578 0.2313 0.2639 -0.0062 -0.0046 0.0360  234  GLU A C   
1561  O O   . GLU A 236  ? 0.2701 0.2471 0.2761 -0.0070 -0.0047 0.0369  234  GLU A O   
1562  C CB  . GLU A 236  ? 0.2947 0.2609 0.3087 -0.0041 -0.0083 0.0380  234  GLU A CB  
1563  N N   . ARG A 237  ? 0.2592 0.2338 0.2626 -0.0074 -0.0041 0.0356  235  ARG A N   
1564  C CA  . ARG A 237  ? 0.2883 0.2688 0.2885 -0.0095 -0.0033 0.0358  235  ARG A CA  
1565  C C   . ARG A 237  ? 0.2859 0.2674 0.2839 -0.0086 -0.0012 0.0324  235  ARG A C   
1566  O O   . ARG A 237  ? 0.2804 0.2667 0.2774 -0.0098 -0.0012 0.0326  235  ARG A O   
1567  C CB  . ARG A 237  ? 0.3048 0.2863 0.3029 -0.0106 -0.0030 0.0356  235  ARG A CB  
1568  C CG  . ARG A 237  ? 0.3748 0.3632 0.3697 -0.0124 -0.0021 0.0351  235  ARG A CG  
1569  C CD  . ARG A 237  ? 0.4610 0.4519 0.4543 -0.0139 -0.0021 0.0358  235  ARG A CD  
1570  N NE  . ARG A 237  ? 0.4854 0.4731 0.4767 -0.0125 -0.0003 0.0320  235  ARG A NE  
1571  C CZ  . ARG A 237  ? 0.4984 0.4808 0.4906 -0.0115 -0.0004 0.0317  235  ARG A CZ  
1572  N NH1 . ARG A 237  ? 0.5046 0.4840 0.5000 -0.0116 -0.0024 0.0345  235  ARG A NH1 
1573  N NH2 . ARG A 237  ? 0.4682 0.4484 0.4585 -0.0102 0.0012  0.0283  235  ARG A NH2 
1574  N N   . TYR A 238  ? 0.2376 0.2150 0.2349 -0.0067 0.0004  0.0293  236  TYR A N   
1575  C CA  . TYR A 238  ? 0.2410 0.2191 0.2371 -0.0060 0.0021  0.0266  236  TYR A CA  
1576  C C   . TYR A 238  ? 0.2351 0.2142 0.2335 -0.0056 0.0016  0.0276  236  TYR A C   
1577  O O   . TYR A 238  ? 0.2620 0.2440 0.2599 -0.0062 0.0020  0.0266  236  TYR A O   
1578  C CB  . TYR A 238  ? 0.2593 0.2333 0.2548 -0.0040 0.0037  0.0240  236  TYR A CB  
1579  C CG  . TYR A 238  ? 0.2966 0.2704 0.2898 -0.0044 0.0044  0.0226  236  TYR A CG  
1580  C CD1 . TYR A 238  ? 0.3939 0.3717 0.3852 -0.0059 0.0047  0.0216  236  TYR A CD1 
1581  C CD2 . TYR A 238  ? 0.2957 0.2659 0.2887 -0.0032 0.0047  0.0220  236  TYR A CD2 
1582  C CE1 . TYR A 238  ? 0.4522 0.4301 0.4416 -0.0062 0.0054  0.0202  236  TYR A CE1 
1583  C CE2 . TYR A 238  ? 0.3975 0.3675 0.3884 -0.0036 0.0052  0.0209  236  TYR A CE2 
1584  C CZ  . TYR A 238  ? 0.4747 0.4486 0.4639 -0.0051 0.0056  0.0201  236  TYR A CZ  
1585  O OH  . TYR A 238  ? 0.5552 0.5293 0.5426 -0.0053 0.0062  0.0188  236  TYR A OH  
1586  N N   . TYR A 239  ? 0.2100 0.1866 0.2111 -0.0046 0.0005  0.0293  237  TYR A N   
1587  C CA  . TYR A 239  ? 0.2044 0.1823 0.2079 -0.0043 -0.0002 0.0304  237  TYR A CA  
1588  C C   . TYR A 239  ? 0.2367 0.2198 0.2398 -0.0066 -0.0014 0.0324  237  TYR A C   
1589  O O   . TYR A 239  ? 0.2038 0.1896 0.2071 -0.0069 -0.0011 0.0317  237  TYR A O   
1590  C CB  . TYR A 239  ? 0.2379 0.2127 0.2450 -0.0027 -0.0015 0.0318  237  TYR A CB  
1591  C CG  . TYR A 239  ? 0.2532 0.2296 0.2629 -0.0024 -0.0022 0.0330  237  TYR A CG  
1592  C CD1 . TYR A 239  ? 0.2554 0.2351 0.2664 -0.0041 -0.0041 0.0361  237  TYR A CD1 
1593  C CD2 . TYR A 239  ? 0.2530 0.2284 0.2639 -0.0004 -0.0009 0.0312  237  TYR A CD2 
1594  C CE1 . TYR A 239  ? 0.2849 0.2663 0.2984 -0.0038 -0.0048 0.0372  237  TYR A CE1 
1595  C CE2 . TYR A 239  ? 0.2640 0.2412 0.2774 -0.0001 -0.0015 0.0323  237  TYR A CE2 
1596  C CZ  . TYR A 239  ? 0.2643 0.2443 0.2791 -0.0018 -0.0034 0.0352  237  TYR A CZ  
1597  O OH  . TYR A 239  ? 0.3046 0.2866 0.3221 -0.0015 -0.0041 0.0364  237  TYR A OH  
1598  N N   . ARG A 240  ? 0.2188 0.2040 0.2219 -0.0082 -0.0029 0.0352  238  ARG A N   
1599  C CA  A ARG A 240  ? 0.2311 0.2225 0.2338 -0.0104 -0.0042 0.0375  238  ARG A CA  
1600  C CA  B ARG A 240  ? 0.2312 0.2227 0.2340 -0.0104 -0.0042 0.0375  238  ARG A CA  
1601  C C   . ARG A 240  ? 0.2256 0.2217 0.2250 -0.0114 -0.0029 0.0347  238  ARG A C   
1602  O O   . ARG A 240  ? 0.2142 0.2154 0.2134 -0.0125 -0.0034 0.0349  238  ARG A O   
1603  C CB  A ARG A 240  ? 0.2578 0.2514 0.2616 -0.0122 -0.0062 0.0417  238  ARG A CB  
1604  C CB  B ARG A 240  ? 0.2578 0.2514 0.2616 -0.0122 -0.0062 0.0417  238  ARG A CB  
1605  C CG  A ARG A 240  ? 0.2796 0.2737 0.2811 -0.0131 -0.0058 0.0414  238  ARG A CG  
1606  C CG  B ARG A 240  ? 0.2795 0.2740 0.2809 -0.0132 -0.0058 0.0415  238  ARG A CG  
1607  C CD  A ARG A 240  ? 0.2779 0.2757 0.2809 -0.0154 -0.0080 0.0465  238  ARG A CD  
1608  C CD  B ARG A 240  ? 0.2782 0.2746 0.2819 -0.0151 -0.0082 0.0466  238  ARG A CD  
1609  N NE  A ARG A 240  ? 0.2447 0.2424 0.2464 -0.0162 -0.0078 0.0467  238  ARG A NE  
1610  N NE  B ARG A 240  ? 0.2714 0.2626 0.2799 -0.0139 -0.0100 0.0487  238  ARG A NE  
1611  C CZ  A ARG A 240  ? 0.2676 0.2598 0.2717 -0.0155 -0.0086 0.0475  238  ARG A CZ  
1612  C CZ  B ARG A 240  ? 0.2636 0.2490 0.2747 -0.0128 -0.0109 0.0490  238  ARG A CZ  
1613  N NH1 A ARG A 240  ? 0.2823 0.2685 0.2902 -0.0138 -0.0098 0.0479  238  ARG A NH1 
1614  N NH1 B ARG A 240  ? 0.2775 0.2619 0.2873 -0.0133 -0.0105 0.0484  238  ARG A NH1 
1615  N NH2 A ARG A 240  ? 0.2916 0.2844 0.2942 -0.0164 -0.0083 0.0476  238  ARG A NH2 
1616  N NH2 B ARG A 240  ? 0.2485 0.2293 0.2642 -0.0111 -0.0123 0.0496  238  ARG A NH2 
1617  N N   . ASP A 241  ? 0.2269 0.2214 0.2241 -0.0109 -0.0014 0.0318  239  ASP A N   
1618  C CA  . ASP A 241  ? 0.2308 0.2289 0.2255 -0.0115 -0.0003 0.0284  239  ASP A CA  
1619  C C   . ASP A 241  ? 0.2400 0.2372 0.2360 -0.0105 0.0003  0.0261  239  ASP A C   
1620  O O   . ASP A 241  ? 0.2369 0.2389 0.2325 -0.0114 0.0000  0.0246  239  ASP A O   
1621  C CB  . ASP A 241  ? 0.2688 0.2646 0.2616 -0.0109 0.0011  0.0259  239  ASP A CB  
1622  C CG  . ASP A 241  ? 0.3354 0.3336 0.3268 -0.0122 0.0005  0.0279  239  ASP A CG  
1623  O OD1 . ASP A 241  ? 0.3592 0.3623 0.3507 -0.0139 -0.0010 0.0311  239  ASP A OD1 
1624  O OD2 . ASP A 241  ? 0.4082 0.4035 0.3986 -0.0116 0.0014  0.0265  239  ASP A OD2 
1625  N N   . TYR A 242  ? 0.2242 0.2159 0.2220 -0.0087 0.0012  0.0257  240  TYR A N   
1626  C CA  . TYR A 242  ? 0.2037 0.1948 0.2033 -0.0080 0.0017  0.0242  240  TYR A CA  
1627  C C   . TYR A 242  ? 0.1958 0.1904 0.1971 -0.0088 0.0003  0.0261  240  TYR A C   
1628  O O   . TYR A 242  ? 0.2113 0.2086 0.2135 -0.0093 0.0001  0.0246  240  TYR A O   
1629  C CB  . TYR A 242  ? 0.2096 0.1954 0.2108 -0.0059 0.0028  0.0241  240  TYR A CB  
1630  C CG  . TYR A 242  ? 0.1988 0.1815 0.1988 -0.0050 0.0044  0.0218  240  TYR A CG  
1631  C CD1 . TYR A 242  ? 0.2445 0.2285 0.2436 -0.0057 0.0049  0.0192  240  TYR A CD1 
1632  C CD2 . TYR A 242  ? 0.2662 0.2449 0.2664 -0.0033 0.0052  0.0221  240  TYR A CD2 
1633  C CE1 . TYR A 242  ? 0.2724 0.2535 0.2708 -0.0048 0.0062  0.0174  240  TYR A CE1 
1634  C CE2 . TYR A 242  ? 0.2270 0.2033 0.2260 -0.0025 0.0066  0.0203  240  TYR A CE2 
1635  C CZ  . TYR A 242  ? 0.2376 0.2150 0.2359 -0.0033 0.0070  0.0182  240  TYR A CZ  
1636  O OH  . TYR A 242  ? 0.2466 0.2217 0.2442 -0.0024 0.0082  0.0168  240  TYR A OH  
1637  N N   . GLU A 243  ? 0.1987 0.1930 0.2013 -0.0088 -0.0009 0.0294  241  GLU A N   
1638  C CA  . GLU A 243  ? 0.2011 0.1986 0.2056 -0.0095 -0.0024 0.0317  241  GLU A CA  
1639  C C   . GLU A 243  ? 0.2171 0.2216 0.2198 -0.0116 -0.0034 0.0316  241  GLU A C   
1640  O O   . GLU A 243  ? 0.2090 0.2168 0.2126 -0.0121 -0.0039 0.0309  241  GLU A O   
1641  C CB  . GLU A 243  ? 0.2142 0.2100 0.2208 -0.0092 -0.0039 0.0355  241  GLU A CB  
1642  C CG  . GLU A 243  ? 0.2507 0.2500 0.2596 -0.0100 -0.0058 0.0385  241  GLU A CG  
1643  C CD  . GLU A 243  ? 0.2937 0.2919 0.3051 -0.0102 -0.0077 0.0426  241  GLU A CD  
1644  O OE1 . GLU A 243  ? 0.3791 0.3765 0.3894 -0.0108 -0.0081 0.0436  241  GLU A OE1 
1645  O OE2 . GLU A 243  ? 0.2733 0.2713 0.2881 -0.0097 -0.0091 0.0447  241  GLU A OE2 
1646  N N   . SER A 244  ? 0.2120 0.2194 0.2121 -0.0128 -0.0036 0.0319  242  SER A N   
1647  C CA  . SER A 244  ? 0.2111 0.2266 0.2094 -0.0146 -0.0044 0.0314  242  SER A CA  
1648  C C   . SER A 244  ? 0.2243 0.2412 0.2217 -0.0143 -0.0035 0.0264  242  SER A C   
1649  O O   . SER A 244  ? 0.2270 0.2498 0.2243 -0.0153 -0.0044 0.0252  242  SER A O   
1650  C CB  . SER A 244  ? 0.2138 0.2329 0.2096 -0.0160 -0.0047 0.0331  242  SER A CB  
1651  O OG  . SER A 244  ? 0.2906 0.3071 0.2846 -0.0153 -0.0032 0.0300  242  SER A OG  
1652  N N   . ALA A 245  ? 0.2120 0.2238 0.2095 -0.0131 -0.0019 0.0234  243  ALA A N   
1653  C CA  . ALA A 245  ? 0.1964 0.2088 0.1944 -0.0127 -0.0014 0.0189  243  ALA A CA  
1654  C C   . ALA A 245  ? 0.2172 0.2287 0.2183 -0.0124 -0.0019 0.0186  243  ALA A C   
1655  O O   . ALA A 245  ? 0.2185 0.2338 0.2204 -0.0130 -0.0026 0.0158  243  ALA A O   
1656  C CB  . ALA A 245  ? 0.2135 0.2202 0.2113 -0.0115 0.0001  0.0165  243  ALA A CB  
1657  N N   . ILE A 246  ? 0.2061 0.2132 0.2092 -0.0115 -0.0016 0.0213  244  ILE A N   
1658  C CA  . ILE A 246  ? 0.1922 0.1991 0.1985 -0.0112 -0.0020 0.0215  244  ILE A CA  
1659  C C   . ILE A 246  ? 0.2232 0.2367 0.2296 -0.0127 -0.0038 0.0222  244  ILE A C   
1660  O O   . ILE A 246  ? 0.2215 0.2373 0.2296 -0.0131 -0.0045 0.0200  244  ILE A O   
1661  C CB  . ILE A 246  ? 0.2028 0.2050 0.2111 -0.0098 -0.0014 0.0243  244  ILE A CB  
1662  C CG1 . ILE A 246  ? 0.2197 0.2164 0.2282 -0.0083 0.0004  0.0230  244  ILE A CG1 
1663  C CG2 . ILE A 246  ? 0.2259 0.2294 0.2376 -0.0098 -0.0021 0.0251  244  ILE A CG2 
1664  C CD1 . ILE A 246  ? 0.2361 0.2291 0.2460 -0.0066 0.0010  0.0253  244  ILE A CD1 
1665  N N   . HIS A 247  ? 0.1976 0.2145 0.2023 -0.0135 -0.0048 0.0253  245  HIS A N   
1666  C CA  . HIS A 247  ? 0.2093 0.2336 0.2138 -0.0150 -0.0066 0.0263  245  HIS A CA  
1667  C C   . HIS A 247  ? 0.2222 0.2522 0.2250 -0.0159 -0.0070 0.0219  245  HIS A C   
1668  O O   . HIS A 247  ? 0.2270 0.2613 0.2312 -0.0165 -0.0081 0.0203  245  HIS A O   
1669  C CB  . HIS A 247  ? 0.2207 0.2482 0.2239 -0.0161 -0.0077 0.0309  245  HIS A CB  
1670  C CG  . HIS A 247  ? 0.2438 0.2671 0.2497 -0.0153 -0.0082 0.0352  245  HIS A CG  
1671  N ND1 . HIS A 247  ? 0.2313 0.2550 0.2401 -0.0151 -0.0092 0.0367  245  HIS A ND1 
1672  C CD2 . HIS A 247  ? 0.2516 0.2703 0.2581 -0.0146 -0.0082 0.0380  245  HIS A CD2 
1673  C CE1 . HIS A 247  ? 0.2572 0.2770 0.2685 -0.0141 -0.0097 0.0402  245  HIS A CE1 
1674  N NE2 . HIS A 247  ? 0.2426 0.2590 0.2526 -0.0138 -0.0091 0.0408  245  HIS A NE2 
1675  N N   . ALA A 248  ? 0.2155 0.2464 0.2158 -0.0160 -0.0062 0.0197  246  ALA A N   
1676  C CA  . ALA A 248  ? 0.2121 0.2491 0.2111 -0.0165 -0.0067 0.0150  246  ALA A CA  
1677  C C   . ALA A 248  ? 0.2362 0.2702 0.2384 -0.0157 -0.0066 0.0105  246  ALA A C   
1678  O O   . ALA A 248  ? 0.2161 0.2553 0.2192 -0.0162 -0.0079 0.0072  246  ALA A O   
1679  C CB  . ALA A 248  ? 0.2305 0.2690 0.2265 -0.0165 -0.0058 0.0135  246  ALA A CB  
1680  N N   . ILE A 249  ? 0.2217 0.2475 0.2260 -0.0145 -0.0053 0.0105  247  ILE A N   
1681  C CA  . ILE A 249  ? 0.2087 0.2313 0.2168 -0.0140 -0.0054 0.0071  247  ILE A CA  
1682  C C   . ILE A 249  ? 0.2139 0.2378 0.2251 -0.0144 -0.0066 0.0082  247  ILE A C   
1683  O O   . ILE A 249  ? 0.2210 0.2469 0.2350 -0.0147 -0.0078 0.0048  247  ILE A O   
1684  C CB  . ILE A 249  ? 0.2168 0.2312 0.2261 -0.0127 -0.0037 0.0078  247  ILE A CB  
1685  C CG1 . ILE A 249  ? 0.2055 0.2190 0.2123 -0.0123 -0.0028 0.0059  247  ILE A CG1 
1686  C CG2 . ILE A 249  ? 0.2235 0.2347 0.2377 -0.0124 -0.0040 0.0058  247  ILE A CG2 
1687  C CD1 . ILE A 249  ? 0.2054 0.2118 0.2122 -0.0111 -0.0010 0.0079  247  ILE A CD1 
1688  N N   . GLY A 250  ? 0.2121 0.2346 0.2233 -0.0143 -0.0064 0.0129  248  GLY A N   
1689  C CA  . GLY A 250  ? 0.2176 0.2416 0.2319 -0.0147 -0.0075 0.0143  248  GLY A CA  
1690  C C   . GLY A 250  ? 0.2242 0.2564 0.2377 -0.0160 -0.0095 0.0130  248  GLY A C   
1691  O O   . GLY A 250  ? 0.2261 0.2602 0.2427 -0.0164 -0.0108 0.0114  248  GLY A O   
1692  N N   . LYS A 251  ? 0.2141 0.2518 0.2237 -0.0167 -0.0099 0.0137  249  LYS A N   
1693  C CA  . LYS A 251  ? 0.2273 0.2742 0.2357 -0.0180 -0.0118 0.0122  249  LYS A CA  
1694  C C   . LYS A 251  ? 0.2562 0.3058 0.2659 -0.0180 -0.0126 0.0057  249  LYS A C   
1695  O O   . LYS A 251  ? 0.2468 0.3015 0.2581 -0.0186 -0.0143 0.0034  249  LYS A O   
1696  C CB  . LYS A 251  ? 0.2390 0.2922 0.2430 -0.0189 -0.0119 0.0144  249  LYS A CB  
1697  C CG  . LYS A 251  ? 0.2445 0.2971 0.2478 -0.0193 -0.0121 0.0210  249  LYS A CG  
1698  C CD  . LYS A 251  ? 0.2373 0.2954 0.2367 -0.0203 -0.0121 0.0228  249  LYS A CD  
1699  C CE  . LYS A 251  ? 0.2344 0.2923 0.2338 -0.0209 -0.0127 0.0296  249  LYS A CE  
1700  N NZ  . LYS A 251  ? 0.2321 0.2943 0.2282 -0.0219 -0.0124 0.0314  249  LYS A NZ  
1701  N N   . ALA A 252  ? 0.2297 0.2758 0.2390 -0.0172 -0.0115 0.0024  250  ALA A N   
1702  C CA  . ALA A 252  ? 0.2331 0.2809 0.2443 -0.0169 -0.0124 -0.0042 250  ALA A CA  
1703  C C   . ALA A 252  ? 0.2705 0.3129 0.2875 -0.0166 -0.0131 -0.0058 250  ALA A C   
1704  O O   . ALA A 252  ? 0.2500 0.2957 0.2700 -0.0168 -0.0149 -0.0105 250  ALA A O   
1705  C CB  . ALA A 252  ? 0.2738 0.3190 0.2834 -0.0160 -0.0111 -0.0067 250  ALA A CB  
1706  N N   . SER A 253  ? 0.2499 0.2847 0.2689 -0.0161 -0.0117 -0.0019 251  SER A N   
1707  C CA  . SER A 253  ? 0.2521 0.2824 0.2768 -0.0160 -0.0122 -0.0024 251  SER A CA  
1708  C C   . SER A 253  ? 0.2500 0.2854 0.2770 -0.0170 -0.0142 -0.0027 251  SER A C   
1709  O O   . SER A 253  ? 0.2546 0.2900 0.2864 -0.0173 -0.0159 -0.0062 251  SER A O   
1710  C CB  . SER A 253  ? 0.2357 0.2591 0.2614 -0.0153 -0.0103 0.0026  251  SER A CB  
1711  O OG  . SER A 253  ? 0.2520 0.2725 0.2833 -0.0155 -0.0108 0.0028  251  SER A OG  
1712  N N   . ALA A 254  ? 0.2395 0.2791 0.2635 -0.0175 -0.0144 0.0009  252  ALA A N   
1713  C CA  . ALA A 254  ? 0.2501 0.2959 0.2755 -0.0184 -0.0164 0.0008  252  ALA A CA  
1714  C C   . ALA A 254  ? 0.2856 0.3279 0.3171 -0.0186 -0.0172 0.0007  252  ALA A C   
1715  O O   . ALA A 254  ? 0.2700 0.3159 0.3047 -0.0193 -0.0194 -0.0029 252  ALA A O   
1716  C CB  . ALA A 254  ? 0.3068 0.3609 0.3305 -0.0190 -0.0183 -0.0046 252  ALA A CB  
1717  N N   . GLY A 255  ? 0.2303 0.2660 0.2636 -0.0180 -0.0156 0.0047  253  GLY A N   
1718  C CA  . GLY A 255  ? 0.2541 0.2873 0.2933 -0.0182 -0.0161 0.0057  253  GLY A CA  
1719  C C   . GLY A 255  ? 0.2727 0.3021 0.3171 -0.0183 -0.0166 0.0023  253  GLY A C   
1720  O O   . GLY A 255  ? 0.2988 0.3271 0.3487 -0.0188 -0.0175 0.0029  253  GLY A O   
1721  N N   . ARG A 256  ? 0.2578 0.2849 0.3010 -0.0178 -0.0162 -0.0010 254  ARG A N   
1722  C CA  . ARG A 256  ? 0.2594 0.2823 0.3085 -0.0179 -0.0170 -0.0037 254  ARG A CA  
1723  C C   . ARG A 256  ? 0.2657 0.2824 0.3177 -0.0175 -0.0151 0.0008  254  ARG A C   
1724  O O   . ARG A 256  ? 0.2619 0.2755 0.3201 -0.0179 -0.0160 0.0000  254  ARG A O   
1725  C CB  . ARG A 256  ? 0.2513 0.2737 0.2988 -0.0173 -0.0171 -0.0084 254  ARG A CB  
1726  C CG  . ARG A 256  ? 0.2897 0.3181 0.3378 -0.0177 -0.0198 -0.0148 254  ARG A CG  
1727  C CD  . ARG A 256  ? 0.3204 0.3489 0.3666 -0.0169 -0.0196 -0.0194 254  ARG A CD  
1728  N NE  . ARG A 256  ? 0.3112 0.3424 0.3497 -0.0164 -0.0177 -0.0175 254  ARG A NE  
1729  C CZ  . ARG A 256  ? 0.3255 0.3569 0.3610 -0.0156 -0.0169 -0.0202 254  ARG A CZ  
1730  N NH1 . ARG A 256  ? 0.3141 0.3427 0.3536 -0.0149 -0.0178 -0.0248 254  ARG A NH1 
1731  N NH2 . ARG A 256  ? 0.2926 0.3273 0.3215 -0.0154 -0.0154 -0.0181 254  ARG A NH2 
1732  N N   . GLY A 257  ? 0.2400 0.2553 0.2882 -0.0167 -0.0128 0.0054  255  GLY A N   
1733  C CA  . GLY A 257  ? 0.2265 0.2373 0.2772 -0.0161 -0.0110 0.0095  255  GLY A CA  
1734  C C   . GLY A 257  ? 0.2278 0.2340 0.2772 -0.0152 -0.0093 0.0095  255  GLY A C   
1735  O O   . GLY A 257  ? 0.2344 0.2402 0.2810 -0.0150 -0.0094 0.0063  255  GLY A O   
1736  N N   . ILE A 258  ? 0.2025 0.2055 0.2539 -0.0147 -0.0076 0.0132  256  ILE A N   
1737  C CA  . ILE A 258  ? 0.2006 0.1997 0.2499 -0.0136 -0.0057 0.0140  256  ILE A CA  
1738  C C   . ILE A 258  ? 0.2109 0.2072 0.2645 -0.0141 -0.0067 0.0117  256  ILE A C   
1739  O O   . ILE A 258  ? 0.2107 0.2042 0.2623 -0.0134 -0.0055 0.0114  256  ILE A O   
1740  C CB  . ILE A 258  ? 0.1948 0.1927 0.2441 -0.0126 -0.0034 0.0188  256  ILE A CB  
1741  C CG1 . ILE A 258  ? 0.1995 0.1977 0.2557 -0.0134 -0.0039 0.0211  256  ILE A CG1 
1742  C CG2 . ILE A 258  ? 0.2195 0.2196 0.2648 -0.0117 -0.0026 0.0208  256  ILE A CG2 
1743  C CD1 . ILE A 258  ? 0.2435 0.2419 0.2997 -0.0123 -0.0016 0.0256  256  ILE A CD1 
1744  N N   . TYR A 259  ? 0.2286 0.2255 0.2887 -0.0154 -0.0090 0.0102  257  TYR A N   
1745  C CA  . TYR A 259  ? 0.2304 0.2242 0.2958 -0.0159 -0.0103 0.0081  257  TYR A CA  
1746  C C   . TYR A 259  ? 0.2430 0.2379 0.3084 -0.0161 -0.0125 0.0018  257  TYR A C   
1747  O O   . TYR A 259  ? 0.2887 0.2812 0.3535 -0.0155 -0.0125 -0.0006 257  TYR A O   
1748  C CB  . TYR A 259  ? 0.2615 0.2549 0.3355 -0.0173 -0.0118 0.0104  257  TYR A CB  
1749  C CG  . TYR A 259  ? 0.2510 0.2448 0.3251 -0.0170 -0.0095 0.0166  257  TYR A CG  
1750  C CD1 . TYR A 259  ? 0.2384 0.2301 0.3102 -0.0160 -0.0070 0.0197  257  TYR A CD1 
1751  C CD2 . TYR A 259  ? 0.2611 0.2581 0.3374 -0.0177 -0.0097 0.0190  257  TYR A CD2 
1752  C CE1 . TYR A 259  ? 0.2546 0.2477 0.3263 -0.0155 -0.0049 0.0248  257  TYR A CE1 
1753  C CE2 . TYR A 259  ? 0.2749 0.2731 0.3515 -0.0172 -0.0076 0.0242  257  TYR A CE2 
1754  C CZ  . TYR A 259  ? 0.2333 0.2298 0.3075 -0.0160 -0.0052 0.0269  257  TYR A CZ  
1755  O OH  . TYR A 259  ? 0.2508 0.2495 0.3251 -0.0153 -0.0030 0.0316  257  TYR A OH  
1756  N N   . GLU A 260  ? 0.2345 0.2336 0.3002 -0.0168 -0.0145 -0.0011 258  GLU A N   
1757  C CA  . GLU A 260  ? 0.2990 0.3006 0.3644 -0.0167 -0.0166 -0.0076 258  GLU A CA  
1758  C C   . GLU A 260  ? 0.3045 0.3086 0.3613 -0.0157 -0.0151 -0.0090 258  GLU A C   
1759  O O   . GLU A 260  ? 0.3310 0.3359 0.3867 -0.0152 -0.0158 -0.0136 258  GLU A O   
1760  C CB  . GLU A 260  ? 0.3065 0.3126 0.3750 -0.0178 -0.0193 -0.0105 258  GLU A CB  
1761  C CG  . GLU A 260  ? 0.3871 0.3975 0.4541 -0.0175 -0.0214 -0.0177 258  GLU A CG  
1762  C CD  . GLU A 260  ? 0.4584 0.4743 0.5282 -0.0184 -0.0242 -0.0211 258  GLU A CD  
1763  O OE1 . GLU A 260  ? 0.5161 0.5315 0.5907 -0.0195 -0.0252 -0.0185 258  GLU A OE1 
1764  O OE2 . GLU A 260  ? 0.4993 0.5206 0.5664 -0.0180 -0.0256 -0.0266 258  GLU A OE2 
1765  N N   . GLY A 261  ? 0.2554 0.2610 0.3067 -0.0155 -0.0131 -0.0049 259  GLY A N   
1766  C CA  . GLY A 261  ? 0.2249 0.2337 0.2688 -0.0149 -0.0120 -0.0055 259  GLY A CA  
1767  C C   . GLY A 261  ? 0.2400 0.2450 0.2801 -0.0138 -0.0095 -0.0034 259  GLY A C   
1768  O O   . GLY A 261  ? 0.2300 0.2300 0.2724 -0.0134 -0.0084 -0.0008 259  GLY A O   
1769  N N   . PRO A 262  ? 0.2338 0.2414 0.2679 -0.0134 -0.0088 -0.0044 260  PRO A N   
1770  C CA  . PRO A 262  ? 0.2082 0.2125 0.2387 -0.0125 -0.0068 -0.0031 260  PRO A CA  
1771  C C   . PRO A 262  ? 0.2173 0.2188 0.2457 -0.0119 -0.0048 0.0024  260  PRO A C   
1772  O O   . PRO A 262  ? 0.2329 0.2361 0.2613 -0.0122 -0.0048 0.0052  260  PRO A O   
1773  C CB  . PRO A 262  ? 0.2415 0.2510 0.2668 -0.0125 -0.0070 -0.0056 260  PRO A CB  
1774  C CG  . PRO A 262  ? 0.2405 0.2559 0.2651 -0.0134 -0.0083 -0.0054 260  PRO A CG  
1775  C CD  . PRO A 262  ? 0.2746 0.2892 0.3054 -0.0139 -0.0100 -0.0067 260  PRO A CD  
1776  N N   . GLY A 263  ? 0.2235 0.2209 0.2502 -0.0110 -0.0030 0.0037  261  GLY A N   
1777  C CA  . GLY A 263  ? 0.2283 0.2234 0.2526 -0.0102 -0.0012 0.0081  261  GLY A CA  
1778  C C   . GLY A 263  ? 0.2326 0.2263 0.2522 -0.0094 0.0002  0.0083  261  GLY A C   
1779  O O   . GLY A 263  ? 0.2074 0.2027 0.2253 -0.0096 -0.0003 0.0052  261  GLY A O   
1780  N N   . ILE A 264  ? 0.2113 0.2025 0.2291 -0.0085 0.0017  0.0116  262  ILE A N   
1781  C CA  . ILE A 264  ? 0.2176 0.2071 0.2313 -0.0077 0.0028  0.0119  262  ILE A CA  
1782  C C   . ILE A 264  ? 0.2177 0.2029 0.2323 -0.0065 0.0044  0.0135  262  ILE A C   
1783  O O   . ILE A 264  ? 0.2149 0.1993 0.2325 -0.0061 0.0048  0.0154  262  ILE A O   
1784  C CB  . ILE A 264  ? 0.2166 0.2078 0.2272 -0.0077 0.0028  0.0143  262  ILE A CB  
1785  C CG1 . ILE A 264  ? 0.2080 0.1984 0.2147 -0.0075 0.0034  0.0141  262  ILE A CG1 
1786  C CG2 . ILE A 264  ? 0.2262 0.2156 0.2381 -0.0068 0.0034  0.0175  262  ILE A CG2 
1787  C CD1 . ILE A 264  ? 0.2371 0.2297 0.2414 -0.0079 0.0028  0.0165  262  ILE A CD1 
1788  N N   . SER A 265  ? 0.1833 0.1665 0.1955 -0.0059 0.0052  0.0127  263  SER A N   
1789  C CA  . SER A 265  ? 0.2170 0.1968 0.2291 -0.0047 0.0068  0.0142  263  SER A CA  
1790  C C   . SER A 265  ? 0.2288 0.2077 0.2369 -0.0039 0.0075  0.0151  263  SER A C   
1791  O O   . SER A 265  ? 0.2636 0.2437 0.2690 -0.0045 0.0069  0.0139  263  SER A O   
1792  C CB  . SER A 265  ? 0.2271 0.2050 0.2408 -0.0046 0.0069  0.0125  263  SER A CB  
1793  O OG  . SER A 265  ? 0.2433 0.2215 0.2619 -0.0053 0.0060  0.0120  263  SER A OG  
1794  N N   . ILE A 266  ? 0.2123 0.1894 0.2201 -0.0025 0.0086  0.0171  264  ILE A N   
1795  C CA  . ILE A 266  ? 0.2110 0.1869 0.2158 -0.0016 0.0090  0.0178  264  ILE A CA  
1796  C C   . ILE A 266  ? 0.2185 0.1920 0.2226 -0.0002 0.0104  0.0180  264  ILE A C   
1797  O O   . ILE A 266  ? 0.2191 0.1925 0.2254 0.0004  0.0112  0.0187  264  ILE A O   
1798  C CB  . ILE A 266  ? 0.2040 0.1806 0.2092 -0.0011 0.0086  0.0197  264  ILE A CB  
1799  C CG1 . ILE A 266  ? 0.2367 0.2134 0.2444 0.0003  0.0095  0.0210  264  ILE A CG1 
1800  C CG2 . ILE A 266  ? 0.2476 0.2271 0.2534 -0.0026 0.0071  0.0200  264  ILE A CG2 
1801  C CD1 . ILE A 266  ? 0.2763 0.2535 0.2847 0.0014  0.0091  0.0224  264  ILE A CD1 
1802  N N   . LYS A 267  ? 0.2208 0.1928 0.2221 0.0003  0.0105  0.0175  265  LYS A N   
1803  C CA  . LYS A 267  ? 0.2104 0.1806 0.2108 0.0018  0.0117  0.0176  265  LYS A CA  
1804  C C   . LYS A 267  ? 0.2004 0.1701 0.2001 0.0032  0.0116  0.0184  265  LYS A C   
1805  O O   . LYS A 267  ? 0.2314 0.2006 0.2300 0.0027  0.0105  0.0184  265  LYS A O   
1806  C CB  . LYS A 267  ? 0.2504 0.2192 0.2487 0.0014  0.0118  0.0161  265  LYS A CB  
1807  C CG  . LYS A 267  ? 0.2740 0.2432 0.2741 0.0006  0.0118  0.0150  265  LYS A CG  
1808  C CD  . LYS A 267  ? 0.2874 0.2556 0.2859 0.0003  0.0118  0.0133  265  LYS A CD  
1809  C CE  . LYS A 267  ? 0.2924 0.2614 0.2933 -0.0008 0.0111  0.0115  265  LYS A CE  
1810  N NZ  . LYS A 267  ? 0.2685 0.2366 0.2729 -0.0005 0.0114  0.0123  265  LYS A NZ  
1811  N N   . LEU A 268  ? 0.1865 0.1566 0.1872 0.0049  0.0125  0.0190  266  LEU A N   
1812  C CA  . LEU A 268  ? 0.2004 0.1703 0.2012 0.0066  0.0122  0.0191  266  LEU A CA  
1813  C C   . LEU A 268  ? 0.1957 0.1633 0.1944 0.0071  0.0117  0.0180  266  LEU A C   
1814  O O   . LEU A 268  ? 0.1977 0.1643 0.1970 0.0077  0.0105  0.0180  266  LEU A O   
1815  C CB  . LEU A 268  ? 0.2095 0.1814 0.2116 0.0085  0.0135  0.0195  266  LEU A CB  
1816  C CG  . LEU A 268  ? 0.2334 0.2081 0.2384 0.0081  0.0138  0.0210  266  LEU A CG  
1817  C CD1 . LEU A 268  ? 0.2355 0.2133 0.2418 0.0101  0.0151  0.0216  266  LEU A CD1 
1818  C CD2 . LEU A 268  ? 0.2622 0.2369 0.2686 0.0075  0.0124  0.0214  266  LEU A CD2 
1819  N N   . SER A 269  ? 0.2251 0.1917 0.2219 0.0069  0.0124  0.0172  267  SER A N   
1820  C CA  . SER A 269  ? 0.2416 0.2061 0.2366 0.0073  0.0119  0.0161  267  SER A CA  
1821  C C   . SER A 269  ? 0.2612 0.2248 0.2557 0.0055  0.0103  0.0166  267  SER A C   
1822  O O   . SER A 269  ? 0.2561 0.2181 0.2501 0.0057  0.0094  0.0163  267  SER A O   
1823  C CB  . SER A 269  ? 0.2171 0.1810 0.2101 0.0073  0.0129  0.0153  267  SER A CB  
1824  O OG  . SER A 269  ? 0.2295 0.1936 0.2222 0.0055  0.0128  0.0153  267  SER A OG  
1825  N N   . ALA A 270  ? 0.2065 0.1718 0.2016 0.0037  0.0099  0.0174  268  ALA A N   
1826  C CA  . ALA A 270  ? 0.2327 0.1986 0.2274 0.0020  0.0085  0.0183  268  ALA A CA  
1827  C C   . ALA A 270  ? 0.2390 0.2044 0.2358 0.0024  0.0070  0.0198  268  ALA A C   
1828  O O   . ALA A 270  ? 0.2275 0.1930 0.2245 0.0013  0.0055  0.0211  268  ALA A O   
1829  C CB  . ALA A 270  ? 0.2556 0.2242 0.2502 0.0002  0.0083  0.0183  268  ALA A CB  
1830  N N   . LEU A 271  ? 0.2199 0.1852 0.2186 0.0041  0.0073  0.0198  269  LEU A N   
1831  C CA  . LEU A 271  ? 0.2266 0.1921 0.2281 0.0045  0.0058  0.0212  269  LEU A CA  
1832  C C   . LEU A 271  ? 0.2195 0.1826 0.2226 0.0067  0.0051  0.0203  269  LEU A C   
1833  O O   . LEU A 271  ? 0.2338 0.1965 0.2398 0.0074  0.0035  0.0212  269  LEU A O   
1834  C CB  . LEU A 271  ? 0.2240 0.1917 0.2271 0.0047  0.0063  0.0217  269  LEU A CB  
1835  C CG  . LEU A 271  ? 0.2159 0.1861 0.2183 0.0025  0.0063  0.0224  269  LEU A CG  
1836  C CD1 . LEU A 271  ? 0.2555 0.2277 0.2599 0.0028  0.0069  0.0228  269  LEU A CD1 
1837  C CD2 . LEU A 271  ? 0.2573 0.2284 0.2601 0.0009  0.0044  0.0243  269  LEU A CD2 
1838  N N   . HIS A 272  ? 0.2234 0.1851 0.2250 0.0080  0.0059  0.0185  270  HIS A N   
1839  C CA  . HIS A 272  ? 0.2065 0.1661 0.2098 0.0101  0.0049  0.0171  270  HIS A CA  
1840  C C   . HIS A 272  ? 0.2295 0.1875 0.2305 0.0104  0.0053  0.0155  270  HIS A C   
1841  O O   . HIS A 272  ? 0.2318 0.1910 0.2302 0.0103  0.0072  0.0148  270  HIS A O   
1842  C CB  . HIS A 272  ? 0.2096 0.1708 0.2145 0.0129  0.0058  0.0156  270  HIS A CB  
1843  C CG  . HIS A 272  ? 0.2177 0.1773 0.2256 0.0153  0.0041  0.0138  270  HIS A CG  
1844  N ND1 . HIS A 272  ? 0.2504 0.2084 0.2576 0.0168  0.0038  0.0114  270  HIS A ND1 
1845  C CD2 . HIS A 272  ? 0.2586 0.2179 0.2706 0.0165  0.0023  0.0139  270  HIS A CD2 
1846  C CE1 . HIS A 272  ? 0.2585 0.2153 0.2695 0.0188  0.0019  0.0097  270  HIS A CE1 
1847  N NE2 . HIS A 272  ? 0.2675 0.2249 0.2815 0.0188  0.0009  0.0112  270  HIS A NE2 
1848  N N   . PRO A 273  ? 0.2159 0.1713 0.2182 0.0106  0.0034  0.0150  271  PRO A N   
1849  C CA  . PRO A 273  ? 0.2301 0.1842 0.2303 0.0107  0.0037  0.0135  271  PRO A CA  
1850  C C   . PRO A 273  ? 0.2476 0.2022 0.2470 0.0136  0.0049  0.0106  271  PRO A C   
1851  O O   . PRO A 273  ? 0.2533 0.2074 0.2505 0.0137  0.0054  0.0093  271  PRO A O   
1852  C CB  . PRO A 273  ? 0.2520 0.2033 0.2549 0.0099  0.0010  0.0144  271  PRO A CB  
1853  C CG  . PRO A 273  ? 0.2528 0.2035 0.2599 0.0111  -0.0008 0.0147  271  PRO A CG  
1854  C CD  . PRO A 273  ? 0.2247 0.1783 0.2311 0.0107  0.0007  0.0161  271  PRO A CD  
1855  N N   . ARG A 274  ? 0.2278 0.1840 0.2289 0.0159  0.0052  0.0094  272  ARG A N   
1856  C CA  . ARG A 274  ? 0.2262 0.1844 0.2264 0.0187  0.0064  0.0066  272  ARG A CA  
1857  C C   . ARG A 274  ? 0.2182 0.1806 0.2177 0.0195  0.0086  0.0072  272  ARG A C   
1858  O O   . ARG A 274  ? 0.2178 0.1829 0.2189 0.0220  0.0089  0.0057  272  ARG A O   
1859  C CB  . ARG A 274  ? 0.2300 0.1872 0.2335 0.0213  0.0044  0.0038  272  ARG A CB  
1860  C CG  . ARG A 274  ? 0.2538 0.2067 0.2588 0.0206  0.0019  0.0031  272  ARG A CG  
1861  C CD  . ARG A 274  ? 0.2389 0.1916 0.2404 0.0200  0.0028  0.0023  272  ARG A CD  
1862  N NE  . ARG A 274  ? 0.2530 0.2091 0.2524 0.0226  0.0045  -0.0005 272  ARG A NE  
1863  C CZ  . ARG A 274  ? 0.2401 0.1967 0.2410 0.0254  0.0034  -0.0042 272  ARG A CZ  
1864  N NH1 . ARG A 274  ? 0.2498 0.2031 0.2549 0.0262  0.0005  -0.0059 272  ARG A NH1 
1865  N NH2 . ARG A 274  ? 0.2694 0.2303 0.2678 0.0276  0.0052  -0.0064 272  ARG A NH2 
1866  N N   . TYR A 275  ? 0.2117 0.1749 0.2094 0.0174  0.0101  0.0094  273  TYR A N   
1867  C CA  . TYR A 275  ? 0.1927 0.1596 0.1902 0.0176  0.0120  0.0106  273  TYR A CA  
1868  C C   . TYR A 275  ? 0.2284 0.1982 0.2239 0.0190  0.0137  0.0098  273  TYR A C   
1869  O O   . TYR A 275  ? 0.2187 0.1883 0.2121 0.0177  0.0146  0.0107  273  TYR A O   
1870  C CB  . TYR A 275  ? 0.2170 0.1834 0.2142 0.0147  0.0123  0.0131  273  TYR A CB  
1871  C CG  . TYR A 275  ? 0.1873 0.1571 0.1850 0.0146  0.0139  0.0145  273  TYR A CG  
1872  C CD1 . TYR A 275  ? 0.2028 0.1757 0.2027 0.0162  0.0143  0.0147  273  TYR A CD1 
1873  C CD2 . TYR A 275  ? 0.1976 0.1677 0.1943 0.0129  0.0149  0.0157  273  TYR A CD2 
1874  C CE1 . TYR A 275  ? 0.2282 0.2047 0.2291 0.0159  0.0158  0.0164  273  TYR A CE1 
1875  C CE2 . TYR A 275  ? 0.2109 0.1839 0.2090 0.0126  0.0161  0.0174  273  TYR A CE2 
1876  C CZ  . TYR A 275  ? 0.2277 0.2040 0.2279 0.0140  0.0165  0.0179  273  TYR A CZ  
1877  O OH  . TYR A 275  ? 0.2264 0.2061 0.2285 0.0136  0.0176  0.0199  273  TYR A OH  
1878  N N   . SER A 276  ? 0.2136 0.1867 0.2098 0.0218  0.0141  0.0079  274  SER A N   
1879  C CA  . SER A 276  ? 0.2073 0.1844 0.2014 0.0234  0.0157  0.0072  274  SER A CA  
1880  C C   . SER A 276  ? 0.2171 0.1997 0.2127 0.0263  0.0163  0.0057  274  SER A C   
1881  O O   . SER A 276  ? 0.2079 0.1901 0.2061 0.0277  0.0151  0.0042  274  SER A O   
1882  C CB  . SER A 276  ? 0.2500 0.2250 0.2422 0.0241  0.0149  0.0048  274  SER A CB  
1883  O OG  . SER A 276  ? 0.3028 0.2773 0.2968 0.0264  0.0133  0.0015  274  SER A OG  
1884  N N   . ARG A 277  ? 0.2208 0.2091 0.2149 0.0273  0.0182  0.0064  275  ARG A N   
1885  C CA  . ARG A 277  ? 0.2068 0.2021 0.2020 0.0303  0.0191  0.0049  275  ARG A CA  
1886  C C   . ARG A 277  ? 0.2158 0.2110 0.2115 0.0333  0.0176  0.0001  275  ARG A C   
1887  O O   . ARG A 277  ? 0.2161 0.2148 0.2141 0.0359  0.0174  -0.0021 275  ARG A O   
1888  C CB  . ARG A 277  ? 0.2041 0.2062 0.1973 0.0307  0.0213  0.0069  275  ARG A CB  
1889  C CG  . ARG A 277  ? 0.2063 0.2175 0.2000 0.0340  0.0224  0.0052  275  ARG A CG  
1890  C CD  . ARG A 277  ? 0.2041 0.2180 0.2010 0.0346  0.0227  0.0058  275  ARG A CD  
1891  N NE  . ARG A 277  ? 0.2112 0.2348 0.2085 0.0379  0.0239  0.0040  275  ARG A NE  
1892  C CZ  . ARG A 277  ? 0.2070 0.2326 0.2051 0.0414  0.0229  -0.0011 275  ARG A CZ  
1893  N NH1 . ARG A 277  ? 0.1964 0.2146 0.1954 0.0419  0.0205  -0.0047 275  ARG A NH1 
1894  N NH2 . ARG A 277  ? 0.1999 0.2355 0.1985 0.0445  0.0242  -0.0028 275  ARG A NH2 
1895  N N   . ALA A 278  ? 0.2262 0.2175 0.2202 0.0332  0.0165  -0.0019 276  ALA A N   
1896  C CA  . ALA A 278  ? 0.2414 0.2323 0.2365 0.0361  0.0146  -0.0068 276  ALA A CA  
1897  C C   . ALA A 278  ? 0.2420 0.2285 0.2413 0.0364  0.0124  -0.0082 276  ALA A C   
1898  O O   . ALA A 278  ? 0.2490 0.2366 0.2509 0.0394  0.0108  -0.0123 276  ALA A O   
1899  C CB  . ALA A 278  ? 0.2508 0.2377 0.2438 0.0354  0.0136  -0.0082 276  ALA A CB  
1900  N N   . GLN A 279  ? 0.2169 0.1987 0.2173 0.0335  0.0119  -0.0048 277  GLN A N   
1901  C CA  . GLN A 279  ? 0.2191 0.1969 0.2235 0.0334  0.0097  -0.0050 277  GLN A CA  
1902  C C   . GLN A 279  ? 0.2382 0.2189 0.2443 0.0330  0.0107  -0.0026 277  GLN A C   
1903  O O   . GLN A 279  ? 0.2303 0.2073 0.2385 0.0313  0.0095  -0.0005 277  GLN A O   
1904  C CB  . GLN A 279  ? 0.2353 0.2061 0.2397 0.0302  0.0080  -0.0029 277  GLN A CB  
1905  C CG  . GLN A 279  ? 0.2345 0.2023 0.2377 0.0302  0.0068  -0.0050 277  GLN A CG  
1906  C CD  . GLN A 279  ? 0.2813 0.2481 0.2880 0.0332  0.0043  -0.0094 277  GLN A CD  
1907  O OE1 . GLN A 279  ? 0.3500 0.3146 0.3612 0.0338  0.0022  -0.0098 277  GLN A OE1 
1908  N NE2 . GLN A 279  ? 0.2467 0.2155 0.2520 0.0352  0.0044  -0.0128 277  GLN A NE2 
1909  N N   . ALA A 280  ? 0.2134 0.2011 0.2186 0.0346  0.0130  -0.0025 278  ALA A N   
1910  C CA  . ALA A 280  ? 0.2463 0.2372 0.2529 0.0340  0.0142  0.0002  278  ALA A CA  
1911  C C   . ALA A 280  ? 0.2242 0.2134 0.2353 0.0351  0.0123  -0.0008 278  ALA A C   
1912  O O   . ALA A 280  ? 0.2264 0.2143 0.2390 0.0331  0.0121  0.0022  278  ALA A O   
1913  C CB  . ALA A 280  ? 0.2326 0.2324 0.2383 0.0359  0.0167  0.0002  278  ALA A CB  
1914  N N   . ALA A 281  ? 0.2115 0.2009 0.2252 0.0383  0.0106  -0.0051 279  ALA A N   
1915  C CA  . ALA A 281  ? 0.2253 0.2131 0.2440 0.0395  0.0084  -0.0062 279  ALA A CA  
1916  C C   . ALA A 281  ? 0.2398 0.2200 0.2601 0.0365  0.0062  -0.0035 279  ALA A C   
1917  O O   . ALA A 281  ? 0.2294 0.2089 0.2527 0.0357  0.0053  -0.0015 279  ALA A O   
1918  C CB  . ALA A 281  ? 0.2555 0.2445 0.2775 0.0437  0.0066  -0.0119 279  ALA A CB  
1919  N N   . ARG A 282  ? 0.2143 0.1895 0.2329 0.0347  0.0051  -0.0032 280  ARG A N   
1920  C CA  . ARG A 282  ? 0.2224 0.1917 0.2420 0.0315  0.0032  -0.0001 280  ARG A CA  
1921  C C   . ARG A 282  ? 0.2112 0.1814 0.2284 0.0283  0.0050  0.0043  280  ARG A C   
1922  O O   . ARG A 282  ? 0.2193 0.1874 0.2383 0.0263  0.0037  0.0069  280  ARG A O   
1923  C CB  . ARG A 282  ? 0.2253 0.1899 0.2434 0.0301  0.0019  -0.0005 280  ARG A CB  
1924  C CG  . ARG A 282  ? 0.2489 0.2110 0.2709 0.0326  -0.0009 -0.0044 280  ARG A CG  
1925  C CD  . ARG A 282  ? 0.2608 0.2178 0.2819 0.0304  -0.0025 -0.0036 280  ARG A CD  
1926  N NE  . ARG A 282  ? 0.2635 0.2170 0.2859 0.0270  -0.0039 0.0008  280  ARG A NE  
1927  C CZ  . ARG A 282  ? 0.2606 0.2110 0.2816 0.0241  -0.0047 0.0031  280  ARG A CZ  
1928  N NH1 . ARG A 282  ? 0.2363 0.1858 0.2546 0.0241  -0.0043 0.0014  280  ARG A NH1 
1929  N NH2 . ARG A 282  ? 0.2746 0.2232 0.2967 0.0211  -0.0058 0.0072  280  ARG A NH2 
1930  N N   . VAL A 283  ? 0.1969 0.1704 0.2101 0.0277  0.0077  0.0050  281  VAL A N   
1931  C CA  . VAL A 283  ? 0.2074 0.1818 0.2190 0.0249  0.0092  0.0086  281  VAL A CA  
1932  C C   . VAL A 283  ? 0.2256 0.2027 0.2402 0.0253  0.0092  0.0099  281  VAL A C   
1933  O O   . VAL A 283  ? 0.2091 0.1848 0.2246 0.0229  0.0085  0.0125  281  VAL A O   
1934  C CB  . VAL A 283  ? 0.2056 0.1831 0.2135 0.0245  0.0118  0.0091  281  VAL A CB  
1935  C CG1 . VAL A 283  ? 0.2371 0.2160 0.2447 0.0220  0.0130  0.0125  281  VAL A CG1 
1936  C CG2 . VAL A 283  ? 0.2188 0.1930 0.2238 0.0235  0.0116  0.0085  281  VAL A CG2 
1937  N N   . MET A 284  ? 0.2054 0.1872 0.2217 0.0283  0.0100  0.0080  282  MET A N   
1938  C CA  . MET A 284  ? 0.1997 0.1845 0.2191 0.0287  0.0101  0.0093  282  MET A CA  
1939  C C   . MET A 284  ? 0.2221 0.2035 0.2457 0.0289  0.0072  0.0091  282  MET A C   
1940  O O   . MET A 284  ? 0.2401 0.2220 0.2657 0.0278  0.0068  0.0115  282  MET A O   
1941  C CB  . MET A 284  ? 0.2153 0.2071 0.2358 0.0320  0.0117  0.0072  282  MET A CB  
1942  C CG  . MET A 284  ? 0.2335 0.2297 0.2503 0.0317  0.0145  0.0081  282  MET A CG  
1943  S SD  . MET A 284  ? 0.2499 0.2464 0.2655 0.0277  0.0160  0.0130  282  MET A SD  
1944  C CE  . MET A 284  ? 0.2301 0.2309 0.2500 0.0282  0.0160  0.0145  282  MET A CE  
1945  N N   . GLY A 285  ? 0.2169 0.1946 0.2421 0.0304  0.0051  0.0066  283  GLY A N   
1946  C CA  . GLY A 285  ? 0.2085 0.1828 0.2384 0.0306  0.0020  0.0069  283  GLY A CA  
1947  C C   . GLY A 285  ? 0.2339 0.2036 0.2633 0.0269  0.0004  0.0105  283  GLY A C   
1948  O O   . GLY A 285  ? 0.2490 0.2176 0.2820 0.0261  -0.0015 0.0126  283  GLY A O   
1949  N N   . GLU A 286  ? 0.2273 0.1950 0.2525 0.0246  0.0012  0.0115  284  GLU A N   
1950  C CA  . GLU A 286  ? 0.2101 0.1743 0.2349 0.0213  -0.0004 0.0144  284  GLU A CA  
1951  C C   . GLU A 286  ? 0.2346 0.2002 0.2553 0.0182  0.0015  0.0171  284  GLU A C   
1952  O O   . GLU A 286  ? 0.2728 0.2379 0.2939 0.0157  0.0003  0.0199  284  GLU A O   
1953  C CB  . GLU A 286  ? 0.2287 0.1890 0.2527 0.0212  -0.0016 0.0131  284  GLU A CB  
1954  C CG  . GLU A 286  ? 0.2595 0.2181 0.2882 0.0243  -0.0039 0.0099  284  GLU A CG  
1955  C CD  . GLU A 286  ? 0.2766 0.2320 0.3042 0.0245  -0.0047 0.0079  284  GLU A CD  
1956  O OE1 . GLU A 286  ? 0.2916 0.2455 0.3160 0.0217  -0.0044 0.0100  284  GLU A OE1 
1957  O OE2 . GLU A 286  ? 0.2898 0.2447 0.3201 0.0276  -0.0059 0.0040  284  GLU A OE2 
1958  N N   . LEU A 287  ? 0.2106 0.1782 0.2277 0.0183  0.0040  0.0161  285  LEU A N   
1959  C CA  . LEU A 287  ? 0.2075 0.1762 0.2215 0.0156  0.0055  0.0181  285  LEU A CA  
1960  C C   . LEU A 287  ? 0.2228 0.1949 0.2384 0.0153  0.0062  0.0196  285  LEU A C   
1961  O O   . LEU A 287  ? 0.2288 0.2012 0.2440 0.0128  0.0059  0.0216  285  LEU A O   
1962  C CB  . LEU A 287  ? 0.2091 0.1785 0.2196 0.0158  0.0077  0.0168  285  LEU A CB  
1963  C CG  . LEU A 287  ? 0.2511 0.2217 0.2594 0.0134  0.0091  0.0184  285  LEU A CG  
1964  C CD1 . LEU A 287  ? 0.2896 0.2585 0.2972 0.0107  0.0078  0.0199  285  LEU A CD1 
1965  C CD2 . LEU A 287  ? 0.2807 0.2515 0.2861 0.0138  0.0108  0.0173  285  LEU A CD2 
1966  N N   . LEU A 288  ? 0.2029 0.1780 0.2203 0.0177  0.0073  0.0185  286  LEU A N   
1967  C CA  . LEU A 288  ? 0.2134 0.1921 0.2326 0.0174  0.0080  0.0200  286  LEU A CA  
1968  C C   . LEU A 288  ? 0.2164 0.1944 0.2381 0.0160  0.0060  0.0220  286  LEU A C   
1969  O O   . LEU A 288  ? 0.2272 0.2067 0.2486 0.0138  0.0063  0.0239  286  LEU A O   
1970  C CB  . LEU A 288  ? 0.2297 0.2125 0.2509 0.0206  0.0092  0.0185  286  LEU A CB  
1971  C CG  . LEU A 288  ? 0.2831 0.2703 0.3070 0.0206  0.0099  0.0201  286  LEU A CG  
1972  C CD1 . LEU A 288  ? 0.2719 0.2604 0.2941 0.0179  0.0113  0.0222  286  LEU A CD1 
1973  C CD2 . LEU A 288  ? 0.3369 0.3290 0.3626 0.0240  0.0111  0.0182  286  LEU A CD2 
1974  N N   . PRO A 289  ? 0.2249 0.2009 0.2495 0.0170  0.0037  0.0218  287  PRO A N   
1975  C CA  . PRO A 289  ? 0.2017 0.1776 0.2287 0.0154  0.0017  0.0244  287  PRO A CA  
1976  C C   . PRO A 289  ? 0.2153 0.1902 0.2395 0.0119  0.0012  0.0265  287  PRO A C   
1977  O O   . PRO A 289  ? 0.2051 0.1818 0.2302 0.0101  0.0004  0.0286  287  PRO A O   
1978  C CB  . PRO A 289  ? 0.2403 0.2134 0.2711 0.0171  -0.0009 0.0238  287  PRO A CB  
1979  C CG  . PRO A 289  ? 0.2814 0.2547 0.3127 0.0204  0.0001  0.0203  287  PRO A CG  
1980  C CD  . PRO A 289  ? 0.2381 0.2123 0.2646 0.0198  0.0027  0.0193  287  PRO A CD  
1981  N N   . ARG A 290  ? 0.1986 0.1714 0.2196 0.0110  0.0017  0.0257  288  ARG A N   
1982  C CA  . ARG A 290  ? 0.1981 0.1709 0.2163 0.0079  0.0013  0.0273  288  ARG A CA  
1983  C C   . ARG A 290  ? 0.1996 0.1751 0.2161 0.0065  0.0030  0.0272  288  ARG A C   
1984  O O   . ARG A 290  ? 0.2127 0.1901 0.2288 0.0044  0.0023  0.0287  288  ARG A O   
1985  C CB  . ARG A 290  ? 0.2342 0.2043 0.2497 0.0074  0.0014  0.0264  288  ARG A CB  
1986  C CG  . ARG A 290  ? 0.2498 0.2170 0.2678 0.0083  -0.0008 0.0267  288  ARG A CG  
1987  C CD  . ARG A 290  ? 0.2888 0.2536 0.3044 0.0078  -0.0007 0.0257  288  ARG A CD  
1988  N NE  . ARG A 290  ? 0.3394 0.3012 0.3582 0.0088  -0.0031 0.0258  288  ARG A NE  
1989  C CZ  . ARG A 290  ? 0.3349 0.2939 0.3531 0.0097  -0.0033 0.0240  288  ARG A CZ  
1990  N NH1 . ARG A 290  ? 0.3054 0.2645 0.3196 0.0097  -0.0012 0.0222  288  ARG A NH1 
1991  N NH2 . ARG A 290  ? 0.3754 0.3315 0.3977 0.0106  -0.0058 0.0240  288  ARG A NH2 
1992  N N   . VAL A 291  ? 0.1925 0.1685 0.2081 0.0078  0.0051  0.0257  289  VAL A N   
1993  C CA  . VAL A 291  ? 0.1977 0.1760 0.2127 0.0065  0.0064  0.0258  289  VAL A CA  
1994  C C   . VAL A 291  ? 0.2014 0.1825 0.2194 0.0063  0.0058  0.0272  289  VAL A C   
1995  O O   . VAL A 291  ? 0.1975 0.1803 0.2156 0.0043  0.0055  0.0279  289  VAL A O   
1996  C CB  . VAL A 291  ? 0.1798 0.1585 0.1941 0.0079  0.0086  0.0246  289  VAL A CB  
1997  C CG1 . VAL A 291  ? 0.2077 0.1884 0.2224 0.0064  0.0095  0.0252  289  VAL A CG1 
1998  C CG2 . VAL A 291  ? 0.2086 0.1847 0.2200 0.0082  0.0090  0.0233  289  VAL A CG2 
1999  N N   . LYS A 292  ? 0.1884 0.1702 0.2093 0.0084  0.0054  0.0274  290  LYS A N   
2000  C CA  . LYS A 292  ? 0.1719 0.1565 0.1960 0.0083  0.0047  0.0288  290  LYS A CA  
2001  C C   . LYS A 292  ? 0.2063 0.1911 0.2305 0.0061  0.0027  0.0305  290  LYS A C   
2002  O O   . LYS A 292  ? 0.1884 0.1758 0.2135 0.0046  0.0024  0.0315  290  LYS A O   
2003  C CB  . LYS A 292  ? 0.1713 0.1566 0.1987 0.0112  0.0044  0.0284  290  LYS A CB  
2004  C CG  . LYS A 292  ? 0.1871 0.1753 0.2181 0.0112  0.0035  0.0300  290  LYS A CG  
2005  C CD  . LYS A 292  ? 0.1992 0.1885 0.2339 0.0143  0.0031  0.0293  290  LYS A CD  
2006  C CE  . LYS A 292  ? 0.2281 0.2205 0.2665 0.0140  0.0021  0.0310  290  LYS A CE  
2007  N NZ  . LYS A 292  ? 0.2274 0.2221 0.2698 0.0174  0.0022  0.0299  290  LYS A NZ  
2008  N N   . ALA A 293  ? 0.1804 0.1630 0.2039 0.0057  0.0011  0.0311  291  ALA A N   
2009  C CA  . ALA A 293  ? 0.1967 0.1807 0.2204 0.0035  -0.0009 0.0333  291  ALA A CA  
2010  C C   . ALA A 293  ? 0.1981 0.1841 0.2187 0.0009  -0.0004 0.0329  291  ALA A C   
2011  O O   . ALA A 293  ? 0.2120 0.2011 0.2331 -0.0007 -0.0014 0.0341  291  ALA A O   
2012  C CB  . ALA A 293  ? 0.2052 0.1866 0.2290 0.0033  -0.0027 0.0345  291  ALA A CB  
2013  N N   . LEU A 294  ? 0.1861 0.1705 0.2037 0.0007  0.0011  0.0310  292  LEU A N   
2014  C CA  . LEU A 294  ? 0.1837 0.1700 0.1992 -0.0014 0.0015  0.0300  292  LEU A CA  
2015  C C   . LEU A 294  ? 0.1933 0.1818 0.2108 -0.0015 0.0021  0.0295  292  LEU A C   
2016  O O   . LEU A 294  ? 0.1820 0.1733 0.1995 -0.0033 0.0013  0.0293  292  LEU A O   
2017  C CB  . LEU A 294  ? 0.2026 0.1866 0.2152 -0.0013 0.0028  0.0281  292  LEU A CB  
2018  C CG  . LEU A 294  ? 0.2058 0.1880 0.2163 -0.0015 0.0021  0.0285  292  LEU A CG  
2019  C CD1 . LEU A 294  ? 0.1975 0.1773 0.2056 -0.0011 0.0036  0.0265  292  LEU A CD1 
2020  C CD2 . LEU A 294  ? 0.2321 0.2175 0.2413 -0.0038 0.0006  0.0298  292  LEU A CD2 
2021  N N   . ALA A 295  ? 0.1663 0.1539 0.1857 0.0002  0.0034  0.0293  293  ALA A N   
2022  C CA  . ALA A 295  ? 0.1862 0.1761 0.2082 0.0000  0.0040  0.0294  293  ALA A CA  
2023  C C   . ALA A 295  ? 0.1946 0.1875 0.2192 -0.0007 0.0025  0.0309  293  ALA A C   
2024  O O   . ALA A 295  ? 0.2000 0.1953 0.2261 -0.0021 0.0021  0.0307  293  ALA A O   
2025  C CB  . ALA A 295  ? 0.1961 0.1857 0.2197 0.0021  0.0057  0.0294  293  ALA A CB  
2026  N N   . LEU A 296  ? 0.1833 0.1761 0.2089 0.0003  0.0014  0.0324  294  LEU A N   
2027  C CA  . LEU A 296  ? 0.1825 0.1782 0.2106 -0.0003 -0.0003 0.0341  294  LEU A CA  
2028  C C   . LEU A 296  ? 0.1997 0.1979 0.2260 -0.0029 -0.0017 0.0342  294  LEU A C   
2029  O O   . LEU A 296  ? 0.1851 0.1867 0.2132 -0.0040 -0.0027 0.0347  294  LEU A O   
2030  C CB  . LEU A 296  ? 0.1830 0.1778 0.2129 0.0012  -0.0016 0.0358  294  LEU A CB  
2031  C CG  . LEU A 296  ? 0.2200 0.2140 0.2527 0.0041  -0.0006 0.0353  294  LEU A CG  
2032  C CD1 . LEU A 296  ? 0.2280 0.2200 0.2625 0.0057  -0.0022 0.0362  294  LEU A CD1 
2033  C CD2 . LEU A 296  ? 0.2530 0.2506 0.2893 0.0045  -0.0004 0.0361  294  LEU A CD2 
2034  N N   . LEU A 297  ? 0.2033 0.2006 0.2263 -0.0039 -0.0019 0.0336  295  LEU A N   
2035  C CA  . LEU A 297  ? 0.2171 0.2179 0.2382 -0.0062 -0.0032 0.0333  295  LEU A CA  
2036  C C   . LEU A 297  ? 0.1968 0.1988 0.2177 -0.0072 -0.0025 0.0306  295  LEU A C   
2037  O O   . LEU A 297  ? 0.2052 0.2112 0.2268 -0.0086 -0.0038 0.0301  295  LEU A O   
2038  C CB  . LEU A 297  ? 0.2447 0.2448 0.2624 -0.0069 -0.0035 0.0335  295  LEU A CB  
2039  C CG  . LEU A 297  ? 0.2612 0.2665 0.2769 -0.0091 -0.0051 0.0340  295  LEU A CG  
2040  C CD1 . LEU A 297  ? 0.2908 0.2995 0.3086 -0.0097 -0.0071 0.0373  295  LEU A CD1 
2041  C CD2 . LEU A 297  ? 0.2941 0.2988 0.3067 -0.0097 -0.0051 0.0344  295  LEU A CD2 
2042  N N   . ALA A 298  ? 0.1915 0.1904 0.2121 -0.0064 -0.0008 0.0288  296  ALA A N   
2043  C CA  . ALA A 298  ? 0.1893 0.1888 0.2110 -0.0072 -0.0005 0.0264  296  ALA A CA  
2044  C C   . ALA A 298  ? 0.1919 0.1935 0.2178 -0.0074 -0.0010 0.0272  296  ALA A C   
2045  O O   . ALA A 298  ? 0.1904 0.1945 0.2178 -0.0088 -0.0021 0.0256  296  ALA A O   
2046  C CB  . ALA A 298  ? 0.2036 0.1993 0.2249 -0.0063 0.0013  0.0253  296  ALA A CB  
2047  N N   . LYS A 299  ? 0.1738 0.1748 0.2018 -0.0060 -0.0005 0.0294  297  LYS A N   
2048  C CA  A LYS A 299  ? 0.1861 0.1897 0.2182 -0.0061 -0.0010 0.0305  297  LYS A CA  
2049  C CA  B LYS A 299  ? 0.1863 0.1899 0.2183 -0.0061 -0.0010 0.0305  297  LYS A CA  
2050  C C   . LYS A 299  ? 0.2095 0.2171 0.2420 -0.0076 -0.0031 0.0309  297  LYS A C   
2051  O O   . LYS A 299  ? 0.2159 0.2261 0.2510 -0.0088 -0.0040 0.0302  297  LYS A O   
2052  C CB  A LYS A 299  ? 0.1913 0.1944 0.2253 -0.0040 0.0000  0.0326  297  LYS A CB  
2053  C CB  B LYS A 299  ? 0.1915 0.1945 0.2255 -0.0040 0.0000  0.0326  297  LYS A CB  
2054  C CG  A LYS A 299  ? 0.2148 0.2213 0.2527 -0.0040 -0.0010 0.0343  297  LYS A CG  
2055  C CG  B LYS A 299  ? 0.2153 0.2215 0.2533 -0.0038 -0.0007 0.0342  297  LYS A CG  
2056  C CD  A LYS A 299  ? 0.2163 0.2228 0.2565 -0.0016 0.0001  0.0358  297  LYS A CD  
2057  C CD  B LYS A 299  ? 0.2127 0.2187 0.2528 -0.0013 0.0006  0.0356  297  LYS A CD  
2058  C CE  A LYS A 299  ? 0.2378 0.2478 0.2817 -0.0015 -0.0012 0.0375  297  LYS A CE  
2059  C CE  B LYS A 299  ? 0.2423 0.2518 0.2864 -0.0009 -0.0003 0.0373  297  LYS A CE  
2060  N NZ  A LYS A 299  ? 0.2329 0.2437 0.2796 0.0011  -0.0002 0.0386  297  LYS A NZ  
2061  N NZ  B LYS A 299  ? 0.2385 0.2490 0.2823 -0.0015 -0.0024 0.0383  297  LYS A NZ  
2062  N N   . ASN A 300  ? 0.1999 0.2084 0.2301 -0.0077 -0.0041 0.0322  298  ASN A N   
2063  C CA  . ASN A 300  ? 0.1992 0.2123 0.2297 -0.0092 -0.0063 0.0330  298  ASN A CA  
2064  C C   . ASN A 300  ? 0.2034 0.2195 0.2326 -0.0111 -0.0072 0.0301  298  ASN A C   
2065  O O   . ASN A 300  ? 0.2255 0.2458 0.2565 -0.0122 -0.0087 0.0297  298  ASN A O   
2066  C CB  . ASN A 300  ? 0.2362 0.2501 0.2649 -0.0091 -0.0074 0.0355  298  ASN A CB  
2067  C CG  . ASN A 300  ? 0.2472 0.2666 0.2768 -0.0105 -0.0097 0.0372  298  ASN A CG  
2068  O OD1 . ASN A 300  ? 0.3010 0.3244 0.3280 -0.0122 -0.0108 0.0365  298  ASN A OD1 
2069  N ND2 . ASN A 300  ? 0.3062 0.3265 0.3395 -0.0098 -0.0103 0.0393  298  ASN A ND2 
2070  N N   . TYR A 301  ? 0.2042 0.2188 0.2305 -0.0113 -0.0064 0.0278  299  TYR A N   
2071  C CA  . TYR A 301  ? 0.2133 0.2307 0.2388 -0.0128 -0.0073 0.0242  299  TYR A CA  
2072  C C   . TYR A 301  ? 0.2164 0.2319 0.2456 -0.0128 -0.0069 0.0218  299  TYR A C   
2073  O O   . TYR A 301  ? 0.2181 0.2359 0.2481 -0.0139 -0.0081 0.0184  299  TYR A O   
2074  C CB  . TYR A 301  ? 0.1919 0.2089 0.2133 -0.0129 -0.0068 0.0225  299  TYR A CB  
2075  C CG  . TYR A 301  ? 0.2055 0.2261 0.2235 -0.0136 -0.0076 0.0245  299  TYR A CG  
2076  C CD1 . TYR A 301  ? 0.2130 0.2406 0.2300 -0.0151 -0.0095 0.0240  299  TYR A CD1 
2077  C CD2 . TYR A 301  ? 0.1911 0.2087 0.2071 -0.0128 -0.0068 0.0269  299  TYR A CD2 
2078  C CE1 . TYR A 301  ? 0.2148 0.2467 0.2289 -0.0159 -0.0103 0.0265  299  TYR A CE1 
2079  C CE2 . TYR A 301  ? 0.2068 0.2279 0.2204 -0.0137 -0.0078 0.0293  299  TYR A CE2 
2080  C CZ  . TYR A 301  ? 0.2341 0.2625 0.2466 -0.0153 -0.0096 0.0294  299  TYR A CZ  
2081  O OH  . TYR A 301  ? 0.2282 0.2609 0.2385 -0.0164 -0.0106 0.0324  299  TYR A OH  
2082  N N   . ASP A 302  ? 0.2042 0.2160 0.2360 -0.0117 -0.0055 0.0235  300  ASP A N   
2083  C CA  . ASP A 302  ? 0.1995 0.2092 0.2352 -0.0118 -0.0051 0.0222  300  ASP A CA  
2084  C C   . ASP A 302  ? 0.2178 0.2255 0.2525 -0.0122 -0.0049 0.0190  300  ASP A C   
2085  O O   . ASP A 302  ? 0.2031 0.2115 0.2406 -0.0132 -0.0061 0.0161  300  ASP A O   
2086  C CB  . ASP A 302  ? 0.2126 0.2257 0.2527 -0.0131 -0.0068 0.0217  300  ASP A CB  
2087  C CG  . ASP A 302  ? 0.2433 0.2545 0.2888 -0.0131 -0.0063 0.0224  300  ASP A CG  
2088  O OD1 . ASP A 302  ? 0.2124 0.2208 0.2580 -0.0118 -0.0043 0.0247  300  ASP A OD1 
2089  O OD2 . ASP A 302  ? 0.2782 0.2908 0.3279 -0.0144 -0.0079 0.0208  300  ASP A OD2 
2090  N N   . ILE A 303  ? 0.2023 0.2071 0.2333 -0.0112 -0.0034 0.0193  301  ILE A N   
2091  C CA  . ILE A 303  ? 0.2052 0.2076 0.2354 -0.0112 -0.0029 0.0166  301  ILE A CA  
2092  C C   . ILE A 303  ? 0.2173 0.2154 0.2481 -0.0099 -0.0009 0.0185  301  ILE A C   
2093  O O   . ILE A 303  ? 0.2006 0.1980 0.2311 -0.0088 0.0003  0.0214  301  ILE A O   
2094  C CB  . ILE A 303  ? 0.1908 0.1945 0.2160 -0.0113 -0.0030 0.0149  301  ILE A CB  
2095  C CG1 . ILE A 303  ? 0.1845 0.1861 0.2062 -0.0102 -0.0016 0.0178  301  ILE A CG1 
2096  C CG2 . ILE A 303  ? 0.2101 0.2196 0.2343 -0.0125 -0.0050 0.0135  301  ILE A CG2 
2097  C CD1 . ILE A 303  ? 0.2250 0.2273 0.2421 -0.0104 -0.0015 0.0165  301  ILE A CD1 
2098  N N   . GLY A 304  ? 0.2086 0.2041 0.2402 -0.0100 -0.0006 0.0166  302  GLY A N   
2099  C CA  . GLY A 304  ? 0.1957 0.1878 0.2274 -0.0088 0.0013  0.0184  302  GLY A CA  
2100  C C   . GLY A 304  ? 0.1957 0.1863 0.2221 -0.0076 0.0026  0.0188  302  GLY A C   
2101  O O   . GLY A 304  ? 0.2091 0.2006 0.2322 -0.0080 0.0020  0.0171  302  GLY A O   
2102  N N   . LEU A 305  ? 0.1839 0.1727 0.2098 -0.0062 0.0042  0.0212  303  LEU A N   
2103  C CA  . LEU A 305  ? 0.1982 0.1850 0.2200 -0.0050 0.0054  0.0214  303  LEU A CA  
2104  C C   . LEU A 305  ? 0.2153 0.2000 0.2379 -0.0040 0.0070  0.0223  303  LEU A C   
2105  O O   . LEU A 305  ? 0.1971 0.1826 0.2218 -0.0031 0.0079  0.0245  303  LEU A O   
2106  C CB  . LEU A 305  ? 0.2142 0.2018 0.2344 -0.0040 0.0055  0.0233  303  LEU A CB  
2107  C CG  . LEU A 305  ? 0.2212 0.2065 0.2377 -0.0028 0.0062  0.0233  303  LEU A CG  
2108  C CD1 . LEU A 305  ? 0.2390 0.2253 0.2542 -0.0028 0.0051  0.0245  303  LEU A CD1 
2109  C CD2 . LEU A 305  ? 0.2674 0.2512 0.2842 -0.0009 0.0079  0.0243  303  LEU A CD2 
2110  N N   . ASN A 306  ? 0.2116 0.1942 0.2327 -0.0040 0.0073  0.0208  304  ASN A N   
2111  C CA  . ASN A 306  ? 0.2299 0.2109 0.2521 -0.0033 0.0086  0.0217  304  ASN A CA  
2112  C C   . ASN A 306  ? 0.1968 0.1761 0.2148 -0.0018 0.0098  0.0218  304  ASN A C   
2113  O O   . ASN A 306  ? 0.2120 0.1902 0.2267 -0.0019 0.0094  0.0202  304  ASN A O   
2114  C CB  . ASN A 306  ? 0.2168 0.1964 0.2411 -0.0044 0.0077  0.0199  304  ASN A CB  
2115  C CG  . ASN A 306  ? 0.2165 0.1944 0.2415 -0.0037 0.0088  0.0210  304  ASN A CG  
2116  O OD1 . ASN A 306  ? 0.2655 0.2416 0.2873 -0.0030 0.0094  0.0199  304  ASN A OD1 
2117  N ND2 . ASN A 306  ? 0.2064 0.1852 0.2357 -0.0038 0.0091  0.0236  304  ASN A ND2 
2118  N N   . ILE A 307  ? 0.1933 0.1729 0.2116 -0.0004 0.0113  0.0237  305  ILE A N   
2119  C CA  . ILE A 307  ? 0.1970 0.1752 0.2119 0.0012  0.0124  0.0235  305  ILE A CA  
2120  C C   . ILE A 307  ? 0.1805 0.1572 0.1956 0.0009  0.0129  0.0232  305  ILE A C   
2121  O O   . ILE A 307  ? 0.2043 0.1822 0.2224 0.0009  0.0134  0.0251  305  ILE A O   
2122  C CB  . ILE A 307  ? 0.2055 0.1857 0.2205 0.0031  0.0136  0.0251  305  ILE A CB  
2123  C CG1 . ILE A 307  ? 0.2068 0.1880 0.2219 0.0035  0.0129  0.0251  305  ILE A CG1 
2124  C CG2 . ILE A 307  ? 0.2075 0.1865 0.2193 0.0048  0.0146  0.0244  305  ILE A CG2 
2125  C CD1 . ILE A 307  ? 0.2375 0.2214 0.2538 0.0055  0.0139  0.0263  305  ILE A CD1 
2126  N N   . ASP A 308  ? 0.1923 0.1668 0.2046 0.0007  0.0125  0.0212  306  ASP A N   
2127  C CA  . ASP A 308  ? 0.1855 0.1584 0.1980 0.0006  0.0128  0.0207  306  ASP A CA  
2128  C C   . ASP A 308  ? 0.1892 0.1625 0.2002 0.0023  0.0143  0.0222  306  ASP A C   
2129  O O   . ASP A 308  ? 0.2059 0.1799 0.2146 0.0037  0.0150  0.0225  306  ASP A O   
2130  C CB  . ASP A 308  ? 0.1985 0.1697 0.2083 0.0001  0.0121  0.0180  306  ASP A CB  
2131  C CG  . ASP A 308  ? 0.2441 0.2160 0.2555 -0.0015 0.0106  0.0160  306  ASP A CG  
2132  O OD1 . ASP A 308  ? 0.2346 0.2074 0.2501 -0.0023 0.0099  0.0164  306  ASP A OD1 
2133  O OD2 . ASP A 308  ? 0.2799 0.2521 0.2887 -0.0019 0.0100  0.0140  306  ASP A OD2 
2134  N N   . ALA A 309  ? 0.1915 0.1644 0.2041 0.0022  0.0146  0.0232  307  ALA A N   
2135  C CA  . ALA A 309  ? 0.1801 0.1544 0.1915 0.0036  0.0160  0.0248  307  ALA A CA  
2136  C C   . ALA A 309  ? 0.2076 0.1795 0.2156 0.0042  0.0162  0.0230  307  ALA A C   
2137  O O   . ALA A 309  ? 0.2193 0.1890 0.2277 0.0032  0.0153  0.0215  307  ALA A O   
2138  C CB  . ALA A 309  ? 0.1829 0.1592 0.1985 0.0031  0.0163  0.0279  307  ALA A CB  
2139  N N   . GLU A 310  ? 0.1988 0.1717 0.2037 0.0058  0.0172  0.0230  308  GLU A N   
2140  C CA  . GLU A 310  ? 0.2153 0.1860 0.2169 0.0064  0.0172  0.0212  308  GLU A CA  
2141  C C   . GLU A 310  ? 0.1850 0.1575 0.1859 0.0076  0.0182  0.0227  308  GLU A C   
2142  O O   . GLU A 310  ? 0.2036 0.1778 0.2075 0.0071  0.0185  0.0251  308  GLU A O   
2143  C CB  . GLU A 310  ? 0.2023 0.1719 0.2008 0.0071  0.0168  0.0193  308  GLU A CB  
2144  C CG  . GLU A 310  ? 0.1937 0.1623 0.1930 0.0056  0.0157  0.0186  308  GLU A CG  
2145  C CD  . GLU A 310  ? 0.2455 0.2130 0.2425 0.0059  0.0150  0.0173  308  GLU A CD  
2146  O OE1 . GLU A 310  ? 0.2452 0.2110 0.2400 0.0058  0.0147  0.0160  308  GLU A OE1 
2147  O OE2 . GLU A 310  ? 0.2272 0.1955 0.2250 0.0062  0.0147  0.0178  308  GLU A OE2 
2148  N N   . GLU A 311  ? 0.2057 0.1783 0.2032 0.0091  0.0187  0.0213  309  GLU A N   
2149  C CA  . GLU A 311  ? 0.2283 0.2031 0.2249 0.0102  0.0195  0.0224  309  GLU A CA  
2150  C C   . GLU A 311  ? 0.1922 0.1722 0.1901 0.0113  0.0206  0.0249  309  GLU A C   
2151  O O   . GLU A 311  ? 0.1951 0.1769 0.1939 0.0117  0.0208  0.0250  309  GLU A O   
2152  C CB  . GLU A 311  ? 0.2314 0.2052 0.2242 0.0116  0.0195  0.0200  309  GLU A CB  
2153  C CG  . GLU A 311  ? 0.2412 0.2108 0.2326 0.0106  0.0186  0.0180  309  GLU A CG  
2154  C CD  . GLU A 311  ? 0.2851 0.2523 0.2759 0.0098  0.0176  0.0163  309  GLU A CD  
2155  O OE1 . GLU A 311  ? 0.2421 0.2101 0.2341 0.0098  0.0175  0.0168  309  GLU A OE1 
2156  O OE2 . GLU A 311  ? 0.3025 0.2673 0.2918 0.0092  0.0169  0.0147  309  GLU A OE2 
2157  N N   . ALA A 312  ? 0.2000 0.1832 0.1981 0.0118  0.0214  0.0270  310  ALA A N   
2158  C CA  . ALA A 312  ? 0.1810 0.1705 0.1806 0.0126  0.0225  0.0299  310  ALA A CA  
2159  C C   . ALA A 312  ? 0.1964 0.1894 0.1935 0.0149  0.0233  0.0280  310  ALA A C   
2160  O O   . ALA A 312  ? 0.2106 0.2085 0.2094 0.0155  0.0241  0.0296  310  ALA A O   
2161  C CB  . ALA A 312  ? 0.1947 0.1877 0.1948 0.0127  0.0231  0.0329  310  ALA A CB  
2162  N N   . ASP A 313  ? 0.2096 0.2005 0.2034 0.0164  0.0229  0.0245  311  ASP A N   
2163  C CA  . ASP A 313  ? 0.2150 0.2090 0.2071 0.0188  0.0233  0.0220  311  ASP A CA  
2164  C C   . ASP A 313  ? 0.1857 0.1773 0.1792 0.0188  0.0225  0.0205  311  ASP A C   
2165  O O   . ASP A 313  ? 0.2011 0.1944 0.1940 0.0209  0.0225  0.0181  311  ASP A O   
2166  C CB  . ASP A 313  ? 0.2358 0.2288 0.2246 0.0205  0.0229  0.0188  311  ASP A CB  
2167  C CG  . ASP A 313  ? 0.2771 0.2627 0.2649 0.0193  0.0214  0.0165  311  ASP A CG  
2168  O OD1 . ASP A 313  ? 0.2444 0.2261 0.2338 0.0174  0.0208  0.0171  311  ASP A OD1 
2169  O OD2 . ASP A 313  ? 0.2705 0.2549 0.2561 0.0203  0.0209  0.0141  311  ASP A OD2 
2170  N N   . ARG A 314  ? 0.1851 0.1729 0.1806 0.0165  0.0219  0.0218  312  ARG A N   
2171  C CA  . ARG A 314  ? 0.1912 0.1775 0.1882 0.0162  0.0212  0.0211  312  ARG A CA  
2172  C C   . ARG A 314  ? 0.2179 0.2076 0.2183 0.0153  0.0217  0.0240  312  ARG A C   
2173  O O   . ARG A 314  ? 0.1964 0.1859 0.1983 0.0153  0.0213  0.0236  312  ARG A O   
2174  C CB  . ARG A 314  ? 0.2112 0.1915 0.2079 0.0143  0.0197  0.0199  312  ARG A CB  
2175  C CG  . ARG A 314  ? 0.2232 0.2004 0.2173 0.0153  0.0188  0.0170  312  ARG A CG  
2176  C CD  . ARG A 314  ? 0.2300 0.2025 0.2232 0.0133  0.0178  0.0164  312  ARG A CD  
2177  N NE  . ARG A 314  ? 0.2538 0.2236 0.2457 0.0139  0.0166  0.0143  312  ARG A NE  
2178  C CZ  . ARG A 314  ? 0.2397 0.2061 0.2306 0.0124  0.0155  0.0136  312  ARG A CZ  
2179  N NH1 . ARG A 314  ? 0.2603 0.2258 0.2509 0.0106  0.0157  0.0143  312  ARG A NH1 
2180  N NH2 . ARG A 314  ? 0.2650 0.2293 0.2555 0.0128  0.0142  0.0123  312  ARG A NH2 
2181  N N   . LEU A 315  ? 0.1982 0.1911 0.2002 0.0146  0.0226  0.0270  313  LEU A N   
2182  C CA  . LEU A 315  ? 0.2059 0.2017 0.2118 0.0133  0.0229  0.0302  313  LEU A CA  
2183  C C   . LEU A 315  ? 0.2004 0.2016 0.2072 0.0151  0.0237  0.0303  313  LEU A C   
2184  O O   . LEU A 315  ? 0.1995 0.2001 0.2084 0.0145  0.0232  0.0304  313  LEU A O   
2185  C CB  . LEU A 315  ? 0.2057 0.2049 0.2136 0.0124  0.0235  0.0340  313  LEU A CB  
2186  C CG  . LEU A 315  ? 0.1789 0.1785 0.1919 0.0100  0.0230  0.0376  313  LEU A CG  
2187  C CD1 . LEU A 315  ? 0.2009 0.2033 0.2163 0.0091  0.0233  0.0416  313  LEU A CD1 
2188  C CD2 . LEU A 315  ? 0.2080 0.2124 0.2235 0.0103  0.0236  0.0391  313  LEU A CD2 
2189  N N   . GLU A 316  ? 0.1991 0.2061 0.2043 0.0174  0.0249  0.0301  314  GLU A N   
2190  C CA  . GLU A 316  ? 0.2117 0.2251 0.2183 0.0192  0.0258  0.0303  314  GLU A CA  
2191  C C   . GLU A 316  ? 0.1967 0.2071 0.2028 0.0207  0.0249  0.0264  314  GLU A C   
2192  O O   . GLU A 316  ? 0.2036 0.2163 0.2121 0.0211  0.0249  0.0268  314  GLU A O   
2193  C CB  . GLU A 316  ? 0.1933 0.2151 0.1985 0.0215  0.0274  0.0307  314  GLU A CB  
2194  C CG  . GLU A 316  ? 0.1908 0.2166 0.1978 0.0197  0.0283  0.0358  314  GLU A CG  
2195  C CD  . GLU A 316  ? 0.1949 0.2301 0.2003 0.0216  0.0299  0.0370  314  GLU A CD  
2196  O OE1 . GLU A 316  ? 0.2192 0.2610 0.2241 0.0242  0.0308  0.0352  314  GLU A OE1 
2197  O OE2 . GLU A 316  ? 0.2069 0.2434 0.2120 0.0206  0.0301  0.0398  314  GLU A OE2 
2198  N N   . LEU A 317  ? 0.1989 0.2039 0.2024 0.0213  0.0238  0.0231  315  LEU A N   
2199  C CA  . LEU A 317  ? 0.2088 0.2100 0.2126 0.0222  0.0224  0.0201  315  LEU A CA  
2200  C C   . LEU A 317  ? 0.2011 0.1991 0.2073 0.0199  0.0215  0.0218  315  LEU A C   
2201  O O   . LEU A 317  ? 0.2033 0.2021 0.2115 0.0207  0.0209  0.0212  315  LEU A O   
2202  C CB  . LEU A 317  ? 0.2284 0.2238 0.2294 0.0224  0.0211  0.0173  315  LEU A CB  
2203  C CG  . LEU A 317  ? 0.2240 0.2150 0.2260 0.0228  0.0193  0.0149  315  LEU A CG  
2204  C CD1 . LEU A 317  ? 0.2624 0.2573 0.2660 0.0260  0.0192  0.0125  315  LEU A CD1 
2205  C CD2 . LEU A 317  ? 0.2702 0.2558 0.2697 0.0226  0.0181  0.0128  315  LEU A CD2 
2206  N N   . SER A 318  ? 0.1790 0.1736 0.1854 0.0171  0.0211  0.0237  316  SER A N   
2207  C CA  . SER A 318  ? 0.1846 0.1767 0.1933 0.0149  0.0201  0.0247  316  SER A CA  
2208  C C   . SER A 318  ? 0.2034 0.2004 0.2155 0.0149  0.0208  0.0271  316  SER A C   
2209  O O   . SER A 318  ? 0.1982 0.1941 0.2123 0.0140  0.0198  0.0273  316  SER A O   
2210  C CB  . SER A 318  ? 0.1950 0.1833 0.2035 0.0123  0.0196  0.0257  316  SER A CB  
2211  O OG  . SER A 318  ? 0.1981 0.1894 0.2087 0.0114  0.0205  0.0285  316  SER A OG  
2212  N N   . LEU A 319  ? 0.1870 0.1899 0.1999 0.0158  0.0223  0.0290  317  LEU A N   
2213  C CA  . LEU A 319  ? 0.2044 0.2130 0.2210 0.0157  0.0230  0.0315  317  LEU A CA  
2214  C C   . LEU A 319  ? 0.1949 0.2058 0.2121 0.0180  0.0229  0.0296  317  LEU A C   
2215  O O   . LEU A 319  ? 0.1869 0.2003 0.2073 0.0176  0.0228  0.0310  317  LEU A O   
2216  C CB  . LEU A 319  ? 0.1829 0.1985 0.2002 0.0162  0.0248  0.0344  317  LEU A CB  
2217  C CG  . LEU A 319  ? 0.2366 0.2507 0.2547 0.0139  0.0247  0.0373  317  LEU A CG  
2218  C CD1 . LEU A 319  ? 0.2079 0.2300 0.2268 0.0146  0.0264  0.0406  317  LEU A CD1 
2219  C CD2 . LEU A 319  ? 0.1952 0.2061 0.2171 0.0109  0.0235  0.0393  317  LEU A CD2 
2220  N N   . ASP A 320  ? 0.1921 0.2024 0.2070 0.0206  0.0228  0.0262  318  ASP A N   
2221  C CA  . ASP A 320  ? 0.2172 0.2292 0.2335 0.0229  0.0223  0.0240  318  ASP A CA  
2222  C C   . ASP A 320  ? 0.2265 0.2328 0.2441 0.0214  0.0203  0.0237  318  ASP A C   
2223  O O   . ASP A 320  ? 0.2268 0.2351 0.2473 0.0221  0.0199  0.0238  318  ASP A O   
2224  C CB  . ASP A 320  ? 0.2200 0.2326 0.2342 0.0261  0.0222  0.0201  318  ASP A CB  
2225  C CG  . ASP A 320  ? 0.2521 0.2731 0.2656 0.0282  0.0242  0.0202  318  ASP A CG  
2226  O OD1 . ASP A 320  ? 0.2585 0.2865 0.2744 0.0292  0.0253  0.0215  318  ASP A OD1 
2227  O OD2 . ASP A 320  ? 0.2917 0.3130 0.3022 0.0288  0.0247  0.0193  318  ASP A OD2 
2228  N N   . LEU A 321  ? 0.1905 0.1904 0.2063 0.0193  0.0191  0.0234  319  LEU A N   
2229  C CA  . LEU A 321  ? 0.1916 0.1873 0.2086 0.0176  0.0174  0.0237  319  LEU A CA  
2230  C C   . LEU A 321  ? 0.2040 0.2018 0.2237 0.0155  0.0175  0.0264  319  LEU A C   
2231  O O   . LEU A 321  ? 0.2074 0.2055 0.2294 0.0153  0.0166  0.0269  319  LEU A O   
2232  C CB  . LEU A 321  ? 0.2025 0.1922 0.2168 0.0158  0.0162  0.0229  319  LEU A CB  
2233  C CG  . LEU A 321  ? 0.2692 0.2560 0.2818 0.0176  0.0153  0.0202  319  LEU A CG  
2234  C CD1 . LEU A 321  ? 0.3091 0.2967 0.3191 0.0188  0.0165  0.0190  319  LEU A CD1 
2235  C CD2 . LEU A 321  ? 0.3287 0.3103 0.3402 0.0155  0.0135  0.0202  319  LEU A CD2 
2236  N N   . LEU A 322  ? 0.1907 0.1898 0.2106 0.0139  0.0185  0.0284  320  LEU A N   
2237  C CA  . LEU A 322  ? 0.2106 0.2114 0.2338 0.0118  0.0184  0.0310  320  LEU A CA  
2238  C C   . LEU A 322  ? 0.2029 0.2096 0.2293 0.0132  0.0191  0.0322  320  LEU A C   
2239  O O   . LEU A 322  ? 0.2207 0.2281 0.2500 0.0121  0.0182  0.0332  320  LEU A O   
2240  C CB  . LEU A 322  ? 0.1851 0.1866 0.2090 0.0101  0.0191  0.0330  320  LEU A CB  
2241  C CG  . LEU A 322  ? 0.1980 0.2008 0.2263 0.0077  0.0186  0.0357  320  LEU A CG  
2242  C CD1 . LEU A 322  ? 0.2013 0.1992 0.2297 0.0056  0.0166  0.0343  320  LEU A CD1 
2243  C CD2 . LEU A 322  ? 0.1732 0.1777 0.2033 0.0066  0.0193  0.0383  320  LEU A CD2 
2244  N N   . GLU A 323  ? 0.1919 0.2036 0.2179 0.0157  0.0206  0.0319  321  GLU A N   
2245  C CA  . GLU A 323  ? 0.2356 0.2541 0.2646 0.0174  0.0215  0.0329  321  GLU A CA  
2246  C C   . GLU A 323  ? 0.2287 0.2457 0.2590 0.0185  0.0201  0.0311  321  GLU A C   
2247  O O   . GLU A 323  ? 0.1965 0.2159 0.2302 0.0178  0.0198  0.0326  321  GLU A O   
2248  C CB  . GLU A 323  ? 0.2207 0.2453 0.2484 0.0203  0.0233  0.0321  321  GLU A CB  
2249  C CG  . GLU A 323  ? 0.2757 0.3081 0.3061 0.0229  0.0242  0.0318  321  GLU A CG  
2250  C CD  . GLU A 323  ? 0.3022 0.3432 0.3349 0.0224  0.0261  0.0357  321  GLU A CD  
2251  O OE1 . GLU A 323  ? 0.3212 0.3622 0.3534 0.0203  0.0267  0.0385  321  GLU A OE1 
2252  O OE2 . GLU A 323  ? 0.3200 0.3681 0.3555 0.0240  0.0269  0.0362  321  GLU A OE2 
2253  N N   . VAL A 324  ? 0.2191 0.2322 0.2474 0.0201  0.0191  0.0280  322  VAL A N   
2254  C CA  . VAL A 324  ? 0.2175 0.2292 0.2477 0.0213  0.0175  0.0265  322  VAL A CA  
2255  C C   . VAL A 324  ? 0.2117 0.2200 0.2432 0.0184  0.0159  0.0283  322  VAL A C   
2256  O O   . VAL A 324  ? 0.2152 0.2253 0.2498 0.0186  0.0151  0.0290  322  VAL A O   
2257  C CB  . VAL A 324  ? 0.2431 0.2506 0.2715 0.0233  0.0163  0.0232  322  VAL A CB  
2258  C CG1 . VAL A 324  ? 0.2367 0.2427 0.2682 0.0244  0.0142  0.0223  322  VAL A CG1 
2259  C CG2 . VAL A 324  ? 0.2476 0.2594 0.2751 0.0265  0.0177  0.0209  322  VAL A CG2 
2260  N N   . LEU A 325  ? 0.1830 0.1867 0.2122 0.0157  0.0153  0.0288  323  LEU A N   
2261  C CA  . LEU A 325  ? 0.1923 0.1935 0.2225 0.0131  0.0137  0.0299  323  LEU A CA  
2262  C C   . LEU A 325  ? 0.1992 0.2045 0.2330 0.0118  0.0141  0.0323  323  LEU A C   
2263  O O   . LEU A 325  ? 0.1797 0.1855 0.2158 0.0110  0.0128  0.0330  323  LEU A O   
2264  C CB  . LEU A 325  ? 0.2012 0.1978 0.2283 0.0108  0.0132  0.0296  323  LEU A CB  
2265  C CG  . LEU A 325  ? 0.2146 0.2071 0.2386 0.0116  0.0125  0.0276  323  LEU A CG  
2266  C CD1 . LEU A 325  ? 0.1960 0.1854 0.2171 0.0098  0.0127  0.0272  323  LEU A CD1 
2267  C CD2 . LEU A 325  ? 0.2278 0.2184 0.2526 0.0111  0.0104  0.0276  323  LEU A CD2 
2268  N N   . CYS A 326  ? 0.2078 0.2162 0.2423 0.0114  0.0157  0.0338  324  CYS A N   
2269  C CA  . CYS A 326  ? 0.1665 0.1788 0.2051 0.0098  0.0159  0.0364  324  CYS A CA  
2270  C C   . CYS A 326  ? 0.2006 0.2185 0.2424 0.0117  0.0164  0.0371  324  CYS A C   
2271  O O   . CYS A 326  ? 0.1971 0.2177 0.2425 0.0104  0.0160  0.0391  324  CYS A O   
2272  C CB  . CYS A 326  ? 0.1967 0.2111 0.2361 0.0087  0.0172  0.0385  324  CYS A CB  
2273  S SG  . CYS A 326  ? 0.2111 0.2192 0.2486 0.0060  0.0161  0.0378  324  CYS A SG  
2274  N N   . LEU A 327  ? 0.2019 0.2217 0.2426 0.0149  0.0171  0.0353  325  LEU A N   
2275  C CA  . LEU A 327  ? 0.1919 0.2173 0.2357 0.0173  0.0175  0.0353  325  LEU A CA  
2276  C C   . LEU A 327  ? 0.1928 0.2152 0.2376 0.0182  0.0155  0.0337  325  LEU A C   
2277  O O   . LEU A 327  ? 0.2089 0.2354 0.2569 0.0200  0.0154  0.0336  325  LEU A O   
2278  C CB  . LEU A 327  ? 0.1996 0.2296 0.2423 0.0207  0.0193  0.0337  325  LEU A CB  
2279  C CG  . LEU A 327  ? 0.2715 0.3067 0.3139 0.0201  0.0215  0.0360  325  LEU A CG  
2280  C CD1 . LEU A 327  ? 0.2920 0.3333 0.3332 0.0237  0.0232  0.0341  325  LEU A CD1 
2281  C CD2 . LEU A 327  ? 0.2313 0.2716 0.2779 0.0181  0.0219  0.0398  325  LEU A CD2 
2282  N N   . ASP A 328  ? 0.2053 0.2212 0.2477 0.0169  0.0138  0.0327  326  ASP A N   
2283  C CA  . ASP A 328  ? 0.1803 0.1933 0.2237 0.0175  0.0116  0.0318  326  ASP A CA  
2284  C C   . ASP A 328  ? 0.1995 0.2136 0.2457 0.0154  0.0103  0.0339  326  ASP A C   
2285  O O   . ASP A 328  ? 0.1911 0.2031 0.2361 0.0124  0.0097  0.0349  326  ASP A O   
2286  C CB  . ASP A 328  ? 0.2099 0.2165 0.2497 0.0166  0.0104  0.0305  326  ASP A CB  
2287  C CG  . ASP A 328  ? 0.2124 0.2163 0.2536 0.0175  0.0080  0.0299  326  ASP A CG  
2288  O OD1 . ASP A 328  ? 0.2144 0.2200 0.2588 0.0172  0.0068  0.0312  326  ASP A OD1 
2289  O OD2 . ASP A 328  ? 0.2824 0.2824 0.3219 0.0184  0.0072  0.0283  326  ASP A OD2 
2290  N N   . GLY A 329  ? 0.1952 0.2129 0.2452 0.0170  0.0098  0.0342  327  GLY A N   
2291  C CA  . GLY A 329  ? 0.2036 0.2230 0.2566 0.0151  0.0086  0.0362  327  GLY A CA  
2292  C C   . GLY A 329  ? 0.2221 0.2371 0.2737 0.0128  0.0063  0.0367  327  GLY A C   
2293  O O   . GLY A 329  ? 0.2065 0.2226 0.2594 0.0104  0.0053  0.0382  327  GLY A O   
2294  N N   . ASP A 330  ? 0.1844 0.1949 0.2336 0.0134  0.0052  0.0354  328  ASP A N   
2295  C CA  . ASP A 330  ? 0.2034 0.2107 0.2511 0.0111  0.0030  0.0362  328  ASP A CA  
2296  C C   . ASP A 330  ? 0.2092 0.2155 0.2540 0.0079  0.0033  0.0364  328  ASP A C   
2297  O O   . ASP A 330  ? 0.2142 0.2200 0.2583 0.0057  0.0016  0.0372  328  ASP A O   
2298  C CB  . ASP A 330  ? 0.2034 0.2063 0.2493 0.0120  0.0018  0.0353  328  ASP A CB  
2299  C CG  . ASP A 330  ? 0.2499 0.2529 0.2996 0.0149  0.0004  0.0350  328  ASP A CG  
2300  O OD1 . ASP A 330  ? 0.2662 0.2725 0.3198 0.0156  -0.0002 0.0360  328  ASP A OD1 
2301  O OD2 . ASP A 330  ? 0.2386 0.2384 0.2879 0.0164  -0.0002 0.0336  328  ASP A OD2 
2302  N N   . LEU A 331  ? 0.1858 0.1921 0.2292 0.0078  0.0052  0.0357  329  LEU A N   
2303  C CA  . LEU A 331  ? 0.1955 0.2007 0.2370 0.0051  0.0054  0.0356  329  LEU A CA  
2304  C C   . LEU A 331  ? 0.2145 0.2232 0.2593 0.0037  0.0057  0.0368  329  LEU A C   
2305  O O   . LEU A 331  ? 0.2048 0.2126 0.2492 0.0015  0.0056  0.0364  329  LEU A O   
2306  C CB  . LEU A 331  ? 0.1813 0.1838 0.2195 0.0055  0.0069  0.0343  329  LEU A CB  
2307  C CG  . LEU A 331  ? 0.2044 0.2029 0.2391 0.0061  0.0062  0.0330  329  LEU A CG  
2308  C CD1 . LEU A 331  ? 0.1872 0.1836 0.2191 0.0072  0.0078  0.0317  329  LEU A CD1 
2309  C CD2 . LEU A 331  ? 0.2193 0.2162 0.2519 0.0036  0.0046  0.0329  329  LEU A CD2 
2310  N N   . SER A 332  ? 0.2159 0.2285 0.2645 0.0048  0.0060  0.0381  330  SER A N   
2311  C CA  . SER A 332  ? 0.2324 0.2486 0.2847 0.0034  0.0063  0.0396  330  SER A CA  
2312  C C   . SER A 332  ? 0.2111 0.2270 0.2643 0.0006  0.0042  0.0396  330  SER A C   
2313  O O   . SER A 332  ? 0.2257 0.2404 0.2774 0.0001  0.0025  0.0390  330  SER A O   
2314  C CB  . SER A 332  ? 0.2241 0.2453 0.2803 0.0053  0.0070  0.0410  330  SER A CB  
2315  O OG  . SER A 332  ? 0.2357 0.2577 0.2936 0.0055  0.0052  0.0413  330  SER A OG  
2316  N N   . GLY A 333  ? 0.1736 0.1911 0.2297 -0.0013 0.0042  0.0403  331  GLY A N   
2317  C CA  . GLY A 333  ? 0.2137 0.2313 0.2712 -0.0039 0.0021  0.0397  331  GLY A CA  
2318  C C   . GLY A 333  ? 0.2132 0.2273 0.2680 -0.0056 0.0015  0.0375  331  GLY A C   
2319  O O   . GLY A 333  ? 0.2417 0.2562 0.2980 -0.0077 -0.0003 0.0363  331  GLY A O   
2320  N N   . TRP A 334  ? 0.1889 0.1999 0.2401 -0.0046 0.0028  0.0366  332  TRP A N   
2321  C CA  . TRP A 334  ? 0.2048 0.2125 0.2531 -0.0058 0.0023  0.0343  332  TRP A CA  
2322  C C   . TRP A 334  ? 0.2002 0.2064 0.2493 -0.0056 0.0038  0.0347  332  TRP A C   
2323  O O   . TRP A 334  ? 0.2123 0.2186 0.2604 -0.0038 0.0057  0.0359  332  TRP A O   
2324  C CB  . TRP A 334  ? 0.2204 0.2259 0.2635 -0.0049 0.0022  0.0331  332  TRP A CB  
2325  C CG  . TRP A 334  ? 0.1963 0.1986 0.2359 -0.0055 0.0022  0.0310  332  TRP A CG  
2326  C CD1 . TRP A 334  ? 0.1914 0.1936 0.2303 -0.0073 0.0008  0.0287  332  TRP A CD1 
2327  C CD2 . TRP A 334  ? 0.2069 0.2063 0.2430 -0.0041 0.0037  0.0306  332  TRP A CD2 
2328  N NE1 . TRP A 334  ? 0.1989 0.1983 0.2342 -0.0071 0.0014  0.0271  332  TRP A NE1 
2329  C CE2 . TRP A 334  ? 0.1958 0.1933 0.2294 -0.0052 0.0031  0.0283  332  TRP A CE2 
2330  C CE3 . TRP A 334  ? 0.2097 0.2083 0.2449 -0.0019 0.0053  0.0316  332  TRP A CE3 
2331  C CZ2 . TRP A 334  ? 0.1944 0.1889 0.2245 -0.0044 0.0042  0.0275  332  TRP A CZ2 
2332  C CZ3 . TRP A 334  ? 0.2127 0.2083 0.2443 -0.0011 0.0063  0.0306  332  TRP A CZ3 
2333  C CH2 . TRP A 334  ? 0.2020 0.1955 0.2312 -0.0024 0.0057  0.0287  332  TRP A CH2 
2334  N N   . ASN A 335  ? 0.1939 0.1988 0.2450 -0.0075 0.0029  0.0335  333  ASN A N   
2335  C CA  . ASN A 335  ? 0.1889 0.1923 0.2415 -0.0077 0.0039  0.0342  333  ASN A CA  
2336  C C   . ASN A 335  ? 0.1990 0.1986 0.2479 -0.0077 0.0039  0.0317  333  ASN A C   
2337  O O   . ASN A 335  ? 0.1928 0.1906 0.2435 -0.0083 0.0041  0.0318  333  ASN A O   
2338  C CB  . ASN A 335  ? 0.2129 0.2176 0.2720 -0.0097 0.0027  0.0352  333  ASN A CB  
2339  C CG  . ASN A 335  ? 0.2321 0.2410 0.2956 -0.0094 0.0036  0.0390  333  ASN A CG  
2340  O OD1 . ASN A 335  ? 0.2167 0.2275 0.2784 -0.0075 0.0056  0.0408  333  ASN A OD1 
2341  N ND2 . ASN A 335  ? 0.2486 0.2592 0.3181 -0.0114 0.0020  0.0399  333  ASN A ND2 
2342  N N   . GLY A 336  ? 0.1907 0.1891 0.2348 -0.0072 0.0035  0.0296  334  GLY A N   
2343  C CA  . GLY A 336  ? 0.1803 0.1757 0.2208 -0.0074 0.0034  0.0271  334  GLY A CA  
2344  C C   . GLY A 336  ? 0.1844 0.1774 0.2215 -0.0058 0.0053  0.0276  334  GLY A C   
2345  O O   . GLY A 336  ? 0.1890 0.1797 0.2238 -0.0060 0.0052  0.0256  334  GLY A O   
2346  N N   . MET A 337  ? 0.1963 0.1904 0.2333 -0.0042 0.0069  0.0299  335  MET A N   
2347  C CA  A MET A 337  ? 0.1914 0.1836 0.2251 -0.0026 0.0086  0.0300  335  MET A CA  
2348  C CA  B MET A 337  ? 0.1913 0.1836 0.2251 -0.0026 0.0086  0.0300  335  MET A CA  
2349  C C   . MET A 337  ? 0.1861 0.1772 0.2216 -0.0032 0.0091  0.0303  335  MET A C   
2350  O O   . MET A 337  ? 0.1908 0.1838 0.2308 -0.0039 0.0092  0.0324  335  MET A O   
2351  C CB  A MET A 337  ? 0.1908 0.1854 0.2246 -0.0004 0.0101  0.0318  335  MET A CB  
2352  C CB  B MET A 337  ? 0.1908 0.1853 0.2244 -0.0004 0.0100  0.0318  335  MET A CB  
2353  C CG  A MET A 337  ? 0.2048 0.1980 0.2351 0.0014  0.0116  0.0315  335  MET A CG  
2354  C CG  B MET A 337  ? 0.2052 0.1987 0.2361 0.0013  0.0117  0.0317  335  MET A CG  
2355  S SD  A MET A 337  ? 0.2637 0.2534 0.2891 0.0020  0.0108  0.0291  335  MET A SD  
2356  S SD  B MET A 337  ? 0.2486 0.2422 0.2766 0.0039  0.0122  0.0310  335  MET A SD  
2357  C CE  A MET A 337  ? 0.2196 0.2112 0.2458 0.0037  0.0104  0.0297  335  MET A CE  
2358  C CE  B MET A 337  ? 0.1816 0.1719 0.2069 0.0026  0.0102  0.0292  335  MET A CE  
2359  N N   . GLY A 338  ? 0.1896 0.1777 0.2218 -0.0030 0.0094  0.0286  336  GLY A N   
2360  C CA  . GLY A 338  ? 0.2154 0.2021 0.2494 -0.0035 0.0096  0.0289  336  GLY A CA  
2361  C C   . GLY A 338  ? 0.1996 0.1851 0.2299 -0.0019 0.0112  0.0292  336  GLY A C   
2362  O O   . GLY A 338  ? 0.1971 0.1821 0.2233 -0.0005 0.0119  0.0283  336  GLY A O   
2363  N N   . PHE A 339  ? 0.1832 0.1684 0.2155 -0.0021 0.0117  0.0306  337  PHE A N   
2364  C CA  . PHE A 339  ? 0.1931 0.1782 0.2226 -0.0006 0.0134  0.0313  337  PHE A CA  
2365  C C   . PHE A 339  ? 0.2177 0.2012 0.2494 -0.0015 0.0130  0.0320  337  PHE A C   
2366  O O   . PHE A 339  ? 0.2095 0.1940 0.2465 -0.0028 0.0123  0.0341  337  PHE A O   
2367  C CB  . PHE A 339  ? 0.1899 0.1795 0.2202 0.0008  0.0150  0.0342  337  PHE A CB  
2368  C CG  . PHE A 339  ? 0.1890 0.1795 0.2154 0.0029  0.0166  0.0342  337  PHE A CG  
2369  C CD1 . PHE A 339  ? 0.1938 0.1835 0.2161 0.0046  0.0170  0.0320  337  PHE A CD1 
2370  C CD2 . PHE A 339  ? 0.1959 0.1887 0.2235 0.0031  0.0176  0.0366  337  PHE A CD2 
2371  C CE1 . PHE A 339  ? 0.2041 0.1948 0.2233 0.0067  0.0182  0.0315  337  PHE A CE1 
2372  C CE2 . PHE A 339  ? 0.2116 0.2059 0.2354 0.0052  0.0191  0.0364  337  PHE A CE2 
2373  C CZ  . PHE A 339  ? 0.2097 0.2029 0.2294 0.0070  0.0194  0.0335  337  PHE A CZ  
2374  N N   . VAL A 340  ? 0.1948 0.1759 0.2229 -0.0007 0.0135  0.0304  338  VAL A N   
2375  C CA  . VAL A 340  ? 0.1838 0.1632 0.2138 -0.0013 0.0131  0.0310  338  VAL A CA  
2376  C C   . VAL A 340  ? 0.1751 0.1574 0.2052 -0.0003 0.0147  0.0344  338  VAL A C   
2377  O O   . VAL A 340  ? 0.2167 0.2010 0.2428 0.0015  0.0163  0.0344  338  VAL A O   
2378  C CB  . VAL A 340  ? 0.1983 0.1742 0.2245 -0.0011 0.0127  0.0275  338  VAL A CB  
2379  C CG1 . VAL A 340  ? 0.1934 0.1676 0.2218 -0.0014 0.0124  0.0281  338  VAL A CG1 
2380  C CG2 . VAL A 340  ? 0.2208 0.1952 0.2470 -0.0021 0.0112  0.0243  338  VAL A CG2 
2381  N N   . VAL A 341  ? 0.1737 0.1566 0.2087 -0.0014 0.0142  0.0372  339  VAL A N   
2382  C CA  . VAL A 341  ? 0.1688 0.1545 0.2037 -0.0007 0.0155  0.0406  339  VAL A CA  
2383  C C   . VAL A 341  ? 0.1866 0.1690 0.2237 -0.0015 0.0143  0.0405  339  VAL A C   
2384  O O   . VAL A 341  ? 0.1980 0.1772 0.2396 -0.0030 0.0123  0.0395  339  VAL A O   
2385  C CB  . VAL A 341  ? 0.2190 0.2103 0.2584 -0.0012 0.0161  0.0455  339  VAL A CB  
2386  C CG1 . VAL A 341  ? 0.2262 0.2209 0.2637 -0.0002 0.0172  0.0451  339  VAL A CG1 
2387  C CG2 . VAL A 341  ? 0.2636 0.2538 0.3108 -0.0036 0.0140  0.0476  339  VAL A CG2 
2388  N N   . GLN A 342  ? 0.1850 0.1683 0.2190 -0.0003 0.0155  0.0414  340  GLN A N   
2389  C CA  . GLN A 342  ? 0.2086 0.1887 0.2434 -0.0006 0.0145  0.0409  340  GLN A CA  
2390  C C   . GLN A 342  ? 0.1919 0.1750 0.2317 -0.0014 0.0144  0.0463  340  GLN A C   
2391  O O   . GLN A 342  ? 0.2204 0.2085 0.2579 -0.0003 0.0161  0.0492  340  GLN A O   
2392  C CB  . GLN A 342  ? 0.1786 0.1575 0.2066 0.0011  0.0157  0.0381  340  GLN A CB  
2393  C CG  . GLN A 342  ? 0.1793 0.1555 0.2029 0.0016  0.0156  0.0334  340  GLN A CG  
2394  C CD  . GLN A 342  ? 0.1896 0.1667 0.2068 0.0036  0.0171  0.0319  340  GLN A CD  
2395  O OE1 . GLN A 342  ? 0.2113 0.1924 0.2270 0.0048  0.0185  0.0337  340  GLN A OE1 
2396  N NE2 . GLN A 342  ? 0.1937 0.1673 0.2075 0.0038  0.0167  0.0284  340  GLN A NE2 
2397  N N   . ALA A 343  ? 0.1683 0.1489 0.2151 -0.0031 0.0122  0.0475  341  ALA A N   
2398  C CA  . ALA A 343  ? 0.1855 0.1688 0.2384 -0.0043 0.0116  0.0534  341  ALA A CA  
2399  C C   . ALA A 343  ? 0.2412 0.2253 0.2919 -0.0034 0.0122  0.0550  341  ALA A C   
2400  O O   . ALA A 343  ? 0.2231 0.2114 0.2775 -0.0040 0.0123  0.0607  341  ALA A O   
2401  C CB  . ALA A 343  ? 0.2366 0.2162 0.2984 -0.0064 0.0086  0.0538  341  ALA A CB  
2402  N N   . TYR A 344  ? 0.2008 0.1814 0.2461 -0.0020 0.0126  0.0505  342  TYR A N   
2403  C CA  . TYR A 344  ? 0.2078 0.1899 0.2508 -0.0011 0.0133  0.0522  342  TYR A CA  
2404  C C   . TYR A 344  ? 0.2176 0.2061 0.2548 0.0005  0.0159  0.0541  342  TYR A C   
2405  O O   . TYR A 344  ? 0.2156 0.2067 0.2507 0.0014  0.0165  0.0559  342  TYR A O   
2406  C CB  . TYR A 344  ? 0.2089 0.1857 0.2485 -0.0003 0.0127  0.0471  342  TYR A CB  
2407  C CG  . TYR A 344  ? 0.2040 0.1795 0.2355 0.0013  0.0141  0.0420  342  TYR A CG  
2408  C CD1 . TYR A 344  ? 0.2089 0.1870 0.2364 0.0021  0.0156  0.0412  342  TYR A CD1 
2409  C CD2 . TYR A 344  ? 0.2032 0.1748 0.2318 0.0019  0.0137  0.0381  342  TYR A CD2 
2410  C CE1 . TYR A 344  ? 0.1920 0.1685 0.2133 0.0033  0.0165  0.0368  342  TYR A CE1 
2411  C CE2 . TYR A 344  ? 0.2320 0.2025 0.2543 0.0030  0.0147  0.0339  342  TYR A CE2 
2412  C CZ  . TYR A 344  ? 0.2134 0.1861 0.2321 0.0037  0.0159  0.0334  342  TYR A CZ  
2413  O OH  . TYR A 344  ? 0.2129 0.1842 0.2261 0.0046  0.0165  0.0297  342  TYR A OH  
2414  N N   . GLY A 345  ? 0.2240 0.2155 0.2590 0.0011  0.0171  0.0535  343  GLY A N   
2415  C CA  . GLY A 345  ? 0.2213 0.2193 0.2512 0.0029  0.0194  0.0543  343  GLY A CA  
2416  C C   . GLY A 345  ? 0.2071 0.2130 0.2407 0.0023  0.0201  0.0606  343  GLY A C   
2417  O O   . GLY A 345  ? 0.2207 0.2273 0.2602 0.0006  0.0193  0.0636  343  GLY A O   
2418  N N   . LYS A 346  ? 0.1950 0.2074 0.2253 0.0038  0.0217  0.0627  344  LYS A N   
2419  C CA  . LYS A 346  ? 0.2186 0.2403 0.2520 0.0034  0.0226  0.0691  344  LYS A CA  
2420  C C   . LYS A 346  ? 0.2395 0.2663 0.2730 0.0038  0.0238  0.0695  344  LYS A C   
2421  O O   . LYS A 346  ? 0.2229 0.2569 0.2607 0.0027  0.0242  0.0752  344  LYS A O   
2422  C CB  . LYS A 346  ? 0.2199 0.2483 0.2487 0.0052  0.0241  0.0704  344  LYS A CB  
2423  C CG  . LYS A 346  ? 0.2154 0.2396 0.2444 0.0047  0.0229  0.0708  344  LYS A CG  
2424  C CD  . LYS A 346  ? 0.2307 0.2617 0.2545 0.0067  0.0243  0.0714  344  LYS A CD  
2425  C CE  . LYS A 346  ? 0.2230 0.2514 0.2487 0.0058  0.0229  0.0736  344  LYS A CE  
2426  N NZ  . LYS A 346  ? 0.2505 0.2855 0.2707 0.0078  0.0242  0.0737  344  LYS A NZ  
2427  N N   . ARG A 347  ? 0.1994 0.2232 0.2287 0.0053  0.0244  0.0639  345  ARG A N   
2428  C CA  . ARG A 347  ? 0.1966 0.2250 0.2263 0.0058  0.0254  0.0640  345  ARG A CA  
2429  C C   . ARG A 347  ? 0.2139 0.2379 0.2491 0.0036  0.0239  0.0645  345  ARG A C   
2430  O O   . ARG A 347  ? 0.2225 0.2506 0.2591 0.0037  0.0246  0.0653  345  ARG A O   
2431  C CB  . ARG A 347  ? 0.2063 0.2341 0.2296 0.0086  0.0265  0.0579  345  ARG A CB  
2432  C CG  . ARG A 347  ? 0.2043 0.2385 0.2225 0.0112  0.0281  0.0571  345  ARG A CG  
2433  C CD  . ARG A 347  ? 0.1881 0.2190 0.2006 0.0138  0.0284  0.0505  345  ARG A CD  
2434  N NE  . ARG A 347  ? 0.2162 0.2376 0.2268 0.0131  0.0271  0.0472  345  ARG A NE  
2435  C CZ  . ARG A 347  ? 0.1950 0.2116 0.2018 0.0145  0.0267  0.0419  345  ARG A CZ  
2436  N NH1 . ARG A 347  ? 0.1936 0.2131 0.1982 0.0168  0.0274  0.0390  345  ARG A NH1 
2437  N NH2 . ARG A 347  ? 0.1889 0.1976 0.1944 0.0136  0.0255  0.0395  345  ARG A NH2 
2438  N N   . CYS A 348  ? 0.1962 0.2125 0.2349 0.0016  0.0218  0.0639  346  CYS A N   
2439  C CA  . CYS A 348  ? 0.2098 0.2211 0.2529 -0.0001 0.0201  0.0628  346  CYS A CA  
2440  C C   . CYS A 348  ? 0.2058 0.2227 0.2547 -0.0016 0.0201  0.0674  346  CYS A C   
2441  O O   . CYS A 348  ? 0.1911 0.2076 0.2399 -0.0015 0.0201  0.0654  346  CYS A O   
2442  C CB  . CYS A 348  ? 0.2287 0.2326 0.2759 -0.0020 0.0176  0.0621  346  CYS A CB  
2443  S SG  . CYS A 348  ? 0.2457 0.2428 0.2962 -0.0035 0.0155  0.0581  346  CYS A SG  
2444  N N   . PRO A 349  ? 0.2081 0.2304 0.2624 -0.0030 0.0199  0.0739  347  PRO A N   
2445  C CA  . PRO A 349  ? 0.1996 0.2273 0.2598 -0.0046 0.0197  0.0785  347  PRO A CA  
2446  C C   . PRO A 349  ? 0.1980 0.2333 0.2542 -0.0025 0.0222  0.0779  347  PRO A C   
2447  O O   . PRO A 349  ? 0.2101 0.2472 0.2694 -0.0033 0.0221  0.0787  347  PRO A O   
2448  C CB  . PRO A 349  ? 0.2177 0.2504 0.2840 -0.0065 0.0191  0.0860  347  PRO A CB  
2449  C CG  . PRO A 349  ? 0.2298 0.2630 0.2912 -0.0049 0.0200  0.0856  347  PRO A CG  
2450  C CD  . PRO A 349  ? 0.2252 0.2494 0.2808 -0.0035 0.0197  0.0779  347  PRO A CD  
2451  N N   . PHE A 350  ? 0.2206 0.2604 0.2702 0.0001  0.0243  0.0764  348  PHE A N   
2452  C CA  . PHE A 350  ? 0.2303 0.2776 0.2763 0.0025  0.0265  0.0751  348  PHE A CA  
2453  C C   . PHE A 350  ? 0.1958 0.2371 0.2382 0.0039  0.0263  0.0686  348  PHE A C   
2454  O O   . PHE A 350  ? 0.2108 0.2561 0.2533 0.0049  0.0272  0.0679  348  PHE A O   
2455  C CB  . PHE A 350  ? 0.1868 0.2410 0.2273 0.0051  0.0285  0.0750  348  PHE A CB  
2456  C CG  . PHE A 350  ? 0.2486 0.3085 0.2923 0.0036  0.0285  0.0815  348  PHE A CG  
2457  C CD1 . PHE A 350  ? 0.2311 0.3017 0.2790 0.0027  0.0295  0.0880  348  PHE A CD1 
2458  C CD2 . PHE A 350  ? 0.2456 0.3002 0.2884 0.0030  0.0275  0.0815  348  PHE A CD2 
2459  C CE1 . PHE A 350  ? 0.2819 0.3582 0.3333 0.0011  0.0293  0.0948  348  PHE A CE1 
2460  C CE2 . PHE A 350  ? 0.2269 0.2866 0.2732 0.0015  0.0272  0.0880  348  PHE A CE2 
2461  C CZ  . PHE A 350  ? 0.2903 0.3609 0.3410 0.0005  0.0280  0.0949  348  PHE A CZ  
2462  N N   . VAL A 351  ? 0.1948 0.2267 0.2344 0.0039  0.0251  0.0641  349  VAL A N   
2463  C CA  . VAL A 351  ? 0.1906 0.2165 0.2277 0.0046  0.0245  0.0587  349  VAL A CA  
2464  C C   . VAL A 351  ? 0.2050 0.2292 0.2477 0.0024  0.0231  0.0600  349  VAL A C   
2465  O O   . VAL A 351  ? 0.2057 0.2304 0.2478 0.0031  0.0232  0.0580  349  VAL A O   
2466  C CB  . VAL A 351  ? 0.1860 0.2031 0.2194 0.0047  0.0234  0.0544  349  VAL A CB  
2467  C CG1 . VAL A 351  ? 0.1905 0.2021 0.2220 0.0050  0.0225  0.0496  349  VAL A CG1 
2468  C CG2 . VAL A 351  ? 0.2165 0.2354 0.2444 0.0070  0.0247  0.0527  349  VAL A CG2 
2469  N N   . LEU A 352  ? 0.2071 0.2293 0.2557 -0.0003 0.0214  0.0635  350  LEU A N   
2470  C CA  . LEU A 352  ? 0.1771 0.1979 0.2317 -0.0025 0.0198  0.0646  350  LEU A CA  
2471  C C   . LEU A 352  ? 0.1982 0.2276 0.2556 -0.0024 0.0211  0.0684  350  LEU A C   
2472  O O   . LEU A 352  ? 0.2070 0.2362 0.2663 -0.0028 0.0205  0.0673  350  LEU A O   
2473  C CB  . LEU A 352  ? 0.2173 0.2345 0.2786 -0.0053 0.0175  0.0675  350  LEU A CB  
2474  C CG  . LEU A 352  ? 0.2166 0.2249 0.2761 -0.0056 0.0159  0.0628  350  LEU A CG  
2475  C CD1 . LEU A 352  ? 0.2372 0.2424 0.3037 -0.0079 0.0136  0.0656  350  LEU A CD1 
2476  C CD2 . LEU A 352  ? 0.2296 0.2331 0.2880 -0.0057 0.0148  0.0578  350  LEU A CD2 
2477  N N   . ASP A 353  ? 0.2205 0.2583 0.2783 -0.0018 0.0228  0.0729  351  ASP A N   
2478  C CA  . ASP A 353  ? 0.2006 0.2480 0.2606 -0.0014 0.0242  0.0763  351  ASP A CA  
2479  C C   . ASP A 353  ? 0.1975 0.2458 0.2525 0.0014  0.0255  0.0713  351  ASP A C   
2480  O O   . ASP A 353  ? 0.2003 0.2519 0.2580 0.0013  0.0256  0.0720  351  ASP A O   
2481  C CB  . ASP A 353  ? 0.2258 0.2833 0.2857 -0.0007 0.0261  0.0813  351  ASP A CB  
2482  C CG  . ASP A 353  ? 0.2297 0.2881 0.2963 -0.0038 0.0247  0.0878  351  ASP A CG  
2483  O OD1 . ASP A 353  ? 0.2708 0.3242 0.3439 -0.0066 0.0224  0.0894  351  ASP A OD1 
2484  O OD2 . ASP A 353  ? 0.2547 0.3193 0.3205 -0.0034 0.0259  0.0915  351  ASP A OD2 
2485  N N   . PHE A 354  ? 0.1939 0.2394 0.2422 0.0040  0.0263  0.0665  352  PHE A N   
2486  C CA  . PHE A 354  ? 0.1838 0.2294 0.2280 0.0067  0.0270  0.0617  352  PHE A CA  
2487  C C   . PHE A 354  ? 0.1892 0.2277 0.2348 0.0055  0.0252  0.0590  352  PHE A C   
2488  O O   . PHE A 354  ? 0.2130 0.2541 0.2594 0.0064  0.0254  0.0580  352  PHE A O   
2489  C CB  . PHE A 354  ? 0.1962 0.2392 0.2337 0.0093  0.0277  0.0572  352  PHE A CB  
2490  C CG  . PHE A 354  ? 0.2289 0.2695 0.2629 0.0117  0.0277  0.0520  352  PHE A CG  
2491  C CD1 . PHE A 354  ? 0.2438 0.2920 0.2767 0.0146  0.0292  0.0507  352  PHE A CD1 
2492  C CD2 . PHE A 354  ? 0.2221 0.2535 0.2547 0.0110  0.0260  0.0483  352  PHE A CD2 
2493  C CE1 . PHE A 354  ? 0.2689 0.3144 0.2996 0.0169  0.0288  0.0460  352  PHE A CE1 
2494  C CE2 . PHE A 354  ? 0.2391 0.2684 0.2693 0.0130  0.0257  0.0442  352  PHE A CE2 
2495  C CZ  . PHE A 354  ? 0.2291 0.2650 0.2587 0.0159  0.0270  0.0430  352  PHE A CZ  
2496  N N   . ILE A 355  ? 0.1808 0.2108 0.2267 0.0036  0.0234  0.0575  353  ILE A N   
2497  C CA  . ILE A 355  ? 0.1707 0.1946 0.2175 0.0025  0.0215  0.0547  353  ILE A CA  
2498  C C   . ILE A 355  ? 0.2060 0.2327 0.2592 0.0004  0.0207  0.0578  353  ILE A C   
2499  O O   . ILE A 355  ? 0.1929 0.2191 0.2467 0.0005  0.0201  0.0561  353  ILE A O   
2500  C CB  . ILE A 355  ? 0.1698 0.1853 0.2157 0.0009  0.0198  0.0524  353  ILE A CB  
2501  C CG1 . ILE A 355  ? 0.1839 0.1963 0.2233 0.0030  0.0205  0.0488  353  ILE A CG1 
2502  C CG2 . ILE A 355  ? 0.1857 0.1964 0.2334 -0.0006 0.0178  0.0500  353  ILE A CG2 
2503  C CD1 . ILE A 355  ? 0.2038 0.2095 0.2425 0.0016  0.0191  0.0471  353  ILE A CD1 
2504  N N   . ILE A 356  ? 0.2004 0.2299 0.2590 -0.0017 0.0203  0.0627  354  ILE A N   
2505  C CA  . ILE A 356  ? 0.1971 0.2295 0.2627 -0.0038 0.0193  0.0660  354  ILE A CA  
2506  C C   . ILE A 356  ? 0.1863 0.2268 0.2518 -0.0022 0.0210  0.0672  354  ILE A C   
2507  O O   . ILE A 356  ? 0.1872 0.2284 0.2557 -0.0028 0.0202  0.0670  354  ILE A O   
2508  C CB  . ILE A 356  ? 0.1748 0.2092 0.2468 -0.0064 0.0185  0.0716  354  ILE A CB  
2509  C CG1 . ILE A 356  ? 0.2186 0.2442 0.2922 -0.0082 0.0160  0.0697  354  ILE A CG1 
2510  C CG2 . ILE A 356  ? 0.2236 0.2634 0.3033 -0.0085 0.0178  0.0763  354  ILE A CG2 
2511  C CD1 . ILE A 356  ? 0.2286 0.2550 0.3071 -0.0100 0.0153  0.0745  354  ILE A CD1 
2512  N N   . ASP A 357  ? 0.1803 0.2274 0.2425 0.0002  0.0234  0.0681  355  ASP A N   
2513  C CA  . ASP A 357  ? 0.2070 0.2624 0.2690 0.0023  0.0251  0.0685  355  ASP A CA  
2514  C C   . ASP A 357  ? 0.2141 0.2656 0.2726 0.0044  0.0248  0.0630  355  ASP A C   
2515  O O   . ASP A 357  ? 0.1934 0.2485 0.2541 0.0049  0.0249  0.0632  355  ASP A O   
2516  C CB  . ASP A 357  ? 0.2055 0.2694 0.2646 0.0047  0.0276  0.0699  355  ASP A CB  
2517  C CG  . ASP A 357  ? 0.2205 0.2931 0.2788 0.0076  0.0294  0.0690  355  ASP A CG  
2518  O OD1 . ASP A 357  ? 0.2536 0.3342 0.3168 0.0067  0.0300  0.0732  355  ASP A OD1 
2519  O OD2 . ASP A 357  ? 0.2097 0.2813 0.2630 0.0108  0.0301  0.0639  355  ASP A OD2 
2520  N N   . LEU A 358  ? 0.1889 0.2332 0.2421 0.0055  0.0243  0.0585  356  LEU A N   
2521  C CA  . LEU A 358  ? 0.1816 0.2217 0.2318 0.0071  0.0236  0.0539  356  LEU A CA  
2522  C C   . LEU A 358  ? 0.1877 0.2238 0.2414 0.0048  0.0216  0.0538  356  LEU A C   
2523  O O   . LEU A 358  ? 0.1926 0.2295 0.2468 0.0058  0.0212  0.0523  356  LEU A O   
2524  C CB  . LEU A 358  ? 0.1723 0.2054 0.2169 0.0082  0.0232  0.0498  356  LEU A CB  
2525  C CG  . LEU A 358  ? 0.1838 0.2116 0.2257 0.0093  0.0221  0.0455  356  LEU A CG  
2526  C CD1 . LEU A 358  ? 0.2178 0.2508 0.2595 0.0123  0.0230  0.0442  356  LEU A CD1 
2527  C CD2 . LEU A 358  ? 0.1998 0.2210 0.2366 0.0099  0.0216  0.0422  356  LEU A CD2 
2528  N N   . ALA A 359  ? 0.1865 0.2187 0.2432 0.0018  0.0201  0.0554  357  ALA A N   
2529  C CA  . ALA A 359  ? 0.1825 0.2117 0.2430 -0.0005 0.0179  0.0552  357  ALA A CA  
2530  C C   . ALA A 359  ? 0.1917 0.2278 0.2574 -0.0009 0.0182  0.0584  357  ALA A C   
2531  O O   . ALA A 359  ? 0.2053 0.2410 0.2724 -0.0012 0.0172  0.0573  357  ALA A O   
2532  C CB  . ALA A 359  ? 0.2101 0.2343 0.2735 -0.0034 0.0161  0.0559  357  ALA A CB  
2533  N N   . ARG A 360  ? 0.1857 0.2288 0.2544 -0.0011 0.0197  0.0628  358  ARG A N   
2534  C CA  . ARG A 360  ? 0.1958 0.2467 0.2697 -0.0015 0.0202  0.0663  358  ARG A CA  
2535  C C   . ARG A 360  ? 0.2328 0.2878 0.3040 0.0017  0.0215  0.0640  358  ARG A C   
2536  O O   . ARG A 360  ? 0.2270 0.2838 0.3012 0.0014  0.0208  0.0640  358  ARG A O   
2537  C CB  . ARG A 360  ? 0.2088 0.2674 0.2862 -0.0022 0.0216  0.0720  358  ARG A CB  
2538  C CG  . ARG A 360  ? 0.2663 0.3217 0.3488 -0.0057 0.0199  0.0755  358  ARG A CG  
2539  C CD  . ARG A 360  ? 0.2838 0.3486 0.3715 -0.0069 0.0210  0.0823  358  ARG A CD  
2540  N NE  . ARG A 360  ? 0.3322 0.3935 0.4238 -0.0096 0.0195  0.0855  358  ARG A NE  
2541  C CZ  . ARG A 360  ? 0.3818 0.4389 0.4804 -0.0129 0.0167  0.0873  358  ARG A CZ  
2542  N NH1 . ARG A 360  ? 0.3842 0.4406 0.4867 -0.0141 0.0152  0.0866  358  ARG A NH1 
2543  N NH2 . ARG A 360  ? 0.3612 0.4146 0.4633 -0.0150 0.0151  0.0897  358  ARG A NH2 
2544  N N   . ARG A 361  ? 0.1992 0.2558 0.2651 0.0048  0.0233  0.0617  359  ARG A N   
2545  C CA  . ARG A 361  ? 0.2089 0.2694 0.2728 0.0082  0.0243  0.0589  359  ARG A CA  
2546  C C   . ARG A 361  ? 0.2078 0.2615 0.2706 0.0084  0.0224  0.0552  359  ARG A C   
2547  O O   . ARG A 361  ? 0.2214 0.2782 0.2861 0.0096  0.0222  0.0546  359  ARG A O   
2548  C CB  . ARG A 361  ? 0.2382 0.3003 0.2969 0.0114  0.0260  0.0563  359  ARG A CB  
2549  C CG  . ARG A 361  ? 0.2738 0.3453 0.3331 0.0121  0.0282  0.0597  359  ARG A CG  
2550  C CD  . ARG A 361  ? 0.2635 0.3369 0.3175 0.0158  0.0296  0.0560  359  ARG A CD  
2551  N NE  . ARG A 361  ? 0.2427 0.3084 0.2924 0.0153  0.0291  0.0542  359  ARG A NE  
2552  C CZ  . ARG A 361  ? 0.2558 0.3156 0.3010 0.0173  0.0285  0.0493  359  ARG A CZ  
2553  N NH1 . ARG A 361  ? 0.2405 0.2998 0.2851 0.0198  0.0281  0.0455  359  ARG A NH1 
2554  N NH2 . ARG A 361  ? 0.2236 0.2778 0.2652 0.0167  0.0282  0.0483  359  ARG A NH2 
2555  N N   . SER A 362  ? 0.1971 0.2420 0.2567 0.0073  0.0209  0.0527  360  SER A N   
2556  C CA  . SER A 362  ? 0.1946 0.2337 0.2527 0.0074  0.0191  0.0495  360  SER A CA  
2557  C C   . SER A 362  ? 0.2148 0.2522 0.2769 0.0045  0.0171  0.0508  360  SER A C   
2558  O O   . SER A 362  ? 0.2294 0.2643 0.2913 0.0046  0.0157  0.0489  360  SER A O   
2559  C CB  . SER A 362  ? 0.2001 0.2314 0.2531 0.0074  0.0184  0.0464  360  SER A CB  
2560  O OG  . SER A 362  ? 0.1994 0.2271 0.2532 0.0045  0.0176  0.0476  360  SER A OG  
2561  N N   . GLY A 363  ? 0.2193 0.2582 0.2856 0.0019  0.0168  0.0540  361  GLY A N   
2562  C CA  . GLY A 363  ? 0.2344 0.2709 0.3047 -0.0010 0.0146  0.0545  361  GLY A CA  
2563  C C   . GLY A 363  ? 0.2513 0.2800 0.3189 -0.0025 0.0126  0.0513  361  GLY A C   
2564  O O   . GLY A 363  ? 0.2505 0.2775 0.3206 -0.0043 0.0105  0.0506  361  GLY A O   
2565  N N   . ARG A 364  ? 0.2044 0.2290 0.2671 -0.0015 0.0131  0.0492  362  ARG A N   
2566  C CA  . ARG A 364  ? 0.2301 0.2480 0.2899 -0.0027 0.0115  0.0462  362  ARG A CA  
2567  C C   . ARG A 364  ? 0.2247 0.2403 0.2866 -0.0047 0.0110  0.0471  362  ARG A C   
2568  O O   . ARG A 364  ? 0.2348 0.2519 0.2964 -0.0040 0.0126  0.0489  362  ARG A O   
2569  C CB  . ARG A 364  ? 0.2355 0.2502 0.2890 -0.0005 0.0123  0.0433  362  ARG A CB  
2570  C CG  . ARG A 364  ? 0.3008 0.3178 0.3526 0.0020  0.0129  0.0426  362  ARG A CG  
2571  C CD  . ARG A 364  ? 0.2216 0.2351 0.2711 0.0019  0.0112  0.0403  362  ARG A CD  
2572  N NE  . ARG A 364  ? 0.1994 0.2156 0.2493 0.0041  0.0113  0.0402  362  ARG A NE  
2573  C CZ  . ARG A 364  ? 0.1953 0.2095 0.2420 0.0063  0.0114  0.0384  362  ARG A CZ  
2574  N NH1 . ARG A 364  ? 0.1836 0.1933 0.2262 0.0064  0.0113  0.0366  362  ARG A NH1 
2575  N NH2 . ARG A 364  ? 0.1946 0.2117 0.2430 0.0085  0.0114  0.0384  362  ARG A NH2 
2576  N N   . ARG A 365  ? 0.1952 0.2074 0.2593 -0.0069 0.0088  0.0456  363  ARG A N   
2577  C CA  . ARG A 365  ? 0.2022 0.2117 0.2692 -0.0087 0.0078  0.0459  363  ARG A CA  
2578  C C   . ARG A 365  ? 0.2114 0.2161 0.2727 -0.0079 0.0081  0.0429  363  ARG A C   
2579  O O   . ARG A 365  ? 0.2233 0.2244 0.2828 -0.0085 0.0065  0.0394  363  ARG A O   
2580  C CB  . ARG A 365  ? 0.2168 0.2249 0.2890 -0.0112 0.0050  0.0449  363  ARG A CB  
2581  C CG  . ARG A 365  ? 0.2063 0.2118 0.2833 -0.0131 0.0036  0.0455  363  ARG A CG  
2582  C CD  . ARG A 365  ? 0.2443 0.2503 0.3290 -0.0156 0.0009  0.0459  363  ARG A CD  
2583  N NE  . ARG A 365  ? 0.2341 0.2375 0.3245 -0.0172 -0.0006 0.0469  363  ARG A NE  
2584  C CZ  . ARG A 365  ? 0.2317 0.2307 0.3238 -0.0182 -0.0031 0.0429  363  ARG A CZ  
2585  N NH1 . ARG A 365  ? 0.2180 0.2154 0.3064 -0.0178 -0.0042 0.0378  363  ARG A NH1 
2586  N NH2 . ARG A 365  ? 0.2282 0.2247 0.3261 -0.0195 -0.0045 0.0441  363  ARG A NH2 
2587  N N   . ILE A 366  ? 0.1928 0.1982 0.2514 -0.0063 0.0101  0.0442  364  ILE A N   
2588  C CA  . ILE A 366  ? 0.1924 0.1938 0.2455 -0.0053 0.0106  0.0415  364  ILE A CA  
2589  C C   . ILE A 366  ? 0.1908 0.1881 0.2459 -0.0070 0.0090  0.0401  364  ILE A C   
2590  O O   . ILE A 366  ? 0.2023 0.2001 0.2628 -0.0084 0.0083  0.0426  364  ILE A O   
2591  C CB  . ILE A 366  ? 0.1725 0.1763 0.2228 -0.0032 0.0130  0.0433  364  ILE A CB  
2592  C CG1 . ILE A 366  ? 0.2005 0.2083 0.2488 -0.0011 0.0144  0.0435  364  ILE A CG1 
2593  C CG2 . ILE A 366  ? 0.2095 0.2091 0.2547 -0.0024 0.0134  0.0407  364  ILE A CG2 
2594  C CD1 . ILE A 366  ? 0.1973 0.2090 0.2436 0.0011  0.0167  0.0450  364  ILE A CD1 
2595  N N   . MET A 367  ? 0.1985 0.1920 0.2498 -0.0070 0.0081  0.0362  365  MET A N   
2596  C CA  . MET A 367  ? 0.2038 0.1936 0.2565 -0.0081 0.0065  0.0340  365  MET A CA  
2597  C C   . MET A 367  ? 0.2202 0.2084 0.2702 -0.0071 0.0080  0.0347  365  MET A C   
2598  O O   . MET A 367  ? 0.2369 0.2244 0.2810 -0.0054 0.0094  0.0335  365  MET A O   
2599  C CB  . MET A 367  ? 0.1874 0.1751 0.2370 -0.0084 0.0051  0.0295  365  MET A CB  
2600  C CG  . MET A 367  ? 0.1993 0.1895 0.2501 -0.0091 0.0039  0.0289  365  MET A CG  
2601  S SD  . MET A 367  ? 0.2506 0.2400 0.2976 -0.0096 0.0022  0.0240  365  MET A SD  
2602  C CE  . MET A 367  ? 0.2636 0.2519 0.3167 -0.0115 -0.0006 0.0210  365  MET A CE  
2603  N N   . VAL A 368  ? 0.1885 0.1763 0.2431 -0.0080 0.0076  0.0369  366  VAL A N   
2604  C CA  . VAL A 368  ? 0.1765 0.1637 0.2291 -0.0070 0.0090  0.0384  366  VAL A CA  
2605  C C   . VAL A 368  ? 0.1903 0.1731 0.2444 -0.0078 0.0073  0.0359  366  VAL A C   
2606  O O   . VAL A 368  ? 0.2002 0.1820 0.2611 -0.0095 0.0053  0.0366  366  VAL A O   
2607  C CB  . VAL A 368  ? 0.2040 0.1954 0.2606 -0.0072 0.0100  0.0438  366  VAL A CB  
2608  C CG1 . VAL A 368  ? 0.2201 0.2114 0.2740 -0.0062 0.0114  0.0452  366  VAL A CG1 
2609  C CG2 . VAL A 368  ? 0.2223 0.2188 0.2778 -0.0063 0.0116  0.0457  366  VAL A CG2 
2610  N N   . ARG A 369  ? 0.1841 0.1645 0.2326 -0.0067 0.0079  0.0328  367  ARG A N   
2611  C CA  . ARG A 369  ? 0.2015 0.1782 0.2510 -0.0071 0.0065  0.0301  367  ARG A CA  
2612  C C   . ARG A 369  ? 0.2027 0.1791 0.2525 -0.0066 0.0076  0.0330  367  ARG A C   
2613  O O   . ARG A 369  ? 0.2015 0.1788 0.2458 -0.0050 0.0095  0.0335  367  ARG A O   
2614  C CB  . ARG A 369  ? 0.2025 0.1774 0.2461 -0.0063 0.0065  0.0255  367  ARG A CB  
2615  C CG  . ARG A 369  ? 0.2251 0.1968 0.2699 -0.0066 0.0052  0.0224  367  ARG A CG  
2616  C CD  . ARG A 369  ? 0.2188 0.1896 0.2568 -0.0055 0.0059  0.0191  367  ARG A CD  
2617  N NE  . ARG A 369  ? 0.2179 0.1903 0.2534 -0.0058 0.0054  0.0165  367  ARG A NE  
2618  C CZ  . ARG A 369  ? 0.2540 0.2269 0.2834 -0.0051 0.0063  0.0152  367  ARG A CZ  
2619  N NH1 . ARG A 369  ? 0.2448 0.2166 0.2701 -0.0040 0.0078  0.0158  367  ARG A NH1 
2620  N NH2 . ARG A 369  ? 0.2492 0.2241 0.2770 -0.0056 0.0056  0.0134  367  ARG A NH2 
2621  N N   . LEU A 370  ? 0.1926 0.1679 0.2492 -0.0078 0.0060  0.0348  368  LEU A N   
2622  C CA  . LEU A 370  ? 0.1936 0.1688 0.2515 -0.0076 0.0065  0.0379  368  LEU A CA  
2623  C C   . LEU A 370  ? 0.1919 0.1629 0.2485 -0.0071 0.0055  0.0340  368  LEU A C   
2624  O O   . LEU A 370  ? 0.1994 0.1676 0.2604 -0.0080 0.0031  0.0309  368  LEU A O   
2625  C CB  . LEU A 370  ? 0.2069 0.1834 0.2736 -0.0093 0.0050  0.0427  368  LEU A CB  
2626  C CG  . LEU A 370  ? 0.1954 0.1730 0.2644 -0.0093 0.0055  0.0473  368  LEU A CG  
2627  C CD1 . LEU A 370  ? 0.2249 0.2076 0.2880 -0.0078 0.0086  0.0505  368  LEU A CD1 
2628  C CD2 . LEU A 370  ? 0.2400 0.2183 0.3192 -0.0115 0.0033  0.0520  368  LEU A CD2 
2629  N N   . VAL A 371  ? 0.1898 0.1607 0.2406 -0.0057 0.0072  0.0337  369  VAL A N   
2630  C CA  . VAL A 371  ? 0.2021 0.1696 0.2515 -0.0051 0.0065  0.0305  369  VAL A CA  
2631  C C   . VAL A 371  ? 0.1992 0.1674 0.2496 -0.0047 0.0072  0.0345  369  VAL A C   
2632  O O   . VAL A 371  ? 0.2082 0.1800 0.2586 -0.0046 0.0086  0.0391  369  VAL A O   
2633  C CB  . VAL A 371  ? 0.2001 0.1670 0.2415 -0.0038 0.0078  0.0264  369  VAL A CB  
2634  C CG1 . VAL A 371  ? 0.1960 0.1634 0.2361 -0.0043 0.0072  0.0235  369  VAL A CG1 
2635  C CG2 . VAL A 371  ? 0.1937 0.1629 0.2293 -0.0024 0.0103  0.0287  369  VAL A CG2 
2636  N N   . LYS A 372  ? 0.2124 0.1776 0.2635 -0.0044 0.0063  0.0325  370  LYS A N   
2637  C CA  . LYS A 372  ? 0.2063 0.1725 0.2576 -0.0040 0.0070  0.0364  370  LYS A CA  
2638  C C   . LYS A 372  ? 0.2110 0.1787 0.2537 -0.0022 0.0095  0.0356  370  LYS A C   
2639  O O   . LYS A 372  ? 0.2296 0.2012 0.2703 -0.0016 0.0112  0.0394  370  LYS A O   
2640  C CB  . LYS A 372  ? 0.2385 0.2010 0.2955 -0.0044 0.0047  0.0354  370  LYS A CB  
2641  C CG  . LYS A 372  ? 0.2246 0.1863 0.2917 -0.0062 0.0021  0.0379  370  LYS A CG  
2642  C CD  . LYS A 372  ? 0.2422 0.2002 0.3167 -0.0066 -0.0007 0.0371  370  LYS A CD  
2643  C CE  . LYS A 372  ? 0.2401 0.1968 0.3251 -0.0085 -0.0037 0.0388  370  LYS A CE  
2644  N NZ  . LYS A 372  ? 0.2318 0.1843 0.3251 -0.0088 -0.0070 0.0373  370  LYS A NZ  
2645  N N   . GLY A 373  ? 0.1998 0.1652 0.2374 -0.0014 0.0097  0.0307  371  GLY A N   
2646  C CA  . GLY A 373  ? 0.1969 0.1635 0.2269 0.0001  0.0118  0.0297  371  GLY A CA  
2647  C C   . GLY A 373  ? 0.2267 0.1905 0.2534 0.0007  0.0115  0.0257  371  GLY A C   
2648  O O   . GLY A 373  ? 0.2399 0.2018 0.2699 0.0006  0.0103  0.0254  371  GLY A O   
2649  N N   . ALA A 374  ? 0.2247 0.1885 0.2454 0.0015  0.0125  0.0230  372  ALA A N   
2650  C CA  . ALA A 374  ? 0.2088 0.1705 0.2267 0.0018  0.0121  0.0191  372  ALA A CA  
2651  C C   . ALA A 374  ? 0.2327 0.1945 0.2457 0.0030  0.0133  0.0192  372  ALA A C   
2652  O O   . ALA A 374  ? 0.2406 0.2011 0.2516 0.0032  0.0130  0.0163  372  ALA A O   
2653  C CB  . ALA A 374  ? 0.2492 0.2110 0.2643 0.0014  0.0119  0.0160  372  ALA A CB  
2654  N N   . TYR A 375  ? 0.2094 0.1734 0.2208 0.0039  0.0145  0.0222  373  TYR A N   
2655  C CA  . TYR A 375  ? 0.2160 0.1805 0.2225 0.0052  0.0156  0.0217  373  TYR A CA  
2656  C C   . TYR A 375  ? 0.1926 0.1583 0.2003 0.0057  0.0158  0.0244  373  TYR A C   
2657  O O   . TYR A 375  ? 0.2235 0.1912 0.2275 0.0069  0.0169  0.0251  373  TYR A O   
2658  C CB  . TYR A 375  ? 0.2002 0.1667 0.2029 0.0061  0.0168  0.0220  373  TYR A CB  
2659  C CG  . TYR A 375  ? 0.2086 0.1742 0.2102 0.0056  0.0164  0.0199  373  TYR A CG  
2660  C CD1 . TYR A 375  ? 0.2015 0.1677 0.2062 0.0047  0.0160  0.0208  373  TYR A CD1 
2661  C CD2 . TYR A 375  ? 0.2435 0.2078 0.2412 0.0059  0.0164  0.0174  373  TYR A CD2 
2662  C CE1 . TYR A 375  ? 0.2173 0.1831 0.2209 0.0043  0.0156  0.0191  373  TYR A CE1 
2663  C CE2 . TYR A 375  ? 0.2347 0.1987 0.2317 0.0054  0.0159  0.0161  373  TYR A CE2 
2664  C CZ  . TYR A 375  ? 0.2541 0.2189 0.2539 0.0046  0.0156  0.0169  373  TYR A CZ  
2665  O OH  . TYR A 375  ? 0.2591 0.2240 0.2581 0.0040  0.0150  0.0159  373  TYR A OH  
2666  N N   . TRP A 376  ? 0.2139 0.1788 0.2269 0.0049  0.0147  0.0260  374  TRP A N   
2667  C CA  . TRP A 376  ? 0.2143 0.1813 0.2294 0.0051  0.0148  0.0299  374  TRP A CA  
2668  C C   . TRP A 376  ? 0.2128 0.1800 0.2237 0.0063  0.0154  0.0291  374  TRP A C   
2669  O O   . TRP A 376  ? 0.2134 0.1842 0.2218 0.0073  0.0165  0.0314  374  TRP A O   
2670  C CB  . TRP A 376  ? 0.2408 0.2059 0.2632 0.0039  0.0130  0.0316  374  TRP A CB  
2671  C CG  . TRP A 376  ? 0.2302 0.1980 0.2554 0.0040  0.0129  0.0365  374  TRP A CG  
2672  C CD1 . TRP A 376  ? 0.2241 0.1963 0.2515 0.0036  0.0134  0.0416  374  TRP A CD1 
2673  C CD2 . TRP A 376  ? 0.2633 0.2303 0.2892 0.0044  0.0122  0.0371  374  TRP A CD2 
2674  N NE1 . TRP A 376  ? 0.2251 0.1995 0.2545 0.0037  0.0131  0.0456  374  TRP A NE1 
2675  C CE2 . TRP A 376  ? 0.2357 0.2067 0.2643 0.0042  0.0123  0.0429  374  TRP A CE2 
2676  C CE3 . TRP A 376  ? 0.2835 0.2473 0.3083 0.0049  0.0116  0.0335  374  TRP A CE3 
2677  C CZ2 . TRP A 376  ? 0.2292 0.2009 0.2596 0.0044  0.0117  0.0454  374  TRP A CZ2 
2678  C CZ3 . TRP A 376  ? 0.2935 0.2577 0.3200 0.0053  0.0109  0.0356  374  TRP A CZ3 
2679  C CH2 . TRP A 376  ? 0.2829 0.2508 0.3121 0.0050  0.0109  0.0415  374  TRP A CH2 
2680  N N   . ASP A 377  ? 0.2442 0.2082 0.2542 0.0063  0.0147  0.0256  375  ASP A N   
2681  C CA  A ASP A 377  ? 0.2648 0.2289 0.2713 0.0073  0.0150  0.0248  375  ASP A CA  
2682  C CA  B ASP A 377  ? 0.2648 0.2291 0.2714 0.0074  0.0151  0.0251  375  ASP A CA  
2683  C C   . ASP A 377  ? 0.2302 0.1962 0.2307 0.0085  0.0164  0.0239  375  ASP A C   
2684  O O   . ASP A 377  ? 0.2381 0.2064 0.2361 0.0096  0.0170  0.0248  375  ASP A O   
2685  C CB  A ASP A 377  ? 0.3093 0.2702 0.3161 0.0071  0.0141  0.0210  375  ASP A CB  
2686  C CB  B ASP A 377  ? 0.3114 0.2725 0.3187 0.0072  0.0140  0.0218  375  ASP A CB  
2687  C CG  A ASP A 377  ? 0.3286 0.2875 0.3419 0.0064  0.0124  0.0212  375  ASP A CG  
2688  C CG  B ASP A 377  ? 0.3176 0.2770 0.3229 0.0067  0.0139  0.0177  375  ASP A CG  
2689  O OD1 A ASP A 377  ? 0.3936 0.3531 0.4101 0.0065  0.0118  0.0243  375  ASP A OD1 
2690  O OD1 B ASP A 377  ? 0.3527 0.3129 0.3541 0.0069  0.0148  0.0169  375  ASP A OD1 
2691  O OD2 A ASP A 377  ? 0.3894 0.3465 0.4049 0.0057  0.0114  0.0184  375  ASP A OD2 
2692  O OD2 B ASP A 377  ? 0.3458 0.3033 0.3537 0.0062  0.0127  0.0151  375  ASP A OD2 
2693  N N   . ALA A 378  ? 0.2265 0.1918 0.2250 0.0083  0.0168  0.0218  376  ALA A N   
2694  C CA  . ALA A 378  ? 0.2471 0.2138 0.2409 0.0095  0.0177  0.0206  376  ALA A CA  
2695  C C   . ALA A 378  ? 0.2220 0.1931 0.2154 0.0106  0.0187  0.0233  376  ALA A C   
2696  O O   . ALA A 378  ? 0.2169 0.1901 0.2067 0.0120  0.0193  0.0226  376  ALA A O   
2697  C CB  . ALA A 378  ? 0.2213 0.1863 0.2140 0.0089  0.0175  0.0184  376  ALA A CB  
2698  N N   . GLU A 379  ? 0.2154 0.1884 0.2123 0.0099  0.0188  0.0264  377  GLU A N   
2699  C CA  . GLU A 379  ? 0.1932 0.1718 0.1899 0.0109  0.0199  0.0293  377  GLU A CA  
2700  C C   . GLU A 379  ? 0.2031 0.1850 0.1993 0.0116  0.0202  0.0316  377  GLU A C   
2701  O O   . GLU A 379  ? 0.2123 0.1992 0.2058 0.0131  0.0212  0.0322  377  GLU A O   
2702  C CB  . GLU A 379  ? 0.2136 0.1939 0.2148 0.0098  0.0199  0.0325  377  GLU A CB  
2703  C CG  . GLU A 379  ? 0.2271 0.2051 0.2291 0.0091  0.0196  0.0307  377  GLU A CG  
2704  C CD  . GLU A 379  ? 0.2413 0.2211 0.2397 0.0105  0.0205  0.0287  377  GLU A CD  
2705  O OE1 . GLU A 379  ? 0.2263 0.2096 0.2216 0.0123  0.0214  0.0285  377  GLU A OE1 
2706  O OE2 . GLU A 379  ? 0.2292 0.2071 0.2281 0.0100  0.0202  0.0273  377  GLU A OE2 
2707  N N   . ILE A 380  ? 0.2179 0.1975 0.2170 0.0106  0.0192  0.0329  378  ILE A N   
2708  C CA  . ILE A 380  ? 0.2217 0.2045 0.2206 0.0112  0.0192  0.0354  378  ILE A CA  
2709  C C   . ILE A 380  ? 0.2364 0.2194 0.2296 0.0128  0.0197  0.0321  378  ILE A C   
2710  O O   . ILE A 380  ? 0.2261 0.2144 0.2168 0.0142  0.0205  0.0331  378  ILE A O   
2711  C CB  . ILE A 380  ? 0.2132 0.1927 0.2170 0.0099  0.0177  0.0369  378  ILE A CB  
2712  C CG1 . ILE A 380  ? 0.2315 0.2103 0.2418 0.0083  0.0168  0.0400  378  ILE A CG1 
2713  C CG2 . ILE A 380  ? 0.2159 0.1990 0.2198 0.0105  0.0176  0.0401  378  ILE A CG2 
2714  C CD1 . ILE A 380  ? 0.2300 0.2151 0.2424 0.0081  0.0175  0.0453  378  ILE A CD1 
2715  N N   . LYS A 381  ? 0.2062 0.1842 0.1977 0.0126  0.0191  0.0280  379  LYS A N   
2716  C CA  . LYS A 381  ? 0.2196 0.1974 0.2065 0.0139  0.0192  0.0249  379  LYS A CA  
2717  C C   . LYS A 381  ? 0.2255 0.2068 0.2091 0.0155  0.0201  0.0236  379  LYS A C   
2718  O O   . LYS A 381  ? 0.2137 0.1983 0.1944 0.0170  0.0204  0.0228  379  LYS A O   
2719  C CB  . LYS A 381  ? 0.2403 0.2126 0.2264 0.0131  0.0184  0.0212  379  LYS A CB  
2720  C CG  . LYS A 381  ? 0.2310 0.2028 0.2130 0.0141  0.0183  0.0181  379  LYS A CG  
2721  C CD  . LYS A 381  ? 0.2359 0.2031 0.2177 0.0131  0.0175  0.0153  379  LYS A CD  
2722  C CE  . LYS A 381  ? 0.2373 0.2040 0.2158 0.0138  0.0171  0.0128  379  LYS A CE  
2723  N NZ  . LYS A 381  ? 0.2121 0.1755 0.1907 0.0126  0.0164  0.0106  379  LYS A NZ  
2724  N N   . ARG A 382  ? 0.2114 0.1924 0.1957 0.0153  0.0204  0.0231  380  ARG A N   
2725  C CA  . ARG A 382  ? 0.2102 0.1940 0.1920 0.0170  0.0210  0.0212  380  ARG A CA  
2726  C C   . ARG A 382  ? 0.2162 0.2076 0.1972 0.0185  0.0221  0.0235  380  ARG A C   
2727  O O   . ARG A 382  ? 0.2249 0.2197 0.2030 0.0205  0.0223  0.0212  380  ARG A O   
2728  C CB  . ARG A 382  ? 0.2448 0.2270 0.2282 0.0163  0.0211  0.0208  380  ARG A CB  
2729  C CG  . ARG A 382  ? 0.3221 0.3064 0.3037 0.0181  0.0214  0.0185  380  ARG A CG  
2730  C CD  . ARG A 382  ? 0.4105 0.3903 0.3901 0.0184  0.0203  0.0146  380  ARG A CD  
2731  N NE  . ARG A 382  ? 0.4321 0.4138 0.4091 0.0201  0.0201  0.0125  380  ARG A NE  
2732  C CZ  . ARG A 382  ? 0.4331 0.4113 0.4086 0.0203  0.0189  0.0096  380  ARG A CZ  
2733  N NH1 . ARG A 382  ? 0.4946 0.4675 0.4709 0.0186  0.0180  0.0087  380  ARG A NH1 
2734  N NH2 . ARG A 382  ? 0.3726 0.3532 0.3461 0.0220  0.0187  0.0075  380  ARG A NH2 
2735  N N   . ALA A 383  ? 0.2301 0.2248 0.2142 0.0176  0.0225  0.0280  381  ALA A N   
2736  C CA  . ALA A 383  ? 0.2142 0.2175 0.1977 0.0188  0.0236  0.0308  381  ALA A CA  
2737  C C   . ALA A 383  ? 0.2419 0.2480 0.2228 0.0199  0.0235  0.0307  381  ALA A C   
2738  O O   . ALA A 383  ? 0.2319 0.2449 0.2101 0.0218  0.0242  0.0301  381  ALA A O   
2739  C CB  . ALA A 383  ? 0.2104 0.2166 0.1985 0.0172  0.0239  0.0365  381  ALA A CB  
2740  N N   . GLN A 384  ? 0.2317 0.2329 0.2135 0.0186  0.0225  0.0310  382  GLN A N   
2741  C CA  . GLN A 384  ? 0.2198 0.2234 0.1994 0.0195  0.0222  0.0308  382  GLN A CA  
2742  C C   . GLN A 384  ? 0.2194 0.2224 0.1946 0.0214  0.0220  0.0254  382  GLN A C   
2743  O O   . GLN A 384  ? 0.2469 0.2557 0.2192 0.0231  0.0223  0.0247  382  GLN A O   
2744  C CB  . GLN A 384  ? 0.2330 0.2312 0.2150 0.0179  0.0211  0.0320  382  GLN A CB  
2745  C CG  . GLN A 384  ? 0.2195 0.2188 0.2067 0.0163  0.0208  0.0375  382  GLN A CG  
2746  C CD  . GLN A 384  ? 0.2585 0.2531 0.2486 0.0151  0.0194  0.0383  382  GLN A CD  
2747  O OE1 . GLN A 384  ? 0.2643 0.2537 0.2527 0.0152  0.0188  0.0343  382  GLN A OE1 
2748  N NE2 . GLN A 384  ? 0.2591 0.2557 0.2538 0.0141  0.0188  0.0434  382  GLN A NE2 
2749  N N   . LEU A 385  ? 0.2285 0.2248 0.2032 0.0210  0.0214  0.0217  383  LEU A N   
2750  C CA  . LEU A 385  ? 0.2236 0.2188 0.1952 0.0225  0.0208  0.0168  383  LEU A CA  
2751  C C   . LEU A 385  ? 0.2577 0.2593 0.2277 0.0248  0.0215  0.0151  383  LEU A C   
2752  O O   . LEU A 385  ? 0.2457 0.2499 0.2130 0.0267  0.0210  0.0119  383  LEU A O   
2753  C CB  . LEU A 385  ? 0.2146 0.2023 0.1869 0.0214  0.0199  0.0140  383  LEU A CB  
2754  C CG  . LEU A 385  ? 0.2430 0.2246 0.2162 0.0195  0.0191  0.0138  383  LEU A CG  
2755  C CD1 . LEU A 385  ? 0.2808 0.2572 0.2546 0.0185  0.0184  0.0115  383  LEU A CD1 
2756  C CD2 . LEU A 385  ? 0.2764 0.2580 0.2476 0.0201  0.0184  0.0120  383  LEU A CD2 
2757  N N   . ASP A 386  ? 0.2291 0.2333 0.2007 0.0248  0.0224  0.0169  384  ASP A N   
2758  C CA  . ASP A 386  ? 0.2384 0.2488 0.2088 0.0271  0.0230  0.0149  384  ASP A CA  
2759  C C   . ASP A 386  ? 0.2548 0.2753 0.2240 0.0285  0.0242  0.0175  384  ASP A C   
2760  O O   . ASP A 386  ? 0.2627 0.2902 0.2309 0.0307  0.0248  0.0158  384  ASP A O   
2761  C CB  . ASP A 386  ? 0.2608 0.2697 0.2335 0.0266  0.0234  0.0155  384  ASP A CB  
2762  C CG  . ASP A 386  ? 0.3298 0.3304 0.3032 0.0259  0.0222  0.0122  384  ASP A CG  
2763  O OD1 . ASP A 386  ? 0.3047 0.3012 0.2767 0.0261  0.0210  0.0091  384  ASP A OD1 
2764  O OD2 . ASP A 386  ? 0.3008 0.2993 0.2763 0.0251  0.0223  0.0129  384  ASP A OD2 
2765  N N   . GLY A 387  ? 0.2555 0.2778 0.2252 0.0273  0.0243  0.0217  385  GLY A N   
2766  C CA  . GLY A 387  ? 0.2501 0.2828 0.2188 0.0283  0.0253  0.0250  385  GLY A CA  
2767  C C   . GLY A 387  ? 0.2651 0.3052 0.2355 0.0285  0.0267  0.0282  385  GLY A C   
2768  O O   . GLY A 387  ? 0.2612 0.3116 0.2297 0.0306  0.0276  0.0281  385  GLY A O   
2769  N N   . LEU A 388  ? 0.2526 0.2884 0.2267 0.0265  0.0268  0.0311  386  LEU A N   
2770  C CA  . LEU A 388  ? 0.2649 0.3074 0.2409 0.0266  0.0280  0.0340  386  LEU A CA  
2771  C C   . LEU A 388  ? 0.2557 0.3046 0.2346 0.0250  0.0286  0.0415  386  LEU A C   
2772  O O   . LEU A 388  ? 0.2545 0.3012 0.2345 0.0236  0.0278  0.0445  386  LEU A O   
2773  C CB  . LEU A 388  ? 0.2304 0.2655 0.2091 0.0254  0.0278  0.0330  386  LEU A CB  
2774  C CG  . LEU A 388  ? 0.2498 0.2799 0.2262 0.0271  0.0271  0.0262  386  LEU A CG  
2775  C CD1 . LEU A 388  ? 0.2618 0.2849 0.2406 0.0258  0.0267  0.0253  386  LEU A CD1 
2776  C CD2 . LEU A 388  ? 0.2852 0.3238 0.2590 0.0303  0.0278  0.0228  386  LEU A CD2 
2777  N N   . ALA A 389  ? 0.2502 0.3077 0.2305 0.0253  0.0299  0.0447  387  ALA A N   
2778  C CA  . ALA A 389  ? 0.2826 0.3487 0.2655 0.0240  0.0304  0.0522  387  ALA A CA  
2779  C C   . ALA A 389  ? 0.2464 0.3054 0.2349 0.0207  0.0292  0.0574  387  ALA A C   
2780  O O   . ALA A 389  ? 0.2632 0.3258 0.2541 0.0193  0.0288  0.0632  387  ALA A O   
2781  C CB  . ALA A 389  ? 0.2919 0.3690 0.2755 0.0250  0.0320  0.0545  387  ALA A CB  
2782  N N   . ASP A 390  ? 0.2317 0.2812 0.2227 0.0193  0.0285  0.0555  388  ASP A N   
2783  C CA  . ASP A 390  ? 0.2729 0.3161 0.2698 0.0164  0.0272  0.0598  388  ASP A CA  
2784  C C   . ASP A 390  ? 0.2336 0.2658 0.2312 0.0157  0.0264  0.0550  388  ASP A C   
2785  O O   . ASP A 390  ? 0.2231 0.2529 0.2167 0.0174  0.0268  0.0493  388  ASP A O   
2786  C CB  . ASP A 390  ? 0.2607 0.3111 0.2627 0.0148  0.0277  0.0668  388  ASP A CB  
2787  C CG  . ASP A 390  ? 0.2439 0.2909 0.2526 0.0119  0.0260  0.0728  388  ASP A CG  
2788  O OD1 . ASP A 390  ? 0.2528 0.2895 0.2636 0.0108  0.0244  0.0705  388  ASP A OD1 
2789  O OD2 . ASP A 390  ? 0.2929 0.3480 0.3055 0.0108  0.0261  0.0798  388  ASP A OD2 
2790  N N   . PHE A 391  ? 0.2314 0.2572 0.2341 0.0133  0.0250  0.0573  389  PHE A N   
2791  C CA  . PHE A 391  ? 0.2228 0.2392 0.2264 0.0125  0.0241  0.0531  389  PHE A CA  
2792  C C   . PHE A 391  ? 0.2271 0.2448 0.2332 0.0119  0.0246  0.0540  389  PHE A C   
2793  O O   . PHE A 391  ? 0.2172 0.2417 0.2265 0.0113  0.0251  0.0591  389  PHE A O   
2794  C CB  . PHE A 391  ? 0.2374 0.2465 0.2454 0.0105  0.0222  0.0542  389  PHE A CB  
2795  C CG  . PHE A 391  ? 0.2145 0.2223 0.2203 0.0111  0.0217  0.0534  389  PHE A CG  
2796  C CD1 . PHE A 391  ? 0.2054 0.2086 0.2064 0.0123  0.0217  0.0477  389  PHE A CD1 
2797  C CD2 . PHE A 391  ? 0.2297 0.2415 0.2384 0.0105  0.0212  0.0587  389  PHE A CD2 
2798  C CE1 . PHE A 391  ? 0.2488 0.2512 0.2478 0.0129  0.0212  0.0468  389  PHE A CE1 
2799  C CE2 . PHE A 391  ? 0.2396 0.2505 0.2462 0.0111  0.0207  0.0579  389  PHE A CE2 
2800  C CZ  . PHE A 391  ? 0.2473 0.2535 0.2490 0.0124  0.0207  0.0518  389  PHE A CZ  
2801  N N   . PRO A 392  ? 0.2187 0.2305 0.2234 0.0121  0.0244  0.0493  390  PRO A N   
2802  C CA  . PRO A 392  ? 0.2035 0.2156 0.2110 0.0113  0.0245  0.0499  390  PRO A CA  
2803  C C   . PRO A 392  ? 0.2035 0.2099 0.2170 0.0088  0.0229  0.0517  390  PRO A C   
2804  O O   . PRO A 392  ? 0.2227 0.2286 0.2388 0.0079  0.0228  0.0520  390  PRO A O   
2805  C CB  . PRO A 392  ? 0.1962 0.2046 0.1993 0.0129  0.0248  0.0439  390  PRO A CB  
2806  C CG  . PRO A 392  ? 0.1981 0.1999 0.1989 0.0128  0.0238  0.0405  390  PRO A CG  
2807  C CD  . PRO A 392  ? 0.1943 0.2000 0.1946 0.0131  0.0240  0.0433  390  PRO A CD  
2808  N N   . VAL A 393  ? 0.2251 0.2273 0.2408 0.0076  0.0215  0.0525  391  VAL A N   
2809  C CA  . VAL A 393  ? 0.2193 0.2161 0.2412 0.0054  0.0196  0.0536  391  VAL A CA  
2810  C C   . VAL A 393  ? 0.2132 0.2121 0.2399 0.0044  0.0186  0.0589  391  VAL A C   
2811  O O   . VAL A 393  ? 0.2354 0.2387 0.2596 0.0053  0.0194  0.0608  391  VAL A O   
2812  C CB  . VAL A 393  ? 0.2213 0.2099 0.2416 0.0054  0.0185  0.0480  391  VAL A CB  
2813  C CG1 . VAL A 393  ? 0.2455 0.2322 0.2621 0.0061  0.0191  0.0436  391  VAL A CG1 
2814  C CG2 . VAL A 393  ? 0.1990 0.1868 0.2152 0.0066  0.0187  0.0463  391  VAL A CG2 
2815  N N   . PHE A 394  ? 0.2178 0.2136 0.2520 0.0023  0.0167  0.0614  392  PHE A N   
2816  C CA  . PHE A 394  ? 0.2244 0.2210 0.2645 0.0011  0.0152  0.0665  392  PHE A CA  
2817  C C   . PHE A 394  ? 0.2305 0.2218 0.2689 0.0017  0.0143  0.0632  392  PHE A C   
2818  O O   . PHE A 394  ? 0.2342 0.2206 0.2683 0.0026  0.0144  0.0572  392  PHE A O   
2819  C CB  . PHE A 394  ? 0.2373 0.2313 0.2867 -0.0013 0.0130  0.0694  392  PHE A CB  
2820  C CG  . PHE A 394  ? 0.2248 0.2245 0.2763 -0.0021 0.0138  0.0732  392  PHE A CG  
2821  C CD1 . PHE A 394  ? 0.2555 0.2642 0.3075 -0.0022 0.0150  0.0796  392  PHE A CD1 
2822  C CD2 . PHE A 394  ? 0.2265 0.2234 0.2793 -0.0027 0.0135  0.0704  392  PHE A CD2 
2823  C CE1 . PHE A 394  ? 0.2309 0.2458 0.2848 -0.0029 0.0160  0.0832  392  PHE A CE1 
2824  C CE2 . PHE A 394  ? 0.2102 0.2127 0.2650 -0.0034 0.0144  0.0739  392  PHE A CE2 
2825  C CZ  . PHE A 394  ? 0.2454 0.2570 0.3009 -0.0035 0.0156  0.0803  392  PHE A CZ  
2826  N N   . THR A 395  ? 0.2360 0.2290 0.2781 0.0012  0.0132  0.0677  393  THR A N   
2827  C CA  . THR A 395  ? 0.2611 0.2497 0.3024 0.0019  0.0122  0.0651  393  THR A CA  
2828  C C   . THR A 395  ? 0.2550 0.2385 0.3053 0.0003  0.0092  0.0667  393  THR A C   
2829  O O   . THR A 395  ? 0.2481 0.2272 0.2984 0.0009  0.0082  0.0637  393  THR A O   
2830  C CB  . THR A 395  ? 0.2578 0.2522 0.2948 0.0031  0.0134  0.0678  393  THR A CB  
2831  O OG1 . THR A 395  ? 0.2518 0.2525 0.2939 0.0019  0.0129  0.0757  393  THR A OG1 
2832  C CG2 . THR A 395  ? 0.2769 0.2756 0.3049 0.0050  0.0161  0.0647  393  THR A CG2 
2833  N N   . ARG A 396  ? 0.2435 0.2275 0.3019 -0.0015 0.0077  0.0711  394  ARG A N   
2834  C CA  . ARG A 396  ? 0.2574 0.2355 0.3254 -0.0029 0.0044  0.0714  394  ARG A CA  
2835  C C   . ARG A 396  ? 0.2596 0.2334 0.3303 -0.0037 0.0035  0.0674  394  ARG A C   
2836  O O   . ARG A 396  ? 0.2634 0.2405 0.3335 -0.0044 0.0046  0.0690  394  ARG A O   
2837  C CB  . ARG A 396  ? 0.2748 0.2565 0.3518 -0.0047 0.0025  0.0800  394  ARG A CB  
2838  C CG  . ARG A 396  ? 0.2781 0.2644 0.3530 -0.0041 0.0031  0.0844  394  ARG A CG  
2839  C CD  . ARG A 396  ? 0.3072 0.2964 0.3922 -0.0061 0.0007  0.0932  394  ARG A CD  
2840  N NE  . ARG A 396  ? 0.3477 0.3436 0.4294 -0.0055 0.0018  0.0981  394  ARG A NE  
2841  C CZ  . ARG A 396  ? 0.3714 0.3678 0.4597 -0.0063 -0.0005 0.1036  394  ARG A CZ  
2842  N NH1 . ARG A 396  ? 0.4097 0.4001 0.5094 -0.0078 -0.0042 0.1051  394  ARG A NH1 
2843  N NH2 . ARG A 396  ? 0.3573 0.3605 0.4413 -0.0055 0.0007  0.1074  394  ARG A NH2 
2844  N N   . LYS A 397  ? 0.2510 0.2181 0.3245 -0.0035 0.0015  0.0617  395  LYS A N   
2845  C CA  . LYS A 397  ? 0.2437 0.2071 0.3192 -0.0041 0.0006  0.0570  395  LYS A CA  
2846  C C   . LYS A 397  ? 0.2844 0.2486 0.3689 -0.0062 -0.0013 0.0617  395  LYS A C   
2847  O O   . LYS A 397  ? 0.2590 0.2235 0.3431 -0.0067 -0.0009 0.0601  395  LYS A O   
2848  C CB  . LYS A 397  ? 0.3012 0.2583 0.3792 -0.0034 -0.0016 0.0506  395  LYS A CB  
2849  C CG  . LYS A 397  ? 0.2967 0.2510 0.3737 -0.0034 -0.0019 0.0441  395  LYS A CG  
2850  C CD  . LYS A 397  ? 0.2831 0.2342 0.3709 -0.0049 -0.0053 0.0440  395  LYS A CD  
2851  C CE  . LYS A 397  ? 0.2831 0.2330 0.3695 -0.0050 -0.0055 0.0382  395  LYS A CE  
2852  N NZ  . LYS A 397  ? 0.2780 0.2249 0.3752 -0.0063 -0.0091 0.0375  395  LYS A NZ  
2853  N N   . ILE A 398  ? 0.2491 0.2141 0.3421 -0.0074 -0.0034 0.0680  396  ILE A N   
2854  C CA  . ILE A 398  ? 0.2735 0.2392 0.3762 -0.0097 -0.0055 0.0730  396  ILE A CA  
2855  C C   . ILE A 398  ? 0.2427 0.2156 0.3416 -0.0103 -0.0029 0.0776  396  ILE A C   
2856  O O   . ILE A 398  ? 0.2531 0.2266 0.3574 -0.0119 -0.0039 0.0795  396  ILE A O   
2857  C CB  . ILE A 398  ? 0.3207 0.2858 0.4337 -0.0110 -0.0085 0.0792  396  ILE A CB  
2858  C CG1 . ILE A 398  ? 0.3169 0.2811 0.4420 -0.0135 -0.0117 0.0834  396  ILE A CG1 
2859  C CG2 . ILE A 398  ? 0.2717 0.2440 0.3810 -0.0108 -0.0065 0.0864  396  ILE A CG2 
2860  C CD1 . ILE A 398  ? 0.3640 0.3248 0.5013 -0.0146 -0.0158 0.0874  396  ILE A CD1 
2861  N N   . HIS A 399  ? 0.2581 0.2366 0.3479 -0.0089 0.0004  0.0790  397  HIS A N   
2862  C CA  . HIS A 399  ? 0.2604 0.2464 0.3462 -0.0091 0.0030  0.0825  397  HIS A CA  
2863  C C   . HIS A 399  ? 0.2228 0.2068 0.3042 -0.0085 0.0041  0.0767  397  HIS A C   
2864  O O   . HIS A 399  ? 0.2342 0.2214 0.3180 -0.0096 0.0044  0.0792  397  HIS A O   
2865  C CB  . HIS A 399  ? 0.2460 0.2384 0.3229 -0.0073 0.0060  0.0841  397  HIS A CB  
2866  C CG  . HIS A 399  ? 0.2626 0.2588 0.3433 -0.0079 0.0052  0.0909  397  HIS A CG  
2867  N ND1 . HIS A 399  ? 0.2551 0.2564 0.3288 -0.0063 0.0072  0.0919  397  HIS A ND1 
2868  C CD2 . HIS A 399  ? 0.2787 0.2746 0.3700 -0.0100 0.0023  0.0972  397  HIS A CD2 
2869  C CE1 . HIS A 399  ? 0.2651 0.2695 0.3446 -0.0074 0.0058  0.0987  397  HIS A CE1 
2870  N NE2 . HIS A 399  ? 0.2719 0.2729 0.3622 -0.0097 0.0027  0.1022  397  HIS A NE2 
2871  N N   . THR A 400  ? 0.2336 0.2126 0.3090 -0.0070 0.0046  0.0691  398  THR A N   
2872  C CA  . THR A 400  ? 0.2190 0.1958 0.2910 -0.0066 0.0052  0.0636  398  THR A CA  
2873  C C   . THR A 400  ? 0.2293 0.2028 0.3103 -0.0085 0.0024  0.0634  398  THR A C   
2874  O O   . THR A 400  ? 0.2184 0.1933 0.2991 -0.0090 0.0029  0.0627  398  THR A O   
2875  C CB  . THR A 400  ? 0.2362 0.2083 0.3015 -0.0049 0.0057  0.0562  398  THR A CB  
2876  O OG1 . THR A 400  ? 0.2200 0.1955 0.2768 -0.0032 0.0084  0.0562  398  THR A OG1 
2877  C CG2 . THR A 400  ? 0.2245 0.1941 0.2873 -0.0049 0.0058  0.0506  398  THR A CG2 
2878  N N   . ASP A 401  ? 0.2162 0.1853 0.3056 -0.0095 -0.0007 0.0638  399  ASP A N   
2879  C CA  . ASP A 401  ? 0.2471 0.2130 0.3460 -0.0113 -0.0039 0.0633  399  ASP A CA  
2880  C C   . ASP A 401  ? 0.2321 0.2030 0.3366 -0.0133 -0.0040 0.0706  399  ASP A C   
2881  O O   . ASP A 401  ? 0.2231 0.1938 0.3306 -0.0143 -0.0047 0.0697  399  ASP A O   
2882  C CB  . ASP A 401  ? 0.2390 0.1994 0.3470 -0.0119 -0.0076 0.0624  399  ASP A CB  
2883  C CG  . ASP A 401  ? 0.2724 0.2279 0.3761 -0.0101 -0.0079 0.0541  399  ASP A CG  
2884  O OD1 . ASP A 401  ? 0.2965 0.2522 0.3922 -0.0089 -0.0059 0.0487  399  ASP A OD1 
2885  O OD2 . ASP A 401  ? 0.3015 0.2536 0.4103 -0.0098 -0.0101 0.0533  399  ASP A OD2 
2886  N N   . VAL A 402  ? 0.2242 0.2002 0.3303 -0.0138 -0.0033 0.0781  400  VAL A N   
2887  C CA  . VAL A 402  ? 0.2342 0.2164 0.3454 -0.0158 -0.0032 0.0858  400  VAL A CA  
2888  C C   . VAL A 402  ? 0.2470 0.2343 0.3503 -0.0149 0.0001  0.0847  400  VAL A C   
2889  O O   . VAL A 402  ? 0.2534 0.2430 0.3608 -0.0163 -0.0003 0.0868  400  VAL A O   
2890  C CB  . VAL A 402  ? 0.2483 0.2363 0.3619 -0.0164 -0.0028 0.0942  400  VAL A CB  
2891  C CG1 . VAL A 402  ? 0.2504 0.2469 0.3680 -0.0182 -0.0021 0.1024  400  VAL A CG1 
2892  C CG2 . VAL A 402  ? 0.2877 0.2704 0.4113 -0.0175 -0.0067 0.0960  400  VAL A CG2 
2893  N N   . SER A 403  ? 0.2350 0.2243 0.3274 -0.0125 0.0033  0.0813  401  SER A N   
2894  C CA  . SER A 403  ? 0.2410 0.2344 0.3259 -0.0113 0.0062  0.0793  401  SER A CA  
2895  C C   . SER A 403  ? 0.2413 0.2301 0.3274 -0.0118 0.0050  0.0741  401  SER A C   
2896  O O   . SER A 403  ? 0.2182 0.2106 0.3047 -0.0123 0.0058  0.0754  401  SER A O   
2897  C CB  . SER A 403  ? 0.2148 0.2090 0.2887 -0.0086 0.0089  0.0752  401  SER A CB  
2898  O OG  . SER A 403  ? 0.2389 0.2361 0.3063 -0.0073 0.0113  0.0725  401  SER A OG  
2899  N N   . TYR A 404  ? 0.2347 0.2161 0.3215 -0.0115 0.0031  0.0681  402  TYR A N   
2900  C CA  . TYR A 404  ? 0.2326 0.2103 0.3202 -0.0119 0.0019  0.0628  402  TYR A CA  
2901  C C   . TYR A 404  ? 0.2394 0.2178 0.3370 -0.0143 -0.0004 0.0665  402  TYR A C   
2902  O O   . TYR A 404  ? 0.2120 0.1921 0.3092 -0.0147 0.0000  0.0656  402  TYR A O   
2903  C CB  . TYR A 404  ? 0.2317 0.2025 0.3190 -0.0112 0.0001  0.0561  402  TYR A CB  
2904  C CG  . TYR A 404  ? 0.2273 0.1953 0.3129 -0.0111 -0.0006 0.0496  402  TYR A CG  
2905  C CD1 . TYR A 404  ? 0.2358 0.2019 0.3295 -0.0128 -0.0034 0.0487  402  TYR A CD1 
2906  C CD2 . TYR A 404  ? 0.2245 0.1919 0.3006 -0.0094 0.0014  0.0444  402  TYR A CD2 
2907  C CE1 . TYR A 404  ? 0.2173 0.1817 0.3093 -0.0126 -0.0042 0.0428  402  TYR A CE1 
2908  C CE2 . TYR A 404  ? 0.2325 0.1983 0.3071 -0.0094 0.0006  0.0390  402  TYR A CE2 
2909  C CZ  . TYR A 404  ? 0.2156 0.1800 0.2979 -0.0109 -0.0021 0.0381  402  TYR A CZ  
2910  O OH  . TYR A 404  ? 0.2262 0.1897 0.3070 -0.0109 -0.0029 0.0328  402  TYR A OH  
2911  N N   . ILE A 405  ? 0.2352 0.2125 0.3423 -0.0160 -0.0030 0.0709  403  ILE A N   
2912  C CA  . ILE A 405  ? 0.2522 0.2296 0.3701 -0.0185 -0.0058 0.0745  403  ILE A CA  
2913  C C   . ILE A 405  ? 0.2272 0.2127 0.3451 -0.0194 -0.0038 0.0813  403  ILE A C   
2914  O O   . ILE A 405  ? 0.2408 0.2275 0.3628 -0.0208 -0.0046 0.0820  403  ILE A O   
2915  C CB  . ILE A 405  ? 0.2548 0.2285 0.3836 -0.0201 -0.0095 0.0776  403  ILE A CB  
2916  C CG1 . ILE A 405  ? 0.2531 0.2189 0.3828 -0.0191 -0.0119 0.0695  403  ILE A CG1 
2917  C CG2 . ILE A 405  ? 0.3014 0.2760 0.4423 -0.0230 -0.0125 0.0828  403  ILE A CG2 
2918  C CD1 . ILE A 405  ? 0.3215 0.2833 0.4608 -0.0198 -0.0153 0.0714  403  ILE A CD1 
2919  N N   . ALA A 406  ? 0.2307 0.2224 0.3439 -0.0186 -0.0011 0.0861  404  ALA A N   
2920  C CA  . ALA A 406  ? 0.2277 0.2285 0.3400 -0.0191 0.0013  0.0921  404  ALA A CA  
2921  C C   . ALA A 406  ? 0.2473 0.2495 0.3525 -0.0177 0.0035  0.0875  404  ALA A C   
2922  O O   . ALA A 406  ? 0.2481 0.2549 0.3564 -0.0188 0.0037  0.0904  404  ALA A O   
2923  C CB  . ALA A 406  ? 0.2796 0.2873 0.3868 -0.0179 0.0039  0.0967  404  ALA A CB  
2924  N N   . CYS A 407  ? 0.2433 0.2420 0.3393 -0.0153 0.0050  0.0805  405  CYS A N   
2925  C CA  . CYS A 407  ? 0.2077 0.2075 0.2972 -0.0139 0.0069  0.0762  405  CYS A CA  
2926  C C   . CYS A 407  ? 0.2332 0.2287 0.3276 -0.0153 0.0045  0.0729  405  CYS A C   
2927  O O   . CYS A 407  ? 0.2177 0.2159 0.3104 -0.0152 0.0054  0.0721  405  CYS A O   
2928  C CB  . CYS A 407  ? 0.2265 0.2235 0.3059 -0.0113 0.0087  0.0702  405  CYS A CB  
2929  S SG  . CYS A 407  ? 0.2581 0.2620 0.3306 -0.0092 0.0119  0.0734  405  CYS A SG  
2930  N N   . ALA A 408  ? 0.2169 0.2059 0.3175 -0.0166 0.0012  0.0707  406  ALA A N   
2931  C CA  . ALA A 408  ? 0.2241 0.2098 0.3305 -0.0181 -0.0015 0.0677  406  ALA A CA  
2932  C C   . ALA A 408  ? 0.1892 0.1792 0.3042 -0.0204 -0.0025 0.0740  406  ALA A C   
2933  O O   . ALA A 408  ? 0.2377 0.2281 0.3545 -0.0211 -0.0033 0.0724  406  ALA A O   
2934  C CB  . ALA A 408  ? 0.2756 0.2540 0.3875 -0.0186 -0.0049 0.0636  406  ALA A CB  
2935  N N   . ALA A 409  ? 0.2271 0.2207 0.3478 -0.0217 -0.0028 0.0813  407  ALA A N   
2936  C CA  . ALA A 409  ? 0.2320 0.2310 0.3608 -0.0241 -0.0036 0.0882  407  ALA A CA  
2937  C C   . ALA A 409  ? 0.2258 0.2322 0.3485 -0.0230 -0.0003 0.0895  407  ALA A C   
2938  O O   . ALA A 409  ? 0.2203 0.2293 0.3477 -0.0245 -0.0010 0.0912  407  ALA A O   
2939  C CB  . ALA A 409  ? 0.2459 0.2485 0.3813 -0.0256 -0.0043 0.0966  407  ALA A CB  
2940  N N   . LYS A 410  ? 0.2303 0.2402 0.3428 -0.0204 0.0033  0.0883  408  LYS A N   
2941  C CA  . LYS A 410  ? 0.2347 0.2514 0.3414 -0.0190 0.0064  0.0885  408  LYS A CA  
2942  C C   . LYS A 410  ? 0.2154 0.2282 0.3195 -0.0184 0.0059  0.0822  408  LYS A C   
2943  O O   . LYS A 410  ? 0.2186 0.2357 0.3243 -0.0189 0.0064  0.0836  408  LYS A O   
2944  C CB  . LYS A 410  ? 0.2198 0.2401 0.3165 -0.0161 0.0098  0.0876  408  LYS A CB  
2945  C CG  . LYS A 410  ? 0.2495 0.2770 0.3403 -0.0141 0.0128  0.0872  408  LYS A CG  
2946  C CD  . LYS A 410  ? 0.2387 0.2688 0.3201 -0.0111 0.0157  0.0851  408  LYS A CD  
2947  C CE  . LYS A 410  ? 0.2486 0.2844 0.3311 -0.0113 0.0165  0.0909  408  LYS A CE  
2948  N NZ  . LYS A 410  ? 0.2467 0.2938 0.3330 -0.0120 0.0179  0.0979  408  LYS A NZ  
2949  N N   . LEU A 411  ? 0.1987 0.2040 0.2987 -0.0175 0.0049  0.0754  409  LEU A N   
2950  C CA  . LEU A 411  ? 0.2070 0.2090 0.3046 -0.0170 0.0043  0.0696  409  LEU A CA  
2951  C C   . LEU A 411  ? 0.2027 0.2036 0.3096 -0.0196 0.0012  0.0704  409  LEU A C   
2952  O O   . LEU A 411  ? 0.2090 0.2118 0.3157 -0.0197 0.0013  0.0692  409  LEU A O   
2953  C CB  . LEU A 411  ? 0.2097 0.2048 0.3019 -0.0158 0.0037  0.0627  409  LEU A CB  
2954  C CG  . LEU A 411  ? 0.2050 0.2008 0.2869 -0.0130 0.0066  0.0602  409  LEU A CG  
2955  C CD1 . LEU A 411  ? 0.2305 0.2198 0.3088 -0.0123 0.0057  0.0548  409  LEU A CD1 
2956  C CD2 . LEU A 411  ? 0.2102 0.2087 0.2865 -0.0116 0.0084  0.0580  409  LEU A CD2 
2957  N N   . LEU A 412  ? 0.2190 0.2166 0.3347 -0.0217 -0.0018 0.0723  410  LEU A N   
2958  C CA  . LEU A 412  ? 0.2133 0.2091 0.3385 -0.0241 -0.0052 0.0724  410  LEU A CA  
2959  C C   . LEU A 412  ? 0.2136 0.2164 0.3442 -0.0258 -0.0047 0.0790  410  LEU A C   
2960  O O   . LEU A 412  ? 0.2533 0.2557 0.3905 -0.0275 -0.0071 0.0787  410  LEU A O   
2961  C CB  . LEU A 412  ? 0.2466 0.2369 0.3808 -0.0258 -0.0089 0.0725  410  LEU A CB  
2962  C CG  . LEU A 412  ? 0.2227 0.2058 0.3536 -0.0245 -0.0104 0.0642  410  LEU A CG  
2963  C CD1 . LEU A 412  ? 0.2617 0.2398 0.4013 -0.0256 -0.0138 0.0645  410  LEU A CD1 
2964  C CD2 . LEU A 412  ? 0.2489 0.2301 0.3798 -0.0246 -0.0120 0.0581  410  LEU A CD2 
2965  N N   . ALA A 413  ? 0.2212 0.2312 0.3493 -0.0251 -0.0018 0.0849  411  ALA A N   
2966  C CA  . ALA A 413  ? 0.2231 0.2413 0.3551 -0.0263 -0.0007 0.0910  411  ALA A CA  
2967  C C   . ALA A 413  ? 0.2614 0.2832 0.3863 -0.0244 0.0018  0.0881  411  ALA A C   
2968  O O   . ALA A 413  ? 0.2482 0.2771 0.3762 -0.0252 0.0026  0.0923  411  ALA A O   
2969  C CB  . ALA A 413  ? 0.2349 0.2605 0.3673 -0.0264 0.0014  0.0986  411  ALA A CB  
2970  N N   . ALA A 414  ? 0.2459 0.2636 0.3619 -0.0220 0.0028  0.0811  412  ALA A N   
2971  C CA  . ALA A 414  ? 0.2547 0.2755 0.3640 -0.0200 0.0051  0.0784  412  ALA A CA  
2972  C C   . ALA A 414  ? 0.2603 0.2750 0.3672 -0.0197 0.0034  0.0714  412  ALA A C   
2973  O O   . ALA A 414  ? 0.2152 0.2300 0.3145 -0.0176 0.0051  0.0676  412  ALA A O   
2974  C CB  . ALA A 414  ? 0.2692 0.2929 0.3691 -0.0170 0.0086  0.0776  412  ALA A CB  
2975  N N   . THR A 415  ? 0.2513 0.2609 0.3648 -0.0219 -0.0001 0.0695  413  THR A N   
2976  C CA  . THR A 415  ? 0.2557 0.2606 0.3667 -0.0216 -0.0017 0.0627  413  THR A CA  
2977  C C   . THR A 415  ? 0.2393 0.2480 0.3495 -0.0214 -0.0013 0.0622  413  THR A C   
2978  O O   . THR A 415  ? 0.2593 0.2655 0.3655 -0.0207 -0.0020 0.0569  413  THR A O   
2979  C CB  . THR A 415  ? 0.2771 0.2765 0.3960 -0.0237 -0.0058 0.0603  413  THR A CB  
2980  O OG1 . THR A 415  ? 0.2823 0.2842 0.4116 -0.0263 -0.0078 0.0651  413  THR A OG1 
2981  C CG2 . THR A 415  ? 0.2582 0.2531 0.3777 -0.0235 -0.0065 0.0596  413  THR A CG2 
2982  N N   . ASP A 416  ? 0.2387 0.2538 0.3525 -0.0220 -0.0001 0.0677  414  ASP A N   
2983  C CA  . ASP A 416  ? 0.2300 0.2490 0.3424 -0.0215 0.0005  0.0671  414  ASP A CA  
2984  C C   . ASP A 416  ? 0.2553 0.2758 0.3579 -0.0184 0.0035  0.0645  414  ASP A C   
2985  O O   . ASP A 416  ? 0.2835 0.3044 0.3833 -0.0176 0.0035  0.0618  414  ASP A O   
2986  C CB  . ASP A 416  ? 0.2985 0.3248 0.4179 -0.0230 0.0009  0.0737  414  ASP A CB  
2987  C CG  . ASP A 416  ? 0.3330 0.3653 0.4509 -0.0220 0.0039  0.0790  414  ASP A CG  
2988  O OD1 . ASP A 416  ? 0.3093 0.3391 0.4244 -0.0213 0.0045  0.0789  414  ASP A OD1 
2989  O OD2 . ASP A 416  ? 0.3983 0.4385 0.5180 -0.0218 0.0056  0.0833  414  ASP A OD2 
2990  N N   . VAL A 417  ? 0.2370 0.2578 0.3343 -0.0166 0.0058  0.0652  415  VAL A N   
2991  C CA  . VAL A 417  ? 0.2442 0.2667 0.3330 -0.0135 0.0085  0.0630  415  VAL A CA  
2992  C C   . VAL A 417  ? 0.2093 0.2258 0.2911 -0.0121 0.0087  0.0583  415  VAL A C   
2993  O O   . VAL A 417  ? 0.2379 0.2542 0.3132 -0.0098 0.0100  0.0555  415  VAL A O   
2994  C CB  . VAL A 417  ? 0.2753 0.3053 0.3633 -0.0120 0.0114  0.0675  415  VAL A CB  
2995  C CG1 . VAL A 417  ? 0.3178 0.3548 0.4120 -0.0132 0.0114  0.0718  415  VAL A CG1 
2996  C CG2 . VAL A 417  ? 0.2494 0.2793 0.3384 -0.0126 0.0118  0.0705  415  VAL A CG2 
2997  N N   . VAL A 418  ? 0.2027 0.2142 0.2860 -0.0132 0.0072  0.0574  416  VAL A N   
2998  C CA  . VAL A 418  ? 0.2000 0.2060 0.2772 -0.0121 0.0072  0.0527  416  VAL A CA  
2999  C C   . VAL A 418  ? 0.2008 0.2014 0.2819 -0.0140 0.0041  0.0496  416  VAL A C   
3000  O O   . VAL A 418  ? 0.2158 0.2165 0.3047 -0.0161 0.0020  0.0516  416  VAL A O   
3001  C CB  . VAL A 418  ? 0.1909 0.1968 0.2645 -0.0108 0.0090  0.0540  416  VAL A CB  
3002  C CG1 . VAL A 418  ? 0.2385 0.2501 0.3078 -0.0084 0.0120  0.0559  416  VAL A CG1 
3003  C CG2 . VAL A 418  ? 0.1984 0.2045 0.2786 -0.0126 0.0080  0.0580  416  VAL A CG2 
3004  N N   . PHE A 419  ? 0.1818 0.1782 0.2576 -0.0131 0.0037  0.0447  417  PHE A N   
3005  C CA  . PHE A 419  ? 0.2143 0.2062 0.2927 -0.0144 0.0010  0.0406  417  PHE A CA  
3006  C C   . PHE A 419  ? 0.1794 0.1677 0.2559 -0.0138 0.0012  0.0396  417  PHE A C   
3007  O O   . PHE A 419  ? 0.1960 0.1828 0.2654 -0.0122 0.0026  0.0370  417  PHE A O   
3008  C CB  . PHE A 419  ? 0.2149 0.2059 0.2886 -0.0139 0.0003  0.0357  417  PHE A CB  
3009  C CG  . PHE A 419  ? 0.2167 0.2043 0.2922 -0.0148 -0.0024 0.0308  417  PHE A CG  
3010  C CD1 . PHE A 419  ? 0.2156 0.2024 0.2994 -0.0167 -0.0053 0.0303  417  PHE A CD1 
3011  C CD2 . PHE A 419  ? 0.2250 0.2107 0.2943 -0.0137 -0.0021 0.0265  417  PHE A CD2 
3012  C CE1 . PHE A 419  ? 0.2331 0.2172 0.3188 -0.0172 -0.0079 0.0250  417  PHE A CE1 
3013  C CE2 . PHE A 419  ? 0.2030 0.1866 0.2738 -0.0143 -0.0045 0.0216  417  PHE A CE2 
3014  C CZ  . PHE A 419  ? 0.2002 0.1831 0.2791 -0.0160 -0.0074 0.0206  417  PHE A CZ  
3015  N N   . PRO A 420  ? 0.1827 0.1696 0.2658 -0.0151 -0.0002 0.0419  418  PRO A N   
3016  C CA  . PRO A 420  ? 0.1978 0.1815 0.2796 -0.0145 0.0000  0.0412  418  PRO A CA  
3017  C C   . PRO A 420  ? 0.2048 0.1841 0.2852 -0.0143 -0.0019 0.0349  418  PRO A C   
3018  O O   . PRO A 420  ? 0.2207 0.1989 0.3055 -0.0155 -0.0044 0.0318  418  PRO A O   
3019  C CB  . PRO A 420  ? 0.1720 0.1559 0.2628 -0.0162 -0.0014 0.0460  418  PRO A CB  
3020  C CG  . PRO A 420  ? 0.1895 0.1783 0.2845 -0.0174 -0.0012 0.0505  418  PRO A CG  
3021  C CD  . PRO A 420  ? 0.1873 0.1762 0.2796 -0.0172 -0.0017 0.0463  418  PRO A CD  
3022  N N   . GLN A 421  ? 0.1896 0.1670 0.2641 -0.0129 -0.0006 0.0330  419  GLN A N   
3023  C CA  . GLN A 421  ? 0.1862 0.1605 0.2586 -0.0124 -0.0019 0.0271  419  GLN A CA  
3024  C C   . GLN A 421  ? 0.2028 0.1744 0.2756 -0.0119 -0.0017 0.0275  419  GLN A C   
3025  O O   . GLN A 421  ? 0.2076 0.1797 0.2746 -0.0106 0.0007  0.0291  419  GLN A O   
3026  C CB  . GLN A 421  ? 0.1799 0.1553 0.2435 -0.0111 -0.0003 0.0241  419  GLN A CB  
3027  C CG  . GLN A 421  ? 0.1815 0.1598 0.2446 -0.0116 -0.0004 0.0241  419  GLN A CG  
3028  C CD  . GLN A 421  ? 0.2219 0.2016 0.2767 -0.0102 0.0015  0.0230  419  GLN A CD  
3029  O OE1 . GLN A 421  ? 0.2211 0.2013 0.2717 -0.0089 0.0037  0.0253  419  GLN A OE1 
3030  N NE2 . GLN A 421  ? 0.1968 0.1775 0.2497 -0.0105 0.0004  0.0195  419  GLN A NE2 
3031  N N   . PHE A 422  ? 0.1946 0.1634 0.2747 -0.0128 -0.0045 0.0261  420  PHE A N   
3032  C CA  . PHE A 422  ? 0.1856 0.1519 0.2679 -0.0125 -0.0047 0.0276  420  PHE A CA  
3033  C C   . PHE A 422  ? 0.1961 0.1598 0.2747 -0.0113 -0.0052 0.0216  420  PHE A C   
3034  O O   . PHE A 422  ? 0.2329 0.1946 0.3161 -0.0117 -0.0079 0.0169  420  PHE A O   
3035  C CB  . PHE A 422  ? 0.2013 0.1660 0.2948 -0.0143 -0.0076 0.0304  420  PHE A CB  
3036  C CG  . PHE A 422  ? 0.2228 0.1909 0.3202 -0.0156 -0.0071 0.0368  420  PHE A CG  
3037  C CD1 . PHE A 422  ? 0.2332 0.2046 0.3276 -0.0152 -0.0043 0.0427  420  PHE A CD1 
3038  C CD2 . PHE A 422  ? 0.2157 0.1845 0.3197 -0.0173 -0.0092 0.0368  420  PHE A CD2 
3039  C CE1 . PHE A 422  ? 0.2379 0.2136 0.3358 -0.0163 -0.0037 0.0486  420  PHE A CE1 
3040  C CE2 . PHE A 422  ? 0.2441 0.2166 0.3519 -0.0186 -0.0087 0.0430  420  PHE A CE2 
3041  C CZ  . PHE A 422  ? 0.2225 0.1988 0.3271 -0.0181 -0.0058 0.0489  420  PHE A CZ  
3042  N N   . ALA A 423  ? 0.2092 0.1734 0.2797 -0.0098 -0.0026 0.0216  421  ALA A N   
3043  C CA  . ALA A 423  ? 0.1885 0.1512 0.2542 -0.0087 -0.0025 0.0165  421  ALA A CA  
3044  C C   . ALA A 423  ? 0.2423 0.2022 0.3117 -0.0083 -0.0034 0.0171  421  ALA A C   
3045  O O   . ALA A 423  ? 0.2710 0.2311 0.3385 -0.0079 -0.0017 0.0213  421  ALA A O   
3046  C CB  . ALA A 423  ? 0.2137 0.1782 0.2697 -0.0074 0.0004  0.0166  421  ALA A CB  
3047  N N   . THR A 424  ? 0.2174 0.1750 0.2925 -0.0085 -0.0061 0.0129  422  THR A N   
3048  C CA  . THR A 424  ? 0.2311 0.1858 0.3103 -0.0081 -0.0073 0.0131  422  THR A CA  
3049  C C   . THR A 424  ? 0.2398 0.1927 0.3232 -0.0077 -0.0101 0.0062  422  THR A C   
3050  O O   . THR A 424  ? 0.2430 0.1964 0.3300 -0.0083 -0.0122 0.0026  422  THR A O   
3051  C CB  . THR A 424  ? 0.2479 0.2016 0.3354 -0.0094 -0.0085 0.0193  422  THR A CB  
3052  O OG1 . THR A 424  ? 0.2505 0.2016 0.3414 -0.0088 -0.0095 0.0200  422  THR A OG1 
3053  C CG2 . THR A 424  ? 0.2614 0.2141 0.3585 -0.0109 -0.0118 0.0186  422  THR A CG2 
3054  N N   . HIS A 425  ? 0.2461 0.1972 0.3293 -0.0065 -0.0104 0.0042  423  HIS A N   
3055  C CA  . HIS A 425  ? 0.2292 0.1786 0.3179 -0.0058 -0.0133 -0.0021 423  HIS A CA  
3056  C C   . HIS A 425  ? 0.2839 0.2295 0.3830 -0.0061 -0.0161 0.0000  423  HIS A C   
3057  O O   . HIS A 425  ? 0.3005 0.2442 0.4050 -0.0053 -0.0187 -0.0051 423  HIS A O   
3058  C CB  . HIS A 425  ? 0.2551 0.2058 0.3366 -0.0041 -0.0119 -0.0067 423  HIS A CB  
3059  C CG  . HIS A 425  ? 0.3035 0.2581 0.3754 -0.0039 -0.0094 -0.0084 423  HIS A CG  
3060  N ND1 . HIS A 425  ? 0.4173 0.3730 0.4802 -0.0034 -0.0062 -0.0057 423  HIS A ND1 
3061  C CD2 . HIS A 425  ? 0.3009 0.2584 0.3709 -0.0042 -0.0099 -0.0122 423  HIS A CD2 
3062  C CE1 . HIS A 425  ? 0.3856 0.3447 0.4422 -0.0035 -0.0050 -0.0075 423  HIS A CE1 
3063  N NE2 . HIS A 425  ? 0.2916 0.2520 0.3520 -0.0040 -0.0071 -0.0114 423  HIS A NE2 
3064  N N   . ASN A 426  ? 0.2701 0.2149 0.3722 -0.0073 -0.0156 0.0075  424  ASN A N   
3065  C CA  . ASN A 426  ? 0.2637 0.2053 0.3757 -0.0079 -0.0181 0.0112  424  ASN A CA  
3066  C C   . ASN A 426  ? 0.2854 0.2254 0.4087 -0.0095 -0.0218 0.0113  424  ASN A C   
3067  O O   . ASN A 426  ? 0.2666 0.2083 0.3909 -0.0111 -0.0213 0.0157  424  ASN A O   
3068  C CB  . ASN A 426  ? 0.2817 0.2248 0.3909 -0.0084 -0.0156 0.0196  424  ASN A CB  
3069  C CG  . ASN A 426  ? 0.2630 0.2035 0.3818 -0.0091 -0.0180 0.0244  424  ASN A CG  
3070  O OD1 . ASN A 426  ? 0.2824 0.2204 0.4124 -0.0103 -0.0217 0.0246  424  ASN A OD1 
3071  N ND2 . ASN A 426  ? 0.2594 0.2008 0.3743 -0.0085 -0.0161 0.0285  424  ASN A ND2 
3072  N N   . ALA A 427  ? 0.2372 0.1739 0.3696 -0.0091 -0.0258 0.0062  425  ALA A N   
3073  C CA  . ALA A 427  ? 0.2936 0.2284 0.4375 -0.0105 -0.0298 0.0052  425  ALA A CA  
3074  C C   . ALA A 427  ? 0.2577 0.1914 0.4101 -0.0127 -0.0311 0.0145  425  ALA A C   
3075  O O   . ALA A 427  ? 0.2625 0.1960 0.4220 -0.0145 -0.0332 0.0160  425  ALA A O   
3076  C CB  . ALA A 427  ? 0.3179 0.2494 0.4705 -0.0093 -0.0341 -0.0024 425  ALA A CB  
3077  N N   . GLN A 428  ? 0.2750 0.2083 0.4271 -0.0128 -0.0298 0.0207  426  GLN A N   
3078  C CA  . GLN A 428  ? 0.2977 0.2314 0.4573 -0.0150 -0.0307 0.0303  426  GLN A CA  
3079  C C   . GLN A 428  ? 0.2736 0.2122 0.4263 -0.0161 -0.0272 0.0357  426  GLN A C   
3080  O O   . GLN A 428  ? 0.2679 0.2075 0.4276 -0.0183 -0.0286 0.0408  426  GLN A O   
3081  C CB  . GLN A 428  ? 0.2700 0.2030 0.4302 -0.0145 -0.0302 0.0355  426  GLN A CB  
3082  C CG  . GLN A 428  ? 0.3042 0.2371 0.4753 -0.0169 -0.0324 0.0452  426  GLN A CG  
3083  C CD  . GLN A 428  ? 0.3395 0.2783 0.5059 -0.0185 -0.0292 0.0534  426  GLN A CD  
3084  O OE1 . GLN A 428  ? 0.3610 0.3038 0.5150 -0.0173 -0.0247 0.0537  426  GLN A OE1 
3085  N NE2 . GLN A 428  ? 0.3091 0.2486 0.4859 -0.0210 -0.0316 0.0599  426  GLN A NE2 
3086  N N   . THR A 429  ? 0.2850 0.2268 0.4243 -0.0147 -0.0228 0.0347  427  THR A N   
3087  C CA  . THR A 429  ? 0.2491 0.1957 0.3814 -0.0153 -0.0195 0.0384  427  THR A CA  
3088  C C   . THR A 429  ? 0.2465 0.1934 0.3817 -0.0163 -0.0210 0.0352  427  THR A C   
3089  O O   . THR A 429  ? 0.2473 0.1968 0.3856 -0.0180 -0.0208 0.0404  427  THR A O   
3090  C CB  . THR A 429  ? 0.2544 0.2034 0.3728 -0.0133 -0.0153 0.0360  427  THR A CB  
3091  O OG1 . THR A 429  ? 0.2730 0.2213 0.3891 -0.0122 -0.0143 0.0377  427  THR A OG1 
3092  C CG2 . THR A 429  ? 0.2650 0.2190 0.3768 -0.0137 -0.0119 0.0406  427  THR A CG2 
3093  N N   . LEU A 430  ? 0.2169 0.1616 0.3511 -0.0152 -0.0224 0.0267  428  LEU A N   
3094  C CA  . LEU A 430  ? 0.2340 0.1794 0.3706 -0.0160 -0.0240 0.0227  428  LEU A CA  
3095  C C   . LEU A 430  ? 0.2595 0.2031 0.4097 -0.0183 -0.0280 0.0261  428  LEU A C   
3096  O O   . LEU A 430  ? 0.2632 0.2093 0.4153 -0.0199 -0.0279 0.0290  428  LEU A O   
3097  C CB  . LEU A 430  ? 0.2429 0.1869 0.3774 -0.0144 -0.0254 0.0128  428  LEU A CB  
3098  C CG  . LEU A 430  ? 0.2721 0.2179 0.4057 -0.0146 -0.0265 0.0070  428  LEU A CG  
3099  C CD1 . LEU A 430  ? 0.3266 0.2728 0.4549 -0.0125 -0.0265 -0.0018 428  LEU A CD1 
3100  C CD2 . LEU A 430  ? 0.2932 0.2370 0.4397 -0.0162 -0.0310 0.0061  428  LEU A CD2 
3101  N N   . ALA A 431  ? 0.2488 0.1882 0.4093 -0.0185 -0.0316 0.0257  429  ALA A N   
3102  C CA  . ALA A 431  ? 0.2800 0.2172 0.4551 -0.0208 -0.0361 0.0286  429  ALA A CA  
3103  C C   . ALA A 431  ? 0.2655 0.2059 0.4430 -0.0230 -0.0348 0.0394  429  ALA A C   
3104  O O   . ALA A 431  ? 0.2634 0.2047 0.4484 -0.0251 -0.0367 0.0421  429  ALA A O   
3105  C CB  . ALA A 431  ? 0.2615 0.1934 0.4470 -0.0204 -0.0402 0.0270  429  ALA A CB  
3106  N N   . ALA A 432  ? 0.2724 0.2153 0.4437 -0.0226 -0.0314 0.0454  430  ALA A N   
3107  C CA  . ALA A 432  ? 0.2634 0.2109 0.4366 -0.0246 -0.0299 0.0557  430  ALA A CA  
3108  C C   . ALA A 432  ? 0.2696 0.2219 0.4372 -0.0252 -0.0274 0.0566  430  ALA A C   
3109  O O   . ALA A 432  ? 0.2827 0.2379 0.4569 -0.0274 -0.0282 0.0629  430  ALA A O   
3110  C CB  . ALA A 432  ? 0.2619 0.2121 0.4280 -0.0235 -0.0265 0.0607  430  ALA A CB  
3111  N N   . ILE A 433  ? 0.2657 0.2191 0.4217 -0.0232 -0.0245 0.0505  431  ILE A N   
3112  C CA  . ILE A 433  ? 0.2464 0.2042 0.3968 -0.0235 -0.0221 0.0511  431  ILE A CA  
3113  C C   . ILE A 433  ? 0.2680 0.2242 0.4256 -0.0248 -0.0255 0.0471  431  ILE A C   
3114  O O   . ILE A 433  ? 0.2735 0.2331 0.4335 -0.0263 -0.0253 0.0507  431  ILE A O   
3115  C CB  . ILE A 433  ? 0.2547 0.2141 0.3907 -0.0210 -0.0181 0.0465  431  ILE A CB  
3116  C CG1 . ILE A 433  ? 0.2594 0.2215 0.3888 -0.0200 -0.0147 0.0515  431  ILE A CG1 
3117  C CG2 . ILE A 433  ? 0.2798 0.2428 0.4108 -0.0211 -0.0165 0.0453  431  ILE A CG2 
3118  C CD1 . ILE A 433  ? 0.2972 0.2598 0.4141 -0.0176 -0.0115 0.0470  431  ILE A CD1 
3119  N N   . TYR A 434  ? 0.2635 0.2150 0.4248 -0.0241 -0.0287 0.0394  432  TYR A N   
3120  C CA  . TYR A 434  ? 0.2897 0.2396 0.4587 -0.0252 -0.0325 0.0349  432  TYR A CA  
3121  C C   . TYR A 434  ? 0.2863 0.2361 0.4687 -0.0282 -0.0356 0.0416  432  TYR A C   
3122  O O   . TYR A 434  ? 0.2949 0.2467 0.4808 -0.0297 -0.0366 0.0422  432  TYR A O   
3123  C CB  . TYR A 434  ? 0.2782 0.2234 0.4507 -0.0238 -0.0357 0.0258  432  TYR A CB  
3124  C CG  . TYR A 434  ? 0.2900 0.2331 0.4732 -0.0250 -0.0406 0.0209  432  TYR A CG  
3125  C CD1 . TYR A 434  ? 0.2876 0.2334 0.4673 -0.0251 -0.0405 0.0166  432  TYR A CD1 
3126  C CD2 . TYR A 434  ? 0.3255 0.2638 0.5225 -0.0259 -0.0456 0.0204  432  TYR A CD2 
3127  C CE1 . TYR A 434  ? 0.3144 0.2587 0.5040 -0.0260 -0.0451 0.0117  432  TYR A CE1 
3128  C CE2 . TYR A 434  ? 0.3066 0.2429 0.5141 -0.0268 -0.0504 0.0153  432  TYR A CE2 
3129  C CZ  . TYR A 434  ? 0.3533 0.2927 0.5568 -0.0268 -0.0501 0.0108  432  TYR A CZ  
3130  O OH  . TYR A 434  ? 0.3678 0.3056 0.5816 -0.0277 -0.0550 0.0054  432  TYR A OH  
3131  N N   . HIS A 435  ? 0.2804 0.2282 0.4707 -0.0291 -0.0372 0.0473  433  HIS A N   
3132  C CA  . HIS A 435  ? 0.3010 0.2492 0.5047 -0.0322 -0.0403 0.0548  433  HIS A CA  
3133  C C   . HIS A 435  ? 0.3018 0.2568 0.5017 -0.0335 -0.0367 0.0642  433  HIS A C   
3134  O O   . HIS A 435  ? 0.2945 0.2518 0.5027 -0.0360 -0.0384 0.0693  433  HIS A O   
3135  C CB  . HIS A 435  ? 0.2876 0.2314 0.5023 -0.0329 -0.0438 0.0578  433  HIS A CB  
3136  C CG  . HIS A 435  ? 0.3450 0.2822 0.5677 -0.0321 -0.0487 0.0490  433  HIS A CG  
3137  N ND1 . HIS A 435  ? 0.3366 0.2709 0.5728 -0.0339 -0.0539 0.0472  433  HIS A ND1 
3138  C CD2 . HIS A 435  ? 0.3317 0.2652 0.5506 -0.0295 -0.0491 0.0409  433  HIS A CD2 
3139  C CE1 . HIS A 435  ? 0.3673 0.2963 0.6080 -0.0323 -0.0575 0.0380  433  HIS A CE1 
3140  N NE2 . HIS A 435  ? 0.3471 0.2758 0.5774 -0.0296 -0.0546 0.0341  433  HIS A NE2 
3141  N N   . MET A 436  ? 0.3113 0.2700 0.4990 -0.0318 -0.0318 0.0662  434  MET A N   
3142  C CA  . MET A 436  ? 0.2908 0.2570 0.4740 -0.0325 -0.0281 0.0740  434  MET A CA  
3143  C C   . MET A 436  ? 0.2588 0.2282 0.4390 -0.0329 -0.0271 0.0719  434  MET A C   
3144  O O   . MET A 436  ? 0.3096 0.2843 0.4930 -0.0346 -0.0263 0.0786  434  MET A O   
3145  C CB  . MET A 436  ? 0.2696 0.2388 0.4399 -0.0301 -0.0233 0.0748  434  MET A CB  
3146  C CG  . MET A 436  ? 0.2763 0.2539 0.4415 -0.0304 -0.0193 0.0820  434  MET A CG  
3147  S SD  . MET A 436  ? 0.3068 0.2874 0.4565 -0.0272 -0.0141 0.0810  434  MET A SD  
3148  C CE  . MET A 436  ? 0.2719 0.2505 0.4265 -0.0275 -0.0155 0.0853  434  MET A CE  
3149  N N   . ALA A 437  ? 0.2636 0.2303 0.4376 -0.0311 -0.0270 0.0629  435  ALA A N   
3150  C CA  . ALA A 437  ? 0.2911 0.2608 0.4613 -0.0312 -0.0260 0.0605  435  ALA A CA  
3151  C C   . ALA A 437  ? 0.3504 0.3191 0.5330 -0.0338 -0.0303 0.0609  435  ALA A C   
3152  O O   . ALA A 437  ? 0.3122 0.2847 0.4939 -0.0345 -0.0295 0.0616  435  ALA A O   
3153  C CB  . ALA A 437  ? 0.2808 0.2484 0.4410 -0.0288 -0.0248 0.0512  435  ALA A CB  
3154  N N   . GLY A 438  ? 0.3424 0.3061 0.5368 -0.0352 -0.0349 0.0603  436  GLY A N   
3155  C CA  . GLY A 438  ? 0.3805 0.3433 0.5883 -0.0379 -0.0394 0.0617  436  GLY A CA  
3156  C C   . GLY A 438  ? 0.4099 0.3701 0.6183 -0.0374 -0.0419 0.0522  436  GLY A C   
3157  O O   . GLY A 438  ? 0.4109 0.3701 0.6098 -0.0349 -0.0406 0.0444  436  GLY A O   
3158  N N   . LYS A 439  ? 0.4581 0.4182 0.6781 -0.0399 -0.0458 0.0535  437  LYS A N   
3159  C CA  . LYS A 439  ? 0.4590 0.4162 0.6830 -0.0398 -0.0496 0.0445  437  LYS A CA  
3160  C C   . LYS A 439  ? 0.4391 0.4010 0.6539 -0.0391 -0.0471 0.0413  437  LYS A C   
3161  O O   . LYS A 439  ? 0.5035 0.4642 0.7156 -0.0378 -0.0486 0.0323  437  LYS A O   
3162  C CB  . LYS A 439  ? 0.5418 0.4966 0.7834 -0.0429 -0.0554 0.0470  437  LYS A CB  
3163  N N   . ASP A 440  ? 0.4405 0.4081 0.6505 -0.0398 -0.0434 0.0483  438  ASP A N   
3164  C CA  . ASP A 440  ? 0.4563 0.4282 0.6578 -0.0390 -0.0411 0.0456  438  ASP A CA  
3165  C C   . ASP A 440  ? 0.4557 0.4279 0.6424 -0.0358 -0.0373 0.0403  438  ASP A C   
3166  O O   . ASP A 440  ? 0.4330 0.4065 0.6121 -0.0345 -0.0334 0.0441  438  ASP A O   
3167  C CB  . ASP A 440  ? 0.4676 0.4459 0.6687 -0.0404 -0.0382 0.0545  438  ASP A CB  
3168  C CG  . ASP A 440  ? 0.5053 0.4842 0.7211 -0.0438 -0.0420 0.0602  438  ASP A CG  
3169  O OD1 . ASP A 440  ? 0.4820 0.4559 0.7087 -0.0451 -0.0471 0.0569  438  ASP A OD1 
3170  O OD2 . ASP A 440  ? 0.4627 0.4475 0.6796 -0.0452 -0.0399 0.0680  438  ASP A OD2 
3171  N N   . PHE A 441  ? 0.4104 0.3818 0.5933 -0.0346 -0.0385 0.0317  439  PHE A N   
3172  C CA  . PHE A 441  ? 0.3694 0.3419 0.5386 -0.0319 -0.0350 0.0271  439  PHE A CA  
3173  C C   . PHE A 441  ? 0.3850 0.3607 0.5493 -0.0315 -0.0352 0.0220  439  PHE A C   
3174  O O   . PHE A 441  ? 0.3474 0.3228 0.5189 -0.0326 -0.0390 0.0180  439  PHE A O   
3175  C CB  . PHE A 441  ? 0.3346 0.3027 0.5020 -0.0302 -0.0361 0.0209  439  PHE A CB  
3176  C CG  . PHE A 441  ? 0.3619 0.3315 0.5155 -0.0276 -0.0324 0.0172  439  PHE A CG  
3177  C CD1 . PHE A 441  ? 0.3373 0.3078 0.4831 -0.0265 -0.0282 0.0220  439  PHE A CD1 
3178  C CD2 . PHE A 441  ? 0.3150 0.2859 0.4635 -0.0264 -0.0332 0.0094  439  PHE A CD2 
3179  C CE1 . PHE A 441  ? 0.2830 0.2547 0.4167 -0.0243 -0.0251 0.0190  439  PHE A CE1 
3180  C CE2 . PHE A 441  ? 0.3345 0.3073 0.4708 -0.0244 -0.0298 0.0069  439  PHE A CE2 
3181  C CZ  . PHE A 441  ? 0.3045 0.2773 0.4337 -0.0234 -0.0259 0.0117  439  PHE A CZ  
3182  N N   . HIS A 442  ? 0.3392 0.3181 0.4916 -0.0298 -0.0311 0.0223  440  HIS A N   
3183  C CA  . HIS A 442  ? 0.3388 0.3208 0.4845 -0.0289 -0.0307 0.0172  440  HIS A CA  
3184  C C   . HIS A 442  ? 0.3459 0.3284 0.4791 -0.0265 -0.0271 0.0154  440  HIS A C   
3185  O O   . HIS A 442  ? 0.2850 0.2669 0.4140 -0.0257 -0.0240 0.0199  440  HIS A O   
3186  C CB  . HIS A 442  ? 0.3443 0.3308 0.4904 -0.0300 -0.0298 0.0216  440  HIS A CB  
3187  C CG  . HIS A 442  ? 0.3304 0.3193 0.4727 -0.0297 -0.0258 0.0294  440  HIS A CG  
3188  N ND1 . HIS A 442  ? 0.3258 0.3173 0.4572 -0.0278 -0.0219 0.0301  440  HIS A ND1 
3189  C CD2 . HIS A 442  ? 0.3132 0.3027 0.4613 -0.0310 -0.0252 0.0366  440  HIS A CD2 
3190  C CE1 . HIS A 442  ? 0.3147 0.3084 0.4453 -0.0277 -0.0191 0.0368  440  HIS A CE1 
3191  N NE2 . HIS A 442  ? 0.3547 0.3477 0.4951 -0.0296 -0.0209 0.0410  440  HIS A NE2 
3192  N N   . VAL A 443  ? 0.3349 0.3190 0.4623 -0.0254 -0.0276 0.0089  441  VAL A N   
3193  C CA  . VAL A 443  ? 0.3705 0.3555 0.4863 -0.0234 -0.0243 0.0075  441  VAL A CA  
3194  C C   . VAL A 443  ? 0.2977 0.2856 0.4077 -0.0230 -0.0207 0.0135  441  VAL A C   
3195  O O   . VAL A 443  ? 0.3333 0.3245 0.4447 -0.0239 -0.0210 0.0152  441  VAL A O   
3196  C CB  . VAL A 443  ? 0.3959 0.3835 0.5072 -0.0226 -0.0257 0.0001  441  VAL A CB  
3197  C CG1 . VAL A 443  ? 0.3908 0.3806 0.4904 -0.0210 -0.0222 0.0004  441  VAL A CG1 
3198  C CG2 . VAL A 443  ? 0.4162 0.4011 0.5316 -0.0222 -0.0285 -0.0063 441  VAL A CG2 
3199  N N   . GLY A 444  ? 0.2761 0.2630 0.3800 -0.0217 -0.0175 0.0164  442  GLY A N   
3200  C CA  . GLY A 444  ? 0.2556 0.2449 0.3551 -0.0211 -0.0142 0.0220  442  GLY A CA  
3201  C C   . GLY A 444  ? 0.2312 0.2198 0.3351 -0.0216 -0.0130 0.0282  442  GLY A C   
3202  O O   . GLY A 444  ? 0.2326 0.2234 0.3321 -0.0206 -0.0099 0.0324  442  GLY A O   
3203  N N   . LYS A 445  ? 0.2419 0.2280 0.3547 -0.0231 -0.0155 0.0289  443  LYS A N   
3204  C CA  . LYS A 445  ? 0.2334 0.2197 0.3505 -0.0237 -0.0145 0.0355  443  LYS A CA  
3205  C C   . LYS A 445  ? 0.2377 0.2220 0.3489 -0.0221 -0.0121 0.0361  443  LYS A C   
3206  O O   . LYS A 445  ? 0.2438 0.2305 0.3513 -0.0212 -0.0091 0.0408  443  LYS A O   
3207  C CB  . LYS A 445  ? 0.2512 0.2352 0.3804 -0.0260 -0.0182 0.0367  443  LYS A CB  
3208  C CG  . LYS A 445  ? 0.2957 0.2814 0.4301 -0.0271 -0.0172 0.0448  443  LYS A CG  
3209  C CD  . LYS A 445  ? 0.3941 0.3781 0.5418 -0.0297 -0.0211 0.0471  443  LYS A CD  
3210  C CE  . LYS A 445  ? 0.4167 0.4049 0.5694 -0.0312 -0.0199 0.0563  443  LYS A CE  
3211  N NZ  . LYS A 445  ? 0.4492 0.4360 0.6158 -0.0341 -0.0240 0.0595  443  LYS A NZ  
3212  N N   . TYR A 446  ? 0.2156 0.1959 0.3260 -0.0215 -0.0135 0.0310  444  TYR A N   
3213  C CA  . TYR A 446  ? 0.2184 0.1967 0.3227 -0.0198 -0.0115 0.0305  444  TYR A CA  
3214  C C   . TYR A 446  ? 0.2312 0.2065 0.3337 -0.0191 -0.0133 0.0232  444  TYR A C   
3215  O O   . TYR A 446  ? 0.2202 0.1951 0.3272 -0.0199 -0.0162 0.0188  444  TYR A O   
3216  C CB  . TYR A 446  ? 0.2225 0.1996 0.3323 -0.0205 -0.0115 0.0358  444  TYR A CB  
3217  C CG  . TYR A 446  ? 0.2489 0.2219 0.3684 -0.0218 -0.0154 0.0340  444  TYR A CG  
3218  C CD1 . TYR A 446  ? 0.3255 0.2984 0.4559 -0.0240 -0.0184 0.0364  444  TYR A CD1 
3219  C CD2 . TYR A 446  ? 0.2627 0.2318 0.3809 -0.0207 -0.0161 0.0299  444  TYR A CD2 
3220  C CE1 . TYR A 446  ? 0.2717 0.2404 0.4118 -0.0251 -0.0224 0.0344  444  TYR A CE1 
3221  C CE2 . TYR A 446  ? 0.3331 0.2983 0.4606 -0.0216 -0.0198 0.0278  444  TYR A CE2 
3222  C CZ  . TYR A 446  ? 0.2993 0.2642 0.4379 -0.0237 -0.0231 0.0300  444  TYR A CZ  
3223  O OH  . TYR A 446  ? 0.4298 0.3904 0.5785 -0.0245 -0.0271 0.0276  444  TYR A OH  
3224  N N   . GLU A 447  ? 0.1983 0.1720 0.2944 -0.0175 -0.0115 0.0217  445  GLU A N   
3225  C CA  . GLU A 447  ? 0.2103 0.1818 0.3052 -0.0167 -0.0132 0.0150  445  GLU A CA  
3226  C C   . GLU A 447  ? 0.2236 0.1923 0.3168 -0.0157 -0.0121 0.0155  445  GLU A C   
3227  O O   . GLU A 447  ? 0.2212 0.1902 0.3124 -0.0153 -0.0098 0.0207  445  GLU A O   
3228  C CB  . GLU A 447  ? 0.1880 0.1621 0.2744 -0.0157 -0.0121 0.0106  445  GLU A CB  
3229  C CG  . GLU A 447  ? 0.2164 0.1917 0.2934 -0.0143 -0.0084 0.0131  445  GLU A CG  
3230  C CD  . GLU A 447  ? 0.2123 0.1903 0.2817 -0.0135 -0.0076 0.0099  445  GLU A CD  
3231  O OE1 . GLU A 447  ? 0.2397 0.2198 0.3106 -0.0142 -0.0095 0.0066  445  GLU A OE1 
3232  O OE2 . GLU A 447  ? 0.2071 0.1853 0.2692 -0.0123 -0.0051 0.0109  445  GLU A OE2 
3233  N N   . PHE A 448  ? 0.2291 0.1957 0.3233 -0.0150 -0.0140 0.0098  446  PHE A N   
3234  C CA  . PHE A 448  ? 0.2164 0.1807 0.3073 -0.0137 -0.0129 0.0089  446  PHE A CA  
3235  C C   . PHE A 448  ? 0.2026 0.1690 0.2833 -0.0122 -0.0109 0.0052  446  PHE A C   
3236  O O   . PHE A 448  ? 0.2126 0.1818 0.2900 -0.0123 -0.0110 0.0024  446  PHE A O   
3237  C CB  . PHE A 448  ? 0.2326 0.1936 0.3315 -0.0138 -0.0163 0.0048  446  PHE A CB  
3238  C CG  . PHE A 448  ? 0.2146 0.1732 0.3244 -0.0153 -0.0187 0.0091  446  PHE A CG  
3239  C CD1 . PHE A 448  ? 0.2429 0.2000 0.3543 -0.0154 -0.0176 0.0150  446  PHE A CD1 
3240  C CD2 . PHE A 448  ? 0.2382 0.1963 0.3570 -0.0167 -0.0222 0.0074  446  PHE A CD2 
3241  C CE1 . PHE A 448  ? 0.2496 0.2050 0.3716 -0.0171 -0.0198 0.0198  446  PHE A CE1 
3242  C CE2 . PHE A 448  ? 0.2599 0.2158 0.3898 -0.0184 -0.0246 0.0119  446  PHE A CE2 
3243  C CZ  . PHE A 448  ? 0.2364 0.1910 0.3677 -0.0187 -0.0234 0.0184  446  PHE A CZ  
3244  N N   . GLN A 449  ? 0.2071 0.1722 0.2830 -0.0110 -0.0091 0.0054  447  GLN A N   
3245  C CA  . GLN A 449  ? 0.2030 0.1698 0.2700 -0.0098 -0.0074 0.0021  447  GLN A CA  
3246  C C   . GLN A 449  ? 0.2232 0.1879 0.2896 -0.0087 -0.0075 -0.0006 447  GLN A C   
3247  O O   . GLN A 449  ? 0.2349 0.1966 0.3059 -0.0086 -0.0080 0.0016  447  GLN A O   
3248  C CB  . GLN A 449  ? 0.2154 0.1838 0.2745 -0.0092 -0.0041 0.0061  447  GLN A CB  
3249  C CG  . GLN A 449  ? 0.1995 0.1703 0.2590 -0.0100 -0.0037 0.0090  447  GLN A CG  
3250  C CD  . GLN A 449  ? 0.2245 0.1972 0.2760 -0.0092 -0.0010 0.0111  447  GLN A CD  
3251  O OE1 . GLN A 449  ? 0.2289 0.2009 0.2751 -0.0081 0.0007  0.0114  447  GLN A OE1 
3252  N NE2 . GLN A 449  ? 0.2116 0.1869 0.2628 -0.0097 -0.0009 0.0125  447  GLN A NE2 
3253  N N   . CYS A 450  ? 0.2249 0.1916 0.2856 -0.0078 -0.0071 -0.0053 448  CYS A N   
3254  C CA  . CYS A 450  ? 0.2296 0.1951 0.2893 -0.0066 -0.0072 -0.0083 448  CYS A CA  
3255  C C   . CYS A 450  ? 0.2645 0.2332 0.3151 -0.0059 -0.0053 -0.0103 448  CYS A C   
3256  O O   . CYS A 450  ? 0.2395 0.2112 0.2856 -0.0063 -0.0043 -0.0097 448  CYS A O   
3257  C CB  . CYS A 450  ? 0.2552 0.2200 0.3223 -0.0065 -0.0105 -0.0141 448  CYS A CB  
3258  S SG  . CYS A 450  ? 0.2678 0.2380 0.3332 -0.0063 -0.0121 -0.0215 448  CYS A SG  
3259  N N   . LEU A 451  ? 0.2373 0.2054 0.2858 -0.0048 -0.0048 -0.0124 449  LEU A N   
3260  C CA  . LEU A 451  ? 0.2809 0.2523 0.3216 -0.0042 -0.0032 -0.0142 449  LEU A CA  
3261  C C   . LEU A 451  ? 0.2730 0.2485 0.3145 -0.0039 -0.0049 -0.0208 449  LEU A C   
3262  O O   . LEU A 451  ? 0.2938 0.2683 0.3416 -0.0034 -0.0072 -0.0248 449  LEU A O   
3263  C CB  . LEU A 451  ? 0.2709 0.2402 0.3085 -0.0033 -0.0015 -0.0126 449  LEU A CB  
3264  C CG  . LEU A 451  ? 0.3018 0.2681 0.3378 -0.0032 0.0004  -0.0065 449  LEU A CG  
3265  C CD1 . LEU A 451  ? 0.3314 0.2961 0.3647 -0.0022 0.0015  -0.0062 449  LEU A CD1 
3266  C CD2 . LEU A 451  ? 0.3136 0.2815 0.3442 -0.0036 0.0021  -0.0033 449  LEU A CD2 
3267  N N   . HIS A 452  ? 0.2560 0.2365 0.2914 -0.0041 -0.0040 -0.0220 450  HIS A N   
3268  C CA  . HIS A 452  ? 0.3069 0.2931 0.3417 -0.0037 -0.0053 -0.0282 450  HIS A CA  
3269  C C   . HIS A 452  ? 0.3203 0.3061 0.3563 -0.0024 -0.0057 -0.0319 450  HIS A C   
3270  O O   . HIS A 452  ? 0.3078 0.2910 0.3412 -0.0019 -0.0040 -0.0291 450  HIS A O   
3271  C CB  . HIS A 452  ? 0.2991 0.2910 0.3262 -0.0042 -0.0039 -0.0273 450  HIS A CB  
3272  C CG  . HIS A 452  ? 0.2934 0.2925 0.3187 -0.0038 -0.0047 -0.0330 450  HIS A CG  
3273  N ND1 . HIS A 452  ? 0.3028 0.3074 0.3299 -0.0040 -0.0066 -0.0373 450  HIS A ND1 
3274  C CD2 . HIS A 452  ? 0.3323 0.3350 0.3542 -0.0030 -0.0039 -0.0352 450  HIS A CD2 
3275  C CE1 . HIS A 452  ? 0.3446 0.3562 0.3693 -0.0034 -0.0068 -0.0420 450  HIS A CE1 
3276  N NE2 . HIS A 452  ? 0.3000 0.3106 0.3215 -0.0028 -0.0052 -0.0407 450  HIS A NE2 
3277  N N   . GLY A 453  ? 0.4036 0.3923 0.4440 -0.0016 -0.0080 -0.0384 451  GLY A N   
3278  C CA  . GLY A 453  ? 0.3980 0.3875 0.4400 -0.0001 -0.0085 -0.0429 451  GLY A CA  
3279  C C   . GLY A 453  ? 0.4152 0.3976 0.4631 0.0005  -0.0092 -0.0415 451  GLY A C   
3280  O O   . GLY A 453  ? 0.5175 0.5001 0.5670 0.0019  -0.0097 -0.0450 451  GLY A O   
3281  N N   . MET A 454  ? 0.4011 0.3778 0.4522 -0.0004 -0.0092 -0.0362 452  MET A N   
3282  C CA  . MET A 454  ? 0.3589 0.3294 0.4160 0.0000  -0.0100 -0.0340 452  MET A CA  
3283  C C   . MET A 454  ? 0.3832 0.3501 0.4495 -0.0008 -0.0127 -0.0334 452  MET A C   
3284  O O   . MET A 454  ? 0.3568 0.3202 0.4311 -0.0002 -0.0150 -0.0350 452  MET A O   
3285  C CB  . MET A 454  ? 0.3433 0.3108 0.3955 -0.0004 -0.0072 -0.0270 452  MET A CB  
3286  N N   . GLY A 455  ? 0.3383 0.3061 0.4041 -0.0021 -0.0126 -0.0312 453  GLY A N   
3287  C CA  . GLY A 455  ? 0.3603 0.3247 0.4350 -0.0031 -0.0150 -0.0296 453  GLY A CA  
3288  C C   . GLY A 455  ? 0.3421 0.3088 0.4223 -0.0032 -0.0182 -0.0358 453  GLY A C   
3289  O O   . GLY A 455  ? 0.3086 0.2723 0.3975 -0.0040 -0.0208 -0.0351 453  GLY A O   
3290  N N   . GLU A 456  ? 0.3568 0.3294 0.4325 -0.0024 -0.0182 -0.0416 454  GLU A N   
3291  C CA  . GLU A 456  ? 0.3533 0.3293 0.4340 -0.0023 -0.0212 -0.0482 454  GLU A CA  
3292  C C   . GLU A 456  ? 0.3459 0.3183 0.4379 -0.0015 -0.0251 -0.0529 454  GLU A C   
3293  O O   . GLU A 456  ? 0.3600 0.3315 0.4595 -0.0022 -0.0281 -0.0549 454  GLU A O   
3294  C CB  . GLU A 456  ? 0.4121 0.3962 0.4858 -0.0014 -0.0205 -0.0539 454  GLU A CB  
3295  C CG  . GLU A 456  ? 0.4512 0.4394 0.5155 -0.0025 -0.0177 -0.0498 454  GLU A CG  
3296  C CD  . GLU A 456  ? 0.3987 0.3869 0.4547 -0.0023 -0.0143 -0.0456 454  GLU A CD  
3297  O OE1 . GLU A 456  ? 0.4368 0.4206 0.4944 -0.0015 -0.0138 -0.0442 454  GLU A OE1 
3298  O OE2 . GLU A 456  ? 0.3762 0.3690 0.4245 -0.0028 -0.0123 -0.0437 454  GLU A OE2 
3299  N N   . PRO A 457  ? 0.3680 0.3384 0.4625 0.0000  -0.0256 -0.0551 455  PRO A N   
3300  C CA  . PRO A 457  ? 0.3918 0.3582 0.4984 0.0008  -0.0298 -0.0594 455  PRO A CA  
3301  C C   . PRO A 457  ? 0.3832 0.3431 0.4987 -0.0010 -0.0317 -0.0536 455  PRO A C   
3302  O O   . PRO A 457  ? 0.3756 0.3340 0.5008 -0.0013 -0.0356 -0.0572 455  PRO A O   
3303  C CB  . PRO A 457  ? 0.3688 0.3335 0.4751 0.0025  -0.0291 -0.0602 455  PRO A CB  
3304  C CG  . PRO A 457  ? 0.4283 0.3988 0.5223 0.0030  -0.0253 -0.0604 455  PRO A CG  
3305  C CD  . PRO A 457  ? 0.3725 0.3441 0.4595 0.0011  -0.0227 -0.0542 455  PRO A CD  
3306  N N   . LEU A 458  ? 0.3740 0.3305 0.4864 -0.0022 -0.0291 -0.0448 456  LEU A N   
3307  C CA  . LEU A 458  ? 0.3318 0.2834 0.4521 -0.0040 -0.0305 -0.0383 456  LEU A CA  
3308  C C   . LEU A 458  ? 0.3343 0.2880 0.4557 -0.0056 -0.0314 -0.0381 456  LEU A C   
3309  O O   . LEU A 458  ? 0.3052 0.2564 0.4371 -0.0065 -0.0350 -0.0387 456  LEU A O   
3310  C CB  . LEU A 458  ? 0.3021 0.2516 0.4173 -0.0048 -0.0271 -0.0292 456  LEU A CB  
3311  C CG  . LEU A 458  ? 0.2974 0.2436 0.4192 -0.0069 -0.0278 -0.0214 456  LEU A CG  
3312  C CD1 . LEU A 458  ? 0.3041 0.2457 0.4403 -0.0073 -0.0325 -0.0222 456  LEU A CD1 
3313  C CD2 . LEU A 458  ? 0.3120 0.2575 0.4278 -0.0072 -0.0243 -0.0133 456  LEU A CD2 
3314  N N   . TYR A 459  ? 0.3161 0.2744 0.4272 -0.0059 -0.0283 -0.0371 457  TYR A N   
3315  C CA  . TYR A 459  ? 0.3137 0.2737 0.4258 -0.0075 -0.0289 -0.0356 457  TYR A CA  
3316  C C   . TYR A 459  ? 0.3244 0.2880 0.4404 -0.0071 -0.0321 -0.0439 457  TYR A C   
3317  O O   . TYR A 459  ? 0.3226 0.2869 0.4422 -0.0085 -0.0336 -0.0432 457  TYR A O   
3318  C CB  . TYR A 459  ? 0.2932 0.2564 0.3940 -0.0080 -0.0247 -0.0307 457  TYR A CB  
3319  C CG  . TYR A 459  ? 0.2880 0.2478 0.3883 -0.0089 -0.0224 -0.0219 457  TYR A CG  
3320  C CD1 . TYR A 459  ? 0.2793 0.2373 0.3854 -0.0106 -0.0232 -0.0165 457  TYR A CD1 
3321  C CD2 . TYR A 459  ? 0.2700 0.2288 0.3643 -0.0079 -0.0196 -0.0191 457  TYR A CD2 
3322  C CE1 . TYR A 459  ? 0.2486 0.2047 0.3543 -0.0113 -0.0212 -0.0086 457  TYR A CE1 
3323  C CE2 . TYR A 459  ? 0.2449 0.2013 0.3387 -0.0086 -0.0177 -0.0114 457  TYR A CE2 
3324  C CZ  . TYR A 459  ? 0.2680 0.2234 0.3674 -0.0102 -0.0184 -0.0062 457  TYR A CZ  
3325  O OH  . TYR A 459  ? 0.2720 0.2264 0.3710 -0.0109 -0.0165 0.0015  457  TYR A OH  
3326  N N   . GLU A 460  ? 0.3263 0.2925 0.4422 -0.0052 -0.0334 -0.0519 458  GLU A N   
3327  C CA  . GLU A 460  ? 0.3566 0.3257 0.4786 -0.0046 -0.0373 -0.0606 458  GLU A CA  
3328  C C   . GLU A 460  ? 0.3750 0.3383 0.5115 -0.0053 -0.0419 -0.0612 458  GLU A C   
3329  O O   . GLU A 460  ? 0.3584 0.3234 0.5016 -0.0053 -0.0455 -0.0671 458  GLU A O   
3330  C CB  . GLU A 460  ? 0.4065 0.3804 0.5256 -0.0021 -0.0376 -0.0691 458  GLU A CB  
3331  N N   . GLU A 461  ? 0.3314 0.2883 0.4733 -0.0059 -0.0420 -0.0551 459  GLU A N   
3332  C CA  . GLU A 461  ? 0.3662 0.3172 0.5222 -0.0071 -0.0462 -0.0534 459  GLU A CA  
3333  C C   . GLU A 461  ? 0.3609 0.3101 0.5187 -0.0098 -0.0455 -0.0446 459  GLU A C   
3334  O O   . GLU A 461  ? 0.3581 0.3026 0.5276 -0.0112 -0.0487 -0.0413 459  GLU A O   
3335  C CB  . GLU A 461  ? 0.3538 0.2993 0.5156 -0.0063 -0.0471 -0.0513 459  GLU A CB  
3336  C CG  . GLU A 461  ? 0.3920 0.3393 0.5521 -0.0035 -0.0476 -0.0594 459  GLU A CG  
3337  C CD  . GLU A 461  ? 0.4465 0.3954 0.6151 -0.0021 -0.0524 -0.0703 459  GLU A CD  
3338  O OE1 . GLU A 461  ? 0.4393 0.3859 0.6182 -0.0033 -0.0562 -0.0710 459  GLU A OE1 
3339  O OE2 . GLU A 461  ? 0.4767 0.4297 0.6420 0.0004  -0.0523 -0.0782 459  GLU A OE2 
3340  N N   . VAL A 462  ? 0.3517 0.3048 0.4987 -0.0105 -0.0415 -0.0406 460  VAL A N   
3341  C CA  . VAL A 462  ? 0.3110 0.2634 0.4583 -0.0128 -0.0402 -0.0322 460  VAL A CA  
3342  C C   . VAL A 462  ? 0.3483 0.3055 0.4923 -0.0136 -0.0402 -0.0344 460  VAL A C   
3343  O O   . VAL A 462  ? 0.3447 0.3010 0.4964 -0.0153 -0.0426 -0.0326 460  VAL A O   
3344  C CB  . VAL A 462  ? 0.3229 0.2754 0.4609 -0.0129 -0.0352 -0.0241 460  VAL A CB  
3345  C CG1 . VAL A 462  ? 0.3017 0.2548 0.4394 -0.0150 -0.0337 -0.0161 460  VAL A CG1 
3346  C CG2 . VAL A 462  ? 0.3152 0.2632 0.4571 -0.0124 -0.0354 -0.0212 460  VAL A CG2 
3347  N N   . VAL A 463  ? 0.3370 0.2995 0.4700 -0.0124 -0.0376 -0.0380 461  VAL A N   
3348  C CA  . VAL A 463  ? 0.3326 0.3002 0.4613 -0.0130 -0.0373 -0.0396 461  VAL A CA  
3349  C C   . VAL A 463  ? 0.3797 0.3488 0.5170 -0.0130 -0.0421 -0.0476 461  VAL A C   
3350  O O   . VAL A 463  ? 0.4197 0.3887 0.5611 -0.0114 -0.0447 -0.0550 461  VAL A O   
3351  C CB  . VAL A 463  ? 0.3118 0.2850 0.4273 -0.0118 -0.0338 -0.0413 461  VAL A CB  
3352  C CG1 . VAL A 463  ? 0.3472 0.3263 0.4587 -0.0124 -0.0338 -0.0431 461  VAL A CG1 
3353  C CG2 . VAL A 463  ? 0.3313 0.3029 0.4389 -0.0118 -0.0293 -0.0337 461  VAL A CG2 
3354  N N   . GLY A 464  ? 0.3689 0.3396 0.5091 -0.0146 -0.0434 -0.0464 462  GLY A N   
3355  C CA  . GLY A 464  ? 0.4140 0.3873 0.5611 -0.0145 -0.0478 -0.0545 462  GLY A CA  
3356  C C   . GLY A 464  ? 0.4198 0.3877 0.5816 -0.0161 -0.0522 -0.0534 462  GLY A C   
3357  O O   . GLY A 464  ? 0.4147 0.3766 0.5833 -0.0166 -0.0529 -0.0488 462  GLY A O   
3358  N N   . ARG A 465  ? 0.4194 0.3899 0.5866 -0.0170 -0.0555 -0.0574 463  ARG A N   
3359  C CA  . ARG A 465  ? 0.3867 0.3525 0.5686 -0.0187 -0.0602 -0.0566 463  ARG A CA  
3360  C C   . ARG A 465  ? 0.4371 0.3978 0.6300 -0.0176 -0.0644 -0.0618 463  ARG A C   
3361  O O   . ARG A 465  ? 0.4694 0.4243 0.6749 -0.0192 -0.0676 -0.0583 463  ARG A O   
3362  C CB  . ARG A 465  ? 0.4504 0.4204 0.6355 -0.0196 -0.0632 -0.0613 463  ARG A CB  
3363  N N   . GLY A 466  ? 0.4052 0.3684 0.5942 -0.0149 -0.0645 -0.0702 464  GLY A N   
3364  C CA  . GLY A 466  ? 0.4191 0.3779 0.6183 -0.0135 -0.0683 -0.0756 464  GLY A CA  
3365  C C   . GLY A 466  ? 0.4557 0.4086 0.6555 -0.0134 -0.0664 -0.0687 464  GLY A C   
3366  O O   . GLY A 466  ? 0.4360 0.3844 0.6452 -0.0123 -0.0697 -0.0721 464  GLY A O   
3367  N N   . LYS A 467  ? 0.4254 0.3785 0.6156 -0.0145 -0.0612 -0.0592 465  LYS A N   
3368  C CA  . LYS A 467  ? 0.3611 0.3094 0.5510 -0.0145 -0.0591 -0.0523 465  LYS A CA  
3369  C C   . LYS A 467  ? 0.3839 0.3295 0.5770 -0.0173 -0.0580 -0.0410 465  LYS A C   
3370  O O   . LYS A 467  ? 0.4238 0.3668 0.6288 -0.0192 -0.0619 -0.0396 465  LYS A O   
3371  C CB  . LYS A 467  ? 0.3812 0.3329 0.5566 -0.0126 -0.0541 -0.0524 465  LYS A CB  
3372  C CG  . LYS A 467  ? 0.4148 0.3705 0.5870 -0.0098 -0.0550 -0.0633 465  LYS A CG  
3373  C CD  . LYS A 467  ? 0.4241 0.3751 0.6078 -0.0084 -0.0592 -0.0684 465  LYS A CD  
3374  C CE  . LYS A 467  ? 0.4174 0.3733 0.5967 -0.0054 -0.0594 -0.0789 465  LYS A CE  
3375  N NZ  . LYS A 467  ? 0.4337 0.3849 0.6238 -0.0037 -0.0632 -0.0837 465  LYS A NZ  
3376  N N   . LEU A 468  ? 0.3896 0.3362 0.5727 -0.0177 -0.0529 -0.0332 466  LEU A N   
3377  C CA  . LEU A 468  ? 0.3578 0.3034 0.5427 -0.0202 -0.0513 -0.0226 466  LEU A CA  
3378  C C   . LEU A 468  ? 0.3556 0.3060 0.5338 -0.0212 -0.0491 -0.0205 466  LEU A C   
3379  O O   . LEU A 468  ? 0.3537 0.3042 0.5343 -0.0233 -0.0482 -0.0125 466  LEU A O   
3380  C CB  . LEU A 468  ? 0.3614 0.3058 0.5398 -0.0198 -0.0472 -0.0153 466  LEU A CB  
3381  C CG  . LEU A 468  ? 0.3697 0.3095 0.5539 -0.0186 -0.0491 -0.0166 466  LEU A CG  
3382  C CD1 . LEU A 468  ? 0.3606 0.2997 0.5391 -0.0186 -0.0452 -0.0083 466  LEU A CD1 
3383  C CD2 . LEU A 468  ? 0.3663 0.3013 0.5675 -0.0201 -0.0549 -0.0167 466  LEU A CD2 
3384  N N   . ASP A 469  ? 0.3712 0.3262 0.5412 -0.0199 -0.0482 -0.0274 467  ASP A N   
3385  C CA  . ASP A 469  ? 0.3473 0.3072 0.5112 -0.0207 -0.0465 -0.0262 467  ASP A CA  
3386  C C   . ASP A 469  ? 0.3235 0.2847 0.4788 -0.0213 -0.0415 -0.0171 467  ASP A C   
3387  O O   . ASP A 469  ? 0.3319 0.2947 0.4882 -0.0230 -0.0408 -0.0117 467  ASP A O   
3388  C CB  . ASP A 469  ? 0.3833 0.3429 0.5584 -0.0228 -0.0507 -0.0266 467  ASP A CB  
3389  C CG  . ASP A 469  ? 0.4012 0.3665 0.5705 -0.0231 -0.0499 -0.0288 467  ASP A CG  
3390  O OD1 . ASP A 469  ? 0.4182 0.3878 0.5763 -0.0215 -0.0474 -0.0326 467  ASP A OD1 
3391  O OD2 . ASP A 469  ? 0.4655 0.4312 0.6416 -0.0251 -0.0519 -0.0263 467  ASP A OD2 
3392  N N   . ARG A 470  ? 0.3481 0.3088 0.4953 -0.0199 -0.0381 -0.0157 468  ARG A N   
3393  C CA  . ARG A 470  ? 0.3017 0.2642 0.4394 -0.0198 -0.0333 -0.0088 468  ARG A CA  
3394  C C   . ARG A 470  ? 0.3120 0.2777 0.4371 -0.0178 -0.0303 -0.0127 468  ARG A C   
3395  O O   . ARG A 470  ? 0.3041 0.2694 0.4278 -0.0163 -0.0311 -0.0185 468  ARG A O   
3396  C CB  . ARG A 470  ? 0.3034 0.2623 0.4432 -0.0200 -0.0320 -0.0021 468  ARG A CB  
3397  C CG  . ARG A 470  ? 0.2871 0.2434 0.4398 -0.0222 -0.0349 0.0032  468  ARG A CG  
3398  C CD  . ARG A 470  ? 0.3027 0.2621 0.4560 -0.0240 -0.0339 0.0090  468  ARG A CD  
3399  N NE  . ARG A 470  ? 0.3293 0.2868 0.4953 -0.0263 -0.0367 0.0144  468  ARG A NE  
3400  C CZ  . ARG A 470  ? 0.3299 0.2866 0.5062 -0.0279 -0.0410 0.0123  468  ARG A CZ  
3401  N NH1 . ARG A 470  ? 0.3289 0.2867 0.5043 -0.0273 -0.0429 0.0044  468  ARG A NH1 
3402  N NH2 . ARG A 470  ? 0.3404 0.2954 0.5285 -0.0302 -0.0435 0.0184  468  ARG A NH2 
3403  N N   . PRO A 471  ? 0.2846 0.2539 0.4011 -0.0179 -0.0271 -0.0096 469  PRO A N   
3404  C CA  . PRO A 471  ? 0.2595 0.2321 0.3648 -0.0163 -0.0246 -0.0128 469  PRO A CA  
3405  C C   . PRO A 471  ? 0.2731 0.2439 0.3720 -0.0151 -0.0215 -0.0102 469  PRO A C   
3406  O O   . PRO A 471  ? 0.2570 0.2250 0.3580 -0.0154 -0.0203 -0.0045 469  PRO A O   
3407  C CB  . PRO A 471  ? 0.2736 0.2501 0.3738 -0.0170 -0.0228 -0.0095 469  PRO A CB  
3408  C CG  . PRO A 471  ? 0.2668 0.2413 0.3723 -0.0183 -0.0222 -0.0021 469  PRO A CG  
3409  C CD  . PRO A 471  ? 0.2897 0.2605 0.4069 -0.0193 -0.0259 -0.0031 469  PRO A CD  
3410  N N   . CYS A 472  ? 0.2722 0.2454 0.3634 -0.0136 -0.0203 -0.0145 470  CYS A N   
3411  C CA  . CYS A 472  ? 0.2399 0.2119 0.3243 -0.0124 -0.0174 -0.0127 470  CYS A CA  
3412  C C   . CYS A 472  ? 0.2492 0.2254 0.3233 -0.0117 -0.0150 -0.0135 470  CYS A C   
3413  O O   . CYS A 472  ? 0.2836 0.2639 0.3558 -0.0116 -0.0161 -0.0185 470  CYS A O   
3414  C CB  . CYS A 472  ? 0.2370 0.2068 0.3243 -0.0113 -0.0189 -0.0174 470  CYS A CB  
3415  S SG  . CYS A 472  ? 0.2745 0.2428 0.3542 -0.0099 -0.0156 -0.0151 470  CYS A SG  
3416  N N   . ARG A 473  ? 0.2138 0.1895 0.2816 -0.0113 -0.0118 -0.0085 471  ARG A N   
3417  C CA  . ARG A 473  ? 0.2115 0.1905 0.2701 -0.0107 -0.0095 -0.0085 471  ARG A CA  
3418  C C   . ARG A 473  ? 0.2047 0.1828 0.2588 -0.0095 -0.0083 -0.0101 471  ARG A C   
3419  O O   . ARG A 473  ? 0.2288 0.2034 0.2833 -0.0090 -0.0071 -0.0071 471  ARG A O   
3420  C CB  . ARG A 473  ? 0.2067 0.1859 0.2618 -0.0109 -0.0071 -0.0024 471  ARG A CB  
3421  C CG  . ARG A 473  ? 0.2272 0.2097 0.2740 -0.0104 -0.0054 -0.0022 471  ARG A CG  
3422  C CD  . ARG A 473  ? 0.2264 0.2089 0.2710 -0.0104 -0.0035 0.0032  471  ARG A CD  
3423  N NE  . ARG A 473  ? 0.2119 0.1953 0.2621 -0.0115 -0.0048 0.0047  471  ARG A NE  
3424  C CZ  . ARG A 473  ? 0.2518 0.2386 0.3024 -0.0122 -0.0061 0.0032  471  ARG A CZ  
3425  N NH1 . ARG A 473  ? 0.2393 0.2294 0.2846 -0.0120 -0.0062 0.0009  471  ARG A NH1 
3426  N NH2 . ARG A 473  ? 0.2061 0.1933 0.2629 -0.0133 -0.0076 0.0043  471  ARG A NH2 
3427  N N   . ILE A 474  ? 0.2386 0.2205 0.2885 -0.0090 -0.0085 -0.0147 472  ILE A N   
3428  C CA  . ILE A 474  ? 0.2258 0.2078 0.2714 -0.0079 -0.0074 -0.0166 472  ILE A CA  
3429  C C   . ILE A 474  ? 0.2265 0.2093 0.2642 -0.0076 -0.0046 -0.0126 472  ILE A C   
3430  O O   . ILE A 474  ? 0.2553 0.2417 0.2890 -0.0081 -0.0042 -0.0118 472  ILE A O   
3431  C CB  . ILE A 474  ? 0.2164 0.2033 0.2615 -0.0074 -0.0091 -0.0235 472  ILE A CB  
3432  C CG1 . ILE A 474  ? 0.2777 0.2633 0.3316 -0.0074 -0.0123 -0.0280 472  ILE A CG1 
3433  C CG2 . ILE A 474  ? 0.2374 0.2253 0.2773 -0.0064 -0.0076 -0.0250 472  ILE A CG2 
3434  C CD1 . ILE A 474  ? 0.3171 0.3085 0.3712 -0.0069 -0.0143 -0.0356 472  ILE A CD1 
3435  N N   . TYR A 475  ? 0.2183 0.1978 0.2541 -0.0069 -0.0029 -0.0102 473  TYR A N   
3436  C CA  . TYR A 475  ? 0.2289 0.2087 0.2578 -0.0065 -0.0005 -0.0070 473  TYR A CA  
3437  C C   . TYR A 475  ? 0.2396 0.2230 0.2639 -0.0062 -0.0004 -0.0104 473  TYR A C   
3438  O O   . TYR A 475  ? 0.2381 0.2206 0.2631 -0.0055 -0.0006 -0.0131 473  TYR A O   
3439  C CB  . TYR A 475  ? 0.2651 0.2405 0.2941 -0.0058 0.0010  -0.0033 473  TYR A CB  
3440  C CG  . TYR A 475  ? 0.2531 0.2283 0.2761 -0.0054 0.0032  0.0002  473  TYR A CG  
3441  C CD1 . TYR A 475  ? 0.2735 0.2487 0.2958 -0.0055 0.0041  0.0040  473  TYR A CD1 
3442  C CD2 . TYR A 475  ? 0.2572 0.2323 0.2757 -0.0047 0.0043  -0.0004 473  TYR A CD2 
3443  C CE1 . TYR A 475  ? 0.2553 0.2302 0.2730 -0.0048 0.0058  0.0067  473  TYR A CE1 
3444  C CE2 . TYR A 475  ? 0.2612 0.2357 0.2749 -0.0042 0.0059  0.0025  473  TYR A CE2 
3445  C CZ  . TYR A 475  ? 0.2745 0.2489 0.2880 -0.0042 0.0066  0.0059  473  TYR A CZ  
3446  O OH  . TYR A 475  ? 0.2933 0.2671 0.3029 -0.0036 0.0079  0.0083  473  TYR A OH  
3447  N N   . ALA A 476  ? 0.2486 0.2363 0.2684 -0.0067 -0.0001 -0.0100 474  ALA A N   
3448  C CA  . ALA A 476  ? 0.2403 0.2332 0.2564 -0.0067 -0.0003 -0.0133 474  ALA A CA  
3449  C C   . ALA A 476  ? 0.2385 0.2319 0.2486 -0.0066 0.0015  -0.0101 474  ALA A C   
3450  O O   . ALA A 476  ? 0.2416 0.2362 0.2491 -0.0073 0.0020  -0.0068 474  ALA A O   
3451  C CB  . ALA A 476  ? 0.2767 0.2756 0.2928 -0.0075 -0.0018 -0.0154 474  ALA A CB  
3452  N N   . PRO A 477  ? 0.2525 0.2450 0.2608 -0.0060 0.0023  -0.0110 475  PRO A N   
3453  C CA  . PRO A 477  ? 0.2564 0.2497 0.2596 -0.0061 0.0037  -0.0082 475  PRO A CA  
3454  C C   . PRO A 477  ? 0.2411 0.2418 0.2411 -0.0070 0.0032  -0.0093 475  PRO A C   
3455  O O   . PRO A 477  ? 0.2688 0.2746 0.2697 -0.0071 0.0021  -0.0136 475  PRO A O   
3456  C CB  . PRO A 477  ? 0.3117 0.3026 0.3148 -0.0052 0.0044  -0.0096 475  PRO A CB  
3457  C CG  . PRO A 477  ? 0.3275 0.3154 0.3360 -0.0045 0.0034  -0.0124 475  PRO A CG  
3458  C CD  . PRO A 477  ? 0.2722 0.2633 0.2836 -0.0051 0.0018  -0.0148 475  PRO A CD  
3459  N N   . VAL A 478  ? 0.2419 0.2436 0.2385 -0.0077 0.0038  -0.0053 476  VAL A N   
3460  C CA  . VAL A 478  ? 0.2759 0.2850 0.2695 -0.0089 0.0033  -0.0048 476  VAL A CA  
3461  C C   . VAL A 478  ? 0.3079 0.3170 0.2982 -0.0092 0.0042  -0.0017 476  VAL A C   
3462  O O   . VAL A 478  ? 0.3218 0.3255 0.3117 -0.0090 0.0049  0.0019  476  VAL A O   
3463  C CB  . VAL A 478  ? 0.2672 0.2782 0.2612 -0.0098 0.0024  -0.0023 476  VAL A CB  
3464  C CG1 . VAL A 478  ? 0.2776 0.2970 0.2686 -0.0112 0.0018  -0.0011 476  VAL A CG1 
3465  C CG2 . VAL A 478  ? 0.2836 0.2943 0.2813 -0.0095 0.0014  -0.0053 476  VAL A CG2 
3466  N N   . GLY A 479  ? 0.2942 0.3096 0.2822 -0.0097 0.0041  -0.0032 477  GLY A N   
3467  C CA  . GLY A 479  ? 0.3311 0.3471 0.3164 -0.0104 0.0048  0.0001  477  GLY A CA  
3468  C C   . GLY A 479  ? 0.3524 0.3754 0.3359 -0.0107 0.0049  -0.0025 477  GLY A C   
3469  O O   . GLY A 479  ? 0.3011 0.3273 0.2856 -0.0099 0.0047  -0.0075 477  GLY A O   
3470  N N   . THR A 480  ? 0.4194 0.4450 0.4005 -0.0118 0.0051  0.0011  478  THR A N   
3471  C CA  . THR A 480  ? 0.4383 0.4715 0.4176 -0.0122 0.0054  -0.0004 478  THR A CA  
3472  C C   . THR A 480  ? 0.4919 0.5210 0.4718 -0.0108 0.0063  -0.0036 478  THR A C   
3473  O O   . THR A 480  ? 0.5237 0.5440 0.5052 -0.0096 0.0068  -0.0037 478  THR A O   
3474  C CB  . THR A 480  ? 0.4581 0.4950 0.4354 -0.0141 0.0052  0.0051  478  THR A CB  
3475  O OG1 . THR A 480  ? 0.5216 0.5499 0.4995 -0.0138 0.0056  0.0081  478  THR A OG1 
3476  C CG2 . THR A 480  ? 0.4721 0.5125 0.4493 -0.0156 0.0041  0.0089  478  THR A CG2 
3477  N N   . HIS A 481  ? 0.5346 0.5707 0.5132 -0.0108 0.0066  -0.0059 479  HIS A N   
3478  C CA  . HIS A 481  ? 0.5525 0.5856 0.5318 -0.0095 0.0074  -0.0089 479  HIS A CA  
3479  C C   . HIS A 481  ? 0.6263 0.6516 0.6052 -0.0095 0.0081  -0.0049 479  HIS A C   
3480  O O   . HIS A 481  ? 0.6738 0.6922 0.6542 -0.0081 0.0086  -0.0064 479  HIS A O   
3481  C CB  . HIS A 481  ? 0.5409 0.5842 0.5188 -0.0097 0.0076  -0.0115 479  HIS A CB  
3482  N N   . GLU A 482  ? 0.6585 0.6851 0.6358 -0.0112 0.0079  0.0003  480  GLU A N   
3483  C CA  . GLU A 482  ? 0.6914 0.7108 0.6687 -0.0112 0.0082  0.0037  480  GLU A CA  
3484  C C   . GLU A 482  ? 0.7201 0.7300 0.6991 -0.0099 0.0083  0.0041  480  GLU A C   
3485  O O   . GLU A 482  ? 0.7498 0.7534 0.7293 -0.0088 0.0089  0.0037  480  GLU A O   
3486  C CB  . GLU A 482  ? 0.6856 0.7081 0.6621 -0.0133 0.0075  0.0092  480  GLU A CB  
3487  N N   . THR A 483  ? 0.6853 0.6949 0.6651 -0.0101 0.0077  0.0048  481  THR A N   
3488  C CA  . THR A 483  ? 0.6995 0.7013 0.6810 -0.0090 0.0079  0.0054  481  THR A CA  
3489  C C   . THR A 483  ? 0.7449 0.7432 0.7281 -0.0074 0.0084  0.0015  481  THR A C   
3490  O O   . THR A 483  ? 0.7722 0.7639 0.7565 -0.0063 0.0089  0.0021  481  THR A O   
3491  C CB  . THR A 483  ? 0.5580 0.5610 0.5401 -0.0097 0.0070  0.0073  481  THR A CB  
3492  N N   . LEU A 484  ? 0.7201 0.7231 0.7039 -0.0072 0.0082  -0.0025 482  LEU A N   
3493  C CA  . LEU A 484  ? 0.7392 0.7388 0.7258 -0.0057 0.0083  -0.0062 482  LEU A CA  
3494  C C   . LEU A 484  ? 0.8372 0.8328 0.8240 -0.0047 0.0090  -0.0068 482  LEU A C   
3495  O O   . LEU A 484  ? 0.8681 0.8579 0.8570 -0.0036 0.0093  -0.0069 482  LEU A O   
3496  C CB  . LEU A 484  ? 0.6644 0.6703 0.6523 -0.0056 0.0075  -0.0109 482  LEU A CB  
3497  N N   . LEU A 485  ? 0.9102 0.9094 0.8949 -0.0051 0.0094  -0.0068 483  LEU A N   
3498  C CA  . LEU A 485  ? 0.9132 0.9093 0.8981 -0.0041 0.0100  -0.0075 483  LEU A CA  
3499  C C   . LEU A 485  ? 0.9999 0.9889 0.9842 -0.0037 0.0105  -0.0041 483  LEU A C   
3500  O O   . LEU A 485  ? 0.9780 0.9637 0.9629 -0.0027 0.0110  -0.0046 483  LEU A O   
3501  C CB  . LEU A 485  ? 0.8467 0.8489 0.8295 -0.0048 0.0102  -0.0078 483  LEU A CB  
3502  N N   . ALA A 486  ? 1.1531 1.1403 1.1367 -0.0043 0.0104  -0.0008 484  ALA A N   
3503  C CA  . ALA A 486  ? 1.1125 1.0942 1.0957 -0.0038 0.0108  0.0020  484  ALA A CA  
3504  C C   . ALA A 486  ? 1.1642 1.1408 1.1491 -0.0022 0.0113  0.0011  484  ALA A C   
3505  O O   . ALA A 486  ? 1.1954 1.1689 1.1798 -0.0014 0.0118  0.0019  484  ALA A O   
3506  C CB  . ALA A 486  ? 1.1103 1.0912 1.0932 -0.0045 0.0103  0.0050  484  ALA A CB  
3507  N N   . TYR A 487  ? 0.9728 0.9490 0.9601 -0.0019 0.0111  -0.0001 485  TYR A N   
3508  C CA  . TYR A 487  ? 0.9215 0.8935 0.9112 -0.0007 0.0114  -0.0001 485  TYR A CA  
3509  C C   . TYR A 487  ? 0.8956 0.8684 0.8888 -0.0005 0.0107  -0.0028 485  TYR A C   
3510  O O   . TYR A 487  ? 0.8227 0.7935 0.8187 -0.0003 0.0105  -0.0021 485  TYR A O   
3511  C CB  . TYR A 487  ? 0.9799 0.9491 0.9696 -0.0004 0.0118  0.0028  485  TYR A CB  
3512  N N   . LEU A 488  ? 0.8429 0.8190 0.8366 -0.0006 0.0103  -0.0061 486  LEU A N   
3513  C CA  . LEU A 488  ? 0.7727 0.7493 0.7706 -0.0001 0.0093  -0.0094 486  LEU A CA  
3514  C C   . LEU A 488  ? 0.7330 0.7058 0.7340 0.0010  0.0092  -0.0097 486  LEU A C   
3515  O O   . LEU A 488  ? 0.6865 0.6584 0.6921 0.0015  0.0081  -0.0119 486  LEU A O   
3516  C CB  . LEU A 488  ? 0.6951 0.6777 0.6926 -0.0004 0.0087  -0.0134 486  LEU A CB  
3517  N N   . VAL A 489  ? 0.7107 0.6812 0.7094 0.0015  0.0101  -0.0075 487  VAL A N   
3518  C CA  . VAL A 489  ? 0.6607 0.6281 0.6620 0.0025  0.0100  -0.0075 487  VAL A CA  
3519  C C   . VAL A 489  ? 0.6978 0.6618 0.7029 0.0027  0.0097  -0.0052 487  VAL A C   
3520  O O   . VAL A 489  ? 0.6671 0.6293 0.6766 0.0033  0.0089  -0.0055 487  VAL A O   
3521  C CB  . VAL A 489  ? 0.5917 0.5581 0.5895 0.0029  0.0110  -0.0056 487  VAL A CB  
3522  N N   . ARG A 490  ? 0.7141 0.6777 0.7181 0.0022  0.0102  -0.0026 488  ARG A N   
3523  C CA  . ARG A 490  ? 0.7533 0.7145 0.7606 0.0023  0.0101  0.0002  488  ARG A CA  
3524  C C   . ARG A 490  ? 0.7016 0.6623 0.7151 0.0021  0.0084  -0.0016 488  ARG A C   
3525  O O   . ARG A 490  ? 0.6658 0.6244 0.6838 0.0024  0.0077  -0.0004 488  ARG A O   
3526  C CB  . ARG A 490  ? 0.7312 0.6928 0.7363 0.0019  0.0109  0.0028  488  ARG A CB  
3527  N N   . ARG A 491  ? 0.7308 0.6937 0.7450 0.0015  0.0075  -0.0045 489  ARG A N   
3528  C CA  . ARG A 491  ? 0.6826 0.6451 0.7033 0.0013  0.0056  -0.0068 489  ARG A CA  
3529  C C   . ARG A 491  ? 0.6948 0.6566 0.7192 0.0022  0.0044  -0.0100 489  ARG A C   
3530  O O   . ARG A 491  ? 0.6590 0.6184 0.6900 0.0023  0.0028  -0.0100 489  ARG A O   
3531  C CB  . ARG A 491  ? 0.6591 0.6249 0.6793 0.0006  0.0049  -0.0097 489  ARG A CB  
3532  N N   . LEU A 492  ? 0.6653 0.6295 0.6861 0.0027  0.0049  -0.0126 490  LEU A N   
3533  C CA  . LEU A 492  ? 0.6534 0.6176 0.6778 0.0037  0.0038  -0.0162 490  LEU A CA  
3534  C C   . LEU A 492  ? 0.6730 0.6332 0.6999 0.0043  0.0038  -0.0131 490  LEU A C   
3535  O O   . LEU A 492  ? 0.6276 0.5860 0.6610 0.0050  0.0020  -0.0145 490  LEU A O   
3536  C CB  . LEU A 492  ? 0.5662 0.5347 0.5859 0.0041  0.0046  -0.0193 490  LEU A CB  
3537  N N   . LEU A 493  ? 0.6508 0.6100 0.6732 0.0042  0.0056  -0.0087 491  LEU A N   
3538  C CA  . LEU A 493  ? 0.6298 0.5861 0.6541 0.0047  0.0056  -0.0053 491  LEU A CA  
3539  C C   . LEU A 493  ? 0.7001 0.6541 0.7307 0.0043  0.0044  -0.0024 491  LEU A C   
3540  O O   . LEU A 493  ? 0.7264 0.6784 0.7621 0.0047  0.0033  -0.0008 491  LEU A O   
3541  C CB  . LEU A 493  ? 0.6087 0.5653 0.6267 0.0048  0.0077  -0.0018 491  LEU A CB  
3542  N N   . GLU A 494  ? 0.6802 0.6346 0.7107 0.0034  0.0046  -0.0012 492  GLU A N   
3543  C CA  . GLU A 494  ? 0.6978 0.6506 0.7348 0.0027  0.0033  0.0018  492  GLU A CA  
3544  C C   . GLU A 494  ? 0.7308 0.6819 0.7760 0.0028  0.0005  -0.0014 492  GLU A C   
3545  O O   . GLU A 494  ? 0.7465 0.6954 0.7979 0.0029  -0.0009 0.0009  492  GLU A O   
3546  C CB  . GLU A 494  ? 0.6943 0.6484 0.7297 0.0018  0.0039  0.0030  492  GLU A CB  
3547  N N   . ASN A 495  ? 0.7448 0.6975 0.7906 0.0029  -0.0005 -0.0069 493  ASN A N   
3548  C CA  . ASN A 495  ? 0.7434 0.6950 0.7974 0.0033  -0.0035 -0.0112 493  ASN A CA  
3549  C C   . ASN A 495  ? 0.7729 0.7232 0.8301 0.0046  -0.0045 -0.0131 493  ASN A C   
3550  O O   . ASN A 495  ? 0.8027 0.7517 0.8676 0.0052  -0.0072 -0.0169 493  ASN A O   
3551  C CB  . ASN A 495  ? 0.7618 0.7167 0.8144 0.0034  -0.0041 -0.0172 493  ASN A CB  
3552  N N   . GLY A 496  ? 0.7980 0.7485 0.8500 0.0052  -0.0026 -0.0109 494  GLY A N   
3553  C CA  . GLY A 496  ? 0.7946 0.7440 0.8496 0.0064  -0.0036 -0.0123 494  GLY A CA  
3554  C C   . GLY A 496  ? 0.8388 0.7854 0.8966 0.0063  -0.0037 -0.0063 494  GLY A C   
3555  O O   . GLY A 496  ? 0.8704 0.8155 0.9324 0.0072  -0.0050 -0.0067 494  GLY A O   
3556  N N   . ALA A 497  ? 0.7904 0.7368 0.8459 0.0052  -0.0024 -0.0006 495  ALA A N   
3557  C CA  . ALA A 497  ? 0.7370 0.6821 0.7950 0.0049  -0.0024 0.0056  495  ALA A CA  
3558  C C   . ALA A 497  ? 0.7687 0.7110 0.8379 0.0045  -0.0056 0.0070  495  ALA A C   
3559  O O   . ALA A 497  ? 0.7159 0.6574 0.7901 0.0037  -0.0072 0.0058  495  ALA A O   
3560  C CB  . ALA A 497  ? 0.7195 0.6663 0.7724 0.0040  -0.0001 0.0108  495  ALA A CB  
3561  N N   . ASN A 498  ? 0.8930 0.8338 0.9666 0.0049  -0.0067 0.0098  496  ASN A N   
3562  C CA  . ASN A 498  ? 0.8589 0.7968 0.9442 0.0045  -0.0102 0.0116  496  ASN A CA  
3563  C C   . ASN A 498  ? 0.8023 0.7402 0.8916 0.0027  -0.0107 0.0173  496  ASN A C   
3564  O O   . ASN A 498  ? 0.8405 0.7758 0.9403 0.0020  -0.0139 0.0181  496  ASN A O   
3565  C CB  . ASN A 498  ? 0.8597 0.7966 0.9483 0.0052  -0.0112 0.0149  496  ASN A CB  
3566  N N   . SER A 499  ? 0.6850 0.6259 0.7669 0.0020  -0.0078 0.0212  497  SER A N   
3567  C CA  . SER A 499  ? 0.6604 0.6022 0.7456 0.0003  -0.0080 0.0263  497  SER A CA  
3568  C C   . SER A 499  ? 0.5546 0.4959 0.6405 -0.0003 -0.0086 0.0221  497  SER A C   
3569  O O   . SER A 499  ? 0.5219 0.4632 0.6134 -0.0018 -0.0097 0.0255  497  SER A O   
3570  C CB  . SER A 499  ? 0.5823 0.5282 0.6597 0.0000  -0.0048 0.0317  497  SER A CB  
3571  O OG  . SER A 499  ? 0.6258 0.5733 0.6927 0.0010  -0.0020 0.0279  497  SER A OG  
3572  N N   . SER A 500  ? 0.5710 0.5125 0.6519 0.0007  -0.0079 0.0152  498  SER A N   
3573  C CA  . SER A 500  ? 0.5405 0.4826 0.6208 0.0002  -0.0081 0.0113  498  SER A CA  
3574  C C   . SER A 500  ? 0.5736 0.5130 0.6646 -0.0002 -0.0120 0.0080  498  SER A C   
3575  O O   . SER A 500  ? 0.5585 0.4959 0.6547 0.0009  -0.0142 0.0042  498  SER A O   
3576  C CB  . SER A 500  ? 0.5922 0.5363 0.6637 0.0013  -0.0062 0.0055  498  SER A CB  
3577  O OG  . SER A 500  ? 0.6494 0.5957 0.7114 0.0014  -0.0029 0.0083  498  SER A OG  
3578  N N   . PHE A 501  ? 0.4547 0.3943 0.5493 -0.0015 -0.0129 0.0090  499  PHE A N   
3579  C CA  . PHE A 501  ? 0.4536 0.3907 0.5584 -0.0019 -0.0168 0.0052  499  PHE A CA  
3580  C C   . PHE A 501  ? 0.5061 0.4436 0.6097 -0.0003 -0.0177 -0.0040 499  PHE A C   
3581  O O   . PHE A 501  ? 0.5000 0.4351 0.6124 0.0004  -0.0211 -0.0083 499  PHE A O   
3582  C CB  . PHE A 501  ? 0.3773 0.3154 0.4842 -0.0036 -0.0171 0.0072  499  PHE A CB  
3583  C CG  . PHE A 501  ? 0.3778 0.3136 0.4953 -0.0041 -0.0212 0.0030  499  PHE A CG  
3584  C CD1 . PHE A 501  ? 0.3970 0.3340 0.5129 -0.0033 -0.0220 -0.0050 499  PHE A CD1 
3585  C CD2 . PHE A 501  ? 0.3644 0.2971 0.4937 -0.0053 -0.0245 0.0072  499  PHE A CD2 
3586  C CE1 . PHE A 501  ? 0.3903 0.3255 0.5162 -0.0035 -0.0261 -0.0095 499  PHE A CE1 
3587  C CE2 . PHE A 501  ? 0.3771 0.3074 0.5171 -0.0058 -0.0287 0.0031  499  PHE A CE2 
3588  C CZ  . PHE A 501  ? 0.3892 0.3207 0.5274 -0.0047 -0.0295 -0.0056 499  PHE A CZ  
3589  N N   . VAL A 502  ? 0.5031 0.4440 0.5964 0.0003  -0.0149 -0.0072 500  VAL A N   
3590  C CA  . VAL A 502  ? 0.5327 0.4756 0.6243 0.0017  -0.0156 -0.0156 500  VAL A CA  
3591  C C   . VAL A 502  ? 0.5899 0.5318 0.6838 0.0034  -0.0165 -0.0186 500  VAL A C   
3592  O O   . VAL A 502  ? 0.5955 0.5374 0.6949 0.0046  -0.0191 -0.0253 500  VAL A O   
3593  C CB  . VAL A 502  ? 0.5457 0.4930 0.6258 0.0017  -0.0124 -0.0170 500  VAL A CB  
3594  N N   . HIS A 503  ? 0.5948 0.5360 0.6846 0.0036  -0.0146 -0.0140 501  HIS A N   
3595  C CA  . HIS A 503  ? 0.6190 0.5591 0.7114 0.0052  -0.0155 -0.0161 501  HIS A CA  
3596  C C   . HIS A 503  ? 0.6223 0.5581 0.7277 0.0053  -0.0196 -0.0157 501  HIS A C   
3597  O O   . HIS A 503  ? 0.5997 0.5347 0.7107 0.0068  -0.0220 -0.0214 501  HIS A O   
3598  C CB  . HIS A 503  ? 0.6975 0.6379 0.7829 0.0053  -0.0126 -0.0107 501  HIS A CB  
3599  C CG  . HIS A 503  ? 0.7611 0.7008 0.8480 0.0069  -0.0132 -0.0128 501  HIS A CG  
3600  N ND1 . HIS A 503  ? 0.7569 0.6936 0.8504 0.0070  -0.0149 -0.0085 501  HIS A ND1 
3601  C CD2 . HIS A 503  ? 0.7495 0.6917 0.8324 0.0084  -0.0125 -0.0184 501  HIS A CD2 
3602  C CE1 . HIS A 503  ? 0.7552 0.6920 0.8486 0.0086  -0.0151 -0.0117 501  HIS A CE1 
3603  N NE2 . HIS A 503  ? 0.7415 0.6818 0.8286 0.0095  -0.0137 -0.0178 501  HIS A NE2 
3604  N N   . ARG A 504  ? 0.5715 0.5049 0.6823 0.0036  -0.0205 -0.0090 502  ARG A N   
3605  C CA  . ARG A 504  ? 0.5732 0.5024 0.6972 0.0034  -0.0246 -0.0073 502  ARG A CA  
3606  C C   . ARG A 504  ? 0.5778 0.5056 0.7108 0.0037  -0.0284 -0.0143 502  ARG A C   
3607  O O   . ARG A 504  ? 0.5509 0.4757 0.6941 0.0048  -0.0321 -0.0175 502  ARG A O   
3608  C CB  . ARG A 504  ? 0.5689 0.4970 0.6962 0.0012  -0.0246 0.0023  502  ARG A CB  
3609  C CG  . ARG A 504  ? 0.5503 0.4798 0.6711 0.0012  -0.0217 0.0090  502  ARG A CG  
3610  C CD  . ARG A 504  ? 0.5900 0.5210 0.7102 -0.0009 -0.0204 0.0178  502  ARG A CD  
3611  N NE  . ARG A 504  ? 0.5886 0.5170 0.7217 -0.0025 -0.0241 0.0218  502  ARG A NE  
3612  C CZ  . ARG A 504  ? 0.5780 0.5043 0.7199 -0.0028 -0.0266 0.0266  502  ARG A CZ  
3613  N NH1 . ARG A 504  ? 0.5877 0.5141 0.7270 -0.0016 -0.0258 0.0275  502  ARG A NH1 
3614  N NH2 . ARG A 504  ? 0.5547 0.4787 0.7087 -0.0046 -0.0302 0.0307  502  ARG A NH2 
3615  N N   . ILE A 505  ? 0.5713 0.5014 0.7010 0.0030  -0.0278 -0.0171 503  ILE A N   
3616  C CA  . ILE A 505  ? 0.5541 0.4835 0.6919 0.0034  -0.0315 -0.0242 503  ILE A CA  
3617  C C   . ILE A 505  ? 0.6085 0.5391 0.7476 0.0060  -0.0329 -0.0334 503  ILE A C   
3618  O O   . ILE A 505  ? 0.5855 0.5143 0.7353 0.0070  -0.0371 -0.0392 503  ILE A O   
3619  C CB  . ILE A 505  ? 0.4871 0.4199 0.6191 0.0024  -0.0300 -0.0258 503  ILE A CB  
3620  N N   . ASN A 506  ? 0.6004 0.5344 0.7293 0.0073  -0.0296 -0.0350 504  ASN A N   
3621  C CA  . ASN A 506  ? 0.6449 0.5813 0.7742 0.0098  -0.0304 -0.0432 504  ASN A CA  
3622  C C   . ASN A 506  ? 0.6535 0.5864 0.7892 0.0110  -0.0321 -0.0420 504  ASN A C   
3623  O O   . ASN A 506  ? 0.6935 0.6271 0.8341 0.0133  -0.0343 -0.0492 504  ASN A O   
3624  C CB  . ASN A 506  ? 0.6424 0.5847 0.7580 0.0104  -0.0262 -0.0453 504  ASN A CB  
3625  C CG  . ASN A 506  ? 0.6558 0.6021 0.7650 0.0093  -0.0247 -0.0469 504  ASN A CG  
3626  O OD1 . ASN A 506  ? 0.6931 0.6393 0.8083 0.0091  -0.0273 -0.0505 504  ASN A OD1 
3627  N ND2 . ASN A 506  ? 0.7074 0.6574 0.8048 0.0088  -0.0207 -0.0443 504  ASN A ND2 
3628  N N   . ASP A 507  ? 0.6518 0.5815 0.7876 0.0098  -0.0311 -0.0331 505  ASP A N   
3629  C CA  . ASP A 507  ? 0.6824 0.6091 0.8240 0.0108  -0.0327 -0.0309 505  ASP A CA  
3630  C C   . ASP A 507  ? 0.7080 0.6299 0.8657 0.0111  -0.0382 -0.0327 505  ASP A C   
3631  O O   . ASP A 507  ? 0.6597 0.5784 0.8243 0.0091  -0.0401 -0.0271 505  ASP A O   
3632  C CB  . ASP A 507  ? 0.6937 0.6193 0.8309 0.0092  -0.0302 -0.0205 505  ASP A CB  
3633  C CG  . ASP A 507  ? 0.7184 0.6418 0.8600 0.0102  -0.0313 -0.0178 505  ASP A CG  
3634  O OD1 . ASP A 507  ? 0.7517 0.6734 0.9014 0.0120  -0.0344 -0.0234 505  ASP A OD1 
3635  O OD2 . ASP A 507  ? 0.6957 0.6193 0.8325 0.0092  -0.0290 -0.0101 505  ASP A OD2 
3636  N N   . PRO A 508  ? 0.8373 0.7587 1.0017 0.0136  -0.0410 -0.0403 506  PRO A N   
3637  C CA  . PRO A 508  ? 0.7766 0.6930 0.9575 0.0140  -0.0468 -0.0423 506  PRO A CA  
3638  C C   . PRO A 508  ? 0.7602 0.6715 0.9491 0.0127  -0.0486 -0.0328 506  PRO A C   
3639  O O   . PRO A 508  ? 0.8120 0.7186 1.0146 0.0119  -0.0532 -0.0313 506  PRO A O   
3640  C CB  . PRO A 508  ? 0.8045 0.7226 0.9889 0.0174  -0.0487 -0.0527 506  PRO A CB  
3641  C CG  . PRO A 508  ? 0.8364 0.7616 1.0058 0.0184  -0.0439 -0.0569 506  PRO A CG  
3642  C CD  . PRO A 508  ? 0.7862 0.7120 0.9442 0.0161  -0.0393 -0.0474 506  PRO A CD  
3643  N N   . LYS A 509  ? 0.6924 0.6048 0.8733 0.0123  -0.0452 -0.0261 507  LYS A N   
3644  C CA  . LYS A 509  ? 0.6854 0.5943 0.8732 0.0111  -0.0467 -0.0167 507  LYS A CA  
3645  C C   . LYS A 509  ? 0.6655 0.5733 0.8553 0.0079  -0.0467 -0.0074 507  LYS A C   
3646  O O   . LYS A 509  ? 0.7179 0.6232 0.9147 0.0065  -0.0484 0.0010  507  LYS A O   
3647  C CB  . LYS A 509  ? 0.6994 0.6108 0.8774 0.0117  -0.0431 -0.0129 507  LYS A CB  
3648  N N   . VAL A 510  ? 0.6590 0.5689 0.8428 0.0066  -0.0448 -0.0083 508  VAL A N   
3649  C CA  . VAL A 510  ? 0.6225 0.5321 0.8083 0.0037  -0.0446 0.0001  508  VAL A CA  
3650  C C   . VAL A 510  ? 0.5406 0.4474 0.7377 0.0029  -0.0489 -0.0037 508  VAL A C   
3651  O O   . VAL A 510  ? 0.5350 0.4429 0.7305 0.0043  -0.0493 -0.0130 508  VAL A O   
3652  C CB  . VAL A 510  ? 0.6055 0.5199 0.7760 0.0026  -0.0390 0.0034  508  VAL A CB  
3653  C CG1 . VAL A 510  ? 0.6205 0.5378 0.7789 0.0041  -0.0350 0.0029  508  VAL A CG1 
3654  C CG2 . VAL A 510  ? 0.5941 0.5105 0.7600 0.0025  -0.0381 -0.0030 508  VAL A CG2 
3655  N N   . SER A 511  ? 0.5462 0.4499 0.7552 0.0008  -0.0523 0.0034  509  SER A N   
3656  C CA  . SER A 511  ? 0.5042 0.4078 0.7232 0.0000  -0.0564 0.0004  509  SER A CA  
3657  C C   . SER A 511  ? 0.5033 0.4075 0.7186 -0.0021 -0.0547 0.0024  509  SER A C   
3658  O O   . SER A 511  ? 0.4984 0.4052 0.7029 -0.0032 -0.0502 0.0079  509  SER A O   
3659  C CB  . SER A 511  ? 0.5240 0.4280 0.7551 -0.0016 -0.0602 0.0075  509  SER A CB  
3660  O OG  . SER A 511  ? 0.5254 0.4310 0.7539 -0.0041 -0.0580 0.0193  509  SER A OG  
3661  N N   . ILE A 512  ? 0.4679 0.3722 0.6906 -0.0025 -0.0580 -0.0025 510  ILE A N   
3662  C CA  . ILE A 512  ? 0.4812 0.3861 0.7021 -0.0047 -0.0570 -0.0001 510  ILE A CA  
3663  C C   . ILE A 512  ? 0.4919 0.3982 0.7158 -0.0077 -0.0566 0.0125  510  ILE A C   
3664  O O   . ILE A 512  ? 0.4863 0.3938 0.7041 -0.0095 -0.0536 0.0176  510  ILE A O   
3665  C CB  . ILE A 512  ? 0.4592 0.3643 0.6881 -0.0043 -0.0611 -0.0081 510  ILE A CB  
3666  C CG1 . ILE A 512  ? 0.4383 0.3439 0.6628 -0.0011 -0.0609 -0.0207 510  ILE A CG1 
3667  C CG2 . ILE A 512  ? 0.4633 0.3692 0.6913 -0.0067 -0.0603 -0.0054 510  ILE A CG2 
3668  C CD1 . ILE A 512  ? 0.4540 0.3609 0.6835 -0.0005 -0.0640 -0.0294 510  ILE A CD1 
3669  N N   . ASP A 513  ? 0.4532 0.3599 0.6863 -0.0082 -0.0596 0.0176  511  ASP A N   
3670  C CA  . ASP A 513  ? 0.4933 0.4026 0.7290 -0.0110 -0.0591 0.0298  511  ASP A CA  
3671  C C   . ASP A 513  ? 0.4824 0.3935 0.7058 -0.0114 -0.0537 0.0363  511  ASP A C   
3672  O O   . ASP A 513  ? 0.4699 0.3840 0.6903 -0.0136 -0.0515 0.0441  511  ASP A O   
3673  C CB  . ASP A 513  ? 0.5237 0.4335 0.7706 -0.0111 -0.0630 0.0336  511  ASP A CB  
3674  C CG  . ASP A 513  ? 0.5836 0.4935 0.8446 -0.0123 -0.0683 0.0334  511  ASP A CG  
3675  O OD1 . ASP A 513  ? 0.5542 0.4639 0.8162 -0.0130 -0.0689 0.0303  511  ASP A OD1 
3676  O OD2 . ASP A 513  ? 0.6826 0.5929 0.9542 -0.0125 -0.0721 0.0364  511  ASP A OD2 
3677  N N   . GLU A 514  ? 0.4621 0.3718 0.6784 -0.0092 -0.0516 0.0332  512  GLU A N   
3678  C CA  . GLU A 514  ? 0.4642 0.3761 0.6684 -0.0093 -0.0465 0.0386  512  GLU A CA  
3679  C C   . GLU A 514  ? 0.4670 0.3829 0.6583 -0.0093 -0.0421 0.0355  512  GLU A C   
3680  O O   . GLU A 514  ? 0.4763 0.3969 0.6580 -0.0101 -0.0380 0.0414  512  GLU A O   
3681  C CB  . GLU A 514  ? 0.5328 0.4444 0.7313 -0.0067 -0.0451 0.0350  512  GLU A CB  
3682  C CG  . GLU A 514  ? 0.5511 0.4616 0.7593 -0.0067 -0.0484 0.0393  512  GLU A CG  
3683  C CD  . GLU A 514  ? 0.6152 0.5239 0.8194 -0.0040 -0.0476 0.0349  512  GLU A CD  
3684  O OE1 . GLU A 514  ? 0.6049 0.5127 0.8039 -0.0017 -0.0467 0.0251  512  GLU A OE1 
3685  O OE2 . GLU A 514  ? 0.6652 0.5755 0.8704 -0.0041 -0.0476 0.0410  512  GLU A OE2 
3686  N N   . LEU A 515  ? 0.4758 0.3904 0.6667 -0.0082 -0.0431 0.0261  513  LEU A N   
3687  C CA  . LEU A 515  ? 0.4661 0.3844 0.6451 -0.0082 -0.0393 0.0230  513  LEU A CA  
3688  C C   . LEU A 515  ? 0.4413 0.3611 0.6239 -0.0108 -0.0396 0.0284  513  LEU A C   
3689  O O   . LEU A 515  ? 0.3990 0.3229 0.5713 -0.0112 -0.0358 0.0297  513  LEU A O   
3690  C CB  . LEU A 515  ? 0.4425 0.3600 0.6195 -0.0062 -0.0401 0.0113  513  LEU A CB  
3691  C CG  . LEU A 515  ? 0.4834 0.4013 0.6537 -0.0034 -0.0387 0.0048  513  LEU A CG  
3692  C CD1 . LEU A 515  ? 0.4637 0.3818 0.6345 -0.0016 -0.0403 -0.0065 513  LEU A CD1 
3693  C CD2 . LEU A 515  ? 0.4526 0.3748 0.6075 -0.0030 -0.0331 0.0076  513  LEU A CD2 
3694  N N   . ILE A 516  ? 0.4163 0.3329 0.6135 -0.0125 -0.0443 0.0315  514  ILE A N   
3695  C CA  . ILE A 516  ? 0.4159 0.3340 0.6179 -0.0153 -0.0450 0.0371  514  ILE A CA  
3696  C C   . ILE A 516  ? 0.4001 0.3209 0.6050 -0.0175 -0.0442 0.0495  514  ILE A C   
3697  O O   . ILE A 516  ? 0.3935 0.3160 0.6042 -0.0200 -0.0452 0.0557  514  ILE A O   
3698  C CB  . ILE A 516  ? 0.4139 0.3274 0.6307 -0.0161 -0.0508 0.0329  514  ILE A CB  
3699  C CG1 . ILE A 516  ? 0.4594 0.3726 0.6875 -0.0160 -0.0549 0.0354  514  ILE A CG1 
3700  C CG2 . ILE A 516  ? 0.4224 0.3347 0.6356 -0.0137 -0.0514 0.0202  514  ILE A CG2 
3701  C CD1 . ILE A 516  ? 0.4356 0.3480 0.6766 -0.0165 -0.0603 0.0317  514  ILE A CD1 
3702  N N   . ALA A 517  ? 0.3867 0.3085 0.5876 -0.0166 -0.0425 0.0533  515  ALA A N   
3703  C CA  . ALA A 517  ? 0.3758 0.3019 0.5774 -0.0185 -0.0412 0.0650  515  ALA A CA  
3704  C C   . ALA A 517  ? 0.3909 0.3235 0.5823 -0.0194 -0.0367 0.0688  515  ALA A C   
3705  O O   . ALA A 517  ? 0.3554 0.2900 0.5337 -0.0177 -0.0327 0.0635  515  ALA A O   
3706  C CB  . ALA A 517  ? 0.4068 0.3338 0.6031 -0.0169 -0.0394 0.0670  515  ALA A CB  
3707  N N   . ASP A 518  ? 0.3457 0.2817 0.5435 -0.0221 -0.0374 0.0780  516  ASP A N   
3708  C CA  . ASP A 518  ? 0.3509 0.2936 0.5410 -0.0231 -0.0335 0.0824  516  ASP A CA  
3709  C C   . ASP A 518  ? 0.3338 0.2829 0.5125 -0.0222 -0.0289 0.0873  516  ASP A C   
3710  O O   . ASP A 518  ? 0.3625 0.3146 0.5454 -0.0232 -0.0294 0.0956  516  ASP A O   
3711  C CB  . ASP A 518  ? 0.3609 0.3067 0.5622 -0.0262 -0.0361 0.0901  516  ASP A CB  
3712  C CG  . ASP A 518  ? 0.3818 0.3342 0.5772 -0.0275 -0.0325 0.0957  516  ASP A CG  
3713  O OD1 . ASP A 518  ? 0.3617 0.3170 0.5434 -0.0256 -0.0280 0.0915  516  ASP A OD1 
3714  O OD2 . ASP A 518  ? 0.4357 0.3936 0.6377 -0.0296 -0.0338 0.1021  516  ASP A OD2 
3715  N N   . PRO A 519  ? 0.3612 0.3130 0.5257 -0.0202 -0.0244 0.0825  517  PRO A N   
3716  C CA  . PRO A 519  ? 0.3627 0.3204 0.5167 -0.0191 -0.0203 0.0864  517  PRO A CA  
3717  C C   . PRO A 519  ? 0.2938 0.2597 0.4487 -0.0210 -0.0187 0.0966  517  PRO A C   
3718  O O   . PRO A 519  ? 0.3310 0.3022 0.4820 -0.0207 -0.0167 0.1021  517  PRO A O   
3719  C CB  . PRO A 519  ? 0.3155 0.2734 0.4558 -0.0168 -0.0165 0.0784  517  PRO A CB  
3720  C CG  . PRO A 519  ? 0.3508 0.3062 0.4942 -0.0176 -0.0179 0.0739  517  PRO A CG  
3721  C CD  . PRO A 519  ? 0.3233 0.2732 0.4812 -0.0191 -0.0231 0.0738  517  PRO A CD  
3722  N N   . VAL A 520  ? 0.3173 0.2851 0.4775 -0.0230 -0.0195 0.0991  518  VAL A N   
3723  C CA  . VAL A 520  ? 0.3200 0.2965 0.4813 -0.0248 -0.0179 0.1088  518  VAL A CA  
3724  C C   . VAL A 520  ? 0.3417 0.3203 0.5135 -0.0268 -0.0206 0.1183  518  VAL A C   
3725  O O   . VAL A 520  ? 0.3427 0.3294 0.5109 -0.0269 -0.0184 0.1254  518  VAL A O   
3726  C CB  . VAL A 520  ? 0.3120 0.2895 0.4781 -0.0266 -0.0187 0.1093  518  VAL A CB  
3727  C CG1 . VAL A 520  ? 0.3212 0.3088 0.4894 -0.0286 -0.0172 0.1196  518  VAL A CG1 
3728  C CG2 . VAL A 520  ? 0.3331 0.3093 0.4885 -0.0246 -0.0160 0.1004  518  VAL A CG2 
3729  N N   . GLU A 521  ? 0.3371 0.3101 0.5206 -0.0277 -0.0255 0.1168  519  GLU A N   
3730  C CA  . GLU A 521  ? 0.3458 0.3230 0.5378 -0.0288 -0.0284 0.1230  519  GLU A CA  
3731  C C   . GLU A 521  ? 0.3735 0.3502 0.5615 -0.0272 -0.0277 0.1235  519  GLU A C   
3732  O O   . GLU A 521  ? 0.3791 0.3629 0.5693 -0.0279 -0.0280 0.1306  519  GLU A O   
3733  C CB  . GLU A 521  ? 0.4033 0.3752 0.6092 -0.0300 -0.0341 0.1205  519  GLU A CB  
3734  C CG  . GLU A 521  ? 0.4164 0.3899 0.6277 -0.0319 -0.0353 0.1214  519  GLU A CG  
3735  C CD  . GLU A 521  ? 0.4738 0.4586 0.6846 -0.0336 -0.0333 0.1310  519  GLU A CD  
3736  O OE1 . GLU A 521  ? 0.5068 0.4981 0.7199 -0.0341 -0.0337 0.1379  519  GLU A OE1 
3737  O OE2 . GLU A 521  ? 0.4869 0.4747 0.6951 -0.0344 -0.0314 0.1316  519  GLU A OE2 
3738  N N   . VAL A 522  ? 0.3662 0.3353 0.5485 -0.0251 -0.0269 0.1160  520  VAL A N   
3739  C CA  . VAL A 522  ? 0.3258 0.2944 0.5037 -0.0235 -0.0260 0.1163  520  VAL A CA  
3740  C C   . VAL A 522  ? 0.4092 0.3868 0.5764 -0.0230 -0.0213 0.1222  520  VAL A C   
3741  O O   . VAL A 522  ? 0.3774 0.3603 0.5442 -0.0229 -0.0212 0.1273  520  VAL A O   
3742  C CB  . VAL A 522  ? 0.3817 0.3411 0.5552 -0.0210 -0.0261 0.1062  520  VAL A CB  
3743  C CG1 . VAL A 522  ? 0.4005 0.3607 0.5682 -0.0191 -0.0248 0.1062  520  VAL A CG1 
3744  C CG2 . VAL A 522  ? 0.4097 0.3610 0.5948 -0.0213 -0.0311 0.1005  520  VAL A CG2 
3745  N N   . VAL A 523  ? 0.3253 0.3064 0.4827 -0.0222 -0.0175 0.1197  521  VAL A N   
3746  C CA  . VAL A 523  ? 0.3329 0.3239 0.4797 -0.0213 -0.0131 0.1237  521  VAL A CA  
3747  C C   . VAL A 523  ? 0.3792 0.3798 0.5325 -0.0238 -0.0135 0.1352  521  VAL A C   
3748  O O   . VAL A 523  ? 0.3414 0.3501 0.4905 -0.0234 -0.0118 0.1403  521  VAL A O   
3749  C CB  . VAL A 523  ? 0.3122 0.3050 0.4475 -0.0197 -0.0092 0.1173  521  VAL A CB  
3750  C CG1 . VAL A 523  ? 0.3517 0.3558 0.4785 -0.0190 -0.0051 0.1221  521  VAL A CG1 
3751  C CG2 . VAL A 523  ? 0.3444 0.3302 0.4712 -0.0169 -0.0082 0.1067  521  VAL A CG2 
3752  N N   . ARG A 524  ? 0.3515 0.3529 0.5136 -0.0259 -0.0159 0.1371  522  ARG A N   
3753  C CA  . ARG A 524  ? 0.3701 0.3827 0.5372 -0.0278 -0.0163 0.1456  522  ARG A CA  
3754  C C   . ARG A 524  ? 0.3996 0.4157 0.5726 -0.0283 -0.0188 0.1508  522  ARG A C   
3755  O O   . ARG A 524  ? 0.4283 0.4558 0.6008 -0.0290 -0.0177 0.1580  522  ARG A O   
3756  C CB  . ARG A 524  ? 0.4199 0.4315 0.5970 -0.0299 -0.0192 0.1464  522  ARG A CB  
3757  C CG  . ARG A 524  ? 0.3898 0.4133 0.5728 -0.0319 -0.0199 0.1555  522  ARG A CG  
3758  C CD  . ARG A 524  ? 0.4185 0.4392 0.6147 -0.0342 -0.0245 0.1565  522  ARG A CD  
3759  N NE  . ARG A 524  ? 0.4262 0.4395 0.6216 -0.0341 -0.0243 0.1499  522  ARG A NE  
3760  C CZ  . ARG A 524  ? 0.3981 0.4159 0.5882 -0.0343 -0.0213 0.1504  522  ARG A CZ  
3761  N NH1 . ARG A 524  ? 0.4066 0.4364 0.5914 -0.0343 -0.0180 0.1565  522  ARG A NH1 
3762  N NH2 . ARG A 524  ? 0.4094 0.4200 0.5997 -0.0343 -0.0217 0.1443  522  ARG A NH2 
3763  N N   . ALA A 525  ? 0.4126 0.4197 0.5916 -0.0280 -0.0222 0.1470  523  ALA A N   
3764  C CA  . ALA A 525  ? 0.4171 0.4263 0.6033 -0.0286 -0.0252 0.1514  523  ALA A CA  
3765  C C   . ALA A 525  ? 0.4171 0.4278 0.5946 -0.0266 -0.0229 0.1515  523  ALA A C   
3766  O O   . ALA A 525  ? 0.4386 0.4522 0.6213 -0.0271 -0.0250 0.1556  523  ALA A O   
3767  C CB  . ALA A 525  ? 0.3839 0.3829 0.5820 -0.0291 -0.0305 0.1471  523  ALA A CB  
3768  N N   . MET A 526  ? 0.4105 0.4195 0.5757 -0.0246 -0.0188 0.1470  524  MET A N   
3769  C CA  A MET A 526  ? 0.4356 0.4466 0.5922 -0.0226 -0.0166 0.1472  524  MET A CA  
3770  C CA  B MET A 526  ? 0.4356 0.4467 0.5920 -0.0226 -0.0165 0.1472  524  MET A CA  
3771  C C   . MET A 526  ? 0.4562 0.4812 0.6107 -0.0233 -0.0150 0.1557  524  MET A C   
3772  O O   . MET A 526  ? 0.4084 0.4422 0.5635 -0.0245 -0.0138 0.1601  524  MET A O   
3773  C CB  A MET A 526  ? 0.4492 0.4568 0.5931 -0.0204 -0.0125 0.1413  524  MET A CB  
3774  C CB  B MET A 526  ? 0.4492 0.4572 0.5929 -0.0204 -0.0123 0.1415  524  MET A CB  
3775  C CG  A MET A 526  ? 0.4253 0.4201 0.5698 -0.0192 -0.0139 0.1317  524  MET A CG  
3776  C CG  B MET A 526  ? 0.4406 0.4384 0.5810 -0.0182 -0.0129 0.1333  524  MET A CG  
3777  S SD  A MET A 526  ? 0.5003 0.4865 0.6522 -0.0186 -0.0179 0.1297  524  MET A SD  
3778  S SD  B MET A 526  ? 0.4519 0.4437 0.5823 -0.0160 -0.0104 0.1205  524  MET A SD  
3779  C CE  A MET A 526  ? 0.4588 0.4509 0.5979 -0.0161 -0.0143 0.1296  524  MET A CE  
3780  C CE  B MET A 526  ? 0.4226 0.4257 0.5397 -0.0148 -0.0050 0.1219  524  MET A CE  
3781  N N   . PRO A 527  ? 0.5022 0.5301 0.6548 -0.0224 -0.0151 0.1579  525  PRO A N   
3782  C CA  . PRO A 527  ? 0.4758 0.5178 0.6270 -0.0231 -0.0139 0.1659  525  PRO A CA  
3783  C C   . PRO A 527  ? 0.4306 0.4821 0.5697 -0.0218 -0.0089 0.1664  525  PRO A C   
3784  O O   . PRO A 527  ? 0.4182 0.4819 0.5580 -0.0228 -0.0079 0.1723  525  PRO A O   
3785  C CB  . PRO A 527  ? 0.4551 0.4961 0.6055 -0.0220 -0.0149 0.1664  525  PRO A CB  
3786  C CG  . PRO A 527  ? 0.4832 0.5117 0.6287 -0.0200 -0.0144 0.1580  525  PRO A CG  
3787  C CD  . PRO A 527  ? 0.4622 0.4813 0.6137 -0.0208 -0.0162 0.1532  525  PRO A CD  
3788  N N   . VAL A 528  ? 0.4584 0.5051 0.5868 -0.0194 -0.0058 0.1603  526  VAL A N   
3789  C CA  . VAL A 528  ? 0.3884 0.4424 0.5055 -0.0179 -0.0012 0.1593  526  VAL A CA  
3790  C C   . VAL A 528  ? 0.4092 0.4536 0.5249 -0.0176 -0.0004 0.1531  526  VAL A C   
3791  O O   . VAL A 528  ? 0.4125 0.4464 0.5252 -0.0160 -0.0009 0.1441  526  VAL A O   
3792  C CB  . VAL A 528  ? 0.3997 0.4574 0.5052 -0.0153 0.0018  0.1575  526  VAL A CB  
3793  C CG1 . VAL A 528  ? 0.3808 0.4470 0.4750 -0.0133 0.0063  0.1543  526  VAL A CG1 
3794  C CG2 . VAL A 528  ? 0.4487 0.5151 0.5566 -0.0157 0.0006  0.1633  526  VAL A CG2 
3795  N N   . VAL A 529  ? 0.3371 0.3860 0.4545 -0.0188 0.0004  0.1547  527  VAL A N   
3796  C CA  . VAL A 529  ? 0.3250 0.3660 0.4410 -0.0184 0.0009  0.1473  527  VAL A CA  
3797  C C   . VAL A 529  ? 0.3763 0.4179 0.4781 -0.0150 0.0047  0.1383  527  VAL A C   
3798  O O   . VAL A 529  ? 0.3510 0.4032 0.4453 -0.0137 0.0079  0.1400  527  VAL A O   
3799  C CB  . VAL A 529  ? 0.3260 0.3720 0.4481 -0.0207 0.0007  0.1525  527  VAL A CB  
3800  C CG1 . VAL A 529  ? 0.3346 0.3741 0.4530 -0.0197 0.0017  0.1438  527  VAL A CG1 
3801  C CG2 . VAL A 529  ? 0.3501 0.3938 0.4861 -0.0233 -0.0041 0.1562  527  VAL A CG2 
3802  N N   . GLY A 530  ? 0.3175 0.3481 0.4161 -0.0135 0.0043  0.1289  528  GLY A N   
3803  C CA  . GLY A 530  ? 0.2927 0.3226 0.3792 -0.0106 0.0075  0.1204  528  GLY A CA  
3804  C C   . GLY A 530  ? 0.3137 0.3458 0.3916 -0.0082 0.0091  0.1179  528  GLY A C   
3805  O O   . GLY A 530  ? 0.3109 0.3454 0.3790 -0.0058 0.0119  0.1124  528  GLY A O   
3806  N N   . ALA A 531  ? 0.3376 0.3689 0.4194 -0.0087 0.0072  0.1216  529  ALA A N   
3807  C CA  . ALA A 531  ? 0.3047 0.3379 0.3787 -0.0065 0.0085  0.1191  529  ALA A CA  
3808  C C   . ALA A 531  ? 0.3022 0.3264 0.3690 -0.0044 0.0093  0.1085  529  ALA A C   
3809  O O   . ALA A 531  ? 0.3166 0.3311 0.3872 -0.0049 0.0075  0.1039  529  ALA A O   
3810  C CB  . ALA A 531  ? 0.3294 0.3620 0.4100 -0.0077 0.0058  0.1248  529  ALA A CB  
3811  N N   . LYS A 532  ? 0.2845 0.3125 0.3413 -0.0020 0.0118  0.1047  530  LYS A N   
3812  C CA  . LYS A 532  ? 0.3250 0.3455 0.3752 0.0000  0.0124  0.0956  530  LYS A CA  
3813  C C   . LYS A 532  ? 0.3329 0.3448 0.3878 -0.0005 0.0097  0.0941  530  LYS A C   
3814  O O   . LYS A 532  ? 0.3123 0.3258 0.3730 -0.0015 0.0079  0.0999  530  LYS A O   
3815  C CB  . LYS A 532  ? 0.3394 0.3663 0.3796 0.0025  0.0149  0.0931  530  LYS A CB  
3816  C CG  . LYS A 532  ? 0.3559 0.3758 0.3892 0.0044  0.0155  0.0843  530  LYS A CG  
3817  C CD  . LYS A 532  ? 0.3117 0.3382 0.3362 0.0067  0.0175  0.0822  530  LYS A CD  
3818  C CE  . LYS A 532  ? 0.2921 0.3244 0.3176 0.0067  0.0169  0.0876  530  LYS A CE  
3819  N NZ  . LYS A 532  ? 0.3243 0.3487 0.3525 0.0064  0.0148  0.0860  530  LYS A NZ  
3820  N N   . HIS A 533  ? 0.2934 0.2965 0.3462 0.0003  0.0094  0.0863  531  HIS A N   
3821  C CA  . HIS A 533  ? 0.2998 0.2955 0.3555 0.0005  0.0073  0.0833  531  HIS A CA  
3822  C C   . HIS A 533  ? 0.3144 0.3140 0.3667 0.0016  0.0076  0.0853  531  HIS A C   
3823  O O   . HIS A 533  ? 0.2979 0.3024 0.3416 0.0032  0.0100  0.0835  531  HIS A O   
3824  C CB  . HIS A 533  ? 0.3051 0.2935 0.3561 0.0016  0.0078  0.0743  531  HIS A CB  
3825  C CG  . HIS A 533  ? 0.3125 0.2931 0.3683 0.0015  0.0053  0.0708  531  HIS A CG  
3826  N ND1 . HIS A 533  ? 0.3200 0.2997 0.3758 0.0023  0.0045  0.0709  531  HIS A ND1 
3827  C CD2 . HIS A 533  ? 0.3637 0.3374 0.4246 0.0009  0.0035  0.0669  531  HIS A CD2 
3828  C CE1 . HIS A 533  ? 0.3724 0.3451 0.4332 0.0022  0.0023  0.0671  531  HIS A CE1 
3829  N NE2 . HIS A 533  ? 0.3896 0.3588 0.4536 0.0014  0.0016  0.0644  531  HIS A NE2 
3830  N N   . ASP A 534  ? 0.3000 0.2973 0.3595 0.0008  0.0050  0.0887  532  ASP A N   
3831  C CA  . ASP A 534  ? 0.3525 0.3537 0.4098 0.0016  0.0050  0.0914  532  ASP A CA  
3832  C C   . ASP A 534  ? 0.3666 0.3646 0.4156 0.0037  0.0062  0.0839  532  ASP A C   
3833  O O   . ASP A 534  ? 0.4028 0.4059 0.4466 0.0049  0.0072  0.0849  532  ASP A O   
3834  C CB  . ASP A 534  ? 0.3905 0.3887 0.4582 0.0003  0.0015  0.0962  532  ASP A CB  
3835  C CG  . ASP A 534  ? 0.5038 0.5078 0.5795 -0.0019 0.0002  0.1060  532  ASP A CG  
3836  O OD1 . ASP A 534  ? 0.5423 0.5555 0.6139 -0.0020 0.0024  0.1101  532  ASP A OD1 
3837  O OD2 . ASP A 534  ? 0.6205 0.6203 0.7071 -0.0034 -0.0031 0.1096  532  ASP A OD2 
3838  N N   . ARG A 535  ? 0.3132 0.3034 0.3611 0.0042  0.0060  0.0766  533  ARG A N   
3839  C CA  . ARG A 535  ? 0.3501 0.3369 0.3916 0.0059  0.0068  0.0700  533  ARG A CA  
3840  C C   . ARG A 535  ? 0.3229 0.3105 0.3553 0.0071  0.0094  0.0646  533  ARG A C   
3841  O O   . ARG A 535  ? 0.3340 0.3179 0.3616 0.0082  0.0099  0.0586  533  ARG A O   
3842  C CB  . ARG A 535  ? 0.3577 0.3359 0.4045 0.0057  0.0046  0.0656  533  ARG A CB  
3843  C CG  . ARG A 535  ? 0.4592 0.4359 0.5153 0.0050  0.0016  0.0699  533  ARG A CG  
3844  C CD  . ARG A 535  ? 0.5158 0.4845 0.5769 0.0053  -0.0005 0.0644  533  ARG A CD  
3845  N N   . ILE A 536  ? 0.2972 0.2898 0.3272 0.0069  0.0110  0.0666  534  ILE A N   
3846  C CA  . ILE A 536  ? 0.2971 0.2909 0.3191 0.0082  0.0133  0.0618  534  ILE A CA  
3847  C C   . ILE A 536  ? 0.2990 0.3022 0.3162 0.0092  0.0150  0.0649  534  ILE A C   
3848  O O   . ILE A 536  ? 0.3071 0.3167 0.3271 0.0085  0.0152  0.0708  534  ILE A O   
3849  C CB  . ILE A 536  ? 0.3007 0.2922 0.3243 0.0073  0.0136  0.0603  534  ILE A CB  
3850  C CG1 . ILE A 536  ? 0.3298 0.3128 0.3578 0.0065  0.0118  0.0565  534  ILE A CG1 
3851  C CG2 . ILE A 536  ? 0.3049 0.2983 0.3207 0.0087  0.0158  0.0561  534  ILE A CG2 
3852  C CD1 . ILE A 536  ? 0.2866 0.2673 0.3168 0.0056  0.0118  0.0552  534  ILE A CD1 
3853  N N   . ALA A 537  ? 0.2587 0.2631 0.2686 0.0110  0.0161  0.0608  535  ALA A N   
3854  C CA  . ALA A 537  ? 0.2852 0.2989 0.2902 0.0124  0.0176  0.0626  535  ALA A CA  
3855  C C   . ALA A 537  ? 0.2843 0.3018 0.2856 0.0132  0.0194  0.0607  535  ALA A C   
3856  O O   . ALA A 537  ? 0.2646 0.2768 0.2634 0.0137  0.0198  0.0552  535  ALA A O   
3857  C CB  . ALA A 537  ? 0.2997 0.3132 0.2992 0.0140  0.0177  0.0586  535  ALA A CB  
3858  N N   . LEU A 538  ? 0.2743 0.3014 0.2756 0.0135  0.0204  0.0653  536  LEU A N   
3859  C CA  . LEU A 538  ? 0.2874 0.3194 0.2841 0.0150  0.0223  0.0627  536  LEU A CA  
3860  C C   . LEU A 538  ? 0.2606 0.2924 0.2504 0.0173  0.0229  0.0562  536  LEU A C   
3861  O O   . LEU A 538  ? 0.2653 0.2968 0.2533 0.0178  0.0222  0.0556  536  LEU A O   
3862  C CB  . LEU A 538  ? 0.2693 0.3135 0.2666 0.0152  0.0234  0.0686  536  LEU A CB  
3863  C CG  . LEU A 538  ? 0.2750 0.3212 0.2794 0.0129  0.0230  0.0754  536  LEU A CG  
3864  C CD1 . LEU A 538  ? 0.3547 0.4143 0.3595 0.0129  0.0239  0.0822  536  LEU A CD1 
3865  C CD2 . LEU A 538  ? 0.2683 0.3108 0.2734 0.0126  0.0236  0.0726  536  LEU A CD2 
3866  N N   . PRO A 539  ? 0.2439 0.2754 0.2300 0.0187  0.0239  0.0512  537  PRO A N   
3867  C CA  . PRO A 539  ? 0.2453 0.2756 0.2258 0.0208  0.0239  0.0448  537  PRO A CA  
3868  C C   . PRO A 539  ? 0.2452 0.2843 0.2222 0.0225  0.0243  0.0455  537  PRO A C   
3869  O O   . PRO A 539  ? 0.2580 0.2946 0.2322 0.0233  0.0236  0.0421  537  PRO A O   
3870  C CB  . PRO A 539  ? 0.2500 0.2801 0.2286 0.0220  0.0248  0.0407  537  PRO A CB  
3871  C CG  . PRO A 539  ? 0.2618 0.2874 0.2452 0.0199  0.0247  0.0433  537  PRO A CG  
3872  C CD  . PRO A 539  ? 0.2355 0.2656 0.2232 0.0183  0.0245  0.0506  537  PRO A CD  
3873  N N   . ALA A 540  ? 0.2414 0.2913 0.2187 0.0229  0.0253  0.0501  538  ALA A N   
3874  C CA  . ALA A 540  ? 0.2789 0.3388 0.2527 0.0246  0.0257  0.0511  538  ALA A CA  
3875  C C   . ALA A 540  ? 0.2881 0.3463 0.2633 0.0234  0.0244  0.0543  538  ALA A C   
3876  O O   . ALA A 540  ? 0.2930 0.3570 0.2646 0.0249  0.0242  0.0533  538  ALA A O   
3877  C CB  . ALA A 540  ? 0.3075 0.3803 0.2821 0.0249  0.0270  0.0564  538  ALA A CB  
3878  N N   . GLU A 541  ? 0.2771 0.3277 0.2575 0.0210  0.0232  0.0577  539  GLU A N   
3879  C CA  . GLU A 541  ? 0.3061 0.3558 0.2892 0.0199  0.0218  0.0617  539  GLU A CA  
3880  C C   . GLU A 541  ? 0.2853 0.3239 0.2684 0.0196  0.0206  0.0570  539  GLU A C   
3881  O O   . GLU A 541  ? 0.2946 0.3300 0.2811 0.0184  0.0192  0.0599  539  GLU A O   
3882  C CB  . GLU A 541  ? 0.3159 0.3667 0.3061 0.0175  0.0212  0.0697  539  GLU A CB  
3883  C CG  . GLU A 541  ? 0.3605 0.4236 0.3508 0.0177  0.0225  0.0749  539  GLU A CG  
3884  C CD  . GLU A 541  ? 0.4195 0.4846 0.4176 0.0151  0.0217  0.0836  539  GLU A CD  
3885  O OE1 . GLU A 541  ? 0.5334 0.5951 0.5363 0.0136  0.0198  0.0876  539  GLU A OE1 
3886  O OE2 . GLU A 541  ? 0.4810 0.5510 0.4809 0.0145  0.0227  0.0865  539  GLU A OE2 
3887  N N   . LEU A 542  ? 0.2554 0.2886 0.2347 0.0207  0.0209  0.0500  540  LEU A N   
3888  C CA  . LEU A 542  ? 0.2928 0.3162 0.2720 0.0203  0.0198  0.0456  540  LEU A CA  
3889  C C   . LEU A 542  ? 0.3047 0.3292 0.2829 0.0207  0.0188  0.0460  540  LEU A C   
3890  O O   . LEU A 542  ? 0.3029 0.3205 0.2833 0.0198  0.0176  0.0452  540  LEU A O   
3891  C CB  . LEU A 542  ? 0.3052 0.3248 0.2803 0.0215  0.0202  0.0386  540  LEU A CB  
3892  C CG  . LEU A 542  ? 0.3019 0.3152 0.2785 0.0207  0.0205  0.0364  540  LEU A CG  
3893  C CD1 . LEU A 542  ? 0.2423 0.2506 0.2154 0.0216  0.0202  0.0297  540  LEU A CD1 
3894  C CD2 . LEU A 542  ? 0.3145 0.3212 0.2965 0.0185  0.0196  0.0388  540  LEU A CD2 
3895  N N   . PHE A 543  ? 0.2567 0.2903 0.2314 0.0222  0.0192  0.0469  541  PHE A N   
3896  C CA  . PHE A 543  ? 0.2870 0.3223 0.2601 0.0227  0.0183  0.0469  541  PHE A CA  
3897  C C   . PHE A 543  ? 0.2967 0.3388 0.2730 0.0219  0.0178  0.0545  541  PHE A C   
3898  O O   . PHE A 543  ? 0.2980 0.3435 0.2730 0.0225  0.0170  0.0554  541  PHE A O   
3899  C CB  . PHE A 543  ? 0.2861 0.3266 0.2530 0.0251  0.0187  0.0417  541  PHE A CB  
3900  C CG  . PHE A 543  ? 0.2913 0.3257 0.2559 0.0258  0.0190  0.0349  541  PHE A CG  
3901  C CD1 . PHE A 543  ? 0.3095 0.3335 0.2756 0.0247  0.0181  0.0319  541  PHE A CD1 
3902  C CD2 . PHE A 543  ? 0.2603 0.2997 0.2219 0.0276  0.0199  0.0318  541  PHE A CD2 
3903  C CE1 . PHE A 543  ? 0.3071 0.3258 0.2716 0.0251  0.0182  0.0264  541  PHE A CE1 
3904  C CE2 . PHE A 543  ? 0.2648 0.2982 0.2252 0.0282  0.0199  0.0260  541  PHE A CE2 
3905  C CZ  . PHE A 543  ? 0.2785 0.3014 0.2403 0.0268  0.0190  0.0236  541  PHE A CZ  
3906  N N   . GLY A 544  ? 0.2844 0.3286 0.2653 0.0205  0.0180  0.0602  542  GLY A N   
3907  C CA  . GLY A 544  ? 0.3282 0.3780 0.3136 0.0193  0.0172  0.0683  542  GLY A CA  
3908  C C   . GLY A 544  ? 0.3250 0.3872 0.3062 0.0208  0.0177  0.0707  542  GLY A C   
3909  O O   . GLY A 544  ? 0.2853 0.3554 0.2617 0.0224  0.0192  0.0685  542  GLY A O   
3910  N N   . ASP A 545  ? 0.3339 0.3983 0.3171 0.0203  0.0163  0.0749  543  ASP A N   
3911  C CA  . ASP A 545  ? 0.3525 0.4299 0.3326 0.0213  0.0165  0.0785  543  ASP A CA  
3912  C C   . ASP A 545  ? 0.3575 0.4380 0.3300 0.0238  0.0170  0.0713  543  ASP A C   
3913  O O   . ASP A 545  ? 0.3575 0.4501 0.3261 0.0252  0.0175  0.0727  543  ASP A O   
3914  C CB  . ASP A 545  ? 0.3972 0.4755 0.3821 0.0200  0.0145  0.0852  543  ASP A CB  
3915  C CG  . ASP A 545  ? 0.4736 0.5501 0.4672 0.0175  0.0135  0.0931  543  ASP A CG  
3916  O OD1 . ASP A 545  ? 0.4816 0.5623 0.4765 0.0168  0.0146  0.0961  543  ASP A OD1 
3917  O OD2 . ASP A 545  ? 0.5833 0.6541 0.5828 0.0162  0.0114  0.0963  543  ASP A OD2 
3918  N N   . ALA A 546  ? 0.3063 0.3767 0.2768 0.0244  0.0168  0.0637  544  ALA A N   
3919  C CA  . ALA A 546  ? 0.3036 0.3759 0.2678 0.0266  0.0168  0.0568  544  ALA A CA  
3920  C C   . ALA A 546  ? 0.3315 0.4124 0.2908 0.0287  0.0183  0.0533  544  ALA A C   
3921  O O   . ALA A 546  ? 0.3194 0.4100 0.2742 0.0306  0.0184  0.0517  544  ALA A O   
3922  C CB  . ALA A 546  ? 0.2992 0.3587 0.2632 0.0265  0.0161  0.0502  544  ALA A CB  
3923  N N   . ARG A 547  ? 0.2987 0.3766 0.2588 0.0285  0.0194  0.0518  545  ARG A N   
3924  C CA  . ARG A 547  ? 0.2913 0.3770 0.2472 0.0307  0.0208  0.0480  545  ARG A CA  
3925  C C   . ARG A 547  ? 0.2503 0.3320 0.2088 0.0299  0.0219  0.0485  545  ARG A C   
3926  O O   . ARG A 547  ? 0.2613 0.3330 0.2241 0.0278  0.0214  0.0501  545  ARG A O   
3927  C CB  . ARG A 547  ? 0.3284 0.4116 0.2796 0.0330  0.0203  0.0389  545  ARG A CB  
3928  C CG  . ARG A 547  ? 0.3083 0.3775 0.2610 0.0322  0.0197  0.0339  545  ARG A CG  
3929  C CD  . ARG A 547  ? 0.3142 0.3811 0.2631 0.0341  0.0188  0.0258  545  ARG A CD  
3930  N NE  . ARG A 547  ? 0.3070 0.3609 0.2578 0.0327  0.0177  0.0230  545  ARG A NE  
3931  C CZ  . ARG A 547  ? 0.2740 0.3199 0.2257 0.0324  0.0178  0.0192  545  ARG A CZ  
3932  N NH1 . ARG A 547  ? 0.2936 0.3423 0.2445 0.0336  0.0187  0.0170  545  ARG A NH1 
3933  N NH2 . ARG A 547  ? 0.2884 0.3238 0.2420 0.0308  0.0169  0.0178  545  ARG A NH2 
3934  N N   . THR A 548  ? 0.2565 0.3471 0.2126 0.0316  0.0232  0.0470  546  THR A N   
3935  C CA  . THR A 548  ? 0.2324 0.3210 0.1905 0.0311  0.0244  0.0472  546  THR A CA  
3936  C C   . THR A 548  ? 0.2349 0.3144 0.1914 0.0323  0.0242  0.0389  546  THR A C   
3937  O O   . THR A 548  ? 0.2575 0.3396 0.2099 0.0347  0.0239  0.0325  546  THR A O   
3938  C CB  . THR A 548  ? 0.2763 0.3797 0.2329 0.0326  0.0260  0.0495  546  THR A CB  
3939  O OG1 . THR A 548  ? 0.3248 0.4374 0.2831 0.0314  0.0260  0.0580  546  THR A OG1 
3940  C CG2 . THR A 548  ? 0.2793 0.3809 0.2384 0.0320  0.0271  0.0502  546  THR A CG2 
3941  N N   . ASN A 549  ? 0.2298 0.2989 0.1897 0.0305  0.0241  0.0390  547  ASN A N   
3942  C CA  . ASN A 549  ? 0.2513 0.3120 0.2102 0.0312  0.0238  0.0322  547  ASN A CA  
3943  C C   . ASN A 549  ? 0.2474 0.3155 0.2041 0.0336  0.0249  0.0289  547  ASN A C   
3944  O O   . ASN A 549  ? 0.2383 0.3156 0.1957 0.0338  0.0262  0.0330  547  ASN A O   
3945  C CB  . ASN A 549  ? 0.2558 0.3056 0.2190 0.0287  0.0235  0.0338  547  ASN A CB  
3946  C CG  . ASN A 549  ? 0.2557 0.2957 0.2181 0.0290  0.0229  0.0274  547  ASN A CG  
3947  O OD1 . ASN A 549  ? 0.2476 0.2872 0.2070 0.0307  0.0222  0.0218  547  ASN A OD1 
3948  N ND2 . ASN A 549  ? 0.2446 0.2768 0.2102 0.0271  0.0228  0.0283  547  ASN A ND2 
3949  N N   . SER A 550  ? 0.2358 0.3005 0.1902 0.0355  0.0242  0.0214  548  SER A N   
3950  C CA  . SER A 550  ? 0.2258 0.2958 0.1793 0.0379  0.0250  0.0174  548  SER A CA  
3951  C C   . SER A 550  ? 0.2351 0.3005 0.1919 0.0363  0.0258  0.0198  548  SER A C   
3952  O O   . SER A 550  ? 0.2400 0.2954 0.1995 0.0338  0.0253  0.0218  548  SER A O   
3953  C CB  . SER A 550  ? 0.2300 0.2953 0.1815 0.0399  0.0236  0.0090  548  SER A CB  
3954  O OG  . SER A 550  ? 0.2319 0.2839 0.1854 0.0380  0.0224  0.0076  548  SER A OG  
3955  N N   . ALA A 551  ? 0.2451 0.3182 0.2017 0.0380  0.0270  0.0192  549  ALA A N   
3956  C CA  . ALA A 551  ? 0.2552 0.3253 0.2150 0.0368  0.0278  0.0212  549  ALA A CA  
3957  C C   . ALA A 551  ? 0.2620 0.3275 0.2216 0.0387  0.0273  0.0144  549  ALA A C   
3958  O O   . ALA A 551  ? 0.2413 0.3116 0.1986 0.0417  0.0269  0.0086  549  ALA A O   
3959  C CB  . ALA A 551  ? 0.2737 0.3563 0.2343 0.0371  0.0296  0.0264  549  ALA A CB  
3960  N N   . GLY A 552  ? 0.2516 0.3080 0.2141 0.0369  0.0270  0.0148  550  GLY A N   
3961  C CA  . GLY A 552  ? 0.2492 0.3010 0.2124 0.0382  0.0264  0.0095  550  GLY A CA  
3962  C C   . GLY A 552  ? 0.2663 0.3236 0.2314 0.0387  0.0278  0.0112  550  GLY A C   
3963  O O   . GLY A 552  ? 0.2625 0.3297 0.2278 0.0388  0.0293  0.0155  550  GLY A O   
3964  N N   . LEU A 553  ? 0.2425 0.2935 0.2094 0.0390  0.0271  0.0080  551  LEU A N   
3965  C CA  . LEU A 553  ? 0.2542 0.3097 0.2233 0.0396  0.0282  0.0090  551  LEU A CA  
3966  C C   . LEU A 553  ? 0.2646 0.3093 0.2365 0.0374  0.0275  0.0096  551  LEU A C   
3967  O O   . LEU A 553  ? 0.2909 0.3262 0.2629 0.0368  0.0259  0.0065  551  LEU A O   
3968  C CB  . LEU A 553  ? 0.2960 0.3581 0.2642 0.0436  0.0281  0.0028  551  LEU A CB  
3969  C CG  . LEU A 553  ? 0.2547 0.3298 0.2199 0.0464  0.0290  0.0015  551  LEU A CG  
3970  C CD1 . LEU A 553  ? 0.3041 0.3833 0.2690 0.0505  0.0281  -0.0063 551  LEU A CD1 
3971  C CD2 . LEU A 553  ? 0.2681 0.3546 0.2337 0.0458  0.0312  0.0078  551  LEU A CD2 
3972  N N   . ASP A 554  ? 0.2419 0.2886 0.2164 0.0361  0.0286  0.0137  552  ASP A N   
3973  C CA  . ASP A 554  ? 0.2702 0.3077 0.2475 0.0338  0.0279  0.0148  552  ASP A CA  
3974  C C   . ASP A 554  ? 0.2676 0.3050 0.2462 0.0358  0.0276  0.0108  552  ASP A C   
3975  O O   . ASP A 554  ? 0.2334 0.2781 0.2134 0.0369  0.0288  0.0119  552  ASP A O   
3976  C CB  . ASP A 554  ? 0.2562 0.2954 0.2363 0.0311  0.0290  0.0215  552  ASP A CB  
3977  C CG  . ASP A 554  ? 0.2469 0.2770 0.2298 0.0287  0.0282  0.0223  552  ASP A CG  
3978  O OD1 . ASP A 554  ? 0.2568 0.2797 0.2394 0.0290  0.0269  0.0183  552  ASP A OD1 
3979  O OD2 . ASP A 554  ? 0.2556 0.2860 0.2414 0.0264  0.0287  0.0272  552  ASP A OD2 
3980  N N   . LEU A 555  ? 0.2407 0.2700 0.2193 0.0361  0.0258  0.0063  553  LEU A N   
3981  C CA  . LEU A 555  ? 0.2356 0.2642 0.2161 0.0381  0.0250  0.0024  553  LEU A CA  
3982  C C   . LEU A 555  ? 0.2209 0.2451 0.2045 0.0361  0.0250  0.0050  553  LEU A C   
3983  O O   . LEU A 555  ? 0.2377 0.2601 0.2232 0.0374  0.0241  0.0022  553  LEU A O   
3984  C CB  . LEU A 555  ? 0.2275 0.2496 0.2076 0.0393  0.0227  -0.0030 553  LEU A CB  
3985  C CG  . LEU A 555  ? 0.2587 0.2861 0.2361 0.0418  0.0226  -0.0066 553  LEU A CG  
3986  C CD1 . LEU A 555  ? 0.2889 0.3104 0.2669 0.0433  0.0200  -0.0123 553  LEU A CD1 
3987  C CD2 . LEU A 555  ? 0.2888 0.3285 0.2658 0.0449  0.0241  -0.0077 553  LEU A CD2 
3988  N N   . SER A 556  ? 0.2326 0.2549 0.2168 0.0330  0.0258  0.0102  554  SER A N   
3989  C CA  . SER A 556  ? 0.2201 0.2401 0.2073 0.0312  0.0259  0.0130  554  SER A CA  
3990  C C   . SER A 556  ? 0.2333 0.2624 0.2221 0.0314  0.0278  0.0168  554  SER A C   
3991  O O   . SER A 556  ? 0.2368 0.2652 0.2285 0.0300  0.0280  0.0192  554  SER A O   
3992  C CB  . SER A 556  ? 0.2561 0.2682 0.2440 0.0277  0.0253  0.0158  554  SER A CB  
3993  O OG  . SER A 556  ? 0.2478 0.2628 0.2357 0.0261  0.0263  0.0201  554  SER A OG  
3994  N N   . ASN A 557  ? 0.2186 0.2568 0.2058 0.0330  0.0290  0.0175  555  ASN A N   
3995  C CA  . ASN A 557  ? 0.2135 0.2617 0.2022 0.0330  0.0308  0.0218  555  ASN A CA  
3996  C C   . ASN A 557  ? 0.2243 0.2806 0.2132 0.0364  0.0315  0.0185  555  ASN A C   
3997  O O   . ASN A 557  ? 0.2331 0.2939 0.2197 0.0395  0.0315  0.0140  555  ASN A O   
3998  C CB  . ASN A 557  ? 0.2338 0.2882 0.2206 0.0326  0.0318  0.0252  555  ASN A CB  
3999  C CG  . ASN A 557  ? 0.2398 0.3052 0.2286 0.0322  0.0335  0.0307  555  ASN A CG  
4000  O OD1 . ASN A 557  ? 0.2595 0.3333 0.2488 0.0343  0.0346  0.0298  555  ASN A OD1 
4001  N ND2 . ASN A 557  ? 0.2445 0.3102 0.2348 0.0294  0.0337  0.0367  555  ASN A ND2 
4002  N N   . GLU A 558  ? 0.2342 0.2929 0.2262 0.0360  0.0321  0.0204  556  GLU A N   
4003  C CA  . GLU A 558  ? 0.2427 0.3088 0.2356 0.0394  0.0326  0.0168  556  GLU A CA  
4004  C C   . GLU A 558  ? 0.2355 0.3155 0.2266 0.0420  0.0344  0.0169  556  GLU A C   
4005  O O   . GLU A 558  ? 0.2496 0.3354 0.2399 0.0458  0.0344  0.0116  556  GLU A O   
4006  C CB  . GLU A 558  ? 0.2422 0.3087 0.2390 0.0384  0.0330  0.0193  556  GLU A CB  
4007  C CG  . GLU A 558  ? 0.2140 0.2684 0.2126 0.0365  0.0312  0.0184  556  GLU A CG  
4008  C CD  . GLU A 558  ? 0.2213 0.2701 0.2196 0.0389  0.0294  0.0120  556  GLU A CD  
4009  O OE1 . GLU A 558  ? 0.2353 0.2896 0.2326 0.0425  0.0294  0.0074  556  GLU A OE1 
4010  O OE2 . GLU A 558  ? 0.2269 0.2659 0.2263 0.0371  0.0278  0.0115  556  GLU A OE2 
4011  N N   . GLU A 559  ? 0.2217 0.3076 0.2124 0.0400  0.0357  0.0230  557  GLU A N   
4012  C CA  . GLU A 559  ? 0.2516 0.3518 0.2403 0.0423  0.0374  0.0235  557  GLU A CA  
4013  C C   . GLU A 559  ? 0.2442 0.3440 0.2288 0.0449  0.0365  0.0178  557  GLU A C   
4014  O O   . GLU A 559  ? 0.2471 0.3565 0.2300 0.0486  0.0371  0.0132  557  GLU A O   
4015  C CB  . GLU A 559  ? 0.2782 0.3839 0.2677 0.0393  0.0386  0.0318  557  GLU A CB  
4016  C CG  . GLU A 559  ? 0.2715 0.3793 0.2657 0.0366  0.0393  0.0382  557  GLU A CG  
4017  C CD  . GLU A 559  ? 0.3847 0.4971 0.3805 0.0335  0.0400  0.0465  557  GLU A CD  
4018  O OE1 . GLU A 559  ? 0.4620 0.5788 0.4550 0.0339  0.0402  0.0475  557  GLU A OE1 
4019  O OE2 . GLU A 559  ? 0.3399 0.4516 0.3403 0.0305  0.0400  0.0523  557  GLU A OE2 
4020  N N   . THR A 560  ? 0.2394 0.3287 0.2227 0.0429  0.0351  0.0176  558  THR A N   
4021  C CA  . THR A 560  ? 0.2515 0.3394 0.2313 0.0451  0.0341  0.0123  558  THR A CA  
4022  C C   . THR A 560  ? 0.2720 0.3572 0.2520 0.0484  0.0327  0.0043  558  THR A C   
4023  O O   . THR A 560  ? 0.2639 0.3553 0.2420 0.0519  0.0324  -0.0011 558  THR A O   
4024  C CB  . THR A 560  ? 0.2395 0.3156 0.2184 0.0421  0.0327  0.0137  558  THR A CB  
4025  O OG1 . THR A 560  ? 0.2733 0.3518 0.2528 0.0392  0.0338  0.0211  558  THR A OG1 
4026  C CG2 . THR A 560  ? 0.2732 0.3481 0.2488 0.0441  0.0316  0.0085  558  THR A CG2 
4027  N N   . LEU A 561  ? 0.2344 0.3106 0.2174 0.0475  0.0316  0.0033  559  LEU A N   
4028  C CA  . LEU A 561  ? 0.2210 0.2940 0.2053 0.0506  0.0299  -0.0039 559  LEU A CA  
4029  C C   . LEU A 561  ? 0.2434 0.3290 0.2286 0.0546  0.0310  -0.0072 559  LEU A C   
4030  O O   . LEU A 561  ? 0.2439 0.3317 0.2289 0.0583  0.0298  -0.0142 559  LEU A O   
4031  C CB  . LEU A 561  ? 0.2293 0.2911 0.2169 0.0485  0.0286  -0.0033 559  LEU A CB  
4032  C CG  . LEU A 561  ? 0.2148 0.2638 0.2017 0.0453  0.0270  -0.0020 559  LEU A CG  
4033  C CD1 . LEU A 561  ? 0.2213 0.2614 0.2113 0.0433  0.0259  -0.0008 559  LEU A CD1 
4034  C CD2 . LEU A 561  ? 0.2081 0.2527 0.1934 0.0470  0.0251  -0.0076 559  LEU A CD2 
4035  N N   . ALA A 562  ? 0.2758 0.3701 0.2622 0.0539  0.0331  -0.0025 560  ALA A N   
4036  C CA  . ALA A 562  ? 0.2519 0.3594 0.2391 0.0578  0.0343  -0.0055 560  ALA A CA  
4037  C C   . ALA A 562  ? 0.2518 0.3715 0.2354 0.0606  0.0352  -0.0080 560  ALA A C   
4038  O O   . ALA A 562  ? 0.2469 0.3739 0.2305 0.0650  0.0348  -0.0148 560  ALA A O   
4039  C CB  . ALA A 562  ? 0.2742 0.3887 0.2638 0.0561  0.0364  0.0009  560  ALA A CB  
4040  N N   . SER A 563  ? 0.2513 0.3736 0.2321 0.0583  0.0362  -0.0027 561  SER A N   
4041  C CA  . SER A 563  ? 0.2904 0.4244 0.2675 0.0607  0.0370  -0.0047 561  SER A CA  
4042  C C   . SER A 563  ? 0.2795 0.4078 0.2549 0.0633  0.0346  -0.0129 561  SER A C   
4043  O O   . SER A 563  ? 0.2826 0.4207 0.2564 0.0674  0.0345  -0.0190 561  SER A O   
4044  C CB  . SER A 563  ? 0.3055 0.4422 0.2805 0.0573  0.0382  0.0033  561  SER A CB  
4045  O OG  . SER A 563  ? 0.4103 0.5585 0.3816 0.0596  0.0388  0.0015  561  SER A OG  
4046  N N   . LEU A 564  ? 0.2772 0.3899 0.2531 0.0609  0.0326  -0.0133 562  LEU A N   
4047  C CA  . LEU A 564  ? 0.2544 0.3606 0.2294 0.0629  0.0302  -0.0205 562  LEU A CA  
4048  C C   . LEU A 564  ? 0.2829 0.3893 0.2609 0.0669  0.0285  -0.0286 562  LEU A C   
4049  O O   . LEU A 564  ? 0.2920 0.4019 0.2694 0.0705  0.0271  -0.0358 562  LEU A O   
4050  C CB  . LEU A 564  ? 0.2637 0.3538 0.2391 0.0591  0.0285  -0.0182 562  LEU A CB  
4051  C CG  . LEU A 564  ? 0.3242 0.4066 0.2982 0.0595  0.0261  -0.0229 562  LEU A CG  
4052  C CD1 . LEU A 564  ? 0.2876 0.3794 0.2575 0.0607  0.0269  -0.0231 562  LEU A CD1 
4053  C CD2 . LEU A 564  ? 0.2612 0.3294 0.2357 0.0553  0.0252  -0.0189 562  LEU A CD2 
4054  N N   . THR A 565  ? 0.2467 0.3497 0.2284 0.0666  0.0285  -0.0277 563  THR A N   
4055  C CA  . THR A 565  ? 0.2758 0.3794 0.2612 0.0705  0.0269  -0.0351 563  THR A CA  
4056  C C   . THR A 565  ? 0.2646 0.3843 0.2489 0.0755  0.0277  -0.0406 563  THR A C   
4057  O O   . THR A 565  ? 0.2796 0.3998 0.2653 0.0794  0.0255  -0.0490 563  THR A O   
4058  C CB  . THR A 565  ? 0.2648 0.3656 0.2541 0.0694  0.0273  -0.0321 563  THR A CB  
4059  O OG1 . THR A 565  ? 0.2704 0.3562 0.2610 0.0653  0.0260  -0.0284 563  THR A OG1 
4060  C CG2 . THR A 565  ? 0.3310 0.4341 0.3246 0.0739  0.0257  -0.0397 563  THR A CG2 
4061  N N   . GLU A 566  ? 0.2789 0.4123 0.2609 0.0753  0.0308  -0.0360 564  GLU A N   
4062  C CA  . GLU A 566  ? 0.2979 0.4484 0.2786 0.0801  0.0319  -0.0410 564  GLU A CA  
4063  C C   . GLU A 566  ? 0.2971 0.4511 0.2740 0.0818  0.0309  -0.0453 564  GLU A C   
4064  O O   . GLU A 566  ? 0.2909 0.4516 0.2682 0.0865  0.0296  -0.0541 564  GLU A O   
4065  C CB  . GLU A 566  ? 0.2879 0.4530 0.2673 0.0791  0.0354  -0.0340 564  GLU A CB  
4066  C CG  . GLU A 566  ? 0.3712 0.5344 0.3547 0.0779  0.0363  -0.0305 564  GLU A CG  
4067  C CD  . GLU A 566  ? 0.4153 0.5770 0.4032 0.0821  0.0344  -0.0389 564  GLU A CD  
4068  O OE1 . GLU A 566  ? 0.4631 0.6364 0.4509 0.0871  0.0343  -0.0462 564  GLU A OE1 
4069  O OE2 . GLU A 566  ? 0.4386 0.5875 0.4302 0.0804  0.0329  -0.0382 564  GLU A OE2 
4070  N N   . ALA A 567  ? 0.2964 0.4458 0.2699 0.0781  0.0313  -0.0396 565  ALA A N   
4071  C CA  . ALA A 567  ? 0.2995 0.4521 0.2693 0.0795  0.0304  -0.0434 565  ALA A CA  
4072  C C   . ALA A 567  ? 0.2868 0.4284 0.2588 0.0816  0.0267  -0.0522 565  ALA A C   
4073  O O   . ALA A 567  ? 0.2903 0.4383 0.2612 0.0853  0.0254  -0.0596 565  ALA A O   
4074  C CB  . ALA A 567  ? 0.3134 0.4619 0.2799 0.0750  0.0313  -0.0353 565  ALA A CB  
4075  N N   . LEU A 568  ? 0.2921 0.4177 0.2677 0.0793  0.0249  -0.0514 566  LEU A N   
4076  C CA  . LEU A 568  ? 0.2605 0.3750 0.2391 0.0808  0.0211  -0.0588 566  LEU A CA  
4077  C C   . LEU A 568  ? 0.2866 0.4073 0.2690 0.0862  0.0195  -0.0680 566  LEU A C   
4078  O O   . LEU A 568  ? 0.3077 0.4286 0.2911 0.0895  0.0169  -0.0762 566  LEU A O   
4079  C CB  . LEU A 568  ? 0.2736 0.3709 0.2553 0.0769  0.0197  -0.0550 566  LEU A CB  
4080  C CG  . LEU A 568  ? 0.2873 0.3759 0.2661 0.0717  0.0204  -0.0474 566  LEU A CG  
4081  C CD1 . LEU A 568  ? 0.2585 0.3322 0.2406 0.0683  0.0191  -0.0443 566  LEU A CD1 
4082  C CD2 . LEU A 568  ? 0.2782 0.3646 0.2542 0.0718  0.0189  -0.0502 566  LEU A CD2 
4083  N N   . ARG A 569  ? 0.2725 0.3985 0.2575 0.0874  0.0209  -0.0671 567  ARG A N   
4084  C CA  . ARG A 569  ? 0.2923 0.4258 0.2811 0.0929  0.0196  -0.0759 567  ARG A CA  
4085  C C   . ARG A 569  ? 0.3090 0.4590 0.2945 0.0972  0.0204  -0.0817 567  ARG A C   
4086  O O   . ARG A 569  ? 0.3065 0.4588 0.2946 0.1017  0.0177  -0.0916 567  ARG A O   
4087  C CB  . ARG A 569  ? 0.3296 0.4681 0.3212 0.0932  0.0216  -0.0729 567  ARG A CB  
4088  C CG  . ARG A 569  ? 0.3317 0.4547 0.3278 0.0902  0.0201  -0.0696 567  ARG A CG  
4089  C CD  . ARG A 569  ? 0.3983 0.5273 0.3969 0.0905  0.0222  -0.0665 567  ARG A CD  
4090  N NE  . ARG A 569  ? 0.4216 0.5365 0.4236 0.0870  0.0212  -0.0620 567  ARG A NE  
4091  C CZ  . ARG A 569  ? 0.4817 0.5987 0.4858 0.0859  0.0228  -0.0576 567  ARG A CZ  
4092  N NH1 . ARG A 569  ? 0.5308 0.6630 0.5340 0.0878  0.0257  -0.0565 567  ARG A NH1 
4093  N NH2 . ARG A 569  ? 0.4792 0.5831 0.4864 0.0828  0.0215  -0.0540 567  ARG A NH2 
4094  N N   . GLU A 570  ? 0.3132 0.4751 0.2932 0.0957  0.0238  -0.0756 568  GLU A N   
4095  C CA  . GLU A 570  ? 0.3022 0.4815 0.2786 0.0996  0.0247  -0.0804 568  GLU A CA  
4096  C C   . GLU A 570  ? 0.3233 0.4977 0.2982 0.1006  0.0219  -0.0862 568  GLU A C   
4097  O O   . GLU A 570  ? 0.3206 0.5039 0.2955 0.1043  0.0201  -0.0939 568  GLU A O   
4098  C CB  . GLU A 570  ? 0.3328 0.5251 0.3039 0.0972  0.0288  -0.0713 568  GLU A CB  
4099  C CG  . GLU A 570  ? 0.3767 0.5779 0.3495 0.0971  0.0316  -0.0665 568  GLU A CG  
4100  C CD  . GLU A 570  ? 0.4708 0.6818 0.4397 0.0935  0.0353  -0.0557 568  GLU A CD  
4101  O OE1 . GLU A 570  ? 0.5214 0.7308 0.4864 0.0908  0.0355  -0.0513 568  GLU A OE1 
4102  O OE2 . GLU A 570  ? 0.5567 0.7772 0.5268 0.0934  0.0377  -0.0513 568  GLU A OE2 
4103  N N   . SER A 571  ? 0.3242 0.4832 0.2984 0.0962  0.0207  -0.0817 569  SER A N   
4104  C CA  . SER A 571  ? 0.3082 0.4617 0.2815 0.0968  0.0178  -0.0869 569  SER A CA  
4105  C C   . SER A 571  ? 0.3284 0.4758 0.3077 0.1007  0.0136  -0.0977 569  SER A C   
4106  O O   . SER A 571  ? 0.3027 0.4525 0.2817 0.1036  0.0112  -0.1054 569  SER A O   
4107  C CB  . SER A 571  ? 0.2883 0.4265 0.2603 0.0912  0.0174  -0.0798 569  SER A CB  
4108  O OG  . SER A 571  ? 0.3120 0.4339 0.2892 0.0895  0.0151  -0.0799 569  SER A OG  
4109  N N   . ALA A 572  ? 0.3192 0.4586 0.3041 0.1010  0.0125  -0.0986 570  ALA A N   
4110  C CA  . ALA A 572  ? 0.3104 0.4438 0.3021 0.1047  0.0082  -0.1085 570  ALA A CA  
4111  C C   . ALA A 572  ? 0.3481 0.4954 0.3416 0.1092  0.0072  -0.1158 570  ALA A C   
4112  O O   . ALA A 572  ? 0.3787 0.5213 0.3780 0.1113  0.0028  -0.1235 570  ALA A O   
4113  C CB  . ALA A 572  ? 0.3519 0.4715 0.3495 0.1027  0.0068  -0.1058 570  ALA A CB  
4114  N N   . ALA A 573  ? 0.3447 0.5080 0.3337 0.1095  0.0106  -0.1124 571  ALA A N   
4115  C CA  . ALA A 573  ? 0.3671 0.5441 0.3572 0.1127  0.0094  -0.1179 571  ALA A CA  
4116  C C   . ALA A 573  ? 0.3875 0.5746 0.3731 0.1132  0.0087  -0.1201 571  ALA A C   
4117  O O   . ALA A 573  ? 0.3862 0.5862 0.3723 0.1159  0.0075  -0.1247 571  ALA A O   
4118  C CB  . ALA A 573  ? 0.3471 0.5365 0.3357 0.1129  0.0132  -0.1130 571  ALA A CB  
4119  N N   . MET A 574  ? 0.3673 0.5496 0.3488 0.1108  0.0092  -0.1168 572  MET A N   
4120  C CA  . MET A 574  ? 0.3829 0.5744 0.3604 0.1112  0.0083  -0.1187 572  MET A CA  
4121  C C   . MET A 574  ? 0.3900 0.5743 0.3722 0.1132  0.0030  -0.1281 572  MET A C   
4122  O O   . MET A 574  ? 0.3585 0.5273 0.3456 0.1128  0.0004  -0.1309 572  MET A O   
4123  C CB  . MET A 574  ? 0.3817 0.5718 0.3528 0.1078  0.0112  -0.1108 572  MET A CB  
4124  C CG  . MET A 574  ? 0.3734 0.5722 0.3404 0.1056  0.0162  -0.1009 572  MET A CG  
4125  S SD  . MET A 574  ? 0.4380 0.6327 0.3987 0.1013  0.0194  -0.0912 572  MET A SD  
4126  C CE  . MET A 574  ? 0.4578 0.6620 0.4164 0.0990  0.0245  -0.0803 572  MET A CE  
4127  N N   . LYS A 575  ? 0.3886 0.5849 0.3697 0.1153  0.0013  -0.1329 573  LYS A N   
4128  C CA  . LYS A 575  ? 0.3631 0.5550 0.3488 0.1173  -0.0039 -0.1421 573  LYS A CA  
4129  C C   . LYS A 575  ? 0.3618 0.5484 0.3439 0.1152  -0.0045 -0.1406 573  LYS A C   
4130  O O   . LYS A 575  ? 0.4005 0.5974 0.3796 0.1160  -0.0052 -0.1424 573  LYS A O   
4131  C CB  . LYS A 575  ? 0.3852 0.5932 0.3722 0.1211  -0.0058 -0.1488 573  LYS A CB  
4132  N N   . TRP A 576  ? 0.3269 0.4975 0.3097 0.1124  -0.0044 -0.1372 574  TRP A N   
4133  C CA  . TRP A 576  ? 0.3109 0.4748 0.2906 0.1102  -0.0049 -0.1354 574  TRP A CA  
4134  C C   . TRP A 576  ? 0.2835 0.4452 0.2675 0.1119  -0.0101 -0.1440 574  TRP A C   
4135  O O   . TRP A 576  ? 0.3203 0.4742 0.3118 0.1134  -0.0142 -0.1503 574  TRP A O   
4136  C CB  . TRP A 576  ? 0.3292 0.4759 0.3097 0.1072  -0.0042 -0.1308 574  TRP A CB  
4137  C CG  . TRP A 576  ? 0.3192 0.4670 0.2959 0.1053  0.0007  -0.1223 574  TRP A CG  
4138  C CD1 . TRP A 576  ? 0.2724 0.4144 0.2525 0.1053  0.0017  -0.1206 574  TRP A CD1 
4139  C CD2 . TRP A 576  ? 0.2824 0.4375 0.2515 0.1030  0.0052  -0.1140 574  TRP A CD2 
4140  N NE1 . TRP A 576  ? 0.2803 0.4258 0.2555 0.1033  0.0065  -0.1120 574  TRP A NE1 
4141  C CE2 . TRP A 576  ? 0.2918 0.4452 0.2604 0.1017  0.0087  -0.1076 574  TRP A CE2 
4142  C CE3 . TRP A 576  ? 0.2616 0.4246 0.2248 0.1019  0.0064  -0.1110 574  TRP A CE3 
4143  C CZ2 . TRP A 576  ? 0.3014 0.4595 0.2645 0.0984  0.0129  -0.0974 574  TRP A CZ2 
4144  C CZ3 . TRP A 576  ? 0.3142 0.4828 0.2715 0.0994  0.0109  -0.1016 574  TRP A CZ3 
4145  C CH2 . TRP A 576  ? 0.3333 0.4992 0.2908 0.0976  0.0140  -0.0948 574  TRP A CH2 
4146  N N   . THR A 577  ? 0.3086 0.4774 0.2883 0.1116  -0.0102 -0.1440 575  THR A N   
4147  C CA  . THR A 577  ? 0.3194 0.4858 0.3027 0.1129  -0.0150 -0.1514 575  THR A CA  
4148  C C   . THR A 577  ? 0.3039 0.4661 0.2826 0.1102  -0.0144 -0.1478 575  THR A C   
4149  O O   . THR A 577  ? 0.3225 0.4882 0.2942 0.1080  -0.0102 -0.1400 575  THR A O   
4150  C CB  . THR A 577  ? 0.3363 0.5198 0.3204 0.1165  -0.0166 -0.1577 575  THR A CB  
4151  O OG1 . THR A 577  ? 0.3362 0.5344 0.3124 0.1160  -0.0129 -0.1523 575  THR A OG1 
4152  C CG2 . THR A 577  ? 0.3589 0.5477 0.3476 0.1194  -0.0173 -0.1617 575  THR A CG2 
4153  N N   . ALA A 578  ? 0.3147 0.4694 0.2978 0.1105  -0.0189 -0.1535 576  ALA A N   
4154  C CA  . ALA A 578  ? 0.3072 0.4595 0.2867 0.1086  -0.0193 -0.1520 576  ALA A CA  
4155  C C   . ALA A 578  ? 0.3561 0.5141 0.3395 0.1111  -0.0239 -0.1605 576  ALA A C   
4156  O O   . ALA A 578  ? 0.3357 0.4877 0.3273 0.1128  -0.0283 -0.1674 576  ALA A O   
4157  C CB  . ALA A 578  ? 0.3117 0.4451 0.2930 0.1054  -0.0203 -0.1493 576  ALA A CB  
4158  N N   . LEU A 579  ? 0.3218 0.4918 0.3000 0.1115  -0.0229 -0.1598 577  LEU A N   
4159  C CA  . LEU A 579  ? 0.3320 0.5102 0.3133 0.1142  -0.0268 -0.1676 577  LEU A CA  
4160  C C   . LEU A 579  ? 0.3118 0.4884 0.2893 0.1123  -0.0271 -0.1658 577  LEU A C   
4161  O O   . LEU A 579  ? 0.3084 0.4834 0.2793 0.1094  -0.0235 -0.1579 577  LEU A O   
4162  C CB  . LEU A 579  ? 0.3236 0.5223 0.3025 0.1174  -0.0255 -0.1695 577  LEU A CB  
4163  C CG  . LEU A 579  ? 0.3649 0.5694 0.3447 0.1189  -0.0235 -0.1688 577  LEU A CG  
4164  C CD1 . LEU A 579  ? 0.3511 0.5772 0.3280 0.1217  -0.0222 -0.1701 577  LEU A CD1 
4165  C CD2 . LEU A 579  ? 0.4380 0.6330 0.4271 0.1208  -0.0275 -0.1760 577  LEU A CD2 
4166  N N   . PRO A 580  ? 0.3020 0.4794 0.2840 0.1139  -0.0316 -0.1730 578  PRO A N   
4167  C CA  . PRO A 580  ? 0.3483 0.5274 0.3264 0.1125  -0.0318 -0.1716 578  PRO A CA  
4168  C C   . PRO A 580  ? 0.3907 0.5885 0.3613 0.1133  -0.0283 -0.1678 578  PRO A C   
4169  O O   . PRO A 580  ? 0.3893 0.6018 0.3612 0.1167  -0.0294 -0.1728 578  PRO A O   
4170  C CB  . PRO A 580  ? 0.3550 0.5325 0.3408 0.1147  -0.0377 -0.1811 578  PRO A CB  
4171  C CG  . PRO A 580  ? 0.3581 0.5290 0.3526 0.1165  -0.0407 -0.1867 578  PRO A CG  
4172  C CD  . PRO A 580  ? 0.3467 0.5245 0.3377 0.1172  -0.0367 -0.1828 578  PRO A CD  
4173  N N   . GLN A 581  ? 0.3031 0.5008 0.2662 0.1103  -0.0240 -0.1586 579  GLN A N   
4174  C CA  . GLN A 581  ? 0.3446 0.5595 0.3008 0.1104  -0.0204 -0.1531 579  GLN A CA  
4175  C C   . GLN A 581  ? 0.3768 0.5953 0.3297 0.1095  -0.0212 -0.1523 579  GLN A C   
4176  O O   . GLN A 581  ? 0.3425 0.5566 0.2903 0.1064  -0.0188 -0.1450 579  GLN A O   
4177  C CB  . GLN A 581  ? 0.3282 0.5416 0.2789 0.1077  -0.0153 -0.1430 579  GLN A CB  
4178  C CG  . GLN A 581  ? 0.3092 0.5206 0.2627 0.1086  -0.0141 -0.1432 579  GLN A CG  
4179  C CD  . GLN A 581  ? 0.3739 0.6031 0.3282 0.1120  -0.0138 -0.1460 579  GLN A CD  
4180  O OE1 . GLN A 581  ? 0.3542 0.5982 0.3064 0.1134  -0.0141 -0.1470 579  GLN A OE1 
4181  N NE2 . GLN A 581  ? 0.3629 0.5910 0.3202 0.1132  -0.0133 -0.1473 579  GLN A NE2 
4182  N N   . LEU A 582  ? 0.3518 0.5787 0.3081 0.1124  -0.0246 -0.1601 580  LEU A N   
4183  C CA  . LEU A 582  ? 0.3847 0.6169 0.3385 0.1121  -0.0257 -0.1603 580  LEU A CA  
4184  C C   . LEU A 582  ? 0.3605 0.6101 0.3074 0.1118  -0.0219 -0.1532 580  LEU A C   
4185  O O   . LEU A 582  ? 0.3923 0.6515 0.3370 0.1123  -0.0190 -0.1493 580  LEU A O   
4186  C CB  . LEU A 582  ? 0.3896 0.6259 0.3499 0.1155  -0.0308 -0.1711 580  LEU A CB  
4187  C CG  . LEU A 582  ? 0.4334 0.6525 0.4003 0.1149  -0.0353 -0.1771 580  LEU A CG  
4188  C CD1 . LEU A 582  ? 0.3979 0.6018 0.3696 0.1141  -0.0360 -0.1776 580  LEU A CD1 
4189  C CD2 . LEU A 582  ? 0.4362 0.6623 0.4095 0.1185  -0.0401 -0.1874 580  LEU A CD2 
4190  N N   . ALA A 583  ? 0.3584 0.6119 0.3019 0.1107  -0.0221 -0.1512 581  ALA A N   
4191  C CA  . ALA A 583  ? 0.3594 0.6291 0.2968 0.1101  -0.0188 -0.1437 581  ALA A CA  
4192  C C   . ALA A 583  ? 0.4086 0.6980 0.3473 0.1137  -0.0188 -0.1473 581  ALA A C   
4193  O O   . ALA A 583  ? 0.4362 0.7390 0.3710 0.1133  -0.0155 -0.1403 581  ALA A O   
4194  C CB  . ALA A 583  ? 0.3611 0.6323 0.2958 0.1088  -0.0197 -0.1423 581  ALA A CB  
4195  N N   . THR A 584  ? 0.3868 0.6785 0.3315 0.1173  -0.0228 -0.1580 582  THR A N   
4196  C CA  . THR A 584  ? 0.4316 0.7424 0.3783 0.1213  -0.0236 -0.1631 582  THR A CA  
4197  C C   . THR A 584  ? 0.4577 0.7705 0.4066 0.1228  -0.0225 -0.1640 582  THR A C   
4198  O O   . THR A 584  ? 0.4578 0.7879 0.4075 0.1258  -0.0225 -0.1667 582  THR A O   
4199  C CB  . THR A 584  ? 0.4823 0.7947 0.4350 0.1247  -0.0287 -0.1748 582  THR A CB  
4200  O OG1 . THR A 584  ? 0.4534 0.7467 0.4119 0.1245  -0.0318 -0.1804 582  THR A OG1 
4201  C CG2 . THR A 584  ? 0.4449 0.7610 0.3950 0.1239  -0.0295 -0.1740 582  THR A CG2 
4202  N N   . GLY A 585  ? 0.4274 0.7236 0.3774 0.1208  -0.0218 -0.1620 583  GLY A N   
4203  C CA  . GLY A 585  ? 0.4111 0.7074 0.3637 0.1222  -0.0210 -0.1633 583  GLY A CA  
4204  C C   . GLY A 585  ? 0.4286 0.7061 0.3874 0.1224  -0.0241 -0.1694 583  GLY A C   
4205  O O   . GLY A 585  ? 0.4229 0.6885 0.3846 0.1217  -0.0271 -0.1732 583  GLY A O   
4206  N N   . PRO A 586  ? 0.4163 0.6913 0.3778 0.1233  -0.0235 -0.1702 584  PRO A N   
4207  C CA  . PRO A 586  ? 0.3859 0.6429 0.3539 0.1232  -0.0263 -0.1752 584  PRO A CA  
4208  C C   . PRO A 586  ? 0.4653 0.7220 0.4408 0.1264  -0.0320 -0.1865 584  PRO A C   
4209  O O   . PRO A 586  ? 0.4138 0.6865 0.3909 0.1299  -0.0336 -0.1922 584  PRO A O   
4210  C CB  . PRO A 586  ? 0.4005 0.6593 0.3694 0.1240  -0.0243 -0.1738 584  PRO A CB  
4211  C CG  . PRO A 586  ? 0.4384 0.7179 0.4020 0.1250  -0.0209 -0.1691 584  PRO A CG  
4212  C CD  . PRO A 586  ? 0.4217 0.7128 0.3822 0.1254  -0.0214 -0.1693 584  PRO A CD  
4213  N N   . ALA A 587  ? 0.4133 0.6521 0.3940 0.1252  -0.0352 -0.1897 585  ALA A N   
4214  C CA  . ALA A 587  ? 0.4463 0.6827 0.4352 0.1278  -0.0410 -0.1999 585  ALA A CA  
4215  C C   . ALA A 587  ? 0.4308 0.6575 0.4281 0.1292  -0.0440 -0.2052 585  ALA A C   
4216  O O   . ALA A 587  ? 0.4469 0.6626 0.4439 0.1270  -0.0420 -0.2004 585  ALA A O   
4217  C CB  . ALA A 587  ? 0.4045 0.6286 0.3944 0.1253  -0.0432 -0.1999 585  ALA A CB  
4218  N N   . ALA A 588  ? 0.4227 0.6539 0.4279 0.1328  -0.0488 -0.2152 586  ALA A N   
4219  C CA  . ALA A 588  ? 0.4563 0.6776 0.4706 0.1341  -0.0525 -0.2208 586  ALA A CA  
4220  C C   . ALA A 588  ? 0.4372 0.6376 0.4570 0.1312  -0.0556 -0.2205 586  ALA A C   
4221  O O   . ALA A 588  ? 0.4647 0.6601 0.4826 0.1291  -0.0561 -0.2188 586  ALA A O   
4222  C CB  . ALA A 588  ? 0.3862 0.6195 0.4078 0.1391  -0.0570 -0.2317 586  ALA A CB  
4223  N N   . GLY A 589  ? 0.4177 0.6062 0.4445 0.1310  -0.0577 -0.2220 587  GLY A N   
4224  C CA  . GLY A 589  ? 0.4220 0.5907 0.4548 0.1281  -0.0608 -0.2213 587  GLY A CA  
4225  C C   . GLY A 589  ? 0.4540 0.6128 0.4949 0.1285  -0.0631 -0.2230 587  GLY A C   
4226  O O   . GLY A 589  ? 0.4662 0.6337 0.5085 0.1314  -0.0628 -0.2262 587  GLY A O   
4227  N N   . GLU A 590  ? 0.4209 0.5616 0.4671 0.1254  -0.0654 -0.2207 588  GLU A N   
4228  C CA  . GLU A 590  ? 0.4310 0.5606 0.4851 0.1251  -0.0676 -0.2213 588  GLU A CA  
4229  C C   . GLU A 590  ? 0.4227 0.5496 0.4703 0.1231  -0.0621 -0.2132 588  GLU A C   
4230  O O   . GLU A 590  ? 0.4184 0.5395 0.4589 0.1197  -0.0584 -0.2055 588  GLU A O   
4231  C CB  . GLU A 590  ? 0.4887 0.6007 0.5515 0.1224  -0.0723 -0.2211 588  GLU A CB  
4232  N N   . THR A 591  ? 0.3794 0.5103 0.4295 0.1254  -0.0618 -0.2151 589  THR A N   
4233  C CA  . THR A 591  ? 0.3892 0.5197 0.4333 0.1241  -0.0566 -0.2082 589  THR A CA  
4234  C C   . THR A 591  ? 0.4076 0.5234 0.4594 0.1227  -0.0585 -0.2068 589  THR A C   
4235  O O   . THR A 591  ? 0.4163 0.5294 0.4780 0.1247  -0.0635 -0.2131 589  THR A O   
4236  C CB  . THR A 591  ? 0.4385 0.5874 0.4785 0.1277  -0.0539 -0.2106 589  THR A CB  
4237  O OG1 . THR A 591  ? 0.4005 0.5634 0.4329 0.1285  -0.0518 -0.2106 589  THR A OG1 
4238  C CG2 . THR A 591  ? 0.3920 0.5405 0.4267 0.1264  -0.0487 -0.2035 589  THR A CG2 
4239  N N   . ARG A 592  ? 0.3715 0.4781 0.4189 0.1194  -0.0547 -0.1984 590  ARG A N   
4240  C CA  . ARG A 592  ? 0.3873 0.4805 0.4410 0.1179  -0.0560 -0.1959 590  ARG A CA  
4241  C C   . ARG A 592  ? 0.3663 0.4597 0.4125 0.1163  -0.0500 -0.1881 590  ARG A C   
4242  O O   . ARG A 592  ? 0.3552 0.4563 0.3915 0.1156  -0.0451 -0.1837 590  ARG A O   
4243  C CB  . ARG A 592  ? 0.3857 0.4618 0.4455 0.1144  -0.0596 -0.1938 590  ARG A CB  
4244  C CG  . ARG A 592  ? 0.4228 0.4930 0.4748 0.1105  -0.0560 -0.1862 590  ARG A CG  
4245  C CD  . ARG A 592  ? 0.4293 0.4816 0.4876 0.1067  -0.0591 -0.1826 590  ARG A CD  
4246  N NE  . ARG A 592  ? 0.4597 0.5072 0.5109 0.1033  -0.0564 -0.1766 590  ARG A NE  
4247  C CZ  . ARG A 592  ? 0.4607 0.5048 0.5051 0.1010  -0.0516 -0.1691 590  ARG A CZ  
4248  N NH1 . ARG A 592  ? 0.4521 0.4965 0.4957 0.1015  -0.0489 -0.1664 590  ARG A NH1 
4249  N NH2 . ARG A 592  ? 0.4660 0.5065 0.5043 0.0982  -0.0495 -0.1644 590  ARG A NH2 
4250  N N   . THR A 593  ? 0.3786 0.4635 0.4299 0.1157  -0.0504 -0.1862 591  THR A N   
4251  C CA  . THR A 593  ? 0.3456 0.4297 0.3907 0.1143  -0.0450 -0.1789 591  THR A CA  
4252  C C   . THR A 593  ? 0.3674 0.4390 0.4092 0.1099  -0.0432 -0.1712 591  THR A C   
4253  O O   . THR A 593  ? 0.3886 0.4491 0.4350 0.1078  -0.0468 -0.1713 591  THR A O   
4254  C CB  . THR A 593  ? 0.4001 0.4800 0.4519 0.1153  -0.0461 -0.1794 591  THR A CB  
4255  O OG1 . THR A 593  ? 0.4123 0.4782 0.4745 0.1140  -0.0517 -0.1811 591  THR A OG1 
4256  C CG2 . THR A 593  ? 0.4081 0.5026 0.4612 0.1197  -0.0465 -0.1858 591  THR A CG2 
4257  N N   . VAL A 594  ? 0.3076 0.3815 0.3415 0.1087  -0.0376 -0.1645 592  VAL A N   
4258  C CA  . VAL A 594  ? 0.3253 0.3878 0.3560 0.1048  -0.0354 -0.1569 592  VAL A CA  
4259  C C   . VAL A 594  ? 0.3423 0.3987 0.3756 0.1042  -0.0339 -0.1529 592  VAL A C   
4260  O O   . VAL A 594  ? 0.3341 0.3999 0.3641 0.1060  -0.0304 -0.1518 592  VAL A O   
4261  C CB  . VAL A 594  ? 0.2994 0.3698 0.3190 0.1038  -0.0302 -0.1521 592  VAL A CB  
4262  C CG1 . VAL A 594  ? 0.3149 0.3741 0.3314 0.1001  -0.0277 -0.1443 592  VAL A CG1 
4263  C CG2 . VAL A 594  ? 0.3162 0.3924 0.3335 0.1042  -0.0319 -0.1558 592  VAL A CG2 
4264  N N   . LEU A 595  ? 0.3268 0.3680 0.3666 0.1017  -0.0368 -0.1505 593  LEU A N   
4265  C CA  . LEU A 595  ? 0.3203 0.3546 0.3644 0.1011  -0.0365 -0.1471 593  LEU A CA  
4266  C C   . LEU A 595  ? 0.3137 0.3404 0.3530 0.0979  -0.0329 -0.1389 593  LEU A C   
4267  O O   . LEU A 595  ? 0.3459 0.3663 0.3827 0.0952  -0.0331 -0.1361 593  LEU A O   
4268  C CB  . LEU A 595  ? 0.3389 0.3621 0.3947 0.1006  -0.0426 -0.1498 593  LEU A CB  
4269  C CG  . LEU A 595  ? 0.3754 0.4042 0.4381 0.1037  -0.0472 -0.1584 593  LEU A CG  
4270  C CD1 . LEU A 595  ? 0.3656 0.3826 0.4403 0.1027  -0.0530 -0.1595 593  LEU A CD1 
4271  C CD2 . LEU A 595  ? 0.3756 0.4185 0.4358 0.1076  -0.0448 -0.1621 593  LEU A CD2 
4272  N N   . ASN A 596  ? 0.2975 0.3249 0.3359 0.0982  -0.0299 -0.1351 594  ASN A N   
4273  C CA  . ASN A 596  ? 0.3049 0.3251 0.3395 0.0930  -0.0269 -0.1244 594  ASN A CA  
4274  C C   . ASN A 596  ? 0.3039 0.3084 0.3455 0.0893  -0.0310 -0.1212 594  ASN A C   
4275  O O   . ASN A 596  ? 0.3007 0.2992 0.3514 0.0908  -0.0349 -0.1246 594  ASN A O   
4276  C CB  . ASN A 596  ? 0.2902 0.3148 0.3240 0.0936  -0.0237 -0.1209 594  ASN A CB  
4277  C CG  . ASN A 596  ? 0.3207 0.3402 0.3498 0.0880  -0.0201 -0.1094 594  ASN A CG  
4278  O OD1 . ASN A 596  ? 0.3149 0.3238 0.3444 0.0836  -0.0211 -0.1040 594  ASN A OD1 
4279  N ND2 . ASN A 596  ? 0.2953 0.3228 0.3200 0.0883  -0.0158 -0.1058 594  ASN A ND2 
4280  N N   . PRO A 597  ? 0.3079 0.3057 0.3459 0.0844  -0.0304 -0.1148 595  PRO A N   
4281  C CA  . PRO A 597  ? 0.2678 0.2518 0.3126 0.0808  -0.0343 -0.1114 595  PRO A CA  
4282  C C   . PRO A 597  ? 0.2981 0.2755 0.3469 0.0785  -0.0342 -0.1055 595  PRO A C   
4283  O O   . PRO A 597  ? 0.2896 0.2567 0.3463 0.0767  -0.0384 -0.1043 595  PRO A O   
4284  C CB  . PRO A 597  ? 0.2865 0.2677 0.3248 0.0762  -0.0323 -0.1051 595  PRO A CB  
4285  C CG  . PRO A 597  ? 0.2893 0.2810 0.3175 0.0763  -0.0265 -0.1019 595  PRO A CG  
4286  C CD  . PRO A 597  ? 0.2675 0.2707 0.2958 0.0821  -0.0263 -0.1102 595  PRO A CD  
4287  N N   . GLY A 598  ? 0.2636 0.2467 0.3073 0.0785  -0.0298 -0.1015 596  GLY A N   
4288  C CA  . GLY A 598  ? 0.2716 0.2492 0.3188 0.0765  -0.0297 -0.0962 596  GLY A CA  
4289  C C   . GLY A 598  ? 0.3081 0.2878 0.3627 0.0809  -0.0320 -0.1021 596  GLY A C   
4290  O O   . GLY A 598  ? 0.2987 0.2738 0.3571 0.0796  -0.0324 -0.0980 596  GLY A O   
4291  N N   . ASP A 599  ? 0.2938 0.2808 0.3504 0.0863  -0.0336 -0.1116 597  ASP A N   
4292  C CA  . ASP A 599  ? 0.3077 0.2978 0.3716 0.0912  -0.0359 -0.1186 597  ASP A CA  
4293  C C   . ASP A 599  ? 0.3035 0.3018 0.3685 0.0959  -0.0378 -0.1288 597  ASP A C   
4294  O O   . ASP A 599  ? 0.3233 0.3342 0.3813 0.0985  -0.0342 -0.1314 597  ASP A O   
4295  C CB  . ASP A 599  ? 0.2970 0.2951 0.3566 0.0921  -0.0313 -0.1155 597  ASP A CB  
4296  C CG  . ASP A 599  ? 0.3566 0.3574 0.4243 0.0969  -0.0337 -0.1219 597  ASP A CG  
4297  O OD1 . ASP A 599  ? 0.3384 0.3375 0.4133 0.0988  -0.0384 -0.1283 597  ASP A OD1 
4298  O OD2 . ASP A 599  ? 0.3664 0.3714 0.4324 0.0970  -0.0307 -0.1184 597  ASP A OD2 
4299  N N   . HIS A 600  ? 0.2957 0.2879 0.3686 0.0954  -0.0434 -0.1324 598  HIS A N   
4300  C CA  . HIS A 600  ? 0.3333 0.3330 0.4069 0.0979  -0.0457 -0.1401 598  HIS A CA  
4301  C C   . HIS A 600  ? 0.3654 0.3771 0.4398 0.1022  -0.0451 -0.1460 598  HIS A C   
4302  O O   . HIS A 600  ? 0.3611 0.3821 0.4342 0.1048  -0.0459 -0.1524 598  HIS A O   
4303  C CB  . HIS A 600  ? 0.3439 0.3340 0.4273 0.0962  -0.0521 -0.1422 598  HIS A CB  
4304  C CG  . HIS A 600  ? 0.4000 0.3813 0.4820 0.0923  -0.0529 -0.1379 598  HIS A CG  
4305  N ND1 . HIS A 600  ? 0.3995 0.3724 0.4895 0.0902  -0.0584 -0.1387 598  HIS A ND1 
4306  C CD2 . HIS A 600  ? 0.3697 0.3494 0.4433 0.0901  -0.0489 -0.1326 598  HIS A CD2 
4307  C CE1 . HIS A 600  ? 0.4074 0.3742 0.4939 0.0868  -0.0576 -0.1340 598  HIS A CE1 
4308  N NE2 . HIS A 600  ? 0.3597 0.3303 0.4363 0.0867  -0.0520 -0.1304 598  HIS A NE2 
4309  N N   . ARG A 601  ? 0.3266 0.3386 0.4030 0.1031  -0.0437 -0.1439 599  ARG A N   
4310  C CA  . ARG A 601  ? 0.3391 0.3634 0.4153 0.1071  -0.0424 -0.1488 599  ARG A CA  
4311  C C   . ARG A 601  ? 0.3819 0.4202 0.4472 0.1087  -0.0366 -0.1485 599  ARG A C   
4312  O O   . ARG A 601  ? 0.3344 0.3853 0.3984 0.1120  -0.0358 -0.1534 599  ARG A O   
4313  C CB  . ARG A 601  ? 0.3748 0.3955 0.4557 0.1073  -0.0422 -0.1458 599  ARG A CB  
4314  C CG  . ARG A 601  ? 0.3443 0.3518 0.4363 0.1055  -0.0479 -0.1452 599  ARG A CG  
4315  C CD  . ARG A 601  ? 0.3780 0.3816 0.4737 0.1052  -0.0472 -0.1408 599  ARG A CD  
4316  N NE  . ARG A 601  ? 0.3389 0.3401 0.4279 0.1029  -0.0426 -0.1330 599  ARG A NE  
4317  C CZ  . ARG A 601  ? 0.4046 0.4028 0.4951 0.1022  -0.0411 -0.1280 599  ARG A CZ  
4318  N NH1 . ARG A 601  ? 0.3995 0.3964 0.4978 0.1036  -0.0437 -0.1295 599  ARG A NH1 
4319  N NH2 . ARG A 601  ? 0.3694 0.3661 0.4537 0.1003  -0.0369 -0.1214 599  ARG A NH2 
4320  N N   . ASP A 602  ? 0.3269 0.3636 0.3846 0.1063  -0.0327 -0.1425 600  ASP A N   
4321  C CA  . ASP A 602  ? 0.3493 0.3989 0.3966 0.1072  -0.0270 -0.1406 600  ASP A CA  
4322  C C   . ASP A 602  ? 0.3659 0.4213 0.4089 0.1075  -0.0276 -0.1442 600  ASP A C   
4323  O O   . ASP A 602  ? 0.3444 0.3931 0.3849 0.1049  -0.0277 -0.1416 600  ASP A O   
4324  C CB  . ASP A 602  ? 0.3509 0.3959 0.3928 0.1044  -0.0228 -0.1323 600  ASP A CB  
4325  C CG  . ASP A 602  ? 0.3750 0.4331 0.4067 0.1046  -0.0169 -0.1289 600  ASP A CG  
4326  O OD1 . ASP A 602  ? 0.3748 0.4467 0.4043 0.1077  -0.0157 -0.1330 600  ASP A OD1 
4327  O OD2 . ASP A 602  ? 0.3425 0.3969 0.3682 0.0995  -0.0140 -0.1196 600  ASP A OD2 
4328  N N   . VAL A 603  ? 0.3466 0.4150 0.3888 0.1107  -0.0279 -0.1501 601  VAL A N   
4329  C CA  . VAL A 603  ? 0.3404 0.4161 0.3786 0.1113  -0.0285 -0.1538 601  VAL A CA  
4330  C C   . VAL A 603  ? 0.3398 0.4256 0.3671 0.1106  -0.0227 -0.1487 601  VAL A C   
4331  O O   . VAL A 603  ? 0.3498 0.4474 0.3732 0.1121  -0.0189 -0.1472 601  VAL A O   
4332  C CB  . VAL A 603  ? 0.3422 0.4283 0.3844 0.1152  -0.0316 -0.1624 601  VAL A CB  
4333  C CG1 . VAL A 603  ? 0.3383 0.4328 0.3765 0.1160  -0.0323 -0.1662 601  VAL A CG1 
4334  C CG2 . VAL A 603  ? 0.3775 0.4532 0.4311 0.1157  -0.0376 -0.1671 601  VAL A CG2 
4335  N N   . VAL A 604  ? 0.3321 0.4137 0.3549 0.1082  -0.0219 -0.1457 602  VAL A N   
4336  C CA  . VAL A 604  ? 0.3154 0.4054 0.3283 0.1070  -0.0165 -0.1399 602  VAL A CA  
4337  C C   . VAL A 604  ? 0.3183 0.4236 0.3264 0.1089  -0.0159 -0.1433 602  VAL A C   
4338  O O   . VAL A 604  ? 0.3222 0.4401 0.3234 0.1092  -0.0115 -0.1396 602  VAL A O   
4339  C CB  . VAL A 604  ? 0.3162 0.3946 0.3263 0.1034  -0.0159 -0.1347 602  VAL A CB  
4340  C CG1 . VAL A 604  ? 0.2841 0.3711 0.2844 0.1020  -0.0105 -0.1284 602  VAL A CG1 
4341  C CG2 . VAL A 604  ? 0.3105 0.3743 0.3255 0.1011  -0.0167 -0.1304 602  VAL A CG2 
4342  N N   . GLY A 605  ? 0.3179 0.4228 0.3299 0.1101  -0.0204 -0.1501 603  GLY A N   
4343  C CA  . GLY A 605  ? 0.3035 0.4229 0.3113 0.1120  -0.0202 -0.1535 603  GLY A CA  
4344  C C   . GLY A 605  ? 0.2870 0.4036 0.3008 0.1134  -0.0259 -0.1614 603  GLY A C   
4345  O O   . GLY A 605  ? 0.3127 0.4181 0.3351 0.1134  -0.0302 -0.1649 603  GLY A O   
4346  N N   . SER A 606  ? 0.2914 0.4186 0.3012 0.1144  -0.0260 -0.1638 604  SER A N   
4347  C CA  . SER A 606  ? 0.2809 0.4081 0.2961 0.1160  -0.0312 -0.1716 604  SER A CA  
4348  C C   . SER A 606  ? 0.3520 0.4810 0.3617 0.1144  -0.0307 -0.1700 604  SER A C   
4349  O O   . SER A 606  ? 0.3356 0.4746 0.3368 0.1138  -0.0264 -0.1652 604  SER A O   
4350  C CB  . SER A 606  ? 0.3637 0.5060 0.3811 0.1202  -0.0328 -0.1788 604  SER A CB  
4351  O OG  . SER A 606  ? 0.4152 0.5547 0.4391 0.1218  -0.0342 -0.1813 604  SER A OG  
4352  N N   . VAL A 607  ? 0.3170 0.4363 0.3319 0.1136  -0.0352 -0.1736 605  VAL A N   
4353  C CA  . VAL A 607  ? 0.3185 0.4383 0.3291 0.1121  -0.0353 -0.1727 605  VAL A CA  
4354  C C   . VAL A 607  ? 0.3646 0.4898 0.3806 0.1148  -0.0403 -0.1815 605  VAL A C   
4355  O O   . VAL A 607  ? 0.3258 0.4443 0.3512 0.1160  -0.0452 -0.1872 605  VAL A O   
4356  C CB  . VAL A 607  ? 0.3488 0.4515 0.3602 0.1082  -0.0358 -0.1680 605  VAL A CB  
4357  C CG1 . VAL A 607  ? 0.3550 0.4433 0.3772 0.1077  -0.0410 -0.1714 605  VAL A CG1 
4358  C CG2 . VAL A 607  ? 0.3465 0.4504 0.3538 0.1068  -0.0362 -0.1676 605  VAL A CG2 
4359  N N   . THR A 608  ? 0.3099 0.4480 0.3203 0.1158  -0.0392 -0.1824 606  THR A N   
4360  C CA  . THR A 608  ? 0.3787 0.5218 0.3934 0.1180  -0.0437 -0.1901 606  THR A CA  
4361  C C   . THR A 608  ? 0.3754 0.5105 0.3879 0.1151  -0.0443 -0.1875 606  THR A C   
4362  O O   . THR A 608  ? 0.3629 0.5022 0.3667 0.1133  -0.0403 -0.1815 606  THR A O   
4363  C CB  . THR A 608  ? 0.3874 0.5511 0.3979 0.1213  -0.0423 -0.1932 606  THR A CB  
4364  O OG1 . THR A 608  ? 0.3514 0.5224 0.3636 0.1239  -0.0415 -0.1951 606  THR A OG1 
4365  C CG2 . THR A 608  ? 0.3953 0.5644 0.4108 0.1239  -0.0472 -0.2017 606  THR A CG2 
4366  N N   . GLU A 609  ? 0.3884 0.5120 0.4090 0.1144  -0.0494 -0.1916 607  GLU A N   
4367  C CA  . GLU A 609  ? 0.3799 0.4945 0.3991 0.1113  -0.0502 -0.1889 607  GLU A CA  
4368  C C   . GLU A 609  ? 0.3667 0.4911 0.3854 0.1130  -0.0524 -0.1939 607  GLU A C   
4369  O O   . GLU A 609  ? 0.3621 0.4981 0.3838 0.1168  -0.0546 -0.2009 607  GLU A O   
4370  C CB  . GLU A 609  ? 0.3724 0.4686 0.4006 0.1090  -0.0543 -0.1890 607  GLU A CB  
4371  C CG  . GLU A 609  ? 0.3771 0.4631 0.4035 0.1063  -0.0511 -0.1817 607  GLU A CG  
4372  C CD  . GLU A 609  ? 0.4352 0.5036 0.4706 0.1038  -0.0549 -0.1808 607  GLU A CD  
4373  O OE1 . GLU A 609  ? 0.4552 0.5202 0.5002 0.1049  -0.0604 -0.1867 607  GLU A OE1 
4374  O OE2 . GLU A 609  ? 0.4087 0.4672 0.4419 0.1007  -0.0525 -0.1740 607  GLU A OE2 
4375  N N   . THR A 610  ? 0.3415 0.4615 0.3561 0.1103  -0.0518 -0.1903 608  THR A N   
4376  C CA  . THR A 610  ? 0.3730 0.5030 0.3846 0.1114  -0.0526 -0.1932 608  THR A CA  
4377  C C   . THR A 610  ? 0.3783 0.5015 0.3993 0.1119  -0.0588 -0.1999 608  THR A C   
4378  O O   . THR A 610  ? 0.3727 0.4804 0.3985 0.1090  -0.0612 -0.1982 608  THR A O   
4379  C CB  . THR A 610  ? 0.3664 0.4952 0.3687 0.1082  -0.0487 -0.1855 608  THR A CB  
4380  O OG1 . THR A 610  ? 0.3616 0.4943 0.3564 0.1073  -0.0431 -0.1784 608  THR A OG1 
4381  C CG2 . THR A 610  ? 0.3650 0.5065 0.3631 0.1094  -0.0488 -0.1876 608  THR A CG2 
4382  N N   . SER A 611  ? 0.3891 0.5244 0.4128 0.1154  -0.0615 -0.2073 609  SER A N   
4383  C CA  . SER A 611  ? 0.3947 0.5254 0.4267 0.1159  -0.0672 -0.2135 609  SER A CA  
4384  C C   . SER A 611  ? 0.4039 0.5299 0.4312 0.1128  -0.0666 -0.2094 609  SER A C   
4385  O O   . SER A 611  ? 0.3704 0.5021 0.3877 0.1114  -0.0619 -0.2036 609  SER A O   
4386  C CB  . SER A 611  ? 0.3833 0.5295 0.4187 0.1207  -0.0700 -0.2224 609  SER A CB  
4387  O OG  . SER A 611  ? 0.3616 0.5219 0.3884 0.1215  -0.0671 -0.2213 609  SER A OG  
4388  N N   . GLU A 612  ? 0.4082 0.5237 0.4433 0.1115  -0.0714 -0.2123 610  GLU A N   
4389  C CA  . GLU A 612  ? 0.4227 0.5340 0.4541 0.1087  -0.0712 -0.2091 610  GLU A CA  
4390  C C   . GLU A 612  ? 0.4054 0.5329 0.4312 0.1110  -0.0703 -0.2120 610  GLU A C   
4391  O O   . GLU A 612  ? 0.4129 0.5420 0.4309 0.1089  -0.0676 -0.2071 610  GLU A O   
4392  C CB  . GLU A 612  ? 0.4875 0.5848 0.5292 0.1068  -0.0769 -0.2116 610  GLU A CB  
4393  C CG  . GLU A 612  ? 0.5356 0.6160 0.5813 0.1032  -0.0772 -0.2062 610  GLU A CG  
4394  C CD  . GLU A 612  ? 0.6539 0.7204 0.7087 0.1004  -0.0823 -0.2065 610  GLU A CD  
4395  O OE1 . GLU A 612  ? 0.7491 0.8175 0.8045 0.1002  -0.0844 -0.2088 610  GLU A OE1 
4396  O OE2 . GLU A 612  ? 0.6356 0.6896 0.6974 0.0984  -0.0842 -0.2042 610  GLU A OE2 
4397  N N   . GLU A 613  ? 0.3851 0.5252 0.4147 0.1154  -0.0724 -0.2196 611  GLU A N   
4398  C CA  . GLU A 613  ? 0.4077 0.5649 0.4319 0.1180  -0.0713 -0.2223 611  GLU A CA  
4399  C C   . GLU A 613  ? 0.3729 0.5406 0.3853 0.1174  -0.0649 -0.2151 611  GLU A C   
4400  O O   . GLU A 613  ? 0.3404 0.5156 0.3456 0.1166  -0.0627 -0.2121 611  GLU A O   
4401  C CB  . GLU A 613  ? 0.3977 0.5669 0.4289 0.1230  -0.0749 -0.2321 611  GLU A CB  
4402  N N   . ASP A 614  ? 0.3932 0.5617 0.4035 0.1176  -0.0619 -0.2121 612  ASP A N   
4403  C CA  . ASP A 614  ? 0.3374 0.5162 0.3372 0.1170  -0.0559 -0.2050 612  ASP A CA  
4404  C C   . ASP A 614  ? 0.3667 0.5355 0.3595 0.1125  -0.0525 -0.1957 612  ASP A C   
4405  O O   . ASP A 614  ? 0.3268 0.5047 0.3108 0.1116  -0.0483 -0.1897 612  ASP A O   
4406  C CB  . ASP A 614  ? 0.3786 0.5613 0.3787 0.1187  -0.0539 -0.2045 612  ASP A CB  
4407  C CG  . ASP A 614  ? 0.3807 0.5779 0.3853 0.1235  -0.0563 -0.2130 612  ASP A CG  
4408  O OD1 . ASP A 614  ? 0.3820 0.5910 0.3864 0.1256  -0.0578 -0.2173 612  ASP A OD1 
4409  O OD2 . ASP A 614  ? 0.4090 0.6064 0.4176 0.1253  -0.0567 -0.2154 612  ASP A OD2 
4410  N N   . ALA A 615  ? 0.3205 0.4714 0.3175 0.1096  -0.0543 -0.1941 613  ALA A N   
4411  C CA  . ALA A 615  ? 0.3310 0.4725 0.3219 0.1053  -0.0515 -0.1860 613  ALA A CA  
4412  C C   . ALA A 615  ? 0.3419 0.4882 0.3289 0.1045  -0.0519 -0.1855 613  ALA A C   
4413  O O   . ALA A 615  ? 0.3344 0.4850 0.3128 0.1027  -0.0479 -0.1788 613  ALA A O   
4414  C CB  . ALA A 615  ? 0.3536 0.4755 0.3510 0.1025  -0.0540 -0.1851 613  ALA A CB  
4415  N N   . ARG A 616  ? 0.3842 0.5307 0.3778 0.1060  -0.0567 -0.1927 614  ARG A N   
4416  C CA  . ARG A 616  ? 0.3838 0.5359 0.3742 0.1056  -0.0574 -0.1930 614  ARG A CA  
4417  C C   . ARG A 616  ? 0.3450 0.5168 0.3281 0.1079  -0.0542 -0.1920 614  ARG A C   
4418  O O   . ARG A 616  ? 0.3618 0.5387 0.3378 0.1064  -0.0519 -0.1872 614  ARG A O   
4419  C CB  . ARG A 616  ? 0.3728 0.5212 0.3727 0.1070  -0.0634 -0.2014 614  ARG A CB  
4420  N N   . ARG A 617  ? 0.3594 0.5429 0.3442 0.1116  -0.0540 -0.1961 615  ARG A N   
4421  C CA  . ARG A 617  ? 0.3550 0.5580 0.3331 0.1136  -0.0507 -0.1944 615  ARG A CA  
4422  C C   . ARG A 617  ? 0.3583 0.5629 0.3270 0.1109  -0.0450 -0.1838 615  ARG A C   
4423  O O   . ARG A 617  ? 0.3362 0.5524 0.2982 0.1105  -0.0423 -0.1792 615  ARG A O   
4424  C CB  . ARG A 617  ? 0.3790 0.5935 0.3613 0.1179  -0.0518 -0.2007 615  ARG A CB  
4425  C CG  . ARG A 617  ? 0.4522 0.6882 0.4286 0.1202  -0.0488 -0.1994 615  ARG A CG  
4426  C CD  . ARG A 617  ? 0.4819 0.7310 0.4644 0.1251  -0.0519 -0.2090 615  ARG A CD  
4427  N NE  . ARG A 617  ? 0.4721 0.7163 0.4600 0.1266  -0.0528 -0.2122 615  ARG A NE  
4428  C CZ  . ARG A 617  ? 0.5293 0.7819 0.5141 0.1275  -0.0496 -0.2092 615  ARG A CZ  
4429  N NH1 . ARG A 617  ? 0.5268 0.7934 0.5035 0.1271  -0.0451 -0.2027 615  ARG A NH1 
4430  N NH2 . ARG A 617  ? 0.4532 0.7002 0.4436 0.1288  -0.0509 -0.2127 615  ARG A NH2 
4431  N N   . ALA A 618  ? 0.3388 0.5324 0.3075 0.1090  -0.0431 -0.1796 616  ALA A N   
4432  C CA  . ALA A 618  ? 0.3218 0.5164 0.2821 0.1064  -0.0378 -0.1696 616  ALA A CA  
4433  C C   . ALA A 618  ? 0.3188 0.5094 0.2737 0.1032  -0.0366 -0.1637 616  ALA A C   
4434  O O   . ALA A 618  ? 0.3140 0.5137 0.2615 0.1021  -0.0328 -0.1564 616  ALA A O   
4435  C CB  . ALA A 618  ? 0.3077 0.4893 0.2698 0.1049  -0.0364 -0.1668 616  ALA A CB  
4436  N N   . VAL A 619  ? 0.2987 0.4761 0.2574 0.1015  -0.0400 -0.1664 617  VAL A N   
4437  C CA  . VAL A 619  ? 0.3343 0.5077 0.2882 0.0985  -0.0392 -0.1611 617  VAL A CA  
4438  C C   . VAL A 619  ? 0.3457 0.5349 0.2958 0.0999  -0.0390 -0.1614 617  VAL A C   
4439  O O   . VAL A 619  ? 0.3280 0.5218 0.2712 0.0980  -0.0362 -0.1542 617  VAL A O   
4440  C CB  . VAL A 619  ? 0.3338 0.4903 0.2935 0.0965  -0.0433 -0.1644 617  VAL A CB  
4441  C CG1 . VAL A 619  ? 0.3735 0.5272 0.3282 0.0936  -0.0428 -0.1596 617  VAL A CG1 
4442  C CG2 . VAL A 619  ? 0.3065 0.4474 0.2694 0.0946  -0.0430 -0.1626 617  VAL A CG2 
4443  N N   . ARG A 620  ? 0.3310 0.5292 0.2859 0.1033  -0.0421 -0.1696 618  ARG A N   
4444  C CA  . ARG A 620  ? 0.3450 0.5593 0.2967 0.1049  -0.0420 -0.1703 618  ARG A CA  
4445  C C   . ARG A 620  ? 0.3411 0.5709 0.2859 0.1054  -0.0372 -0.1634 618  ARG A C   
4446  O O   . ARG A 620  ? 0.3542 0.5927 0.2933 0.1043  -0.0353 -0.1579 618  ARG A O   
4447  C CB  . ARG A 620  ? 0.3694 0.5907 0.3282 0.1089  -0.0463 -0.1810 618  ARG A CB  
4448  C CG  . ARG A 620  ? 0.4382 0.6460 0.4040 0.1082  -0.0513 -0.1871 618  ARG A CG  
4449  C CD  . ARG A 620  ? 0.5043 0.7203 0.4770 0.1121  -0.0557 -0.1973 618  ARG A CD  
4450  N NE  . ARG A 620  ? 0.5422 0.7488 0.5242 0.1136  -0.0593 -0.2042 618  ARG A NE  
4451  C CZ  . ARG A 620  ? 0.4931 0.7080 0.4790 0.1172  -0.0601 -0.2096 618  ARG A CZ  
4452  N NH1 . ARG A 620  ? 0.5294 0.7628 0.5109 0.1199  -0.0576 -0.2094 618  ARG A NH1 
4453  N NH2 . ARG A 620  ? 0.5750 0.7797 0.5697 0.1181  -0.0636 -0.2150 618  ARG A NH2 
4454  N N   . LEU A 621  ? 0.3267 0.5598 0.2722 0.1067  -0.0354 -0.1631 619  LEU A N   
4455  C CA  . LEU A 621  ? 0.3366 0.5839 0.2762 0.1068  -0.0310 -0.1560 619  LEU A CA  
4456  C C   . LEU A 621  ? 0.3348 0.5762 0.2678 0.1028  -0.0271 -0.1449 619  LEU A C   
4457  O O   . LEU A 621  ? 0.3725 0.6260 0.3001 0.1020  -0.0242 -0.1377 619  LEU A O   
4458  C CB  . LEU A 621  ? 0.3020 0.5526 0.2444 0.1090  -0.0301 -0.1582 619  LEU A CB  
4459  C CG  . LEU A 621  ? 0.3429 0.6007 0.2920 0.1133  -0.0339 -0.1692 619  LEU A CG  
4460  C CD1 . LEU A 621  ? 0.3412 0.5977 0.2936 0.1149  -0.0333 -0.1712 619  LEU A CD1 
4461  C CD2 . LEU A 621  ? 0.3726 0.6517 0.3198 0.1159  -0.0337 -0.1706 619  LEU A CD2 
4462  N N   . ALA A 622  ? 0.3319 0.5553 0.2657 0.1002  -0.0273 -0.1432 620  ALA A N   
4463  C CA  . ALA A 622  ? 0.3301 0.5471 0.2582 0.0964  -0.0242 -0.1334 620  ALA A CA  
4464  C C   . ALA A 622  ? 0.3269 0.5475 0.2515 0.0950  -0.0247 -0.1305 620  ALA A C   
4465  O O   . ALA A 622  ? 0.3411 0.5681 0.2601 0.0931  -0.0216 -0.1216 620  ALA A O   
4466  C CB  . ALA A 622  ? 0.2992 0.4963 0.2296 0.0942  -0.0248 -0.1334 620  ALA A CB  
4467  N N   . ALA A 623  ? 0.3057 0.5222 0.2340 0.0958  -0.0288 -0.1377 621  ALA A N   
4468  C CA  . ALA A 623  ? 0.3550 0.5752 0.2804 0.0946  -0.0296 -0.1356 621  ALA A CA  
4469  C C   . ALA A 623  ? 0.3568 0.5972 0.2786 0.0961  -0.0278 -0.1326 621  ALA A C   
4470  O O   . ALA A 623  ? 0.3505 0.5959 0.2673 0.0941  -0.0259 -0.1251 621  ALA A O   
4471  C CB  . ALA A 623  ? 0.3609 0.5742 0.2919 0.0955  -0.0345 -0.1446 621  ALA A CB  
4472  N N   . ASP A 624  ? 0.3651 0.6176 0.2898 0.0996  -0.0284 -0.1382 622  ASP A N   
4473  C CA  . ASP A 624  ? 0.4102 0.6830 0.3319 0.1012  -0.0267 -0.1355 622  ASP A CA  
4474  C C   . ASP A 624  ? 0.3833 0.6622 0.2998 0.0991  -0.0220 -0.1241 622  ASP A C   
4475  O O   . ASP A 624  ? 0.4001 0.6914 0.3128 0.0983  -0.0202 -0.1177 622  ASP A O   
4476  C CB  . ASP A 624  ? 0.4367 0.7211 0.3630 0.1055  -0.0283 -0.1441 622  ASP A CB  
4477  C CG  . ASP A 624  ? 0.4858 0.7660 0.4182 0.1079  -0.0332 -0.1555 622  ASP A CG  
4478  O OD1 . ASP A 624  ? 0.4971 0.7721 0.4293 0.1066  -0.0352 -0.1564 622  ASP A OD1 
4479  O OD2 . ASP A 624  ? 0.5371 0.8192 0.4749 0.1110  -0.0352 -0.1634 622  ASP A OD2 
4480  N N   . ALA A 625  ? 0.3777 0.6479 0.2942 0.0980  -0.0200 -0.1212 623  ALA A N   
4481  C CA  . ALA A 625  ? 0.3908 0.6659 0.3031 0.0960  -0.0157 -0.1105 623  ALA A CA  
4482  C C   . ALA A 625  ? 0.4013 0.6659 0.3096 0.0919  -0.0139 -0.1014 623  ALA A C   
4483  O O   . ALA A 625  ? 0.4366 0.7054 0.3419 0.0900  -0.0105 -0.0916 623  ALA A O   
4484  C CB  . ALA A 625  ? 0.4138 0.6850 0.3282 0.0968  -0.0143 -0.1116 623  ALA A CB  
4485  N N   . ALA A 626  ? 0.3903 0.6418 0.2991 0.0906  -0.0163 -0.1041 624  ALA A N   
4486  C CA  . ALA A 626  ? 0.3656 0.6063 0.2709 0.0869  -0.0148 -0.0960 624  ALA A CA  
4487  C C   . ALA A 626  ? 0.4032 0.6547 0.3042 0.0851  -0.0126 -0.0857 624  ALA A C   
4488  O O   . ALA A 626  ? 0.3739 0.6216 0.2724 0.0824  -0.0098 -0.0764 624  ALA A O   
4489  C CB  . ALA A 626  ? 0.3646 0.5910 0.2716 0.0860  -0.0182 -0.1013 624  ALA A CB  
4490  N N   . PRO A 627  ? 0.3983 0.6631 0.2988 0.0862  -0.0136 -0.0864 625  PRO A N   
4491  C CA  . PRO A 627  ? 0.3810 0.6560 0.2782 0.0842  -0.0115 -0.0756 625  PRO A CA  
4492  C C   . PRO A 627  ? 0.3840 0.6679 0.2803 0.0835  -0.0079 -0.0673 625  PRO A C   
4493  O O   . PRO A 627  ? 0.3866 0.6700 0.2809 0.0806  -0.0057 -0.0566 625  PRO A O   
4494  C CB  . PRO A 627  ? 0.4219 0.7110 0.3195 0.0863  -0.0134 -0.0799 625  PRO A CB  
4495  C CG  . PRO A 627  ? 0.3907 0.6712 0.2915 0.0883  -0.0172 -0.0918 625  PRO A CG  
4496  C CD  . PRO A 627  ? 0.4139 0.6844 0.3173 0.0891  -0.0170 -0.0965 625  PRO A CD  
4497  N N   . ASP A 628  ? 0.3683 0.6604 0.2667 0.0861  -0.0074 -0.0719 626  ASP A N   
4498  C CA  . ASP A 628  ? 0.3565 0.6587 0.2546 0.0856  -0.0042 -0.0642 626  ASP A CA  
4499  C C   . ASP A 628  ? 0.4030 0.6920 0.3003 0.0829  -0.0019 -0.0578 626  ASP A C   
4500  O O   . ASP A 628  ? 0.4018 0.6957 0.2983 0.0807  0.0008  -0.0474 626  ASP A O   
4501  C CB  . ASP A 628  ? 0.3636 0.6767 0.2643 0.0892  -0.0045 -0.0715 626  ASP A CB  
4502  C CG  . ASP A 628  ? 0.4393 0.7693 0.3408 0.0919  -0.0062 -0.0762 626  ASP A CG  
4503  O OD1 . ASP A 628  ? 0.5022 0.8340 0.4023 0.0911  -0.0074 -0.0748 626  ASP A OD1 
4504  O OD2 . ASP A 628  ? 0.4605 0.8026 0.3642 0.0949  -0.0064 -0.0811 626  ASP A OD2 
4505  N N   . TRP A 629  ? 0.3404 0.6130 0.2386 0.0830  -0.0030 -0.0637 627  TRP A N   
4506  C CA  . TRP A 629  ? 0.3543 0.6147 0.2518 0.0806  -0.0008 -0.0581 627  TRP A CA  
4507  C C   . TRP A 629  ? 0.3450 0.5973 0.2400 0.0771  -0.0003 -0.0497 627  TRP A C   
4508  O O   . TRP A 629  ? 0.3426 0.5922 0.2367 0.0747  0.0023  -0.0404 627  TRP A O   
4509  C CB  . TRP A 629  ? 0.3274 0.5736 0.2271 0.0819  -0.0022 -0.0671 627  TRP A CB  
4510  C CG  . TRP A 629  ? 0.2923 0.5259 0.1914 0.0796  0.0000  -0.0619 627  TRP A CG  
4511  C CD1 . TRP A 629  ? 0.2798 0.4966 0.1787 0.0781  -0.0008 -0.0632 627  TRP A CD1 
4512  C CD2 . TRP A 629  ? 0.2823 0.5197 0.1810 0.0785  0.0034  -0.0541 627  TRP A CD2 
4513  N NE1 . TRP A 629  ? 0.2613 0.4697 0.1616 0.0757  0.0018  -0.0563 627  TRP A NE1 
4514  C CE2 . TRP A 629  ? 0.2583 0.4805 0.1567 0.0764  0.0046  -0.0514 627  TRP A CE2 
4515  C CE3 . TRP A 629  ? 0.3065 0.5589 0.2057 0.0789  0.0054  -0.0493 627  TRP A CE3 
4516  C CZ2 . TRP A 629  ? 0.2651 0.4855 0.1643 0.0746  0.0075  -0.0438 627  TRP A CZ2 
4517  C CZ3 . TRP A 629  ? 0.3154 0.5667 0.2149 0.0772  0.0084  -0.0418 627  TRP A CZ3 
4518  C CH2 . TRP A 629  ? 0.2955 0.5312 0.1945 0.0752  0.0095  -0.0393 627  TRP A CH2 
4519  N N   . ALA A 630  ? 0.3199 0.5684 0.2140 0.0770  -0.0028 -0.0528 628  ALA A N   
4520  C CA  . ALA A 630  ? 0.3568 0.5989 0.2487 0.0739  -0.0026 -0.0450 628  ALA A CA  
4521  C C   . ALA A 630  ? 0.3730 0.6272 0.2641 0.0721  -0.0006 -0.0334 628  ALA A C   
4522  O O   . ALA A 630  ? 0.3286 0.5774 0.2188 0.0692  0.0005  -0.0241 628  ALA A O   
4523  C CB  . ALA A 630  ? 0.3604 0.5983 0.2520 0.0743  -0.0060 -0.0509 628  ALA A CB  
4524  N N   . ALA A 631  ? 0.3340 0.6047 0.2259 0.0737  -0.0002 -0.0335 629  ALA A N   
4525  C CA  . ALA A 631  ? 0.3471 0.6306 0.2391 0.0720  0.0014  -0.0226 629  ALA A CA  
4526  C C   . ALA A 631  ? 0.3678 0.6527 0.2611 0.0703  0.0044  -0.0142 629  ALA A C   
4527  O O   . ALA A 631  ? 0.3634 0.6557 0.2577 0.0681  0.0057  -0.0035 629  ALA A O   
4528  C CB  . ALA A 631  ? 0.3681 0.6698 0.2608 0.0744  0.0006  -0.0260 629  ALA A CB  
4529  N N   . VAL A 632  ? 0.3298 0.6077 0.2237 0.0712  0.0054  -0.0184 630  VAL A N   
4530  C CA  . VAL A 632  ? 0.3114 0.5883 0.2066 0.0693  0.0081  -0.0102 630  VAL A CA  
4531  C C   . VAL A 632  ? 0.3099 0.5737 0.2046 0.0659  0.0086  -0.0022 630  VAL A C   
4532  O O   . VAL A 632  ? 0.3189 0.5686 0.2122 0.0659  0.0075  -0.0070 630  VAL A O   
4533  C CB  . VAL A 632  ? 0.3141 0.5862 0.2101 0.0712  0.0090  -0.0172 630  VAL A CB  
4534  C CG1 . VAL A 632  ? 0.3207 0.5909 0.2182 0.0690  0.0118  -0.0084 630  VAL A CG1 
4535  C CG2 . VAL A 632  ? 0.3237 0.6099 0.2209 0.0748  0.0082  -0.0250 630  VAL A CG2 
4536  N N   . PRO A 633  ? 0.3136 0.5819 0.2101 0.0631  0.0099  0.0098  631  PRO A N   
4537  C CA  . PRO A 633  ? 0.2778 0.5343 0.1746 0.0600  0.0099  0.0176  631  PRO A CA  
4538  C C   . PRO A 633  ? 0.3227 0.5613 0.2217 0.0589  0.0106  0.0156  631  PRO A C   
4539  O O   . PRO A 633  ? 0.3064 0.5457 0.2056 0.0600  0.0122  0.0130  631  PRO A O   
4540  C CB  . PRO A 633  ? 0.2920 0.5572 0.1924 0.0573  0.0112  0.0305  631  PRO A CB  
4541  C CG  . PRO A 633  ? 0.3238 0.6074 0.2248 0.0591  0.0112  0.0290  631  PRO A CG  
4542  C CD  . PRO A 633  ? 0.3327 0.6174 0.2317 0.0626  0.0112  0.0169  631  PRO A CD  
4543  N N   . PRO A 634  ? 0.2854 0.5067 0.1880 0.0565  0.0094  0.0164  632  PRO A N   
4544  C CA  . PRO A 634  ? 0.2767 0.4799 0.1833 0.0550  0.0098  0.0142  632  PRO A CA  
4545  C C   . PRO A 634  ? 0.2821 0.4851 0.1913 0.0534  0.0122  0.0210  632  PRO A C   
4546  O O   . PRO A 634  ? 0.2559 0.4514 0.1664 0.0538  0.0131  0.0168  632  PRO A O   
4547  C CB  . PRO A 634  ? 0.2664 0.4552 0.1763 0.0523  0.0083  0.0170  632  PRO A CB  
4548  C CG  . PRO A 634  ? 0.3270 0.5246 0.2339 0.0534  0.0064  0.0157  632  PRO A CG  
4549  C CD  . PRO A 634  ? 0.2964 0.5149 0.1994 0.0552  0.0074  0.0190  632  PRO A CD  
4550  N N   . SER A 635  ? 0.2879 0.4991 0.1984 0.0515  0.0132  0.0318  633  SER A N   
4551  C CA  . SER A 635  ? 0.3036 0.5151 0.2173 0.0498  0.0152  0.0389  633  SER A CA  
4552  C C   . SER A 635  ? 0.2946 0.5171 0.2053 0.0525  0.0169  0.0345  633  SER A C   
4553  O O   . SER A 635  ? 0.2777 0.4944 0.1909 0.0518  0.0184  0.0348  633  SER A O   
4554  C CB  . SER A 635  ? 0.3276 0.5481 0.2434 0.0475  0.0155  0.0514  633  SER A CB  
4555  O OG  . SER A 635  ? 0.4300 0.6707 0.3413 0.0494  0.0156  0.0527  633  SER A OG  
4556  N N   . GLU A 636  ? 0.2858 0.5247 0.1913 0.0556  0.0168  0.0301  634  GLU A N   
4557  C CA  . GLU A 636  ? 0.3087 0.5589 0.2122 0.0584  0.0182  0.0251  634  GLU A CA  
4558  C C   . GLU A 636  ? 0.3125 0.5524 0.2150 0.0609  0.0176  0.0131  634  GLU A C   
4559  O O   . GLU A 636  ? 0.3043 0.5454 0.2074 0.0621  0.0190  0.0102  634  GLU A O   
4560  C CB  . GLU A 636  ? 0.3337 0.6016 0.2373 0.0601  0.0174  0.0238  634  GLU A CB  
4561  C CG  . GLU A 636  ? 0.3732 0.6518 0.2774 0.0629  0.0181  0.0179  634  GLU A CG  
4562  C CD  . GLU A 636  ? 0.4678 0.7471 0.3749 0.0614  0.0205  0.0240  634  GLU A CD  
4563  O OE1 . GLU A 636  ? 0.4543 0.7336 0.3644 0.0581  0.0214  0.0353  634  GLU A OE1 
4564  O OE2 . GLU A 636  ? 0.4114 0.6909 0.3185 0.0636  0.0212  0.0176  634  GLU A OE2 
4565  N N   . ARG A 637  ? 0.2979 0.5271 0.2003 0.0613  0.0153  0.0062  635  ARG A N   
4566  C CA  . ARG A 637  ? 0.2651 0.4813 0.1688 0.0627  0.0143  -0.0039 635  ARG A CA  
4567  C C   . ARG A 637  ? 0.2667 0.4675 0.1750 0.0600  0.0155  -0.0003 635  ARG A C   
4568  O O   . ARG A 637  ? 0.2758 0.4729 0.1851 0.0613  0.0161  -0.0054 635  ARG A O   
4569  C CB  . ARG A 637  ? 0.2585 0.4652 0.1621 0.0629  0.0115  -0.0103 635  ARG A CB  
4570  C CG  . ARG A 637  ? 0.2828 0.5048 0.1818 0.0657  0.0101  -0.0144 635  ARG A CG  
4571  C CD  . ARG A 637  ? 0.2685 0.4819 0.1676 0.0667  0.0070  -0.0232 635  ARG A CD  
4572  N NE  . ARG A 637  ? 0.2601 0.4581 0.1623 0.0632  0.0060  -0.0190 635  ARG A NE  
4573  C CZ  . ARG A 637  ? 0.3308 0.5300 0.2322 0.0622  0.0046  -0.0163 635  ARG A CZ  
4574  N NH1 . ARG A 637  ? 0.3017 0.5172 0.1990 0.0641  0.0040  -0.0166 635  ARG A NH1 
4575  N NH2 . ARG A 637  ? 0.2975 0.4817 0.2022 0.0593  0.0038  -0.0134 635  ARG A NH2 
4576  N N   . ALA A 638  ? 0.2649 0.4569 0.1763 0.0563  0.0157  0.0084  636  ALA A N   
4577  C CA  . ALA A 638  ? 0.2654 0.4441 0.1813 0.0537  0.0168  0.0122  636  ALA A CA  
4578  C C   . ALA A 638  ? 0.2930 0.4807 0.2094 0.0539  0.0191  0.0164  636  ALA A C   
4579  O O   . ALA A 638  ? 0.2572 0.4361 0.1761 0.0533  0.0200  0.0152  636  ALA A O   
4580  C CB  . ALA A 638  ? 0.2450 0.4146 0.1644 0.0500  0.0163  0.0206  636  ALA A CB  
4581  N N   . ALA A 639  ? 0.2719 0.4775 0.1858 0.0547  0.0202  0.0215  637  ALA A N   
4582  C CA  . ALA A 639  ? 0.2779 0.4939 0.1922 0.0550  0.0225  0.0254  637  ALA A CA  
4583  C C   . ALA A 639  ? 0.2701 0.4887 0.1826 0.0585  0.0230  0.0154  637  ALA A C   
4584  O O   . ALA A 639  ? 0.2652 0.4828 0.1798 0.0583  0.0245  0.0164  637  ALA A O   
4585  C CB  . ALA A 639  ? 0.2797 0.5160 0.1917 0.0553  0.0234  0.0327  637  ALA A CB  
4586  N N   . CYS A 640  ? 0.2845 0.5062 0.1936 0.0618  0.0214  0.0055  638  CYS A N   
4587  C CA  . CYS A 640  ? 0.2622 0.4846 0.1707 0.0653  0.0213  -0.0048 638  CYS A CA  
4588  C C   . CYS A 640  ? 0.2711 0.4739 0.1838 0.0638  0.0209  -0.0074 638  CYS A C   
4589  O O   . CYS A 640  ? 0.2759 0.4783 0.1899 0.0650  0.0219  -0.0101 638  CYS A O   
4590  C CB  . CYS A 640  ? 0.2663 0.4932 0.1715 0.0688  0.0190  -0.0153 638  CYS A CB  
4591  S SG  . CYS A 640  ? 0.2954 0.5443 0.1984 0.0705  0.0186  -0.0140 638  CYS A SG  
4592  N N   . LEU A 641  ? 0.2602 0.4470 0.1749 0.0613  0.0193  -0.0067 639  LEU A N   
4593  C CA  . LEU A 641  ? 0.2423 0.4111 0.1609 0.0596  0.0190  -0.0086 639  LEU A CA  
4594  C C   . LEU A 641  ? 0.2419 0.4085 0.1634 0.0572  0.0212  -0.0009 639  LEU A C   
4595  O O   . LEU A 641  ? 0.2631 0.4231 0.1868 0.0575  0.0216  -0.0038 639  LEU A O   
4596  C CB  . LEU A 641  ? 0.2422 0.3964 0.1624 0.0570  0.0172  -0.0078 639  LEU A CB  
4597  C CG  . LEU A 641  ? 0.2545 0.4023 0.1742 0.0588  0.0145  -0.0175 639  LEU A CG  
4598  C CD1 . LEU A 641  ? 0.2736 0.4359 0.1893 0.0620  0.0134  -0.0225 639  LEU A CD1 
4599  C CD2 . LEU A 641  ? 0.2297 0.3631 0.1515 0.0558  0.0131  -0.0155 639  LEU A CD2 
4600  N N   . ASP A 642  ? 0.2632 0.4351 0.1852 0.0548  0.0223  0.0091  640  ASP A N   
4601  C CA  . ASP A 642  ? 0.2562 0.4261 0.1817 0.0523  0.0242  0.0166  640  ASP A CA  
4602  C C   . ASP A 642  ? 0.2469 0.4290 0.1714 0.0546  0.0260  0.0152  640  ASP A C   
4603  O O   . ASP A 642  ? 0.2449 0.4217 0.1724 0.0537  0.0270  0.0164  640  ASP A O   
4604  C CB  . ASP A 642  ? 0.2554 0.4295 0.1826 0.0494  0.0246  0.0277  640  ASP A CB  
4605  C CG  . ASP A 642  ? 0.2701 0.4288 0.2002 0.0464  0.0232  0.0303  640  ASP A CG  
4606  O OD1 . ASP A 642  ? 0.2656 0.4096 0.1971 0.0460  0.0223  0.0252  640  ASP A OD1 
4607  O OD2 . ASP A 642  ? 0.2619 0.4236 0.1930 0.0446  0.0228  0.0376  640  ASP A OD2 
4608  N N   . ARG A 643  ? 0.2829 0.4820 0.2035 0.0578  0.0263  0.0124  641  ARG A N   
4609  C CA  . ARG A 643  ? 0.2621 0.4740 0.1817 0.0604  0.0280  0.0101  641  ARG A CA  
4610  C C   . ARG A 643  ? 0.2581 0.4612 0.1786 0.0628  0.0273  -0.0001 641  ARG A C   
4611  O O   . ARG A 643  ? 0.2825 0.4869 0.2048 0.0634  0.0286  -0.0004 641  ARG A O   
4612  C CB  . ARG A 643  ? 0.2699 0.5029 0.1848 0.0635  0.0284  0.0086  641  ARG A CB  
4613  C CG  . ARG A 643  ? 0.2562 0.5023 0.1708 0.0612  0.0298  0.0202  641  ARG A CG  
4614  C CD  . ARG A 643  ? 0.3011 0.5649 0.2157 0.0633  0.0288  0.0181  641  ARG A CD  
4615  N NE  . ARG A 643  ? 0.3087 0.5741 0.2204 0.0655  0.0266  0.0110  641  ARG A NE  
4616  C CZ  . ARG A 643  ? 0.2818 0.5508 0.1928 0.0641  0.0256  0.0156  641  ARG A CZ  
4617  N NH1 . ARG A 643  ? 0.2956 0.5662 0.2088 0.0605  0.0264  0.0274  641  ARG A NH1 
4618  N NH2 . ARG A 643  ? 0.3245 0.5952 0.2329 0.0662  0.0235  0.0083  641  ARG A NH2 
4619  N N   . ALA A 644  ? 0.2557 0.4498 0.1755 0.0641  0.0249  -0.0084 642  ALA A N   
4620  C CA  . ALA A 644  ? 0.2466 0.4309 0.1682 0.0661  0.0237  -0.0175 642  ALA A CA  
4621  C C   . ALA A 644  ? 0.2584 0.4270 0.1844 0.0629  0.0242  -0.0138 642  ALA A C   
4622  O O   . ALA A 644  ? 0.2389 0.4042 0.1669 0.0642  0.0245  -0.0176 642  ALA A O   
4623  C CB  . ALA A 644  ? 0.2580 0.4351 0.1789 0.0675  0.0208  -0.0259 642  ALA A CB  
4624  N N   . ALA A 645  ? 0.2558 0.4149 0.1833 0.0590  0.0243  -0.0064 643  ALA A N   
4625  C CA  . ALA A 645  ? 0.2315 0.3766 0.1631 0.0560  0.0247  -0.0026 643  ALA A CA  
4626  C C   . ALA A 645  ? 0.2467 0.3988 0.1798 0.0555  0.0270  0.0025  643  ALA A C   
4627  O O   . ALA A 645  ? 0.2519 0.3963 0.1879 0.0551  0.0273  0.0012  643  ALA A O   
4628  C CB  . ALA A 645  ? 0.2459 0.3815 0.1790 0.0521  0.0242  0.0041  643  ALA A CB  
4629  N N   . GLU A 646  ? 0.2664 0.4333 0.1981 0.0554  0.0286  0.0089  644  GLU A N   
4630  C CA  . GLU A 646  ? 0.2763 0.4517 0.2097 0.0551  0.0308  0.0139  644  GLU A CA  
4631  C C   . GLU A 646  ? 0.2891 0.4704 0.2217 0.0589  0.0313  0.0060  644  GLU A C   
4632  O O   . GLU A 646  ? 0.2784 0.4576 0.2138 0.0585  0.0324  0.0070  644  GLU A O   
4633  C CB  . GLU A 646  ? 0.2983 0.4906 0.2302 0.0546  0.0322  0.0219  644  GLU A CB  
4634  C CG  . GLU A 646  ? 0.3320 0.5198 0.2661 0.0506  0.0319  0.0314  644  GLU A CG  
4635  C CD  . GLU A 646  ? 0.4107 0.5852 0.3500 0.0471  0.0321  0.0367  644  GLU A CD  
4636  O OE1 . GLU A 646  ? 0.4619 0.6393 0.4033 0.0470  0.0335  0.0383  644  GLU A OE1 
4637  O OE2 . GLU A 646  ? 0.4056 0.5672 0.3470 0.0445  0.0308  0.0390  644  GLU A OE2 
4638  N N   . LEU A 647  ? 0.2823 0.4717 0.2115 0.0627  0.0303  -0.0021 645  LEU A N   
4639  C CA  . LEU A 647  ? 0.2650 0.4605 0.1940 0.0668  0.0304  -0.0107 645  LEU A CA  
4640  C C   . LEU A 647  ? 0.3031 0.4814 0.2355 0.0666  0.0290  -0.0161 645  LEU A C   
4641  O O   . LEU A 647  ? 0.2903 0.4694 0.2249 0.0679  0.0298  -0.0181 645  LEU A O   
4642  C CB  . LEU A 647  ? 0.2586 0.4650 0.1838 0.0709  0.0291  -0.0190 645  LEU A CB  
4643  C CG  . LEU A 647  ? 0.2791 0.5068 0.2003 0.0723  0.0306  -0.0154 645  LEU A CG  
4644  C CD1 . LEU A 647  ? 0.2574 0.4925 0.1754 0.0758  0.0286  -0.0241 645  LEU A CD1 
4645  C CD2 . LEU A 647  ? 0.2994 0.5413 0.2215 0.0737  0.0328  -0.0135 645  LEU A CD2 
4646  N N   . MET A 648  ? 0.2544 0.4174 0.1877 0.0650  0.0269  -0.0181 646  MET A N   
4647  C CA  . MET A 648  ? 0.2678 0.4151 0.2046 0.0646  0.0254  -0.0227 646  MET A CA  
4648  C C   . MET A 648  ? 0.2549 0.3949 0.1950 0.0613  0.0269  -0.0158 646  MET A C   
4649  O O   . MET A 648  ? 0.2726 0.4066 0.2154 0.0620  0.0267  -0.0189 646  MET A O   
4650  C CB  . MET A 648  ? 0.2387 0.3723 0.1758 0.0632  0.0229  -0.0255 646  MET A CB  
4651  C CG  . MET A 648  ? 0.2787 0.4161 0.2141 0.0667  0.0207  -0.0348 646  MET A CG  
4652  S SD  . MET A 648  ? 0.2962 0.4154 0.2335 0.0650  0.0175  -0.0385 646  MET A SD  
4653  C CE  . MET A 648  ? 0.3047 0.4325 0.2398 0.0693  0.0150  -0.0484 646  MET A CE  
4654  N N   . GLN A 649  ? 0.2686 0.4085 0.2088 0.0579  0.0282  -0.0065 647  GLN A N   
4655  C CA  . GLN A 649  ? 0.2444 0.3781 0.1880 0.0548  0.0295  0.0000  647  GLN A CA  
4656  C C   . GLN A 649  ? 0.2678 0.4122 0.2122 0.0566  0.0313  0.0002  647  GLN A C   
4657  O O   . GLN A 649  ? 0.2755 0.4131 0.2229 0.0561  0.0315  -0.0003 647  GLN A O   
4658  C CB  . GLN A 649  ? 0.2684 0.4023 0.2126 0.0512  0.0303  0.0097  647  GLN A CB  
4659  C CG  . GLN A 649  ? 0.2690 0.3949 0.2173 0.0478  0.0311  0.0160  647  GLN A CG  
4660  C CD  . GLN A 649  ? 0.2663 0.3743 0.2168 0.0459  0.0295  0.0135  647  GLN A CD  
4661  O OE1 . GLN A 649  ? 0.2714 0.3716 0.2219 0.0441  0.0284  0.0149  647  GLN A OE1 
4662  N NE2 . GLN A 649  ? 0.2911 0.3931 0.2436 0.0465  0.0294  0.0100  647  GLN A NE2 
4663  N N   . ALA A 650  ? 0.2927 0.4544 0.2345 0.0589  0.0326  0.0009  648  ALA A N   
4664  C CA  . ALA A 650  ? 0.2787 0.4526 0.2213 0.0607  0.0345  0.0014  648  ALA A CA  
4665  C C   . ALA A 650  ? 0.3208 0.4930 0.2642 0.0644  0.0336  -0.0085 648  ALA A C   
4666  O O   . ALA A 650  ? 0.3042 0.4788 0.2499 0.0650  0.0347  -0.0083 648  ALA A O   
4667  C CB  . ALA A 650  ? 0.3019 0.4962 0.2412 0.0624  0.0360  0.0041  648  ALA A CB  
4668  N N   . ARG A 651  ? 0.2737 0.4419 0.2157 0.0669  0.0314  -0.0170 649  ARG A N   
4669  C CA  . ARG A 651  ? 0.3054 0.4722 0.2488 0.0707  0.0300  -0.0270 649  ARG A CA  
4670  C C   . ARG A 651  ? 0.2614 0.4089 0.2084 0.0691  0.0280  -0.0296 649  ARG A C   
4671  O O   . ARG A 651  ? 0.2742 0.4182 0.2233 0.0720  0.0262  -0.0378 649  ARG A O   
4672  C CB  . ARG A 651  ? 0.2906 0.4649 0.2310 0.0745  0.0283  -0.0353 649  ARG A CB  
4673  C CG  . ARG A 651  ? 0.3491 0.5295 0.2908 0.0796  0.0273  -0.0456 649  ARG A CG  
4674  C CD  . ARG A 651  ? 0.3676 0.5639 0.3057 0.0838  0.0269  -0.0518 649  ARG A CD  
4675  N NE  . ARG A 651  ? 0.3885 0.5873 0.3287 0.0887  0.0249  -0.0635 649  ARG A NE  
4676  C CZ  . ARG A 651  ? 0.3982 0.6060 0.3403 0.0916  0.0257  -0.0666 649  ARG A CZ  
4677  N NH1 . ARG A 651  ? 0.4327 0.6479 0.3747 0.0902  0.0289  -0.0591 649  ARG A NH1 
4678  N NH2 . ARG A 651  ? 0.4318 0.6393 0.3774 0.0951  0.0226  -0.0766 649  ARG A NH2 
4679  N N   . MET A 652  ? 0.2778 0.4133 0.2260 0.0647  0.0281  -0.0228 650  MET A N   
4680  C CA  . MET A 652  ? 0.2735 0.3915 0.2248 0.0630  0.0262  -0.0249 650  MET A CA  
4681  C C   . MET A 652  ? 0.2809 0.3960 0.2357 0.0648  0.0257  -0.0294 650  MET A C   
4682  O O   . MET A 652  ? 0.2726 0.3788 0.2295 0.0661  0.0232  -0.0360 650  MET A O   
4683  C CB  . MET A 652  ? 0.2705 0.3785 0.2229 0.0581  0.0269  -0.0165 650  MET A CB  
4684  C CG  . MET A 652  ? 0.2734 0.3652 0.2290 0.0561  0.0253  -0.0178 650  MET A CG  
4685  S SD  . MET A 652  ? 0.3007 0.3816 0.2575 0.0508  0.0259  -0.0091 650  MET A SD  
4686  C CE  . MET A 652  ? 0.2668 0.3459 0.2206 0.0500  0.0247  -0.0091 650  MET A CE  
4687  N N   . PRO A 653  ? 0.2786 0.4010 0.2346 0.0651  0.0278  -0.0264 651  PRO A N   
4688  C CA  . PRO A 653  ? 0.2885 0.4074 0.2483 0.0670  0.0271  -0.0309 651  PRO A CA  
4689  C C   . PRO A 653  ? 0.2792 0.4015 0.2397 0.0718  0.0250  -0.0413 651  PRO A C   
4690  O O   . PRO A 653  ? 0.2788 0.3907 0.2429 0.0725  0.0226  -0.0462 651  PRO A O   
4691  C CB  . PRO A 653  ? 0.2618 0.3921 0.2220 0.0670  0.0299  -0.0258 651  PRO A CB  
4692  C CG  . PRO A 653  ? 0.3172 0.4488 0.2756 0.0631  0.0316  -0.0163 651  PRO A CG  
4693  C CD  . PRO A 653  ? 0.2909 0.4239 0.2458 0.0635  0.0306  -0.0181 651  PRO A CD  
4694  N N   . THR A 654  ? 0.2414 0.3782 0.1989 0.0750  0.0256  -0.0446 652  THR A N   
4695  C CA  . THR A 654  ? 0.2586 0.3995 0.2169 0.0798  0.0233  -0.0553 652  THR A CA  
4696  C C   . THR A 654  ? 0.2609 0.3892 0.2199 0.0793  0.0200  -0.0598 652  THR A C   
4697  O O   . THR A 654  ? 0.2835 0.4055 0.2464 0.0817  0.0172  -0.0674 652  THR A O   
4698  C CB  . THR A 654  ? 0.2832 0.4438 0.2376 0.0832  0.0248  -0.0574 652  THR A CB  
4699  O OG1 . THR A 654  ? 0.3201 0.4928 0.2743 0.0836  0.0279  -0.0529 652  THR A OG1 
4700  C CG2 . THR A 654  ? 0.3072 0.4729 0.2627 0.0886  0.0223  -0.0692 652  THR A CG2 
4701  N N   . LEU A 655  ? 0.2598 0.3845 0.2157 0.0763  0.0202  -0.0550 653  LEU A N   
4702  C CA  . LEU A 655  ? 0.2564 0.3688 0.2132 0.0753  0.0172  -0.0584 653  LEU A CA  
4703  C C   . LEU A 655  ? 0.3004 0.3962 0.2619 0.0730  0.0154  -0.0582 653  LEU A C   
4704  O O   . LEU A 655  ? 0.2777 0.3654 0.2424 0.0741  0.0122  -0.0643 653  LEU A O   
4705  C CB  . LEU A 655  ? 0.2676 0.3789 0.2207 0.0720  0.0180  -0.0522 653  LEU A CB  
4706  C CG  . LEU A 655  ? 0.2530 0.3807 0.2013 0.0739  0.0195  -0.0519 653  LEU A CG  
4707  C CD1 . LEU A 655  ? 0.2839 0.4094 0.2292 0.0706  0.0200  -0.0456 653  LEU A CD1 
4708  C CD2 . LEU A 655  ? 0.3251 0.4602 0.2733 0.0788  0.0173  -0.0623 653  LEU A CD2 
4709  N N   . LEU A 656  ? 0.2741 0.3652 0.2365 0.0699  0.0173  -0.0510 654  LEU A N   
4710  C CA  . LEU A 656  ? 0.2839 0.3609 0.2507 0.0678  0.0158  -0.0505 654  LEU A CA  
4711  C C   . LEU A 656  ? 0.2894 0.3655 0.2607 0.0715  0.0134  -0.0585 654  LEU A C   
4712  O O   . LEU A 656  ? 0.2790 0.3440 0.2541 0.0712  0.0104  -0.0619 654  LEU A O   
4713  C CB  . LEU A 656  ? 0.2818 0.3566 0.2490 0.0647  0.0182  -0.0426 654  LEU A CB  
4714  C CG  . LEU A 656  ? 0.2858 0.3604 0.2501 0.0608  0.0204  -0.0340 654  LEU A CG  
4715  C CD1 . LEU A 656  ? 0.2944 0.3647 0.2607 0.0580  0.0219  -0.0280 654  LEU A CD1 
4716  C CD2 . LEU A 656  ? 0.2636 0.3281 0.2271 0.0583  0.0188  -0.0335 654  LEU A CD2 
4717  N N   . GLY A 657  ? 0.2701 0.3582 0.2415 0.0750  0.0148  -0.0612 655  GLY A N   
4718  C CA  . GLY A 657  ? 0.3030 0.3910 0.2794 0.0788  0.0125  -0.0689 655  GLY A CA  
4719  C C   . GLY A 657  ? 0.2912 0.3765 0.2697 0.0816  0.0088  -0.0777 655  GLY A C   
4720  O O   . GLY A 657  ? 0.2969 0.3734 0.2810 0.0826  0.0056  -0.0824 655  GLY A O   
4721  N N   . LEU A 658  ? 0.2639 0.3568 0.2382 0.0828  0.0090  -0.0798 656  LEU A N   
4722  C CA  . LEU A 658  ? 0.2904 0.3811 0.2668 0.0854  0.0052  -0.0883 656  LEU A CA  
4723  C C   . LEU A 658  ? 0.2701 0.3441 0.2493 0.0818  0.0025  -0.0868 656  LEU A C   
4724  O O   . LEU A 658  ? 0.2727 0.3388 0.2576 0.0832  -0.0013 -0.0927 656  LEU A O   
4725  C CB  . LEU A 658  ? 0.2667 0.3698 0.2377 0.0870  0.0062  -0.0902 656  LEU A CB  
4726  C CG  . LEU A 658  ? 0.2914 0.3945 0.2643 0.0903  0.0023  -0.1000 656  LEU A CG  
4727  C CD1 . LEU A 658  ? 0.2857 0.3895 0.2649 0.0949  -0.0005 -0.1093 656  LEU A CD1 
4728  C CD2 . LEU A 658  ? 0.2685 0.3868 0.2356 0.0924  0.0037  -0.1017 656  LEU A CD2 
4729  N N   . ILE A 659  ? 0.2647 0.3335 0.2404 0.0772  0.0042  -0.0787 657  ILE A N   
4730  C CA  . ILE A 659  ? 0.2401 0.2944 0.2179 0.0737  0.0020  -0.0766 657  ILE A CA  
4731  C C   . ILE A 659  ? 0.2834 0.3266 0.2672 0.0725  0.0002  -0.0761 657  ILE A C   
4732  O O   . ILE A 659  ? 0.2633 0.2965 0.2517 0.0720  -0.0034 -0.0791 657  ILE A O   
4733  C CB  . ILE A 659  ? 0.2682 0.3203 0.2412 0.0693  0.0046  -0.0679 657  ILE A CB  
4734  C CG1 . ILE A 659  ? 0.2906 0.3526 0.2584 0.0704  0.0055  -0.0687 657  ILE A CG1 
4735  C CG2 . ILE A 659  ? 0.2848 0.3226 0.2601 0.0654  0.0027  -0.0651 657  ILE A CG2 
4736  C CD1 . ILE A 659  ? 0.2726 0.3353 0.2359 0.0668  0.0083  -0.0601 657  ILE A CD1 
4737  N N   . ILE A 660  ? 0.2797 0.3249 0.2637 0.0721  0.0026  -0.0722 658  ILE A N   
4738  C CA  . ILE A 660  ? 0.2703 0.3061 0.2598 0.0710  0.0010  -0.0714 658  ILE A CA  
4739  C C   . ILE A 660  ? 0.2721 0.3058 0.2680 0.0748  -0.0030 -0.0801 658  ILE A C   
4740  O O   . ILE A 660  ? 0.2801 0.3026 0.2813 0.0734  -0.0063 -0.0808 658  ILE A O   
4741  C CB  . ILE A 660  ? 0.2767 0.3174 0.2654 0.0707  0.0042  -0.0668 658  ILE A CB  
4742  C CG1 . ILE A 660  ? 0.2831 0.3212 0.2675 0.0660  0.0072  -0.0575 658  ILE A CG1 
4743  C CG2 . ILE A 660  ? 0.2749 0.3086 0.2698 0.0710  0.0023  -0.0680 658  ILE A CG2 
4744  C CD1 . ILE A 660  ? 0.3299 0.3747 0.3131 0.0657  0.0105  -0.0528 658  ILE A CD1 
4745  N N   . ARG A 661  ? 0.2816 0.3265 0.2775 0.0796  -0.0031 -0.0870 659  ARG A N   
4746  C CA  . ARG A 661  ? 0.2986 0.3423 0.3014 0.0837  -0.0070 -0.0959 659  ARG A CA  
4747  C C   . ARG A 661  ? 0.3335 0.3735 0.3386 0.0848  -0.0110 -0.1022 659  ARG A C   
4748  O O   . ARG A 661  ? 0.3126 0.3450 0.3252 0.0861  -0.0153 -0.1072 659  ARG A O   
4749  C CB  . ARG A 661  ? 0.3175 0.3756 0.3200 0.0888  -0.0056 -0.1013 659  ARG A CB  
4750  C CG  . ARG A 661  ? 0.2980 0.3574 0.3017 0.0883  -0.0033 -0.0970 659  ARG A CG  
4751  C CD  . ARG A 661  ? 0.3116 0.3866 0.3141 0.0930  -0.0012 -0.1013 659  ARG A CD  
4752  N NE  . ARG A 661  ? 0.3198 0.3982 0.3279 0.0985  -0.0048 -0.1123 659  ARG A NE  
4753  C CZ  . ARG A 661  ? 0.3026 0.3941 0.3087 0.1029  -0.0047 -0.1195 659  ARG A CZ  
4754  N NH1 . ARG A 661  ? 0.3242 0.4270 0.3226 0.1025  -0.0013 -0.1166 659  ARG A NH1 
4755  N NH2 . ARG A 661  ? 0.3223 0.4156 0.3345 0.1070  -0.0085 -0.1289 659  ARG A NH2 
4756  N N   . GLU A 662  ? 0.2666 0.3119 0.2660 0.0844  -0.0098 -0.1019 660  GLU A N   
4757  C CA  . GLU A 662  ? 0.2899 0.3323 0.2916 0.0856  -0.0136 -0.1083 660  GLU A CA  
4758  C C   . GLU A 662  ? 0.2731 0.3009 0.2774 0.0810  -0.0159 -0.1040 660  GLU A C   
4759  O O   . GLU A 662  ? 0.3230 0.3441 0.3332 0.0818  -0.0204 -0.1093 660  GLU A O   
4760  C CB  . GLU A 662  ? 0.3041 0.3582 0.2989 0.0870  -0.0117 -0.1099 660  GLU A CB  
4761  C CG  . GLU A 662  ? 0.3100 0.3625 0.3072 0.0888  -0.0158 -0.1174 660  GLU A CG  
4762  C CD  . GLU A 662  ? 0.2995 0.3648 0.2899 0.0906  -0.0141 -0.1195 660  GLU A CD  
4763  O OE1 . GLU A 662  ? 0.2749 0.3465 0.2584 0.0885  -0.0099 -0.1124 660  GLU A OE1 
4764  O OE2 . GLU A 662  ? 0.2866 0.3558 0.2791 0.0940  -0.0173 -0.1283 660  GLU A OE2 
4765  N N   . ALA A 663  ? 0.2584 0.2813 0.2588 0.0762  -0.0131 -0.0946 661  ALA A N   
4766  C CA  . ALA A 663  ? 0.2554 0.2674 0.2565 0.0719  -0.0145 -0.0903 661  ALA A CA  
4767  C C   . ALA A 663  ? 0.2922 0.2936 0.2964 0.0680  -0.0146 -0.0837 661  ALA A C   
4768  O O   . ALA A 663  ? 0.3237 0.3171 0.3276 0.0639  -0.0150 -0.0789 661  ALA A O   
4769  C CB  . ALA A 663  ? 0.3000 0.3162 0.2934 0.0696  -0.0114 -0.0855 661  ALA A CB  
4770  N N   . GLY A 664  ? 0.3258 0.3274 0.3327 0.0690  -0.0141 -0.0833 662  GLY A N   
4771  C CA  . GLY A 664  ? 0.2910 0.2829 0.3012 0.0654  -0.0145 -0.0774 662  GLY A CA  
4772  C C   . GLY A 664  ? 0.3022 0.2930 0.3067 0.0612  -0.0106 -0.0685 662  GLY A C   
4773  O O   . GLY A 664  ? 0.3411 0.3233 0.3474 0.0575  -0.0112 -0.0634 662  GLY A O   
4774  N N   . LYS A 665  ? 0.2807 0.2804 0.2787 0.0617  -0.0068 -0.0665 663  LYS A N   
4775  C CA  . LYS A 665  ? 0.2656 0.2645 0.2587 0.0578  -0.0033 -0.0585 663  LYS A CA  
4776  C C   . LYS A 665  ? 0.2522 0.2535 0.2451 0.0576  -0.0009 -0.0548 663  LYS A C   
4777  O O   . LYS A 665  ? 0.2334 0.2420 0.2271 0.0610  -0.0002 -0.0582 663  LYS A O   
4778  C CB  . LYS A 665  ? 0.2846 0.2914 0.2713 0.0581  -0.0008 -0.0576 663  LYS A CB  
4779  C CG  . LYS A 665  ? 0.2869 0.2928 0.2733 0.0587  -0.0031 -0.0616 663  LYS A CG  
4780  C CD  . LYS A 665  ? 0.3418 0.3369 0.3298 0.0547  -0.0048 -0.0583 663  LYS A CD  
4781  C CE  . LYS A 665  ? 0.3203 0.3155 0.3075 0.0551  -0.0067 -0.0616 663  LYS A CE  
4782  N NZ  . LYS A 665  ? 0.3159 0.3005 0.3066 0.0519  -0.0094 -0.0599 663  LYS A NZ  
4783  N N   . SER A 666  ? 0.2609 0.2566 0.2529 0.0536  0.0005  -0.0481 664  SER A N   
4784  C CA  . SER A 666  ? 0.2961 0.2947 0.2869 0.0528  0.0034  -0.0436 664  SER A CA  
4785  C C   . SER A 666  ? 0.3082 0.3165 0.2936 0.0533  0.0069  -0.0413 664  SER A C   
4786  O O   . SER A 666  ? 0.2779 0.2897 0.2599 0.0536  0.0072  -0.0421 664  SER A O   
4787  C CB  . SER A 666  ? 0.3001 0.2905 0.2914 0.0484  0.0037  -0.0374 664  SER A CB  
4788  O OG  . SER A 666  ? 0.3085 0.2976 0.2958 0.0456  0.0050  -0.0337 664  SER A OG  
4789  N N   . ALA A 667  ? 0.3041 0.3172 0.2889 0.0532  0.0093  -0.0381 665  ALA A N   
4790  C CA  . ALA A 667  ? 0.2648 0.2871 0.2451 0.0532  0.0126  -0.0347 665  ALA A CA  
4791  C C   . ALA A 667  ? 0.2872 0.3061 0.2644 0.0497  0.0136  -0.0296 665  ALA A C   
4792  O O   . ALA A 667  ? 0.2643 0.2893 0.2379 0.0501  0.0148  -0.0289 665  ALA A O   
4793  C CB  . ALA A 667  ? 0.2847 0.3114 0.2659 0.0531  0.0147  -0.0313 665  ALA A CB  
4794  N N   . LEU A 668  ? 0.2772 0.2867 0.2556 0.0462  0.0131  -0.0259 666  LEU A N   
4795  C CA  . LEU A 668  ? 0.2827 0.2885 0.2585 0.0430  0.0139  -0.0216 666  LEU A CA  
4796  C C   . LEU A 668  ? 0.3163 0.3216 0.2905 0.0437  0.0124  -0.0247 666  LEU A C   
4797  O O   . LEU A 668  ? 0.3117 0.3205 0.2827 0.0430  0.0137  -0.0225 666  LEU A O   
4798  C CB  . LEU A 668  ? 0.3113 0.3076 0.2891 0.0396  0.0132  -0.0184 666  LEU A CB  
4799  C CG  . LEU A 668  ? 0.4061 0.4028 0.3846 0.0379  0.0150  -0.0138 666  LEU A CG  
4800  C CD1 . LEU A 668  ? 0.3375 0.3254 0.3180 0.0349  0.0138  -0.0117 666  LEU A CD1 
4801  C CD2 . LEU A 668  ? 0.3950 0.3965 0.3707 0.0366  0.0174  -0.0093 666  LEU A CD2 
4802  N N   . ASN A 669  ? 0.2836 0.2843 0.2605 0.0449  0.0096  -0.0296 667  ASN A N   
4803  C CA  . ASN A 669  ? 0.2988 0.2990 0.2746 0.0456  0.0079  -0.0329 667  ASN A CA  
4804  C C   . ASN A 669  ? 0.2959 0.3068 0.2686 0.0485  0.0090  -0.0354 667  ASN A C   
4805  O O   . ASN A 669  ? 0.2844 0.2973 0.2542 0.0481  0.0092  -0.0350 667  ASN A O   
4806  C CB  . ASN A 669  ? 0.3020 0.2968 0.2822 0.0469  0.0043  -0.0384 667  ASN A CB  
4807  C CG  . ASN A 669  ? 0.3634 0.3484 0.3474 0.0441  0.0028  -0.0360 667  ASN A CG  
4808  O OD1 . ASN A 669  ? 0.4237 0.4049 0.4123 0.0452  0.0001  -0.0393 667  ASN A OD1 
4809  N ND2 . ASN A 669  ? 0.3499 0.3312 0.3321 0.0405  0.0042  -0.0303 667  ASN A ND2 
4810  N N   . ALA A 670  ? 0.2652 0.2834 0.2384 0.0516  0.0097  -0.0381 668  ALA A N   
4811  C CA  . ALA A 670  ? 0.2537 0.2836 0.2241 0.0548  0.0107  -0.0410 668  ALA A CA  
4812  C C   . ALA A 670  ? 0.2499 0.2861 0.2160 0.0531  0.0137  -0.0347 668  ALA A C   
4813  O O   . ALA A 670  ? 0.2653 0.3087 0.2283 0.0542  0.0142  -0.0354 668  ALA A O   
4814  C CB  . ALA A 670  ? 0.2680 0.3050 0.2402 0.0585  0.0107  -0.0453 668  ALA A CB  
4815  N N   . ILE A 671  ? 0.2619 0.2960 0.2284 0.0505  0.0156  -0.0286 669  ILE A N   
4816  C CA  . ILE A 671  ? 0.2441 0.2831 0.2077 0.0486  0.0181  -0.0223 669  ILE A CA  
4817  C C   . ILE A 671  ? 0.2583 0.2927 0.2201 0.0466  0.0173  -0.0207 669  ILE A C   
4818  O O   . ILE A 671  ? 0.2819 0.3230 0.2409 0.0468  0.0183  -0.0189 669  ILE A O   
4819  C CB  . ILE A 671  ? 0.2581 0.2939 0.2233 0.0459  0.0197  -0.0164 669  ILE A CB  
4820  C CG1 . ILE A 671  ? 0.2626 0.3054 0.2293 0.0480  0.0208  -0.0171 669  ILE A CG1 
4821  C CG2 . ILE A 671  ? 0.2832 0.3213 0.2466 0.0434  0.0215  -0.0097 669  ILE A CG2 
4822  C CD1 . ILE A 671  ? 0.2691 0.3074 0.2382 0.0455  0.0218  -0.0124 669  ILE A CD1 
4823  N N   . ALA A 672  ? 0.2643 0.2877 0.2279 0.0445  0.0156  -0.0212 670  ALA A N   
4824  C CA  . ALA A 672  ? 0.2787 0.2975 0.2410 0.0426  0.0148  -0.0201 670  ALA A CA  
4825  C C   . ALA A 672  ? 0.2530 0.2767 0.2134 0.0451  0.0135  -0.0248 670  ALA A C   
4826  O O   . ALA A 672  ? 0.2800 0.3060 0.2380 0.0444  0.0139  -0.0230 670  ALA A O   
4827  C CB  . ALA A 672  ? 0.3163 0.3236 0.2812 0.0402  0.0131  -0.0203 670  ALA A CB  
4828  N N   . GLU A 673  ? 0.2670 0.2924 0.2288 0.0480  0.0119  -0.0312 671  GLU A N   
4829  C CA  . GLU A 673  ? 0.2492 0.2798 0.2097 0.0507  0.0103  -0.0367 671  GLU A CA  
4830  C C   . GLU A 673  ? 0.2666 0.3099 0.2232 0.0523  0.0124  -0.0352 671  GLU A C   
4831  O O   . GLU A 673  ? 0.2541 0.3005 0.2081 0.0525  0.0120  -0.0355 671  GLU A O   
4832  C CB  . GLU A 673  ? 0.2790 0.3096 0.2427 0.0539  0.0081  -0.0440 671  GLU A CB  
4833  C CG  . GLU A 673  ? 0.3111 0.3468 0.2742 0.0571  0.0060  -0.0509 671  GLU A CG  
4834  C CD  . GLU A 673  ? 0.3107 0.3373 0.2758 0.0556  0.0031  -0.0531 671  GLU A CD  
4835  O OE1 . GLU A 673  ? 0.3190 0.3352 0.2865 0.0525  0.0024  -0.0499 671  GLU A OE1 
4836  O OE2 . GLU A 673  ? 0.2902 0.3206 0.2544 0.0575  0.0014  -0.0578 671  GLU A OE2 
4837  N N   . VAL A 674  ? 0.2476 0.2986 0.2036 0.0534  0.0145  -0.0331 672  VAL A N   
4838  C CA  . VAL A 674  ? 0.2370 0.3015 0.1895 0.0549  0.0164  -0.0312 672  VAL A CA  
4839  C C   . VAL A 674  ? 0.2522 0.3162 0.2028 0.0517  0.0180  -0.0234 672  VAL A C   
4840  O O   . VAL A 674  ? 0.2342 0.3060 0.1819 0.0522  0.0185  -0.0220 672  VAL A O   
4841  C CB  . VAL A 674  ? 0.2490 0.3227 0.2019 0.0569  0.0183  -0.0309 672  VAL A CB  
4842  C CG1 . VAL A 674  ? 0.2477 0.3367 0.1970 0.0583  0.0203  -0.0283 672  VAL A CG1 
4843  C CG2 . VAL A 674  ? 0.2356 0.3098 0.1909 0.0605  0.0165  -0.0392 672  VAL A CG2 
4844  N N   . ARG A 675  ? 0.2541 0.3095 0.2068 0.0484  0.0187  -0.0183 673  ARG A N   
4845  C CA  . ARG A 675  ? 0.2201 0.2738 0.1720 0.0454  0.0197  -0.0115 673  ARG A CA  
4846  C C   . ARG A 675  ? 0.2295 0.2800 0.1799 0.0449  0.0181  -0.0131 673  ARG A C   
4847  O O   . ARG A 675  ? 0.2393 0.2946 0.1880 0.0442  0.0187  -0.0093 673  ARG A O   
4848  C CB  . ARG A 675  ? 0.2347 0.2784 0.1895 0.0422  0.0200  -0.0074 673  ARG A CB  
4849  C CG  . ARG A 675  ? 0.2348 0.2821 0.1911 0.0418  0.0219  -0.0038 673  ARG A CG  
4850  C CD  . ARG A 675  ? 0.2599 0.2979 0.2189 0.0384  0.0221  0.0007  673  ARG A CD  
4851  N NE  . ARG A 675  ? 0.2559 0.2936 0.2147 0.0362  0.0226  0.0061  673  ARG A NE  
4852  C CZ  . ARG A 675  ? 0.2570 0.2865 0.2179 0.0333  0.0224  0.0093  673  ARG A CZ  
4853  N NH1 . ARG A 675  ? 0.2591 0.2802 0.2219 0.0321  0.0218  0.0080  673  ARG A NH1 
4854  N NH2 . ARG A 675  ? 0.2467 0.2767 0.2079 0.0317  0.0226  0.0138  673  ARG A NH2 
4855  N N   . GLU A 676  ? 0.2219 0.2646 0.1735 0.0453  0.0159  -0.0184 674  GLU A N   
4856  C CA  . GLU A 676  ? 0.2422 0.2815 0.1928 0.0447  0.0143  -0.0199 674  GLU A CA  
4857  C C   . GLU A 676  ? 0.2350 0.2851 0.1825 0.0473  0.0140  -0.0227 674  GLU A C   
4858  O O   . GLU A 676  ? 0.2252 0.2771 0.1709 0.0465  0.0138  -0.0206 674  GLU A O   
4859  C CB  . GLU A 676  ? 0.2344 0.2638 0.1875 0.0443  0.0118  -0.0248 674  GLU A CB  
4860  C CG  . GLU A 676  ? 0.2745 0.2999 0.2269 0.0432  0.0102  -0.0255 674  GLU A CG  
4861  C CD  . GLU A 676  ? 0.3893 0.4031 0.3446 0.0408  0.0087  -0.0258 674  GLU A CD  
4862  O OE1 . GLU A 676  ? 0.4880 0.4970 0.4460 0.0410  0.0077  -0.0284 674  GLU A OE1 
4863  O OE2 . GLU A 676  ? 0.3828 0.3927 0.3378 0.0386  0.0085  -0.0231 674  GLU A OE2 
4864  N N   . ALA A 677  ? 0.2474 0.3053 0.1943 0.0507  0.0138  -0.0277 675  ALA A N   
4865  C CA  . ALA A 677  ? 0.2372 0.3071 0.1809 0.0535  0.0136  -0.0305 675  ALA A CA  
4866  C C   . ALA A 677  ? 0.2300 0.3094 0.1711 0.0526  0.0160  -0.0234 675  ALA A C   
4867  O O   . ALA A 677  ? 0.2173 0.3024 0.1559 0.0528  0.0157  -0.0225 675  ALA A O   
4868  C CB  . ALA A 677  ? 0.2379 0.3153 0.1819 0.0575  0.0131  -0.0374 675  ALA A CB  
4869  N N   . ILE A 678  ? 0.2093 0.2903 0.1514 0.0513  0.0181  -0.0179 676  ILE A N   
4870  C CA  . ILE A 678  ? 0.2092 0.2987 0.1500 0.0500  0.0201  -0.0102 676  ILE A CA  
4871  C C   . ILE A 678  ? 0.2293 0.3124 0.1703 0.0471  0.0196  -0.0054 676  ILE A C   
4872  O O   . ILE A 678  ? 0.2300 0.3208 0.1691 0.0469  0.0200  -0.0016 676  ILE A O   
4873  C CB  . ILE A 678  ? 0.2283 0.3185 0.1712 0.0488  0.0221  -0.0052 676  ILE A CB  
4874  C CG1 . ILE A 678  ? 0.2630 0.3627 0.2054 0.0522  0.0228  -0.0096 676  ILE A CG1 
4875  C CG2 . ILE A 678  ? 0.2486 0.3446 0.1917 0.0466  0.0238  0.0039  676  ILE A CG2 
4876  C CD1 . ILE A 678  ? 0.2398 0.3376 0.1850 0.0512  0.0243  -0.0066 676  ILE A CD1 
4877  N N   . ASP A 679  ? 0.2124 0.2819 0.1559 0.0448  0.0187  -0.0055 677  ASP A N   
4878  C CA  . ASP A 679  ? 0.2071 0.2699 0.1513 0.0421  0.0182  -0.0015 677  ASP A CA  
4879  C C   . ASP A 679  ? 0.2250 0.2894 0.1671 0.0431  0.0165  -0.0049 677  ASP A C   
4880  O O   . ASP A 679  ? 0.2426 0.3090 0.1840 0.0420  0.0165  -0.0007 677  ASP A O   
4881  C CB  . ASP A 679  ? 0.2201 0.2692 0.1674 0.0397  0.0176  -0.0015 677  ASP A CB  
4882  C CG  . ASP A 679  ? 0.2450 0.2924 0.1948 0.0382  0.0192  0.0028  677  ASP A CG  
4883  O OD1 . ASP A 679  ? 0.2763 0.3311 0.2261 0.0380  0.0207  0.0080  677  ASP A OD1 
4884  O OD2 . ASP A 679  ? 0.2659 0.3043 0.2178 0.0371  0.0188  0.0013  677  ASP A OD2 
4885  N N   . PHE A 680  ? 0.2143 0.2776 0.1556 0.0453  0.0149  -0.0125 678  PHE A N   
4886  C CA  . PHE A 680  ? 0.2264 0.2926 0.1656 0.0465  0.0131  -0.0162 678  PHE A CA  
4887  C C   . PHE A 680  ? 0.2310 0.3114 0.1670 0.0480  0.0141  -0.0137 678  PHE A C   
4888  O O   . PHE A 680  ? 0.2175 0.2999 0.1523 0.0472  0.0136  -0.0111 678  PHE A O   
4889  C CB  . PHE A 680  ? 0.2135 0.2782 0.1531 0.0490  0.0110  -0.0251 678  PHE A CB  
4890  C CG  . PHE A 680  ? 0.2125 0.2637 0.1552 0.0474  0.0092  -0.0277 678  PHE A CG  
4891  C CD1 . PHE A 680  ? 0.2457 0.2900 0.1890 0.0448  0.0084  -0.0252 678  PHE A CD1 
4892  C CD2 . PHE A 680  ? 0.2320 0.2780 0.1773 0.0483  0.0081  -0.0324 678  PHE A CD2 
4893  C CE1 . PHE A 680  ? 0.2576 0.2906 0.2037 0.0432  0.0068  -0.0272 678  PHE A CE1 
4894  C CE2 . PHE A 680  ? 0.2426 0.2769 0.1909 0.0465  0.0063  -0.0342 678  PHE A CE2 
4895  C CZ  . PHE A 680  ? 0.2532 0.2813 0.2019 0.0439  0.0057  -0.0315 678  PHE A CZ  
4896  N N   . LEU A 681  ? 0.2207 0.3117 0.1553 0.0503  0.0153  -0.0145 679  LEU A N   
4897  C CA  . LEU A 681  ? 0.2111 0.3174 0.1425 0.0519  0.0163  -0.0121 679  LEU A CA  
4898  C C   . LEU A 681  ? 0.2397 0.3472 0.1716 0.0490  0.0174  -0.0025 679  LEU A C   
4899  O O   . LEU A 681  ? 0.2163 0.3303 0.1462 0.0491  0.0170  -0.0003 679  LEU A O   
4900  C CB  . LEU A 681  ? 0.2193 0.3365 0.1499 0.0543  0.0178  -0.0133 679  LEU A CB  
4901  C CG  . LEU A 681  ? 0.2455 0.3648 0.1755 0.0579  0.0165  -0.0233 679  LEU A CG  
4902  C CD1 . LEU A 681  ? 0.2299 0.3563 0.1604 0.0598  0.0182  -0.0241 679  LEU A CD1 
4903  C CD2 . LEU A 681  ? 0.2338 0.3639 0.1604 0.0607  0.0151  -0.0282 679  LEU A CD2 
4904  N N   . ARG A 682  ? 0.2218 0.3229 0.1567 0.0465  0.0187  0.0031  680  ARG A N   
4905  C CA  . ARG A 682  ? 0.2098 0.3124 0.1463 0.0439  0.0195  0.0122  680  ARG A CA  
4906  C C   . ARG A 682  ? 0.2385 0.3316 0.1762 0.0418  0.0180  0.0135  680  ARG A C   
4907  O O   . ARG A 682  ? 0.2273 0.3245 0.1653 0.0407  0.0180  0.0192  680  ARG A O   
4908  C CB  . ARG A 682  ? 0.2151 0.3139 0.1550 0.0419  0.0210  0.0174  680  ARG A CB  
4909  C CG  . ARG A 682  ? 0.2313 0.3422 0.1702 0.0436  0.0227  0.0182  680  ARG A CG  
4910  C CD  . ARG A 682  ? 0.2331 0.3393 0.1757 0.0416  0.0240  0.0225  680  ARG A CD  
4911  N NE  . ARG A 682  ? 0.2494 0.3679 0.1913 0.0431  0.0257  0.0241  680  ARG A NE  
4912  C CZ  . ARG A 682  ? 0.2563 0.3728 0.2009 0.0423  0.0269  0.0261  680  ARG A CZ  
4913  N NH1 . ARG A 682  ? 0.2518 0.3548 0.1998 0.0400  0.0265  0.0267  680  ARG A NH1 
4914  N NH2 . ARG A 682  ? 0.2642 0.3932 0.2081 0.0437  0.0285  0.0275  680  ARG A NH2 
4915  N N   . TYR A 683  ? 0.2225 0.3037 0.1612 0.0414  0.0168  0.0083  681  TYR A N   
4916  C CA  . TYR A 683  ? 0.2076 0.2802 0.1477 0.0395  0.0155  0.0092  681  TYR A CA  
4917  C C   . TYR A 683  ? 0.2325 0.3114 0.1696 0.0410  0.0141  0.0069  681  TYR A C   
4918  O O   . TYR A 683  ? 0.2282 0.3079 0.1658 0.0398  0.0137  0.0112  681  TYR A O   
4919  C CB  . TYR A 683  ? 0.2150 0.2744 0.1569 0.0386  0.0145  0.0046  681  TYR A CB  
4920  C CG  . TYR A 683  ? 0.2311 0.2824 0.1744 0.0369  0.0132  0.0047  681  TYR A CG  
4921  C CD1 . TYR A 683  ? 0.2267 0.2726 0.1729 0.0344  0.0136  0.0103  681  TYR A CD1 
4922  C CD2 . TYR A 683  ? 0.2037 0.2530 0.1456 0.0379  0.0113  -0.0010 681  TYR A CD2 
4923  C CE1 . TYR A 683  ? 0.2213 0.2603 0.1688 0.0330  0.0124  0.0101  681  TYR A CE1 
4924  C CE2 . TYR A 683  ? 0.2272 0.2697 0.1704 0.0363  0.0102  -0.0008 681  TYR A CE2 
4925  C CZ  . TYR A 683  ? 0.2355 0.2732 0.1814 0.0339  0.0108  0.0048  681  TYR A CZ  
4926  O OH  . TYR A 683  ? 0.2406 0.2721 0.1879 0.0325  0.0097  0.0047  681  TYR A OH  
4927  N N   . TYR A 684  ? 0.2012 0.2848 0.1356 0.0437  0.0133  -0.0002 682  TYR A N   
4928  C CA  . TYR A 684  ? 0.2038 0.2937 0.1354 0.0452  0.0118  -0.0030 682  TYR A CA  
4929  C C   . TYR A 684  ? 0.2522 0.3562 0.1816 0.0458  0.0128  0.0026  682  TYR A C   
4930  O O   . TYR A 684  ? 0.2317 0.3399 0.1597 0.0458  0.0117  0.0038  682  TYR A O   
4931  C CB  . TYR A 684  ? 0.2169 0.3090 0.1468 0.0481  0.0103  -0.0123 682  TYR A CB  
4932  C CG  . TYR A 684  ? 0.2043 0.2827 0.1369 0.0473  0.0088  -0.0175 682  TYR A CG  
4933  C CD1 . TYR A 684  ? 0.2182 0.2860 0.1529 0.0447  0.0079  -0.0156 682  TYR A CD1 
4934  C CD2 . TYR A 684  ? 0.2366 0.3132 0.1699 0.0492  0.0081  -0.0241 682  TYR A CD2 
4935  C CE1 . TYR A 684  ? 0.2336 0.2899 0.1709 0.0438  0.0066  -0.0196 682  TYR A CE1 
4936  C CE2 . TYR A 684  ? 0.1999 0.2643 0.1362 0.0482  0.0065  -0.0280 682  TYR A CE2 
4937  C CZ  . TYR A 684  ? 0.2432 0.2979 0.1814 0.0454  0.0058  -0.0255 682  TYR A CZ  
4938  O OH  . TYR A 684  ? 0.2343 0.2780 0.1756 0.0443  0.0042  -0.0288 682  TYR A OH  
4939  N N   . ALA A 685  ? 0.2150 0.3269 0.1442 0.0462  0.0147  0.0062  683  ALA A N   
4940  C CA  . ALA A 685  ? 0.2279 0.3535 0.1556 0.0463  0.0156  0.0130  683  ALA A CA  
4941  C C   . ALA A 685  ? 0.2517 0.3728 0.1826 0.0432  0.0155  0.0214  683  ALA A C   
4942  O O   . ALA A 685  ? 0.2335 0.3618 0.1632 0.0431  0.0148  0.0250  683  ALA A O   
4943  C CB  . ALA A 685  ? 0.2493 0.3839 0.1770 0.0470  0.0177  0.0157  683  ALA A CB  
4944  N N   . GLU A 686  ? 0.2387 0.3480 0.1736 0.0408  0.0159  0.0244  684  GLU A N   
4945  C CA  . GLU A 686  ? 0.2484 0.3528 0.1871 0.0380  0.0155  0.0317  684  GLU A CA  
4946  C C   . GLU A 686  ? 0.2454 0.3441 0.1838 0.0378  0.0136  0.0292  684  GLU A C   
4947  O O   . GLU A 686  ? 0.2379 0.3401 0.1773 0.0369  0.0129  0.0344  684  GLU A O   
4948  C CB  . GLU A 686  ? 0.2424 0.3355 0.1858 0.0357  0.0161  0.0343  684  GLU A CB  
4949  C CG  . GLU A 686  ? 0.2697 0.3560 0.2177 0.0331  0.0153  0.0405  684  GLU A CG  
4950  C CD  . GLU A 686  ? 0.3035 0.3997 0.2535 0.0322  0.0153  0.0495  684  GLU A CD  
4951  O OE1 . GLU A 686  ? 0.3094 0.4180 0.2575 0.0332  0.0164  0.0522  684  GLU A OE1 
4952  O OE2 . GLU A 686  ? 0.3101 0.4019 0.2641 0.0305  0.0142  0.0542  684  GLU A OE2 
4953  N N   . GLN A 687  ? 0.2227 0.3132 0.1601 0.0385  0.0127  0.0214  685  GLN A N   
4954  C CA  . GLN A 687  ? 0.2183 0.3036 0.1556 0.0382  0.0109  0.0189  685  GLN A CA  
4955  C C   . GLN A 687  ? 0.2358 0.3330 0.1696 0.0399  0.0100  0.0187  685  GLN A C   
4956  O O   . GLN A 687  ? 0.2343 0.3310 0.1687 0.0391  0.0088  0.0210  685  GLN A O   
4957  C CB  . GLN A 687  ? 0.2081 0.2839 0.1451 0.0386  0.0099  0.0108  685  GLN A CB  
4958  C CG  . GLN A 687  ? 0.2132 0.2762 0.1538 0.0366  0.0104  0.0111  685  GLN A CG  
4959  C CD  . GLN A 687  ? 0.2537 0.3104 0.1979 0.0342  0.0102  0.0165  685  GLN A CD  
4960  O OE1 . GLN A 687  ? 0.2486 0.3034 0.1931 0.0338  0.0088  0.0159  685  GLN A OE1 
4961  N NE2 . GLN A 687  ? 0.2814 0.3350 0.2289 0.0326  0.0113  0.0214  685  GLN A NE2 
4962  N N   . THR A 688  ? 0.2103 0.3187 0.1404 0.0423  0.0105  0.0158  686  THR A N   
4963  C CA  . THR A 688  ? 0.2122 0.3340 0.1387 0.0441  0.0098  0.0159  686  THR A CA  
4964  C C   . THR A 688  ? 0.2217 0.3507 0.1496 0.0425  0.0103  0.0259  686  THR A C   
4965  O O   . THR A 688  ? 0.2556 0.3883 0.1830 0.0424  0.0090  0.0280  686  THR A O   
4966  C CB  . THR A 688  ? 0.2459 0.3797 0.1685 0.0471  0.0105  0.0112  686  THR A CB  
4967  O OG1 . THR A 688  ? 0.2537 0.3811 0.1756 0.0487  0.0093  0.0015  686  THR A OG1 
4968  C CG2 . THR A 688  ? 0.2237 0.3736 0.1425 0.0489  0.0099  0.0122  686  THR A CG2 
4969  N N   . ARG A 689  ? 0.2317 0.3629 0.1619 0.0413  0.0119  0.0323  687  ARG A N   
4970  C CA  . ARG A 689  ? 0.2675 0.4052 0.2002 0.0397  0.0121  0.0424  687  ARG A CA  
4971  C C   . ARG A 689  ? 0.2384 0.3655 0.1754 0.0374  0.0107  0.0461  687  ARG A C   
4972  O O   . ARG A 689  ? 0.2619 0.3947 0.2007 0.0364  0.0100  0.0532  687  ARG A O   
4973  C CB  . ARG A 689  ? 0.2690 0.4091 0.2044 0.0385  0.0139  0.0484  687  ARG A CB  
4974  C CG  . ARG A 689  ? 0.2446 0.3998 0.1761 0.0407  0.0154  0.0475  687  ARG A CG  
4975  C CD  . ARG A 689  ? 0.2746 0.4323 0.2094 0.0391  0.0171  0.0545  687  ARG A CD  
4976  N NE  . ARG A 689  ? 0.2795 0.4228 0.2176 0.0379  0.0176  0.0521  687  ARG A NE  
4977  C CZ  . ARG A 689  ? 0.2833 0.4259 0.2201 0.0392  0.0189  0.0472  687  ARG A CZ  
4978  N NH1 . ARG A 689  ? 0.3189 0.4743 0.2513 0.0419  0.0198  0.0435  687  ARG A NH1 
4979  N NH2 . ARG A 689  ? 0.2710 0.4004 0.2111 0.0378  0.0192  0.0458  687  ARG A NH2 
4980  N N   . ARG A 690  ? 0.2467 0.3592 0.1857 0.0366  0.0103  0.0414  688  ARG A N   
4981  C CA  . ARG A 690  ? 0.2488 0.3518 0.1918 0.0347  0.0089  0.0440  688  ARG A CA  
4982  C C   . ARG A 690  ? 0.2637 0.3678 0.2044 0.0356  0.0072  0.0404  688  ARG A C   
4983  O O   . ARG A 690  ? 0.2478 0.3475 0.1918 0.0343  0.0060  0.0438  688  ARG A O   
4984  C CB  . ARG A 690  ? 0.2505 0.3385 0.1967 0.0334  0.0092  0.0407  688  ARG A CB  
4985  C CG  . ARG A 690  ? 0.2923 0.3774 0.2420 0.0320  0.0106  0.0448  688  ARG A CG  
4986  C CD  . ARG A 690  ? 0.2938 0.3781 0.2493 0.0299  0.0101  0.0537  688  ARG A CD  
4987  N NE  . ARG A 690  ? 0.3398 0.4136 0.2989 0.0288  0.0087  0.0531  688  ARG A NE  
4988  C CZ  . ARG A 690  ? 0.3418 0.4175 0.3029 0.0284  0.0072  0.0567  688  ARG A CZ  
4989  N NH1 . ARG A 690  ? 0.3520 0.4395 0.3118 0.0290  0.0068  0.0616  688  ARG A NH1 
4990  N NH2 . ARG A 690  ? 0.3217 0.3878 0.2862 0.0275  0.0060  0.0553  688  ARG A NH2 
4991  N N   . THR A 691  ? 0.2339 0.3434 0.1696 0.0379  0.0068  0.0334  689  THR A N   
4992  C CA  . THR A 691  ? 0.2209 0.3283 0.1552 0.0384  0.0049  0.0290  689  THR A CA  
4993  C C   . THR A 691  ? 0.2664 0.3872 0.1960 0.0406  0.0040  0.0269  689  THR A C   
4994  O O   . THR A 691  ? 0.2869 0.4098 0.2166 0.0404  0.0025  0.0284  689  THR A O   
4995  C CB  . THR A 691  ? 0.2269 0.3232 0.1610 0.0387  0.0044  0.0206  689  THR A CB  
4996  O OG1 . THR A 691  ? 0.2528 0.3525 0.1841 0.0404  0.0053  0.0153  689  THR A OG1 
4997  C CG2 . THR A 691  ? 0.2519 0.3344 0.1908 0.0363  0.0049  0.0223  689  THR A CG2 
4998  N N   . LEU A 692  ? 0.2409 0.3709 0.1665 0.0428  0.0047  0.0229  690  LEU A N   
4999  C CA  . LEU A 692  ? 0.2620 0.4021 0.1830 0.0453  0.0034  0.0173  690  LEU A CA  
5000  C C   . LEU A 692  ? 0.2649 0.4201 0.1839 0.0458  0.0032  0.0236  690  LEU A C   
5001  O O   . LEU A 692  ? 0.2905 0.4548 0.2094 0.0455  0.0047  0.0301  690  LEU A O   
5002  C CB  . LEU A 692  ? 0.2628 0.4074 0.1807 0.0479  0.0040  0.0097  690  LEU A CB  
5003  C CG  . LEU A 692  ? 0.2617 0.3922 0.1813 0.0478  0.0036  0.0023  690  LEU A CG  
5004  C CD1 . LEU A 692  ? 0.2879 0.4241 0.2048 0.0507  0.0035  -0.0059 690  LEU A CD1 
5005  C CD2 . LEU A 692  ? 0.2769 0.3977 0.1980 0.0469  0.0014  -0.0014 690  LEU A CD2 
5006  N N   . GLY A 693  ? 0.2771 0.4353 0.1947 0.0463  0.0013  0.0218  691  GLY A N   
5007  C CA  . GLY A 693  ? 0.2979 0.4706 0.2133 0.0468  0.0007  0.0272  691  GLY A CA  
5008  C C   . GLY A 693  ? 0.3217 0.5037 0.2323 0.0495  -0.0010 0.0195  691  GLY A C   
5009  O O   . GLY A 693  ? 0.3373 0.5144 0.2465 0.0511  -0.0017 0.0100  691  GLY A O   
5010  N N   . PRO A 694  ? 0.3177 0.5132 0.2260 0.0500  -0.0018 0.0238  692  PRO A N   
5011  C CA  . PRO A 694  ? 0.3873 0.5941 0.2906 0.0529  -0.0035 0.0165  692  PRO A CA  
5012  C C   . PRO A 694  ? 0.3868 0.5831 0.2907 0.0532  -0.0058 0.0080  692  PRO A C   
5013  O O   . PRO A 694  ? 0.3898 0.5909 0.2905 0.0558  -0.0071 -0.0013 692  PRO A O   
5014  C CB  . PRO A 694  ? 0.3723 0.5934 0.2744 0.0525  -0.0040 0.0249  692  PRO A CB  
5015  C CG  . PRO A 694  ? 0.3429 0.5650 0.2483 0.0503  -0.0021 0.0360  692  PRO A CG  
5016  C CD  . PRO A 694  ? 0.3420 0.5448 0.2524 0.0483  -0.0013 0.0356  692  PRO A CD  
5017  N N   . GLY A 695  ? 0.2896 0.4721 0.1978 0.0508  -0.0065 0.0106  693  GLY A N   
5018  C CA  . GLY A 695  ? 0.3434 0.5165 0.2525 0.0508  -0.0087 0.0035  693  GLY A CA  
5019  C C   . GLY A 695  ? 0.3496 0.5099 0.2603 0.0510  -0.0087 -0.0045 693  GLY A C   
5020  O O   . GLY A 695  ? 0.3351 0.4881 0.2469 0.0509  -0.0108 -0.0107 693  GLY A O   
5021  N N   . HIS A 696  ? 0.3278 0.4855 0.2390 0.0510  -0.0067 -0.0043 694  HIS A N   
5022  C CA  . HIS A 696  ? 0.3230 0.4690 0.2359 0.0511  -0.0068 -0.0115 694  HIS A CA  
5023  C C   . HIS A 696  ? 0.3399 0.4954 0.2493 0.0544  -0.0072 -0.0196 694  HIS A C   
5024  O O   . HIS A 696  ? 0.3426 0.5017 0.2510 0.0555  -0.0055 -0.0198 694  HIS A O   
5025  C CB  . HIS A 696  ? 0.3047 0.4410 0.2208 0.0491  -0.0045 -0.0066 694  HIS A CB  
5026  C CG  . HIS A 696  ? 0.2745 0.4048 0.1941 0.0463  -0.0039 0.0021  694  HIS A CG  
5027  N ND1 . HIS A 696  ? 0.3179 0.4526 0.2386 0.0452  -0.0022 0.0109  694  HIS A ND1 
5028  C CD2 . HIS A 696  ? 0.3001 0.4208 0.2228 0.0445  -0.0051 0.0031  694  HIS A CD2 
5029  C CE1 . HIS A 696  ? 0.2961 0.4236 0.2206 0.0429  -0.0024 0.0167  694  HIS A CE1 
5030  N NE2 . HIS A 696  ? 0.3123 0.4316 0.2380 0.0425  -0.0041 0.0120  694  HIS A NE2 
5031  N N   . GLY A 697  ? 0.3322 0.4922 0.2398 0.0562  -0.0098 -0.0265 695  GLY A N   
5032  C CA  . GLY A 697  ? 0.3179 0.4883 0.2223 0.0597  -0.0107 -0.0348 695  GLY A CA  
5033  C C   . GLY A 697  ? 0.3171 0.4775 0.2240 0.0605  -0.0112 -0.0425 695  GLY A C   
5034  O O   . GLY A 697  ? 0.3044 0.4498 0.2153 0.0585  -0.0121 -0.0439 695  GLY A O   
5035  N N   . PRO A 698  ? 0.2857 0.4546 0.1905 0.0633  -0.0107 -0.0474 696  PRO A N   
5036  C CA  . PRO A 698  ? 0.3215 0.4814 0.2291 0.0643  -0.0114 -0.0550 696  PRO A CA  
5037  C C   . PRO A 698  ? 0.2876 0.4420 0.1974 0.0653  -0.0152 -0.0645 696  PRO A C   
5038  O O   . PRO A 698  ? 0.3004 0.4619 0.2084 0.0664  -0.0173 -0.0673 696  PRO A O   
5039  C CB  . PRO A 698  ? 0.3355 0.5091 0.2401 0.0677  -0.0101 -0.0581 696  PRO A CB  
5040  C CG  . PRO A 698  ? 0.3830 0.5709 0.2835 0.0674  -0.0078 -0.0494 696  PRO A CG  
5041  C CD  . PRO A 698  ? 0.3501 0.5378 0.2502 0.0658  -0.0093 -0.0459 696  PRO A CD  
5042  N N   . LEU A 699  ? 0.2784 0.4197 0.1926 0.0648  -0.0162 -0.0690 697  LEU A N   
5043  C CA  . LEU A 699  ? 0.2811 0.4167 0.1985 0.0658  -0.0202 -0.0783 697  LEU A CA  
5044  C C   . LEU A 699  ? 0.3083 0.4566 0.2237 0.0702  -0.0221 -0.0879 697  LEU A C   
5045  O O   . LEU A 699  ? 0.2835 0.4349 0.1992 0.0716  -0.0254 -0.0943 697  LEU A O   
5046  C CB  . LEU A 699  ? 0.2533 0.3729 0.1762 0.0642  -0.0208 -0.0803 697  LEU A CB  
5047  C CG  . LEU A 699  ? 0.2684 0.3747 0.1939 0.0599  -0.0194 -0.0724 697  LEU A CG  
5048  C CD1 . LEU A 699  ? 0.2627 0.3555 0.1934 0.0588  -0.0202 -0.0752 697  LEU A CD1 
5049  C CD2 . LEU A 699  ? 0.3056 0.4092 0.2318 0.0580  -0.0212 -0.0709 697  LEU A CD2 
5050  N N   . GLY A 700  ? 0.2832 0.4392 0.1968 0.0726  -0.0203 -0.0894 698  GLY A N   
5051  C CA  . GLY A 700  ? 0.2888 0.4554 0.2016 0.0771  -0.0223 -0.0998 698  GLY A CA  
5052  C C   . GLY A 700  ? 0.2842 0.4440 0.2006 0.0783  -0.0220 -0.1039 698  GLY A C   
5053  O O   . GLY A 700  ? 0.2812 0.4322 0.1991 0.0757  -0.0195 -0.0973 698  GLY A O   
5054  N N   . PRO A 701  ? 0.3100 0.4739 0.2284 0.0821  -0.0248 -0.1149 699  PRO A N   
5055  C CA  . PRO A 701  ? 0.2994 0.4574 0.2221 0.0833  -0.0247 -0.1188 699  PRO A CA  
5056  C C   . PRO A 701  ? 0.2778 0.4160 0.2058 0.0798  -0.0254 -0.1163 699  PRO A C   
5057  O O   . PRO A 701  ? 0.2891 0.4173 0.2211 0.0782  -0.0285 -0.1186 699  PRO A O   
5058  C CB  . PRO A 701  ? 0.3009 0.4631 0.2297 0.0863  -0.0285 -0.1287 699  PRO A CB  
5059  C CG  . PRO A 701  ? 0.3067 0.4832 0.2325 0.0873  -0.0289 -0.1284 699  PRO A CG  
5060  C CD  . PRO A 701  ? 0.2769 0.4494 0.1977 0.0842  -0.0279 -0.1214 699  PRO A CD  
5061  N N   . ILE A 702  ? 0.3164 0.4493 0.2451 0.0785  -0.0225 -0.1109 700  ILE A N   
5062  C CA  . ILE A 702  ? 0.2755 0.3907 0.2095 0.0749  -0.0227 -0.1075 700  ILE A CA  
5063  C C   . ILE A 702  ? 0.2765 0.3876 0.2148 0.0770  -0.0237 -0.1134 700  ILE A C   
5064  O O   . ILE A 702  ? 0.2702 0.3902 0.2063 0.0795  -0.0215 -0.1139 700  ILE A O   
5065  C CB  . ILE A 702  ? 0.2651 0.3761 0.1967 0.0711  -0.0187 -0.0955 700  ILE A CB  
5066  C CG1 . ILE A 702  ? 0.2635 0.3755 0.1926 0.0687  -0.0186 -0.0903 700  ILE A CG1 
5067  C CG2 . ILE A 702  ? 0.2743 0.3689 0.2109 0.0680  -0.0185 -0.0924 700  ILE A CG2 
5068  C CD1 . ILE A 702  ? 0.2899 0.3965 0.2178 0.0649  -0.0154 -0.0793 700  ILE A CD1 
5069  N N   . VAL A 703  ? 0.2691 0.3672 0.2142 0.0761  -0.0272 -0.1177 701  VAL A N   
5070  C CA  . VAL A 703  ? 0.2872 0.3790 0.2378 0.0776  -0.0287 -0.1229 701  VAL A CA  
5071  C C   . VAL A 703  ? 0.2606 0.3408 0.2128 0.0738  -0.0262 -0.1144 701  VAL A C   
5072  O O   . VAL A 703  ? 0.2593 0.3286 0.2135 0.0699  -0.0265 -0.1093 701  VAL A O   
5073  C CB  . VAL A 703  ? 0.2741 0.3582 0.2320 0.0784  -0.0343 -0.1317 701  VAL A CB  
5074  C CG1 . VAL A 703  ? 0.2844 0.3594 0.2492 0.0792  -0.0361 -0.1355 701  VAL A CG1 
5075  C CG2 . VAL A 703  ? 0.3184 0.4153 0.2749 0.0828  -0.0370 -0.1414 701  VAL A CG2 
5076  N N   . CYS A 704  ? 0.2499 0.3331 0.2012 0.0750  -0.0235 -0.1129 702  CYS A N   
5077  C CA  . CYS A 704  ? 0.2707 0.3442 0.2233 0.0718  -0.0210 -0.1053 702  CYS A CA  
5078  C C   . CYS A 704  ? 0.2642 0.3300 0.2236 0.0730  -0.0235 -0.1108 702  CYS A C   
5079  O O   . CYS A 704  ? 0.2647 0.3377 0.2245 0.0769  -0.0237 -0.1165 702  CYS A O   
5080  C CB  . CYS A 704  ? 0.2682 0.3507 0.2152 0.0719  -0.0163 -0.0988 702  CYS A CB  
5081  S SG  . CYS A 704  ? 0.2729 0.3642 0.2130 0.0702  -0.0135 -0.0912 702  CYS A SG  
5082  N N   . ILE A 705  ? 0.2322 0.2838 0.1970 0.0699  -0.0254 -0.1089 703  ILE A N   
5083  C CA  . ILE A 705  ? 0.2612 0.3040 0.2332 0.0705  -0.0282 -0.1132 703  ILE A CA  
5084  C C   . ILE A 705  ? 0.2521 0.2858 0.2251 0.0669  -0.0257 -0.1049 703  ILE A C   
5085  O O   . ILE A 705  ? 0.2637 0.2908 0.2357 0.0628  -0.0246 -0.0979 703  ILE A O   
5086  C CB  . ILE A 705  ? 0.2594 0.2940 0.2383 0.0699  -0.0335 -0.1185 703  ILE A CB  
5087  C CG1 . ILE A 705  ? 0.2844 0.3286 0.2630 0.0741  -0.0364 -0.1282 703  ILE A CG1 
5088  C CG2 . ILE A 705  ? 0.2796 0.3036 0.2668 0.0696  -0.0364 -0.1208 703  ILE A CG2 
5089  C CD1 . ILE A 705  ? 0.2935 0.3308 0.2777 0.0729  -0.0413 -0.1322 703  ILE A CD1 
5090  N N   . SER A 706  ? 0.2541 0.2880 0.2287 0.0684  -0.0248 -0.1057 704  SER A N   
5091  C CA  . SER A 706  ? 0.2561 0.2841 0.2302 0.0654  -0.0216 -0.0976 704  SER A CA  
5092  C C   . SER A 706  ? 0.2995 0.3181 0.2807 0.0652  -0.0240 -0.0995 704  SER A C   
5093  O O   . SER A 706  ? 0.2792 0.2983 0.2655 0.0684  -0.0274 -0.1075 704  SER A O   
5094  C CB  . SER A 706  ? 0.2754 0.3141 0.2434 0.0669  -0.0172 -0.0943 704  SER A CB  
5095  O OG  . SER A 706  ? 0.2843 0.3322 0.2529 0.0716  -0.0180 -0.1018 704  SER A OG  
5096  N N   . PRO A 707  ? 0.3097 0.3201 0.2919 0.0616  -0.0223 -0.0923 705  PRO A N   
5097  C CA  . PRO A 707  ? 0.3083 0.3094 0.2975 0.0609  -0.0246 -0.0929 705  PRO A CA  
5098  C C   . PRO A 707  ? 0.2581 0.2635 0.2472 0.0634  -0.0227 -0.0938 705  PRO A C   
5099  O O   . PRO A 707  ? 0.2773 0.2920 0.2605 0.0648  -0.0191 -0.0921 705  PRO A O   
5100  C CB  . PRO A 707  ? 0.2975 0.2897 0.2865 0.0558  -0.0231 -0.0842 705  PRO A CB  
5101  C CG  . PRO A 707  ? 0.2628 0.2615 0.2439 0.0548  -0.0185 -0.0785 705  PRO A CG  
5102  C CD  . PRO A 707  ? 0.2541 0.2628 0.2314 0.0578  -0.0187 -0.0832 705  PRO A CD  
5103  N N   . TRP A 708  ? 0.2743 0.2728 0.2704 0.0638  -0.0255 -0.0962 706  TRP A N   
5104  C CA  . TRP A 708  ? 0.2529 0.2550 0.2495 0.0662  -0.0239 -0.0972 706  TRP A CA  
5105  C C   . TRP A 708  ? 0.2681 0.2680 0.2612 0.0630  -0.0198 -0.0881 706  TRP A C   
5106  O O   . TRP A 708  ? 0.2982 0.3044 0.2890 0.0647  -0.0171 -0.0874 706  TRP A O   
5107  C CB  . TRP A 708  ? 0.2736 0.2692 0.2795 0.0679  -0.0284 -0.1027 706  TRP A CB  
5108  C CG  . TRP A 708  ? 0.2921 0.2755 0.3026 0.0637  -0.0296 -0.0967 706  TRP A CG  
5109  C CD1 . TRP A 708  ? 0.2938 0.2680 0.3096 0.0608  -0.0331 -0.0957 706  TRP A CD1 
5110  C CD2 . TRP A 708  ? 0.3021 0.2823 0.3125 0.0617  -0.0271 -0.0904 706  TRP A CD2 
5111  N NE1 . TRP A 708  ? 0.2944 0.2604 0.3130 0.0571  -0.0328 -0.0889 706  TRP A NE1 
5112  C CE2 . TRP A 708  ? 0.2866 0.2559 0.3017 0.0576  -0.0292 -0.0858 706  TRP A CE2 
5113  C CE3 . TRP A 708  ? 0.2778 0.2637 0.2844 0.0628  -0.0233 -0.0881 706  TRP A CE3 
5114  C CZ2 . TRP A 708  ? 0.2543 0.2185 0.2704 0.0549  -0.0278 -0.0793 706  TRP A CZ2 
5115  C CZ3 . TRP A 708  ? 0.3019 0.2821 0.3096 0.0600  -0.0220 -0.0817 706  TRP A CZ3 
5116  C CH2 . TRP A 708  ? 0.2865 0.2561 0.2989 0.0562  -0.0242 -0.0776 706  TRP A CH2 
5117  N N   . ASN A 709  ? 0.2686 0.2606 0.2614 0.0584  -0.0193 -0.0814 707  ASN A N   
5118  C CA  . ASN A 709  ? 0.2660 0.2537 0.2582 0.0555  -0.0167 -0.0742 707  ASN A CA  
5119  C C   . ASN A 709  ? 0.2576 0.2521 0.2425 0.0548  -0.0119 -0.0688 707  ASN A C   
5120  O O   . ASN A 709  ? 0.2836 0.2773 0.2679 0.0536  -0.0095 -0.0643 707  ASN A O   
5121  C CB  . ASN A 709  ? 0.2613 0.2384 0.2564 0.0511  -0.0181 -0.0693 707  ASN A CB  
5122  C CG  . ASN A 709  ? 0.2811 0.2585 0.2717 0.0484  -0.0166 -0.0653 707  ASN A CG  
5123  O OD1 . ASN A 709  ? 0.3051 0.2853 0.2947 0.0495  -0.0180 -0.0689 707  ASN A OD1 
5124  N ND2 . ASN A 709  ? 0.2946 0.2693 0.2825 0.0450  -0.0138 -0.0581 707  ASN A ND2 
5125  N N   . PHE A 710  ? 0.2669 0.2679 0.2467 0.0553  -0.0105 -0.0687 708  PHE A N   
5126  C CA  . PHE A 710  ? 0.2487 0.2578 0.2224 0.0551  -0.0063 -0.0642 708  PHE A CA  
5127  C C   . PHE A 710  ? 0.2758 0.2966 0.2468 0.0593  -0.0063 -0.0699 708  PHE A C   
5128  O O   . PHE A 710  ? 0.2632 0.2893 0.2305 0.0596  -0.0059 -0.0701 708  PHE A O   
5129  C CB  . PHE A 710  ? 0.2714 0.2782 0.2416 0.0516  -0.0047 -0.0580 708  PHE A CB  
5130  C CG  . PHE A 710  ? 0.2978 0.2942 0.2702 0.0475  -0.0046 -0.0526 708  PHE A CG  
5131  C CD1 . PHE A 710  ? 0.2858 0.2785 0.2604 0.0467  -0.0038 -0.0502 708  PHE A CD1 
5132  C CD2 . PHE A 710  ? 0.3201 0.3111 0.2924 0.0447  -0.0054 -0.0501 708  PHE A CD2 
5133  C CE1 . PHE A 710  ? 0.2841 0.2684 0.2605 0.0430  -0.0038 -0.0454 708  PHE A CE1 
5134  C CE2 . PHE A 710  ? 0.2870 0.2698 0.2612 0.0411  -0.0053 -0.0454 708  PHE A CE2 
5135  C CZ  . PHE A 710  ? 0.3071 0.2868 0.2833 0.0403  -0.0045 -0.0431 708  PHE A CZ  
5136  N N   . PRO A 711  ? 0.2512 0.2770 0.2243 0.0628  -0.0067 -0.0748 709  PRO A N   
5137  C CA  . PRO A 711  ? 0.2642 0.3005 0.2364 0.0674  -0.0079 -0.0824 709  PRO A CA  
5138  C C   . PRO A 711  ? 0.2564 0.3062 0.2221 0.0687  -0.0044 -0.0802 709  PRO A C   
5139  O O   . PRO A 711  ? 0.2545 0.3141 0.2183 0.0721  -0.0052 -0.0860 709  PRO A O   
5140  C CB  . PRO A 711  ? 0.2687 0.3052 0.2458 0.0704  -0.0093 -0.0878 709  PRO A CB  
5141  C CG  . PRO A 711  ? 0.2423 0.2744 0.2195 0.0678  -0.0067 -0.0807 709  PRO A CG  
5142  C CD  . PRO A 711  ? 0.2299 0.2516 0.2066 0.0629  -0.0065 -0.0740 709  PRO A CD  
5143  N N   . LEU A 712  ? 0.2712 0.3221 0.2335 0.0661  -0.0008 -0.0720 710  LEU A N   
5144  C CA  . LEU A 712  ? 0.2593 0.3222 0.2158 0.0666  0.0022  -0.0684 710  LEU A CA  
5145  C C   . LEU A 712  ? 0.2660 0.3257 0.2195 0.0629  0.0034  -0.0617 710  LEU A C   
5146  O O   . LEU A 712  ? 0.2537 0.3217 0.2034 0.0637  0.0039  -0.0614 710  LEU A O   
5147  C CB  . LEU A 712  ? 0.2618 0.3308 0.2173 0.0668  0.0055  -0.0641 710  LEU A CB  
5148  C CG  . LEU A 712  ? 0.2830 0.3656 0.2331 0.0672  0.0086  -0.0597 710  LEU A CG  
5149  C CD1 . LEU A 712  ? 0.2844 0.3804 0.2324 0.0716  0.0077  -0.0667 710  LEU A CD1 
5150  C CD2 . LEU A 712  ? 0.2803 0.3673 0.2301 0.0666  0.0117  -0.0541 710  LEU A CD2 
5151  N N   . ALA A 713  ? 0.2477 0.2957 0.2031 0.0591  0.0036  -0.0565 711  ALA A N   
5152  C CA  . ALA A 713  ? 0.2309 0.2763 0.1838 0.0557  0.0050  -0.0497 711  ALA A CA  
5153  C C   . ALA A 713  ? 0.2542 0.2981 0.2064 0.0555  0.0027  -0.0525 711  ALA A C   
5154  O O   . ALA A 713  ? 0.2530 0.3038 0.2016 0.0555  0.0037  -0.0503 711  ALA A O   
5155  C CB  . ALA A 713  ? 0.2587 0.2926 0.2139 0.0519  0.0055  -0.0444 711  ALA A CB  
5156  N N   . ILE A 714  ? 0.2634 0.2984 0.2195 0.0552  -0.0004 -0.0568 712  ILE A N   
5157  C CA  . ILE A 714  ? 0.2324 0.2656 0.1883 0.0548  -0.0026 -0.0592 712  ILE A CA  
5158  C C   . ILE A 714  ? 0.2486 0.2929 0.2024 0.0586  -0.0037 -0.0655 712  ILE A C   
5159  O O   . ILE A 714  ? 0.2532 0.3019 0.2041 0.0586  -0.0040 -0.0653 712  ILE A O   
5160  C CB  . ILE A 714  ? 0.2414 0.2627 0.2026 0.0532  -0.0059 -0.0618 712  ILE A CB  
5161  C CG1 . ILE A 714  ? 0.2708 0.2829 0.2329 0.0491  -0.0045 -0.0547 712  ILE A CG1 
5162  C CG2 . ILE A 714  ? 0.2441 0.2648 0.2059 0.0535  -0.0089 -0.0660 712  ILE A CG2 
5163  C CD1 . ILE A 714  ? 0.3331 0.3349 0.2993 0.0466  -0.0071 -0.0551 712  ILE A CD1 
5164  N N   . PHE A 715  ? 0.2263 0.2757 0.1815 0.0621  -0.0044 -0.0712 713  PHE A N   
5165  C CA  . PHE A 715  ? 0.2327 0.2947 0.1856 0.0662  -0.0051 -0.0775 713  PHE A CA  
5166  C C   . PHE A 715  ? 0.2657 0.3393 0.2124 0.0661  -0.0021 -0.0724 713  PHE A C   
5167  O O   . PHE A 715  ? 0.2454 0.3254 0.1894 0.0671  -0.0029 -0.0742 713  PHE A O   
5168  C CB  . PHE A 715  ? 0.2633 0.3300 0.2184 0.0698  -0.0054 -0.0831 713  PHE A CB  
5169  C CG  . PHE A 715  ? 0.2385 0.3195 0.1913 0.0744  -0.0060 -0.0901 713  PHE A CG  
5170  C CD1 . PHE A 715  ? 0.2634 0.3445 0.2189 0.0771  -0.0099 -0.0991 713  PHE A CD1 
5171  C CD2 . PHE A 715  ? 0.2744 0.3694 0.2227 0.0762  -0.0027 -0.0877 713  PHE A CD2 
5172  C CE1 . PHE A 715  ? 0.2967 0.3918 0.2501 0.0816  -0.0106 -0.1063 713  PHE A CE1 
5173  C CE2 . PHE A 715  ? 0.3030 0.4125 0.2489 0.0805  -0.0032 -0.0942 713  PHE A CE2 
5174  C CZ  . PHE A 715  ? 0.3089 0.4186 0.2572 0.0834  -0.0071 -0.1039 713  PHE A CZ  
5175  N N   . THR A 716  ? 0.2395 0.3160 0.1844 0.0649  0.0014  -0.0656 714  THR A N   
5176  C CA  . THR A 716  ? 0.2412 0.3289 0.1811 0.0646  0.0042  -0.0597 714  THR A CA  
5177  C C   . THR A 716  ? 0.2492 0.3324 0.1875 0.0614  0.0042  -0.0544 714  THR A C   
5178  O O   . THR A 716  ? 0.2473 0.3398 0.1821 0.0621  0.0046  -0.0532 714  THR A O   
5179  C CB  . THR A 716  ? 0.2754 0.3656 0.2149 0.0635  0.0074  -0.0532 714  THR A CB  
5180  O OG1 . THR A 716  ? 0.2537 0.3492 0.1946 0.0667  0.0075  -0.0584 714  THR A OG1 
5181  C CG2 . THR A 716  ? 0.2660 0.3678 0.2013 0.0629  0.0101  -0.0465 714  THR A CG2 
5182  N N   . GLY A 717  ? 0.2326 0.3022 0.1738 0.0581  0.0037  -0.0514 715  GLY A N   
5183  C CA  . GLY A 717  ? 0.2534 0.3186 0.1936 0.0550  0.0038  -0.0462 715  GLY A CA  
5184  C C   . GLY A 717  ? 0.2453 0.3136 0.1842 0.0562  0.0014  -0.0505 715  GLY A C   
5185  O O   . GLY A 717  ? 0.2497 0.3243 0.1856 0.0558  0.0022  -0.0470 715  GLY A O   
5186  N N   . GLN A 718  ? 0.2268 0.2911 0.1685 0.0578  -0.0016 -0.0583 716  GLN A N   
5187  C CA  . GLN A 718  ? 0.2275 0.2941 0.1685 0.0587  -0.0042 -0.0627 716  GLN A CA  
5188  C C   . GLN A 718  ? 0.2434 0.3257 0.1799 0.0619  -0.0036 -0.0649 716  GLN A C   
5189  O O   . GLN A 718  ? 0.2360 0.3233 0.1698 0.0616  -0.0038 -0.0633 716  GLN A O   
5190  C CB  . GLN A 718  ? 0.2277 0.2874 0.1734 0.0600  -0.0080 -0.0709 716  GLN A CB  
5191  C CG  . GLN A 718  ? 0.2396 0.2846 0.1899 0.0567  -0.0089 -0.0687 716  GLN A CG  
5192  C CD  . GLN A 718  ? 0.2652 0.3031 0.2209 0.0574  -0.0132 -0.0758 716  GLN A CD  
5193  O OE1 . GLN A 718  ? 0.2592 0.2880 0.2178 0.0547  -0.0148 -0.0745 716  GLN A OE1 
5194  N NE2 . GLN A 718  ? 0.2484 0.2908 0.2059 0.0611  -0.0150 -0.0834 716  GLN A NE2 
5195  N N   . ILE A 719  ? 0.2483 0.3391 0.1842 0.0650  -0.0029 -0.0685 717  ILE A N   
5196  C CA  . ILE A 719  ? 0.2428 0.3500 0.1745 0.0684  -0.0024 -0.0713 717  ILE A CA  
5197  C C   . ILE A 719  ? 0.2637 0.3793 0.1911 0.0668  0.0007  -0.0622 717  ILE A C   
5198  O O   . ILE A 719  ? 0.2627 0.3886 0.1866 0.0678  0.0006  -0.0620 717  ILE A O   
5199  C CB  . ILE A 719  ? 0.2758 0.3902 0.2082 0.0721  -0.0021 -0.0769 717  ILE A CB  
5200  C CG1 . ILE A 719  ? 0.2473 0.3548 0.1845 0.0742  -0.0060 -0.0869 717  ILE A CG1 
5201  C CG2 . ILE A 719  ? 0.2921 0.4255 0.2196 0.0753  -0.0007 -0.0780 717  ILE A CG2 
5202  C CD1 . ILE A 719  ? 0.3262 0.4355 0.2661 0.0769  -0.0058 -0.0914 717  ILE A CD1 
5203  N N   . ALA A 720  ? 0.2433 0.3548 0.1713 0.0642  0.0034  -0.0544 718  ALA A N   
5204  C CA  . ALA A 720  ? 0.2552 0.3737 0.1802 0.0624  0.0061  -0.0452 718  ALA A CA  
5205  C C   . ALA A 720  ? 0.2213 0.3365 0.1455 0.0602  0.0052  -0.0416 718  ALA A C   
5206  O O   . ALA A 720  ? 0.2578 0.3836 0.1788 0.0604  0.0059  -0.0380 718  ALA A O   
5207  C CB  . ALA A 720  ? 0.2453 0.3573 0.1724 0.0598  0.0085  -0.0382 718  ALA A CB  
5208  N N   . ALA A 721  ? 0.2425 0.3433 0.1698 0.0579  0.0037  -0.0422 719  ALA A N   
5209  C CA  . ALA A 721  ? 0.2208 0.3177 0.1479 0.0557  0.0027  -0.0392 719  ALA A CA  
5210  C C   . ALA A 721  ? 0.2539 0.3601 0.1783 0.0581  0.0007  -0.0444 719  ALA A C   
5211  O O   . ALA A 721  ? 0.2446 0.3578 0.1665 0.0576  0.0011  -0.0401 719  ALA A O   
5212  C CB  . ALA A 721  ? 0.2170 0.2980 0.1481 0.0532  0.0012  -0.0402 719  ALA A CB  
5213  N N   . ALA A 722  ? 0.2172 0.3238 0.1426 0.0608  -0.0017 -0.0536 720  ALA A N   
5214  C CA  . ALA A 722  ? 0.2314 0.3467 0.1546 0.0633  -0.0040 -0.0596 720  ALA A CA  
5215  C C   . ALA A 722  ? 0.2694 0.4027 0.1877 0.0655  -0.0023 -0.0576 720  ALA A C   
5216  O O   . ALA A 722  ? 0.2402 0.3811 0.1557 0.0657  -0.0028 -0.0560 720  ALA A O   
5217  C CB  . ALA A 722  ? 0.2477 0.3603 0.1737 0.0660  -0.0070 -0.0703 720  ALA A CB  
5218  N N   . LEU A 723  ? 0.2203 0.3609 0.1377 0.0672  -0.0002 -0.0571 721  LEU A N   
5219  C CA  . LEU A 723  ? 0.2396 0.3985 0.1524 0.0693  0.0016  -0.0548 721  LEU A CA  
5220  C C   . LEU A 723  ? 0.2535 0.4158 0.1645 0.0663  0.0035  -0.0438 721  LEU A C   
5221  O O   . LEU A 723  ? 0.2360 0.4114 0.1434 0.0673  0.0036  -0.0418 721  LEU A O   
5222  C CB  . LEU A 723  ? 0.2446 0.4097 0.1575 0.0711  0.0037  -0.0554 721  LEU A CB  
5223  C CG  . LEU A 723  ? 0.2594 0.4268 0.1735 0.0751  0.0019  -0.0666 721  LEU A CG  
5224  C CD1 . LEU A 723  ? 0.2692 0.4400 0.1841 0.0760  0.0044  -0.0652 721  LEU A CD1 
5225  C CD2 . LEU A 723  ? 0.2761 0.4595 0.1867 0.0789  0.0005  -0.0732 721  LEU A CD2 
5226  N N   . VAL A 724  ? 0.2544 0.4055 0.1681 0.0628  0.0051  -0.0365 722  VAL A N   
5227  C CA  . VAL A 724  ? 0.2530 0.4079 0.1658 0.0603  0.0068  -0.0259 722  VAL A CA  
5228  C C   . VAL A 724  ? 0.2631 0.4158 0.1755 0.0590  0.0050  -0.0246 722  VAL A C   
5229  O O   . VAL A 724  ? 0.2711 0.4321 0.1818 0.0581  0.0057  -0.0178 722  VAL A O   
5230  C CB  . VAL A 724  ? 0.2420 0.3861 0.1583 0.0571  0.0088  -0.0190 722  VAL A CB  
5231  C CG1 . VAL A 724  ? 0.2476 0.3742 0.1674 0.0543  0.0075  -0.0187 722  VAL A CG1 
5232  C CG2 . VAL A 724  ? 0.2691 0.4218 0.1848 0.0555  0.0109  -0.0086 722  VAL A CG2 
5233  N N   . ALA A 725  ? 0.2457 0.3878 0.1599 0.0589  0.0026  -0.0310 723  ALA A N   
5234  C CA  . ALA A 725  ? 0.2672 0.4079 0.1809 0.0581  0.0006  -0.0310 723  ALA A CA  
5235  C C   . ALA A 725  ? 0.2753 0.4310 0.1850 0.0612  -0.0008 -0.0358 723  ALA A C   
5236  O O   . ALA A 725  ? 0.2686 0.4249 0.1777 0.0608  -0.0026 -0.0362 723  ALA A O   
5237  C CB  . ALA A 725  ? 0.2476 0.3727 0.1648 0.0569  -0.0016 -0.0362 723  ALA A CB  
5238  N N   . GLY A 726  ? 0.2455 0.4140 0.1526 0.0643  -0.0001 -0.0395 724  GLY A N   
5239  C CA  . GLY A 726  ? 0.2545 0.4392 0.1575 0.0675  -0.0012 -0.0440 724  GLY A CA  
5240  C C   . GLY A 726  ? 0.2754 0.4602 0.1787 0.0707  -0.0042 -0.0565 724  GLY A C   
5241  O O   . GLY A 726  ? 0.3150 0.5120 0.2151 0.0732  -0.0057 -0.0610 724  GLY A O   
5242  N N   . ASN A 727  ? 0.2703 0.4423 0.1775 0.0708  -0.0052 -0.0620 725  ASN A N   
5243  C CA  . ASN A 727  ? 0.2523 0.4223 0.1613 0.0736  -0.0085 -0.0738 725  ASN A CA  
5244  C C   . ASN A 727  ? 0.2500 0.4275 0.1588 0.0772  -0.0079 -0.0801 725  ASN A C   
5245  O O   . ASN A 727  ? 0.2528 0.4261 0.1630 0.0763  -0.0057 -0.0765 725  ASN A O   
5246  C CB  . ASN A 727  ? 0.2561 0.4065 0.1706 0.0712  -0.0104 -0.0758 725  ASN A CB  
5247  C CG  . ASN A 727  ? 0.2564 0.3985 0.1715 0.0675  -0.0107 -0.0693 725  ASN A CG  
5248  O OD1 . ASN A 727  ? 0.2805 0.4252 0.1948 0.0678  -0.0129 -0.0719 725  ASN A OD1 
5249  N ND2 . ASN A 727  ? 0.2741 0.4064 0.1909 0.0641  -0.0085 -0.0612 725  ASN A ND2 
5250  N N   . PRO A 728  ? 0.2603 0.4487 0.1678 0.0813  -0.0101 -0.0898 726  PRO A N   
5251  C CA  . PRO A 728  ? 0.2933 0.4842 0.2044 0.0840  -0.0104 -0.0961 726  PRO A CA  
5252  C C   . PRO A 728  ? 0.2767 0.4510 0.1923 0.0841  -0.0127 -0.1026 726  PRO A C   
5253  O O   . PRO A 728  ? 0.3045 0.4669 0.2230 0.0822  -0.0153 -0.1041 726  PRO A O   
5254  C CB  . PRO A 728  ? 0.2585 0.4621 0.1716 0.0869  -0.0129 -0.1026 726  PRO A CB  
5255  C CG  . PRO A 728  ? 0.2713 0.4723 0.1832 0.0857  -0.0152 -0.1033 726  PRO A CG  
5256  C CD  . PRO A 728  ? 0.2760 0.4716 0.1832 0.0823  -0.0128 -0.0935 726  PRO A CD  
5257  N N   . VAL A 729  ? 0.2854 0.4578 0.2039 0.0853  -0.0118 -0.1047 727  VAL A N   
5258  C CA  . VAL A 729  ? 0.2616 0.4171 0.1855 0.0843  -0.0133 -0.1076 727  VAL A CA  
5259  C C   . VAL A 729  ? 0.2593 0.4162 0.1886 0.0878  -0.0161 -0.1178 727  VAL A C   
5260  O O   . VAL A 729  ? 0.2673 0.4361 0.1969 0.0901  -0.0151 -0.1189 727  VAL A O   
5261  C CB  . VAL A 729  ? 0.2587 0.4071 0.1832 0.0813  -0.0097 -0.0983 727  VAL A CB  
5262  C CG1 . VAL A 729  ? 0.2447 0.3780 0.1755 0.0806  -0.0113 -0.1017 727  VAL A CG1 
5263  C CG2 . VAL A 729  ? 0.2619 0.4043 0.1846 0.0767  -0.0080 -0.0878 727  VAL A CG2 
5264  N N   . LEU A 730  ? 0.2650 0.4089 0.1999 0.0877  -0.0199 -0.1240 728  LEU A N   
5265  C CA  . LEU A 730  ? 0.2684 0.4080 0.2108 0.0899  -0.0229 -0.1318 728  LEU A CA  
5266  C C   . LEU A 730  ? 0.2597 0.3848 0.2043 0.0882  -0.0220 -0.1296 728  LEU A C   
5267  O O   . LEU A 730  ? 0.2720 0.3831 0.2193 0.0847  -0.0232 -0.1264 728  LEU A O   
5268  C CB  . LEU A 730  ? 0.2919 0.4271 0.2402 0.0907  -0.0281 -0.1398 728  LEU A CB  
5269  C CG  . LEU A 730  ? 0.2795 0.4273 0.2265 0.0923  -0.0297 -0.1429 728  LEU A CG  
5270  C CD1 . LEU A 730  ? 0.2690 0.4350 0.2136 0.0952  -0.0276 -0.1430 728  LEU A CD1 
5271  C CD2 . LEU A 730  ? 0.3066 0.4545 0.2479 0.0898  -0.0287 -0.1375 728  LEU A CD2 
5272  N N   . ALA A 731  ? 0.2669 0.3951 0.2123 0.0895  -0.0199 -0.1288 729  ALA A N   
5273  C CA  . ALA A 731  ? 0.2607 0.3764 0.2088 0.0873  -0.0186 -0.1246 729  ALA A CA  
5274  C C   . ALA A 731  ? 0.2786 0.3863 0.2347 0.0895  -0.0225 -0.1332 729  ALA A C   
5275  O O   . ALA A 731  ? 0.3176 0.4328 0.2766 0.0922  -0.0232 -0.1375 729  ALA A O   
5276  C CB  . ALA A 731  ? 0.2864 0.4104 0.2303 0.0874  -0.0139 -0.1181 729  ALA A CB  
5277  N N   . LYS A 732  ? 0.2605 0.3521 0.2222 0.0865  -0.0252 -0.1326 730  LYS A N   
5278  C CA  . LYS A 732  ? 0.2689 0.3515 0.2391 0.0881  -0.0293 -0.1399 730  LYS A CA  
5279  C C   . LYS A 732  ? 0.2793 0.3498 0.2526 0.0849  -0.0278 -0.1330 730  LYS A C   
5280  O O   . LYS A 732  ? 0.2712 0.3291 0.2468 0.0806  -0.0284 -0.1274 730  LYS A O   
5281  C CB  . LYS A 732  ? 0.2969 0.3710 0.2727 0.0871  -0.0343 -0.1444 730  LYS A CB  
5282  C CG  . LYS A 732  ? 0.2789 0.3521 0.2641 0.0893  -0.0393 -0.1523 730  LYS A CG  
5283  C CD  . LYS A 732  ? 0.3105 0.3743 0.3022 0.0892  -0.0402 -0.1526 730  LYS A CD  
5284  C CE  . LYS A 732  ? 0.3165 0.3633 0.3123 0.0856  -0.0419 -0.1492 730  LYS A CE  
5285  N NZ  . LYS A 732  ? 0.3037 0.3424 0.3058 0.0855  -0.0426 -0.1486 730  LYS A NZ  
5286  N N   . PRO A 733  ? 0.2667 0.3412 0.2402 0.0868  -0.0258 -0.1331 731  PRO A N   
5287  C CA  . PRO A 733  ? 0.2903 0.3538 0.2668 0.0838  -0.0245 -0.1267 731  PRO A CA  
5288  C C   . PRO A 733  ? 0.2709 0.3217 0.2569 0.0838  -0.0292 -0.1316 731  PRO A C   
5289  O O   . PRO A 733  ? 0.2884 0.3403 0.2794 0.0872  -0.0335 -0.1412 731  PRO A O   
5290  C CB  . PRO A 733  ? 0.2931 0.3669 0.2669 0.0866  -0.0212 -0.1267 731  PRO A CB  
5291  C CG  . PRO A 733  ? 0.2569 0.3430 0.2311 0.0920  -0.0232 -0.1370 731  PRO A CG  
5292  C CD  . PRO A 733  ? 0.2829 0.3724 0.2546 0.0915  -0.0248 -0.1385 731  PRO A CD  
5293  N N   . ALA A 734  ? 0.2689 0.3079 0.2576 0.0799  -0.0286 -0.1247 732  ALA A N   
5294  C CA  . ALA A 734  ? 0.3009 0.3280 0.2989 0.0795  -0.0328 -0.1276 732  ALA A CA  
5295  C C   . ALA A 734  ? 0.2796 0.3114 0.2824 0.0845  -0.0349 -0.1364 732  ALA A C   
5296  O O   . ALA A 734  ? 0.3189 0.3604 0.3179 0.0871  -0.0317 -0.1367 732  ALA A O   
5297  C CB  . ALA A 734  ? 0.2645 0.2810 0.2635 0.0749  -0.0309 -0.1183 732  ALA A CB  
5298  N N   . GLU A 735  ? 0.2960 0.3209 0.3078 0.0860  -0.0404 -0.1435 733  GLU A N   
5299  C CA  . GLU A 735  ? 0.3148 0.3445 0.3326 0.0891  -0.0426 -0.1491 733  GLU A CA  
5300  C C   . GLU A 735  ? 0.2858 0.3129 0.3050 0.0895  -0.0406 -0.1463 733  GLU A C   
5301  O O   . GLU A 735  ? 0.3007 0.3359 0.3217 0.0925  -0.0405 -0.1499 733  GLU A O   
5302  C CB  . GLU A 735  ? 0.3155 0.3377 0.3442 0.0888  -0.0491 -0.1540 733  GLU A CB  
5303  C CG  . GLU A 735  ? 0.3631 0.3690 0.3983 0.0850  -0.0517 -0.1498 733  GLU A CG  
5304  C CD  . GLU A 735  ? 0.3958 0.3958 0.4295 0.0818  -0.0529 -0.1475 733  GLU A CD  
5305  O OE1 . GLU A 735  ? 0.3500 0.3570 0.3750 0.0820  -0.0497 -0.1466 733  GLU A OE1 
5306  O OE2 . GLU A 735  ? 0.3443 0.3329 0.3859 0.0791  -0.0570 -0.1463 733  GLU A OE2 
5307  N N   . GLU A 736  ? 0.3124 0.3294 0.3310 0.0861  -0.0389 -0.1390 734  GLU A N   
5308  C CA  . GLU A 736  ? 0.2933 0.3076 0.3138 0.0857  -0.0371 -0.1352 734  GLU A CA  
5309  C C   . GLU A 736  ? 0.3257 0.3518 0.3377 0.0869  -0.0314 -0.1318 734  GLU A C   
5310  O O   . GLU A 736  ? 0.3148 0.3431 0.3285 0.0886  -0.0302 -0.1320 734  GLU A O   
5311  C CB  . GLU A 736  ? 0.3120 0.3130 0.3347 0.0800  -0.0370 -0.1258 734  GLU A CB  
5312  C CG  . GLU A 736  ? 0.3246 0.3135 0.3567 0.0783  -0.0427 -0.1276 734  GLU A CG  
5313  C CD  . GLU A 736  ? 0.3459 0.3318 0.3757 0.0751  -0.0435 -0.1253 734  GLU A CD  
5314  O OE1 . GLU A 736  ? 0.3251 0.3194 0.3467 0.0755  -0.0404 -0.1248 734  GLU A OE1 
5315  O OE2 . GLU A 736  ? 0.3683 0.3435 0.4047 0.0721  -0.0472 -0.1235 734  GLU A OE2 
5316  N N   . THR A 737  ? 0.2991 0.3328 0.3025 0.0858  -0.0279 -0.1281 735  THR A N   
5317  C CA  . THR A 737  ? 0.2804 0.3239 0.2761 0.0856  -0.0223 -0.1224 735  THR A CA  
5318  C C   . THR A 737  ? 0.3069 0.3658 0.2958 0.0885  -0.0204 -0.1257 735  THR A C   
5319  O O   . THR A 737  ? 0.2531 0.3165 0.2350 0.0862  -0.0169 -0.1190 735  THR A O   
5320  C CB  . THR A 737  ? 0.2634 0.2997 0.2553 0.0799  -0.0192 -0.1111 735  THR A CB  
5321  O OG1 . THR A 737  ? 0.2934 0.3253 0.2837 0.0772  -0.0204 -0.1093 735  THR A OG1 
5322  C CG2 . THR A 737  ? 0.2523 0.2761 0.2499 0.0772  -0.0203 -0.1071 735  THR A CG2 
5323  N N   . PRO A 738  ? 0.2794 0.3474 0.2704 0.0939  -0.0227 -0.1360 736  PRO A N   
5324  C CA  . PRO A 738  ? 0.2893 0.3729 0.2743 0.0958  -0.0210 -0.1377 736  PRO A CA  
5325  C C   . PRO A 738  ? 0.2957 0.3929 0.2747 0.0970  -0.0161 -0.1338 736  PRO A C   
5326  O O   . PRO A 738  ? 0.3064 0.4159 0.2790 0.0974  -0.0138 -0.1320 736  PRO A O   
5327  C CB  . PRO A 738  ? 0.3200 0.4072 0.3118 0.0985  -0.0259 -0.1463 736  PRO A CB  
5328  C CG  . PRO A 738  ? 0.2999 0.3796 0.2994 0.0993  -0.0278 -0.1483 736  PRO A CG  
5329  C CD  . PRO A 738  ? 0.2818 0.3463 0.2822 0.0959  -0.0271 -0.1425 736  PRO A CD  
5330  N N   . LEU A 739  ? 0.2616 0.3575 0.2428 0.0977  -0.0146 -0.1324 737  LEU A N   
5331  C CA  . LEU A 739  ? 0.2794 0.3895 0.2561 0.0991  -0.0105 -0.1295 737  LEU A CA  
5332  C C   . LEU A 739  ? 0.2551 0.3686 0.2240 0.0960  -0.0056 -0.1196 737  LEU A C   
5333  O O   . LEU A 739  ? 0.3020 0.4303 0.2649 0.0973  -0.0028 -0.1181 737  LEU A O   
5334  C CB  . LEU A 739  ? 0.2795 0.3867 0.2612 0.1003  -0.0104 -0.1301 737  LEU A CB  
5335  C CG  . LEU A 739  ? 0.2844 0.3889 0.2747 0.1027  -0.0153 -0.1384 737  LEU A CG  
5336  C CD1 . LEU A 739  ? 0.2624 0.3634 0.2572 0.1035  -0.0148 -0.1378 737  LEU A CD1 
5337  C CD2 . LEU A 739  ? 0.2849 0.4049 0.2745 0.1058  -0.0165 -0.1440 737  LEU A CD2 
5338  N N   . ILE A 740  ? 0.2689 0.3686 0.2386 0.0910  -0.0050 -0.1114 738  ILE A N   
5339  C CA  . ILE A 740  ? 0.2615 0.3628 0.2253 0.0870  -0.0010 -0.1008 738  ILE A CA  
5340  C C   . ILE A 740  ? 0.2810 0.3870 0.2402 0.0863  -0.0011 -0.1003 738  ILE A C   
5341  O O   . ILE A 740  ? 0.2822 0.3973 0.2357 0.0852  0.0021  -0.0942 738  ILE A O   
5342  C CB  . ILE A 740  ? 0.2734 0.3592 0.2396 0.0820  -0.0005 -0.0930 738  ILE A CB  
5343  C CG1 . ILE A 740  ? 0.2965 0.3843 0.2574 0.0781  0.0035  -0.0823 738  ILE A CG1 
5344  C CG2 . ILE A 740  ? 0.2785 0.3505 0.2480 0.0798  -0.0040 -0.0944 738  ILE A CG2 
5345  C CD1 . ILE A 740  ? 0.2988 0.3988 0.2571 0.0793  0.0072  -0.0789 738  ILE A CD1 
5346  N N   . ALA A 741  ? 0.2874 0.3879 0.2493 0.0872  -0.0050 -0.1068 739  ALA A N   
5347  C CA  . ALA A 741  ? 0.3149 0.4208 0.2727 0.0872  -0.0056 -0.1077 739  ALA A CA  
5348  C C   . ALA A 741  ? 0.2756 0.4010 0.2286 0.0913  -0.0040 -0.1114 739  ALA A C   
5349  O O   . ALA A 741  ? 0.2888 0.4229 0.2360 0.0902  -0.0017 -0.1064 739  ALA A O   
5350  C CB  . ALA A 741  ? 0.2853 0.3821 0.2479 0.0879  -0.0105 -0.1151 739  ALA A CB  
5351  N N   . ALA A 742  ? 0.2745 0.4071 0.2307 0.0956  -0.0055 -0.1195 740  ALA A N   
5352  C CA  . ALA A 742  ? 0.2759 0.4262 0.2297 0.0978  -0.0047 -0.1207 740  ALA A CA  
5353  C C   . ALA A 742  ? 0.2821 0.4431 0.2303 0.0968  0.0004  -0.1121 740  ALA A C   
5354  O O   . ALA A 742  ? 0.2943 0.4692 0.2381 0.0969  0.0020  -0.1091 740  ALA A O   
5355  C CB  . ALA A 742  ? 0.3005 0.4544 0.2607 0.1012  -0.0077 -0.1288 740  ALA A CB  
5356  N N   . GLU A 743  ? 0.2712 0.4260 0.2199 0.0957  0.0029  -0.1078 741  GLU A N   
5357  C CA  . GLU A 743  ? 0.3005 0.4646 0.2446 0.0943  0.0076  -0.0990 741  GLU A CA  
5358  C C   . GLU A 743  ? 0.2936 0.4561 0.2333 0.0899  0.0094  -0.0894 741  GLU A C   
5359  O O   . GLU A 743  ? 0.2835 0.4593 0.2185 0.0896  0.0123  -0.0836 741  GLU A O   
5360  C CB  . GLU A 743  ? 0.2660 0.4209 0.2140 0.0926  0.0088  -0.0950 741  GLU A CB  
5361  C CG  . GLU A 743  ? 0.3130 0.4741 0.2579 0.0899  0.0131  -0.0844 741  GLU A CG  
5362  C CD  . GLU A 743  ? 0.3202 0.5022 0.2620 0.0934  0.0156  -0.0854 741  GLU A CD  
5363  O OE1 . GLU A 743  ? 0.2835 0.4727 0.2276 0.0963  0.0130  -0.0928 741  GLU A OE1 
5364  O OE2 . GLU A 743  ? 0.3708 0.5594 0.3102 0.0911  0.0190  -0.0764 741  GLU A OE2 
5365  N N   . GLY A 744  ? 0.2624 0.4093 0.2038 0.0866  0.0075  -0.0874 742  GLY A N   
5366  C CA  . GLY A 744  ? 0.2779 0.4233 0.2155 0.0828  0.0088  -0.0793 742  GLY A CA  
5367  C C   . GLY A 744  ? 0.2777 0.4369 0.2107 0.0849  0.0085  -0.0817 742  GLY A C   
5368  O O   . GLY A 744  ? 0.2814 0.4489 0.2103 0.0831  0.0109  -0.0742 742  GLY A O   
5369  N N   . VAL A 745  ? 0.2588 0.4210 0.1929 0.0887  0.0054  -0.0923 743  VAL A N   
5370  C CA  . VAL A 745  ? 0.3089 0.4852 0.2395 0.0907  0.0047  -0.0951 743  VAL A CA  
5371  C C   . VAL A 745  ? 0.3091 0.5031 0.2380 0.0918  0.0070  -0.0915 743  VAL A C   
5372  O O   . VAL A 745  ? 0.3110 0.5166 0.2362 0.0910  0.0082  -0.0867 743  VAL A O   
5373  C CB  . VAL A 745  ? 0.3030 0.4762 0.2383 0.0932  -0.0002 -0.1058 743  VAL A CB  
5374  C CG1 . VAL A 745  ? 0.2914 0.4803 0.2253 0.0950  -0.0014 -0.1083 743  VAL A CG1 
5375  C CG2 . VAL A 745  ? 0.3107 0.4681 0.2472 0.0915  -0.0026 -0.1078 743  VAL A CG2 
5376  N N   . ARG A 746  ? 0.2876 0.4842 0.2196 0.0934  0.0076  -0.0936 744  ARG A N   
5377  C CA  . ARG A 746  ? 0.2788 0.4924 0.2094 0.0943  0.0098  -0.0898 744  ARG A CA  
5378  C C   . ARG A 746  ? 0.2725 0.4905 0.1987 0.0910  0.0138  -0.0778 744  ARG A C   
5379  O O   . ARG A 746  ? 0.3140 0.5466 0.2378 0.0907  0.0151  -0.0729 744  ARG A O   
5380  C CB  . ARG A 746  ? 0.2890 0.5033 0.2238 0.0964  0.0098  -0.0936 744  ARG A CB  
5381  C CG  . ARG A 746  ? 0.3034 0.5363 0.2374 0.0978  0.0115  -0.0912 744  ARG A CG  
5382  C CD  . ARG A 746  ? 0.3036 0.5364 0.2408 0.0989  0.0127  -0.0916 744  ARG A CD  
5383  N NE  . ARG A 746  ? 0.3132 0.5373 0.2491 0.0958  0.0160  -0.0834 744  ARG A NE  
5384  C CZ  . ARG A 746  ? 0.3303 0.5616 0.2629 0.0931  0.0195  -0.0731 744  ARG A CZ  
5385  N NH1 . ARG A 746  ? 0.3455 0.5926 0.2757 0.0930  0.0202  -0.0692 744  ARG A NH1 
5386  N NH2 . ARG A 746  ? 0.3164 0.5392 0.2487 0.0905  0.0222  -0.0663 744  ARG A NH2 
5387  N N   . ILE A 747  ? 0.2707 0.4763 0.1963 0.0885  0.0157  -0.0728 745  ILE A N   
5388  C CA  . ILE A 747  ? 0.2798 0.4877 0.2019 0.0850  0.0193  -0.0612 745  ILE A CA  
5389  C C   . ILE A 747  ? 0.2849 0.4958 0.2034 0.0832  0.0190  -0.0568 745  ILE A C   
5390  O O   . ILE A 747  ? 0.2631 0.4847 0.1795 0.0814  0.0210  -0.0483 745  ILE A O   
5391  C CB  . ILE A 747  ? 0.2700 0.4590 0.1963 0.0811  0.0195  -0.0560 745  ILE A CB  
5392  C CG1 . ILE A 747  ? 0.2518 0.4418 0.1811 0.0826  0.0207  -0.0576 745  ILE A CG1 
5393  C CG2 . ILE A 747  ? 0.2656 0.4513 0.1908 0.0762  0.0215  -0.0439 745  ILE A CG2 
5394  C CD1 . ILE A 747  ? 0.2894 0.4607 0.2230 0.0793  0.0204  -0.0547 745  ILE A CD1 
5395  N N   . LEU A 748  ? 0.2657 0.4660 0.1850 0.0829  0.0161  -0.0616 746  LEU A N   
5396  C CA  . LEU A 748  ? 0.2762 0.4791 0.1922 0.0813  0.0155  -0.0580 746  LEU A CA  
5397  C C   . LEU A 748  ? 0.2728 0.4945 0.1868 0.0835  0.0152  -0.0591 746  LEU A C   
5398  O O   . LEU A 748  ? 0.2898 0.5199 0.2013 0.0816  0.0163  -0.0514 746  LEU A O   
5399  C CB  . LEU A 748  ? 0.2649 0.4532 0.1829 0.0808  0.0121  -0.0638 746  LEU A CB  
5400  C CG  . LEU A 748  ? 0.2989 0.4674 0.2202 0.0762  0.0119  -0.0580 746  LEU A CG  
5401  C CD1 . LEU A 748  ? 0.3275 0.4820 0.2519 0.0763  0.0083  -0.0653 746  LEU A CD1 
5402  C CD2 . LEU A 748  ? 0.3222 0.4910 0.2414 0.0725  0.0133  -0.0478 746  LEU A CD2 
5403  N N   . ARG A 749  ? 0.2638 0.4916 0.1807 0.0869  0.0131  -0.0679 747  ARG A N   
5404  C CA  . ARG A 749  ? 0.2599 0.5054 0.1765 0.0887  0.0124  -0.0688 747  ARG A CA  
5405  C C   . ARG A 749  ? 0.2975 0.5565 0.2132 0.0876  0.0155  -0.0599 747  ARG A C   
5406  O O   . ARG A 749  ? 0.2932 0.5656 0.2074 0.0870  0.0160  -0.0548 747  ARG A O   
5407  C CB  . ARG A 749  ? 0.2889 0.5373 0.2092 0.0927  0.0092  -0.0806 747  ARG A CB  
5408  C CG  . ARG A 749  ? 0.3290 0.5686 0.2505 0.0938  0.0055  -0.0890 747  ARG A CG  
5409  C CD  . ARG A 749  ? 0.3967 0.6390 0.3229 0.0978  0.0021  -0.1004 747  ARG A CD  
5410  N NE  . ARG A 749  ? 0.3789 0.6166 0.3067 0.0989  -0.0017 -0.1078 747  ARG A NE  
5411  C CZ  . ARG A 749  ? 0.4103 0.6537 0.3421 0.1023  -0.0051 -0.1173 747  ARG A CZ  
5412  N NH1 . ARG A 749  ? 0.3394 0.5934 0.2736 0.1051  -0.0051 -0.1208 747  ARG A NH1 
5413  N NH2 . ARG A 749  ? 0.3596 0.5982 0.2931 0.1029  -0.0086 -0.1235 747  ARG A NH2 
5414  N N   . GLU A 750  ? 0.2754 0.5314 0.1928 0.0873  0.0174  -0.0578 748  GLU A N   
5415  C CA  . GLU A 750  ? 0.3169 0.5846 0.2341 0.0858  0.0203  -0.0486 748  GLU A CA  
5416  C C   . GLU A 750  ? 0.2740 0.5414 0.1888 0.0817  0.0222  -0.0369 748  GLU A C   
5417  O O   . GLU A 750  ? 0.2912 0.5722 0.2058 0.0805  0.0234  -0.0293 748  GLU A O   
5418  C CB  . GLU A 750  ? 0.2604 0.5226 0.1799 0.0857  0.0220  -0.0481 748  GLU A CB  
5419  C CG  . GLU A 750  ? 0.3386 0.6141 0.2588 0.0846  0.0246  -0.0397 748  GLU A CG  
5420  C CD  . GLU A 750  ? 0.3364 0.6053 0.2588 0.0839  0.0266  -0.0376 748  GLU A CD  
5421  O OE1 . GLU A 750  ? 0.4145 0.6725 0.3386 0.0857  0.0256  -0.0454 748  GLU A OE1 
5422  O OE2 . GLU A 750  ? 0.3674 0.6417 0.2903 0.0814  0.0291  -0.0280 748  GLU A OE2 
5423  N N   . ALA A 751  ? 0.2568 0.5090 0.1702 0.0796  0.0222  -0.0353 749  ALA A N   
5424  C CA  . ALA A 751  ? 0.2615 0.5114 0.1731 0.0758  0.0237  -0.0246 749  ALA A CA  
5425  C C   . ALA A 751  ? 0.2866 0.5451 0.1963 0.0756  0.0222  -0.0230 749  ALA A C   
5426  O O   . ALA A 751  ? 0.3094 0.5682 0.2183 0.0725  0.0231  -0.0136 749  ALA A O   
5427  C CB  . ALA A 751  ? 0.2640 0.4951 0.1749 0.0740  0.0238  -0.0245 749  ALA A CB  
5428  N N   . GLY A 752  ? 0.2563 0.5217 0.1660 0.0788  0.0199  -0.0318 750  GLY A N   
5429  C CA  . GLY A 752  ? 0.2787 0.5547 0.1870 0.0789  0.0185  -0.0307 750  GLY A CA  
5430  C C   . GLY A 752  ? 0.2945 0.5635 0.2014 0.0803  0.0157  -0.0388 750  GLY A C   
5431  O O   . GLY A 752  ? 0.2852 0.5631 0.1910 0.0806  0.0144  -0.0385 750  GLY A O   
5432  N N   . ILE A 753  ? 0.2950 0.5486 0.2024 0.0811  0.0144  -0.0460 751  ILE A N   
5433  C CA  . ILE A 753  ? 0.3053 0.5525 0.2124 0.0825  0.0113  -0.0544 751  ILE A CA  
5434  C C   . ILE A 753  ? 0.3211 0.5800 0.2302 0.0862  0.0089  -0.0635 751  ILE A C   
5435  O O   . ILE A 753  ? 0.2933 0.5538 0.2051 0.0886  0.0087  -0.0690 751  ILE A O   
5436  C CB  . ILE A 753  ? 0.2645 0.4929 0.1727 0.0824  0.0102  -0.0601 751  ILE A CB  
5437  C CG1 . ILE A 753  ? 0.2787 0.4962 0.1851 0.0789  0.0126  -0.0513 751  ILE A CG1 
5438  C CG2 . ILE A 753  ? 0.3428 0.5650 0.2514 0.0835  0.0067  -0.0681 751  ILE A CG2 
5439  C CD1 . ILE A 753  ? 0.2415 0.4557 0.1465 0.0759  0.0120  -0.0449 751  ILE A CD1 
5440  N N   . PRO A 754  ? 0.3218 0.5891 0.2300 0.0871  0.0071  -0.0654 752  PRO A N   
5441  C CA  . PRO A 754  ? 0.3260 0.6051 0.2363 0.0909  0.0048  -0.0742 752  PRO A CA  
5442  C C   . PRO A 754  ? 0.3097 0.5778 0.2235 0.0934  0.0018  -0.0860 752  PRO A C   
5443  O O   . PRO A 754  ? 0.2791 0.5309 0.1932 0.0922  0.0006  -0.0883 752  PRO A O   
5444  C CB  . PRO A 754  ? 0.3494 0.6368 0.2579 0.0907  0.0035  -0.0732 752  PRO A CB  
5445  C CG  . PRO A 754  ? 0.3442 0.6291 0.2496 0.0867  0.0059  -0.0613 752  PRO A CG  
5446  C CD  . PRO A 754  ? 0.2975 0.5651 0.2027 0.0846  0.0072  -0.0590 752  PRO A CD  
5447  N N   . ALA A 755  ? 0.3353 0.6127 0.2523 0.0969  0.0003  -0.0934 753  ALA A N   
5448  C CA  . ALA A 755  ? 0.3154 0.5838 0.2369 0.0995  -0.0031 -0.1049 753  ALA A CA  
5449  C C   . ALA A 755  ? 0.3256 0.5871 0.2479 0.0996  -0.0065 -0.1104 753  ALA A C   
5450  O O   . ALA A 755  ? 0.3134 0.5603 0.2390 0.0999  -0.0090 -0.1168 753  ALA A O   
5451  C CB  . ALA A 755  ? 0.3575 0.6400 0.2824 0.1034  -0.0044 -0.1117 753  ALA A CB  
5452  N N   . SER A 756  ? 0.3173 0.5888 0.2367 0.0993  -0.0066 -0.1078 754  SER A N   
5453  C CA  . SER A 756  ? 0.3217 0.5869 0.2417 0.0992  -0.0097 -0.1126 754  SER A CA  
5454  C C   . SER A 756  ? 0.3126 0.5607 0.2305 0.0957  -0.0092 -0.1080 754  SER A C   
5455  O O   . SER A 756  ? 0.3283 0.5660 0.2481 0.0956  -0.0122 -0.1135 754  SER A O   
5456  C CB  . SER A 756  ? 0.3170 0.5985 0.2347 0.0998  -0.0099 -0.1108 754  SER A CB  
5457  O OG  . SER A 756  ? 0.3489 0.6351 0.2619 0.0968  -0.0065 -0.0991 754  SER A OG  
5458  N N   . ALA A 757  ? 0.3113 0.5563 0.2258 0.0928  -0.0056 -0.0983 755  ALA A N   
5459  C CA  . ALA A 757  ? 0.2793 0.5090 0.1918 0.0895  -0.0050 -0.0937 755  ALA A CA  
5460  C C   . ALA A 757  ? 0.2840 0.4972 0.1993 0.0892  -0.0054 -0.0971 755  ALA A C   
5461  O O   . ALA A 757  ? 0.2953 0.4944 0.2100 0.0871  -0.0059 -0.0959 755  ALA A O   
5462  C CB  . ALA A 757  ? 0.2971 0.5309 0.2050 0.0865  -0.0012 -0.0812 755  ALA A CB  
5463  N N   . LEU A 758  ? 0.2776 0.4924 0.1963 0.0913  -0.0053 -0.1011 756  LEU A N   
5464  C CA  . LEU A 758  ? 0.2750 0.4749 0.1969 0.0910  -0.0056 -0.1039 756  LEU A CA  
5465  C C   . LEU A 758  ? 0.3003 0.5021 0.2280 0.0945  -0.0083 -0.1135 756  LEU A C   
5466  O O   . LEU A 758  ? 0.3132 0.5259 0.2414 0.0963  -0.0069 -0.1134 756  LEU A O   
5467  C CB  . LEU A 758  ? 0.3157 0.5145 0.2351 0.0891  -0.0014 -0.0952 756  LEU A CB  
5468  C CG  . LEU A 758  ? 0.2912 0.4756 0.2138 0.0888  -0.0013 -0.0972 756  LEU A CG  
5469  C CD1 . LEU A 758  ? 0.2757 0.4430 0.2002 0.0875  -0.0039 -0.1008 756  LEU A CD1 
5470  C CD2 . LEU A 758  ? 0.3256 0.5098 0.2451 0.0866  0.0031  -0.0877 756  LEU A CD2 
5471  N N   . GLN A 759  ? 0.2875 0.4788 0.2199 0.0953  -0.0123 -0.1215 757  GLN A N   
5472  C CA  . GLN A 759  ? 0.3203 0.5112 0.2593 0.0984  -0.0156 -0.1309 757  GLN A CA  
5473  C C   . GLN A 759  ? 0.3065 0.4798 0.2502 0.0975  -0.0169 -0.1331 757  GLN A C   
5474  O O   . GLN A 759  ? 0.3408 0.5005 0.2844 0.0949  -0.0175 -0.1313 757  GLN A O   
5475  C CB  . GLN A 759  ? 0.2851 0.4791 0.2273 0.1002  -0.0199 -0.1387 757  GLN A CB  
5476  C CG  . GLN A 759  ? 0.3284 0.5409 0.2667 0.1015  -0.0190 -0.1373 757  GLN A CG  
5477  C CD  . GLN A 759  ? 0.3243 0.5392 0.2655 0.1030  -0.0231 -0.1446 757  GLN A CD  
5478  O OE1 . GLN A 759  ? 0.3131 0.5347 0.2591 0.1064  -0.0260 -0.1526 757  GLN A OE1 
5479  N NE2 . GLN A 759  ? 0.3024 0.5119 0.2410 0.1007  -0.0236 -0.1419 757  GLN A NE2 
5480  N N   . LEU A 760  ? 0.2821 0.4561 0.2299 0.0995  -0.0172 -0.1366 758  LEU A N   
5481  C CA  . LEU A 760  ? 0.3141 0.4725 0.2672 0.0988  -0.0185 -0.1385 758  LEU A CA  
5482  C C   . LEU A 760  ? 0.3181 0.4717 0.2796 0.1010  -0.0239 -0.1483 758  LEU A C   
5483  O O   . LEU A 760  ? 0.3267 0.4914 0.2908 0.1042  -0.0255 -0.1540 758  LEU A O   
5484  C CB  . LEU A 760  ? 0.2927 0.4543 0.2454 0.0994  -0.0153 -0.1354 758  LEU A CB  
5485  C CG  . LEU A 760  ? 0.3068 0.4535 0.2651 0.0990  -0.0165 -0.1371 758  LEU A CG  
5486  C CD1 . LEU A 760  ? 0.3097 0.4439 0.2651 0.0955  -0.0141 -0.1301 758  LEU A CD1 
5487  C CD2 . LEU A 760  ? 0.3149 0.4686 0.2750 0.1011  -0.0151 -0.1378 758  LEU A CD2 
5488  N N   . LEU A 761  ? 0.3071 0.4445 0.2731 0.0993  -0.0268 -0.1502 759  LEU A N   
5489  C CA  . LEU A 761  ? 0.3325 0.4640 0.3074 0.1008  -0.0324 -0.1588 759  LEU A CA  
5490  C C   . LEU A 761  ? 0.3283 0.4440 0.3096 0.0996  -0.0339 -0.1590 759  LEU A C   
5491  O O   . LEU A 761  ? 0.3182 0.4197 0.3016 0.0968  -0.0355 -0.1573 759  LEU A O   
5492  C CB  . LEU A 761  ? 0.3326 0.4603 0.3084 0.0997  -0.0354 -0.1610 759  LEU A CB  
5493  C CG  . LEU A 761  ? 0.3367 0.4788 0.3073 0.1008  -0.0348 -0.1614 759  LEU A CG  
5494  C CD1 . LEU A 761  ? 0.3239 0.4829 0.2953 0.1048  -0.0350 -0.1662 759  LEU A CD1 
5495  C CD2 . LEU A 761  ? 0.3631 0.5084 0.3243 0.0982  -0.0302 -0.1524 759  LEU A CD2 
5496  N N   . PRO A 762  ? 0.3171 0.4349 0.3016 0.1015  -0.0336 -0.1607 760  PRO A N   
5497  C CA  . PRO A 762  ? 0.3379 0.4410 0.3292 0.1004  -0.0354 -0.1609 760  PRO A CA  
5498  C C   . PRO A 762  ? 0.3566 0.4505 0.3576 0.1006  -0.0415 -0.1674 760  PRO A C   
5499  O O   . PRO A 762  ? 0.3734 0.4744 0.3772 0.1028  -0.0446 -0.1736 760  PRO A O   
5500  C CB  . PRO A 762  ? 0.3094 0.4202 0.3019 0.1031  -0.0339 -0.1623 760  PRO A CB  
5501  C CG  . PRO A 762  ? 0.3193 0.4475 0.3035 0.1044  -0.0298 -0.1597 760  PRO A CG  
5502  C CD  . PRO A 762  ? 0.2938 0.4278 0.2756 0.1045  -0.0313 -0.1617 760  PRO A CD  
5503  N N   . GLY A 763  ? 0.3104 0.3885 0.3168 0.0982  -0.0434 -0.1656 761  GLY A N   
5504  C CA  . GLY A 763  ? 0.3385 0.4069 0.3553 0.0979  -0.0493 -0.1706 761  GLY A CA  
5505  C C   . GLY A 763  ? 0.3566 0.4084 0.3758 0.0938  -0.0504 -0.1657 761  GLY A C   
5506  O O   . GLY A 763  ? 0.3338 0.3816 0.3468 0.0913  -0.0465 -0.1590 761  GLY A O   
5507  N N   . ASP A 764  ? 0.3731 0.4158 0.4020 0.0929  -0.0559 -0.1691 762  ASP A N   
5508  C CA  . ASP A 764  ? 0.3817 0.4085 0.4149 0.0888  -0.0577 -0.1646 762  ASP A CA  
5509  C C   . ASP A 764  ? 0.3861 0.4108 0.4164 0.0866  -0.0584 -0.1634 762  ASP A C   
5510  O O   . ASP A 764  ? 0.3593 0.3945 0.3822 0.0878  -0.0563 -0.1644 762  ASP A O   
5511  C CB  . ASP A 764  ? 0.3785 0.3964 0.4245 0.0887  -0.0634 -0.1677 762  ASP A CB  
5512  C CG  . ASP A 764  ? 0.4294 0.4522 0.4822 0.0912  -0.0684 -0.1756 762  ASP A CG  
5513  O OD1 . ASP A 764  ? 0.4335 0.4604 0.4833 0.0911  -0.0689 -0.1773 762  ASP A OD1 
5514  O OD2 . ASP A 764  ? 0.5027 0.5252 0.5643 0.0932  -0.0720 -0.1802 762  ASP A OD2 
5515  N N   . GLY A 765  ? 0.3538 0.3652 0.3900 0.0830  -0.0616 -0.1608 763  GLY A N   
5516  C CA  . GLY A 765  ? 0.3313 0.3396 0.3652 0.0805  -0.0623 -0.1591 763  GLY A CA  
5517  C C   . GLY A 765  ? 0.3549 0.3712 0.3902 0.0825  -0.0652 -0.1654 763  GLY A C   
5518  O O   . GLY A 765  ? 0.3769 0.3951 0.4072 0.0813  -0.0645 -0.1643 763  GLY A O   
5519  N N   . ARG A 766  ? 0.3872 0.4085 0.4294 0.0857  -0.0686 -0.1722 764  ARG A N   
5520  C CA  . ARG A 766  ? 0.3849 0.4152 0.4286 0.0882  -0.0713 -0.1788 764  ARG A CA  
5521  C C   . ARG A 766  ? 0.3581 0.4030 0.3904 0.0903  -0.0668 -0.1790 764  ARG A C   
5522  O O   . ARG A 766  ? 0.3499 0.4003 0.3797 0.0906  -0.0676 -0.1811 764  ARG A O   
5523  C CB  . ARG A 766  ? 0.4337 0.4676 0.4868 0.0917  -0.0756 -0.1862 764  ARG A CB  
5524  C CG  . ARG A 766  ? 0.5106 0.5319 0.5766 0.0900  -0.0811 -0.1870 764  ARG A CG  
5525  C CD  . ARG A 766  ? 0.5277 0.5542 0.6018 0.0940  -0.0845 -0.1941 764  ARG A CD  
5526  N NE  . ARG A 766  ? 0.5179 0.5486 0.5881 0.0957  -0.0808 -0.1929 764  ARG A NE  
5527  C CZ  . ARG A 766  ? 0.5221 0.5631 0.5939 0.1000  -0.0813 -0.1990 764  ARG A CZ  
5528  N NH1 . ARG A 766  ? 0.5790 0.6279 0.6560 0.1033  -0.0852 -0.2070 764  ARG A NH1 
5529  N NH2 . ARG A 766  ? 0.5696 0.6134 0.6381 0.1011  -0.0779 -0.1971 764  ARG A NH2 
5530  N N   . VAL A 767  ? 0.3379 0.3898 0.3637 0.0919  -0.0622 -0.1769 765  VAL A N   
5531  C CA  . VAL A 767  ? 0.3676 0.4337 0.3828 0.0935  -0.0577 -0.1757 765  VAL A CA  
5532  C C   . VAL A 767  ? 0.3418 0.4044 0.3492 0.0901  -0.0548 -0.1692 765  VAL A C   
5533  O O   . VAL A 767  ? 0.3230 0.3943 0.3245 0.0905  -0.0537 -0.1693 765  VAL A O   
5534  C CB  . VAL A 767  ? 0.3462 0.4203 0.3570 0.0956  -0.0536 -0.1741 765  VAL A CB  
5535  C CG1 . VAL A 767  ? 0.3227 0.4130 0.3235 0.0972  -0.0494 -0.1727 765  VAL A CG1 
5536  C CG2 . VAL A 767  ? 0.3834 0.4597 0.4026 0.0987  -0.0569 -0.1806 765  VAL A CG2 
5537  N N   . GLY A 768  ? 0.3404 0.3903 0.3478 0.0868  -0.0537 -0.1634 766  GLY A N   
5538  C CA  . GLY A 768  ? 0.2959 0.3414 0.2970 0.0836  -0.0515 -0.1577 766  GLY A CA  
5539  C C   . GLY A 768  ? 0.3158 0.3590 0.3198 0.0823  -0.0553 -0.1603 766  GLY A C   
5540  O O   . GLY A 768  ? 0.3153 0.3645 0.3124 0.0819  -0.0536 -0.1587 766  GLY A O   
5541  N N   . ALA A 769  ? 0.3242 0.3590 0.3388 0.0818  -0.0607 -0.1641 767  ALA A N   
5542  C CA  . ALA A 769  ? 0.3329 0.3645 0.3515 0.0803  -0.0646 -0.1664 767  ALA A CA  
5543  C C   . ALA A 769  ? 0.3344 0.3800 0.3501 0.0835  -0.0651 -0.1718 767  ALA A C   
5544  O O   . ALA A 769  ? 0.3535 0.4012 0.3661 0.0824  -0.0655 -0.1714 767  ALA A O   
5545  C CB  . ALA A 769  ? 0.3297 0.3503 0.3613 0.0792  -0.0704 -0.1691 767  ALA A CB  
5546  N N   . ALA A 770  ? 0.3384 0.3942 0.3552 0.0875  -0.0651 -0.1767 768  ALA A N   
5547  C CA  . ALA A 770  ? 0.3566 0.4269 0.3709 0.0907  -0.0656 -0.1819 768  ALA A CA  
5548  C C   . ALA A 770  ? 0.3346 0.4150 0.3368 0.0904  -0.0606 -0.1773 768  ALA A C   
5549  O O   . ALA A 770  ? 0.3360 0.4246 0.3354 0.0913  -0.0612 -0.1792 768  ALA A O   
5550  C CB  . ALA A 770  ? 0.3320 0.4117 0.3500 0.0950  -0.0664 -0.1879 768  ALA A CB  
5551  N N   . LEU A 771  ? 0.3117 0.3917 0.3071 0.0893  -0.0557 -0.1709 769  LEU A N   
5552  C CA  . LEU A 771  ? 0.3146 0.4033 0.2990 0.0886  -0.0510 -0.1653 769  LEU A CA  
5553  C C   . LEU A 771  ? 0.3457 0.4271 0.3275 0.0852  -0.0515 -0.1616 769  LEU A C   
5554  O O   . LEU A 771  ? 0.3413 0.4314 0.3175 0.0853  -0.0505 -0.1606 769  LEU A O   
5555  C CB  . LEU A 771  ? 0.3128 0.4017 0.2915 0.0882  -0.0460 -0.1592 769  LEU A CB  
5556  C CG  . LEU A 771  ? 0.3128 0.4115 0.2921 0.0916  -0.0446 -0.1617 769  LEU A CG  
5557  C CD1 . LEU A 771  ? 0.2960 0.3923 0.2710 0.0905  -0.0400 -0.1553 769  LEU A CD1 
5558  C CD2 . LEU A 771  ? 0.3475 0.4645 0.3222 0.0944  -0.0433 -0.1637 769  LEU A CD2 
5559  N N   . VAL A 772  ? 0.3248 0.3908 0.3111 0.0821  -0.0531 -0.1594 770  VAL A N   
5560  C CA  . VAL A 772  ? 0.3153 0.3740 0.3000 0.0786  -0.0539 -0.1560 770  VAL A CA  
5561  C C   . VAL A 772  ? 0.3371 0.3993 0.3250 0.0792  -0.0579 -0.1610 770  VAL A C   
5562  O O   . VAL A 772  ? 0.3755 0.4411 0.3581 0.0779  -0.0572 -0.1588 770  VAL A O   
5563  C CB  . VAL A 772  ? 0.3367 0.3786 0.3280 0.0747  -0.0553 -0.1517 770  VAL A CB  
5564  C CG1 . VAL A 772  ? 0.3179 0.3526 0.3105 0.0703  -0.0565 -0.1467 770  VAL A CG1 
5565  C CG2 . VAL A 772  ? 0.3261 0.3653 0.3139 0.0728  -0.0503 -0.1429 770  VAL A CG2 
5566  N N   . ALA A 773  ? 0.3692 0.4309 0.3662 0.0811  -0.0622 -0.1678 771  ALA A N   
5567  C CA  . ALA A 773  ? 0.3434 0.4071 0.3449 0.0815  -0.0665 -0.1728 771  ALA A CA  
5568  C C   . ALA A 773  ? 0.3865 0.4670 0.3823 0.0847  -0.0652 -0.1758 771  ALA A C   
5569  O O   . ALA A 773  ? 0.4197 0.5030 0.4177 0.0850  -0.0682 -0.1793 771  ALA A O   
5570  C CB  . ALA A 773  ? 0.3580 0.4154 0.3719 0.0825  -0.0718 -0.1789 771  ALA A CB  
5571  N N   . ALA A 774  ? 0.3968 0.4888 0.3858 0.0870  -0.0610 -0.1742 772  ALA A N   
5572  C CA  . ALA A 774  ? 0.3903 0.4993 0.3751 0.0902  -0.0600 -0.1772 772  ALA A CA  
5573  C C   . ALA A 774  ? 0.4007 0.5145 0.3782 0.0886  -0.0586 -0.1732 772  ALA A C   
5574  O O   . ALA A 774  ? 0.3442 0.4528 0.3161 0.0855  -0.0559 -0.1663 772  ALA A O   
5575  C CB  . ALA A 774  ? 0.3699 0.4902 0.3494 0.0927  -0.0558 -0.1754 772  ALA A CB  
5576  N N   . ALA A 775  ? 0.4131 0.5378 0.3910 0.0907  -0.0604 -0.1778 773  ALA A N   
5577  C CA  . ALA A 775  ? 0.4006 0.5283 0.3738 0.0891  -0.0604 -0.1752 773  ALA A CA  
5578  C C   . ALA A 775  ? 0.3420 0.4761 0.3044 0.0877  -0.0551 -0.1665 773  ALA A C   
5579  O O   . ALA A 775  ? 0.3802 0.5099 0.3387 0.0847  -0.0545 -0.1617 773  ALA A O   
5580  C CB  . ALA A 775  ? 0.4025 0.5426 0.3777 0.0922  -0.0629 -0.1817 773  ALA A CB  
5581  N N   . GLU A 776  ? 0.3649 0.5096 0.3227 0.0896  -0.0514 -0.1643 774  GLU A N   
5582  C CA  . GLU A 776  ? 0.3094 0.4622 0.2576 0.0885  -0.0465 -0.1558 774  GLU A CA  
5583  C C   . GLU A 776  ? 0.3259 0.4687 0.2708 0.0858  -0.0434 -0.1487 774  GLU A C   
5584  O O   . GLU A 776  ? 0.3290 0.4776 0.2665 0.0848  -0.0393 -0.1411 774  GLU A O   
5585  C CB  . GLU A 776  ? 0.3490 0.5196 0.2941 0.0918  -0.0440 -0.1560 774  GLU A CB  
5586  C CG  . GLU A 776  ? 0.3950 0.5776 0.3430 0.0949  -0.0468 -0.1632 774  GLU A CG  
5587  C CD  . GLU A 776  ? 0.4361 0.6171 0.3930 0.0979  -0.0505 -0.1727 774  GLU A CD  
5588  O OE1 . GLU A 776  ? 0.3691 0.5378 0.3306 0.0973  -0.0514 -0.1739 774  GLU A OE1 
5589  O OE2 . GLU A 776  ? 0.4526 0.6450 0.4121 0.1010  -0.0526 -0.1789 774  GLU A OE2 
5590  N N   . THR A 777  ? 0.3140 0.4421 0.2646 0.0846  -0.0452 -0.1508 775  THR A N   
5591  C CA  . THR A 777  ? 0.3234 0.4416 0.2712 0.0821  -0.0423 -0.1445 775  THR A CA  
5592  C C   . THR A 777  ? 0.3118 0.4248 0.2564 0.0782  -0.0412 -0.1367 775  THR A C   
5593  O O   . THR A 777  ? 0.3396 0.4455 0.2881 0.0764  -0.0445 -0.1385 775  THR A O   
5594  C CB  . THR A 777  ? 0.3184 0.4219 0.2744 0.0815  -0.0450 -0.1481 775  THR A CB  
5595  O OG1 . THR A 777  ? 0.3346 0.4433 0.2945 0.0845  -0.0452 -0.1527 775  THR A OG1 
5596  C CG2 . THR A 777  ? 0.2942 0.3860 0.2498 0.0774  -0.0418 -0.1385 775  THR A CG2 
5597  N N   . ALA A 778  ? 0.3062 0.4228 0.2451 0.0764  -0.0364 -0.1268 776  ALA A N   
5598  C CA  . ALA A 778  ? 0.2735 0.3873 0.2100 0.0727  -0.0348 -0.1179 776  ALA A CA  
5599  C C   . ALA A 778  ? 0.2735 0.3731 0.2125 0.0684  -0.0326 -0.1094 776  ALA A C   
5600  O O   . ALA A 778  ? 0.2796 0.3743 0.2183 0.0651  -0.0318 -0.1029 776  ALA A O   
5601  C CB  . ALA A 778  ? 0.2904 0.4191 0.2191 0.0736  -0.0314 -0.1124 776  ALA A CB  
5602  N N   . GLY A 779  ? 0.2706 0.3640 0.2123 0.0684  -0.0315 -0.1095 777  GLY A N   
5603  C CA  . GLY A 779  ? 0.2632 0.3437 0.2074 0.0645  -0.0296 -0.1020 777  GLY A CA  
5604  C C   . GLY A 779  ? 0.2442 0.3191 0.1923 0.0655  -0.0298 -0.1051 777  GLY A C   
5605  O O   . GLY A 779  ? 0.2820 0.3652 0.2291 0.0693  -0.0299 -0.1108 777  GLY A O   
5606  N N   . VAL A 780  ? 0.2700 0.3314 0.2226 0.0623  -0.0299 -0.1016 778  VAL A N   
5607  C CA  . VAL A 780  ? 0.2633 0.3182 0.2204 0.0629  -0.0304 -0.1039 778  VAL A CA  
5608  C C   . VAL A 780  ? 0.2563 0.3036 0.2128 0.0594  -0.0269 -0.0947 778  VAL A C   
5609  O O   . VAL A 780  ? 0.2552 0.2955 0.2124 0.0558  -0.0263 -0.0889 778  VAL A O   
5610  C CB  . VAL A 780  ? 0.2930 0.3383 0.2581 0.0626  -0.0354 -0.1103 778  VAL A CB  
5611  C CG1 . VAL A 780  ? 0.2630 0.3009 0.2330 0.0628  -0.0358 -0.1114 778  VAL A CG1 
5612  C CG2 . VAL A 780  ? 0.2847 0.3377 0.2508 0.0664  -0.0392 -0.1204 778  VAL A CG2 
5613  N N   . MET A 781  ? 0.2614 0.3109 0.2168 0.0606  -0.0244 -0.0935 779  MET A N   
5614  C CA  . MET A 781  ? 0.2514 0.2933 0.2071 0.0577  -0.0215 -0.0860 779  MET A CA  
5615  C C   . MET A 781  ? 0.2510 0.2857 0.2124 0.0583  -0.0233 -0.0898 779  MET A C   
5616  O O   . MET A 781  ? 0.2455 0.2860 0.2070 0.0617  -0.0235 -0.0948 779  MET A O   
5617  C CB  . MET A 781  ? 0.2564 0.3069 0.2063 0.0582  -0.0171 -0.0804 779  MET A CB  
5618  C CG  . MET A 781  ? 0.2682 0.3275 0.2129 0.0581  -0.0156 -0.0768 779  MET A CG  
5619  S SD  . MET A 781  ? 0.2646 0.3360 0.2035 0.0592  -0.0111 -0.0709 779  MET A SD  
5620  C CE  . MET A 781  ? 0.2239 0.2840 0.1643 0.0549  -0.0083 -0.0616 779  MET A CE  
5621  N N   . PHE A 782  ? 0.2668 0.2895 0.2332 0.0551  -0.0247 -0.0875 780  PHE A N   
5622  C CA  . PHE A 782  ? 0.2603 0.2749 0.2331 0.0551  -0.0270 -0.0904 780  PHE A CA  
5623  C C   . PHE A 782  ? 0.2592 0.2660 0.2326 0.0517  -0.0245 -0.0827 780  PHE A C   
5624  O O   . PHE A 782  ? 0.2481 0.2502 0.2207 0.0482  -0.0233 -0.0767 780  PHE A O   
5625  C CB  . PHE A 782  ? 0.2547 0.2619 0.2342 0.0542  -0.0319 -0.0948 780  PHE A CB  
5626  C CG  . PHE A 782  ? 0.2578 0.2558 0.2448 0.0537  -0.0346 -0.0966 780  PHE A CG  
5627  C CD1 . PHE A 782  ? 0.2745 0.2748 0.2652 0.0574  -0.0371 -0.1043 780  PHE A CD1 
5628  C CD2 . PHE A 782  ? 0.2451 0.2330 0.2356 0.0495  -0.0346 -0.0905 780  PHE A CD2 
5629  C CE1 . PHE A 782  ? 0.2732 0.2651 0.2714 0.0570  -0.0398 -0.1058 780  PHE A CE1 
5630  C CE2 . PHE A 782  ? 0.2778 0.2579 0.2755 0.0489  -0.0372 -0.0916 780  PHE A CE2 
5631  C CZ  . PHE A 782  ? 0.2554 0.2371 0.2571 0.0526  -0.0398 -0.0991 780  PHE A CZ  
5632  N N   . THR A 783  ? 0.2521 0.2577 0.2272 0.0529  -0.0238 -0.0834 781  THR A N   
5633  C CA  . THR A 783  ? 0.2803 0.2775 0.2577 0.0499  -0.0225 -0.0776 781  THR A CA  
5634  C C   . THR A 783  ? 0.2349 0.2265 0.2193 0.0510  -0.0258 -0.0824 781  THR A C   
5635  O O   . THR A 783  ? 0.2608 0.2574 0.2461 0.0548  -0.0268 -0.0884 781  THR A O   
5636  C CB  . THR A 783  ? 0.2515 0.2533 0.2237 0.0498  -0.0179 -0.0723 781  THR A CB  
5637  O OG1 . THR A 783  ? 0.2736 0.2810 0.2401 0.0490  -0.0153 -0.0682 781  THR A OG1 
5638  C CG2 . THR A 783  ? 0.2452 0.2384 0.2196 0.0466  -0.0166 -0.0664 781  THR A CG2 
5639  N N   . GLY A 784  ? 0.2627 0.2443 0.2525 0.0478  -0.0278 -0.0797 782  GLY A N   
5640  C CA  . GLY A 784  ? 0.2728 0.2482 0.2704 0.0485  -0.0317 -0.0839 782  GLY A CA  
5641  C C   . GLY A 784  ? 0.2649 0.2306 0.2681 0.0444  -0.0342 -0.0801 782  GLY A C   
5642  O O   . GLY A 784  ? 0.2932 0.2568 0.2936 0.0410  -0.0320 -0.0737 782  GLY A O   
5643  N N   . SER A 785  ? 0.2676 0.2276 0.2791 0.0448  -0.0388 -0.0842 783  SER A N   
5644  C CA  . SER A 785  ? 0.2723 0.2235 0.2901 0.0407  -0.0415 -0.0802 783  SER A CA  
5645  C C   . SER A 785  ? 0.3047 0.2557 0.3223 0.0388  -0.0429 -0.0798 783  SER A C   
5646  O O   . SER A 785  ? 0.2937 0.2499 0.3094 0.0412  -0.0439 -0.0852 783  SER A O   
5647  C CB  . SER A 785  ? 0.2986 0.2438 0.3263 0.0417  -0.0466 -0.0845 783  SER A CB  
5648  O OG  . SER A 785  ? 0.3150 0.2628 0.3461 0.0450  -0.0504 -0.0932 783  SER A OG  
5649  N N   . THR A 786  ? 0.2946 0.2400 0.3143 0.0343  -0.0430 -0.0734 784  THR A N   
5650  C CA  . THR A 786  ? 0.3194 0.2641 0.3398 0.0321  -0.0445 -0.0725 784  THR A CA  
5651  C C   . THR A 786  ? 0.2977 0.2405 0.3255 0.0335  -0.0502 -0.0794 784  THR A C   
5652  O O   . THR A 786  ? 0.2960 0.2419 0.3227 0.0341  -0.0514 -0.0824 784  THR A O   
5653  C CB  . THR A 786  ? 0.3281 0.2677 0.3506 0.0272  -0.0439 -0.0645 784  THR A CB  
5654  O OG1 . THR A 786  ? 0.3055 0.2471 0.3214 0.0263  -0.0388 -0.0589 784  THR A OG1 
5655  C CG2 . THR A 786  ? 0.3369 0.2766 0.3596 0.0248  -0.0449 -0.0630 784  THR A CG2 
5656  N N   . GLU A 787  ? 0.3611 0.2988 0.3971 0.0342  -0.0540 -0.0822 785  GLU A N   
5657  C CA  . GLU A 787  ? 0.3315 0.2664 0.3762 0.0355  -0.0600 -0.0890 785  GLU A CA  
5658  C C   . GLU A 787  ? 0.3035 0.2456 0.3450 0.0405  -0.0607 -0.0980 785  GLU A C   
5659  O O   . GLU A 787  ? 0.3106 0.2536 0.3551 0.0412  -0.0642 -0.1030 785  GLU A O   
5660  C CB  . GLU A 787  ? 0.3641 0.2922 0.4185 0.0355  -0.0639 -0.0899 785  GLU A CB  
5661  C CG  . GLU A 787  ? 0.4422 0.3632 0.5013 0.0305  -0.0644 -0.0811 785  GLU A CG  
5662  C CD  . GLU A 787  ? 0.4358 0.3588 0.4868 0.0286  -0.0584 -0.0735 785  GLU A CD  
5663  O OE1 . GLU A 787  ? 0.4301 0.3576 0.4747 0.0315  -0.0548 -0.0751 785  GLU A OE1 
5664  O OE2 . GLU A 787  ? 0.5425 0.4630 0.5938 0.0242  -0.0573 -0.0659 785  GLU A OE2 
5665  N N   . VAL A 788  ? 0.3142 0.2624 0.3499 0.0440  -0.0574 -0.1004 786  VAL A N   
5666  C CA  . VAL A 788  ? 0.3034 0.2601 0.3354 0.0487  -0.0576 -0.1087 786  VAL A CA  
5667  C C   . VAL A 788  ? 0.2866 0.2497 0.3107 0.0481  -0.0549 -0.1070 786  VAL A C   
5668  O O   . VAL A 788  ? 0.2945 0.2626 0.3183 0.0504  -0.0571 -0.1133 786  VAL A O   
5669  C CB  . VAL A 788  ? 0.2885 0.2509 0.3164 0.0525  -0.0547 -0.1111 786  VAL A CB  
5670  C CG1 . VAL A 788  ? 0.2929 0.2666 0.3152 0.0570  -0.0539 -0.1183 786  VAL A CG1 
5671  C CG2 . VAL A 788  ? 0.3423 0.2991 0.3795 0.0540  -0.0585 -0.1151 786  VAL A CG2 
5672  N N   . ALA A 789  ? 0.2755 0.2390 0.2933 0.0451  -0.0502 -0.0985 787  ALA A N   
5673  C CA  . ALA A 789  ? 0.2586 0.2276 0.2695 0.0444  -0.0478 -0.0964 787  ALA A CA  
5674  C C   . ALA A 789  ? 0.2805 0.2463 0.2963 0.0426  -0.0519 -0.0981 787  ALA A C   
5675  O O   . ALA A 789  ? 0.2808 0.2525 0.2933 0.0439  -0.0523 -0.1012 787  ALA A O   
5676  C CB  . ALA A 789  ? 0.2572 0.2255 0.2623 0.0411  -0.0428 -0.0870 787  ALA A CB  
5677  N N   . ARG A 790  ? 0.3088 0.2656 0.3328 0.0395  -0.0552 -0.0960 788  ARG A N   
5678  C CA  . ARG A 790  ? 0.2752 0.2287 0.3051 0.0374  -0.0595 -0.0972 788  ARG A CA  
5679  C C   . ARG A 790  ? 0.2621 0.2182 0.2962 0.0411  -0.0642 -0.1074 788  ARG A C   
5680  O O   . ARG A 790  ? 0.2970 0.2551 0.3318 0.0409  -0.0664 -0.1100 788  ARG A O   
5681  C CB  . ARG A 790  ? 0.3129 0.2569 0.3513 0.0333  -0.0620 -0.0922 788  ARG A CB  
5682  C CG  . ARG A 790  ? 0.3233 0.2636 0.3679 0.0301  -0.0659 -0.0913 788  ARG A CG  
5683  C CD  . ARG A 790  ? 0.3417 0.2739 0.3938 0.0255  -0.0676 -0.0844 788  ARG A CD  
5684  N NE  . ARG A 790  ? 0.3126 0.2453 0.3586 0.0225  -0.0625 -0.0756 788  ARG A NE  
5685  C CZ  . ARG A 790  ? 0.3325 0.2620 0.3789 0.0209  -0.0606 -0.0704 788  ARG A CZ  
5686  N NH1 . ARG A 790  ? 0.3447 0.2700 0.3974 0.0220  -0.0633 -0.0725 788  ARG A NH1 
5687  N NH2 . ARG A 790  ? 0.3355 0.2665 0.3761 0.0184  -0.0560 -0.0631 788  ARG A NH2 
5688  N N   . LEU A 791  ? 0.2803 0.2372 0.3173 0.0448  -0.0659 -0.1136 789  LEU A N   
5689  C CA  . LEU A 791  ? 0.2959 0.2567 0.3364 0.0490  -0.0702 -0.1243 789  LEU A CA  
5690  C C   . LEU A 791  ? 0.3263 0.2986 0.3571 0.0521  -0.0673 -0.1276 789  LEU A C   
5691  O O   . LEU A 791  ? 0.2929 0.2690 0.3249 0.0537  -0.0704 -0.1339 789  LEU A O   
5692  C CB  . LEU A 791  ? 0.3013 0.2607 0.3470 0.0525  -0.0723 -0.1302 789  LEU A CB  
5693  C CG  . LEU A 791  ? 0.3588 0.3070 0.4160 0.0500  -0.0765 -0.1283 789  LEU A CG  
5694  C CD1 . LEU A 791  ? 0.3606 0.3084 0.4213 0.0535  -0.0774 -0.1329 789  LEU A CD1 
5695  C CD2 . LEU A 791  ? 0.3569 0.3002 0.4240 0.0492  -0.0832 -0.1330 789  LEU A CD2 
5696  N N   . ILE A 792  ? 0.2820 0.2603 0.3036 0.0528  -0.0615 -0.1233 790  ILE A N   
5697  C CA  . ILE A 792  ? 0.2873 0.2770 0.2997 0.0553  -0.0586 -0.1251 790  ILE A CA  
5698  C C   . ILE A 792  ? 0.3116 0.3017 0.3215 0.0523  -0.0583 -0.1212 790  ILE A C   
5699  O O   . ILE A 792  ? 0.3212 0.3185 0.3285 0.0543  -0.0595 -0.1259 790  ILE A O   
5700  C CB  . ILE A 792  ? 0.2830 0.2786 0.2872 0.0562  -0.0527 -0.1204 790  ILE A CB  
5701  C CG1 . ILE A 792  ? 0.2882 0.2861 0.2944 0.0601  -0.0533 -0.1263 790  ILE A CG1 
5702  C CG2 . ILE A 792  ? 0.3056 0.3123 0.3004 0.0575  -0.0493 -0.1193 790  ILE A CG2 
5703  C CD1 . ILE A 792  ? 0.2827 0.2834 0.2831 0.0602  -0.0480 -0.1206 790  ILE A CD1 
5704  N N   . GLN A 793  ? 0.3102 0.2931 0.3209 0.0477  -0.0568 -0.1126 791  GLN A N   
5705  C CA  . GLN A 793  ? 0.3053 0.2880 0.3147 0.0447  -0.0567 -0.1088 791  GLN A CA  
5706  C C   . GLN A 793  ? 0.3045 0.2858 0.3206 0.0451  -0.0626 -0.1155 791  GLN A C   
5707  O O   . GLN A 793  ? 0.3272 0.3139 0.3402 0.0455  -0.0630 -0.1171 791  GLN A O   
5708  C CB  . GLN A 793  ? 0.3012 0.2758 0.3122 0.0398  -0.0549 -0.0995 791  GLN A CB  
5709  C CG  . GLN A 793  ? 0.2936 0.2671 0.3048 0.0364  -0.0552 -0.0954 791  GLN A CG  
5710  C CD  . GLN A 793  ? 0.3121 0.2771 0.3278 0.0317  -0.0551 -0.0880 791  GLN A CD  
5711  O OE1 . GLN A 793  ? 0.3472 0.3055 0.3699 0.0306  -0.0576 -0.0881 791  GLN A OE1 
5712  N NE2 . GLN A 793  ? 0.3522 0.3179 0.3641 0.0289  -0.0522 -0.0815 791  GLN A NE2 
5713  N N   . ALA A 794  ? 0.2887 0.2629 0.3144 0.0451  -0.0673 -0.1196 792  ALA A N   
5714  C CA  . ALA A 794  ? 0.3266 0.2990 0.3600 0.0455  -0.0734 -0.1263 792  ALA A CA  
5715  C C   . ALA A 794  ? 0.3225 0.3047 0.3528 0.0506  -0.0749 -0.1361 792  ALA A C   
5716  O O   . ALA A 794  ? 0.3395 0.3247 0.3708 0.0509  -0.0777 -0.1400 792  ALA A O   
5717  C CB  . ALA A 794  ? 0.3228 0.2856 0.3680 0.0446  -0.0784 -0.1285 792  ALA A CB  
5718  N N   . GLN A 795  ? 0.3320 0.3200 0.3586 0.0546  -0.0731 -0.1402 793  GLN A N   
5719  C CA  . GLN A 795  ? 0.3499 0.3489 0.3733 0.0597  -0.0743 -0.1497 793  GLN A CA  
5720  C C   . GLN A 795  ? 0.3675 0.3762 0.3810 0.0598  -0.0708 -0.1470 793  GLN A C   
5721  O O   . GLN A 795  ? 0.3889 0.4046 0.4018 0.0621  -0.0734 -0.1536 793  GLN A O   
5722  C CB  . GLN A 795  ? 0.3751 0.3791 0.3963 0.0639  -0.0725 -0.1538 793  GLN A CB  
5723  N N   . LEU A 796  ? 0.3411 0.3505 0.3475 0.0573  -0.0652 -0.1374 794  LEU A N   
5724  C CA  . LEU A 796  ? 0.3383 0.3566 0.3359 0.0572  -0.0619 -0.1339 794  LEU A CA  
5725  C C   . LEU A 796  ? 0.3532 0.3682 0.3531 0.0541  -0.0641 -0.1317 794  LEU A C   
5726  O O   . LEU A 796  ? 0.4090 0.4321 0.4033 0.0547  -0.0631 -0.1316 794  LEU A O   
5727  C CB  . LEU A 796  ? 0.3266 0.3460 0.3170 0.0556  -0.0556 -0.1244 794  LEU A CB  
5728  C CG  . LEU A 796  ? 0.3289 0.3549 0.3146 0.0588  -0.0524 -0.1254 794  LEU A CG  
5729  C CD1 . LEU A 796  ? 0.3324 0.3583 0.3119 0.0566  -0.0467 -0.1154 794  LEU A CD1 
5730  C CD2 . LEU A 796  ? 0.3820 0.4218 0.3628 0.0634  -0.0528 -0.1324 794  LEU A CD2 
5731  N N   . ALA A 797  ? 0.3646 0.3686 0.3727 0.0506  -0.0670 -0.1296 795  ALA A N   
5732  C CA  . ALA A 797  ? 0.3606 0.3616 0.3711 0.0473  -0.0689 -0.1270 795  ALA A CA  
5733  C C   . ALA A 797  ? 0.4254 0.4324 0.4377 0.0498  -0.0734 -0.1358 795  ALA A C   
5734  O O   . ALA A 797  ? 0.4894 0.4983 0.5005 0.0481  -0.0739 -0.1339 795  ALA A O   
5735  C CB  . ALA A 797  ? 0.4024 0.3912 0.4222 0.0431  -0.0716 -0.1233 795  ALA A CB  
5736  N N   . ASP A 798  ? 0.5102 0.5206 0.5253 0.0540  -0.0766 -0.1455 796  ASP A N   
5737  C CA  . ASP A 798  ? 0.5431 0.5608 0.5592 0.0571  -0.0807 -0.1549 796  ASP A CA  
5738  C C   . ASP A 798  ? 0.5386 0.5700 0.5439 0.0596  -0.0772 -0.1550 796  ASP A C   
5739  O O   . ASP A 798  ? 0.4945 0.5327 0.4992 0.0613  -0.0800 -0.1607 796  ASP A O   
5740  C CB  . ASP A 798  ? 0.4774 0.4962 0.4994 0.0612  -0.0846 -0.1650 796  ASP A CB  
5741  C CG  . ASP A 798  ? 0.6345 0.6407 0.6687 0.0590  -0.0886 -0.1649 796  ASP A CG  
5742  O OD1 . ASP A 798  ? 0.6868 0.6848 0.7271 0.0552  -0.0918 -0.1627 796  ASP A OD1 
5743  O OD2 . ASP A 798  ? 0.6405 0.6455 0.6784 0.0611  -0.0886 -0.1669 796  ASP A OD2 
5744  N N   . ARG A 799  ? 0.4036 0.4394 0.4007 0.0598  -0.0714 -0.1486 797  ARG A N   
5745  C CA  . ARG A 799  ? 0.4304 0.4804 0.4181 0.0633  -0.0683 -0.1500 797  ARG A CA  
5746  C C   . ARG A 799  ? 0.3906 0.4447 0.3711 0.0609  -0.0644 -0.1412 797  ARG A C   
5747  O O   . ARG A 799  ? 0.3770 0.4233 0.3576 0.0569  -0.0619 -0.1324 797  ARG A O   
5748  C CB  . ARG A 799  ? 0.4578 0.5110 0.4418 0.0656  -0.0646 -0.1492 797  ARG A CB  
5749  C CG  . ARG A 799  ? 0.4464 0.4930 0.4384 0.0673  -0.0680 -0.1559 797  ARG A CG  
5750  C CD  . ARG A 799  ? 0.4631 0.5194 0.4572 0.0718  -0.0708 -0.1654 797  ARG A CD  
5751  N NE  . ARG A 799  ? 0.4873 0.5583 0.4720 0.0747  -0.0665 -0.1646 797  ARG A NE  
5752  C CZ  . ARG A 799  ? 0.4255 0.5005 0.4064 0.0764  -0.0628 -0.1628 797  ARG A CZ  
5753  N NH1 . ARG A 799  ? 0.4494 0.5148 0.4347 0.0758  -0.0629 -0.1621 797  ARG A NH1 
5754  N NH2 . ARG A 799  ? 0.4904 0.5796 0.4632 0.0787  -0.0591 -0.1612 797  ARG A NH2 
5755  N N   . LEU A 800  ? 0.3773 0.4443 0.3517 0.0635  -0.0640 -0.1440 798  LEU A N   
5756  C CA  . LEU A 800  ? 0.3624 0.4356 0.3293 0.0621  -0.0601 -0.1359 798  LEU A CA  
5757  C C   . LEU A 800  ? 0.3635 0.4517 0.3221 0.0658  -0.0572 -0.1370 798  LEU A C   
5758  O O   . LEU A 800  ? 0.3813 0.4776 0.3398 0.0699  -0.0593 -0.1459 798  LEU A O   
5759  C CB  . LEU A 800  ? 0.4092 0.4834 0.3772 0.0606  -0.0629 -0.1364 798  LEU A CB  
5760  C CG  . LEU A 800  ? 0.3971 0.4579 0.3723 0.0561  -0.0649 -0.1329 798  LEU A CG  
5761  C CD1 . LEU A 800  ? 0.3778 0.4411 0.3550 0.0556  -0.0688 -0.1363 798  LEU A CD1 
5762  C CD2 . LEU A 800  ? 0.3714 0.4268 0.3438 0.0524  -0.0602 -0.1215 798  LEU A CD2 
5763  N N   . SER A 801  ? 0.3770 0.4693 0.3291 0.0645  -0.0525 -0.1278 799  SER A N   
5764  C CA  . SER A 801  ? 0.4016 0.5092 0.3459 0.0674  -0.0497 -0.1269 799  SER A CA  
5765  C C   . SER A 801  ? 0.4072 0.5263 0.3491 0.0695  -0.0524 -0.1322 799  SER A C   
5766  O O   . SER A 801  ? 0.4111 0.5253 0.3568 0.0680  -0.0559 -0.1344 799  SER A O   
5767  C CB  . SER A 801  ? 0.4060 0.5139 0.3453 0.0648  -0.0446 -0.1151 799  SER A CB  
5768  O OG  . SER A 801  ? 0.4168 0.5224 0.3561 0.0620  -0.0449 -0.1101 799  SER A OG  
5769  N N   . PRO A 802  ? 0.3802 0.5153 0.3156 0.0729  -0.0510 -0.1340 800  PRO A N   
5770  C CA  . PRO A 802  ? 0.4434 0.5905 0.3757 0.0746  -0.0533 -0.1377 800  PRO A CA  
5771  C C   . PRO A 802  ? 0.4465 0.5908 0.3777 0.0711  -0.0527 -0.1297 800  PRO A C   
5772  O O   . PRO A 802  ? 0.4967 0.6443 0.4288 0.0713  -0.0560 -0.1336 800  PRO A O   
5773  C CB  . PRO A 802  ? 0.4627 0.6260 0.3900 0.0773  -0.0497 -0.1353 800  PRO A CB  
5774  C CG  . PRO A 802  ? 0.4686 0.6289 0.3977 0.0787  -0.0481 -0.1371 800  PRO A CG  
5775  C CD  . PRO A 802  ? 0.4092 0.5529 0.3403 0.0756  -0.0479 -0.1338 800  PRO A CD  
5776  N N   . ALA A 803  ? 0.4410 0.5791 0.3708 0.0679  -0.0487 -0.1190 801  ALA A N   
5777  C CA  . ALA A 803  ? 0.4726 0.6060 0.4028 0.0644  -0.0483 -0.1115 801  ALA A CA  
5778  C C   . ALA A 803  ? 0.4637 0.5823 0.4013 0.0615  -0.0512 -0.1132 801  ALA A C   
5779  O O   . ALA A 803  ? 0.4601 0.5747 0.3986 0.0587  -0.0513 -0.1080 801  ALA A O   
5780  C CB  . ALA A 803  ? 0.4504 0.5816 0.3777 0.0621  -0.0433 -0.1000 801  ALA A CB  
5781  N N   . GLY A 804  ? 0.4671 0.5779 0.4103 0.0621  -0.0538 -0.1201 802  GLY A N   
5782  C CA  . GLY A 804  ? 0.4096 0.5067 0.3604 0.0591  -0.0568 -0.1212 802  GLY A CA  
5783  C C   . GLY A 804  ? 0.4186 0.5032 0.3719 0.0552  -0.0539 -0.1127 802  GLY A C   
5784  O O   . GLY A 804  ? 0.3889 0.4653 0.3463 0.0519  -0.0551 -0.1096 802  GLY A O   
5785  N N   . ARG A 805  ? 0.3789 0.4621 0.3299 0.0554  -0.0503 -0.1089 803  ARG A N   
5786  C CA  . ARG A 805  ? 0.3749 0.4473 0.3278 0.0520  -0.0473 -0.1010 803  ARG A CA  
5787  C C   . ARG A 805  ? 0.3252 0.3910 0.2813 0.0526  -0.0473 -0.1038 803  ARG A C   
5788  O O   . ARG A 805  ? 0.3469 0.4187 0.3020 0.0560  -0.0482 -0.1103 803  ARG A O   
5789  C CB  . ARG A 805  ? 0.3947 0.4720 0.3415 0.0514  -0.0425 -0.0920 803  ARG A CB  
5790  C CG  . ARG A 805  ? 0.4273 0.5104 0.3714 0.0506  -0.0425 -0.0881 803  ARG A CG  
5791  C CD  . ARG A 805  ? 0.4121 0.4859 0.3615 0.0473  -0.0446 -0.0868 803  ARG A CD  
5792  N NE  . ARG A 805  ? 0.3900 0.4694 0.3372 0.0466  -0.0447 -0.0834 803  ARG A NE  
5793  C CZ  . ARG A 805  ? 0.4180 0.5023 0.3659 0.0475  -0.0482 -0.0883 803  ARG A CZ  
5794  N NH1 . ARG A 805  ? 0.4520 0.5365 0.4030 0.0491  -0.0521 -0.0973 803  ARG A NH1 
5795  N NH2 . ARG A 805  ? 0.4543 0.5436 0.4002 0.0468  -0.0480 -0.0843 803  ARG A NH2 
5796  N N   . PRO A 806  ? 0.3431 0.3970 0.3032 0.0494  -0.0463 -0.0992 804  PRO A N   
5797  C CA  . PRO A 806  ? 0.3282 0.3756 0.2920 0.0498  -0.0465 -0.1016 804  PRO A CA  
5798  C C   . PRO A 806  ? 0.3324 0.3865 0.2910 0.0524  -0.0431 -0.1008 804  PRO A C   
5799  O O   . PRO A 806  ? 0.3064 0.3663 0.2592 0.0523  -0.0393 -0.0946 804  PRO A O   
5800  C CB  . PRO A 806  ? 0.3145 0.3501 0.2819 0.0455  -0.0451 -0.0945 804  PRO A CB  
5801  C CG  . PRO A 806  ? 0.3726 0.4070 0.3413 0.0431  -0.0464 -0.0921 804  PRO A CG  
5802  C CD  . PRO A 806  ? 0.3417 0.3880 0.3042 0.0453  -0.0456 -0.0925 804  PRO A CD  
5803  N N   . ILE A 807  ? 0.2928 0.3460 0.2539 0.0547  -0.0446 -0.1070 805  ILE A N   
5804  C CA  . ILE A 807  ? 0.2942 0.3530 0.2514 0.0571  -0.0415 -0.1066 805  ILE A CA  
5805  C C   . ILE A 807  ? 0.2896 0.3396 0.2474 0.0541  -0.0381 -0.0987 805  ILE A C   
5806  O O   . ILE A 807  ? 0.2897 0.3288 0.2534 0.0521  -0.0396 -0.0989 805  ILE A O   
5807  C CB  . ILE A 807  ? 0.2980 0.3585 0.2586 0.0606  -0.0444 -0.1162 805  ILE A CB  
5808  C CG1 . ILE A 807  ? 0.3289 0.3981 0.2895 0.0637  -0.0483 -0.1250 805  ILE A CG1 
5809  C CG2 . ILE A 807  ? 0.2957 0.3625 0.2522 0.0631  -0.0410 -0.1155 805  ILE A CG2 
5810  C CD1 . ILE A 807  ? 0.3303 0.4146 0.2828 0.0659  -0.0459 -0.1240 805  ILE A CD1 
5811  N N   . PRO A 808  ? 0.2878 0.3422 0.2401 0.0536  -0.0337 -0.0915 806  PRO A N   
5812  C CA  . PRO A 808  ? 0.2749 0.3210 0.2279 0.0508  -0.0306 -0.0842 806  PRO A CA  
5813  C C   . PRO A 808  ? 0.2681 0.3092 0.2243 0.0517  -0.0308 -0.0871 806  PRO A C   
5814  O O   . PRO A 808  ? 0.2738 0.3217 0.2288 0.0550  -0.0310 -0.0921 806  PRO A O   
5815  C CB  . PRO A 808  ? 0.2626 0.3169 0.2092 0.0511  -0.0264 -0.0777 806  PRO A CB  
5816  C CG  . PRO A 808  ? 0.2958 0.3603 0.2390 0.0526  -0.0275 -0.0793 806  PRO A CG  
5817  C CD  . PRO A 808  ? 0.2942 0.3615 0.2398 0.0554  -0.0316 -0.0894 806  PRO A CD  
5818  N N   . LEU A 809  ? 0.2722 0.3019 0.2328 0.0486  -0.0308 -0.0836 807  LEU A N   
5819  C CA  . LEU A 809  ? 0.2758 0.2995 0.2400 0.0487  -0.0309 -0.0849 807  LEU A CA  
5820  C C   . LEU A 809  ? 0.2624 0.2807 0.2254 0.0458  -0.0272 -0.0765 807  LEU A C   
5821  O O   . LEU A 809  ? 0.2647 0.2769 0.2290 0.0425  -0.0268 -0.0717 807  LEU A O   
5822  C CB  . LEU A 809  ? 0.2880 0.3027 0.2600 0.0476  -0.0354 -0.0893 807  LEU A CB  
5823  C CG  . LEU A 809  ? 0.2703 0.2772 0.2469 0.0470  -0.0356 -0.0892 807  LEU A CG  
5824  C CD1 . LEU A 809  ? 0.2693 0.2821 0.2448 0.0511  -0.0355 -0.0948 807  LEU A CD1 
5825  C CD2 . LEU A 809  ? 0.2890 0.2866 0.2738 0.0451  -0.0401 -0.0918 807  LEU A CD2 
5826  N N   . ILE A 810  ? 0.2445 0.2654 0.2052 0.0472  -0.0245 -0.0751 808  ILE A N   
5827  C CA  . ILE A 810  ? 0.2570 0.2717 0.2180 0.0447  -0.0217 -0.0687 808  ILE A CA  
5828  C C   . ILE A 810  ? 0.2561 0.2641 0.2223 0.0449  -0.0236 -0.0721 808  ILE A C   
5829  O O   . ILE A 810  ? 0.2547 0.2669 0.2213 0.0481  -0.0244 -0.0775 808  ILE A O   
5830  C CB  . ILE A 810  ? 0.2289 0.2505 0.1845 0.0457  -0.0176 -0.0643 808  ILE A CB  
5831  C CG1 . ILE A 810  ? 0.2480 0.2769 0.1990 0.0456  -0.0161 -0.0607 808  ILE A CG1 
5832  C CG2 . ILE A 810  ? 0.2418 0.2564 0.1982 0.0430  -0.0150 -0.0579 808  ILE A CG2 
5833  C CD1 . ILE A 810  ? 0.2654 0.3009 0.2120 0.0461  -0.0123 -0.0554 808  ILE A CD1 
5834  N N   . ALA A 811  ? 0.2374 0.2357 0.2080 0.0417  -0.0245 -0.0693 809  ALA A N   
5835  C CA  . ALA A 811  ? 0.2379 0.2293 0.2146 0.0416  -0.0269 -0.0720 809  ALA A CA  
5836  C C   . ALA A 811  ? 0.2473 0.2323 0.2247 0.0386  -0.0245 -0.0654 809  ALA A C   
5837  O O   . ALA A 811  ? 0.2603 0.2398 0.2394 0.0352  -0.0245 -0.0611 809  ALA A O   
5838  C CB  . ALA A 811  ? 0.2581 0.2442 0.2410 0.0406  -0.0315 -0.0759 809  ALA A CB  
5839  N N   . GLU A 812  ? 0.2308 0.2170 0.2068 0.0398  -0.0224 -0.0646 810  GLU A N   
5840  C CA  . GLU A 812  ? 0.2431 0.2244 0.2191 0.0373  -0.0199 -0.0586 810  GLU A CA  
5841  C C   . GLU A 812  ? 0.2428 0.2180 0.2246 0.0373  -0.0222 -0.0607 810  GLU A C   
5842  O O   . GLU A 812  ? 0.2542 0.2320 0.2370 0.0403  -0.0230 -0.0654 810  GLU A O   
5843  C CB  . GLU A 812  ? 0.2692 0.2566 0.2396 0.0385  -0.0158 -0.0554 810  GLU A CB  
5844  C CG  . GLU A 812  ? 0.2315 0.2250 0.1968 0.0385  -0.0139 -0.0529 810  GLU A CG  
5845  C CD  . GLU A 812  ? 0.2651 0.2538 0.2310 0.0351  -0.0135 -0.0480 810  GLU A CD  
5846  O OE1 . GLU A 812  ? 0.2701 0.2560 0.2353 0.0330  -0.0110 -0.0427 810  GLU A OE1 
5847  O OE2 . GLU A 812  ? 0.2598 0.2477 0.2271 0.0344  -0.0157 -0.0498 810  GLU A OE2 
5848  N N   . THR A 813  ? 0.2293 0.1970 0.2154 0.0340  -0.0234 -0.0575 811  THR A N   
5849  C CA  . THR A 813  ? 0.2549 0.2164 0.2480 0.0337  -0.0269 -0.0599 811  THR A CA  
5850  C C   . THR A 813  ? 0.2490 0.2050 0.2441 0.0309  -0.0257 -0.0544 811  THR A C   
5851  O O   . THR A 813  ? 0.2686 0.2265 0.2593 0.0305  -0.0219 -0.0503 811  THR A O   
5852  C CB  . THR A 813  ? 0.2459 0.2039 0.2442 0.0324  -0.0311 -0.0623 811  THR A CB  
5853  O OG1 . THR A 813  ? 0.2553 0.2127 0.2518 0.0292  -0.0298 -0.0574 811  THR A OG1 
5854  C CG2 . THR A 813  ? 0.2537 0.2173 0.2513 0.0359  -0.0330 -0.0695 811  THR A CG2 
5855  N N   . GLY A 814  ? 0.2452 0.1947 0.2472 0.0291  -0.0290 -0.0542 812  GLY A N   
5856  C CA  . GLY A 814  ? 0.2767 0.2218 0.2814 0.0272  -0.0285 -0.0500 812  GLY A CA  
5857  C C   . GLY A 814  ? 0.2759 0.2195 0.2781 0.0234  -0.0258 -0.0429 812  GLY A C   
5858  O O   . GLY A 814  ? 0.2638 0.2094 0.2629 0.0220  -0.0244 -0.0409 812  GLY A O   
5859  N N   . GLY A 815  ? 0.2467 0.1873 0.2507 0.0217  -0.0250 -0.0391 813  GLY A N   
5860  C CA  . GLY A 815  ? 0.2576 0.1973 0.2598 0.0183  -0.0227 -0.0327 813  GLY A CA  
5861  C C   . GLY A 815  ? 0.2538 0.1887 0.2620 0.0156  -0.0249 -0.0294 813  GLY A C   
5862  O O   . GLY A 815  ? 0.2693 0.2012 0.2827 0.0166  -0.0277 -0.0317 813  GLY A O   
5863  N N   . GLN A 816  ? 0.2509 0.1855 0.2585 0.0121  -0.0236 -0.0240 814  GLN A N   
5864  C CA  . GLN A 816  ? 0.2399 0.1714 0.2522 0.0092  -0.0250 -0.0196 814  GLN A CA  
5865  C C   . GLN A 816  ? 0.2320 0.1661 0.2393 0.0075  -0.0210 -0.0149 814  GLN A C   
5866  O O   . GLN A 816  ? 0.2513 0.1864 0.2585 0.0046  -0.0204 -0.0110 814  GLN A O   
5867  C CB  . GLN A 816  ? 0.2611 0.1903 0.2794 0.0063  -0.0285 -0.0179 814  GLN A CB  
5868  C CG  . GLN A 816  ? 0.2926 0.2188 0.3170 0.0034  -0.0307 -0.0133 814  GLN A CG  
5869  C CD  . GLN A 816  ? 0.3248 0.2473 0.3545 0.0052  -0.0336 -0.0159 814  GLN A CD  
5870  O OE1 . GLN A 816  ? 0.3152 0.2382 0.3423 0.0072  -0.0317 -0.0168 814  GLN A OE1 
5871  N NE2 . GLN A 816  ? 0.3292 0.2478 0.3669 0.0047  -0.0384 -0.0173 814  GLN A NE2 
5872  N N   . ASN A 817  ? 0.2261 0.1617 0.2294 0.0095  -0.0183 -0.0157 815  ASN A N   
5873  C CA  . ASN A 817  ? 0.1984 0.1371 0.1960 0.0089  -0.0143 -0.0130 815  ASN A CA  
5874  C C   . ASN A 817  ? 0.2414 0.1797 0.2401 0.0062  -0.0136 -0.0083 815  ASN A C   
5875  O O   . ASN A 817  ? 0.2314 0.1676 0.2330 0.0062  -0.0147 -0.0076 815  ASN A O   
5876  C CB  . ASN A 817  ? 0.2014 0.1424 0.1948 0.0121  -0.0119 -0.0155 815  ASN A CB  
5877  C CG  . ASN A 817  ? 0.2087 0.1511 0.2013 0.0150  -0.0130 -0.0204 815  ASN A CG  
5878  O OD1 . ASN A 817  ? 0.2231 0.1668 0.2145 0.0148  -0.0132 -0.0213 815  ASN A OD1 
5879  N ND2 . ASN A 817  ? 0.2206 0.1631 0.2141 0.0178  -0.0137 -0.0239 815  ASN A ND2 
5880  N N   . ALA A 818  ? 0.2137 0.1545 0.2100 0.0041  -0.0116 -0.0053 816  ALA A N   
5881  C CA  . ALA A 818  ? 0.2066 0.1483 0.2035 0.0015  -0.0109 -0.0009 816  ALA A CA  
5882  C C   . ALA A 818  ? 0.2063 0.1506 0.1983 0.0020  -0.0072 -0.0002 816  ALA A C   
5883  O O   . ALA A 818  ? 0.2077 0.1536 0.1960 0.0038  -0.0053 -0.0021 816  ALA A O   
5884  C CB  . ALA A 818  ? 0.2259 0.1693 0.2246 -0.0016 -0.0117 0.0019  816  ALA A CB  
5885  N N   . MET A 819  ? 0.2200 0.1650 0.2124 0.0005  -0.0066 0.0027  817  MET A N   
5886  C CA  . MET A 819  ? 0.2133 0.1611 0.2021 0.0003  -0.0036 0.0039  817  MET A CA  
5887  C C   . MET A 819  ? 0.2049 0.1555 0.1948 -0.0028 -0.0036 0.0075  817  MET A C   
5888  O O   . MET A 819  ? 0.2127 0.1626 0.2061 -0.0045 -0.0055 0.0100  817  MET A O   
5889  C CB  . MET A 819  ? 0.2181 0.1650 0.2059 0.0019  -0.0026 0.0034  817  MET A CB  
5890  C CG  . MET A 819  ? 0.2291 0.1787 0.2141 0.0014  0.0000  0.0047  817  MET A CG  
5891  S SD  . MET A 819  ? 0.2299 0.1786 0.2145 0.0028  0.0010  0.0047  817  MET A SD  
5892  C CE  . MET A 819  ? 0.2625 0.2102 0.2453 0.0062  0.0017  0.0012  817  MET A CE  
5893  N N   . ILE A 820  ? 0.2166 0.1708 0.2040 -0.0035 -0.0017 0.0079  818  ILE A N   
5894  C CA  . ILE A 820  ? 0.2020 0.1603 0.1898 -0.0061 -0.0013 0.0110  818  ILE A CA  
5895  C C   . ILE A 820  ? 0.2093 0.1699 0.1947 -0.0058 0.0009  0.0111  818  ILE A C   
5896  O O   . ILE A 820  ? 0.2112 0.1716 0.1939 -0.0040 0.0028  0.0089  818  ILE A O   
5897  C CB  . ILE A 820  ? 0.2326 0.1943 0.2199 -0.0071 -0.0009 0.0109  818  ILE A CB  
5898  C CG1 . ILE A 820  ? 0.2397 0.1994 0.2301 -0.0077 -0.0034 0.0111  818  ILE A CG1 
5899  C CG2 . ILE A 820  ? 0.2164 0.1838 0.2038 -0.0095 -0.0002 0.0136  818  ILE A CG2 
5900  C CD1 . ILE A 820  ? 0.2408 0.2040 0.2311 -0.0088 -0.0032 0.0113  818  ILE A CD1 
5901  N N   . VAL A 821  ? 0.2151 0.1778 0.2018 -0.0077 0.0004  0.0139  819  VAL A N   
5902  C CA  . VAL A 821  ? 0.2279 0.1928 0.2127 -0.0076 0.0020  0.0141  819  VAL A CA  
5903  C C   . VAL A 821  ? 0.2161 0.1874 0.2011 -0.0101 0.0023  0.0164  819  VAL A C   
5904  O O   . VAL A 821  ? 0.2524 0.2256 0.2400 -0.0123 0.0006  0.0197  819  VAL A O   
5905  C CB  . VAL A 821  ? 0.2261 0.1882 0.2123 -0.0073 0.0011  0.0151  819  VAL A CB  
5906  C CG1 . VAL A 821  ? 0.2398 0.2046 0.2243 -0.0073 0.0027  0.0153  819  VAL A CG1 
5907  C CG2 . VAL A 821  ? 0.2262 0.1831 0.2126 -0.0046 0.0008  0.0125  819  VAL A CG2 
5908  N N   . ASP A 822  ? 0.2232 0.1984 0.2058 -0.0097 0.0043  0.0148  820  ASP A N   
5909  C CA  . ASP A 822  ? 0.2241 0.2066 0.2066 -0.0117 0.0047  0.0165  820  ASP A CA  
5910  C C   . ASP A 822  ? 0.2305 0.2154 0.2119 -0.0118 0.0055  0.0166  820  ASP A C   
5911  O O   . ASP A 822  ? 0.2349 0.2156 0.2161 -0.0105 0.0057  0.0158  820  ASP A O   
5912  C CB  . ASP A 822  ? 0.2330 0.2193 0.2141 -0.0113 0.0061  0.0143  820  ASP A CB  
5913  C CG  . ASP A 822  ? 0.2288 0.2147 0.2080 -0.0091 0.0079  0.0105  820  ASP A CG  
5914  O OD1 . ASP A 822  ? 0.2298 0.2135 0.2084 -0.0081 0.0084  0.0097  820  ASP A OD1 
5915  O OD2 . ASP A 822  ? 0.2497 0.2374 0.2284 -0.0083 0.0087  0.0085  820  ASP A OD2 
5916  N N   . SER A 823  ? 0.2369 0.2294 0.2179 -0.0135 0.0060  0.0177  821  SER A N   
5917  C CA  . SER A 823  ? 0.2499 0.2459 0.2302 -0.0139 0.0064  0.0181  821  SER A CA  
5918  C C   . SER A 823  ? 0.2666 0.2620 0.2451 -0.0118 0.0081  0.0140  821  SER A C   
5919  O O   . SER A 823  ? 0.2840 0.2821 0.2620 -0.0120 0.0083  0.0138  821  SER A O   
5920  C CB  . SER A 823  ? 0.3014 0.3071 0.2818 -0.0164 0.0062  0.0206  821  SER A CB  
5921  O OG  . SER A 823  ? 0.2799 0.2909 0.2592 -0.0160 0.0075  0.0181  821  SER A OG  
5922  N N   . SER A 824  ? 0.2352 0.2275 0.2132 -0.0098 0.0090  0.0108  822  SER A N   
5923  C CA  . SER A 824  ? 0.2511 0.2420 0.2284 -0.0079 0.0102  0.0073  822  SER A CA  
5924  C C   . SER A 824  ? 0.2795 0.2631 0.2570 -0.0064 0.0101  0.0072  822  SER A C   
5925  O O   . SER A 824  ? 0.2782 0.2604 0.2556 -0.0050 0.0109  0.0051  822  SER A O   
5926  C CB  . SER A 824  ? 0.2688 0.2605 0.2460 -0.0066 0.0110  0.0042  822  SER A CB  
5927  O OG  . SER A 824  ? 0.2565 0.2427 0.2338 -0.0056 0.0108  0.0043  822  SER A OG  
5928  N N   . ALA A 825  ? 0.2556 0.2348 0.2335 -0.0065 0.0092  0.0092  823  ALA A N   
5929  C CA  . ALA A 825  ? 0.2290 0.2024 0.2071 -0.0048 0.0092  0.0088  823  ALA A CA  
5930  C C   . ALA A 825  ? 0.2536 0.2269 0.2321 -0.0051 0.0090  0.0098  823  ALA A C   
5931  O O   . ALA A 825  ? 0.2709 0.2481 0.2497 -0.0068 0.0085  0.0115  823  ALA A O   
5932  C CB  . ALA A 825  ? 0.2328 0.2022 0.2117 -0.0047 0.0080  0.0100  823  ALA A CB  
5933  N N   . LEU A 826  ? 0.2494 0.2189 0.2279 -0.0035 0.0095  0.0089  824  LEU A N   
5934  C CA  . LEU A 826  ? 0.2920 0.2612 0.2711 -0.0035 0.0094  0.0097  824  LEU A CA  
5935  C C   . LEU A 826  ? 0.2740 0.2400 0.2542 -0.0034 0.0082  0.0116  824  LEU A C   
5936  O O   . LEU A 826  ? 0.2768 0.2390 0.2571 -0.0019 0.0081  0.0109  824  LEU A O   
5937  C CB  . LEU A 826  ? 0.3308 0.2982 0.3099 -0.0019 0.0106  0.0080  824  LEU A CB  
5938  C CG  . LEU A 826  ? 0.3830 0.3503 0.3628 -0.0019 0.0105  0.0087  824  LEU A CG  
5939  C CD1 . LEU A 826  ? 0.4373 0.4094 0.4172 -0.0036 0.0101  0.0091  824  LEU A CD1 
5940  C CD2 . LEU A 826  ? 0.4787 0.4443 0.4591 -0.0005 0.0115  0.0073  824  LEU A CD2 
5941  N N   . ALA A 827  ? 0.2608 0.2286 0.2421 -0.0050 0.0070  0.0140  825  ALA A N   
5942  C CA  . ALA A 827  ? 0.2529 0.2179 0.2363 -0.0052 0.0053  0.0160  825  ALA A CA  
5943  C C   . ALA A 827  ? 0.2534 0.2141 0.2374 -0.0030 0.0055  0.0148  825  ALA A C   
5944  O O   . ALA A 827  ? 0.2506 0.2079 0.2358 -0.0019 0.0045  0.0143  825  ALA A O   
5945  C CB  . ALA A 827  ? 0.3097 0.2778 0.2946 -0.0073 0.0040  0.0192  825  ALA A CB  
5946  N N   . GLU A 828  ? 0.2551 0.2163 0.2384 -0.0022 0.0066  0.0141  826  GLU A N   
5947  C CA  . GLU A 828  ? 0.2645 0.2227 0.2485 -0.0002 0.0069  0.0132  826  GLU A CA  
5948  C C   . GLU A 828  ? 0.2877 0.2438 0.2706 0.0018  0.0077  0.0111  826  GLU A C   
5949  O O   . GLU A 828  ? 0.2674 0.2213 0.2512 0.0035  0.0073  0.0103  826  GLU A O   
5950  C CB  . GLU A 828  ? 0.3116 0.2713 0.2954 0.0001  0.0080  0.0130  826  GLU A CB  
5951  C CG  . GLU A 828  ? 0.3282 0.2897 0.3132 -0.0013 0.0071  0.0150  826  GLU A CG  
5952  C CD  . GLU A 828  ? 0.3783 0.3441 0.3625 -0.0035 0.0069  0.0159  826  GLU A CD  
5953  O OE1 . GLU A 828  ? 0.3864 0.3538 0.3693 -0.0039 0.0075  0.0148  826  GLU A OE1 
5954  O OE2 . GLU A 828  ? 0.4053 0.3737 0.3903 -0.0047 0.0062  0.0176  826  GLU A OE2 
5955  N N   . GLN A 829  ? 0.2744 0.2317 0.2557 0.0017  0.0088  0.0100  827  GLN A N   
5956  C CA  . GLN A 829  ? 0.2870 0.2428 0.2672 0.0033  0.0094  0.0084  827  GLN A CA  
5957  C C   . GLN A 829  ? 0.2493 0.2034 0.2301 0.0034  0.0080  0.0082  827  GLN A C   
5958  O O   . GLN A 829  ? 0.2589 0.2115 0.2398 0.0053  0.0078  0.0069  827  GLN A O   
5959  C CB  . GLN A 829  ? 0.3113 0.2688 0.2904 0.0029  0.0105  0.0076  827  GLN A CB  
5960  C CG  . GLN A 829  ? 0.4166 0.3746 0.3957 0.0037  0.0118  0.0071  827  GLN A CG  
5961  C CD  . GLN A 829  ? 0.4400 0.3990 0.4187 0.0036  0.0125  0.0060  827  GLN A CD  
5962  O OE1 . GLN A 829  ? 0.3945 0.3545 0.3727 0.0028  0.0121  0.0056  827  GLN A OE1 
5963  N NE2 . GLN A 829  ? 0.4608 0.4197 0.4403 0.0044  0.0133  0.0058  827  GLN A NE2 
5964  N N   . VAL A 830  ? 0.2429 0.1979 0.2244 0.0015  0.0069  0.0094  828  VAL A N   
5965  C CA  . VAL A 830  ? 0.2209 0.1743 0.2038 0.0013  0.0052  0.0094  828  VAL A CA  
5966  C C   . VAL A 830  ? 0.2399 0.1905 0.2251 0.0024  0.0036  0.0093  828  VAL A C   
5967  O O   . VAL A 830  ? 0.2227 0.1713 0.2086 0.0040  0.0028  0.0075  828  VAL A O   
5968  C CB  . VAL A 830  ? 0.2254 0.1810 0.2092 -0.0014 0.0041  0.0116  828  VAL A CB  
5969  C CG1 . VAL A 830  ? 0.2536 0.2071 0.2400 -0.0019 0.0018  0.0123  828  VAL A CG1 
5970  C CG2 . VAL A 830  ? 0.2775 0.2363 0.2593 -0.0021 0.0055  0.0110  828  VAL A CG2 
5971  N N   . VAL A 831  ? 0.2366 0.1875 0.2233 0.0018  0.0031  0.0109  829  VAL A N   
5972  C CA  . VAL A 831  ? 0.2273 0.1755 0.2170 0.0029  0.0013  0.0108  829  VAL A CA  
5973  C C   . VAL A 831  ? 0.2416 0.1887 0.2306 0.0059  0.0021  0.0079  829  VAL A C   
5974  O O   . VAL A 831  ? 0.2253 0.1704 0.2163 0.0075  0.0006  0.0061  829  VAL A O   
5975  C CB  . VAL A 831  ? 0.2650 0.2141 0.2565 0.0016  0.0007  0.0133  829  VAL A CB  
5976  C CG1 . VAL A 831  ? 0.2670 0.2135 0.2620 0.0032  -0.0011 0.0128  829  VAL A CG1 
5977  C CG2 . VAL A 831  ? 0.2851 0.2360 0.2781 -0.0013 -0.0008 0.0165  829  VAL A CG2 
5978  N N   . GLY A 832  ? 0.2260 0.1749 0.2124 0.0067  0.0044  0.0074  830  GLY A N   
5979  C CA  . GLY A 832  ? 0.2341 0.1833 0.2197 0.0095  0.0054  0.0051  830  GLY A CA  
5980  C C   . GLY A 832  ? 0.2226 0.1714 0.2072 0.0107  0.0052  0.0030  830  GLY A C   
5981  O O   . GLY A 832  ? 0.2191 0.1676 0.2044 0.0129  0.0045  0.0007  830  GLY A O   
5982  N N   . ASP A 833  ? 0.2205 0.1698 0.2035 0.0094  0.0056  0.0034  831  ASP A N   
5983  C CA  . ASP A 833  ? 0.2129 0.1620 0.1949 0.0105  0.0054  0.0014  831  ASP A CA  
5984  C C   . ASP A 833  ? 0.2184 0.1651 0.2030 0.0105  0.0027  0.0003  831  ASP A C   
5985  O O   . ASP A 833  ? 0.2306 0.1772 0.2152 0.0123  0.0020  -0.0023 831  ASP A O   
5986  C CB  . ASP A 833  ? 0.2270 0.1772 0.2069 0.0091  0.0064  0.0022  831  ASP A CB  
5987  C CG  . ASP A 833  ? 0.2309 0.1831 0.2089 0.0096  0.0087  0.0027  831  ASP A CG  
5988  O OD1 . ASP A 833  ? 0.2450 0.1981 0.2228 0.0111  0.0095  0.0025  831  ASP A OD1 
5989  O OD2 . ASP A 833  ? 0.2322 0.1853 0.2093 0.0084  0.0094  0.0034  831  ASP A OD2 
5990  N N   . VAL A 834  ? 0.2114 0.1567 0.1987 0.0085  0.0011  0.0023  832  VAL A N   
5991  C CA  . VAL A 834  ? 0.2004 0.1430 0.1914 0.0083  -0.0019 0.0017  832  VAL A CA  
5992  C C   . VAL A 834  ? 0.2262 0.1673 0.2199 0.0107  -0.0033 -0.0006 832  VAL A C   
5993  O O   . VAL A 834  ? 0.2198 0.1595 0.2154 0.0124  -0.0051 -0.0035 832  VAL A O   
5994  C CB  . VAL A 834  ? 0.2187 0.1609 0.2123 0.0052  -0.0034 0.0053  832  VAL A CB  
5995  C CG1 . VAL A 834  ? 0.2190 0.1582 0.2179 0.0048  -0.0069 0.0054  832  VAL A CG1 
5996  C CG2 . VAL A 834  ? 0.2307 0.1751 0.2221 0.0031  -0.0023 0.0068  832  VAL A CG2 
5997  N N   . ILE A 835  ? 0.2102 0.1519 0.2043 0.0111  -0.0026 0.0003  833  ILE A N   
5998  C CA  . ILE A 835  ? 0.2222 0.1630 0.2190 0.0137  -0.0037 -0.0020 833  ILE A CA  
5999  C C   . ILE A 835  ? 0.2402 0.1829 0.2348 0.0168  -0.0027 -0.0060 833  ILE A C   
6000  O O   . ILE A 835  ? 0.2607 0.2026 0.2579 0.0190  -0.0047 -0.0094 833  ILE A O   
6001  C CB  . ILE A 835  ? 0.2350 0.1769 0.2319 0.0136  -0.0026 -0.0002 833  ILE A CB  
6002  C CG1 . ILE A 835  ? 0.2444 0.1847 0.2444 0.0108  -0.0043 0.0036  833  ILE A CG1 
6003  C CG2 . ILE A 835  ? 0.2646 0.2068 0.2634 0.0167  -0.0031 -0.0031 833  ILE A CG2 
6004  C CD1 . ILE A 835  ? 0.2776 0.2146 0.2834 0.0110  -0.0079 0.0033  833  ILE A CD1 
6005  N N   . THR A 836  ? 0.2274 0.1732 0.2176 0.0171  0.0001  -0.0056 834  THR A N   
6006  C CA  . THR A 836  ? 0.2493 0.1981 0.2372 0.0198  0.0012  -0.0087 834  THR A CA  
6007  C C   . THR A 836  ? 0.2371 0.1849 0.2252 0.0202  -0.0005 -0.0111 834  THR A C   
6008  O O   . THR A 836  ? 0.2510 0.1998 0.2402 0.0228  -0.0017 -0.0149 834  THR A O   
6009  C CB  . THR A 836  ? 0.2674 0.2195 0.2512 0.0195  0.0043  -0.0068 834  THR A CB  
6010  O OG1 . THR A 836  ? 0.3186 0.2719 0.3026 0.0195  0.0056  -0.0052 834  THR A OG1 
6011  C CG2 . THR A 836  ? 0.3028 0.2586 0.2841 0.0218  0.0054  -0.0091 834  THR A CG2 
6012  N N   . SER A 837  ? 0.2393 0.1856 0.2268 0.0177  -0.0007 -0.0092 835  SER A N   
6013  C CA  . SER A 837  ? 0.2485 0.1944 0.2360 0.0181  -0.0020 -0.0113 835  SER A CA  
6014  C C   . SER A 837  ? 0.2309 0.1737 0.2233 0.0186  -0.0056 -0.0137 835  SER A C   
6015  O O   . SER A 837  ? 0.2403 0.1835 0.2332 0.0204  -0.0069 -0.0173 835  SER A O   
6016  C CB  . SER A 837  ? 0.2232 0.1686 0.2093 0.0153  -0.0015 -0.0086 835  SER A CB  
6017  O OG  . SER A 837  ? 0.2262 0.1742 0.2085 0.0150  0.0014  -0.0069 835  SER A OG  
6018  N N   . ALA A 838  ? 0.2174 0.1571 0.2138 0.0171  -0.0073 -0.0117 836  ALA A N   
6019  C CA  . ALA A 838  ? 0.2372 0.1733 0.2394 0.0173  -0.0112 -0.0134 836  ALA A CA  
6020  C C   . ALA A 838  ? 0.2504 0.1866 0.2554 0.0207  -0.0125 -0.0175 836  ALA A C   
6021  O O   . ALA A 838  ? 0.2445 0.1791 0.2533 0.0223  -0.0154 -0.0214 836  ALA A O   
6022  C CB  . ALA A 838  ? 0.2221 0.1554 0.2281 0.0140  -0.0128 -0.0089 836  ALA A CB  
6023  N N   . PHE A 839  ? 0.2479 0.1861 0.2515 0.0219  -0.0106 -0.0171 837  PHE A N   
6024  C CA  . PHE A 839  ? 0.2509 0.1891 0.2581 0.0248  -0.0121 -0.0206 837  PHE A CA  
6025  C C   . PHE A 839  ? 0.2529 0.1964 0.2565 0.0283  -0.0098 -0.0240 837  PHE A C   
6026  O O   . PHE A 839  ? 0.2711 0.2155 0.2778 0.0313  -0.0112 -0.0279 837  PHE A O   
6027  C CB  . PHE A 839  ? 0.2325 0.1684 0.2431 0.0235  -0.0129 -0.0173 837  PHE A CB  
6028  C CG  . PHE A 839  ? 0.2360 0.1678 0.2504 0.0199  -0.0152 -0.0133 837  PHE A CG  
6029  C CD1 . PHE A 839  ? 0.2578 0.1859 0.2777 0.0197  -0.0191 -0.0148 837  PHE A CD1 
6030  C CD2 . PHE A 839  ? 0.2609 0.1929 0.2734 0.0168  -0.0137 -0.0080 837  PHE A CD2 
6031  C CE1 . PHE A 839  ? 0.2678 0.1928 0.2915 0.0162  -0.0214 -0.0105 837  PHE A CE1 
6032  C CE2 . PHE A 839  ? 0.2611 0.1908 0.2769 0.0135  -0.0158 -0.0040 837  PHE A CE2 
6033  C CZ  . PHE A 839  ? 0.2701 0.1963 0.2916 0.0131  -0.0196 -0.0049 837  PHE A CZ  
6034  N N   . ASP A 840  ? 0.2411 0.1885 0.2388 0.0280  -0.0064 -0.0226 838  ASP A N   
6035  C CA  . ASP A 840  ? 0.2495 0.2029 0.2439 0.0312  -0.0044 -0.0255 838  ASP A CA  
6036  C C   . ASP A 840  ? 0.2844 0.2390 0.2808 0.0341  -0.0068 -0.0314 838  ASP A C   
6037  O O   . ASP A 840  ? 0.2477 0.1994 0.2456 0.0332  -0.0089 -0.0325 838  ASP A O   
6038  C CB  . ASP A 840  ? 0.2849 0.2418 0.2736 0.0301  -0.0012 -0.0229 838  ASP A CB  
6039  C CG  . ASP A 840  ? 0.3247 0.2887 0.3101 0.0330  0.0009  -0.0249 838  ASP A CG  
6040  O OD1 . ASP A 840  ? 0.3284 0.2954 0.3131 0.0352  0.0000  -0.0289 838  ASP A OD1 
6041  O OD2 . ASP A 840  ? 0.4110 0.3782 0.3945 0.0329  0.0034  -0.0223 838  ASP A OD2 
6042  N N   . SER A 841  ? 0.2389 0.1981 0.2359 0.0377  -0.0067 -0.0354 839  SER A N   
6043  C CA  . SER A 841  ? 0.2298 0.1910 0.2289 0.0411  -0.0091 -0.0420 839  SER A CA  
6044  C C   . SER A 841  ? 0.2396 0.1939 0.2455 0.0405  -0.0135 -0.0441 839  SER A C   
6045  O O   . SER A 841  ? 0.2662 0.2202 0.2742 0.0420  -0.0161 -0.0486 839  SER A O   
6046  C CB  . SER A 841  ? 0.2727 0.2383 0.2671 0.0417  -0.0079 -0.0434 839  SER A CB  
6047  O OG  . SER A 841  ? 0.3107 0.2824 0.2994 0.0417  -0.0040 -0.0404 839  SER A OG  
6048  N N   . ALA A 842  ? 0.2542 0.2031 0.2641 0.0384  -0.0147 -0.0406 840  ALA A N   
6049  C CA  . ALA A 842  ? 0.2327 0.1747 0.2498 0.0372  -0.0191 -0.0411 840  ALA A CA  
6050  C C   . ALA A 842  ? 0.2452 0.1844 0.2624 0.0350  -0.0206 -0.0405 840  ALA A C   
6051  O O   . ALA A 842  ? 0.2458 0.1815 0.2685 0.0355  -0.0246 -0.0437 840  ALA A O   
6052  C CB  . ALA A 842  ? 0.2776 0.2196 0.3009 0.0411  -0.0224 -0.0476 840  ALA A CB  
6053  N N   . GLY A 843  ? 0.2477 0.1884 0.2591 0.0325  -0.0176 -0.0364 841  GLY A N   
6054  C CA  . GLY A 843  ? 0.2244 0.1628 0.2355 0.0303  -0.0188 -0.0354 841  GLY A CA  
6055  C C   . GLY A 843  ? 0.2413 0.1826 0.2513 0.0328  -0.0197 -0.0408 841  GLY A C   
6056  O O   . GLY A 843  ? 0.2523 0.1917 0.2628 0.0311  -0.0211 -0.0406 841  GLY A O   
6057  N N   . GLN A 844  ? 0.2388 0.1855 0.2471 0.0367  -0.0189 -0.0457 842  GLN A N   
6058  C CA  . GLN A 844  ? 0.2386 0.1891 0.2458 0.0395  -0.0199 -0.0515 842  GLN A CA  
6059  C C   . GLN A 844  ? 0.2620 0.2187 0.2614 0.0395  -0.0161 -0.0500 842  GLN A C   
6060  O O   . GLN A 844  ? 0.2662 0.2300 0.2621 0.0427  -0.0147 -0.0534 842  GLN A O   
6061  C CB  . GLN A 844  ? 0.2450 0.1987 0.2555 0.0439  -0.0217 -0.0582 842  GLN A CB  
6062  C CG  . GLN A 844  ? 0.2434 0.1901 0.2628 0.0439  -0.0263 -0.0601 842  GLN A CG  
6063  C CD  . GLN A 844  ? 0.2556 0.2050 0.2786 0.0481  -0.0275 -0.0657 842  GLN A CD  
6064  O OE1 . GLN A 844  ? 0.2441 0.1924 0.2731 0.0507  -0.0315 -0.0720 842  GLN A OE1 
6065  N NE2 . GLN A 844  ? 0.2893 0.2425 0.3091 0.0489  -0.0242 -0.0635 842  GLN A NE2 
6066  N N   . ARG A 845  ? 0.2275 0.1820 0.2242 0.0360  -0.0145 -0.0444 843  ARG A N   
6067  C CA  . ARG A 845  ? 0.2423 0.2009 0.2331 0.0354  -0.0118 -0.0426 843  ARG A CA  
6068  C C   . ARG A 845  ? 0.2378 0.1925 0.2300 0.0329  -0.0138 -0.0417 843  ARG A C   
6069  O O   . ARG A 845  ? 0.2363 0.1851 0.2324 0.0302  -0.0155 -0.0390 843  ARG A O   
6070  C CB  . ARG A 845  ? 0.2539 0.2135 0.2405 0.0333  -0.0080 -0.0366 843  ARG A CB  
6071  C CG  . ARG A 845  ? 0.2511 0.2147 0.2363 0.0351  -0.0058 -0.0363 843  ARG A CG  
6072  C CD  . ARG A 845  ? 0.2704 0.2345 0.2520 0.0327  -0.0024 -0.0304 843  ARG A CD  
6073  N NE  . ARG A 845  ? 0.3178 0.2867 0.2977 0.0344  -0.0001 -0.0298 843  ARG A NE  
6074  C CZ  . ARG A 845  ? 0.3403 0.3160 0.3162 0.0359  0.0022  -0.0295 843  ARG A CZ  
6075  N NH1 . ARG A 845  ? 0.3389 0.3175 0.3119 0.0360  0.0026  -0.0296 843  ARG A NH1 
6076  N NH2 . ARG A 845  ? 0.3729 0.3533 0.3481 0.0374  0.0040  -0.0289 843  ARG A NH2 
6077  N N   . CYS A 846  ? 0.2362 0.1946 0.2254 0.0338  -0.0136 -0.0437 844  CYS A N   
6078  C CA  . CYS A 846  ? 0.2376 0.1926 0.2280 0.0314  -0.0152 -0.0425 844  CYS A CA  
6079  C C   . CYS A 846  ? 0.2221 0.1746 0.2107 0.0276  -0.0130 -0.0360 844  CYS A C   
6080  O O   . CYS A 846  ? 0.2200 0.1685 0.2113 0.0249  -0.0146 -0.0340 844  CYS A O   
6081  C CB  . CYS A 846  ? 0.2282 0.1884 0.2152 0.0331  -0.0150 -0.0455 844  CYS A CB  
6082  S SG  . CYS A 846  ? 0.2591 0.2270 0.2384 0.0342  -0.0104 -0.0430 844  CYS A SG  
6083  N N   . SER A 847  ? 0.2200 0.1751 0.2046 0.0275  -0.0096 -0.0328 845  SER A N   
6084  C CA  . SER A 847  ? 0.2119 0.1656 0.1946 0.0245  -0.0073 -0.0273 845  SER A CA  
6085  C C   . SER A 847  ? 0.2255 0.1748 0.2116 0.0224  -0.0078 -0.0244 845  SER A C   
6086  O O   . SER A 847  ? 0.2179 0.1662 0.2028 0.0199  -0.0062 -0.0202 845  SER A O   
6087  C CB  . SER A 847  ? 0.2402 0.1988 0.2181 0.0255  -0.0037 -0.0254 845  SER A CB  
6088  O OG  . SER A 847  ? 0.2364 0.1971 0.2144 0.0278  -0.0032 -0.0271 845  SER A OG  
6089  N N   . ALA A 848  ? 0.2232 0.1702 0.2135 0.0235  -0.0101 -0.0267 846  ALA A N   
6090  C CA  . ALA A 848  ? 0.2107 0.1544 0.2038 0.0219  -0.0104 -0.0238 846  ALA A CA  
6091  C C   . ALA A 848  ? 0.2311 0.1714 0.2266 0.0182  -0.0115 -0.0198 846  ALA A C   
6092  O O   . ALA A 848  ? 0.2189 0.1577 0.2163 0.0170  -0.0135 -0.0203 846  ALA A O   
6093  C CB  . ALA A 848  ? 0.2218 0.1635 0.2201 0.0239  -0.0133 -0.0273 846  ALA A CB  
6094  N N   . LEU A 849  ? 0.2157 0.1552 0.2111 0.0162  -0.0102 -0.0158 847  LEU A N   
6095  C CA  . LEU A 849  ? 0.2036 0.1410 0.2009 0.0126  -0.0110 -0.0116 847  LEU A CA  
6096  C C   . LEU A 849  ? 0.2338 0.1673 0.2379 0.0117  -0.0150 -0.0117 847  LEU A C   
6097  O O   . LEU A 849  ? 0.2305 0.1623 0.2379 0.0127  -0.0163 -0.0123 847  LEU A O   
6098  C CB  . LEU A 849  ? 0.2308 0.1694 0.2262 0.0110  -0.0086 -0.0077 847  LEU A CB  
6099  C CG  . LEU A 849  ? 0.2147 0.1525 0.2121 0.0073  -0.0094 -0.0033 847  LEU A CG  
6100  C CD1 . LEU A 849  ? 0.2371 0.1765 0.2328 0.0057  -0.0088 -0.0024 847  LEU A CD1 
6101  C CD2 . LEU A 849  ? 0.2249 0.1641 0.2206 0.0062  -0.0073 -0.0003 847  LEU A CD2 
6102  N N   . ARG A 850  ? 0.2162 0.1484 0.2229 0.0097  -0.0171 -0.0109 848  ARG A N   
6103  C CA  . ARG A 850  ? 0.2453 0.1737 0.2593 0.0085  -0.0213 -0.0104 848  ARG A CA  
6104  C C   . ARG A 850  ? 0.2360 0.1640 0.2526 0.0044  -0.0220 -0.0044 848  ARG A C   
6105  O O   . ARG A 850  ? 0.2524 0.1776 0.2753 0.0031  -0.0251 -0.0026 848  ARG A O   
6106  C CB  . ARG A 850  ? 0.2438 0.1711 0.2603 0.0091  -0.0239 -0.0138 848  ARG A CB  
6107  C CG  . ARG A 850  ? 0.2587 0.1876 0.2725 0.0131  -0.0234 -0.0199 848  ARG A CG  
6108  C CD  . ARG A 850  ? 0.2612 0.1893 0.2770 0.0161  -0.0242 -0.0231 848  ARG A CD  
6109  N NE  . ARG A 850  ? 0.2394 0.1703 0.2527 0.0199  -0.0238 -0.0291 848  ARG A NE  
6110  C CZ  . ARG A 850  ? 0.2555 0.1876 0.2693 0.0232  -0.0239 -0.0330 848  ARG A CZ  
6111  N NH1 . ARG A 850  ? 0.2426 0.1727 0.2592 0.0232  -0.0243 -0.0315 848  ARG A NH1 
6112  N NH2 . ARG A 850  ? 0.2530 0.1887 0.2644 0.0267  -0.0237 -0.0384 848  ARG A NH2 
6113  N N   . VAL A 851  ? 0.2449 0.1762 0.2573 0.0023  -0.0194 -0.0014 849  VAL A N   
6114  C CA  . VAL A 851  ? 0.2403 0.1729 0.2548 -0.0015 -0.0199 0.0041  849  VAL A CA  
6115  C C   . VAL A 851  ? 0.2481 0.1847 0.2568 -0.0023 -0.0160 0.0064  849  VAL A C   
6116  O O   . VAL A 851  ? 0.2380 0.1772 0.2419 -0.0017 -0.0134 0.0052  849  VAL A O   
6117  C CB  . VAL A 851  ? 0.2642 0.1975 0.2807 -0.0036 -0.0214 0.0051  849  VAL A CB  
6118  C CG1 . VAL A 851  ? 0.2878 0.2231 0.3074 -0.0076 -0.0224 0.0112  849  VAL A CG1 
6119  C CG2 . VAL A 851  ? 0.3182 0.2475 0.3399 -0.0023 -0.0252 0.0016  849  VAL A CG2 
6120  N N   . LEU A 852  ? 0.2315 0.1688 0.2412 -0.0036 -0.0157 0.0096  850  LEU A N   
6121  C CA  . LEU A 852  ? 0.2334 0.1747 0.2384 -0.0046 -0.0125 0.0118  850  LEU A CA  
6122  C C   . LEU A 852  ? 0.2146 0.1594 0.2211 -0.0082 -0.0130 0.0165  850  LEU A C   
6123  O O   . LEU A 852  ? 0.2263 0.1704 0.2381 -0.0103 -0.0158 0.0198  850  LEU A O   
6124  C CB  . LEU A 852  ? 0.2083 0.1491 0.2133 -0.0038 -0.0119 0.0124  850  LEU A CB  
6125  C CG  . LEU A 852  ? 0.2176 0.1625 0.2188 -0.0049 -0.0091 0.0148  850  LEU A CG  
6126  C CD1 . LEU A 852  ? 0.2130 0.1597 0.2086 -0.0032 -0.0058 0.0120  850  LEU A CD1 
6127  C CD2 . LEU A 852  ? 0.2207 0.1645 0.2232 -0.0043 -0.0094 0.0156  850  LEU A CD2 
6128  N N   . CYS A 853  ? 0.2315 0.1806 0.2339 -0.0090 -0.0104 0.0168  851  CYS A N   
6129  C CA  . CYS A 853  ? 0.2293 0.1832 0.2326 -0.0122 -0.0106 0.0207  851  CYS A CA  
6130  C C   . CYS A 853  ? 0.2227 0.1815 0.2224 -0.0129 -0.0079 0.0222  851  CYS A C   
6131  O O   . CYS A 853  ? 0.2363 0.1965 0.2315 -0.0113 -0.0052 0.0196  851  CYS A O   
6132  C CB  . CYS A 853  ? 0.2367 0.1922 0.2386 -0.0123 -0.0100 0.0193  851  CYS A CB  
6133  S SG  . CYS A 853  ? 0.2597 0.2097 0.2649 -0.0108 -0.0128 0.0162  851  CYS A SG  
6134  N N   . LEU A 854  ? 0.2290 0.1906 0.2310 -0.0153 -0.0090 0.0265  852  LEU A N   
6135  C CA  . LEU A 854  ? 0.2282 0.1945 0.2274 -0.0159 -0.0070 0.0278  852  LEU A CA  
6136  C C   . LEU A 854  ? 0.2290 0.2031 0.2279 -0.0188 -0.0065 0.0311  852  LEU A C   
6137  O O   . LEU A 854  ? 0.2514 0.2275 0.2544 -0.0214 -0.0088 0.0353  852  LEU A O   
6138  C CB  . LEU A 854  ? 0.2309 0.1954 0.2326 -0.0163 -0.0084 0.0301  852  LEU A CB  
6139  C CG  . LEU A 854  ? 0.2502 0.2082 0.2523 -0.0133 -0.0087 0.0267  852  LEU A CG  
6140  C CD1 . LEU A 854  ? 0.2160 0.1729 0.2212 -0.0139 -0.0104 0.0294  852  LEU A CD1 
6141  C CD2 . LEU A 854  ? 0.2535 0.2116 0.2502 -0.0108 -0.0055 0.0227  852  LEU A CD2 
6142  N N   . GLN A 855  ? 0.2263 0.2051 0.2209 -0.0183 -0.0037 0.0293  853  GLN A N   
6143  C CA  . GLN A 855  ? 0.2339 0.2214 0.2280 -0.0207 -0.0031 0.0320  853  GLN A CA  
6144  C C   . GLN A 855  ? 0.2591 0.2506 0.2554 -0.0231 -0.0044 0.0369  853  GLN A C   
6145  O O   . GLN A 855  ? 0.2591 0.2486 0.2549 -0.0223 -0.0043 0.0366  853  GLN A O   
6146  C CB  . GLN A 855  ? 0.2491 0.2411 0.2387 -0.0194 -0.0001 0.0285  853  GLN A CB  
6147  C CG  . GLN A 855  ? 0.2283 0.2299 0.2175 -0.0215 0.0006  0.0304  853  GLN A CG  
6148  C CD  . GLN A 855  ? 0.2829 0.2897 0.2684 -0.0201 0.0032  0.0267  853  GLN A CD  
6149  O OE1 . GLN A 855  ? 0.2870 0.2898 0.2706 -0.0176 0.0046  0.0223  853  GLN A OE1 
6150  N NE2 . GLN A 855  ? 0.3433 0.3594 0.3282 -0.0218 0.0038  0.0284  853  GLN A NE2 
6151  N N   . GLU A 856  ? 0.2654 0.2631 0.2643 -0.0262 -0.0057 0.0415  854  GLU A N   
6152  C CA  . GLU A 856  ? 0.2835 0.2844 0.2857 -0.0289 -0.0077 0.0473  854  GLU A CA  
6153  C C   . GLU A 856  ? 0.2994 0.3048 0.2987 -0.0286 -0.0062 0.0472  854  GLU A C   
6154  O O   . GLU A 856  ? 0.3126 0.3163 0.3141 -0.0292 -0.0078 0.0500  854  GLU A O   
6155  C CB  . GLU A 856  ? 0.2893 0.2983 0.2943 -0.0324 -0.0089 0.0525  854  GLU A CB  
6156  C CG  . GLU A 856  ? 0.3293 0.3436 0.3378 -0.0356 -0.0110 0.0594  854  GLU A CG  
6157  C CD  . GLU A 856  ? 0.3874 0.3932 0.4017 -0.0359 -0.0144 0.0620  854  GLU A CD  
6158  O OE1 . GLU A 856  ? 0.3694 0.3674 0.3868 -0.0350 -0.0161 0.0604  854  GLU A OE1 
6159  O OE2 . GLU A 856  ? 0.3811 0.3882 0.3970 -0.0368 -0.0155 0.0653  854  GLU A OE2 
6160  N N   . ASP A 857  ? 0.2824 0.2933 0.2770 -0.0276 -0.0034 0.0438  855  ASP A N   
6161  C CA  . ASP A 857  ? 0.2960 0.3124 0.2879 -0.0275 -0.0021 0.0435  855  ASP A CA  
6162  C C   . ASP A 857  ? 0.3017 0.3107 0.2929 -0.0253 -0.0019 0.0410  855  ASP A C   
6163  O O   . ASP A 857  ? 0.3324 0.3447 0.3230 -0.0257 -0.0019 0.0423  855  ASP A O   
6164  C CB  . ASP A 857  ? 0.3835 0.4068 0.3712 -0.0265 0.0007  0.0393  855  ASP A CB  
6165  N N   . VAL A 858  ? 0.2616 0.2613 0.2530 -0.0229 -0.0019 0.0376  856  VAL A N   
6166  C CA  . VAL A 858  ? 0.2597 0.2529 0.2506 -0.0206 -0.0017 0.0353  856  VAL A CA  
6167  C C   . VAL A 858  ? 0.2622 0.2476 0.2572 -0.0203 -0.0041 0.0368  856  VAL A C   
6168  O O   . VAL A 858  ? 0.2516 0.2317 0.2466 -0.0183 -0.0041 0.0349  856  VAL A O   
6169  C CB  . VAL A 858  ? 0.2714 0.2613 0.2589 -0.0177 0.0007  0.0296  856  VAL A CB  
6170  C CG1 . VAL A 858  ? 0.2999 0.2970 0.2842 -0.0177 0.0027  0.0276  856  VAL A CG1 
6171  C CG2 . VAL A 858  ? 0.2684 0.2547 0.2561 -0.0168 0.0007  0.0276  856  VAL A CG2 
6172  N N   . ALA A 859  ? 0.2619 0.2468 0.2607 -0.0221 -0.0064 0.0401  857  ALA A N   
6173  C CA  . ALA A 859  ? 0.2588 0.2358 0.2620 -0.0213 -0.0090 0.0404  857  ALA A CA  
6174  C C   . ALA A 859  ? 0.2881 0.2630 0.2942 -0.0215 -0.0106 0.0427  857  ALA A C   
6175  O O   . ALA A 859  ? 0.2439 0.2120 0.2514 -0.0192 -0.0114 0.0403  857  ALA A O   
6176  C CB  . ALA A 859  ? 0.2555 0.2327 0.2632 -0.0236 -0.0115 0.0437  857  ALA A CB  
6177  N N   . ASP A 860  ? 0.2589 0.2401 0.2659 -0.0240 -0.0113 0.0475  858  ASP A N   
6178  C CA  . ASP A 860  ? 0.3020 0.2815 0.3124 -0.0243 -0.0132 0.0503  858  ASP A CA  
6179  C C   . ASP A 860  ? 0.2668 0.2436 0.2739 -0.0216 -0.0113 0.0463  858  ASP A C   
6180  O O   . ASP A 860  ? 0.2833 0.2542 0.2931 -0.0200 -0.0127 0.0456  858  ASP A O   
6181  C CB  . ASP A 860  ? 0.2970 0.2850 0.3086 -0.0278 -0.0142 0.0565  858  ASP A CB  
6182  C CG  . ASP A 860  ? 0.3593 0.3489 0.3766 -0.0309 -0.0173 0.0623  858  ASP A CG  
6183  O OD1 . ASP A 860  ? 0.3762 0.3587 0.3982 -0.0303 -0.0196 0.0620  858  ASP A OD1 
6184  O OD2 . ASP A 860  ? 0.4979 0.4965 0.5154 -0.0339 -0.0175 0.0674  858  ASP A OD2 
6185  N N   . ARG A 861  ? 0.2513 0.2322 0.2529 -0.0208 -0.0082 0.0434  859  ARG A N   
6186  C CA  . ARG A 861  ? 0.3060 0.2849 0.3048 -0.0185 -0.0064 0.0399  859  ARG A CA  
6187  C C   . ARG A 861  ? 0.2743 0.2453 0.2731 -0.0154 -0.0060 0.0355  859  ARG A C   
6188  O O   . ARG A 861  ? 0.2648 0.2318 0.2646 -0.0136 -0.0063 0.0344  859  ARG A O   
6189  C CB  . ARG A 861  ? 0.3475 0.3325 0.3414 -0.0185 -0.0036 0.0376  859  ARG A CB  
6190  C CG  . ARG A 861  ? 0.4282 0.4129 0.4198 -0.0168 -0.0021 0.0349  859  ARG A CG  
6191  C CD  . ARG A 861  ? 0.4732 0.4528 0.4624 -0.0139 -0.0001 0.0298  859  ARG A CD  
6192  N NE  . ARG A 861  ? 0.5365 0.5197 0.5224 -0.0133 0.0021  0.0268  859  ARG A NE  
6193  C CZ  . ARG A 861  ? 0.5136 0.4963 0.4989 -0.0122 0.0028  0.0254  859  ARG A CZ  
6194  N NH1 . ARG A 861  ? 0.5791 0.5582 0.5663 -0.0116 0.0018  0.0267  859  ARG A NH1 
6195  N NH2 . ARG A 861  ? 0.6166 0.6022 0.5996 -0.0117 0.0045  0.0224  859  ARG A NH2 
6196  N N   . ILE A 862  ? 0.2590 0.2282 0.2567 -0.0147 -0.0054 0.0331  860  ILE A N   
6197  C CA  . ILE A 862  ? 0.2377 0.2006 0.2350 -0.0117 -0.0049 0.0290  860  ILE A CA  
6198  C C   . ILE A 862  ? 0.2417 0.1993 0.2441 -0.0110 -0.0078 0.0298  860  ILE A C   
6199  O O   . ILE A 862  ? 0.2393 0.1927 0.2421 -0.0085 -0.0077 0.0271  860  ILE A O   
6200  C CB  . ILE A 862  ? 0.2377 0.2006 0.2327 -0.0112 -0.0037 0.0265  860  ILE A CB  
6201  C CG1 . ILE A 862  ? 0.2847 0.2521 0.2753 -0.0111 -0.0009 0.0247  860  ILE A CG1 
6202  C CG2 . ILE A 862  ? 0.2456 0.2026 0.2407 -0.0083 -0.0037 0.0227  860  ILE A CG2 
6203  C CD1 . ILE A 862  ? 0.2949 0.2634 0.2837 -0.0109 0.0002  0.0227  860  ILE A CD1 
6204  N N   . LEU A 863  ? 0.2400 0.1978 0.2467 -0.0133 -0.0105 0.0335  861  LEU A N   
6205  C CA  . LEU A 863  ? 0.2620 0.2144 0.2745 -0.0127 -0.0138 0.0341  861  LEU A CA  
6206  C C   . LEU A 863  ? 0.2519 0.2030 0.2665 -0.0119 -0.0146 0.0351  861  LEU A C   
6207  O O   . LEU A 863  ? 0.2317 0.1779 0.2491 -0.0095 -0.0158 0.0325  861  LEU A O   
6208  C CB  . LEU A 863  ? 0.2958 0.2494 0.3133 -0.0157 -0.0168 0.0387  861  LEU A CB  
6209  C CG  . LEU A 863  ? 0.3280 0.2756 0.3527 -0.0154 -0.0207 0.0390  861  LEU A CG  
6210  C CD1 . LEU A 863  ? 0.2848 0.2271 0.3087 -0.0119 -0.0204 0.0328  861  LEU A CD1 
6211  C CD2 . LEU A 863  ? 0.3691 0.3187 0.3979 -0.0188 -0.0231 0.0436  861  LEU A CD2 
6212  N N   . THR A 864  ? 0.2496 0.2058 0.2632 -0.0138 -0.0140 0.0385  862  THR A N   
6213  C CA  . THR A 864  ? 0.2472 0.2026 0.2625 -0.0131 -0.0146 0.0395  862  THR A CA  
6214  C C   . THR A 864  ? 0.2330 0.1858 0.2450 -0.0097 -0.0122 0.0344  862  THR A C   
6215  O O   . THR A 864  ? 0.2439 0.1929 0.2587 -0.0077 -0.0133 0.0331  862  THR A O   
6216  C CB  . THR A 864  ? 0.2450 0.2073 0.2587 -0.0157 -0.0140 0.0436  862  THR A CB  
6217  O OG1 . THR A 864  ? 0.2649 0.2302 0.2824 -0.0189 -0.0166 0.0492  862  THR A OG1 
6218  C CG2 . THR A 864  ? 0.2570 0.2189 0.2718 -0.0148 -0.0144 0.0443  862  THR A CG2 
6219  N N   . MET A 865  ? 0.2175 0.1726 0.2239 -0.0091 -0.0091 0.0316  863  MET A N   
6220  C CA  . MET A 865  ? 0.2355 0.1886 0.2390 -0.0062 -0.0069 0.0274  863  MET A CA  
6221  C C   . MET A 865  ? 0.2246 0.1726 0.2298 -0.0035 -0.0077 0.0240  863  MET A C   
6222  O O   . MET A 865  ? 0.2125 0.1583 0.2185 -0.0011 -0.0074 0.0217  863  MET A O   
6223  C CB  . MET A 865  ? 0.2542 0.2106 0.2524 -0.0062 -0.0038 0.0255  863  MET A CB  
6224  C CG  . MET A 865  ? 0.2826 0.2377 0.2781 -0.0036 -0.0015 0.0221  863  MET A CG  
6225  S SD  . MET A 865  ? 0.3251 0.2840 0.3157 -0.0040 0.0014  0.0203  863  MET A SD  
6226  C CE  . MET A 865  ? 0.3256 0.2903 0.3163 -0.0073 0.0008  0.0239  863  MET A CE  
6227  N N   . LEU A 866  ? 0.2136 0.1602 0.2198 -0.0040 -0.0087 0.0235  864  LEU A N   
6228  C CA  . LEU A 866  ? 0.2293 0.1717 0.2372 -0.0014 -0.0097 0.0199  864  LEU A CA  
6229  C C   . LEU A 866  ? 0.2186 0.1574 0.2323 -0.0002 -0.0127 0.0199  864  LEU A C   
6230  O O   . LEU A 866  ? 0.2446 0.1812 0.2589 0.0028  -0.0126 0.0161  864  LEU A O   
6231  C CB  . LEU A 866  ? 0.2461 0.1879 0.2545 -0.0026 -0.0107 0.0199  864  LEU A CB  
6232  C CG  . LEU A 866  ? 0.3094 0.2474 0.3193 -0.0001 -0.0118 0.0158  864  LEU A CG  
6233  C CD1 . LEU A 866  ? 0.2809 0.2196 0.2860 0.0028  -0.0089 0.0118  864  LEU A CD1 
6234  C CD2 . LEU A 866  ? 0.2816 0.2196 0.2921 -0.0017 -0.0129 0.0164  864  LEU A CD2 
6235  N N   . LYS A 867  ? 0.2305 0.1690 0.2489 -0.0026 -0.0155 0.0241  865  LYS A N   
6236  C CA  . LYS A 867  ? 0.2303 0.1653 0.2553 -0.0014 -0.0187 0.0243  865  LYS A CA  
6237  C C   . LYS A 867  ? 0.2417 0.1772 0.2658 0.0005  -0.0174 0.0231  865  LYS A C   
6238  O O   . LYS A 867  ? 0.2495 0.1821 0.2770 0.0033  -0.0187 0.0202  865  LYS A O   
6239  C CB  . LYS A 867  ? 0.2505 0.1857 0.2811 -0.0047 -0.0220 0.0300  865  LYS A CB  
6240  C CG  . LYS A 867  ? 0.2715 0.2056 0.3048 -0.0066 -0.0241 0.0313  865  LYS A CG  
6241  C CD  . LYS A 867  ? 0.2802 0.2158 0.3189 -0.0103 -0.0272 0.0381  865  LYS A CD  
6242  C CE  . LYS A 867  ? 0.3161 0.2515 0.3573 -0.0125 -0.0289 0.0397  865  LYS A CE  
6243  N NZ  . LYS A 867  ? 0.3336 0.2718 0.3798 -0.0166 -0.0317 0.0471  865  LYS A NZ  
6244  N N   . GLY A 868  ? 0.2156 0.1552 0.2356 -0.0008 -0.0150 0.0252  866  GLY A N   
6245  C CA  . GLY A 868  ? 0.2319 0.1723 0.2509 0.0009  -0.0136 0.0242  866  GLY A CA  
6246  C C   . GLY A 868  ? 0.2253 0.1647 0.2414 0.0044  -0.0114 0.0190  866  GLY A C   
6247  O O   . GLY A 868  ? 0.2374 0.1759 0.2555 0.0068  -0.0117 0.0170  866  GLY A O   
6248  N N   . ALA A 869  ? 0.2265 0.1668 0.2382 0.0046  -0.0093 0.0169  867  ALA A N   
6249  C CA  . ALA A 869  ? 0.2388 0.1792 0.2478 0.0077  -0.0073 0.0125  867  ALA A CA  
6250  C C   . ALA A 869  ? 0.2233 0.1606 0.2361 0.0103  -0.0095 0.0090  867  ALA A C   
6251  O O   . ALA A 869  ? 0.2237 0.1616 0.2361 0.0134  -0.0086 0.0057  867  ALA A O   
6252  C CB  . ALA A 869  ? 0.2306 0.1727 0.2344 0.0071  -0.0049 0.0115  867  ALA A CB  
6253  N N   . LEU A 870  ? 0.2222 0.1568 0.2388 0.0093  -0.0124 0.0096  868  LEU A N   
6254  C CA  . LEU A 870  ? 0.2417 0.1730 0.2630 0.0118  -0.0151 0.0060  868  LEU A CA  
6255  C C   . LEU A 870  ? 0.2564 0.1870 0.2819 0.0141  -0.0164 0.0047  868  LEU A C   
6256  O O   . LEU A 870  ? 0.2443 0.1748 0.2708 0.0176  -0.0166 -0.0001 868  LEU A O   
6257  C CB  . LEU A 870  ? 0.2571 0.1853 0.2836 0.0096  -0.0188 0.0082  868  LEU A CB  
6258  C CG  . LEU A 870  ? 0.2733 0.1978 0.3052 0.0118  -0.0221 0.0041  868  LEU A CG  
6259  C CD1 . LEU A 870  ? 0.2877 0.2129 0.3157 0.0126  -0.0208 0.0007  868  LEU A CD1 
6260  C CD2 . LEU A 870  ? 0.2981 0.2191 0.3377 0.0094  -0.0266 0.0075  868  LEU A CD2 
6261  N N   . HIS A 871  ? 0.2151 0.1458 0.2429 0.0123  -0.0173 0.0087  869  HIS A N   
6262  C CA  . HIS A 871  ? 0.2729 0.2026 0.3056 0.0144  -0.0190 0.0079  869  HIS A CA  
6263  C C   . HIS A 871  ? 0.2583 0.1914 0.2874 0.0168  -0.0159 0.0056  869  HIS A C   
6264  O O   . HIS A 871  ? 0.2927 0.2255 0.3256 0.0190  -0.0170 0.0042  869  HIS A O   
6265  C CB  . HIS A 871  ? 0.2976 0.2265 0.3345 0.0114  -0.0212 0.0135  869  HIS A CB  
6266  C CG  . HIS A 871  ? 0.3179 0.2432 0.3611 0.0097  -0.0253 0.0156  869  HIS A CG  
6267  N ND1 . HIS A 871  ? 0.3110 0.2322 0.3619 0.0117  -0.0292 0.0131  869  HIS A ND1 
6268  C CD2 . HIS A 871  ? 0.2922 0.2176 0.3354 0.0061  -0.0263 0.0199  869  HIS A CD2 
6269  C CE1 . HIS A 871  ? 0.3338 0.2523 0.3895 0.0093  -0.0326 0.0161  869  HIS A CE1 
6270  N NE2 . HIS A 871  ? 0.3115 0.2329 0.3626 0.0058  -0.0307 0.0204  869  HIS A NE2 
6271  N N   . GLU A 872  ? 0.2320 0.1682 0.2544 0.0165  -0.0122 0.0051  870  GLU A N   
6272  C CA  . GLU A 872  ? 0.2448 0.1845 0.2639 0.0188  -0.0092 0.0031  870  GLU A CA  
6273  C C   . GLU A 872  ? 0.2508 0.1919 0.2688 0.0223  -0.0085 -0.0021 870  GLU A C   
6274  O O   . GLU A 872  ? 0.2469 0.1917 0.2623 0.0242  -0.0060 -0.0037 870  GLU A O   
6275  C CB  . GLU A 872  ? 0.2314 0.1741 0.2446 0.0166  -0.0059 0.0057  870  GLU A CB  
6276  C CG  . GLU A 872  ? 0.2579 0.2007 0.2716 0.0135  -0.0064 0.0104  870  GLU A CG  
6277  C CD  . GLU A 872  ? 0.3070 0.2504 0.3242 0.0143  -0.0072 0.0114  870  GLU A CD  
6278  O OE1 . GLU A 872  ? 0.3017 0.2465 0.3192 0.0171  -0.0063 0.0086  870  GLU A OE1 
6279  O OE2 . GLU A 872  ? 0.3127 0.2556 0.3324 0.0120  -0.0090 0.0150  870  GLU A OE2 
6280  N N   . LEU A 873  ? 0.2333 0.1719 0.2533 0.0231  -0.0106 -0.0047 871  LEU A N   
6281  C CA  . LEU A 873  ? 0.2319 0.1725 0.2507 0.0265  -0.0100 -0.0100 871  LEU A CA  
6282  C C   . LEU A 873  ? 0.2386 0.1794 0.2625 0.0301  -0.0120 -0.0141 871  LEU A C   
6283  O O   . LEU A 873  ? 0.2604 0.1975 0.2907 0.0300  -0.0154 -0.0137 871  LEU A O   
6284  C CB  . LEU A 873  ? 0.2545 0.1925 0.2736 0.0259  -0.0117 -0.0115 871  LEU A CB  
6285  C CG  . LEU A 873  ? 0.2375 0.1759 0.2516 0.0227  -0.0097 -0.0082 871  LEU A CG  
6286  C CD1 . LEU A 873  ? 0.2456 0.1813 0.2609 0.0222  -0.0118 -0.0097 871  LEU A CD1 
6287  C CD2 . LEU A 873  ? 0.2991 0.2422 0.3069 0.0237  -0.0058 -0.0089 871  LEU A CD2 
6288  N N   . HIS A 874  ? 0.2652 0.2110 0.2868 0.0334  -0.0100 -0.0179 872  HIS A N   
6289  C CA  . HIS A 874  ? 0.2508 0.1985 0.2767 0.0374  -0.0114 -0.0227 872  HIS A CA  
6290  C C   . HIS A 874  ? 0.2488 0.1971 0.2754 0.0402  -0.0129 -0.0286 872  HIS A C   
6291  O O   . HIS A 874  ? 0.2433 0.1957 0.2645 0.0408  -0.0105 -0.0300 872  HIS A O   
6292  C CB  . HIS A 874  ? 0.2676 0.2217 0.2904 0.0392  -0.0081 -0.0229 872  HIS A CB  
6293  C CG  . HIS A 874  ? 0.2799 0.2373 0.3069 0.0436  -0.0092 -0.0280 872  HIS A CG  
6294  N ND1 . HIS A 874  ? 0.3165 0.2802 0.3419 0.0455  -0.0066 -0.0283 872  HIS A ND1 
6295  C CD2 . HIS A 874  ? 0.3318 0.2874 0.3648 0.0465  -0.0127 -0.0332 872  HIS A CD2 
6296  C CE1 . HIS A 874  ? 0.3053 0.2714 0.3353 0.0495  -0.0083 -0.0336 872  HIS A CE1 
6297  N NE2 . HIS A 874  ? 0.2982 0.2592 0.3329 0.0503  -0.0121 -0.0368 872  HIS A NE2 
6298  N N   . ILE A 875  ? 0.2500 0.1943 0.2836 0.0417  -0.0171 -0.0318 873  ILE A N   
6299  C CA  . ILE A 875  ? 0.2721 0.2165 0.3078 0.0444  -0.0193 -0.0380 873  ILE A CA  
6300  C C   . ILE A 875  ? 0.2787 0.2271 0.3184 0.0493  -0.0204 -0.0443 873  ILE A C   
6301  O O   . ILE A 875  ? 0.2919 0.2385 0.3371 0.0502  -0.0222 -0.0441 873  ILE A O   
6302  C CB  . ILE A 875  ? 0.2982 0.2351 0.3399 0.0424  -0.0238 -0.0373 873  ILE A CB  
6303  C CG1 . ILE A 875  ? 0.3432 0.2780 0.3803 0.0382  -0.0225 -0.0325 873  ILE A CG1 
6304  C CG2 . ILE A 875  ? 0.3254 0.2621 0.3714 0.0459  -0.0269 -0.0447 873  ILE A CG2 
6305  C CD1 . ILE A 875  ? 0.3378 0.2718 0.3720 0.0342  -0.0203 -0.0252 873  ILE A CD1 
6306  N N   . GLY A 876  ? 0.2787 0.2329 0.3156 0.0527  -0.0193 -0.0499 874  GLY A N   
6307  C CA  . GLY A 876  ? 0.2638 0.2228 0.3042 0.0577  -0.0203 -0.0567 874  GLY A CA  
6308  C C   . GLY A 876  ? 0.2930 0.2607 0.3285 0.0609  -0.0182 -0.0619 874  GLY A C   
6309  O O   . GLY A 876  ? 0.2767 0.2456 0.3063 0.0593  -0.0164 -0.0605 874  GLY A O   
6310  N N   . ARG A 877  ? 0.2911 0.2651 0.3290 0.0657  -0.0186 -0.0681 875  ARG A N   
6311  C CA  . ARG A 877  ? 0.2857 0.2699 0.3188 0.0692  -0.0164 -0.0732 875  ARG A CA  
6312  C C   . ARG A 877  ? 0.2742 0.2645 0.2986 0.0670  -0.0111 -0.0673 875  ARG A C   
6313  O O   . ARG A 877  ? 0.2749 0.2654 0.2982 0.0652  -0.0089 -0.0622 875  ARG A O   
6314  C CB  . ARG A 877  ? 0.3214 0.3125 0.3589 0.0746  -0.0174 -0.0804 875  ARG A CB  
6315  C CG  . ARG A 877  ? 0.3193 0.3205 0.3540 0.0789  -0.0167 -0.0876 875  ARG A CG  
6316  C CD  . ARG A 877  ? 0.3549 0.3627 0.3947 0.0845  -0.0182 -0.0955 875  ARG A CD  
6317  N NE  . ARG A 877  ? 0.3387 0.3560 0.3748 0.0856  -0.0140 -0.0932 875  ARG A NE  
6318  C CZ  . ARG A 877  ? 0.4335 0.4594 0.4727 0.0904  -0.0141 -0.0992 875  ARG A CZ  
6319  N NH1 . ARG A 877  ? 0.3903 0.4162 0.4365 0.0949  -0.0183 -0.1082 875  ARG A NH1 
6320  N NH2 . ARG A 877  ? 0.4231 0.4580 0.4586 0.0909  -0.0101 -0.0961 875  ARG A NH2 
6321  N N   . THR A 878  ? 0.2622 0.2574 0.2808 0.0670  -0.0093 -0.0680 876  THR A N   
6322  C CA  . THR A 878  ? 0.2437 0.2416 0.2550 0.0638  -0.0052 -0.0613 876  THR A CA  
6323  C C   . THR A 878  ? 0.2749 0.2842 0.2820 0.0656  -0.0013 -0.0605 876  THR A C   
6324  O O   . THR A 878  ? 0.2740 0.2864 0.2755 0.0632  0.0020  -0.0551 876  THR A O   
6325  C CB  . THR A 878  ? 0.2414 0.2387 0.2485 0.0625  -0.0052 -0.0614 876  THR A CB  
6326  O OG1 . THR A 878  ? 0.3060 0.3093 0.3140 0.0667  -0.0068 -0.0692 876  THR A OG1 
6327  C CG2 . THR A 878  ? 0.3022 0.2882 0.3123 0.0591  -0.0079 -0.0591 876  THR A CG2 
6328  N N   . ASP A 879  ? 0.2600 0.2759 0.2702 0.0698  -0.0017 -0.0656 877  ASP A N   
6329  C CA  . ASP A 879  ? 0.2991 0.3265 0.3057 0.0714  0.0021  -0.0643 877  ASP A CA  
6330  C C   . ASP A 879  ? 0.2941 0.3195 0.3017 0.0692  0.0038  -0.0584 877  ASP A C   
6331  O O   . ASP A 879  ? 0.2604 0.2944 0.2680 0.0713  0.0058  -0.0586 877  ASP A O   
6332  C CB  . ASP A 879  ? 0.2650 0.3023 0.2739 0.0772  0.0012  -0.0727 877  ASP A CB  
6333  C CG  . ASP A 879  ? 0.3571 0.3898 0.3741 0.0797  -0.0023 -0.0776 877  ASP A CG  
6334  O OD1 . ASP A 879  ? 0.3749 0.3957 0.3965 0.0778  -0.0056 -0.0770 877  ASP A OD1 
6335  O OD2 . ASP A 879  ? 0.3400 0.3814 0.3590 0.0837  -0.0018 -0.0818 877  ASP A OD2 
6336  N N   . ARG A 880  ? 0.2713 0.2861 0.2798 0.0650  0.0030  -0.0531 878  ARG A N   
6337  C CA  . ARG A 880  ? 0.2719 0.2843 0.2807 0.0621  0.0046  -0.0468 878  ARG A CA  
6338  C C   . ARG A 880  ? 0.2554 0.2630 0.2598 0.0573  0.0063  -0.0402 878  ARG A C   
6339  O O   . ARG A 880  ? 0.2696 0.2698 0.2739 0.0554  0.0044  -0.0399 878  ARG A O   
6340  C CB  . ARG A 880  ? 0.3049 0.3090 0.3202 0.0618  0.0015  -0.0473 878  ARG A CB  
6341  C CG  . ARG A 880  ? 0.3947 0.4034 0.4153 0.0661  0.0003  -0.0524 878  ARG A CG  
6342  C CD  . ARG A 880  ? 0.4341 0.4333 0.4616 0.0653  -0.0033 -0.0521 878  ARG A CD  
6343  N NE  . ARG A 880  ? 0.5919 0.5949 0.6241 0.0682  -0.0036 -0.0541 878  ARG A NE  
6344  C CZ  . ARG A 880  ? 0.5664 0.5745 0.6029 0.0731  -0.0053 -0.0614 878  ARG A CZ  
6345  N NH1 . ARG A 880  ? 0.5716 0.5823 0.6081 0.0761  -0.0067 -0.0678 878  ARG A NH1 
6346  N NH2 . ARG A 880  ? 0.5574 0.5683 0.5983 0.0754  -0.0056 -0.0626 878  ARG A NH2 
6347  N N   . LEU A 881  ? 0.2436 0.2554 0.2448 0.0555  0.0095  -0.0348 879  LEU A N   
6348  C CA  . LEU A 881  ? 0.2467 0.2543 0.2442 0.0511  0.0110  -0.0287 879  LEU A CA  
6349  C C   . LEU A 881  ? 0.2350 0.2318 0.2350 0.0479  0.0090  -0.0263 879  LEU A C   
6350  O O   . LEU A 881  ? 0.2358 0.2276 0.2334 0.0449  0.0090  -0.0234 879  LEU A O   
6351  C CB  . LEU A 881  ? 0.2590 0.2726 0.2543 0.0498  0.0143  -0.0236 879  LEU A CB  
6352  C CG  . LEU A 881  ? 0.2641 0.2744 0.2563 0.0456  0.0159  -0.0175 879  LEU A CG  
6353  C CD1 . LEU A 881  ? 0.2700 0.2820 0.2583 0.0454  0.0164  -0.0178 879  LEU A CD1 
6354  C CD2 . LEU A 881  ? 0.2629 0.2789 0.2547 0.0445  0.0185  -0.0128 879  LEU A CD2 
6355  N N   . SER A 882  ? 0.2344 0.2279 0.2392 0.0486  0.0071  -0.0273 880  SER A N   
6356  C CA  . SER A 882  ? 0.2497 0.2340 0.2569 0.0455  0.0051  -0.0243 880  SER A CA  
6357  C C   . SER A 882  ? 0.2564 0.2341 0.2655 0.0451  0.0020  -0.0268 880  SER A C   
6358  O O   . SER A 882  ? 0.2549 0.2256 0.2655 0.0421  0.0004  -0.0238 880  SER A O   
6359  C CB  . SER A 882  ? 0.2691 0.2522 0.2813 0.0462  0.0038  -0.0242 880  SER A CB  
6360  O OG  . SER A 882  ? 0.2705 0.2549 0.2872 0.0502  0.0015  -0.0302 880  SER A OG  
6361  N N   . VAL A 883  ? 0.2628 0.2430 0.2719 0.0480  0.0010  -0.0320 881  VAL A N   
6362  C CA  . VAL A 883  ? 0.2689 0.2429 0.2805 0.0476  -0.0023 -0.0344 881  VAL A CA  
6363  C C   . VAL A 883  ? 0.2640 0.2360 0.2709 0.0446  -0.0011 -0.0314 881  VAL A C   
6364  O O   . VAL A 883  ? 0.2901 0.2675 0.2920 0.0450  0.0014  -0.0312 881  VAL A O   
6365  C CB  . VAL A 883  ? 0.2594 0.2369 0.2735 0.0521  -0.0042 -0.0419 881  VAL A CB  
6366  C CG1 . VAL A 883  ? 0.2589 0.2302 0.2750 0.0513  -0.0074 -0.0440 881  VAL A CG1 
6367  C CG2 . VAL A 883  ? 0.2714 0.2492 0.2918 0.0550  -0.0063 -0.0452 881  VAL A CG2 
6368  N N   . ASP A 884  ? 0.2567 0.2211 0.2652 0.0414  -0.0030 -0.0287 882  ASP A N   
6369  C CA  . ASP A 884  ? 0.2651 0.2272 0.2698 0.0385  -0.0022 -0.0259 882  ASP A CA  
6370  C C   . ASP A 884  ? 0.2930 0.2533 0.2988 0.0395  -0.0045 -0.0299 882  ASP A C   
6371  O O   . ASP A 884  ? 0.3121 0.2741 0.3137 0.0389  -0.0033 -0.0297 882  ASP A O   
6372  C CB  . ASP A 884  ? 0.2672 0.2233 0.2730 0.0345  -0.0029 -0.0208 882  ASP A CB  
6373  C CG  . ASP A 884  ? 0.2395 0.1973 0.2444 0.0333  -0.0008 -0.0170 882  ASP A CG  
6374  O OD1 . ASP A 884  ? 0.2659 0.2281 0.2665 0.0331  0.0023  -0.0155 882  ASP A OD1 
6375  O OD2 . ASP A 884  ? 0.2557 0.2104 0.2644 0.0324  -0.0024 -0.0154 882  ASP A OD2 
6376  N N   . VAL A 885  ? 0.2665 0.2230 0.2782 0.0409  -0.0082 -0.0332 883  VAL A N   
6377  C CA  . VAL A 885  ? 0.2682 0.2213 0.2825 0.0412  -0.0113 -0.0365 883  VAL A CA  
6378  C C   . VAL A 885  ? 0.2556 0.2108 0.2746 0.0457  -0.0138 -0.0435 883  VAL A C   
6379  O O   . VAL A 885  ? 0.2750 0.2286 0.2993 0.0469  -0.0156 -0.0445 883  VAL A O   
6380  C CB  . VAL A 885  ? 0.2731 0.2184 0.2917 0.0377  -0.0141 -0.0329 883  VAL A CB  
6381  C CG1 . VAL A 885  ? 0.2624 0.2042 0.2848 0.0381  -0.0178 -0.0364 883  VAL A CG1 
6382  C CG2 . VAL A 885  ? 0.2922 0.2367 0.3061 0.0336  -0.0116 -0.0266 883  VAL A CG2 
6383  N N   . GLY A 886  ? 0.2474 0.2065 0.2646 0.0482  -0.0140 -0.0485 884  GLY A N   
6384  C CA  . GLY A 886  ? 0.2374 0.1995 0.2588 0.0527  -0.0164 -0.0561 884  GLY A CA  
6385  C C   . GLY A 886  ? 0.2528 0.2086 0.2809 0.0530  -0.0213 -0.0598 884  GLY A C   
6386  O O   . GLY A 886  ? 0.2699 0.2183 0.3006 0.0494  -0.0233 -0.0557 884  GLY A O   
6387  N N   . PRO A 887  ? 0.2608 0.2197 0.2921 0.0573  -0.0236 -0.0676 885  PRO A N   
6388  C CA  . PRO A 887  ? 0.2491 0.2020 0.2882 0.0579  -0.0290 -0.0719 885  PRO A CA  
6389  C C   . PRO A 887  ? 0.2552 0.2066 0.2918 0.0562  -0.0296 -0.0721 885  PRO A C   
6390  O O   . PRO A 887  ? 0.2758 0.2322 0.3045 0.0554  -0.0260 -0.0703 885  PRO A O   
6391  C CB  . PRO A 887  ? 0.2606 0.2191 0.3032 0.0637  -0.0307 -0.0810 885  PRO A CB  
6392  C CG  . PRO A 887  ? 0.2628 0.2321 0.2966 0.0656  -0.0259 -0.0819 885  PRO A CG  
6393  C CD  . PRO A 887  ? 0.2790 0.2481 0.3072 0.0618  -0.0216 -0.0731 885  PRO A CD  
6394  N N   . VAL A 888  ? 0.2637 0.2081 0.3076 0.0554  -0.0345 -0.0740 886  VAL A N   
6395  C CA  . VAL A 888  ? 0.2707 0.2148 0.3139 0.0552  -0.0361 -0.0768 886  VAL A CA  
6396  C C   . VAL A 888  ? 0.2984 0.2487 0.3429 0.0606  -0.0377 -0.0867 886  VAL A C   
6397  O O   . VAL A 888  ? 0.2701 0.2229 0.3187 0.0644  -0.0389 -0.0917 886  VAL A O   
6398  C CB  . VAL A 888  ? 0.2860 0.2206 0.3367 0.0519  -0.0406 -0.0744 886  VAL A CB  
6399  C CG1 . VAL A 888  ? 0.3023 0.2325 0.3509 0.0466  -0.0387 -0.0647 886  VAL A CG1 
6400  C CG2 . VAL A 888  ? 0.3044 0.2341 0.3662 0.0540  -0.0460 -0.0789 886  VAL A CG2 
6401  N N   . ILE A 889  ? 0.2760 0.2295 0.3169 0.0611  -0.0376 -0.0896 887  ILE A N   
6402  C CA  . ILE A 889  ? 0.2920 0.2549 0.3303 0.0661  -0.0372 -0.0979 887  ILE A CA  
6403  C C   . ILE A 889  ? 0.3231 0.2844 0.3710 0.0701  -0.0427 -0.1070 887  ILE A C   
6404  O O   . ILE A 889  ? 0.3092 0.2784 0.3571 0.0750  -0.0425 -0.1141 887  ILE A O   
6405  C CB  . ILE A 889  ? 0.2769 0.2441 0.3087 0.0653  -0.0357 -0.0981 887  ILE A CB  
6406  C CG1 . ILE A 889  ? 0.2947 0.2735 0.3227 0.0705  -0.0347 -0.1060 887  ILE A CG1 
6407  C CG2 . ILE A 889  ? 0.2753 0.2346 0.3125 0.0631  -0.0401 -0.0988 887  ILE A CG2 
6408  C CD1 . ILE A 889  ? 0.2832 0.2713 0.3052 0.0724  -0.0300 -0.1045 887  ILE A CD1 
6409  N N   . THR A 890  ? 0.2669 0.2185 0.3236 0.0683  -0.0478 -0.1072 888  THR A N   
6410  C CA  . THR A 890  ? 0.2721 0.2213 0.3392 0.0720  -0.0537 -0.1161 888  THR A CA  
6411  C C   . THR A 890  ? 0.2948 0.2323 0.3725 0.0692  -0.0583 -0.1125 888  THR A C   
6412  O O   . THR A 890  ? 0.2997 0.2312 0.3765 0.0641  -0.0573 -0.1034 888  THR A O   
6413  C CB  . THR A 890  ? 0.3149 0.2652 0.3831 0.0733  -0.0567 -0.1226 888  THR A CB  
6414  O OG1 . THR A 890  ? 0.3153 0.2583 0.3839 0.0681  -0.0577 -0.1162 888  THR A OG1 
6415  C CG2 . THR A 890  ? 0.3237 0.2864 0.3821 0.0763  -0.0528 -0.1267 888  THR A CG2 
6416  N N   . SER A 891  ? 0.2945 0.2310 0.3819 0.0715  -0.0631 -0.1181 889  SER A N   
6417  C CA  A SER A 891  ? 0.3154 0.2423 0.4138 0.0684  -0.0681 -0.1142 889  SER A CA  
6418  C CA  B SER A 891  ? 0.3154 0.2423 0.4137 0.0683  -0.0680 -0.1140 889  SER A CA  
6419  C C   . SER A 891  ? 0.3370 0.2572 0.4384 0.0643  -0.0710 -0.1109 889  SER A C   
6420  O O   . SER A 891  ? 0.3373 0.2491 0.4444 0.0601  -0.0732 -0.1040 889  SER A O   
6421  C CB  A SER A 891  ? 0.3312 0.2606 0.4389 0.0712  -0.0726 -0.1204 889  SER A CB  
6422  C CB  B SER A 891  ? 0.3313 0.2605 0.4389 0.0711  -0.0724 -0.1200 889  SER A CB  
6423  O OG  A SER A 891  ? 0.3051 0.2403 0.4113 0.0746  -0.0703 -0.1229 889  SER A OG  
6424  O OG  B SER A 891  ? 0.3687 0.3027 0.4781 0.0732  -0.0750 -0.1272 889  SER A OG  
6425  N N   . GLU A 892  ? 0.3233 0.2477 0.4211 0.0653  -0.0710 -0.1156 890  GLU A N   
6426  C CA  . GLU A 892  ? 0.3438 0.2624 0.4442 0.0616  -0.0737 -0.1127 890  GLU A CA  
6427  C C   . GLU A 892  ? 0.3645 0.2785 0.4583 0.0576  -0.0701 -0.1044 890  GLU A C   
6428  O O   . GLU A 892  ? 0.3723 0.2792 0.4708 0.0529  -0.0724 -0.0980 890  GLU A O   
6429  C CB  . GLU A 892  ? 0.3513 0.2764 0.4486 0.0638  -0.0742 -0.1197 890  GLU A CB  
6430  C CG  . GLU A 892  ? 0.4452 0.3765 0.5482 0.0679  -0.0775 -0.1282 890  GLU A CG  
6431  C CD  . GLU A 892  ? 0.4422 0.3847 0.5372 0.0728  -0.0733 -0.1339 890  GLU A CD  
6432  O OE1 . GLU A 892  ? 0.4138 0.3577 0.5078 0.0742  -0.0711 -0.1327 890  GLU A OE1 
6433  O OE2 . GLU A 892  ? 0.5540 0.5045 0.6437 0.0751  -0.0723 -0.1392 890  GLU A OE2 
6434  N N   . ALA A 893  ? 0.3359 0.2575 0.4180 0.0580  -0.0637 -0.1020 891  ALA A N   
6435  C CA  . ALA A 893  ? 0.3259 0.2466 0.4005 0.0530  -0.0592 -0.0919 891  ALA A CA  
6436  C C   . ALA A 893  ? 0.3466 0.2608 0.4262 0.0498  -0.0600 -0.0845 891  ALA A C   
6437  O O   . ALA A 893  ? 0.3427 0.2522 0.4231 0.0449  -0.0602 -0.0769 891  ALA A O   
6438  C CB  . ALA A 893  ? 0.2743 0.2042 0.3367 0.0543  -0.0527 -0.0910 891  ALA A CB  
6439  N N   . LYS A 894  ? 0.3244 0.2390 0.4078 0.0526  -0.0607 -0.0869 892  LYS A N   
6440  C CA  . LYS A 894  ? 0.3169 0.2256 0.4058 0.0499  -0.0619 -0.0803 892  LYS A CA  
6441  C C   . LYS A 894  ? 0.3594 0.2593 0.4594 0.0467  -0.0679 -0.0776 892  LYS A C   
6442  O O   . LYS A 894  ? 0.3374 0.2332 0.4383 0.0419  -0.0677 -0.0688 892  LYS A O   
6443  C CB  . LYS A 894  ? 0.3004 0.2109 0.3932 0.0541  -0.0626 -0.0848 892  LYS A CB  
6444  C CG  . LYS A 894  ? 0.3653 0.2700 0.4645 0.0518  -0.0642 -0.0785 892  LYS A CG  
6445  C CD  . LYS A 894  ? 0.3666 0.2735 0.4700 0.0564  -0.0650 -0.0838 892  LYS A CD  
6446  C CE  . LYS A 894  ? 0.3766 0.2783 0.4860 0.0541  -0.0665 -0.0772 892  LYS A CE  
6447  N NZ  . LYS A 894  ? 0.5298 0.4324 0.6462 0.0587  -0.0689 -0.0831 892  LYS A NZ  
6448  N N   . ASP A 895  ? 0.3448 0.2421 0.4534 0.0494  -0.0733 -0.0852 893  ASP A N   
6449  C CA  . ASP A 895  ? 0.3792 0.2698 0.4987 0.0458  -0.0789 -0.0818 893  ASP A CA  
6450  C C   . ASP A 895  ? 0.3519 0.2393 0.4688 0.0411  -0.0785 -0.0757 893  ASP A C   
6451  O O   . ASP A 895  ? 0.3585 0.2403 0.4812 0.0365  -0.0808 -0.0681 893  ASP A O   
6452  C CB  . ASP A 895  ? 0.3718 0.2651 0.4988 0.0485  -0.0835 -0.0896 893  ASP A CB  
6453  C CG  . ASP A 895  ? 0.4310 0.3276 0.5627 0.0525  -0.0848 -0.0948 893  ASP A CG  
6454  O OD1 . ASP A 895  ? 0.4982 0.3934 0.6302 0.0523  -0.0835 -0.0909 893  ASP A OD1 
6455  O OD2 . ASP A 895  ? 0.5071 0.4080 0.6423 0.0560  -0.0874 -0.1029 893  ASP A OD2 
6456  N N   . ASN A 896  ? 0.3551 0.2478 0.4625 0.0417  -0.0750 -0.0782 894  ASN A N   
6457  C CA  . ASN A 896  ? 0.3518 0.2438 0.4555 0.0370  -0.0737 -0.0720 894  ASN A CA  
6458  C C   . ASN A 896  ? 0.3594 0.2516 0.4574 0.0325  -0.0695 -0.0616 894  ASN A C   
6459  O O   . ASN A 896  ? 0.3490 0.2378 0.4499 0.0278  -0.0708 -0.0544 894  ASN A O   
6460  C CB  . ASN A 896  ? 0.3752 0.2737 0.4693 0.0388  -0.0703 -0.0765 894  ASN A CB  
6461  C CG  . ASN A 896  ? 0.4711 0.3705 0.5700 0.0431  -0.0744 -0.0871 894  ASN A CG  
6462  O OD1 . ASN A 896  ? 0.5595 0.4532 0.6702 0.0434  -0.0806 -0.0900 894  ASN A OD1 
6463  N ND2 . ASN A 896  ? 0.4783 0.3855 0.5685 0.0465  -0.0710 -0.0927 894  ASN A ND2 
6464  N N   . ILE A 897  ? 0.3346 0.2315 0.4245 0.0341  -0.0644 -0.0607 895  ILE A N   
6465  C CA  . ILE A 897  ? 0.3111 0.2089 0.3954 0.0302  -0.0603 -0.0516 895  ILE A CA  
6466  C C   . ILE A 897  ? 0.3461 0.2380 0.4395 0.0274  -0.0639 -0.0458 895  ILE A C   
6467  O O   . ILE A 897  ? 0.3260 0.2165 0.4195 0.0226  -0.0635 -0.0376 895  ILE A O   
6468  C CB  . ILE A 897  ? 0.3152 0.2191 0.3900 0.0327  -0.0547 -0.0526 895  ILE A CB  
6469  C CG1 . ILE A 897  ? 0.3099 0.2200 0.3757 0.0352  -0.0512 -0.0574 895  ILE A CG1 
6470  C CG2 . ILE A 897  ? 0.3299 0.2345 0.3994 0.0289  -0.0508 -0.0437 895  ILE A CG2 
6471  C CD1 . ILE A 897  ? 0.2965 0.2130 0.3557 0.0389  -0.0471 -0.0605 895  ILE A CD1 
6472  N N   . GLU A 898  ? 0.3287 0.2179 0.4303 0.0304  -0.0675 -0.0499 896  GLU A N   
6473  C CA  . GLU A 898  ? 0.3568 0.2407 0.4678 0.0279  -0.0712 -0.0442 896  GLU A CA  
6474  C C   . GLU A 898  ? 0.3395 0.2179 0.4598 0.0240  -0.0763 -0.0402 896  GLU A C   
6475  O O   . GLU A 898  ? 0.3691 0.2450 0.4934 0.0197  -0.0776 -0.0317 896  GLU A O   
6476  C CB  . GLU A 898  ? 0.3503 0.2323 0.4688 0.0324  -0.0744 -0.0504 896  GLU A CB  
6477  C CG  . GLU A 898  ? 0.3768 0.2640 0.4878 0.0353  -0.0695 -0.0518 896  GLU A CG  
6478  C CD  . GLU A 898  ? 0.3931 0.2790 0.5121 0.0400  -0.0728 -0.0582 896  GLU A CD  
6479  O OE1 . GLU A 898  ? 0.5003 0.3836 0.6281 0.0420  -0.0779 -0.0641 896  GLU A OE1 
6480  O OE2 . GLU A 898  ? 0.5037 0.3922 0.6199 0.0413  -0.0702 -0.0571 896  GLU A OE2 
6481  N N   . LYS A 899  ? 0.3613 0.2381 0.4853 0.0253  -0.0795 -0.0460 897  LYS A N   
6482  C CA  . LYS A 899  ? 0.3527 0.2247 0.4856 0.0213  -0.0844 -0.0421 897  LYS A CA  
6483  C C   . LYS A 899  ? 0.3854 0.2598 0.5115 0.0160  -0.0808 -0.0328 897  LYS A C   
6484  O O   . LYS A 899  ? 0.3843 0.2558 0.5171 0.0114  -0.0837 -0.0251 897  LYS A O   
6485  C CB  . LYS A 899  ? 0.3617 0.2337 0.4975 0.0237  -0.0874 -0.0502 897  LYS A CB  
6486  N N   . HIS A 900  ? 0.3320 0.2123 0.4452 0.0165  -0.0747 -0.0334 898  HIS A N   
6487  C CA  . HIS A 900  ? 0.3424 0.2257 0.4491 0.0118  -0.0711 -0.0253 898  HIS A CA  
6488  C C   . HIS A 900  ? 0.3353 0.2191 0.4415 0.0088  -0.0695 -0.0169 898  HIS A C   
6489  O O   . HIS A 900  ? 0.3647 0.2485 0.4732 0.0040  -0.0702 -0.0090 898  HIS A O   
6490  C CB  . HIS A 900  ? 0.3484 0.2378 0.4420 0.0134  -0.0651 -0.0282 898  HIS A CB  
6491  C CG  . HIS A 900  ? 0.3426 0.2356 0.4286 0.0093  -0.0607 -0.0205 898  HIS A CG  
6492  N ND1 . HIS A 900  ? 0.3336 0.2269 0.4203 0.0057  -0.0615 -0.0167 898  HIS A ND1 
6493  C CD2 . HIS A 900  ? 0.3129 0.2097 0.3911 0.0084  -0.0558 -0.0163 898  HIS A CD2 
6494  C CE1 . HIS A 900  ? 0.3516 0.2490 0.4310 0.0028  -0.0571 -0.0106 898  HIS A CE1 
6495  N NE2 . HIS A 900  ? 0.3385 0.2380 0.4128 0.0044  -0.0537 -0.0104 898  HIS A NE2 
6496  N N   . ILE A 901  ? 0.3190 0.2040 0.4223 0.0115  -0.0673 -0.0186 899  ILE A N   
6497  C CA  . ILE A 901  ? 0.3604 0.2463 0.4632 0.0090  -0.0658 -0.0112 899  ILE A CA  
6498  C C   . ILE A 901  ? 0.3923 0.2733 0.5076 0.0058  -0.0716 -0.0055 899  ILE A C   
6499  O O   . ILE A 901  ? 0.3898 0.2723 0.5054 0.0013  -0.0712 0.0032  899  ILE A O   
6500  C CB  . ILE A 901  ? 0.3401 0.2275 0.4395 0.0129  -0.0634 -0.0150 899  ILE A CB  
6501  C CG1 . ILE A 901  ? 0.3248 0.2180 0.4115 0.0152  -0.0572 -0.0187 899  ILE A CG1 
6502  C CG2 . ILE A 901  ? 0.3471 0.2344 0.4486 0.0105  -0.0633 -0.0077 899  ILE A CG2 
6503  C CD1 . ILE A 901  ? 0.2846 0.1801 0.3677 0.0195  -0.0548 -0.0233 899  ILE A CD1 
6504  N N   . GLU A 902  ? 0.3727 0.2483 0.4988 0.0080  -0.0774 -0.0103 900  GLU A N   
6505  C CA  . GLU A 902  ? 0.4043 0.2748 0.5435 0.0051  -0.0834 -0.0047 900  GLU A CA  
6506  C C   . GLU A 902  ? 0.3967 0.2664 0.5402 0.0002  -0.0859 0.0012  900  GLU A C   
6507  O O   . GLU A 902  ? 0.4242 0.2941 0.5739 -0.0040 -0.0883 0.0098  900  GLU A O   
6508  C CB  . GLU A 902  ? 0.4215 0.2890 0.5705 0.0091  -0.0883 -0.0119 900  GLU A CB  
6509  C CG  . GLU A 902  ? 0.4185 0.2866 0.5655 0.0132  -0.0866 -0.0160 900  GLU A CG  
6510  C CD  . GLU A 902  ? 0.4974 0.3661 0.6426 0.0105  -0.0846 -0.0074 900  GLU A CD  
6511  O OE1 . GLU A 902  ? 0.5112 0.3801 0.6633 0.0064  -0.0874 0.0005  900  GLU A OE1 
6512  O OE2 . GLU A 902  ? 0.4642 0.3368 0.5996 0.0122  -0.0793 -0.0083 900  GLU A OE2 
6513  N N   . ARG A 903  ? 0.4043 0.2751 0.5442 0.0007  -0.0851 -0.0030 901  ARG A N   
6514  C CA  . ARG A 903  ? 0.4119 0.2833 0.5541 -0.0041 -0.0865 0.0030  901  ARG A CA  
6515  C C   . ARG A 903  ? 0.4398 0.3170 0.5744 -0.0085 -0.0819 0.0123  901  ARG A C   
6516  O O   . ARG A 903  ? 0.4591 0.3367 0.5996 -0.0133 -0.0843 0.0209  901  ARG A O   
6517  C CB  . ARG A 903  ? 0.4254 0.2978 0.5630 -0.0024 -0.0854 -0.0036 901  ARG A CB  
6518  N N   . MET A 904  ? 0.4151 0.2974 0.5368 -0.0068 -0.0754 0.0107  902  MET A N   
6519  C CA  . MET A 904  ? 0.4258 0.3142 0.5401 -0.0104 -0.0709 0.0185  902  MET A CA  
6520  C C   . MET A 904  ? 0.4104 0.2983 0.5307 -0.0129 -0.0730 0.0259  902  MET A C   
6521  O O   . MET A 904  ? 0.4310 0.3224 0.5525 -0.0176 -0.0731 0.0346  902  MET A O   
6522  C CB  . MET A 904  ? 0.3741 0.2669 0.4750 -0.0076 -0.0643 0.0147  902  MET A CB  
6523  C CG  . MET A 904  ? 0.3680 0.2627 0.4619 -0.0056 -0.0616 0.0088  902  MET A CG  
6524  S SD  . MET A 904  ? 0.4708 0.3689 0.5635 -0.0105 -0.0612 0.0145  902  MET A SD  
6525  C CE  . MET A 904  ? 0.4720 0.3646 0.5742 -0.0095 -0.0670 0.0093  902  MET A CE  
6526  N N   . ARG A 905  ? 0.3889 0.2734 0.5129 -0.0097 -0.0745 0.0227  903  ARG A N   
6527  C CA  . ARG A 905  ? 0.4238 0.3077 0.5540 -0.0119 -0.0768 0.0296  903  ARG A CA  
6528  C C   . ARG A 905  ? 0.4830 0.3637 0.6264 -0.0159 -0.0832 0.0361  903  ARG A C   
6529  O O   . ARG A 905  ? 0.4717 0.3553 0.6182 -0.0199 -0.0841 0.0452  903  ARG A O   
6530  C CB  . ARG A 905  ? 0.4147 0.2950 0.5476 -0.0073 -0.0779 0.0241  903  ARG A CB  
6531  C CG  . ARG A 905  ? 0.4637 0.3454 0.5982 -0.0088 -0.0778 0.0304  903  ARG A CG  
6532  C CD  . ARG A 905  ? 0.4383 0.3156 0.5786 -0.0044 -0.0803 0.0251  903  ARG A CD  
6533  N NE  . ARG A 905  ? 0.4462 0.3238 0.5794 0.0009  -0.0771 0.0150  903  ARG A NE  
6534  C CZ  . ARG A 905  ? 0.4450 0.3264 0.5689 0.0032  -0.0720 0.0127  903  ARG A CZ  
6535  N NH1 . ARG A 905  ? 0.4298 0.3150 0.5494 0.0009  -0.0692 0.0192  903  ARG A NH1 
6536  N NH2 . ARG A 905  ? 0.4321 0.3140 0.5511 0.0081  -0.0697 0.0037  903  ARG A NH2 
6537  N N   . GLY A 906  ? 0.4456 0.3223 0.5961 -0.0147 -0.0873 0.0313  904  GLY A N   
6538  C CA  . GLY A 906  ? 0.4888 0.3669 0.6501 -0.0180 -0.0923 0.0363  904  GLY A CA  
6539  C C   . GLY A 906  ? 0.5059 0.3887 0.6657 -0.0235 -0.0913 0.0451  904  GLY A C   
6540  O O   . GLY A 906  ? 0.5644 0.4505 0.7321 -0.0272 -0.0946 0.0523  904  GLY A O   
6541  N N   . LEU A 907  ? 0.5009 0.3847 0.6510 -0.0242 -0.0870 0.0446  905  LEU A N   
6542  C CA  . LEU A 907  ? 0.4933 0.3830 0.6407 -0.0294 -0.0854 0.0528  905  LEU A CA  
6543  C C   . LEU A 907  ? 0.4938 0.3905 0.6358 -0.0322 -0.0820 0.0608  905  LEU A C   
6544  O O   . LEU A 907  ? 0.4979 0.4015 0.6368 -0.0363 -0.0801 0.0676  905  LEU A O   
6545  C CB  . LEU A 907  ? 0.5061 0.3991 0.6430 -0.0281 -0.0808 0.0476  905  LEU A CB  
6546  C CG  . LEU A 907  ? 0.5153 0.4027 0.6562 -0.0254 -0.0838 0.0394  905  LEU A CG  
6547  C CD1 . LEU A 907  ? 0.5355 0.4271 0.6651 -0.0242 -0.0787 0.0350  905  LEU A CD1 
6548  C CD2 . LEU A 907  ? 0.5651 0.4496 0.7195 -0.0288 -0.0903 0.0438  905  LEU A CD2 
6549  N N   . GLY A 908  ? 0.4379 0.3337 0.5788 -0.0300 -0.0811 0.0600  906  GLY A N   
6550  C CA  . GLY A 908  ? 0.4802 0.3826 0.6158 -0.0323 -0.0780 0.0669  906  GLY A CA  
6551  C C   . GLY A 908  ? 0.4125 0.3206 0.5333 -0.0303 -0.0707 0.0633  906  GLY A C   
6552  O O   . GLY A 908  ? 0.4322 0.3465 0.5480 -0.0322 -0.0678 0.0685  906  GLY A O   
6553  N N   . ARG A 909  ? 0.4116 0.3178 0.5255 -0.0266 -0.0678 0.0546  907  ARG A N   
6554  C CA  . ARG A 909  ? 0.3493 0.2604 0.4501 -0.0246 -0.0613 0.0512  907  ARG A CA  
6555  C C   . ARG A 909  ? 0.3831 0.2933 0.4813 -0.0219 -0.0597 0.0493  907  ARG A C   
6556  O O   . ARG A 909  ? 0.4035 0.3078 0.5081 -0.0192 -0.0629 0.0459  907  ARG A O   
6557  C CB  . ARG A 909  ? 0.3893 0.2985 0.4845 -0.0213 -0.0591 0.0427  907  ARG A CB  
6558  C CG  . ARG A 909  ? 0.3940 0.3031 0.4926 -0.0235 -0.0612 0.0435  907  ARG A CG  
6559  C CD  . ARG A 909  ? 0.4470 0.3641 0.5402 -0.0275 -0.0581 0.0498  907  ARG A CD  
6560  N NE  . ARG A 909  ? 0.5160 0.4334 0.6109 -0.0290 -0.0592 0.0495  907  ARG A NE  
6561  C CZ  . ARG A 909  ? 0.5699 0.4879 0.6735 -0.0330 -0.0633 0.0556  907  ARG A CZ  
6562  N NH1 . ARG A 909  ? 0.5704 0.4888 0.6819 -0.0361 -0.0667 0.0630  907  ARG A NH1 
6563  N NH2 . ARG A 909  ? 0.5290 0.4472 0.6335 -0.0341 -0.0641 0.0545  907  ARG A NH2 
6564  N N   . LYS A 910  ? 0.3357 0.2521 0.4249 -0.0225 -0.0549 0.0514  908  LYS A N   
6565  C CA  . LYS A 910  ? 0.3418 0.2581 0.4280 -0.0201 -0.0531 0.0498  908  LYS A CA  
6566  C C   . LYS A 910  ? 0.3716 0.2844 0.4531 -0.0149 -0.0509 0.0405  908  LYS A C   
6567  O O   . LYS A 910  ? 0.3134 0.2279 0.3875 -0.0136 -0.0475 0.0363  908  LYS A O   
6568  C CB  . LYS A 910  ? 0.3529 0.2771 0.4308 -0.0221 -0.0487 0.0541  908  LYS A CB  
6569  C CG  . LYS A 910  ? 0.4201 0.3494 0.5024 -0.0270 -0.0507 0.0636  908  LYS A CG  
6570  C CD  . LYS A 910  ? 0.4022 0.3398 0.4760 -0.0283 -0.0462 0.0666  908  LYS A CD  
6571  C CE  . LYS A 910  ? 0.4434 0.3796 0.5136 -0.0253 -0.0443 0.0632  908  LYS A CE  
6572  N NZ  . LYS A 910  ? 0.5212 0.4654 0.5854 -0.0271 -0.0412 0.0673  908  LYS A NZ  
6573  N N   . VAL A 911  ? 0.3305 0.2389 0.4164 -0.0120 -0.0529 0.0374  909  VAL A N   
6574  C CA  . VAL A 911  ? 0.3338 0.2394 0.4166 -0.0070 -0.0514 0.0287  909  VAL A CA  
6575  C C   . VAL A 911  ? 0.3283 0.2353 0.4079 -0.0050 -0.0491 0.0281  909  VAL A C   
6576  O O   . VAL A 911  ? 0.3120 0.2176 0.3980 -0.0058 -0.0519 0.0318  909  VAL A O   
6577  C CB  . VAL A 911  ? 0.3737 0.2727 0.4662 -0.0046 -0.0566 0.0240  909  VAL A CB  
6578  C CG1 . VAL A 911  ? 0.3245 0.2222 0.4133 0.0008  -0.0548 0.0147  909  VAL A CG1 
6579  C CG2 . VAL A 911  ? 0.3649 0.2624 0.4611 -0.0068 -0.0591 0.0246  909  VAL A CG2 
6580  N N   . GLU A 912  ? 0.3096 0.2194 0.3798 -0.0026 -0.0443 0.0238  910  GLU A N   
6581  C CA  . GLU A 912  ? 0.3079 0.2194 0.3743 -0.0004 -0.0417 0.0224  910  GLU A CA  
6582  C C   . GLU A 912  ? 0.3466 0.2559 0.4122 0.0046  -0.0411 0.0141  910  GLU A C   
6583  O O   . GLU A 912  ? 0.3016 0.2115 0.3625 0.0061  -0.0393 0.0097  910  GLU A O   
6584  C CB  . GLU A 912  ? 0.3029 0.2203 0.3594 -0.0019 -0.0365 0.0246  910  GLU A CB  
6585  C CG  . GLU A 912  ? 0.3175 0.2370 0.3705 -0.0004 -0.0339 0.0244  910  GLU A CG  
6586  C CD  . GLU A 912  ? 0.3376 0.2579 0.3955 -0.0029 -0.0362 0.0306  910  GLU A CD  
6587  O OE1 . GLU A 912  ? 0.3750 0.2957 0.4371 -0.0064 -0.0387 0.0362  910  GLU A OE1 
6588  O OE2 . GLU A 912  ? 0.3627 0.2835 0.4204 -0.0013 -0.0354 0.0303  910  GLU A OE2 
6589  N N   . GLN A 913  ? 0.2921 0.1994 0.3623 0.0071  -0.0429 0.0121  911  GLN A N   
6590  C CA  . GLN A 913  ? 0.3031 0.2095 0.3725 0.0120  -0.0422 0.0042  911  GLN A CA  
6591  C C   . GLN A 913  ? 0.3469 0.2554 0.4148 0.0142  -0.0404 0.0035  911  GLN A C   
6592  O O   . GLN A 913  ? 0.3292 0.2368 0.4015 0.0128  -0.0421 0.0079  911  GLN A O   
6593  C CB  . GLN A 913  ? 0.3108 0.2121 0.3901 0.0142  -0.0476 0.0000  911  GLN A CB  
6594  C CG  . GLN A 913  ? 0.3326 0.2317 0.4142 0.0126  -0.0498 -0.0005 911  GLN A CG  
6595  C CD  . GLN A 913  ? 0.3446 0.2388 0.4355 0.0155  -0.0549 -0.0064 911  GLN A CD  
6596  O OE1 . GLN A 913  ? 0.3885 0.2787 0.4893 0.0155  -0.0595 -0.0052 911  GLN A OE1 
6597  N NE2 . GLN A 913  ? 0.3407 0.2355 0.4287 0.0181  -0.0542 -0.0131 911  GLN A NE2 
6598  N N   . ILE A 914  ? 0.3486 0.2601 0.4102 0.0175  -0.0368 -0.0018 912  ILE A N   
6599  C CA  . ILE A 914  ? 0.3595 0.2729 0.4206 0.0203  -0.0354 -0.0037 912  ILE A CA  
6600  C C   . ILE A 914  ? 0.3614 0.2712 0.4319 0.0234  -0.0398 -0.0078 912  ILE A C   
6601  O O   . ILE A 914  ? 0.3623 0.2694 0.4370 0.0253  -0.0427 -0.0125 912  ILE A O   
6602  C CB  . ILE A 914  ? 0.3781 0.2962 0.4308 0.0230  -0.0307 -0.0082 912  ILE A CB  
6603  C CG1 . ILE A 914  ? 0.3666 0.2876 0.4108 0.0203  -0.0269 -0.0053 912  ILE A CG1 
6604  C CG2 . ILE A 914  ? 0.4363 0.3573 0.4878 0.0251  -0.0288 -0.0087 912  ILE A CG2 
6605  C CD1 . ILE A 914  ? 0.3505 0.2756 0.3877 0.0230  -0.0230 -0.0096 912  ILE A CD1 
6606  N N   . GLY A 915  ? 0.4042 0.3140 0.4783 0.0242  -0.0406 -0.0063 913  GLY A N   
6607  C CA  . GLY A 915  ? 0.3868 0.2939 0.4694 0.0280  -0.0444 -0.0112 913  GLY A CA  
6608  C C   . GLY A 915  ? 0.3917 0.3030 0.4702 0.0329  -0.0417 -0.0188 913  GLY A C   
6609  O O   . GLY A 915  ? 0.4744 0.3907 0.5448 0.0333  -0.0370 -0.0186 913  GLY A O   
6610  N N   . LEU A 916  ? 0.4021 0.3116 0.4866 0.0366  -0.0449 -0.0257 914  LEU A N   
6611  C CA  . LEU A 916  ? 0.4104 0.3249 0.4916 0.0415  -0.0427 -0.0335 914  LEU A CA  
6612  C C   . LEU A 916  ? 0.4422 0.3579 0.5284 0.0450  -0.0438 -0.0364 914  LEU A C   
6613  O O   . LEU A 916  ? 0.4219 0.3330 0.5176 0.0449  -0.0482 -0.0351 914  LEU A O   
6614  C CB  . LEU A 916  ? 0.3812 0.2943 0.4653 0.0439  -0.0454 -0.0403 914  LEU A CB  
6615  C CG  . LEU A 916  ? 0.3753 0.2879 0.4540 0.0410  -0.0441 -0.0384 914  LEU A CG  
6616  C CD1 . LEU A 916  ? 0.4100 0.3222 0.4915 0.0440  -0.0467 -0.0461 914  LEU A CD1 
6617  C CD2 . LEU A 916  ? 0.4003 0.3188 0.4672 0.0398  -0.0379 -0.0360 914  LEU A CD2 
6618  N N   . ALA A 917  ? 0.4314 0.3539 0.5118 0.0481  -0.0399 -0.0401 915  ALA A N   
6619  C CA  . ALA A 917  ? 0.4225 0.3475 0.5073 0.0520  -0.0405 -0.0435 915  ALA A CA  
6620  C C   . ALA A 917  ? 0.4325 0.3562 0.5258 0.0566  -0.0449 -0.0520 915  ALA A C   
6621  O O   . ALA A 917  ? 0.4199 0.3433 0.5129 0.0578  -0.0461 -0.0567 915  ALA A O   
6622  C CB  . ALA A 917  ? 0.4626 0.3961 0.5389 0.0538  -0.0350 -0.0448 915  ALA A CB  
6623  N N   . SER A 918  ? 0.4169 0.3398 0.5182 0.0594  -0.0476 -0.0543 916  SER A N   
6624  C CA  . SER A 918  ? 0.4682 0.3899 0.5789 0.0642  -0.0523 -0.0629 916  SER A CA  
6625  C C   . SER A 918  ? 0.4461 0.3756 0.5517 0.0688  -0.0499 -0.0716 916  SER A C   
6626  O O   . SER A 918  ? 0.4120 0.3403 0.5230 0.0719  -0.0535 -0.0789 916  SER A O   
6627  C CB  . SER A 918  ? 0.4468 0.3679 0.5659 0.0668  -0.0548 -0.0639 916  SER A CB  
6628  O OG  . SER A 918  ? 0.5554 0.4756 0.6840 0.0719  -0.0594 -0.0729 916  SER A OG  
6629  N N   . GLU A 919  ? 0.4290 0.3667 0.5244 0.0692  -0.0440 -0.0707 917  GLU A N   
6630  C CA  . GLU A 919  ? 0.4217 0.3683 0.5118 0.0733  -0.0414 -0.0781 917  GLU A CA  
6631  C C   . GLU A 919  ? 0.4067 0.3524 0.4936 0.0726  -0.0419 -0.0805 917  GLU A C   
6632  O O   . GLU A 919  ? 0.3974 0.3493 0.4826 0.0766  -0.0415 -0.0882 917  GLU A O   
6633  C CB  . GLU A 919  ? 0.5048 0.4600 0.5848 0.0729  -0.0350 -0.0748 917  GLU A CB  
6634  C CG  . GLU A 919  ? 0.5642 0.5239 0.6467 0.0754  -0.0340 -0.0753 917  GLU A CG  
6635  C CD  . GLU A 919  ? 0.6209 0.5753 0.7046 0.0713  -0.0338 -0.0667 917  GLU A CD  
6636  O OE1 . GLU A 919  ? 0.5733 0.5198 0.6580 0.0669  -0.0356 -0.0610 917  GLU A OE1 
6637  O OE2 . GLU A 919  ? 0.6578 0.6167 0.7413 0.0725  -0.0319 -0.0656 917  GLU A OE2 
6638  N N   . THR A 920  ? 0.4091 0.3478 0.4949 0.0676  -0.0426 -0.0742 918  THR A N   
6639  C CA  . THR A 920  ? 0.3746 0.3124 0.4576 0.0668  -0.0432 -0.0764 918  THR A CA  
6640  C C   . THR A 920  ? 0.3675 0.3018 0.4602 0.0701  -0.0491 -0.0843 918  THR A C   
6641  O O   . THR A 920  ? 0.3450 0.2804 0.4358 0.0708  -0.0497 -0.0885 918  THR A O   
6642  C CB  . THR A 920  ? 0.3552 0.2868 0.4354 0.0607  -0.0428 -0.0678 918  THR A CB  
6643  O OG1 . THR A 920  ? 0.3755 0.2986 0.4651 0.0584  -0.0474 -0.0641 918  THR A OG1 
6644  C CG2 . THR A 920  ? 0.3586 0.2939 0.4293 0.0577  -0.0371 -0.0607 918  THR A CG2 
6645  N N   . GLY A 921  ? 0.3881 0.3181 0.4916 0.0720  -0.0536 -0.0866 919  GLY A N   
6646  C CA  . GLY A 921  ? 0.3857 0.3113 0.4996 0.0746  -0.0598 -0.0936 919  GLY A CA  
6647  C C   . GLY A 921  ? 0.3595 0.2943 0.4707 0.0789  -0.0591 -0.1031 919  GLY A C   
6648  O O   . GLY A 921  ? 0.3977 0.3315 0.5130 0.0789  -0.0628 -0.1072 919  GLY A O   
6649  N N   . VAL A 922  ? 0.3766 0.3209 0.4807 0.0827  -0.0545 -0.1066 920  VAL A N   
6650  C CA  . VAL A 922  ? 0.3258 0.2804 0.4266 0.0867  -0.0536 -0.1151 920  VAL A CA  
6651  C C   . VAL A 922  ? 0.3584 0.3155 0.4512 0.0861  -0.0514 -0.1161 920  VAL A C   
6652  O O   . VAL A 922  ? 0.3531 0.3184 0.4435 0.0889  -0.0513 -0.1228 920  VAL A O   
6653  C CB  . VAL A 922  ? 0.3633 0.3289 0.4595 0.0907  -0.0494 -0.1180 920  VAL A CB  
6654  C CG1 . VAL A 922  ? 0.3654 0.3301 0.4701 0.0922  -0.0522 -0.1192 920  VAL A CG1 
6655  C CG2 . VAL A 922  ? 0.3192 0.2868 0.4061 0.0885  -0.0436 -0.1107 920  VAL A CG2 
6656  N N   . GLY A 923  ? 0.3311 0.2827 0.4191 0.0814  -0.0495 -0.1083 921  GLY A N   
6657  C CA  . GLY A 923  ? 0.3206 0.2744 0.4009 0.0796  -0.0475 -0.1077 921  GLY A CA  
6658  C C   . GLY A 923  ? 0.3119 0.2552 0.3962 0.0751  -0.0509 -0.1035 921  GLY A C   
6659  O O   . GLY A 923  ? 0.3326 0.2675 0.4271 0.0743  -0.0559 -0.1030 921  GLY A O   
6660  N N   . THR A 924  ? 0.3038 0.2478 0.3806 0.0721  -0.0485 -0.1000 922  THR A N   
6661  C CA  . THR A 924  ? 0.3010 0.2362 0.3809 0.0677  -0.0514 -0.0958 922  THR A CA  
6662  C C   . THR A 924  ? 0.3075 0.2413 0.3795 0.0623  -0.0470 -0.0854 922  THR A C   
6663  O O   . THR A 924  ? 0.3031 0.2417 0.3660 0.0612  -0.0431 -0.0837 922  THR A O   
6664  C CB  . THR A 924  ? 0.2865 0.2234 0.3659 0.0692  -0.0533 -0.1020 922  THR A CB  
6665  O OG1 . THR A 924  ? 0.2753 0.2221 0.3437 0.0706  -0.0482 -0.1033 922  THR A OG1 
6666  C CG2 . THR A 924  ? 0.2862 0.2235 0.3751 0.0741  -0.0585 -0.1123 922  THR A CG2 
6667  N N   . PHE A 925  ? 0.2839 0.2115 0.3599 0.0589  -0.0480 -0.0785 923  PHE A N   
6668  C CA  . PHE A 925  ? 0.2812 0.2079 0.3504 0.0541  -0.0440 -0.0691 923  PHE A CA  
6669  C C   . PHE A 925  ? 0.2970 0.2153 0.3712 0.0492  -0.0472 -0.0630 923  PHE A C   
6670  O O   . PHE A 925  ? 0.3245 0.2367 0.4090 0.0492  -0.0524 -0.0637 923  PHE A O   
6671  C CB  . PHE A 925  ? 0.2774 0.2059 0.3455 0.0541  -0.0415 -0.0653 923  PHE A CB  
6672  C CG  . PHE A 925  ? 0.2943 0.2320 0.3562 0.0579  -0.0374 -0.0692 923  PHE A CG  
6673  C CD1 . PHE A 925  ? 0.2800 0.2215 0.3464 0.0632  -0.0392 -0.0771 923  PHE A CD1 
6674  C CD2 . PHE A 925  ? 0.2654 0.2083 0.3173 0.0562  -0.0319 -0.0648 923  PHE A CD2 
6675  C CE1 . PHE A 925  ? 0.2678 0.2190 0.3285 0.0666  -0.0353 -0.0802 923  PHE A CE1 
6676  C CE2 . PHE A 925  ? 0.2704 0.2223 0.3171 0.0593  -0.0282 -0.0675 923  PHE A CE2 
6677  C CZ  . PHE A 925  ? 0.2711 0.2275 0.3219 0.0645  -0.0298 -0.0750 923  PHE A CZ  
6678  N N   . VAL A 926  ? 0.2837 0.2022 0.3508 0.0452  -0.0440 -0.0567 924  VAL A N   
6679  C CA  . VAL A 926  ? 0.2831 0.1956 0.3531 0.0401  -0.0457 -0.0494 924  VAL A CA  
6680  C C   . VAL A 926  ? 0.2734 0.1879 0.3367 0.0369  -0.0413 -0.0419 924  VAL A C   
6681  O O   . VAL A 926  ? 0.2797 0.1994 0.3339 0.0371  -0.0365 -0.0414 924  VAL A O   
6682  C CB  . VAL A 926  ? 0.2834 0.1949 0.3516 0.0380  -0.0464 -0.0494 924  VAL A CB  
6683  C CG1 . VAL A 926  ? 0.3030 0.2102 0.3726 0.0325  -0.0471 -0.0410 924  VAL A CG1 
6684  C CG2 . VAL A 926  ? 0.2893 0.1982 0.3654 0.0409  -0.0515 -0.0569 924  VAL A CG2 
6685  N N   . PRO A 927  ? 0.2953 0.2061 0.3631 0.0341  -0.0428 -0.0359 925  PRO A N   
6686  C CA  . PRO A 927  ? 0.3029 0.2161 0.3643 0.0313  -0.0386 -0.0294 925  PRO A CA  
6687  C C   . PRO A 927  ? 0.2847 0.1988 0.3397 0.0276  -0.0361 -0.0249 925  PRO A C   
6688  O O   . PRO A 927  ? 0.2773 0.1882 0.3355 0.0255  -0.0388 -0.0238 925  PRO A O   
6689  C CB  . PRO A 927  ? 0.3263 0.2352 0.3954 0.0292  -0.0418 -0.0244 925  PRO A CB  
6690  C CG  . PRO A 927  ? 0.3349 0.2381 0.4135 0.0288  -0.0475 -0.0257 925  PRO A CG  
6691  C CD  . PRO A 927  ? 0.3066 0.2110 0.3857 0.0331  -0.0485 -0.0346 925  PRO A CD  
6692  N N   . PRO A 928  ? 0.2920 0.2105 0.3384 0.0268  -0.0312 -0.0225 926  PRO A N   
6693  C CA  . PRO A 928  ? 0.2748 0.1940 0.3158 0.0229  -0.0289 -0.0175 926  PRO A CA  
6694  C C   . PRO A 928  ? 0.2561 0.1716 0.3023 0.0188  -0.0318 -0.0115 926  PRO A C   
6695  O O   . PRO A 928  ? 0.2705 0.1844 0.3212 0.0179  -0.0334 -0.0083 926  PRO A O   
6696  C CB  . PRO A 928  ? 0.2643 0.1881 0.2980 0.0228  -0.0241 -0.0152 926  PRO A CB  
6697  C CG  . PRO A 928  ? 0.3168 0.2436 0.3493 0.0272  -0.0231 -0.0210 926  PRO A CG  
6698  C CD  . PRO A 928  ? 0.2884 0.2117 0.3297 0.0295  -0.0276 -0.0245 926  PRO A CD  
6699  N N   . THR A 929  ? 0.2537 0.1683 0.2994 0.0163  -0.0324 -0.0097 927  THR A N   
6700  C CA  . THR A 929  ? 0.2680 0.1794 0.3198 0.0126  -0.0358 -0.0045 927  THR A CA  
6701  C C   . THR A 929  ? 0.2785 0.1926 0.3247 0.0089  -0.0333 0.0000  927  THR A C   
6702  O O   . THR A 929  ? 0.2681 0.1844 0.3087 0.0097  -0.0309 -0.0026 927  THR A O   
6703  C CB  . THR A 929  ? 0.2910 0.1981 0.3508 0.0136  -0.0407 -0.0081 927  THR A CB  
6704  O OG1 . THR A 929  ? 0.2845 0.1893 0.3500 0.0172  -0.0433 -0.0128 927  THR A OG1 
6705  C CG2 . THR A 929  ? 0.3020 0.2060 0.3688 0.0094  -0.0445 -0.0022 927  THR A CG2 
6706  N N   . ILE A 930  ? 0.2713 0.1860 0.3192 0.0052  -0.0338 0.0067  928  ILE A N   
6707  C CA  . ILE A 930  ? 0.2859 0.2036 0.3300 0.0015  -0.0321 0.0113  928  ILE A CA  
6708  C C   . ILE A 930  ? 0.3054 0.2208 0.3573 -0.0017 -0.0365 0.0156  928  ILE A C   
6709  O O   . ILE A 930  ? 0.3079 0.2214 0.3665 -0.0029 -0.0395 0.0191  928  ILE A O   
6710  C CB  . ILE A 930  ? 0.2342 0.1562 0.2730 -0.0003 -0.0287 0.0155  928  ILE A CB  
6711  C CG1 . ILE A 930  ? 0.2606 0.1847 0.2923 0.0027  -0.0246 0.0116  928  ILE A CG1 
6712  C CG2 . ILE A 930  ? 0.2737 0.1995 0.3093 -0.0039 -0.0272 0.0199  928  ILE A CG2 
6713  C CD1 . ILE A 930  ? 0.2757 0.2034 0.3035 0.0013  -0.0219 0.0152  928  ILE A CD1 
6714  N N   . ILE A 931  ? 0.2889 0.2047 0.3405 -0.0033 -0.0369 0.0158  929  ILE A N   
6715  C CA  . ILE A 931  ? 0.3039 0.2180 0.3631 -0.0065 -0.0410 0.0201  929  ILE A CA  
6716  C C   . ILE A 931  ? 0.3431 0.2625 0.3979 -0.0102 -0.0386 0.0251  929  ILE A C   
6717  O O   . ILE A 931  ? 0.2985 0.2204 0.3467 -0.0096 -0.0355 0.0226  929  ILE A O   
6718  C CB  . ILE A 931  ? 0.3212 0.2310 0.3853 -0.0049 -0.0443 0.0151  929  ILE A CB  
6719  C CG1 . ILE A 931  ? 0.3075 0.2128 0.3763 -0.0008 -0.0467 0.0093  929  ILE A CG1 
6720  C CG2 . ILE A 931  ? 0.2873 0.1954 0.3597 -0.0086 -0.0487 0.0200  929  ILE A CG2 
6721  C CD1 . ILE A 931  ? 0.3301 0.2311 0.4053 0.0009  -0.0509 0.0041  929  ILE A CD1 
6722  N N   . GLU A 932  ? 0.3399 0.2616 0.3983 -0.0140 -0.0401 0.0323  930  GLU A N   
6723  C CA  . GLU A 932  ? 0.2987 0.2267 0.3532 -0.0175 -0.0379 0.0372  930  GLU A CA  
6724  C C   . GLU A 932  ? 0.2827 0.2100 0.3428 -0.0201 -0.0411 0.0395  930  GLU A C   
6725  O O   . GLU A 932  ? 0.3166 0.2414 0.3858 -0.0221 -0.0457 0.0434  930  GLU A O   
6726  C CB  . GLU A 932  ? 0.3100 0.2424 0.3648 -0.0203 -0.0376 0.0437  930  GLU A CB  
6727  C CG  . GLU A 932  ? 0.2945 0.2285 0.3425 -0.0180 -0.0339 0.0413  930  GLU A CG  
6728  C CD  . GLU A 932  ? 0.3539 0.2915 0.4033 -0.0202 -0.0342 0.0471  930  GLU A CD  
6729  O OE1 . GLU A 932  ? 0.3271 0.2709 0.3760 -0.0237 -0.0338 0.0528  930  GLU A OE1 
6730  O OE2 . GLU A 932  ? 0.3371 0.2720 0.3882 -0.0183 -0.0349 0.0461  930  GLU A OE2 
6731  N N   . LEU A 933  ? 0.3203 0.2499 0.3756 -0.0200 -0.0389 0.0372  931  LEU A N   
6732  C CA  . LEU A 933  ? 0.3281 0.2574 0.3883 -0.0223 -0.0416 0.0389  931  LEU A CA  
6733  C C   . LEU A 933  ? 0.4082 0.3451 0.4666 -0.0265 -0.0401 0.0455  931  LEU A C   
6734  O O   . LEU A 933  ? 0.3671 0.3097 0.4185 -0.0268 -0.0362 0.0467  931  LEU A O   
6735  C CB  . LEU A 933  ? 0.3542 0.2813 0.4110 -0.0196 -0.0405 0.0322  931  LEU A CB  
6736  C CG  . LEU A 933  ? 0.3732 0.2940 0.4313 -0.0152 -0.0419 0.0249  931  LEU A CG  
6737  C CD1 . LEU A 933  ? 0.3886 0.3087 0.4436 -0.0132 -0.0412 0.0192  931  LEU A CD1 
6738  C CD2 . LEU A 933  ? 0.4205 0.3357 0.4895 -0.0156 -0.0476 0.0258  931  LEU A CD2 
6739  N N   . GLU A 934  ? 0.4267 0.3641 0.4919 -0.0296 -0.0435 0.0495  932  GLU A N   
6740  C CA  . GLU A 934  ? 0.4989 0.4443 0.5628 -0.0335 -0.0423 0.0554  932  GLU A CA  
6741  C C   . GLU A 934  ? 0.5006 0.4485 0.5585 -0.0326 -0.0393 0.0516  932  GLU A C   
6742  O O   . GLU A 934  ? 0.5042 0.4592 0.5554 -0.0333 -0.0354 0.0526  932  GLU A O   
6743  C CB  . GLU A 934  ? 0.5144 0.4599 0.5888 -0.0376 -0.0473 0.0624  932  GLU A CB  
6744  C CG  . GLU A 934  ? 0.5677 0.5103 0.6494 -0.0386 -0.0508 0.0667  932  GLU A CG  
6745  C CD  . GLU A 934  ? 0.6097 0.5589 0.6864 -0.0396 -0.0479 0.0708  932  GLU A CD  
6746  O OE1 . GLU A 934  ? 0.7043 0.6625 0.7763 -0.0421 -0.0450 0.0745  932  GLU A OE1 
6747  O OE2 . GLU A 934  ? 0.5876 0.5334 0.6652 -0.0379 -0.0484 0.0699  932  GLU A OE2 
6748  N N   . LYS A 935  ? 0.5058 0.4482 0.5661 -0.0309 -0.0413 0.0468  933  LYS A N   
6749  C CA  . LYS A 935  ? 0.5506 0.4948 0.6061 -0.0299 -0.0390 0.0431  933  LYS A CA  
6750  C C   . LYS A 935  ? 0.5434 0.4814 0.5964 -0.0254 -0.0387 0.0349  933  LYS A C   
6751  O O   . LYS A 935  ? 0.5350 0.4667 0.5929 -0.0236 -0.0418 0.0323  933  LYS A O   
6752  C CB  . LYS A 935  ? 0.5453 0.4908 0.6072 -0.0332 -0.0422 0.0466  933  LYS A CB  
6753  N N   . LEU A 936  ? 0.5519 0.4921 0.5973 -0.0234 -0.0351 0.0308  934  LEU A N   
6754  C CA  . LEU A 936  ? 0.5411 0.4768 0.5837 -0.0193 -0.0346 0.0234  934  LEU A CA  
6755  C C   . LEU A 936  ? 0.5471 0.4779 0.5968 -0.0191 -0.0392 0.0210  934  LEU A C   
6756  O O   . LEU A 936  ? 0.5385 0.4647 0.5886 -0.0157 -0.0403 0.0150  934  LEU A O   
6757  C CB  . LEU A 936  ? 0.5512 0.4908 0.5854 -0.0178 -0.0303 0.0205  934  LEU A CB  
6758  C CG  . LEU A 936  ? 0.5343 0.4724 0.5621 -0.0137 -0.0274 0.0150  934  LEU A CG  
6759  C CD1 . LEU A 936  ? 0.4960 0.4389 0.5160 -0.0132 -0.0229 0.0145  934  LEU A CD1 
6760  C CD2 . LEU A 936  ? 0.5076 0.4411 0.5367 -0.0106 -0.0293 0.0091  934  LEU A CD2 
6761  N N   . SER A 937  ? 0.5956 0.5277 0.6514 -0.0227 -0.0420 0.0254  935  SER A N   
6762  C CA  . SER A 937  ? 0.5870 0.5142 0.6509 -0.0229 -0.0469 0.0236  935  SER A CA  
6763  C C   . SER A 937  ? 0.5504 0.4713 0.6223 -0.0221 -0.0513 0.0229  935  SER A C   
6764  O O   . SER A 937  ? 0.5976 0.5136 0.6764 -0.0213 -0.0556 0.0195  935  SER A O   
6765  C CB  . SER A 937  ? 0.6102 0.5408 0.6793 -0.0274 -0.0490 0.0295  935  SER A CB  
6766  O OG  . SER A 937  ? 0.6319 0.5652 0.7053 -0.0311 -0.0501 0.0372  935  SER A OG  
6767  N N   . ASP A 938  ? 0.5571 0.4781 0.6286 -0.0222 -0.0505 0.0256  936  ASP A N   
6768  C CA  . ASP A 938  ? 0.5479 0.4628 0.6266 -0.0208 -0.0543 0.0242  936  ASP A CA  
6769  C C   . ASP A 938  ? 0.5468 0.4574 0.6237 -0.0157 -0.0545 0.0151  936  ASP A C   
6770  O O   . ASP A 938  ? 0.5164 0.4215 0.6007 -0.0141 -0.0586 0.0124  936  ASP A O   
6771  C CB  . ASP A 938  ? 0.5356 0.4522 0.6131 -0.0215 -0.0528 0.0286  936  ASP A CB  
6772  C CG  . ASP A 938  ? 0.5527 0.4741 0.6335 -0.0266 -0.0535 0.0379  936  ASP A CG  
6773  O OD1 . ASP A 938  ? 0.5807 0.5027 0.6674 -0.0297 -0.0564 0.0414  936  ASP A OD1 
6774  O OD2 . ASP A 938  ? 0.5155 0.4404 0.5931 -0.0275 -0.0512 0.0418  936  ASP A OD2 
6775  N N   . LEU A 939  ? 0.5024 0.4156 0.5700 -0.0131 -0.0502 0.0105  937  LEU A N   
6776  C CA  . LEU A 939  ? 0.5454 0.4561 0.6105 -0.0084 -0.0501 0.0021  937  LEU A CA  
6777  C C   . LEU A 939  ? 0.5396 0.4494 0.6065 -0.0078 -0.0522 -0.0019 937  LEU A C   
6778  O O   . LEU A 939  ? 0.6259 0.5391 0.6905 -0.0101 -0.0509 0.0007  937  LEU A O   
6779  C CB  . LEU A 939  ? 0.5235 0.4381 0.5776 -0.0058 -0.0443 -0.0002 937  LEU A CB  
6780  C CG  . LEU A 939  ? 0.4668 0.3819 0.5186 -0.0051 -0.0422 0.0017  937  LEU A CG  
6781  C CD1 . LEU A 939  ? 0.4422 0.3606 0.4841 -0.0023 -0.0371 -0.0014 937  LEU A CD1 
6782  C CD2 . LEU A 939  ? 0.4217 0.3317 0.4807 -0.0032 -0.0461 -0.0010 937  LEU A CD2 
6783  N N   . GLN A 940  ? 0.4744 0.3803 0.5454 -0.0045 -0.0554 -0.0086 938  GLN A N   
6784  C CA  . GLN A 940  ? 0.5145 0.4194 0.5882 -0.0037 -0.0581 -0.0133 938  GLN A CA  
6785  C C   . GLN A 940  ? 0.5224 0.4296 0.5884 0.0008  -0.0554 -0.0209 938  GLN A C   
6786  O O   . GLN A 940  ? 0.6091 0.5192 0.6708 0.0008  -0.0540 -0.0222 938  GLN A O   
6787  C CB  . GLN A 940  ? 0.5419 0.4408 0.6279 -0.0037 -0.0648 -0.0155 938  GLN A CB  
6788  N N   . ARG A 941  ? 0.4786 0.3851 0.5430 0.0047  -0.0548 -0.0258 939  ARG A N   
6789  C CA  . ARG A 941  ? 0.4548 0.3645 0.5121 0.0090  -0.0524 -0.0327 939  ARG A CA  
6790  C C   . ARG A 941  ? 0.3511 0.2628 0.4028 0.0114  -0.0487 -0.0332 939  ARG A C   
6791  O O   . ARG A 941  ? 0.4033 0.3129 0.4578 0.0103  -0.0489 -0.0295 939  ARG A O   
6792  C CB  . ARG A 941  ? 0.4765 0.3841 0.5397 0.0121  -0.0569 -0.0406 939  ARG A CB  
6793  N N   . GLU A 942  ? 0.3443 0.2604 0.3882 0.0147  -0.0453 -0.0374 940  GLU A N   
6794  C CA  . GLU A 942  ? 0.3333 0.2521 0.3714 0.0171  -0.0416 -0.0380 940  GLU A CA  
6795  C C   . GLU A 942  ? 0.3284 0.2440 0.3727 0.0193  -0.0444 -0.0410 940  GLU A C   
6796  O O   . GLU A 942  ? 0.3142 0.2280 0.3643 0.0217  -0.0484 -0.0470 940  GLU A O   
6797  C CB  . GLU A 942  ? 0.2875 0.2118 0.3178 0.0204  -0.0385 -0.0426 940  GLU A CB  
6798  C CG  . GLU A 942  ? 0.2799 0.2078 0.3046 0.0232  -0.0349 -0.0437 940  GLU A CG  
6799  C CD  . GLU A 942  ? 0.2807 0.2144 0.2995 0.0268  -0.0330 -0.0490 940  GLU A CD  
6800  O OE1 . GLU A 942  ? 0.3156 0.2498 0.3376 0.0294  -0.0361 -0.0553 940  GLU A OE1 
6801  O OE2 . GLU A 942  ? 0.2700 0.2082 0.2815 0.0271  -0.0287 -0.0468 940  GLU A OE2 
6802  N N   . VAL A 943  ? 0.3047 0.2200 0.3482 0.0187  -0.0425 -0.0372 941  VAL A N   
6803  C CA  . VAL A 943  ? 0.3045 0.2174 0.3530 0.0210  -0.0446 -0.0398 941  VAL A CA  
6804  C C   . VAL A 943  ? 0.3305 0.2484 0.3713 0.0241  -0.0401 -0.0419 941  VAL A C   
6805  O O   . VAL A 943  ? 0.2701 0.1899 0.3056 0.0226  -0.0363 -0.0370 941  VAL A O   
6806  C CB  . VAL A 943  ? 0.3404 0.2491 0.3951 0.0177  -0.0465 -0.0335 941  VAL A CB  
6807  C CG1 . VAL A 943  ? 0.3382 0.2445 0.3984 0.0203  -0.0487 -0.0364 941  VAL A CG1 
6808  C CG2 . VAL A 943  ? 0.3521 0.2566 0.4145 0.0143  -0.0509 -0.0307 941  VAL A CG2 
6809  N N   . PHE A 944  ? 0.3109 0.2316 0.3511 0.0285  -0.0406 -0.0493 942  PHE A N   
6810  C CA  . PHE A 944  ? 0.2719 0.1989 0.3042 0.0315  -0.0363 -0.0515 942  PHE A CA  
6811  C C   . PHE A 944  ? 0.3099 0.2365 0.3445 0.0333  -0.0362 -0.0520 942  PHE A C   
6812  O O   . PHE A 944  ? 0.3073 0.2357 0.3444 0.0373  -0.0377 -0.0583 942  PHE A O   
6813  C CB  . PHE A 944  ? 0.2646 0.1961 0.2949 0.0353  -0.0370 -0.0590 942  PHE A CB  
6814  C CG  . PHE A 944  ? 0.2565 0.1956 0.2776 0.0373  -0.0321 -0.0595 942  PHE A CG  
6815  C CD1 . PHE A 944  ? 0.2509 0.1922 0.2653 0.0349  -0.0286 -0.0547 942  PHE A CD1 
6816  C CD2 . PHE A 944  ? 0.2652 0.2098 0.2848 0.0416  -0.0312 -0.0648 942  PHE A CD2 
6817  C CE1 . PHE A 944  ? 0.2557 0.2039 0.2625 0.0365  -0.0244 -0.0547 942  PHE A CE1 
6818  C CE2 . PHE A 944  ? 0.2825 0.2347 0.2939 0.0432  -0.0269 -0.0646 942  PHE A CE2 
6819  C CZ  . PHE A 944  ? 0.2444 0.1982 0.2497 0.0406  -0.0236 -0.0593 942  PHE A CZ  
6820  N N   . GLY A 945  ? 0.2601 0.1848 0.2940 0.0304  -0.0344 -0.0454 943  GLY A N   
6821  C CA  . GLY A 945  ? 0.2736 0.1976 0.3101 0.0316  -0.0344 -0.0450 943  GLY A CA  
6822  C C   . GLY A 945  ? 0.2633 0.1871 0.2962 0.0283  -0.0313 -0.0376 943  GLY A C   
6823  O O   . GLY A 945  ? 0.2542 0.1790 0.2824 0.0255  -0.0288 -0.0333 943  GLY A O   
6824  N N   . PRO A 946  ? 0.2614 0.1843 0.2969 0.0288  -0.0313 -0.0362 944  PRO A N   
6825  C CA  . PRO A 946  ? 0.2671 0.1905 0.2989 0.0260  -0.0282 -0.0297 944  PRO A CA  
6826  C C   . PRO A 946  ? 0.2414 0.1604 0.2779 0.0217  -0.0305 -0.0236 944  PRO A C   
6827  O O   . PRO A 946  ? 0.2619 0.1788 0.3024 0.0207  -0.0317 -0.0205 944  PRO A O   
6828  C CB  . PRO A 946  ? 0.2378 0.1627 0.2709 0.0288  -0.0277 -0.0315 944  PRO A CB  
6829  C CG  . PRO A 946  ? 0.2665 0.1880 0.3082 0.0313  -0.0326 -0.0366 944  PRO A CG  
6830  C CD  . PRO A 946  ? 0.2584 0.1801 0.3002 0.0322  -0.0342 -0.0410 944  PRO A CD  
6831  N N   . VAL A 947  ? 0.2583 0.1764 0.2944 0.0192  -0.0311 -0.0217 945  VAL A N   
6832  C CA  . VAL A 947  ? 0.2720 0.1868 0.3130 0.0150  -0.0336 -0.0161 945  VAL A CA  
6833  C C   . VAL A 947  ? 0.2581 0.1758 0.2928 0.0119  -0.0304 -0.0116 945  VAL A C   
6834  O O   . VAL A 947  ? 0.2696 0.1884 0.3018 0.0118  -0.0299 -0.0133 945  VAL A O   
6835  C CB  . VAL A 947  ? 0.2722 0.1828 0.3214 0.0148  -0.0388 -0.0183 945  VAL A CB  
6836  C CG1 . VAL A 947  ? 0.2684 0.1763 0.3233 0.0103  -0.0414 -0.0114 945  VAL A CG1 
6837  C CG2 . VAL A 947  ? 0.2679 0.1760 0.3235 0.0187  -0.0421 -0.0241 945  VAL A CG2 
6838  N N   . LEU A 948  ? 0.2629 0.1821 0.2955 0.0094  -0.0284 -0.0063 946  LEU A N   
6839  C CA  . LEU A 948  ? 0.2619 0.1842 0.2892 0.0065  -0.0255 -0.0021 946  LEU A CA  
6840  C C   . LEU A 948  ? 0.2560 0.1771 0.2885 0.0025  -0.0282 0.0033  946  LEU A C   
6841  O O   . LEU A 948  ? 0.2971 0.2163 0.3350 0.0012  -0.0306 0.0065  946  LEU A O   
6842  C CB  . LEU A 948  ? 0.2626 0.1881 0.2845 0.0063  -0.0217 0.0002  946  LEU A CB  
6843  C CG  . LEU A 948  ? 0.2574 0.1864 0.2745 0.0034  -0.0190 0.0042  946  LEU A CG  
6844  C CD1 . LEU A 948  ? 0.2550 0.1857 0.2675 0.0042  -0.0171 0.0015  946  LEU A CD1 
6845  C CD2 . LEU A 948  ? 0.2690 0.2006 0.2822 0.0032  -0.0160 0.0063  946  LEU A CD2 
6846  N N   . HIS A 949  ? 0.2693 0.1918 0.3003 0.0005  -0.0279 0.0046  947  HIS A N   
6847  C CA  . HIS A 949  ? 0.2669 0.1898 0.3021 -0.0036 -0.0299 0.0103  947  HIS A CA  
6848  C C   . HIS A 949  ? 0.2675 0.1957 0.2967 -0.0059 -0.0262 0.0143  947  HIS A C   
6849  O O   . HIS A 949  ? 0.2820 0.2128 0.3043 -0.0046 -0.0226 0.0121  947  HIS A O   
6850  C CB  . HIS A 949  ? 0.2628 0.1841 0.3016 -0.0044 -0.0326 0.0091  947  HIS A CB  
6851  C CG  . HIS A 949  ? 0.2881 0.2046 0.3326 -0.0016 -0.0362 0.0039  947  HIS A CG  
6852  N ND1 . HIS A 949  ? 0.2838 0.2002 0.3247 0.0023  -0.0351 -0.0028 947  HIS A ND1 
6853  C CD2 . HIS A 949  ? 0.3164 0.2285 0.3703 -0.0021 -0.0412 0.0042  947  HIS A CD2 
6854  C CE1 . HIS A 949  ? 0.3024 0.2147 0.3499 0.0042  -0.0391 -0.0069 947  HIS A CE1 
6855  N NE2 . HIS A 949  ? 0.3068 0.2160 0.3626 0.0017  -0.0430 -0.0028 947  HIS A NE2 
6856  N N   . VAL A 950  ? 0.2721 0.2023 0.3041 -0.0093 -0.0272 0.0203  948  VAL A N   
6857  C CA  . VAL A 950  ? 0.2746 0.2106 0.3013 -0.0114 -0.0239 0.0239  948  VAL A CA  
6858  C C   . VAL A 950  ? 0.2614 0.2006 0.2910 -0.0153 -0.0253 0.0289  948  VAL A C   
6859  O O   . VAL A 950  ? 0.3060 0.2437 0.3427 -0.0174 -0.0290 0.0326  948  VAL A O   
6860  C CB  . VAL A 950  ? 0.2645 0.2019 0.2907 -0.0118 -0.0230 0.0265  948  VAL A CB  
6861  C CG1 . VAL A 950  ? 0.3018 0.2458 0.3231 -0.0141 -0.0201 0.0300  948  VAL A CG1 
6862  C CG2 . VAL A 950  ? 0.2813 0.2163 0.3044 -0.0080 -0.0213 0.0218  948  VAL A CG2 
6863  N N   . ILE A 951  ? 0.3024 0.2463 0.3270 -0.0161 -0.0225 0.0289  949  ILE A N   
6864  C CA  . ILE A 951  ? 0.3116 0.2602 0.3381 -0.0198 -0.0233 0.0339  949  ILE A CA  
6865  C C   . ILE A 951  ? 0.3276 0.2834 0.3480 -0.0209 -0.0195 0.0355  949  ILE A C   
6866  O O   . ILE A 951  ? 0.2705 0.2268 0.2852 -0.0185 -0.0164 0.0319  949  ILE A O   
6867  C CB  . ILE A 951  ? 0.3052 0.2529 0.3330 -0.0201 -0.0243 0.0321  949  ILE A CB  
6868  C CG1 . ILE A 951  ? 0.3185 0.2674 0.3392 -0.0176 -0.0208 0.0273  949  ILE A CG1 
6869  C CG2 . ILE A 951  ? 0.3655 0.3062 0.3999 -0.0189 -0.0285 0.0299  949  ILE A CG2 
6870  C CD1 . ILE A 951  ? 0.4215 0.3773 0.4390 -0.0197 -0.0185 0.0295  949  ILE A CD1 
6871  N N   . ARG A 952  ? 0.2616 0.2235 0.2839 -0.0244 -0.0201 0.0411  950  ARG A N   
6872  C CA  . ARG A 952  ? 0.2690 0.2389 0.2863 -0.0256 -0.0170 0.0428  950  ARG A CA  
6873  C C   . ARG A 952  ? 0.2717 0.2472 0.2880 -0.0273 -0.0161 0.0436  950  ARG A C   
6874  O O   . ARG A 952  ? 0.2996 0.2742 0.3206 -0.0290 -0.0186 0.0458  950  ARG A O   
6875  C CB  . ARG A 952  ? 0.3126 0.2869 0.3325 -0.0283 -0.0182 0.0487  950  ARG A CB  
6876  C CG  . ARG A 952  ? 0.3163 0.2848 0.3392 -0.0271 -0.0200 0.0488  950  ARG A CG  
6877  C CD  . ARG A 952  ? 0.3768 0.3488 0.4050 -0.0304 -0.0226 0.0558  950  ARG A CD  
6878  N NE  . ARG A 952  ? 0.4075 0.3877 0.4316 -0.0317 -0.0203 0.0584  950  ARG A NE  
6879  C CZ  . ARG A 952  ? 0.3607 0.3410 0.3840 -0.0311 -0.0200 0.0590  950  ARG A CZ  
6880  N NH1 . ARG A 952  ? 0.3206 0.2931 0.3467 -0.0291 -0.0217 0.0572  950  ARG A NH1 
6881  N NH2 . ARG A 952  ? 0.3056 0.2943 0.3253 -0.0325 -0.0181 0.0613  950  ARG A NH2 
6882  N N   . TYR A 953  ? 0.2636 0.2448 0.2741 -0.0267 -0.0126 0.0419  951  TYR A N   
6883  C CA  . TYR A 953  ? 0.2717 0.2589 0.2811 -0.0280 -0.0116 0.0423  951  TYR A CA  
6884  C C   . TYR A 953  ? 0.2590 0.2557 0.2643 -0.0288 -0.0088 0.0433  951  TYR A C   
6885  O O   . TYR A 953  ? 0.2563 0.2534 0.2580 -0.0272 -0.0069 0.0411  951  TYR A O   
6886  C CB  . TYR A 953  ? 0.2451 0.2282 0.2518 -0.0252 -0.0103 0.0368  951  TYR A CB  
6887  C CG  . TYR A 953  ? 0.2542 0.2371 0.2550 -0.0223 -0.0070 0.0320  951  TYR A CG  
6888  C CD1 . TYR A 953  ? 0.2238 0.2005 0.2231 -0.0197 -0.0066 0.0291  951  TYR A CD1 
6889  C CD2 . TYR A 953  ? 0.2543 0.2435 0.2515 -0.0220 -0.0044 0.0305  951  TYR A CD2 
6890  C CE1 . TYR A 953  ? 0.2325 0.2091 0.2271 -0.0172 -0.0038 0.0253  951  TYR A CE1 
6891  C CE2 . TYR A 953  ? 0.2275 0.2161 0.2202 -0.0194 -0.0017 0.0263  951  TYR A CE2 
6892  C CZ  . TYR A 953  ? 0.2505 0.2329 0.2421 -0.0172 -0.0015 0.0239  951  TYR A CZ  
6893  O OH  . TYR A 953  ? 0.2409 0.2228 0.2287 -0.0148 0.0009  0.0203  951  TYR A OH  
6894  N N   . ARG A 954  ? 0.2599 0.2647 0.2663 -0.0314 -0.0088 0.0464  952  ARG A N   
6895  C CA  . ARG A 954  ? 0.3035 0.3185 0.3060 -0.0319 -0.0061 0.0463  952  ARG A CA  
6896  C C   . ARG A 954  ? 0.2704 0.2853 0.2687 -0.0291 -0.0034 0.0404  952  ARG A C   
6897  O O   . ARG A 954  ? 0.2932 0.3038 0.2924 -0.0283 -0.0039 0.0385  952  ARG A O   
6898  C CB  . ARG A 954  ? 0.3201 0.3450 0.3257 -0.0357 -0.0071 0.0522  952  ARG A CB  
6899  C CG  . ARG A 954  ? 0.3817 0.4091 0.3914 -0.0387 -0.0096 0.0590  952  ARG A CG  
6900  C CD  . ARG A 954  ? 0.4216 0.4557 0.4277 -0.0386 -0.0077 0.0592  952  ARG A CD  
6901  N NE  . ARG A 954  ? 0.5349 0.5684 0.5443 -0.0405 -0.0100 0.0644  952  ARG A NE  
6902  C CZ  . ARG A 954  ? 0.5615 0.6041 0.5737 -0.0441 -0.0114 0.0715  952  ARG A CZ  
6903  N NH1 . ARG A 954  ? 0.6312 0.6847 0.6434 -0.0463 -0.0106 0.0742  952  ARG A NH1 
6904  N NH2 . ARG A 954  ? 0.5310 0.5723 0.5466 -0.0456 -0.0136 0.0761  952  ARG A NH2 
6905  N N   . ARG A 955  ? 0.2856 0.3053 0.2797 -0.0277 -0.0008 0.0374  953  ARG A N   
6906  C CA  . ARG A 955  ? 0.2799 0.2982 0.2707 -0.0248 0.0014  0.0316  953  ARG A CA  
6907  C C   . ARG A 955  ? 0.2696 0.2918 0.2612 -0.0254 0.0016  0.0313  953  ARG A C   
6908  O O   . ARG A 955  ? 0.3100 0.3271 0.3008 -0.0233 0.0021  0.0277  953  ARG A O   
6909  C CB  . ARG A 955  ? 0.3375 0.3615 0.3247 -0.0235 0.0038  0.0287  953  ARG A CB  
6910  C CG  . ARG A 955  ? 0.4025 0.4251 0.3872 -0.0205 0.0058  0.0228  953  ARG A CG  
6911  C CD  . ARG A 955  ? 0.4221 0.4337 0.4068 -0.0183 0.0054  0.0203  953  ARG A CD  
6912  N NE  . ARG A 955  ? 0.4599 0.4697 0.4426 -0.0155 0.0070  0.0154  953  ARG A NE  
6913  C CZ  . ARG A 955  ? 0.4489 0.4603 0.4319 -0.0149 0.0074  0.0138  953  ARG A CZ  
6914  N NH1 . ARG A 955  ? 0.3871 0.4026 0.3719 -0.0170 0.0065  0.0165  953  ARG A NH1 
6915  N NH2 . ARG A 955  ? 0.4001 0.4091 0.3819 -0.0123 0.0086  0.0097  953  ARG A NH2 
6916  N N   . ASP A 956  ? 0.2711 0.3027 0.2645 -0.0282 0.0012  0.0354  954  ASP A N   
6917  C CA  . ASP A 956  ? 0.2941 0.3298 0.2885 -0.0289 0.0014  0.0353  954  ASP A CA  
6918  C C   . ASP A 956  ? 0.3035 0.3309 0.3011 -0.0291 -0.0008 0.0361  954  ASP A C   
6919  O O   . ASP A 956  ? 0.3118 0.3402 0.3099 -0.0288 -0.0006 0.0346  954  ASP A O   
6920  C CB  . ASP A 956  ? 0.3110 0.3591 0.3071 -0.0322 0.0012  0.0402  954  ASP A CB  
6921  C CG  . ASP A 956  ? 0.3253 0.3839 0.3181 -0.0316 0.0036  0.0384  954  ASP A CG  
6922  O OD1 . ASP A 956  ? 0.3513 0.4074 0.3408 -0.0285 0.0054  0.0328  954  ASP A OD1 
6923  O OD2 . ASP A 956  ? 0.4025 0.4721 0.3964 -0.0343 0.0034  0.0428  954  ASP A OD2 
6924  N N   . ASP A 957  ? 0.2751 0.2948 0.2752 -0.0296 -0.0031 0.0381  955  ASP A N   
6925  C CA  . ASP A 957  ? 0.2690 0.2808 0.2725 -0.0297 -0.0056 0.0383  955  ASP A CA  
6926  C C   . ASP A 957  ? 0.2878 0.2901 0.2890 -0.0261 -0.0051 0.0328  955  ASP A C   
6927  O O   . ASP A 957  ? 0.2829 0.2779 0.2866 -0.0257 -0.0073 0.0323  955  ASP A O   
6928  C CB  . ASP A 957  ? 0.3161 0.3252 0.3248 -0.0323 -0.0088 0.0435  955  ASP A CB  
6929  C CG  . ASP A 957  ? 0.3559 0.3746 0.3682 -0.0363 -0.0099 0.0499  955  ASP A CG  
6930  O OD1 . ASP A 957  ? 0.3281 0.3533 0.3402 -0.0373 -0.0091 0.0503  955  ASP A OD1 
6931  O OD2 . ASP A 957  ? 0.3859 0.4060 0.4011 -0.0385 -0.0116 0.0548  955  ASP A OD2 
6932  N N   . LEU A 958  ? 0.2591 0.2616 0.2556 -0.0235 -0.0024 0.0286  956  LEU A N   
6933  C CA  . LEU A 958  ? 0.2466 0.2410 0.2409 -0.0202 -0.0018 0.0240  956  LEU A CA  
6934  C C   . LEU A 958  ? 0.2749 0.2662 0.2700 -0.0193 -0.0026 0.0220  956  LEU A C   
6935  O O   . LEU A 958  ? 0.2658 0.2500 0.2616 -0.0178 -0.0039 0.0202  956  LEU A O   
6936  C CB  . LEU A 958  ? 0.2573 0.2536 0.2474 -0.0179 0.0011  0.0205  956  LEU A CB  
6937  C CG  . LEU A 958  ? 0.2514 0.2408 0.2392 -0.0146 0.0019  0.0162  956  LEU A CG  
6938  C CD1 . LEU A 958  ? 0.2659 0.2481 0.2543 -0.0138 0.0006  0.0163  956  LEU A CD1 
6939  C CD2 . LEU A 958  ? 0.2616 0.2533 0.2463 -0.0127 0.0044  0.0132  956  LEU A CD2 
6940  N N   . ASP A 959  ? 0.2521 0.2493 0.2474 -0.0201 -0.0019 0.0222  957  ASP A N   
6941  C CA  . ASP A 959  ? 0.2399 0.2345 0.2360 -0.0192 -0.0026 0.0203  957  ASP A CA  
6942  C C   . ASP A 959  ? 0.2472 0.2377 0.2477 -0.0209 -0.0059 0.0226  957  ASP A C   
6943  O O   . ASP A 959  ? 0.2652 0.2498 0.2661 -0.0194 -0.0071 0.0200  957  ASP A O   
6944  C CB  . ASP A 959  ? 0.2789 0.2812 0.2747 -0.0199 -0.0014 0.0202  957  ASP A CB  
6945  C CG  . ASP A 959  ? 0.3159 0.3155 0.3116 -0.0183 -0.0016 0.0174  957  ASP A CG  
6946  O OD1 . ASP A 959  ? 0.2840 0.2787 0.2770 -0.0154 -0.0006 0.0138  957  ASP A OD1 
6947  O OD2 . ASP A 959  ? 0.3624 0.3649 0.3607 -0.0200 -0.0028 0.0190  957  ASP A OD2 
6948  N N   . ARG A 960  ? 0.2663 0.2599 0.2705 -0.0241 -0.0076 0.0274  958  ARG A N   
6949  C CA  . ARG A 960  ? 0.2830 0.2723 0.2927 -0.0259 -0.0112 0.0298  958  ARG A CA  
6950  C C   . ARG A 960  ? 0.2827 0.2633 0.2929 -0.0239 -0.0127 0.0276  958  ARG A C   
6951  O O   . ARG A 960  ? 0.3077 0.2825 0.3209 -0.0234 -0.0153 0.0262  958  ARG A O   
6952  C CB  . ARG A 960  ? 0.2956 0.2907 0.3097 -0.0299 -0.0129 0.0361  958  ARG A CB  
6953  N N   . LEU A 961  ? 0.2425 0.2224 0.2497 -0.0227 -0.0110 0.0270  959  LEU A N   
6954  C CA  . LEU A 961  ? 0.2658 0.2382 0.2730 -0.0206 -0.0120 0.0247  959  LEU A CA  
6955  C C   . LEU A 961  ? 0.2622 0.2299 0.2669 -0.0173 -0.0114 0.0194  959  LEU A C   
6956  O O   . LEU A 961  ? 0.2685 0.2304 0.2754 -0.0161 -0.0137 0.0174  959  LEU A O   
6957  C CB  . LEU A 961  ? 0.2417 0.2152 0.2459 -0.0198 -0.0100 0.0249  959  LEU A CB  
6958  C CG  . LEU A 961  ? 0.2500 0.2166 0.2533 -0.0172 -0.0102 0.0220  959  LEU A CG  
6959  C CD1 . LEU A 961  ? 0.2861 0.2481 0.2953 -0.0182 -0.0140 0.0238  959  LEU A CD1 
6960  C CD2 . LEU A 961  ? 0.2848 0.2533 0.2848 -0.0166 -0.0080 0.0223  959  LEU A CD2 
6961  N N   . VAL A 962  ? 0.2343 0.2048 0.2345 -0.0157 -0.0086 0.0170  960  VAL A N   
6962  C CA  . VAL A 962  ? 0.2423 0.2093 0.2401 -0.0128 -0.0081 0.0126  960  VAL A CA  
6963  C C   . VAL A 962  ? 0.2968 0.2619 0.2980 -0.0134 -0.0109 0.0121  960  VAL A C   
6964  O O   . VAL A 962  ? 0.2605 0.2210 0.2619 -0.0114 -0.0122 0.0090  960  VAL A O   
6965  C CB  . VAL A 962  ? 0.2825 0.2533 0.2760 -0.0115 -0.0050 0.0109  960  VAL A CB  
6966  C CG1 . VAL A 962  ? 0.2929 0.2609 0.2843 -0.0087 -0.0047 0.0071  960  VAL A CG1 
6967  C CG2 . VAL A 962  ? 0.2663 0.2383 0.2569 -0.0107 -0.0027 0.0109  960  VAL A CG2 
6968  N N   . ASP A 963  ? 0.2765 0.2458 0.2808 -0.0163 -0.0119 0.0152  961  ASP A N   
6969  C CA  . ASP A 963  ? 0.2964 0.2639 0.3051 -0.0173 -0.0149 0.0153  961  ASP A CA  
6970  C C   . ASP A 963  ? 0.3025 0.2639 0.3156 -0.0173 -0.0183 0.0150  961  ASP A C   
6971  O O   . ASP A 963  ? 0.3245 0.2817 0.3391 -0.0158 -0.0204 0.0117  961  ASP A O   
6972  C CB  . ASP A 963  ? 0.3103 0.2837 0.3225 -0.0210 -0.0157 0.0197  961  ASP A CB  
6973  C CG  . ASP A 963  ? 0.3796 0.3590 0.3887 -0.0207 -0.0132 0.0191  961  ASP A CG  
6974  O OD1 . ASP A 963  ? 0.4180 0.3960 0.4232 -0.0179 -0.0115 0.0151  961  ASP A OD1 
6975  O OD2 . ASP A 963  ? 0.4572 0.4432 0.4680 -0.0235 -0.0129 0.0228  961  ASP A OD2 
6976  N N   . ASP A 964  ? 0.3000 0.2611 0.3154 -0.0189 -0.0191 0.0183  962  ASP A N   
6977  C CA  . ASP A 964  ? 0.3129 0.2683 0.3334 -0.0189 -0.0225 0.0182  962  ASP A CA  
6978  C C   . ASP A 964  ? 0.3474 0.2975 0.3652 -0.0150 -0.0222 0.0127  962  ASP A C   
6979  O O   . ASP A 964  ? 0.3570 0.3024 0.3786 -0.0139 -0.0253 0.0101  962  ASP A O   
6980  C CB  . ASP A 964  ? 0.3361 0.2926 0.3588 -0.0210 -0.0229 0.0229  962  ASP A CB  
6981  C CG  . ASP A 964  ? 0.3127 0.2746 0.3398 -0.0253 -0.0241 0.0290  962  ASP A CG  
6982  O OD1 . ASP A 964  ? 0.3805 0.3443 0.4097 -0.0267 -0.0252 0.0296  962  ASP A OD1 
6983  O OD2 . ASP A 964  ? 0.4250 0.3896 0.4531 -0.0272 -0.0240 0.0333  962  ASP A OD2 
6984  N N   . VAL A 965  ? 0.2949 0.2462 0.3064 -0.0128 -0.0187 0.0108  963  VAL A N   
6985  C CA  . VAL A 965  ? 0.3239 0.2717 0.3326 -0.0091 -0.0180 0.0060  963  VAL A CA  
6986  C C   . VAL A 965  ? 0.3225 0.2694 0.3305 -0.0073 -0.0189 0.0022  963  VAL A C   
6987  O O   . VAL A 965  ? 0.3126 0.2560 0.3220 -0.0052 -0.0208 -0.0016 963  VAL A O   
6988  C CB  . VAL A 965  ? 0.2778 0.2277 0.2804 -0.0074 -0.0141 0.0055  963  VAL A CB  
6989  C CG1 . VAL A 965  ? 0.2725 0.2198 0.2720 -0.0038 -0.0133 0.0009  963  VAL A CG1 
6990  C CG2 . VAL A 965  ? 0.2984 0.2487 0.3017 -0.0088 -0.0136 0.0087  963  VAL A CG2 
6991  N N   . ASN A 966  ? 0.3071 0.2577 0.3131 -0.0081 -0.0175 0.0027  964  ASN A N   
6992  C CA  . ASN A 966  ? 0.2921 0.2425 0.2975 -0.0067 -0.0183 -0.0006 964  ASN A CA  
6993  C C   . ASN A 966  ? 0.3151 0.2627 0.3269 -0.0079 -0.0226 -0.0011 964  ASN A C   
6994  O O   . ASN A 966  ? 0.2776 0.2235 0.2898 -0.0059 -0.0243 -0.0052 964  ASN A O   
6995  C CB  . ASN A 966  ? 0.3178 0.2729 0.3206 -0.0075 -0.0162 0.0005  964  ASN A CB  
6996  C CG  . ASN A 966  ? 0.2965 0.2540 0.2934 -0.0057 -0.0124 0.0000  964  ASN A CG  
6997  O OD1 . ASN A 966  ? 0.2707 0.2264 0.2647 -0.0033 -0.0112 -0.0021 964  ASN A OD1 
6998  N ND2 . ASN A 966  ? 0.2926 0.2545 0.2883 -0.0070 -0.0105 0.0019  964  ASN A ND2 
6999  N N   . ALA A 967  ? 0.3139 0.2613 0.3311 -0.0111 -0.0247 0.0030  965  ALA A N   
7000  C CA  . ALA A 967  ? 0.3261 0.2713 0.3504 -0.0129 -0.0291 0.0035  965  ALA A CA  
7001  C C   . ALA A 967  ? 0.3340 0.2735 0.3622 -0.0108 -0.0324 -0.0005 965  ALA A C   
7002  O O   . ALA A 967  ? 0.3452 0.2823 0.3791 -0.0115 -0.0363 -0.0019 965  ALA A O   
7003  C CB  . ALA A 967  ? 0.3710 0.3180 0.4006 -0.0171 -0.0305 0.0098  965  ALA A CB  
7004  N N   . THR A 968  ? 0.3158 0.2533 0.3413 -0.0083 -0.0312 -0.0027 966  THR A N   
7005  C CA  . THR A 968  ? 0.3023 0.2352 0.3313 -0.0059 -0.0342 -0.0073 966  THR A CA  
7006  C C   . THR A 968  ? 0.2888 0.2218 0.3159 -0.0031 -0.0349 -0.0131 966  THR A C   
7007  O O   . THR A 968  ? 0.3184 0.2481 0.3499 -0.0014 -0.0384 -0.0174 966  THR A O   
7008  C CB  . THR A 968  ? 0.2962 0.2279 0.3219 -0.0034 -0.0323 -0.0086 966  THR A CB  
7009  O OG1 . THR A 968  ? 0.2767 0.2115 0.2946 -0.0007 -0.0283 -0.0112 966  THR A OG1 
7010  C CG2 . THR A 968  ? 0.2916 0.2241 0.3182 -0.0060 -0.0311 -0.0029 966  THR A CG2 
7011  N N   . GLY A 969  ? 0.2691 0.2061 0.2901 -0.0024 -0.0319 -0.0135 967  GLY A N   
7012  C CA  . GLY A 969  ? 0.2876 0.2258 0.3059 0.0004  -0.0320 -0.0187 967  GLY A CA  
7013  C C   . GLY A 969  ? 0.2668 0.2061 0.2793 0.0042  -0.0296 -0.0225 967  GLY A C   
7014  O O   . GLY A 969  ? 0.2644 0.2061 0.2734 0.0066  -0.0291 -0.0261 967  GLY A O   
7015  N N   . TYR A 970  ? 0.2621 0.2002 0.2737 0.0049  -0.0282 -0.0215 968  TYR A N   
7016  C CA  . TYR A 970  ? 0.2430 0.1830 0.2489 0.0083  -0.0255 -0.0242 968  TYR A CA  
7017  C C   . TYR A 970  ? 0.2315 0.1752 0.2311 0.0079  -0.0211 -0.0212 968  TYR A C   
7018  O O   . TYR A 970  ? 0.2746 0.2193 0.2742 0.0052  -0.0202 -0.0174 968  TYR A O   
7019  C CB  . TYR A 970  ? 0.2510 0.1884 0.2589 0.0091  -0.0259 -0.0244 968  TYR A CB  
7020  C CG  . TYR A 970  ? 0.2293 0.1631 0.2436 0.0103  -0.0303 -0.0284 968  TYR A CG  
7021  C CD1 . TYR A 970  ? 0.2798 0.2147 0.2932 0.0142  -0.0311 -0.0345 968  TYR A CD1 
7022  C CD2 . TYR A 970  ? 0.3077 0.2374 0.3295 0.0077  -0.0338 -0.0260 968  TYR A CD2 
7023  C CE1 . TYR A 970  ? 0.3024 0.2342 0.3223 0.0156  -0.0354 -0.0389 968  TYR A CE1 
7024  C CE2 . TYR A 970  ? 0.2853 0.2112 0.3140 0.0088  -0.0382 -0.0297 968  TYR A CE2 
7025  C CZ  . TYR A 970  ? 0.3317 0.2585 0.3595 0.0129  -0.0390 -0.0365 968  TYR A CZ  
7026  O OH  . TYR A 970  ? 0.4091 0.3322 0.4444 0.0143  -0.0437 -0.0409 968  TYR A OH  
7027  N N   . GLY A 971  ? 0.2103 0.1564 0.2049 0.0106  -0.0186 -0.0229 969  GLY A N   
7028  C CA  . GLY A 971  ? 0.2329 0.1821 0.2223 0.0105  -0.0148 -0.0202 969  GLY A CA  
7029  C C   . GLY A 971  ? 0.2237 0.1753 0.2086 0.0134  -0.0124 -0.0218 969  GLY A C   
7030  O O   . GLY A 971  ? 0.2309 0.1860 0.2119 0.0147  -0.0107 -0.0222 969  GLY A O   
7031  N N   . LEU A 972  ? 0.2127 0.1629 0.1983 0.0144  -0.0124 -0.0224 970  LEU A N   
7032  C CA  . LEU A 972  ? 0.2085 0.1615 0.1904 0.0172  -0.0104 -0.0240 970  LEU A CA  
7033  C C   . LEU A 972  ? 0.2366 0.1903 0.2159 0.0164  -0.0071 -0.0202 970  LEU A C   
7034  O O   . LEU A 972  ? 0.2264 0.1826 0.2025 0.0162  -0.0050 -0.0183 970  LEU A O   
7035  C CB  . LEU A 972  ? 0.2130 0.1649 0.1974 0.0194  -0.0123 -0.0277 970  LEU A CB  
7036  C CG  . LEU A 972  ? 0.2371 0.1933 0.2178 0.0227  -0.0106 -0.0301 970  LEU A CG  
7037  C CD1 . LEU A 972  ? 0.2248 0.1861 0.2015 0.0241  -0.0096 -0.0311 970  LEU A CD1 
7038  C CD2 . LEU A 972  ? 0.2478 0.2035 0.2317 0.0251  -0.0132 -0.0351 970  LEU A CD2 
7039  N N   . THR A 973  ? 0.2159 0.1673 0.1968 0.0159  -0.0070 -0.0190 971  THR A N   
7040  C CA  . THR A 973  ? 0.2068 0.1587 0.1856 0.0149  -0.0042 -0.0155 971  THR A CA  
7041  C C   . THR A 973  ? 0.2218 0.1714 0.2030 0.0118  -0.0045 -0.0123 971  THR A C   
7042  O O   . THR A 973  ? 0.2168 0.1639 0.2018 0.0104  -0.0070 -0.0123 971  THR A O   
7043  C CB  . THR A 973  ? 0.2119 0.1642 0.1902 0.0166  -0.0033 -0.0162 971  THR A CB  
7044  O OG1 . THR A 973  ? 0.2202 0.1693 0.2026 0.0165  -0.0057 -0.0174 971  THR A OG1 
7045  C CG2 . THR A 973  ? 0.2398 0.1960 0.2153 0.0198  -0.0026 -0.0190 971  THR A CG2 
7046  N N   . PHE A 974  ? 0.2265 0.1774 0.2057 0.0107  -0.0021 -0.0095 972  PHE A N   
7047  C CA  . PHE A 974  ? 0.2289 0.1791 0.2096 0.0079  -0.0020 -0.0065 972  PHE A CA  
7048  C C   . PHE A 974  ? 0.2090 0.1604 0.1876 0.0077  0.0005  -0.0046 972  PHE A C   
7049  O O   . PHE A 974  ? 0.2308 0.1840 0.2068 0.0090  0.0024  -0.0048 972  PHE A O   
7050  C CB  . PHE A 974  ? 0.2179 0.1695 0.1987 0.0063  -0.0022 -0.0056 972  PHE A CB  
7051  C CG  . PHE A 974  ? 0.2196 0.1722 0.2015 0.0036  -0.0017 -0.0026 972  PHE A CG  
7052  C CD1 . PHE A 974  ? 0.2053 0.1569 0.1907 0.0014  -0.0037 -0.0009 972  PHE A CD1 
7053  C CD2 . PHE A 974  ? 0.2216 0.1767 0.2013 0.0033  0.0007  -0.0015 972  PHE A CD2 
7054  C CE1 . PHE A 974  ? 0.2033 0.1571 0.1895 -0.0011 -0.0031 0.0021  972  PHE A CE1 
7055  C CE2 . PHE A 974  ? 0.2049 0.1620 0.1855 0.0011  0.0012  0.0008  972  PHE A CE2 
7056  C CZ  . PHE A 974  ? 0.2239 0.1808 0.2073 -0.0011 -0.0005 0.0027  972  PHE A CZ  
7057  N N   . GLY A 975  ? 0.2047 0.1553 0.1849 0.0060  0.0004  -0.0026 973  GLY A N   
7058  C CA  . GLY A 975  ? 0.2093 0.1611 0.1880 0.0057  0.0025  -0.0010 973  GLY A CA  
7059  C C   . GLY A 975  ? 0.1944 0.1479 0.1738 0.0032  0.0029  0.0013  973  GLY A C   
7060  O O   . GLY A 975  ? 0.2161 0.1696 0.1978 0.0012  0.0013  0.0026  973  GLY A O   
7061  N N   . LEU A 976  ? 0.2091 0.1645 0.1868 0.0031  0.0049  0.0018  974  LEU A N   
7062  C CA  . LEU A 976  ? 0.1939 0.1521 0.1721 0.0011  0.0054  0.0034  974  LEU A CA  
7063  C C   . LEU A 976  ? 0.2020 0.1609 0.1793 0.0014  0.0070  0.0038  974  LEU A C   
7064  O O   . LEU A 976  ? 0.2192 0.1778 0.1953 0.0029  0.0082  0.0028  974  LEU A O   
7065  C CB  . LEU A 976  ? 0.2183 0.1790 0.1958 0.0008  0.0061  0.0029  974  LEU A CB  
7066  C CG  . LEU A 976  ? 0.2178 0.1826 0.1955 -0.0008 0.0070  0.0037  974  LEU A CG  
7067  C CD1 . LEU A 976  ? 0.2422 0.2090 0.2216 -0.0033 0.0057  0.0059  974  LEU A CD1 
7068  C CD2 . LEU A 976  ? 0.2211 0.1880 0.1983 -0.0002 0.0078  0.0024  974  LEU A CD2 
7069  N N   . HIS A 977  ? 0.2152 0.1752 0.1935 -0.0003 0.0066  0.0054  975  HIS A N   
7070  C CA  . HIS A 977  ? 0.2170 0.1783 0.1947 -0.0004 0.0078  0.0057  975  HIS A CA  
7071  C C   . HIS A 977  ? 0.1993 0.1652 0.1771 -0.0021 0.0083  0.0062  975  HIS A C   
7072  O O   . HIS A 977  ? 0.2025 0.1708 0.1812 -0.0040 0.0074  0.0081  975  HIS A O   
7073  C CB  . HIS A 977  ? 0.2259 0.1857 0.2046 -0.0007 0.0071  0.0070  975  HIS A CB  
7074  C CG  . HIS A 977  ? 0.2232 0.1802 0.2014 0.0015  0.0076  0.0059  975  HIS A CG  
7075  N ND1 . HIS A 977  ? 0.2644 0.2218 0.2422 0.0020  0.0087  0.0060  975  HIS A ND1 
7076  C CD2 . HIS A 977  ? 0.2602 0.2147 0.2383 0.0032  0.0070  0.0047  975  HIS A CD2 
7077  C CE1 . HIS A 977  ? 0.2544 0.2097 0.2319 0.0039  0.0090  0.0052  975  HIS A CE1 
7078  N NE2 . HIS A 977  ? 0.2576 0.2114 0.2352 0.0047  0.0080  0.0043  975  HIS A NE2 
7079  N N   . THR A 978  ? 0.1883 0.1558 0.1653 -0.0012 0.0096  0.0046  976  THR A N   
7080  C CA  . THR A 978  ? 0.2194 0.1919 0.1966 -0.0023 0.0102  0.0041  976  THR A CA  
7081  C C   . THR A 978  ? 0.2125 0.1852 0.1897 -0.0009 0.0114  0.0019  976  THR A C   
7082  O O   . THR A 978  ? 0.2300 0.1994 0.2072 0.0008  0.0117  0.0012  976  THR A O   
7083  C CB  . THR A 978  ? 0.2089 0.1842 0.1864 -0.0031 0.0099  0.0040  976  THR A CB  
7084  O OG1 . THR A 978  ? 0.2140 0.1952 0.1916 -0.0039 0.0105  0.0032  976  THR A OG1 
7085  C CG2 . THR A 978  ? 0.2121 0.1851 0.1893 -0.0014 0.0102  0.0023  976  THR A CG2 
7086  N N   . ARG A 979  ? 0.2233 0.2002 0.2009 -0.0015 0.0118  0.0009  977  ARG A N   
7087  C CA  . ARG A 979  ? 0.2371 0.2145 0.2158 -0.0002 0.0125  -0.0016 977  ARG A CA  
7088  C C   . ARG A 979  ? 0.2622 0.2432 0.2417 0.0001  0.0127  -0.0037 977  ARG A C   
7089  O O   . ARG A 979  ? 0.2682 0.2495 0.2493 0.0014  0.0130  -0.0061 977  ARG A O   
7090  C CB  . ARG A 979  ? 0.2529 0.2326 0.2320 -0.0006 0.0126  -0.0023 977  ARG A CB  
7091  C CG  . ARG A 979  ? 0.3309 0.3064 0.3098 -0.0004 0.0126  -0.0007 977  ARG A CG  
7092  C CD  . ARG A 979  ? 0.4212 0.3986 0.4010 -0.0006 0.0126  -0.0016 977  ARG A CD  
7093  N NE  . ARG A 979  ? 0.4665 0.4466 0.4453 -0.0023 0.0122  0.0003  977  ARG A NE  
7094  C CZ  . ARG A 979  ? 0.4339 0.4169 0.4130 -0.0029 0.0121  -0.0002 977  ARG A CZ  
7095  N NH1 . ARG A 979  ? 0.4138 0.3972 0.3944 -0.0020 0.0123  -0.0028 977  ARG A NH1 
7096  N NH2 . ARG A 979  ? 0.5133 0.4988 0.4916 -0.0045 0.0116  0.0021  977  ARG A NH2 
7097  N N   . LEU A 980  ? 0.2201 0.2036 0.1990 -0.0009 0.0124  -0.0028 978  LEU A N   
7098  C CA  . LEU A 980  ? 0.1997 0.1885 0.1793 -0.0009 0.0126  -0.0046 978  LEU A CA  
7099  C C   . LEU A 980  ? 0.2280 0.2145 0.2080 0.0001  0.0125  -0.0051 978  LEU A C   
7100  O O   . LEU A 980  ? 0.2242 0.2086 0.2034 -0.0005 0.0120  -0.0031 978  LEU A O   
7101  C CB  . LEU A 980  ? 0.2150 0.2098 0.1939 -0.0031 0.0124  -0.0029 978  LEU A CB  
7102  C CG  . LEU A 980  ? 0.2390 0.2370 0.2173 -0.0045 0.0123  -0.0018 978  LEU A CG  
7103  C CD1 . LEU A 980  ? 0.2510 0.2551 0.2289 -0.0069 0.0119  0.0009  978  LEU A CD1 
7104  C CD2 . LEU A 980  ? 0.2340 0.2354 0.2130 -0.0035 0.0129  -0.0053 978  LEU A CD2 
7105  N N   . ASP A 981  ? 0.2108 0.1980 0.1926 0.0017  0.0128  -0.0077 979  ASP A N   
7106  C CA  . ASP A 981  ? 0.2148 0.1999 0.1973 0.0028  0.0126  -0.0080 979  ASP A CA  
7107  C C   . ASP A 981  ? 0.2064 0.1949 0.1882 0.0017  0.0124  -0.0072 979  ASP A C   
7108  O O   . ASP A 981  ? 0.2390 0.2249 0.2205 0.0020  0.0119  -0.0062 979  ASP A O   
7109  C CB  . ASP A 981  ? 0.2221 0.2080 0.2074 0.0046  0.0127  -0.0110 979  ASP A CB  
7110  C CG  . ASP A 981  ? 0.2373 0.2186 0.2241 0.0058  0.0126  -0.0112 979  ASP A CG  
7111  O OD1 . ASP A 981  ? 0.2440 0.2213 0.2292 0.0056  0.0126  -0.0089 979  ASP A OD1 
7112  O OD2 . ASP A 981  ? 0.2572 0.2391 0.2472 0.0071  0.0123  -0.0137 979  ASP A OD2 
7113  N N   . GLU A 982  ? 0.2063 0.2014 0.1882 0.0004  0.0126  -0.0076 980  GLU A N   
7114  C CA  . GLU A 982  ? 0.2225 0.2215 0.2043 -0.0010 0.0123  -0.0064 980  GLU A CA  
7115  C C   . GLU A 982  ? 0.2112 0.2064 0.1918 -0.0024 0.0114  -0.0030 980  GLU A C   
7116  O O   . GLU A 982  ? 0.2143 0.2088 0.1952 -0.0028 0.0108  -0.0021 980  GLU A O   
7117  C CB  . GLU A 982  ? 0.2465 0.2542 0.2284 -0.0024 0.0127  -0.0068 980  GLU A CB  
7118  C CG  . GLU A 982  ? 0.2568 0.2693 0.2391 -0.0040 0.0124  -0.0049 980  GLU A CG  
7119  C CD  . GLU A 982  ? 0.2956 0.3176 0.2778 -0.0060 0.0127  -0.0039 980  GLU A CD  
7120  O OE1 . GLU A 982  ? 0.3249 0.3479 0.3062 -0.0071 0.0127  -0.0023 980  GLU A OE1 
7121  O OE2 . GLU A 982  ? 0.2774 0.3065 0.2605 -0.0063 0.0130  -0.0046 980  GLU A OE2 
7122  N N   . THR A 983  ? 0.2023 0.1951 0.1820 -0.0032 0.0112  -0.0014 981  THR A N   
7123  C CA  . THR A 983  ? 0.1952 0.1843 0.1746 -0.0044 0.0101  0.0014  981  THR A CA  
7124  C C   . THR A 983  ? 0.2033 0.1858 0.1822 -0.0027 0.0097  0.0009  981  THR A C   
7125  O O   . THR A 983  ? 0.2094 0.1898 0.1886 -0.0031 0.0086  0.0020  981  THR A O   
7126  C CB  . THR A 983  ? 0.2099 0.1986 0.1889 -0.0054 0.0098  0.0032  981  THR A CB  
7127  O OG1 . THR A 983  ? 0.2397 0.2357 0.2189 -0.0072 0.0101  0.0041  981  THR A OG1 
7128  C CG2 . THR A 983  ? 0.2116 0.1956 0.1909 -0.0063 0.0084  0.0057  981  THR A CG2 
7129  N N   . ILE A 984  ? 0.2103 0.1899 0.1888 -0.0007 0.0104  -0.0008 982  ILE A N   
7130  C CA  . ILE A 984  ? 0.2054 0.1804 0.1835 0.0010  0.0102  -0.0011 982  ILE A CA  
7131  C C   . ILE A 984  ? 0.2290 0.2050 0.2075 0.0013  0.0098  -0.0017 982  ILE A C   
7132  O O   . ILE A 984  ? 0.2152 0.1889 0.1933 0.0015  0.0089  -0.0012 982  ILE A O   
7133  C CB  . ILE A 984  ? 0.1974 0.1702 0.1755 0.0027  0.0111  -0.0022 982  ILE A CB  
7134  C CG1 . ILE A 984  ? 0.2290 0.2005 0.2068 0.0024  0.0113  -0.0014 982  ILE A CG1 
7135  C CG2 . ILE A 984  ? 0.2116 0.1811 0.1893 0.0044  0.0109  -0.0020 982  ILE A CG2 
7136  C CD1 . ILE A 984  ? 0.2559 0.2261 0.2345 0.0037  0.0120  -0.0023 982  ILE A CD1 
7137  N N   . ALA A 985  ? 0.1915 0.1713 0.1711 0.0015  0.0104  -0.0031 983  ALA A N   
7138  C CA  . ALA A 985  ? 0.2233 0.2044 0.2036 0.0020  0.0101  -0.0037 983  ALA A CA  
7139  C C   . ALA A 985  ? 0.2286 0.2112 0.2090 0.0002  0.0090  -0.0022 983  ALA A C   
7140  O O   . ALA A 985  ? 0.2311 0.2119 0.2115 0.0006  0.0082  -0.0021 983  ALA A O   
7141  C CB  . ALA A 985  ? 0.2261 0.2117 0.2082 0.0027  0.0108  -0.0058 983  ALA A CB  
7142  N N   . HIS A 986  ? 0.2200 0.2061 0.2007 -0.0018 0.0089  -0.0010 984  HIS A N   
7143  C CA  . HIS A 986  ? 0.2348 0.2226 0.2165 -0.0039 0.0077  0.0011  984  HIS A CA  
7144  C C   . HIS A 986  ? 0.2352 0.2173 0.2167 -0.0040 0.0062  0.0022  984  HIS A C   
7145  O O   . HIS A 986  ? 0.2227 0.2036 0.2049 -0.0040 0.0050  0.0022  984  HIS A O   
7146  C CB  . HIS A 986  ? 0.2465 0.2395 0.2288 -0.0061 0.0078  0.0029  984  HIS A CB  
7147  C CG  . HIS A 986  ? 0.2297 0.2244 0.2137 -0.0087 0.0063  0.0060  984  HIS A CG  
7148  N ND1 . HIS A 986  ? 0.2955 0.2945 0.2802 -0.0111 0.0060  0.0087  984  HIS A ND1 
7149  C CD2 . HIS A 986  ? 0.2496 0.2425 0.2350 -0.0094 0.0047  0.0070  984  HIS A CD2 
7150  C CE1 . HIS A 986  ? 0.3132 0.3128 0.3002 -0.0132 0.0042  0.0116  984  HIS A CE1 
7151  N NE2 . HIS A 986  ? 0.2498 0.2455 0.2373 -0.0123 0.0034  0.0104  984  HIS A NE2 
7152  N N   . VAL A 987  ? 0.2281 0.2070 0.2089 -0.0038 0.0062  0.0027  985  VAL A N   
7153  C CA  . VAL A 987  ? 0.2422 0.2163 0.2233 -0.0038 0.0046  0.0034  985  VAL A CA  
7154  C C   . VAL A 987  ? 0.2381 0.2088 0.2181 -0.0016 0.0044  0.0014  985  VAL A C   
7155  O O   . VAL A 987  ? 0.2421 0.2109 0.2230 -0.0016 0.0028  0.0012  985  VAL A O   
7156  C CB  . VAL A 987  ? 0.2043 0.1761 0.1849 -0.0038 0.0047  0.0041  985  VAL A CB  
7157  C CG1 . VAL A 987  ? 0.2078 0.1746 0.1889 -0.0031 0.0032  0.0039  985  VAL A CG1 
7158  C CG2 . VAL A 987  ? 0.2502 0.2257 0.2321 -0.0063 0.0045  0.0066  985  VAL A CG2 
7159  N N   . THR A 988  ? 0.2371 0.2073 0.2156 0.0004  0.0058  0.0001  986  THR A N   
7160  C CA  . THR A 988  ? 0.2598 0.2275 0.2371 0.0025  0.0056  -0.0012 986  THR A CA  
7161  C C   . THR A 988  ? 0.2823 0.2518 0.2602 0.0025  0.0050  -0.0018 986  THR A C   
7162  O O   . THR A 988  ? 0.2722 0.2402 0.2495 0.0037  0.0041  -0.0027 986  THR A O   
7163  C CB  . THR A 988  ? 0.2662 0.2332 0.2423 0.0043  0.0071  -0.0018 986  THR A CB  
7164  O OG1 . THR A 988  ? 0.2668 0.2365 0.2438 0.0044  0.0081  -0.0022 986  THR A OG1 
7165  C CG2 . THR A 988  ? 0.2460 0.2113 0.2217 0.0043  0.0076  -0.0012 986  THR A CG2 
7166  N N   . SER A 989  ? 0.2455 0.2187 0.2247 0.0014  0.0054  -0.0015 987  SER A N   
7167  C CA  . SER A 989  ? 0.2629 0.2380 0.2429 0.0014  0.0047  -0.0020 987  SER A CA  
7168  C C   . SER A 989  ? 0.2820 0.2569 0.2635 -0.0003 0.0027  -0.0012 987  SER A C   
7169  O O   . SER A 989  ? 0.3355 0.3106 0.3174 0.0000  0.0017  -0.0019 987  SER A O   
7170  C CB  . SER A 989  ? 0.2998 0.2795 0.2809 0.0010  0.0058  -0.0023 987  SER A CB  
7171  O OG  . SER A 989  ? 0.3473 0.3306 0.3295 -0.0012 0.0058  -0.0011 987  SER A OG  
7172  N N   . ARG A 990  ? 0.2370 0.2113 0.2195 -0.0021 0.0020  0.0003  988  ARG A N   
7173  C CA  . ARG A 990  ? 0.2682 0.2424 0.2532 -0.0042 -0.0002 0.0016  988  ARG A CA  
7174  C C   . ARG A 990  ? 0.2672 0.2365 0.2528 -0.0036 -0.0021 0.0009  988  ARG A C   
7175  O O   . ARG A 990  ? 0.2800 0.2481 0.2680 -0.0045 -0.0043 0.0009  988  ARG A O   
7176  C CB  . ARG A 990  ? 0.2881 0.2658 0.2751 -0.0069 -0.0002 0.0043  988  ARG A CB  
7177  C CG  . ARG A 990  ? 0.3374 0.3213 0.3240 -0.0074 0.0015  0.0046  988  ARG A CG  
7178  C CD  . ARG A 990  ? 0.3356 0.3230 0.3241 -0.0084 0.0007  0.0049  988  ARG A CD  
7179  N NE  . ARG A 990  ? 0.3556 0.3469 0.3470 -0.0116 -0.0004 0.0082  988  ARG A NE  
7180  C CZ  . ARG A 990  ? 0.3427 0.3376 0.3366 -0.0132 -0.0015 0.0094  988  ARG A CZ  
7181  N NH1 . ARG A 990  ? 0.3522 0.3469 0.3460 -0.0119 -0.0016 0.0075  988  ARG A NH1 
7182  N NH2 . ARG A 990  ? 0.3271 0.3264 0.3238 -0.0163 -0.0024 0.0130  988  ARG A NH2 
7183  N N   . ILE A 991  ? 0.2572 0.2236 0.2410 -0.0021 -0.0013 0.0002  989  ILE A N   
7184  C CA  . ILE A 991  ? 0.2375 0.1999 0.2219 -0.0011 -0.0030 -0.0011 989  ILE A CA  
7185  C C   . ILE A 991  ? 0.2439 0.2054 0.2271 0.0010  -0.0037 -0.0037 989  ILE A C   
7186  O O   . ILE A 991  ? 0.2551 0.2185 0.2361 0.0023  -0.0022 -0.0044 989  ILE A O   
7187  C CB  . ILE A 991  ? 0.2153 0.1758 0.1980 0.0001  -0.0017 -0.0012 989  ILE A CB  
7188  C CG1 . ILE A 991  ? 0.2355 0.1923 0.2197 0.0008  -0.0037 -0.0023 989  ILE A CG1 
7189  C CG2 . ILE A 991  ? 0.2243 0.1854 0.2037 0.0025  0.0004  -0.0026 989  ILE A CG2 
7190  C CD1 . ILE A 991  ? 0.2557 0.2113 0.2439 -0.0017 -0.0060 -0.0002 989  ILE A CD1 
7191  N N   . LYS A 992  ? 0.2245 0.1835 0.2095 0.0013  -0.0061 -0.0052 990  LYS A N   
7192  C CA  . LYS A 992  ? 0.2091 0.1679 0.1931 0.0034  -0.0071 -0.0082 990  LYS A CA  
7193  C C   . LYS A 992  ? 0.2139 0.1703 0.1973 0.0055  -0.0078 -0.0105 990  LYS A C   
7194  O O   . LYS A 992  ? 0.2541 0.2081 0.2405 0.0054  -0.0104 -0.0120 990  LYS A O   
7195  C CB  . LYS A 992  ? 0.2629 0.2217 0.2502 0.0020  -0.0098 -0.0086 990  LYS A CB  
7196  N N   . ALA A 993  ? 0.2314 0.1887 0.2113 0.0075  -0.0056 -0.0109 991  ALA A N   
7197  C CA  . ALA A 993  ? 0.2215 0.1778 0.2006 0.0097  -0.0059 -0.0131 991  ALA A CA  
7198  C C   . ALA A 993  ? 0.2262 0.1853 0.2013 0.0120  -0.0038 -0.0136 991  ALA A C   
7199  O O   . ALA A 993  ? 0.2227 0.1835 0.1961 0.0117  -0.0018 -0.0116 991  ALA A O   
7200  C CB  . ALA A 993  ? 0.2226 0.1766 0.2027 0.0090  -0.0055 -0.0117 991  ALA A CB  
7201  N N   . GLY A 994  ? 0.2242 0.1842 0.1980 0.0144  -0.0043 -0.0163 992  GLY A N   
7202  C CA  . GLY A 994  ? 0.2424 0.2062 0.2127 0.0166  -0.0027 -0.0165 992  GLY A CA  
7203  C C   . GLY A 994  ? 0.2147 0.1792 0.1834 0.0171  -0.0002 -0.0143 992  GLY A C   
7204  O O   . GLY A 994  ? 0.2090 0.1764 0.1755 0.0179  0.0015  -0.0128 992  GLY A O   
7205  N N   . ASN A 995  ? 0.2115 0.1734 0.1814 0.0165  0.0000  -0.0139 993  ASN A N   
7206  C CA  . ASN A 995  ? 0.2145 0.1770 0.1832 0.0169  0.0022  -0.0119 993  ASN A CA  
7207  C C   . ASN A 995  ? 0.2019 0.1614 0.1724 0.0146  0.0026  -0.0098 993  ASN A C   
7208  O O   . ASN A 995  ? 0.2102 0.1671 0.1830 0.0138  0.0012  -0.0103 993  ASN A O   
7209  C CB  . ASN A 995  ? 0.2082 0.1720 0.1763 0.0191  0.0020  -0.0139 993  ASN A CB  
7210  C CG  . ASN A 995  ? 0.2218 0.1906 0.1871 0.0215  0.0026  -0.0150 993  ASN A CG  
7211  O OD1 . ASN A 995  ? 0.2237 0.1942 0.1888 0.0226  0.0010  -0.0178 993  ASN A OD1 
7212  N ND2 . ASN A 995  ? 0.2068 0.1786 0.1704 0.0221  0.0047  -0.0126 993  ASN A ND2 
7213  N N   . LEU A 996  ? 0.1978 0.1580 0.1678 0.0136  0.0043  -0.0074 994  LEU A N   
7214  C CA  . LEU A 996  ? 0.1936 0.1521 0.1649 0.0116  0.0049  -0.0055 994  LEU A CA  
7215  C C   . LEU A 996  ? 0.2071 0.1658 0.1777 0.0121  0.0066  -0.0042 994  LEU A C   
7216  O O   . LEU A 996  ? 0.1935 0.1541 0.1628 0.0135  0.0078  -0.0037 994  LEU A O   
7217  C CB  . LEU A 996  ? 0.1836 0.1431 0.1553 0.0102  0.0054  -0.0043 994  LEU A CB  
7218  C CG  . LEU A 996  ? 0.2001 0.1603 0.1722 0.0100  0.0041  -0.0054 994  LEU A CG  
7219  C CD1 . LEU A 996  ? 0.2412 0.2030 0.2139 0.0088  0.0049  -0.0042 994  LEU A CD1 
7220  C CD2 . LEU A 996  ? 0.2190 0.1774 0.1932 0.0088  0.0020  -0.0062 994  LEU A CD2 
7221  N N   . TYR A 997  ? 0.2128 0.1699 0.1847 0.0108  0.0066  -0.0033 995  TYR A N   
7222  C CA  . TYR A 997  ? 0.2223 0.1794 0.1939 0.0111  0.0080  -0.0022 995  TYR A CA  
7223  C C   . TYR A 997  ? 0.1945 0.1511 0.1673 0.0090  0.0084  -0.0008 995  TYR A C   
7224  O O   . TYR A 997  ? 0.2030 0.1587 0.1771 0.0075  0.0073  -0.0005 995  TYR A O   
7225  C CB  . TYR A 997  ? 0.2029 0.1592 0.1748 0.0122  0.0075  -0.0031 995  TYR A CB  
7226  C CG  . TYR A 997  ? 0.2134 0.1711 0.1841 0.0145  0.0069  -0.0051 995  TYR A CG  
7227  C CD1 . TYR A 997  ? 0.2300 0.1867 0.2016 0.0148  0.0049  -0.0073 995  TYR A CD1 
7228  C CD2 . TYR A 997  ? 0.2204 0.1810 0.1895 0.0163  0.0083  -0.0048 995  TYR A CD2 
7229  C CE1 . TYR A 997  ? 0.2717 0.2304 0.2424 0.0170  0.0042  -0.0098 995  TYR A CE1 
7230  C CE2 . TYR A 997  ? 0.2518 0.2150 0.2196 0.0184  0.0078  -0.0068 995  TYR A CE2 
7231  C CZ  . TYR A 997  ? 0.2689 0.2311 0.2374 0.0189  0.0058  -0.0096 995  TYR A CZ  
7232  O OH  . TYR A 997  ? 0.2934 0.2588 0.2608 0.0212  0.0051  -0.0123 995  TYR A OH  
7233  N N   . ILE A 998  ? 0.1979 0.1555 0.1706 0.0090  0.0098  0.0002  996  ILE A N   
7234  C CA  . ILE A 998  ? 0.1959 0.1541 0.1697 0.0073  0.0103  0.0009  996  ILE A CA  
7235  C C   . ILE A 998  ? 0.1956 0.1533 0.1696 0.0074  0.0110  0.0017  996  ILE A C   
7236  O O   . ILE A 998  ? 0.2071 0.1650 0.1811 0.0085  0.0120  0.0021  996  ILE A O   
7237  C CB  . ILE A 998  ? 0.2234 0.1832 0.1975 0.0072  0.0109  0.0007  996  ILE A CB  
7238  C CG1 . ILE A 998  ? 0.2817 0.2421 0.2555 0.0073  0.0102  0.0000  996  ILE A CG1 
7239  C CG2 . ILE A 998  ? 0.1951 0.1564 0.1703 0.0056  0.0112  0.0008  996  ILE A CG2 
7240  C CD1 . ILE A 998  ? 0.2836 0.2441 0.2578 0.0057  0.0090  -0.0001 996  ILE A CD1 
7241  N N   . ASN A 999  ? 0.1908 0.1481 0.1655 0.0061  0.0106  0.0022  997  ASN A N   
7242  C CA  . ASN A 999  ? 0.1879 0.1452 0.1631 0.0059  0.0112  0.0030  997  ASN A CA  
7243  C C   . ASN A 999  ? 0.1835 0.1397 0.1583 0.0075  0.0115  0.0030  997  ASN A C   
7244  O O   . ASN A 999  ? 0.2034 0.1600 0.1786 0.0079  0.0124  0.0037  997  ASN A O   
7245  C CB  . ASN A 999  ? 0.1974 0.1562 0.1733 0.0055  0.0121  0.0029  997  ASN A CB  
7246  C CG  . ASN A 999  ? 0.1947 0.1557 0.1710 0.0039  0.0119  0.0025  997  ASN A CG  
7247  O OD1 . ASN A 999  ? 0.2126 0.1742 0.1888 0.0026  0.0111  0.0032  997  ASN A OD1 
7248  N ND2 . ASN A 999  ? 0.2107 0.1733 0.1877 0.0040  0.0124  0.0015  997  ASN A ND2 
7249  N N   . ARG A 1000 ? 0.1986 0.1540 0.1731 0.0085  0.0106  0.0023  998  ARG A N   
7250  C CA  . ARG A 1000 ? 0.2082 0.1636 0.1823 0.0104  0.0108  0.0019  998  ARG A CA  
7251  C C   . ARG A 1000 ? 0.2190 0.1730 0.1936 0.0109  0.0091  0.0004  998  ARG A C   
7252  O O   . ARG A 1000 ? 0.2187 0.1716 0.1942 0.0097  0.0078  0.0002  998  ARG A O   
7253  C CB  . ARG A 1000 ? 0.2092 0.1665 0.1822 0.0119  0.0119  0.0019  998  ARG A CB  
7254  C CG  . ARG A 1000 ? 0.1981 0.1559 0.1702 0.0122  0.0114  0.0011  998  ARG A CG  
7255  C CD  . ARG A 1000 ? 0.2002 0.1603 0.1709 0.0141  0.0120  0.0009  998  ARG A CD  
7256  N NE  . ARG A 1000 ? 0.2065 0.1673 0.1766 0.0157  0.0114  -0.0007 998  ARG A NE  
7257  C CZ  . ARG A 1000 ? 0.2242 0.1883 0.1931 0.0177  0.0118  -0.0012 998  ARG A CZ  
7258  N NH1 . ARG A 1000 ? 0.2145 0.1814 0.1825 0.0182  0.0128  0.0004  998  ARG A NH1 
7259  N NH2 . ARG A 1000 ? 0.2188 0.1838 0.1874 0.0193  0.0110  -0.0034 998  ARG A NH2 
7260  N N   . ASN A 1001 ? 0.2160 0.1704 0.1905 0.0129  0.0090  -0.0007 999  ASN A N   
7261  C CA  . ASN A 1001 ? 0.2279 0.1811 0.2036 0.0138  0.0072  -0.0028 999  ASN A CA  
7262  C C   . ASN A 1001 ? 0.2286 0.1827 0.2031 0.0146  0.0066  -0.0044 999  ASN A C   
7263  O O   . ASN A 1001 ? 0.2145 0.1704 0.1873 0.0147  0.0079  -0.0037 999  ASN A O   
7264  C CB  . ASN A 1001 ? 0.2242 0.1783 0.2005 0.0159  0.0071  -0.0040 999  ASN A CB  
7265  C CG  . ASN A 1001 ? 0.2744 0.2323 0.2485 0.0181  0.0086  -0.0048 999  ASN A CG  
7266  O OD1 . ASN A 1001 ? 0.2628 0.2224 0.2354 0.0189  0.0086  -0.0058 999  ASN A OD1 
7267  N ND2 . ASN A 1001 ? 0.3223 0.2823 0.2964 0.0192  0.0097  -0.0043 999  ASN A ND2 
7268  N N   A ILE A 1002 ? 0.2216 0.1743 0.1976 0.0152  0.0045  -0.0066 1000 ILE A N   
7269  N N   B ILE A 1002 ? 0.2217 0.1744 0.1977 0.0153  0.0045  -0.0066 1000 ILE A N   
7270  C CA  A ILE A 1002 ? 0.2216 0.1749 0.1970 0.0157  0.0036  -0.0084 1000 ILE A CA  
7271  C CA  B ILE A 1002 ? 0.2216 0.1751 0.1968 0.0160  0.0037  -0.0085 1000 ILE A CA  
7272  C C   A ILE A 1002 ? 0.2253 0.1807 0.2002 0.0186  0.0029  -0.0117 1000 ILE A C   
7273  C C   B ILE A 1002 ? 0.2249 0.1808 0.1995 0.0189  0.0032  -0.0117 1000 ILE A C   
7274  O O   A ILE A 1002 ? 0.2474 0.2028 0.2226 0.0192  0.0013  -0.0140 1000 ILE A O   
7275  O O   B ILE A 1002 ? 0.2493 0.2055 0.2241 0.0198  0.0017  -0.0142 1000 ILE A O   
7276  C CB  A ILE A 1002 ? 0.2198 0.1703 0.1979 0.0137  0.0014  -0.0082 1000 ILE A CB  
7277  C CB  B ILE A 1002 ? 0.2195 0.1701 0.1973 0.0142  0.0013  -0.0087 1000 ILE A CB  
7278  C CG1 A ILE A 1002 ? 0.2147 0.1626 0.1963 0.0142  -0.0012 -0.0099 1000 ILE A CG1 
7279  C CG1 B ILE A 1002 ? 0.2146 0.1627 0.1961 0.0146  -0.0011 -0.0103 1000 ILE A CG1 
7280  C CG2 A ILE A 1002 ? 0.2092 0.1590 0.1875 0.0110  0.0022  -0.0050 1000 ILE A CG2 
7281  C CG2 B ILE A 1002 ? 0.2089 0.1589 0.1871 0.0113  0.0020  -0.0055 1000 ILE A CG2 
7282  C CD1 A ILE A 1002 ? 0.2191 0.1644 0.2041 0.0124  -0.0039 -0.0099 1000 ILE A CD1 
7283  C CD1 B ILE A 1002 ? 0.2196 0.1650 0.2045 0.0127  -0.0039 -0.0102 1000 ILE A CD1 
7284  N N   A ILE A 1003 ? 0.2369 0.1946 0.2110 0.0205  0.0040  -0.0122 1001 ILE A N   
7285  N N   B ILE A 1003 ? 0.2357 0.1939 0.2095 0.0206  0.0044  -0.0119 1001 ILE A N   
7286  C CA  A ILE A 1003 ? 0.2435 0.2045 0.2170 0.0235  0.0034  -0.0157 1001 ILE A CA  
7287  C CA  B ILE A 1003 ? 0.2435 0.2050 0.2168 0.0236  0.0040  -0.0152 1001 ILE A CA  
7288  C C   A ILE A 1003 ? 0.2495 0.2160 0.2196 0.0248  0.0056  -0.0149 1001 ILE A C   
7289  C C   B ILE A 1003 ? 0.2351 0.2020 0.2054 0.0250  0.0065  -0.0139 1001 ILE A C   
7290  O O   A ILE A 1003 ? 0.2473 0.2182 0.2162 0.0274  0.0058  -0.0172 1001 ILE A O   
7291  O O   B ILE A 1003 ? 0.2297 0.1968 0.1989 0.0236  0.0083  -0.0104 1001 ILE A O   
7292  C CB  A ILE A 1003 ? 0.2398 0.2004 0.2155 0.0250  0.0027  -0.0175 1001 ILE A CB  
7293  C CB  B ILE A 1003 ? 0.2419 0.2019 0.2181 0.0248  0.0025  -0.0174 1001 ILE A CB  
7294  C CG1 A ILE A 1003 ? 0.2517 0.2130 0.2268 0.0243  0.0049  -0.0143 1001 ILE A CG1 
7295  C CG1 B ILE A 1003 ? 0.2560 0.2161 0.2324 0.0243  0.0042  -0.0148 1001 ILE A CG1 
7296  C CG2 A ILE A 1003 ? 0.2286 0.1840 0.2086 0.0239  -0.0002 -0.0187 1001 ILE A CG2 
7297  C CG2 B ILE A 1003 ? 0.2285 0.1833 0.2086 0.0234  -0.0004 -0.0183 1001 ILE A CG2 
7298  C CD1 A ILE A 1003 ? 0.2619 0.2235 0.2393 0.0260  0.0043  -0.0160 1001 ILE A CD1 
7299  C CD1 B ILE A 1003 ? 0.2555 0.2154 0.2346 0.0261  0.0031  -0.0171 1001 ILE A CD1 
7300  N N   A GLY A 1004 ? 0.2564 0.2230 0.2250 0.0232  0.0071  -0.0117 1002 GLY A N   
7301  N N   B GLY A 1004 ? 0.2481 0.2197 0.2174 0.0278  0.0064  -0.0168 1002 GLY A N   
7302  C CA  A GLY A 1004 ? 0.2375 0.2091 0.2035 0.0242  0.0089  -0.0101 1002 GLY A CA  
7303  C CA  B GLY A 1004 ? 0.2368 0.2148 0.2034 0.0292  0.0086  -0.0153 1002 GLY A CA  
7304  C C   A GLY A 1004 ? 0.2307 0.2057 0.1950 0.0257  0.0081  -0.0122 1002 GLY A C   
7305  C C   B GLY A 1004 ? 0.2440 0.2244 0.2083 0.0284  0.0097  -0.0127 1002 GLY A C   
7306  O O   A GLY A 1004 ? 0.2407 0.2133 0.2054 0.0247  0.0068  -0.0131 1002 GLY A O   
7307  O O   B GLY A 1004 ? 0.2456 0.2289 0.2089 0.0280  0.0116  -0.0092 1002 GLY A O   
7308  N N   A ALA A 1005 ? 0.2249 0.2061 0.1874 0.0280  0.0089  -0.0129 1003 ALA A N   
7309  N N   B ALA A 1005 ? 0.2256 0.2047 0.1895 0.0281  0.0083  -0.0142 1003 ALA A N   
7310  C CA  A ALA A 1005 ? 0.2391 0.2249 0.1996 0.0294  0.0083  -0.0147 1003 ALA A CA  
7311  C CA  B ALA A 1005 ? 0.2319 0.2135 0.1939 0.0275  0.0091  -0.0120 1003 ALA A CA  
7312  C C   A ALA A 1005 ? 0.2350 0.2282 0.1931 0.0306  0.0102  -0.0120 1003 ALA A C   
7313  C C   B ALA A 1005 ? 0.2445 0.2339 0.2042 0.0295  0.0106  -0.0109 1003 ALA A C   
7314  O O   A ALA A 1005 ? 0.2448 0.2445 0.2010 0.0329  0.0099  -0.0142 1003 ALA A O   
7315  O O   B ALA A 1005 ? 0.2615 0.2556 0.2203 0.0319  0.0103  -0.0139 1003 ALA A O   
7316  C CB  A ALA A 1005 ? 0.2413 0.2281 0.2023 0.0316  0.0062  -0.0202 1003 ALA A CB  
7317  C CB  B ALA A 1005 ? 0.2452 0.2254 0.2071 0.0275  0.0072  -0.0145 1003 ALA A CB  
7318  N N   A VAL A 1006 ? 0.2272 0.2200 0.1858 0.0291  0.0119  -0.0074 1004 VAL A N   
7319  N N   B VAL A 1006 ? 0.2280 0.2192 0.1870 0.0284  0.0120  -0.0066 1004 VAL A N   
7320  C CA  A VAL A 1006 ? 0.2416 0.2414 0.1989 0.0299  0.0136  -0.0039 1004 VAL A CA  
7321  C CA  B VAL A 1006 ? 0.2418 0.2408 0.1993 0.0297  0.0135  -0.0040 1004 VAL A CA  
7322  C C   A VAL A 1006 ? 0.2356 0.2399 0.1911 0.0304  0.0132  -0.0033 1004 VAL A C   
7323  C C   B VAL A 1006 ? 0.2361 0.2394 0.1917 0.0304  0.0130  -0.0039 1004 VAL A C   
7324  O O   A VAL A 1006 ? 0.2274 0.2283 0.1835 0.0289  0.0128  -0.0017 1004 VAL A O   
7325  O O   B VAL A 1006 ? 0.2309 0.2306 0.1870 0.0290  0.0124  -0.0031 1004 VAL A O   
7326  C CB  A VAL A 1006 ? 0.2388 0.2360 0.1980 0.0278  0.0149  0.0009  1004 VAL A CB  
7327  C CB  B VAL A 1006 ? 0.2381 0.2363 0.1972 0.0280  0.0151  0.0012  1004 VAL A CB  
7328  C CG1 A VAL A 1006 ? 0.2399 0.2444 0.1987 0.0283  0.0164  0.0052  1004 VAL A CG1 
7329  C CG1 B VAL A 1006 ? 0.2413 0.2478 0.1994 0.0289  0.0164  0.0048  1004 VAL A CG1 
7330  C CG2 A VAL A 1006 ? 0.2381 0.2316 0.1990 0.0274  0.0152  0.0002  1004 VAL A CG2 
7331  C CG2 B VAL A 1006 ? 0.2393 0.2340 0.2001 0.0274  0.0155  0.0009  1004 VAL A CG2 
7332  N N   A VAL A 1007 ? 0.2259 0.2384 0.1791 0.0328  0.0134  -0.0047 1005 VAL A N   
7333  N N   B VAL A 1007 ? 0.2258 0.2377 0.1792 0.0326  0.0134  -0.0047 1005 VAL A N   
7334  C CA  A VAL A 1007 ? 0.2268 0.2449 0.1779 0.0337  0.0129  -0.0045 1005 VAL A CA  
7335  C CA  B VAL A 1007 ? 0.2269 0.2444 0.1782 0.0335  0.0129  -0.0045 1005 VAL A CA  
7336  C C   A VAL A 1007 ? 0.2260 0.2441 0.1780 0.0318  0.0137  0.0015  1005 VAL A C   
7337  C C   B VAL A 1007 ? 0.2260 0.2437 0.1782 0.0317  0.0137  0.0014  1005 VAL A C   
7338  O O   A VAL A 1007 ? 0.2331 0.2529 0.1864 0.0310  0.0151  0.0060  1005 VAL A O   
7339  O O   B VAL A 1007 ? 0.2330 0.2519 0.1865 0.0309  0.0151  0.0059  1005 VAL A O   
7340  C CB  A VAL A 1007 ? 0.2184 0.2472 0.1670 0.0365  0.0134  -0.0061 1005 VAL A CB  
7341  C CB  B VAL A 1007 ? 0.2185 0.2467 0.1673 0.0364  0.0134  -0.0061 1005 VAL A CB  
7342  C CG1 A VAL A 1007 ? 0.2314 0.2671 0.1776 0.0373  0.0129  -0.0054 1005 VAL A CG1 
7343  C CG1 B VAL A 1007 ? 0.2316 0.2669 0.1781 0.0372  0.0130  -0.0051 1005 VAL A CG1 
7344  C CG2 A VAL A 1007 ? 0.2318 0.2600 0.1803 0.0386  0.0121  -0.0128 1005 VAL A CG2 
7345  C CG2 B VAL A 1007 ? 0.2319 0.2595 0.1806 0.0385  0.0120  -0.0129 1005 VAL A CG2 
7346  N N   . GLY A 1008 ? 0.2179 0.2342 0.1698 0.0311  0.0127  0.0014  1006 GLY A N   
7347  C CA  . GLY A 1008 ? 0.2167 0.2329 0.1700 0.0296  0.0131  0.0066  1006 GLY A CA  
7348  C C   . GLY A 1008 ? 0.2164 0.2246 0.1730 0.0273  0.0135  0.0090  1006 GLY A C   
7349  O O   . GLY A 1008 ? 0.2462 0.2539 0.2049 0.0261  0.0136  0.0131  1006 GLY A O   
7350  N N   . VAL A 1009 ? 0.2250 0.2274 0.1824 0.0267  0.0135  0.0064  1007 VAL A N   
7351  C CA  . VAL A 1009 ? 0.2106 0.2062 0.1710 0.0246  0.0138  0.0080  1007 VAL A CA  
7352  C C   . VAL A 1009 ? 0.2180 0.2070 0.1787 0.0237  0.0127  0.0044  1007 VAL A C   
7353  O O   . VAL A 1009 ? 0.2142 0.1991 0.1767 0.0222  0.0123  0.0051  1007 VAL A O   
7354  C CB  . VAL A 1009 ? 0.2410 0.2366 0.2026 0.0244  0.0150  0.0096  1007 VAL A CB  
7355  C CG1 . VAL A 1009 ? 0.2520 0.2410 0.2166 0.0223  0.0151  0.0109  1007 VAL A CG1 
7356  C CG2 . VAL A 1009 ? 0.2228 0.2255 0.1845 0.0250  0.0160  0.0139  1007 VAL A CG2 
7357  N N   . GLN A 1010 ? 0.2119 0.2003 0.1714 0.0246  0.0120  0.0004  1008 GLN A N   
7358  C CA  . GLN A 1010 ? 0.2264 0.2103 0.1863 0.0240  0.0104  -0.0030 1008 GLN A CA  
7359  C C   . GLN A 1010 ? 0.2172 0.2050 0.1752 0.0260  0.0092  -0.0064 1008 GLN A C   
7360  O O   . GLN A 1010 ? 0.2308 0.2189 0.1885 0.0272  0.0084  -0.0099 1008 GLN A O   
7361  C CB  . GLN A 1010 ? 0.2388 0.2179 0.2002 0.0232  0.0101  -0.0046 1008 GLN A CB  
7362  C CG  . GLN A 1010 ? 0.2251 0.2010 0.1883 0.0214  0.0113  -0.0017 1008 GLN A CG  
7363  C CD  . GLN A 1010 ? 0.2539 0.2320 0.2172 0.0222  0.0125  -0.0003 1008 GLN A CD  
7364  O OE1 . GLN A 1010 ? 0.2366 0.2170 0.1990 0.0238  0.0123  -0.0023 1008 GLN A OE1 
7365  N NE2 . GLN A 1010 ? 0.2225 0.1999 0.1873 0.0210  0.0137  0.0030  1008 GLN A NE2 
7366  N N   . PRO A 1011 ? 0.2285 0.2196 0.1853 0.0264  0.0088  -0.0058 1009 PRO A N   
7367  C CA  . PRO A 1011 ? 0.2250 0.2193 0.1803 0.0280  0.0072  -0.0097 1009 PRO A CA  
7368  C C   . PRO A 1011 ? 0.2076 0.1962 0.1645 0.0274  0.0054  -0.0136 1009 PRO A C   
7369  O O   . PRO A 1011 ? 0.1946 0.1776 0.1535 0.0253  0.0051  -0.0127 1009 PRO A O   
7370  C CB  . PRO A 1011 ? 0.2013 0.1973 0.1561 0.0275  0.0069  -0.0078 1009 PRO A CB  
7371  C CG  . PRO A 1011 ? 0.2127 0.2101 0.1681 0.0268  0.0086  -0.0026 1009 PRO A CG  
7372  C CD  . PRO A 1011 ? 0.2219 0.2139 0.1793 0.0254  0.0095  -0.0017 1009 PRO A CD  
7373  N N   . PHE A 1012 ? 0.2355 0.2260 0.1921 0.0293  0.0041  -0.0179 1010 PHE A N   
7374  C CA  . PHE A 1012 ? 0.2232 0.2083 0.1824 0.0288  0.0023  -0.0211 1010 PHE A CA  
7375  C C   . PHE A 1012 ? 0.2280 0.2127 0.1880 0.0294  -0.0004 -0.0253 1010 PHE A C   
7376  O O   . PHE A 1012 ? 0.2168 0.2072 0.1750 0.0317  -0.0010 -0.0282 1010 PHE A O   
7377  C CB  . PHE A 1012 ? 0.2044 0.1908 0.1640 0.0306  0.0025  -0.0232 1010 PHE A CB  
7378  C CG  . PHE A 1012 ? 0.2207 0.2009 0.1837 0.0299  0.0006  -0.0258 1010 PHE A CG  
7379  C CD1 . PHE A 1012 ? 0.2537 0.2283 0.2188 0.0275  0.0011  -0.0228 1010 PHE A CD1 
7380  C CD2 . PHE A 1012 ? 0.2512 0.2314 0.2160 0.0316  -0.0020 -0.0310 1010 PHE A CD2 
7381  C CE1 . PHE A 1012 ? 0.2409 0.2102 0.2096 0.0266  -0.0009 -0.0245 1010 PHE A CE1 
7382  C CE2 . PHE A 1012 ? 0.2577 0.2320 0.2266 0.0308  -0.0042 -0.0329 1010 PHE A CE2 
7383  C CZ  . PHE A 1012 ? 0.2400 0.2089 0.2108 0.0282  -0.0036 -0.0293 1010 PHE A CZ  
7384  N N   . GLY A 1013 ? 0.2175 0.1962 0.1805 0.0274  -0.0020 -0.0257 1011 GLY A N   
7385  C CA  . GLY A 1013 ? 0.2173 0.1948 0.1821 0.0277  -0.0049 -0.0297 1011 GLY A CA  
7386  C C   . GLY A 1013 ? 0.2277 0.2001 0.1950 0.0247  -0.0058 -0.0276 1011 GLY A C   
7387  O O   . GLY A 1013 ? 0.2379 0.2098 0.2044 0.0230  -0.0040 -0.0237 1011 GLY A O   
7388  N N   . GLY A 1014 ? 0.2301 0.1990 0.2010 0.0241  -0.0087 -0.0304 1012 GLY A N   
7389  C CA  . GLY A 1014 ? 0.2578 0.2222 0.2318 0.0211  -0.0098 -0.0284 1012 GLY A CA  
7390  C C   . GLY A 1014 ? 0.2586 0.2234 0.2342 0.0207  -0.0122 -0.0304 1012 GLY A C   
7391  O O   . GLY A 1014 ? 0.2526 0.2215 0.2261 0.0227  -0.0128 -0.0332 1012 GLY A O   
7392  N N   . ARG A 1015 ? 0.2249 0.1857 0.2041 0.0179  -0.0137 -0.0290 1013 ARG A N   
7393  C CA  . ARG A 1015 ? 0.2307 0.1915 0.2119 0.0168  -0.0158 -0.0297 1013 ARG A CA  
7394  C C   . ARG A 1015 ? 0.2469 0.2033 0.2342 0.0153  -0.0194 -0.0311 1013 ARG A C   
7395  O O   . ARG A 1015 ? 0.2332 0.1864 0.2230 0.0151  -0.0201 -0.0311 1013 ARG A O   
7396  C CB  . ARG A 1015 ? 0.2444 0.2058 0.2247 0.0144  -0.0139 -0.0254 1013 ARG A CB  
7397  C CG  . ARG A 1015 ? 0.2604 0.2186 0.2430 0.0118  -0.0132 -0.0218 1013 ARG A CG  
7398  C CD  . ARG A 1015 ? 0.2746 0.2340 0.2571 0.0095  -0.0120 -0.0184 1013 ARG A CD  
7399  N NE  . ARG A 1015 ? 0.3193 0.2804 0.3028 0.0092  -0.0136 -0.0195 1013 ARG A NE  
7400  C CZ  . ARG A 1015 ? 0.3409 0.3003 0.3288 0.0077  -0.0166 -0.0204 1013 ARG A CZ  
7401  N NH1 . ARG A 1015 ? 0.3354 0.2913 0.3273 0.0062  -0.0185 -0.0200 1013 ARG A NH1 
7402  N NH2 . ARG A 1015 ? 0.2847 0.2459 0.2731 0.0075  -0.0180 -0.0215 1013 ARG A NH2 
7403  N N   . GLY A 1016 ? 0.2398 0.1959 0.2299 0.0141  -0.0218 -0.0320 1014 GLY A N   
7404  C CA  . GLY A 1016 ? 0.2241 0.1759 0.2208 0.0123  -0.0256 -0.0328 1014 GLY A CA  
7405  C C   . GLY A 1016 ? 0.2397 0.1900 0.2389 0.0148  -0.0282 -0.0379 1014 GLY A C   
7406  O O   . GLY A 1016 ? 0.2642 0.2178 0.2608 0.0179  -0.0285 -0.0425 1014 GLY A O   
7407  N N   . LEU A 1017 ? 0.2423 0.1880 0.2468 0.0136  -0.0303 -0.0373 1015 LEU A N   
7408  C CA  . LEU A 1017 ? 0.2413 0.1852 0.2492 0.0161  -0.0330 -0.0424 1015 LEU A CA  
7409  C C   . LEU A 1017 ? 0.2417 0.1885 0.2445 0.0193  -0.0302 -0.0441 1015 LEU A C   
7410  O O   . LEU A 1017 ? 0.2647 0.2111 0.2697 0.0219  -0.0321 -0.0489 1015 LEU A O   
7411  C CB  . LEU A 1017 ? 0.2636 0.2017 0.2790 0.0138  -0.0359 -0.0404 1015 LEU A CB  
7412  C CG  . LEU A 1017 ? 0.2828 0.2180 0.3049 0.0104  -0.0394 -0.0383 1015 LEU A CG  
7413  C CD1 . LEU A 1017 ? 0.2619 0.1921 0.2908 0.0080  -0.0417 -0.0350 1015 LEU A CD1 
7414  C CD2 . LEU A 1017 ? 0.2745 0.2095 0.3004 0.0119  -0.0435 -0.0442 1015 LEU A CD2 
7415  N N   . SER A 1018 ? 0.2245 0.1744 0.2211 0.0192  -0.0259 -0.0406 1016 SER A N   
7416  C CA  . SER A 1018 ? 0.2386 0.1915 0.2308 0.0218  -0.0231 -0.0414 1016 SER A CA  
7417  C C   . SER A 1018 ? 0.2234 0.1828 0.2102 0.0247  -0.0216 -0.0441 1016 SER A C   
7418  O O   . SER A 1018 ? 0.2401 0.2029 0.2235 0.0271  -0.0196 -0.0451 1016 SER A O   
7419  C CB  . SER A 1018 ? 0.2229 0.1752 0.2123 0.0199  -0.0195 -0.0356 1016 SER A CB  
7420  O OG  . SER A 1018 ? 0.2303 0.1776 0.2245 0.0174  -0.0209 -0.0330 1016 SER A OG  
7421  N N   . GLY A 1019 ? 0.2412 0.2028 0.2271 0.0244  -0.0224 -0.0450 1017 GLY A N   
7422  C CA  . GLY A 1019 ? 0.2373 0.2057 0.2180 0.0271  -0.0209 -0.0470 1017 GLY A CA  
7423  C C   . GLY A 1019 ? 0.2461 0.2171 0.2254 0.0265  -0.0214 -0.0468 1017 GLY A C   
7424  O O   . GLY A 1019 ? 0.2465 0.2144 0.2277 0.0236  -0.0218 -0.0437 1017 GLY A O   
7425  N N   . THR A 1020 ? 0.2470 0.2244 0.2230 0.0293  -0.0215 -0.0503 1018 THR A N   
7426  C CA  . THR A 1020 ? 0.2501 0.2314 0.2236 0.0291  -0.0214 -0.0496 1018 THR A CA  
7427  C C   . THR A 1020 ? 0.2514 0.2369 0.2197 0.0292  -0.0176 -0.0449 1018 THR A C   
7428  O O   . THR A 1020 ? 0.2617 0.2491 0.2285 0.0282  -0.0170 -0.0425 1018 THR A O   
7429  C CB  . THR A 1020 ? 0.2327 0.2197 0.2054 0.0321  -0.0237 -0.0558 1018 THR A CB  
7430  O OG1 . THR A 1020 ? 0.2457 0.2384 0.2148 0.0352  -0.0221 -0.0577 1018 THR A OG1 
7431  C CG2 . THR A 1020 ? 0.2788 0.2615 0.2576 0.0322  -0.0282 -0.0611 1018 THR A CG2 
7432  N N   . GLY A 1021 ? 0.2494 0.2367 0.2153 0.0303  -0.0151 -0.0435 1019 GLY A N   
7433  C CA  . GLY A 1021 ? 0.2419 0.2345 0.2031 0.0311  -0.0120 -0.0398 1019 GLY A CA  
7434  C C   . GLY A 1021 ? 0.2447 0.2458 0.2027 0.0337  -0.0126 -0.0427 1019 GLY A C   
7435  O O   . GLY A 1021 ? 0.2434 0.2460 0.2026 0.0352  -0.0154 -0.0482 1019 GLY A O   
7436  N N   . PRO A 1022 ? 0.2386 0.2455 0.1927 0.0344  -0.0101 -0.0390 1020 PRO A N   
7437  C CA  . PRO A 1022 ? 0.2457 0.2512 0.1988 0.0330  -0.0071 -0.0328 1020 PRO A CA  
7438  C C   . PRO A 1022 ? 0.2396 0.2441 0.1928 0.0336  -0.0056 -0.0326 1020 PRO A C   
7439  O O   . PRO A 1022 ? 0.2510 0.2576 0.2043 0.0356  -0.0067 -0.0371 1020 PRO A O   
7440  C CB  . PRO A 1022 ? 0.2197 0.2334 0.1693 0.0341  -0.0057 -0.0299 1020 PRO A CB  
7441  C CG  . PRO A 1022 ? 0.2547 0.2760 0.2022 0.0371  -0.0072 -0.0351 1020 PRO A CG  
7442  C CD  . PRO A 1022 ? 0.2420 0.2585 0.1926 0.0369  -0.0104 -0.0408 1020 PRO A CD  
7443  N N   . LYS A 1023 ? 0.2212 0.2228 0.1746 0.0320  -0.0033 -0.0276 1021 LYS A N   
7444  C CA  . LYS A 1023 ? 0.2194 0.2196 0.1732 0.0322  -0.0019 -0.0270 1021 LYS A CA  
7445  C C   . LYS A 1023 ? 0.2298 0.2382 0.1805 0.0349  -0.0006 -0.0273 1021 LYS A C   
7446  O O   . LYS A 1023 ? 0.2196 0.2341 0.1680 0.0353  0.0008  -0.0240 1021 LYS A O   
7447  C CB  . LYS A 1023 ? 0.2061 0.2020 0.1607 0.0299  0.0003  -0.0216 1021 LYS A CB  
7448  C CG  . LYS A 1023 ? 0.2176 0.2057 0.1753 0.0273  -0.0005 -0.0210 1021 LYS A CG  
7449  C CD  . LYS A 1023 ? 0.2066 0.1926 0.1647 0.0255  0.0016  -0.0161 1021 LYS A CD  
7450  C CE  . LYS A 1023 ? 0.2109 0.1902 0.1717 0.0230  0.0013  -0.0154 1021 LYS A CE  
7451  N NZ  . LYS A 1023 ? 0.1919 0.1678 0.1541 0.0227  0.0012  -0.0163 1021 LYS A NZ  
7452  N N   . ALA A 1024 ? 0.2445 0.2535 0.1958 0.0365  -0.0010 -0.0309 1022 ALA A N   
7453  C CA  . ALA A 1024 ? 0.2469 0.2633 0.1959 0.0386  0.0007  -0.0304 1022 ALA A CA  
7454  C C   . ALA A 1024 ? 0.2408 0.2563 0.1896 0.0369  0.0035  -0.0239 1022 ALA A C   
7455  O O   . ALA A 1024 ? 0.2511 0.2589 0.2021 0.0346  0.0039  -0.0216 1022 ALA A O   
7456  C CB  . ALA A 1024 ? 0.2322 0.2482 0.1827 0.0405  -0.0003 -0.0355 1022 ALA A CB  
7457  N N   . GLY A 1025 ? 0.2127 0.2365 0.1589 0.0381  0.0053  -0.0210 1023 GLY A N   
7458  C CA  . GLY A 1025 ? 0.2209 0.2443 0.1676 0.0365  0.0075  -0.0147 1023 GLY A CA  
7459  C C   . GLY A 1025 ? 0.2428 0.2621 0.1905 0.0341  0.0078  -0.0103 1023 GLY A C   
7460  O O   . GLY A 1025 ? 0.2201 0.2360 0.1695 0.0324  0.0091  -0.0059 1023 GLY A O   
7461  N N   . GLY A 1026 ? 0.2292 0.2490 0.1763 0.0341  0.0063  -0.0116 1024 GLY A N   
7462  C CA  . GLY A 1026 ? 0.2307 0.2476 0.1791 0.0322  0.0064  -0.0078 1024 GLY A CA  
7463  C C   . GLY A 1026 ? 0.2265 0.2511 0.1728 0.0332  0.0059  -0.0065 1024 GLY A C   
7464  O O   . GLY A 1026 ? 0.2166 0.2489 0.1603 0.0354  0.0055  -0.0090 1024 GLY A O   
7465  N N   . PRO A 1027 ? 0.2020 0.2250 0.1496 0.0318  0.0059  -0.0026 1025 PRO A N   
7466  C CA  . PRO A 1027 ? 0.2289 0.2597 0.1750 0.0326  0.0058  0.0004  1025 PRO A CA  
7467  C C   . PRO A 1027 ? 0.2025 0.2356 0.1470 0.0335  0.0038  -0.0034 1025 PRO A C   
7468  O O   . PRO A 1027 ? 0.2205 0.2614 0.1633 0.0344  0.0035  -0.0015 1025 PRO A O   
7469  C CB  . PRO A 1027 ? 0.2238 0.2507 0.1730 0.0306  0.0063  0.0060  1025 PRO A CB  
7470  C CG  . PRO A 1027 ? 0.2526 0.2696 0.2042 0.0289  0.0061  0.0038  1025 PRO A CG  
7471  C CD  . PRO A 1027 ? 0.2228 0.2377 0.1736 0.0295  0.0064  0.0001  1025 PRO A CD  
7472  N N   . LEU A 1028 ? 0.2207 0.2479 0.1661 0.0331  0.0024  -0.0084 1026 LEU A N   
7473  C CA  . LEU A 1028 ? 0.2072 0.2364 0.1516 0.0339  0.0002  -0.0125 1026 LEU A CA  
7474  C C   . LEU A 1028 ? 0.2223 0.2569 0.1644 0.0364  -0.0009 -0.0182 1026 LEU A C   
7475  O O   . LEU A 1028 ? 0.2393 0.2770 0.1804 0.0374  -0.0028 -0.0220 1026 LEU A O   
7476  C CB  . LEU A 1028 ? 0.2092 0.2294 0.1564 0.0321  -0.0011 -0.0146 1026 LEU A CB  
7477  C CG  . LEU A 1028 ? 0.2310 0.2477 0.1804 0.0301  -0.0006 -0.0101 1026 LEU A CG  
7478  C CD1 . LEU A 1028 ? 0.2551 0.2635 0.2072 0.0282  -0.0015 -0.0122 1026 LEU A CD1 
7479  C CD2 . LEU A 1028 ? 0.2774 0.3001 0.2255 0.0308  -0.0016 -0.0090 1026 LEU A CD2 
7480  N N   . TYR A 1029 ? 0.2181 0.2545 0.1595 0.0375  0.0003  -0.0190 1027 TYR A N   
7481  C CA  . TYR A 1029 ? 0.2312 0.2714 0.1714 0.0400  -0.0010 -0.0254 1027 TYR A CA  
7482  C C   . TYR A 1029 ? 0.2150 0.2671 0.1517 0.0425  -0.0015 -0.0271 1027 TYR A C   
7483  O O   . TYR A 1029 ? 0.2241 0.2783 0.1603 0.0440  -0.0038 -0.0331 1027 TYR A O   
7484  C CB  . TYR A 1029 ? 0.2159 0.2557 0.1564 0.0406  0.0007  -0.0252 1027 TYR A CB  
7485  C CG  . TYR A 1029 ? 0.2150 0.2547 0.1561 0.0426  -0.0007 -0.0321 1027 TYR A CG  
7486  C CD1 . TYR A 1029 ? 0.2390 0.2695 0.1834 0.0417  -0.0028 -0.0360 1027 TYR A CD1 
7487  C CD2 . TYR A 1029 ? 0.2276 0.2764 0.1664 0.0453  0.0000  -0.0342 1027 TYR A CD2 
7488  C CE1 . TYR A 1029 ? 0.2315 0.2613 0.1775 0.0436  -0.0043 -0.0422 1027 TYR A CE1 
7489  C CE2 . TYR A 1029 ? 0.2420 0.2905 0.1821 0.0475  -0.0014 -0.0409 1027 TYR A CE2 
7490  C CZ  . TYR A 1029 ? 0.2460 0.2847 0.1899 0.0466  -0.0036 -0.0448 1027 TYR A CZ  
7491  O OH  . TYR A 1029 ? 0.2568 0.2949 0.2027 0.0487  -0.0053 -0.0512 1027 TYR A OH  
7492  N N   . LEU A 1030 ? 0.2176 0.2780 0.1521 0.0429  0.0004  -0.0219 1028 LEU A N   
7493  C CA  . LEU A 1030 ? 0.2287 0.3019 0.1595 0.0453  0.0000  -0.0231 1028 LEU A CA  
7494  C C   . LEU A 1030 ? 0.2447 0.3193 0.1750 0.0452  -0.0021 -0.0245 1028 LEU A C   
7495  O O   . LEU A 1030 ? 0.2364 0.3193 0.1643 0.0476  -0.0036 -0.0292 1028 LEU A O   
7496  C CB  . LEU A 1030 ? 0.2256 0.3074 0.1548 0.0452  0.0023  -0.0157 1028 LEU A CB  
7497  C CG  . LEU A 1030 ? 0.2233 0.3069 0.1526 0.0456  0.0044  -0.0139 1028 LEU A CG  
7498  C CD1 . LEU A 1030 ? 0.2540 0.3478 0.1819 0.0454  0.0062  -0.0064 1028 LEU A CD1 
7499  C CD2 . LEU A 1030 ? 0.2562 0.3449 0.1839 0.0486  0.0038  -0.0215 1028 LEU A CD2 
7500  N N   . GLY A 1031 ? 0.2343 0.3011 0.1669 0.0427  -0.0023 -0.0210 1029 GLY A N   
7501  C CA  . GLY A 1031 ? 0.2625 0.3307 0.1948 0.0425  -0.0042 -0.0217 1029 GLY A CA  
7502  C C   . GLY A 1031 ? 0.2570 0.3230 0.1899 0.0435  -0.0070 -0.0297 1029 GLY A C   
7503  O O   . GLY A 1031 ? 0.2523 0.3224 0.1842 0.0441  -0.0088 -0.0315 1029 GLY A O   
7504  N N   . ARG A 1032 ? 0.2381 0.2977 0.1730 0.0437  -0.0076 -0.0344 1030 ARG A N   
7505  C CA  . ARG A 1032 ? 0.2313 0.2884 0.1678 0.0447  -0.0106 -0.0422 1030 ARG A CA  
7506  C C   . ARG A 1032 ? 0.2475 0.3153 0.1812 0.0483  -0.0118 -0.0482 1030 ARG A C   
7507  O O   . ARG A 1032 ? 0.2570 0.3250 0.1918 0.0495  -0.0148 -0.0550 1030 ARG A O   
7508  C CB  . ARG A 1032 ? 0.2402 0.2864 0.1806 0.0435  -0.0110 -0.0444 1030 ARG A CB  
7509  C CG  . ARG A 1032 ? 0.2230 0.2640 0.1666 0.0437  -0.0145 -0.0513 1030 ARG A CG  
7510  C CD  . ARG A 1032 ? 0.2330 0.2689 0.1788 0.0413  -0.0160 -0.0497 1030 ARG A CD  
7511  N NE  . ARG A 1032 ? 0.2385 0.2679 0.1887 0.0408  -0.0192 -0.0552 1030 ARG A NE  
7512  C CZ  . ARG A 1032 ? 0.2723 0.3031 0.2238 0.0411  -0.0223 -0.0594 1030 ARG A CZ  
7513  N NH1 . ARG A 1032 ? 0.2878 0.3266 0.2361 0.0422  -0.0224 -0.0590 1030 ARG A NH1 
7514  N NH2 . ARG A 1032 ? 0.3045 0.3286 0.2609 0.0404  -0.0254 -0.0638 1030 ARG A NH2 
7515  N N   . LEU A 1033 ? 0.2272 0.3045 0.1576 0.0499  -0.0097 -0.0459 1031 LEU A N   
7516  C CA  . LEU A 1033 ? 0.2526 0.3412 0.1802 0.0535  -0.0104 -0.0517 1031 LEU A CA  
7517  C C   . LEU A 1033 ? 0.2652 0.3671 0.1886 0.0549  -0.0104 -0.0501 1031 LEU A C   
7518  O O   . LEU A 1033 ? 0.2598 0.3740 0.1800 0.0579  -0.0102 -0.0532 1031 LEU A O   
7519  C CB  . LEU A 1033 ? 0.2627 0.3541 0.1895 0.0546  -0.0080 -0.0506 1031 LEU A CB  
7520  C CG  . LEU A 1033 ? 0.2569 0.3352 0.1878 0.0529  -0.0076 -0.0506 1031 LEU A CG  
7521  C CD1 . LEU A 1033 ? 0.2466 0.3284 0.1769 0.0540  -0.0053 -0.0493 1031 LEU A CD1 
7522  C CD2 . LEU A 1033 ? 0.2582 0.3295 0.1928 0.0536  -0.0110 -0.0588 1031 LEU A CD2 
7523  N N   . VAL A 1034 ? 0.2670 0.3673 0.1905 0.0529  -0.0106 -0.0453 1032 VAL A N   
7524  C CA  . VAL A 1034 ? 0.2758 0.3879 0.1957 0.0539  -0.0109 -0.0432 1032 VAL A CA  
7525  C C   . VAL A 1034 ? 0.2712 0.3782 0.1929 0.0527  -0.0135 -0.0451 1032 VAL A C   
7526  O O   . VAL A 1034 ? 0.2781 0.3725 0.2037 0.0505  -0.0143 -0.0455 1032 VAL A O   
7527  C CB  . VAL A 1034 ? 0.2585 0.3753 0.1770 0.0524  -0.0082 -0.0330 1032 VAL A CB  
7528  C CG1 . VAL A 1034 ? 0.2758 0.4000 0.1925 0.0537  -0.0057 -0.0311 1032 VAL A CG1 
7529  C CG2 . VAL A 1034 ? 0.2659 0.3695 0.1882 0.0489  -0.0072 -0.0271 1032 VAL A CG2 
7530  N N   . THR A 1035 ? 0.2859 0.4035 0.2048 0.0541  -0.0149 -0.0462 1033 THR A N   
7531  C CA  . THR A 1035 ? 0.2832 0.3971 0.2037 0.0532  -0.0177 -0.0487 1033 THR A CA  
7532  C C   . THR A 1035 ? 0.3114 0.4184 0.2339 0.0501  -0.0168 -0.0409 1033 THR A C   
7533  O O   . THR A 1035 ? 0.3735 0.4718 0.2992 0.0484  -0.0185 -0.0423 1033 THR A O   
7534  C CB  . THR A 1035 ? 0.3315 0.4593 0.2483 0.0558  -0.0196 -0.0525 1033 THR A CB  
7535  O OG1 . THR A 1035 ? 0.4166 0.5565 0.3295 0.0563  -0.0174 -0.0456 1033 THR A OG1 
7536  C CG2 . THR A 1035 ? 0.3077 0.4411 0.2237 0.0591  -0.0212 -0.0623 1033 THR A CG2 
7537  N N   . THR A 1036 ? 0.2885 0.3994 0.2097 0.0492  -0.0142 -0.0325 1034 THR A N   
7538  C CA  . THR A 1036 ? 0.2801 0.3848 0.2037 0.0465  -0.0133 -0.0250 1034 THR A CA  
7539  C C   . THR A 1036 ? 0.2956 0.3941 0.2210 0.0450  -0.0106 -0.0197 1034 THR A C   
7540  O O   . THR A 1036 ? 0.3101 0.4160 0.2335 0.0458  -0.0087 -0.0160 1034 THR A O   
7541  C CB  . THR A 1036 ? 0.3573 0.4729 0.2787 0.0468  -0.0134 -0.0194 1034 THR A CB  
7542  O OG1 . THR A 1036 ? 0.3625 0.4845 0.2821 0.0483  -0.0161 -0.0248 1034 THR A OG1 
7543  C CG2 . THR A 1036 ? 0.3641 0.4728 0.2889 0.0441  -0.0128 -0.0121 1034 THR A CG2 
7544  N N   . ALA A 1037 ? 0.2876 0.3733 0.2168 0.0428  -0.0104 -0.0195 1035 ALA A N   
7545  C CA  . ALA A 1037 ? 0.2964 0.3756 0.2274 0.0415  -0.0080 -0.0156 1035 ALA A CA  
7546  C C   . ALA A 1037 ? 0.3079 0.3896 0.2397 0.0403  -0.0063 -0.0068 1035 ALA A C   
7547  O O   . ALA A 1037 ? 0.2810 0.3623 0.2142 0.0393  -0.0071 -0.0035 1035 ALA A O   
7548  C CB  . ALA A 1037 ? 0.2860 0.3518 0.2209 0.0395  -0.0083 -0.0177 1035 ALA A CB  
7549  N N   . PRO A 1038 ? 0.2665 0.3510 0.1979 0.0404  -0.0042 -0.0026 1036 PRO A N   
7550  C CA  . PRO A 1038 ? 0.2614 0.3464 0.1949 0.0389  -0.0029 0.0060  1036 PRO A CA  
7551  C C   . PRO A 1038 ? 0.2686 0.3408 0.2067 0.0366  -0.0024 0.0078  1036 PRO A C   
7552  O O   . PRO A 1038 ? 0.2716 0.3352 0.2108 0.0360  -0.0027 0.0030  1036 PRO A O   
7553  C CB  . PRO A 1038 ? 0.2772 0.3691 0.2090 0.0398  -0.0010 0.0088  1036 PRO A CB  
7554  C CG  . PRO A 1038 ? 0.2750 0.3623 0.2059 0.0406  -0.0007 0.0019  1036 PRO A CG  
7555  C CD  . PRO A 1038 ? 0.2503 0.3370 0.1799 0.0417  -0.0031 -0.0057 1036 PRO A CD  
7556  N N   . VAL A 1039 ? 0.2450 0.3165 0.1861 0.0353  -0.0018 0.0149  1037 VAL A N   
7557  C CA  . VAL A 1039 ? 0.2315 0.2921 0.1771 0.0333  -0.0011 0.0170  1037 VAL A CA  
7558  C C   . VAL A 1039 ? 0.2361 0.2947 0.1824 0.0329  0.0008  0.0187  1037 VAL A C   
7559  O O   . VAL A 1039 ? 0.2535 0.3184 0.2000 0.0330  0.0017  0.0242  1037 VAL A O   
7560  C CB  . VAL A 1039 ? 0.2496 0.3101 0.1991 0.0322  -0.0017 0.0234  1037 VAL A CB  
7561  C CG1 . VAL A 1039 ? 0.2709 0.3209 0.2253 0.0305  -0.0011 0.0249  1037 VAL A CG1 
7562  C CG2 . VAL A 1039 ? 0.2770 0.3393 0.2260 0.0326  -0.0036 0.0215  1037 VAL A CG2 
7563  N N   . PRO A 1040 ? 0.2317 0.2821 0.1786 0.0323  0.0014  0.0146  1038 PRO A N   
7564  C CA  . PRO A 1040 ? 0.2706 0.3193 0.2180 0.0320  0.0031  0.0160  1038 PRO A CA  
7565  C C   . PRO A 1040 ? 0.2634 0.3090 0.2152 0.0305  0.0039  0.0226  1038 PRO A C   
7566  O O   . PRO A 1040 ? 0.2337 0.2755 0.1888 0.0295  0.0031  0.0248  1038 PRO A O   
7567  C CB  . PRO A 1040 ? 0.2444 0.2842 0.1921 0.0316  0.0031  0.0102  1038 PRO A CB  
7568  C CG  . PRO A 1040 ? 0.2658 0.3052 0.2121 0.0321  0.0013  0.0050  1038 PRO A CG  
7569  C CD  . PRO A 1040 ? 0.2657 0.3090 0.2128 0.0320  0.0003  0.0085  1038 PRO A CD  
7570  N N   . PRO A 1041 ? 0.2356 0.2828 0.1881 0.0303  0.0053  0.0257  1039 PRO A N   
7571  C CA  . PRO A 1041 ? 0.1941 0.2371 0.1517 0.0287  0.0058  0.0313  1039 PRO A CA  
7572  C C   . PRO A 1041 ? 0.2423 0.2742 0.2030 0.0274  0.0056  0.0285  1039 PRO A C   
7573  O O   . PRO A 1041 ? 0.2448 0.2719 0.2038 0.0274  0.0058  0.0231  1039 PRO A O   
7574  C CB  . PRO A 1041 ? 0.2755 0.3215 0.2326 0.0288  0.0073  0.0333  1039 PRO A CB  
7575  C CG  . PRO A 1041 ? 0.2747 0.3303 0.2265 0.0307  0.0076  0.0308  1039 PRO A CG  
7576  C CD  . PRO A 1041 ? 0.2596 0.3126 0.2087 0.0316  0.0064  0.0240  1039 PRO A CD  
7577  N N   . GLN A 1042 ? 0.2136 0.2419 0.1792 0.0263  0.0050  0.0324  1040 GLN A N   
7578  C CA  . GLN A 1042 ? 0.2294 0.2485 0.1988 0.0251  0.0047  0.0305  1040 GLN A CA  
7579  C C   . GLN A 1042 ? 0.2292 0.2449 0.1968 0.0252  0.0040  0.0252  1040 GLN A C   
7580  O O   . GLN A 1042 ? 0.2229 0.2318 0.1929 0.0242  0.0040  0.0229  1040 GLN A O   
7581  C CB  . GLN A 1042 ? 0.2696 0.2835 0.2400 0.0243  0.0060  0.0294  1040 GLN A CB  
7582  C CG  . GLN A 1042 ? 0.3353 0.3525 0.3076 0.0240  0.0067  0.0347  1040 GLN A CG  
7583  C CD  . GLN A 1042 ? 0.3819 0.3934 0.3561 0.0231  0.0078  0.0337  1040 GLN A CD  
7584  O OE1 . GLN A 1042 ? 0.4112 0.4239 0.3823 0.0235  0.0089  0.0319  1040 GLN A OE1 
7585  N NE2 . GLN A 1042 ? 0.4104 0.4160 0.3897 0.0220  0.0073  0.0348  1040 GLN A NE2 
7586  N N   . HIS A 1043 ? 0.2008 0.2216 0.1648 0.0262  0.0032  0.0231  1041 HIS A N   
7587  C CA  . HIS A 1043 ? 0.2374 0.2553 0.1997 0.0262  0.0023  0.0178  1041 HIS A CA  
7588  C C   . HIS A 1043 ? 0.2311 0.2485 0.1962 0.0259  0.0010  0.0191  1041 HIS A C   
7589  O O   . HIS A 1043 ? 0.2266 0.2499 0.1906 0.0268  0.0000  0.0205  1041 HIS A O   
7590  C CB  . HIS A 1043 ? 0.2182 0.2417 0.1757 0.0276  0.0019  0.0144  1041 HIS A CB  
7591  C CG  . HIS A 1043 ? 0.2309 0.2516 0.1873 0.0275  0.0007  0.0090  1041 HIS A CG  
7592  N ND1 . HIS A 1043 ? 0.2246 0.2398 0.1805 0.0270  0.0008  0.0046  1041 HIS A ND1 
7593  C CD2 . HIS A 1043 ? 0.2239 0.2465 0.1798 0.0278  -0.0009 0.0075  1041 HIS A CD2 
7594  C CE1 . HIS A 1043 ? 0.2453 0.2593 0.2010 0.0268  -0.0007 0.0009  1041 HIS A CE1 
7595  N NE2 . HIS A 1043 ? 0.2295 0.2479 0.1850 0.0273  -0.0017 0.0024  1041 HIS A NE2 
7596  N N   . SER A 1044 ? 0.2034 0.2142 0.1723 0.0248  0.0011  0.0186  1042 SER A N   
7597  C CA  . SER A 1044 ? 0.2059 0.2157 0.1781 0.0246  -0.0001 0.0191  1042 SER A CA  
7598  C C   . SER A 1044 ? 0.2041 0.2069 0.1793 0.0235  0.0003  0.0168  1042 SER A C   
7599  O O   . SER A 1044 ? 0.2354 0.2346 0.2108 0.0229  0.0015  0.0159  1042 SER A O   
7600  C CB  . SER A 1044 ? 0.2298 0.2426 0.2056 0.0249  -0.0008 0.0248  1042 SER A CB  
7601  O OG  . SER A 1044 ? 0.2266 0.2358 0.2065 0.0243  -0.0001 0.0275  1042 SER A OG  
7602  N N   . SER A 1045 ? 0.1978 0.1994 0.1756 0.0233  -0.0006 0.0158  1043 SER A N   
7603  C CA  . SER A 1045 ? 0.2168 0.2134 0.1979 0.0224  -0.0002 0.0138  1043 SER A CA  
7604  C C   . SER A 1045 ? 0.1928 0.1899 0.1783 0.0227  -0.0013 0.0149  1043 SER A C   
7605  O O   . SER A 1045 ? 0.2159 0.2163 0.2006 0.0232  -0.0025 0.0151  1043 SER A O   
7606  C CB  . SER A 1045 ? 0.2311 0.2256 0.2096 0.0215  0.0000  0.0093  1043 SER A CB  
7607  O OG  . SER A 1045 ? 0.2297 0.2207 0.2113 0.0206  0.0004  0.0076  1043 SER A OG  
7608  N N   . VAL A 1046 ? 0.2201 0.2140 0.2106 0.0226  -0.0012 0.0154  1044 VAL A N   
7609  C CA  . VAL A 1046 ? 0.2465 0.2407 0.2418 0.0231  -0.0024 0.0158  1044 VAL A CA  
7610  C C   . VAL A 1046 ? 0.2245 0.2178 0.2198 0.0225  -0.0023 0.0116  1044 VAL A C   
7611  O O   . VAL A 1046 ? 0.2157 0.2098 0.2149 0.0231  -0.0032 0.0113  1044 VAL A O   
7612  C CB  . VAL A 1046 ? 0.2350 0.2266 0.2367 0.0234  -0.0027 0.0177  1044 VAL A CB  
7613  C CG1 . VAL A 1046 ? 0.2750 0.2679 0.2776 0.0237  -0.0030 0.0227  1044 VAL A CG1 
7614  C CG2 . VAL A 1046 ? 0.2227 0.2103 0.2251 0.0227  -0.0014 0.0145  1044 VAL A CG2 
7615  N N   . HIS A 1047 ? 0.2148 0.2069 0.2062 0.0215  -0.0013 0.0086  1045 HIS A N   
7616  C CA  . HIS A 1047 ? 0.2557 0.2475 0.2475 0.0206  -0.0012 0.0052  1045 HIS A CA  
7617  C C   . HIS A 1047 ? 0.2426 0.2371 0.2318 0.0204  -0.0022 0.0042  1045 HIS A C   
7618  O O   . HIS A 1047 ? 0.2496 0.2455 0.2350 0.0206  -0.0025 0.0047  1045 HIS A O   
7619  C CB  . HIS A 1047 ? 0.2533 0.2424 0.2432 0.0194  0.0001  0.0031  1045 HIS A CB  
7620  C CG  . HIS A 1047 ? 0.2945 0.2811 0.2869 0.0196  0.0010  0.0038  1045 HIS A CG  
7621  N ND1 . HIS A 1047 ? 0.3310 0.3171 0.3284 0.0200  0.0009  0.0030  1045 HIS A ND1 
7622  C CD2 . HIS A 1047 ? 0.3198 0.3045 0.3109 0.0195  0.0018  0.0052  1045 HIS A CD2 
7623  C CE1 . HIS A 1047 ? 0.3194 0.3031 0.3185 0.0202  0.0015  0.0037  1045 HIS A CE1 
7624  N NE2 . HIS A 1047 ? 0.3171 0.2999 0.3124 0.0198  0.0020  0.0052  1045 HIS A NE2 
7625  N N   . THR A 1048 ? 0.2233 0.2192 0.2149 0.0202  -0.0028 0.0027  1046 THR A N   
7626  C CA  . THR A 1048 ? 0.2533 0.2518 0.2433 0.0199  -0.0039 0.0017  1046 THR A CA  
7627  C C   . THR A 1048 ? 0.2519 0.2499 0.2417 0.0182  -0.0036 -0.0012 1046 THR A C   
7628  O O   . THR A 1048 ? 0.2390 0.2369 0.2317 0.0178  -0.0028 -0.0022 1046 THR A O   
7629  C CB  . THR A 1048 ? 0.2200 0.2215 0.2134 0.0209  -0.0052 0.0028  1046 THR A CB  
7630  O OG1 . THR A 1048 ? 0.2541 0.2560 0.2487 0.0223  -0.0056 0.0062  1046 THR A OG1 
7631  C CG2 . THR A 1048 ? 0.2241 0.2285 0.2153 0.0206  -0.0065 0.0020  1046 THR A CG2 
7632  N N   . ASP A 1049 ? 0.2330 0.2312 0.2197 0.0173  -0.0043 -0.0024 1047 ASP A N   
7633  C CA  . ASP A 1049 ? 0.2073 0.2052 0.1943 0.0154  -0.0042 -0.0044 1047 ASP A CA  
7634  C C   . ASP A 1049 ? 0.2240 0.2249 0.2143 0.0151  -0.0048 -0.0049 1047 ASP A C   
7635  O O   . ASP A 1049 ? 0.2061 0.2095 0.1971 0.0159  -0.0060 -0.0044 1047 ASP A O   
7636  C CB  . ASP A 1049 ? 0.1998 0.1971 0.1838 0.0146  -0.0055 -0.0056 1047 ASP A CB  
7637  C CG  . ASP A 1049 ? 0.2098 0.2066 0.1950 0.0124  -0.0058 -0.0070 1047 ASP A CG  
7638  O OD1 . ASP A 1049 ? 0.2083 0.2077 0.1956 0.0116  -0.0067 -0.0075 1047 ASP A OD1 
7639  O OD2 . ASP A 1049 ? 0.2382 0.2324 0.2224 0.0114  -0.0051 -0.0073 1047 ASP A OD2 
7640  N N   . PRO A 1050 ? 0.2026 0.2042 0.1952 0.0140  -0.0039 -0.0058 1048 PRO A N   
7641  C CA  . PRO A 1050 ? 0.2097 0.2151 0.2059 0.0139  -0.0042 -0.0063 1048 PRO A CA  
7642  C C   . PRO A 1050 ? 0.2267 0.2344 0.2229 0.0125  -0.0056 -0.0069 1048 PRO A C   
7643  O O   . PRO A 1050 ? 0.2156 0.2267 0.2143 0.0128  -0.0064 -0.0070 1048 PRO A O   
7644  C CB  . PRO A 1050 ? 0.2289 0.2350 0.2271 0.0132  -0.0026 -0.0072 1048 PRO A CB  
7645  C CG  . PRO A 1050 ? 0.2319 0.2348 0.2270 0.0118  -0.0019 -0.0072 1048 PRO A CG  
7646  C CD  . PRO A 1050 ? 0.2307 0.2303 0.2229 0.0129  -0.0024 -0.0062 1048 PRO A CD  
7647  N N   . VAL A 1051 ? 0.2070 0.2129 0.2011 0.0108  -0.0062 -0.0073 1049 VAL A N   
7648  C CA  . VAL A 1051 ? 0.2250 0.2326 0.2196 0.0094  -0.0080 -0.0078 1049 VAL A CA  
7649  C C   . VAL A 1051 ? 0.2200 0.2281 0.2132 0.0108  -0.0097 -0.0080 1049 VAL A C   
7650  O O   . VAL A 1051 ? 0.2116 0.2226 0.2065 0.0105  -0.0111 -0.0083 1049 VAL A O   
7651  C CB  . VAL A 1051 ? 0.2165 0.2216 0.2101 0.0073  -0.0086 -0.0082 1049 VAL A CB  
7652  C CG1 . VAL A 1051 ? 0.2497 0.2564 0.2450 0.0056  -0.0108 -0.0088 1049 VAL A CG1 
7653  C CG2 . VAL A 1051 ? 0.2327 0.2382 0.2276 0.0058  -0.0069 -0.0076 1049 VAL A CG2 
7654  N N   . LEU A 1052 ? 0.2061 0.2121 0.1964 0.0124  -0.0095 -0.0076 1050 LEU A N   
7655  C CA  . LEU A 1052 ? 0.2136 0.2215 0.2025 0.0140  -0.0108 -0.0073 1050 LEU A CA  
7656  C C   . LEU A 1052 ? 0.2173 0.2284 0.2090 0.0151  -0.0110 -0.0061 1050 LEU A C   
7657  O O   . LEU A 1052 ? 0.2035 0.2175 0.1958 0.0154  -0.0126 -0.0063 1050 LEU A O   
7658  C CB  . LEU A 1052 ? 0.2145 0.2207 0.2000 0.0156  -0.0102 -0.0065 1050 LEU A CB  
7659  C CG  . LEU A 1052 ? 0.2023 0.2114 0.1860 0.0175  -0.0113 -0.0054 1050 LEU A CG  
7660  C CD1 . LEU A 1052 ? 0.2150 0.2262 0.2013 0.0189  -0.0109 -0.0028 1050 LEU A CD1 
7661  C CD2 . LEU A 1052 ? 0.1921 0.2037 0.1749 0.0172  -0.0136 -0.0074 1050 LEU A CD2 
7662  N N   . LEU A 1053 ? 0.2084 0.2191 0.2024 0.0159  -0.0094 -0.0051 1051 LEU A N   
7663  C CA  . LEU A 1053 ? 0.2250 0.2386 0.2226 0.0171  -0.0097 -0.0042 1051 LEU A CA  
7664  C C   . LEU A 1053 ? 0.2127 0.2296 0.2130 0.0159  -0.0105 -0.0054 1051 LEU A C   
7665  O O   . LEU A 1053 ? 0.2133 0.2332 0.2153 0.0168  -0.0117 -0.0050 1051 LEU A O   
7666  C CB  . LEU A 1053 ? 0.2178 0.2301 0.2182 0.0181  -0.0081 -0.0037 1051 LEU A CB  
7667  C CG  . LEU A 1053 ? 0.2478 0.2574 0.2468 0.0195  -0.0077 -0.0017 1051 LEU A CG  
7668  C CD1 . LEU A 1053 ? 0.2320 0.2399 0.2343 0.0202  -0.0064 -0.0017 1051 LEU A CD1 
7669  C CD2 . LEU A 1053 ? 0.2458 0.2575 0.2452 0.0210  -0.0091 0.0005  1051 LEU A CD2 
7670  N N   . ASP A 1054 ? 0.2107 0.2275 0.2115 0.0139  -0.0098 -0.0066 1052 ASP A N   
7671  C CA  . ASP A 1054 ? 0.2078 0.2285 0.2113 0.0125  -0.0106 -0.0073 1052 ASP A CA  
7672  C C   . ASP A 1054 ? 0.2182 0.2399 0.2207 0.0119  -0.0129 -0.0076 1052 ASP A C   
7673  O O   . ASP A 1054 ? 0.2374 0.2628 0.2424 0.0118  -0.0140 -0.0077 1052 ASP A O   
7674  C CB  . ASP A 1054 ? 0.2344 0.2553 0.2386 0.0101  -0.0096 -0.0079 1052 ASP A CB  
7675  C CG  . ASP A 1054 ? 0.2914 0.3133 0.2975 0.0107  -0.0075 -0.0082 1052 ASP A CG  
7676  O OD1 . ASP A 1054 ? 0.2495 0.2721 0.2574 0.0129  -0.0070 -0.0082 1052 ASP A OD1 
7677  O OD2 . ASP A 1054 ? 0.3084 0.3305 0.3143 0.0089  -0.0065 -0.0083 1052 ASP A OD2 
7678  N N   . PHE A 1055 ? 0.2062 0.2249 0.2052 0.0116  -0.0137 -0.0081 1053 PHE A N   
7679  C CA  . PHE A 1055 ? 0.2388 0.2585 0.2368 0.0112  -0.0161 -0.0090 1053 PHE A CA  
7680  C C   . PHE A 1055 ? 0.2121 0.2346 0.2097 0.0133  -0.0171 -0.0083 1053 PHE A C   
7681  O O   . PHE A 1055 ? 0.2212 0.2468 0.2201 0.0131  -0.0190 -0.0088 1053 PHE A O   
7682  C CB  . PHE A 1055 ? 0.2179 0.2339 0.2124 0.0108  -0.0167 -0.0102 1053 PHE A CB  
7683  C CG  . PHE A 1055 ? 0.2333 0.2503 0.2268 0.0107  -0.0194 -0.0120 1053 PHE A CG  
7684  C CD1 . PHE A 1055 ? 0.2638 0.2825 0.2603 0.0089  -0.0213 -0.0130 1053 PHE A CD1 
7685  C CD2 . PHE A 1055 ? 0.2259 0.2427 0.2157 0.0125  -0.0201 -0.0129 1053 PHE A CD2 
7686  C CE1 . PHE A 1055 ? 0.2654 0.2849 0.2614 0.0088  -0.0242 -0.0151 1053 PHE A CE1 
7687  C CE2 . PHE A 1055 ? 0.2368 0.2551 0.2257 0.0127  -0.0227 -0.0152 1053 PHE A CE2 
7688  C CZ  . PHE A 1055 ? 0.2445 0.2638 0.2366 0.0108  -0.0248 -0.0165 1053 PHE A CZ  
7689  N N   . ALA A 1056 ? 0.2232 0.2448 0.2193 0.0154  -0.0160 -0.0068 1054 ALA A N   
7690  C CA  . ALA A 1056 ? 0.2127 0.2374 0.2089 0.0173  -0.0171 -0.0053 1054 ALA A CA  
7691  C C   . ALA A 1056 ? 0.2516 0.2797 0.2524 0.0175  -0.0175 -0.0048 1054 ALA A C   
7692  O O   . ALA A 1056 ? 0.2503 0.2818 0.2517 0.0181  -0.0192 -0.0045 1054 ALA A O   
7693  C CB  . ALA A 1056 ? 0.2368 0.2600 0.2318 0.0191  -0.0158 -0.0031 1054 ALA A CB  
7694  N N   . LYS A 1057 ? 0.2425 0.2702 0.2465 0.0171  -0.0159 -0.0049 1055 LYS A N   
7695  C CA  . LYS A 1057 ? 0.2703 0.3019 0.2790 0.0173  -0.0163 -0.0050 1055 LYS A CA  
7696  C C   . LYS A 1057 ? 0.2608 0.2953 0.2703 0.0154  -0.0178 -0.0062 1055 LYS A C   
7697  O O   . LYS A 1057 ? 0.3074 0.3458 0.3195 0.0159  -0.0191 -0.0060 1055 LYS A O   
7698  C CB  . LYS A 1057 ? 0.2755 0.3069 0.2873 0.0173  -0.0143 -0.0055 1055 LYS A CB  
7699  C CG  . LYS A 1057 ? 0.2705 0.3002 0.2839 0.0195  -0.0134 -0.0043 1055 LYS A CG  
7700  C CD  . LYS A 1057 ? 0.2796 0.3104 0.2971 0.0199  -0.0119 -0.0057 1055 LYS A CD  
7701  C CE  . LYS A 1057 ? 0.2844 0.3144 0.3002 0.0178  -0.0103 -0.0072 1055 LYS A CE  
7702  N NZ  . LYS A 1057 ? 0.3329 0.3625 0.3511 0.0187  -0.0086 -0.0083 1055 LYS A NZ  
7703  N N   . TRP A 1058 ? 0.2441 0.2768 0.2522 0.0132  -0.0177 -0.0074 1056 TRP A N   
7704  C CA  . TRP A 1058 ? 0.3008 0.3357 0.3102 0.0111  -0.0195 -0.0083 1056 TRP A CA  
7705  C C   . TRP A 1058 ? 0.2842 0.3204 0.2920 0.0119  -0.0220 -0.0088 1056 TRP A C   
7706  O O   . TRP A 1058 ? 0.3164 0.3563 0.3267 0.0113  -0.0237 -0.0090 1056 TRP A O   
7707  C CB  . TRP A 1058 ? 0.2781 0.3101 0.2865 0.0087  -0.0194 -0.0091 1056 TRP A CB  
7708  C CG  . TRP A 1058 ? 0.3049 0.3386 0.3153 0.0063  -0.0218 -0.0099 1056 TRP A CG  
7709  C CD1 . TRP A 1058 ? 0.3486 0.3860 0.3632 0.0042  -0.0219 -0.0094 1056 TRP A CD1 
7710  C CD2 . TRP A 1058 ? 0.3248 0.3570 0.3337 0.0058  -0.0244 -0.0114 1056 TRP A CD2 
7711  N NE1 . TRP A 1058 ? 0.3610 0.3987 0.3771 0.0022  -0.0246 -0.0101 1056 TRP A NE1 
7712  C CE2 . TRP A 1058 ? 0.3502 0.3846 0.3629 0.0033  -0.0263 -0.0117 1056 TRP A CE2 
7713  C CE3 . TRP A 1058 ? 0.2952 0.3250 0.3001 0.0073  -0.0254 -0.0128 1056 TRP A CE3 
7714  C CZ2 . TRP A 1058 ? 0.3289 0.3624 0.3419 0.0022  -0.0294 -0.0135 1056 TRP A CZ2 
7715  C CZ3 . TRP A 1058 ? 0.3233 0.3529 0.3281 0.0065  -0.0283 -0.0149 1056 TRP A CZ3 
7716  C CH2 . TRP A 1058 ? 0.3323 0.3633 0.3413 0.0040  -0.0304 -0.0154 1056 TRP A CH2 
7717  N N   . LEU A 1059 ? 0.2579 0.2918 0.2616 0.0132  -0.0223 -0.0088 1057 LEU A N   
7718  C CA  . LEU A 1059 ? 0.3081 0.3444 0.3099 0.0142  -0.0247 -0.0094 1057 LEU A CA  
7719  C C   . LEU A 1059 ? 0.3015 0.3421 0.3054 0.0158  -0.0253 -0.0077 1057 LEU A C   
7720  O O   . LEU A 1059 ? 0.3230 0.3671 0.3277 0.0157  -0.0274 -0.0083 1057 LEU A O   
7721  C CB  . LEU A 1059 ? 0.2668 0.3010 0.2637 0.0156  -0.0245 -0.0095 1057 LEU A CB  
7722  C CG  . LEU A 1059 ? 0.2616 0.2921 0.2562 0.0143  -0.0248 -0.0119 1057 LEU A CG  
7723  C CD1 . LEU A 1059 ? 0.2398 0.2687 0.2301 0.0159  -0.0238 -0.0116 1057 LEU A CD1 
7724  C CD2 . LEU A 1059 ? 0.2903 0.3224 0.2851 0.0133  -0.0278 -0.0146 1057 LEU A CD2 
7725  N N   . ASP A 1060 ? 0.2862 0.3265 0.2915 0.0174  -0.0236 -0.0056 1058 ASP A N   
7726  C CA  . ASP A 1060 ? 0.3298 0.3739 0.3382 0.0190  -0.0243 -0.0038 1058 ASP A CA  
7727  C C   . ASP A 1060 ? 0.3269 0.3743 0.3397 0.0179  -0.0250 -0.0047 1058 ASP A C   
7728  O O   . ASP A 1060 ? 0.3545 0.4059 0.3692 0.0186  -0.0267 -0.0041 1058 ASP A O   
7729  C CB  . ASP A 1060 ? 0.3558 0.3984 0.3659 0.0208  -0.0227 -0.0017 1058 ASP A CB  
7730  C CG  . ASP A 1060 ? 0.3127 0.3550 0.3200 0.0225  -0.0231 0.0008  1058 ASP A CG  
7731  O OD1 . ASP A 1060 ? 0.3682 0.4138 0.3731 0.0230  -0.0249 0.0013  1058 ASP A OD1 
7732  O OD2 . ASP A 1060 ? 0.3915 0.4311 0.3992 0.0234  -0.0216 0.0023  1058 ASP A OD2 
7733  N N   . GLY A 1061 ? 0.3381 0.3846 0.3527 0.0161  -0.0237 -0.0059 1059 GLY A N   
7734  C CA  . GLY A 1061 ? 0.3086 0.3591 0.3274 0.0148  -0.0243 -0.0066 1059 GLY A CA  
7735  C C   . GLY A 1061 ? 0.3627 0.4151 0.3812 0.0131  -0.0268 -0.0077 1059 GLY A C   
7736  O O   . GLY A 1061 ? 0.3556 0.4125 0.3776 0.0127  -0.0281 -0.0077 1059 GLY A O   
7737  N N   . LYS A 1062 ? 0.3103 0.3596 0.3250 0.0122  -0.0278 -0.0088 1060 LYS A N   
7738  C CA  . LYS A 1062 ? 0.3542 0.4050 0.3689 0.0108  -0.0307 -0.0105 1060 LYS A CA  
7739  C C   . LYS A 1062 ? 0.3674 0.4211 0.3803 0.0127  -0.0327 -0.0105 1060 LYS A C   
7740  O O   . LYS A 1062 ? 0.4038 0.4593 0.4168 0.0118  -0.0354 -0.0122 1060 LYS A O   
7741  C CB  . LYS A 1062 ? 0.3776 0.4240 0.3898 0.0092  -0.0312 -0.0123 1060 LYS A CB  
7742  C CG  . LYS A 1062 ? 0.3737 0.4182 0.3885 0.0065  -0.0300 -0.0121 1060 LYS A CG  
7743  C CD  . LYS A 1062 ? 0.4273 0.4754 0.4470 0.0041  -0.0316 -0.0120 1060 LYS A CD  
7744  C CE  . LYS A 1062 ? 0.4483 0.4957 0.4708 0.0014  -0.0304 -0.0110 1060 LYS A CE  
7745  N NZ  . LYS A 1062 ? 0.4768 0.5282 0.5044 -0.0014 -0.0321 -0.0105 1060 LYS A NZ  
7746  N N   . GLY A 1063 ? 0.3445 0.3988 0.3559 0.0152  -0.0318 -0.0086 1061 GLY A N   
7747  C CA  . GLY A 1063 ? 0.3593 0.4171 0.3688 0.0169  -0.0337 -0.0080 1061 GLY A CA  
7748  C C   . GLY A 1063 ? 0.3920 0.4486 0.3959 0.0179  -0.0342 -0.0087 1061 GLY A C   
7749  O O   . GLY A 1063 ? 0.3561 0.4166 0.3579 0.0195  -0.0357 -0.0079 1061 GLY A O   
7750  N N   . ALA A 1064 ? 0.3598 0.4117 0.3614 0.0171  -0.0329 -0.0100 1062 ALA A N   
7751  C CA  . ALA A 1064 ? 0.3328 0.3838 0.3293 0.0181  -0.0331 -0.0111 1062 ALA A CA  
7752  C C   . ALA A 1064 ? 0.3438 0.3945 0.3384 0.0201  -0.0311 -0.0078 1062 ALA A C   
7753  O O   . ALA A 1064 ? 0.2975 0.3442 0.2904 0.0201  -0.0292 -0.0075 1062 ALA A O   
7754  C CB  . ALA A 1064 ? 0.3196 0.3658 0.3151 0.0164  -0.0328 -0.0138 1062 ALA A CB  
7755  N N   . ARG A 1065 ? 0.3071 0.3622 0.3023 0.0217  -0.0319 -0.0052 1063 ARG A N   
7756  C CA  . ARG A 1065 ? 0.2766 0.3316 0.2718 0.0234  -0.0303 -0.0013 1063 ARG A CA  
7757  C C   . ARG A 1065 ? 0.3027 0.3574 0.2928 0.0243  -0.0297 -0.0009 1063 ARG A C   
7758  O O   . ARG A 1065 ? 0.3221 0.3735 0.3120 0.0247  -0.0276 0.0010  1063 ARG A O   
7759  C CB  . ARG A 1065 ? 0.3479 0.4081 0.3454 0.0248  -0.0318 0.0018  1063 ARG A CB  
7760  N N   . ALA A 1066 ? 0.2974 0.3560 0.2835 0.0247  -0.0314 -0.0028 1064 ALA A N   
7761  C CA  . ALA A 1066 ? 0.2593 0.3189 0.2405 0.0258  -0.0308 -0.0027 1064 ALA A CA  
7762  C C   . ALA A 1066 ? 0.2673 0.3207 0.2473 0.0248  -0.0291 -0.0051 1064 ALA A C   
7763  O O   . ALA A 1066 ? 0.2643 0.3164 0.2421 0.0255  -0.0274 -0.0034 1064 ALA A O   
7764  C CB  . ALA A 1066 ? 0.3167 0.3825 0.2940 0.0266  -0.0332 -0.0052 1064 ALA A CB  
7765  N N   . GLU A 1067 ? 0.2863 0.3362 0.2680 0.0230  -0.0296 -0.0087 1065 GLU A N   
7766  C CA  . GLU A 1067 ? 0.2675 0.3116 0.2484 0.0219  -0.0283 -0.0107 1065 GLU A CA  
7767  C C   . GLU A 1067 ? 0.2865 0.3262 0.2697 0.0215  -0.0256 -0.0079 1065 GLU A C   
7768  O O   . GLU A 1067 ? 0.2526 0.2887 0.2341 0.0214  -0.0239 -0.0079 1065 GLU A O   
7769  C CB  . GLU A 1067 ? 0.2942 0.3360 0.2771 0.0200  -0.0299 -0.0147 1065 GLU A CB  
7770  C CG  . GLU A 1067 ? 0.2703 0.3151 0.2509 0.0204  -0.0327 -0.0188 1065 GLU A CG  
7771  C CD  . GLU A 1067 ? 0.3239 0.3748 0.3051 0.0210  -0.0350 -0.0189 1065 GLU A CD  
7772  O OE1 . GLU A 1067 ? 0.2660 0.3184 0.2499 0.0209  -0.0346 -0.0157 1065 GLU A OE1 
7773  O OE2 . GLU A 1067 ? 0.3684 0.4227 0.3476 0.0217  -0.0375 -0.0223 1065 GLU A OE2 
7774  N N   . ALA A 1068 ? 0.2878 0.3280 0.2751 0.0213  -0.0252 -0.0058 1066 ALA A N   
7775  C CA  . ALA A 1068 ? 0.2724 0.3092 0.2623 0.0213  -0.0229 -0.0036 1066 ALA A CA  
7776  C C   . ALA A 1068 ? 0.2664 0.3033 0.2546 0.0229  -0.0218 -0.0004 1066 ALA A C   
7777  O O   . ALA A 1068 ? 0.2307 0.2637 0.2190 0.0228  -0.0198 0.0003  1066 ALA A O   
7778  C CB  . ALA A 1068 ? 0.2939 0.3323 0.2888 0.0212  -0.0232 -0.0024 1066 ALA A CB  
7779  N N   . GLU A 1069 ? 0.2669 0.3086 0.2537 0.0244  -0.0230 0.0018  1067 GLU A N   
7780  C CA  . GLU A 1069 ? 0.2676 0.3105 0.2528 0.0257  -0.0222 0.0053  1067 GLU A CA  
7781  C C   . GLU A 1069 ? 0.2933 0.3347 0.2739 0.0257  -0.0212 0.0037  1067 GLU A C   
7782  O O   . GLU A 1069 ? 0.2540 0.2930 0.2344 0.0260  -0.0195 0.0058  1067 GLU A O   
7783  C CB  . GLU A 1069 ? 0.2864 0.3361 0.2709 0.0271  -0.0240 0.0082  1067 GLU A CB  
7784  C CG  . GLU A 1069 ? 0.3371 0.3894 0.3194 0.0284  -0.0234 0.0123  1067 GLU A CG  
7785  C CD  . GLU A 1069 ? 0.4337 0.4832 0.4207 0.0287  -0.0223 0.0167  1067 GLU A CD  
7786  O OE1 . GLU A 1069 ? 0.4888 0.5346 0.4807 0.0283  -0.0220 0.0161  1067 GLU A OE1 
7787  O OE2 . GLU A 1069 ? 0.5116 0.5631 0.4980 0.0295  -0.0219 0.0208  1067 GLU A OE2 
7788  N N   . ALA A 1070 ? 0.2675 0.3105 0.2448 0.0254  -0.0224 -0.0001 1068 ALA A N   
7789  C CA  . ALA A 1070 ? 0.2193 0.2609 0.1926 0.0255  -0.0216 -0.0021 1068 ALA A CA  
7790  C C   . ALA A 1070 ? 0.2021 0.2367 0.1769 0.0241  -0.0198 -0.0033 1068 ALA A C   
7791  O O   . ALA A 1070 ? 0.2354 0.2680 0.2081 0.0244  -0.0183 -0.0029 1068 ALA A O   
7792  C CB  . ALA A 1070 ? 0.2638 0.3081 0.2343 0.0255  -0.0237 -0.0068 1068 ALA A CB  
7793  N N   . ALA A 1071 ? 0.2232 0.2545 0.2014 0.0227  -0.0198 -0.0045 1069 ALA A N   
7794  C CA  . ALA A 1071 ? 0.2231 0.2487 0.2029 0.0213  -0.0181 -0.0052 1069 ALA A CA  
7795  C C   . ALA A 1071 ? 0.2489 0.2726 0.2300 0.0220  -0.0160 -0.0018 1069 ALA A C   
7796  O O   . ALA A 1071 ? 0.2209 0.2411 0.2009 0.0217  -0.0144 -0.0018 1069 ALA A O   
7797  C CB  . ALA A 1071 ? 0.2281 0.2523 0.2116 0.0196  -0.0186 -0.0066 1069 ALA A CB  
7798  N N   . ARG A 1072 ? 0.2482 0.2741 0.2322 0.0229  -0.0162 0.0012  1070 ARG A N   
7799  C CA  . ARG A 1072 ? 0.2371 0.2611 0.2232 0.0236  -0.0147 0.0044  1070 ARG A CA  
7800  C C   . ARG A 1072 ? 0.2318 0.2567 0.2145 0.0245  -0.0141 0.0065  1070 ARG A C   
7801  O O   . ARG A 1072 ? 0.2468 0.2684 0.2299 0.0244  -0.0125 0.0075  1070 ARG A O   
7802  C CB  . ARG A 1072 ? 0.2614 0.2878 0.2520 0.0246  -0.0156 0.0072  1070 ARG A CB  
7803  C CG  . ARG A 1072 ? 0.2977 0.3228 0.2927 0.0238  -0.0155 0.0054  1070 ARG A CG  
7804  C CD  . ARG A 1072 ? 0.3167 0.3439 0.3168 0.0251  -0.0164 0.0079  1070 ARG A CD  
7805  N NE  . ARG A 1072 ? 0.3265 0.3588 0.3257 0.0259  -0.0184 0.0095  1070 ARG A NE  
7806  C CZ  . ARG A 1072 ? 0.3351 0.3702 0.3350 0.0255  -0.0198 0.0079  1070 ARG A CZ  
7807  N NH1 . ARG A 1072 ? 0.3200 0.3539 0.3218 0.0243  -0.0194 0.0049  1070 ARG A NH1 
7808  N NH2 . ARG A 1072 ? 0.3209 0.3609 0.3199 0.0264  -0.0216 0.0096  1070 ARG A NH2 
7809  N N   . ASN A 1073 ? 0.2256 0.2556 0.2050 0.0254  -0.0154 0.0069  1071 ASN A N   
7810  C CA  . ASN A 1073 ? 0.2493 0.2815 0.2252 0.0263  -0.0147 0.0088  1071 ASN A CA  
7811  C C   . ASN A 1073 ? 0.2455 0.2739 0.2185 0.0256  -0.0135 0.0057  1071 ASN A C   
7812  O O   . ASN A 1073 ? 0.2598 0.2872 0.2320 0.0259  -0.0121 0.0076  1071 ASN A O   
7813  C CB  . ASN A 1073 ? 0.2551 0.2948 0.2277 0.0274  -0.0164 0.0092  1071 ASN A CB  
7814  C CG  . ASN A 1073 ? 0.3195 0.3635 0.2948 0.0282  -0.0176 0.0136  1071 ASN A CG  
7815  O OD1 . ASN A 1073 ? 0.3381 0.3796 0.3179 0.0282  -0.0171 0.0170  1071 ASN A OD1 
7816  N ND2 . ASN A 1073 ? 0.3311 0.3817 0.3041 0.0290  -0.0194 0.0134  1071 ASN A ND2 
7817  N N   . ALA A 1074 ? 0.2351 0.2615 0.2072 0.0247  -0.0141 0.0012  1072 ALA A N   
7818  C CA  . ALA A 1074 ? 0.2188 0.2413 0.1890 0.0240  -0.0132 -0.0016 1072 ALA A CA  
7819  C C   . ALA A 1074 ? 0.2279 0.2449 0.2008 0.0231  -0.0112 -0.0003 1072 ALA A C   
7820  O O   . ALA A 1074 ? 0.2225 0.2373 0.1938 0.0231  -0.0099 -0.0002 1072 ALA A O   
7821  C CB  . ALA A 1074 ? 0.2452 0.2664 0.2153 0.0229  -0.0147 -0.0061 1072 ALA A CB  
7822  N N   . GLY A 1075 ? 0.2135 0.2287 0.1903 0.0223  -0.0111 0.0005  1073 GLY A N   
7823  C CA  . GLY A 1075 ? 0.2102 0.2212 0.1897 0.0217  -0.0093 0.0014  1073 GLY A CA  
7824  C C   . GLY A 1075 ? 0.2417 0.2523 0.2214 0.0227  -0.0082 0.0047  1073 GLY A C   
7825  O O   . GLY A 1075 ? 0.2453 0.2524 0.2251 0.0222  -0.0068 0.0047  1073 GLY A O   
7826  N N   . SER A 1076 ? 0.2379 0.2525 0.2180 0.0239  -0.0090 0.0080  1074 SER A N   
7827  C CA  . SER A 1076 ? 0.2309 0.2458 0.2118 0.0247  -0.0083 0.0120  1074 SER A CA  
7828  C C   . SER A 1076 ? 0.2534 0.2700 0.2298 0.0250  -0.0076 0.0120  1074 SER A C   
7829  O O   . SER A 1076 ? 0.2640 0.2785 0.2406 0.0249  -0.0063 0.0138  1074 SER A O   
7830  C CB  . SER A 1076 ? 0.2649 0.2843 0.2483 0.0258  -0.0096 0.0161  1074 SER A CB  
7831  O OG  . SER A 1076 ? 0.3510 0.3688 0.3395 0.0257  -0.0102 0.0162  1074 SER A OG  
7832  N N   . SER A 1077 ? 0.2371 0.2575 0.2093 0.0254  -0.0085 0.0098  1075 SER A N   
7833  C CA  A SER A 1077 ? 0.2639 0.2870 0.2318 0.0261  -0.0080 0.0094  1075 SER A CA  
7834  C CA  B SER A 1077 ? 0.2640 0.2871 0.2319 0.0261  -0.0080 0.0093  1075 SER A CA  
7835  C C   . SER A 1077 ? 0.2606 0.2785 0.2273 0.0253  -0.0068 0.0062  1075 SER A C   
7836  O O   . SER A 1077 ? 0.2695 0.2883 0.2339 0.0258  -0.0058 0.0066  1075 SER A O   
7837  C CB  A SER A 1077 ? 0.2588 0.2881 0.2231 0.0271  -0.0095 0.0073  1075 SER A CB  
7838  C CB  B SER A 1077 ? 0.2585 0.2874 0.2227 0.0270  -0.0096 0.0068  1075 SER A CB  
7839  O OG  A SER A 1077 ? 0.2633 0.2987 0.2279 0.0280  -0.0104 0.0113  1075 SER A OG  
7840  O OG  B SER A 1077 ? 0.2896 0.3217 0.2497 0.0279  -0.0092 0.0054  1075 SER A OG  
7841  N N   . SER A 1078 ? 0.2187 0.2319 0.1872 0.0240  -0.0069 0.0032  1076 SER A N   
7842  C CA  . SER A 1078 ? 0.2338 0.2422 0.2015 0.0231  -0.0059 0.0006  1076 SER A CA  
7843  C C   . SER A 1078 ? 0.2311 0.2369 0.1998 0.0230  -0.0041 0.0031  1076 SER A C   
7844  O O   . SER A 1078 ? 0.2199 0.2249 0.1918 0.0229  -0.0036 0.0061  1076 SER A O   
7845  C CB  . SER A 1078 ? 0.2067 0.2113 0.1769 0.0215  -0.0063 -0.0018 1076 SER A CB  
7846  O OG  . SER A 1078 ? 0.2007 0.2008 0.1708 0.0204  -0.0053 -0.0034 1076 SER A OG  
7847  N N   . ALA A 1079 ? 0.1990 0.2035 0.1655 0.0230  -0.0033 0.0018  1077 ALA A N   
7848  C CA  . ALA A 1079 ? 0.2005 0.2022 0.1680 0.0227  -0.0016 0.0038  1077 ALA A CA  
7849  C C   . ALA A 1079 ? 0.2080 0.2041 0.1768 0.0212  -0.0009 0.0016  1077 ALA A C   
7850  O O   . ALA A 1079 ? 0.1931 0.1866 0.1621 0.0209  0.0003  0.0023  1077 ALA A O   
7851  C CB  . ALA A 1079 ? 0.2077 0.2124 0.1720 0.0238  -0.0010 0.0045  1077 ALA A CB  
7852  N N   . LEU A 1080 ? 0.2117 0.2063 0.1815 0.0202  -0.0018 -0.0008 1078 LEU A N   
7853  C CA  . LEU A 1080 ? 0.1826 0.1730 0.1540 0.0186  -0.0012 -0.0023 1078 LEU A CA  
7854  C C   . LEU A 1080 ? 0.2012 0.1898 0.1754 0.0184  0.0001  -0.0001 1078 LEU A C   
7855  O O   . LEU A 1080 ? 0.2168 0.2069 0.1934 0.0190  -0.0001 0.0016  1078 LEU A O   
7856  C CB  . LEU A 1080 ? 0.2004 0.1908 0.1732 0.0175  -0.0025 -0.0042 1078 LEU A CB  
7857  C CG  . LEU A 1080 ? 0.1983 0.1859 0.1734 0.0157  -0.0019 -0.0049 1078 LEU A CG  
7858  C CD1 . LEU A 1080 ? 0.2396 0.2246 0.2136 0.0147  -0.0019 -0.0065 1078 LEU A CD1 
7859  C CD2 . LEU A 1080 ? 0.1998 0.1891 0.1770 0.0148  -0.0030 -0.0058 1078 LEU A CD2 
7860  N N   . GLY A 1081 ? 0.1926 0.1782 0.1670 0.0176  0.0013  -0.0005 1079 GLY A N   
7861  C CA  . GLY A 1081 ? 0.2301 0.2141 0.2072 0.0175  0.0023  0.0010  1079 GLY A CA  
7862  C C   . GLY A 1081 ? 0.2499 0.2338 0.2270 0.0184  0.0031  0.0035  1079 GLY A C   
7863  O O   . GLY A 1081 ? 0.2330 0.2151 0.2128 0.0182  0.0038  0.0045  1079 GLY A O   
7864  N N   . LEU A 1082 ? 0.2245 0.2108 0.1988 0.0193  0.0029  0.0045  1080 LEU A N   
7865  C CA  . LEU A 1082 ? 0.2063 0.1931 0.1802 0.0200  0.0037  0.0070  1080 LEU A CA  
7866  C C   . LEU A 1082 ? 0.2074 0.1905 0.1816 0.0191  0.0049  0.0061  1080 LEU A C   
7867  O O   . LEU A 1082 ? 0.2085 0.1898 0.1812 0.0183  0.0049  0.0034  1080 LEU A O   
7868  C CB  . LEU A 1082 ? 0.2080 0.1988 0.1781 0.0211  0.0034  0.0072  1080 LEU A CB  
7869  C CG  . LEU A 1082 ? 0.2242 0.2172 0.1935 0.0218  0.0043  0.0100  1080 LEU A CG  
7870  C CD1 . LEU A 1082 ? 0.3107 0.3040 0.2839 0.0218  0.0044  0.0142  1080 LEU A CD1 
7871  C CD2 . LEU A 1082 ? 0.2260 0.2249 0.1917 0.0231  0.0039  0.0100  1080 LEU A CD2 
7872  N N   . ASP A 1083 ? 0.2256 0.2076 0.2023 0.0191  0.0056  0.0084  1081 ASP A N   
7873  C CA  . ASP A 1083 ? 0.2299 0.2086 0.2075 0.0182  0.0065  0.0075  1081 ASP A CA  
7874  C C   . ASP A 1083 ? 0.2442 0.2232 0.2233 0.0186  0.0071  0.0107  1081 ASP A C   
7875  O O   . ASP A 1083 ? 0.2796 0.2581 0.2628 0.0187  0.0068  0.0128  1081 ASP A O   
7876  C CB  . ASP A 1083 ? 0.2541 0.2306 0.2349 0.0174  0.0065  0.0060  1081 ASP A CB  
7877  C CG  . ASP A 1083 ? 0.3258 0.2996 0.3071 0.0164  0.0074  0.0047  1081 ASP A CG  
7878  O OD1 . ASP A 1083 ? 0.3716 0.3446 0.3505 0.0162  0.0080  0.0048  1081 ASP A OD1 
7879  O OD2 . ASP A 1083 ? 0.4069 0.3797 0.3909 0.0159  0.0074  0.0034  1081 ASP A OD2 
7880  N N   . LEU A 1084 ? 0.2343 0.2143 0.2105 0.0188  0.0078  0.0111  1082 LEU A N   
7881  C CA  . LEU A 1084 ? 0.2269 0.2085 0.2041 0.0192  0.0083  0.0146  1082 LEU A CA  
7882  C C   . LEU A 1084 ? 0.2234 0.2026 0.2004 0.0186  0.0093  0.0139  1082 LEU A C   
7883  O O   . LEU A 1084 ? 0.2439 0.2213 0.2186 0.0182  0.0096  0.0109  1082 LEU A O   
7884  C CB  . LEU A 1084 ? 0.2518 0.2388 0.2257 0.0204  0.0083  0.0161  1082 LEU A CB  
7885  C CG  . LEU A 1084 ? 0.2579 0.2488 0.2317 0.0212  0.0072  0.0175  1082 LEU A CG  
7886  C CD1 . LEU A 1084 ? 0.2862 0.2833 0.2561 0.0224  0.0073  0.0183  1082 LEU A CD1 
7887  C CD2 . LEU A 1084 ? 0.2803 0.2712 0.2591 0.0210  0.0067  0.0216  1082 LEU A CD2 
7888  N N   . GLU A 1085 ? 0.2324 0.2116 0.2122 0.0185  0.0097  0.0170  1083 GLU A N   
7889  C CA  . GLU A 1085 ? 0.2191 0.1972 0.1985 0.0181  0.0106  0.0170  1083 GLU A CA  
7890  C C   . GLU A 1085 ? 0.2313 0.2142 0.2091 0.0189  0.0111  0.0201  1083 GLU A C   
7891  O O   . GLU A 1085 ? 0.2490 0.2349 0.2290 0.0192  0.0107  0.0241  1083 GLU A O   
7892  C CB  . GLU A 1085 ? 0.2168 0.1915 0.2008 0.0172  0.0106  0.0179  1083 GLU A CB  
7893  C CG  . GLU A 1085 ? 0.2403 0.2143 0.2237 0.0167  0.0116  0.0182  1083 GLU A CG  
7894  C CD  . GLU A 1085 ? 0.2989 0.2696 0.2867 0.0158  0.0115  0.0184  1083 GLU A CD  
7895  O OE1 . GLU A 1085 ? 0.3166 0.2852 0.3079 0.0155  0.0106  0.0173  1083 GLU A OE1 
7896  O OE2 . GLU A 1085 ? 0.2865 0.2571 0.2744 0.0155  0.0121  0.0194  1083 GLU A OE2 
7897  N N   . LEU A 1086 ? 0.2274 0.2115 0.2016 0.0193  0.0119  0.0185  1084 LEU A N   
7898  C CA  . LEU A 1086 ? 0.2353 0.2252 0.2075 0.0204  0.0125  0.0206  1084 LEU A CA  
7899  C C   . LEU A 1086 ? 0.2450 0.2349 0.2192 0.0199  0.0134  0.0231  1084 LEU A C   
7900  O O   . LEU A 1086 ? 0.2554 0.2408 0.2305 0.0190  0.0137  0.0213  1084 LEU A O   
7901  C CB  . LEU A 1086 ? 0.2344 0.2262 0.2020 0.0215  0.0126  0.0167  1084 LEU A CB  
7902  C CG  . LEU A 1086 ? 0.2490 0.2408 0.2147 0.0220  0.0115  0.0138  1084 LEU A CG  
7903  C CD1 . LEU A 1086 ? 0.2389 0.2322 0.2009 0.0232  0.0113  0.0097  1084 LEU A CD1 
7904  C CD2 . LEU A 1086 ? 0.2561 0.2527 0.2219 0.0226  0.0110  0.0167  1084 LEU A CD2 
7905  N N   . PRO A 1087 ? 0.2490 0.2444 0.2241 0.0202  0.0137  0.0275  1085 PRO A N   
7906  C CA  . PRO A 1087 ? 0.2833 0.2794 0.2606 0.0196  0.0145  0.0304  1085 PRO A CA  
7907  C C   . PRO A 1087 ? 0.2824 0.2786 0.2566 0.0202  0.0155  0.0272  1085 PRO A C   
7908  O O   . PRO A 1087 ? 0.2918 0.2912 0.2618 0.0216  0.0158  0.0245  1085 PRO A O   
7909  C CB  . PRO A 1087 ? 0.2793 0.2831 0.2574 0.0201  0.0146  0.0358  1085 PRO A CB  
7910  C CG  . PRO A 1087 ? 0.3102 0.3156 0.2880 0.0205  0.0135  0.0365  1085 PRO A CG  
7911  C CD  . PRO A 1087 ? 0.2488 0.2504 0.2233 0.0210  0.0132  0.0306  1085 PRO A CD  
7912  N N   . GLY A 1088 ? 0.2607 0.2534 0.2372 0.0192  0.0159  0.0274  1086 GLY A N   
7913  C CA  . GLY A 1088 ? 0.2639 0.2563 0.2381 0.0196  0.0168  0.0248  1086 GLY A CA  
7914  C C   . GLY A 1088 ? 0.2172 0.2071 0.1949 0.0184  0.0172  0.0266  1086 GLY A C   
7915  O O   . GLY A 1088 ? 0.2443 0.2342 0.2262 0.0174  0.0169  0.0305  1086 GLY A O   
7916  N N   . PRO A 1089 ? 0.2496 0.2371 0.2261 0.0184  0.0176  0.0238  1087 PRO A N   
7917  C CA  . PRO A 1089 ? 0.2496 0.2352 0.2291 0.0173  0.0180  0.0252  1087 PRO A CA  
7918  C C   . PRO A 1089 ? 0.2667 0.2463 0.2497 0.0157  0.0172  0.0249  1087 PRO A C   
7919  O O   . PRO A 1089 ? 0.2603 0.2366 0.2427 0.0155  0.0165  0.0223  1087 PRO A O   
7920  C CB  . PRO A 1089 ? 0.2616 0.2464 0.2383 0.0180  0.0185  0.0218  1087 PRO A CB  
7921  C CG  . PRO A 1089 ? 0.2716 0.2543 0.2452 0.0186  0.0178  0.0177  1087 PRO A CG  
7922  C CD  . PRO A 1089 ? 0.2534 0.2399 0.2261 0.0194  0.0176  0.0191  1087 PRO A CD  
7923  N N   . VAL A 1090 ? 0.2398 0.2185 0.2269 0.0146  0.0171  0.0273  1088 VAL A N   
7924  C CA  . VAL A 1090 ? 0.2268 0.2002 0.2174 0.0133  0.0162  0.0260  1088 VAL A CA  
7925  C C   . VAL A 1090 ? 0.2375 0.2075 0.2254 0.0131  0.0164  0.0216  1088 VAL A C   
7926  O O   . VAL A 1090 ? 0.2455 0.2166 0.2300 0.0138  0.0170  0.0201  1088 VAL A O   
7927  C CB  . VAL A 1090 ? 0.2607 0.2338 0.2565 0.0122  0.0159  0.0290  1088 VAL A CB  
7928  C CG1 . VAL A 1090 ? 0.2799 0.2566 0.2792 0.0121  0.0155  0.0342  1088 VAL A CG1 
7929  C CG2 . VAL A 1090 ? 0.2517 0.2263 0.2461 0.0122  0.0169  0.0289  1088 VAL A CG2 
7930  N N   . GLY A 1091 ? 0.2344 0.2007 0.2242 0.0122  0.0156  0.0195  1089 GLY A N   
7931  C CA  . GLY A 1091 ? 0.2746 0.2385 0.2623 0.0117  0.0156  0.0160  1089 GLY A CA  
7932  C C   . GLY A 1091 ? 0.2447 0.2085 0.2284 0.0123  0.0156  0.0136  1089 GLY A C   
7933  O O   . GLY A 1091 ? 0.2349 0.1972 0.2168 0.0119  0.0156  0.0113  1089 GLY A O   
7934  N N   . GLU A 1092 ? 0.2314 0.1967 0.2141 0.0131  0.0155  0.0142  1090 GLU A N   
7935  C CA  . GLU A 1092 ? 0.2399 0.2053 0.2193 0.0136  0.0152  0.0120  1090 GLU A CA  
7936  C C   . GLU A 1092 ? 0.2484 0.2145 0.2287 0.0140  0.0147  0.0126  1090 GLU A C   
7937  O O   . GLU A 1092 ? 0.2631 0.2310 0.2454 0.0143  0.0147  0.0155  1090 GLU A O   
7938  C CB  . GLU A 1092 ? 0.2830 0.2510 0.2593 0.0149  0.0157  0.0119  1090 GLU A CB  
7939  C CG  . GLU A 1092 ? 0.3089 0.2759 0.2824 0.0152  0.0152  0.0089  1090 GLU A CG  
7940  C CD  . GLU A 1092 ? 0.2864 0.2561 0.2578 0.0167  0.0155  0.0083  1090 GLU A CD  
7941  O OE1 . GLU A 1092 ? 0.2535 0.2269 0.2236 0.0180  0.0156  0.0090  1090 GLU A OE1 
7942  O OE2 . GLU A 1092 ? 0.2913 0.2599 0.2625 0.0166  0.0155  0.0073  1090 GLU A OE2 
7943  N N   . ARG A 1093 ? 0.2106 0.1755 0.1897 0.0137  0.0142  0.0103  1091 ARG A N   
7944  C CA  . ARG A 1093 ? 0.2265 0.1924 0.2060 0.0142  0.0136  0.0106  1091 ARG A CA  
7945  C C   . ARG A 1093 ? 0.2186 0.1859 0.1944 0.0150  0.0134  0.0091  1091 ARG A C   
7946  O O   . ARG A 1093 ? 0.2236 0.1893 0.1978 0.0145  0.0131  0.0067  1091 ARG A O   
7947  C CB  . ARG A 1093 ? 0.2357 0.1998 0.2176 0.0135  0.0130  0.0090  1091 ARG A CB  
7948  N N   . ASN A 1094 ? 0.2044 0.1748 0.1791 0.0161  0.0133  0.0105  1092 ASN A N   
7949  C CA  . ASN A 1094 ? 0.1920 0.1643 0.1634 0.0171  0.0129  0.0087  1092 ASN A CA  
7950  C C   . ASN A 1094 ? 0.2110 0.1844 0.1824 0.0174  0.0122  0.0088  1092 ASN A C   
7951  O O   . ASN A 1094 ? 0.2247 0.2006 0.1974 0.0179  0.0122  0.0115  1092 ASN A O   
7952  C CB  . ASN A 1094 ? 0.1954 0.1716 0.1649 0.0184  0.0135  0.0098  1092 ASN A CB  
7953  C CG  . ASN A 1094 ? 0.2117 0.1866 0.1808 0.0183  0.0140  0.0088  1092 ASN A CG  
7954  O OD1 . ASN A 1094 ? 0.2022 0.1748 0.1702 0.0181  0.0135  0.0060  1092 ASN A OD1 
7955  N ND2 . ASN A 1094 ? 0.2325 0.2087 0.2031 0.0182  0.0149  0.0113  1092 ASN A ND2 
7956  N N   . LEU A 1095 ? 0.2060 0.1778 0.1766 0.0169  0.0114  0.0062  1093 LEU A N   
7957  C CA  . LEU A 1095 ? 0.2014 0.1738 0.1726 0.0169  0.0107  0.0060  1093 LEU A CA  
7958  C C   . LEU A 1095 ? 0.2091 0.1835 0.1775 0.0178  0.0098  0.0041  1093 LEU A C   
7959  O O   . LEU A 1095 ? 0.2045 0.1782 0.1712 0.0179  0.0095  0.0019  1093 LEU A O   
7960  C CB  . LEU A 1095 ? 0.2134 0.1829 0.1863 0.0155  0.0104  0.0044  1093 LEU A CB  
7961  C CG  . LEU A 1095 ? 0.2449 0.2125 0.2205 0.0148  0.0111  0.0053  1093 LEU A CG  
7962  C CD1 . LEU A 1095 ? 0.3284 0.2945 0.3054 0.0135  0.0109  0.0033  1093 LEU A CD1 
7963  C CD2 . LEU A 1095 ? 0.2622 0.2307 0.2407 0.0154  0.0111  0.0080  1093 LEU A CD2 
7964  N N   . TYR A 1096 ? 0.2253 0.2022 0.1937 0.0184  0.0092  0.0049  1094 TYR A N   
7965  C CA  . TYR A 1096 ? 0.1968 0.1762 0.1628 0.0193  0.0083  0.0031  1094 TYR A CA  
7966  C C   . TYR A 1096 ? 0.2020 0.1814 0.1692 0.0189  0.0074  0.0030  1094 TYR A C   
7967  O O   . TYR A 1096 ? 0.2146 0.1950 0.1836 0.0191  0.0075  0.0054  1094 TYR A O   
7968  C CB  . TYR A 1096 ? 0.2221 0.2067 0.1862 0.0210  0.0085  0.0047  1094 TYR A CB  
7969  C CG  . TYR A 1096 ? 0.1998 0.1882 0.1614 0.0222  0.0074  0.0029  1094 TYR A CG  
7970  C CD1 . TYR A 1096 ? 0.1937 0.1828 0.1533 0.0230  0.0067  -0.0007 1094 TYR A CD1 
7971  C CD2 . TYR A 1096 ? 0.2317 0.2233 0.1936 0.0226  0.0068  0.0046  1094 TYR A CD2 
7972  C CE1 . TYR A 1096 ? 0.2090 0.2020 0.1666 0.0243  0.0055  -0.0029 1094 TYR A CE1 
7973  C CE2 . TYR A 1096 ? 0.2308 0.2266 0.1903 0.0238  0.0057  0.0028  1094 TYR A CE2 
7974  C CZ  . TYR A 1096 ? 0.2152 0.2117 0.1726 0.0246  0.0050  -0.0012 1094 TYR A CZ  
7975  O OH  . TYR A 1096 ? 0.2063 0.2071 0.1616 0.0259  0.0037  -0.0035 1094 TYR A OH  
7976  N N   . THR A 1097 ? 0.2052 0.1833 0.1719 0.0183  0.0064  0.0002  1095 THR A N   
7977  C CA  . THR A 1097 ? 0.2041 0.1821 0.1723 0.0177  0.0056  -0.0001 1095 THR A CA  
7978  C C   . THR A 1097 ? 0.2120 0.1915 0.1786 0.0181  0.0041  -0.0025 1095 THR A C   
7979  O O   . THR A 1097 ? 0.2118 0.1908 0.1771 0.0182  0.0035  -0.0046 1095 THR A O   
7980  C CB  . THR A 1097 ? 0.2535 0.2283 0.2238 0.0160  0.0059  -0.0008 1095 THR A CB  
7981  O OG1 . THR A 1097 ? 0.3200 0.2928 0.2895 0.0151  0.0055  -0.0027 1095 THR A OG1 
7982  C CG2 . THR A 1097 ? 0.2497 0.2232 0.2219 0.0158  0.0071  0.0009  1095 THR A CG2 
7983  N N   . LEU A 1098 ? 0.2132 0.1946 0.1805 0.0182  0.0033  -0.0022 1096 LEU A N   
7984  C CA  . LEU A 1098 ? 0.2199 0.2028 0.1862 0.0184  0.0017  -0.0045 1096 LEU A CA  
7985  C C   . LEU A 1098 ? 0.1869 0.1680 0.1555 0.0168  0.0010  -0.0054 1096 LEU A C   
7986  O O   . LEU A 1098 ? 0.2094 0.1908 0.1800 0.0164  0.0014  -0.0040 1096 LEU A O   
7987  C CB  . LEU A 1098 ? 0.2060 0.1936 0.1712 0.0199  0.0011  -0.0034 1096 LEU A CB  
7988  C CG  . LEU A 1098 ? 0.1925 0.1836 0.1552 0.0215  0.0017  -0.0022 1096 LEU A CG  
7989  C CD1 . LEU A 1098 ? 0.1978 0.1945 0.1593 0.0229  0.0010  -0.0009 1096 LEU A CD1 
7990  C CD2 . LEU A 1098 ? 0.2088 0.1995 0.1695 0.0221  0.0013  -0.0054 1096 LEU A CD2 
7991  N N   . HIS A 1099 ? 0.2092 0.1886 0.1779 0.0158  -0.0002 -0.0077 1097 HIS A N   
7992  C CA  . HIS A 1099 ? 0.2263 0.2045 0.1974 0.0140  -0.0010 -0.0084 1097 HIS A CA  
7993  C C   . HIS A 1099 ? 0.2104 0.1900 0.1817 0.0140  -0.0032 -0.0104 1097 HIS A C   
7994  O O   . HIS A 1099 ? 0.2128 0.1940 0.1822 0.0155  -0.0042 -0.0119 1097 HIS A O   
7995  C CB  . HIS A 1099 ? 0.2204 0.1954 0.1925 0.0124  -0.0009 -0.0087 1097 HIS A CB  
7996  C CG  . HIS A 1099 ? 0.2729 0.2467 0.2450 0.0122  0.0010  -0.0071 1097 HIS A CG  
7997  N ND1 . HIS A 1099 ? 0.3360 0.3096 0.3100 0.0108  0.0019  -0.0061 1097 HIS A ND1 
7998  C CD2 . HIS A 1099 ? 0.2923 0.2655 0.2630 0.0133  0.0022  -0.0064 1097 HIS A CD2 
7999  C CE1 . HIS A 1099 ? 0.3366 0.3091 0.3103 0.0111  0.0034  -0.0051 1097 HIS A CE1 
8000  N NE2 . HIS A 1099 ? 0.2910 0.2630 0.2628 0.0125  0.0036  -0.0050 1097 HIS A NE2 
8001  N N   . ALA A 1100 ? 0.1956 0.1749 0.1693 0.0122  -0.0041 -0.0106 1098 ALA A N   
8002  C CA  . ALA A 1100 ? 0.2357 0.2155 0.2104 0.0118  -0.0065 -0.0126 1098 ALA A CA  
8003  C C   . ALA A 1100 ? 0.2515 0.2286 0.2265 0.0115  -0.0079 -0.0147 1098 ALA A C   
8004  O O   . ALA A 1100 ? 0.2467 0.2212 0.2221 0.0108  -0.0072 -0.0140 1098 ALA A O   
8005  C CB  . ALA A 1100 ? 0.2140 0.1943 0.1918 0.0096  -0.0071 -0.0119 1098 ALA A CB  
8006  N N   . ARG A 1101 ? 0.2189 0.1967 0.1939 0.0123  -0.0102 -0.0174 1099 ARG A N   
8007  C CA  A ARG A 1101 ? 0.2543 0.2295 0.2307 0.0122  -0.0122 -0.0200 1099 ARG A CA  
8008  C CA  B ARG A 1101 ? 0.2541 0.2293 0.2306 0.0122  -0.0122 -0.0199 1099 ARG A CA  
8009  C C   . ARG A 1101 ? 0.2286 0.2010 0.2094 0.0094  -0.0138 -0.0193 1099 ARG A C   
8010  O O   . ARG A 1101 ? 0.2457 0.2150 0.2284 0.0085  -0.0145 -0.0194 1099 ARG A O   
8011  C CB  A ARG A 1101 ? 0.2444 0.2218 0.2200 0.0141  -0.0145 -0.0237 1099 ARG A CB  
8012  C CB  B ARG A 1101 ? 0.2446 0.2220 0.2201 0.0142  -0.0144 -0.0237 1099 ARG A CB  
8013  C CG  A ARG A 1101 ? 0.2528 0.2340 0.2241 0.0170  -0.0131 -0.0243 1099 ARG A CG  
8014  C CG  B ARG A 1101 ? 0.2557 0.2362 0.2270 0.0170  -0.0132 -0.0247 1099 ARG A CG  
8015  C CD  A ARG A 1101 ? 0.2299 0.2141 0.2003 0.0190  -0.0155 -0.0286 1099 ARG A CD  
8016  C CD  B ARG A 1101 ? 0.2660 0.2463 0.2375 0.0187  -0.0151 -0.0289 1099 ARG A CD  
8017  N NE  A ARG A 1101 ? 0.2341 0.2161 0.2057 0.0199  -0.0171 -0.0322 1099 ARG A NE  
8018  N NE  B ARG A 1101 ? 0.2510 0.2350 0.2186 0.0213  -0.0135 -0.0295 1099 ARG A NE  
8019  C CZ  A ARG A 1101 ? 0.2629 0.2464 0.2321 0.0219  -0.0159 -0.0332 1099 ARG A CZ  
8020  C CZ  B ARG A 1101 ? 0.2606 0.2462 0.2274 0.0235  -0.0148 -0.0335 1099 ARG A CZ  
8021  N NH1 A ARG A 1101 ? 0.2588 0.2458 0.2241 0.0231  -0.0132 -0.0306 1099 ARG A NH1 
8022  N NH1 B ARG A 1101 ? 0.2668 0.2501 0.2369 0.0234  -0.0179 -0.0377 1099 ARG A NH1 
8023  N NH2 A ARG A 1101 ? 0.2670 0.2484 0.2380 0.0227  -0.0177 -0.0369 1099 ARG A NH2 
8024  N NH2 B ARG A 1101 ? 0.2382 0.2284 0.2013 0.0257  -0.0131 -0.0334 1099 ARG A NH2 
8025  N N   . GLY A 1102 ? 0.2256 0.1996 0.2084 0.0079  -0.0145 -0.0182 1100 GLY A N   
8026  C CA  . GLY A 1102 ? 0.2416 0.2140 0.2289 0.0050  -0.0162 -0.0172 1100 GLY A CA  
8027  C C   . GLY A 1102 ? 0.2130 0.1873 0.2025 0.0042  -0.0183 -0.0181 1100 GLY A C   
8028  O O   . GLY A 1102 ? 0.2285 0.2062 0.2166 0.0048  -0.0172 -0.0173 1100 GLY A O   
8029  N N   . ARG A 1103 ? 0.2133 0.1856 0.2069 0.0030  -0.0216 -0.0196 1101 ARG A N   
8030  C CA  . ARG A 1103 ? 0.1891 0.1632 0.1855 0.0022  -0.0242 -0.0207 1101 ARG A CA  
8031  C C   . ARG A 1103 ? 0.2462 0.2203 0.2415 0.0047  -0.0264 -0.0254 1101 ARG A C   
8032  O O   . ARG A 1103 ? 0.2357 0.2068 0.2323 0.0054  -0.0283 -0.0281 1101 ARG A O   
8033  C CB  . ARG A 1103 ? 0.2435 0.2159 0.2461 -0.0012 -0.0267 -0.0190 1101 ARG A CB  
8034  C CG  . ARG A 1103 ? 0.2762 0.2508 0.2820 -0.0024 -0.0291 -0.0195 1101 ARG A CG  
8035  C CD  . ARG A 1103 ? 0.3139 0.2880 0.3261 -0.0063 -0.0311 -0.0164 1101 ARG A CD  
8036  N NE  . ARG A 1103 ? 0.3584 0.3349 0.3703 -0.0082 -0.0282 -0.0119 1101 ARG A NE  
8037  C CZ  . ARG A 1103 ? 0.3754 0.3566 0.3872 -0.0093 -0.0266 -0.0095 1101 ARG A CZ  
8038  N NH1 . ARG A 1103 ? 0.3225 0.3065 0.3345 -0.0088 -0.0274 -0.0108 1101 ARG A NH1 
8039  N NH2 . ARG A 1103 ? 0.4054 0.3890 0.4170 -0.0108 -0.0241 -0.0060 1101 ARG A NH2 
8040  N N   . ILE A 1104 ? 0.2144 0.1923 0.2074 0.0061  -0.0263 -0.0265 1102 ILE A N   
8041  C CA  . ILE A 1104 ? 0.2526 0.2323 0.2439 0.0087  -0.0283 -0.0310 1102 ILE A CA  
8042  C C   . ILE A 1104 ? 0.2357 0.2156 0.2316 0.0074  -0.0321 -0.0332 1102 ILE A C   
8043  O O   . ILE A 1104 ? 0.2279 0.2094 0.2257 0.0055  -0.0322 -0.0309 1102 ILE A O   
8044  C CB  . ILE A 1104 ? 0.2223 0.2067 0.2082 0.0111  -0.0259 -0.0306 1102 ILE A CB  
8045  C CG1 . ILE A 1104 ? 0.2237 0.2078 0.2060 0.0119  -0.0223 -0.0278 1102 ILE A CG1 
8046  C CG2 . ILE A 1104 ? 0.2180 0.2056 0.2017 0.0138  -0.0279 -0.0352 1102 ILE A CG2 
8047  C CD1 . ILE A 1104 ? 0.2452 0.2274 0.2258 0.0136  -0.0221 -0.0299 1102 ILE A CD1 
8048  N N   . LEU A 1105 ? 0.2165 0.1947 0.2147 0.0084  -0.0354 -0.0377 1103 LEU A N   
8049  C CA  . LEU A 1105 ? 0.2464 0.2248 0.2492 0.0075  -0.0395 -0.0406 1103 LEU A CA  
8050  C C   . LEU A 1105 ? 0.2242 0.2080 0.2232 0.0097  -0.0396 -0.0429 1103 LEU A C   
8051  O O   . LEU A 1105 ? 0.2457 0.2323 0.2402 0.0129  -0.0390 -0.0459 1103 LEU A O   
8052  C CB  . LEU A 1105 ? 0.2627 0.2373 0.2698 0.0081  -0.0433 -0.0452 1103 LEU A CB  
8053  C CG  . LEU A 1105 ? 0.2571 0.2317 0.2694 0.0078  -0.0482 -0.0495 1103 LEU A CG  
8054  C CD1 . LEU A 1105 ? 0.2882 0.2609 0.3070 0.0037  -0.0499 -0.0457 1103 LEU A CD1 
8055  C CD2 . LEU A 1105 ? 0.2751 0.2464 0.2910 0.0093  -0.0517 -0.0550 1103 LEU A CD2 
8056  N N   . LEU A 1106 ? 0.2358 0.2219 0.2366 0.0081  -0.0404 -0.0413 1104 LEU A N   
8057  C CA  . LEU A 1106 ? 0.2230 0.2145 0.2210 0.0100  -0.0409 -0.0433 1104 LEU A CA  
8058  C C   . LEU A 1106 ? 0.2625 0.2539 0.2654 0.0095  -0.0458 -0.0478 1104 LEU A C   
8059  O O   . LEU A 1106 ? 0.2327 0.2213 0.2417 0.0065  -0.0480 -0.0466 1104 LEU A O   
8060  C CB  . LEU A 1106 ? 0.2227 0.2172 0.2197 0.0087  -0.0387 -0.0388 1104 LEU A CB  
8061  C CG  . LEU A 1106 ? 0.2697 0.2647 0.2626 0.0091  -0.0342 -0.0345 1104 LEU A CG  
8062  C CD1 . LEU A 1106 ? 0.2155 0.2145 0.2076 0.0088  -0.0326 -0.0313 1104 LEU A CD1 
8063  C CD2 . LEU A 1106 ? 0.2960 0.2922 0.2836 0.0122  -0.0324 -0.0358 1104 LEU A CD2 
8064  N N   . VAL A 1107 ? 0.2427 0.2376 0.2430 0.0125  -0.0475 -0.0529 1105 VAL A N   
8065  C CA  . VAL A 1107 ? 0.2380 0.2335 0.2426 0.0125  -0.0523 -0.0581 1105 VAL A CA  
8066  C C   . VAL A 1107 ? 0.2576 0.2603 0.2580 0.0144  -0.0522 -0.0593 1105 VAL A C   
8067  O O   . VAL A 1107 ? 0.2707 0.2779 0.2672 0.0176  -0.0528 -0.0637 1105 VAL A O   
8068  C CB  . VAL A 1107 ? 0.2525 0.2459 0.2590 0.0145  -0.0552 -0.0643 1105 VAL A CB  
8069  C CG1 . VAL A 1107 ? 0.2512 0.2442 0.2639 0.0141  -0.0607 -0.0697 1105 VAL A CG1 
8070  C CG2 . VAL A 1107 ? 0.2407 0.2273 0.2505 0.0129  -0.0546 -0.0622 1105 VAL A CG2 
8071  N N   . PRO A 1108 ? 0.2306 0.2352 0.2319 0.0126  -0.0516 -0.0555 1106 PRO A N   
8072  C CA  . PRO A 1108 ? 0.2554 0.2669 0.2530 0.0142  -0.0515 -0.0561 1106 PRO A CA  
8073  C C   . PRO A 1108 ? 0.2726 0.2861 0.2739 0.0144  -0.0564 -0.0614 1106 PRO A C   
8074  O O   . PRO A 1108 ? 0.2606 0.2696 0.2684 0.0126  -0.0598 -0.0638 1106 PRO A O   
8075  C CB  . PRO A 1108 ? 0.2558 0.2676 0.2540 0.0120  -0.0490 -0.0499 1106 PRO A CB  
8076  C CG  . PRO A 1108 ? 0.2604 0.2665 0.2653 0.0085  -0.0503 -0.0482 1106 PRO A CG  
8077  C CD  . PRO A 1108 ? 0.2786 0.2797 0.2842 0.0089  -0.0506 -0.0503 1106 PRO A CD  
8078  N N   . ALA A 1109 ? 0.2374 0.2578 0.2346 0.0166  -0.0567 -0.0631 1107 ALA A N   
8079  C CA  . ALA A 1109 ? 0.2527 0.2764 0.2530 0.0167  -0.0611 -0.0676 1107 ALA A CA  
8080  C C   . ALA A 1109 ? 0.2706 0.2987 0.2705 0.0157  -0.0606 -0.0641 1107 ALA A C   
8081  O O   . ALA A 1109 ? 0.2917 0.3201 0.2966 0.0141  -0.0641 -0.0659 1107 ALA A O   
8082  C CB  . ALA A 1109 ? 0.2549 0.2844 0.2511 0.0205  -0.0629 -0.0742 1107 ALA A CB  
8083  N N   . THR A 1110 ? 0.2491 0.2804 0.2439 0.0165  -0.0566 -0.0591 1108 THR A N   
8084  C CA  . THR A 1110 ? 0.2614 0.2971 0.2559 0.0159  -0.0560 -0.0557 1108 THR A CA  
8085  C C   . THR A 1110 ? 0.2706 0.3036 0.2654 0.0141  -0.0521 -0.0490 1108 THR A C   
8086  O O   . THR A 1110 ? 0.2586 0.2876 0.2519 0.0141  -0.0493 -0.0468 1108 THR A O   
8087  C CB  . THR A 1110 ? 0.2789 0.3230 0.2672 0.0191  -0.0554 -0.0563 1108 THR A CB  
8088  O OG1 . THR A 1110 ? 0.2525 0.2972 0.2354 0.0208  -0.0516 -0.0534 1108 THR A OG1 
8089  C CG2 . THR A 1110 ? 0.2967 0.3448 0.2842 0.0212  -0.0593 -0.0636 1108 THR A CG2 
8090  N N   . GLU A 1111 ? 0.2702 0.3058 0.2669 0.0129  -0.0520 -0.0459 1109 GLU A N   
8091  C CA  . GLU A 1111 ? 0.2655 0.2997 0.2626 0.0117  -0.0484 -0.0401 1109 GLU A CA  
8092  C C   . GLU A 1111 ? 0.2895 0.3250 0.2808 0.0140  -0.0447 -0.0373 1109 GLU A C   
8093  O O   . GLU A 1111 ? 0.2682 0.3000 0.2593 0.0134  -0.0418 -0.0344 1109 GLU A O   
8094  C CB  . GLU A 1111 ? 0.3065 0.3444 0.3064 0.0106  -0.0491 -0.0379 1109 GLU A CB  
8095  C CG  . GLU A 1111 ? 0.2972 0.3351 0.2973 0.0100  -0.0455 -0.0325 1109 GLU A CG  
8096  C CD  . GLU A 1111 ? 0.3557 0.3970 0.3597 0.0087  -0.0463 -0.0306 1109 GLU A CD  
8097  O OE1 . GLU A 1111 ? 0.3502 0.3900 0.3593 0.0060  -0.0480 -0.0309 1109 GLU A OE1 
8098  O OE2 . GLU A 1111 ? 0.3662 0.4119 0.3684 0.0103  -0.0454 -0.0286 1109 GLU A OE2 
8099  N N   . SER A 1112 ? 0.2835 0.3250 0.2707 0.0166  -0.0449 -0.0379 1110 SER A N   
8100  C CA  . SER A 1112 ? 0.2538 0.2971 0.2361 0.0186  -0.0418 -0.0347 1110 SER A CA  
8101  C C   . SER A 1112 ? 0.2609 0.3007 0.2407 0.0194  -0.0405 -0.0363 1110 SER A C   
8102  O O   . SER A 1112 ? 0.2400 0.2778 0.2181 0.0197  -0.0373 -0.0329 1110 SER A O   
8103  C CB  . SER A 1112 ? 0.2900 0.3413 0.2685 0.0211  -0.0426 -0.0348 1110 SER A CB  
8104  O OG  . SER A 1112 ? 0.2825 0.3357 0.2573 0.0227  -0.0397 -0.0308 1110 SER A OG  
8105  N N   . GLY A 1113 ? 0.2458 0.2849 0.2259 0.0197  -0.0431 -0.0416 1111 GLY A N   
8106  C CA  . GLY A 1113 ? 0.2151 0.2505 0.1936 0.0204  -0.0421 -0.0434 1111 GLY A CA  
8107  C C   . GLY A 1113 ? 0.2151 0.2433 0.1966 0.0181  -0.0401 -0.0406 1111 GLY A C   
8108  O O   . GLY A 1113 ? 0.2159 0.2417 0.1951 0.0186  -0.0374 -0.0386 1111 GLY A O   
8109  N N   . LEU A 1114 ? 0.2230 0.2480 0.2098 0.0154  -0.0415 -0.0401 1112 LEU A N   
8110  C CA  . LEU A 1114 ? 0.2102 0.2296 0.2000 0.0130  -0.0397 -0.0370 1112 LEU A CA  
8111  C C   . LEU A 1114 ? 0.1991 0.2190 0.1867 0.0133  -0.0357 -0.0320 1112 LEU A C   
8112  O O   . LEU A 1114 ? 0.2229 0.2391 0.2097 0.0129  -0.0333 -0.0301 1112 LEU A O   
8113  C CB  . LEU A 1114 ? 0.2286 0.2463 0.2245 0.0099  -0.0419 -0.0367 1112 LEU A CB  
8114  C CG  . LEU A 1114 ? 0.2279 0.2417 0.2271 0.0072  -0.0399 -0.0329 1112 LEU A CG  
8115  C CD1 . LEU A 1114 ? 0.2347 0.2433 0.2336 0.0069  -0.0389 -0.0332 1112 LEU A CD1 
8116  C CD2 . LEU A 1114 ? 0.2704 0.2840 0.2760 0.0041  -0.0424 -0.0324 1112 LEU A CD2 
8117  N N   . TYR A 1115 ? 0.2139 0.2383 0.2007 0.0140  -0.0352 -0.0298 1113 TYR A N   
8118  C CA  . TYR A 1115 ? 0.2048 0.2296 0.1905 0.0144  -0.0319 -0.0253 1113 TYR A CA  
8119  C C   . TYR A 1115 ? 0.2377 0.2624 0.2189 0.0165  -0.0297 -0.0245 1113 TYR A C   
8120  O O   . TYR A 1115 ? 0.2125 0.2343 0.1935 0.0162  -0.0270 -0.0217 1113 TYR A O   
8121  C CB  . TYR A 1115 ? 0.2235 0.2535 0.2097 0.0151  -0.0322 -0.0234 1113 TYR A CB  
8122  C CG  . TYR A 1115 ? 0.2408 0.2715 0.2319 0.0130  -0.0339 -0.0234 1113 TYR A CG  
8123  C CD1 . TYR A 1115 ? 0.2238 0.2507 0.2188 0.0104  -0.0342 -0.0238 1113 TYR A CD1 
8124  C CD2 . TYR A 1115 ? 0.2546 0.2903 0.2466 0.0136  -0.0351 -0.0228 1113 TYR A CD2 
8125  C CE1 . TYR A 1115 ? 0.2678 0.2962 0.2675 0.0082  -0.0357 -0.0234 1113 TYR A CE1 
8126  C CE2 . TYR A 1115 ? 0.2530 0.2897 0.2496 0.0117  -0.0365 -0.0227 1113 TYR A CE2 
8127  C CZ  . TYR A 1115 ? 0.2830 0.3163 0.2835 0.0089  -0.0368 -0.0229 1113 TYR A CZ  
8128  O OH  . TYR A 1115 ? 0.3045 0.3396 0.3098 0.0068  -0.0382 -0.0225 1113 TYR A OH  
8129  N N   . HIS A 1116 ? 0.2196 0.2479 0.1972 0.0186  -0.0309 -0.0267 1114 HIS A N   
8130  C CA  . HIS A 1116 ? 0.2156 0.2446 0.1889 0.0205  -0.0290 -0.0260 1114 HIS A CA  
8131  C C   . HIS A 1116 ? 0.2390 0.2624 0.2126 0.0198  -0.0281 -0.0274 1114 HIS A C   
8132  O O   . HIS A 1116 ? 0.2233 0.2448 0.1952 0.0202  -0.0254 -0.0249 1114 HIS A O   
8133  C CB  . HIS A 1116 ? 0.2409 0.2763 0.2104 0.0229  -0.0307 -0.0286 1114 HIS A CB  
8134  C CG  . HIS A 1116 ? 0.2436 0.2855 0.2115 0.0242  -0.0305 -0.0254 1114 HIS A CG  
8135  N ND1 . HIS A 1116 ? 0.3002 0.3456 0.2698 0.0239  -0.0327 -0.0260 1114 HIS A ND1 
8136  C CD2 . HIS A 1116 ? 0.2485 0.2941 0.2137 0.0257  -0.0286 -0.0214 1114 HIS A CD2 
8137  C CE1 . HIS A 1116 ? 0.2758 0.3268 0.2437 0.0253  -0.0321 -0.0224 1114 HIS A CE1 
8138  N NE2 . HIS A 1116 ? 0.2642 0.3154 0.2296 0.0263  -0.0298 -0.0195 1114 HIS A NE2 
8139  N N   . GLN A 1117 ? 0.2130 0.2333 0.1890 0.0186  -0.0304 -0.0312 1115 GLN A N   
8140  C CA  . GLN A 1117 ? 0.1987 0.2135 0.1756 0.0178  -0.0298 -0.0323 1115 GLN A CA  
8141  C C   . GLN A 1117 ? 0.1980 0.2086 0.1770 0.0157  -0.0273 -0.0283 1115 GLN A C   
8142  O O   . GLN A 1117 ? 0.2148 0.2226 0.1925 0.0159  -0.0252 -0.0270 1115 GLN A O   
8143  C CB  . GLN A 1117 ? 0.2267 0.2390 0.2072 0.0166  -0.0333 -0.0367 1115 GLN A CB  
8144  C CG  . GLN A 1117 ? 0.2073 0.2232 0.1859 0.0189  -0.0359 -0.0420 1115 GLN A CG  
8145  C CD  . GLN A 1117 ? 0.2486 0.2612 0.2320 0.0177  -0.0397 -0.0465 1115 GLN A CD  
8146  O OE1 . GLN A 1117 ? 0.2446 0.2528 0.2329 0.0149  -0.0405 -0.0449 1115 GLN A OE1 
8147  N NE2 . GLN A 1117 ? 0.2318 0.2469 0.2143 0.0199  -0.0423 -0.0521 1115 GLN A NE2 
8148  N N   . LEU A 1118 ? 0.1962 0.2069 0.1787 0.0139  -0.0277 -0.0265 1116 LEU A N   
8149  C CA  A LEU A 1118 ? 0.2025 0.2104 0.1872 0.0121  -0.0254 -0.0232 1116 LEU A CA  
8150  C CA  B LEU A 1118 ? 0.2026 0.2105 0.1872 0.0121  -0.0254 -0.0231 1116 LEU A CA  
8151  C C   . LEU A 1118 ? 0.2171 0.2260 0.1990 0.0135  -0.0223 -0.0200 1116 LEU A C   
8152  O O   . LEU A 1118 ? 0.2081 0.2140 0.1901 0.0130  -0.0201 -0.0183 1116 LEU A O   
8153  C CB  A LEU A 1118 ? 0.2149 0.2241 0.2037 0.0100  -0.0264 -0.0221 1116 LEU A CB  
8154  C CB  B LEU A 1118 ? 0.2149 0.2244 0.2036 0.0101  -0.0263 -0.0220 1116 LEU A CB  
8155  C CG  A LEU A 1118 ? 0.2136 0.2213 0.2054 0.0079  -0.0246 -0.0192 1116 LEU A CG  
8156  C CG  B LEU A 1118 ? 0.2156 0.2228 0.2089 0.0074  -0.0286 -0.0231 1116 LEU A CG  
8157  C CD1 A LEU A 1118 ? 0.2130 0.2161 0.2055 0.0064  -0.0241 -0.0192 1116 LEU A CD1 
8158  C CD1 B LEU A 1118 ? 0.2245 0.2350 0.2213 0.0060  -0.0296 -0.0220 1116 LEU A CD1 
8159  C CD2 A LEU A 1118 ? 0.2412 0.2512 0.2374 0.0058  -0.0263 -0.0189 1116 LEU A CD2 
8160  C CD2 B LEU A 1118 ? 0.2254 0.2288 0.2202 0.0056  -0.0269 -0.0212 1116 LEU A CD2 
8161  N N   . ALA A 1119 ? 0.2122 0.2254 0.1922 0.0154  -0.0222 -0.0191 1117 ALA A N   
8162  C CA  . ALA A 1119 ? 0.2214 0.2356 0.1997 0.0168  -0.0197 -0.0158 1117 ALA A CA  
8163  C C   . ALA A 1119 ? 0.2225 0.2346 0.1977 0.0178  -0.0183 -0.0159 1117 ALA A C   
8164  O O   . ALA A 1119 ? 0.2326 0.2423 0.2079 0.0176  -0.0160 -0.0136 1117 ALA A O   
8165  C CB  . ALA A 1119 ? 0.2250 0.2445 0.2020 0.0185  -0.0204 -0.0145 1117 ALA A CB  
8166  N N   . ALA A 1120 ? 0.1934 0.2066 0.1661 0.0188  -0.0197 -0.0188 1118 ALA A N   
8167  C CA  . ALA A 1120 ? 0.1838 0.1957 0.1537 0.0199  -0.0183 -0.0191 1118 ALA A CA  
8168  C C   . ALA A 1120 ? 0.2038 0.2098 0.1755 0.0182  -0.0172 -0.0191 1118 ALA A C   
8169  O O   . ALA A 1120 ? 0.2068 0.2109 0.1775 0.0184  -0.0150 -0.0170 1118 ALA A O   
8170  C CB  . ALA A 1120 ? 0.1960 0.2108 0.1633 0.0214  -0.0202 -0.0230 1118 ALA A CB  
8171  N N   . ALA A 1121 ? 0.2222 0.2255 0.1969 0.0163  -0.0189 -0.0210 1119 ALA A N   
8172  C CA  . ALA A 1121 ? 0.2313 0.2296 0.2080 0.0145  -0.0182 -0.0208 1119 ALA A CA  
8173  C C   . ALA A 1121 ? 0.1939 0.1909 0.1720 0.0133  -0.0158 -0.0173 1119 ALA A C   
8174  O O   . ALA A 1121 ? 0.1927 0.1869 0.1705 0.0129  -0.0140 -0.0162 1119 ALA A O   
8175  C CB  . ALA A 1121 ? 0.2134 0.2096 0.1937 0.0126  -0.0209 -0.0232 1119 ALA A CB  
8176  N N   . LEU A 1122 ? 0.2081 0.2075 0.1881 0.0128  -0.0158 -0.0159 1120 LEU A N   
8177  C CA  . LEU A 1122 ? 0.1881 0.1871 0.1699 0.0119  -0.0137 -0.0133 1120 LEU A CA  
8178  C C   . LEU A 1122 ? 0.2080 0.2072 0.1878 0.0137  -0.0115 -0.0113 1120 LEU A C   
8179  O O   . LEU A 1122 ? 0.2177 0.2150 0.1982 0.0132  -0.0096 -0.0099 1120 LEU A O   
8180  C CB  . LEU A 1122 ? 0.2131 0.2152 0.1977 0.0112  -0.0144 -0.0126 1120 LEU A CB  
8181  C CG  . LEU A 1122 ? 0.2356 0.2379 0.2234 0.0090  -0.0165 -0.0138 1120 LEU A CG  
8182  C CD1 . LEU A 1122 ? 0.2526 0.2588 0.2428 0.0087  -0.0170 -0.0131 1120 LEU A CD1 
8183  C CD2 . LEU A 1122 ? 0.2207 0.2203 0.2105 0.0067  -0.0157 -0.0131 1120 LEU A CD2 
8184  N N   . ALA A 1123 ? 0.2126 0.2145 0.1901 0.0157  -0.0118 -0.0109 1121 ALA A N   
8185  C CA  . ALA A 1123 ? 0.1849 0.1873 0.1613 0.0172  -0.0101 -0.0083 1121 ALA A CA  
8186  C C   . ALA A 1123 ? 0.2093 0.2085 0.1840 0.0172  -0.0086 -0.0083 1121 ALA A C   
8187  O O   . ALA A 1123 ? 0.2296 0.2280 0.2044 0.0178  -0.0070 -0.0061 1121 ALA A O   
8188  C CB  . ALA A 1123 ? 0.2126 0.2194 0.1868 0.0191  -0.0109 -0.0075 1121 ALA A CB  
8189  N N   . THR A 1124 ? 0.1894 0.1868 0.1629 0.0166  -0.0095 -0.0108 1122 THR A N   
8190  C CA  . THR A 1124 ? 0.1810 0.1755 0.1530 0.0167  -0.0083 -0.0110 1122 THR A CA  
8191  C C   . THR A 1124 ? 0.1926 0.1832 0.1668 0.0146  -0.0079 -0.0113 1122 THR A C   
8192  O O   . THR A 1124 ? 0.2159 0.2039 0.1894 0.0143  -0.0074 -0.0120 1122 THR A O   
8193  C CB  . THR A 1124 ? 0.2093 0.2049 0.1786 0.0179  -0.0096 -0.0136 1122 THR A CB  
8194  O OG1 . THR A 1124 ? 0.2115 0.2077 0.1820 0.0173  -0.0121 -0.0164 1122 THR A OG1 
8195  C CG2 . THR A 1124 ? 0.2166 0.2169 0.1831 0.0201  -0.0093 -0.0123 1122 THR A CG2 
8196  N N   . GLY A 1125 ? 0.2000 0.1909 0.1771 0.0131  -0.0080 -0.0107 1123 GLY A N   
8197  C CA  . GLY A 1125 ? 0.2050 0.1938 0.1843 0.0111  -0.0072 -0.0102 1123 GLY A CA  
8198  C C   . GLY A 1125 ? 0.2121 0.1994 0.1930 0.0091  -0.0089 -0.0116 1123 GLY A C   
8199  O O   . GLY A 1125 ? 0.2194 0.2055 0.2022 0.0072  -0.0084 -0.0107 1123 GLY A O   
8200  N N   . ASN A 1126 ? 0.2063 0.1939 0.1870 0.0095  -0.0112 -0.0136 1124 ASN A N   
8201  C CA  . ASN A 1126 ? 0.1982 0.1837 0.1811 0.0078  -0.0134 -0.0151 1124 ASN A CA  
8202  C C   . ASN A 1126 ? 0.1914 0.1785 0.1780 0.0057  -0.0147 -0.0145 1124 ASN A C   
8203  O O   . ASN A 1126 ? 0.2241 0.2145 0.2111 0.0060  -0.0145 -0.0139 1124 ASN A O   
8204  C CB  . ASN A 1126 ? 0.1913 0.1767 0.1730 0.0094  -0.0156 -0.0183 1124 ASN A CB  
8205  C CG  . ASN A 1126 ? 0.2103 0.1950 0.1884 0.0115  -0.0143 -0.0190 1124 ASN A CG  
8206  O OD1 . ASN A 1126 ? 0.2224 0.2041 0.2007 0.0111  -0.0137 -0.0189 1124 ASN A OD1 
8207  N ND2 . ASN A 1126 ? 0.1946 0.1827 0.1696 0.0138  -0.0138 -0.0192 1124 ASN A ND2 
8208  N N   . SER A 1127 ? 0.2143 0.1994 0.2041 0.0034  -0.0163 -0.0145 1125 SER A N   
8209  C CA  . SER A 1127 ? 0.2245 0.2110 0.2184 0.0013  -0.0186 -0.0144 1125 SER A CA  
8210  C C   . SER A 1127 ? 0.2083 0.1936 0.2030 0.0020  -0.0218 -0.0177 1125 SER A C   
8211  O O   . SER A 1127 ? 0.2153 0.1990 0.2073 0.0041  -0.0221 -0.0201 1125 SER A O   
8212  C CB  . SER A 1127 ? 0.2686 0.2543 0.2663 -0.0018 -0.0189 -0.0120 1125 SER A CB  
8213  O OG  . SER A 1127 ? 0.2803 0.2618 0.2786 -0.0021 -0.0199 -0.0127 1125 SER A OG  
8214  N N   . VAL A 1128 ? 0.2353 0.2218 0.2338 0.0004  -0.0244 -0.0180 1126 VAL A N   
8215  C CA  . VAL A 1128 ? 0.2156 0.2013 0.2154 0.0011  -0.0278 -0.0217 1126 VAL A CA  
8216  C C   . VAL A 1128 ? 0.2530 0.2371 0.2591 -0.0019 -0.0311 -0.0214 1126 VAL A C   
8217  O O   . VAL A 1128 ? 0.2511 0.2367 0.2604 -0.0046 -0.0307 -0.0180 1126 VAL A O   
8218  C CB  . VAL A 1128 ? 0.2481 0.2379 0.2457 0.0029  -0.0282 -0.0232 1126 VAL A CB  
8219  C CG1 . VAL A 1128 ? 0.2602 0.2518 0.2522 0.0058  -0.0253 -0.0229 1126 VAL A CG1 
8220  C CG2 . VAL A 1128 ? 0.2719 0.2650 0.2725 0.0010  -0.0282 -0.0208 1126 VAL A CG2 
8221  N N   . ALA A 1129 ? 0.2185 0.1999 0.2268 -0.0014 -0.0345 -0.0250 1127 ALA A N   
8222  C CA  . ALA A 1129 ? 0.2564 0.2367 0.2714 -0.0039 -0.0385 -0.0255 1127 ALA A CA  
8223  C C   . ALA A 1129 ? 0.2623 0.2444 0.2769 -0.0019 -0.0412 -0.0301 1127 ALA A C   
8224  O O   . ALA A 1129 ? 0.2735 0.2549 0.2853 0.0009  -0.0419 -0.0343 1127 ALA A O   
8225  C CB  . ALA A 1129 ? 0.2949 0.2700 0.3144 -0.0052 -0.0409 -0.0260 1127 ALA A CB  
8226  N N   . ILE A 1130 ? 0.2542 0.2394 0.2715 -0.0034 -0.0425 -0.0293 1128 ILE A N   
8227  C CA  . ILE A 1130 ? 0.2616 0.2494 0.2783 -0.0017 -0.0449 -0.0333 1128 ILE A CA  
8228  C C   . ILE A 1130 ? 0.2929 0.2780 0.3167 -0.0033 -0.0500 -0.0361 1128 ILE A C   
8229  O O   . ILE A 1130 ? 0.2941 0.2779 0.3241 -0.0068 -0.0516 -0.0330 1128 ILE A O   
8230  C CB  . ILE A 1130 ? 0.2490 0.2420 0.2644 -0.0020 -0.0435 -0.0311 1128 ILE A CB  
8231  C CG1 . ILE A 1130 ? 0.2650 0.2601 0.2750 -0.0007 -0.0386 -0.0279 1128 ILE A CG1 
8232  C CG2 . ILE A 1130 ? 0.2350 0.2312 0.2488 0.0002  -0.0457 -0.0353 1128 ILE A CG2 
8233  C CD1 . ILE A 1130 ? 0.2662 0.2661 0.2761 -0.0013 -0.0372 -0.0252 1128 ILE A CD1 
8234  N N   . ASP A 1131 ? 0.2837 0.2685 0.3070 -0.0009 -0.0528 -0.0419 1129 ASP A N   
8235  C CA  . ASP A 1131 ? 0.2791 0.2614 0.3095 -0.0019 -0.0582 -0.0457 1129 ASP A CA  
8236  C C   . ASP A 1131 ? 0.2916 0.2764 0.3269 -0.0046 -0.0603 -0.0439 1129 ASP A C   
8237  O O   . ASP A 1131 ? 0.2914 0.2810 0.3236 -0.0034 -0.0600 -0.0450 1129 ASP A O   
8238  C CB  . ASP A 1131 ? 0.2837 0.2672 0.3115 0.0019  -0.0604 -0.0529 1129 ASP A CB  
8239  C CG  . ASP A 1131 ? 0.3325 0.3134 0.3681 0.0011  -0.0664 -0.0577 1129 ASP A CG  
8240  O OD1 . ASP A 1131 ? 0.2972 0.2734 0.3404 -0.0020 -0.0688 -0.0555 1129 ASP A OD1 
8241  O OD2 . ASP A 1131 ? 0.2917 0.2755 0.3261 0.0037  -0.0688 -0.0637 1129 ASP A OD2 
8242  N N   . ALA A 1132 ? 0.3049 0.2868 0.3480 -0.0085 -0.0626 -0.0407 1130 ALA A N   
8243  C CA  . ALA A 1132 ? 0.3219 0.3064 0.3703 -0.0114 -0.0648 -0.0386 1130 ALA A CA  
8244  C C   . ALA A 1132 ? 0.3307 0.3155 0.3827 -0.0105 -0.0698 -0.0444 1130 ALA A C   
8245  O O   . ALA A 1132 ? 0.3871 0.3755 0.4413 -0.0118 -0.0711 -0.0438 1130 ALA A O   
8246  C CB  . ALA A 1132 ? 0.3565 0.3384 0.4128 -0.0159 -0.0661 -0.0333 1130 ALA A CB  
8247  N N   . ALA A 1133 ? 0.3312 0.3128 0.3840 -0.0082 -0.0726 -0.0504 1131 ALA A N   
8248  C CA  . ALA A 1133 ? 0.3396 0.3219 0.3957 -0.0068 -0.0775 -0.0570 1131 ALA A CA  
8249  C C   . ALA A 1133 ? 0.3634 0.3521 0.4118 -0.0036 -0.0759 -0.0600 1131 ALA A C   
8250  O O   . ALA A 1133 ? 0.3860 0.3769 0.4366 -0.0026 -0.0797 -0.0651 1131 ALA A O   
8251  C CB  . ALA A 1133 ? 0.3379 0.3154 0.3969 -0.0049 -0.0810 -0.0631 1131 ALA A CB  
8252  N N   . SER A 1134 ? 0.3316 0.3236 0.3715 -0.0019 -0.0705 -0.0569 1132 SER A N   
8253  C CA  . SER A 1134 ? 0.3166 0.3152 0.3499 0.0008  -0.0688 -0.0585 1132 SER A CA  
8254  C C   . SER A 1134 ? 0.3146 0.3169 0.3507 -0.0013 -0.0699 -0.0562 1132 SER A C   
8255  O O   . SER A 1134 ? 0.3013 0.3090 0.3339 0.0007  -0.0703 -0.0586 1132 SER A O   
8256  C CB  . SER A 1134 ? 0.3029 0.3036 0.3279 0.0025  -0.0630 -0.0547 1132 SER A CB  
8257  O OG  . SER A 1134 ? 0.3085 0.3089 0.3347 -0.0003 -0.0601 -0.0481 1132 SER A OG  
8258  N N   . GLY A 1135 ? 0.3287 0.3291 0.3711 -0.0053 -0.0703 -0.0514 1133 GLY A N   
8259  C CA  . GLY A 1135 ? 0.3202 0.3245 0.3655 -0.0074 -0.0711 -0.0487 1133 GLY A CA  
8260  C C   . GLY A 1135 ? 0.3371 0.3467 0.3759 -0.0063 -0.0664 -0.0451 1133 GLY A C   
8261  O O   . GLY A 1135 ? 0.3421 0.3563 0.3820 -0.0069 -0.0671 -0.0443 1133 GLY A O   
8262  N N   . LEU A 1136 ? 0.2900 0.2993 0.3226 -0.0046 -0.0619 -0.0429 1134 LEU A N   
8263  C CA  . LEU A 1136 ? 0.3423 0.3562 0.3691 -0.0030 -0.0578 -0.0399 1134 LEU A CA  
8264  C C   . LEU A 1136 ? 0.3494 0.3637 0.3777 -0.0055 -0.0545 -0.0338 1134 LEU A C   
8265  O O   . LEU A 1136 ? 0.3071 0.3242 0.3310 -0.0041 -0.0508 -0.0312 1134 LEU A O   
8266  C CB  . LEU A 1136 ? 0.2743 0.2885 0.2934 0.0007  -0.0551 -0.0415 1134 LEU A CB  
8267  C CG  . LEU A 1136 ? 0.2897 0.3063 0.3059 0.0037  -0.0576 -0.0474 1134 LEU A CG  
8268  C CD1 . LEU A 1136 ? 0.2733 0.2902 0.2825 0.0069  -0.0549 -0.0484 1134 LEU A CD1 
8269  C CD2 . LEU A 1136 ? 0.3231 0.3459 0.3383 0.0045  -0.0587 -0.0478 1134 LEU A CD2 
8270  N N   . GLN A 1137 ? 0.3260 0.3379 0.3610 -0.0091 -0.0560 -0.0315 1135 GLN A N   
8271  C CA  . GLN A 1137 ? 0.3627 0.3761 0.3993 -0.0115 -0.0530 -0.0259 1135 GLN A CA  
8272  C C   . GLN A 1137 ? 0.3189 0.3385 0.3540 -0.0110 -0.0509 -0.0237 1135 GLN A C   
8273  O O   . GLN A 1137 ? 0.3156 0.3371 0.3480 -0.0105 -0.0469 -0.0205 1135 GLN A O   
8274  C CB  . GLN A 1137 ? 0.3666 0.3784 0.4115 -0.0157 -0.0558 -0.0234 1135 GLN A CB  
8275  C CG  . GLN A 1137 ? 0.3426 0.3483 0.3897 -0.0168 -0.0569 -0.0236 1135 GLN A CG  
8276  C CD  . GLN A 1137 ? 0.3214 0.3229 0.3710 -0.0158 -0.0615 -0.0291 1135 GLN A CD  
8277  O OE1 . GLN A 1137 ? 0.3635 0.3669 0.4120 -0.0140 -0.0636 -0.0332 1135 GLN A OE1 
8278  N NE2 . GLN A 1137 ? 0.3632 0.3593 0.4165 -0.0170 -0.0634 -0.0293 1135 GLN A NE2 
8279  N N   . ALA A 1138 ? 0.3273 0.3501 0.3644 -0.0109 -0.0536 -0.0255 1136 ALA A N   
8280  C CA  . ALA A 1138 ? 0.3405 0.3693 0.3770 -0.0105 -0.0519 -0.0233 1136 ALA A CA  
8281  C C   . ALA A 1138 ? 0.3657 0.3963 0.3951 -0.0068 -0.0486 -0.0237 1136 ALA A C   
8282  O O   . ALA A 1138 ? 0.3859 0.4209 0.4148 -0.0062 -0.0467 -0.0215 1136 ALA A O   
8283  C CB  . ALA A 1138 ? 0.3294 0.3613 0.3700 -0.0114 -0.0558 -0.0252 1136 ALA A CB  
8284  N N   . SER A 1139 ? 0.3521 0.3797 0.3764 -0.0042 -0.0481 -0.0263 1137 SER A N   
8285  C CA  . SER A 1139 ? 0.3600 0.3893 0.3781 -0.0009 -0.0451 -0.0258 1137 SER A CA  
8286  C C   . SER A 1139 ? 0.3359 0.3640 0.3523 -0.0009 -0.0409 -0.0223 1137 SER A C   
8287  O O   . SER A 1139 ? 0.3277 0.3573 0.3402 0.0015  -0.0384 -0.0213 1137 SER A O   
8288  C CB  . SER A 1139 ? 0.3082 0.3356 0.3215 0.0017  -0.0460 -0.0295 1137 SER A CB  
8289  O OG  . SER A 1139 ? 0.3392 0.3691 0.3531 0.0025  -0.0497 -0.0332 1137 SER A OG  
8290  N N   . LEU A 1140 ? 0.3265 0.3522 0.3462 -0.0036 -0.0403 -0.0204 1138 LEU A N   
8291  C CA  . LEU A 1140 ? 0.3496 0.3744 0.3678 -0.0036 -0.0365 -0.0176 1138 LEU A CA  
8292  C C   . LEU A 1140 ? 0.3857 0.4137 0.4084 -0.0063 -0.0355 -0.0143 1138 LEU A C   
8293  O O   . LEU A 1140 ? 0.4141 0.4408 0.4380 -0.0080 -0.0339 -0.0123 1138 LEU A O   
8294  C CB  . LEU A 1140 ? 0.3608 0.3800 0.3775 -0.0039 -0.0362 -0.0183 1138 LEU A CB  
8295  C CG  . LEU A 1140 ? 0.3607 0.3770 0.3718 -0.0009 -0.0354 -0.0205 1138 LEU A CG  
8296  C CD1 . LEU A 1140 ? 0.3359 0.3475 0.3467 -0.0018 -0.0343 -0.0200 1138 LEU A CD1 
8297  C CD2 . LEU A 1140 ? 0.3090 0.3280 0.3158 0.0018  -0.0325 -0.0194 1138 LEU A CD2 
8298  N N   . LYS A 1141 ? 0.3701 0.4031 0.3957 -0.0068 -0.0364 -0.0137 1139 LYS A N   
8299  C CA  . LYS A 1141 ? 0.4466 0.4842 0.4766 -0.0092 -0.0354 -0.0107 1139 LYS A CA  
8300  C C   . LYS A 1141 ? 0.4128 0.4532 0.4407 -0.0074 -0.0315 -0.0091 1139 LYS A C   
8301  O O   . LYS A 1141 ? 0.3864 0.4271 0.4110 -0.0044 -0.0303 -0.0101 1139 LYS A O   
8302  C CB  . LYS A 1141 ? 0.4549 0.4971 0.4890 -0.0102 -0.0379 -0.0108 1139 LYS A CB  
8303  N N   . ASN A 1142 ? 0.3934 0.4364 0.4238 -0.0094 -0.0296 -0.0067 1140 ASN A N   
8304  C CA  . ASN A 1142 ? 0.3984 0.4454 0.4281 -0.0080 -0.0262 -0.0056 1140 ASN A CA  
8305  C C   . ASN A 1142 ? 0.3900 0.4327 0.4147 -0.0053 -0.0238 -0.0065 1140 ASN A C   
8306  O O   . ASN A 1142 ? 0.3610 0.4054 0.3844 -0.0028 -0.0219 -0.0068 1140 ASN A O   
8307  C CB  . ASN A 1142 ? 0.4363 0.4888 0.4677 -0.0065 -0.0262 -0.0059 1140 ASN A CB  
8308  C CG  . ASN A 1142 ? 0.5209 0.5773 0.5570 -0.0089 -0.0289 -0.0052 1140 ASN A CG  
8309  O OD1 . ASN A 1142 ? 0.5407 0.5968 0.5768 -0.0081 -0.0313 -0.0067 1140 ASN A OD1 
8310  N ND2 . ASN A 1142 ? 0.4922 0.5532 0.5326 -0.0119 -0.0286 -0.0029 1140 ASN A ND2 
8311  N N   . LEU A 1143 ? 0.3910 0.4282 0.4134 -0.0059 -0.0240 -0.0068 1141 LEU A N   
8312  C CA  . LEU A 1143 ? 0.3599 0.3933 0.3780 -0.0036 -0.0217 -0.0074 1141 LEU A CA  
8313  C C   . LEU A 1143 ? 0.3859 0.4223 0.4045 -0.0035 -0.0186 -0.0061 1141 LEU A C   
8314  O O   . LEU A 1143 ? 0.3654 0.4056 0.3870 -0.0060 -0.0182 -0.0045 1141 LEU A O   
8315  C CB  . LEU A 1143 ? 0.3206 0.3479 0.3366 -0.0043 -0.0226 -0.0081 1141 LEU A CB  
8316  C CG  . LEU A 1143 ? 0.3094 0.3328 0.3229 -0.0030 -0.0250 -0.0105 1141 LEU A CG  
8317  C CD1 . LEU A 1143 ? 0.3316 0.3496 0.3443 -0.0041 -0.0258 -0.0111 1141 LEU A CD1 
8318  C CD2 . LEU A 1143 ? 0.3122 0.3352 0.3215 0.0005  -0.0237 -0.0115 1141 LEU A CD2 
8319  N N   . PRO A 1144 ? 0.3478 0.3830 0.3637 -0.0007 -0.0166 -0.0068 1142 PRO A N   
8320  C CA  . PRO A 1144 ? 0.3647 0.4016 0.3807 -0.0005 -0.0138 -0.0063 1142 PRO A CA  
8321  C C   . PRO A 1144 ? 0.3449 0.3795 0.3603 -0.0028 -0.0134 -0.0052 1142 PRO A C   
8322  O O   . PRO A 1144 ? 0.3333 0.3626 0.3467 -0.0033 -0.0148 -0.0055 1142 PRO A O   
8323  C CB  . PRO A 1144 ? 0.3532 0.3869 0.3663 0.0028  -0.0125 -0.0073 1142 PRO A CB  
8324  C CG  . PRO A 1144 ? 0.3679 0.4011 0.3804 0.0044  -0.0144 -0.0079 1142 PRO A CG  
8325  C CD  . PRO A 1144 ? 0.3626 0.3948 0.3754 0.0022  -0.0169 -0.0080 1142 PRO A CD  
8326  N N   . GLN A 1145 ? 0.3325 0.3716 0.3497 -0.0042 -0.0117 -0.0041 1143 GLN A N   
8327  C CA  . GLN A 1145 ? 0.3398 0.3775 0.3567 -0.0066 -0.0114 -0.0026 1143 GLN A CA  
8328  C C   . GLN A 1145 ? 0.3171 0.3480 0.3300 -0.0051 -0.0107 -0.0035 1143 GLN A C   
8329  O O   . GLN A 1145 ? 0.3184 0.3455 0.3307 -0.0068 -0.0116 -0.0026 1143 GLN A O   
8330  C CB  . GLN A 1145 ? 0.3849 0.4298 0.4039 -0.0077 -0.0093 -0.0013 1143 GLN A CB  
8331  N N   . THR A 1146 ? 0.3172 0.3464 0.3277 -0.0021 -0.0091 -0.0050 1144 THR A N   
8332  C CA  . THR A 1146 ? 0.3656 0.3889 0.3725 -0.0007 -0.0084 -0.0056 1144 THR A CA  
8333  C C   . THR A 1146 ? 0.3071 0.3251 0.3121 -0.0007 -0.0105 -0.0061 1144 THR A C   
8334  O O   . THR A 1146 ? 0.3208 0.3342 0.3237 -0.0010 -0.0106 -0.0061 1144 THR A O   
8335  C CB  . THR A 1146 ? 0.3472 0.3699 0.3528 0.0025  -0.0069 -0.0068 1144 THR A CB  
8336  O OG1 . THR A 1146 ? 0.2939 0.3178 0.3004 0.0040  -0.0081 -0.0074 1144 THR A OG1 
8337  C CG2 . THR A 1146 ? 0.3355 0.3628 0.3430 0.0028  -0.0048 -0.0072 1144 THR A CG2 
8338  N N   . VAL A 1147 ? 0.2891 0.3078 0.2948 -0.0002 -0.0124 -0.0068 1145 VAL A N   
8339  C CA  . VAL A 1147 ? 0.2769 0.2916 0.2809 0.0000  -0.0146 -0.0079 1145 VAL A CA  
8340  C C   . VAL A 1147 ? 0.2922 0.3062 0.2989 -0.0030 -0.0168 -0.0074 1145 VAL A C   
8341  O O   . VAL A 1147 ? 0.2705 0.2799 0.2761 -0.0033 -0.0180 -0.0082 1145 VAL A O   
8342  C CB  . VAL A 1147 ? 0.2689 0.2853 0.2727 0.0018  -0.0160 -0.0090 1145 VAL A CB  
8343  C CG1 . VAL A 1147 ? 0.2571 0.2703 0.2590 0.0022  -0.0184 -0.0107 1145 VAL A CG1 
8344  C CG2 . VAL A 1147 ? 0.2799 0.2970 0.2820 0.0046  -0.0142 -0.0089 1145 VAL A CG2 
8345  N N   . GLY A 1148 ? 0.2791 0.2976 0.2898 -0.0053 -0.0174 -0.0060 1146 GLY A N   
8346  C CA  . GLY A 1148 ? 0.2688 0.2868 0.2830 -0.0085 -0.0195 -0.0047 1146 GLY A CA  
8347  C C   . GLY A 1148 ? 0.2856 0.3003 0.2993 -0.0098 -0.0189 -0.0035 1146 GLY A C   
8348  O O   . GLY A 1148 ? 0.2841 0.2953 0.2996 -0.0115 -0.0213 -0.0034 1146 GLY A O   
8349  N N   . LEU A 1149 ? 0.2722 0.2881 0.2838 -0.0090 -0.0159 -0.0027 1147 LEU A N   
8350  C CA  . LEU A 1149 ? 0.2936 0.3066 0.3044 -0.0101 -0.0152 -0.0016 1147 LEU A CA  
8351  C C   . LEU A 1149 ? 0.2889 0.2949 0.2972 -0.0087 -0.0164 -0.0035 1147 LEU A C   
8352  O O   . LEU A 1149 ? 0.3107 0.3135 0.3198 -0.0102 -0.0172 -0.0026 1147 LEU A O   
8353  C CB  . LEU A 1149 ? 0.2973 0.3126 0.3059 -0.0089 -0.0118 -0.0012 1147 LEU A CB  
8354  C CG  . LEU A 1149 ? 0.4129 0.4360 0.4239 -0.0102 -0.0103 0.0005  1147 LEU A CG  
8355  C CD1 . LEU A 1149 ? 0.4000 0.4245 0.4087 -0.0086 -0.0073 -0.0002 1147 LEU A CD1 
8356  C CD2 . LEU A 1149 ? 0.4270 0.4531 0.4418 -0.0140 -0.0115 0.0036  1147 LEU A CD2 
8357  N N   . ARG A 1150 ? 0.2833 0.2875 0.2887 -0.0060 -0.0166 -0.0060 1148 ARG A N   
8358  C CA  . ARG A 1150 ? 0.2707 0.2696 0.2734 -0.0043 -0.0175 -0.0081 1148 ARG A CA  
8359  C C   . ARG A 1150 ? 0.2743 0.2714 0.2791 -0.0048 -0.0211 -0.0100 1148 ARG A C   
8360  O O   . ARG A 1150 ? 0.2726 0.2658 0.2756 -0.0035 -0.0222 -0.0122 1148 ARG A O   
8361  C CB  . ARG A 1150 ? 0.2694 0.2682 0.2678 -0.0009 -0.0159 -0.0095 1148 ARG A CB  
8362  C CG  . ARG A 1150 ? 0.2672 0.2665 0.2637 0.0001  -0.0127 -0.0084 1148 ARG A CG  
8363  C CD  . ARG A 1150 ? 0.2764 0.2718 0.2690 0.0022  -0.0119 -0.0094 1148 ARG A CD  
8364  N NE  . ARG A 1150 ? 0.2500 0.2458 0.2411 0.0035  -0.0092 -0.0085 1148 ARG A NE  
8365  C CZ  . ARG A 1150 ? 0.2513 0.2465 0.2398 0.0059  -0.0082 -0.0089 1148 ARG A CZ  
8366  N NH1 . ARG A 1150 ? 0.2160 0.2107 0.2026 0.0075  -0.0095 -0.0100 1148 ARG A NH1 
8367  N NH2 . ARG A 1150 ? 0.2321 0.2276 0.2203 0.0069  -0.0061 -0.0080 1148 ARG A NH2 
8368  N N   . VAL A 1151 ? 0.2496 0.2495 0.2582 -0.0067 -0.0230 -0.0093 1149 VAL A N   
8369  C CA  . VAL A 1151 ? 0.2655 0.2642 0.2764 -0.0069 -0.0266 -0.0116 1149 VAL A CA  
8370  C C   . VAL A 1151 ? 0.3148 0.3125 0.3316 -0.0104 -0.0293 -0.0100 1149 VAL A C   
8371  O O   . VAL A 1151 ? 0.3120 0.3134 0.3322 -0.0130 -0.0288 -0.0068 1149 VAL A O   
8372  C CB  . VAL A 1151 ? 0.2658 0.2688 0.2767 -0.0060 -0.0271 -0.0123 1149 VAL A CB  
8373  C CG1 . VAL A 1151 ? 0.2662 0.2684 0.2803 -0.0067 -0.0312 -0.0147 1149 VAL A CG1 
8374  C CG2 . VAL A 1151 ? 0.2681 0.2718 0.2738 -0.0026 -0.0250 -0.0137 1149 VAL A CG2 
8375  N N   . SER A 1152 ? 0.2890 0.2822 0.3075 -0.0105 -0.0323 -0.0123 1150 SER A N   
8376  C CA  . SER A 1152 ? 0.3119 0.3036 0.3372 -0.0137 -0.0359 -0.0112 1150 SER A CA  
8377  C C   . SER A 1152 ? 0.3316 0.3212 0.3585 -0.0126 -0.0397 -0.0156 1150 SER A C   
8378  O O   . SER A 1152 ? 0.2898 0.2784 0.3122 -0.0093 -0.0395 -0.0194 1150 SER A O   
8379  C CB  . SER A 1152 ? 0.3197 0.3073 0.3470 -0.0152 -0.0363 -0.0095 1150 SER A CB  
8380  O OG  . SER A 1152 ? 0.3668 0.3496 0.3913 -0.0126 -0.0368 -0.0132 1150 SER A OG  
8381  N N   . TRP A 1153 ? 0.3230 0.3126 0.3567 -0.0153 -0.0434 -0.0149 1151 TRP A N   
8382  C CA  . TRP A 1153 ? 0.3372 0.3247 0.3740 -0.0147 -0.0478 -0.0193 1151 TRP A CA  
8383  C C   . TRP A 1153 ? 0.3435 0.3253 0.3861 -0.0163 -0.0513 -0.0199 1151 TRP A C   
8384  O O   . TRP A 1153 ? 0.3800 0.3612 0.4275 -0.0196 -0.0518 -0.0154 1151 TRP A O   
8385  C CB  . TRP A 1153 ? 0.3045 0.2960 0.3455 -0.0166 -0.0498 -0.0185 1151 TRP A CB  
8386  C CG  . TRP A 1153 ? 0.3375 0.3340 0.3733 -0.0145 -0.0472 -0.0189 1151 TRP A CG  
8387  C CD1 . TRP A 1153 ? 0.3291 0.3302 0.3626 -0.0149 -0.0434 -0.0153 1151 TRP A CD1 
8388  C CD2 . TRP A 1153 ? 0.2934 0.2912 0.3259 -0.0116 -0.0482 -0.0233 1151 TRP A CD2 
8389  N NE1 . TRP A 1153 ? 0.3364 0.3411 0.3659 -0.0124 -0.0422 -0.0170 1151 TRP A NE1 
8390  C CE2 . TRP A 1153 ? 0.3077 0.3106 0.3364 -0.0104 -0.0451 -0.0216 1151 TRP A CE2 
8391  C CE3 . TRP A 1153 ? 0.2925 0.2882 0.3252 -0.0097 -0.0516 -0.0287 1151 TRP A CE3 
8392  C CZ2 . TRP A 1153 ? 0.3057 0.3115 0.3307 -0.0077 -0.0452 -0.0245 1151 TRP A CZ2 
8393  C CZ3 . TRP A 1153 ? 0.3123 0.3116 0.3409 -0.0070 -0.0516 -0.0317 1151 TRP A CZ3 
8394  C CH2 . TRP A 1153 ? 0.2958 0.3000 0.3206 -0.0061 -0.0485 -0.0293 1151 TRP A CH2 
8395  N N   . SER A 1154 ? 0.3220 0.3002 0.3642 -0.0138 -0.0539 -0.0254 1152 SER A N   
8396  C CA  . SER A 1154 ? 0.3444 0.3168 0.3920 -0.0145 -0.0573 -0.0269 1152 SER A CA  
8397  C C   . SER A 1154 ? 0.3494 0.3199 0.4031 -0.0145 -0.0628 -0.0316 1152 SER A C   
8398  O O   . SER A 1154 ? 0.3184 0.2903 0.3686 -0.0114 -0.0636 -0.0371 1152 SER A O   
8399  C CB  . SER A 1154 ? 0.3329 0.3025 0.3749 -0.0112 -0.0553 -0.0298 1152 SER A CB  
8400  O OG  . SER A 1154 ? 0.3563 0.3203 0.4040 -0.0118 -0.0586 -0.0311 1152 SER A OG  
8401  N N   . LYS A 1155 ? 0.3414 0.3091 0.4045 -0.0181 -0.0669 -0.0294 1153 LYS A N   
8402  C CA  . LYS A 1155 ? 0.3620 0.3263 0.4325 -0.0182 -0.0729 -0.0343 1153 LYS A CA  
8403  C C   . LYS A 1155 ? 0.4101 0.3683 0.4834 -0.0166 -0.0754 -0.0380 1153 LYS A C   
8404  O O   . LYS A 1155 ? 0.4925 0.4489 0.5669 -0.0138 -0.0787 -0.0451 1153 LYS A O   
8405  C CB  . LYS A 1155 ? 0.3771 0.3415 0.4575 -0.0230 -0.0766 -0.0298 1153 LYS A CB  
8406  N N   . ASP A 1156 ? 0.3831 0.3385 0.4575 -0.0181 -0.0739 -0.0336 1154 ASP A N   
8407  C CA  . ASP A 1156 ? 0.3663 0.3159 0.4434 -0.0167 -0.0759 -0.0364 1154 ASP A CA  
8408  C C   . ASP A 1156 ? 0.4022 0.3529 0.4695 -0.0138 -0.0705 -0.0363 1154 ASP A C   
8409  O O   . ASP A 1156 ? 0.3890 0.3401 0.4547 -0.0156 -0.0672 -0.0305 1154 ASP A O   
8410  C CB  . ASP A 1156 ? 0.4084 0.3540 0.4955 -0.0210 -0.0790 -0.0310 1154 ASP A CB  
8411  C CG  . ASP A 1156 ? 0.4738 0.4130 0.5652 -0.0195 -0.0818 -0.0341 1154 ASP A CG  
8412  O OD1 . ASP A 1156 ? 0.4619 0.4003 0.5476 -0.0151 -0.0807 -0.0402 1154 ASP A OD1 
8413  O OD2 . ASP A 1156 ? 0.4887 0.4240 0.5895 -0.0228 -0.0853 -0.0301 1154 ASP A OD2 
8414  N N   . TRP A 1157 ? 0.3719 0.3236 0.4330 -0.0093 -0.0696 -0.0428 1155 TRP A N   
8415  C CA  . TRP A 1157 ? 0.3141 0.2674 0.3660 -0.0065 -0.0644 -0.0427 1155 TRP A CA  
8416  C C   . TRP A 1157 ? 0.3634 0.3121 0.4174 -0.0070 -0.0641 -0.0406 1155 TRP A C   
8417  O O   . TRP A 1157 ? 0.3925 0.3422 0.4409 -0.0069 -0.0596 -0.0369 1155 TRP A O   
8418  C CB  . TRP A 1157 ? 0.3360 0.2915 0.3820 -0.0017 -0.0642 -0.0500 1155 TRP A CB  
8419  C CG  . TRP A 1157 ? 0.3112 0.2714 0.3550 -0.0007 -0.0649 -0.0527 1155 TRP A CG  
8420  C CD1 . TRP A 1157 ? 0.3002 0.2632 0.3451 -0.0034 -0.0647 -0.0490 1155 TRP A CD1 
8421  C CD2 . TRP A 1157 ? 0.2946 0.2580 0.3345 0.0032  -0.0659 -0.0597 1155 TRP A CD2 
8422  N NE1 . TRP A 1157 ? 0.3210 0.2884 0.3632 -0.0013 -0.0656 -0.0532 1155 TRP A NE1 
8423  C CE2 . TRP A 1157 ? 0.3093 0.2772 0.3482 0.0027  -0.0663 -0.0597 1155 TRP A CE2 
8424  C CE3 . TRP A 1157 ? 0.3095 0.2732 0.3467 0.0072  -0.0665 -0.0660 1155 TRP A CE3 
8425  C CZ2 . TRP A 1157 ? 0.3034 0.2759 0.3385 0.0060  -0.0674 -0.0657 1155 TRP A CZ2 
8426  C CZ3 . TRP A 1157 ? 0.2949 0.2637 0.3282 0.0105  -0.0675 -0.0720 1155 TRP A CZ3 
8427  C CH2 . TRP A 1157 ? 0.3176 0.2908 0.3499 0.0099  -0.0680 -0.0717 1155 TRP A CH2 
8428  N N   . ALA A 1158 ? 0.3355 0.2789 0.3978 -0.0074 -0.0691 -0.0433 1156 ALA A N   
8429  C CA  . ALA A 1158 ? 0.3642 0.3032 0.4289 -0.0076 -0.0691 -0.0416 1156 ALA A CA  
8430  C C   . ALA A 1158 ? 0.3899 0.3288 0.4569 -0.0120 -0.0674 -0.0328 1156 ALA A C   
8431  O O   . ALA A 1158 ? 0.4488 0.3861 0.5143 -0.0121 -0.0653 -0.0301 1156 ALA A O   
8432  C CB  . ALA A 1158 ? 0.4132 0.3466 0.4875 -0.0071 -0.0753 -0.0464 1156 ALA A CB  
8433  N N   . ALA A 1159 ? 0.3847 0.3261 0.4552 -0.0156 -0.0681 -0.0284 1157 ALA A N   
8434  C CA  . ALA A 1159 ? 0.4296 0.3725 0.5023 -0.0198 -0.0664 -0.0200 1157 ALA A CA  
8435  C C   . ALA A 1159 ? 0.4330 0.3812 0.4960 -0.0192 -0.0600 -0.0167 1157 ALA A C   
8436  O O   . ALA A 1159 ? 0.3986 0.3483 0.4616 -0.0217 -0.0578 -0.0108 1157 ALA A O   
8437  C CB  . ALA A 1159 ? 0.3987 0.3432 0.4793 -0.0239 -0.0698 -0.0164 1157 ALA A CB  
8438  N N   . ASP A 1160 ? 0.4081 0.3595 0.4634 -0.0161 -0.0573 -0.0205 1158 ASP A N   
8439  C CA  . ASP A 1160 ? 0.4021 0.3587 0.4495 -0.0158 -0.0518 -0.0176 1158 ASP A CA  
8440  C C   . ASP A 1160 ? 0.3617 0.3180 0.4010 -0.0122 -0.0480 -0.0197 1158 ASP A C   
8441  O O   . ASP A 1160 ? 0.3841 0.3443 0.4169 -0.0114 -0.0436 -0.0181 1158 ASP A O   
8442  C CB  . ASP A 1160 ? 0.3568 0.3178 0.4020 -0.0152 -0.0515 -0.0192 1158 ASP A CB  
8443  C CG  . ASP A 1160 ? 0.4141 0.3762 0.4671 -0.0189 -0.0549 -0.0164 1158 ASP A CG  
8444  O OD1 . ASP A 1160 ? 0.4660 0.4273 0.5250 -0.0225 -0.0563 -0.0115 1158 ASP A OD1 
8445  O OD2 . ASP A 1160 ? 0.3871 0.3514 0.4405 -0.0184 -0.0564 -0.0190 1158 ASP A OD2 
8446  N N   . GLY A 1161 ? 0.3389 0.2909 0.3790 -0.0102 -0.0496 -0.0233 1159 GLY A N   
8447  C CA  . GLY A 1161 ? 0.3379 0.2897 0.3711 -0.0070 -0.0461 -0.0251 1159 GLY A CA  
8448  C C   . GLY A 1161 ? 0.3581 0.3089 0.3909 -0.0087 -0.0437 -0.0201 1159 GLY A C   
8449  O O   . GLY A 1161 ? 0.3989 0.3502 0.4362 -0.0123 -0.0443 -0.0149 1159 GLY A O   
8450  N N   . PRO A 1162 ? 0.3216 0.2716 0.3493 -0.0061 -0.0411 -0.0215 1160 PRO A N   
8451  C CA  . PRO A 1162 ? 0.3369 0.2870 0.3596 -0.0019 -0.0403 -0.0271 1160 PRO A CA  
8452  C C   . PRO A 1162 ? 0.3246 0.2796 0.3404 -0.0002 -0.0371 -0.0275 1160 PRO A C   
8453  O O   . PRO A 1162 ? 0.3471 0.3049 0.3599 -0.0015 -0.0338 -0.0235 1160 PRO A O   
8454  C CB  . PRO A 1162 ? 0.3177 0.2657 0.3383 -0.0009 -0.0383 -0.0262 1160 PRO A CB  
8455  C CG  . PRO A 1162 ? 0.3431 0.2924 0.3631 -0.0039 -0.0357 -0.0199 1160 PRO A CG  
8456  C CD  . PRO A 1162 ? 0.3455 0.2951 0.3720 -0.0075 -0.0385 -0.0169 1160 PRO A CD  
8457  N N   . PHE A 1163 ? 0.2706 0.2272 0.2840 0.0027  -0.0380 -0.0326 1161 PHE A N   
8458  C CA  . PHE A 1163 ? 0.2443 0.2057 0.2512 0.0046  -0.0350 -0.0330 1161 PHE A CA  
8459  C C   . PHE A 1163 ? 0.2616 0.2239 0.2626 0.0076  -0.0320 -0.0340 1161 PHE A C   
8460  O O   . PHE A 1163 ? 0.2878 0.2472 0.2897 0.0084  -0.0325 -0.0353 1161 PHE A O   
8461  C CB  . PHE A 1163 ? 0.2528 0.2166 0.2601 0.0060  -0.0377 -0.0373 1161 PHE A CB  
8462  C CG  . PHE A 1163 ? 0.2708 0.2337 0.2844 0.0031  -0.0409 -0.0362 1161 PHE A CG  
8463  C CD1 . PHE A 1163 ? 0.2694 0.2343 0.2833 0.0004  -0.0392 -0.0314 1161 PHE A CD1 
8464  C CD2 . PHE A 1163 ? 0.2554 0.2155 0.2752 0.0029  -0.0457 -0.0401 1161 PHE A CD2 
8465  C CE1 . PHE A 1163 ? 0.3029 0.2677 0.3229 -0.0026 -0.0421 -0.0300 1161 PHE A CE1 
8466  C CE2 . PHE A 1163 ? 0.3033 0.2626 0.3296 -0.0001 -0.0489 -0.0388 1161 PHE A CE2 
8467  C CZ  . PHE A 1163 ? 0.2817 0.2435 0.3080 -0.0029 -0.0470 -0.0335 1161 PHE A CZ  
8468  N N   . ALA A 1164 ? 0.2254 0.1918 0.2207 0.0090  -0.0289 -0.0329 1162 ALA A N   
8469  C CA  . ALA A 1164 ? 0.2370 0.2049 0.2269 0.0115  -0.0259 -0.0333 1162 ALA A CA  
8470  C C   . ALA A 1164 ? 0.2419 0.2146 0.2277 0.0146  -0.0259 -0.0367 1162 ALA A C   
8471  O O   . ALA A 1164 ? 0.2583 0.2336 0.2395 0.0167  -0.0234 -0.0364 1162 ALA A O   
8472  C CB  . ALA A 1164 ? 0.2766 0.2453 0.2637 0.0104  -0.0221 -0.0283 1162 ALA A CB  
8473  N N   . GLY A 1165 ? 0.2296 0.2039 0.2172 0.0149  -0.0288 -0.0397 1163 GLY A N   
8474  C CA  . GLY A 1165 ? 0.2198 0.1995 0.2036 0.0178  -0.0291 -0.0430 1163 GLY A CA  
8475  C C   . GLY A 1165 ? 0.2251 0.2061 0.2118 0.0169  -0.0320 -0.0448 1163 GLY A C   
8476  O O   . GLY A 1165 ? 0.2321 0.2099 0.2234 0.0140  -0.0334 -0.0428 1163 GLY A O   
8477  N N   . ALA A 1166 ? 0.2286 0.2148 0.2125 0.0193  -0.0330 -0.0482 1164 ALA A N   
8478  C CA  . ALA A 1166 ? 0.2239 0.2117 0.2104 0.0186  -0.0360 -0.0503 1164 ALA A CA  
8479  C C   . ALA A 1166 ? 0.2223 0.2174 0.2037 0.0209  -0.0352 -0.0511 1164 ALA A C   
8480  O O   . ALA A 1166 ? 0.2505 0.2499 0.2272 0.0236  -0.0336 -0.0522 1164 ALA A O   
8481  C CB  . ALA A 1166 ? 0.2377 0.2232 0.2294 0.0190  -0.0406 -0.0562 1164 ALA A CB  
8482  N N   . LEU A 1167 ? 0.2182 0.2153 0.2010 0.0197  -0.0363 -0.0503 1165 LEU A N   
8483  C CA  . LEU A 1167 ? 0.2153 0.2194 0.1943 0.0216  -0.0364 -0.0512 1165 LEU A CA  
8484  C C   . LEU A 1167 ? 0.2294 0.2345 0.2121 0.0214  -0.0408 -0.0558 1165 LEU A C   
8485  O O   . LEU A 1167 ? 0.2519 0.2529 0.2399 0.0187  -0.0426 -0.0550 1165 LEU A O   
8486  C CB  . LEU A 1167 ? 0.2180 0.2238 0.1951 0.0205  -0.0336 -0.0454 1165 LEU A CB  
8487  C CG  . LEU A 1167 ? 0.2302 0.2348 0.2044 0.0205  -0.0295 -0.0407 1165 LEU A CG  
8488  C CD1 . LEU A 1167 ? 0.2376 0.2436 0.2116 0.0193  -0.0274 -0.0356 1165 LEU A CD1 
8489  C CD2 . LEU A 1167 ? 0.2412 0.2503 0.2103 0.0235  -0.0281 -0.0417 1165 LEU A CD2 
8490  N N   . VAL A 1168 ? 0.2392 0.2501 0.2193 0.0243  -0.0425 -0.0607 1166 VAL A N   
8491  C CA  . VAL A 1168 ? 0.2442 0.2563 0.2280 0.0245  -0.0470 -0.0663 1166 VAL A CA  
8492  C C   . VAL A 1168 ? 0.2389 0.2595 0.2185 0.0263  -0.0472 -0.0671 1166 VAL A C   
8493  O O   . VAL A 1168 ? 0.2261 0.2529 0.1997 0.0288  -0.0449 -0.0664 1166 VAL A O   
8494  C CB  . VAL A 1168 ? 0.2270 0.2380 0.2129 0.0266  -0.0499 -0.0733 1166 VAL A CB  
8495  C CG1 . VAL A 1168 ? 0.2473 0.2596 0.2377 0.0269  -0.0551 -0.0797 1166 VAL A CG1 
8496  C CG2 . VAL A 1168 ? 0.2316 0.2342 0.2219 0.0248  -0.0498 -0.0720 1166 VAL A CG2 
8497  N N   . GLU A 1169 ? 0.2214 0.2427 0.2043 0.0250  -0.0500 -0.0681 1167 GLU A N   
8498  C CA  . GLU A 1169 ? 0.2312 0.2606 0.2111 0.0266  -0.0511 -0.0697 1167 GLU A CA  
8499  C C   . GLU A 1169 ? 0.2563 0.2870 0.2400 0.0274  -0.0562 -0.0773 1167 GLU A C   
8500  O O   . GLU A 1169 ? 0.2609 0.2854 0.2514 0.0251  -0.0592 -0.0788 1167 GLU A O   
8501  C CB  . GLU A 1169 ? 0.2347 0.2646 0.2153 0.0244  -0.0499 -0.0641 1167 GLU A CB  
8502  C CG  . GLU A 1169 ? 0.2204 0.2586 0.1982 0.0258  -0.0512 -0.0651 1167 GLU A CG  
8503  C CD  . GLU A 1169 ? 0.2525 0.2902 0.2327 0.0234  -0.0510 -0.0605 1167 GLU A CD  
8504  O OE1 . GLU A 1169 ? 0.2456 0.2769 0.2302 0.0205  -0.0503 -0.0574 1167 GLU A OE1 
8505  O OE2 . GLU A 1169 ? 0.2535 0.2979 0.2315 0.0244  -0.0515 -0.0600 1167 GLU A OE2 
8506  N N   . GLY A 1170 ? 0.2299 0.2689 0.2095 0.0307  -0.0574 -0.0820 1168 GLY A N   
8507  C CA  . GLY A 1170 ? 0.2608 0.3022 0.2440 0.0317  -0.0624 -0.0896 1168 GLY A CA  
8508  C C   . GLY A 1170 ? 0.2774 0.3288 0.2551 0.0358  -0.0631 -0.0953 1168 GLY A C   
8509  O O   . GLY A 1170 ? 0.2814 0.3379 0.2529 0.0379  -0.0597 -0.0931 1168 GLY A O   
8510  N N   . ASP A 1171 ? 0.2954 0.3499 0.2761 0.0371  -0.0679 -0.1029 1169 ASP A N   
8511  C CA  . ASP A 1171 ? 0.2673 0.3316 0.2436 0.0413  -0.0691 -0.1098 1169 ASP A CA  
8512  C C   . ASP A 1171 ? 0.3176 0.3784 0.2957 0.0431  -0.0695 -0.1147 1169 ASP A C   
8513  O O   . ASP A 1171 ? 0.3096 0.3604 0.2920 0.0410  -0.0689 -0.1123 1169 ASP A O   
8514  C CB  . ASP A 1171 ? 0.2961 0.3659 0.2746 0.0424  -0.0740 -0.1166 1169 ASP A CB  
8515  C CG  . ASP A 1171 ? 0.3634 0.4248 0.3518 0.0407  -0.0793 -0.1223 1169 ASP A CG  
8516  O OD1 . ASP A 1171 ? 0.3163 0.3689 0.3096 0.0397  -0.0798 -0.1230 1169 ASP A OD1 
8517  O OD2 . ASP A 1171 ? 0.4066 0.4705 0.3981 0.0404  -0.0833 -0.1261 1169 ASP A OD2 
8518  N N   . ALA A 1172 ? 0.3030 0.3729 0.2773 0.0472  -0.0704 -0.1215 1170 ALA A N   
8519  C CA  . ALA A 1172 ? 0.3154 0.3838 0.2903 0.0494  -0.0702 -0.1257 1170 ALA A CA  
8520  C C   . ALA A 1172 ? 0.3461 0.4035 0.3306 0.0481  -0.0744 -0.1306 1170 ALA A C   
8521  O O   . ALA A 1172 ? 0.3292 0.3792 0.3162 0.0475  -0.0732 -0.1292 1170 ALA A O   
8522  C CB  . ALA A 1172 ? 0.3263 0.4077 0.2961 0.0543  -0.0710 -0.1331 1170 ALA A CB  
8523  N N   . GLU A 1173 ? 0.3436 0.3997 0.3341 0.0476  -0.0796 -0.1361 1171 GLU A N   
8524  C CA  . GLU A 1173 ? 0.3466 0.3924 0.3472 0.0463  -0.0841 -0.1407 1171 GLU A CA  
8525  C C   . GLU A 1173 ? 0.3466 0.3806 0.3523 0.0413  -0.0830 -0.1323 1171 GLU A C   
8526  O O   . GLU A 1173 ? 0.3468 0.3717 0.3592 0.0400  -0.0846 -0.1329 1171 GLU A O   
8527  C CB  . GLU A 1173 ? 0.3718 0.4198 0.3781 0.0472  -0.0904 -0.1495 1171 GLU A CB  
8528  C CG  . GLU A 1173 ? 0.4053 0.4639 0.4086 0.0526  -0.0925 -0.1598 1171 GLU A CG  
8529  C CD  . GLU A 1173 ? 0.4515 0.5086 0.4552 0.0552  -0.0916 -0.1635 1171 GLU A CD  
8530  O OE1 . GLU A 1173 ? 0.4380 0.4837 0.4497 0.0534  -0.0934 -0.1634 1171 GLU A OE1 
8531  O OE2 . GLU A 1173 ? 0.4200 0.4876 0.4163 0.0591  -0.0891 -0.1662 1171 GLU A OE2 
8532  N N   . ARG A 1174 ? 0.3090 0.3435 0.3118 0.0385  -0.0802 -0.1245 1172 ARG A N   
8533  C CA  . ARG A 1174 ? 0.3114 0.3364 0.3178 0.0341  -0.0784 -0.1162 1172 ARG A CA  
8534  C C   . ARG A 1174 ? 0.3063 0.3279 0.3095 0.0341  -0.0738 -0.1115 1172 ARG A C   
8535  O O   . ARG A 1174 ? 0.2917 0.3043 0.3004 0.0316  -0.0740 -0.1087 1172 ARG A O   
8536  C CB  . ARG A 1174 ? 0.2873 0.3150 0.2907 0.0317  -0.0760 -0.1093 1172 ARG A CB  
8537  C CG  . ARG A 1174 ? 0.2968 0.3165 0.3029 0.0275  -0.0734 -0.1005 1172 ARG A CG  
8538  C CD  . ARG A 1174 ? 0.3600 0.3710 0.3764 0.0243  -0.0777 -0.1014 1172 ARG A CD  
8539  N NE  . ARG A 1174 ? 0.3322 0.3371 0.3509 0.0202  -0.0751 -0.0930 1172 ARG A NE  
8540  C CZ  . ARG A 1174 ? 0.3395 0.3363 0.3664 0.0171  -0.0774 -0.0915 1172 ARG A CZ  
8541  N NH1 . ARG A 1174 ? 0.3485 0.3414 0.3827 0.0175  -0.0825 -0.0976 1172 ARG A NH1 
8542  N NH2 . ARG A 1174 ? 0.2932 0.2863 0.3213 0.0136  -0.0747 -0.0836 1172 ARG A NH2 
8543  N N   . ILE A 1175 ? 0.2959 0.3249 0.2905 0.0369  -0.0698 -0.1103 1173 ILE A N   
8544  C CA  . ILE A 1175 ? 0.2836 0.3101 0.2750 0.0371  -0.0656 -0.1062 1173 ILE A CA  
8545  C C   . ILE A 1175 ? 0.2897 0.3113 0.2861 0.0385  -0.0681 -0.1120 1173 ILE A C   
8546  O O   . ILE A 1175 ? 0.2977 0.3118 0.2967 0.0368  -0.0667 -0.1084 1173 ILE A O   
8547  C CB  . ILE A 1175 ? 0.2829 0.3195 0.2647 0.0400  -0.0614 -0.1044 1173 ILE A CB  
8548  C CG1 . ILE A 1175 ? 0.3044 0.3443 0.2821 0.0382  -0.0587 -0.0972 1173 ILE A CG1 
8549  C CG2 . ILE A 1175 ? 0.2952 0.3298 0.2743 0.0408  -0.0577 -0.1017 1173 ILE A CG2 
8550  C CD1 . ILE A 1175 ? 0.2949 0.3460 0.2640 0.0410  -0.0555 -0.0954 1173 ILE A CD1 
8551  N N   . ARG A 1176 ? 0.3212 0.3473 0.3194 0.0417  -0.0721 -0.1214 1174 ARG A N   
8552  C CA  . ARG A 1176 ? 0.3048 0.3268 0.3085 0.0435  -0.0750 -0.1278 1174 ARG A CA  
8553  C C   . ARG A 1176 ? 0.2969 0.3067 0.3107 0.0398  -0.0782 -0.1262 1174 ARG A C   
8554  O O   . ARG A 1176 ? 0.3263 0.3293 0.3436 0.0391  -0.0778 -0.1249 1174 ARG A O   
8555  C CB  . ARG A 1176 ? 0.2725 0.3020 0.2769 0.0477  -0.0792 -0.1388 1174 ARG A CB  
8556  C CG  . ARG A 1176 ? 0.3693 0.3974 0.3770 0.0509  -0.0810 -0.1459 1174 ARG A CG  
8557  C CD  . ARG A 1176 ? 0.3678 0.4022 0.3786 0.0548  -0.0862 -0.1579 1174 ARG A CD  
8558  N NE  . ARG A 1176 ? 0.4189 0.4668 0.4213 0.0576  -0.0848 -0.1602 1174 ARG A NE  
8559  C CZ  . ARG A 1176 ? 0.4687 0.5276 0.4634 0.0616  -0.0819 -0.1626 1174 ARG A CZ  
8560  N NH1 . ARG A 1176 ? 0.4107 0.4686 0.4047 0.0633  -0.0799 -0.1631 1174 ARG A NH1 
8561  N NH2 . ARG A 1176 ? 0.4806 0.5523 0.4683 0.0638  -0.0812 -0.1644 1174 ARG A NH2 
8562  N N   . ALA A 1177 ? 0.3186 0.3259 0.3374 0.0371  -0.0814 -0.1256 1175 ALA A N   
8563  C CA  . ALA A 1177 ? 0.3242 0.3209 0.3533 0.0333  -0.0848 -0.1237 1175 ALA A CA  
8564  C C   . ALA A 1177 ? 0.3179 0.3085 0.3462 0.0296  -0.0806 -0.1137 1175 ALA A C   
8565  O O   . ALA A 1177 ? 0.3342 0.3168 0.3688 0.0278  -0.0818 -0.1121 1175 ALA A O   
8566  C CB  . ALA A 1177 ? 0.2810 0.2778 0.3149 0.0310  -0.0887 -0.1245 1175 ALA A CB  
8567  N N   . VAL A 1178 ? 0.2880 0.2825 0.3089 0.0285  -0.0757 -0.1069 1176 VAL A N   
8568  C CA  . VAL A 1178 ? 0.2722 0.2618 0.2920 0.0253  -0.0716 -0.0978 1176 VAL A CA  
8569  C C   . VAL A 1178 ? 0.3117 0.2992 0.3292 0.0268  -0.0690 -0.0973 1176 VAL A C   
8570  O O   . VAL A 1178 ? 0.3010 0.2815 0.3225 0.0243  -0.0684 -0.0929 1176 VAL A O   
8571  C CB  . VAL A 1178 ? 0.2851 0.2799 0.2975 0.0244  -0.0671 -0.0915 1176 VAL A CB  
8572  C CG1 . VAL A 1178 ? 0.2564 0.2472 0.2670 0.0219  -0.0626 -0.0832 1176 VAL A CG1 
8573  C CG2 . VAL A 1178 ? 0.2819 0.2776 0.2978 0.0222  -0.0697 -0.0908 1176 VAL A CG2 
8574  N N   . ASN A 1179 ? 0.3087 0.3029 0.3201 0.0310  -0.0675 -0.1017 1177 ASN A N   
8575  C CA  . ASN A 1179 ? 0.3046 0.2977 0.3135 0.0328  -0.0649 -0.1015 1177 ASN A CA  
8576  C C   . ASN A 1179 ? 0.3346 0.3202 0.3522 0.0326  -0.0689 -0.1055 1177 ASN A C   
8577  O O   . ASN A 1179 ? 0.3265 0.3071 0.3452 0.0317  -0.0671 -0.1021 1177 ASN A O   
8578  C CB  . ASN A 1179 ? 0.3492 0.3523 0.3505 0.0373  -0.0630 -0.1060 1177 ASN A CB  
8579  C CG  . ASN A 1179 ? 0.3941 0.3985 0.3897 0.0385  -0.0582 -0.1023 1177 ASN A CG  
8580  O OD1 . ASN A 1179 ? 0.4281 0.4271 0.4235 0.0358  -0.0552 -0.0952 1177 ASN A OD1 
8581  N ND2 . ASN A 1179 ? 0.4161 0.4283 0.4071 0.0426  -0.0575 -0.1073 1177 ASN A ND2 
8582  N N   . LYS A 1180 ? 0.3098 0.2945 0.3342 0.0335  -0.0746 -0.1127 1178 LYS A N   
8583  C CA  . LYS A 1180 ? 0.3090 0.2859 0.3434 0.0331  -0.0791 -0.1163 1178 LYS A CA  
8584  C C   . LYS A 1180 ? 0.3407 0.3086 0.3814 0.0279  -0.0795 -0.1085 1178 LYS A C   
8585  O O   . LYS A 1180 ? 0.3288 0.2904 0.3737 0.0269  -0.0797 -0.1064 1178 LYS A O   
8586  C CB  . LYS A 1180 ? 0.3574 0.3353 0.3983 0.0350  -0.0855 -0.1258 1178 LYS A CB  
8587  C CG  . LYS A 1180 ? 0.3745 0.3612 0.4107 0.0406  -0.0858 -0.1348 1178 LYS A CG  
8588  C CD  . LYS A 1180 ? 0.3267 0.3171 0.3671 0.0426  -0.0914 -0.1440 1178 LYS A CD  
8589  C CE  . LYS A 1180 ? 0.4339 0.4150 0.4879 0.0410  -0.0983 -0.1481 1178 LYS A CE  
8590  N NZ  . LYS A 1180 ? 0.5089 0.4934 0.5676 0.0429  -0.1041 -0.1574 1178 LYS A NZ  
8591  N N   . ALA A 1181 ? 0.3073 0.2750 0.3487 0.0246  -0.0794 -0.1038 1179 ALA A N   
8592  C CA  . ALA A 1181 ? 0.3047 0.2657 0.3512 0.0196  -0.0793 -0.0957 1179 ALA A CA  
8593  C C   . ALA A 1181 ? 0.2877 0.2477 0.3287 0.0185  -0.0736 -0.0884 1179 ALA A C   
8594  O O   . ALA A 1181 ? 0.2933 0.2471 0.3394 0.0158  -0.0739 -0.0839 1179 ALA A O   
8595  C CB  . ALA A 1181 ? 0.2763 0.2393 0.3232 0.0167  -0.0795 -0.0921 1179 ALA A CB  
8596  N N   . ILE A 1182 ? 0.3014 0.2676 0.3322 0.0206  -0.0686 -0.0870 1180 ILE A N   
8597  C CA  . ILE A 1182 ? 0.2844 0.2498 0.3102 0.0196  -0.0633 -0.0803 1180 ILE A CA  
8598  C C   . ILE A 1182 ? 0.2924 0.2543 0.3198 0.0212  -0.0634 -0.0823 1180 ILE A C   
8599  O O   . ILE A 1182 ? 0.3008 0.2581 0.3298 0.0190  -0.0618 -0.0769 1180 ILE A O   
8600  C CB  . ILE A 1182 ? 0.2547 0.2275 0.2703 0.0214  -0.0584 -0.0784 1180 ILE A CB  
8601  C CG1 . ILE A 1182 ? 0.2920 0.2672 0.3066 0.0192  -0.0579 -0.0747 1180 ILE A CG1 
8602  C CG2 . ILE A 1182 ? 0.3163 0.2882 0.3269 0.0212  -0.0534 -0.0730 1180 ILE A CG2 
8603  C CD1 . ILE A 1182 ? 0.3036 0.2860 0.3092 0.0209  -0.0536 -0.0727 1180 ILE A CD1 
8604  N N   . ALA A 1183 ? 0.2817 0.2464 0.3089 0.0253  -0.0654 -0.0902 1181 ALA A N   
8605  C CA  . ALA A 1183 ? 0.2901 0.2521 0.3189 0.0273  -0.0656 -0.0926 1181 ALA A CA  
8606  C C   . ALA A 1183 ? 0.3350 0.2881 0.3744 0.0245  -0.0697 -0.0916 1181 ALA A C   
8607  O O   . ALA A 1183 ? 0.2931 0.2423 0.3342 0.0245  -0.0689 -0.0898 1181 ALA A O   
8608  C CB  . ALA A 1183 ? 0.3102 0.2777 0.3376 0.0323  -0.0675 -0.1021 1181 ALA A CB  
8609  N N   . ALA A 1184 ? 0.3131 0.2631 0.3600 0.0221  -0.0741 -0.0920 1182 ALA A N   
8610  C CA  . ALA A 1184 ? 0.3282 0.2699 0.3862 0.0191  -0.0786 -0.0904 1182 ALA A CA  
8611  C C   . ALA A 1184 ? 0.3246 0.2627 0.3834 0.0143  -0.0760 -0.0803 1182 ALA A C   
8612  O O   . ALA A 1184 ? 0.3178 0.2496 0.3855 0.0116  -0.0792 -0.0776 1182 ALA A O   
8613  C CB  . ALA A 1184 ? 0.3310 0.2711 0.3976 0.0181  -0.0847 -0.0947 1182 ALA A CB  
8614  N N   . LEU A 1185 ? 0.2884 0.2307 0.3387 0.0133  -0.0707 -0.0748 1183 LEU A N   
8615  C CA  . LEU A 1185 ? 0.3170 0.2569 0.3678 0.0091  -0.0681 -0.0658 1183 LEU A CA  
8616  C C   . LEU A 1185 ? 0.3195 0.2558 0.3710 0.0092  -0.0667 -0.0635 1183 LEU A C   
8617  O O   . LEU A 1185 ? 0.2953 0.2333 0.3419 0.0128  -0.0648 -0.0672 1183 LEU A O   
8618  C CB  . LEU A 1185 ? 0.2759 0.2213 0.3176 0.0086  -0.0627 -0.0613 1183 LEU A CB  
8619  C CG  . LEU A 1185 ? 0.2863 0.2359 0.3266 0.0084  -0.0635 -0.0627 1183 LEU A CG  
8620  C CD1 . LEU A 1185 ? 0.3020 0.2569 0.3332 0.0084  -0.0580 -0.0586 1183 LEU A CD1 
8621  C CD2 . LEU A 1185 ? 0.3195 0.2658 0.3688 0.0043  -0.0675 -0.0600 1183 LEU A CD2 
8622  N N   . PRO A 1186 ? 0.3294 0.2612 0.3868 0.0053  -0.0677 -0.0574 1184 PRO A N   
8623  C CA  . PRO A 1186 ? 0.2845 0.2130 0.3426 0.0053  -0.0664 -0.0548 1184 PRO A CA  
8624  C C   . PRO A 1186 ? 0.2690 0.2015 0.3168 0.0062  -0.0599 -0.0513 1184 PRO A C   
8625  O O   . PRO A 1186 ? 0.2944 0.2310 0.3361 0.0053  -0.0565 -0.0484 1184 PRO A O   
8626  C CB  . PRO A 1186 ? 0.3436 0.2680 0.4101 0.0003  -0.0688 -0.0479 1184 PRO A CB  
8627  C CG  . PRO A 1186 ? 0.3790 0.3067 0.4446 -0.0025 -0.0682 -0.0445 1184 PRO A CG  
8628  C CD  . PRO A 1186 ? 0.3403 0.2708 0.4037 0.0007  -0.0696 -0.0518 1184 PRO A CD  
8629  N N   . GLY A 1187 ? 0.2825 0.2134 0.3288 0.0079  -0.0585 -0.0517 1185 GLY A N   
8630  C CA  . GLY A 1187 ? 0.3250 0.2586 0.3633 0.0080  -0.0529 -0.0475 1185 GLY A CA  
8631  C C   . GLY A 1187 ? 0.2640 0.2025 0.2936 0.0122  -0.0495 -0.0517 1185 GLY A C   
8632  O O   . GLY A 1187 ? 0.2892 0.2282 0.3191 0.0157  -0.0511 -0.0579 1185 GLY A O   
8633  N N   . PRO A 1188 ? 0.2948 0.2375 0.3168 0.0118  -0.0449 -0.0481 1186 PRO A N   
8634  C CA  . PRO A 1188 ? 0.2638 0.2113 0.2778 0.0153  -0.0413 -0.0503 1186 PRO A CA  
8635  C C   . PRO A 1188 ? 0.2710 0.2228 0.2828 0.0183  -0.0427 -0.0563 1186 PRO A C   
8636  O O   . PRO A 1188 ? 0.2581 0.2104 0.2725 0.0172  -0.0451 -0.0574 1186 PRO A O   
8637  C CB  . PRO A 1188 ? 0.2835 0.2335 0.2918 0.0135  -0.0367 -0.0443 1186 PRO A CB  
8638  C CG  . PRO A 1188 ? 0.2679 0.2168 0.2800 0.0100  -0.0382 -0.0410 1186 PRO A CG  
8639  C CD  . PRO A 1188 ? 0.2688 0.2124 0.2899 0.0083  -0.0430 -0.0419 1186 PRO A CD  
8640  N N   . LEU A 1189 ? 0.2708 0.2265 0.2780 0.0220  -0.0412 -0.0602 1187 LEU A N   
8641  C CA  . LEU A 1189 ? 0.2361 0.1980 0.2394 0.0249  -0.0415 -0.0651 1187 LEU A CA  
8642  C C   . LEU A 1189 ? 0.2756 0.2416 0.2732 0.0238  -0.0382 -0.0606 1187 LEU A C   
8643  O O   . LEU A 1189 ? 0.2944 0.2605 0.2883 0.0226  -0.0343 -0.0552 1187 LEU A O   
8644  C CB  . LEU A 1189 ? 0.2531 0.2196 0.2523 0.0290  -0.0401 -0.0692 1187 LEU A CB  
8645  C CG  . LEU A 1189 ? 0.2746 0.2394 0.2792 0.0316  -0.0440 -0.0763 1187 LEU A CG  
8646  C CD1 . LEU A 1189 ? 0.2626 0.2200 0.2732 0.0299  -0.0452 -0.0742 1187 LEU A CD1 
8647  C CD2 . LEU A 1189 ? 0.3371 0.3093 0.3363 0.0360  -0.0423 -0.0809 1187 LEU A CD2 
8648  N N   . LEU A 1190 ? 0.2552 0.2244 0.2526 0.0241  -0.0399 -0.0630 1188 LEU A N   
8649  C CA  . LEU A 1190 ? 0.2537 0.2266 0.2465 0.0230  -0.0373 -0.0590 1188 LEU A CA  
8650  C C   . LEU A 1190 ? 0.2596 0.2404 0.2458 0.0264  -0.0356 -0.0615 1188 LEU A C   
8651  O O   . LEU A 1190 ? 0.2712 0.2555 0.2577 0.0291  -0.0381 -0.0676 1188 LEU A O   
8652  C CB  . LEU A 1190 ? 0.2737 0.2453 0.2707 0.0207  -0.0401 -0.0588 1188 LEU A CB  
8653  C CG  . LEU A 1190 ? 0.2978 0.2628 0.3016 0.0169  -0.0419 -0.0554 1188 LEU A CG  
8654  C CD1 . LEU A 1190 ? 0.3058 0.2713 0.3125 0.0145  -0.0437 -0.0541 1188 LEU A CD1 
8655  C CD2 . LEU A 1190 ? 0.2840 0.2470 0.2858 0.0150  -0.0381 -0.0491 1188 LEU A CD2 
8656  N N   . LEU A 1191 ? 0.2579 0.2418 0.2386 0.0264  -0.0315 -0.0567 1189 LEU A N   
8657  C CA  . LEU A 1191 ? 0.2184 0.2105 0.1933 0.0289  -0.0299 -0.0575 1189 LEU A CA  
8658  C C   . LEU A 1191 ? 0.2303 0.2249 0.2054 0.0282  -0.0315 -0.0577 1189 LEU A C   
8659  O O   . LEU A 1191 ? 0.2553 0.2483 0.2306 0.0258  -0.0302 -0.0530 1189 LEU A O   
8660  C CB  . LEU A 1191 ? 0.2243 0.2183 0.1944 0.0288  -0.0254 -0.0518 1189 LEU A CB  
8661  C CG  . LEU A 1191 ? 0.2329 0.2353 0.1971 0.0317  -0.0234 -0.0520 1189 LEU A CG  
8662  C CD1 . LEU A 1191 ? 0.2458 0.2479 0.2074 0.0311  -0.0194 -0.0462 1189 LEU A CD1 
8663  C CD2 . LEU A 1191 ? 0.2308 0.2391 0.1928 0.0321  -0.0239 -0.0517 1189 LEU A CD2 
8664  N N   . VAL A 1192 ? 0.2430 0.2419 0.2184 0.0304  -0.0344 -0.0637 1190 VAL A N   
8665  C CA  . VAL A 1192 ? 0.2362 0.2378 0.2123 0.0299  -0.0366 -0.0650 1190 VAL A CA  
8666  C C   . VAL A 1192 ? 0.2401 0.2510 0.2099 0.0323  -0.0348 -0.0646 1190 VAL A C   
8667  O O   . VAL A 1192 ? 0.2652 0.2820 0.2314 0.0353  -0.0342 -0.0676 1190 VAL A O   
8668  C CB  . VAL A 1192 ? 0.2839 0.2843 0.2652 0.0308  -0.0416 -0.0722 1190 VAL A CB  
8669  C CG1 . VAL A 1192 ? 0.2693 0.2721 0.2519 0.0299  -0.0440 -0.0732 1190 VAL A CG1 
8670  C CG2 . VAL A 1192 ? 0.3066 0.2980 0.2947 0.0286  -0.0436 -0.0723 1190 VAL A CG2 
8671  N N   . GLN A 1193 ? 0.2526 0.2655 0.2212 0.0309  -0.0341 -0.0609 1191 GLN A N   
8672  C CA  . GLN A 1193 ? 0.2132 0.2350 0.1769 0.0328  -0.0334 -0.0606 1191 GLN A CA  
8673  C C   . GLN A 1193 ? 0.2479 0.2715 0.2139 0.0324  -0.0367 -0.0635 1191 GLN A C   
8674  O O   . GLN A 1193 ? 0.2355 0.2537 0.2056 0.0296  -0.0378 -0.0617 1191 GLN A O   
8675  C CB  . GLN A 1193 ? 0.2249 0.2481 0.1855 0.0318  -0.0296 -0.0532 1191 GLN A CB  
8676  C CG  . GLN A 1193 ? 0.2406 0.2616 0.1993 0.0319  -0.0263 -0.0498 1191 GLN A CG  
8677  C CD  . GLN A 1193 ? 0.2417 0.2652 0.1976 0.0314  -0.0231 -0.0431 1191 GLN A CD  
8678  O OE1 . GLN A 1193 ? 0.2569 0.2884 0.2090 0.0332  -0.0224 -0.0420 1191 GLN A OE1 
8679  N NE2 . GLN A 1193 ? 0.2623 0.2796 0.2203 0.0290  -0.0214 -0.0387 1191 GLN A NE2 
8680  N N   . ALA A 1194 ? 0.2354 0.2672 0.1985 0.0351  -0.0383 -0.0678 1192 ALA A N   
8681  C CA  . ALA A 1194 ? 0.2229 0.2573 0.1880 0.0350  -0.0418 -0.0714 1192 ALA A CA  
8682  C C   . ALA A 1194 ? 0.2710 0.3154 0.2308 0.0367  -0.0408 -0.0697 1192 ALA A C   
8683  O O   . ALA A 1194 ? 0.2597 0.3109 0.2143 0.0388  -0.0385 -0.0684 1192 ALA A O   
8684  C CB  . ALA A 1194 ? 0.2247 0.2595 0.1929 0.0369  -0.0459 -0.0801 1192 ALA A CB  
8685  N N   . ALA A 1195 ? 0.2399 0.2855 0.2012 0.0355  -0.0428 -0.0695 1193 ALA A N   
8686  C CA  . ALA A 1195 ? 0.2448 0.3000 0.2018 0.0369  -0.0424 -0.0679 1193 ALA A CA  
8687  C C   . ALA A 1195 ? 0.2670 0.3236 0.2270 0.0364  -0.0463 -0.0717 1193 ALA A C   
8688  O O   . ALA A 1195 ? 0.2552 0.3043 0.2209 0.0339  -0.0483 -0.0725 1193 ALA A O   
8689  C CB  . ALA A 1195 ? 0.2466 0.3014 0.2017 0.0354  -0.0388 -0.0593 1193 ALA A CB  
8690  N N   . SER A 1196 ? 0.2403 0.3071 0.1967 0.0386  -0.0475 -0.0739 1194 SER A N   
8691  C CA  . SER A 1196 ? 0.2833 0.3523 0.2421 0.0380  -0.0510 -0.0766 1194 SER A CA  
8692  C C   . SER A 1196 ? 0.2452 0.3131 0.2043 0.0357  -0.0493 -0.0693 1194 SER A C   
8693  O O   . SER A 1196 ? 0.2593 0.3269 0.2160 0.0352  -0.0457 -0.0626 1194 SER A O   
8694  C CB  . SER A 1196 ? 0.3179 0.3989 0.2724 0.0413  -0.0529 -0.0816 1194 SER A CB  
8695  O OG  . SER A 1196 ? 0.2816 0.3711 0.2301 0.0425  -0.0498 -0.0759 1194 SER A OG  
8696  N N   . SER A 1197 ? 0.2291 0.2967 0.1918 0.0344  -0.0523 -0.0708 1195 SER A N   
8697  C CA  . SER A 1197 ? 0.2532 0.3211 0.2163 0.0326  -0.0510 -0.0645 1195 SER A CA  
8698  C C   . SER A 1197 ? 0.2584 0.3361 0.2156 0.0346  -0.0491 -0.0606 1195 SER A C   
8699  O O   . SER A 1197 ? 0.2647 0.3416 0.2211 0.0337  -0.0462 -0.0536 1195 SER A O   
8700  C CB  . SER A 1197 ? 0.2892 0.3567 0.2568 0.0312  -0.0548 -0.0674 1195 SER A CB  
8701  O OG  . SER A 1197 ? 0.2827 0.3412 0.2566 0.0289  -0.0568 -0.0700 1195 SER A OG  
8702  N N   . GLY A 1198 ? 0.2840 0.3713 0.2373 0.0374  -0.0507 -0.0650 1196 GLY A N   
8703  C CA  . GLY A 1198 ? 0.2663 0.3641 0.2141 0.0393  -0.0490 -0.0609 1196 GLY A CA  
8704  C C   . GLY A 1198 ? 0.2960 0.3935 0.2406 0.0397  -0.0449 -0.0554 1196 GLY A C   
8705  O O   . GLY A 1198 ? 0.2664 0.3676 0.2090 0.0397  -0.0427 -0.0485 1196 GLY A O   
8706  N N   . GLU A 1199 ? 0.2770 0.3699 0.2218 0.0402  -0.0440 -0.0582 1197 GLU A N   
8707  C CA  . GLU A 1199 ? 0.2714 0.3632 0.2137 0.0404  -0.0402 -0.0531 1197 GLU A CA  
8708  C C   . GLU A 1199 ? 0.2793 0.3626 0.2246 0.0377  -0.0377 -0.0460 1197 GLU A C   
8709  O O   . GLU A 1199 ? 0.2623 0.3477 0.2057 0.0377  -0.0350 -0.0395 1197 GLU A O   
8710  C CB  . GLU A 1199 ? 0.2699 0.3578 0.2125 0.0413  -0.0401 -0.0583 1197 GLU A CB  
8711  C CG  . GLU A 1199 ? 0.3343 0.4218 0.2744 0.0417  -0.0364 -0.0541 1197 GLU A CG  
8712  C CD  . GLU A 1199 ? 0.4082 0.4937 0.3483 0.0432  -0.0369 -0.0603 1197 GLU A CD  
8713  O OE1 . GLU A 1199 ? 0.3969 0.4802 0.3399 0.0436  -0.0402 -0.0675 1197 GLU A OE1 
8714  O OE2 . GLU A 1199 ? 0.4809 0.5674 0.4187 0.0440  -0.0342 -0.0579 1197 GLU A OE2 
8715  N N   . ILE A 1200 ? 0.2635 0.3378 0.2138 0.0353  -0.0388 -0.0472 1198 ILE A N   
8716  C CA  . ILE A 1200 ? 0.2392 0.3065 0.1924 0.0329  -0.0367 -0.0411 1198 ILE A CA  
8717  C C   . ILE A 1200 ? 0.2852 0.3581 0.2377 0.0330  -0.0362 -0.0358 1198 ILE A C   
8718  O O   . ILE A 1200 ? 0.2585 0.3297 0.2113 0.0324  -0.0336 -0.0296 1198 ILE A O   
8719  C CB  . ILE A 1200 ? 0.2471 0.3058 0.2059 0.0304  -0.0383 -0.0435 1198 ILE A CB  
8720  C CG1 . ILE A 1200 ? 0.2489 0.3012 0.2091 0.0301  -0.0384 -0.0473 1198 ILE A CG1 
8721  C CG2 . ILE A 1200 ? 0.2468 0.3004 0.2087 0.0282  -0.0364 -0.0376 1198 ILE A CG2 
8722  C CD1 . ILE A 1200 ? 0.2681 0.3127 0.2341 0.0276  -0.0406 -0.0499 1198 ILE A CD1 
8723  N N   . ALA A 1201 ? 0.2518 0.3317 0.2035 0.0339  -0.0389 -0.0381 1199 ALA A N   
8724  C CA  . ALA A 1201 ? 0.2601 0.3456 0.2115 0.0340  -0.0388 -0.0330 1199 ALA A CA  
8725  C C   . ALA A 1201 ? 0.2652 0.3584 0.2122 0.0358  -0.0369 -0.0282 1199 ALA A C   
8726  O O   . ALA A 1201 ? 0.2693 0.3637 0.2171 0.0354  -0.0355 -0.0216 1199 ALA A O   
8727  C CB  . ALA A 1201 ? 0.2598 0.3512 0.2114 0.0345  -0.0424 -0.0370 1199 ALA A CB  
8728  N N   . ARG A 1202 ? 0.2639 0.3628 0.2067 0.0378  -0.0368 -0.0313 1200 ARG A N   
8729  C CA  . ARG A 1202 ? 0.2615 0.3698 0.2001 0.0395  -0.0352 -0.0268 1200 ARG A CA  
8730  C C   . ARG A 1202 ? 0.2931 0.3968 0.2317 0.0390  -0.0319 -0.0219 1200 ARG A C   
8731  O O   . ARG A 1202 ? 0.2995 0.4075 0.2372 0.0392  -0.0303 -0.0151 1200 ARG A O   
8732  C CB  . ARG A 1202 ? 0.2576 0.3760 0.1914 0.0420  -0.0367 -0.0324 1200 ARG A CB  
8733  C CG  . ARG A 1202 ? 0.2635 0.3901 0.1964 0.0430  -0.0400 -0.0361 1200 ARG A CG  
8734  C CD  . ARG A 1202 ? 0.2925 0.4309 0.2204 0.0459  -0.0413 -0.0415 1200 ARG A CD  
8735  N NE  . ARG A 1202 ? 0.3093 0.4427 0.2375 0.0466  -0.0415 -0.0486 1200 ARG A NE  
8736  C CZ  . ARG A 1202 ? 0.3280 0.4584 0.2585 0.0469  -0.0446 -0.0571 1200 ARG A CZ  
8737  N NH1 . ARG A 1202 ? 0.3072 0.4408 0.2389 0.0469  -0.0478 -0.0602 1200 ARG A NH1 
8738  N NH2 . ARG A 1202 ? 0.3183 0.4423 0.2502 0.0472  -0.0447 -0.0623 1200 ARG A NH2 
8739  N N   . ASN A 1203 ? 0.2521 0.3474 0.1920 0.0383  -0.0309 -0.0252 1201 ASN A N   
8740  C CA  . ASN A 1203 ? 0.2720 0.3642 0.2112 0.0382  -0.0279 -0.0217 1201 ASN A CA  
8741  C C   . ASN A 1203 ? 0.2968 0.3770 0.2404 0.0359  -0.0264 -0.0194 1201 ASN A C   
8742  O O   . ASN A 1203 ? 0.2640 0.3367 0.2098 0.0348  -0.0270 -0.0240 1201 ASN A O   
8743  C CB  . ASN A 1203 ? 0.2822 0.3762 0.2186 0.0398  -0.0279 -0.0274 1201 ASN A CB  
8744  C CG  . ASN A 1203 ? 0.3012 0.3925 0.2369 0.0397  -0.0248 -0.0239 1201 ASN A CG  
8745  O OD1 . ASN A 1203 ? 0.3107 0.4001 0.2477 0.0386  -0.0228 -0.0170 1201 ASN A OD1 
8746  N ND2 . ASN A 1203 ? 0.3159 0.4070 0.2501 0.0408  -0.0246 -0.0288 1201 ASN A ND2 
8747  N N   . PRO A 1204 ? 0.3033 0.3817 0.2488 0.0350  -0.0245 -0.0126 1202 PRO A N   
8748  C CA  . PRO A 1204 ? 0.3071 0.3750 0.2567 0.0330  -0.0230 -0.0109 1202 PRO A CA  
8749  C C   . PRO A 1204 ? 0.3106 0.3724 0.2598 0.0327  -0.0216 -0.0134 1202 PRO A C   
8750  O O   . PRO A 1204 ? 0.3150 0.3683 0.2673 0.0310  -0.0210 -0.0142 1202 PRO A O   
8751  C CB  . PRO A 1204 ? 0.3585 0.4275 0.3097 0.0328  -0.0215 -0.0033 1202 PRO A CB  
8752  C CG  . PRO A 1204 ? 0.3775 0.4566 0.3268 0.0341  -0.0230 -0.0011 1202 PRO A CG  
8753  C CD  . PRO A 1204 ? 0.3499 0.4360 0.2943 0.0357  -0.0241 -0.0061 1202 PRO A CD  
8754  N N   . ASP A 1205 ? 0.3041 0.3708 0.2496 0.0343  -0.0209 -0.0147 1203 ASP A N   
8755  C CA  . ASP A 1205 ? 0.3046 0.3663 0.2496 0.0342  -0.0197 -0.0173 1203 ASP A CA  
8756  C C   . ASP A 1205 ? 0.2997 0.3616 0.2438 0.0351  -0.0218 -0.0250 1203 ASP A C   
8757  O O   . ASP A 1205 ? 0.3311 0.3922 0.2738 0.0359  -0.0211 -0.0277 1203 ASP A O   
8758  C CB  . ASP A 1205 ? 0.3405 0.4074 0.2828 0.0354  -0.0175 -0.0136 1203 ASP A CB  
8759  C CG  . ASP A 1205 ? 0.3553 0.4210 0.2995 0.0344  -0.0157 -0.0059 1203 ASP A CG  
8760  O OD1 . ASP A 1205 ? 0.3423 0.4011 0.2904 0.0328  -0.0156 -0.0042 1203 ASP A OD1 
8761  O OD2 . ASP A 1205 ? 0.4137 0.4860 0.3561 0.0354  -0.0146 -0.0017 1203 ASP A OD2 
8762  N N   . ALA A 1206 ? 0.2753 0.3382 0.2205 0.0349  -0.0245 -0.0286 1204 ALA A N   
8763  C CA  . ALA A 1206 ? 0.2975 0.3598 0.2431 0.0356  -0.0270 -0.0362 1204 ALA A CA  
8764  C C   . ALA A 1206 ? 0.2691 0.3221 0.2172 0.0345  -0.0264 -0.0384 1204 ALA A C   
8765  O O   . ALA A 1206 ? 0.3111 0.3646 0.2583 0.0359  -0.0272 -0.0433 1204 ALA A O   
8766  C CB  . ALA A 1206 ? 0.2732 0.3350 0.2214 0.0347  -0.0299 -0.0387 1204 ALA A CB  
8767  N N   . TYR A 1207 ? 0.2619 0.3068 0.2133 0.0321  -0.0251 -0.0349 1205 TYR A N   
8768  C CA  . TYR A 1207 ? 0.2754 0.3122 0.2289 0.0308  -0.0240 -0.0352 1205 TYR A CA  
8769  C C   . TYR A 1207 ? 0.2705 0.3067 0.2226 0.0308  -0.0206 -0.0297 1205 TYR A C   
8770  O O   . TYR A 1207 ? 0.3166 0.3524 0.2695 0.0298  -0.0192 -0.0247 1205 TYR A O   
8771  C CB  . TYR A 1207 ? 0.2446 0.2737 0.2030 0.0281  -0.0249 -0.0352 1205 TYR A CB  
8772  C CG  . TYR A 1207 ? 0.2459 0.2754 0.2067 0.0278  -0.0286 -0.0402 1205 TYR A CG  
8773  C CD1 . TYR A 1207 ? 0.2731 0.3022 0.2346 0.0289  -0.0309 -0.0464 1205 TYR A CD1 
8774  C CD2 . TYR A 1207 ? 0.2527 0.2829 0.2156 0.0266  -0.0298 -0.0391 1205 TYR A CD2 
8775  C CE1 . TYR A 1207 ? 0.2564 0.2855 0.2207 0.0286  -0.0346 -0.0512 1205 TYR A CE1 
8776  C CE2 . TYR A 1207 ? 0.2486 0.2791 0.2141 0.0262  -0.0334 -0.0437 1205 TYR A CE2 
8777  C CZ  . TYR A 1207 ? 0.2425 0.2723 0.2089 0.0272  -0.0358 -0.0497 1205 TYR A CZ  
8778  O OH  . TYR A 1207 ? 0.2497 0.2796 0.2194 0.0268  -0.0397 -0.0544 1205 TYR A OH  
8779  N N   . CYS A 1208 ? 0.2588 0.2949 0.2092 0.0318  -0.0193 -0.0307 1206 CYS A N   
8780  C CA  . CYS A 1208 ? 0.2684 0.3047 0.2173 0.0319  -0.0163 -0.0256 1206 CYS A CA  
8781  C C   . CYS A 1208 ? 0.2651 0.2923 0.2173 0.0297  -0.0149 -0.0236 1206 CYS A C   
8782  O O   . CYS A 1208 ? 0.2469 0.2687 0.2009 0.0289  -0.0156 -0.0269 1206 CYS A O   
8783  C CB  . CYS A 1208 ? 0.2988 0.3405 0.2444 0.0341  -0.0156 -0.0275 1206 CYS A CB  
8784  S SG  . CYS A 1208 ? 0.3127 0.3545 0.2571 0.0340  -0.0121 -0.0213 1206 CYS A SG  
8785  N N   . LEU A 1209 ? 0.2375 0.2633 0.1907 0.0286  -0.0130 -0.0183 1207 LEU A N   
8786  C CA  . LEU A 1209 ? 0.2130 0.2310 0.1693 0.0266  -0.0117 -0.0166 1207 LEU A CA  
8787  C C   . LEU A 1209 ? 0.1934 0.2085 0.1489 0.0267  -0.0100 -0.0164 1207 LEU A C   
8788  O O   . LEU A 1209 ? 0.2149 0.2237 0.1727 0.0251  -0.0093 -0.0161 1207 LEU A O   
8789  C CB  . LEU A 1209 ? 0.2193 0.2369 0.1774 0.0258  -0.0105 -0.0116 1207 LEU A CB  
8790  C CG  . LEU A 1209 ? 0.2110 0.2315 0.1703 0.0256  -0.0121 -0.0112 1207 LEU A CG  
8791  C CD1 . LEU A 1209 ? 0.2307 0.2500 0.1926 0.0250  -0.0109 -0.0066 1207 LEU A CD1 
8792  C CD2 . LEU A 1209 ? 0.2186 0.2357 0.1799 0.0243  -0.0140 -0.0151 1207 LEU A CD2 
8793  N N   . ASN A 1210 ? 0.2373 0.2575 0.1897 0.0286  -0.0094 -0.0166 1208 ASN A N   
8794  C CA  . ASN A 1210 ? 0.2455 0.2635 0.1973 0.0289  -0.0079 -0.0167 1208 ASN A CA  
8795  C C   . ASN A 1210 ? 0.2294 0.2415 0.1830 0.0281  -0.0090 -0.0211 1208 ASN A C   
8796  O O   . ASN A 1210 ? 0.2443 0.2515 0.1990 0.0272  -0.0078 -0.0204 1208 ASN A O   
8797  C CB  . ASN A 1210 ? 0.2621 0.2877 0.2102 0.0313  -0.0075 -0.0173 1208 ASN A CB  
8798  C CG  . ASN A 1210 ? 0.3013 0.3334 0.2480 0.0319  -0.0061 -0.0119 1208 ASN A CG  
8799  O OD1 . ASN A 1210 ? 0.3508 0.3823 0.2991 0.0309  -0.0061 -0.0083 1208 ASN A OD1 
8800  N ND2 . ASN A 1210 ? 0.3643 0.4031 0.3082 0.0336  -0.0052 -0.0113 1208 ASN A ND2 
8801  N N   . TRP A 1211 ? 0.2122 0.2249 0.1664 0.0284  -0.0116 -0.0256 1209 TRP A N   
8802  C CA  . TRP A 1211 ? 0.2213 0.2291 0.1778 0.0280  -0.0133 -0.0300 1209 TRP A CA  
8803  C C   . TRP A 1211 ? 0.2535 0.2548 0.2139 0.0253  -0.0143 -0.0295 1209 TRP A C   
8804  O O   . TRP A 1211 ? 0.2673 0.2644 0.2305 0.0245  -0.0161 -0.0326 1209 TRP A O   
8805  C CB  . TRP A 1211 ? 0.2425 0.2547 0.1981 0.0301  -0.0159 -0.0358 1209 TRP A CB  
8806  C CG  . TRP A 1211 ? 0.2262 0.2473 0.1774 0.0327  -0.0151 -0.0359 1209 TRP A CG  
8807  C CD1 . TRP A 1211 ? 0.2487 0.2774 0.1977 0.0343  -0.0164 -0.0375 1209 TRP A CD1 
8808  C CD2 . TRP A 1211 ? 0.2376 0.2619 0.1862 0.0340  -0.0126 -0.0337 1209 TRP A CD2 
8809  N NE1 . TRP A 1211 ? 0.2706 0.3074 0.2157 0.0365  -0.0149 -0.0364 1209 TRP A NE1 
8810  C CE2 . TRP A 1211 ? 0.2422 0.2765 0.1871 0.0363  -0.0126 -0.0339 1209 TRP A CE2 
8811  C CE3 . TRP A 1211 ? 0.2520 0.2722 0.2012 0.0333  -0.0105 -0.0314 1209 TRP A CE3 
8812  C CZ2 . TRP A 1211 ? 0.2457 0.2861 0.1876 0.0378  -0.0105 -0.0318 1209 TRP A CZ2 
8813  C CZ3 . TRP A 1211 ? 0.2724 0.2982 0.2187 0.0349  -0.0085 -0.0295 1209 TRP A CZ3 
8814  C CH2 . TRP A 1211 ? 0.2582 0.2941 0.2010 0.0371  -0.0085 -0.0295 1209 TRP A CH2 
8815  N N   . LEU A 1212 ? 0.2182 0.2191 0.1793 0.0239  -0.0132 -0.0256 1210 LEU A N   
8816  C CA  . LEU A 1212 ? 0.2192 0.2154 0.1840 0.0213  -0.0137 -0.0246 1210 LEU A CA  
8817  C C   . LEU A 1212 ? 0.2102 0.2025 0.1760 0.0198  -0.0113 -0.0209 1210 LEU A C   
8818  O O   . LEU A 1212 ? 0.2052 0.1945 0.1739 0.0177  -0.0113 -0.0197 1210 LEU A O   
8819  C CB  . LEU A 1212 ? 0.1880 0.1871 0.1534 0.0210  -0.0146 -0.0236 1210 LEU A CB  
8820  C CG  . LEU A 1212 ? 0.1979 0.1998 0.1636 0.0218  -0.0176 -0.0279 1210 LEU A CG  
8821  C CD1 . LEU A 1212 ? 0.2302 0.2368 0.1953 0.0222  -0.0183 -0.0268 1210 LEU A CD1 
8822  C CD2 . LEU A 1212 ? 0.2171 0.2140 0.1870 0.0197  -0.0198 -0.0303 1210 LEU A CD2 
8823  N N   . VAL A 1213 ? 0.2198 0.2127 0.1835 0.0209  -0.0092 -0.0192 1211 VAL A N   
8824  C CA  . VAL A 1213 ? 0.2002 0.1894 0.1650 0.0196  -0.0071 -0.0164 1211 VAL A CA  
8825  C C   . VAL A 1213 ? 0.2052 0.1919 0.1696 0.0199  -0.0070 -0.0181 1211 VAL A C   
8826  O O   . VAL A 1213 ? 0.2202 0.2089 0.1831 0.0216  -0.0081 -0.0211 1211 VAL A O   
8827  C CB  . VAL A 1213 ? 0.2148 0.2061 0.1784 0.0203  -0.0049 -0.0126 1211 VAL A CB  
8828  C CG1 . VAL A 1213 ? 0.2151 0.2082 0.1800 0.0199  -0.0051 -0.0107 1211 VAL A CG1 
8829  C CG2 . VAL A 1213 ? 0.2126 0.2085 0.1731 0.0225  -0.0044 -0.0124 1211 VAL A CG2 
8830  N N   . GLU A 1214 ? 0.2266 0.2093 0.1924 0.0185  -0.0057 -0.0164 1212 GLU A N   
8831  C CA  . GLU A 1214 ? 0.2704 0.2503 0.2364 0.0185  -0.0055 -0.0174 1212 GLU A CA  
8832  C C   . GLU A 1214 ? 0.1933 0.1732 0.1580 0.0188  -0.0029 -0.0145 1212 GLU A C   
8833  O O   . GLU A 1214 ? 0.2064 0.1854 0.1720 0.0177  -0.0016 -0.0117 1212 GLU A O   
8834  C CB  . GLU A 1214 ? 0.2832 0.2586 0.2525 0.0161  -0.0066 -0.0177 1212 GLU A CB  
8835  C CG  . GLU A 1214 ? 0.3474 0.3195 0.3178 0.0157  -0.0066 -0.0183 1212 GLU A CG  
8836  C CD  . GLU A 1214 ? 0.3293 0.2979 0.3034 0.0133  -0.0082 -0.0182 1212 GLU A CD  
8837  O OE1 . GLU A 1214 ? 0.4072 0.3753 0.3834 0.0130  -0.0109 -0.0206 1212 GLU A OE1 
8838  O OE2 . GLU A 1214 ? 0.3804 0.3472 0.3556 0.0115  -0.0070 -0.0157 1212 GLU A OE2 
8839  N N   . GLU A 1215 ? 0.1987 0.1800 0.1616 0.0204  -0.0024 -0.0153 1213 GLU A N   
8840  C CA  . GLU A 1215 ? 0.2121 0.1934 0.1741 0.0207  -0.0001 -0.0125 1213 GLU A CA  
8841  C C   . GLU A 1215 ? 0.2153 0.1919 0.1791 0.0191  0.0003  -0.0123 1213 GLU A C   
8842  O O   . GLU A 1215 ? 0.2054 0.1796 0.1704 0.0189  -0.0011 -0.0147 1213 GLU A O   
8843  C CB  . GLU A 1215 ? 0.1933 0.1789 0.1528 0.0229  0.0003  -0.0133 1213 GLU A CB  
8844  C CG  . GLU A 1215 ? 0.2060 0.1977 0.1633 0.0246  -0.0001 -0.0132 1213 GLU A CG  
8845  C CD  . GLU A 1215 ? 0.1934 0.1902 0.1482 0.0269  0.0000  -0.0152 1213 GLU A CD  
8846  O OE1 . GLU A 1215 ? 0.2089 0.2059 0.1636 0.0279  -0.0018 -0.0197 1213 GLU A OE1 
8847  O OE2 . GLU A 1215 ? 0.2229 0.2235 0.1762 0.0277  0.0016  -0.0122 1213 GLU A OE2 
8848  N N   . VAL A 1216 ? 0.1961 0.1713 0.1605 0.0182  0.0021  -0.0094 1214 VAL A N   
8849  C CA  . VAL A 1216 ? 0.2158 0.1874 0.1816 0.0169  0.0027  -0.0088 1214 VAL A CA  
8850  C C   . VAL A 1216 ? 0.2112 0.1836 0.1762 0.0175  0.0047  -0.0066 1214 VAL A C   
8851  O O   . VAL A 1216 ? 0.2129 0.1870 0.1780 0.0178  0.0057  -0.0043 1214 VAL A O   
8852  C CB  . VAL A 1216 ? 0.2178 0.1872 0.1858 0.0147  0.0027  -0.0078 1214 VAL A CB  
8853  C CG1 . VAL A 1216 ? 0.2314 0.1981 0.2005 0.0134  0.0035  -0.0070 1214 VAL A CG1 
8854  C CG2 . VAL A 1216 ? 0.2306 0.1994 0.1999 0.0137  0.0007  -0.0096 1214 VAL A CG2 
8855  N N   . SER A 1217 ? 0.2074 0.1786 0.1721 0.0179  0.0050  -0.0072 1215 SER A N   
8856  C CA  . SER A 1217 ? 0.1995 0.1711 0.1639 0.0182  0.0067  -0.0051 1215 SER A CA  
8857  C C   . SER A 1217 ? 0.1966 0.1645 0.1628 0.0164  0.0072  -0.0044 1215 SER A C   
8858  O O   . SER A 1217 ? 0.2079 0.1733 0.1750 0.0155  0.0061  -0.0058 1215 SER A O   
8859  C CB  . SER A 1217 ? 0.2169 0.1908 0.1798 0.0200  0.0068  -0.0063 1215 SER A CB  
8860  O OG  . SER A 1217 ? 0.2461 0.2195 0.2093 0.0199  0.0082  -0.0045 1215 SER A OG  
8861  N N   . ALA A 1218 ? 0.2153 0.1829 0.1824 0.0159  0.0085  -0.0021 1216 ALA A N   
8862  C CA  . ALA A 1218 ? 0.2121 0.1771 0.1807 0.0143  0.0090  -0.0015 1216 ALA A CA  
8863  C C   . ALA A 1218 ? 0.2017 0.1671 0.1705 0.0148  0.0104  0.0002  1216 ALA A C   
8864  O O   . ALA A 1218 ? 0.2132 0.1802 0.1825 0.0154  0.0110  0.0021  1216 ALA A O   
8865  C CB  . ALA A 1218 ? 0.2181 0.1825 0.1883 0.0129  0.0091  -0.0011 1216 ALA A CB  
8866  N N   . SER A 1219 ? 0.2102 0.1740 0.1791 0.0145  0.0106  0.0000  1217 SER A N   
8867  C CA  . SER A 1219 ? 0.2097 0.1739 0.1792 0.0147  0.0117  0.0016  1217 SER A CA  
8868  C C   . SER A 1219 ? 0.1881 0.1500 0.1591 0.0131  0.0120  0.0019  1217 SER A C   
8869  O O   . SER A 1219 ? 0.2080 0.1683 0.1790 0.0123  0.0114  0.0009  1217 SER A O   
8870  C CB  . SER A 1219 ? 0.2256 0.1910 0.1938 0.0161  0.0118  0.0010  1217 SER A CB  
8871  O OG  . SER A 1219 ? 0.2181 0.1842 0.1869 0.0163  0.0130  0.0029  1217 SER A OG  
8872  N N   . ILE A 1220 ? 0.2030 0.1650 0.1757 0.0126  0.0127  0.0032  1218 ILE A N   
8873  C CA  . ILE A 1220 ? 0.2057 0.1663 0.1799 0.0112  0.0129  0.0031  1218 ILE A CA  
8874  C C   . ILE A 1220 ? 0.1919 0.1525 0.1673 0.0114  0.0137  0.0045  1218 ILE A C   
8875  O O   . ILE A 1220 ? 0.2200 0.1815 0.1966 0.0121  0.0141  0.0061  1218 ILE A O   
8876  C CB  . ILE A 1220 ? 0.2528 0.2138 0.2289 0.0107  0.0128  0.0028  1218 ILE A CB  
8877  C CG1 . ILE A 1220 ? 0.2854 0.2471 0.2605 0.0106  0.0121  0.0017  1218 ILE A CG1 
8878  C CG2 . ILE A 1220 ? 0.2765 0.2372 0.2542 0.0094  0.0130  0.0021  1218 ILE A CG2 
8879  C CD1 . ILE A 1220 ? 0.3792 0.3419 0.3560 0.0110  0.0120  0.0017  1218 ILE A CD1 
8880  N N   . ASN A 1221 ? 0.2068 0.1663 0.1820 0.0106  0.0137  0.0041  1219 ASN A N   
8881  C CA  . ASN A 1221 ? 0.2217 0.1812 0.1982 0.0106  0.0143  0.0053  1219 ASN A CA  
8882  C C   . ASN A 1221 ? 0.2405 0.1996 0.2195 0.0096  0.0143  0.0052  1219 ASN A C   
8883  O O   . ASN A 1221 ? 0.2635 0.2225 0.2428 0.0085  0.0141  0.0040  1219 ASN A O   
8884  C CB  . ASN A 1221 ? 0.2180 0.1766 0.1937 0.0102  0.0141  0.0049  1219 ASN A CB  
8885  C CG  . ASN A 1221 ? 0.2342 0.1929 0.2114 0.0099  0.0147  0.0060  1219 ASN A CG  
8886  O OD1 . ASN A 1221 ? 0.2302 0.1895 0.2090 0.0101  0.0152  0.0072  1219 ASN A OD1 
8887  N ND2 . ASN A 1221 ? 0.2733 0.2313 0.2502 0.0094  0.0144  0.0057  1219 ASN A ND2 
8888  N N   . THR A 1222 ? 0.2310 0.1905 0.2122 0.0101  0.0145  0.0064  1220 THR A N   
8889  C CA  . THR A 1222 ? 0.2588 0.2179 0.2432 0.0095  0.0142  0.0057  1220 THR A CA  
8890  C C   . THR A 1222 ? 0.3051 0.2638 0.2915 0.0089  0.0143  0.0060  1220 THR A C   
8891  O O   . THR A 1222 ? 0.3353 0.2938 0.3248 0.0085  0.0138  0.0049  1220 THR A O   
8892  C CB  . THR A 1222 ? 0.2839 0.2433 0.2710 0.0102  0.0138  0.0068  1220 THR A CB  
8893  O OG1 . THR A 1222 ? 0.2643 0.2244 0.2521 0.0109  0.0141  0.0098  1220 THR A OG1 
8894  C CG2 . THR A 1222 ? 0.2546 0.2146 0.2399 0.0108  0.0136  0.0062  1220 THR A CG2 
8895  N N   . ALA A 1223 ? 0.2539 0.2127 0.2390 0.0090  0.0148  0.0072  1221 ALA A N   
8896  C CA  . ALA A 1223 ? 0.3035 0.2620 0.2901 0.0083  0.0148  0.0075  1221 ALA A CA  
8897  C C   . ALA A 1223 ? 0.3498 0.3083 0.3345 0.0074  0.0147  0.0059  1221 ALA A C   
8898  O O   . ALA A 1223 ? 0.3885 0.3471 0.3741 0.0068  0.0147  0.0061  1221 ALA A O   
8899  C CB  . ALA A 1223 ? 0.3063 0.2655 0.2930 0.0090  0.0154  0.0099  1221 ALA A CB  
8900  N N   . ALA A 1224 ? 0.3403 0.2991 0.3229 0.0071  0.0145  0.0047  1222 ALA A N   
8901  C CA  . ALA A 1224 ? 0.3537 0.3128 0.3347 0.0061  0.0142  0.0041  1222 ALA A CA  
8902  C C   . ALA A 1224 ? 0.3940 0.3546 0.3764 0.0049  0.0139  0.0030  1222 ALA A C   
8903  O O   . ALA A 1224 ? 0.4021 0.3633 0.3838 0.0040  0.0137  0.0033  1222 ALA A O   
8904  C CB  . ALA A 1224 ? 0.3452 0.3046 0.3244 0.0058  0.0138  0.0034  1222 ALA A CB  
8905  N N   . ALA A 1225 ? 0.3935 0.3548 0.3781 0.0049  0.0138  0.0016  1223 ALA A N   
8906  C CA  . ALA A 1225 ? 0.4469 0.4103 0.4330 0.0041  0.0134  -0.0001 1223 ALA A CA  
8907  C C   . ALA A 1225 ? 0.4628 0.4255 0.4507 0.0039  0.0134  0.0005  1223 ALA A C   
8908  O O   . ALA A 1225 ? 0.4908 0.4554 0.4799 0.0032  0.0130  -0.0010 1223 ALA A O   
8909  C CB  . ALA A 1225 ? 0.3918 0.3563 0.3803 0.0045  0.0131  -0.0025 1223 ALA A CB  
8910  N N   . GLY A 1226 ? 0.4174 0.3781 0.4055 0.0046  0.0138  0.0027  1224 GLY A N   
8911  C CA  . GLY A 1226 ? 0.4381 0.3983 0.4280 0.0044  0.0138  0.0038  1224 GLY A CA  
8912  C C   . GLY A 1226 ? 0.4616 0.4207 0.4551 0.0051  0.0137  0.0050  1224 GLY A C   
8913  O O   . GLY A 1226 ? 0.4892 0.4482 0.4847 0.0048  0.0136  0.0063  1224 GLY A O   
8914  N N   . GLY A 1227 ? 0.3841 0.3426 0.3788 0.0057  0.0135  0.0051  1225 GLY A N   
8915  C CA  . GLY A 1227 ? 0.4050 0.3626 0.4037 0.0061  0.0132  0.0069  1225 GLY A CA  
8916  C C   . GLY A 1227 ? 0.4316 0.3888 0.4307 0.0069  0.0131  0.0074  1225 GLY A C   
8917  O O   . GLY A 1227 ? 0.4256 0.3832 0.4221 0.0072  0.0132  0.0057  1225 GLY A O   
8918  N N   . ASN A 1228 ? 0.3653 0.3221 0.3678 0.0073  0.0127  0.0100  1226 ASN A N   
8919  C CA  . ASN A 1228 ? 0.3926 0.3494 0.3958 0.0080  0.0125  0.0115  1226 ASN A CA  
8920  C C   . ASN A 1228 ? 0.4699 0.4254 0.4794 0.0080  0.0110  0.0108  1226 ASN A C   
8921  O O   . ASN A 1228 ? 0.4619 0.4168 0.4764 0.0076  0.0101  0.0130  1226 ASN A O   
8922  C CB  . ASN A 1228 ? 0.4291 0.3875 0.4316 0.0085  0.0133  0.0156  1226 ASN A CB  
8923  C CG  . ASN A 1228 ? 0.4535 0.4129 0.4560 0.0093  0.0132  0.0174  1226 ASN A CG  
8924  O OD1 . ASN A 1228 ? 0.4349 0.3931 0.4396 0.0095  0.0122  0.0162  1226 ASN A OD1 
8925  N ND2 . ASN A 1228 ? 0.3852 0.3471 0.3852 0.0100  0.0141  0.0203  1226 ASN A ND2 
8926  N N   . ALA A 1229 ? 0.4433 0.3985 0.4530 0.0084  0.0104  0.0078  1227 ALA A N   
8927  C CA  . ALA A 1229 ? 0.5091 0.4630 0.5251 0.0086  0.0087  0.0064  1227 ALA A CA  
8928  C C   . ALA A 1229 ? 0.4956 0.4487 0.5159 0.0089  0.0078  0.0104  1227 ALA A C   
8929  O O   . ALA A 1229 ? 0.5074 0.4591 0.5345 0.0087  0.0062  0.0113  1227 ALA A O   
8930  C CB  . ALA A 1229 ? 0.4638 0.4184 0.4789 0.0091  0.0084  0.0023  1227 ALA A CB  
8931  N N   . SER A 1230 ? 0.4713 0.4257 0.4881 0.0094  0.0087  0.0130  1228 SER A N   
8932  C CA  . SER A 1230 ? 0.4934 0.4482 0.5139 0.0097  0.0080  0.0174  1228 SER A CA  
8933  C C   . SER A 1230 ? 0.5373 0.4925 0.5615 0.0089  0.0077  0.0216  1228 SER A C   
8934  O O   . SER A 1230 ? 0.5525 0.5068 0.5836 0.0086  0.0060  0.0243  1228 SER A O   
8935  C CB  . SER A 1230 ? 0.4847 0.4419 0.4998 0.0104  0.0092  0.0193  1228 SER A CB  
8936  O OG  . SER A 1230 ? 0.6292 0.5861 0.6413 0.0110  0.0094  0.0158  1228 SER A OG  
8937  N N   . LEU A 1231 ? 0.4846 0.4411 0.5048 0.0085  0.0091  0.0222  1229 LEU A N   
8938  C CA  . LEU A 1231 ? 0.5426 0.5004 0.5659 0.0078  0.0090  0.0264  1229 LEU A CA  
8939  C C   . LEU A 1231 ? 0.6214 0.5767 0.6511 0.0068  0.0075  0.0252  1229 LEU A C   
8940  O O   . LEU A 1231 ? 0.6339 0.5897 0.6687 0.0060  0.0067  0.0292  1229 LEU A O   
8941  C CB  . LEU A 1231 ? 0.4748 0.4353 0.4921 0.0079  0.0111  0.0272  1229 LEU A CB  
8942  C CG  . LEU A 1231 ? 0.4562 0.4211 0.4708 0.0085  0.0122  0.0315  1229 LEU A CG  
8943  C CD1 . LEU A 1231 ? 0.3916 0.3590 0.4026 0.0086  0.0138  0.0319  1229 LEU A CD1 
8944  C CD2 . LEU A 1231 ? 0.4382 0.4047 0.4589 0.0079  0.0111  0.0370  1229 LEU A CD2 
8945  N N   . MET A 1232 ? 0.5991 0.5523 0.6287 0.0068  0.0069  0.0199  1230 MET A N   
8946  C CA  . MET A 1232 ? 0.6585 0.6096 0.6946 0.0062  0.0051  0.0180  1230 MET A CA  
8947  C C   . MET A 1232 ? 0.7007 0.6499 0.7457 0.0061  0.0026  0.0198  1230 MET A C   
8948  O O   . MET A 1232 ? 0.6923 0.6397 0.7442 0.0054  0.0007  0.0196  1230 MET A O   
8949  C CB  . MET A 1232 ? 0.6573 0.6077 0.6913 0.0065  0.0050  0.0116  1230 MET A CB  
8950  N N   . ALA A 1233 ? 0.7520 0.7014 0.7974 0.0068  0.0023  0.0216  1231 ALA A N   
8951  C CA  . ALA A 1233 ? 0.7297 0.6776 0.7838 0.0067  -0.0001 0.0245  1231 ALA A CA  
8952  C C   . ALA A 1233 ? 0.7649 0.7153 0.8199 0.0060  0.0003  0.0321  1231 ALA A C   
8953  O O   . ALA A 1233 ? 0.7820 0.7345 0.8354 0.0052  0.0014  0.0351  1231 ALA A O   
8954  C CB  . ALA A 1233 ? 0.7254 0.6722 0.7802 0.0080  -0.0009 0.0218  1231 ALA A CB  
8955  N N   . ALA B 16   ? 0.6289 0.5129 0.5849 0.0765  -0.0212 -0.0383 14   ALA B N   
8956  C CA  . ALA B 16   ? 0.6762 0.5673 0.6356 0.0701  -0.0198 -0.0373 14   ALA B CA  
8957  C C   . ALA B 16   ? 0.7521 0.6338 0.7037 0.0643  -0.0214 -0.0372 14   ALA B C   
8958  O O   . ALA B 16   ? 0.7920 0.6658 0.7369 0.0648  -0.0214 -0.0391 14   ALA B O   
8959  C CB  . ALA B 16   ? 0.6159 0.5164 0.5799 0.0713  -0.0160 -0.0386 14   ALA B CB  
8960  N N   . PRO B 17   ? 0.6537 0.5363 0.6061 0.0587  -0.0228 -0.0350 15   PRO B N   
8961  C CA  . PRO B 17   ? 0.5975 0.4727 0.5433 0.0527  -0.0242 -0.0346 15   PRO B CA  
8962  C C   . PRO B 17   ? 0.5540 0.4315 0.4990 0.0505  -0.0219 -0.0361 15   PRO B C   
8963  O O   . PRO B 17   ? 0.5169 0.4050 0.4683 0.0505  -0.0192 -0.0363 15   PRO B O   
8964  C CB  . PRO B 17   ? 0.6281 0.5086 0.5777 0.0478  -0.0249 -0.0319 15   PRO B CB  
8965  C CG  . PRO B 17   ? 0.6645 0.5494 0.6192 0.0518  -0.0255 -0.0310 15   PRO B CG  
8966  C CD  . PRO B 17   ? 0.6220 0.5121 0.5809 0.0578  -0.0233 -0.0328 15   PRO B CD  
8967  N N   . ALA B 18   ? 0.5252 0.3924 0.4619 0.0485  -0.0233 -0.0371 16   ALA B N   
8968  C CA  . ALA B 18   ? 0.5034 0.3718 0.4384 0.0459  -0.0217 -0.0385 16   ALA B CA  
8969  C C   . ALA B 18   ? 0.4315 0.3087 0.3713 0.0400  -0.0206 -0.0367 16   ALA B C   
8970  O O   . ALA B 18   ? 0.4108 0.2875 0.3507 0.0360  -0.0222 -0.0346 16   ALA B O   
8971  C CB  . ALA B 18   ? 0.4902 0.3453 0.4150 0.0438  -0.0240 -0.0395 16   ALA B CB  
8972  N N   . PRO B 19   ? 0.4080 0.2933 0.3517 0.0394  -0.0179 -0.0375 17   PRO B N   
8973  C CA  . PRO B 19   ? 0.3852 0.2792 0.3337 0.0345  -0.0168 -0.0359 17   PRO B CA  
8974  C C   . PRO B 19   ? 0.3478 0.2366 0.2915 0.0283  -0.0188 -0.0347 17   PRO B C   
8975  O O   . PRO B 19   ? 0.3833 0.2643 0.3203 0.0267  -0.0199 -0.0357 17   PRO B O   
8976  C CB  . PRO B 19   ? 0.3804 0.2809 0.3315 0.0355  -0.0139 -0.0373 17   PRO B CB  
8977  C CG  . PRO B 19   ? 0.4176 0.3173 0.3689 0.0420  -0.0128 -0.0391 17   PRO B CG  
8978  C CD  . PRO B 19   ? 0.4443 0.3320 0.3886 0.0440  -0.0155 -0.0398 17   PRO B CD  
8979  N N   . PHE B 20   ? 0.3777 0.2709 0.3246 0.0247  -0.0192 -0.0324 18   PHE B N   
8980  C CA  . PHE B 20   ? 0.3512 0.2422 0.2951 0.0185  -0.0207 -0.0308 18   PHE B CA  
8981  C C   . PHE B 20   ? 0.3763 0.2552 0.3123 0.0169  -0.0238 -0.0304 18   PHE B C   
8982  O O   . PHE B 20   ? 0.4100 0.2858 0.3423 0.0116  -0.0252 -0.0293 18   PHE B O   
8983  C CB  . PHE B 20   ? 0.3403 0.2345 0.2838 0.0152  -0.0194 -0.0315 18   PHE B CB  
8984  C CG  . PHE B 20   ? 0.3338 0.2395 0.2847 0.0162  -0.0165 -0.0316 18   PHE B CG  
8985  C CD1 . PHE B 20   ? 0.3070 0.2208 0.2634 0.0139  -0.0157 -0.0298 18   PHE B CD1 
8986  C CD2 . PHE B 20   ? 0.3154 0.2235 0.2673 0.0194  -0.0146 -0.0335 18   PHE B CD2 
8987  C CE1 . PHE B 20   ? 0.2943 0.2179 0.2571 0.0147  -0.0132 -0.0299 18   PHE B CE1 
8988  C CE2 . PHE B 20   ? 0.2958 0.2141 0.2542 0.0200  -0.0120 -0.0334 18   PHE B CE2 
8989  C CZ  . PHE B 20   ? 0.3078 0.2335 0.2716 0.0177  -0.0114 -0.0316 18   PHE B CZ  
8990  N N   . ALA B 21   ? 0.4132 0.2851 0.3464 0.0214  -0.0251 -0.0312 19   ALA B N   
8991  C CA  . ALA B 21   ? 0.4202 0.2794 0.3453 0.0201  -0.0283 -0.0308 19   ALA B CA  
8992  C C   . ALA B 21   ? 0.4458 0.3043 0.3704 0.0157  -0.0301 -0.0279 19   ALA B C   
8993  O O   . ALA B 21   ? 0.4929 0.3421 0.4107 0.0122  -0.0327 -0.0270 19   ALA B O   
8994  C CB  . ALA B 21   ? 0.4504 0.3029 0.3731 0.0267  -0.0292 -0.0322 19   ALA B CB  
8995  N N   . ASP B 22   ? 0.3966 0.2644 0.3279 0.0155  -0.0289 -0.0264 20   ASP B N   
8996  C CA  . ASP B 22   ? 0.4012 0.2693 0.3321 0.0113  -0.0303 -0.0237 20   ASP B CA  
8997  C C   . ASP B 22   ? 0.3429 0.2226 0.2799 0.0079  -0.0281 -0.0226 20   ASP B C   
8998  O O   . ASP B 22   ? 0.3643 0.2492 0.3048 0.0073  -0.0278 -0.0210 20   ASP B O   
8999  C CB  . ASP B 22   ? 0.4317 0.2981 0.3636 0.0148  -0.0315 -0.0228 20   ASP B CB  
9000  N N   . PHE B 23   ? 0.2943 0.1779 0.2322 0.0057  -0.0265 -0.0235 21   PHE B N   
9001  C CA  . PHE B 23   ? 0.3042 0.1992 0.2484 0.0037  -0.0242 -0.0228 21   PHE B CA  
9002  C C   . PHE B 23   ? 0.3100 0.2073 0.2541 -0.0012 -0.0248 -0.0203 21   PHE B C   
9003  O O   . PHE B 23   ? 0.3073 0.2115 0.2560 -0.0010 -0.0238 -0.0193 21   PHE B O   
9004  C CB  . PHE B 23   ? 0.2976 0.1956 0.2422 0.0023  -0.0227 -0.0241 21   PHE B CB  
9005  C CG  . PHE B 23   ? 0.3040 0.2130 0.2545 0.0000  -0.0206 -0.0233 21   PHE B CG  
9006  C CD1 . PHE B 23   ? 0.2919 0.2090 0.2489 0.0029  -0.0185 -0.0236 21   PHE B CD1 
9007  C CD2 . PHE B 23   ? 0.2955 0.2064 0.2447 -0.0052 -0.0207 -0.0222 21   PHE B CD2 
9008  C CE1 . PHE B 23   ? 0.2810 0.2074 0.2430 0.0010  -0.0167 -0.0229 21   PHE B CE1 
9009  C CE2 . PHE B 23   ? 0.3087 0.2296 0.2632 -0.0069 -0.0187 -0.0214 21   PHE B CE2 
9010  C CZ  . PHE B 23   ? 0.2874 0.2157 0.2481 -0.0037 -0.0167 -0.0219 21   PHE B CZ  
9011  N N   . ALA B 24   ? 0.3167 0.2082 0.2552 -0.0058 -0.0265 -0.0192 22   ALA B N   
9012  C CA  . ALA B 24   ? 0.3080 0.2020 0.2461 -0.0108 -0.0270 -0.0166 22   ALA B CA  
9013  C C   . ALA B 24   ? 0.3079 0.1921 0.2384 -0.0150 -0.0298 -0.0153 22   ALA B C   
9014  O O   . ALA B 24   ? 0.3277 0.2135 0.2569 -0.0202 -0.0299 -0.0141 22   ALA B O   
9015  C CB  . ALA B 24   ? 0.3153 0.2195 0.2580 -0.0137 -0.0248 -0.0162 22   ALA B CB  
9016  N N   . PRO B 25   ? 0.3196 0.1936 0.2451 -0.0131 -0.0321 -0.0152 23   PRO B N   
9017  C CA  . PRO B 25   ? 0.3766 0.2402 0.2943 -0.0173 -0.0350 -0.0139 23   PRO B CA  
9018  C C   . PRO B 25   ? 0.3493 0.2161 0.2666 -0.0228 -0.0354 -0.0107 23   PRO B C   
9019  O O   . PRO B 25   ? 0.3464 0.2188 0.2673 -0.0219 -0.0345 -0.0095 23   PRO B O   
9020  C CB  . PRO B 25   ? 0.4029 0.2562 0.3164 -0.0129 -0.0372 -0.0144 23   PRO B CB  
9021  C CG  . PRO B 25   ? 0.4024 0.2628 0.3221 -0.0084 -0.0356 -0.0146 23   PRO B CG  
9022  C CD  . PRO B 25   ? 0.3322 0.2044 0.2591 -0.0074 -0.0324 -0.0160 23   PRO B CD  
9023  N N   . PRO B 26   ? 0.3391 0.2031 0.2524 -0.0288 -0.0366 -0.0092 24   PRO B N   
9024  C CA  . PRO B 26   ? 0.3385 0.2063 0.2515 -0.0342 -0.0368 -0.0060 24   PRO B CA  
9025  C C   . PRO B 26   ? 0.3816 0.2416 0.2900 -0.0343 -0.0390 -0.0041 24   PRO B C   
9026  O O   . PRO B 26   ? 0.3778 0.2270 0.2814 -0.0314 -0.0412 -0.0050 24   PRO B O   
9027  C CB  . PRO B 26   ? 0.3678 0.2333 0.2771 -0.0404 -0.0380 -0.0051 24   PRO B CB  
9028  C CG  . PRO B 26   ? 0.3860 0.2398 0.2897 -0.0383 -0.0401 -0.0073 24   PRO B CG  
9029  C CD  . PRO B 26   ? 0.3944 0.2506 0.3023 -0.0309 -0.0384 -0.0103 24   PRO B CD  
9030  N N   . VAL B 27   ? 0.3592 0.2247 0.2687 -0.0376 -0.0384 -0.0015 25   VAL B N   
9031  C CA  . VAL B 27   ? 0.3543 0.2130 0.2592 -0.0382 -0.0404 0.0008  25   VAL B CA  
9032  C C   . VAL B 27   ? 0.3771 0.2226 0.2734 -0.0418 -0.0439 0.0020  25   VAL B C   
9033  O O   . VAL B 27   ? 0.4146 0.2497 0.3058 -0.0398 -0.0464 0.0024  25   VAL B O   
9034  C CB  . VAL B 27   ? 0.3594 0.2269 0.2666 -0.0416 -0.0390 0.0034  25   VAL B CB  
9035  C CG1 . VAL B 27   ? 0.3742 0.2340 0.2755 -0.0434 -0.0414 0.0062  25   VAL B CG1 
9036  C CG2 . VAL B 27   ? 0.3401 0.2183 0.2547 -0.0372 -0.0361 0.0020  25   VAL B CG2 
9037  N N   . ARG B 28   ? 0.3779 0.2234 0.2724 -0.0471 -0.0443 0.0026  26   ARG B N   
9038  C CA  . ARG B 28   ? 0.3918 0.2247 0.2779 -0.0514 -0.0477 0.0039  26   ARG B CA  
9039  C C   . ARG B 28   ? 0.4270 0.2603 0.3128 -0.0542 -0.0477 0.0025  26   ARG B C   
9040  O O   . ARG B 28   ? 0.3945 0.2393 0.2867 -0.0543 -0.0450 0.0016  26   ARG B O   
9041  C CB  . ARG B 28   ? 0.4251 0.2575 0.3077 -0.0579 -0.0488 0.0080  26   ARG B CB  
9042  C CG  . ARG B 28   ? 0.4045 0.2493 0.2914 -0.0636 -0.0466 0.0098  26   ARG B CG  
9043  C CD  . ARG B 28   ? 0.3948 0.2404 0.2788 -0.0696 -0.0473 0.0140  26   ARG B CD  
9044  N NE  . ARG B 28   ? 0.4515 0.3021 0.3380 -0.0666 -0.0457 0.0149  26   ARG B NE  
9045  C CZ  . ARG B 28   ? 0.4630 0.3051 0.3448 -0.0651 -0.0477 0.0161  26   ARG B CZ  
9046  N NH1 . ARG B 28   ? 0.4994 0.3272 0.3734 -0.0664 -0.0514 0.0168  26   ARG B NH1 
9047  N NH2 . ARG B 28   ? 0.4233 0.2711 0.3079 -0.0622 -0.0462 0.0166  26   ARG B NH2 
9048  N N   . PRO B 29   ? 0.4336 0.2541 0.3118 -0.0563 -0.0509 0.0022  27   PRO B N   
9049  C CA  . PRO B 29   ? 0.4259 0.2465 0.3031 -0.0601 -0.0513 0.0014  27   PRO B CA  
9050  C C   . PRO B 29   ? 0.4469 0.2781 0.3272 -0.0673 -0.0503 0.0044  27   PRO B C   
9051  O O   . PRO B 29   ? 0.4468 0.2780 0.3251 -0.0717 -0.0510 0.0078  27   PRO B O   
9052  C CB  . PRO B 29   ? 0.4808 0.2842 0.3479 -0.0620 -0.0555 0.0014  27   PRO B CB  
9053  C CG  . PRO B 29   ? 0.5279 0.3226 0.3921 -0.0560 -0.0566 0.0006  27   PRO B CG  
9054  C CD  . PRO B 29   ? 0.4579 0.2628 0.3278 -0.0552 -0.0544 0.0027  27   PRO B CD  
9055  N N   . GLN B 30   ? 0.4207 0.2612 0.3059 -0.0682 -0.0484 0.0032  28   GLN B N   
9056  C CA  . GLN B 30   ? 0.4404 0.2929 0.3299 -0.0740 -0.0469 0.0057  28   GLN B CA  
9057  C C   . GLN B 30   ? 0.4434 0.2896 0.3269 -0.0819 -0.0500 0.0080  28   GLN B C   
9058  O O   . GLN B 30   ? 0.4472 0.2869 0.3270 -0.0830 -0.0519 0.0062  28   GLN B O   
9059  C CB  . GLN B 30   ? 0.4218 0.2866 0.3189 -0.0716 -0.0439 0.0036  28   GLN B CB  
9060  C CG  . GLN B 30   ? 0.3721 0.2423 0.2749 -0.0639 -0.0410 0.0013  28   GLN B CG  
9061  C CD  . GLN B 30   ? 0.3758 0.2541 0.2826 -0.0635 -0.0390 0.0034  28   GLN B CD  
9062  O OE1 . GLN B 30   ? 0.3728 0.2631 0.2847 -0.0659 -0.0368 0.0048  28   GLN B OE1 
9063  N NE2 . GLN B 30   ? 0.3641 0.2359 0.2683 -0.0605 -0.0399 0.0036  28   GLN B NE2 
9064  N N   . SER B 31   ? 0.4139 0.2619 0.2959 -0.0876 -0.0505 0.0118  29   SER B N   
9065  C CA  . SER B 31   ? 0.4249 0.2684 0.3018 -0.0960 -0.0534 0.0146  29   SER B CA  
9066  C C   . SER B 31   ? 0.4018 0.2567 0.2836 -0.0999 -0.0522 0.0147  29   SER B C   
9067  O O   . SER B 31   ? 0.3999 0.2669 0.2894 -0.0964 -0.0490 0.0131  29   SER B O   
9068  C CB  . SER B 31   ? 0.4443 0.2891 0.3194 -0.1010 -0.0537 0.0189  29   SER B CB  
9069  O OG  . SER B 31   ? 0.4092 0.2710 0.2923 -0.1021 -0.0501 0.0205  29   SER B OG  
9070  N N   . THR B 32   ? 0.4479 0.2986 0.3253 -0.1075 -0.0551 0.0168  30   THR B N   
9071  C CA  . THR B 32   ? 0.4248 0.2867 0.3067 -0.1123 -0.0544 0.0177  30   THR B CA  
9072  C C   . THR B 32   ? 0.3934 0.2732 0.2840 -0.1129 -0.0505 0.0199  30   THR B C   
9073  O O   . THR B 32   ? 0.4092 0.3012 0.3068 -0.1111 -0.0480 0.0187  30   THR B O   
9074  C CB  . THR B 32   ? 0.4694 0.3240 0.3448 -0.1213 -0.0583 0.0204  30   THR B CB  
9075  O OG1 . THR B 32   ? 0.5242 0.3629 0.3918 -0.1202 -0.0618 0.0177  30   THR B OG1 
9076  C CG2 . THR B 32   ? 0.5114 0.3797 0.3923 -0.1270 -0.0576 0.0222  30   THR B CG2 
9077  N N   . LEU B 33   ? 0.3863 0.2675 0.2760 -0.1152 -0.0500 0.0231  31   LEU B N   
9078  C CA  . LEU B 33   ? 0.3626 0.2602 0.2598 -0.1156 -0.0463 0.0251  31   LEU B CA  
9079  C C   . LEU B 33   ? 0.3549 0.2597 0.2585 -0.1071 -0.0426 0.0221  31   LEU B C   
9080  O O   . LEU B 33   ? 0.3462 0.2655 0.2572 -0.1060 -0.0395 0.0222  31   LEU B O   
9081  C CB  . LEU B 33   ? 0.3610 0.2572 0.2548 -0.1197 -0.0466 0.0291  31   LEU B CB  
9082  C CG  . LEU B 33   ? 0.3780 0.2703 0.2669 -0.1292 -0.0498 0.0327  31   LEU B CG  
9083  C CD1 . LEU B 33   ? 0.4091 0.2961 0.2928 -0.1332 -0.0509 0.0364  31   LEU B CD1 
9084  C CD2 . LEU B 33   ? 0.4229 0.3309 0.3184 -0.1340 -0.0481 0.0345  31   LEU B CD2 
9085  N N   . ARG B 34   ? 0.3425 0.2376 0.2432 -0.1009 -0.0431 0.0196  32   ARG B N   
9086  C CA  . ARG B 34   ? 0.3391 0.2407 0.2458 -0.0932 -0.0399 0.0168  32   ARG B CA  
9087  C C   . ARG B 34   ? 0.3418 0.2488 0.2531 -0.0907 -0.0389 0.0139  32   ARG B C   
9088  O O   . ARG B 34   ? 0.3222 0.2409 0.2406 -0.0872 -0.0357 0.0128  32   ARG B O   
9089  C CB  . ARG B 34   ? 0.3277 0.2180 0.2307 -0.0873 -0.0409 0.0148  32   ARG B CB  
9090  C CG  . ARG B 34   ? 0.3577 0.2448 0.2576 -0.0879 -0.0412 0.0173  32   ARG B CG  
9091  C CD  . ARG B 34   ? 0.3515 0.2518 0.2578 -0.0856 -0.0375 0.0180  32   ARG B CD  
9092  N NE  . ARG B 34   ? 0.3481 0.2513 0.2591 -0.0779 -0.0354 0.0146  32   ARG B NE  
9093  C CZ  . ARG B 34   ? 0.3416 0.2390 0.2511 -0.0729 -0.0357 0.0135  32   ARG B CZ  
9094  N NH1 . ARG B 34   ? 0.3367 0.2245 0.2400 -0.0744 -0.0380 0.0154  32   ARG B NH1 
9095  N NH2 . ARG B 34   ? 0.3139 0.2150 0.2282 -0.0664 -0.0339 0.0106  32   ARG B NH2 
9096  N N   . ARG B 35   ? 0.3390 0.2374 0.2460 -0.0925 -0.0416 0.0126  33   ARG B N   
9097  C CA  . ARG B 35   ? 0.3806 0.2836 0.2911 -0.0905 -0.0409 0.0100  33   ARG B CA  
9098  C C   . ARG B 35   ? 0.3473 0.2651 0.2640 -0.0945 -0.0391 0.0119  33   ARG B C   
9099  O O   . ARG B 35   ? 0.3277 0.2545 0.2503 -0.0911 -0.0369 0.0101  33   ARG B O   
9100  C CB  . ARG B 35   ? 0.4078 0.2978 0.3113 -0.0923 -0.0444 0.0085  33   ARG B CB  
9101  C CG  . ARG B 35   ? 0.4138 0.2914 0.3130 -0.0860 -0.0454 0.0054  33   ARG B CG  
9102  C CD  . ARG B 35   ? 0.4398 0.3040 0.3314 -0.0874 -0.0489 0.0036  33   ARG B CD  
9103  N NE  . ARG B 35   ? 0.5216 0.3738 0.4088 -0.0812 -0.0496 0.0010  33   ARG B NE  
9104  C CZ  . ARG B 35   ? 0.6116 0.4656 0.5020 -0.0739 -0.0476 -0.0023 33   ARG B CZ  
9105  N NH1 . ARG B 35   ? 0.6320 0.4976 0.5293 -0.0720 -0.0449 -0.0035 33   ARG B NH1 
9106  N NH2 . ARG B 35   ? 0.5416 0.3857 0.4286 -0.0684 -0.0482 -0.0041 33   ARG B NH2 
9107  N N   . ALA B 36   ? 0.3440 0.2648 0.2595 -0.1016 -0.0401 0.0156  34   ALA B N   
9108  C CA  . ALA B 36   ? 0.3297 0.2654 0.2514 -0.1054 -0.0385 0.0176  34   ALA B CA  
9109  C C   . ALA B 36   ? 0.3149 0.2639 0.2441 -0.1010 -0.0342 0.0177  34   ALA B C   
9110  O O   . ALA B 36   ? 0.3226 0.2840 0.2583 -0.1004 -0.0321 0.0176  34   ALA B O   
9111  C CB  . ALA B 36   ? 0.3444 0.2805 0.2631 -0.1141 -0.0405 0.0218  34   ALA B CB  
9112  N N   . ILE B 37   ? 0.2980 0.2443 0.2262 -0.0979 -0.0331 0.0179  35   ILE B N   
9113  C CA  . ILE B 37   ? 0.2697 0.2266 0.2041 -0.0929 -0.0293 0.0173  35   ILE B CA  
9114  C C   . ILE B 37   ? 0.3082 0.2674 0.2468 -0.0864 -0.0277 0.0136  35   ILE B C   
9115  O O   . ILE B 37   ? 0.2731 0.2442 0.2182 -0.0845 -0.0251 0.0132  35   ILE B O   
9116  C CB  . ILE B 37   ? 0.2609 0.2125 0.1923 -0.0908 -0.0289 0.0180  35   ILE B CB  
9117  C CG1 . ILE B 37   ? 0.2822 0.2337 0.2100 -0.0975 -0.0299 0.0221  35   ILE B CG1 
9118  C CG2 . ILE B 37   ? 0.2704 0.2310 0.2076 -0.0848 -0.0253 0.0166  35   ILE B CG2 
9119  C CD1 . ILE B 37   ? 0.3128 0.2554 0.2356 -0.0962 -0.0307 0.0229  35   ILE B CD1 
9120  N N   . THR B 38   ? 0.2855 0.2333 0.2205 -0.0826 -0.0293 0.0108  36   THR B N   
9121  C CA  . THR B 38   ? 0.2747 0.2243 0.2135 -0.0763 -0.0277 0.0074  36   THR B CA  
9122  C C   . THR B 38   ? 0.2759 0.2326 0.2182 -0.0776 -0.0274 0.0068  36   THR B C   
9123  O O   . THR B 38   ? 0.2826 0.2476 0.2306 -0.0736 -0.0250 0.0053  36   THR B O   
9124  C CB  . THR B 38   ? 0.3025 0.2386 0.2362 -0.0725 -0.0296 0.0049  36   THR B CB  
9125  O OG1 . THR B 38   ? 0.3005 0.2298 0.2306 -0.0718 -0.0303 0.0059  36   THR B OG1 
9126  C CG2 . THR B 38   ? 0.2966 0.2352 0.2345 -0.0657 -0.0276 0.0015  36   THR B CG2 
9127  N N   . ALA B 39   ? 0.2921 0.2454 0.2309 -0.0833 -0.0301 0.0080  37   ALA B N   
9128  C CA  . ALA B 39   ? 0.3205 0.2802 0.2622 -0.0850 -0.0303 0.0075  37   ALA B CA  
9129  C C   . ALA B 39   ? 0.3097 0.2855 0.2589 -0.0857 -0.0275 0.0092  37   ALA B C   
9130  O O   . ALA B 39   ? 0.3033 0.2863 0.2567 -0.0845 -0.0267 0.0083  37   ALA B O   
9131  C CB  . ALA B 39   ? 0.3276 0.2807 0.2637 -0.0920 -0.0339 0.0090  37   ALA B CB  
9132  N N   . ALA B 40   ? 0.2769 0.2586 0.2278 -0.0873 -0.0260 0.0118  38   ALA B N   
9133  C CA  . ALA B 40   ? 0.2837 0.2808 0.2414 -0.0879 -0.0232 0.0135  38   ALA B CA  
9134  C C   . ALA B 40   ? 0.2740 0.2774 0.2368 -0.0809 -0.0198 0.0117  38   ALA B C   
9135  O O   . ALA B 40   ? 0.2637 0.2796 0.2321 -0.0803 -0.0173 0.0128  38   ALA B O   
9136  C CB  . ALA B 40   ? 0.2780 0.2792 0.2348 -0.0934 -0.0232 0.0173  38   ALA B CB  
9137  N N   . TYR B 41   ? 0.2644 0.2595 0.2253 -0.0757 -0.0197 0.0091  39   TYR B N   
9138  C CA  . TYR B 41   ? 0.2397 0.2389 0.2043 -0.0697 -0.0167 0.0077  39   TYR B CA  
9139  C C   . TYR B 41   ? 0.2482 0.2598 0.2196 -0.0672 -0.0142 0.0072  39   TYR B C   
9140  O O   . TYR B 41   ? 0.2226 0.2428 0.1976 -0.0656 -0.0117 0.0080  39   TYR B O   
9141  C CB  . TYR B 41   ? 0.2362 0.2251 0.1983 -0.0646 -0.0174 0.0047  39   TYR B CB  
9142  C CG  . TYR B 41   ? 0.2609 0.2496 0.2243 -0.0595 -0.0155 0.0036  39   TYR B CG  
9143  C CD1 . TYR B 41   ? 0.2398 0.2386 0.2080 -0.0573 -0.0127 0.0040  39   TYR B CD1 
9144  C CD2 . TYR B 41   ? 0.2309 0.2089 0.1905 -0.0567 -0.0168 0.0020  39   TYR B CD2 
9145  C CE1 . TYR B 41   ? 0.2444 0.2423 0.2134 -0.0528 -0.0113 0.0028  39   TYR B CE1 
9146  C CE2 . TYR B 41   ? 0.2479 0.2256 0.2087 -0.0522 -0.0154 0.0011  39   TYR B CE2 
9147  C CZ  . TYR B 41   ? 0.2219 0.2093 0.1873 -0.0504 -0.0127 0.0014  39   TYR B CZ  
9148  O OH  . TYR B 41   ? 0.2420 0.2287 0.2082 -0.0462 -0.0116 0.0004  39   TYR B OH  
9149  N N   . ARG B 42   ? 0.2511 0.2633 0.2239 -0.0666 -0.0149 0.0057  40   ARG B N   
9150  C CA  . ARG B 42   ? 0.2383 0.2611 0.2172 -0.0638 -0.0128 0.0051  40   ARG B CA  
9151  C C   . ARG B 42   ? 0.2526 0.2811 0.2330 -0.0681 -0.0141 0.0064  40   ARG B C   
9152  O O   . ARG B 42   ? 0.2720 0.3051 0.2557 -0.0660 -0.0137 0.0053  40   ARG B O   
9153  C CB  . ARG B 42   ? 0.2517 0.2708 0.2317 -0.0577 -0.0121 0.0019  40   ARG B CB  
9154  C CG  . ARG B 42   ? 0.2525 0.2686 0.2323 -0.0535 -0.0105 0.0009  40   ARG B CG  
9155  C CD  . ARG B 42   ? 0.2657 0.2775 0.2463 -0.0479 -0.0099 -0.0020 40   ARG B CD  
9156  N NE  . ARG B 42   ? 0.2387 0.2450 0.2175 -0.0453 -0.0096 -0.0026 40   ARG B NE  
9157  C CZ  . ARG B 42   ? 0.2580 0.2687 0.2392 -0.0426 -0.0075 -0.0026 40   ARG B CZ  
9158  N NH1 . ARG B 42   ? 0.2343 0.2550 0.2201 -0.0414 -0.0054 -0.0022 40   ARG B NH1 
9159  N NH2 . ARG B 42   ? 0.2516 0.2566 0.2305 -0.0408 -0.0077 -0.0030 40   ARG B NH2 
9160  N N   . ARG B 43   ? 0.2417 0.2701 0.2197 -0.0743 -0.0158 0.0090  41   ARG B N   
9161  C CA  . ARG B 43   ? 0.2357 0.2693 0.2148 -0.0792 -0.0175 0.0106  41   ARG B CA  
9162  C C   . ARG B 43   ? 0.2665 0.3149 0.2529 -0.0776 -0.0151 0.0114  41   ARG B C   
9163  O O   . ARG B 43   ? 0.2513 0.3074 0.2412 -0.0755 -0.0124 0.0123  41   ARG B O   
9164  C CB  . ARG B 43   ? 0.2457 0.2781 0.2215 -0.0865 -0.0194 0.0137  41   ARG B CB  
9165  C CG  . ARG B 43   ? 0.2506 0.2889 0.2276 -0.0924 -0.0214 0.0158  41   ARG B CG  
9166  C CD  . ARG B 43   ? 0.2898 0.3224 0.2616 -0.0997 -0.0241 0.0184  41   ARG B CD  
9167  N NE  . ARG B 43   ? 0.3233 0.3395 0.2876 -0.0998 -0.0268 0.0165  41   ARG B NE  
9168  C CZ  . ARG B 43   ? 0.3553 0.3619 0.3136 -0.1032 -0.0286 0.0178  41   ARG B CZ  
9169  N NH1 . ARG B 43   ? 0.2781 0.2897 0.2369 -0.1071 -0.0279 0.0210  41   ARG B NH1 
9170  N NH2 . ARG B 43   ? 0.3332 0.3249 0.2848 -0.1025 -0.0311 0.0157  41   ARG B NH2 
9171  N N   . PRO B 44   ? 0.2746 0.3272 0.2633 -0.0781 -0.0161 0.0110  42   PRO B N   
9172  C CA  . PRO B 44   ? 0.2605 0.3273 0.2562 -0.0764 -0.0140 0.0119  42   PRO B CA  
9173  C C   . PRO B 44   ? 0.2355 0.3129 0.2342 -0.0801 -0.0128 0.0153  42   PRO B C   
9174  O O   . PRO B 44   ? 0.2652 0.3408 0.2609 -0.0863 -0.0146 0.0176  42   PRO B O   
9175  C CB  . PRO B 44   ? 0.2850 0.3529 0.2811 -0.0785 -0.0163 0.0116  42   PRO B CB  
9176  C CG  . PRO B 44   ? 0.2904 0.3439 0.2806 -0.0770 -0.0182 0.0088  42   PRO B CG  
9177  C CD  . PRO B 44   ? 0.3057 0.3497 0.2907 -0.0789 -0.0188 0.0092  42   PRO B CD  
9178  N N   . GLU B 45   ? 0.2453 0.3335 0.2495 -0.0761 -0.0097 0.0156  43   GLU B N   
9179  C CA  . GLU B 45   ? 0.2401 0.3392 0.2473 -0.0786 -0.0078 0.0186  43   GLU B CA  
9180  C C   . GLU B 45   ? 0.2660 0.3736 0.2755 -0.0849 -0.0096 0.0215  43   GLU B C   
9181  O O   . GLU B 45   ? 0.2817 0.3938 0.2910 -0.0900 -0.0096 0.0245  43   GLU B O   
9182  C CB  . GLU B 45   ? 0.2745 0.3832 0.2871 -0.0723 -0.0042 0.0178  43   GLU B CB  
9183  C CG  . GLU B 45   ? 0.2905 0.4066 0.3044 -0.0725 -0.0015 0.0198  43   GLU B CG  
9184  C CD  . GLU B 45   ? 0.2312 0.3496 0.2472 -0.0652 0.0017  0.0178  43   GLU B CD  
9185  O OE1 . GLU B 45   ? 0.2312 0.3441 0.2471 -0.0603 0.0018  0.0149  43   GLU B OE1 
9186  O OE2 . GLU B 45   ? 0.2401 0.3655 0.2574 -0.0647 0.0042  0.0192  43   GLU B OE2 
9187  N N   . THR B 46   ? 0.2840 0.3940 0.2956 -0.0851 -0.0112 0.0209  44   THR B N   
9188  C CA  . THR B 46   ? 0.2759 0.3938 0.2896 -0.0914 -0.0133 0.0237  44   THR B CA  
9189  C C   . THR B 46   ? 0.2888 0.3972 0.2964 -0.0988 -0.0168 0.0250  44   THR B C   
9190  O O   . THR B 46   ? 0.3142 0.4291 0.3230 -0.1053 -0.0184 0.0281  44   THR B O   
9191  C CB  . THR B 46   ? 0.2816 0.4033 0.2983 -0.0898 -0.0145 0.0226  44   THR B CB  
9192  O OG1 . THR B 46   ? 0.2797 0.3878 0.2914 -0.0876 -0.0163 0.0194  44   THR B OG1 
9193  C CG2 . THR B 46   ? 0.2837 0.4169 0.3071 -0.0833 -0.0113 0.0221  44   THR B CG2 
9194  N N   . GLU B 47   ? 0.2891 0.3821 0.2900 -0.0979 -0.0182 0.0228  45   GLU B N   
9195  C CA  . GLU B 47   ? 0.2762 0.3588 0.2705 -0.1045 -0.0214 0.0240  45   GLU B CA  
9196  C C   . GLU B 47   ? 0.2857 0.3678 0.2781 -0.1069 -0.0202 0.0262  45   GLU B C   
9197  O O   . GLU B 47   ? 0.3064 0.3857 0.2953 -0.1139 -0.0225 0.0288  45   GLU B O   
9198  C CB  . GLU B 47   ? 0.2953 0.3615 0.2830 -0.1024 -0.0235 0.0207  45   GLU B CB  
9199  C CG  . GLU B 47   ? 0.3605 0.4257 0.3487 -0.1010 -0.0252 0.0186  45   GLU B CG  
9200  C CD  . GLU B 47   ? 0.4232 0.4728 0.4050 -0.0981 -0.0267 0.0152  45   GLU B CD  
9201  O OE1 . GLU B 47   ? 0.4346 0.4728 0.4103 -0.0999 -0.0280 0.0150  45   GLU B OE1 
9202  O OE2 . GLU B 47   ? 0.4847 0.5335 0.4675 -0.0939 -0.0265 0.0127  45   GLU B OE2 
9203  N N   . CYS B 48   ? 0.2787 0.3629 0.2728 -0.1014 -0.0168 0.0253  46   CYS B N   
9204  C CA  . CYS B 48   ? 0.2650 0.3479 0.2567 -0.1033 -0.0157 0.0273  46   CYS B CA  
9205  C C   . CYS B 48   ? 0.3008 0.3980 0.2967 -0.1081 -0.0144 0.0313  46   CYS B C   
9206  O O   . CYS B 48   ? 0.2823 0.3777 0.2750 -0.1135 -0.0151 0.0340  46   CYS B O   
9207  C CB  . CYS B 48   ? 0.2819 0.3636 0.2742 -0.0961 -0.0125 0.0251  46   CYS B CB  
9208  S SG  . CYS B 48   ? 0.2690 0.3341 0.2562 -0.0906 -0.0136 0.0208  46   CYS B SG  
9209  N N   . LEU B 49   ? 0.3072 0.4186 0.3102 -0.1061 -0.0125 0.0318  47   LEU B N   
9210  C CA  . LEU B 49   ? 0.2896 0.4162 0.2974 -0.1089 -0.0103 0.0354  47   LEU B CA  
9211  C C   . LEU B 49   ? 0.2920 0.4233 0.2998 -0.1180 -0.0128 0.0393  47   LEU B C   
9212  O O   . LEU B 49   ? 0.2729 0.4103 0.2810 -0.1220 -0.0117 0.0425  47   LEU B O   
9213  C CB  . LEU B 49   ? 0.2941 0.4348 0.3097 -0.1032 -0.0072 0.0347  47   LEU B CB  
9214  C CG  . LEU B 49   ? 0.2909 0.4347 0.3078 -0.0965 -0.0031 0.0335  47   LEU B CG  
9215  C CD1 . LEU B 49   ? 0.3043 0.4534 0.3203 -0.1003 -0.0014 0.0367  47   LEU B CD1 
9216  C CD2 . LEU B 49   ? 0.2621 0.3911 0.2741 -0.0914 -0.0033 0.0297  47   LEU B CD2 
9217  N N   . PRO B 50   ? 0.3132 0.4424 0.3208 -0.1217 -0.0163 0.0392  48   PRO B N   
9218  C CA  . PRO B 50   ? 0.3282 0.4636 0.3365 -0.1307 -0.0188 0.0432  48   PRO B CA  
9219  C C   . PRO B 50   ? 0.3388 0.4657 0.3407 -0.1373 -0.0204 0.0456  48   PRO B C   
9220  O O   . PRO B 50   ? 0.3668 0.5034 0.3708 -0.1431 -0.0200 0.0497  48   PRO B O   
9221  C CB  . PRO B 50   ? 0.2819 0.4121 0.2890 -0.1326 -0.0227 0.0417  48   PRO B CB  
9222  C CG  . PRO B 50   ? 0.3044 0.4352 0.3145 -0.1239 -0.0208 0.0380  48   PRO B CG  
9223  C CD  . PRO B 50   ? 0.2901 0.4142 0.2978 -0.1178 -0.0178 0.0359  48   PRO B CD  
9224  N N   . PRO B 51   ? 0.3163 0.4254 0.3102 -0.1367 -0.0222 0.0435  49   PRO B N   
9225  C CA  . PRO B 51   ? 0.3426 0.4441 0.3305 -0.1427 -0.0236 0.0461  49   PRO B CA  
9226  C C   . PRO B 51   ? 0.3177 0.4264 0.3072 -0.1410 -0.0197 0.0480  49   PRO B C   
9227  O O   . PRO B 51   ? 0.3435 0.4537 0.3309 -0.1474 -0.0201 0.0517  49   PRO B O   
9228  C CB  . PRO B 51   ? 0.3662 0.4474 0.3458 -0.1407 -0.0262 0.0429  49   PRO B CB  
9229  C CG  . PRO B 51   ? 0.3587 0.4387 0.3408 -0.1320 -0.0246 0.0385  49   PRO B CG  
9230  C CD  . PRO B 51   ? 0.3194 0.4144 0.3092 -0.1317 -0.0238 0.0391  49   PRO B CD  
9231  N N   . LEU B 52   ? 0.3273 0.4405 0.3203 -0.1327 -0.0159 0.0455  50   LEU B N   
9232  C CA  . LEU B 52   ? 0.3148 0.4359 0.3094 -0.1308 -0.0120 0.0471  50   LEU B CA  
9233  C C   . LEU B 52   ? 0.3481 0.4884 0.3497 -0.1341 -0.0099 0.0509  50   LEU B C   
9234  O O   . LEU B 52   ? 0.3417 0.4878 0.3428 -0.1376 -0.0082 0.0541  50   LEU B O   
9235  C CB  . LEU B 52   ? 0.2989 0.4196 0.2953 -0.1211 -0.0088 0.0434  50   LEU B CB  
9236  C CG  . LEU B 52   ? 0.3043 0.4075 0.2947 -0.1169 -0.0103 0.0396  50   LEU B CG  
9237  C CD1 . LEU B 52   ? 0.2851 0.3898 0.2784 -0.1076 -0.0073 0.0361  50   LEU B CD1 
9238  C CD2 . LEU B 52   ? 0.3192 0.4119 0.3025 -0.1200 -0.0113 0.0410  50   LEU B CD2 
9239  N N   . VAL B 53   ? 0.2869 0.4377 0.2949 -0.1329 -0.0098 0.0505  51   VAL B N   
9240  C CA  . VAL B 53   ? 0.3233 0.4931 0.3385 -0.1363 -0.0081 0.0542  51   VAL B CA  
9241  C C   . VAL B 53   ? 0.3596 0.5277 0.3712 -0.1448 -0.0109 0.0580  51   VAL B C   
9242  O O   . VAL B 53   ? 0.3319 0.5089 0.3447 -0.1461 -0.0090 0.0609  51   VAL B O   
9243  C CB  . VAL B 53   ? 0.2713 0.4503 0.2931 -0.1339 -0.0086 0.0530  51   VAL B CB  
9244  C CG1 . VAL B 53   ? 0.3428 0.5361 0.3693 -0.1364 -0.0085 0.0563  51   VAL B CG1 
9245  C CG2 . VAL B 53   ? 0.3046 0.4873 0.3302 -0.1238 -0.0051 0.0495  51   VAL B CG2 
9246  N N   . GLU B 54   ? 0.3382 0.4932 0.3443 -0.1497 -0.0156 0.0576  52   GLU B N   
9247  C CA  . GLU B 54   ? 0.3874 0.5386 0.3889 -0.1568 -0.0187 0.0608  52   GLU B CA  
9248  C C   . GLU B 54   ? 0.3934 0.5395 0.3897 -0.1591 -0.0176 0.0628  52   GLU B C   
9249  O O   . GLU B 54   ? 0.3669 0.5191 0.3630 -0.1629 -0.0175 0.0662  52   GLU B O   
9250  C CB  . GLU B 54   ? 0.3999 0.5361 0.3954 -0.1608 -0.0239 0.0595  52   GLU B CB  
9251  N N   . ALA B 55   ? 0.3650 0.5003 0.3572 -0.1569 -0.0169 0.0609  53   ALA B N   
9252  C CA  . ALA B 55   ? 0.3835 0.5129 0.3702 -0.1589 -0.0160 0.0628  53   ALA B CA  
9253  C C   . ALA B 55   ? 0.3616 0.5061 0.3529 -0.1560 -0.0111 0.0645  53   ALA B C   
9254  O O   . ALA B 55   ? 0.3671 0.5119 0.3551 -0.1591 -0.0106 0.0673  53   ALA B O   
9255  C CB  . ALA B 55   ? 0.3669 0.4802 0.3477 -0.1558 -0.0165 0.0598  53   ALA B CB  
9256  N N   . ALA B 56   ? 0.3618 0.5188 0.3604 -0.1498 -0.0075 0.0628  54   ALA B N   
9257  C CA  . ALA B 56   ? 0.3475 0.5181 0.3502 -0.1458 -0.0027 0.0639  54   ALA B CA  
9258  C C   . ALA B 56   ? 0.3785 0.5644 0.3864 -0.1473 -0.0019 0.0667  54   ALA B C   
9259  O O   . ALA B 56   ? 0.4049 0.6027 0.4162 -0.1440 0.0020  0.0676  54   ALA B O   
9260  C CB  . ALA B 56   ? 0.3525 0.5287 0.3602 -0.1379 0.0009  0.0606  54   ALA B CB  
9261  N N   . THR B 57   ? 0.3890 0.5748 0.3974 -0.1520 -0.0056 0.0679  55   THR B N   
9262  C CA  . THR B 57   ? 0.4270 0.6276 0.4408 -0.1535 -0.0052 0.0706  55   THR B CA  
9263  C C   . THR B 57   ? 0.4187 0.6233 0.4301 -0.1573 -0.0042 0.0742  55   THR B C   
9264  O O   . THR B 57   ? 0.4277 0.6206 0.4320 -0.1625 -0.0065 0.0756  55   THR B O   
9265  C CB  . THR B 57   ? 0.4922 0.6898 0.5057 -0.1584 -0.0098 0.0712  55   THR B CB  
9266  O OG1 . THR B 57   ? 0.5475 0.7282 0.5525 -0.1644 -0.0139 0.0717  55   THR B OG1 
9267  C CG2 . THR B 57   ? 0.3786 0.5766 0.3960 -0.1541 -0.0104 0.0680  55   THR B CG2 
9268  N N   . GLN B 58   ? 0.4476 0.6686 0.4650 -0.1547 -0.0008 0.0757  56   GLN B N   
9269  C CA  . GLN B 58   ? 0.4556 0.6829 0.4719 -0.1580 0.0006  0.0792  56   GLN B CA  
9270  C C   . GLN B 58   ? 0.4901 0.7330 0.5126 -0.1594 0.0006  0.0817  56   GLN B C   
9271  O O   . GLN B 58   ? 0.4767 0.7288 0.5056 -0.1552 0.0015  0.0804  56   GLN B O   
9272  C CB  . GLN B 58   ? 0.4856 0.7175 0.5020 -0.1525 0.0055  0.0785  56   GLN B CB  
9273  C CG  . GLN B 58   ? 0.4330 0.6512 0.4441 -0.1498 0.0061  0.0757  56   GLN B CG  
9274  C CD  . GLN B 58   ? 0.4795 0.6949 0.4856 -0.1500 0.0084  0.0769  56   GLN B CD  
9275  O OE1 . GLN B 58   ? 0.5411 0.7521 0.5424 -0.1561 0.0065  0.0799  56   GLN B OE1 
9276  N NE2 . GLN B 58   ? 0.4658 0.6837 0.4726 -0.1432 0.0125  0.0747  56   GLN B NE2 
9277  N N   . SER B 59   ? 0.5247 0.7705 0.5452 -0.1654 -0.0003 0.0855  57   SER B N   
9278  C CA  . SER B 59   ? 0.5028 0.7634 0.5289 -0.1677 -0.0004 0.0884  57   SER B CA  
9279  C C   . SER B 59   ? 0.5007 0.7780 0.5341 -0.1605 0.0046  0.0879  57   SER B C   
9280  O O   . SER B 59   ? 0.4868 0.7647 0.5200 -0.1547 0.0084  0.0860  57   SER B O   
9281  C CB  . SER B 59   ? 0.5404 0.8006 0.5624 -0.1754 -0.0021 0.0926  57   SER B CB  
9282  O OG  . SER B 59   ? 0.5347 0.7985 0.5554 -0.1737 0.0017  0.0935  57   SER B OG  
9283  N N   . LYS B 60   ? 0.4826 0.7737 0.5223 -0.1607 0.0046  0.0896  58   LYS B N   
9284  C CA  . LYS B 60   ? 0.5208 0.8283 0.5675 -0.1540 0.0091  0.0895  58   LYS B CA  
9285  C C   . LYS B 60   ? 0.4854 0.7978 0.5305 -0.1534 0.0128  0.0911  58   LYS B C   
9286  O O   . LYS B 60   ? 0.5033 0.8232 0.5514 -0.1462 0.0172  0.0895  58   LYS B O   
9287  C CB  . LYS B 60   ? 0.4486 0.7697 0.5017 -0.1556 0.0080  0.0918  58   LYS B CB  
9288  N N   . GLU B 61   ? 0.4824 0.7905 0.5225 -0.1609 0.0110  0.0943  59   GLU B N   
9289  C CA  . GLU B 61   ? 0.5049 0.8175 0.5431 -0.1609 0.0143  0.0961  59   GLU B CA  
9290  C C   . GLU B 61   ? 0.5091 0.8129 0.5432 -0.1556 0.0170  0.0931  59   GLU B C   
9291  O O   . GLU B 61   ? 0.5011 0.8129 0.5373 -0.1496 0.0216  0.0922  59   GLU B O   
9292  C CB  . GLU B 61   ? 0.5107 0.8183 0.5437 -0.1704 0.0112  0.1001  59   GLU B CB  
9293  N N   . ILE B 62   ? 0.5285 0.8157 0.5566 -0.1578 0.0142  0.0915  60   ILE B N   
9294  C CA  . ILE B 62   ? 0.4939 0.7717 0.5176 -0.1534 0.0164  0.0887  60   ILE B CA  
9295  C C   . ILE B 62   ? 0.4688 0.7527 0.4974 -0.1439 0.0200  0.0850  60   ILE B C   
9296  O O   . ILE B 62   ? 0.4788 0.7645 0.5066 -0.1384 0.0240  0.0835  60   ILE B O   
9297  C CB  . ILE B 62   ? 0.5395 0.7984 0.5561 -0.1575 0.0123  0.0877  60   ILE B CB  
9298  C CG1 . ILE B 62   ? 0.5223 0.7740 0.5327 -0.1662 0.0093  0.0913  60   ILE B CG1 
9299  C CG2 . ILE B 62   ? 0.5183 0.7677 0.5313 -0.1521 0.0144  0.0843  60   ILE B CG2 
9300  C CD1 . ILE B 62   ? 0.5257 0.7578 0.5282 -0.1700 0.0053  0.0904  60   ILE B CD1 
9301  N N   . ARG B 63   ? 0.4602 0.7475 0.4940 -0.1417 0.0187  0.0834  61   ARG B N   
9302  C CA  . ARG B 63   ? 0.4494 0.7408 0.4876 -0.1327 0.0216  0.0798  61   ARG B CA  
9303  C C   . ARG B 63   ? 0.4596 0.7663 0.5026 -0.1268 0.0263  0.0800  61   ARG B C   
9304  O O   . ARG B 63   ? 0.4580 0.7654 0.5010 -0.1195 0.0299  0.0773  61   ARG B O   
9305  C CB  . ARG B 63   ? 0.4661 0.7583 0.5087 -0.1322 0.0189  0.0784  61   ARG B CB  
9306  C CG  . ARG B 63   ? 0.4915 0.7680 0.5293 -0.1369 0.0144  0.0775  61   ARG B CG  
9307  C CD  . ARG B 63   ? 0.4776 0.7543 0.5197 -0.1341 0.0126  0.0751  61   ARG B CD  
9308  N NE  . ARG B 63   ? 0.4878 0.7777 0.5363 -0.1345 0.0120  0.0769  61   ARG B NE  
9309  C CZ  . ARG B 63   ? 0.5324 0.8218 0.5807 -0.1412 0.0080  0.0792  61   ARG B CZ  
9310  N NH1 . ARG B 63   ? 0.5694 0.8455 0.6114 -0.1481 0.0042  0.0800  61   ARG B NH1 
9311  N NH2 . ARG B 63   ? 0.5415 0.8439 0.5960 -0.1409 0.0079  0.0808  61   ARG B NH2 
9312  N N   . ASP B 64   ? 0.4584 0.7773 0.5052 -0.1297 0.0263  0.0832  62   ASP B N   
9313  C CA  . ASP B 64   ? 0.4568 0.7902 0.5078 -0.1243 0.0308  0.0837  62   ASP B CA  
9314  C C   . ASP B 64   ? 0.4291 0.7599 0.4749 -0.1235 0.0339  0.0840  62   ASP B C   
9315  O O   . ASP B 64   ? 0.4509 0.7862 0.4975 -0.1161 0.0381  0.0819  62   ASP B O   
9316  C CB  . ASP B 64   ? 0.4469 0.7936 0.5027 -0.1283 0.0300  0.0874  62   ASP B CB  
9317  C CG  . ASP B 64   ? 0.5248 0.8763 0.5864 -0.1276 0.0276  0.0870  62   ASP B CG  
9318  O OD1 . ASP B 64   ? 0.5301 0.8820 0.5947 -0.1204 0.0289  0.0836  62   ASP B OD1 
9319  O OD2 . ASP B 64   ? 0.5760 0.9306 0.6390 -0.1342 0.0244  0.0900  62   ASP B OD2 
9320  N N   . ALA B 65   ? 0.3844 0.7073 0.4244 -0.1310 0.0318  0.0865  63   ALA B N   
9321  C CA  . ALA B 65   ? 0.4450 0.7643 0.4792 -0.1308 0.0345  0.0870  63   ALA B CA  
9322  C C   . ALA B 65   ? 0.4979 0.8076 0.5286 -0.1245 0.0363  0.0829  63   ALA B C   
9323  O O   . ALA B 65   ? 0.4961 0.8079 0.5247 -0.1198 0.0402  0.0819  63   ALA B O   
9324  C CB  . ALA B 65   ? 0.4710 0.7812 0.4991 -0.1402 0.0311  0.0902  63   ALA B CB  
9325  N N   . ALA B 66   ? 0.4664 0.7656 0.4962 -0.1243 0.0336  0.0805  64   ALA B N   
9326  C CA  . ALA B 66   ? 0.4374 0.7270 0.4636 -0.1188 0.0351  0.0768  64   ALA B CA  
9327  C C   . ALA B 66   ? 0.4615 0.7595 0.4926 -0.1091 0.0389  0.0736  64   ALA B C   
9328  O O   . ALA B 66   ? 0.4342 0.7293 0.4624 -0.1035 0.0419  0.0712  64   ALA B O   
9329  C CB  . ALA B 66   ? 0.4897 0.7656 0.5135 -0.1218 0.0310  0.0754  64   ALA B CB  
9330  N N   . ALA B 67   ? 0.4278 0.7361 0.4661 -0.1070 0.0386  0.0735  65   ALA B N   
9331  C CA  . ALA B 67   ? 0.4805 0.7966 0.5233 -0.0976 0.0420  0.0705  65   ALA B CA  
9332  C C   . ALA B 67   ? 0.4905 0.8157 0.5331 -0.0935 0.0465  0.0711  65   ALA B C   
9333  O O   . ALA B 67   ? 0.4727 0.7995 0.5155 -0.0854 0.0498  0.0680  65   ALA B O   
9334  C CB  . ALA B 67   ? 0.4713 0.7965 0.5216 -0.0965 0.0406  0.0707  65   ALA B CB  
9335  N N   . SER B 68   ? 0.5187 0.8497 0.5605 -0.0991 0.0466  0.0748  66   SER B N   
9336  C CA  . SER B 68   ? 0.5088 0.8483 0.5500 -0.0959 0.0508  0.0756  66   SER B CA  
9337  C C   . SER B 68   ? 0.5330 0.8624 0.5662 -0.0950 0.0525  0.0744  66   SER B C   
9338  O O   . SER B 68   ? 0.5579 0.8896 0.5898 -0.0881 0.0564  0.0722  66   SER B O   
9339  C CB  . SER B 68   ? 0.5229 0.8721 0.5659 -0.1025 0.0502  0.0803  66   SER B CB  
9340  O OG  . SER B 68   ? 0.5901 0.9479 0.6325 -0.0995 0.0544  0.0811  66   SER B OG  
9341  N N   . THR B 69   ? 0.4897 0.8074 0.5173 -0.1019 0.0496  0.0758  67   THR B N   
9342  C CA  . THR B 69   ? 0.4720 0.7787 0.4917 -0.1013 0.0507  0.0747  67   THR B CA  
9343  C C   . THR B 69   ? 0.4855 0.7870 0.5043 -0.0930 0.0525  0.0700  67   THR B C   
9344  O O   . THR B 69   ? 0.4982 0.7985 0.5130 -0.0880 0.0558  0.0682  67   THR B O   
9345  C CB  . THR B 69   ? 0.4600 0.7534 0.4743 -0.1096 0.0465  0.0765  67   THR B CB  
9346  O OG1 . THR B 69   ? 0.4568 0.7541 0.4704 -0.1171 0.0451  0.0809  67   THR B OG1 
9347  C CG2 . THR B 69   ? 0.4816 0.7625 0.4876 -0.1083 0.0472  0.0749  67   THR B CG2 
9348  N N   . ALA B 70   ? 0.4640 0.7621 0.4862 -0.0914 0.0504  0.0678  68   ALA B N   
9349  C CA  . ALA B 70   ? 0.4609 0.7543 0.4826 -0.0836 0.0519  0.0634  68   ALA B CA  
9350  C C   . ALA B 70   ? 0.4908 0.7950 0.5162 -0.0750 0.0560  0.0614  68   ALA B C   
9351  O O   . ALA B 70   ? 0.4754 0.7760 0.4977 -0.0684 0.0585  0.0582  68   ALA B O   
9352  C CB  . ALA B 70   ? 0.4581 0.7467 0.4833 -0.0840 0.0487  0.0618  68   ALA B CB  
9353  N N   . ARG B 71   ? 0.5046 0.8218 0.5363 -0.0751 0.0566  0.0633  69   ARG B N   
9354  C CA  . ARG B 71   ? 0.5141 0.8418 0.5489 -0.0673 0.0605  0.0619  69   ARG B CA  
9355  C C   . ARG B 71   ? 0.4133 0.7408 0.4422 -0.0653 0.0640  0.0618  69   ARG B C   
9356  O O   . ARG B 71   ? 0.4750 0.8024 0.5023 -0.0575 0.0670  0.0587  69   ARG B O   
9357  C CB  . ARG B 71   ? 0.4806 0.8225 0.5226 -0.0689 0.0603  0.0647  69   ARG B CB  
9358  N N   . LYS B 72   ? 0.4198 0.7466 0.4452 -0.0724 0.0634  0.0654  70   LYS B N   
9359  C CA  . LYS B 72   ? 0.4729 0.7995 0.4924 -0.0712 0.0665  0.0657  70   LYS B CA  
9360  C C   . LYS B 72   ? 0.5083 0.8223 0.5207 -0.0672 0.0673  0.0622  70   LYS B C   
9361  O O   . LYS B 72   ? 0.4774 0.7921 0.4863 -0.0613 0.0708  0.0602  70   LYS B O   
9362  C CB  . LYS B 72   ? 0.4863 0.8128 0.5029 -0.0803 0.0651  0.0703  70   LYS B CB  
9363  N N   . LEU B 73   ? 0.5068 0.8091 0.5168 -0.0703 0.0641  0.0614  71   LEU B N   
9364  C CA  . LEU B 73   ? 0.4755 0.7656 0.4786 -0.0670 0.0645  0.0583  71   LEU B CA  
9365  C C   . LEU B 73   ? 0.4851 0.7761 0.4900 -0.0573 0.0667  0.0537  71   LEU B C   
9366  O O   . LEU B 73   ? 0.4992 0.7861 0.4987 -0.0521 0.0691  0.0512  71   LEU B O   
9367  C CB  . LEU B 73   ? 0.4453 0.7233 0.4460 -0.0727 0.0604  0.0587  71   LEU B CB  
9368  C CG  . LEU B 73   ? 0.4681 0.7428 0.4659 -0.0824 0.0577  0.0631  71   LEU B CG  
9369  C CD1 . LEU B 73   ? 0.4474 0.7111 0.4441 -0.0878 0.0533  0.0634  71   LEU B CD1 
9370  C CD2 . LEU B 73   ? 0.4368 0.7067 0.4264 -0.0834 0.0594  0.0641  71   LEU B CD2 
9371  N N   . ILE B 74   ? 0.4913 0.7872 0.5033 -0.0547 0.0658  0.0526  72   ILE B N   
9372  C CA  . ILE B 74   ? 0.5356 0.8307 0.5492 -0.0458 0.0673  0.0482  72   ILE B CA  
9373  C C   . ILE B 74   ? 0.5195 0.8233 0.5337 -0.0388 0.0713  0.0470  72   ILE B C   
9374  O O   . ILE B 74   ? 0.5106 0.8104 0.5215 -0.0315 0.0733  0.0433  72   ILE B O   
9375  C CB  . ILE B 74   ? 0.5111 0.8087 0.5320 -0.0454 0.0648  0.0476  72   ILE B CB  
9376  C CG1 . ILE B 74   ? 0.5087 0.7962 0.5282 -0.0517 0.0610  0.0483  72   ILE B CG1 
9377  C CG2 . ILE B 74   ? 0.5154 0.8126 0.5382 -0.0360 0.0663  0.0433  72   ILE B CG2 
9378  C CD1 . ILE B 74   ? 0.4551 0.7463 0.4815 -0.0548 0.0580  0.0495  72   ILE B CD1 
9379  N N   . GLU B 75   ? 0.5056 0.8211 0.5235 -0.0410 0.0725  0.0501  73   GLU B N   
9380  C CA  . GLU B 75   ? 0.5159 0.8398 0.5337 -0.0350 0.0764  0.0493  73   GLU B CA  
9381  C C   . GLU B 75   ? 0.5051 0.8223 0.5140 -0.0336 0.0787  0.0482  73   GLU B C   
9382  O O   . GLU B 75   ? 0.5353 0.8515 0.5414 -0.0260 0.0815  0.0450  73   GLU B O   
9383  C CB  . GLU B 75   ? 0.4504 0.7881 0.4735 -0.0387 0.0771  0.0533  73   GLU B CB  
9384  N N   . ALA B 76   ? 0.4914 0.8035 0.4956 -0.0410 0.0774  0.0510  74   ALA B N   
9385  C CA  . ALA B 76   ? 0.5480 0.8524 0.5431 -0.0404 0.0790  0.0501  74   ALA B CA  
9386  C C   . ALA B 76   ? 0.5193 0.8123 0.5097 -0.0345 0.0789  0.0455  74   ALA B C   
9387  O O   . ALA B 76   ? 0.5467 0.8370 0.5317 -0.0288 0.0815  0.0428  74   ALA B O   
9388  C CB  . ALA B 76   ? 0.4664 0.7653 0.4573 -0.0497 0.0767  0.0539  74   ALA B CB  
9389  N N   . LEU B 77   ? 0.4986 0.7847 0.4908 -0.0358 0.0758  0.0444  75   LEU B N   
9390  C CA  . LEU B 77   ? 0.5209 0.7961 0.5088 -0.0307 0.0754  0.0401  75   LEU B CA  
9391  C C   . LEU B 77   ? 0.5505 0.8290 0.5404 -0.0210 0.0778  0.0361  75   LEU B C   
9392  O O   . LEU B 77   ? 0.5297 0.8016 0.5136 -0.0154 0.0793  0.0327  75   LEU B O   
9393  C CB  . LEU B 77   ? 0.5021 0.7705 0.4923 -0.0342 0.0717  0.0399  75   LEU B CB  
9394  C CG  . LEU B 77   ? 0.5146 0.7759 0.5012 -0.0432 0.0688  0.0431  75   LEU B CG  
9395  C CD1 . LEU B 77   ? 0.4715 0.7284 0.4621 -0.0464 0.0653  0.0430  75   LEU B CD1 
9396  C CD2 . LEU B 77   ? 0.4826 0.7329 0.4594 -0.0429 0.0691  0.0418  75   LEU B CD2 
9397  N N   . ARG B 78   ? 0.4941 0.7820 0.4922 -0.0189 0.0780  0.0365  76   ARG B N   
9398  C CA  . ARG B 78   ? 0.5309 0.8217 0.5310 -0.0098 0.0800  0.0329  76   ARG B CA  
9399  C C   . ARG B 78   ? 0.5382 0.8350 0.5354 -0.0057 0.0838  0.0327  76   ARG B C   
9400  O O   . ARG B 78   ? 0.5505 0.8470 0.5469 0.0023  0.0857  0.0292  76   ARG B O   
9401  C CB  . ARG B 78   ? 0.5256 0.8246 0.5351 -0.0089 0.0788  0.0336  76   ARG B CB  
9402  C CG  . ARG B 78   ? 0.5337 0.8262 0.5459 -0.0116 0.0752  0.0331  76   ARG B CG  
9403  C CD  . ARG B 78   ? 0.5676 0.8671 0.5882 -0.0094 0.0741  0.0330  76   ARG B CD  
9404  N NE  . ARG B 78   ? 0.6247 0.9158 0.6460 -0.0070 0.0719  0.0301  76   ARG B NE  
9405  C CZ  . ARG B 78   ? 0.6319 0.9262 0.6596 -0.0045 0.0705  0.0295  76   ARG B CZ  
9406  N NH1 . ARG B 78   ? 0.6260 0.9318 0.6601 -0.0043 0.0709  0.0315  76   ARG B NH1 
9407  N NH2 . ARG B 78   ? 0.6632 0.9490 0.6907 -0.0023 0.0687  0.0267  76   ARG B NH2 
9408  N N   . GLY B 79   ? 0.4629 0.7647 0.4583 -0.0110 0.0849  0.0362  77   GLY B N   
9409  C CA  . GLY B 79   ? 0.5336 0.8413 0.5259 -0.0078 0.0886  0.0363  77   GLY B CA  
9410  C C   . GLY B 79   ? 0.5649 0.8631 0.5472 -0.0055 0.0901  0.0341  77   GLY B C   
9411  O O   . GLY B 79   ? 0.4759 0.7779 0.4549 -0.0018 0.0933  0.0335  77   GLY B O   
9412  N N   . LYS B 80   ? 0.5635 0.8494 0.5406 -0.0075 0.0878  0.0328  78   LYS B N   
9413  C CA  . LYS B 80   ? 0.5449 0.8209 0.5120 -0.0058 0.0886  0.0307  78   LYS B CA  
9414  C C   . LYS B 80   ? 0.5691 0.8333 0.5330 -0.0012 0.0869  0.0263  78   LYS B C   
9415  O O   . LYS B 80   ? 0.6701 0.9294 0.6290 0.0056  0.0885  0.0224  78   LYS B O   
9416  C CB  . LYS B 80   ? 0.5592 0.8314 0.5214 -0.0141 0.0873  0.0343  78   LYS B CB  
9417  C CG  . LYS B 80   ? 0.5388 0.8056 0.5033 -0.0207 0.0834  0.0361  78   LYS B CG  
9418  C CD  . LYS B 80   ? 0.5125 0.7784 0.4742 -0.0297 0.0820  0.0407  78   LYS B CD  
9419  C CE  . LYS B 80   ? 0.5002 0.7584 0.4628 -0.0358 0.0779  0.0420  78   LYS B CE  
9420  N NZ  . LYS B 80   ? 0.4579 0.7136 0.4173 -0.0448 0.0761  0.0464  78   LYS B NZ  
9421  N N   . GLY B 85   ? 0.5644 0.7352 0.4799 0.0269  0.0752  -0.0041 83   GLY B N   
9422  C CA  . GLY B 85   ? 0.5524 0.7126 0.4584 0.0309  0.0746  -0.0078 83   GLY B CA  
9423  C C   . GLY B 85   ? 0.5782 0.7301 0.4843 0.0374  0.0730  -0.0126 83   GLY B C   
9424  O O   . GLY B 85   ? 0.5497 0.7003 0.4503 0.0437  0.0751  -0.0159 83   GLY B O   
9425  N N   . VAL B 86   ? 0.5661 0.7119 0.4783 0.0357  0.0693  -0.0129 84   VAL B N   
9426  C CA  . VAL B 86   ? 0.5499 0.6875 0.4626 0.0412  0.0675  -0.0171 84   VAL B CA  
9427  C C   . VAL B 86   ? 0.5427 0.6903 0.4599 0.0472  0.0710  -0.0182 84   VAL B C   
9428  O O   . VAL B 86   ? 0.5226 0.6654 0.4367 0.0537  0.0715  -0.0221 84   VAL B O   
9429  C CB  . VAL B 86   ? 0.5606 0.6895 0.4784 0.0375  0.0627  -0.0169 84   VAL B CB  
9430  C CG1 . VAL B 86   ? 0.5870 0.7254 0.5147 0.0340  0.0630  -0.0137 84   VAL B CG1 
9431  C CG2 . VAL B 86   ? 0.5652 0.6840 0.4823 0.0425  0.0605  -0.0212 84   VAL B CG2 
9432  N N   . GLU B 87   ? 0.5654 0.7269 0.4897 0.0452  0.0736  -0.0148 85   GLU B N   
9433  C CA  . GLU B 87   ? 0.5560 0.7263 0.4860 0.0502  0.0762  -0.0153 85   GLU B CA  
9434  C C   . GLU B 87   ? 0.4898 0.6594 0.4143 0.0554  0.0786  -0.0173 85   GLU B C   
9435  O O   . GLU B 87   ? 0.5019 0.6701 0.4275 0.0616  0.0791  -0.0199 85   GLU B O   
9436  C CB  . GLU B 87   ? 0.6096 0.7934 0.5484 0.0457  0.0775  -0.0107 85   GLU B CB  
9437  N N   . GLY B 88   ? 0.5580 0.7285 0.4761 0.0530  0.0801  -0.0161 86   GLY B N   
9438  C CA  . GLY B 88   ? 0.5008 0.6704 0.4130 0.0578  0.0824  -0.0181 86   GLY B CA  
9439  C C   . GLY B 88   ? 0.4932 0.6487 0.3969 0.0625  0.0807  -0.0229 86   GLY B C   
9440  O O   . GLY B 88   ? 0.4760 0.6293 0.3766 0.0683  0.0820  -0.0257 86   GLY B O   
9441  N N   . LEU B 89   ? 0.4703 0.6160 0.3699 0.0601  0.0775  -0.0240 87   LEU B N   
9442  C CA  . LEU B 89   ? 0.5142 0.6459 0.4064 0.0643  0.0752  -0.0287 87   LEU B CA  
9443  C C   . LEU B 89   ? 0.4494 0.5782 0.3463 0.0698  0.0743  -0.0314 87   LEU B C   
9444  O O   . LEU B 89   ? 0.4619 0.5836 0.3540 0.0752  0.0742  -0.0349 87   LEU B O   
9445  C CB  . LEU B 89   ? 0.5162 0.6390 0.4044 0.0603  0.0716  -0.0290 87   LEU B CB  
9446  C CG  . LEU B 89   ? 0.4974 0.6043 0.3790 0.0630  0.0680  -0.0333 87   LEU B CG  
9447  C CD1 . LEU B 89   ? 0.5225 0.6248 0.3930 0.0656  0.0692  -0.0354 87   LEU B CD1 
9448  C CD2 . LEU B 89   ? 0.5347 0.6318 0.4184 0.0568  0.0628  -0.0322 87   LEU B CD2 
9449  N N   . VAL B 90   ? 0.4592 0.5935 0.3653 0.0682  0.0736  -0.0297 88   VAL B N   
9450  C CA  . VAL B 90   ? 0.4731 0.6051 0.3842 0.0729  0.0727  -0.0317 88   VAL B CA  
9451  C C   . VAL B 90   ? 0.4713 0.6089 0.3838 0.0782  0.0755  -0.0323 88   VAL B C   
9452  O O   . VAL B 90   ? 0.4322 0.5632 0.3431 0.0838  0.0748  -0.0355 88   VAL B O   
9453  C CB  . VAL B 90   ? 0.4369 0.5752 0.3577 0.0696  0.0717  -0.0292 88   VAL B CB  
9454  C CG1 . VAL B 90   ? 0.4389 0.5772 0.3656 0.0744  0.0712  -0.0306 88   VAL B CG1 
9455  C CG2 . VAL B 90   ? 0.4285 0.5579 0.3482 0.0649  0.0679  -0.0292 88   VAL B CG2 
9456  N N   . GLN B 91   ? 0.4809 0.6307 0.3962 0.0764  0.0786  -0.0292 89   GLN B N   
9457  C CA  . GLN B 91   ? 0.4871 0.6434 0.4040 0.0814  0.0814  -0.0295 89   GLN B CA  
9458  C C   . GLN B 91   ? 0.4530 0.6014 0.3599 0.0858  0.0823  -0.0328 89   GLN B C   
9459  O O   . GLN B 91   ? 0.4763 0.6219 0.3822 0.0918  0.0827  -0.0355 89   GLN B O   
9460  C CB  . GLN B 91   ? 0.4980 0.6697 0.4208 0.0780  0.0843  -0.0251 89   GLN B CB  
9461  N N   . GLU B 92   ? 0.4681 0.6126 0.3674 0.0827  0.0823  -0.0328 90   GLU B N   
9462  C CA  . GLU B 92   ? 0.4814 0.6190 0.3709 0.0864  0.0833  -0.0358 90   GLU B CA  
9463  C C   . GLU B 92   ? 0.4917 0.6150 0.3763 0.0912  0.0805  -0.0405 90   GLU B C   
9464  O O   . GLU B 92   ? 0.5018 0.6216 0.3821 0.0966  0.0814  -0.0432 90   GLU B O   
9465  C CB  . GLU B 92   ? 0.4971 0.6319 0.3789 0.0817  0.0832  -0.0349 90   GLU B CB  
9466  C CG  . GLU B 92   ? 0.5461 0.6736 0.4173 0.0852  0.0841  -0.0380 90   GLU B CG  
9467  C CD  . GLU B 92   ? 0.5478 0.6718 0.4108 0.0806  0.0837  -0.0370 90   GLU B CD  
9468  O OE1 . GLU B 92   ? 0.5640 0.6912 0.4295 0.0747  0.0828  -0.0339 90   GLU B OE1 
9469  O OE2 . GLU B 92   ? 0.5185 0.6363 0.3724 0.0829  0.0842  -0.0394 90   GLU B OE2 
9470  N N   . TYR B 93   ? 0.4783 0.5934 0.3636 0.0893  0.0769  -0.0414 91   TYR B N   
9471  C CA  . TYR B 93   ? 0.4751 0.5760 0.3556 0.0931  0.0738  -0.0456 91   TYR B CA  
9472  C C   . TYR B 93   ? 0.4720 0.5727 0.3600 0.0959  0.0726  -0.0461 91   TYR B C   
9473  O O   . TYR B 93   ? 0.4757 0.5645 0.3608 0.0984  0.0696  -0.0492 91   TYR B O   
9474  C CB  . TYR B 93   ? 0.4453 0.5352 0.3197 0.0894  0.0704  -0.0468 91   TYR B CB  
9475  C CG  . TYR B 93   ? 0.4742 0.5609 0.3390 0.0879  0.0710  -0.0473 91   TYR B CG  
9476  C CD1 . TYR B 93   ? 0.4817 0.5577 0.3373 0.0916  0.0701  -0.0510 91   TYR B CD1 
9477  C CD2 . TYR B 93   ? 0.4892 0.5833 0.3538 0.0827  0.0725  -0.0439 91   TYR B CD2 
9478  C CE1 . TYR B 93   ? 0.4458 0.5188 0.2923 0.0902  0.0706  -0.0515 91   TYR B CE1 
9479  C CE2 . TYR B 93   ? 0.4834 0.5744 0.3388 0.0813  0.0730  -0.0442 91   TYR B CE2 
9480  C CZ  . TYR B 93   ? 0.4544 0.5350 0.3009 0.0851  0.0721  -0.0481 91   TYR B CZ  
9481  O OH  . TYR B 93   ? 0.4904 0.5679 0.3277 0.0836  0.0725  -0.0484 91   TYR B OH  
9482  N N   . SER B 94   ? 0.4347 0.5480 0.3321 0.0955  0.0745  -0.0431 92   SER B N   
9483  C CA  . SER B 94   ? 0.4067 0.5214 0.3116 0.0983  0.0736  -0.0432 92   SER B CA  
9484  C C   . SER B 94   ? 0.4172 0.5225 0.3231 0.0964  0.0697  -0.0443 92   SER B C   
9485  O O   . SER B 94   ? 0.4214 0.5185 0.3273 0.1000  0.0677  -0.0466 92   SER B O   
9486  C CB  . SER B 94   ? 0.4445 0.5552 0.3467 0.1054  0.0742  -0.0459 92   SER B CB  
9487  O OG  . SER B 94   ? 0.4957 0.6158 0.3973 0.1073  0.0779  -0.0449 92   SER B OG  
9488  N N   . LEU B 95   ? 0.3410 0.4474 0.2477 0.0907  0.0688  -0.0424 93   LEU B N   
9489  C CA  . LEU B 95   ? 0.3728 0.4706 0.2801 0.0886  0.0652  -0.0434 93   LEU B CA  
9490  C C   . LEU B 95   ? 0.3717 0.4755 0.2890 0.0881  0.0647  -0.0416 93   LEU B C   
9491  O O   . LEU B 95   ? 0.3698 0.4863 0.2942 0.0860  0.0668  -0.0383 93   LEU B O   
9492  C CB  . LEU B 95   ? 0.3327 0.4296 0.2369 0.0827  0.0643  -0.0421 93   LEU B CB  
9493  C CG  . LEU B 95   ? 0.4082 0.4990 0.3021 0.0824  0.0644  -0.0436 93   LEU B CG  
9494  C CD1 . LEU B 95   ? 0.3662 0.4543 0.2579 0.0762  0.0624  -0.0421 93   LEU B CD1 
9495  C CD2 . LEU B 95   ? 0.3856 0.4625 0.2722 0.0870  0.0623  -0.0480 93   LEU B CD2 
9496  N N   . SER B 96   ? 0.3340 0.4283 0.2517 0.0896  0.0617  -0.0437 94   SER B N   
9497  C CA  . SER B 96   ? 0.3319 0.4303 0.2583 0.0879  0.0606  -0.0419 94   SER B CA  
9498  C C   . SER B 96   ? 0.3434 0.4433 0.2721 0.0807  0.0592  -0.0395 94   SER B C   
9499  O O   . SER B 96   ? 0.3227 0.4179 0.2459 0.0773  0.0583  -0.0395 94   SER B O   
9500  C CB  . SER B 96   ? 0.3379 0.4247 0.2637 0.0909  0.0576  -0.0447 94   SER B CB  
9501  O OG  . SER B 96   ? 0.2923 0.3668 0.2121 0.0885  0.0545  -0.0466 94   SER B OG  
9502  N N   . SER B 97   ? 0.2923 0.3968 0.2297 0.0774  0.0580  -0.0369 95   SER B N   
9503  C CA  . SER B 97   ? 0.2957 0.3992 0.2365 0.0696  0.0556  -0.0342 95   SER B CA  
9504  C C   . SER B 97   ? 0.3028 0.3913 0.2389 0.0673  0.0515  -0.0361 95   SER B C   
9505  O O   . SER B 97   ? 0.3000 0.3853 0.2331 0.0626  0.0502  -0.0352 95   SER B O   
9506  C CB  . SER B 97   ? 0.3611 0.4708 0.3115 0.0670  0.0547  -0.0317 95   SER B CB  
9507  O OG  . SER B 97   ? 0.4195 0.5441 0.3745 0.0681  0.0583  -0.0294 95   SER B OG  
9508  N N   . GLN B 98   ? 0.2726 0.3520 0.2080 0.0706  0.0493  -0.0387 96   GLN B N   
9509  C CA  . GLN B 98   ? 0.2978 0.3636 0.2293 0.0684  0.0453  -0.0405 96   GLN B CA  
9510  C C   . GLN B 98   ? 0.2762 0.3358 0.1981 0.0693  0.0454  -0.0425 96   GLN B C   
9511  O O   . GLN B 98   ? 0.3008 0.3527 0.2197 0.0653  0.0426  -0.0426 96   GLN B O   
9512  C CB  . GLN B 98   ? 0.2805 0.3381 0.2128 0.0719  0.0433  -0.0428 96   GLN B CB  
9513  C CG  . GLN B 98   ? 0.2928 0.3536 0.2340 0.0698  0.0420  -0.0408 96   GLN B CG  
9514  C CD  . GLN B 98   ? 0.3095 0.3672 0.2538 0.0630  0.0391  -0.0388 96   GLN B CD  
9515  O OE1 . GLN B 98   ? 0.3442 0.4087 0.2911 0.0587  0.0399  -0.0362 96   GLN B OE1 
9516  N NE2 . GLN B 98   ? 0.2710 0.3181 0.2147 0.0619  0.0357  -0.0401 96   GLN B NE2 
9517  N N   . GLU B 99   ? 0.2786 0.3415 0.1954 0.0747  0.0486  -0.0442 97   GLU B N   
9518  C CA  . GLU B 99   ? 0.2872 0.3449 0.1944 0.0755  0.0489  -0.0461 97   GLU B CA  
9519  C C   . GLU B 99   ? 0.3258 0.3894 0.2327 0.0701  0.0498  -0.0432 97   GLU B C   
9520  O O   . GLU B 99   ? 0.3100 0.3665 0.2108 0.0675  0.0479  -0.0437 97   GLU B O   
9521  C CB  . GLU B 99   ? 0.3176 0.3781 0.2194 0.0828  0.0525  -0.0486 97   GLU B CB  
9522  C CG  . GLU B 99   ? 0.3128 0.3638 0.2118 0.0884  0.0511  -0.0522 97   GLU B CG  
9523  C CD  . GLU B 99   ? 0.3212 0.3753 0.2182 0.0943  0.0539  -0.0534 97   GLU B CD  
9524  O OE1 . GLU B 99   ? 0.3422 0.4071 0.2406 0.0943  0.0573  -0.0514 97   GLU B OE1 
9525  O OE2 . GLU B 99   ? 0.3237 0.3688 0.2182 0.0982  0.0523  -0.0559 97   GLU B OE2 
9526  N N   . GLY B 100  ? 0.2945 0.3710 0.2076 0.0682  0.0525  -0.0399 98   GLY B N   
9527  C CA  . GLY B 100  ? 0.2970 0.3787 0.2101 0.0625  0.0530  -0.0368 98   GLY B CA  
9528  C C   . GLY B 100  ? 0.3142 0.3884 0.2292 0.0563  0.0488  -0.0354 98   GLY B C   
9529  O O   . GLY B 100  ? 0.2988 0.3696 0.2093 0.0527  0.0477  -0.0346 98   GLY B O   
9530  N N   . VAL B 101  ? 0.2949 0.3664 0.2165 0.0552  0.0464  -0.0352 99   VAL B N   
9531  C CA  . VAL B 101  ? 0.2867 0.3511 0.2104 0.0498  0.0424  -0.0341 99   VAL B CA  
9532  C C   . VAL B 101  ? 0.3242 0.3760 0.2408 0.0502  0.0394  -0.0368 99   VAL B C   
9533  O O   . VAL B 101  ? 0.3140 0.3613 0.2281 0.0460  0.0372  -0.0358 99   VAL B O   
9534  C CB  . VAL B 101  ? 0.2951 0.3594 0.2270 0.0491  0.0407  -0.0335 99   VAL B CB  
9535  C CG1 . VAL B 101  ? 0.3036 0.3596 0.2369 0.0444  0.0366  -0.0330 99   VAL B CG1 
9536  C CG2 . VAL B 101  ? 0.3104 0.3871 0.2495 0.0477  0.0431  -0.0305 99   VAL B CG2 
9537  N N   . ALA B 102  ? 0.3002 0.3459 0.2132 0.0552  0.0391  -0.0401 100  ALA B N   
9538  C CA  . ALA B 102  ? 0.3044 0.3379 0.2106 0.0556  0.0360  -0.0428 100  ALA B CA  
9539  C C   . ALA B 102  ? 0.2985 0.3311 0.1966 0.0548  0.0367  -0.0430 100  ALA B C   
9540  O O   . ALA B 102  ? 0.3201 0.3449 0.2143 0.0517  0.0335  -0.0433 100  ALA B O   
9541  C CB  . ALA B 102  ? 0.2733 0.3009 0.1763 0.0615  0.0360  -0.0464 100  ALA B CB  
9542  N N   . LEU B 103  ? 0.2849 0.3256 0.1802 0.0574  0.0408  -0.0427 101  LEU B N   
9543  C CA  . LEU B 103  ? 0.3183 0.3585 0.2052 0.0569  0.0418  -0.0429 101  LEU B CA  
9544  C C   . LEU B 103  ? 0.3331 0.3751 0.2214 0.0504  0.0404  -0.0395 101  LEU B C   
9545  O O   . LEU B 103  ? 0.3467 0.3824 0.2285 0.0483  0.0385  -0.0398 101  LEU B O   
9546  C CB  . LEU B 103  ? 0.3122 0.3623 0.1966 0.0611  0.0469  -0.0430 101  LEU B CB  
9547  C CG  . LEU B 103  ? 0.3144 0.3663 0.1906 0.0607  0.0488  -0.0427 101  LEU B CG  
9548  C CD1 . LEU B 103  ? 0.3551 0.3948 0.2212 0.0630  0.0465  -0.0463 101  LEU B CD1 
9549  C CD2 . LEU B 103  ? 0.3235 0.3875 0.1994 0.0646  0.0542  -0.0422 101  LEU B CD2 
9550  N N   . MET B 104  ? 0.3028 0.3527 0.1992 0.0470  0.0412  -0.0362 102  MET B N   
9551  C CA  . MET B 104  ? 0.3492 0.4001 0.2470 0.0408  0.0397  -0.0329 102  MET B CA  
9552  C C   . MET B 104  ? 0.3428 0.3830 0.2409 0.0378  0.0348  -0.0334 102  MET B C   
9553  O O   . MET B 104  ? 0.3485 0.3851 0.2434 0.0341  0.0328  -0.0321 102  MET B O   
9554  C CB  . MET B 104  ? 0.3347 0.3960 0.2410 0.0380  0.0415  -0.0294 102  MET B CB  
9555  C CG  . MET B 104  ? 0.3432 0.4165 0.2495 0.0402  0.0464  -0.0283 102  MET B CG  
9556  S SD  . MET B 104  ? 0.4631 0.5387 0.3595 0.0401  0.0488  -0.0278 102  MET B SD  
9557  C CE  . MET B 104  ? 0.4918 0.5672 0.3897 0.0319  0.0466  -0.0235 102  MET B CE  
9558  N N   . CYS B 105  ? 0.2919 0.3270 0.1939 0.0395  0.0328  -0.0352 103  CYS B N   
9559  C CA  . CYS B 105  ? 0.3224 0.3476 0.2247 0.0371  0.0282  -0.0360 103  CYS B CA  
9560  C C   . CYS B 105  ? 0.3459 0.3627 0.2390 0.0381  0.0264  -0.0382 103  CYS B C   
9561  O O   . CYS B 105  ? 0.3541 0.3655 0.2453 0.0346  0.0232  -0.0374 103  CYS B O   
9562  C CB  . CYS B 105  ? 0.3011 0.3228 0.2086 0.0391  0.0267  -0.0376 103  CYS B CB  
9563  S SG  . CYS B 105  ? 0.3195 0.3489 0.2379 0.0371  0.0276  -0.0349 103  CYS B SG  
9564  N N   . LEU B 106  ? 0.3093 0.3247 0.1964 0.0429  0.0281  -0.0411 104  LEU B N   
9565  C CA  . LEU B 106  ? 0.3229 0.3304 0.2003 0.0439  0.0266  -0.0434 104  LEU B CA  
9566  C C   . LEU B 106  ? 0.3746 0.3850 0.2472 0.0410  0.0273  -0.0412 104  LEU B C   
9567  O O   . LEU B 106  ? 0.3858 0.3893 0.2534 0.0387  0.0242  -0.0415 104  LEU B O   
9568  C CB  . LEU B 106  ? 0.3434 0.3497 0.2149 0.0500  0.0289  -0.0468 104  LEU B CB  
9569  C CG  . LEU B 106  ? 0.3525 0.3512 0.2128 0.0515  0.0278  -0.0493 104  LEU B CG  
9570  C CD1 . LEU B 106  ? 0.3822 0.3692 0.2408 0.0500  0.0227  -0.0511 104  LEU B CD1 
9571  C CD2 . LEU B 106  ? 0.3732 0.3726 0.2274 0.0578  0.0311  -0.0524 104  LEU B CD2 
9572  N N   . ALA B 107  ? 0.3474 0.3681 0.2214 0.0408  0.0313  -0.0390 105  ALA B N   
9573  C CA  . ALA B 107  ? 0.3650 0.3889 0.2344 0.0377  0.0323  -0.0366 105  ALA B CA  
9574  C C   . ALA B 107  ? 0.4090 0.4301 0.2818 0.0320  0.0288  -0.0338 105  ALA B C   
9575  O O   . ALA B 107  ? 0.4369 0.4541 0.3038 0.0295  0.0270  -0.0330 105  ALA B O   
9576  C CB  . ALA B 107  ? 0.3394 0.3759 0.2111 0.0382  0.0372  -0.0343 105  ALA B CB  
9577  N N   . GLU B 108  ? 0.3787 0.4015 0.2605 0.0300  0.0277  -0.0323 106  GLU B N   
9578  C CA  . GLU B 108  ? 0.4017 0.4212 0.2870 0.0250  0.0242  -0.0299 106  GLU B CA  
9579  C C   . GLU B 108  ? 0.4388 0.4477 0.3199 0.0246  0.0198  -0.0318 106  GLU B C   
9580  O O   . GLU B 108  ? 0.4453 0.4509 0.3237 0.0213  0.0175  -0.0302 106  GLU B O   
9581  C CB  . GLU B 108  ? 0.3955 0.4178 0.2908 0.0238  0.0238  -0.0288 106  GLU B CB  
9582  C CG  . GLU B 108  ? 0.4247 0.4420 0.3237 0.0197  0.0199  -0.0272 106  GLU B CG  
9583  C CD  . GLU B 108  ? 0.4738 0.4922 0.3818 0.0194  0.0191  -0.0270 106  GLU B CD  
9584  O OE1 . GLU B 108  ? 0.4512 0.4759 0.3633 0.0214  0.0219  -0.0271 106  GLU B OE1 
9585  O OE2 . GLU B 108  ? 0.4729 0.4860 0.3840 0.0172  0.0157  -0.0266 106  GLU B OE2 
9586  N N   . ALA B 109  ? 0.4299 0.4332 0.3104 0.0278  0.0186  -0.0351 107  ALA B N   
9587  C CA  . ALA B 109  ? 0.4616 0.4550 0.3386 0.0272  0.0142  -0.0368 107  ALA B CA  
9588  C C   . ALA B 109  ? 0.4773 0.4672 0.3440 0.0275  0.0138  -0.0376 107  ALA B C   
9589  O O   . ALA B 109  ? 0.4498 0.4339 0.3136 0.0249  0.0102  -0.0371 107  ALA B O   
9590  C CB  . ALA B 109  ? 0.4689 0.4572 0.3472 0.0305  0.0130  -0.0400 107  ALA B CB  
9591  N N   . LEU B 110  ? 0.4293 0.4227 0.2903 0.0307  0.0174  -0.0388 108  LEU B N   
9592  C CA  . LEU B 110  ? 0.4422 0.4326 0.2927 0.0311  0.0174  -0.0396 108  LEU B CA  
9593  C C   . LEU B 110  ? 0.4810 0.4746 0.3302 0.0269  0.0173  -0.0360 108  LEU B C   
9594  O O   . LEU B 110  ? 0.5123 0.5011 0.3540 0.0256  0.0153  -0.0360 108  LEU B O   
9595  C CB  . LEU B 110  ? 0.4320 0.4263 0.2769 0.0359  0.0218  -0.0417 108  LEU B CB  
9596  C CG  . LEU B 110  ? 0.4090 0.3977 0.2521 0.0407  0.0214  -0.0459 108  LEU B CG  
9597  C CD1 . LEU B 110  ? 0.4429 0.4369 0.2818 0.0458  0.0263  -0.0476 108  LEU B CD1 
9598  C CD2 . LEU B 110  ? 0.4713 0.4485 0.3069 0.0405  0.0170  -0.0484 108  LEU B CD2 
9599  N N   . LEU B 111  ? 0.4510 0.4522 0.3069 0.0244  0.0192  -0.0327 109  LEU B N   
9600  C CA  . LEU B 111  ? 0.5010 0.5046 0.3558 0.0200  0.0189  -0.0290 109  LEU B CA  
9601  C C   . LEU B 111  ? 0.5168 0.5135 0.3737 0.0165  0.0139  -0.0278 109  LEU B C   
9602  O O   . LEU B 111  ? 0.5202 0.5162 0.3741 0.0132  0.0127  -0.0252 109  LEU B O   
9603  C CB  . LEU B 111  ? 0.5009 0.5144 0.3619 0.0183  0.0224  -0.0259 109  LEU B CB  
9604  C CG  . LEU B 111  ? 0.4883 0.5101 0.3459 0.0211  0.0276  -0.0261 109  LEU B CG  
9605  C CD1 . LEU B 111  ? 0.5197 0.5518 0.3844 0.0189  0.0306  -0.0229 109  LEU B CD1 
9606  C CD2 . LEU B 111  ? 0.5320 0.5528 0.3793 0.0206  0.0283  -0.0257 109  LEU B CD2 
9607  N N   . ARG B 112  ? 0.4894 0.4812 0.3513 0.0172  0.0110  -0.0296 110  ARG B N   
9608  C CA  . ARG B 112  ? 0.5298 0.5149 0.3931 0.0144  0.0062  -0.0288 110  ARG B CA  
9609  C C   . ARG B 112  ? 0.5342 0.5122 0.3887 0.0147  0.0032  -0.0304 110  ARG B C   
9610  O O   . ARG B 112  ? 0.5688 0.5416 0.4235 0.0124  -0.0009 -0.0295 110  ARG B O   
9611  C CB  . ARG B 112  ? 0.5281 0.5109 0.3996 0.0150  0.0041  -0.0301 110  ARG B CB  
9612  C CG  . ARG B 112  ? 0.5621 0.5517 0.4424 0.0145  0.0066  -0.0285 110  ARG B CG  
9613  C CD  . ARG B 112  ? 0.6270 0.6140 0.5155 0.0140  0.0041  -0.0289 110  ARG B CD  
9614  N NE  . ARG B 112  ? 0.6443 0.6289 0.5340 0.0173  0.0041  -0.0320 110  ARG B NE  
9615  C CZ  . ARG B 112  ? 0.7110 0.7000 0.6054 0.0194  0.0068  -0.0327 110  ARG B CZ  
9616  N NH1 . ARG B 112  ? 0.6317 0.6282 0.5303 0.0185  0.0097  -0.0306 110  ARG B NH1 
9617  N NH2 . ARG B 112  ? 0.6983 0.6839 0.5930 0.0223  0.0063  -0.0356 110  ARG B NH2 
9618  N N   . ILE B 113  ? 0.5408 0.5182 0.3873 0.0176  0.0052  -0.0326 111  ILE B N   
9619  C CA  . ILE B 113  ? 0.5742 0.5453 0.4110 0.0178  0.0028  -0.0339 111  ILE B CA  
9620  C C   . ILE B 113  ? 0.5885 0.5629 0.4198 0.0155  0.0043  -0.0309 111  ILE B C   
9621  O O   . ILE B 113  ? 0.5940 0.5746 0.4224 0.0168  0.0088  -0.0305 111  ILE B O   
9622  C CB  . ILE B 113  ? 0.5966 0.5648 0.4268 0.0221  0.0042  -0.0380 111  ILE B CB  
9623  C CG1 . ILE B 113  ? 0.5589 0.5229 0.3943 0.0240  0.0022  -0.0407 111  ILE B CG1 
9624  C CG2 . ILE B 113  ? 0.5418 0.5038 0.3608 0.0221  0.0020  -0.0392 111  ILE B CG2 
9625  C CD1 . ILE B 113  ? 0.5514 0.5125 0.3811 0.0286  0.0039  -0.0447 111  ILE B CD1 
9626  N N   . PRO B 114  ? 0.6059 0.5767 0.4357 0.0120  0.0007  -0.0287 112  PRO B N   
9627  C CA  . PRO B 114  ? 0.5728 0.5469 0.3981 0.0094  0.0021  -0.0253 112  PRO B CA  
9628  C C   . PRO B 114  ? 0.5553 0.5288 0.3691 0.0109  0.0038  -0.0264 112  PRO B C   
9629  O O   . PRO B 114  ? 0.6306 0.6103 0.4413 0.0104  0.0076  -0.0244 112  PRO B O   
9630  C CB  . PRO B 114  ? 0.5324 0.5013 0.3590 0.0059  -0.0029 -0.0230 112  PRO B CB  
9631  C CG  . PRO B 114  ? 0.5714 0.5365 0.4056 0.0066  -0.0061 -0.0248 112  PRO B CG  
9632  C CD  . PRO B 114  ? 0.5713 0.5353 0.4040 0.0104  -0.0047 -0.0288 112  PRO B CD  
9633  N N   . ASP B 115  ? 0.5791 0.5454 0.3865 0.0128  0.0010  -0.0295 113  ASP B N   
9634  C CA  . ASP B 115  ? 0.6427 0.6072 0.4381 0.0142  0.0021  -0.0307 113  ASP B CA  
9635  C C   . ASP B 115  ? 0.6333 0.6027 0.4264 0.0184  0.0073  -0.0332 113  ASP B C   
9636  O O   . ASP B 115  ? 0.6388 0.6065 0.4350 0.0216  0.0075  -0.0364 113  ASP B O   
9637  C CB  . ASP B 115  ? 0.6266 0.5815 0.4159 0.0146  -0.0029 -0.0333 113  ASP B CB  
9638  C CG  . ASP B 115  ? 0.7028 0.6551 0.4792 0.0166  -0.0018 -0.0353 113  ASP B CG  
9639  O OD1 . ASP B 115  ? 0.7439 0.6994 0.5144 0.0153  0.0002  -0.0328 113  ASP B OD1 
9640  O OD2 . ASP B 115  ? 0.7441 0.6907 0.5159 0.0196  -0.0031 -0.0393 113  ASP B OD2 
9641  N N   . THR B 116  ? 0.6555 0.6310 0.4432 0.0186  0.0115  -0.0316 114  THR B N   
9642  C CA  . THR B 116  ? 0.6750 0.6565 0.4607 0.0228  0.0169  -0.0337 114  THR B CA  
9643  C C   . THR B 116  ? 0.7068 0.6814 0.4842 0.0272  0.0161  -0.0386 114  THR B C   
9644  O O   . THR B 116  ? 0.6720 0.6479 0.4513 0.0314  0.0185  -0.0415 114  THR B O   
9645  C CB  . THR B 116  ? 0.6886 0.6780 0.4694 0.0217  0.0213  -0.0307 114  THR B CB  
9646  O OG1 . THR B 116  ? 0.7553 0.7514 0.5446 0.0177  0.0222  -0.0263 114  THR B OG1 
9647  C CG2 . THR B 116  ? 0.7291 0.7249 0.5067 0.0265  0.0269  -0.0330 114  THR B CG2 
9648  N N   . ALA B 117  ? 0.7088 0.6757 0.4769 0.0264  0.0127  -0.0395 115  ALA B N   
9649  C CA  . ALA B 117  ? 0.7204 0.6800 0.4795 0.0304  0.0118  -0.0442 115  ALA B CA  
9650  C C   . ALA B 117  ? 0.6656 0.6188 0.4302 0.0319  0.0085  -0.0473 115  ALA B C   
9651  O O   . ALA B 117  ? 0.7019 0.6522 0.4631 0.0363  0.0097  -0.0513 115  ALA B O   
9652  C CB  . ALA B 117  ? 0.7178 0.6704 0.4658 0.0286  0.0083  -0.0443 115  ALA B CB  
9653  N N   . THR B 118  ? 0.6704 0.6211 0.4431 0.0284  0.0043  -0.0456 116  THR B N   
9654  C CA  . THR B 118  ? 0.6577 0.6029 0.4362 0.0293  0.0012  -0.0481 116  THR B CA  
9655  C C   . THR B 118  ? 0.6679 0.6188 0.4540 0.0324  0.0052  -0.0490 116  THR B C   
9656  O O   . THR B 118  ? 0.6367 0.5831 0.4223 0.0357  0.0048  -0.0525 116  THR B O   
9657  C CB  . THR B 118  ? 0.6473 0.5901 0.4334 0.0249  -0.0037 -0.0456 116  THR B CB  
9658  O OG1 . THR B 118  ? 0.6791 0.6162 0.4579 0.0225  -0.0078 -0.0450 116  THR B OG1 
9659  C CG2 . THR B 118  ? 0.6016 0.5396 0.3942 0.0257  -0.0066 -0.0479 116  THR B CG2 
9660  N N   . ARG B 119  ? 0.6326 0.5930 0.4256 0.0312  0.0088  -0.0457 117  ARG B N   
9661  C CA  . ARG B 119  ? 0.6103 0.5770 0.4110 0.0338  0.0125  -0.0462 117  ARG B CA  
9662  C C   . ARG B 119  ? 0.6147 0.5830 0.4086 0.0392  0.0167  -0.0493 117  ARG B C   
9663  O O   . ARG B 119  ? 0.6135 0.5801 0.4096 0.0429  0.0174  -0.0522 117  ARG B O   
9664  C CB  . ARG B 119  ? 0.5913 0.5679 0.3998 0.0309  0.0153  -0.0419 117  ARG B CB  
9665  C CG  . ARG B 119  ? 0.5331 0.5171 0.3500 0.0332  0.0190  -0.0418 117  ARG B CG  
9666  C CD  . ARG B 119  ? 0.5357 0.5303 0.3564 0.0309  0.0228  -0.0378 117  ARG B CD  
9667  N NE  . ARG B 119  ? 0.5785 0.5723 0.4026 0.0255  0.0198  -0.0342 117  ARG B NE  
9668  C CZ  . ARG B 119  ? 0.6103 0.6089 0.4323 0.0223  0.0212  -0.0307 117  ARG B CZ  
9669  N NH1 . ARG B 119  ? 0.5664 0.5714 0.3829 0.0236  0.0256  -0.0301 117  ARG B NH1 
9670  N NH2 . ARG B 119  ? 0.6047 0.6015 0.4300 0.0177  0.0181  -0.0276 117  ARG B NH2 
9671  N N   . ASP B 120  ? 0.6263 0.5978 0.4117 0.0399  0.0196  -0.0488 118  ASP B N   
9672  C CA  . ASP B 120  ? 0.6469 0.6202 0.4251 0.0454  0.0238  -0.0518 118  ASP B CA  
9673  C C   . ASP B 120  ? 0.6436 0.6056 0.4145 0.0489  0.0209  -0.0567 118  ASP B C   
9674  O O   . ASP B 120  ? 0.6296 0.5915 0.3979 0.0541  0.0236  -0.0599 118  ASP B O   
9675  C CB  . ASP B 120  ? 0.6658 0.6439 0.4353 0.0451  0.0269  -0.0502 118  ASP B CB  
9676  C CG  . ASP B 120  ? 0.6718 0.6621 0.4480 0.0424  0.0308  -0.0456 118  ASP B CG  
9677  O OD1 . ASP B 120  ? 0.6358 0.6311 0.4230 0.0414  0.0314  -0.0440 118  ASP B OD1 
9678  O OD2 . ASP B 120  ? 0.6771 0.6720 0.4471 0.0412  0.0332  -0.0436 118  ASP B OD2 
9679  N N   . ALA B 121  ? 0.6698 0.6223 0.4374 0.0460  0.0153  -0.0574 119  ALA B N   
9680  C CA  . ALA B 121  ? 0.6737 0.6149 0.4345 0.0486  0.0120  -0.0619 119  ALA B CA  
9681  C C   . ALA B 121  ? 0.6733 0.6114 0.4426 0.0497  0.0103  -0.0634 119  ALA B C   
9682  O O   . ALA B 121  ? 0.6828 0.6149 0.4478 0.0538  0.0102  -0.0674 119  ALA B O   
9683  C CB  . ALA B 121  ? 0.6263 0.5589 0.3809 0.0449  0.0064  -0.0619 119  ALA B CB  
9684  N N   . LEU B 122  ? 0.6439 0.5857 0.4248 0.0461  0.0089  -0.0604 120  LEU B N   
9685  C CA  . LEU B 122  ? 0.6366 0.5766 0.4260 0.0470  0.0078  -0.0615 120  LEU B CA  
9686  C C   . LEU B 122  ? 0.6329 0.5789 0.4245 0.0520  0.0130  -0.0627 120  LEU B C   
9687  O O   . LEU B 122  ? 0.6455 0.5867 0.4375 0.0553  0.0125  -0.0657 120  LEU B O   
9688  C CB  . LEU B 122  ? 0.6301 0.5738 0.4312 0.0423  0.0058  -0.0578 120  LEU B CB  
9689  C CG  . LEU B 122  ? 0.6299 0.5710 0.4398 0.0425  0.0039  -0.0586 120  LEU B CG  
9690  C CD1 . LEU B 122  ? 0.6672 0.5969 0.4729 0.0420  -0.0014 -0.0614 120  LEU B CD1 
9691  C CD2 . LEU B 122  ? 0.6260 0.5730 0.4476 0.0385  0.0032  -0.0548 120  LEU B CD2 
9692  N N   . ILE B 123  ? 0.6171 0.5737 0.4100 0.0526  0.0179  -0.0604 121  ILE B N   
9693  C CA  . ILE B 123  ? 0.6034 0.5673 0.3989 0.0574  0.0231  -0.0612 121  ILE B CA  
9694  C C   . ILE B 123  ? 0.6821 0.6401 0.4672 0.0633  0.0243  -0.0658 121  ILE B C   
9695  O O   . ILE B 123  ? 0.6616 0.6173 0.4484 0.0675  0.0251  -0.0683 121  ILE B O   
9696  C CB  . ILE B 123  ? 0.5809 0.5574 0.3786 0.0564  0.0278  -0.0576 121  ILE B CB  
9697  C CG1 . ILE B 123  ? 0.5016 0.4841 0.3105 0.0511  0.0269  -0.0533 121  ILE B CG1 
9698  C CG2 . ILE B 123  ? 0.5771 0.5614 0.3750 0.0620  0.0335  -0.0588 121  ILE B CG2 
9699  C CD1 . ILE B 123  ? 0.5096 0.5035 0.3201 0.0490  0.0309  -0.0494 121  ILE B CD1 
9700  N N   . ARG B 124  ? 0.6188 0.5736 0.3926 0.0638  0.0244  -0.0670 122  ARG B N   
9701  C CA  . ARG B 124  ? 0.6894 0.6403 0.4554 0.0686  0.0261  -0.0704 122  ARG B CA  
9702  C C   . ARG B 124  ? 0.7321 0.6696 0.4950 0.0693  0.0213  -0.0740 122  ARG B C   
9703  O O   . ARG B 124  ? 0.7776 0.7120 0.5391 0.0733  0.0224  -0.0766 122  ARG B O   
9704  C CB  . ARG B 124  ? 0.7397 0.6926 0.4972 0.0676  0.0277  -0.0697 122  ARG B CB  
9705  C CG  . ARG B 124  ? 0.7724 0.7232 0.5238 0.0716  0.0298  -0.0724 122  ARG B CG  
9706  C CD  . ARG B 124  ? 0.8071 0.7622 0.5511 0.0703  0.0321  -0.0710 122  ARG B CD  
9707  N NE  . ARG B 124  ? 0.7875 0.7562 0.5364 0.0696  0.0371  -0.0673 122  ARG B NE  
9708  C CZ  . ARG B 124  ? 0.8136 0.7911 0.5621 0.0721  0.0424  -0.0667 122  ARG B CZ  
9709  N NH1 . ARG B 124  ? 0.8217 0.7956 0.5646 0.0760  0.0437  -0.0697 122  ARG B NH1 
9710  N NH2 . ARG B 124  ? 0.7994 0.7894 0.5531 0.0707  0.0464  -0.0629 122  ARG B NH2 
9711  N N   . ASP B 125  ? 0.7256 0.6551 0.4873 0.0654  0.0158  -0.0741 123  ASP B N   
9712  C CA  . ASP B 125  ? 0.7630 0.6799 0.5213 0.0651  0.0108  -0.0771 123  ASP B CA  
9713  C C   . ASP B 125  ? 0.7491 0.6617 0.5147 0.0645  0.0078  -0.0776 123  ASP B C   
9714  O O   . ASP B 125  ? 0.8063 0.7089 0.5700 0.0645  0.0040  -0.0800 123  ASP B O   
9715  C CB  . ASP B 125  ? 0.7961 0.7062 0.5472 0.0610  0.0061  -0.0769 123  ASP B CB  
9716  C CG  . ASP B 125  ? 0.8362 0.7500 0.5796 0.0612  0.0088  -0.0763 123  ASP B CG  
9717  O OD1 . ASP B 125  ? 0.8429 0.7624 0.5852 0.0651  0.0137  -0.0769 123  ASP B OD1 
9718  O OD2 . ASP B 125  ? 0.8676 0.7788 0.6059 0.0575  0.0058  -0.0751 123  ASP B OD2 
9719  N N   . LYS B 126  ? 0.6996 0.6202 0.4755 0.0630  0.0093  -0.0748 124  LYS B N   
9720  C CA  . LYS B 126  ? 0.7060 0.6236 0.4911 0.0617  0.0066  -0.0746 124  LYS B CA  
9721  C C   . LYS B 126  ? 0.7564 0.6829 0.5511 0.0640  0.0106  -0.0731 124  LYS B C   
9722  O O   . LYS B 126  ? 0.8003 0.7229 0.5982 0.0662  0.0099  -0.0748 124  LYS B O   
9723  C CB  . LYS B 126  ? 0.7239 0.6408 0.5153 0.0551  0.0021  -0.0716 124  LYS B CB  
9724  N N   . ILE B 127  ? 0.6860 0.6244 0.4854 0.0634  0.0148  -0.0700 125  ILE B N   
9725  C CA  . ILE B 127  ? 0.6977 0.6451 0.5073 0.0648  0.0181  -0.0683 125  ILE B CA  
9726  C C   . ILE B 127  ? 0.6405 0.5907 0.4463 0.0716  0.0226  -0.0707 125  ILE B C   
9727  O O   . ILE B 127  ? 0.6392 0.5901 0.4503 0.0745  0.0236  -0.0715 125  ILE B O   
9728  C CB  . ILE B 127  ? 0.6122 0.5710 0.4290 0.0608  0.0202  -0.0637 125  ILE B CB  
9729  C CG1 . ILE B 127  ? 0.6354 0.5908 0.4542 0.0546  0.0157  -0.0614 125  ILE B CG1 
9730  C CG2 . ILE B 127  ? 0.5772 0.5443 0.4055 0.0612  0.0225  -0.0617 125  ILE B CG2 
9731  C CD1 . ILE B 127  ? 0.6823 0.6326 0.5086 0.0522  0.0117  -0.0613 125  ILE B CD1 
9732  N N   . ALA B 128  ? 0.6420 0.5939 0.4385 0.0745  0.0255  -0.0720 126  ALA B N   
9733  C CA  . ALA B 128  ? 0.6360 0.5923 0.4324 0.0796  0.0298  -0.0731 126  ALA B CA  
9734  C C   . ALA B 128  ? 0.7027 0.6488 0.4977 0.0829  0.0276  -0.0763 126  ALA B C   
9735  O O   . ALA B 128  ? 0.6931 0.6428 0.4911 0.0872  0.0305  -0.0769 126  ALA B O   
9736  C CB  . ALA B 128  ? 0.6381 0.5977 0.4270 0.0803  0.0325  -0.0730 126  ALA B CB  
9737  N N   . ASP B 129  ? 0.7351 0.6690 0.5258 0.0807  0.0224  -0.0782 127  ASP B N   
9738  C CA  . ASP B 129  ? 0.8179 0.7414 0.6078 0.0828  0.0196  -0.0809 127  ASP B CA  
9739  C C   . ASP B 129  ? 0.8512 0.7736 0.6494 0.0818  0.0177  -0.0802 127  ASP B C   
9740  O O   . ASP B 129  ? 0.8930 0.8048 0.6902 0.0810  0.0135  -0.0819 127  ASP B O   
9741  C CB  . ASP B 129  ? 0.8774 0.7884 0.6586 0.0806  0.0148  -0.0831 127  ASP B CB  
9742  C CG  . ASP B 129  ? 0.9478 0.8578 0.7202 0.0829  0.0166  -0.0846 127  ASP B CG  
9743  O OD1 . ASP B 129  ? 0.9548 0.8734 0.7279 0.0865  0.0216  -0.0841 127  ASP B OD1 
9744  O OD2 . ASP B 129  ? 1.0322 0.9329 0.7970 0.0810  0.0129  -0.0863 127  ASP B OD2 
9745  N N   . GLY B 130  ? 0.8114 0.7443 0.6176 0.0816  0.0205  -0.0777 128  GLY B N   
9746  C CA  . GLY B 130  ? 0.8078 0.7408 0.6223 0.0812  0.0193  -0.0771 128  GLY B CA  
9747  C C   . GLY B 130  ? 0.8461 0.7732 0.6644 0.0752  0.0142  -0.0759 128  GLY B C   
9748  O O   . GLY B 130  ? 0.7985 0.7294 0.6270 0.0727  0.0135  -0.0735 128  GLY B O   
9749  N N   . ASN B 131  ? 1.0800 0.9984 0.8909 0.0726  0.0104  -0.0772 129  ASN B N   
9750  C CA  . ASN B 131  ? 1.0676 0.9809 0.8826 0.0667  0.0052  -0.0759 129  ASN B CA  
9751  C C   . ASN B 131  ? 1.0440 0.9670 0.8678 0.0617  0.0057  -0.0715 129  ASN B C   
9752  O O   . ASN B 131  ? 1.0987 1.0200 0.9209 0.0575  0.0029  -0.0703 129  ASN B O   
9753  C CB  . ASN B 131  ? 1.0348 0.9373 0.8394 0.0652  0.0011  -0.0783 129  ASN B CB  
9754  N N   . TRP B 132  ? 0.8324 0.7652 0.6653 0.0622  0.0090  -0.0691 130  TRP B N   
9755  C CA  . TRP B 132  ? 0.7710 0.7131 0.6119 0.0579  0.0098  -0.0651 130  TRP B CA  
9756  C C   . TRP B 132  ? 0.7678 0.7084 0.6175 0.0534  0.0063  -0.0631 130  TRP B C   
9757  O O   . TRP B 132  ? 0.7997 0.7446 0.6540 0.0490  0.0054  -0.0602 130  TRP B O   
9758  C CB  . TRP B 132  ? 0.6928 0.6468 0.5389 0.0603  0.0151  -0.0633 130  TRP B CB  
9759  C CG  . TRP B 132  ? 0.5787 0.5347 0.4322 0.0626  0.0161  -0.0633 130  TRP B CG  
9760  C CD1 . TRP B 132  ? 0.5772 0.5320 0.4283 0.0683  0.0183  -0.0657 130  TRP B CD1 
9761  C CD2 . TRP B 132  ? 0.5488 0.5081 0.4130 0.0594  0.0150  -0.0607 130  TRP B CD2 
9762  N NE1 . TRP B 132  ? 0.5330 0.4903 0.3927 0.0687  0.0185  -0.0647 130  TRP B NE1 
9763  C CE2 . TRP B 132  ? 0.5527 0.5128 0.4204 0.0632  0.0165  -0.0617 130  TRP B CE2 
9764  C CE3 . TRP B 132  ? 0.5307 0.4921 0.4015 0.0539  0.0128  -0.0578 130  TRP B CE3 
9765  C CZ2 . TRP B 132  ? 0.5172 0.4803 0.3946 0.0615  0.0160  -0.0597 130  TRP B CZ2 
9766  C CZ3 . TRP B 132  ? 0.5166 0.4810 0.3969 0.0523  0.0124  -0.0560 130  TRP B CZ3 
9767  C CH2 . TRP B 132  ? 0.4916 0.4568 0.3751 0.0560  0.0139  -0.0570 130  TRP B CH2 
9768  N N   . LYS B 133  ? 0.7464 0.6813 0.5987 0.0544  0.0044  -0.0645 131  LYS B N   
9769  C CA  . LYS B 133  ? 0.7668 0.7014 0.6281 0.0504  0.0015  -0.0625 131  LYS B CA  
9770  C C   . LYS B 133  ? 0.8887 0.8182 0.7486 0.0456  -0.0030 -0.0619 131  LYS B C   
9771  O O   . LYS B 133  ? 0.8999 0.8334 0.7667 0.0416  -0.0042 -0.0590 131  LYS B O   
9772  C CB  . LYS B 133  ? 0.7103 0.6390 0.5735 0.0525  0.0003  -0.0642 131  LYS B CB  
9773  C CG  . LYS B 133  ? 0.6884 0.6204 0.5511 0.0581  0.0044  -0.0655 131  LYS B CG  
9774  C CD  . LYS B 133  ? 0.6964 0.6290 0.5671 0.0585  0.0042  -0.0647 131  LYS B CD  
9775  C CE  . LYS B 133  ? 0.6930 0.6292 0.5634 0.0643  0.0082  -0.0658 131  LYS B CE  
9776  N NZ  . LYS B 133  ? 0.5925 0.5318 0.4716 0.0646  0.0086  -0.0643 131  LYS B NZ  
9777  N N   . SER B 134  ? 0.9614 0.8821 0.8120 0.0462  -0.0056 -0.0645 132  SER B N   
9778  C CA  . SER B 134  ? 0.9677 0.8834 0.8167 0.0418  -0.0102 -0.0640 132  SER B CA  
9779  C C   . SER B 134  ? 0.9568 0.8787 0.8059 0.0392  -0.0095 -0.0615 132  SER B C   
9780  O O   . SER B 134  ? 0.9586 0.8820 0.8131 0.0351  -0.0121 -0.0591 132  SER B O   
9781  C CB  . SER B 134  ? 0.9521 0.8569 0.7903 0.0431  -0.0131 -0.0676 132  SER B CB  
9782  N N   . HIS B 135  ? 0.9391 0.8648 0.7823 0.0417  -0.0060 -0.0618 133  HIS B N   
9783  C CA  . HIS B 135  ? 0.9382 0.8669 0.7780 0.0393  -0.0060 -0.0600 133  HIS B CA  
9784  C C   . HIS B 135  ? 0.8933 0.8304 0.7423 0.0360  -0.0051 -0.0560 133  HIS B C   
9785  O O   . HIS B 135  ? 0.8721 0.8097 0.7204 0.0326  -0.0071 -0.0541 133  HIS B O   
9786  C CB  . HIS B 135  ? 0.8514 0.7824 0.6826 0.0429  -0.0021 -0.0614 133  HIS B CB  
9787  N N   . LEU B 136  ? 0.8626 0.8063 0.7198 0.0368  -0.0023 -0.0547 134  LEU B N   
9788  C CA  . LEU B 136  ? 0.8116 0.7633 0.6764 0.0339  -0.0010 -0.0510 134  LEU B CA  
9789  C C   . LEU B 136  ? 0.8026 0.7557 0.6777 0.0324  -0.0021 -0.0498 134  LEU B C   
9790  O O   . LEU B 136  ? 0.7299 0.6902 0.6118 0.0322  0.0006  -0.0478 134  LEU B O   
9791  C CB  . LEU B 136  ? 0.7133 0.6737 0.5777 0.0360  0.0042  -0.0499 134  LEU B CB  
9792  C CG  . LEU B 136  ? 0.7063 0.6666 0.5606 0.0374  0.0058  -0.0508 134  LEU B CG  
9793  C CD1 . LEU B 136  ? 0.6330 0.6004 0.4862 0.0413  0.0111  -0.0512 134  LEU B CD1 
9794  C CD2 . LEU B 136  ? 0.6763 0.6388 0.5295 0.0334  0.0048  -0.0479 134  LEU B CD2 
9795  N N   . GLY B 137  ? 0.8539 0.8001 0.7302 0.0310  -0.0061 -0.0508 135  GLY B N   
9796  C CA  . GLY B 137  ? 0.7944 0.7417 0.6801 0.0292  -0.0075 -0.0495 135  GLY B CA  
9797  C C   . GLY B 137  ? 0.8241 0.7719 0.7135 0.0320  -0.0057 -0.0506 135  GLY B C   
9798  O O   . GLY B 137  ? 0.8170 0.7643 0.7133 0.0306  -0.0072 -0.0500 135  GLY B O   
9799  N N   . GLY B 138  ? 0.9193 0.8685 0.8046 0.0360  -0.0024 -0.0523 136  GLY B N   
9800  C CA  . GLY B 138  ? 0.8894 0.8385 0.7777 0.0390  -0.0008 -0.0535 136  GLY B CA  
9801  C C   . GLY B 138  ? 0.8144 0.7729 0.7100 0.0395  0.0028  -0.0513 136  GLY B C   
9802  O O   . GLY B 138  ? 0.8206 0.7857 0.7195 0.0373  0.0041  -0.0488 136  GLY B O   
9803  N N   . SER B 139  ? 0.6603 0.6189 0.5585 0.0425  0.0041  -0.0523 137  SER B N   
9804  C CA  . SER B 139  ? 0.6219 0.5893 0.5266 0.0437  0.0076  -0.0506 137  SER B CA  
9805  C C   . SER B 139  ? 0.6363 0.6087 0.5493 0.0395  0.0069  -0.0475 137  SER B C   
9806  O O   . SER B 139  ? 0.6313 0.6117 0.5478 0.0386  0.0094  -0.0453 137  SER B O   
9807  C CB  . SER B 139  ? 0.5952 0.5604 0.5015 0.0472  0.0082  -0.0521 137  SER B CB  
9808  O OG  . SER B 139  ? 0.6557 0.6117 0.5547 0.0497  0.0065  -0.0552 137  SER B OG  
9809  N N   . ARG B 140  ? 0.7118 0.6794 0.6282 0.0368  0.0035  -0.0472 138  ARG B N   
9810  C CA  . ARG B 140  ? 0.7095 0.6810 0.6335 0.0332  0.0027  -0.0445 138  ARG B CA  
9811  C C   . ARG B 140  ? 0.6421 0.6178 0.5654 0.0306  0.0032  -0.0426 138  ARG B C   
9812  O O   . ARG B 140  ? 0.6595 0.6421 0.5873 0.0294  0.0051  -0.0404 138  ARG B O   
9813  C CB  . ARG B 140  ? 0.6378 0.6032 0.5643 0.0309  -0.0012 -0.0447 138  ARG B CB  
9814  C CG  . ARG B 140  ? 0.6316 0.5911 0.5571 0.0332  -0.0021 -0.0469 138  ARG B CG  
9815  C CD  . ARG B 140  ? 0.6244 0.5845 0.5575 0.0318  -0.0031 -0.0457 138  ARG B CD  
9816  N NE  . ARG B 140  ? 0.6916 0.6479 0.6241 0.0346  -0.0028 -0.0473 138  ARG B NE  
9817  C CZ  . ARG B 140  ? 0.7186 0.6668 0.6481 0.0346  -0.0056 -0.0489 138  ARG B CZ  
9818  N NH1 . ARG B 140  ? 0.6831 0.6264 0.6103 0.0318  -0.0089 -0.0493 138  ARG B NH1 
9819  N NH2 . ARG B 140  ? 0.6365 0.5812 0.5652 0.0373  -0.0052 -0.0502 138  ARG B NH2 
9820  N N   . SER B 141  ? 0.5831 0.5545 0.5001 0.0298  0.0013  -0.0433 139  SER B N   
9821  C CA  . SER B 141  ? 0.5798 0.5544 0.4952 0.0274  0.0016  -0.0414 139  SER B CA  
9822  C C   . SER B 141  ? 0.5122 0.4933 0.4249 0.0291  0.0057  -0.0408 139  SER B C   
9823  O O   . SER B 141  ? 0.5257 0.5126 0.4409 0.0271  0.0071  -0.0384 139  SER B O   
9824  C CB  . SER B 141  ? 0.5454 0.5135 0.4542 0.0263  -0.0015 -0.0424 139  SER B CB  
9825  O OG  . SER B 141  ? 0.6812 0.6517 0.5842 0.0261  0.0001  -0.0418 139  SER B OG  
9826  N N   . LEU B 142  ? 0.5044 0.4847 0.4121 0.0330  0.0076  -0.0431 140  LEU B N   
9827  C CA  A LEU B 142  ? 0.4612 0.4475 0.3651 0.0349  0.0113  -0.0428 140  LEU B CA  
9828  C CA  B LEU B 142  ? 0.4605 0.4468 0.3644 0.0347  0.0113  -0.0427 140  LEU B CA  
9829  C C   . LEU B 142  ? 0.3937 0.3894 0.3043 0.0344  0.0144  -0.0404 140  LEU B C   
9830  O O   . LEU B 142  ? 0.3394 0.3414 0.2490 0.0333  0.0167  -0.0386 140  LEU B O   
9831  C CB  A LEU B 142  ? 0.4499 0.4333 0.3477 0.0397  0.0128  -0.0460 140  LEU B CB  
9832  C CB  B LEU B 142  ? 0.4476 0.4311 0.3448 0.0395  0.0128  -0.0458 140  LEU B CB  
9833  C CG  A LEU B 142  ? 0.4472 0.4294 0.3354 0.0415  0.0140  -0.0474 140  LEU B CG  
9834  C CG  B LEU B 142  ? 0.4286 0.4152 0.3186 0.0406  0.0153  -0.0459 140  LEU B CG  
9835  C CD1 A LEU B 142  ? 0.4202 0.4114 0.3078 0.0444  0.0189  -0.0468 140  LEU B CD1 
9836  C CD1 B LEU B 142  ? 0.4844 0.4646 0.3681 0.0382  0.0122  -0.0462 140  LEU B CD1 
9837  C CD2 A LEU B 142  ? 0.4860 0.4666 0.3712 0.0375  0.0120  -0.0458 140  LEU B CD2 
9838  C CD2 B LEU B 142  ? 0.4267 0.4132 0.3114 0.0460  0.0180  -0.0487 140  LEU B CD2 
9839  N N   . PHE B 143  ? 0.3440 0.3410 0.2613 0.0350  0.0144  -0.0403 141  PHE B N   
9840  C CA  . PHE B 143  ? 0.3561 0.3619 0.2794 0.0352  0.0173  -0.0384 141  PHE B CA  
9841  C C   . PHE B 143  ? 0.3560 0.3642 0.2864 0.0310  0.0160  -0.0358 141  PHE B C   
9842  O O   . PHE B 143  ? 0.3220 0.3364 0.2582 0.0309  0.0177  -0.0344 141  PHE B O   
9843  C CB  . PHE B 143  ? 0.3203 0.3264 0.2455 0.0393  0.0186  -0.0402 141  PHE B CB  
9844  C CG  . PHE B 143  ? 0.3216 0.3244 0.2395 0.0438  0.0197  -0.0431 141  PHE B CG  
9845  C CD1 . PHE B 143  ? 0.3092 0.3169 0.2222 0.0456  0.0227  -0.0431 141  PHE B CD1 
9846  C CD2 . PHE B 143  ? 0.3123 0.3066 0.2277 0.0462  0.0177  -0.0458 141  PHE B CD2 
9847  C CE1 . PHE B 143  ? 0.3432 0.3474 0.2488 0.0500  0.0238  -0.0460 141  PHE B CE1 
9848  C CE2 . PHE B 143  ? 0.3288 0.3190 0.2366 0.0505  0.0186  -0.0486 141  PHE B CE2 
9849  C CZ  . PHE B 143  ? 0.3323 0.3274 0.2352 0.0526  0.0217  -0.0488 141  PHE B CZ  
9850  N N   . VAL B 144  ? 0.3529 0.3565 0.2827 0.0277  0.0130  -0.0350 142  VAL B N   
9851  C CA  . VAL B 144  ? 0.3839 0.3889 0.3197 0.0240  0.0117  -0.0327 142  VAL B CA  
9852  C C   . VAL B 144  ? 0.3919 0.4053 0.3306 0.0224  0.0143  -0.0302 142  VAL B C   
9853  O O   . VAL B 144  ? 0.3592 0.3759 0.3040 0.0211  0.0145  -0.0288 142  VAL B O   
9854  C CB  . VAL B 144  ? 0.3901 0.3895 0.3237 0.0212  0.0083  -0.0322 142  VAL B CB  
9855  C CG1 . VAL B 144  ? 0.4424 0.4438 0.3808 0.0176  0.0074  -0.0296 142  VAL B CG1 
9856  C CG2 . VAL B 144  ? 0.4261 0.4181 0.3595 0.0220  0.0053  -0.0342 142  VAL B CG2 
9857  N N   . ASN B 145  ? 0.3671 0.3841 0.3010 0.0225  0.0164  -0.0295 143  ASN B N   
9858  C CA  . ASN B 145  ? 0.3737 0.3987 0.3098 0.0203  0.0187  -0.0268 143  ASN B CA  
9859  C C   . ASN B 145  ? 0.3798 0.4127 0.3170 0.0233  0.0225  -0.0270 143  ASN B C   
9860  O O   . ASN B 145  ? 0.3615 0.4016 0.2982 0.0221  0.0249  -0.0250 143  ASN B O   
9861  C CB  . ASN B 145  ? 0.3875 0.4122 0.3182 0.0178  0.0185  -0.0252 143  ASN B CB  
9862  C CG  . ASN B 145  ? 0.4295 0.4481 0.3604 0.0144  0.0149  -0.0242 143  ASN B CG  
9863  O OD1 . ASN B 145  ? 0.4922 0.5102 0.4287 0.0126  0.0135  -0.0232 143  ASN B OD1 
9864  N ND2 . ASN B 145  ? 0.4479 0.4619 0.3726 0.0137  0.0134  -0.0244 143  ASN B ND2 
9865  N N   . ALA B 146  ? 0.3244 0.3564 0.2631 0.0271  0.0230  -0.0291 144  ALA B N   
9866  C CA  . ALA B 146  ? 0.3342 0.3735 0.2733 0.0306  0.0265  -0.0296 144  ALA B CA  
9867  C C   . ALA B 146  ? 0.3226 0.3709 0.2685 0.0290  0.0282  -0.0271 144  ALA B C   
9868  O O   . ALA B 146  ? 0.3538 0.4104 0.3004 0.0309  0.0314  -0.0265 144  ALA B O   
9869  C CB  . ALA B 146  ? 0.3092 0.3441 0.2478 0.0353  0.0262  -0.0326 144  ALA B CB  
9870  N N   . ALA B 147  ? 0.3326 0.3799 0.2838 0.0256  0.0262  -0.0256 145  ALA B N   
9871  C CA  . ALA B 147  ? 0.3664 0.4220 0.3235 0.0236  0.0277  -0.0232 145  ALA B CA  
9872  C C   . ALA B 147  ? 0.3701 0.4324 0.3255 0.0209  0.0296  -0.0207 145  ALA B C   
9873  O O   . ALA B 147  ? 0.3725 0.4441 0.3306 0.0211  0.0322  -0.0192 145  ALA B O   
9874  C CB  . ALA B 147  ? 0.3882 0.4404 0.3501 0.0204  0.0250  -0.0221 145  ALA B CB  
9875  N N   . THR B 148  ? 0.3720 0.4299 0.3226 0.0183  0.0283  -0.0201 146  THR B N   
9876  C CA  . THR B 148  ? 0.3902 0.4538 0.3385 0.0153  0.0300  -0.0175 146  THR B CA  
9877  C C   . THR B 148  ? 0.3879 0.4582 0.3329 0.0187  0.0336  -0.0181 146  THR B C   
9878  O O   . THR B 148  ? 0.4434 0.5233 0.3904 0.0177  0.0363  -0.0159 146  THR B O   
9879  C CB  . THR B 148  ? 0.4544 0.5108 0.3976 0.0123  0.0276  -0.0169 146  THR B CB  
9880  O OG1 . THR B 148  ? 0.5325 0.5828 0.4789 0.0098  0.0243  -0.0165 146  THR B OG1 
9881  C CG2 . THR B 148  ? 0.5386 0.6004 0.4793 0.0088  0.0291  -0.0139 146  THR B CG2 
9882  N N   . TRP B 149  ? 0.3814 0.4470 0.3214 0.0229  0.0338  -0.0210 147  TRP B N   
9883  C CA  . TRP B 149  ? 0.3891 0.4607 0.3257 0.0268  0.0373  -0.0219 147  TRP B CA  
9884  C C   . TRP B 149  ? 0.3504 0.4298 0.2926 0.0301  0.0397  -0.0222 147  TRP B C   
9885  O O   . TRP B 149  ? 0.4169 0.5054 0.3588 0.0321  0.0432  -0.0215 147  TRP B O   
9886  C CB  . TRP B 149  ? 0.3813 0.4448 0.3107 0.0306  0.0366  -0.0253 147  TRP B CB  
9887  C CG  . TRP B 149  ? 0.3696 0.4262 0.2932 0.0275  0.0344  -0.0249 147  TRP B CG  
9888  C CD1 . TRP B 149  ? 0.3797 0.4259 0.3013 0.0267  0.0306  -0.0263 147  TRP B CD1 
9889  C CD2 . TRP B 149  ? 0.3921 0.4521 0.3112 0.0247  0.0356  -0.0227 147  TRP B CD2 
9890  N NE1 . TRP B 149  ? 0.4102 0.4529 0.3263 0.0238  0.0293  -0.0253 147  TRP B NE1 
9891  C CE2 . TRP B 149  ? 0.4047 0.4554 0.3190 0.0225  0.0324  -0.0230 147  TRP B CE2 
9892  C CE3 . TRP B 149  ? 0.4016 0.4716 0.3203 0.0238  0.0392  -0.0204 147  TRP B CE3 
9893  C CZ2 . TRP B 149  ? 0.4057 0.4566 0.3146 0.0195  0.0325  -0.0211 147  TRP B CZ2 
9894  C CZ3 . TRP B 149  ? 0.4227 0.4929 0.3359 0.0206  0.0394  -0.0185 147  TRP B CZ3 
9895  C CH2 . TRP B 149  ? 0.4285 0.4889 0.3367 0.0186  0.0360  -0.0188 147  TRP B CH2 
9896  N N   . GLY B 150  ? 0.3479 0.4243 0.2953 0.0307  0.0379  -0.0230 148  GLY B N   
9897  C CA  . GLY B 150  ? 0.4085 0.4927 0.3618 0.0333  0.0397  -0.0227 148  GLY B CA  
9898  C C   . GLY B 150  ? 0.3919 0.4873 0.3497 0.0299  0.0417  -0.0193 148  GLY B C   
9899  O O   . GLY B 150  ? 0.4135 0.5187 0.3737 0.0324  0.0447  -0.0187 148  GLY B O   
9900  N N   . LEU B 151  ? 0.4081 0.5023 0.3672 0.0241  0.0399  -0.0168 149  LEU B N   
9901  C CA  . LEU B 151  ? 0.4377 0.5419 0.4004 0.0202  0.0414  -0.0134 149  LEU B CA  
9902  C C   . LEU B 151  ? 0.4204 0.5317 0.3789 0.0205  0.0446  -0.0123 149  LEU B C   
9903  O O   . LEU B 151  ? 0.4354 0.5582 0.3971 0.0203  0.0475  -0.0103 149  LEU B O   
9904  C CB  . LEU B 151  ? 0.4555 0.5552 0.4193 0.0140  0.0385  -0.0112 149  LEU B CB  
9905  C CG  . LEU B 151  ? 0.5130 0.6128 0.4835 0.0123  0.0367  -0.0106 149  LEU B CG  
9906  C CD1 . LEU B 151  ? 0.6306 0.7229 0.6009 0.0074  0.0334  -0.0094 149  LEU B CD1 
9907  C CD2 . LEU B 151  ? 0.5351 0.6472 0.5108 0.0110  0.0389  -0.0081 149  LEU B CD2 
9908  N N   . VAL B 152  ? 0.4359 0.5409 0.3871 0.0209  0.0443  -0.0134 150  VAL B N   
9909  C CA  . VAL B 152  ? 0.4406 0.5517 0.3870 0.0212  0.0474  -0.0124 150  VAL B CA  
9910  C C   . VAL B 152  ? 0.4382 0.5575 0.3851 0.0271  0.0511  -0.0139 150  VAL B C   
9911  O O   . VAL B 152  ? 0.4580 0.5885 0.4056 0.0269  0.0545  -0.0119 150  VAL B O   
9912  C CB  . VAL B 152  ? 0.4366 0.5380 0.3746 0.0210  0.0459  -0.0138 150  VAL B CB  
9913  C CG1 . VAL B 152  ? 0.4863 0.5938 0.4186 0.0221  0.0494  -0.0132 150  VAL B CG1 
9914  C CG2 . VAL B 152  ? 0.4492 0.5438 0.3869 0.0152  0.0425  -0.0119 150  VAL B CG2 
9915  N N   . VAL B 153  ? 0.4052 0.5190 0.3515 0.0325  0.0506  -0.0174 151  VAL B N   
9916  C CA  . VAL B 153  ? 0.4286 0.5483 0.3739 0.0390  0.0539  -0.0193 151  VAL B CA  
9917  C C   . VAL B 153  ? 0.4448 0.5745 0.3983 0.0405  0.0555  -0.0181 151  VAL B C   
9918  O O   . VAL B 153  ? 0.4263 0.5669 0.3809 0.0436  0.0592  -0.0175 151  VAL B O   
9919  C CB  . VAL B 153  ? 0.4210 0.5294 0.3612 0.0441  0.0525  -0.0235 151  VAL B CB  
9920  C CG1 . VAL B 153  ? 0.3960 0.5094 0.3352 0.0513  0.0557  -0.0257 151  VAL B CG1 
9921  C CG2 . VAL B 153  ? 0.3846 0.4841 0.3163 0.0428  0.0511  -0.0246 151  VAL B CG2 
9922  N N   . THR B 154  ? 0.3811 0.5079 0.3404 0.0386  0.0528  -0.0177 152  THR B N   
9923  C CA  . THR B 154  ? 0.4273 0.5623 0.3940 0.0405  0.0537  -0.0170 152  THR B CA  
9924  C C   . THR B 154  ? 0.4072 0.5498 0.3805 0.0346  0.0532  -0.0132 152  THR B C   
9925  O O   . THR B 154  ? 0.4844 0.6368 0.4638 0.0357  0.0546  -0.0119 152  THR B O   
9926  C CB  . THR B 154  ? 0.4415 0.5677 0.4099 0.0437  0.0512  -0.0196 152  THR B CB  
9927  O OG1 . THR B 154  ? 0.3883 0.5081 0.3595 0.0386  0.0477  -0.0186 152  THR B OG1 
9928  C CG2 . THR B 154  ? 0.4473 0.5628 0.4084 0.0481  0.0506  -0.0233 152  THR B CG2 
9929  N N   . GLY B 155  ? 0.4130 0.5510 0.3851 0.0284  0.0510  -0.0114 153  GLY B N   
9930  C CA  . GLY B 155  ? 0.4381 0.5810 0.4159 0.0226  0.0499  -0.0081 153  GLY B CA  
9931  C C   . GLY B 155  ? 0.4817 0.6191 0.4641 0.0217  0.0468  -0.0087 153  GLY B C   
9932  O O   . GLY B 155  ? 0.5205 0.6610 0.5073 0.0169  0.0455  -0.0062 153  GLY B O   
9933  N N   . LYS B 156  ? 0.4436 0.5729 0.4250 0.0261  0.0455  -0.0119 154  LYS B N   
9934  C CA  . LYS B 156  ? 0.4415 0.5653 0.4269 0.0257  0.0427  -0.0125 154  LYS B CA  
9935  C C   . LYS B 156  ? 0.4281 0.5385 0.4096 0.0244  0.0396  -0.0142 154  LYS B C   
9936  O O   . LYS B 156  ? 0.4383 0.5427 0.4139 0.0263  0.0397  -0.0160 154  LYS B O   
9937  C CB  . LYS B 156  ? 0.4768 0.6024 0.4648 0.0317  0.0436  -0.0145 154  LYS B CB  
9938  N N   . LEU B 157  ? 0.4219 0.5278 0.4066 0.0212  0.0369  -0.0136 155  LEU B N   
9939  C CA  . LEU B 157  ? 0.4506 0.5448 0.4327 0.0199  0.0339  -0.0150 155  LEU B CA  
9940  C C   . LEU B 157  ? 0.4843 0.5732 0.4687 0.0231  0.0324  -0.0171 155  LEU B C   
9941  O O   . LEU B 157  ? 0.4653 0.5578 0.4548 0.0231  0.0322  -0.0164 155  LEU B O   
9942  C CB  . LEU B 157  ? 0.4680 0.5603 0.4516 0.0139  0.0318  -0.0128 155  LEU B CB  
9943  C CG  . LEU B 157  ? 0.4873 0.5683 0.4695 0.0128  0.0285  -0.0141 155  LEU B CG  
9944  C CD1 . LEU B 157  ? 0.4868 0.5612 0.4627 0.0134  0.0280  -0.0153 155  LEU B CD1 
9945  C CD2 . LEU B 157  ? 0.5187 0.5981 0.5031 0.0077  0.0265  -0.0120 155  LEU B CD2 
9946  N N   . THR B 158  ? 0.4707 0.5509 0.4510 0.0258  0.0314  -0.0197 156  THR B N   
9947  C CA  . THR B 158  ? 0.4772 0.5506 0.4590 0.0280  0.0295  -0.0216 156  THR B CA  
9948  C C   . THR B 158  ? 0.4339 0.4982 0.4143 0.0248  0.0265  -0.0218 156  THR B C   
9949  O O   . THR B 158  ? 0.4544 0.5154 0.4307 0.0230  0.0259  -0.0217 156  THR B O   
9950  C CB  . THR B 158  ? 0.5101 0.5804 0.4885 0.0335  0.0304  -0.0243 156  THR B CB  
9951  O OG1 . THR B 158  ? 0.5678 0.6470 0.5465 0.0367  0.0335  -0.0240 156  THR B OG1 
9952  C CG2 . THR B 158  ? 0.5160 0.5810 0.4967 0.0358  0.0287  -0.0257 156  THR B CG2 
9953  N N   . SER B 159  ? 0.3679 0.4286 0.3519 0.0242  0.0246  -0.0220 157  SER B N   
9954  C CA  . SER B 159  ? 0.3761 0.4296 0.3599 0.0211  0.0219  -0.0220 157  SER B CA  
9955  C C   . SER B 159  ? 0.3906 0.4355 0.3700 0.0227  0.0204  -0.0241 157  SER B C   
9956  O O   . SER B 159  ? 0.3972 0.4373 0.3742 0.0204  0.0187  -0.0240 157  SER B O   
9957  C CB  . SER B 159  ? 0.3837 0.4362 0.3724 0.0202  0.0205  -0.0216 157  SER B CB  
9958  O OG  . SER B 159  ? 0.4317 0.4769 0.4201 0.0182  0.0180  -0.0219 157  SER B OG  
9959  N N   . THR B 160  ? 0.3708 0.4136 0.3492 0.0267  0.0207  -0.0261 158  THR B N   
9960  C CA  . THR B 160  ? 0.3066 0.3413 0.2805 0.0284  0.0193  -0.0283 158  THR B CA  
9961  C C   . THR B 160  ? 0.3055 0.3414 0.2749 0.0323  0.0213  -0.0298 158  THR B C   
9962  O O   . THR B 160  ? 0.3604 0.4038 0.3308 0.0341  0.0238  -0.0292 158  THR B O   
9963  C CB  . THR B 160  ? 0.3149 0.3438 0.2911 0.0293  0.0173  -0.0294 158  THR B CB  
9964  O OG1 . THR B 160  ? 0.3613 0.3939 0.3402 0.0323  0.0188  -0.0297 158  THR B OG1 
9965  C CG2 . THR B 160  ? 0.3421 0.3699 0.3224 0.0256  0.0155  -0.0280 158  THR B CG2 
9966  N N   . VAL B 161  ? 0.2248 0.2534 0.1892 0.0337  0.0199  -0.0318 159  VAL B N   
9967  C CA  . VAL B 161  ? 0.2697 0.2977 0.2282 0.0372  0.0214  -0.0336 159  VAL B CA  
9968  C C   . VAL B 161  ? 0.2664 0.2891 0.2237 0.0412  0.0209  -0.0360 159  VAL B C   
9969  O O   . VAL B 161  ? 0.2792 0.2947 0.2369 0.0404  0.0183  -0.0368 159  VAL B O   
9970  C CB  . VAL B 161  ? 0.2953 0.3181 0.2481 0.0354  0.0200  -0.0342 159  VAL B CB  
9971  C CG1 . VAL B 161  ? 0.3511 0.3712 0.2970 0.0391  0.0211  -0.0365 159  VAL B CG1 
9972  C CG2 . VAL B 161  ? 0.3739 0.4019 0.3273 0.0316  0.0207  -0.0317 159  VAL B CG2 
9973  N N   . ASN B 162  ? 0.2540 0.2802 0.2097 0.0456  0.0234  -0.0370 160  ASN B N   
9974  C CA  . ASN B 162  ? 0.2506 0.2704 0.2034 0.0499  0.0228  -0.0396 160  ASN B CA  
9975  C C   . ASN B 162  ? 0.2334 0.2468 0.1781 0.0512  0.0222  -0.0418 160  ASN B C   
9976  O O   . ASN B 162  ? 0.2491 0.2651 0.1893 0.0545  0.0245  -0.0429 160  ASN B O   
9977  C CB  . ASN B 162  ? 0.2574 0.2830 0.2119 0.0545  0.0254  -0.0398 160  ASN B CB  
9978  C CG  . ASN B 162  ? 0.2465 0.2643 0.1976 0.0590  0.0245  -0.0424 160  ASN B CG  
9979  O OD1 . ASN B 162  ? 0.2617 0.2702 0.2077 0.0590  0.0223  -0.0444 160  ASN B OD1 
9980  N ND2 . ASN B 162  ? 0.2736 0.2949 0.2276 0.0626  0.0258  -0.0424 160  ASN B ND2 
9981  N N   . ASP B 163  ? 0.2508 0.2559 0.1936 0.0485  0.0190  -0.0425 161  ASP B N   
9982  C CA  . ASP B 163  ? 0.2522 0.2508 0.1874 0.0489  0.0178  -0.0444 161  ASP B CA  
9983  C C   . ASP B 163  ? 0.2539 0.2460 0.1834 0.0538  0.0178  -0.0474 161  ASP B C   
9984  O O   . ASP B 163  ? 0.2616 0.2503 0.1838 0.0554  0.0180  -0.0492 161  ASP B O   
9985  C CB  . ASP B 163  ? 0.2511 0.2432 0.1863 0.0446  0.0142  -0.0441 161  ASP B CB  
9986  C CG  . ASP B 163  ? 0.2913 0.2788 0.2310 0.0435  0.0117  -0.0440 161  ASP B CG  
9987  O OD1 . ASP B 163  ? 0.2557 0.2474 0.2013 0.0437  0.0127  -0.0428 161  ASP B OD1 
9988  O OD2 . ASP B 163  ? 0.3082 0.2877 0.2455 0.0421  0.0087  -0.0451 161  ASP B OD2 
9989  N N   . ARG B 164  ? 0.2475 0.2375 0.1796 0.0561  0.0175  -0.0480 162  ARG B N   
9990  C CA  . ARG B 164  ? 0.2378 0.2215 0.1639 0.0612  0.0176  -0.0509 162  ARG B CA  
9991  C C   . ARG B 164  ? 0.2252 0.2159 0.1490 0.0659  0.0216  -0.0515 162  ARG B C   
9992  O O   . ARG B 164  ? 0.2320 0.2184 0.1483 0.0696  0.0222  -0.0541 162  ARG B O   
9993  C CB  . ARG B 164  ? 0.2466 0.2259 0.1759 0.0625  0.0162  -0.0513 162  ARG B CB  
9994  C CG  . ARG B 164  ? 0.2579 0.2298 0.1890 0.0582  0.0123  -0.0509 162  ARG B CG  
9995  C CD  . ARG B 164  ? 0.3279 0.2922 0.2525 0.0563  0.0099  -0.0525 162  ARG B CD  
9996  N NE  . ARG B 164  ? 0.4005 0.3582 0.3167 0.0606  0.0100  -0.0555 162  ARG B NE  
9997  C CZ  . ARG B 164  ? 0.4454 0.3977 0.3543 0.0603  0.0088  -0.0573 162  ARG B CZ  
9998  N NH1 . ARG B 164  ? 0.4321 0.3853 0.3413 0.0559  0.0074  -0.0561 162  ARG B NH1 
9999  N NH2 . ARG B 164  ? 0.4187 0.3643 0.3196 0.0645  0.0088  -0.0603 162  ARG B NH2 
10000 N N   . SER B 165  ? 0.2363 0.2378 0.1663 0.0659  0.0242  -0.0492 163  SER B N   
10001 C CA  . SER B 165  ? 0.2348 0.2448 0.1636 0.0699  0.0281  -0.0493 163  SER B CA  
10002 C C   . SER B 165  ? 0.2251 0.2369 0.1482 0.0690  0.0294  -0.0496 163  SER B C   
10003 O O   . SER B 165  ? 0.2275 0.2403 0.1450 0.0734  0.0317  -0.0514 163  SER B O   
10004 C CB  . SER B 165  ? 0.2323 0.2540 0.1696 0.0688  0.0302  -0.0463 163  SER B CB  
10005 O OG  . SER B 165  ? 0.2534 0.2848 0.1901 0.0717  0.0340  -0.0459 163  SER B OG  
10006 N N   . LEU B 166  ? 0.2600 0.2724 0.1846 0.0634  0.0280  -0.0478 164  LEU B N   
10007 C CA  . LEU B 166  ? 0.2513 0.2652 0.1705 0.0620  0.0289  -0.0476 164  LEU B CA  
10008 C C   . LEU B 166  ? 0.2638 0.2673 0.1738 0.0640  0.0273  -0.0508 164  LEU B C   
10009 O O   . LEU B 166  ? 0.2608 0.2656 0.1643 0.0662  0.0292  -0.0519 164  LEU B O   
10010 C CB  . LEU B 166  ? 0.2590 0.2747 0.1819 0.0557  0.0273  -0.0449 164  LEU B CB  
10011 C CG  . LEU B 166  ? 0.2509 0.2779 0.1812 0.0536  0.0295  -0.0417 164  LEU B CG  
10012 C CD1 . LEU B 166  ? 0.2905 0.3178 0.2238 0.0477  0.0276  -0.0393 164  LEU B CD1 
10013 C CD2 . LEU B 166  ? 0.2706 0.3068 0.1986 0.0560  0.0335  -0.0412 164  LEU B CD2 
10014 N N   . ALA B 167  ? 0.2662 0.2593 0.1752 0.0630  0.0236  -0.0522 165  ALA B N   
10015 C CA  . ALA B 167  ? 0.2643 0.2469 0.1643 0.0647  0.0216  -0.0553 165  ALA B CA  
10016 C C   . ALA B 167  ? 0.2833 0.2645 0.1777 0.0714  0.0239  -0.0581 165  ALA B C   
10017 O O   . ALA B 167  ? 0.3067 0.2844 0.1926 0.0737  0.0245  -0.0603 165  ALA B O   
10018 C CB  . ALA B 167  ? 0.3138 0.2863 0.2147 0.0622  0.0171  -0.0561 165  ALA B CB  
10019 N N   . ALA B 168  ? 0.2701 0.2540 0.1690 0.0746  0.0252  -0.0581 166  ALA B N   
10020 C CA  . ALA B 168  ? 0.2774 0.2608 0.1717 0.0815  0.0276  -0.0605 166  ALA B CA  
10021 C C   . ALA B 168  ? 0.2584 0.2516 0.1502 0.0839  0.0319  -0.0602 166  ALA B C   
10022 O O   . ALA B 168  ? 0.2806 0.2711 0.1645 0.0885  0.0334  -0.0628 166  ALA B O   
10023 C CB  . ALA B 168  ? 0.2641 0.2502 0.1648 0.0842  0.0282  -0.0599 166  ALA B CB  
10024 N N   . ALA B 169  ? 0.2613 0.2661 0.1599 0.0807  0.0339  -0.0568 167  ALA B N   
10025 C CA  . ALA B 169  ? 0.2602 0.2757 0.1575 0.0825  0.0381  -0.0559 167  ALA B CA  
10026 C C   . ALA B 169  ? 0.2813 0.2931 0.1700 0.0811  0.0380  -0.0570 167  ALA B C   
10027 O O   . ALA B 169  ? 0.2875 0.3028 0.1705 0.0850  0.0411  -0.0582 167  ALA B O   
10028 C CB  . ALA B 169  ? 0.2661 0.2939 0.1726 0.0784  0.0397  -0.0519 167  ALA B CB  
10029 N N   . LEU B 170  ? 0.2794 0.2845 0.1672 0.0758  0.0344  -0.0564 168  LEU B N   
10030 C CA  . LEU B 170  ? 0.2800 0.2815 0.1596 0.0744  0.0339  -0.0573 168  LEU B CA  
10031 C C   . LEU B 170  ? 0.2998 0.2910 0.1692 0.0792  0.0331  -0.0615 168  LEU B C   
10032 O O   . LEU B 170  ? 0.2864 0.2782 0.1480 0.0816  0.0351  -0.0629 168  LEU B O   
10033 C CB  . LEU B 170  ? 0.2890 0.2856 0.1703 0.0678  0.0299  -0.0557 168  LEU B CB  
10034 C CG  . LEU B 170  ? 0.2981 0.2919 0.1718 0.0654  0.0291  -0.0558 168  LEU B CG  
10035 C CD1 . LEU B 170  ? 0.3157 0.3205 0.1887 0.0655  0.0333  -0.0539 168  LEU B CD1 
10036 C CD2 . LEU B 170  ? 0.3571 0.3470 0.2341 0.0593  0.0251  -0.0540 168  LEU B CD2 
10037 N N   . THR B 171  ? 0.2899 0.2714 0.1590 0.0805  0.0301  -0.0636 169  THR B N   
10038 C CA  . THR B 171  ? 0.3037 0.2749 0.1632 0.0854  0.0294  -0.0677 169  THR B CA  
10039 C C   . THR B 171  ? 0.3282 0.3053 0.1848 0.0920  0.0339  -0.0690 169  THR B C   
10040 O O   . THR B 171  ? 0.3200 0.2940 0.1695 0.0939  0.0346  -0.0705 169  THR B O   
10041 C CB  . THR B 171  ? 0.3110 0.2718 0.1718 0.0857  0.0257  -0.0692 169  THR B CB  
10042 O OG1 . THR B 171  ? 0.3601 0.3158 0.2237 0.0793  0.0214  -0.0678 169  THR B OG1 
10043 C CG2 . THR B 171  ? 0.3441 0.2933 0.1946 0.0905  0.0246  -0.0734 169  THR B CG2 
10044 N N   . ARG B 172  ? 0.3208 0.3075 0.1856 0.0939  0.0366  -0.0671 170  ARG B N   
10045 C CA  . ARG B 172  ? 0.3039 0.2971 0.1697 0.0985  0.0401  -0.0669 170  ARG B CA  
10046 C C   . ARG B 172  ? 0.2993 0.3010 0.1620 0.0982  0.0435  -0.0658 170  ARG B C   
10047 O O   . ARG B 172  ? 0.3256 0.3261 0.1829 0.1015  0.0450  -0.0673 170  ARG B O   
10048 C CB  . ARG B 172  ? 0.2977 0.3002 0.1734 0.1000  0.0419  -0.0647 170  ARG B CB  
10049 C CG  . ARG B 172  ? 0.2914 0.2991 0.1684 0.1052  0.0448  -0.0647 170  ARG B CG  
10050 C CD  . ARG B 172  ? 0.3079 0.3260 0.1951 0.1062  0.0465  -0.0622 170  ARG B CD  
10051 N NE  . ARG B 172  ? 0.2753 0.2885 0.1670 0.1044  0.0436  -0.0620 170  ARG B NE  
10052 C CZ  . ARG B 172  ? 0.2642 0.2831 0.1619 0.1004  0.0434  -0.0599 170  ARG B CZ  
10053 N NH1 . ARG B 172  ? 0.2793 0.3085 0.1790 0.0974  0.0457  -0.0577 170  ARG B NH1 
10054 N NH2 . ARG B 172  ? 0.2667 0.2805 0.1680 0.0993  0.0407  -0.0599 170  ARG B NH2 
10055 N N   . LEU B 173  ? 0.3034 0.3136 0.1691 0.0942  0.0448  -0.0633 171  LEU B N   
10056 C CA  . LEU B 173  ? 0.3128 0.3322 0.1763 0.0936  0.0482  -0.0618 171  LEU B CA  
10057 C C   . LEU B 173  ? 0.3120 0.3227 0.1647 0.0931  0.0469  -0.0639 171  LEU B C   
10058 O O   . LEU B 173  ? 0.3148 0.3293 0.1635 0.0951  0.0496  -0.0641 171  LEU B O   
10059 C CB  . LEU B 173  ? 0.2979 0.3281 0.1669 0.0891  0.0496  -0.0583 171  LEU B CB  
10060 C CG  . LEU B 173  ? 0.3285 0.3539 0.1975 0.0820  0.0461  -0.0567 171  LEU B CG  
10061 C CD1 . LEU B 173  ? 0.3393 0.3660 0.2008 0.0802  0.0472  -0.0563 171  LEU B CD1 
10062 C CD2 . LEU B 173  ? 0.3712 0.4048 0.2513 0.0769  0.0458  -0.0526 171  LEU B CD2 
10063 N N   . ILE B 174  ? 0.3276 0.3270 0.1756 0.0905  0.0427  -0.0656 172  ILE B N   
10064 C CA  . ILE B 174  ? 0.3303 0.3213 0.1680 0.0898  0.0411  -0.0675 172  ILE B CA  
10065 C C   . ILE B 174  ? 0.3372 0.3204 0.1696 0.0944  0.0408  -0.0706 172  ILE B C   
10066 O O   . ILE B 174  ? 0.3630 0.3454 0.1884 0.0958  0.0422  -0.0716 172  ILE B O   
10067 C CB  . ILE B 174  ? 0.3122 0.2931 0.1467 0.0855  0.0362  -0.0684 172  ILE B CB  
10068 C CG1 . ILE B 174  ? 0.3424 0.3313 0.1849 0.0788  0.0358  -0.0639 172  ILE B CG1 
10069 C CG2 . ILE B 174  ? 0.4027 0.3739 0.2264 0.0849  0.0340  -0.0706 172  ILE B CG2 
10070 C CD1 . ILE B 174  ? 0.3684 0.3490 0.2128 0.0731  0.0305  -0.0631 172  ILE B CD1 
10071 N N   . SER B 175  ? 0.3331 0.3099 0.1682 0.0967  0.0388  -0.0720 173  SER B N   
10072 C CA  . SER B 175  ? 0.3427 0.3117 0.1724 0.1012  0.0384  -0.0748 173  SER B CA  
10073 C C   . SER B 175  ? 0.3417 0.3204 0.1725 0.1057  0.0432  -0.0742 173  SER B C   
10074 O O   . SER B 175  ? 0.3865 0.3605 0.2106 0.1091  0.0437  -0.0764 173  SER B O   
10075 C CB  . SER B 175  ? 0.3869 0.3476 0.2197 0.1026  0.0355  -0.0760 173  SER B CB  
10076 O OG  . SER B 175  ? 0.4297 0.3799 0.2603 0.0986  0.0307  -0.0769 173  SER B OG  
10077 N N   . ARG B 176  ? 0.3364 0.3288 0.1755 0.1056  0.0467  -0.0713 174  ARG B N   
10078 C CA  . ARG B 176  ? 0.3356 0.3385 0.1767 0.1095  0.0512  -0.0703 174  ARG B CA  
10079 C C   . ARG B 176  ? 0.3394 0.3490 0.1761 0.1081  0.0540  -0.0694 174  ARG B C   
10080 O O   . ARG B 176  ? 0.3490 0.3602 0.1813 0.1118  0.0565  -0.0705 174  ARG B O   
10081 C CB  . ARG B 176  ? 0.3243 0.3393 0.1767 0.1098  0.0534  -0.0674 174  ARG B CB  
10082 C CG  . ARG B 176  ? 0.3293 0.3557 0.1852 0.1141  0.0577  -0.0662 174  ARG B CG  
10083 C CD  . ARG B 176  ? 0.3212 0.3585 0.1885 0.1140  0.0590  -0.0633 174  ARG B CD  
10084 N NE  . ARG B 176  ? 0.3455 0.3939 0.2184 0.1090  0.0606  -0.0599 174  ARG B NE  
10085 C CZ  . ARG B 176  ? 0.3829 0.4322 0.2612 0.1050  0.0588  -0.0582 174  ARG B CZ  
10086 N NH1 . ARG B 176  ? 0.3361 0.3767 0.2161 0.1052  0.0555  -0.0595 174  ARG B NH1 
10087 N NH2 . ARG B 176  ? 0.3733 0.4327 0.2555 0.1005  0.0604  -0.0551 174  ARG B NH2 
10088 N N   . CYS B 177  ? 0.3504 0.3637 0.1877 0.1029  0.0538  -0.0673 175  CYS B N   
10089 C CA  . CYS B 177  ? 0.3524 0.3743 0.1870 0.1011  0.0569  -0.0655 175  CYS B CA  
10090 C C   . CYS B 177  ? 0.3951 0.4091 0.2206 0.0976  0.0546  -0.0665 175  CYS B C   
10091 O O   . CYS B 177  ? 0.4105 0.4294 0.2316 0.0968  0.0571  -0.0656 175  CYS B O   
10092 C CB  . CYS B 177  ? 0.3732 0.4090 0.2168 0.0976  0.0593  -0.0613 175  CYS B CB  
10093 S SG  . CYS B 177  ? 0.4290 0.4762 0.2841 0.1012  0.0622  -0.0595 175  CYS B SG  
10094 N N   . GLY B 178  ? 0.3915 0.3937 0.2140 0.0955  0.0500  -0.0682 176  GLY B N   
10095 C CA  . GLY B 178  ? 0.4266 0.4200 0.2394 0.0931  0.0474  -0.0696 176  GLY B CA  
10096 C C   . GLY B 178  ? 0.4493 0.4488 0.2613 0.0880  0.0480  -0.0668 176  GLY B C   
10097 O O   . GLY B 178  ? 0.4294 0.4378 0.2486 0.0854  0.0492  -0.0637 176  GLY B O   
10098 N N   . GLU B 179  ? 0.4546 0.4490 0.2573 0.0866  0.0470  -0.0677 177  GLU B N   
10099 C CA  . GLU B 179  ? 0.4832 0.4817 0.2837 0.0817  0.0470  -0.0650 177  GLU B CA  
10100 C C   . GLU B 179  ? 0.4266 0.4404 0.2323 0.0807  0.0519  -0.0612 177  GLU B C   
10101 O O   . GLU B 179  ? 0.4237 0.4426 0.2323 0.0764  0.0517  -0.0582 177  GLU B O   
10102 C CB  . GLU B 179  ? 0.5562 0.5467 0.3454 0.0808  0.0452  -0.0667 177  GLU B CB  
10103 C CG  . GLU B 179  ? 0.5868 0.5818 0.3730 0.0760  0.0455  -0.0637 177  GLU B CG  
10104 C CD  . GLU B 179  ? 0.7108 0.6992 0.4859 0.0752  0.0442  -0.0650 177  GLU B CD  
10105 O OE1 . GLU B 179  ? 0.7740 0.7507 0.5434 0.0767  0.0408  -0.0685 177  GLU B OE1 
10106 O OE2 . GLU B 179  ? 0.7873 0.7822 0.5592 0.0730  0.0465  -0.0626 177  GLU B OE2 
10107 N N   . PRO B 180  ? 0.4108 0.4325 0.2178 0.0842  0.0563  -0.0610 178  PRO B N   
10108 C CA  . PRO B 180  ? 0.4155 0.4521 0.2276 0.0824  0.0608  -0.0570 178  PRO B CA  
10109 C C   . PRO B 180  ? 0.4735 0.5182 0.2961 0.0799  0.0611  -0.0540 178  PRO B C   
10110 O O   . PRO B 180  ? 0.4332 0.4871 0.2586 0.0758  0.0628  -0.0503 178  PRO B O   
10111 C CB  . PRO B 180  ? 0.4541 0.4963 0.2667 0.0875  0.0648  -0.0580 178  PRO B CB  
10112 C CG  . PRO B 180  ? 0.4542 0.4838 0.2572 0.0907  0.0627  -0.0622 178  PRO B CG  
10113 C CD  . PRO B 180  ? 0.4411 0.4584 0.2436 0.0896  0.0574  -0.0642 178  PRO B CD  
10114 N N   . VAL B 181  ? 0.3881 0.4296 0.2166 0.0820  0.0594  -0.0554 179  VAL B N   
10115 C CA  . VAL B 181  ? 0.3990 0.4484 0.2374 0.0795  0.0596  -0.0525 179  VAL B CA  
10116 C C   . VAL B 181  ? 0.4012 0.4454 0.2386 0.0743  0.0559  -0.0514 179  VAL B C   
10117 O O   . VAL B 181  ? 0.4040 0.4554 0.2495 0.0692  0.0558  -0.0475 179  VAL B O   
10118 C CB  . VAL B 181  ? 0.4262 0.4749 0.2719 0.0832  0.0592  -0.0539 179  VAL B CB  
10119 C CG1 . VAL B 181  ? 0.4150 0.4493 0.2577 0.0839  0.0544  -0.0571 179  VAL B CG1 
10120 C CG2 . VAL B 181  ? 0.4194 0.4794 0.2759 0.0808  0.0606  -0.0504 179  VAL B CG2 
10121 N N   . ILE B 182  ? 0.4105 0.4413 0.2413 0.0735  0.0516  -0.0540 180  ILE B N   
10122 C CA  . ILE B 182  ? 0.4241 0.4489 0.2571 0.0669  0.0469  -0.0520 180  ILE B CA  
10123 C C   . ILE B 182  ? 0.4290 0.4594 0.2594 0.0623  0.0481  -0.0486 180  ILE B C   
10124 O O   . ILE B 182  ? 0.4105 0.4441 0.2473 0.0566  0.0467  -0.0449 180  ILE B O   
10125 C CB  . ILE B 182  ? 0.4102 0.4199 0.2364 0.0672  0.0421  -0.0554 180  ILE B CB  
10126 C CG1 . ILE B 182  ? 0.3952 0.3990 0.2245 0.0711  0.0406  -0.0584 180  ILE B CG1 
10127 C CG2 . ILE B 182  ? 0.4138 0.4184 0.2425 0.0605  0.0374  -0.0532 180  ILE B CG2 
10128 C CD1 . ILE B 182  ? 0.4426 0.4319 0.2637 0.0723  0.0365  -0.0622 180  ILE B CD1 
10129 N N   . ARG B 183  ? 0.4279 0.4594 0.2486 0.0647  0.0506  -0.0497 181  ARG B N   
10130 C CA  . ARG B 183  ? 0.4619 0.4988 0.2793 0.0606  0.0520  -0.0464 181  ARG B CA  
10131 C C   . ARG B 183  ? 0.4558 0.5068 0.2820 0.0579  0.0555  -0.0420 181  ARG B C   
10132 O O   . ARG B 183  ? 0.4716 0.5251 0.3008 0.0518  0.0543  -0.0382 181  ARG B O   
10133 C CB  . ARG B 183  ? 0.5007 0.5368 0.3057 0.0646  0.0548  -0.0488 181  ARG B CB  
10134 C CG  . ARG B 183  ? 0.5826 0.6275 0.3840 0.0618  0.0580  -0.0454 181  ARG B CG  
10135 C CD  . ARG B 183  ? 0.6053 0.6480 0.4074 0.0544  0.0547  -0.0417 181  ARG B CD  
10136 N NE  . ARG B 183  ? 0.6213 0.6501 0.4202 0.0526  0.0487  -0.0436 181  ARG B NE  
10137 C CZ  . ARG B 183  ? 0.6042 0.6293 0.4073 0.0467  0.0446  -0.0409 181  ARG B CZ  
10138 N NH1 . ARG B 183  ? 0.5643 0.5972 0.3744 0.0420  0.0456  -0.0364 181  ARG B NH1 
10139 N NH2 . ARG B 183  ? 0.6679 0.6809 0.4679 0.0456  0.0394  -0.0429 181  ARG B NH2 
10140 N N   . ARG B 184  ? 0.4509 0.5110 0.2817 0.0622  0.0596  -0.0424 182  ARG B N   
10141 C CA  . ARG B 184  ? 0.4617 0.5358 0.3014 0.0596  0.0628  -0.0383 182  ARG B CA  
10142 C C   . ARG B 184  ? 0.4704 0.5435 0.3203 0.0544  0.0593  -0.0357 182  ARG B C   
10143 O O   . ARG B 184  ? 0.4520 0.5326 0.3071 0.0493  0.0600  -0.0315 182  ARG B O   
10144 C CB  . ARG B 184  ? 0.4685 0.5515 0.3123 0.0652  0.0671  -0.0392 182  ARG B CB  
10145 C CG  . ARG B 184  ? 0.5368 0.6237 0.3757 0.0674  0.0706  -0.0393 182  ARG B CG  
10146 C CD  . ARG B 184  ? 0.5590 0.6602 0.4025 0.0637  0.0744  -0.0346 182  ARG B CD  
10147 N NE  . ARG B 184  ? 0.5482 0.6602 0.4021 0.0657  0.0771  -0.0332 182  ARG B NE  
10148 C CZ  . ARG B 184  ? 0.5494 0.6710 0.4123 0.0619  0.0777  -0.0295 182  ARG B CZ  
10149 N NH1 . ARG B 184  ? 0.5285 0.6506 0.3916 0.0558  0.0760  -0.0266 182  ARG B NH1 
10150 N NH2 . ARG B 184  ? 0.4858 0.6166 0.3577 0.0641  0.0798  -0.0286 182  ARG B NH2 
10151 N N   . GLY B 185  ? 0.4242 0.4880 0.2770 0.0556  0.0557  -0.0382 183  GLY B N   
10152 C CA  . GLY B 185  ? 0.4189 0.4815 0.2809 0.0509  0.0525  -0.0360 183  GLY B CA  
10153 C C   . GLY B 185  ? 0.4387 0.4960 0.2990 0.0446  0.0490  -0.0336 183  GLY B C   
10154 O O   . GLY B 185  ? 0.4294 0.4908 0.2963 0.0396  0.0482  -0.0301 183  GLY B O   
10155 N N   . VAL B 186  ? 0.3926 0.4405 0.2439 0.0447  0.0467  -0.0355 184  VAL B N   
10156 C CA  . VAL B 186  ? 0.4288 0.4714 0.2777 0.0391  0.0432  -0.0333 184  VAL B CA  
10157 C C   . VAL B 186  ? 0.4714 0.5232 0.3198 0.0353  0.0460  -0.0291 184  VAL B C   
10158 O O   . VAL B 186  ? 0.4742 0.5264 0.3266 0.0298  0.0440  -0.0257 184  VAL B O   
10159 C CB  . VAL B 186  ? 0.4568 0.4884 0.2952 0.0406  0.0406  -0.0363 184  VAL B CB  
10160 C CG1 . VAL B 186  ? 0.4931 0.5210 0.3276 0.0352  0.0378  -0.0337 184  VAL B CG1 
10161 C CG2 . VAL B 186  ? 0.4307 0.4521 0.2705 0.0427  0.0368  -0.0398 184  VAL B CG2 
10162 N N   . ASP B 187  ? 0.4709 0.5300 0.3142 0.0380  0.0505  -0.0292 185  ASP B N   
10163 C CA  . ASP B 187  ? 0.4866 0.5550 0.3292 0.0342  0.0534  -0.0250 185  ASP B CA  
10164 C C   . ASP B 187  ? 0.5341 0.6123 0.3876 0.0311  0.0547  -0.0215 185  ASP B C   
10165 O O   . ASP B 187  ? 0.4863 0.5672 0.3417 0.0253  0.0540  -0.0175 185  ASP B O   
10166 C CB  . ASP B 187  ? 0.4922 0.5675 0.3276 0.0384  0.0583  -0.0260 185  ASP B CB  
10167 C CG  . ASP B 187  ? 0.5401 0.6057 0.3635 0.0408  0.0570  -0.0292 185  ASP B CG  
10168 O OD1 . ASP B 187  ? 0.5610 0.6159 0.3815 0.0380  0.0522  -0.0296 185  ASP B OD1 
10169 O OD2 . ASP B 187  ? 0.5698 0.6387 0.3867 0.0456  0.0606  -0.0313 185  ASP B OD2 
10170 N N   . MET B 188  ? 0.5179 0.6008 0.3781 0.0348  0.0564  -0.0230 186  MET B N   
10171 C CA  . MET B 188  ? 0.5026 0.5943 0.3733 0.0320  0.0573  -0.0200 186  MET B CA  
10172 C C   . MET B 188  ? 0.5351 0.6201 0.4110 0.0267  0.0526  -0.0183 186  MET B C   
10173 O O   . MET B 188  ? 0.5655 0.6556 0.4461 0.0215  0.0525  -0.0144 186  MET B O   
10174 C CB  . MET B 188  ? 0.5130 0.6094 0.3892 0.0376  0.0594  -0.0223 186  MET B CB  
10175 C CG  . MET B 188  ? 0.5609 0.6672 0.4478 0.0353  0.0606  -0.0194 186  MET B CG  
10176 S SD  . MET B 188  ? 0.7084 0.8306 0.5962 0.0321  0.0654  -0.0148 186  MET B SD  
10177 C CE  . MET B 188  ? 0.6091 0.7352 0.4880 0.0391  0.0701  -0.0177 186  MET B CE  
10178 N N   . ALA B 189  ? 0.5045 0.5780 0.3796 0.0280  0.0486  -0.0211 187  ALA B N   
10179 C CA  . ALA B 189  ? 0.5377 0.6047 0.4175 0.0235  0.0442  -0.0198 187  ALA B CA  
10180 C C   . ALA B 189  ? 0.6057 0.6700 0.4813 0.0180  0.0424  -0.0167 187  ALA B C   
10181 O O   . ALA B 189  ? 0.5890 0.6536 0.4694 0.0132  0.0406  -0.0137 187  ALA B O   
10182 C CB  . ALA B 189  ? 0.4682 0.5239 0.3475 0.0260  0.0405  -0.0234 187  ALA B CB  
10183 N N   . MET B 190  ? 0.5447 0.6058 0.4108 0.0189  0.0428  -0.0175 188  MET B N   
10184 C CA  . MET B 190  ? 0.6150 0.6733 0.4763 0.0140  0.0411  -0.0145 188  MET B CA  
10185 C C   . MET B 190  ? 0.5932 0.6615 0.4577 0.0096  0.0437  -0.0100 188  MET B C   
10186 O O   . MET B 190  ? 0.6202 0.6862 0.4864 0.0043  0.0413  -0.0068 188  MET B O   
10187 C CB  . MET B 190  ? 0.5196 0.5741 0.3697 0.0161  0.0416  -0.0162 188  MET B CB  
10188 C CG  . MET B 190  ? 0.6145 0.6590 0.4590 0.0128  0.0372  -0.0154 188  MET B CG  
10189 S SD  . MET B 190  ? 0.7536 0.7950 0.5844 0.0146  0.0381  -0.0167 188  MET B SD  
10190 C CE  . MET B 190  ? 0.5896 0.6267 0.4176 0.0218  0.0386  -0.0226 188  MET B CE  
10191 N N   . ARG B 191  ? 0.5709 0.6502 0.4362 0.0117  0.0485  -0.0095 189  ARG B N   
10192 C CA  . ARG B 191  ? 0.6155 0.7053 0.4842 0.0073  0.0512  -0.0050 189  ARG B CA  
10193 C C   . ARG B 191  ? 0.6673 0.7583 0.5457 0.0036  0.0492  -0.0030 189  ARG B C   
10194 O O   . ARG B 191  ? 0.6873 0.7799 0.5671 -0.0021 0.0484  0.0010  189  ARG B O   
10195 C CB  . ARG B 191  ? 0.5676 0.6700 0.4367 0.0110  0.0568  -0.0052 189  ARG B CB  
10196 N N   . MET B 192  ? 0.6051 0.6946 0.4898 0.0068  0.0482  -0.0056 190  MET B N   
10197 C CA  . MET B 192  ? 0.5812 0.6717 0.4748 0.0036  0.0464  -0.0038 190  MET B CA  
10198 C C   . MET B 192  ? 0.6223 0.7018 0.5154 -0.0003 0.0414  -0.0031 190  MET B C   
10199 O O   . MET B 192  ? 0.6167 0.6968 0.5121 -0.0057 0.0402  0.0004  190  MET B O   
10200 C CB  . MET B 192  ? 0.5979 0.6898 0.4979 0.0082  0.0469  -0.0068 190  MET B CB  
10201 C CG  . MET B 192  ? 0.5896 0.6921 0.4906 0.0129  0.0516  -0.0079 190  MET B CG  
10202 S SD  . MET B 192  ? 0.6970 0.8001 0.6058 0.0178  0.0515  -0.0110 190  MET B SD  
10203 C CE  . MET B 192  ? 0.5148 0.6232 0.4333 0.0122  0.0503  -0.0072 190  MET B CE  
10204 N N   . MET B 193  ? 0.6133 0.6826 0.5035 0.0023  0.0385  -0.0063 191  MET B N   
10205 C CA  . MET B 193  ? 0.6456 0.7048 0.5366 -0.0005 0.0337  -0.0060 191  MET B CA  
10206 C C   . MET B 193  ? 0.6674 0.7224 0.5521 -0.0047 0.0319  -0.0032 191  MET B C   
10207 O O   . MET B 193  ? 0.6745 0.7211 0.5593 -0.0069 0.0279  -0.0028 191  MET B O   
10208 C CB  . MET B 193  ? 0.5854 0.6357 0.4752 0.0035  0.0310  -0.0100 191  MET B CB  
10209 C CG  . MET B 193  ? 0.5914 0.6422 0.4889 0.0060  0.0308  -0.0121 191  MET B CG  
10210 S SD  . MET B 193  ? 0.6766 0.7153 0.5738 0.0084  0.0263  -0.0156 191  MET B SD  
10211 C CE  . MET B 193  ? 0.5500 0.5858 0.4376 0.0128  0.0275  -0.0188 191  MET B CE  
10212 N N   . GLY B 194  ? 0.7121 0.7728 0.5913 -0.0058 0.0348  -0.0013 192  GLY B N   
10213 C CA  . GLY B 194  ? 0.6649 0.7216 0.5378 -0.0100 0.0332  0.0016  192  GLY B CA  
10214 C C   . GLY B 194  ? 0.7011 0.7664 0.5745 -0.0146 0.0358  0.0060  192  GLY B C   
10215 O O   . GLY B 194  ? 0.7211 0.7831 0.5906 -0.0191 0.0341  0.0092  192  GLY B O   
10216 N N   . GLU B 195  ? 0.6175 0.6939 0.4957 -0.0136 0.0398  0.0065  193  GLU B N   
10217 C CA  . GLU B 195  ? 0.6493 0.7354 0.5277 -0.0179 0.0427  0.0107  193  GLU B CA  
10218 C C   . GLU B 195  ? 0.5819 0.6767 0.4695 -0.0197 0.0443  0.0124  193  GLU B C   
10219 O O   . GLU B 195  ? 0.5125 0.6123 0.4012 -0.0250 0.0449  0.0165  193  GLU B O   
10220 C CB  . GLU B 195  ? 0.7119 0.8057 0.5842 -0.0153 0.0473  0.0105  193  GLU B CB  
10221 C CG  . GLU B 195  ? 0.7482 0.8342 0.6103 -0.0140 0.0461  0.0093  193  GLU B CG  
10222 C CD  . GLU B 195  ? 0.7648 0.8583 0.6207 -0.0108 0.0507  0.0086  193  GLU B CD  
10223 O OE1 . GLU B 195  ? 0.8062 0.9120 0.6653 -0.0112 0.0550  0.0105  193  GLU B OE1 
10224 O OE2 . GLU B 195  ? 0.7763 0.8634 0.6241 -0.0079 0.0501  0.0062  193  GLU B OE2 
10225 N N   . GLN B 196  ? 0.6906 0.7876 0.5847 -0.0156 0.0448  0.0095  194  GLN B N   
10226 C CA  . GLN B 196  ? 0.6096 0.7149 0.5124 -0.0171 0.0460  0.0109  194  GLN B CA  
10227 C C   . GLN B 196  ? 0.6268 0.7249 0.5354 -0.0187 0.0420  0.0104  194  GLN B C   
10228 O O   . GLN B 196  ? 0.6523 0.7544 0.5664 -0.0227 0.0416  0.0130  194  GLN B O   
10229 C CB  . GLN B 196  ? 0.5588 0.6732 0.4652 -0.0114 0.0497  0.0084  194  GLN B CB  
10230 N N   . PHE B 197  ? 0.4882 0.5759 0.3957 -0.0157 0.0390  0.0071  195  PHE B N   
10231 C CA  . PHE B 197  ? 0.4967 0.5772 0.4091 -0.0171 0.0351  0.0067  195  PHE B CA  
10232 C C   . PHE B 197  ? 0.4862 0.5585 0.3951 -0.0221 0.0317  0.0092  195  PHE B C   
10233 O O   . PHE B 197  ? 0.4610 0.5306 0.3740 -0.0255 0.0294  0.0107  195  PHE B O   
10234 C CB  . PHE B 197  ? 0.5032 0.5767 0.4163 -0.0120 0.0335  0.0023  195  PHE B CB  
10235 C CG  . PHE B 197  ? 0.5138 0.5937 0.4316 -0.0072 0.0361  -0.0001 195  PHE B CG  
10236 C CD1 . PHE B 197  ? 0.5337 0.6230 0.4581 -0.0083 0.0381  0.0014  195  PHE B CD1 
10237 C CD2 . PHE B 197  ? 0.5628 0.6391 0.4781 -0.0017 0.0363  -0.0040 195  PHE B CD2 
10238 C CE1 . PHE B 197  ? 0.5467 0.6420 0.4754 -0.0037 0.0404  -0.0007 195  PHE B CE1 
10239 C CE2 . PHE B 197  ? 0.5709 0.6525 0.4901 0.0028  0.0386  -0.0062 195  PHE B CE2 
10240 C CZ  . PHE B 197  ? 0.5693 0.6605 0.4953 0.0020  0.0406  -0.0046 195  PHE B CZ  
10241 N N   . VAL B 198  ? 0.4461 0.5139 0.3472 -0.0224 0.0311  0.0096  196  VAL B N   
10242 C CA  . VAL B 198  ? 0.4304 0.4905 0.3273 -0.0269 0.0279  0.0122  196  VAL B CA  
10243 C C   . VAL B 198  ? 0.4700 0.5350 0.3608 -0.0301 0.0302  0.0155  196  VAL B C   
10244 O O   . VAL B 198  ? 0.4815 0.5530 0.3691 -0.0275 0.0337  0.0148  196  VAL B O   
10245 C CB  . VAL B 198  ? 0.4293 0.4779 0.3222 -0.0246 0.0242  0.0097  196  VAL B CB  
10246 C CG1 . VAL B 198  ? 0.4670 0.5110 0.3662 -0.0220 0.0220  0.0069  196  VAL B CG1 
10247 C CG2 . VAL B 198  ? 0.5119 0.5606 0.3984 -0.0208 0.0259  0.0075  196  VAL B CG2 
10248 N N   . THR B 199  ? 0.3928 0.4543 0.2815 -0.0356 0.0282  0.0192  197  THR B N   
10249 C CA  . THR B 199  ? 0.3999 0.4645 0.2819 -0.0391 0.0298  0.0226  197  THR B CA  
10250 C C   . THR B 199  ? 0.4415 0.4983 0.3149 -0.0374 0.0282  0.0216  197  THR B C   
10251 O O   . THR B 199  ? 0.4719 0.5323 0.3389 -0.0382 0.0304  0.0232  197  THR B O   
10252 C CB  . THR B 199  ? 0.3872 0.4502 0.2698 -0.0458 0.0280  0.0270  197  THR B CB  
10253 O OG1 . THR B 199  ? 0.4400 0.5097 0.3309 -0.0471 0.0291  0.0275  197  THR B OG1 
10254 C CG2 . THR B 199  ? 0.3887 0.4566 0.2652 -0.0500 0.0301  0.0312  197  THR B CG2 
10255 N N   . GLY B 200  ? 0.4089 0.4557 0.2823 -0.0350 0.0244  0.0190  198  GLY B N   
10256 C CA  . GLY B 200  ? 0.4621 0.5017 0.3280 -0.0328 0.0226  0.0175  198  GLY B CA  
10257 C C   . GLY B 200  ? 0.4277 0.4579 0.2963 -0.0301 0.0186  0.0144  198  GLY B C   
10258 O O   . GLY B 200  ? 0.4102 0.4385 0.2855 -0.0308 0.0168  0.0143  198  GLY B O   
10259 N N   . GLU B 201  ? 0.4408 0.4656 0.3041 -0.0269 0.0172  0.0120  199  GLU B N   
10260 C CA  . GLU B 201  ? 0.4440 0.4602 0.3096 -0.0244 0.0132  0.0092  199  GLU B CA  
10261 C C   . GLU B 201  ? 0.4095 0.4171 0.2737 -0.0276 0.0087  0.0115  199  GLU B C   
10262 O O   . GLU B 201  ? 0.4597 0.4616 0.3284 -0.0266 0.0056  0.0102  199  GLU B O   
10263 C CB  . GLU B 201  ? 0.4729 0.4860 0.3332 -0.0202 0.0128  0.0058  199  GLU B CB  
10264 N N   . THR B 202  ? 0.3917 0.3981 0.2495 -0.0313 0.0084  0.0150  200  THR B N   
10265 C CA  . THR B 202  ? 0.4068 0.4050 0.2626 -0.0345 0.0043  0.0177  200  THR B CA  
10266 C C   . THR B 202  ? 0.3891 0.3905 0.2443 -0.0398 0.0057  0.0222  200  THR B C   
10267 O O   . THR B 202  ? 0.3984 0.4085 0.2528 -0.0411 0.0097  0.0234  200  THR B O   
10268 C CB  . THR B 202  ? 0.4052 0.3969 0.2523 -0.0342 0.0018  0.0181  200  THR B CB  
10269 O OG1 . THR B 202  ? 0.4430 0.4398 0.2831 -0.0358 0.0050  0.0201  200  THR B OG1 
10270 C CG2 . THR B 202  ? 0.4531 0.4416 0.3000 -0.0294 0.0003  0.0139  200  THR B CG2 
10271 N N   . ILE B 203  ? 0.4047 0.3990 0.2600 -0.0428 0.0021  0.0246  201  ILE B N   
10272 C CA  . ILE B 203  ? 0.3673 0.3632 0.2212 -0.0483 0.0028  0.0290  201  ILE B CA  
10273 C C   . ILE B 203  ? 0.4053 0.4034 0.2505 -0.0508 0.0044  0.0319  201  ILE B C   
10274 O O   . ILE B 203  ? 0.3862 0.3908 0.2306 -0.0547 0.0072  0.0350  201  ILE B O   
10275 C CB  . ILE B 203  ? 0.3815 0.3680 0.2365 -0.0507 -0.0017 0.0308  201  ILE B CB  
10276 C CG1 . ILE B 203  ? 0.3713 0.3597 0.2264 -0.0565 -0.0009 0.0349  201  ILE B CG1 
10277 C CG2 . ILE B 203  ? 0.3727 0.3494 0.2206 -0.0504 -0.0056 0.0317  201  ILE B CG2 
10278 C CD1 . ILE B 203  ? 0.3278 0.3255 0.1905 -0.0569 0.0025  0.0341  201  ILE B CD1 
10279 N N   . ARG B 204  ? 0.4087 0.4018 0.2473 -0.0487 0.0028  0.0309  202  ARG B N   
10280 C CA  . ARG B 204  ? 0.4517 0.4471 0.2815 -0.0504 0.0045  0.0332  202  ARG B CA  
10281 C C   . ARG B 204  ? 0.4297 0.4371 0.2602 -0.0496 0.0102  0.0326  202  ARG B C   
10282 O O   . ARG B 204  ? 0.4446 0.4578 0.2718 -0.0533 0.0129  0.0361  202  ARG B O   
10283 C CB  . ARG B 204  ? 0.4397 0.4282 0.2632 -0.0471 0.0018  0.0312  202  ARG B CB  
10284 C CG  . ARG B 204  ? 0.5673 0.5574 0.3808 -0.0480 0.0034  0.0328  202  ARG B CG  
10285 C CD  . ARG B 204  ? 0.5802 0.5653 0.3890 -0.0436 0.0013  0.0294  202  ARG B CD  
10286 N NE  . ARG B 204  ? 0.6559 0.6483 0.4614 -0.0408 0.0056  0.0272  202  ARG B NE  
10287 C CZ  . ARG B 204  ? 0.6180 0.6154 0.4286 -0.0367 0.0080  0.0231  202  ARG B CZ  
10288 N NH1 . ARG B 204  ? 0.5742 0.5701 0.3936 -0.0348 0.0065  0.0208  202  ARG B NH1 
10289 N NH2 . ARG B 204  ? 0.7029 0.7068 0.5096 -0.0343 0.0121  0.0215  202  ARG B NH2 
10290 N N   . GLU B 205  ? 0.4264 0.4378 0.2613 -0.0446 0.0120  0.0282  203  GLU B N   
10291 C CA  . GLU B 205  ? 0.4545 0.4772 0.2901 -0.0430 0.0173  0.0273  203  GLU B CA  
10292 C C   . GLU B 205  ? 0.4049 0.4361 0.2472 -0.0462 0.0200  0.0296  203  GLU B C   
10293 O O   . GLU B 205  ? 0.4486 0.4890 0.2892 -0.0481 0.0241  0.0318  203  GLU B O   
10294 C CB  . GLU B 205  ? 0.4699 0.4934 0.3085 -0.0368 0.0181  0.0220  203  GLU B CB  
10295 C CG  . GLU B 205  ? 0.5456 0.5793 0.3832 -0.0339 0.0233  0.0205  203  GLU B CG  
10296 C CD  . GLU B 205  ? 0.5900 0.6231 0.4301 -0.0278 0.0237  0.0152  203  GLU B CD  
10297 O OE1 . GLU B 205  ? 0.5532 0.5824 0.4000 -0.0263 0.0212  0.0132  203  GLU B OE1 
10298 O OE2 . GLU B 205  ? 0.7022 0.7386 0.5373 -0.0244 0.0263  0.0131  203  GLU B OE2 
10299 N N   . ALA B 206  ? 0.3924 0.4209 0.2422 -0.0469 0.0179  0.0292  204  ALA B N   
10300 C CA  . ALA B 206  ? 0.4010 0.4372 0.2572 -0.0501 0.0200  0.0313  204  ALA B CA  
10301 C C   . ALA B 206  ? 0.4045 0.4422 0.2564 -0.0566 0.0204  0.0366  204  ALA B C   
10302 O O   . ALA B 206  ? 0.4091 0.4572 0.2626 -0.0590 0.0242  0.0388  204  ALA B O   
10303 C CB  . ALA B 206  ? 0.3754 0.4066 0.2392 -0.0500 0.0171  0.0300  204  ALA B CB  
10304 N N   . LEU B 207  ? 0.3758 0.4034 0.2221 -0.0594 0.0166  0.0389  205  LEU B N   
10305 C CA  . LEU B 207  ? 0.4279 0.4555 0.2693 -0.0657 0.0165  0.0441  205  LEU B CA  
10306 C C   . LEU B 207  ? 0.4443 0.4807 0.2798 -0.0665 0.0208  0.0459  205  LEU B C   
10307 O O   . LEU B 207  ? 0.4457 0.4892 0.2808 -0.0714 0.0232  0.0499  205  LEU B O   
10308 C CB  . LEU B 207  ? 0.4307 0.4449 0.2663 -0.0676 0.0114  0.0459  205  LEU B CB  
10309 C CG  . LEU B 207  ? 0.4446 0.4505 0.2855 -0.0685 0.0073  0.0455  205  LEU B CG  
10310 C CD1 . LEU B 207  ? 0.4224 0.4148 0.2577 -0.0687 0.0021  0.0463  205  LEU B CD1 
10311 C CD2 . LEU B 207  ? 0.3995 0.4090 0.2438 -0.0742 0.0080  0.0490  205  LEU B CD2 
10312 N N   . LYS B 208  ? 0.4335 0.4696 0.2642 -0.0618 0.0218  0.0431  206  LYS B N   
10313 C CA  . LYS B 208  ? 0.4712 0.5154 0.2956 -0.0620 0.0260  0.0444  206  LYS B CA  
10314 C C   . LYS B 208  ? 0.4694 0.5279 0.2996 -0.0608 0.0314  0.0438  206  LYS B C   
10315 O O   . LYS B 208  ? 0.4856 0.5534 0.3133 -0.0637 0.0352  0.0470  206  LYS B O   
10316 C CB  . LYS B 208  ? 0.4631 0.5025 0.2806 -0.0570 0.0254  0.0411  206  LYS B CB  
10317 N N   . ARG B 209  ? 0.4567 0.5177 0.2948 -0.0564 0.0320  0.0398  207  ARG B N   
10318 C CA  . ARG B 209  ? 0.4492 0.5238 0.2932 -0.0549 0.0369  0.0391  207  ARG B CA  
10319 C C   . ARG B 209  ? 0.4735 0.5549 0.3234 -0.0606 0.0378  0.0431  207  ARG B C   
10320 O O   . ARG B 209  ? 0.4698 0.5640 0.3237 -0.0606 0.0421  0.0438  207  ARG B O   
10321 C CB  . ARG B 209  ? 0.4656 0.5401 0.3158 -0.0485 0.0370  0.0338  207  ARG B CB  
10322 C CG  . ARG B 209  ? 0.5287 0.5984 0.3732 -0.0427 0.0368  0.0297  207  ARG B CG  
10323 C CD  . ARG B 209  ? 0.5109 0.5810 0.3617 -0.0368 0.0370  0.0248  207  ARG B CD  
10324 N NE  . ARG B 209  ? 0.6732 0.7399 0.5186 -0.0312 0.0373  0.0207  207  ARG B NE  
10325 C CZ  . ARG B 209  ? 0.7170 0.7809 0.5660 -0.0260 0.0366  0.0162  207  ARG B CZ  
10326 N NH1 . ARG B 209  ? 0.6349 0.6989 0.4928 -0.0255 0.0354  0.0151  207  ARG B NH1 
10327 N NH2 . ARG B 209  ? 0.7638 0.8245 0.6069 -0.0213 0.0369  0.0127  207  ARG B NH2 
10328 N N   . SER B 210  ? 0.4331 0.5061 0.2832 -0.0655 0.0337  0.0458  208  SER B N   
10329 C CA  . SER B 210  ? 0.4454 0.5234 0.3009 -0.0713 0.0339  0.0494  208  SER B CA  
10330 C C   . SER B 210  ? 0.4332 0.5179 0.2839 -0.0774 0.0362  0.0548  208  SER B C   
10331 O O   . SER B 210  ? 0.4508 0.5438 0.3064 -0.0819 0.0378  0.0578  208  SER B O   
10332 C CB  . SER B 210  ? 0.4169 0.4824 0.2740 -0.0739 0.0284  0.0499  208  SER B CB  
10333 O OG  . SER B 210  ? 0.4255 0.4866 0.2880 -0.0686 0.0267  0.0451  208  SER B OG  
10334 N N   . LYS B 211  ? 0.4661 0.5478 0.3076 -0.0778 0.0365  0.0562  209  LYS B N   
10335 C CA  . LYS B 211  ? 0.4531 0.5403 0.2895 -0.0841 0.0385  0.0617  209  LYS B CA  
10336 C C   . LYS B 211  ? 0.4570 0.5616 0.2977 -0.0845 0.0443  0.0630  209  LYS B C   
10337 O O   . LYS B 211  ? 0.4777 0.5890 0.3189 -0.0910 0.0457  0.0679  209  LYS B O   
10338 C CB  . LYS B 211  ? 0.4809 0.5625 0.3063 -0.0835 0.0382  0.0625  209  LYS B CB  
10339 N N   . GLU B 212  ? 0.4586 0.5707 0.3029 -0.0778 0.0477  0.0587  210  GLU B N   
10340 C CA  . GLU B 212  ? 0.4622 0.5913 0.3100 -0.0773 0.0535  0.0597  210  GLU B CA  
10341 C C   . GLU B 212  ? 0.4630 0.6002 0.3201 -0.0820 0.0538  0.0624  210  GLU B C   
10342 O O   . GLU B 212  ? 0.4591 0.6043 0.3190 -0.0859 0.0556  0.0659  210  GLU B O   
10343 C CB  . GLU B 212  ? 0.5253 0.6592 0.3752 -0.0686 0.0565  0.0542  210  GLU B CB  
10344 C CG  . GLU B 212  ? 0.5888 0.7394 0.4433 -0.0665 0.0623  0.0545  210  GLU B CG  
10345 C CD  . GLU B 212  ? 0.6753 0.8302 0.5315 -0.0579 0.0651  0.0490  210  GLU B CD  
10346 O OE1 . GLU B 212  ? 0.7947 0.9428 0.6435 -0.0533 0.0648  0.0459  210  GLU B OE1 
10347 O OE2 . GLU B 212  ? 0.7617 0.9258 0.6271 -0.0555 0.0671  0.0478  210  GLU B OE2 
10348 N N   . LEU B 213  ? 0.4399 0.5725 0.3043 -0.0801 0.0511  0.0596  211  LEU B N   
10349 C CA  . LEU B 213  ? 0.4532 0.5932 0.3262 -0.0844 0.0512  0.0618  211  LEU B CA  
10350 C C   . LEU B 213  ? 0.4377 0.5706 0.3087 -0.0929 0.0474  0.0666  211  LEU B C   
10351 O O   . LEU B 213  ? 0.4234 0.5642 0.2992 -0.0984 0.0482  0.0702  211  LEU B O   
10352 C CB  . LEU B 213  ? 0.4133 0.5511 0.2945 -0.0795 0.0497  0.0572  211  LEU B CB  
10353 C CG  . LEU B 213  ? 0.4301 0.5776 0.3148 -0.0717 0.0539  0.0531  211  LEU B CG  
10354 C CD1 . LEU B 213  ? 0.4357 0.5808 0.3281 -0.0671 0.0523  0.0489  211  LEU B CD1 
10355 C CD2 . LEU B 213  ? 0.4739 0.6394 0.3616 -0.0732 0.0592  0.0560  211  LEU B CD2 
10356 N N   . GLU B 214  ? 0.3985 0.5160 0.2626 -0.0940 0.0431  0.0667  212  GLU B N   
10357 C CA  . GLU B 214  ? 0.4215 0.5314 0.2823 -0.1020 0.0395  0.0715  212  GLU B CA  
10358 C C   . GLU B 214  ? 0.4076 0.5261 0.2658 -0.1073 0.0422  0.0764  212  GLU B C   
10359 O O   . GLU B 214  ? 0.4170 0.5371 0.2790 -0.1134 0.0408  0.0798  212  GLU B O   
10360 C CB  . GLU B 214  ? 0.4356 0.5280 0.2889 -0.1012 0.0347  0.0706  212  GLU B CB  
10361 C CG  . GLU B 214  ? 0.3840 0.4656 0.2418 -0.0973 0.0306  0.0663  212  GLU B CG  
10362 C CD  . GLU B 214  ? 0.4106 0.4751 0.2616 -0.0975 0.0255  0.0662  212  GLU B CD  
10363 O OE1 . GLU B 214  ? 0.4583 0.5189 0.3008 -0.0993 0.0251  0.0686  212  GLU B OE1 
10364 O OE2 . GLU B 214  ? 0.3985 0.4538 0.2530 -0.0958 0.0217  0.0637  212  GLU B OE2 
10365 N N   . GLU B 215  ? 0.4396 0.5627 0.2934 -0.1040 0.0454  0.0758  213  GLU B N   
10366 C CA  . GLU B 215  ? 0.4432 0.5743 0.2969 -0.1072 0.0478  0.0793  213  GLU B CA  
10367 C C   . GLU B 215  ? 0.4382 0.5843 0.3023 -0.1081 0.0507  0.0800  213  GLU B C   
10368 O O   . GLU B 215  ? 0.4479 0.5998 0.3135 -0.1129 0.0514  0.0837  213  GLU B O   
10369 C CB  . GLU B 215  ? 0.5215 0.6554 0.3688 -0.1025 0.0511  0.0779  213  GLU B CB  
10370 C CG  . GLU B 215  ? 0.5419 0.6620 0.3780 -0.1033 0.0481  0.0788  213  GLU B CG  
10371 C CD  . GLU B 215  ? 0.6214 0.7444 0.4510 -0.0986 0.0514  0.0773  213  GLU B CD  
10372 O OE1 . GLU B 215  ? 0.7256 0.8584 0.5561 -0.0993 0.0550  0.0792  213  GLU B OE1 
10373 O OE2 . GLU B 215  ? 0.6562 0.7714 0.4795 -0.0941 0.0503  0.0742  213  GLU B OE2 
10374 N N   . LYS B 216  ? 0.4144 0.5668 0.2857 -0.1036 0.0523  0.0766  214  LYS B N   
10375 C CA  . LYS B 216  ? 0.4367 0.6028 0.3183 -0.1042 0.0545  0.0771  214  LYS B CA  
10376 C C   . LYS B 216  ? 0.4644 0.6273 0.3511 -0.1105 0.0507  0.0793  214  LYS B C   
10377 O O   . LYS B 216  ? 0.4788 0.6524 0.3737 -0.1124 0.0518  0.0805  214  LYS B O   
10378 C CB  . LYS B 216  ? 0.4362 0.6104 0.3232 -0.0963 0.0578  0.0724  214  LYS B CB  
10379 N N   . GLY B 217  ? 0.4392 0.5875 0.3211 -0.1136 0.0461  0.0799  215  GLY B N   
10380 C CA  . GLY B 217  ? 0.3765 0.5200 0.2623 -0.1193 0.0422  0.0817  215  GLY B CA  
10381 C C   . GLY B 217  ? 0.4289 0.5662 0.3171 -0.1167 0.0402  0.0785  215  GLY B C   
10382 O O   . GLY B 217  ? 0.4300 0.5625 0.3211 -0.1212 0.0369  0.0797  215  GLY B O   
10383 N N   . PHE B 218  ? 0.4030 0.5404 0.2900 -0.1097 0.0421  0.0744  216  PHE B N   
10384 C CA  . PHE B 218  ? 0.3833 0.5108 0.2738 -0.1052 0.0389  0.0698  216  PHE B CA  
10385 C C   . PHE B 218  ? 0.3708 0.4798 0.2546 -0.1067 0.0336  0.0698  216  PHE B C   
10386 O O   . PHE B 218  ? 0.3832 0.4868 0.2589 -0.1095 0.0329  0.0725  216  PHE B O   
10387 C CB  . PHE B 218  ? 0.3980 0.5287 0.2905 -0.0959 0.0414  0.0644  216  PHE B CB  
10388 C CG  . PHE B 218  ? 0.4261 0.5734 0.3264 -0.0930 0.0460  0.0634  216  PHE B CG  
10389 C CD1 . PHE B 218  ? 0.4284 0.5894 0.3275 -0.0924 0.0511  0.0651  216  PHE B CD1 
10390 C CD2 . PHE B 218  ? 0.3982 0.5475 0.3068 -0.0904 0.0452  0.0607  216  PHE B CD2 
10391 C CE1 . PHE B 218  ? 0.4105 0.5858 0.3175 -0.0885 0.0548  0.0636  216  PHE B CE1 
10392 C CE2 . PHE B 218  ? 0.4274 0.5918 0.3432 -0.0874 0.0492  0.0598  216  PHE B CE2 
10393 C CZ  . PHE B 218  ? 0.3819 0.5600 0.2966 -0.0867 0.0542  0.0615  216  PHE B CZ  
10394 N N   . SER B 219  ? 0.3651 0.4647 0.2525 -0.1046 0.0299  0.0667  217  SER B N   
10395 C CA  . SER B 219  ? 0.3566 0.4389 0.2387 -0.1037 0.0252  0.0654  217  SER B CA  
10396 C C   . SER B 219  ? 0.3667 0.4445 0.2527 -0.0958 0.0243  0.0595  217  SER B C   
10397 O O   . SER B 219  ? 0.3872 0.4746 0.2793 -0.0913 0.0273  0.0567  217  SER B O   
10398 C CB  . SER B 219  ? 0.3268 0.3998 0.2083 -0.1103 0.0208  0.0683  217  SER B CB  
10399 O OG  . SER B 219  ? 0.3673 0.4439 0.2568 -0.1107 0.0203  0.0670  217  SER B OG  
10400 N N   . TYR B 220  ? 0.3233 0.3865 0.2057 -0.0940 0.0201  0.0577  218  TYR B N   
10401 C CA  . TYR B 220  ? 0.3175 0.3761 0.2026 -0.0866 0.0193  0.0524  218  TYR B CA  
10402 C C   . TYR B 220  ? 0.2994 0.3449 0.1855 -0.0866 0.0144  0.0510  218  TYR B C   
10403 O O   . TYR B 220  ? 0.3157 0.3520 0.1975 -0.0912 0.0111  0.0538  218  TYR B O   
10404 C CB  . TYR B 220  ? 0.3103 0.3658 0.1892 -0.0822 0.0200  0.0507  218  TYR B CB  
10405 C CG  . TYR B 220  ? 0.3331 0.4015 0.2128 -0.0789 0.0251  0.0496  218  TYR B CG  
10406 C CD1 . TYR B 220  ? 0.3643 0.4412 0.2401 -0.0825 0.0283  0.0534  218  TYR B CD1 
10407 C CD2 . TYR B 220  ? 0.3226 0.3943 0.2066 -0.0720 0.0267  0.0449  218  TYR B CD2 
10408 C CE1 . TYR B 220  ? 0.3428 0.4318 0.2192 -0.0791 0.0331  0.0523  218  TYR B CE1 
10409 C CE2 . TYR B 220  ? 0.3717 0.4547 0.2560 -0.0686 0.0314  0.0437  218  TYR B CE2 
10410 C CZ  . TYR B 220  ? 0.3366 0.4283 0.2171 -0.0720 0.0346  0.0474  218  TYR B CZ  
10411 O OH  . TYR B 220  ? 0.4076 0.5106 0.2882 -0.0682 0.0394  0.0461  218  TYR B OH  
10412 N N   . SER B 221  ? 0.2659 0.3107 0.1576 -0.0812 0.0141  0.0467  219  SER B N   
10413 C CA  . SER B 221  ? 0.2618 0.2944 0.1545 -0.0793 0.0099  0.0444  219  SER B CA  
10414 C C   . SER B 221  ? 0.2829 0.3142 0.1771 -0.0719 0.0103  0.0396  219  SER B C   
10415 O O   . SER B 221  ? 0.3182 0.3581 0.2178 -0.0683 0.0132  0.0371  219  SER B O   
10416 C CB  . SER B 221  ? 0.2843 0.3177 0.1833 -0.0813 0.0089  0.0441  219  SER B CB  
10417 O OG  . SER B 221  ? 0.2747 0.2968 0.1746 -0.0789 0.0051  0.0417  219  SER B OG  
10418 N N   . TYR B 222  ? 0.2928 0.3134 0.1824 -0.0697 0.0074  0.0386  220  TYR B N   
10419 C CA  . TYR B 222  ? 0.2788 0.2979 0.1687 -0.0633 0.0076  0.0345  220  TYR B CA  
10420 C C   . TYR B 222  ? 0.2871 0.3002 0.1822 -0.0598 0.0051  0.0311  220  TYR B C   
10421 O O   . TYR B 222  ? 0.3002 0.3050 0.1954 -0.0617 0.0018  0.0319  220  TYR B O   
10422 C CB  . TYR B 222  ? 0.2603 0.2723 0.1423 -0.0627 0.0058  0.0352  220  TYR B CB  
10423 C CG  . TYR B 222  ? 0.3008 0.3195 0.1775 -0.0656 0.0087  0.0383  220  TYR B CG  
10424 C CD1 . TYR B 222  ? 0.3102 0.3382 0.1870 -0.0624 0.0127  0.0367  220  TYR B CD1 
10425 C CD2 . TYR B 222  ? 0.2798 0.2954 0.1512 -0.0715 0.0076  0.0428  220  TYR B CD2 
10426 C CE1 . TYR B 222  ? 0.3136 0.3486 0.1857 -0.0649 0.0158  0.0394  220  TYR B CE1 
10427 C CE2 . TYR B 222  ? 0.3239 0.3463 0.1903 -0.0744 0.0105  0.0459  220  TYR B CE2 
10428 C CZ  . TYR B 222  ? 0.3399 0.3724 0.2069 -0.0710 0.0147  0.0441  220  TYR B CZ  
10429 O OH  . TYR B 222  ? 0.3339 0.3738 0.1961 -0.0736 0.0179  0.0470  220  TYR B OH  
10430 N N   . ASP B 223  ? 0.2808 0.2981 0.1801 -0.0545 0.0068  0.0274  221  ASP B N   
10431 C CA  . ASP B 223  ? 0.3093 0.3230 0.2141 -0.0507 0.0052  0.0239  221  ASP B CA  
10432 C C   . ASP B 223  ? 0.3408 0.3506 0.2436 -0.0456 0.0044  0.0209  221  ASP B C   
10433 O O   . ASP B 223  ? 0.3479 0.3637 0.2505 -0.0427 0.0071  0.0192  221  ASP B O   
10434 C CB  . ASP B 223  ? 0.3511 0.3745 0.2630 -0.0495 0.0082  0.0225  221  ASP B CB  
10435 C CG  . ASP B 223  ? 0.3967 0.4183 0.3140 -0.0445 0.0075  0.0184  221  ASP B CG  
10436 O OD1 . ASP B 223  ? 0.3950 0.4077 0.3122 -0.0431 0.0043  0.0172  221  ASP B OD1 
10437 O OD2 . ASP B 223  ? 0.3968 0.4264 0.3185 -0.0419 0.0103  0.0166  221  ASP B OD2 
10438 N N   . MET B 224  ? 0.3362 0.3360 0.2372 -0.0448 0.0007  0.0203  222  MET B N   
10439 C CA  . MET B 224  ? 0.3784 0.3741 0.2780 -0.0403 -0.0006 0.0175  222  MET B CA  
10440 C C   . MET B 224  ? 0.3798 0.3775 0.2865 -0.0362 -0.0002 0.0139  222  MET B C   
10441 O O   . MET B 224  ? 0.4131 0.4062 0.3236 -0.0358 -0.0024 0.0131  222  MET B O   
10442 C CB  . MET B 224  ? 0.3820 0.3671 0.2775 -0.0407 -0.0049 0.0185  222  MET B CB  
10443 C CG  . MET B 224  ? 0.3733 0.3554 0.2614 -0.0450 -0.0057 0.0224  222  MET B CG  
10444 S SD  . MET B 224  ? 0.4487 0.4381 0.3307 -0.0458 -0.0022 0.0237  222  MET B SD  
10445 C CE  . MET B 224  ? 0.4363 0.4215 0.3155 -0.0406 -0.0038 0.0204  222  MET B CE  
10446 N N   . LEU B 225  ? 0.3886 0.3930 0.2966 -0.0333 0.0027  0.0118  223  LEU B N   
10447 C CA  . LEU B 225  ? 0.4214 0.4289 0.3360 -0.0297 0.0037  0.0086  223  LEU B CA  
10448 C C   . LEU B 225  ? 0.4831 0.4832 0.3995 -0.0268 0.0006  0.0062  223  LEU B C   
10449 O O   . LEU B 225  ? 0.4769 0.4718 0.3892 -0.0255 -0.0014 0.0057  223  LEU B O   
10450 C CB  . LEU B 225  ? 0.4229 0.4374 0.3370 -0.0268 0.0071  0.0068  223  LEU B CB  
10451 C CG  . LEU B 225  ? 0.4346 0.4589 0.3488 -0.0287 0.0109  0.0086  223  LEU B CG  
10452 C CD1 . LEU B 225  ? 0.4619 0.4915 0.3739 -0.0251 0.0139  0.0066  223  LEU B CD1 
10453 C CD2 . LEU B 225  ? 0.4394 0.4687 0.3606 -0.0298 0.0120  0.0089  223  LEU B CD2 
10454 N N   . GLY B 226  ? 0.4813 0.4813 0.4040 -0.0256 0.0002  0.0047  224  GLY B N   
10455 C CA  . GLY B 226  ? 0.5627 0.5573 0.4882 -0.0226 -0.0023 0.0024  224  GLY B CA  
10456 C C   . GLY B 226  ? 0.6096 0.6055 0.5420 -0.0217 -0.0021 0.0010  224  GLY B C   
10457 O O   . GLY B 226  ? 0.6274 0.6255 0.5618 -0.0242 -0.0014 0.0025  224  GLY B O   
10458 N N   . GLU B 227  ? 0.5895 0.5841 0.5253 -0.0182 -0.0029 -0.0017 225  GLU B N   
10459 C CA  . GLU B 227  ? 0.5651 0.5602 0.5072 -0.0172 -0.0030 -0.0030 225  GLU B CA  
10460 C C   . GLU B 227  ? 0.5494 0.5386 0.4919 -0.0190 -0.0056 -0.0017 225  GLU B C   
10461 O O   . GLU B 227  ? 0.5716 0.5553 0.5102 -0.0200 -0.0079 -0.0004 225  GLU B O   
10462 C CB  . GLU B 227  ? 0.5537 0.5480 0.4988 -0.0134 -0.0034 -0.0059 225  GLU B CB  
10463 N N   . ALA B 228  ? 0.4481 0.4385 0.3952 -0.0193 -0.0052 -0.0020 226  ALA B N   
10464 C CA  . ALA B 228  ? 0.4261 0.4105 0.3739 -0.0202 -0.0076 -0.0014 226  ALA B CA  
10465 C C   . ALA B 228  ? 0.3698 0.3487 0.3179 -0.0175 -0.0102 -0.0027 226  ALA B C   
10466 O O   . ALA B 228  ? 0.3871 0.3676 0.3373 -0.0146 -0.0099 -0.0048 226  ALA B O   
10467 C CB  . ALA B 228  ? 0.3486 0.3354 0.3016 -0.0202 -0.0068 -0.0022 226  ALA B CB  
10468 N N   . ALA B 229  ? 0.2902 0.2626 0.2361 -0.0183 -0.0128 -0.0015 227  ALA B N   
10469 C CA  . ALA B 229  ? 0.2895 0.2570 0.2356 -0.0157 -0.0154 -0.0025 227  ALA B CA  
10470 C C   . ALA B 229  ? 0.2638 0.2324 0.2160 -0.0128 -0.0153 -0.0048 227  ALA B C   
10471 O O   . ALA B 229  ? 0.2745 0.2434 0.2297 -0.0132 -0.0148 -0.0051 227  ALA B O   
10472 C CB  . ALA B 229  ? 0.2612 0.2215 0.2039 -0.0169 -0.0182 -0.0007 227  ALA B CB  
10473 N N   . THR B 230  ? 0.2582 0.2275 0.2121 -0.0102 -0.0159 -0.0064 228  THR B N   
10474 C CA  . THR B 230  ? 0.2839 0.2538 0.2433 -0.0075 -0.0163 -0.0084 228  THR B CA  
10475 C C   . THR B 230  ? 0.2758 0.2408 0.2357 -0.0059 -0.0192 -0.0083 228  THR B C   
10476 O O   . THR B 230  ? 0.2508 0.2154 0.2150 -0.0043 -0.0196 -0.0092 228  THR B O   
10477 C CB  . THR B 230  ? 0.3119 0.2858 0.2732 -0.0058 -0.0151 -0.0102 228  THR B CB  
10478 O OG1 . THR B 230  ? 0.3235 0.3021 0.2841 -0.0068 -0.0123 -0.0102 228  THR B OG1 
10479 C CG2 . THR B 230  ? 0.2605 0.2355 0.2276 -0.0034 -0.0153 -0.0120 228  THR B CG2 
10480 N N   . THR B 231  ? 0.2519 0.2135 0.2076 -0.0063 -0.0213 -0.0071 229  THR B N   
10481 C CA  . THR B 231  ? 0.2262 0.1835 0.1822 -0.0045 -0.0243 -0.0069 229  THR B CA  
10482 C C   . THR B 231  ? 0.2405 0.1923 0.1911 -0.0062 -0.0262 -0.0046 229  THR B C   
10483 O O   . THR B 231  ? 0.2361 0.1876 0.1822 -0.0089 -0.0252 -0.0031 229  THR B O   
10484 C CB  . THR B 231  ? 0.2444 0.2026 0.2005 -0.0029 -0.0258 -0.0077 229  THR B CB  
10485 O OG1 . THR B 231  ? 0.2827 0.2397 0.2326 -0.0046 -0.0261 -0.0066 229  THR B OG1 
10486 C CG2 . THR B 231  ? 0.2622 0.2254 0.2226 -0.0017 -0.0240 -0.0099 229  THR B CG2 
10487 N N   . ALA B 232  ? 0.2477 0.1950 0.1987 -0.0044 -0.0289 -0.0042 230  ALA B N   
10488 C CA  . ALA B 232  ? 0.2692 0.2103 0.2146 -0.0056 -0.0312 -0.0020 230  ALA B CA  
10489 C C   . ALA B 232  ? 0.2599 0.2007 0.1999 -0.0071 -0.0318 -0.0007 230  ALA B C   
10490 O O   . ALA B 232  ? 0.2681 0.2056 0.2026 -0.0096 -0.0322 0.0014  230  ALA B O   
10491 C CB  . ALA B 232  ? 0.2632 0.2002 0.2104 -0.0026 -0.0341 -0.0020 230  ALA B CB  
10492 N N   . ALA B 233  ? 0.2576 0.2016 0.1989 -0.0057 -0.0321 -0.0020 231  ALA B N   
10493 C CA  . ALA B 233  ? 0.2799 0.2236 0.2157 -0.0069 -0.0327 -0.0011 231  ALA B CA  
10494 C C   . ALA B 233  ? 0.2843 0.2309 0.2167 -0.0098 -0.0297 -0.0004 231  ALA B C   
10495 O O   . ALA B 233  ? 0.2778 0.2225 0.2040 -0.0118 -0.0300 0.0014  231  ALA B O   
10496 C CB  . ALA B 233  ? 0.3028 0.2492 0.2407 -0.0049 -0.0335 -0.0028 231  ALA B CB  
10497 N N   . ASP B 234  ? 0.2590 0.2104 0.1953 -0.0099 -0.0267 -0.0019 232  ASP B N   
10498 C CA  . ASP B 234  ? 0.2748 0.2299 0.2087 -0.0124 -0.0237 -0.0012 232  ASP B CA  
10499 C C   . ASP B 234  ? 0.2680 0.2197 0.1979 -0.0154 -0.0240 0.0015  232  ASP B C   
10500 O O   . ASP B 234  ? 0.2769 0.2290 0.2015 -0.0179 -0.0232 0.0032  232  ASP B O   
10501 C CB  . ASP B 234  ? 0.2836 0.2439 0.2229 -0.0118 -0.0208 -0.0029 232  ASP B CB  
10502 C CG  . ASP B 234  ? 0.2981 0.2621 0.2408 -0.0094 -0.0201 -0.0054 232  ASP B CG  
10503 O OD1 . ASP B 234  ? 0.3185 0.2824 0.2583 -0.0087 -0.0208 -0.0059 232  ASP B OD1 
10504 O OD2 . ASP B 234  ? 0.2964 0.2634 0.2443 -0.0083 -0.0186 -0.0069 232  ASP B OD2 
10505 N N   . ALA B 235  ? 0.2494 0.1976 0.1815 -0.0153 -0.0251 0.0018  233  ALA B N   
10506 C CA  . ALA B 235  ? 0.2685 0.2128 0.1970 -0.0185 -0.0255 0.0042  233  ALA B CA  
10507 C C   . ALA B 235  ? 0.2725 0.2111 0.1944 -0.0197 -0.0280 0.0065  233  ALA B C   
10508 O O   . ALA B 235  ? 0.2775 0.2149 0.1945 -0.0231 -0.0276 0.0089  233  ALA B O   
10509 C CB  . ALA B 235  ? 0.2769 0.2178 0.2088 -0.0176 -0.0264 0.0036  233  ALA B CB  
10510 N N   . GLU B 236  ? 0.2697 0.2049 0.1916 -0.0169 -0.0308 0.0061  234  GLU B N   
10511 C CA  . GLU B 236  ? 0.2816 0.2112 0.1972 -0.0178 -0.0335 0.0083  234  GLU B CA  
10512 C C   . GLU B 236  ? 0.2829 0.2157 0.1936 -0.0199 -0.0321 0.0093  234  GLU B C   
10513 O O   . GLU B 236  ? 0.2848 0.2142 0.1891 -0.0226 -0.0328 0.0120  234  GLU B O   
10514 C CB  . GLU B 236  ? 0.2949 0.2215 0.2122 -0.0142 -0.0367 0.0075  234  GLU B CB  
10515 C CG  . GLU B 236  ? 0.3341 0.2539 0.2451 -0.0147 -0.0400 0.0100  234  GLU B CG  
10516 C CD  . GLU B 236  ? 0.4345 0.3517 0.3477 -0.0110 -0.0433 0.0093  234  GLU B CD  
10517 O OE1 . GLU B 236  ? 0.4753 0.3959 0.3951 -0.0082 -0.0430 0.0069  234  GLU B OE1 
10518 O OE2 . GLU B 236  ? 0.4299 0.3420 0.3382 -0.0110 -0.0463 0.0112  234  GLU B OE2 
10519 N N   . ARG B 237  ? 0.2712 0.2101 0.1842 -0.0185 -0.0301 0.0072  235  ARG B N   
10520 C CA  . ARG B 237  ? 0.2542 0.1963 0.1624 -0.0201 -0.0285 0.0079  235  ARG B CA  
10521 C C   . ARG B 237  ? 0.3044 0.2494 0.2102 -0.0237 -0.0256 0.0097  235  ARG B C   
10522 O O   . ARG B 237  ? 0.2846 0.2287 0.1841 -0.0263 -0.0255 0.0120  235  ARG B O   
10523 C CB  . ARG B 237  ? 0.3022 0.2497 0.2134 -0.0176 -0.0269 0.0050  235  ARG B CB  
10524 C CG  . ARG B 237  ? 0.3509 0.3015 0.2565 -0.0188 -0.0251 0.0054  235  ARG B CG  
10525 C CD  . ARG B 237  ? 0.4087 0.3653 0.3171 -0.0169 -0.0225 0.0026  235  ARG B CD  
10526 N NE  . ARG B 237  ? 0.4161 0.3751 0.3185 -0.0178 -0.0208 0.0030  235  ARG B NE  
10527 C CZ  . ARG B 237  ? 0.4301 0.3919 0.3317 -0.0158 -0.0197 0.0007  235  ARG B CZ  
10528 N NH1 . ARG B 237  ? 0.4557 0.4183 0.3624 -0.0131 -0.0201 -0.0021 235  ARG B NH1 
10529 N NH2 . ARG B 237  ? 0.4193 0.3830 0.3146 -0.0166 -0.0181 0.0012  235  ARG B NH2 
10530 N N   . TYR B 238  ? 0.2814 0.2301 0.1922 -0.0242 -0.0234 0.0088  236  TYR B N   
10531 C CA  . TYR B 238  ? 0.2730 0.2252 0.1821 -0.0278 -0.0208 0.0106  236  TYR B CA  
10532 C C   . TYR B 238  ? 0.2785 0.2246 0.1826 -0.0313 -0.0227 0.0140  236  TYR B C   
10533 O O   . TYR B 238  ? 0.2804 0.2281 0.1799 -0.0348 -0.0214 0.0164  236  TYR B O   
10534 C CB  . TYR B 238  ? 0.2637 0.2204 0.1793 -0.0277 -0.0186 0.0091  236  TYR B CB  
10535 C CG  . TYR B 238  ? 0.3493 0.3125 0.2695 -0.0247 -0.0163 0.0062  236  TYR B CG  
10536 C CD1 . TYR B 238  ? 0.4692 0.4362 0.3867 -0.0239 -0.0149 0.0056  236  TYR B CD1 
10537 C CD2 . TYR B 238  ? 0.3748 0.3399 0.3015 -0.0227 -0.0158 0.0040  236  TYR B CD2 
10538 C CE1 . TYR B 238  ? 0.5142 0.4861 0.4352 -0.0211 -0.0130 0.0028  236  TYR B CE1 
10539 C CE2 . TYR B 238  ? 0.4180 0.3883 0.3485 -0.0201 -0.0139 0.0015  236  TYR B CE2 
10540 C CZ  . TYR B 238  ? 0.5236 0.4971 0.4512 -0.0193 -0.0126 0.0009  236  TYR B CZ  
10541 O OH  . TYR B 238  ? 0.5391 0.5169 0.4701 -0.0166 -0.0109 -0.0017 236  TYR B OH  
10542 N N   . TYR B 239  ? 0.2678 0.2065 0.1723 -0.0303 -0.0259 0.0142  237  TYR B N   
10543 C CA  . TYR B 239  ? 0.2736 0.2049 0.1725 -0.0332 -0.0282 0.0173  237  TYR B CA  
10544 C C   . TYR B 239  ? 0.2893 0.2188 0.1811 -0.0346 -0.0292 0.0195  237  TYR B C   
10545 O O   . TYR B 239  ? 0.2912 0.2199 0.1778 -0.0387 -0.0287 0.0225  237  TYR B O   
10546 C CB  . TYR B 239  ? 0.2903 0.2137 0.1906 -0.0309 -0.0317 0.0168  237  TYR B CB  
10547 C CG  . TYR B 239  ? 0.3201 0.2347 0.2139 -0.0335 -0.0345 0.0200  237  TYR B CG  
10548 C CD1 . TYR B 239  ? 0.3314 0.2428 0.2240 -0.0368 -0.0345 0.0216  237  TYR B CD1 
10549 C CD2 . TYR B 239  ? 0.3587 0.2682 0.2471 -0.0329 -0.0372 0.0216  237  TYR B CD2 
10550 C CE1 . TYR B 239  ? 0.3059 0.2087 0.1921 -0.0394 -0.0372 0.0247  237  TYR B CE1 
10551 C CE2 . TYR B 239  ? 0.3683 0.2694 0.2503 -0.0354 -0.0399 0.0248  237  TYR B CE2 
10552 C CZ  . TYR B 239  ? 0.3721 0.2697 0.2531 -0.0386 -0.0398 0.0263  237  TYR B CZ  
10553 O OH  . TYR B 239  ? 0.4485 0.3370 0.3229 -0.0413 -0.0426 0.0294  237  TYR B OH  
10554 N N   . ARG B 240  ? 0.2998 0.2286 0.1912 -0.0314 -0.0307 0.0182  238  ARG B N   
10555 C CA  . ARG B 240  ? 0.3218 0.2484 0.2060 -0.0324 -0.0319 0.0201  238  ARG B CA  
10556 C C   . ARG B 240  ? 0.3182 0.2517 0.1994 -0.0349 -0.0284 0.0209  238  ARG B C   
10557 O O   . ARG B 240  ? 0.3023 0.2341 0.1766 -0.0378 -0.0286 0.0237  238  ARG B O   
10558 C CB  . ARG B 240  ? 0.3156 0.2410 0.2006 -0.0284 -0.0342 0.0182  238  ARG B CB  
10559 C CG  . ARG B 240  ? 0.3368 0.2556 0.2243 -0.0257 -0.0379 0.0178  238  ARG B CG  
10560 C CD  . ARG B 240  ? 0.3779 0.2883 0.2592 -0.0279 -0.0408 0.0212  238  ARG B CD  
10561 N NE  . ARG B 240  ? 0.3824 0.2865 0.2663 -0.0249 -0.0442 0.0208  238  ARG B NE  
10562 C CZ  . ARG B 240  ? 0.4752 0.3710 0.3550 -0.0258 -0.0471 0.0232  238  ARG B CZ  
10563 N NH1 . ARG B 240  ? 0.4419 0.3341 0.3148 -0.0300 -0.0471 0.0264  238  ARG B NH1 
10564 N NH2 . ARG B 240  ? 0.4658 0.3566 0.3483 -0.0223 -0.0500 0.0225  238  ARG B NH2 
10565 N N   . ASP B 241  ? 0.2886 0.2299 0.1747 -0.0338 -0.0250 0.0185  239  ASP B N   
10566 C CA  . ASP B 241  ? 0.3191 0.2677 0.2028 -0.0357 -0.0213 0.0190  239  ASP B CA  
10567 C C   . ASP B 241  ? 0.3080 0.2580 0.1899 -0.0405 -0.0198 0.0222  239  ASP B C   
10568 O O   . ASP B 241  ? 0.2969 0.2496 0.1734 -0.0433 -0.0182 0.0245  239  ASP B O   
10569 C CB  . ASP B 241  ? 0.3266 0.2829 0.2163 -0.0329 -0.0184 0.0157  239  ASP B CB  
10570 C CG  . ASP B 241  ? 0.3729 0.3288 0.2627 -0.0289 -0.0194 0.0129  239  ASP B CG  
10571 O OD1 . ASP B 241  ? 0.3548 0.3062 0.2392 -0.0286 -0.0218 0.0138  239  ASP B OD1 
10572 O OD2 . ASP B 241  ? 0.4425 0.4025 0.3376 -0.0262 -0.0179 0.0099  239  ASP B OD2 
10573 N N   . TYR B 242  ? 0.3072 0.2554 0.1931 -0.0416 -0.0203 0.0224  240  TYR B N   
10574 C CA  . TYR B 242  ? 0.3193 0.2677 0.2030 -0.0467 -0.0194 0.0256  240  TYR B CA  
10575 C C   . TYR B 242  ? 0.3261 0.2668 0.2021 -0.0496 -0.0222 0.0292  240  TYR B C   
10576 O O   . TYR B 242  ? 0.2911 0.2336 0.1625 -0.0540 -0.0210 0.0323  240  TYR B O   
10577 C CB  . TYR B 242  ? 0.2973 0.2439 0.1862 -0.0472 -0.0201 0.0250  240  TYR B CB  
10578 C CG  . TYR B 242  ? 0.2895 0.2446 0.1855 -0.0461 -0.0169 0.0226  240  TYR B CG  
10579 C CD1 . TYR B 242  ? 0.3336 0.2984 0.2303 -0.0474 -0.0131 0.0229  240  TYR B CD1 
10580 C CD2 . TYR B 242  ? 0.3102 0.2636 0.2120 -0.0437 -0.0178 0.0202  240  TYR B CD2 
10581 C CE1 . TYR B 242  ? 0.3533 0.3256 0.2565 -0.0462 -0.0104 0.0208  240  TYR B CE1 
10582 C CE2 . TYR B 242  ? 0.3371 0.2978 0.2451 -0.0427 -0.0151 0.0182  240  TYR B CE2 
10583 C CZ  . TYR B 242  ? 0.3480 0.3181 0.2568 -0.0439 -0.0115 0.0185  240  TYR B CZ  
10584 O OH  . TYR B 242  ? 0.3352 0.3125 0.2501 -0.0428 -0.0090 0.0166  240  TYR B OH  
10585 N N   . GLU B 243  ? 0.3335 0.2654 0.2081 -0.0473 -0.0261 0.0288  241  GLU B N   
10586 C CA  . GLU B 243  ? 0.3045 0.2280 0.1716 -0.0496 -0.0292 0.0321  241  GLU B CA  
10587 C C   . GLU B 243  ? 0.3304 0.2568 0.1911 -0.0510 -0.0280 0.0339  241  GLU B C   
10588 O O   . GLU B 243  ? 0.3089 0.2334 0.1635 -0.0554 -0.0281 0.0376  241  GLU B O   
10589 C CB  . GLU B 243  ? 0.3179 0.2330 0.1854 -0.0456 -0.0333 0.0309  241  GLU B CB  
10590 C CG  . GLU B 243  ? 0.3638 0.2696 0.2237 -0.0472 -0.0370 0.0341  241  GLU B CG  
10591 C CD  . GLU B 243  ? 0.4304 0.3294 0.2912 -0.0426 -0.0409 0.0327  241  GLU B CD  
10592 O OE1 . GLU B 243  ? 0.4254 0.3285 0.2908 -0.0385 -0.0406 0.0296  241  GLU B OE1 
10593 O OE2 . GLU B 243  ? 0.4688 0.3586 0.3260 -0.0431 -0.0443 0.0348  241  GLU B OE2 
10594 N N   . SER B 244  ? 0.3267 0.2576 0.1885 -0.0474 -0.0269 0.0313  242  SER B N   
10595 C CA  A SER B 244  ? 0.3243 0.2582 0.1798 -0.0483 -0.0256 0.0325  242  SER B CA  
10596 C CA  B SER B 244  ? 0.3246 0.2585 0.1800 -0.0483 -0.0256 0.0325  242  SER B CA  
10597 C C   . SER B 244  ? 0.3140 0.2561 0.1683 -0.0522 -0.0214 0.0343  242  SER B C   
10598 O O   . SER B 244  ? 0.3133 0.2555 0.1607 -0.0554 -0.0208 0.0374  242  SER B O   
10599 C CB  A SER B 244  ? 0.3235 0.2608 0.1810 -0.0436 -0.0252 0.0288  242  SER B CB  
10600 C CB  B SER B 244  ? 0.3243 0.2615 0.1815 -0.0437 -0.0252 0.0290  242  SER B CB  
10601 O OG  A SER B 244  ? 0.3579 0.2981 0.2091 -0.0441 -0.0238 0.0296  242  SER B OG  
10602 O OG  B SER B 244  ? 0.3449 0.2747 0.2014 -0.0408 -0.0294 0.0281  242  SER B OG  
10603 N N   . ALA B 245  ? 0.3045 0.2536 0.1655 -0.0519 -0.0184 0.0325  243  ALA B N   
10604 C CA  . ALA B 245  ? 0.3260 0.2839 0.1868 -0.0554 -0.0144 0.0342  243  ALA B CA  
10605 C C   . ALA B 245  ? 0.3173 0.2718 0.1742 -0.0613 -0.0152 0.0387  243  ALA B C   
10606 O O   . ALA B 245  ? 0.3264 0.2856 0.1789 -0.0650 -0.0130 0.0416  243  ALA B O   
10607 C CB  . ALA B 245  ? 0.3230 0.2885 0.1922 -0.0538 -0.0116 0.0315  243  ALA B CB  
10608 N N   . ILE B 246  ? 0.3089 0.2552 0.1669 -0.0623 -0.0185 0.0394  244  ILE B N   
10609 C CA  . ILE B 246  ? 0.3258 0.2678 0.1799 -0.0681 -0.0197 0.0436  244  ILE B CA  
10610 C C   . ILE B 246  ? 0.3380 0.2751 0.1829 -0.0706 -0.0212 0.0471  244  ILE B C   
10611 O O   . ILE B 246  ? 0.3487 0.2879 0.1893 -0.0758 -0.0200 0.0509  244  ILE B O   
10612 C CB  . ILE B 246  ? 0.2988 0.2318 0.1554 -0.0680 -0.0232 0.0433  244  ILE B CB  
10613 C CG1 . ILE B 246  ? 0.3315 0.2705 0.1964 -0.0672 -0.0211 0.0407  244  ILE B CG1 
10614 C CG2 . ILE B 246  ? 0.3211 0.2464 0.1714 -0.0737 -0.0255 0.0478  244  ILE B CG2 
10615 C CD1 . ILE B 246  ? 0.3416 0.2724 0.2096 -0.0657 -0.0242 0.0393  244  ILE B CD1 
10616 N N   . HIS B 247  ? 0.3276 0.2584 0.1693 -0.0670 -0.0240 0.0461  245  HIS B N   
10617 C CA  . HIS B 247  ? 0.3231 0.2495 0.1558 -0.0690 -0.0255 0.0493  245  HIS B CA  
10618 C C   . HIS B 247  ? 0.3356 0.2718 0.1651 -0.0709 -0.0212 0.0504  245  HIS B C   
10619 O O   . HIS B 247  ? 0.3578 0.2936 0.1808 -0.0756 -0.0208 0.0545  245  HIS B O   
10620 C CB  . HIS B 247  ? 0.3385 0.2581 0.1691 -0.0643 -0.0290 0.0475  245  HIS B CB  
10621 C CG  . HIS B 247  ? 0.3577 0.2661 0.1887 -0.0631 -0.0336 0.0477  245  HIS B CG  
10622 N ND1 . HIS B 247  ? 0.3702 0.2697 0.1953 -0.0670 -0.0365 0.0517  245  HIS B ND1 
10623 C CD2 . HIS B 247  ? 0.3796 0.2843 0.2160 -0.0584 -0.0359 0.0446  245  HIS B CD2 
10624 C CE1 . HIS B 247  ? 0.4202 0.3107 0.2469 -0.0644 -0.0403 0.0508  245  HIS B CE1 
10625 N NE2 . HIS B 247  ? 0.4094 0.3034 0.2432 -0.0592 -0.0400 0.0465  245  HIS B NE2 
10626 N N   . ALA B 248  ? 0.3164 0.2615 0.1504 -0.0673 -0.0180 0.0469  246  ALA B N   
10627 C CA  . ALA B 248  ? 0.3401 0.2948 0.1710 -0.0684 -0.0138 0.0477  246  ALA B CA  
10628 C C   . ALA B 248  ? 0.3184 0.2806 0.1508 -0.0735 -0.0105 0.0505  246  ALA B C   
10629 O O   . ALA B 248  ? 0.3522 0.3179 0.1788 -0.0774 -0.0086 0.0540  246  ALA B O   
10630 C CB  . ALA B 248  ? 0.3414 0.3031 0.1767 -0.0629 -0.0112 0.0430  246  ALA B CB  
10631 N N   . ILE B 249  ? 0.3339 0.2987 0.1740 -0.0738 -0.0098 0.0492  247  ILE B N   
10632 C CA  . ILE B 249  ? 0.3169 0.2894 0.1592 -0.0787 -0.0069 0.0518  247  ILE B CA  
10633 C C   . ILE B 249  ? 0.3495 0.3153 0.1858 -0.0851 -0.0092 0.0569  247  ILE B C   
10634 O O   . ILE B 249  ? 0.3545 0.3265 0.1882 -0.0902 -0.0068 0.0605  247  ILE B O   
10635 C CB  . ILE B 249  ? 0.3177 0.2935 0.1693 -0.0775 -0.0063 0.0492  247  ILE B CB  
10636 C CG1 . ILE B 249  ? 0.3334 0.3166 0.1905 -0.0715 -0.0036 0.0446  247  ILE B CG1 
10637 C CG2 . ILE B 249  ? 0.3240 0.3070 0.1778 -0.0832 -0.0040 0.0524  247  ILE B CG2 
10638 C CD1 . ILE B 249  ? 0.3221 0.3051 0.1877 -0.0688 -0.0043 0.0413  247  ILE B CD1 
10639 N N   . GLY B 250  ? 0.3347 0.2879 0.1688 -0.0850 -0.0140 0.0574  248  GLY B N   
10640 C CA  . GLY B 250  ? 0.3570 0.3021 0.1849 -0.0909 -0.0167 0.0621  248  GLY B CA  
10641 C C   . GLY B 250  ? 0.4056 0.3506 0.2245 -0.0937 -0.0162 0.0658  248  GLY B C   
10642 O O   . GLY B 250  ? 0.4045 0.3505 0.2192 -0.0999 -0.0155 0.0703  248  GLY B O   
10643 N N   . LYS B 251  ? 0.3862 0.3296 0.2016 -0.0893 -0.0167 0.0640  249  LYS B N   
10644 C CA  . LYS B 251  ? 0.4013 0.3447 0.2077 -0.0916 -0.0162 0.0673  249  LYS B CA  
10645 C C   . LYS B 251  ? 0.3911 0.3482 0.1976 -0.0942 -0.0107 0.0686  249  LYS B C   
10646 O O   . LYS B 251  ? 0.4066 0.3650 0.2067 -0.0995 -0.0097 0.0732  249  LYS B O   
10647 C CB  . LYS B 251  ? 0.4285 0.3677 0.2314 -0.0861 -0.0180 0.0647  249  LYS B CB  
10648 N N   . ALA B 252  ? 0.3688 0.3363 0.1824 -0.0907 -0.0070 0.0649  250  ALA B N   
10649 C CA  . ALA B 252  ? 0.3906 0.3719 0.2051 -0.0926 -0.0015 0.0660  250  ALA B CA  
10650 C C   . ALA B 252  ? 0.3956 0.3810 0.2121 -0.0995 -0.0004 0.0701  250  ALA B C   
10651 O O   . ALA B 252  ? 0.4032 0.3969 0.2166 -0.1036 0.0029  0.0735  250  ALA B O   
10652 C CB  . ALA B 252  ? 0.4092 0.3999 0.2314 -0.0869 0.0018  0.0610  250  ALA B CB  
10653 N N   . SER B 253  ? 0.3797 0.3596 0.2011 -0.1008 -0.0031 0.0698  251  SER B N   
10654 C CA  . SER B 253  ? 0.3988 0.3810 0.2215 -0.1078 -0.0028 0.0737  251  SER B CA  
10655 C C   . SER B 253  ? 0.4066 0.3840 0.2201 -0.1142 -0.0041 0.0794  251  SER B C   
10656 O O   . SER B 253  ? 0.4592 0.4446 0.2718 -0.1199 -0.0014 0.0833  251  SER B O   
10657 C CB  . SER B 253  ? 0.4070 0.3808 0.2345 -0.1080 -0.0065 0.0724  251  SER B CB  
10658 O OG  . SER B 253  ? 0.3867 0.3622 0.2150 -0.1150 -0.0065 0.0762  251  SER B OG  
10659 N N   . ALA B 254  ? 0.4003 0.3646 0.2069 -0.1133 -0.0083 0.0802  252  ALA B N   
10660 C CA  . ALA B 254  ? 0.4576 0.4160 0.2543 -0.1186 -0.0099 0.0855  252  ALA B CA  
10661 C C   . ALA B 254  ? 0.4948 0.4523 0.2908 -0.1269 -0.0106 0.0904  252  ALA B C   
10662 O O   . ALA B 254  ? 0.4886 0.4506 0.2795 -0.1327 -0.0087 0.0951  252  ALA B O   
10663 C CB  . ALA B 254  ? 0.4812 0.4487 0.2728 -0.1183 -0.0059 0.0867  252  ALA B CB  
10664 N N   . GLY B 255  ? 0.4833 0.4348 0.2841 -0.1275 -0.0133 0.0892  253  GLY B N   
10665 C CA  . GLY B 255  ? 0.5103 0.4584 0.3100 -0.1352 -0.0149 0.0935  253  GLY B CA  
10666 C C   . GLY B 255  ? 0.4767 0.4393 0.2826 -0.1395 -0.0107 0.0948  253  GLY B C   
10667 O O   . GLY B 255  ? 0.5150 0.4765 0.3199 -0.1466 -0.0118 0.0988  253  GLY B O   
10668 N N   . ARG B 256  ? 0.4486 0.4251 0.2614 -0.1352 -0.0062 0.0915  254  ARG B N   
10669 C CA  . ARG B 256  ? 0.4438 0.4348 0.2629 -0.1390 -0.0022 0.0927  254  ARG B CA  
10670 C C   . ARG B 256  ? 0.4588 0.4471 0.2844 -0.1409 -0.0043 0.0917  254  ARG B C   
10671 O O   . ARG B 256  ? 0.4646 0.4635 0.2949 -0.1455 -0.0020 0.0936  254  ARG B O   
10672 C CB  . ARG B 256  ? 0.4254 0.4311 0.2500 -0.1332 0.0030  0.0891  254  ARG B CB  
10673 C CG  . ARG B 256  ? 0.4583 0.4717 0.2770 -0.1337 0.0066  0.0915  254  ARG B CG  
10674 C CD  . ARG B 256  ? 0.4576 0.4846 0.2815 -0.1275 0.0116  0.0875  254  ARG B CD  
10675 N NE  . ARG B 256  ? 0.4346 0.4549 0.2584 -0.1194 0.0102  0.0822  254  ARG B NE  
10676 C CZ  . ARG B 256  ? 0.4166 0.4448 0.2457 -0.1128 0.0132  0.0775  254  ARG B CZ  
10677 N NH1 . ARG B 256  ? 0.3828 0.4259 0.2181 -0.1127 0.0178  0.0772  254  ARG B NH1 
10678 N NH2 . ARG B 256  ? 0.4253 0.4462 0.2535 -0.1062 0.0113  0.0732  254  ARG B NH2 
10679 N N   . GLY B 257  ? 0.4483 0.4234 0.2743 -0.1376 -0.0087 0.0888  255  GLY B N   
10680 C CA  . GLY B 257  ? 0.4386 0.4100 0.2697 -0.1394 -0.0110 0.0878  255  GLY B CA  
10681 C C   . GLY B 257  ? 0.4159 0.3970 0.2569 -0.1340 -0.0083 0.0829  255  GLY B C   
10682 O O   . GLY B 257  ? 0.4087 0.3996 0.2529 -0.1288 -0.0046 0.0802  255  GLY B O   
10683 N N   . ILE B 258  ? 0.4293 0.4072 0.2750 -0.1353 -0.0103 0.0817  256  ILE B N   
10684 C CA  . ILE B 258  ? 0.4009 0.3849 0.2555 -0.1296 -0.0088 0.0767  256  ILE B CA  
10685 C C   . ILE B 258  ? 0.3626 0.3645 0.2243 -0.1308 -0.0040 0.0770  256  ILE B C   
10686 O O   . ILE B 258  ? 0.3654 0.3741 0.2342 -0.1254 -0.0020 0.0728  256  ILE B O   
10687 C CB  . ILE B 258  ? 0.4359 0.4092 0.2925 -0.1299 -0.0129 0.0750  256  ILE B CB  
10688 C CG1 . ILE B 258  ? 0.4465 0.4201 0.3026 -0.1386 -0.0141 0.0792  256  ILE B CG1 
10689 C CG2 . ILE B 258  ? 0.4036 0.3596 0.2537 -0.1275 -0.0175 0.0743  256  ILE B CG2 
10690 C CD1 . ILE B 258  ? 0.4794 0.4433 0.3374 -0.1390 -0.0179 0.0773  256  ILE B CD1 
10691 N N   . TYR B 259  ? 0.3894 0.3993 0.2494 -0.1378 -0.0021 0.0818  257  TYR B N   
10692 C CA  . TYR B 259  ? 0.3965 0.4242 0.2636 -0.1390 0.0024  0.0823  257  TYR B CA  
10693 C C   . TYR B 259  ? 0.3618 0.4011 0.2280 -0.1359 0.0072  0.0823  257  TYR B C   
10694 O O   . TYR B 259  ? 0.3838 0.4336 0.2561 -0.1303 0.0107  0.0789  257  TYR B O   
10695 C CB  . TYR B 259  ? 0.3956 0.4271 0.2626 -0.1485 0.0018  0.0875  257  TYR B CB  
10696 C CG  . TYR B 259  ? 0.4147 0.4334 0.2813 -0.1516 -0.0032 0.0874  257  TYR B CG  
10697 C CD1 . TYR B 259  ? 0.4220 0.4415 0.2958 -0.1483 -0.0038 0.0835  257  TYR B CD1 
10698 C CD2 . TYR B 259  ? 0.4551 0.4603 0.3138 -0.1576 -0.0073 0.0911  257  TYR B CD2 
10699 C CE1 . TYR B 259  ? 0.4650 0.4725 0.3381 -0.1509 -0.0083 0.0831  257  TYR B CE1 
10700 C CE2 . TYR B 259  ? 0.4525 0.4452 0.3104 -0.1601 -0.0120 0.0907  257  TYR B CE2 
10701 C CZ  . TYR B 259  ? 0.4753 0.4693 0.3403 -0.1567 -0.0124 0.0866  257  TYR B CZ  
10702 O OH  . TYR B 259  ? 0.5073 0.4888 0.3710 -0.1589 -0.0169 0.0860  257  TYR B OH  
10703 N N   . GLU B 260  ? 0.3841 0.4214 0.2425 -0.1393 0.0075  0.0862  258  GLU B N   
10704 C CA  . GLU B 260  ? 0.4092 0.4564 0.2657 -0.1362 0.0119  0.0861  258  GLU B CA  
10705 C C   . GLU B 260  ? 0.4247 0.4659 0.2798 -0.1275 0.0116  0.0811  258  GLU B C   
10706 O O   . GLU B 260  ? 0.4348 0.4860 0.2930 -0.1220 0.0155  0.0782  258  GLU B O   
10707 C CB  . GLU B 260  ? 0.4373 0.4831 0.2855 -0.1422 0.0119  0.0915  258  GLU B CB  
10708 C CG  . GLU B 260  ? 0.4987 0.5540 0.3447 -0.1384 0.0163  0.0910  258  GLU B CG  
10709 C CD  . GLU B 260  ? 0.5410 0.5939 0.3808 -0.1423 0.0157  0.0947  258  GLU B CD  
10710 O OE1 . GLU B 260  ? 0.5777 0.6228 0.4157 -0.1482 0.0121  0.0978  258  GLU B OE1 
10711 O OE2 . GLU B 260  ? 0.5799 0.6383 0.4164 -0.1393 0.0189  0.0945  258  GLU B OE2 
10712 N N   . GLY B 261  ? 0.3917 0.4169 0.2425 -0.1261 0.0069  0.0800  259  GLY B N   
10713 C CA  . GLY B 261  ? 0.3801 0.3988 0.2285 -0.1188 0.0060  0.0760  259  GLY B CA  
10714 C C   . GLY B 261  ? 0.3870 0.4061 0.2431 -0.1121 0.0059  0.0703  259  GLY B C   
10715 O O   . GLY B 261  ? 0.3702 0.3918 0.2329 -0.1131 0.0056  0.0694  259  GLY B O   
10716 N N   . PRO B 262  ? 0.3542 0.3705 0.2092 -0.1054 0.0060  0.0666  260  PRO B N   
10717 C CA  . PRO B 262  ? 0.3595 0.3764 0.2214 -0.0987 0.0061  0.0612  260  PRO B CA  
10718 C C   . PRO B 262  ? 0.3597 0.3637 0.2229 -0.0978 0.0013  0.0595  260  PRO B C   
10719 O O   . PRO B 262  ? 0.3796 0.3720 0.2374 -0.1008 -0.0025 0.0618  260  PRO B O   
10720 C CB  . PRO B 262  ? 0.3617 0.3784 0.2202 -0.0927 0.0072  0.0584  260  PRO B CB  
10721 C CG  . PRO B 262  ? 0.3582 0.3667 0.2072 -0.0959 0.0051  0.0619  260  PRO B CG  
10722 C CD  . PRO B 262  ? 0.3751 0.3879 0.2221 -0.1037 0.0060  0.0672  260  PRO B CD  
10723 N N   . GLY B 263  ? 0.3218 0.3280 0.1925 -0.0935 0.0017  0.0554  261  GLY B N   
10724 C CA  . GLY B 263  ? 0.3168 0.3122 0.1896 -0.0914 -0.0022 0.0531  261  GLY B CA  
10725 C C   . GLY B 263  ? 0.3293 0.3247 0.2063 -0.0838 -0.0019 0.0479  261  GLY B C   
10726 O O   . GLY B 263  ? 0.3128 0.3156 0.1905 -0.0801 0.0011  0.0461  261  GLY B O   
10727 N N   . ILE B 264  ? 0.3112 0.2982 0.1909 -0.0816 -0.0050 0.0456  262  ILE B N   
10728 C CA  . ILE B 264  ? 0.3043 0.2908 0.1885 -0.0748 -0.0051 0.0409  262  ILE B CA  
10729 C C   . ILE B 264  ? 0.3023 0.2898 0.1936 -0.0742 -0.0054 0.0389  262  ILE B C   
10730 O O   . ILE B 264  ? 0.3078 0.2919 0.1992 -0.0786 -0.0071 0.0409  262  ILE B O   
10731 C CB  . ILE B 264  ? 0.3368 0.3115 0.2168 -0.0716 -0.0087 0.0397  262  ILE B CB  
10732 C CG1 . ILE B 264  ? 0.3203 0.2970 0.2041 -0.0649 -0.0080 0.0352  262  ILE B CG1 
10733 C CG2 . ILE B 264  ? 0.3473 0.3109 0.2270 -0.0730 -0.0128 0.0401  262  ILE B CG2 
10734 C CD1 . ILE B 264  ? 0.3571 0.3237 0.2376 -0.0615 -0.0115 0.0340  262  ILE B CD1 
10735 N N   . SER B 265  ? 0.2575 0.2500 0.1545 -0.0691 -0.0037 0.0350  263  SER B N   
10736 C CA  . SER B 265  ? 0.2745 0.2681 0.1784 -0.0675 -0.0039 0.0326  263  SER B CA  
10737 C C   . SER B 265  ? 0.2787 0.2661 0.1845 -0.0616 -0.0057 0.0288  263  SER B C   
10738 O O   . SER B 265  ? 0.3123 0.3001 0.2167 -0.0579 -0.0051 0.0272  263  SER B O   
10739 C CB  . SER B 265  ? 0.3113 0.3180 0.2209 -0.0668 0.0001  0.0317  263  SER B CB  
10740 O OG  . SER B 265  ? 0.3160 0.3291 0.2253 -0.0726 0.0015  0.0353  263  SER B OG  
10741 N N   . ILE B 266  ? 0.2721 0.2536 0.1808 -0.0610 -0.0080 0.0275  264  ILE B N   
10742 C CA  . ILE B 266  ? 0.2707 0.2465 0.1815 -0.0558 -0.0098 0.0241  264  ILE B CA  
10743 C C   . ILE B 266  ? 0.2878 0.2665 0.2055 -0.0538 -0.0091 0.0215  264  ILE B C   
10744 O O   . ILE B 266  ? 0.2650 0.2459 0.1847 -0.0571 -0.0088 0.0226  264  ILE B O   
10745 C CB  . ILE B 266  ? 0.3201 0.2833 0.2263 -0.0561 -0.0139 0.0250  264  ILE B CB  
10746 C CG1 . ILE B 266  ? 0.3265 0.2844 0.2323 -0.0600 -0.0158 0.0266  264  ILE B CG1 
10747 C CG2 . ILE B 266  ? 0.3271 0.2872 0.2262 -0.0579 -0.0147 0.0277  264  ILE B CG2 
10748 C CD1 . ILE B 266  ? 0.3511 0.2962 0.2535 -0.0590 -0.0199 0.0266  264  ILE B CD1 
10749 N N   . LYS B 267  ? 0.2931 0.2721 0.2145 -0.0486 -0.0089 0.0182  265  LYS B N   
10750 C CA  . LYS B 267  ? 0.2474 0.2280 0.1750 -0.0463 -0.0086 0.0156  265  LYS B CA  
10751 C C   . LYS B 267  ? 0.2494 0.2202 0.1768 -0.0438 -0.0118 0.0141  265  LYS B C   
10752 O O   . LYS B 267  ? 0.2616 0.2289 0.1876 -0.0407 -0.0130 0.0130  265  LYS B O   
10753 C CB  . LYS B 267  ? 0.3170 0.3059 0.2492 -0.0425 -0.0058 0.0131  265  LYS B CB  
10754 C CG  . LYS B 267  ? 0.3401 0.3395 0.2736 -0.0447 -0.0024 0.0144  265  LYS B CG  
10755 C CD  . LYS B 267  ? 0.3871 0.3942 0.3244 -0.0406 0.0004  0.0119  265  LYS B CD  
10756 C CE  . LYS B 267  ? 0.3348 0.3514 0.2712 -0.0422 0.0036  0.0135  265  LYS B CE  
10757 N NZ  . LYS B 267  ? 0.2922 0.3143 0.2309 -0.0465 0.0046  0.0158  265  LYS B NZ  
10758 N N   . LEU B 268  ? 0.2396 0.2061 0.1681 -0.0453 -0.0134 0.0142  266  LEU B N   
10759 C CA  . LEU B 268  ? 0.2539 0.2111 0.1818 -0.0429 -0.0163 0.0130  266  LEU B CA  
10760 C C   . LEU B 268  ? 0.2730 0.2318 0.2057 -0.0374 -0.0159 0.0097  266  LEU B C   
10761 O O   . LEU B 268  ? 0.2633 0.2159 0.1952 -0.0345 -0.0181 0.0087  266  LEU B O   
10762 C CB  . LEU B 268  ? 0.2477 0.2005 0.1760 -0.0451 -0.0177 0.0133  266  LEU B CB  
10763 C CG  . LEU B 268  ? 0.2663 0.2157 0.1893 -0.0509 -0.0188 0.0167  266  LEU B CG  
10764 C CD1 . LEU B 268  ? 0.2914 0.2347 0.2141 -0.0527 -0.0208 0.0166  266  LEU B CD1 
10765 C CD2 . LEU B 268  ? 0.3159 0.2581 0.2327 -0.0516 -0.0210 0.0187  266  LEU B CD2 
10766 N N   . SER B 269  ? 0.2541 0.2213 0.1918 -0.0358 -0.0132 0.0079  267  SER B N   
10767 C CA  . SER B 269  ? 0.2582 0.2267 0.2001 -0.0310 -0.0129 0.0050  267  SER B CA  
10768 C C   . SER B 269  ? 0.2598 0.2274 0.1996 -0.0286 -0.0134 0.0046  267  SER B C   
10769 O O   . SER B 269  ? 0.2869 0.2535 0.2294 -0.0249 -0.0140 0.0024  267  SER B O   
10770 C CB  . SER B 269  ? 0.2674 0.2446 0.2146 -0.0299 -0.0100 0.0034  267  SER B CB  
10771 O OG  . SER B 269  ? 0.2638 0.2479 0.2101 -0.0307 -0.0076 0.0042  267  SER B OG  
10772 N N   . ALA B 270  ? 0.2366 0.2047 0.1716 -0.0309 -0.0131 0.0066  268  ALA B N   
10773 C CA  . ALA B 270  ? 0.2581 0.2241 0.1899 -0.0290 -0.0141 0.0065  268  ALA B CA  
10774 C C   . ALA B 270  ? 0.2709 0.2280 0.2002 -0.0281 -0.0177 0.0070  268  ALA B C   
10775 O O   . ALA B 270  ? 0.2482 0.2031 0.1764 -0.0256 -0.0190 0.0062  268  ALA B O   
10776 C CB  . ALA B 270  ? 0.2870 0.2560 0.2137 -0.0319 -0.0128 0.0088  268  ALA B CB  
10777 N N   . LEU B 271  ? 0.2493 0.2007 0.1773 -0.0301 -0.0194 0.0083  269  LEU B N   
10778 C CA  . LEU B 271  ? 0.2645 0.2069 0.1887 -0.0296 -0.0228 0.0093  269  LEU B CA  
10779 C C   . LEU B 271  ? 0.2645 0.2027 0.1923 -0.0261 -0.0245 0.0073  269  LEU B C   
10780 O O   . LEU B 271  ? 0.2767 0.2074 0.2020 -0.0250 -0.0274 0.0080  269  LEU B O   
10781 C CB  . LEU B 271  ? 0.2612 0.1985 0.1801 -0.0341 -0.0239 0.0124  269  LEU B CB  
10782 C CG  . LEU B 271  ? 0.2730 0.2139 0.1873 -0.0377 -0.0225 0.0149  269  LEU B CG  
10783 C CD1 . LEU B 271  ? 0.3549 0.2912 0.2645 -0.0427 -0.0236 0.0181  269  LEU B CD1 
10784 C CD2 . LEU B 271  ? 0.3068 0.2459 0.2175 -0.0359 -0.0237 0.0152  269  LEU B CD2 
10785 N N   . HIS B 272  ? 0.2469 0.1898 0.1807 -0.0242 -0.0228 0.0050  270  HIS B N   
10786 C CA  . HIS B 272  ? 0.2655 0.2052 0.2030 -0.0207 -0.0242 0.0030  270  HIS B CA  
10787 C C   . HIS B 272  ? 0.2563 0.2030 0.2001 -0.0184 -0.0219 0.0005  270  HIS B C   
10788 O O   . HIS B 272  ? 0.2684 0.2206 0.2139 -0.0201 -0.0195 0.0003  270  HIS B O   
10789 C CB  . HIS B 272  ? 0.2666 0.2003 0.2028 -0.0220 -0.0254 0.0036  270  HIS B CB  
10790 C CG  . HIS B 272  ? 0.3022 0.2311 0.2405 -0.0181 -0.0273 0.0020  270  HIS B CG  
10791 N ND1 . HIS B 272  ? 0.2967 0.2293 0.2410 -0.0151 -0.0262 -0.0005 270  HIS B ND1 
10792 C CD2 . HIS B 272  ? 0.3207 0.2417 0.2562 -0.0165 -0.0303 0.0027  270  HIS B CD2 
10793 C CE1 . HIS B 272  ? 0.2860 0.2137 0.2311 -0.0119 -0.0281 -0.0013 270  HIS B CE1 
10794 N NE2 . HIS B 272  ? 0.3486 0.2692 0.2885 -0.0125 -0.0307 0.0005  270  HIS B NE2 
10795 N N   . PRO B 273  ? 0.2399 0.1868 0.1874 -0.0145 -0.0226 -0.0014 271  PRO B N   
10796 C CA  . PRO B 273  ? 0.2242 0.1774 0.1774 -0.0125 -0.0206 -0.0037 271  PRO B CA  
10797 C C   . PRO B 273  ? 0.2316 0.1855 0.1884 -0.0121 -0.0196 -0.0048 271  PRO B C   
10798 O O   . PRO B 273  ? 0.2561 0.2154 0.2172 -0.0110 -0.0176 -0.0063 271  PRO B O   
10799 C CB  . PRO B 273  ? 0.2467 0.1992 0.2021 -0.0090 -0.0221 -0.0049 271  PRO B CB  
10800 C CG  . PRO B 273  ? 0.2767 0.2219 0.2290 -0.0084 -0.0251 -0.0037 271  PRO B CG  
10801 C CD  . PRO B 273  ? 0.2637 0.2056 0.2100 -0.0121 -0.0255 -0.0013 271  PRO B CD  
10802 N N   . ARG B 274  ? 0.2348 0.1830 0.1896 -0.0130 -0.0210 -0.0040 272  ARG B N   
10803 C CA  . ARG B 274  ? 0.2438 0.1921 0.2012 -0.0128 -0.0202 -0.0051 272  ARG B CA  
10804 C C   . ARG B 274  ? 0.2476 0.1930 0.2011 -0.0168 -0.0204 -0.0035 272  ARG B C   
10805 O O   . ARG B 274  ? 0.2483 0.1879 0.2001 -0.0170 -0.0218 -0.0034 272  ARG B O   
10806 C CB  . ARG B 274  ? 0.2460 0.1897 0.2051 -0.0094 -0.0219 -0.0064 272  ARG B CB  
10807 C CG  . ARG B 274  ? 0.2520 0.1992 0.2158 -0.0056 -0.0217 -0.0080 272  ARG B CG  
10808 C CD  . ARG B 274  ? 0.2298 0.1845 0.1984 -0.0052 -0.0191 -0.0095 272  ARG B CD  
10809 N NE  . ARG B 274  ? 0.2456 0.2011 0.2161 -0.0055 -0.0179 -0.0103 272  ARG B NE  
10810 C CZ  . ARG B 274  ? 0.2491 0.2036 0.2225 -0.0029 -0.0180 -0.0117 272  ARG B CZ  
10811 N NH1 . ARG B 274  ? 0.2514 0.2042 0.2265 0.0002  -0.0194 -0.0123 272  ARG B NH1 
10812 N NH2 . ARG B 274  ? 0.2576 0.2129 0.2321 -0.0034 -0.0168 -0.0124 272  ARG B NH2 
10813 N N   . TYR B 275  ? 0.2218 0.1714 0.1736 -0.0200 -0.0190 -0.0020 273  TYR B N   
10814 C CA  . TYR B 275  ? 0.2534 0.2015 0.2019 -0.0244 -0.0190 -0.0002 273  TYR B CA  
10815 C C   . TYR B 275  ? 0.2728 0.2250 0.2250 -0.0250 -0.0174 -0.0013 273  TYR B C   
10816 O O   . TYR B 275  ? 0.2332 0.1931 0.1882 -0.0258 -0.0151 -0.0015 273  TYR B O   
10817 C CB  . TYR B 275  ? 0.2398 0.1916 0.1855 -0.0276 -0.0180 0.0020  273  TYR B CB  
10818 C CG  . TYR B 275  ? 0.2357 0.1875 0.1787 -0.0326 -0.0178 0.0041  273  TYR B CG  
10819 C CD1 . TYR B 275  ? 0.2633 0.2069 0.2023 -0.0347 -0.0202 0.0053  273  TYR B CD1 
10820 C CD2 . TYR B 275  ? 0.2490 0.2091 0.1933 -0.0350 -0.0153 0.0050  273  TYR B CD2 
10821 C CE1 . TYR B 275  ? 0.2630 0.2063 0.1994 -0.0397 -0.0203 0.0073  273  TYR B CE1 
10822 C CE2 . TYR B 275  ? 0.2463 0.2072 0.1885 -0.0399 -0.0152 0.0071  273  TYR B CE2 
10823 C CZ  . TYR B 275  ? 0.2473 0.1996 0.1855 -0.0424 -0.0178 0.0083  273  TYR B CZ  
10824 O OH  . TYR B 275  ? 0.2587 0.2114 0.1947 -0.0476 -0.0180 0.0105  273  TYR B OH  
10825 N N   . SER B 276  ? 0.2449 0.1918 0.1969 -0.0243 -0.0187 -0.0022 274  SER B N   
10826 C CA  . SER B 276  ? 0.2425 0.1926 0.1976 -0.0246 -0.0174 -0.0034 274  SER B CA  
10827 C C   . SER B 276  ? 0.2407 0.1827 0.1930 -0.0250 -0.0194 -0.0037 274  SER B C   
10828 O O   . SER B 276  ? 0.2514 0.1858 0.2008 -0.0234 -0.0215 -0.0037 274  SER B O   
10829 C CB  . SER B 276  ? 0.2941 0.2495 0.2550 -0.0206 -0.0158 -0.0057 274  SER B CB  
10830 O OG  . SER B 276  ? 0.3103 0.2607 0.2718 -0.0170 -0.0172 -0.0071 274  SER B OG  
10831 N N   . ARG B 277  ? 0.2361 0.1798 0.1893 -0.0270 -0.0188 -0.0040 275  ARG B N   
10832 C CA  . ARG B 277  ? 0.2399 0.1758 0.1900 -0.0274 -0.0206 -0.0046 275  ARG B CA  
10833 C C   . ARG B 277  ? 0.2619 0.1941 0.2136 -0.0223 -0.0211 -0.0069 275  ARG B C   
10834 O O   . ARG B 277  ? 0.2588 0.1823 0.2067 -0.0214 -0.0232 -0.0073 275  ARG B O   
10835 C CB  . ARG B 277  ? 0.2332 0.1726 0.1844 -0.0303 -0.0198 -0.0048 275  ARG B CB  
10836 C CG  . ARG B 277  ? 0.2622 0.1939 0.2103 -0.0305 -0.0215 -0.0058 275  ARG B CG  
10837 C CD  . ARG B 277  ? 0.2884 0.2097 0.2296 -0.0331 -0.0244 -0.0043 275  ARG B CD  
10838 N NE  . ARG B 277  ? 0.2734 0.1865 0.2110 -0.0331 -0.0262 -0.0055 275  ARG B NE  
10839 C CZ  . ARG B 277  ? 0.3029 0.2093 0.2393 -0.0287 -0.0272 -0.0074 275  ARG B CZ  
10840 N NH1 . ARG B 277  ? 0.2919 0.1996 0.2311 -0.0240 -0.0266 -0.0084 275  ARG B NH1 
10841 N NH2 . ARG B 277  ? 0.2780 0.1762 0.2101 -0.0291 -0.0289 -0.0084 275  ARG B NH2 
10842 N N   . ALA B 278  ? 0.2634 0.2021 0.2206 -0.0189 -0.0193 -0.0085 276  ALA B N   
10843 C CA  . ALA B 278  ? 0.2454 0.1817 0.2047 -0.0141 -0.0195 -0.0105 276  ALA B CA  
10844 C C   . ALA B 278  ? 0.2685 0.1986 0.2253 -0.0119 -0.0216 -0.0101 276  ALA B C   
10845 O O   . ALA B 278  ? 0.2776 0.2035 0.2346 -0.0084 -0.0224 -0.0114 276  ALA B O   
10846 C CB  . ALA B 278  ? 0.2650 0.2096 0.2305 -0.0114 -0.0173 -0.0119 276  ALA B CB  
10847 N N   . GLN B 279  ? 0.2629 0.1926 0.2174 -0.0138 -0.0223 -0.0082 277  GLN B N   
10848 C CA  . GLN B 279  ? 0.2602 0.1841 0.2120 -0.0120 -0.0245 -0.0075 277  GLN B CA  
10849 C C   . GLN B 279  ? 0.2653 0.1817 0.2103 -0.0156 -0.0266 -0.0053 277  GLN B C   
10850 O O   . GLN B 279  ? 0.2635 0.1772 0.2057 -0.0161 -0.0280 -0.0037 277  GLN B O   
10851 C CB  . GLN B 279  ? 0.2621 0.1913 0.2166 -0.0106 -0.0239 -0.0072 277  GLN B CB  
10852 C CG  . GLN B 279  ? 0.2526 0.1887 0.2135 -0.0073 -0.0220 -0.0092 277  GLN B CG  
10853 C CD  . GLN B 279  ? 0.2873 0.2202 0.2500 -0.0030 -0.0229 -0.0108 277  GLN B CD  
10854 O OE1 . GLN B 279  ? 0.3163 0.2425 0.2760 -0.0016 -0.0251 -0.0103 277  GLN B OE1 
10855 N NE2 . GLN B 279  ? 0.2434 0.1814 0.2112 -0.0007 -0.0212 -0.0125 277  GLN B NE2 
10856 N N   . ALA B 280  ? 0.2766 0.1891 0.2187 -0.0184 -0.0270 -0.0051 278  ALA B N   
10857 C CA  . ALA B 280  ? 0.2835 0.1892 0.2191 -0.0228 -0.0290 -0.0028 278  ALA B CA  
10858 C C   . ALA B 280  ? 0.3124 0.2085 0.2434 -0.0208 -0.0319 -0.0020 278  ALA B C   
10859 O O   . ALA B 280  ? 0.2933 0.1857 0.2198 -0.0237 -0.0333 0.0004  278  ALA B O   
10860 C CB  . ALA B 280  ? 0.2972 0.1992 0.2303 -0.0257 -0.0295 -0.0030 278  ALA B CB  
10861 N N   . ALA B 281  ? 0.2953 0.1877 0.2275 -0.0158 -0.0327 -0.0040 279  ALA B N   
10862 C CA  . ALA B 281  ? 0.3289 0.2124 0.2570 -0.0134 -0.0355 -0.0034 279  ALA B CA  
10863 C C   . ALA B 281  ? 0.3028 0.1890 0.2314 -0.0129 -0.0358 -0.0018 279  ALA B C   
10864 O O   . ALA B 281  ? 0.3180 0.1976 0.2413 -0.0143 -0.0381 0.0003  279  ALA B O   
10865 C CB  . ALA B 281  ? 0.3439 0.2245 0.2741 -0.0076 -0.0359 -0.0058 279  ALA B CB  
10866 N N   . ARG B 282  ? 0.2972 0.1929 0.2319 -0.0110 -0.0338 -0.0028 280  ARG B N   
10867 C CA  . ARG B 282  ? 0.2746 0.1733 0.2096 -0.0108 -0.0341 -0.0015 280  ARG B CA  
10868 C C   . ARG B 282  ? 0.2759 0.1756 0.2071 -0.0161 -0.0338 0.0010  280  ARG B C   
10869 O O   . ARG B 282  ? 0.2977 0.1951 0.2255 -0.0169 -0.0352 0.0029  280  ARG B O   
10870 C CB  . ARG B 282  ? 0.2830 0.1913 0.2250 -0.0081 -0.0319 -0.0032 280  ARG B CB  
10871 C CG  . ARG B 282  ? 0.2909 0.1994 0.2372 -0.0027 -0.0323 -0.0053 280  ARG B CG  
10872 C CD  . ARG B 282  ? 0.2967 0.2140 0.2490 -0.0007 -0.0307 -0.0064 280  ARG B CD  
10873 N NE  . ARG B 282  ? 0.2973 0.2149 0.2479 -0.0011 -0.0320 -0.0049 280  ARG B NE  
10874 C CZ  . ARG B 282  ? 0.2949 0.2193 0.2489 -0.0007 -0.0309 -0.0052 280  ARG B CZ  
10875 N NH1 . ARG B 282  ? 0.2861 0.2175 0.2454 0.0001  -0.0286 -0.0069 280  ARG B NH1 
10876 N NH2 . ARG B 282  ? 0.2958 0.2195 0.2473 -0.0011 -0.0324 -0.0039 280  ARG B NH2 
10877 N N   . VAL B 283  ? 0.2695 0.1732 0.2013 -0.0198 -0.0319 0.0011  281  VAL B N   
10878 C CA  . VAL B 283  ? 0.2765 0.1822 0.2050 -0.0250 -0.0314 0.0036  281  VAL B CA  
10879 C C   . VAL B 283  ? 0.2855 0.1811 0.2066 -0.0278 -0.0342 0.0061  281  VAL B C   
10880 O O   . VAL B 283  ? 0.3197 0.2142 0.2371 -0.0299 -0.0350 0.0084  281  VAL B O   
10881 C CB  . VAL B 283  ? 0.2659 0.1780 0.1968 -0.0281 -0.0290 0.0033  281  VAL B CB  
10882 C CG1 . VAL B 283  ? 0.3114 0.2242 0.2383 -0.0339 -0.0288 0.0062  281  VAL B CG1 
10883 C CG2 . VAL B 283  ? 0.2528 0.1753 0.1903 -0.0258 -0.0261 0.0015  281  VAL B CG2 
10884 N N   . MET B 284  ? 0.2898 0.1773 0.2081 -0.0278 -0.0359 0.0056  282  MET B N   
10885 C CA  . MET B 284  ? 0.3223 0.1993 0.2331 -0.0306 -0.0389 0.0079  282  MET B CA  
10886 C C   . MET B 284  ? 0.3424 0.2130 0.2504 -0.0273 -0.0413 0.0086  282  MET B C   
10887 O O   . MET B 284  ? 0.3596 0.2237 0.2615 -0.0300 -0.0434 0.0112  282  MET B O   
10888 C CB  . MET B 284  ? 0.3046 0.1737 0.2128 -0.0311 -0.0403 0.0069  282  MET B CB  
10889 C CG  . MET B 284  ? 0.3094 0.1836 0.2193 -0.0350 -0.0384 0.0066  282  MET B CG  
10890 S SD  . MET B 284  ? 0.3594 0.2385 0.2669 -0.0426 -0.0376 0.0102  282  MET B SD  
10891 C CE  . MET B 284  ? 0.3683 0.2327 0.2661 -0.0466 -0.0416 0.0129  282  MET B CE  
10892 N N   . GLY B 285  ? 0.2955 0.1680 0.2079 -0.0215 -0.0412 0.0063  283  GLY B N   
10893 C CA  . GLY B 285  ? 0.3460 0.2128 0.2564 -0.0179 -0.0438 0.0068  283  GLY B CA  
10894 C C   . GLY B 285  ? 0.3242 0.1962 0.2352 -0.0180 -0.0435 0.0082  283  GLY B C   
10895 O O   . GLY B 285  ? 0.3548 0.2208 0.2615 -0.0173 -0.0461 0.0100  283  GLY B O   
10896 N N   . GLU B 286  ? 0.2958 0.1784 0.2117 -0.0187 -0.0406 0.0075  284  GLU B N   
10897 C CA  . GLU B 286  ? 0.2926 0.1807 0.2096 -0.0181 -0.0402 0.0081  284  GLU B CA  
10898 C C   . GLU B 286  ? 0.3312 0.2245 0.2463 -0.0231 -0.0383 0.0100  284  GLU B C   
10899 O O   . GLU B 286  ? 0.3535 0.2464 0.2651 -0.0242 -0.0391 0.0119  284  GLU B O   
10900 C CB  . GLU B 286  ? 0.3225 0.2187 0.2470 -0.0139 -0.0384 0.0053  284  GLU B CB  
10901 C CG  . GLU B 286  ? 0.3201 0.2129 0.2476 -0.0090 -0.0397 0.0034  284  GLU B CG  
10902 C CD  . GLU B 286  ? 0.3335 0.2346 0.2686 -0.0055 -0.0378 0.0008  284  GLU B CD  
10903 O OE1 . GLU B 286  ? 0.3220 0.2305 0.2596 -0.0064 -0.0361 0.0007  284  GLU B OE1 
10904 O OE2 . GLU B 286  ? 0.3615 0.2617 0.2998 -0.0020 -0.0379 -0.0010 284  GLU B OE2 
10905 N N   . LEU B 287  ? 0.2967 0.1953 0.2139 -0.0258 -0.0358 0.0095  285  LEU B N   
10906 C CA  . LEU B 287  ? 0.2934 0.1980 0.2094 -0.0303 -0.0337 0.0112  285  LEU B CA  
10907 C C   . LEU B 287  ? 0.3227 0.2209 0.2316 -0.0353 -0.0352 0.0145  285  LEU B C   
10908 O O   . LEU B 287  ? 0.3052 0.2047 0.2105 -0.0379 -0.0351 0.0168  285  LEU B O   
10909 C CB  . LEU B 287  ? 0.2951 0.2079 0.2163 -0.0312 -0.0306 0.0096  285  LEU B CB  
10910 C CG  . LEU B 287  ? 0.3826 0.3056 0.3058 -0.0331 -0.0275 0.0100  285  LEU B CG  
10911 C CD1 . LEU B 287  ? 0.3281 0.2580 0.2566 -0.0334 -0.0250 0.0083  285  LEU B CD1 
10912 C CD2 . LEU B 287  ? 0.3733 0.2962 0.2913 -0.0382 -0.0274 0.0132  285  LEU B CD2 
10913 N N   . LEU B 288  ? 0.3283 0.2198 0.2351 -0.0369 -0.0366 0.0147  286  LEU B N   
10914 C CA  . LEU B 288  ? 0.3127 0.1977 0.2126 -0.0423 -0.0382 0.0179  286  LEU B CA  
10915 C C   . LEU B 288  ? 0.3443 0.2225 0.2381 -0.0426 -0.0408 0.0204  286  LEU B C   
10916 O O   . LEU B 288  ? 0.3279 0.2065 0.2173 -0.0474 -0.0406 0.0234  286  LEU B O   
10917 C CB  . LEU B 288  ? 0.3292 0.2059 0.2273 -0.0430 -0.0400 0.0173  286  LEU B CB  
10918 C CG  . LEU B 288  ? 0.3781 0.2456 0.2684 -0.0483 -0.0425 0.0205  286  LEU B CG  
10919 C CD1 . LEU B 288  ? 0.3754 0.2499 0.2650 -0.0547 -0.0405 0.0231  286  LEU B CD1 
10920 C CD2 . LEU B 288  ? 0.4275 0.2859 0.3157 -0.0481 -0.0445 0.0194  286  LEU B CD2 
10921 N N   . PRO B 289  ? 0.3642 0.2365 0.2574 -0.0379 -0.0431 0.0195  287  PRO B N   
10922 C CA  . PRO B 289  ? 0.3662 0.2326 0.2534 -0.0383 -0.0456 0.0221  287  PRO B CA  
10923 C C   . PRO B 289  ? 0.3441 0.2184 0.2311 -0.0398 -0.0438 0.0234  287  PRO B C   
10924 O O   . PRO B 289  ? 0.3542 0.2249 0.2351 -0.0429 -0.0450 0.0265  287  PRO B O   
10925 C CB  . PRO B 289  ? 0.3752 0.2366 0.2639 -0.0320 -0.0479 0.0203  287  PRO B CB  
10926 C CG  . PRO B 289  ? 0.3960 0.2556 0.2882 -0.0297 -0.0477 0.0176  287  PRO B CG  
10927 C CD  . PRO B 289  ? 0.3368 0.2064 0.2338 -0.0322 -0.0440 0.0165  287  PRO B CD  
10928 N N   . ARG B 290  ? 0.3253 0.2100 0.2185 -0.0377 -0.0408 0.0211  288  ARG B N   
10929 C CA  . ARG B 290  ? 0.3383 0.2304 0.2310 -0.0391 -0.0389 0.0221  288  ARG B CA  
10930 C C   . ARG B 290  ? 0.3205 0.2165 0.2105 -0.0451 -0.0369 0.0246  288  ARG B C   
10931 O O   . ARG B 290  ? 0.3079 0.2044 0.1931 -0.0479 -0.0368 0.0272  288  ARG B O   
10932 C CB  . ARG B 290  ? 0.3259 0.2275 0.2257 -0.0353 -0.0364 0.0189  288  ARG B CB  
10933 C CG  . ARG B 290  ? 0.3406 0.2394 0.2430 -0.0297 -0.0385 0.0169  288  ARG B CG  
10934 C CD  . ARG B 290  ? 0.4106 0.3178 0.3205 -0.0264 -0.0362 0.0136  288  ARG B CD  
10935 N NE  . ARG B 290  ? 0.4800 0.3850 0.3932 -0.0213 -0.0381 0.0118  288  ARG B NE  
10936 C CZ  . ARG B 290  ? 0.4557 0.3648 0.3755 -0.0181 -0.0369 0.0089  288  ARG B CZ  
10937 N NH1 . ARG B 290  ? 0.4013 0.3165 0.3250 -0.0191 -0.0340 0.0076  288  ARG B NH1 
10938 N NH2 . ARG B 290  ? 0.4899 0.3972 0.4125 -0.0137 -0.0388 0.0076  288  ARG B NH2 
10939 N N   . VAL B 291  ? 0.3109 0.2096 0.2038 -0.0472 -0.0354 0.0240  289  VAL B N   
10940 C CA  . VAL B 291  ? 0.2828 0.1857 0.1737 -0.0531 -0.0335 0.0265  289  VAL B CA  
10941 C C   . VAL B 291  ? 0.2930 0.1867 0.1759 -0.0575 -0.0362 0.0302  289  VAL B C   
10942 O O   . VAL B 291  ? 0.3307 0.2272 0.2098 -0.0619 -0.0353 0.0332  289  VAL B O   
10943 C CB  . VAL B 291  ? 0.3162 0.2233 0.2118 -0.0545 -0.0319 0.0251  289  VAL B CB  
10944 C CG1 . VAL B 291  ? 0.3312 0.2431 0.2249 -0.0609 -0.0302 0.0280  289  VAL B CG1 
10945 C CG2 . VAL B 291  ? 0.3250 0.2414 0.2281 -0.0503 -0.0291 0.0217  289  VAL B CG2 
10946 N N   . LYS B 292  ? 0.3208 0.2032 0.2009 -0.0564 -0.0397 0.0302  290  LYS B N   
10947 C CA  . LYS B 292  ? 0.3278 0.2000 0.1998 -0.0603 -0.0426 0.0337  290  LYS B CA  
10948 C C   . LYS B 292  ? 0.3685 0.2398 0.2357 -0.0605 -0.0434 0.0360  290  LYS B C   
10949 O O   . LYS B 292  ? 0.3492 0.2190 0.2107 -0.0656 -0.0437 0.0397  290  LYS B O   
10950 C CB  . LYS B 292  ? 0.3526 0.2123 0.2224 -0.0577 -0.0463 0.0328  290  LYS B CB  
10951 C CG  . LYS B 292  ? 0.4204 0.2678 0.2813 -0.0619 -0.0497 0.0364  290  LYS B CG  
10952 C CD  . LYS B 292  ? 0.4205 0.2611 0.2765 -0.0593 -0.0525 0.0378  290  LYS B CD  
10953 C CE  . LYS B 292  ? 0.4494 0.2784 0.2961 -0.0642 -0.0557 0.0420  290  LYS B CE  
10954 N NZ  . LYS B 292  ? 0.4865 0.3037 0.3306 -0.0640 -0.0586 0.0413  290  LYS B NZ  
10955 N N   . ALA B 293  ? 0.3417 0.2142 0.2111 -0.0550 -0.0438 0.0340  291  ALA B N   
10956 C CA  . ALA B 293  ? 0.3596 0.2314 0.2244 -0.0548 -0.0447 0.0360  291  ALA B CA  
10957 C C   . ALA B 293  ? 0.3636 0.2451 0.2275 -0.0587 -0.0413 0.0377  291  ALA B C   
10958 O O   . ALA B 293  ? 0.3402 0.2194 0.1976 -0.0621 -0.0420 0.0411  291  ALA B O   
10959 C CB  . ALA B 293  ? 0.3577 0.2307 0.2262 -0.0483 -0.0454 0.0331  291  ALA B CB  
10960 N N   . LEU B 294  ? 0.3399 0.2324 0.2103 -0.0581 -0.0376 0.0354  292  LEU B N   
10961 C CA  . LEU B 294  ? 0.3290 0.2313 0.1989 -0.0614 -0.0342 0.0369  292  LEU B CA  
10962 C C   . LEU B 294  ? 0.3335 0.2350 0.1994 -0.0682 -0.0339 0.0406  292  LEU B C   
10963 O O   . LEU B 294  ? 0.3485 0.2526 0.2097 -0.0719 -0.0328 0.0436  292  LEU B O   
10964 C CB  . LEU B 294  ? 0.3140 0.2277 0.1918 -0.0590 -0.0305 0.0336  292  LEU B CB  
10965 C CG  . LEU B 294  ? 0.3146 0.2303 0.1967 -0.0527 -0.0305 0.0300  292  LEU B CG  
10966 C CD1 . LEU B 294  ? 0.3125 0.2379 0.2020 -0.0507 -0.0271 0.0270  292  LEU B CD1 
10967 C CD2 . LEU B 294  ? 0.3041 0.2208 0.1819 -0.0515 -0.0306 0.0308  292  LEU B CD2 
10968 N N   . ALA B 295  ? 0.3433 0.2411 0.2108 -0.0701 -0.0348 0.0404  293  ALA B N   
10969 C CA  . ALA B 295  ? 0.3661 0.2628 0.2300 -0.0771 -0.0348 0.0440  293  ALA B CA  
10970 C C   . ALA B 295  ? 0.3761 0.2627 0.2310 -0.0803 -0.0379 0.0479  293  ALA B C   
10971 O O   . ALA B 295  ? 0.3591 0.2478 0.2097 -0.0862 -0.0371 0.0516  293  ALA B O   
10972 C CB  . ALA B 295  ? 0.3447 0.2379 0.2114 -0.0782 -0.0358 0.0428  293  ALA B CB  
10973 N N   . LEU B 296  ? 0.3827 0.2587 0.2346 -0.0765 -0.0414 0.0472  294  LEU B N   
10974 C CA  . LEU B 296  ? 0.4065 0.2721 0.2496 -0.0791 -0.0447 0.0509  294  LEU B CA  
10975 C C   . LEU B 296  ? 0.4184 0.2896 0.2578 -0.0804 -0.0431 0.0532  294  LEU B C   
10976 O O   . LEU B 296  ? 0.4196 0.2873 0.2521 -0.0856 -0.0439 0.0574  294  LEU B O   
10977 C CB  . LEU B 296  ? 0.4135 0.2674 0.2549 -0.0738 -0.0487 0.0494  294  LEU B CB  
10978 C CG  . LEU B 296  ? 0.4708 0.3125 0.3032 -0.0754 -0.0527 0.0529  294  LEU B CG  
10979 C CD1 . LEU B 296  ? 0.4848 0.3196 0.3113 -0.0825 -0.0541 0.0567  294  LEU B CD1 
10980 C CD2 . LEU B 296  ? 0.4972 0.3288 0.3296 -0.0692 -0.0564 0.0508  294  LEU B CD2 
10981 N N   . LEU B 297  ? 0.3909 0.2706 0.2345 -0.0759 -0.0408 0.0505  295  LEU B N   
10982 C CA  . LEU B 297  ? 0.3908 0.2768 0.2310 -0.0770 -0.0388 0.0523  295  LEU B CA  
10983 C C   . LEU B 297  ? 0.3846 0.2800 0.2246 -0.0829 -0.0352 0.0547  295  LEU B C   
10984 O O   . LEU B 297  ? 0.3788 0.2747 0.2126 -0.0871 -0.0348 0.0584  295  LEU B O   
10985 C CB  . LEU B 297  ? 0.3487 0.2417 0.1937 -0.0710 -0.0371 0.0484  295  LEU B CB  
10986 C CG  . LEU B 297  ? 0.4466 0.3323 0.2907 -0.0654 -0.0405 0.0467  295  LEU B CG  
10987 C CD1 . LEU B 297  ? 0.4222 0.3161 0.2727 -0.0600 -0.0385 0.0425  295  LEU B CD1 
10988 C CD2 . LEU B 297  ? 0.4289 0.3087 0.2644 -0.0670 -0.0428 0.0501  295  LEU B CD2 
10989 N N   . ALA B 298  ? 0.3671 0.2708 0.2141 -0.0832 -0.0324 0.0527  296  ALA B N   
10990 C CA  . ALA B 298  ? 0.3579 0.2713 0.2056 -0.0886 -0.0290 0.0550  296  ALA B CA  
10991 C C   . ALA B 298  ? 0.4099 0.3164 0.2514 -0.0957 -0.0310 0.0597  296  ALA B C   
10992 O O   . ALA B 298  ? 0.3975 0.3095 0.2356 -0.1009 -0.0291 0.0634  296  ALA B O   
10993 C CB  . ALA B 298  ? 0.3535 0.2753 0.2098 -0.0876 -0.0264 0.0521  296  ALA B CB  
10994 N N   . LYS B 299  ? 0.3797 0.2742 0.2194 -0.0961 -0.0350 0.0598  297  LYS B N   
10995 C CA  . LYS B 299  ? 0.4276 0.3136 0.2608 -0.1028 -0.0375 0.0642  297  LYS B CA  
10996 C C   . LYS B 299  ? 0.4544 0.3350 0.2789 -0.1050 -0.0390 0.0680  297  LYS B C   
10997 O O   . LYS B 299  ? 0.4608 0.3422 0.2804 -0.1117 -0.0386 0.0725  297  LYS B O   
10998 C CB  . LYS B 299  ? 0.4473 0.3203 0.2800 -0.1016 -0.0416 0.0629  297  LYS B CB  
10999 C CG  . LYS B 299  ? 0.4887 0.3515 0.3145 -0.1084 -0.0446 0.0670  297  LYS B CG  
11000 C CD  . LYS B 299  ? 0.5068 0.3548 0.3244 -0.1075 -0.0490 0.0689  297  LYS B CD  
11001 C CE  . LYS B 299  ? 0.5335 0.3702 0.3441 -0.1144 -0.0523 0.0728  297  LYS B CE  
11002 N NZ  . LYS B 299  ? 0.5713 0.3949 0.3728 -0.1146 -0.0562 0.0758  297  LYS B NZ  
11003 N N   . ASN B 300  ? 0.4399 0.3151 0.2622 -0.0995 -0.0409 0.0665  298  ASN B N   
11004 C CA  . ASN B 300  ? 0.4403 0.3097 0.2539 -0.1012 -0.0426 0.0701  298  ASN B CA  
11005 C C   . ASN B 300  ? 0.4505 0.3318 0.2626 -0.1043 -0.0386 0.0724  298  ASN B C   
11006 O O   . ASN B 300  ? 0.4801 0.3582 0.2845 -0.1089 -0.0393 0.0768  298  ASN B O   
11007 C CB  . ASN B 300  ? 0.4803 0.3430 0.2929 -0.0943 -0.0454 0.0677  298  ASN B CB  
11008 C CG  . ASN B 300  ? 0.5053 0.3547 0.3175 -0.0916 -0.0498 0.0665  298  ASN B CG  
11009 O OD1 . ASN B 300  ? 0.5473 0.3891 0.3569 -0.0957 -0.0518 0.0684  298  ASN B OD1 
11010 N ND2 . ASN B 300  ? 0.5819 0.4282 0.3965 -0.0846 -0.0515 0.0632  298  ASN B ND2 
11011 N N   . TYR B 301  ? 0.3934 0.2882 0.2124 -0.1019 -0.0343 0.0695  299  TYR B N   
11012 C CA  . TYR B 301  ? 0.4330 0.3398 0.2509 -0.1046 -0.0300 0.0714  299  TYR B CA  
11013 C C   . TYR B 301  ? 0.3862 0.3012 0.2063 -0.1110 -0.0273 0.0739  299  TYR B C   
11014 O O   . TYR B 301  ? 0.3990 0.3246 0.2183 -0.1138 -0.0236 0.0759  299  TYR B O   
11015 C CB  . TYR B 301  ? 0.3894 0.3066 0.2129 -0.0985 -0.0267 0.0670  299  TYR B CB  
11016 C CG  . TYR B 301  ? 0.3912 0.3033 0.2115 -0.0930 -0.0286 0.0652  299  TYR B CG  
11017 C CD1 . TYR B 301  ? 0.3982 0.3082 0.2103 -0.0945 -0.0291 0.0682  299  TYR B CD1 
11018 C CD2 . TYR B 301  ? 0.3842 0.2939 0.2098 -0.0864 -0.0300 0.0606  299  TYR B CD2 
11019 C CE1 . TYR B 301  ? 0.4051 0.3106 0.2143 -0.0895 -0.0311 0.0665  299  TYR B CE1 
11020 C CE2 . TYR B 301  ? 0.4221 0.3277 0.2453 -0.0816 -0.0319 0.0591  299  TYR B CE2 
11021 C CZ  . TYR B 301  ? 0.3823 0.2857 0.1972 -0.0832 -0.0326 0.0620  299  TYR B CZ  
11022 O OH  . TYR B 301  ? 0.4142 0.3136 0.2267 -0.0786 -0.0347 0.0604  299  TYR B OH  
11023 N N   . ASP B 302  ? 0.3875 0.2980 0.2105 -0.1134 -0.0290 0.0738  300  ASP B N   
11024 C CA  . ASP B 302  ? 0.4145 0.3332 0.2412 -0.1191 -0.0268 0.0756  300  ASP B CA  
11025 C C   . ASP B 302  ? 0.3964 0.3321 0.2304 -0.1170 -0.0214 0.0733  300  ASP B C   
11026 O O   . ASP B 302  ? 0.4240 0.3704 0.2581 -0.1213 -0.0181 0.0761  300  ASP B O   
11027 C CB  . ASP B 302  ? 0.4447 0.3615 0.2642 -0.1275 -0.0273 0.0816  300  ASP B CB  
11028 C CG  . ASP B 302  ? 0.4714 0.3914 0.2939 -0.1339 -0.0270 0.0836  300  ASP B CG  
11029 O OD1 . ASP B 302  ? 0.4971 0.4138 0.3245 -0.1321 -0.0285 0.0807  300  ASP B OD1 
11030 O OD2 . ASP B 302  ? 0.4997 0.4262 0.3199 -0.1407 -0.0252 0.0880  300  ASP B OD2 
11031 N N   . ILE B 303  ? 0.3605 0.2986 0.2008 -0.1101 -0.0207 0.0682  301  ILE B N   
11032 C CA  . ILE B 303  ? 0.3628 0.3155 0.2109 -0.1076 -0.0162 0.0656  301  ILE B CA  
11033 C C   . ILE B 303  ? 0.3755 0.3282 0.2308 -0.1064 -0.0168 0.0627  301  ILE B C   
11034 O O   . ILE B 303  ? 0.3821 0.3232 0.2366 -0.1057 -0.0206 0.0618  301  ILE B O   
11035 C CB  . ILE B 303  ? 0.3369 0.2939 0.1862 -0.1006 -0.0142 0.0620  301  ILE B CB  
11036 C CG1 . ILE B 303  ? 0.3879 0.3363 0.2399 -0.0943 -0.0171 0.0577  301  ILE B CG1 
11037 C CG2 . ILE B 303  ? 0.3342 0.2893 0.1754 -0.1016 -0.0143 0.0647  301  ILE B CG2 
11038 C CD1 . ILE B 303  ? 0.3798 0.3326 0.2338 -0.0875 -0.0155 0.0539  301  ILE B CD1 
11039 N N   . GLY B 304  ? 0.3636 0.3294 0.2259 -0.1059 -0.0130 0.0613  302  GLY B N   
11040 C CA  . GLY B 304  ? 0.3627 0.3298 0.2322 -0.1040 -0.0132 0.0582  302  GLY B CA  
11041 C C   . GLY B 304  ? 0.3644 0.3295 0.2378 -0.0960 -0.0135 0.0531  302  GLY B C   
11042 O O   . GLY B 304  ? 0.3519 0.3213 0.2254 -0.0917 -0.0116 0.0514  302  GLY B O   
11043 N N   . LEU B 305  ? 0.3155 0.2738 0.1920 -0.0942 -0.0160 0.0507  303  LEU B N   
11044 C CA  . LEU B 305  ? 0.3443 0.3017 0.2257 -0.0870 -0.0161 0.0459  303  LEU B CA  
11045 C C   . LEU B 305  ? 0.3560 0.3176 0.2444 -0.0869 -0.0153 0.0438  303  LEU B C   
11046 O O   . LEU B 305  ? 0.3713 0.3263 0.2589 -0.0900 -0.0178 0.0447  303  LEU B O   
11047 C CB  . LEU B 305  ? 0.3557 0.2991 0.2333 -0.0840 -0.0202 0.0448  303  LEU B CB  
11048 C CG  . LEU B 305  ? 0.3622 0.3042 0.2448 -0.0768 -0.0206 0.0401  303  LEU B CG  
11049 C CD1 . LEU B 305  ? 0.3701 0.3045 0.2485 -0.0730 -0.0229 0.0394  303  LEU B CD1 
11050 C CD2 . LEU B 305  ? 0.4092 0.3455 0.2950 -0.0762 -0.0227 0.0383  303  LEU B CD2 
11051 N N   . ASN B 306  ? 0.3210 0.2932 0.2157 -0.0832 -0.0120 0.0411  304  ASN B N   
11052 C CA  . ASN B 306  ? 0.3396 0.3182 0.2411 -0.0834 -0.0108 0.0396  304  ASN B CA  
11053 C C   . ASN B 306  ? 0.3073 0.2842 0.2137 -0.0769 -0.0111 0.0350  304  ASN B C   
11054 O O   . ASN B 306  ? 0.2921 0.2717 0.1998 -0.0719 -0.0097 0.0327  304  ASN B O   
11055 C CB  . ASN B 306  ? 0.3471 0.3406 0.2523 -0.0848 -0.0065 0.0406  304  ASN B CB  
11056 C CG  . ASN B 306  ? 0.3293 0.3303 0.2421 -0.0833 -0.0049 0.0383  304  ASN B CG  
11057 O OD1 . ASN B 306  ? 0.3503 0.3551 0.2676 -0.0776 -0.0034 0.0348  304  ASN B OD1 
11058 N ND2 . ASN B 306  ? 0.3435 0.3463 0.2577 -0.0884 -0.0056 0.0403  304  ASN B ND2 
11059 N N   . ILE B 307  ? 0.2903 0.2630 0.1995 -0.0770 -0.0128 0.0336  305  ILE B N   
11060 C CA  . ILE B 307  ? 0.2922 0.2643 0.2065 -0.0713 -0.0129 0.0295  305  ILE B CA  
11061 C C   . ILE B 307  ? 0.2953 0.2797 0.2164 -0.0704 -0.0095 0.0281  305  ILE B C   
11062 O O   . ILE B 307  ? 0.2713 0.2592 0.1946 -0.0741 -0.0093 0.0292  305  ILE B O   
11063 C CB  . ILE B 307  ? 0.3084 0.2697 0.2219 -0.0713 -0.0163 0.0285  305  ILE B CB  
11064 C CG1 . ILE B 307  ? 0.3285 0.2774 0.2355 -0.0710 -0.0196 0.0295  305  ILE B CG1 
11065 C CG2 . ILE B 307  ? 0.2920 0.2547 0.2116 -0.0658 -0.0158 0.0244  305  ILE B CG2 
11066 C CD1 . ILE B 307  ? 0.3315 0.2690 0.2367 -0.0713 -0.0231 0.0289  305  ILE B CD1 
11067 N N   . ASP B 308  ? 0.2622 0.2528 0.1864 -0.0655 -0.0071 0.0258  306  ASP B N   
11068 C CA  . ASP B 308  ? 0.2785 0.2802 0.2091 -0.0638 -0.0041 0.0242  306  ASP B CA  
11069 C C   . ASP B 308  ? 0.2518 0.2511 0.1870 -0.0619 -0.0052 0.0217  306  ASP B C   
11070 O O   . ASP B 308  ? 0.2667 0.2567 0.2009 -0.0598 -0.0078 0.0201  306  ASP B O   
11071 C CB  . ASP B 308  ? 0.2604 0.2677 0.1925 -0.0588 -0.0016 0.0221  306  ASP B CB  
11072 C CG  . ASP B 308  ? 0.2912 0.3024 0.2188 -0.0605 0.0002  0.0245  306  ASP B CG  
11073 O OD1 . ASP B 308  ? 0.3084 0.3226 0.2338 -0.0658 0.0006  0.0279  306  ASP B OD1 
11074 O OD2 . ASP B 308  ? 0.3402 0.3517 0.2664 -0.0568 0.0010  0.0230  306  ASP B OD2 
11075 N N   . ALA B 309  ? 0.2382 0.2466 0.1786 -0.0625 -0.0032 0.0214  307  ALA B N   
11076 C CA  . ALA B 309  ? 0.2157 0.2228 0.1603 -0.0611 -0.0041 0.0193  307  ALA B CA  
11077 C C   . ALA B 309  ? 0.2233 0.2356 0.1730 -0.0552 -0.0021 0.0160  307  ALA B C   
11078 O O   . ALA B 309  ? 0.2445 0.2654 0.1962 -0.0535 0.0007  0.0158  307  ALA B O   
11079 C CB  . ALA B 309  ? 0.2410 0.2541 0.1878 -0.0660 -0.0038 0.0212  307  ALA B CB  
11080 N N   . GLU B 310  ? 0.2135 0.2201 0.1651 -0.0521 -0.0036 0.0134  308  GLU B N   
11081 C CA  . GLU B 310  ? 0.2104 0.2201 0.1662 -0.0465 -0.0021 0.0103  308  GLU B CA  
11082 C C   . GLU B 310  ? 0.1942 0.2068 0.1550 -0.0456 -0.0018 0.0087  308  GLU B C   
11083 O O   . GLU B 310  ? 0.2161 0.2349 0.1788 -0.0487 -0.0010 0.0102  308  GLU B O   
11084 C CB  . GLU B 310  ? 0.2135 0.2145 0.1671 -0.0429 -0.0039 0.0085  308  GLU B CB  
11085 C CG  . GLU B 310  ? 0.2420 0.2407 0.1905 -0.0439 -0.0042 0.0102  308  GLU B CG  
11086 C CD  . GLU B 310  ? 0.2583 0.2499 0.2050 -0.0402 -0.0058 0.0086  308  GLU B CD  
11087 O OE1 . GLU B 310  ? 0.2748 0.2691 0.2244 -0.0360 -0.0046 0.0062  308  GLU B OE1 
11088 O OE2 . GLU B 310  ? 0.2463 0.2296 0.1885 -0.0415 -0.0083 0.0097  308  GLU B OE2 
11089 N N   . GLU B 311  ? 0.1975 0.2064 0.1605 -0.0414 -0.0025 0.0060  309  GLU B N   
11090 C CA  . GLU B 311  ? 0.1996 0.2114 0.1672 -0.0402 -0.0021 0.0044  309  GLU B CA  
11091 C C   . GLU B 311  ? 0.2189 0.2266 0.1851 -0.0442 -0.0041 0.0055  309  GLU B C   
11092 O O   . GLU B 311  ? 0.2126 0.2126 0.1743 -0.0468 -0.0063 0.0068  309  GLU B O   
11093 C CB  . GLU B 311  ? 0.2037 0.2117 0.1734 -0.0352 -0.0025 0.0015  309  GLU B CB  
11094 C CG  . GLU B 311  ? 0.2442 0.2566 0.2159 -0.0312 -0.0005 0.0000  309  GLU B CG  
11095 C CD  . GLU B 311  ? 0.2706 0.2786 0.2385 -0.0302 -0.0012 0.0002  309  GLU B CD  
11096 O OE1 . GLU B 311  ? 0.2513 0.2535 0.2149 -0.0328 -0.0030 0.0018  309  GLU B OE1 
11097 O OE2 . GLU B 311  ? 0.2972 0.3071 0.2661 -0.0268 -0.0001 -0.0013 309  GLU B OE2 
11098 N N   . ALA B 312  ? 0.2075 0.2201 0.1775 -0.0445 -0.0035 0.0050  310  ALA B N   
11099 C CA  . ALA B 312  ? 0.2070 0.2163 0.1757 -0.0484 -0.0055 0.0059  310  ALA B CA  
11100 C C   . ALA B 312  ? 0.2070 0.2046 0.1725 -0.0474 -0.0081 0.0045  310  ALA B C   
11101 O O   . ALA B 312  ? 0.2129 0.2042 0.1746 -0.0511 -0.0103 0.0058  310  ALA B O   
11102 C CB  . ALA B 312  ? 0.2207 0.2373 0.1942 -0.0483 -0.0044 0.0052  310  ALA B CB  
11103 N N   . ASP B 313  ? 0.2115 0.2061 0.1785 -0.0424 -0.0079 0.0020  311  ASP B N   
11104 C CA  . ASP B 313  ? 0.2281 0.2125 0.1925 -0.0409 -0.0102 0.0006  311  ASP B CA  
11105 C C   . ASP B 313  ? 0.2356 0.2122 0.1951 -0.0414 -0.0119 0.0016  311  ASP B C   
11106 O O   . ASP B 313  ? 0.2423 0.2105 0.1996 -0.0396 -0.0138 0.0005  311  ASP B O   
11107 C CB  . ASP B 313  ? 0.2366 0.2213 0.2047 -0.0356 -0.0094 -0.0022 311  ASP B CB  
11108 C CG  . ASP B 313  ? 0.2361 0.2235 0.2061 -0.0319 -0.0080 -0.0030 311  ASP B CG  
11109 O OD1 . ASP B 313  ? 0.2277 0.2159 0.1956 -0.0330 -0.0077 -0.0016 311  ASP B OD1 
11110 O OD2 . ASP B 313  ? 0.2768 0.2652 0.2501 -0.0280 -0.0073 -0.0051 311  ASP B OD2 
11111 N N   . ARG B 314  ? 0.2165 0.1958 0.1741 -0.0437 -0.0113 0.0038  312  ARG B N   
11112 C CA  . ARG B 314  ? 0.2409 0.2126 0.1932 -0.0449 -0.0132 0.0052  312  ARG B CA  
11113 C C   . ARG B 314  ? 0.2110 0.1805 0.1590 -0.0509 -0.0145 0.0082  312  ARG B C   
11114 O O   . ARG B 314  ? 0.2248 0.1869 0.1676 -0.0525 -0.0164 0.0097  312  ARG B O   
11115 C CB  . ARG B 314  ? 0.2098 0.1851 0.1622 -0.0429 -0.0118 0.0055  312  ARG B CB  
11116 C CG  . ARG B 314  ? 0.2284 0.2021 0.1832 -0.0373 -0.0116 0.0028  312  ARG B CG  
11117 C CD  . ARG B 314  ? 0.2711 0.2508 0.2274 -0.0351 -0.0097 0.0025  312  ARG B CD  
11118 N NE  . ARG B 314  ? 0.2469 0.2229 0.2040 -0.0306 -0.0104 0.0005  312  ARG B NE  
11119 C CZ  . ARG B 314  ? 0.2405 0.2200 0.1988 -0.0280 -0.0093 -0.0003 312  ARG B CZ  
11120 N NH1 . ARG B 314  ? 0.2416 0.2285 0.2006 -0.0286 -0.0070 0.0002  312  ARG B NH1 
11121 N NH2 . ARG B 314  ? 0.2413 0.2168 0.2000 -0.0245 -0.0105 -0.0018 312  ARG B NH2 
11122 N N   . LEU B 315  ? 0.2053 0.1809 0.1552 -0.0544 -0.0137 0.0092  313  LEU B N   
11123 C CA  . LEU B 315  ? 0.2367 0.2115 0.1830 -0.0606 -0.0148 0.0123  313  LEU B CA  
11124 C C   . LEU B 315  ? 0.2438 0.2058 0.1843 -0.0626 -0.0183 0.0127  313  LEU B C   
11125 O O   . LEU B 315  ? 0.2441 0.2003 0.1794 -0.0654 -0.0198 0.0149  313  LEU B O   
11126 C CB  . LEU B 315  ? 0.2283 0.2119 0.1783 -0.0637 -0.0137 0.0130  313  LEU B CB  
11127 C CG  . LEU B 315  ? 0.2219 0.2104 0.1704 -0.0700 -0.0135 0.0166  313  LEU B CG  
11128 C CD1 . LEU B 315  ? 0.2294 0.2279 0.1830 -0.0719 -0.0123 0.0168  313  LEU B CD1 
11129 C CD2 . LEU B 315  ? 0.2677 0.2458 0.2097 -0.0751 -0.0168 0.0187  313  LEU B CD2 
11130 N N   . GLU B 316  ? 0.2433 0.2004 0.1842 -0.0612 -0.0196 0.0106  314  GLU B N   
11131 C CA  . GLU B 316  ? 0.2493 0.1943 0.1844 -0.0635 -0.0229 0.0110  314  GLU B CA  
11132 C C   . GLU B 316  ? 0.2714 0.2067 0.2026 -0.0601 -0.0245 0.0103  314  GLU B C   
11133 O O   . GLU B 316  ? 0.2910 0.2168 0.2162 -0.0628 -0.0271 0.0119  314  GLU B O   
11134 C CB  . GLU B 316  ? 0.2558 0.1985 0.1920 -0.0629 -0.0238 0.0088  314  GLU B CB  
11135 C CG  . GLU B 316  ? 0.2708 0.2217 0.2094 -0.0675 -0.0230 0.0102  314  GLU B CG  
11136 C CD  . GLU B 316  ? 0.2867 0.2359 0.2262 -0.0673 -0.0240 0.0082  314  GLU B CD  
11137 O OE1 . GLU B 316  ? 0.3014 0.2395 0.2364 -0.0668 -0.0264 0.0070  314  GLU B OE1 
11138 O OE2 . GLU B 316  ? 0.2960 0.2549 0.2405 -0.0675 -0.0222 0.0079  314  GLU B OE2 
11139 N N   . LEU B 317  ? 0.2615 0.1991 0.1962 -0.0544 -0.0231 0.0082  315  LEU B N   
11140 C CA  . LEU B 317  ? 0.2812 0.2114 0.2130 -0.0511 -0.0245 0.0078  315  LEU B CA  
11141 C C   . LEU B 317  ? 0.2853 0.2140 0.2128 -0.0545 -0.0251 0.0110  315  LEU B C   
11142 O O   . LEU B 317  ? 0.2933 0.2120 0.2153 -0.0549 -0.0277 0.0119  315  LEU B O   
11143 C CB  . LEU B 317  ? 0.2559 0.1913 0.1928 -0.0452 -0.0225 0.0055  315  LEU B CB  
11144 C CG  . LEU B 317  ? 0.2858 0.2151 0.2207 -0.0415 -0.0239 0.0050  315  LEU B CG  
11145 C CD1 . LEU B 317  ? 0.3063 0.2239 0.2372 -0.0403 -0.0268 0.0043  315  LEU B CD1 
11146 C CD2 . LEU B 317  ? 0.2809 0.2162 0.2214 -0.0363 -0.0220 0.0026  315  LEU B CD2 
11147 N N   . SER B 318  ? 0.2529 0.1914 0.1825 -0.0569 -0.0228 0.0126  316  SER B N   
11148 C CA  . SER B 318  ? 0.2695 0.2073 0.1948 -0.0601 -0.0232 0.0156  316  SER B CA  
11149 C C   . SER B 318  ? 0.2641 0.1940 0.1834 -0.0659 -0.0258 0.0184  316  SER B C   
11150 O O   . SER B 318  ? 0.2970 0.2211 0.2109 -0.0678 -0.0273 0.0206  316  SER B O   
11151 C CB  . SER B 318  ? 0.2356 0.1860 0.1644 -0.0615 -0.0199 0.0168  316  SER B CB  
11152 O OG  . SER B 318  ? 0.2484 0.2048 0.1787 -0.0661 -0.0191 0.0183  316  SER B OG  
11153 N N   . LEU B 319  ? 0.2602 0.1894 0.1798 -0.0689 -0.0265 0.0183  317  LEU B N   
11154 C CA  . LEU B 319  ? 0.2778 0.1991 0.1914 -0.0748 -0.0293 0.0208  317  LEU B CA  
11155 C C   . LEU B 319  ? 0.2967 0.2031 0.2041 -0.0730 -0.0327 0.0204  317  LEU B C   
11156 O O   . LEU B 319  ? 0.3108 0.2093 0.2118 -0.0773 -0.0351 0.0231  317  LEU B O   
11157 C CB  . LEU B 319  ? 0.2670 0.1903 0.1823 -0.0779 -0.0296 0.0204  317  LEU B CB  
11158 C CG  . LEU B 319  ? 0.2696 0.2075 0.1909 -0.0801 -0.0266 0.0211  317  LEU B CG  
11159 C CD1 . LEU B 319  ? 0.2928 0.2314 0.2156 -0.0826 -0.0275 0.0203  317  LEU B CD1 
11160 C CD2 . LEU B 319  ? 0.2783 0.2219 0.1980 -0.0858 -0.0258 0.0252  317  LEU B CD2 
11161 N N   . ASP B 320  ? 0.3074 0.2099 0.2165 -0.0668 -0.0330 0.0171  318  ASP B N   
11162 C CA  . ASP B 320  ? 0.3360 0.2250 0.2397 -0.0644 -0.0361 0.0166  318  ASP B CA  
11163 C C   . ASP B 320  ? 0.3392 0.2253 0.2395 -0.0640 -0.0368 0.0186  318  ASP B C   
11164 O O   . ASP B 320  ? 0.3500 0.2247 0.2438 -0.0648 -0.0399 0.0199  318  ASP B O   
11165 C CB  . ASP B 320  ? 0.2970 0.1844 0.2042 -0.0576 -0.0359 0.0127  318  ASP B CB  
11166 C CG  . ASP B 320  ? 0.3168 0.2024 0.2247 -0.0582 -0.0363 0.0108  318  ASP B CG  
11167 O OD1 . ASP B 320  ? 0.3666 0.2428 0.2686 -0.0617 -0.0390 0.0118  318  ASP B OD1 
11168 O OD2 . ASP B 320  ? 0.3458 0.2390 0.2596 -0.0553 -0.0341 0.0084  318  ASP B OD2 
11169 N N   . LEU B 321  ? 0.2852 0.1813 0.1893 -0.0627 -0.0342 0.0190  319  LEU B N   
11170 C CA  . LEU B 321  ? 0.2949 0.1887 0.1952 -0.0630 -0.0349 0.0212  319  LEU B CA  
11171 C C   . LEU B 321  ? 0.3093 0.2022 0.2046 -0.0702 -0.0356 0.0253  319  LEU B C   
11172 O O   . LEU B 321  ? 0.3291 0.2134 0.2181 -0.0719 -0.0380 0.0276  319  LEU B O   
11173 C CB  . LEU B 321  ? 0.3235 0.2278 0.2288 -0.0595 -0.0320 0.0202  319  LEU B CB  
11174 C CG  . LEU B 321  ? 0.3312 0.2346 0.2401 -0.0524 -0.0319 0.0169  319  LEU B CG  
11175 C CD1 . LEU B 321  ? 0.3390 0.2493 0.2546 -0.0500 -0.0298 0.0139  319  LEU B CD1 
11176 C CD2 . LEU B 321  ? 0.3409 0.2490 0.2507 -0.0499 -0.0308 0.0171  319  LEU B CD2 
11177 N N   . LEU B 322  ? 0.3062 0.2082 0.2043 -0.0745 -0.0335 0.0263  320  LEU B N   
11178 C CA  . LEU B 322  ? 0.3099 0.2125 0.2039 -0.0818 -0.0340 0.0304  320  LEU B CA  
11179 C C   . LEU B 322  ? 0.3138 0.2024 0.2006 -0.0854 -0.0380 0.0319  320  LEU B C   
11180 O O   . LEU B 322  ? 0.3562 0.2393 0.2369 -0.0898 -0.0397 0.0354  320  LEU B O   
11181 C CB  . LEU B 322  ? 0.3044 0.2192 0.2034 -0.0855 -0.0313 0.0310  320  LEU B CB  
11182 C CG  . LEU B 322  ? 0.3500 0.2673 0.2456 -0.0934 -0.0314 0.0354  320  LEU B CG  
11183 C CD1 . LEU B 322  ? 0.3236 0.2450 0.2171 -0.0938 -0.0299 0.0378  320  LEU B CD1 
11184 C CD2 . LEU B 322  ? 0.3407 0.2699 0.2418 -0.0965 -0.0292 0.0356  320  LEU B CD2 
11185 N N   . GLU B 323  ? 0.3240 0.2063 0.2111 -0.0837 -0.0396 0.0294  321  GLU B N   
11186 C CA  . GLU B 323  ? 0.3296 0.1975 0.2095 -0.0865 -0.0436 0.0303  321  GLU B CA  
11187 C C   . GLU B 323  ? 0.3719 0.2281 0.2456 -0.0843 -0.0462 0.0313  321  GLU B C   
11188 O O   . GLU B 323  ? 0.3889 0.2360 0.2554 -0.0891 -0.0489 0.0344  321  GLU B O   
11189 C CB  . GLU B 323  ? 0.3519 0.2154 0.2335 -0.0833 -0.0445 0.0267  321  GLU B CB  
11190 C CG  . GLU B 323  ? 0.4222 0.2696 0.2961 -0.0849 -0.0487 0.0268  321  GLU B CG  
11191 C CD  . GLU B 323  ? 0.4449 0.2908 0.3161 -0.0924 -0.0500 0.0286  321  GLU B CD  
11192 O OE1 . GLU B 323  ? 0.4386 0.2968 0.3152 -0.0955 -0.0476 0.0291  321  GLU B OE1 
11193 O OE2 . GLU B 323  ? 0.4305 0.2628 0.2943 -0.0953 -0.0537 0.0296  321  GLU B OE2 
11194 N N   . VAL B 324  ? 0.3698 0.2258 0.2459 -0.0772 -0.0457 0.0287  322  VAL B N   
11195 C CA  . VAL B 324  ? 0.3733 0.2184 0.2440 -0.0744 -0.0484 0.0295  322  VAL B CA  
11196 C C   . VAL B 324  ? 0.3871 0.2339 0.2540 -0.0784 -0.0483 0.0334  322  VAL B C   
11197 O O   . VAL B 324  ? 0.4124 0.2481 0.2718 -0.0807 -0.0514 0.0360  322  VAL B O   
11198 C CB  . VAL B 324  ? 0.4036 0.2505 0.2789 -0.0661 -0.0475 0.0260  322  VAL B CB  
11199 C CG1 . VAL B 324  ? 0.3987 0.2365 0.2690 -0.0633 -0.0501 0.0271  322  VAL B CG1 
11200 C CG2 . VAL B 324  ? 0.4197 0.2633 0.2976 -0.0621 -0.0479 0.0223  322  VAL B CG2 
11201 N N   . LEU B 325  ? 0.3448 0.2051 0.2165 -0.0792 -0.0448 0.0340  323  LEU B N   
11202 C CA  . LEU B 325  ? 0.3767 0.2394 0.2448 -0.0826 -0.0444 0.0377  323  LEU B CA  
11203 C C   . LEU B 325  ? 0.3921 0.2502 0.2542 -0.0908 -0.0460 0.0418  323  LEU B C   
11204 O O   . LEU B 325  ? 0.3893 0.2407 0.2447 -0.0935 -0.0479 0.0451  323  LEU B O   
11205 C CB  . LEU B 325  ? 0.3434 0.2217 0.2177 -0.0818 -0.0401 0.0372  323  LEU B CB  
11206 C CG  . LEU B 325  ? 0.3483 0.2306 0.2278 -0.0741 -0.0387 0.0336  323  LEU B CG  
11207 C CD1 . LEU B 325  ? 0.3237 0.2211 0.2099 -0.0732 -0.0345 0.0325  323  LEU B CD1 
11208 C CD2 . LEU B 325  ? 0.3479 0.2237 0.2229 -0.0713 -0.0406 0.0345  323  LEU B CD2 
11209 N N   . CYS B 326  ? 0.3809 0.2425 0.2450 -0.0950 -0.0454 0.0419  324  CYS B N   
11210 C CA  . CYS B 326  ? 0.3912 0.2496 0.2501 -0.1034 -0.0469 0.0460  324  CYS B CA  
11211 C C   . CYS B 326  ? 0.4141 0.2546 0.2644 -0.1051 -0.0517 0.0472  324  CYS B C   
11212 O O   . CYS B 326  ? 0.4144 0.2497 0.2584 -0.1117 -0.0536 0.0513  324  CYS B O   
11213 C CB  . CYS B 326  ? 0.4032 0.2703 0.2668 -0.1075 -0.0453 0.0458  324  CYS B CB  
11214 S SG  . CYS B 326  ? 0.3922 0.2806 0.2643 -0.1077 -0.0398 0.0460  324  CYS B SG  
11215 N N   . LEU B 327  ? 0.3857 0.2167 0.2354 -0.0993 -0.0538 0.0438  325  LEU B N   
11216 C CA  . LEU B 327  ? 0.4487 0.2619 0.2900 -0.0997 -0.0584 0.0445  325  LEU B CA  
11217 C C   . LEU B 327  ? 0.4667 0.2720 0.3037 -0.0953 -0.0602 0.0451  325  LEU B C   
11218 O O   . LEU B 327  ? 0.4843 0.2744 0.3143 -0.0945 -0.0641 0.0455  325  LEU B O   
11219 C CB  . LEU B 327  ? 0.4191 0.2259 0.2616 -0.0958 -0.0597 0.0405  325  LEU B CB  
11220 C CG  . LEU B 327  ? 0.4420 0.2552 0.2878 -0.1006 -0.0586 0.0400  325  LEU B CG  
11221 C CD1 . LEU B 327  ? 0.4889 0.2983 0.3371 -0.0957 -0.0591 0.0355  325  LEU B CD1 
11222 C CD2 . LEU B 327  ? 0.5371 0.3431 0.3759 -0.1095 -0.0613 0.0440  325  LEU B CD2 
11223 N N   . ASP B 328  ? 0.4217 0.2367 0.2626 -0.0923 -0.0576 0.0451  326  ASP B N   
11224 C CA  . ASP B 328  ? 0.4581 0.2669 0.2956 -0.0877 -0.0592 0.0455  326  ASP B CA  
11225 C C   . ASP B 328  ? 0.4597 0.2628 0.2892 -0.0936 -0.0611 0.0505  326  ASP B C   
11226 O O   . ASP B 328  ? 0.4649 0.2779 0.2954 -0.0980 -0.0586 0.0532  326  ASP B O   
11227 C CB  . ASP B 328  ? 0.4260 0.2475 0.2708 -0.0824 -0.0558 0.0433  326  ASP B CB  
11228 C CG  . ASP B 328  ? 0.4945 0.3102 0.3368 -0.0769 -0.0576 0.0431  326  ASP B CG  
11229 O OD1 . ASP B 328  ? 0.4650 0.2689 0.2996 -0.0784 -0.0611 0.0458  326  ASP B OD1 
11230 O OD2 . ASP B 328  ? 0.4784 0.3015 0.3267 -0.0711 -0.0557 0.0403  326  ASP B OD2 
11231 N N   . GLY B 329  ? 0.5138 0.3010 0.3354 -0.0936 -0.0654 0.0519  327  GLY B N   
11232 C CA  . GLY B 329  ? 0.4688 0.2486 0.2819 -0.0993 -0.0676 0.0569  327  GLY B CA  
11233 C C   . GLY B 329  ? 0.5371 0.3233 0.3498 -0.0984 -0.0662 0.0589  327  GLY B C   
11234 O O   . GLY B 329  ? 0.5072 0.2927 0.3145 -0.1044 -0.0666 0.0634  327  GLY B O   
11235 N N   . ASP B 330  ? 0.5121 0.3044 0.3302 -0.0911 -0.0646 0.0558  328  ASP B N   
11236 C CA  . ASP B 330  ? 0.4665 0.2654 0.2843 -0.0902 -0.0632 0.0575  328  ASP B CA  
11237 C C   . ASP B 330  ? 0.5104 0.3234 0.3308 -0.0957 -0.0591 0.0595  328  ASP B C   
11238 O O   . ASP B 330  ? 0.5391 0.3557 0.3564 -0.0977 -0.0583 0.0624  328  ASP B O   
11239 C CB  . ASP B 330  ? 0.4902 0.2942 0.3141 -0.0817 -0.0621 0.0535  328  ASP B CB  
11240 C CG  . ASP B 330  ? 0.5119 0.3029 0.3329 -0.0758 -0.0661 0.0521  328  ASP B CG  
11241 O OD1 . ASP B 330  ? 0.5376 0.3148 0.3507 -0.0781 -0.0699 0.0546  328  ASP B OD1 
11242 O OD2 . ASP B 330  ? 0.5349 0.3293 0.3614 -0.0689 -0.0655 0.0485  328  ASP B OD2 
11243 N N   . LEU B 331  ? 0.4772 0.2985 0.3031 -0.0982 -0.0566 0.0582  329  LEU B N   
11244 C CA  . LEU B 331  ? 0.4665 0.3019 0.2956 -0.1031 -0.0526 0.0599  329  LEU B CA  
11245 C C   . LEU B 331  ? 0.4490 0.2815 0.2731 -0.1121 -0.0536 0.0642  329  LEU B C   
11246 O O   . LEU B 331  ? 0.4612 0.3055 0.2889 -0.1167 -0.0505 0.0655  329  LEU B O   
11247 C CB  . LEU B 331  ? 0.4552 0.3031 0.2941 -0.1000 -0.0491 0.0559  329  LEU B CB  
11248 C CG  . LEU B 331  ? 0.4624 0.3135 0.3065 -0.0914 -0.0481 0.0517  329  LEU B CG  
11249 C CD1 . LEU B 331  ? 0.4372 0.2991 0.2904 -0.0885 -0.0449 0.0478  329  LEU B CD1 
11250 C CD2 . LEU B 331  ? 0.4044 0.2611 0.2471 -0.0901 -0.0466 0.0530  329  LEU B CD2 
11251 N N   . SER B 332  ? 0.4771 0.2941 0.2930 -0.1147 -0.0580 0.0666  330  SER B N   
11252 C CA  . SER B 332  ? 0.5094 0.3210 0.3197 -0.1234 -0.0598 0.0707  330  SER B CA  
11253 C C   . SER B 332  ? 0.5354 0.3586 0.3454 -0.1301 -0.0568 0.0749  330  SER B C   
11254 O O   . SER B 332  ? 0.5432 0.3693 0.3505 -0.1296 -0.0558 0.0769  330  SER B O   
11255 C CB  . SER B 332  ? 0.5413 0.3341 0.3417 -0.1244 -0.0650 0.0731  330  SER B CB  
11256 O OG  . SER B 332  ? 0.6078 0.3945 0.4020 -0.1333 -0.0670 0.0774  330  SER B OG  
11257 N N   . GLY B 333  ? 0.4991 0.3291 0.3116 -0.1366 -0.0554 0.0764  331  GLY B N   
11258 C CA  . GLY B 333  ? 0.5372 0.3779 0.3491 -0.1438 -0.0528 0.0809  331  GLY B CA  
11259 C C   . GLY B 333  ? 0.5401 0.3993 0.3593 -0.1411 -0.0474 0.0797  331  GLY B C   
11260 O O   . GLY B 333  ? 0.5285 0.3977 0.3473 -0.1466 -0.0447 0.0833  331  GLY B O   
11261 N N   . TRP B 334  ? 0.5115 0.3754 0.3369 -0.1330 -0.0456 0.0748  332  TRP B N   
11262 C CA  . TRP B 334  ? 0.5065 0.3870 0.3386 -0.1298 -0.0407 0.0731  332  TRP B CA  
11263 C C   . TRP B 334  ? 0.4692 0.3620 0.3096 -0.1312 -0.0378 0.0715  332  TRP B C   
11264 O O   . TRP B 334  ? 0.4745 0.3644 0.3189 -0.1284 -0.0388 0.0680  332  TRP B O   
11265 C CB  . TRP B 334  ? 0.4767 0.3556 0.3112 -0.1207 -0.0406 0.0688  332  TRP B CB  
11266 C CG  . TRP B 334  ? 0.4407 0.3347 0.2819 -0.1163 -0.0359 0.0663  332  TRP B CG  
11267 C CD1 . TRP B 334  ? 0.4287 0.3335 0.2694 -0.1180 -0.0325 0.0684  332  TRP B CD1 
11268 C CD2 . TRP B 334  ? 0.4404 0.3394 0.2891 -0.1093 -0.0344 0.0612  332  TRP B CD2 
11269 N NE1 . TRP B 334  ? 0.4141 0.3301 0.2617 -0.1122 -0.0290 0.0647  332  TRP B NE1 
11270 C CE2 . TRP B 334  ? 0.3938 0.3064 0.2464 -0.1070 -0.0301 0.0604  332  TRP B CE2 
11271 C CE3 . TRP B 334  ? 0.4015 0.2949 0.2540 -0.1047 -0.0361 0.0572  332  TRP B CE3 
11272 C CZ2 . TRP B 334  ? 0.3801 0.3000 0.2399 -0.1006 -0.0278 0.0558  332  TRP B CZ2 
11273 C CZ3 . TRP B 334  ? 0.4547 0.3561 0.3146 -0.0984 -0.0336 0.0529  332  TRP B CZ3 
11274 C CH2 . TRP B 334  ? 0.4158 0.3300 0.2792 -0.0966 -0.0296 0.0523  332  TRP B CH2 
11275 N N   . ASN B 335  ? 0.4545 0.3611 0.2973 -0.1356 -0.0342 0.0740  333  ASN B N   
11276 C CA  . ASN B 335  ? 0.4179 0.3374 0.2688 -0.1369 -0.0313 0.0728  333  ASN B CA  
11277 C C   . ASN B 335  ? 0.4121 0.3456 0.2704 -0.1307 -0.0268 0.0694  333  ASN B C   
11278 O O   . ASN B 335  ? 0.4162 0.3629 0.2811 -0.1317 -0.0236 0.0689  333  ASN B O   
11279 C CB  . ASN B 335  ? 0.4390 0.3654 0.2886 -0.1461 -0.0303 0.0779  333  ASN B CB  
11280 C CG  . ASN B 335  ? 0.5126 0.4250 0.3555 -0.1527 -0.0350 0.0809  333  ASN B CG  
11281 O OD1 . ASN B 335  ? 0.4646 0.3649 0.3063 -0.1505 -0.0385 0.0783  333  ASN B OD1 
11282 N ND2 . ASN B 335  ? 0.4881 0.4014 0.3261 -0.1608 -0.0353 0.0863  333  ASN B ND2 
11283 N N   . GLY B 336  ? 0.4241 0.3547 0.2813 -0.1242 -0.0266 0.0671  334  GLY B N   
11284 C CA  . GLY B 336  ? 0.4103 0.3526 0.2734 -0.1182 -0.0226 0.0639  334  GLY B CA  
11285 C C   . GLY B 336  ? 0.3885 0.3309 0.2582 -0.1116 -0.0226 0.0586  334  GLY B C   
11286 O O   . GLY B 336  ? 0.3794 0.3314 0.2543 -0.1067 -0.0194 0.0559  334  GLY B O   
11287 N N   . MET B 337  ? 0.3949 0.3268 0.2643 -0.1112 -0.0260 0.0572  335  MET B N   
11288 C CA  . MET B 337  ? 0.3716 0.3047 0.2476 -0.1054 -0.0257 0.0524  335  MET B CA  
11289 C C   . MET B 337  ? 0.3888 0.3360 0.2722 -0.1066 -0.0222 0.0516  335  MET B C   
11290 O O   . MET B 337  ? 0.3851 0.3350 0.2687 -0.1128 -0.0224 0.0542  335  MET B O   
11291 C CB  . MET B 337  ? 0.4130 0.3323 0.2868 -0.1053 -0.0298 0.0512  335  MET B CB  
11292 C CG  . MET B 337  ? 0.4452 0.3652 0.3252 -0.0991 -0.0295 0.0463  335  MET B CG  
11293 S SD  . MET B 337  ? 0.4964 0.4129 0.3770 -0.0905 -0.0296 0.0430  335  MET B SD  
11294 C CE  . MET B 337  ? 0.4404 0.3720 0.3305 -0.0857 -0.0252 0.0392  335  MET B CE  
11295 N N   . GLY B 338  ? 0.3386 0.2948 0.2280 -0.1008 -0.0192 0.0483  336  GLY B N   
11296 C CA  . GLY B 338  ? 0.3417 0.3119 0.2383 -0.1010 -0.0157 0.0474  336  GLY B CA  
11297 C C   . GLY B 338  ? 0.3316 0.3023 0.2344 -0.0955 -0.0156 0.0429  336  GLY B C   
11298 O O   . GLY B 338  ? 0.3289 0.2920 0.2313 -0.0902 -0.0171 0.0400  336  GLY B O   
11299 N N   . PHE B 339  ? 0.2936 0.2737 0.2023 -0.0968 -0.0138 0.0424  337  PHE B N   
11300 C CA  . PHE B 339  ? 0.2843 0.2647 0.1985 -0.0923 -0.0139 0.0385  337  PHE B CA  
11301 C C   . PHE B 339  ? 0.3153 0.3103 0.2365 -0.0925 -0.0105 0.0381  337  PHE B C   
11302 O O   . PHE B 339  ? 0.3329 0.3343 0.2547 -0.0982 -0.0099 0.0411  337  PHE B O   
11303 C CB  . PHE B 339  ? 0.2766 0.2457 0.1885 -0.0947 -0.0177 0.0383  337  PHE B CB  
11304 C CG  . PHE B 339  ? 0.2820 0.2483 0.1980 -0.0895 -0.0183 0.0341  337  PHE B CG  
11305 C CD1 . PHE B 339  ? 0.3135 0.2708 0.2281 -0.0840 -0.0198 0.0314  337  PHE B CD1 
11306 C CD2 . PHE B 339  ? 0.2640 0.2368 0.1854 -0.0903 -0.0174 0.0330  337  PHE B CD2 
11307 C CE1 . PHE B 339  ? 0.3120 0.2673 0.2305 -0.0794 -0.0202 0.0277  337  PHE B CE1 
11308 C CE2 . PHE B 339  ? 0.2772 0.2474 0.2020 -0.0856 -0.0180 0.0293  337  PHE B CE2 
11309 C CZ  . PHE B 339  ? 0.2994 0.2609 0.2227 -0.0802 -0.0192 0.0267  337  PHE B CZ  
11310 N N   . VAL B 340  ? 0.2813 0.2815 0.2077 -0.0864 -0.0085 0.0346  338  VAL B N   
11311 C CA  . VAL B 340  ? 0.2511 0.2649 0.1843 -0.0854 -0.0052 0.0339  338  VAL B CA  
11312 C C   . VAL B 340  ? 0.2838 0.2968 0.2209 -0.0857 -0.0066 0.0322  338  VAL B C   
11313 O O   . VAL B 340  ? 0.2607 0.2643 0.1973 -0.0828 -0.0088 0.0297  338  VAL B O   
11314 C CB  . VAL B 340  ? 0.2911 0.3103 0.2274 -0.0786 -0.0025 0.0309  338  VAL B CB  
11315 C CG1 . VAL B 340  ? 0.2821 0.3142 0.2255 -0.0768 0.0006  0.0297  338  VAL B CG1 
11316 C CG2 . VAL B 340  ? 0.2887 0.3094 0.2207 -0.0784 -0.0010 0.0325  338  VAL B CG2 
11317 N N   . VAL B 341  ? 0.2560 0.2794 0.1973 -0.0889 -0.0052 0.0337  339  VAL B N   
11318 C CA  . VAL B 341  ? 0.2378 0.2629 0.1837 -0.0887 -0.0059 0.0320  339  VAL B CA  
11319 C C   . VAL B 341  ? 0.2427 0.2827 0.1955 -0.0862 -0.0022 0.0314  339  VAL B C   
11320 O O   . VAL B 341  ? 0.2733 0.3234 0.2271 -0.0880 0.0003  0.0337  339  VAL B O   
11321 C CB  . VAL B 341  ? 0.2985 0.3202 0.2423 -0.0959 -0.0087 0.0346  339  VAL B CB  
11322 C CG1 . VAL B 341  ? 0.3053 0.3110 0.2419 -0.0975 -0.0124 0.0349  339  VAL B CG1 
11323 C CG2 . VAL B 341  ? 0.3256 0.3574 0.2697 -0.1020 -0.0072 0.0389  339  VAL B CG2 
11324 N N   . GLN B 342  ? 0.2420 0.2832 0.1993 -0.0819 -0.0020 0.0282  340  GLN B N   
11325 C CA  . GLN B 342  ? 0.2337 0.2871 0.1974 -0.0780 0.0012  0.0268  340  GLN B CA  
11326 C C   . GLN B 342  ? 0.2674 0.3285 0.2357 -0.0814 0.0010  0.0279  340  GLN B C   
11327 O O   . GLN B 342  ? 0.2483 0.3040 0.2173 -0.0815 -0.0013 0.0264  340  GLN B O   
11328 C CB  . GLN B 342  ? 0.2169 0.2664 0.1826 -0.0709 0.0015  0.0227  340  GLN B CB  
11329 C CG  . GLN B 342  ? 0.2145 0.2580 0.1764 -0.0674 0.0019  0.0216  340  GLN B CG  
11330 C CD  . GLN B 342  ? 0.2092 0.2435 0.1710 -0.0624 0.0004  0.0181  340  GLN B CD  
11331 O OE1 . GLN B 342  ? 0.2340 0.2608 0.1950 -0.0633 -0.0022 0.0173  340  GLN B OE1 
11332 N NE2 . GLN B 342  ? 0.2101 0.2453 0.1726 -0.0571 0.0020  0.0160  340  GLN B NE2 
11333 N N   . ALA B 343  ? 0.2178 0.2918 0.1892 -0.0839 0.0033  0.0304  341  ALA B N   
11334 C CA  . ALA B 343  ? 0.2417 0.3243 0.2176 -0.0875 0.0031  0.0319  341  ALA B CA  
11335 C C   . ALA B 343  ? 0.2304 0.3176 0.2120 -0.0826 0.0039  0.0290  341  ALA B C   
11336 O O   . ALA B 343  ? 0.2320 0.3229 0.2167 -0.0852 0.0027  0.0296  341  ALA B O   
11337 C CB  . ALA B 343  ? 0.2695 0.3660 0.2477 -0.0909 0.0058  0.0355  341  ALA B CB  
11338 N N   . TYR B 344  ? 0.2359 0.3228 0.2190 -0.0756 0.0058  0.0259  342  TYR B N   
11339 C CA  . TYR B 344  ? 0.2182 0.3081 0.2062 -0.0711 0.0062  0.0233  342  TYR B CA  
11340 C C   . TYR B 344  ? 0.1937 0.2719 0.1799 -0.0709 0.0030  0.0211  342  TYR B C   
11341 O O   . TYR B 344  ? 0.2055 0.2852 0.1953 -0.0677 0.0030  0.0190  342  TYR B O   
11342 C CB  . TYR B 344  ? 0.2171 0.3106 0.2073 -0.0639 0.0091  0.0207  342  TYR B CB  
11343 C CG  . TYR B 344  ? 0.2288 0.3115 0.2154 -0.0594 0.0086  0.0179  342  TYR B CG  
11344 C CD1 . TYR B 344  ? 0.2282 0.2982 0.2095 -0.0613 0.0059  0.0178  342  TYR B CD1 
11345 C CD2 . TYR B 344  ? 0.2032 0.2884 0.1917 -0.0531 0.0109  0.0155  342  TYR B CD2 
11346 C CE1 . TYR B 344  ? 0.1996 0.2608 0.1783 -0.0570 0.0055  0.0153  342  TYR B CE1 
11347 C CE2 . TYR B 344  ? 0.2029 0.2791 0.1886 -0.0492 0.0104  0.0131  342  TYR B CE2 
11348 C CZ  . TYR B 344  ? 0.2179 0.2826 0.1989 -0.0511 0.0077  0.0131  342  TYR B CZ  
11349 O OH  . TYR B 344  ? 0.2049 0.2616 0.1836 -0.0472 0.0072  0.0108  342  TYR B OH  
11350 N N   . GLY B 345  ? 0.2192 0.2860 0.1997 -0.0742 0.0003  0.0218  343  GLY B N   
11351 C CA  . GLY B 345  ? 0.2338 0.2889 0.2118 -0.0737 -0.0026 0.0197  343  GLY B CA  
11352 C C   . GLY B 345  ? 0.2256 0.2795 0.2029 -0.0796 -0.0053 0.0213  343  GLY B C   
11353 O O   . GLY B 345  ? 0.2362 0.2925 0.2119 -0.0855 -0.0060 0.0245  343  GLY B O   
11354 N N   . LYS B 346  ? 0.2217 0.2716 0.2000 -0.0780 -0.0068 0.0191  344  LYS B N   
11355 C CA  . LYS B 346  ? 0.2401 0.2886 0.2177 -0.0831 -0.0094 0.0201  344  LYS B CA  
11356 C C   . LYS B 346  ? 0.2529 0.2893 0.2236 -0.0881 -0.0127 0.0214  344  LYS B C   
11357 O O   . LYS B 346  ? 0.2551 0.2910 0.2243 -0.0940 -0.0149 0.0233  344  LYS B O   
11358 C CB  . LYS B 346  ? 0.2329 0.2791 0.2125 -0.0796 -0.0102 0.0171  344  LYS B CB  
11359 C CG  . LYS B 346  ? 0.2177 0.2763 0.2042 -0.0757 -0.0075 0.0164  344  LYS B CG  
11360 C CD  . LYS B 346  ? 0.2315 0.2871 0.2195 -0.0721 -0.0082 0.0135  344  LYS B CD  
11361 C CE  . LYS B 346  ? 0.2232 0.2911 0.2179 -0.0687 -0.0058 0.0132  344  LYS B CE  
11362 N NZ  . LYS B 346  ? 0.2235 0.2882 0.2195 -0.0644 -0.0062 0.0103  344  LYS B NZ  
11363 N N   . ARG B 347  ? 0.2502 0.2764 0.2164 -0.0858 -0.0132 0.0204  345  ARG B N   
11364 C CA  . ARG B 347  ? 0.2805 0.2943 0.2396 -0.0899 -0.0164 0.0215  345  ARG B CA  
11365 C C   . ARG B 347  ? 0.2632 0.2791 0.2197 -0.0951 -0.0162 0.0252  345  ARG B C   
11366 O O   . ARG B 347  ? 0.2783 0.2843 0.2288 -0.0995 -0.0191 0.0267  345  ARG B O   
11367 C CB  . ARG B 347  ? 0.2329 0.2345 0.1883 -0.0849 -0.0172 0.0187  345  ARG B CB  
11368 C CG  . ARG B 347  ? 0.2221 0.2204 0.1793 -0.0805 -0.0177 0.0152  345  ARG B CG  
11369 C CD  . ARG B 347  ? 0.2410 0.2311 0.1966 -0.0744 -0.0175 0.0124  345  ARG B CD  
11370 N NE  . ARG B 347  ? 0.2186 0.2165 0.1786 -0.0696 -0.0143 0.0116  345  ARG B NE  
11371 C CZ  . ARG B 347  ? 0.2375 0.2305 0.1967 -0.0647 -0.0138 0.0098  345  ARG B CZ  
11372 N NH1 . ARG B 347  ? 0.2307 0.2118 0.1855 -0.0635 -0.0160 0.0086  345  ARG B NH1 
11373 N NH2 . ARG B 347  ? 0.1998 0.2002 0.1628 -0.0609 -0.0111 0.0092  345  ARG B NH2 
11374 N N   . CYS B 348  ? 0.2476 0.2760 0.2082 -0.0948 -0.0131 0.0268  346  CYS B N   
11375 C CA  . CYS B 348  ? 0.2668 0.2976 0.2248 -0.0986 -0.0123 0.0302  346  CYS B CA  
11376 C C   . CYS B 348  ? 0.2878 0.3147 0.2416 -0.1070 -0.0152 0.0337  346  CYS B C   
11377 O O   . CYS B 348  ? 0.2861 0.3039 0.2338 -0.1095 -0.0168 0.0352  346  CYS B O   
11378 C CB  . CYS B 348  ? 0.2320 0.2787 0.1958 -0.0972 -0.0083 0.0314  346  CYS B CB  
11379 S SG  . CYS B 348  ? 0.3044 0.3542 0.2648 -0.0999 -0.0065 0.0348  346  CYS B SG  
11380 N N   . PRO B 349  ? 0.2750 0.3079 0.2314 -0.1118 -0.0162 0.0351  347  PRO B N   
11381 C CA  . PRO B 349  ? 0.3035 0.3318 0.2553 -0.1202 -0.0192 0.0386  347  PRO B CA  
11382 C C   . PRO B 349  ? 0.2900 0.3001 0.2342 -0.1213 -0.0233 0.0374  347  PRO B C   
11383 O O   . PRO B 349  ? 0.3049 0.3076 0.2431 -0.1267 -0.0255 0.0401  347  PRO B O   
11384 C CB  . PRO B 349  ? 0.2823 0.3209 0.2392 -0.1240 -0.0197 0.0396  347  PRO B CB  
11385 C CG  . PRO B 349  ? 0.2922 0.3352 0.2544 -0.1172 -0.0180 0.0360  347  PRO B CG  
11386 C CD  . PRO B 349  ? 0.2675 0.3110 0.2308 -0.1099 -0.0150 0.0339  347  PRO B CD  
11387 N N   . PHE B 350  ? 0.3081 0.3108 0.2520 -0.1161 -0.0242 0.0334  348  PHE B N   
11388 C CA  . PHE B 350  ? 0.3124 0.2978 0.2491 -0.1162 -0.0278 0.0319  348  PHE B CA  
11389 C C   . PHE B 350  ? 0.3153 0.2917 0.2473 -0.1131 -0.0278 0.0317  348  PHE B C   
11390 O O   . PHE B 350  ? 0.3197 0.2829 0.2446 -0.1158 -0.0309 0.0325  348  PHE B O   
11391 C CB  . PHE B 350  ? 0.2895 0.2712 0.2279 -0.1113 -0.0285 0.0278  348  PHE B CB  
11392 C CG  . PHE B 350  ? 0.3148 0.3064 0.2581 -0.1138 -0.0284 0.0280  348  PHE B CG  
11393 C CD1 . PHE B 350  ? 0.3583 0.3459 0.2984 -0.1206 -0.0317 0.0296  348  PHE B CD1 
11394 C CD2 . PHE B 350  ? 0.2978 0.3026 0.2488 -0.1095 -0.0251 0.0268  348  PHE B CD2 
11395 C CE1 . PHE B 350  ? 0.3576 0.3547 0.3023 -0.1231 -0.0319 0.0300  348  PHE B CE1 
11396 C CE2 . PHE B 350  ? 0.3272 0.3415 0.2828 -0.1118 -0.0252 0.0273  348  PHE B CE2 
11397 C CZ  . PHE B 350  ? 0.3188 0.3294 0.2713 -0.1186 -0.0286 0.0289  348  PHE B CZ  
11398 N N   . VAL B 351  ? 0.2815 0.2648 0.2173 -0.1077 -0.0244 0.0307  349  VAL B N   
11399 C CA  . VAL B 351  ? 0.2859 0.2625 0.2176 -0.1052 -0.0242 0.0309  349  VAL B CA  
11400 C C   . VAL B 351  ? 0.3063 0.2828 0.2339 -0.1118 -0.0249 0.0354  349  VAL B C   
11401 O O   . VAL B 351  ? 0.3347 0.2997 0.2557 -0.1130 -0.0271 0.0364  349  VAL B O   
11402 C CB  . VAL B 351  ? 0.2761 0.2612 0.2130 -0.0984 -0.0205 0.0290  349  VAL B CB  
11403 C CG1 . VAL B 351  ? 0.2911 0.2700 0.2237 -0.0962 -0.0203 0.0295  349  VAL B CG1 
11404 C CG2 . VAL B 351  ? 0.2759 0.2596 0.2163 -0.0920 -0.0201 0.0247  349  VAL B CG2 
11405 N N   . LEU B 352  ? 0.2920 0.2817 0.2235 -0.1163 -0.0230 0.0382  350  LEU B N   
11406 C CA  . LEU B 352  ? 0.2916 0.2821 0.2192 -0.1233 -0.0236 0.0428  350  LEU B CA  
11407 C C   . LEU B 352  ? 0.3147 0.2923 0.2356 -0.1296 -0.0281 0.0445  350  LEU B C   
11408 O O   . LEU B 352  ? 0.3210 0.2903 0.2354 -0.1332 -0.0299 0.0470  350  LEU B O   
11409 C CB  . LEU B 352  ? 0.3124 0.3205 0.2462 -0.1269 -0.0207 0.0455  350  LEU B CB  
11410 C CG  . LEU B 352  ? 0.3424 0.3634 0.2816 -0.1215 -0.0161 0.0447  350  LEU B CG  
11411 C CD1 . LEU B 352  ? 0.3292 0.3672 0.2744 -0.1250 -0.0135 0.0473  350  LEU B CD1 
11412 C CD2 . LEU B 352  ? 0.3474 0.3642 0.2817 -0.1207 -0.0152 0.0461  350  LEU B CD2 
11413 N N   . ASP B 353  ? 0.3289 0.3041 0.2507 -0.1310 -0.0302 0.0430  351  ASP B N   
11414 C CA  . ASP B 353  ? 0.3538 0.3150 0.2685 -0.1364 -0.0348 0.0439  351  ASP B CA  
11415 C C   . ASP B 353  ? 0.3773 0.3215 0.2848 -0.1329 -0.0371 0.0423  351  ASP B C   
11416 O O   . ASP B 353  ? 0.3668 0.2997 0.2669 -0.1377 -0.0402 0.0446  351  ASP B O   
11417 C CB  . ASP B 353  ? 0.3749 0.3354 0.2916 -0.1368 -0.0365 0.0416  351  ASP B CB  
11418 C CG  . ASP B 353  ? 0.3868 0.3620 0.3092 -0.1423 -0.0356 0.0441  351  ASP B CG  
11419 O OD1 . ASP B 353  ? 0.3760 0.3589 0.2990 -0.1478 -0.0347 0.0482  351  ASP B OD1 
11420 O OD2 . ASP B 353  ? 0.4108 0.3900 0.3371 -0.1410 -0.0358 0.0420  351  ASP B OD2 
11421 N N   . PHE B 354  ? 0.3470 0.2892 0.2565 -0.1246 -0.0357 0.0383  352  PHE B N   
11422 C CA  . PHE B 354  ? 0.3484 0.2757 0.2519 -0.1205 -0.0376 0.0366  352  PHE B CA  
11423 C C   . PHE B 354  ? 0.3496 0.2751 0.2493 -0.1218 -0.0372 0.0396  352  PHE B C   
11424 O O   . PHE B 354  ? 0.3721 0.2839 0.2643 -0.1234 -0.0403 0.0407  352  PHE B O   
11425 C CB  . PHE B 354  ? 0.3383 0.2662 0.2459 -0.1114 -0.0358 0.0321  352  PHE B CB  
11426 C CG  . PHE B 354  ? 0.3261 0.2420 0.2290 -0.1065 -0.0370 0.0306  352  PHE B CG  
11427 C CD1 . PHE B 354  ? 0.3642 0.2649 0.2613 -0.1053 -0.0405 0.0289  352  PHE B CD1 
11428 C CD2 . PHE B 354  ? 0.3304 0.2503 0.2345 -0.1030 -0.0349 0.0311  352  PHE B CD2 
11429 C CE1 . PHE B 354  ? 0.3405 0.2307 0.2335 -0.1005 -0.0417 0.0277  352  PHE B CE1 
11430 C CE2 . PHE B 354  ? 0.3573 0.2665 0.2572 -0.0987 -0.0362 0.0299  352  PHE B CE2 
11431 C CZ  . PHE B 354  ? 0.3783 0.2730 0.2730 -0.0973 -0.0396 0.0283  352  PHE B CZ  
11432 N N   . ILE B 355  ? 0.3371 0.2761 0.2417 -0.1210 -0.0335 0.0409  353  ILE B N   
11433 C CA  . ILE B 355  ? 0.3343 0.2725 0.2353 -0.1219 -0.0328 0.0436  353  ILE B CA  
11434 C C   . ILE B 355  ? 0.3648 0.2995 0.2603 -0.1308 -0.0350 0.0484  353  ILE B C   
11435 O O   . ILE B 355  ? 0.3555 0.2799 0.2440 -0.1325 -0.0371 0.0504  353  ILE B O   
11436 C CB  . ILE B 355  ? 0.3421 0.2960 0.2495 -0.1188 -0.0282 0.0437  353  ILE B CB  
11437 C CG1 . ILE B 355  ? 0.3384 0.2934 0.2501 -0.1099 -0.0264 0.0391  353  ILE B CG1 
11438 C CG2 . ILE B 355  ? 0.3527 0.3072 0.2560 -0.1211 -0.0273 0.0471  353  ILE B CG2 
11439 C CD1 . ILE B 355  ? 0.3014 0.2717 0.2198 -0.1065 -0.0220 0.0385  353  ILE B CD1 
11440 N N   . ILE B 356  ? 0.3351 0.2783 0.2335 -0.1369 -0.0348 0.0505  354  ILE B N   
11441 C CA  . ILE B 356  ? 0.3745 0.3153 0.2680 -0.1461 -0.0369 0.0553  354  ILE B CA  
11442 C C   . ILE B 356  ? 0.3817 0.3030 0.2664 -0.1486 -0.0420 0.0553  354  ILE B C   
11443 O O   . ILE B 356  ? 0.4078 0.3207 0.2856 -0.1534 -0.0442 0.0587  354  ILE B O   
11444 C CB  . ILE B 356  ? 0.3699 0.3241 0.2688 -0.1520 -0.0359 0.0573  354  ILE B CB  
11445 C CG1 . ILE B 356  ? 0.3950 0.3683 0.3013 -0.1504 -0.0309 0.0584  354  ILE B CG1 
11446 C CG2 . ILE B 356  ? 0.4036 0.3529 0.2970 -0.1620 -0.0391 0.0620  354  ILE B CG2 
11447 C CD1 . ILE B 356  ? 0.3411 0.3296 0.2549 -0.1534 -0.0293 0.0592  354  ILE B CD1 
11448 N N   . ASP B 357  ? 0.3901 0.3038 0.2747 -0.1451 -0.0439 0.0514  355  ASP B N   
11449 C CA  . ASP B 357  ? 0.4112 0.3058 0.2873 -0.1465 -0.0487 0.0509  355  ASP B CA  
11450 C C   . ASP B 357  ? 0.3868 0.2698 0.2575 -0.1415 -0.0496 0.0502  355  ASP B C   
11451 O O   . ASP B 357  ? 0.3866 0.2558 0.2490 -0.1449 -0.0531 0.0523  355  ASP B O   
11452 C CB  . ASP B 357  ? 0.4064 0.2962 0.2838 -0.1431 -0.0501 0.0466  355  ASP B CB  
11453 C CG  . ASP B 357  ? 0.4140 0.2836 0.2825 -0.1426 -0.0546 0.0452  355  ASP B CG  
11454 O OD1 . ASP B 357  ? 0.4402 0.3011 0.3024 -0.1499 -0.0582 0.0478  355  ASP B OD1 
11455 O OD2 . ASP B 357  ? 0.4101 0.2724 0.2777 -0.1349 -0.0547 0.0416  355  ASP B OD2 
11456 N N   . LEU B 358  ? 0.3893 0.2776 0.2646 -0.1335 -0.0466 0.0473  356  LEU B N   
11457 C CA  . LEU B 358  ? 0.3821 0.2611 0.2530 -0.1286 -0.0473 0.0468  356  LEU B CA  
11458 C C   . LEU B 358  ? 0.3873 0.2659 0.2535 -0.1337 -0.0475 0.0515  356  LEU B C   
11459 O O   . LEU B 358  ? 0.3944 0.2594 0.2531 -0.1340 -0.0504 0.0527  356  LEU B O   
11460 C CB  . LEU B 358  ? 0.3590 0.2462 0.2365 -0.1200 -0.0438 0.0432  356  LEU B CB  
11461 C CG  . LEU B 358  ? 0.3525 0.2329 0.2269 -0.1144 -0.0441 0.0426  356  LEU B CG  
11462 C CD1 . LEU B 358  ? 0.3931 0.2554 0.2606 -0.1123 -0.0482 0.0412  356  LEU B CD1 
11463 C CD2 . LEU B 358  ? 0.3300 0.2199 0.2117 -0.1066 -0.0406 0.0391  356  LEU B CD2 
11464 N N   . ALA B 359  ? 0.3644 0.2580 0.2350 -0.1376 -0.0444 0.0543  357  ALA B N   
11465 C CA  . ALA B 359  ? 0.3755 0.2699 0.2417 -0.1429 -0.0442 0.0591  357  ALA B CA  
11466 C C   . ALA B 359  ? 0.4207 0.3021 0.2786 -0.1508 -0.0487 0.0625  357  ALA B C   
11467 O O   . ALA B 359  ? 0.4156 0.2866 0.2661 -0.1525 -0.0508 0.0650  357  ALA B O   
11468 C CB  . ALA B 359  ? 0.4156 0.3291 0.2882 -0.1461 -0.0400 0.0614  357  ALA B CB  
11469 N N   . ARG B 360  ? 0.4050 0.2866 0.2639 -0.1556 -0.0503 0.0626  358  ARG B N   
11470 C CA  . ARG B 360  ? 0.4309 0.3003 0.2818 -0.1637 -0.0547 0.0658  358  ARG B CA  
11471 C C   . ARG B 360  ? 0.3995 0.2480 0.2418 -0.1607 -0.0589 0.0643  358  ARG B C   
11472 O O   . ARG B 360  ? 0.4462 0.2861 0.2816 -0.1630 -0.0616 0.0666  358  ARG B O   
11473 C CB  . ARG B 360  ? 0.4394 0.3133 0.2937 -0.1673 -0.0557 0.0649  358  ARG B CB  
11474 C CG  . ARG B 360  ? 0.4802 0.3730 0.3412 -0.1724 -0.0528 0.0678  358  ARG B CG  
11475 C CD  . ARG B 360  ? 0.5553 0.4497 0.4174 -0.1762 -0.0550 0.0673  358  ARG B CD  
11476 N NE  . ARG B 360  ? 0.5575 0.4714 0.4275 -0.1798 -0.0519 0.0693  358  ARG B NE  
11477 C CZ  . ARG B 360  ? 0.5608 0.4858 0.4386 -0.1782 -0.0497 0.0673  358  ARG B CZ  
11478 N NH1 . ARG B 360  ? 0.6375 0.5560 0.5162 -0.1736 -0.0503 0.0632  358  ARG B NH1 
11479 N NH2 . ARG B 360  ? 0.6481 0.5912 0.5330 -0.1812 -0.0470 0.0694  358  ARG B NH2 
11480 N N   . ARG B 361  ? 0.4449 0.2877 0.2887 -0.1530 -0.0593 0.0593  359  ARG B N   
11481 C CA  . ARG B 361  ? 0.4701 0.2930 0.3056 -0.1502 -0.0636 0.0577  359  ARG B CA  
11482 C C   . ARG B 361  ? 0.4299 0.2469 0.2623 -0.1447 -0.0635 0.0578  359  ARG B C   
11483 O O   . ARG B 361  ? 0.4551 0.2553 0.2793 -0.1438 -0.0673 0.0579  359  ARG B O   
11484 C CB  . ARG B 361  ? 0.5020 0.3204 0.3396 -0.1445 -0.0643 0.0525  359  ARG B CB  
11485 C CG  . ARG B 361  ? 0.5055 0.3336 0.3511 -0.1354 -0.0606 0.0483  359  ARG B CG  
11486 C CD  . ARG B 361  ? 0.4591 0.2842 0.3070 -0.1312 -0.0612 0.0436  359  ARG B CD  
11487 N NE  . ARG B 361  ? 0.4232 0.2629 0.2807 -0.1252 -0.0570 0.0405  359  ARG B NE  
11488 C CZ  . ARG B 361  ? 0.4303 0.2699 0.2906 -0.1167 -0.0554 0.0372  359  ARG B CZ  
11489 N NH1 . ARG B 361  ? 0.4362 0.2629 0.2910 -0.1126 -0.0576 0.0365  359  ARG B NH1 
11490 N NH2 . ARG B 361  ? 0.3974 0.2505 0.2663 -0.1122 -0.0517 0.0348  359  ARG B NH2 
11491 N N   . SER B 362  ? 0.4258 0.2559 0.2639 -0.1412 -0.0594 0.0578  360  SER B N   
11492 C CA  . SER B 362  ? 0.4316 0.2570 0.2668 -0.1364 -0.0594 0.0581  360  SER B CA  
11493 C C   . SER B 362  ? 0.4261 0.2531 0.2569 -0.1423 -0.0593 0.0634  360  SER B C   
11494 O O   . SER B 362  ? 0.4750 0.2966 0.3020 -0.1392 -0.0599 0.0642  360  SER B O   
11495 C CB  . SER B 362  ? 0.4521 0.2893 0.2954 -0.1282 -0.0554 0.0545  360  SER B CB  
11496 O OG  . SER B 362  ? 0.3995 0.2544 0.2493 -0.1308 -0.0513 0.0561  360  SER B OG  
11497 N N   . GLY B 363  ? 0.4149 0.2501 0.2464 -0.1506 -0.0584 0.0671  361  GLY B N   
11498 C CA  . GLY B 363  ? 0.4391 0.2765 0.2664 -0.1565 -0.0580 0.0724  361  GLY B CA  
11499 C C   . GLY B 363  ? 0.4531 0.3045 0.2854 -0.1526 -0.0535 0.0725  361  GLY B C   
11500 O O   . GLY B 363  ? 0.4478 0.2966 0.2751 -0.1537 -0.0536 0.0754  361  GLY B O   
11501 N N   . ARG B 364  ? 0.4497 0.3154 0.2911 -0.1482 -0.0496 0.0692  362  ARG B N   
11502 C CA  . ARG B 364  ? 0.4831 0.3626 0.3297 -0.1440 -0.0451 0.0686  362  ARG B CA  
11503 C C   . ARG B 364  ? 0.4415 0.3393 0.2956 -0.1476 -0.0412 0.0696  362  ARG B C   
11504 O O   . ARG B 364  ? 0.4626 0.3641 0.3215 -0.1480 -0.0412 0.0676  362  ARG B O   
11505 C CB  . ARG B 364  ? 0.4428 0.3223 0.2940 -0.1341 -0.0441 0.0633  362  ARG B CB  
11506 C CG  . ARG B 364  ? 0.4378 0.3007 0.2832 -0.1292 -0.0477 0.0616  362  ARG B CG  
11507 C CD  . ARG B 364  ? 0.4763 0.3379 0.3177 -0.1273 -0.0473 0.0635  362  ARG B CD  
11508 N NE  . ARG B 364  ? 0.4891 0.3344 0.3243 -0.1234 -0.0512 0.0625  362  ARG B NE  
11509 C CZ  . ARG B 364  ? 0.4761 0.3188 0.3138 -0.1151 -0.0514 0.0586  362  ARG B CZ  
11510 N NH1 . ARG B 364  ? 0.4567 0.3114 0.3026 -0.1099 -0.0478 0.0551  362  ARG B NH1 
11511 N NH2 . ARG B 364  ? 0.5098 0.3375 0.3416 -0.1120 -0.0552 0.0582  362  ARG B NH2 
11512 N N   . ARG B 365  ? 0.4236 0.3327 0.2786 -0.1501 -0.0381 0.0727  363  ARG B N   
11513 C CA  . ARG B 365  ? 0.4392 0.3671 0.3024 -0.1510 -0.0337 0.0727  363  ARG B CA  
11514 C C   . ARG B 365  ? 0.3696 0.3049 0.2390 -0.1419 -0.0304 0.0681  363  ARG B C   
11515 O O   . ARG B 365  ? 0.3897 0.3243 0.2570 -0.1378 -0.0294 0.0677  363  ARG B O   
11516 C CB  . ARG B 365  ? 0.4644 0.4025 0.3262 -0.1574 -0.0312 0.0779  363  ARG B CB  
11517 C CG  . ARG B 365  ? 0.4626 0.4205 0.3330 -0.1590 -0.0269 0.0783  363  ARG B CG  
11518 C CD  . ARG B 365  ? 0.4760 0.4432 0.3445 -0.1668 -0.0250 0.0841  363  ARG B CD  
11519 N NE  . ARG B 365  ? 0.5019 0.4874 0.3785 -0.1694 -0.0215 0.0850  363  ARG B NE  
11520 C CZ  . ARG B 365  ? 0.4848 0.4863 0.3650 -0.1691 -0.0168 0.0865  363  ARG B CZ  
11521 N NH1 . ARG B 365  ? 0.4789 0.4807 0.3551 -0.1668 -0.0149 0.0875  363  ARG B NH1 
11522 N NH2 . ARG B 365  ? 0.4462 0.4640 0.3346 -0.1703 -0.0140 0.0867  363  ARG B NH2 
11523 N N   . ILE B 366  ? 0.4087 0.3501 0.2852 -0.1386 -0.0293 0.0646  364  ILE B N   
11524 C CA  . ILE B 366  ? 0.3752 0.3228 0.2576 -0.1301 -0.0266 0.0600  364  ILE B CA  
11525 C C   . ILE B 366  ? 0.4070 0.3733 0.2960 -0.1301 -0.0217 0.0607  364  ILE B C   
11526 O O   . ILE B 366  ? 0.3733 0.3489 0.2660 -0.1350 -0.0206 0.0625  364  ILE B O   
11527 C CB  . ILE B 366  ? 0.3426 0.2857 0.2288 -0.1262 -0.0281 0.0558  364  ILE B CB  
11528 C CG1 . ILE B 366  ? 0.3547 0.2790 0.2340 -0.1257 -0.0328 0.0550  364  ILE B CG1 
11529 C CG2 . ILE B 366  ? 0.3110 0.2614 0.2038 -0.1178 -0.0251 0.0513  364  ILE B CG2 
11530 C CD1 . ILE B 366  ? 0.3959 0.3148 0.2780 -0.1221 -0.0344 0.0510  364  ILE B CD1 
11531 N N   . MET B 367  ? 0.3618 0.3336 0.2520 -0.1248 -0.0188 0.0593  365  MET B N   
11532 C CA  . MET B 367  ? 0.3488 0.3377 0.2452 -0.1234 -0.0141 0.0592  365  MET B CA  
11533 C C   . MET B 367  ? 0.3376 0.3321 0.2417 -0.1179 -0.0127 0.0548  365  MET B C   
11534 O O   . MET B 367  ? 0.3247 0.3124 0.2294 -0.1117 -0.0137 0.0510  365  MET B O   
11535 C CB  . MET B 367  ? 0.3299 0.3216 0.2239 -0.1195 -0.0117 0.0591  365  MET B CB  
11536 C CG  . MET B 367  ? 0.3449 0.3278 0.2301 -0.1237 -0.0137 0.0629  365  MET B CG  
11537 S SD  . MET B 367  ? 0.3846 0.3720 0.2665 -0.1199 -0.0108 0.0632  365  MET B SD  
11538 C CE  . MET B 367  ? 0.4292 0.4203 0.3176 -0.1099 -0.0089 0.0570  365  MET B CE  
11539 N N   . VAL B 368  ? 0.2978 0.3047 0.2079 -0.1203 -0.0106 0.0554  366  VAL B N   
11540 C CA  . VAL B 368  ? 0.3082 0.3204 0.2255 -0.1158 -0.0096 0.0516  366  VAL B CA  
11541 C C   . VAL B 368  ? 0.3406 0.3692 0.2640 -0.1128 -0.0049 0.0511  366  VAL B C   
11542 O O   . VAL B 368  ? 0.3098 0.3502 0.2358 -0.1172 -0.0028 0.0540  366  VAL B O   
11543 C CB  . VAL B 368  ? 0.3335 0.3448 0.2527 -0.1208 -0.0119 0.0524  366  VAL B CB  
11544 C CG1 . VAL B 368  ? 0.3603 0.3763 0.2865 -0.1158 -0.0109 0.0484  366  VAL B CG1 
11545 C CG2 . VAL B 368  ? 0.3513 0.3455 0.2636 -0.1239 -0.0167 0.0531  366  VAL B CG2 
11546 N N   . ARG B 369  ? 0.2880 0.3176 0.2138 -0.1053 -0.0031 0.0473  367  ARG B N   
11547 C CA  . ARG B 369  ? 0.2943 0.3382 0.2257 -0.1014 0.0012  0.0461  367  ARG B CA  
11548 C C   . ARG B 369  ? 0.3123 0.3620 0.2509 -0.0992 0.0017  0.0436  367  ARG B C   
11549 O O   . ARG B 369  ? 0.2854 0.3282 0.2253 -0.0947 0.0002  0.0401  367  ARG B O   
11550 C CB  . ARG B 369  ? 0.3011 0.3431 0.2309 -0.0946 0.0027  0.0434  367  ARG B CB  
11551 C CG  . ARG B 369  ? 0.3095 0.3656 0.2445 -0.0904 0.0072  0.0420  367  ARG B CG  
11552 C CD  . ARG B 369  ? 0.2921 0.3455 0.2267 -0.0831 0.0082  0.0383  367  ARG B CD  
11553 N NE  . ARG B 369  ? 0.3258 0.3724 0.2534 -0.0833 0.0075  0.0395  367  ARG B NE  
11554 C CZ  . ARG B 369  ? 0.3433 0.3813 0.2683 -0.0785 0.0062  0.0368  367  ARG B CZ  
11555 N NH1 . ARG B 369  ? 0.3203 0.3558 0.2493 -0.0733 0.0057  0.0329  367  ARG B NH1 
11556 N NH2 . ARG B 369  ? 0.3216 0.3537 0.2400 -0.0792 0.0054  0.0382  367  ARG B NH2 
11557 N N   . LEU B 370  ? 0.2825 0.3451 0.2258 -0.1024 0.0037  0.0457  368  LEU B N   
11558 C CA  . LEU B 370  ? 0.2570 0.3270 0.2074 -0.1002 0.0045  0.0436  368  LEU B CA  
11559 C C   . LEU B 370  ? 0.2808 0.3612 0.2358 -0.0935 0.0085  0.0412  368  LEU B C   
11560 O O   . LEU B 370  ? 0.3120 0.4031 0.2677 -0.0939 0.0118  0.0431  368  LEU B O   
11561 C CB  . LEU B 370  ? 0.2920 0.3708 0.2454 -0.1071 0.0043  0.0471  368  LEU B CB  
11562 C CG  . LEU B 370  ? 0.3070 0.3931 0.2675 -0.1060 0.0045  0.0455  368  LEU B CG  
11563 C CD1 . LEU B 370  ? 0.3179 0.3914 0.2774 -0.1047 0.0009  0.0427  368  LEU B CD1 
11564 C CD2 . LEU B 370  ? 0.3005 0.3976 0.2640 -0.1131 0.0047  0.0495  368  LEU B CD2 
11565 N N   . VAL B 371  ? 0.2492 0.3259 0.2067 -0.0873 0.0083  0.0371  369  VAL B N   
11566 C CA  . VAL B 371  ? 0.2754 0.3608 0.2374 -0.0808 0.0116  0.0345  369  VAL B CA  
11567 C C   . VAL B 371  ? 0.2580 0.3485 0.2265 -0.0794 0.0115  0.0329  369  VAL B C   
11568 O O   . VAL B 371  ? 0.2822 0.3675 0.2510 -0.0827 0.0087  0.0332  369  VAL B O   
11569 C CB  . VAL B 371  ? 0.2669 0.3438 0.2262 -0.0746 0.0115  0.0311  369  VAL B CB  
11570 C CG1 . VAL B 371  ? 0.2798 0.3502 0.2321 -0.0762 0.0110  0.0327  369  VAL B CG1 
11571 C CG2 . VAL B 371  ? 0.2678 0.3337 0.2275 -0.0725 0.0084  0.0283  369  VAL B CG2 
11572 N N   . LYS B 372  ? 0.2476 0.3476 0.2209 -0.0742 0.0146  0.0311  370  LYS B N   
11573 C CA  . LYS B 372  ? 0.2425 0.3457 0.2215 -0.0720 0.0142  0.0291  370  LYS B CA  
11574 C C   . LYS B 372  ? 0.2401 0.3323 0.2185 -0.0670 0.0124  0.0252  370  LYS B C   
11575 O O   . LYS B 372  ? 0.2383 0.3242 0.2172 -0.0683 0.0098  0.0244  370  LYS B O   
11576 C CB  . LYS B 372  ? 0.2456 0.3637 0.2305 -0.0688 0.0179  0.0290  370  LYS B CB  
11577 C CG  . LYS B 372  ? 0.2596 0.3894 0.2461 -0.0746 0.0192  0.0333  370  LYS B CG  
11578 C CD  . LYS B 372  ? 0.2901 0.4358 0.2827 -0.0717 0.0228  0.0336  370  LYS B CD  
11579 C CE  . LYS B 372  ? 0.3144 0.4715 0.3081 -0.0778 0.0242  0.0381  370  LYS B CE  
11580 N NZ  . LYS B 372  ? 0.3125 0.4864 0.3125 -0.0750 0.0279  0.0387  370  LYS B NZ  
11581 N N   . GLY B 373  ? 0.2706 0.3599 0.2473 -0.0617 0.0137  0.0229  371  GLY B N   
11582 C CA  . GLY B 373  ? 0.2156 0.2946 0.1916 -0.0574 0.0120  0.0195  371  GLY B CA  
11583 C C   . GLY B 373  ? 0.2313 0.3127 0.2088 -0.0506 0.0143  0.0166  371  GLY B C   
11584 O O   . GLY B 373  ? 0.2737 0.3651 0.2553 -0.0482 0.0169  0.0162  371  GLY B O   
11585 N N   . ALA B 374  ? 0.2096 0.2816 0.1838 -0.0475 0.0132  0.0145  372  ALA B N   
11586 C CA  . ALA B 374  ? 0.2115 0.2846 0.1858 -0.0418 0.0151  0.0120  372  ALA B CA  
11587 C C   . ALA B 374  ? 0.2173 0.2867 0.1947 -0.0370 0.0144  0.0087  372  ALA B C   
11588 O O   . ALA B 374  ? 0.2543 0.3249 0.2322 -0.0322 0.0160  0.0065  372  ALA B O   
11589 C CB  . ALA B 374  ? 0.2283 0.2943 0.1967 -0.0414 0.0145  0.0120  372  ALA B CB  
11590 N N   . TYR B 375  ? 0.2173 0.2820 0.1964 -0.0382 0.0122  0.0082  373  TYR B N   
11591 C CA  . TYR B 375  ? 0.2114 0.2711 0.1927 -0.0342 0.0113  0.0052  373  TYR B CA  
11592 C C   . TYR B 375  ? 0.2060 0.2715 0.1926 -0.0333 0.0118  0.0046  373  TYR B C   
11593 O O   . TYR B 375  ? 0.2048 0.2656 0.1930 -0.0317 0.0104  0.0029  373  TYR B O   
11594 C CB  . TYR B 375  ? 0.2166 0.2649 0.1950 -0.0354 0.0082  0.0047  373  TYR B CB  
11595 C CG  . TYR B 375  ? 0.2260 0.2677 0.1992 -0.0361 0.0072  0.0053  373  TYR B CG  
11596 C CD1 . TYR B 375  ? 0.2376 0.2790 0.2071 -0.0408 0.0067  0.0082  373  TYR B CD1 
11597 C CD2 . TYR B 375  ? 0.2425 0.2783 0.2142 -0.0323 0.0065  0.0032  373  TYR B CD2 
11598 C CE1 . TYR B 375  ? 0.2332 0.2683 0.1975 -0.0415 0.0056  0.0090  373  TYR B CE1 
11599 C CE2 . TYR B 375  ? 0.2664 0.2963 0.2333 -0.0330 0.0054  0.0039  373  TYR B CE2 
11600 C CZ  . TYR B 375  ? 0.2436 0.2731 0.2067 -0.0375 0.0049  0.0067  373  TYR B CZ  
11601 O OH  . TYR B 375  ? 0.2635 0.2869 0.2215 -0.0380 0.0037  0.0075  373  TYR B OH  
11602 N N   . TRP B 376  ? 0.2038 0.2799 0.1932 -0.0344 0.0138  0.0062  374  TRP B N   
11603 C CA  . TRP B 376  ? 0.2078 0.2895 0.2020 -0.0346 0.0138  0.0062  374  TRP B CA  
11604 C C   . TRP B 376  ? 0.2148 0.2947 0.2119 -0.0294 0.0139  0.0033  374  TRP B C   
11605 O O   . TRP B 376  ? 0.2032 0.2795 0.2018 -0.0296 0.0123  0.0025  374  TRP B O   
11606 C CB  . TRP B 376  ? 0.2078 0.3021 0.2050 -0.0357 0.0162  0.0083  374  TRP B CB  
11607 C CG  . TRP B 376  ? 0.2066 0.3067 0.2087 -0.0365 0.0158  0.0086  374  TRP B CG  
11608 C CD1 . TRP B 376  ? 0.2120 0.3120 0.2147 -0.0415 0.0137  0.0104  374  TRP B CD1 
11609 C CD2 . TRP B 376  ? 0.2219 0.3283 0.2286 -0.0321 0.0172  0.0072  374  TRP B CD2 
11610 N NE1 . TRP B 376  ? 0.2188 0.3250 0.2262 -0.0406 0.0138  0.0101  374  TRP B NE1 
11611 C CE2 . TRP B 376  ? 0.2215 0.3317 0.2315 -0.0347 0.0159  0.0083  374  TRP B CE2 
11612 C CE3 . TRP B 376  ? 0.2786 0.3873 0.2865 -0.0262 0.0193  0.0052  374  TRP B CE3 
11613 C CZ2 . TRP B 376  ? 0.2141 0.3308 0.2289 -0.0316 0.0167  0.0075  374  TRP B CZ2 
11614 C CZ3 . TRP B 376  ? 0.2655 0.3801 0.2780 -0.0230 0.0200  0.0044  374  TRP B CZ3 
11615 C CH2 . TRP B 376  ? 0.2564 0.3750 0.2723 -0.0256 0.0188  0.0056  374  TRP B CH2 
11616 N N   . ASP B 377  ? 0.1889 0.2710 0.1863 -0.0247 0.0159  0.0017  375  ASP B N   
11617 C CA  . ASP B 377  ? 0.2221 0.3027 0.2221 -0.0200 0.0160  -0.0008 375  ASP B CA  
11618 C C   . ASP B 377  ? 0.2154 0.2854 0.2139 -0.0196 0.0137  -0.0025 375  ASP B C   
11619 O O   . ASP B 377  ? 0.2080 0.2763 0.2090 -0.0179 0.0129  -0.0038 375  ASP B O   
11620 C CB  . ASP B 377  ? 0.2683 0.3510 0.2678 -0.0152 0.0182  -0.0024 375  ASP B CB  
11621 C CG  . ASP B 377  ? 0.3382 0.4320 0.3404 -0.0138 0.0208  -0.0015 375  ASP B CG  
11622 O OD1 . ASP B 377  ? 0.4486 0.5472 0.4550 -0.0124 0.0211  -0.0017 375  ASP B OD1 
11623 O OD2 . ASP B 377  ? 0.3838 0.4818 0.3840 -0.0140 0.0225  -0.0005 375  ASP B OD2 
11624 N N   . ALA B 378  ? 0.2100 0.2728 0.2043 -0.0209 0.0125  -0.0024 376  ALA B N   
11625 C CA  . ALA B 378  ? 0.1922 0.2454 0.1852 -0.0202 0.0103  -0.0039 376  ALA B CA  
11626 C C   . ALA B 378  ? 0.2052 0.2556 0.1989 -0.0233 0.0084  -0.0032 376  ALA B C   
11627 O O   . ALA B 378  ? 0.2006 0.2459 0.1952 -0.0218 0.0072  -0.0048 376  ALA B O   
11628 C CB  . ALA B 378  ? 0.2069 0.2537 0.1954 -0.0208 0.0094  -0.0037 376  ALA B CB  
11629 N N   . GLU B 379  ? 0.1965 0.2501 0.1896 -0.0277 0.0081  -0.0009 377  GLU B N   
11630 C CA  . GLU B 379  ? 0.1908 0.2412 0.1838 -0.0309 0.0061  -0.0003 377  GLU B CA  
11631 C C   . GLU B 379  ? 0.1975 0.2524 0.1948 -0.0295 0.0064  -0.0011 377  GLU B C   
11632 O O   . GLU B 379  ? 0.1893 0.2394 0.1866 -0.0298 0.0048  -0.0020 377  GLU B O   
11633 C CB  . GLU B 379  ? 0.2038 0.2562 0.1948 -0.0364 0.0054  0.0025  377  GLU B CB  
11634 C CG  . GLU B 379  ? 0.2151 0.2624 0.2012 -0.0384 0.0048  0.0037  377  GLU B CG  
11635 C CD  . GLU B 379  ? 0.2232 0.2589 0.2057 -0.0386 0.0023  0.0028  377  GLU B CD  
11636 O OE1 . GLU B 379  ? 0.2385 0.2697 0.2220 -0.0371 0.0011  0.0011  377  GLU B OE1 
11637 O OE2 . GLU B 379  ? 0.2376 0.2686 0.2159 -0.0401 0.0015  0.0039  377  GLU B OE2 
11638 N N   . ILE B 380  ? 0.2048 0.2690 0.2055 -0.0278 0.0085  -0.0008 378  ILE B N   
11639 C CA  . ILE B 380  ? 0.1732 0.2416 0.1779 -0.0260 0.0088  -0.0016 378  ILE B CA  
11640 C C   . ILE B 380  ? 0.1854 0.2479 0.1906 -0.0219 0.0085  -0.0042 378  ILE B C   
11641 O O   . ILE B 380  ? 0.1850 0.2448 0.1911 -0.0218 0.0073  -0.0049 378  ILE B O   
11642 C CB  . ILE B 380  ? 0.1965 0.2760 0.2047 -0.0243 0.0112  -0.0008 378  ILE B CB  
11643 C CG1 . ILE B 380  ? 0.2094 0.2957 0.2175 -0.0287 0.0117  0.0020  378  ILE B CG1 
11644 C CG2 . ILE B 380  ? 0.1884 0.2718 0.2006 -0.0225 0.0112  -0.0015 378  ILE B CG2 
11645 C CD1 . ILE B 380  ? 0.1987 0.2849 0.2069 -0.0338 0.0096  0.0036  378  ILE B CD1 
11646 N N   . LYS B 381  ? 0.1661 0.2265 0.1703 -0.0185 0.0095  -0.0054 379  LYS B N   
11647 C CA  . LYS B 381  ? 0.1779 0.2331 0.1828 -0.0148 0.0091  -0.0076 379  LYS B CA  
11648 C C   . LYS B 381  ? 0.1910 0.2378 0.1940 -0.0162 0.0070  -0.0083 379  LYS B C   
11649 O O   . LYS B 381  ? 0.1956 0.2400 0.2000 -0.0147 0.0064  -0.0094 379  LYS B O   
11650 C CB  . LYS B 381  ? 0.1879 0.2417 0.1916 -0.0117 0.0102  -0.0088 379  LYS B CB  
11651 C CG  . LYS B 381  ? 0.1751 0.2233 0.1793 -0.0083 0.0096  -0.0109 379  LYS B CG  
11652 C CD  . LYS B 381  ? 0.1731 0.2202 0.1759 -0.0054 0.0105  -0.0120 379  LYS B CD  
11653 C CE  . LYS B 381  ? 0.2017 0.2441 0.2055 -0.0023 0.0100  -0.0139 379  LYS B CE  
11654 N NZ  . LYS B 381  ? 0.1960 0.2368 0.1980 0.0002  0.0105  -0.0150 379  LYS B NZ  
11655 N N   . ARG B 382  ? 0.1825 0.2246 0.1819 -0.0189 0.0058  -0.0074 380  ARG B N   
11656 C CA  . ARG B 382  ? 0.1794 0.2130 0.1767 -0.0195 0.0039  -0.0082 380  ARG B CA  
11657 C C   . ARG B 382  ? 0.1992 0.2319 0.1971 -0.0214 0.0027  -0.0080 380  ARG B C   
11658 O O   . ARG B 382  ? 0.2001 0.2281 0.1981 -0.0198 0.0019  -0.0095 380  ARG B O   
11659 C CB  . ARG B 382  ? 0.2236 0.2524 0.2168 -0.0220 0.0027  -0.0070 380  ARG B CB  
11660 C CG  . ARG B 382  ? 0.3059 0.3255 0.2966 -0.0221 0.0006  -0.0078 380  ARG B CG  
11661 C CD  . ARG B 382  ? 0.3131 0.3295 0.3052 -0.0179 0.0007  -0.0099 380  ARG B CD  
11662 N NE  . ARG B 382  ? 0.3699 0.3783 0.3599 -0.0176 -0.0011 -0.0106 380  ARG B NE  
11663 C CZ  . ARG B 382  ? 0.4680 0.4710 0.4548 -0.0181 -0.0024 -0.0102 380  ARG B CZ  
11664 N NH1 . ARG B 382  ? 0.4552 0.4597 0.4402 -0.0191 -0.0020 -0.0090 380  ARG B NH1 
11665 N NH2 . ARG B 382  ? 0.4550 0.4511 0.4402 -0.0175 -0.0040 -0.0109 380  ARG B NH2 
11666 N N   . ALA B 383  ? 0.1915 0.2291 0.1897 -0.0248 0.0026  -0.0063 381  ALA B N   
11667 C CA  . ALA B 383  ? 0.1737 0.2105 0.1720 -0.0269 0.0013  -0.0062 381  ALA B CA  
11668 C C   . ALA B 383  ? 0.2010 0.2406 0.2028 -0.0238 0.0020  -0.0075 381  ALA B C   
11669 O O   . ALA B 383  ? 0.1837 0.2193 0.1850 -0.0237 0.0009  -0.0085 381  ALA B O   
11670 C CB  . ALA B 383  ? 0.1675 0.2099 0.1659 -0.0314 0.0011  -0.0039 381  ALA B CB  
11671 N N   . GLN B 384  ? 0.1549 0.2011 0.1598 -0.0211 0.0039  -0.0077 382  GLN B N   
11672 C CA  . GLN B 384  ? 0.1720 0.2205 0.1800 -0.0180 0.0046  -0.0088 382  GLN B CA  
11673 C C   . GLN B 384  ? 0.1678 0.2094 0.1752 -0.0150 0.0043  -0.0108 382  GLN B C   
11674 O O   . GLN B 384  ? 0.1978 0.2376 0.2059 -0.0141 0.0038  -0.0117 382  GLN B O   
11675 C CB  . GLN B 384  ? 0.1826 0.2389 0.1937 -0.0155 0.0066  -0.0086 382  GLN B CB  
11676 C CG  . GLN B 384  ? 0.1768 0.2416 0.1896 -0.0180 0.0070  -0.0066 382  GLN B CG  
11677 C CD  . GLN B 384  ? 0.2034 0.2760 0.2192 -0.0149 0.0091  -0.0065 382  GLN B CD  
11678 O OE1 . GLN B 384  ? 0.2252 0.2963 0.2410 -0.0114 0.0102  -0.0077 382  GLN B OE1 
11679 N NE2 . GLN B 384  ? 0.1791 0.2602 0.1976 -0.0160 0.0095  -0.0050 382  GLN B NE2 
11680 N N   . LEU B 385  ? 0.1930 0.2313 0.1992 -0.0135 0.0046  -0.0114 383  LEU B N   
11681 C CA  . LEU B 385  ? 0.1878 0.2203 0.1938 -0.0108 0.0043  -0.0130 383  LEU B CA  
11682 C C   . LEU B 385  ? 0.2035 0.2298 0.2075 -0.0122 0.0027  -0.0135 383  LEU B C   
11683 O O   . LEU B 385  ? 0.2043 0.2279 0.2092 -0.0101 0.0025  -0.0147 383  LEU B O   
11684 C CB  . LEU B 385  ? 0.2256 0.2552 0.2300 -0.0097 0.0044  -0.0134 383  LEU B CB  
11685 C CG  . LEU B 385  ? 0.2253 0.2592 0.2312 -0.0073 0.0060  -0.0136 383  LEU B CG  
11686 C CD1 . LEU B 385  ? 0.2566 0.2867 0.2602 -0.0067 0.0057  -0.0139 383  LEU B CD1 
11687 C CD2 . LEU B 385  ? 0.2534 0.2880 0.2620 -0.0042 0.0066  -0.0148 383  LEU B CD2 
11688 N N   . ASP B 386  ? 0.2223 0.2463 0.2235 -0.0155 0.0014  -0.0125 384  ASP B N   
11689 C CA  . ASP B 386  ? 0.2065 0.2235 0.2050 -0.0164 -0.0002 -0.0131 384  ASP B CA  
11690 C C   . ASP B 386  ? 0.2338 0.2514 0.2321 -0.0181 -0.0009 -0.0130 384  ASP B C   
11691 O O   . ASP B 386  ? 0.2530 0.2646 0.2486 -0.0188 -0.0022 -0.0137 384  ASP B O   
11692 C CB  . ASP B 386  ? 0.2216 0.2339 0.2163 -0.0191 -0.0015 -0.0121 384  ASP B CB  
11693 C CG  . ASP B 386  ? 0.2854 0.2950 0.2794 -0.0172 -0.0013 -0.0124 384  ASP B CG  
11694 O OD1 . ASP B 386  ? 0.2531 0.2638 0.2495 -0.0139 -0.0004 -0.0135 384  ASP B OD1 
11695 O OD2 . ASP B 386  ? 0.2779 0.2842 0.2688 -0.0192 -0.0023 -0.0114 384  ASP B OD2 
11696 N N   . GLY B 387  ? 0.2109 0.2356 0.2119 -0.0185 0.0000  -0.0124 385  GLY B N   
11697 C CA  . GLY B 387  ? 0.1958 0.2219 0.1968 -0.0201 -0.0008 -0.0122 385  GLY B CA  
11698 C C   . GLY B 387  ? 0.2402 0.2626 0.2374 -0.0243 -0.0027 -0.0114 385  GLY B C   
11699 O O   . GLY B 387  ? 0.2350 0.2535 0.2302 -0.0252 -0.0040 -0.0121 385  GLY B O   
11700 N N   . LEU B 388  ? 0.2065 0.2300 0.2026 -0.0272 -0.0030 -0.0098 386  LEU B N   
11701 C CA  . LEU B 388  ? 0.2344 0.2533 0.2264 -0.0315 -0.0051 -0.0089 386  LEU B CA  
11702 C C   . LEU B 388  ? 0.2223 0.2474 0.2155 -0.0351 -0.0057 -0.0074 386  LEU B C   
11703 O O   . LEU B 388  ? 0.2227 0.2562 0.2199 -0.0341 -0.0044 -0.0069 386  LEU B O   
11704 C CB  . LEU B 388  ? 0.2271 0.2431 0.2167 -0.0331 -0.0054 -0.0078 386  LEU B CB  
11705 C CG  . LEU B 388  ? 0.2016 0.2109 0.1900 -0.0296 -0.0053 -0.0094 386  LEU B CG  
11706 C CD1 . LEU B 388  ? 0.2690 0.2746 0.2545 -0.0310 -0.0059 -0.0083 386  LEU B CD1 
11707 C CD2 . LEU B 388  ? 0.2367 0.2383 0.2227 -0.0283 -0.0066 -0.0111 386  LEU B CD2 
11708 N N   . ALA B 389  ? 0.2317 0.2523 0.2210 -0.0394 -0.0079 -0.0066 387  ALA B N   
11709 C CA  . ALA B 389  ? 0.2153 0.2407 0.2052 -0.0429 -0.0090 -0.0055 387  ALA B CA  
11710 C C   . ALA B 389  ? 0.2194 0.2555 0.2132 -0.0450 -0.0079 -0.0031 387  ALA B C   
11711 O O   . ALA B 389  ? 0.2393 0.2832 0.2363 -0.0456 -0.0077 -0.0024 387  ALA B O   
11712 C CB  . ALA B 389  ? 0.2676 0.2852 0.2521 -0.0474 -0.0118 -0.0051 387  ALA B CB  
11713 N N   . ASP B 390  ? 0.2440 0.2809 0.2373 -0.0458 -0.0071 -0.0019 388  ASP B N   
11714 C CA  . ASP B 390  ? 0.2193 0.2664 0.2159 -0.0477 -0.0057 0.0004  388  ASP B CA  
11715 C C   . ASP B 390  ? 0.1999 0.2460 0.1957 -0.0462 -0.0043 0.0007  388  ASP B C   
11716 O O   . ASP B 390  ? 0.2260 0.2638 0.2191 -0.0440 -0.0046 -0.0008 388  ASP B O   
11717 C CB  . ASP B 390  ? 0.2191 0.2684 0.2143 -0.0540 -0.0077 0.0027  388  ASP B CB  
11718 C CG  . ASP B 390  ? 0.2552 0.3177 0.2554 -0.0555 -0.0064 0.0049  388  ASP B CG  
11719 O OD1 . ASP B 390  ? 0.2524 0.3217 0.2555 -0.0532 -0.0040 0.0055  388  ASP B OD1 
11720 O OD2 . ASP B 390  ? 0.2472 0.3135 0.2483 -0.0589 -0.0079 0.0059  388  ASP B OD2 
11721 N N   . PHE B 391  ? 0.2069 0.2617 0.2051 -0.0475 -0.0028 0.0026  389  PHE B N   
11722 C CA  . PHE B 391  ? 0.2039 0.2582 0.2008 -0.0467 -0.0015 0.0032  389  PHE B CA  
11723 C C   . PHE B 391  ? 0.2110 0.2597 0.2032 -0.0519 -0.0033 0.0050  389  PHE B C   
11724 O O   . PHE B 391  ? 0.2088 0.2577 0.1998 -0.0567 -0.0051 0.0065  389  PHE B O   
11725 C CB  . PHE B 391  ? 0.2146 0.2807 0.2157 -0.0456 0.0011  0.0044  389  PHE B CB  
11726 C CG  . PHE B 391  ? 0.1999 0.2709 0.2052 -0.0405 0.0028  0.0028  389  PHE B CG  
11727 C CD1 . PHE B 391  ? 0.1924 0.2597 0.1977 -0.0355 0.0039  0.0006  389  PHE B CD1 
11728 C CD2 . PHE B 391  ? 0.2071 0.2861 0.2163 -0.0409 0.0028  0.0034  389  PHE B CD2 
11729 C CE1 . PHE B 391  ? 0.2007 0.2716 0.2095 -0.0310 0.0052  -0.0009 389  PHE B CE1 
11730 C CE2 . PHE B 391  ? 0.1874 0.2702 0.2002 -0.0362 0.0042  0.0019  389  PHE B CE2 
11731 C CZ  . PHE B 391  ? 0.1722 0.2505 0.1846 -0.0313 0.0053  -0.0002 389  PHE B CZ  
11732 N N   . PRO B 392  ? 0.1941 0.2375 0.1833 -0.0510 -0.0030 0.0049  390  PRO B N   
11733 C CA  . PRO B 392  ? 0.1827 0.2214 0.1673 -0.0558 -0.0046 0.0070  390  PRO B CA  
11734 C C   . PRO B 392  ? 0.2045 0.2523 0.1902 -0.0587 -0.0029 0.0098  390  PRO B C   
11735 O O   . PRO B 392  ? 0.2028 0.2474 0.1847 -0.0627 -0.0039 0.0119  390  PRO B O   
11736 C CB  . PRO B 392  ? 0.2096 0.2389 0.1907 -0.0527 -0.0049 0.0055  390  PRO B CB  
11737 C CG  . PRO B 392  ? 0.2029 0.2374 0.1878 -0.0472 -0.0023 0.0039  390  PRO B CG  
11738 C CD  . PRO B 392  ? 0.1707 0.2116 0.1602 -0.0456 -0.0016 0.0029  390  PRO B CD  
11739 N N   . VAL B 393  ? 0.2036 0.2624 0.1943 -0.0563 -0.0004 0.0099  391  VAL B N   
11740 C CA  . VAL B 393  ? 0.2116 0.2809 0.2042 -0.0581 0.0017  0.0123  391  VAL B CA  
11741 C C   . VAL B 393  ? 0.1848 0.2653 0.1828 -0.0587 0.0025  0.0131  391  VAL B C   
11742 O O   . VAL B 393  ? 0.1905 0.2708 0.1909 -0.0564 0.0019  0.0114  391  VAL B O   
11743 C CB  . VAL B 393  ? 0.2108 0.2826 0.2039 -0.0534 0.0043  0.0114  391  VAL B CB  
11744 C CG1 . VAL B 393  ? 0.2034 0.2643 0.1912 -0.0529 0.0033  0.0107  391  VAL B CG1 
11745 C CG2 . VAL B 393  ? 0.1816 0.2560 0.1786 -0.0473 0.0058  0.0086  391  VAL B CG2 
11746 N N   . PHE B 394  ? 0.2188 0.3095 0.2187 -0.0618 0.0039  0.0159  392  PHE B N   
11747 C CA  . PHE B 394  ? 0.1947 0.2976 0.2003 -0.0619 0.0049  0.0169  392  PHE B CA  
11748 C C   . PHE B 394  ? 0.1979 0.3065 0.2074 -0.0549 0.0077  0.0148  392  PHE B C   
11749 O O   . PHE B 394  ? 0.2243 0.3294 0.2322 -0.0509 0.0091  0.0132  392  PHE B O   
11750 C CB  . PHE B 394  ? 0.1874 0.3003 0.1942 -0.0671 0.0057  0.0206  392  PHE B CB  
11751 C CG  . PHE B 394  ? 0.2080 0.3148 0.2108 -0.0743 0.0027  0.0227  392  PHE B CG  
11752 C CD1 . PHE B 394  ? 0.2392 0.3433 0.2421 -0.0775 -0.0001 0.0228  392  PHE B CD1 
11753 C CD2 . PHE B 394  ? 0.2210 0.3234 0.2191 -0.0775 0.0026  0.0245  392  PHE B CD2 
11754 C CE1 . PHE B 394  ? 0.2236 0.3208 0.2221 -0.0841 -0.0032 0.0245  392  PHE B CE1 
11755 C CE2 . PHE B 394  ? 0.2310 0.3265 0.2249 -0.0841 -0.0005 0.0264  392  PHE B CE2 
11756 C CZ  . PHE B 394  ? 0.2150 0.3076 0.2090 -0.0874 -0.0034 0.0264  392  PHE B CZ  
11757 N N   . THR B 395  ? 0.2062 0.3237 0.2208 -0.0537 0.0082  0.0149  393  THR B N   
11758 C CA  . THR B 395  ? 0.2091 0.3320 0.2275 -0.0471 0.0105  0.0131  393  THR B CA  
11759 C C   . THR B 395  ? 0.1930 0.3305 0.2160 -0.0464 0.0132  0.0150  393  THR B C   
11760 O O   . THR B 395  ? 0.2392 0.3810 0.2646 -0.0406 0.0154  0.0135  393  THR B O   
11761 C CB  . THR B 395  ? 0.2251 0.3454 0.2455 -0.0446 0.0092  0.0112  393  THR B CB  
11762 O OG1 . THR B 395  ? 0.2197 0.3462 0.2428 -0.0486 0.0077  0.0130  393  THR B OG1 
11763 C CG2 . THR B 395  ? 0.2209 0.3272 0.2369 -0.0444 0.0070  0.0090  393  THR B CG2 
11764 N N   . ARG B 396  ? 0.1987 0.3438 0.2229 -0.0518 0.0129  0.0181  394  ARG B N   
11765 C CA  . ARG B 396  ? 0.2218 0.3814 0.2502 -0.0514 0.0157  0.0203  394  ARG B CA  
11766 C C   . ARG B 396  ? 0.2361 0.3961 0.2610 -0.0546 0.0169  0.0222  394  ARG B C   
11767 O O   . ARG B 396  ? 0.2312 0.3852 0.2525 -0.0604 0.0148  0.0238  394  ARG B O   
11768 C CB  . ARG B 396  ? 0.2396 0.4098 0.2727 -0.0554 0.0147  0.0228  394  ARG B CB  
11769 C CG  . ARG B 396  ? 0.2572 0.4279 0.2937 -0.0524 0.0134  0.0212  394  ARG B CG  
11770 C CD  . ARG B 396  ? 0.2464 0.4292 0.2881 -0.0562 0.0125  0.0239  394  ARG B CD  
11771 N NE  . ARG B 396  ? 0.2702 0.4515 0.3140 -0.0540 0.0107  0.0223  394  ARG B NE  
11772 C CZ  . ARG B 396  ? 0.3029 0.4951 0.3525 -0.0511 0.0114  0.0228  394  ARG B CZ  
11773 N NH1 . ARG B 396  ? 0.3144 0.5206 0.3686 -0.0501 0.0140  0.0248  394  ARG B NH1 
11774 N NH2 . ARG B 396  ? 0.2960 0.4850 0.3466 -0.0490 0.0097  0.0212  394  ARG B NH2 
11775 N N   . LYS B 397  ? 0.2637 0.4306 0.2895 -0.0507 0.0203  0.0221  395  LYS B N   
11776 C CA  . LYS B 397  ? 0.2576 0.4249 0.2798 -0.0532 0.0217  0.0239  395  LYS B CA  
11777 C C   . LYS B 397  ? 0.2611 0.4360 0.2843 -0.0608 0.0211  0.0280  395  LYS B C   
11778 O O   . LYS B 397  ? 0.2418 0.4119 0.2606 -0.0656 0.0202  0.0298  395  LYS B O   
11779 C CB  . LYS B 397  ? 0.2818 0.4562 0.3049 -0.0474 0.0256  0.0230  395  LYS B CB  
11780 C CG  . LYS B 397  ? 0.2971 0.4685 0.3150 -0.0482 0.0271  0.0237  395  LYS B CG  
11781 C CD  . LYS B 397  ? 0.3487 0.5328 0.3683 -0.0524 0.0290  0.0275  395  LYS B CD  
11782 C CE  . LYS B 397  ? 0.3461 0.5285 0.3604 -0.0527 0.0310  0.0282  395  LYS B CE  
11783 N NZ  . LYS B 397  ? 0.3150 0.5106 0.3313 -0.0570 0.0330  0.0321  395  LYS B NZ  
11784 N N   . ILE B 398  ? 0.2419 0.4286 0.2710 -0.0621 0.0212  0.0297  396  ILE B N   
11785 C CA  . ILE B 398  ? 0.2706 0.4653 0.3013 -0.0697 0.0204  0.0338  396  ILE B CA  
11786 C C   . ILE B 398  ? 0.2396 0.4224 0.2658 -0.0763 0.0162  0.0346  396  ILE B C   
11787 O O   . ILE B 398  ? 0.2554 0.4396 0.2798 -0.0832 0.0153  0.0378  396  ILE B O   
11788 C CB  . ILE B 398  ? 0.2889 0.4986 0.3272 -0.0695 0.0210  0.0353  396  ILE B CB  
11789 C CG1 . ILE B 398  ? 0.3780 0.5988 0.4185 -0.0769 0.0210  0.0398  396  ILE B CG1 
11790 C CG2 . ILE B 398  ? 0.2853 0.4896 0.3251 -0.0695 0.0177  0.0337  396  ILE B CG2 
11791 C CD1 . ILE B 398  ? 0.4081 0.6475 0.4561 -0.0748 0.0237  0.0416  396  ILE B CD1 
11792 N N   . HIS B 399  ? 0.2368 0.4076 0.2609 -0.0743 0.0138  0.0316  397  HIS B N   
11793 C CA  . HIS B 399  ? 0.2279 0.3865 0.2472 -0.0799 0.0099  0.0320  397  HIS B CA  
11794 C C   . HIS B 399  ? 0.2170 0.3653 0.2295 -0.0818 0.0096  0.0323  397  HIS B C   
11795 O O   . HIS B 399  ? 0.2479 0.3912 0.2568 -0.0885 0.0073  0.0346  397  HIS B O   
11796 C CB  . HIS B 399  ? 0.2417 0.3904 0.2604 -0.0766 0.0077  0.0286  397  HIS B CB  
11797 C CG  . HIS B 399  ? 0.2571 0.4141 0.2814 -0.0758 0.0071  0.0285  397  HIS B CG  
11798 N ND1 . HIS B 399  ? 0.2574 0.4084 0.2822 -0.0721 0.0057  0.0256  397  HIS B ND1 
11799 C CD2 . HIS B 399  ? 0.2907 0.4620 0.3206 -0.0783 0.0076  0.0311  397  HIS B CD2 
11800 C CE1 . HIS B 399  ? 0.2577 0.4183 0.2877 -0.0723 0.0054  0.0264  397  HIS B CE1 
11801 N NE2 . HIS B 399  ? 0.2545 0.4277 0.2878 -0.0760 0.0065  0.0297  397  HIS B NE2 
11802 N N   . THR B 400  ? 0.2159 0.3608 0.2267 -0.0761 0.0118  0.0301  398  THR B N   
11803 C CA  . THR B 400  ? 0.2293 0.3659 0.2339 -0.0774 0.0118  0.0306  398  THR B CA  
11804 C C   . THR B 400  ? 0.2437 0.3892 0.2480 -0.0828 0.0132  0.0347  398  THR B C   
11805 O O   . THR B 400  ? 0.2748 0.4132 0.2739 -0.0879 0.0116  0.0366  398  THR B O   
11806 C CB  . THR B 400  ? 0.2014 0.3347 0.2048 -0.0701 0.0141  0.0276  398  THR B CB  
11807 O OG1 . THR B 400  ? 0.2196 0.3425 0.2222 -0.0662 0.0123  0.0241  398  THR B OG1 
11808 C CG2 . THR B 400  ? 0.2159 0.3432 0.2134 -0.0714 0.0146  0.0285  398  THR B CG2 
11809 N N   . ASP B 401  ? 0.2878 0.4488 0.2976 -0.0817 0.0162  0.0362  399  ASP B N   
11810 C CA  . ASP B 401  ? 0.2745 0.4456 0.2845 -0.0868 0.0179  0.0403  399  ASP B CA  
11811 C C   . ASP B 401  ? 0.2680 0.4387 0.2775 -0.0956 0.0147  0.0436  399  ASP B C   
11812 O O   . ASP B 401  ? 0.2653 0.4345 0.2710 -0.1014 0.0142  0.0467  399  ASP B O   
11813 C CB  . ASP B 401  ? 0.2703 0.4589 0.2870 -0.0833 0.0217  0.0410  399  ASP B CB  
11814 C CG  . ASP B 401  ? 0.3493 0.5387 0.3651 -0.0755 0.0252  0.0384  399  ASP B CG  
11815 O OD1 . ASP B 401  ? 0.3269 0.5057 0.3366 -0.0745 0.0251  0.0372  399  ASP B OD1 
11816 O OD2 . ASP B 401  ? 0.2991 0.4992 0.3201 -0.0703 0.0279  0.0374  399  ASP B OD2 
11817 N N   . VAL B 402  ? 0.2585 0.4305 0.2717 -0.0970 0.0124  0.0432  400  VAL B N   
11818 C CA  . VAL B 402  ? 0.2775 0.4476 0.2896 -0.1055 0.0089  0.0461  400  VAL B CA  
11819 C C   . VAL B 402  ? 0.2774 0.4295 0.2814 -0.1087 0.0056  0.0455  400  VAL B C   
11820 O O   . VAL B 402  ? 0.3049 0.4541 0.3054 -0.1160 0.0037  0.0487  400  VAL B O   
11821 C CB  . VAL B 402  ? 0.2926 0.4667 0.3097 -0.1055 0.0070  0.0452  400  VAL B CB  
11822 C CG1 . VAL B 402  ? 0.3097 0.4786 0.3245 -0.1140 0.0026  0.0475  400  VAL B CG1 
11823 C CG2 . VAL B 402  ? 0.3254 0.5185 0.3507 -0.1031 0.0101  0.0465  400  VAL B CG2 
11824 N N   . SER B 403  ? 0.2642 0.4041 0.2654 -0.1032 0.0047  0.0416  401  SER B N   
11825 C CA  . SER B 403  ? 0.2964 0.4191 0.2900 -0.1051 0.0018  0.0407  401  SER B CA  
11826 C C   . SER B 403  ? 0.2667 0.3873 0.2555 -0.1077 0.0028  0.0431  401  SER B C   
11827 O O   . SER B 403  ? 0.2765 0.3881 0.2597 -0.1136 0.0001  0.0451  401  SER B O   
11828 C CB  . SER B 403  ? 0.2518 0.3643 0.2440 -0.0978 0.0016  0.0361  401  SER B CB  
11829 O OG  . SER B 403  ? 0.2810 0.3777 0.2662 -0.0987 -0.0009 0.0353  401  SER B OG  
11830 N N   . TYR B 404  ? 0.2873 0.4159 0.2778 -0.1034 0.0067  0.0430  402  TYR B N   
11831 C CA  . TYR B 404  ? 0.3014 0.4289 0.2872 -0.1056 0.0080  0.0453  402  TYR B CA  
11832 C C   . TYR B 404  ? 0.2969 0.4307 0.2822 -0.1144 0.0073  0.0503  402  TYR B C   
11833 O O   . TYR B 404  ? 0.3044 0.4296 0.2836 -0.1195 0.0053  0.0524  402  TYR B O   
11834 C CB  . TYR B 404  ? 0.2650 0.4020 0.2533 -0.0993 0.0125  0.0442  402  TYR B CB  
11835 C CG  . TYR B 404  ? 0.2705 0.4041 0.2531 -0.0995 0.0139  0.0454  402  TYR B CG  
11836 C CD1 . TYR B 404  ? 0.2946 0.4355 0.2759 -0.1053 0.0151  0.0497  402  TYR B CD1 
11837 C CD2 . TYR B 404  ? 0.3028 0.4262 0.2814 -0.0939 0.0140  0.0423  402  TYR B CD2 
11838 C CE1 . TYR B 404  ? 0.3172 0.4549 0.2929 -0.1054 0.0165  0.0509  402  TYR B CE1 
11839 C CE2 . TYR B 404  ? 0.2868 0.4071 0.2600 -0.0940 0.0152  0.0433  402  TYR B CE2 
11840 C CZ  . TYR B 404  ? 0.3178 0.4451 0.2894 -0.0997 0.0164  0.0476  402  TYR B CZ  
11841 O OH  . TYR B 404  ? 0.3483 0.4723 0.3141 -0.0998 0.0175  0.0488  402  TYR B OH  
11842 N N   . ILE B 405  ? 0.3029 0.4518 0.2948 -0.1164 0.0086  0.0522  403  ILE B N   
11843 C CA  . ILE B 405  ? 0.3005 0.4575 0.2930 -0.1249 0.0082  0.0572  403  ILE B CA  
11844 C C   . ILE B 405  ? 0.3054 0.4507 0.2936 -0.1323 0.0032  0.0585  403  ILE B C   
11845 O O   . ILE B 405  ? 0.3319 0.4742 0.3158 -0.1394 0.0017  0.0621  403  ILE B O   
11846 C CB  . ILE B 405  ? 0.3060 0.4826 0.3072 -0.1248 0.0108  0.0588  403  ILE B CB  
11847 C CG1 . ILE B 405  ? 0.3385 0.5259 0.3426 -0.1179 0.0159  0.0578  403  ILE B CG1 
11848 C CG2 . ILE B 405  ? 0.3000 0.4849 0.3022 -0.1337 0.0099  0.0638  403  ILE B CG2 
11849 C CD1 . ILE B 405  ? 0.3807 0.5854 0.3937 -0.1145 0.0186  0.0577  403  ILE B CD1 
11850 N N   . ALA B 406  ? 0.3175 0.4557 0.3065 -0.1305 0.0004  0.0556  404  ALA B N   
11851 C CA  . ALA B 406  ? 0.3102 0.4356 0.2944 -0.1366 -0.0045 0.0562  404  ALA B CA  
11852 C C   . ALA B 406  ? 0.3194 0.4278 0.2947 -0.1376 -0.0064 0.0559  404  ALA B C   
11853 O O   . ALA B 406  ? 0.3366 0.4372 0.3067 -0.1448 -0.0096 0.0586  404  ALA B O   
11854 C CB  . ALA B 406  ? 0.3156 0.4359 0.3018 -0.1332 -0.0066 0.0525  404  ALA B CB  
11855 N N   . CYS B 407  ? 0.3201 0.4224 0.2935 -0.1303 -0.0048 0.0527  405  CYS B N   
11856 C CA  . CYS B 407  ? 0.3360 0.4227 0.3013 -0.1304 -0.0066 0.0523  405  CYS B CA  
11857 C C   . CYS B 407  ? 0.3214 0.4114 0.2834 -0.1348 -0.0052 0.0564  405  CYS B C   
11858 O O   . CYS B 407  ? 0.3296 0.4078 0.2845 -0.1392 -0.0078 0.0581  405  CYS B O   
11859 C CB  . CYS B 407  ? 0.2966 0.3768 0.2614 -0.1214 -0.0053 0.0478  405  CYS B CB  
11860 S SG  . CYS B 407  ? 0.3540 0.4256 0.3204 -0.1171 -0.0079 0.0432  405  CYS B SG  
11861 N N   . ALA B 408  ? 0.3210 0.4271 0.2879 -0.1339 -0.0010 0.0581  406  ALA B N   
11862 C CA  . ALA B 408  ? 0.3535 0.4646 0.3176 -0.1389 0.0005  0.0624  406  ALA B CA  
11863 C C   . ALA B 408  ? 0.3373 0.4480 0.2995 -0.1491 -0.0025 0.0669  406  ALA B C   
11864 O O   . ALA B 408  ? 0.3794 0.4837 0.3354 -0.1544 -0.0038 0.0700  406  ALA B O   
11865 C CB  . ALA B 408  ? 0.3433 0.4730 0.3135 -0.1359 0.0056  0.0633  406  ALA B CB  
11866 N N   . ALA B 409  ? 0.3373 0.4541 0.3046 -0.1520 -0.0039 0.0672  407  ALA B N   
11867 C CA  . ALA B 409  ? 0.3763 0.4914 0.3416 -0.1607 -0.0075 0.0707  407  ALA B CA  
11868 C C   . ALA B 409  ? 0.3871 0.4817 0.3434 -0.1645 -0.0121 0.0706  407  ALA B C   
11869 O O   . ALA B 409  ? 0.3960 0.4847 0.3470 -0.1697 -0.0146 0.0733  407  ALA B O   
11870 C CB  . ALA B 409  ? 0.3353 0.4590 0.3071 -0.1611 -0.0087 0.0700  407  ALA B CB  
11871 N N   . LYS B 410  ? 0.3718 0.4541 0.3260 -0.1592 -0.0137 0.0662  408  LYS B N   
11872 C CA  . LYS B 410  ? 0.3594 0.4216 0.3050 -0.1611 -0.0181 0.0654  408  LYS B CA  
11873 C C   . LYS B 410  ? 0.3958 0.4501 0.3346 -0.1613 -0.0177 0.0670  408  LYS B C   
11874 O O   . LYS B 410  ? 0.4090 0.4517 0.3407 -0.1672 -0.0210 0.0695  408  LYS B O   
11875 C CB  . LYS B 410  ? 0.3452 0.3974 0.2908 -0.1538 -0.0194 0.0600  408  LYS B CB  
11876 C CG  . LYS B 410  ? 0.3427 0.3743 0.2797 -0.1548 -0.0238 0.0587  408  LYS B CG  
11877 C CD  . LYS B 410  ? 0.3630 0.3865 0.3004 -0.1463 -0.0241 0.0533  408  LYS B CD  
11878 C CE  . LYS B 410  ? 0.3483 0.3778 0.2915 -0.1447 -0.0243 0.0509  408  LYS B CE  
11879 N NZ  . LYS B 410  ? 0.3584 0.3796 0.2978 -0.1515 -0.0288 0.0519  408  LYS B NZ  
11880 N N   . LEU B 411  ? 0.3750 0.4352 0.3158 -0.1547 -0.0137 0.0656  409  LEU B N   
11881 C CA  . LEU B 411  ? 0.3818 0.4353 0.3162 -0.1544 -0.0132 0.0670  409  LEU B CA  
11882 C C   . LEU B 411  ? 0.4037 0.4633 0.3359 -0.1630 -0.0129 0.0728  409  LEU B C   
11883 O O   . LEU B 411  ? 0.4260 0.4740 0.3504 -0.1674 -0.0153 0.0752  409  LEU B O   
11884 C CB  . LEU B 411  ? 0.3294 0.3897 0.2668 -0.1460 -0.0089 0.0644  409  LEU B CB  
11885 C CG  . LEU B 411  ? 0.3877 0.4374 0.3245 -0.1378 -0.0098 0.0591  409  LEU B CG  
11886 C CD1 . LEU B 411  ? 0.3634 0.4221 0.3044 -0.1299 -0.0055 0.0565  409  LEU B CD1 
11887 C CD2 . LEU B 411  ? 0.3853 0.4168 0.3134 -0.1382 -0.0132 0.0589  409  LEU B CD2 
11888 N N   . LEU B 412  ? 0.4299 0.5076 0.3688 -0.1656 -0.0098 0.0752  410  LEU B N   
11889 C CA  . LEU B 412  ? 0.4243 0.5087 0.3622 -0.1701 -0.0097 0.0790  410  LEU B CA  
11890 C C   . LEU B 412  ? 0.4385 0.5131 0.3719 -0.1768 -0.0149 0.0809  410  LEU B C   
11891 O O   . LEU B 412  ? 0.4787 0.5523 0.4080 -0.1812 -0.0158 0.0841  410  LEU B O   
11892 C CB  . LEU B 412  ? 0.4076 0.5131 0.3545 -0.1684 -0.0057 0.0796  410  LEU B CB  
11893 C CG  . LEU B 412  ? 0.4470 0.5625 0.3966 -0.1622 -0.0003 0.0786  410  LEU B CG  
11894 C CD1 . LEU B 412  ? 0.4539 0.5888 0.4130 -0.1587 0.0034  0.0780  410  LEU B CD1 
11895 C CD2 . LEU B 412  ? 0.4565 0.5709 0.4005 -0.1638 0.0009  0.0814  410  LEU B CD2 
11896 N N   . ALA B 413  ? 0.4579 0.5249 0.3914 -0.1778 -0.0183 0.0789  411  ALA B N   
11897 C CA  . ALA B 413  ? 0.4732 0.5288 0.4011 -0.1837 -0.0235 0.0803  411  ALA B CA  
11898 C C   . ALA B 413  ? 0.4881 0.5229 0.4063 -0.1844 -0.0269 0.0798  411  ALA B C   
11899 O O   . ALA B 413  ? 0.5370 0.5606 0.4493 -0.1890 -0.0313 0.0810  411  ALA B O   
11900 C CB  . ALA B 413  ? 0.4836 0.5393 0.4151 -0.1842 -0.0259 0.0782  411  ALA B CB  
11901 N N   . ALA B 414  ? 0.4788 0.5080 0.3947 -0.1797 -0.0250 0.0783  412  ALA B N   
11902 C CA  . ALA B 414  ? 0.4824 0.4919 0.3891 -0.1794 -0.0281 0.0778  412  ALA B CA  
11903 C C   . ALA B 414  ? 0.5039 0.5131 0.4068 -0.1781 -0.0258 0.0797  412  ALA B C   
11904 O O   . ALA B 414  ? 0.5102 0.5054 0.4069 -0.1757 -0.0271 0.0787  412  ALA B O   
11905 C CB  . ALA B 414  ? 0.4680 0.4672 0.3744 -0.1746 -0.0291 0.0736  412  ALA B CB  
11906 N N   . THR B 415  ? 0.4888 0.5132 0.3952 -0.1794 -0.0224 0.0823  413  THR B N   
11907 C CA  . THR B 415  ? 0.4643 0.4893 0.3670 -0.1781 -0.0199 0.0841  413  THR B CA  
11908 C C   . THR B 415  ? 0.5046 0.5129 0.3975 -0.1813 -0.0239 0.0859  413  THR B C   
11909 O O   . THR B 415  ? 0.4914 0.4958 0.3796 -0.1796 -0.0228 0.0869  413  THR B O   
11910 C CB  . THR B 415  ? 0.4780 0.5219 0.3858 -0.1795 -0.0161 0.0867  413  THR B CB  
11911 O OG1 . THR B 415  ? 0.5058 0.5515 0.4134 -0.1859 -0.0187 0.0894  413  THR B OG1 
11912 C CG2 . THR B 415  ? 0.4788 0.5394 0.3961 -0.1753 -0.0118 0.0847  413  THR B CG2 
11913 N N   . ASP B 416  ? 0.5224 0.5205 0.4117 -0.1858 -0.0287 0.0865  414  ASP B N   
11914 C CA  . ASP B 416  ? 0.4951 0.4758 0.3748 -0.1883 -0.0329 0.0878  414  ASP B CA  
11915 C C   . ASP B 416  ? 0.4789 0.4426 0.3535 -0.1836 -0.0350 0.0848  414  ASP B C   
11916 O O   . ASP B 416  ? 0.5688 0.5182 0.4353 -0.1839 -0.0377 0.0857  414  ASP B O   
11917 C CB  . ASP B 416  ? 0.4831 0.4586 0.3603 -0.1944 -0.0373 0.0892  414  ASP B CB  
11918 N N   . VAL B 417  ? 0.5149 0.4796 0.3940 -0.1793 -0.0339 0.0814  415  VAL B N   
11919 C CA  . VAL B 417  ? 0.4573 0.4064 0.3323 -0.1747 -0.0359 0.0783  415  VAL B CA  
11920 C C   . VAL B 417  ? 0.4204 0.3761 0.2999 -0.1652 -0.0321 0.0746  415  VAL B C   
11921 O O   . VAL B 417  ? 0.4737 0.4180 0.3498 -0.1591 -0.0334 0.0718  415  VAL B O   
11922 C CB  . VAL B 417  ? 0.5750 0.5170 0.4512 -0.1744 -0.0389 0.0752  415  VAL B CB  
11923 N N   . VAL B 418  ? 0.4536 0.4275 0.3410 -0.1634 -0.0275 0.0744  416  VAL B N   
11924 C CA  . VAL B 418  ? 0.4144 0.3951 0.3063 -0.1544 -0.0239 0.0707  416  VAL B CA  
11925 C C   . VAL B 418  ? 0.4557 0.4531 0.3510 -0.1555 -0.0192 0.0733  416  VAL B C   
11926 O O   . VAL B 418  ? 0.4439 0.4513 0.3410 -0.1623 -0.0181 0.0772  416  VAL B O   
11927 C CB  . VAL B 418  ? 0.4343 0.4194 0.3336 -0.1486 -0.0230 0.0658  416  VAL B CB  
11928 C CG1 . VAL B 418  ? 0.3842 0.3526 0.2798 -0.1463 -0.0272 0.0628  416  VAL B CG1 
11929 C CG2 . VAL B 418  ? 0.4147 0.4136 0.3205 -0.1533 -0.0217 0.0673  416  VAL B CG2 
11930 N N   . PHE B 419  ? 0.3958 0.3961 0.2916 -0.1487 -0.0164 0.0712  417  PHE B N   
11931 C CA  . PHE B 419  ? 0.3832 0.3987 0.2817 -0.1483 -0.0117 0.0730  417  PHE B CA  
11932 C C   . PHE B 419  ? 0.3969 0.4254 0.3043 -0.1418 -0.0081 0.0692  417  PHE B C   
11933 O O   . PHE B 419  ? 0.3514 0.3768 0.2597 -0.1340 -0.0073 0.0651  417  PHE B O   
11934 C CB  . PHE B 419  ? 0.4045 0.4141 0.2967 -0.1454 -0.0112 0.0735  417  PHE B CB  
11935 C CG  . PHE B 419  ? 0.4202 0.4444 0.3143 -0.1444 -0.0064 0.0749  417  PHE B CG  
11936 C CD1 . PHE B 419  ? 0.4169 0.4525 0.3115 -0.1513 -0.0043 0.0796  417  PHE B CD1 
11937 C CD2 . PHE B 419  ? 0.3644 0.3908 0.2593 -0.1365 -0.0039 0.0716  417  PHE B CD2 
11938 C CE1 . PHE B 419  ? 0.4461 0.4954 0.3422 -0.1499 0.0004  0.0809  417  PHE B CE1 
11939 C CE2 . PHE B 419  ? 0.3565 0.3958 0.2524 -0.1352 0.0006  0.0727  417  PHE B CE2 
11940 C CZ  . PHE B 419  ? 0.4017 0.4526 0.2982 -0.1417 0.0029  0.0773  417  PHE B CZ  
11941 N N   . PRO B 420  ? 0.3662 0.4089 0.2801 -0.1447 -0.0059 0.0705  418  PRO B N   
11942 C CA  . PRO B 420  ? 0.3269 0.3810 0.2491 -0.1384 -0.0029 0.0668  418  PRO B CA  
11943 C C   . PRO B 420  ? 0.3717 0.4366 0.2957 -0.1333 0.0018  0.0662  418  PRO B C   
11944 O O   . PRO B 420  ? 0.3500 0.4225 0.2721 -0.1368 0.0041  0.0698  418  PRO B O   
11945 C CB  . PRO B 420  ? 0.3546 0.4202 0.2826 -0.1440 -0.0025 0.0691  418  PRO B CB  
11946 C CG  . PRO B 420  ? 0.3645 0.4205 0.2868 -0.1528 -0.0066 0.0729  418  PRO B CG  
11947 C CD  . PRO B 420  ? 0.3706 0.4182 0.2847 -0.1539 -0.0070 0.0751  418  PRO B CD  
11948 N N   . GLN B 421  ? 0.3422 0.4074 0.2694 -0.1251 0.0032  0.0615  419  GLN B N   
11949 C CA  . GLN B 421  ? 0.3447 0.4185 0.2732 -0.1193 0.0074  0.0600  419  GLN B CA  
11950 C C   . GLN B 421  ? 0.3470 0.4316 0.2839 -0.1140 0.0100  0.0568  419  GLN B C   
11951 O O   . GLN B 421  ? 0.2992 0.3776 0.2383 -0.1092 0.0085  0.0528  419  GLN B O   
11952 C CB  . GLN B 421  ? 0.3219 0.3834 0.2448 -0.1141 0.0062  0.0575  419  GLN B CB  
11953 C CG  . GLN B 421  ? 0.3221 0.3713 0.2364 -0.1191 0.0031  0.0606  419  GLN B CG  
11954 C CD  . GLN B 421  ? 0.3378 0.3727 0.2472 -0.1141 0.0007  0.0578  419  GLN B CD  
11955 O OE1 . GLN B 421  ? 0.3452 0.3758 0.2485 -0.1142 0.0007  0.0592  419  GLN B OE1 
11956 N NE2 . GLN B 421  ? 0.3151 0.3427 0.2269 -0.1101 -0.0014 0.0541  419  GLN B NE2 
11957 N N   . PHE B 422  ? 0.3370 0.4379 0.2788 -0.1148 0.0137  0.0585  420  PHE B N   
11958 C CA  . PHE B 422  ? 0.2996 0.4116 0.2496 -0.1108 0.0159  0.0561  420  PHE B CA  
11959 C C   . PHE B 422  ? 0.3227 0.4402 0.2741 -0.1027 0.0196  0.0530  420  PHE B C   
11960 O O   . PHE B 422  ? 0.3173 0.4465 0.2695 -0.1020 0.0234  0.0544  420  PHE B O   
11961 C CB  . PHE B 422  ? 0.2975 0.4241 0.2525 -0.1165 0.0174  0.0599  420  PHE B CB  
11962 C CG  . PHE B 422  ? 0.3387 0.4591 0.2921 -0.1246 0.0134  0.0628  420  PHE B CG  
11963 C CD1 . PHE B 422  ? 0.3470 0.4598 0.3023 -0.1243 0.0100  0.0605  420  PHE B CD1 
11964 C CD2 . PHE B 422  ? 0.3610 0.4824 0.3104 -0.1326 0.0128  0.0678  420  PHE B CD2 
11965 C CE1 . PHE B 422  ? 0.3592 0.4653 0.3124 -0.1317 0.0061  0.0629  420  PHE B CE1 
11966 C CE2 . PHE B 422  ? 0.3805 0.4952 0.3280 -0.1402 0.0088  0.0703  420  PHE B CE2 
11967 C CZ  . PHE B 422  ? 0.3434 0.4503 0.2927 -0.1396 0.0054  0.0678  420  PHE B CZ  
11968 N N   . ALA B 423  ? 0.2919 0.4004 0.2433 -0.0965 0.0183  0.0486  421  ALA B N   
11969 C CA  . ALA B 423  ? 0.3030 0.4142 0.2553 -0.0887 0.0211  0.0451  421  ALA B CA  
11970 C C   . ALA B 423  ? 0.3368 0.4598 0.2970 -0.0848 0.0235  0.0432  421  ALA B C   
11971 O O   . ALA B 423  ? 0.3274 0.4470 0.2913 -0.0829 0.0217  0.0408  421  ALA B O   
11972 C CB  . ALA B 423  ? 0.2872 0.3836 0.2360 -0.0843 0.0184  0.0415  421  ALA B CB  
11973 N N   . THR B 424  ? 0.3401 0.4769 0.3028 -0.0832 0.0277  0.0442  422  THR B N   
11974 C CA  . THR B 424  ? 0.3383 0.4868 0.3083 -0.0788 0.0302  0.0424  422  THR B CA  
11975 C C   . THR B 424  ? 0.3187 0.4791 0.2889 -0.0754 0.0350  0.0427  422  THR B C   
11976 O O   . THR B 424  ? 0.3461 0.5101 0.3124 -0.0789 0.0365  0.0458  422  THR B O   
11977 C CB  . THR B 424  ? 0.3532 0.5100 0.3291 -0.0839 0.0294  0.0449  422  THR B CB  
11978 O OG1 . THR B 424  ? 0.3314 0.4987 0.3144 -0.0789 0.0316  0.0429  422  THR B OG1 
11979 C CG2 . THR B 424  ? 0.3619 0.5286 0.3372 -0.0907 0.0309  0.0500  422  THR B CG2 
11980 N N   . HIS B 425  ? 0.3487 0.5146 0.3229 -0.0683 0.0372  0.0395  423  HIS B N   
11981 C CA  . HIS B 425  ? 0.3743 0.5528 0.3495 -0.0644 0.0419  0.0395  423  HIS B CA  
11982 C C   . HIS B 425  ? 0.4099 0.6043 0.3932 -0.0644 0.0442  0.0409  423  HIS B C   
11983 O O   . HIS B 425  ? 0.3988 0.6046 0.3841 -0.0600 0.0482  0.0404  423  HIS B O   
11984 C CB  . HIS B 425  ? 0.3453 0.5187 0.3186 -0.0560 0.0431  0.0348  423  HIS B CB  
11985 C CG  . HIS B 425  ? 0.3862 0.5444 0.3522 -0.0555 0.0407  0.0333  423  HIS B CG  
11986 N ND1 . HIS B 425  ? 0.4685 0.6143 0.4341 -0.0528 0.0375  0.0300  423  HIS B ND1 
11987 C CD2 . HIS B 425  ? 0.4074 0.5612 0.3663 -0.0576 0.0409  0.0347  423  HIS B CD2 
11988 C CE1 . HIS B 425  ? 0.4195 0.5542 0.3783 -0.0530 0.0359  0.0294  423  HIS B CE1 
11989 N NE2 . HIS B 425  ? 0.3652 0.5042 0.3198 -0.0559 0.0378  0.0323  423  HIS B NE2 
11990 N N   . ASN B 426  ? 0.3986 0.5939 0.3863 -0.0691 0.0416  0.0425  424  ASN B N   
11991 C CA  . ASN B 426  ? 0.4116 0.6212 0.4074 -0.0693 0.0430  0.0437  424  ASN B CA  
11992 C C   . ASN B 426  ? 0.3705 0.5923 0.3675 -0.0762 0.0445  0.0489  424  ASN B C   
11993 O O   . ASN B 426  ? 0.3479 0.5650 0.3428 -0.0839 0.0417  0.0519  424  ASN B O   
11994 C CB  . ASN B 426  ? 0.3655 0.5689 0.3649 -0.0707 0.0391  0.0425  424  ASN B CB  
11995 C CG  . ASN B 426  ? 0.4003 0.6175 0.4082 -0.0699 0.0402  0.0432  424  ASN B CG  
11996 O OD1 . ASN B 426  ? 0.3900 0.6215 0.4015 -0.0731 0.0423  0.0467  424  ASN B OD1 
11997 N ND2 . ASN B 426  ? 0.3665 0.5798 0.3777 -0.0657 0.0386  0.0401  424  ASN B ND2 
11998 N N   . ALA B 427  ? 0.4168 0.6543 0.4172 -0.0736 0.0490  0.0500  425  ALA B N   
11999 C CA  . ALA B 427  ? 0.4043 0.6500 0.4059 -0.0782 0.0493  0.0538  425  ALA B CA  
12000 C C   . ALA B 427  ? 0.3758 0.6258 0.3833 -0.0838 0.0463  0.0562  425  ALA B C   
12001 O O   . ALA B 427  ? 0.3828 0.6344 0.3895 -0.0905 0.0448  0.0599  425  ALA B O   
12002 C CB  . ALA B 427  ? 0.4522 0.7095 0.4563 -0.0720 0.0534  0.0531  425  ALA B CB  
12003 N N   . GLN B 428  ? 0.3621 0.6138 0.3752 -0.0812 0.0452  0.0543  426  GLN B N   
12004 C CA  . GLN B 428  ? 0.3875 0.6418 0.4053 -0.0867 0.0419  0.0564  426  GLN B CA  
12005 C C   . GLN B 428  ? 0.3659 0.6076 0.3789 -0.0946 0.0379  0.0580  426  GLN B C   
12006 O O   . GLN B 428  ? 0.3430 0.5850 0.3557 -0.1017 0.0354  0.0613  426  GLN B O   
12007 C CB  . GLN B 428  ? 0.3931 0.6515 0.4175 -0.0818 0.0415  0.0538  426  GLN B CB  
12008 C CG  . GLN B 428  ? 0.4408 0.7053 0.4710 -0.0862 0.0386  0.0560  426  GLN B CG  
12009 C CD  . GLN B 428  ? 0.4286 0.6826 0.4561 -0.0940 0.0341  0.0573  426  GLN B CD  
12010 O OE1 . GLN B 428  ? 0.3866 0.6298 0.4112 -0.0938 0.0329  0.0552  426  GLN B OE1 
12011 N NE2 . GLN B 428  ? 0.4056 0.6622 0.4338 -0.1010 0.0317  0.0607  426  GLN B NE2 
12012 N N   . THR B 429  ? 0.3989 0.6287 0.4075 -0.0933 0.0371  0.0556  427  THR B N   
12013 C CA  . THR B 429  ? 0.3745 0.5884 0.3773 -0.0991 0.0326  0.0563  427  THR B CA  
12014 C C   . THR B 429  ? 0.3615 0.5744 0.3586 -0.1056 0.0329  0.0603  427  THR B C   
12015 O O   . THR B 429  ? 0.3242 0.5323 0.3193 -0.1134 0.0296  0.0632  427  THR B O   
12016 C CB  . THR B 429  ? 0.3676 0.5649 0.3659 -0.0935 0.0308  0.0516  427  THR B CB  
12017 O OG1 . THR B 429  ? 0.3142 0.5133 0.3176 -0.0869 0.0311  0.0479  427  THR B OG1 
12018 C CG2 . THR B 429  ? 0.3586 0.5403 0.3520 -0.0989 0.0260  0.0520  427  THR B CG2 
12019 N N   . LEU B 430  ? 0.3760 0.5924 0.3700 -0.1023 0.0365  0.0602  428  LEU B N   
12020 C CA  . LEU B 430  ? 0.3799 0.5937 0.3681 -0.1071 0.0364  0.0634  428  LEU B CA  
12021 C C   . LEU B 430  ? 0.3714 0.5945 0.3634 -0.1121 0.0355  0.0669  428  LEU B C   
12022 O O   . LEU B 430  ? 0.3207 0.5379 0.3090 -0.1194 0.0326  0.0700  428  LEU B O   
12023 C CB  . LEU B 430  ? 0.3715 0.5882 0.3561 -0.1014 0.0406  0.0622  428  LEU B CB  
12024 C CG  . LEU B 430  ? 0.3806 0.5930 0.3577 -0.1048 0.0410  0.0647  428  LEU B CG  
12025 C CD1 . LEU B 430  ? 0.3749 0.5883 0.3484 -0.0977 0.0449  0.0622  428  LEU B CD1 
12026 C CD2 . LEU B 430  ? 0.4418 0.6633 0.4209 -0.1094 0.0412  0.0685  428  LEU B CD2 
12027 N N   . ALA B 431  ? 0.3988 0.6362 0.3979 -0.1081 0.0380  0.0666  429  ALA B N   
12028 C CA  . ALA B 431  ? 0.3808 0.6283 0.3838 -0.1126 0.0374  0.0700  429  ALA B CA  
12029 C C   . ALA B 431  ? 0.3645 0.6069 0.3684 -0.1199 0.0325  0.0718  429  ALA B C   
12030 O O   . ALA B 431  ? 0.4359 0.6780 0.4380 -0.1268 0.0304  0.0753  429  ALA B O   
12031 C CB  . ALA B 431  ? 0.3836 0.6465 0.3943 -0.1065 0.0404  0.0689  429  ALA B CB  
12032 N N   . ALA B 432  ? 0.4250 0.6625 0.4312 -0.1185 0.0305  0.0694  430  ALA B N   
12033 C CA  . ALA B 432  ? 0.3666 0.5983 0.3733 -0.1249 0.0258  0.0707  430  ALA B CA  
12034 C C   . ALA B 432  ? 0.3635 0.5811 0.3622 -0.1321 0.0225  0.0727  430  ALA B C   
12035 O O   . ALA B 432  ? 0.4060 0.6219 0.4037 -0.1390 0.0193  0.0756  430  ALA B O   
12036 C CB  . ALA B 432  ? 0.3762 0.6039 0.3859 -0.1216 0.0245  0.0674  430  ALA B CB  
12037 N N   . ILE B 433  ? 0.4002 0.6070 0.3926 -0.1304 0.0232  0.0714  431  ILE B N   
12038 C CA  . ILE B 433  ? 0.3817 0.5737 0.3659 -0.1366 0.0199  0.0732  431  ILE B CA  
12039 C C   . ILE B 433  ? 0.3911 0.5863 0.3719 -0.1403 0.0208  0.0767  431  ILE B C   
12040 O O   . ILE B 433  ? 0.3627 0.5497 0.3388 -0.1472 0.0174  0.0794  431  ILE B O   
12041 C CB  . ILE B 433  ? 0.3882 0.5676 0.3669 -0.1335 0.0202  0.0707  431  ILE B CB  
12042 C CG1 . ILE B 433  ? 0.3901 0.5653 0.3723 -0.1297 0.0188  0.0669  431  ILE B CG1 
12043 C CG2 . ILE B 433  ? 0.4128 0.5763 0.3825 -0.1394 0.0168  0.0727  431  ILE B CG2 
12044 C CD1 . ILE B 433  ? 0.3936 0.5545 0.3712 -0.1229 0.0180  0.0625  431  ILE B CD1 
12045 N N   . TYR B 434  ? 0.4027 0.6091 0.3854 -0.1357 0.0253  0.0766  432  TYR B N   
12046 C CA  . TYR B 434  ? 0.4086 0.6199 0.3888 -0.1388 0.0265  0.0799  432  TYR B CA  
12047 C C   . TYR B 434  ? 0.4184 0.6354 0.4017 -0.1455 0.0239  0.0833  432  TYR B C   
12048 O O   . TYR B 434  ? 0.4628 0.6743 0.4412 -0.1520 0.0216  0.0864  432  TYR B O   
12049 C CB  . TYR B 434  ? 0.4013 0.6257 0.3847 -0.1319 0.0319  0.0788  432  TYR B CB  
12050 C CG  . TYR B 434  ? 0.4323 0.6654 0.4149 -0.1344 0.0338  0.0821  432  TYR B CG  
12051 C CD1 . TYR B 434  ? 0.4160 0.6414 0.3907 -0.1372 0.0339  0.0839  432  TYR B CD1 
12052 C CD2 . TYR B 434  ? 0.4586 0.7076 0.4482 -0.1336 0.0358  0.0834  432  TYR B CD2 
12053 C CE1 . TYR B 434  ? 0.4106 0.6442 0.3845 -0.1394 0.0358  0.0870  432  TYR B CE1 
12054 C CE2 . TYR B 434  ? 0.4605 0.7179 0.4495 -0.1357 0.0378  0.0864  432  TYR B CE2 
12055 C CZ  . TYR B 434  ? 0.4725 0.7222 0.4537 -0.1387 0.0378  0.0882  432  TYR B CZ  
12056 O OH  . TYR B 434  ? 0.4134 0.6715 0.3938 -0.1409 0.0399  0.0913  432  TYR B OH  
12057 N N   . HIS B 435  ? 0.4348 0.6620 0.4258 -0.1441 0.0239  0.0827  433  HIS B N   
12058 C CA  . HIS B 435  ? 0.4436 0.6767 0.4375 -0.1504 0.0213  0.0859  433  HIS B CA  
12059 C C   . HIS B 435  ? 0.4321 0.6521 0.4228 -0.1566 0.0158  0.0863  433  HIS B C   
12060 O O   . HIS B 435  ? 0.3923 0.6099 0.3805 -0.1637 0.0127  0.0894  433  HIS B O   
12061 C CB  . HIS B 435  ? 0.4577 0.7073 0.4608 -0.1465 0.0234  0.0853  433  HIS B CB  
12062 C CG  . HIS B 435  ? 0.4619 0.7251 0.4679 -0.1416 0.0284  0.0856  433  HIS B CG  
12063 N ND1 . HIS B 435  ? 0.4632 0.7335 0.4683 -0.1453 0.0294  0.0892  433  HIS B ND1 
12064 C CD2 . HIS B 435  ? 0.4556 0.7260 0.4648 -0.1330 0.0326  0.0828  433  HIS B CD2 
12065 C CE1 . HIS B 435  ? 0.4834 0.7649 0.4912 -0.1393 0.0342  0.0885  433  HIS B CE1 
12066 N NE2 . HIS B 435  ? 0.4580 0.7396 0.4683 -0.1317 0.0361  0.0845  433  HIS B NE2 
12067 N N   . MET B 436  ? 0.4570 0.6677 0.4472 -0.1539 0.0144  0.0830  434  MET B N   
12068 C CA  . MET B 436  ? 0.4227 0.6192 0.4088 -0.1592 0.0092  0.0831  434  MET B CA  
12069 C C   . MET B 436  ? 0.3862 0.5693 0.3634 -0.1650 0.0066  0.0854  434  MET B C   
12070 O O   . MET B 436  ? 0.4546 0.6288 0.4284 -0.1713 0.0021  0.0869  434  MET B O   
12071 C CB  . MET B 436  ? 0.4123 0.6004 0.3985 -0.1547 0.0087  0.0791  434  MET B CB  
12072 C CG  . MET B 436  ? 0.4346 0.6050 0.4149 -0.1594 0.0036  0.0786  434  MET B CG  
12073 S SD  . MET B 436  ? 0.4874 0.6479 0.4676 -0.1539 0.0036  0.0740  434  MET B SD  
12074 C CE  . MET B 436  ? 0.3990 0.5717 0.3886 -0.1513 0.0036  0.0723  434  MET B CE  
12075 N N   . ALA B 437  ? 0.4076 0.5887 0.3807 -0.1629 0.0093  0.0856  435  ALA B N   
12076 C CA  . ALA B 437  ? 0.3959 0.5643 0.3603 -0.1680 0.0069  0.0879  435  ALA B CA  
12077 C C   . ALA B 437  ? 0.4391 0.6148 0.4034 -0.1737 0.0065  0.0920  435  ALA B C   
12078 O O   . ALA B 437  ? 0.4935 0.6588 0.4512 -0.1796 0.0032  0.0944  435  ALA B O   
12079 C CB  . ALA B 437  ? 0.4617 0.6253 0.4214 -0.1635 0.0098  0.0867  435  ALA B CB  
12080 N N   . PHE B 441  ? 0.5185 0.6802 0.4527 -0.1855 0.0103  0.1051  439  PHE B N   
12081 C CA  . PHE B 441  ? 0.4741 0.6252 0.4038 -0.1802 0.0110  0.1021  439  PHE B CA  
12082 C C   . PHE B 441  ? 0.5013 0.6420 0.4218 -0.1817 0.0106  0.1039  439  PHE B C   
12083 O O   . PHE B 441  ? 0.4785 0.6246 0.3973 -0.1851 0.0116  0.1071  439  PHE B O   
12084 C CB  . PHE B 441  ? 0.4362 0.5996 0.3716 -0.1720 0.0163  0.0990  439  PHE B CB  
12085 C CG  . PHE B 441  ? 0.4994 0.6527 0.4301 -0.1664 0.0172  0.0960  439  PHE B CG  
12086 C CD1 . PHE B 441  ? 0.4553 0.5992 0.3862 -0.1644 0.0150  0.0930  439  PHE B CD1 
12087 C CD2 . PHE B 441  ? 0.4753 0.6282 0.4010 -0.1635 0.0201  0.0962  439  PHE B CD2 
12088 C CE1 . PHE B 441  ? 0.4636 0.5982 0.3900 -0.1595 0.0156  0.0904  439  PHE B CE1 
12089 C CE2 . PHE B 441  ? 0.4948 0.6381 0.4157 -0.1586 0.0206  0.0935  439  PHE B CE2 
12090 C CZ  . PHE B 441  ? 0.4759 0.6102 0.3973 -0.1567 0.0183  0.0907  439  PHE B CZ  
12091 N N   . HIS B 442  ? 0.4982 0.6241 0.4127 -0.1792 0.0090  0.1018  440  HIS B N   
12092 C CA  . HIS B 442  ? 0.5191 0.6354 0.4249 -0.1791 0.0090  0.1030  440  HIS B CA  
12093 C C   . HIS B 442  ? 0.4811 0.5878 0.3838 -0.1730 0.0093  0.0995  440  HIS B C   
12094 O O   . HIS B 442  ? 0.4929 0.5957 0.3983 -0.1708 0.0080  0.0967  440  HIS B O   
12095 C CB  . HIS B 442  ? 0.5126 0.6149 0.4113 -0.1862 0.0039  0.1060  440  HIS B CB  
12096 C CG  . HIS B 442  ? 0.5496 0.6361 0.4456 -0.1876 -0.0012 0.1044  440  HIS B CG  
12097 N ND1 . HIS B 442  ? 0.5462 0.6324 0.4455 -0.1919 -0.0043 0.1048  440  HIS B ND1 
12098 C CD2 . HIS B 442  ? 0.5633 0.6337 0.4535 -0.1851 -0.0036 0.1024  440  HIS B CD2 
12099 C CE1 . HIS B 442  ? 0.5780 0.6484 0.4735 -0.1918 -0.0084 0.1029  440  HIS B CE1 
12100 N NE2 . HIS B 442  ? 0.5946 0.6552 0.4847 -0.1877 -0.0080 0.1015  440  HIS B NE2 
12101 N N   . VAL B 443  ? 0.4818 0.5845 0.3783 -0.1704 0.0109  0.0997  441  VAL B N   
12102 C CA  . VAL B 443  ? 0.5315 0.6242 0.4238 -0.1649 0.0109  0.0967  441  VAL B CA  
12103 C C   . VAL B 443  ? 0.5021 0.5757 0.3889 -0.1677 0.0053  0.0966  441  VAL B C   
12104 O O   . VAL B 443  ? 0.5277 0.5912 0.4084 -0.1727 0.0018  0.0993  441  VAL B O   
12105 C CB  . VAL B 443  ? 0.5234 0.6157 0.4096 -0.1619 0.0135  0.0971  441  VAL B CB  
12106 C CG1 . VAL B 443  ? 0.4819 0.5617 0.3626 -0.1569 0.0124  0.0944  441  VAL B CG1 
12107 C CG2 . VAL B 443  ? 0.4873 0.5981 0.3789 -0.1578 0.0193  0.0965  441  VAL B CG2 
12108 N N   . GLY B 444  ? 0.5041 0.5726 0.3930 -0.1644 0.0043  0.0934  442  GLY B N   
12109 C CA  . GLY B 444  ? 0.4718 0.5226 0.3562 -0.1664 -0.0009 0.0928  442  GLY B CA  
12110 C C   . GLY B 444  ? 0.4902 0.5418 0.3803 -0.1690 -0.0031 0.0920  442  GLY B C   
12111 O O   . GLY B 444  ? 0.4391 0.4768 0.3265 -0.1691 -0.0069 0.0905  442  GLY B O   
12112 N N   . LYS B 445  ? 0.4807 0.5477 0.3782 -0.1709 -0.0011 0.0928  443  LYS B N   
12113 C CA  . LYS B 445  ? 0.4902 0.5595 0.3937 -0.1726 -0.0029 0.0917  443  LYS B CA  
12114 C C   . LYS B 445  ? 0.4554 0.5271 0.3636 -0.1666 -0.0010 0.0878  443  LYS B C   
12115 O O   . LYS B 445  ? 0.4760 0.5377 0.3838 -0.1666 -0.0040 0.0858  443  LYS B O   
12116 C CB  . LYS B 445  ? 0.4526 0.5386 0.3629 -0.1759 -0.0011 0.0937  443  LYS B CB  
12117 N N   . TYR B 446  ? 0.4528 0.5374 0.3651 -0.1614 0.0040  0.0864  444  TYR B N   
12118 C CA  . TYR B 446  ? 0.4190 0.5066 0.3356 -0.1548 0.0062  0.0825  444  TYR B CA  
12119 C C   . TYR B 446  ? 0.3944 0.4929 0.3121 -0.1489 0.0112  0.0814  444  TYR B C   
12120 O O   . TYR B 446  ? 0.4165 0.5220 0.3325 -0.1509 0.0134  0.0842  444  TYR B O   
12121 C CB  . TYR B 446  ? 0.4018 0.4989 0.3271 -0.1553 0.0064  0.0813  444  TYR B CB  
12122 C CG  . TYR B 446  ? 0.4486 0.5652 0.3814 -0.1548 0.0100  0.0824  444  TYR B CG  
12123 C CD1 . TYR B 446  ? 0.4502 0.5719 0.3844 -0.1606 0.0085  0.0855  444  TYR B CD1 
12124 C CD2 . TYR B 446  ? 0.3898 0.5193 0.3281 -0.1482 0.0147  0.0801  444  TYR B CD2 
12125 C CE1 . TYR B 446  ? 0.4703 0.6097 0.4113 -0.1600 0.0117  0.0866  444  TYR B CE1 
12126 C CE2 . TYR B 446  ? 0.4554 0.6023 0.4005 -0.1472 0.0179  0.0809  444  TYR B CE2 
12127 C CZ  . TYR B 446  ? 0.4412 0.5930 0.3876 -0.1531 0.0164  0.0842  444  TYR B CZ  
12128 O OH  . TYR B 446  ? 0.5216 0.6907 0.4748 -0.1521 0.0195  0.0852  444  TYR B OH  
12129 N N   . GLU B 447  ? 0.3859 0.4847 0.3071 -0.1401 0.0126  0.0762  445  GLU B N   
12130 C CA  . GLU B 447  ? 0.3534 0.4621 0.2759 -0.1339 0.0173  0.0746  445  GLU B CA  
12131 C C   . GLU B 447  ? 0.3552 0.4711 0.2856 -0.1267 0.0193  0.0700  445  GLU B C   
12132 O O   . GLU B 447  ? 0.3495 0.4603 0.2833 -0.1257 0.0167  0.0677  445  GLU B O   
12133 C CB  . GLU B 447  ? 0.3327 0.4298 0.2475 -0.1300 0.0166  0.0732  445  GLU B CB  
12134 C CG  . GLU B 447  ? 0.3338 0.4163 0.2477 -0.1246 0.0133  0.0685  445  GLU B CG  
12135 C CD  . GLU B 447  ? 0.3366 0.4080 0.2431 -0.1212 0.0123  0.0674  445  GLU B CD  
12136 O OE1 . GLU B 447  ? 0.3516 0.4242 0.2524 -0.1242 0.0134  0.0707  445  GLU B OE1 
12137 O OE2 . GLU B 447  ? 0.3353 0.3971 0.2416 -0.1155 0.0103  0.0632  445  GLU B OE2 
12138 N N   . PHE B 448  ? 0.2961 0.4238 0.2289 -0.1216 0.0238  0.0688  446  PHE B N   
12139 C CA  . PHE B 448  ? 0.3421 0.4741 0.2807 -0.1134 0.0257  0.0640  446  PHE B CA  
12140 C C   . PHE B 448  ? 0.3249 0.4463 0.2587 -0.1066 0.0253  0.0601  446  PHE B C   
12141 O O   . PHE B 448  ? 0.3303 0.4439 0.2567 -0.1079 0.0245  0.0614  446  PHE B O   
12142 C CB  . PHE B 448  ? 0.3527 0.5038 0.2970 -0.1113 0.0308  0.0646  446  PHE B CB  
12143 C CG  . PHE B 448  ? 0.3485 0.5115 0.2991 -0.1172 0.0311  0.0680  446  PHE B CG  
12144 C CD1 . PHE B 448  ? 0.3348 0.4997 0.2922 -0.1161 0.0297  0.0660  446  PHE B CD1 
12145 C CD2 . PHE B 448  ? 0.3998 0.5717 0.3497 -0.1233 0.0325  0.0727  446  PHE B CD2 
12146 C CE1 . PHE B 448  ? 0.3696 0.5456 0.3328 -0.1216 0.0297  0.0691  446  PHE B CE1 
12147 C CE2 . PHE B 448  ? 0.3967 0.5774 0.3532 -0.1270 0.0316  0.0746  446  PHE B CE2 
12148 C CZ  . PHE B 448  ? 0.3616 0.5447 0.3246 -0.1263 0.0302  0.0729  446  PHE B CZ  
12149 N N   . GLN B 449  ? 0.3115 0.4324 0.2495 -0.0995 0.0257  0.0554  447  GLN B N   
12150 C CA  . GLN B 449  ? 0.3036 0.4161 0.2381 -0.0926 0.0257  0.0515  447  GLN B CA  
12151 C C   . GLN B 449  ? 0.3270 0.4485 0.2671 -0.0852 0.0289  0.0478  447  GLN B C   
12152 O O   . GLN B 449  ? 0.3040 0.4341 0.2510 -0.0847 0.0299  0.0473  447  GLN B O   
12153 C CB  . GLN B 449  ? 0.3037 0.3997 0.2359 -0.0919 0.0209  0.0493  447  GLN B CB  
12154 C CG  . GLN B 449  ? 0.3226 0.4081 0.2490 -0.0988 0.0173  0.0527  447  GLN B CG  
12155 C CD  . GLN B 449  ? 0.3016 0.3704 0.2236 -0.0964 0.0133  0.0504  447  GLN B CD  
12156 O OE1 . GLN B 449  ? 0.3100 0.3753 0.2344 -0.0902 0.0130  0.0462  447  GLN B OE1 
12157 N NE2 . GLN B 449  ? 0.3018 0.3604 0.2172 -0.1012 0.0103  0.0532  447  GLN B NE2 
12158 N N   . CYS B 450  ? 0.3016 0.4204 0.2381 -0.0795 0.0304  0.0451  448  CYS B N   
12159 C CA  . CYS B 450  ? 0.3379 0.4632 0.2784 -0.0721 0.0332  0.0413  448  CYS B CA  
12160 C C   . CYS B 450  ? 0.3219 0.4363 0.2578 -0.0666 0.0320  0.0376  448  CYS B C   
12161 O O   . CYS B 450  ? 0.3321 0.4362 0.2616 -0.0685 0.0297  0.0385  448  CYS B O   
12162 C CB  . CYS B 450  ? 0.3693 0.5099 0.3109 -0.0711 0.0382  0.0428  448  CYS B CB  
12163 S SG  . CYS B 450  ? 0.3529 0.4920 0.2852 -0.0707 0.0402  0.0440  448  CYS B SG  
12164 N N   . LEU B 451  ? 0.3336 0.4503 0.2727 -0.0598 0.0336  0.0337  449  LEU B N   
12165 C CA  . LEU B 451  ? 0.3636 0.4717 0.2985 -0.0543 0.0329  0.0301  449  LEU B CA  
12166 C C   . LEU B 451  ? 0.3884 0.5019 0.3183 -0.0521 0.0363  0.0304  449  LEU B C   
12167 O O   . LEU B 451  ? 0.3822 0.5085 0.3144 -0.0517 0.0402  0.0315  449  LEU B O   
12168 C CB  . LEU B 451  ? 0.3466 0.4539 0.2866 -0.0482 0.0328  0.0258  449  LEU B CB  
12169 C CG  . LEU B 451  ? 0.3908 0.4928 0.3356 -0.0498 0.0296  0.0252  449  LEU B CG  
12170 C CD1 . LEU B 451  ? 0.4827 0.5839 0.4320 -0.0436 0.0297  0.0211  449  LEU B CD1 
12171 C CD2 . LEU B 451  ? 0.3682 0.4567 0.3085 -0.0529 0.0255  0.0259  449  LEU B CD2 
12172 N N   . HIS B 452  ? 0.3491 0.4531 0.2722 -0.0507 0.0348  0.0293  450  HIS B N   
12173 C CA  . HIS B 452  ? 0.4311 0.5384 0.3487 -0.0477 0.0377  0.0286  450  HIS B CA  
12174 C C   . HIS B 452  ? 0.4299 0.5453 0.3512 -0.0411 0.0411  0.0253  450  HIS B C   
12175 O O   . HIS B 452  ? 0.3540 0.4663 0.2795 -0.0372 0.0400  0.0220  450  HIS B O   
12176 C CB  . HIS B 452  ? 0.3652 0.4595 0.2759 -0.0460 0.0349  0.0270  450  HIS B CB  
12177 C CG  . HIS B 452  ? 0.4161 0.5122 0.3208 -0.0420 0.0374  0.0254  450  HIS B CG  
12178 N ND1 . HIS B 452  ? 0.4610 0.5597 0.3590 -0.0447 0.0390  0.0283  450  HIS B ND1 
12179 C CD2 . HIS B 452  ? 0.4370 0.5324 0.3411 -0.0355 0.0385  0.0212  450  HIS B CD2 
12180 C CE1 . HIS B 452  ? 0.4410 0.5406 0.3344 -0.0399 0.0411  0.0258  450  HIS B CE1 
12181 N NE2 . HIS B 452  ? 0.4388 0.5362 0.3357 -0.0343 0.0407  0.0215  450  HIS B NE2 
12182 N N   . GLY B 453  ? 0.4361 0.5618 0.3554 -0.0400 0.0453  0.0262  451  GLY B N   
12183 C CA  . GLY B 453  ? 0.4515 0.5849 0.3732 -0.0335 0.0488  0.0232  451  GLY B CA  
12184 C C   . GLY B 453  ? 0.4925 0.6377 0.4228 -0.0335 0.0508  0.0240  451  GLY B C   
12185 O O   . GLY B 453  ? 0.5023 0.6603 0.4342 -0.0323 0.0549  0.0251  451  GLY B O   
12186 N N   . MET B 454  ? 0.4404 0.5816 0.3765 -0.0348 0.0479  0.0235  452  MET B N   
12187 C CA  . MET B 454  ? 0.4741 0.6255 0.4186 -0.0345 0.0492  0.0239  452  MET B CA  
12188 C C   . MET B 454  ? 0.4790 0.6411 0.4260 -0.0409 0.0507  0.0288  452  MET B C   
12189 O O   . MET B 454  ? 0.5318 0.7073 0.4840 -0.0400 0.0538  0.0298  452  MET B O   
12190 C CB  . MET B 454  ? 0.5099 0.6530 0.4589 -0.0344 0.0454  0.0221  452  MET B CB  
12191 C CG  . MET B 454  ? 0.5234 0.6756 0.4810 -0.0341 0.0462  0.0223  452  MET B CG  
12192 S SD  . MET B 454  ? 0.7374 0.8790 0.6992 -0.0346 0.0416  0.0204  452  MET B SD  
12193 C CE  . MET B 454  ? 0.7342 0.8651 0.6927 -0.0272 0.0407  0.0153  452  MET B CE  
12194 N N   . GLY B 455  ? 0.4547 0.6114 0.3980 -0.0475 0.0484  0.0320  453  GLY B N   
12195 C CA  . GLY B 455  ? 0.4447 0.6097 0.3907 -0.0545 0.0488  0.0368  453  GLY B CA  
12196 C C   . GLY B 455  ? 0.4818 0.6571 0.4244 -0.0572 0.0525  0.0403  453  GLY B C   
12197 O O   . GLY B 455  ? 0.4777 0.6635 0.4240 -0.0623 0.0537  0.0442  453  GLY B O   
12198 N N   . GLU B 456  ? 0.4744 0.6470 0.4100 -0.0541 0.0541  0.0391  454  GLU B N   
12199 C CA  . GLU B 456  ? 0.4860 0.6676 0.4175 -0.0570 0.0575  0.0427  454  GLU B CA  
12200 C C   . GLU B 456  ? 0.4426 0.6427 0.3800 -0.0557 0.0623  0.0441  454  GLU B C   
12201 O O   . GLU B 456  ? 0.4350 0.6440 0.3729 -0.0614 0.0639  0.0486  454  GLU B O   
12202 C CB  . GLU B 456  ? 0.5220 0.6972 0.4446 -0.0530 0.0585  0.0406  454  GLU B CB  
12203 C CG  . GLU B 456  ? 0.5500 0.7091 0.4656 -0.0560 0.0542  0.0409  454  GLU B CG  
12204 C CD  . GLU B 456  ? 0.5004 0.6466 0.4166 -0.0516 0.0506  0.0364  454  GLU B CD  
12205 O OE1 . GLU B 456  ? 0.5062 0.6538 0.4295 -0.0494 0.0499  0.0344  454  GLU B OE1 
12206 O OE2 . GLU B 456  ? 0.4919 0.6266 0.4013 -0.0503 0.0484  0.0349  454  GLU B OE2 
12207 N N   . PRO B 457  ? 0.4677 0.6739 0.4096 -0.0486 0.0646  0.0405  455  PRO B N   
12208 C CA  . PRO B 457  ? 0.4466 0.6690 0.3953 -0.0470 0.0683  0.0417  455  PRO B CA  
12209 C C   . PRO B 457  ? 0.4635 0.6923 0.4194 -0.0537 0.0667  0.0457  455  PRO B C   
12210 O O   . PRO B 457  ? 0.4690 0.7072 0.4277 -0.0557 0.0682  0.0484  455  PRO B O   
12211 C CB  . PRO B 457  ? 0.4604 0.6846 0.4133 -0.0388 0.0695  0.0371  455  PRO B CB  
12212 C CG  . PRO B 457  ? 0.5261 0.7361 0.4721 -0.0346 0.0678  0.0332  455  PRO B CG  
12213 C CD  . PRO B 457  ? 0.5074 0.7045 0.4489 -0.0410 0.0635  0.0350  455  PRO B CD  
12214 N N   . LEU B 458  ? 0.4511 0.6748 0.4097 -0.0574 0.0634  0.0461  456  LEU B N   
12215 C CA  . LEU B 458  ? 0.4576 0.6861 0.4223 -0.0642 0.0614  0.0497  456  LEU B CA  
12216 C C   . LEU B 458  ? 0.4293 0.6543 0.3892 -0.0722 0.0598  0.0541  456  LEU B C   
12217 O O   . LEU B 458  ? 0.3850 0.6181 0.3484 -0.0763 0.0600  0.0574  456  LEU B O   
12218 C CB  . LEU B 458  ? 0.4379 0.6599 0.4062 -0.0656 0.0579  0.0485  456  LEU B CB  
12219 C CG  . LEU B 458  ? 0.4430 0.6678 0.4160 -0.0736 0.0552  0.0523  456  LEU B CG  
12220 C CD1 . LEU B 458  ? 0.4273 0.6664 0.4083 -0.0731 0.0567  0.0538  456  LEU B CD1 
12221 C CD2 . LEU B 458  ? 0.3607 0.5754 0.3367 -0.0732 0.0510  0.0498  456  LEU B CD2 
12222 N N   . TYR B 459  ? 0.4332 0.6458 0.3845 -0.0745 0.0581  0.0543  457  TYR B N   
12223 C CA  . TYR B 459  ? 0.4077 0.6149 0.3543 -0.0825 0.0558  0.0585  457  TYR B CA  
12224 C C   . TYR B 459  ? 0.4007 0.6118 0.3426 -0.0824 0.0584  0.0602  457  TYR B C   
12225 O O   . TYR B 459  ? 0.3813 0.5909 0.3207 -0.0891 0.0570  0.0642  457  TYR B O   
12226 C CB  . TYR B 459  ? 0.4169 0.6062 0.3576 -0.0844 0.0513  0.0575  457  TYR B CB  
12227 C CG  . TYR B 459  ? 0.3846 0.5685 0.3308 -0.0866 0.0474  0.0568  457  TYR B CG  
12228 C CD1 . TYR B 459  ? 0.3776 0.5625 0.3253 -0.0950 0.0452  0.0611  457  TYR B CD1 
12229 C CD2 . TYR B 459  ? 0.4053 0.5838 0.3551 -0.0805 0.0460  0.0521  457  TYR B CD2 
12230 C CE1 . TYR B 459  ? 0.3647 0.5448 0.3170 -0.0970 0.0416  0.0604  457  TYR B CE1 
12231 C CE2 . TYR B 459  ? 0.3867 0.5607 0.3413 -0.0826 0.0425  0.0516  457  TYR B CE2 
12232 C CZ  . TYR B 459  ? 0.3540 0.5288 0.3097 -0.0908 0.0404  0.0557  457  TYR B CZ  
12233 O OH  . TYR B 459  ? 0.3612 0.5314 0.3210 -0.0930 0.0369  0.0552  457  TYR B OH  
12234 N N   . GLU B 460  ? 0.4097 0.6259 0.3506 -0.0751 0.0621  0.0574  458  GLU B N   
12235 C CA  . GLU B 460  ? 0.4358 0.6588 0.3741 -0.0747 0.0651  0.0590  458  GLU B CA  
12236 C C   . GLU B 460  ? 0.5037 0.7397 0.4498 -0.0777 0.0661  0.0620  458  GLU B C   
12237 O O   . GLU B 460  ? 0.4875 0.7289 0.4318 -0.0801 0.0678  0.0648  458  GLU B O   
12238 C CB  . GLU B 460  ? 0.4688 0.6943 0.4046 -0.0658 0.0688  0.0550  458  GLU B CB  
12239 N N   . GLU B 461  ? 0.4535 0.6948 0.4081 -0.0778 0.0650  0.0616  459  GLU B N   
12240 C CA  . GLU B 461  ? 0.4733 0.7263 0.4355 -0.0814 0.0651  0.0646  459  GLU B CA  
12241 C C   . GLU B 461  ? 0.4797 0.7280 0.4424 -0.0907 0.0609  0.0684  459  GLU B C   
12242 O O   . GLU B 461  ? 0.4438 0.7007 0.4131 -0.0942 0.0601  0.0707  459  GLU B O   
12243 C CB  . GLU B 461  ? 0.4273 0.6890 0.3983 -0.0759 0.0661  0.0620  459  GLU B CB  
12244 C CG  . GLU B 461  ? 0.4268 0.6917 0.3973 -0.0663 0.0698  0.0578  459  GLU B CG  
12245 C CD  . GLU B 461  ? 0.5253 0.7974 0.4930 -0.0641 0.0736  0.0587  459  GLU B CD  
12246 O OE1 . GLU B 461  ? 0.5113 0.7907 0.4809 -0.0693 0.0738  0.0626  459  GLU B OE1 
12247 O OE2 . GLU B 461  ? 0.5730 0.8432 0.5364 -0.0573 0.0763  0.0554  459  GLU B OE2 
12248 N N   . VAL B 462  ? 0.4615 0.6959 0.4171 -0.0948 0.0579  0.0691  460  VAL B N   
12249 C CA  . VAL B 462  ? 0.4437 0.6713 0.3992 -0.1031 0.0535  0.0721  460  VAL B CA  
12250 C C   . VAL B 462  ? 0.4441 0.6633 0.3913 -0.1091 0.0519  0.0754  460  VAL B C   
12251 O O   . VAL B 462  ? 0.4528 0.6742 0.4009 -0.1158 0.0502  0.0792  460  VAL B O   
12252 C CB  . VAL B 462  ? 0.4268 0.6438 0.3823 -0.1026 0.0504  0.0696  460  VAL B CB  
12253 C CG1 . VAL B 462  ? 0.3728 0.5813 0.3272 -0.1111 0.0457  0.0726  460  VAL B CG1 
12254 C CG2 . VAL B 462  ? 0.4368 0.6622 0.4007 -0.0970 0.0518  0.0666  460  VAL B CG2 
12255 N N   . VAL B 463  ? 0.4260 0.6353 0.3650 -0.1068 0.0521  0.0740  461  VAL B N   
12256 C CA  . VAL B 463  ? 0.4445 0.6449 0.3753 -0.1123 0.0504  0.0772  461  VAL B CA  
12257 C C   . VAL B 463  ? 0.4498 0.6600 0.3796 -0.1121 0.0538  0.0792  461  VAL B C   
12258 O O   . VAL B 463  ? 0.4835 0.7039 0.4160 -0.1059 0.0580  0.0772  461  VAL B O   
12259 C CB  . VAL B 463  ? 0.4624 0.6483 0.3842 -0.1100 0.0490  0.0752  461  VAL B CB  
12260 C CG1 . VAL B 463  ? 0.3673 0.5466 0.2912 -0.1073 0.0471  0.0719  461  VAL B CG1 
12261 C CG2 . VAL B 463  ? 0.4496 0.6384 0.3669 -0.1038 0.0529  0.0732  461  VAL B CG2 
12262 N N   . GLY B 464  ? 0.4643 0.6712 0.3901 -0.1190 0.0520  0.0833  462  GLY B N   
12263 C CA  . GLY B 464  ? 0.4884 0.7036 0.4124 -0.1197 0.0551  0.0857  462  GLY B CA  
12264 C C   . GLY B 464  ? 0.5355 0.7634 0.4668 -0.1240 0.0555  0.0888  462  GLY B C   
12265 O O   . GLY B 464  ? 0.5403 0.7749 0.4796 -0.1237 0.0550  0.0881  462  GLY B O   
12266 N N   . ARG B 465  ? 0.6212 0.8527 0.5494 -0.1281 0.0564  0.0924  463  ARG B N   
12267 C CA  . ARG B 465  ? 0.5615 0.8049 0.4958 -0.1330 0.0566  0.0959  463  ARG B CA  
12268 C C   . ARG B 465  ? 0.5700 0.8299 0.5129 -0.1272 0.0607  0.0941  463  ARG B C   
12269 O O   . ARG B 465  ? 0.5959 0.8647 0.5465 -0.1298 0.0598  0.0954  463  ARG B O   
12270 C CB  . ARG B 465  ? 0.5933 0.8375 0.5220 -0.1378 0.0574  0.0999  463  ARG B CB  
12271 N N   . GLY B 466  ? 0.5768 0.8405 0.5183 -0.1193 0.0649  0.0910  464  GLY B N   
12272 C CA  . GLY B 466  ? 0.5547 0.8331 0.5037 -0.1130 0.0687  0.0890  464  GLY B CA  
12273 C C   . GLY B 466  ? 0.5532 0.8333 0.5095 -0.1097 0.0675  0.0861  464  GLY B C   
12274 O O   . GLY B 466  ? 0.5226 0.8152 0.4860 -0.1053 0.0701  0.0849  464  GLY B O   
12275 N N   . LYS B 467  ? 0.5487 0.8165 0.5034 -0.1117 0.0636  0.0850  465  LYS B N   
12276 C CA  . LYS B 467  ? 0.4979 0.7660 0.4590 -0.1090 0.0621  0.0823  465  LYS B CA  
12277 C C   . LYS B 467  ? 0.5172 0.7811 0.4809 -0.1169 0.0573  0.0849  465  LYS B C   
12278 O O   . LYS B 467  ? 0.4900 0.7602 0.4561 -0.1228 0.0563  0.0886  465  LYS B O   
12279 C CB  . LYS B 467  ? 0.4814 0.7390 0.4384 -0.1031 0.0622  0.0779  465  LYS B CB  
12280 C CG  . LYS B 467  ? 0.4841 0.7447 0.4376 -0.0951 0.0666  0.0750  465  LYS B CG  
12281 C CD  . LYS B 467  ? 0.5573 0.8339 0.5181 -0.0902 0.0704  0.0743  465  LYS B CD  
12282 C CE  . LYS B 467  ? 0.5570 0.8363 0.5137 -0.0826 0.0749  0.0717  465  LYS B CE  
12283 N NZ  . LYS B 467  ? 0.5081 0.7919 0.4695 -0.0738 0.0770  0.0672  465  LYS B NZ  
12284 N N   . LEU B 468  ? 0.4844 0.7374 0.4474 -0.1171 0.0541  0.0829  466  LEU B N   
12285 C CA  . LEU B 468  ? 0.4557 0.7035 0.4206 -0.1243 0.0494  0.0850  466  LEU B CA  
12286 C C   . LEU B 468  ? 0.4069 0.6411 0.3636 -0.1315 0.0459  0.0878  466  LEU B C   
12287 O O   . LEU B 468  ? 0.3902 0.6196 0.3475 -0.1383 0.0418  0.0901  466  LEU B O   
12288 C CB  . LEU B 468  ? 0.4458 0.6884 0.4140 -0.1214 0.0475  0.0817  466  LEU B CB  
12289 C CG  . LEU B 468  ? 0.4756 0.7298 0.4517 -0.1140 0.0504  0.0786  466  LEU B CG  
12290 C CD1 . LEU B 468  ? 0.4659 0.7150 0.4456 -0.1127 0.0479  0.0760  466  LEU B CD1 
12291 C CD2 . LEU B 468  ? 0.5074 0.7775 0.4904 -0.1151 0.0520  0.0809  466  LEU B CD2 
12292 N N   . ASP B 469  ? 0.4525 0.6800 0.4015 -0.1300 0.0473  0.0876  467  ASP B N   
12293 C CA  . ASP B 469  ? 0.4935 0.7075 0.4339 -0.1360 0.0441  0.0902  467  ASP B CA  
12294 C C   . ASP B 469  ? 0.4355 0.6344 0.3734 -0.1388 0.0393  0.0893  467  ASP B C   
12295 O O   . ASP B 469  ? 0.4364 0.6264 0.3709 -0.1458 0.0353  0.0921  467  ASP B O   
12296 C CB  . ASP B 469  ? 0.5172 0.7358 0.4576 -0.1435 0.0430  0.0949  467  ASP B CB  
12297 C CG  . ASP B 469  ? 0.5160 0.7234 0.4468 -0.1477 0.0414  0.0975  467  ASP B CG  
12298 O OD1 . ASP B 469  ? 0.5162 0.7175 0.4410 -0.1434 0.0430  0.0957  467  ASP B OD1 
12299 O OD2 . ASP B 469  ? 0.5994 0.8037 0.5284 -0.1552 0.0385  0.1012  467  ASP B OD2 
12300 N N   . ARG B 470  ? 0.4336 0.6295 0.3730 -0.1331 0.0398  0.0854  468  ARG B N   
12301 C CA  . ARG B 470  ? 0.4245 0.6058 0.3609 -0.1349 0.0357  0.0843  468  ARG B CA  
12302 C C   . ARG B 470  ? 0.4227 0.5942 0.3525 -0.1299 0.0365  0.0815  468  ARG B C   
12303 O O   . ARG B 470  ? 0.4082 0.5865 0.3392 -0.1230 0.0403  0.0788  468  ARG B O   
12304 C CB  . ARG B 470  ? 0.4003 0.5852 0.3445 -0.1335 0.0347  0.0821  468  ARG B CB  
12305 C CG  . ARG B 470  ? 0.4188 0.6110 0.3690 -0.1391 0.0328  0.0848  468  ARG B CG  
12306 C CD  . ARG B 470  ? 0.4000 0.5814 0.3447 -0.1476 0.0283  0.0883  468  ARG B CD  
12307 N NE  . ARG B 470  ? 0.4954 0.6844 0.4453 -0.1530 0.0266  0.0909  468  ARG B NE  
12308 C CZ  . ARG B 470  ? 0.4705 0.6701 0.4220 -0.1558 0.0281  0.0940  468  ARG B CZ  
12309 N NH1 . ARG B 470  ? 0.4285 0.6320 0.3766 -0.1539 0.0315  0.0949  468  ARG B NH1 
12310 N NH2 . ARG B 470  ? 0.4924 0.6990 0.4488 -0.1606 0.0263  0.0962  468  ARG B NH2 
12311 N N   . PRO B 471  ? 0.4081 0.5635 0.3306 -0.1329 0.0327  0.0821  469  PRO B N   
12312 C CA  . PRO B 471  ? 0.3896 0.5354 0.3053 -0.1283 0.0331  0.0797  469  PRO B CA  
12313 C C   . PRO B 471  ? 0.3830 0.5273 0.3024 -0.1224 0.0333  0.0753  469  PRO B C   
12314 O O   . PRO B 471  ? 0.3288 0.4747 0.2547 -0.1230 0.0318  0.0742  469  PRO B O   
12315 C CB  . PRO B 471  ? 0.3996 0.5284 0.3071 -0.1339 0.0283  0.0821  469  PRO B CB  
12316 C CG  . PRO B 471  ? 0.3866 0.5139 0.2981 -0.1400 0.0250  0.0840  469  PRO B CG  
12317 C CD  . PRO B 471  ? 0.3663 0.5111 0.2861 -0.1406 0.0278  0.0850  469  PRO B CD  
12318 N N   . CYS B 472  ? 0.3472 0.4868 0.2635 -0.1150 0.0343  0.0714  470  CYS B N   
12319 C CA  . CYS B 472  ? 0.3565 0.4913 0.2765 -0.1073 0.0335  0.0658  470  CYS B CA  
12320 C C   . CYS B 472  ? 0.3739 0.4935 0.2867 -0.1037 0.0311  0.0633  470  CYS B C   
12321 O O   . CYS B 472  ? 0.3492 0.4685 0.2557 -0.1028 0.0327  0.0641  470  CYS B O   
12322 C CB  . CYS B 472  ? 0.3627 0.5119 0.2883 -0.1008 0.0384  0.0631  470  CYS B CB  
12323 S SG  . CYS B 472  ? 0.3812 0.5249 0.3113 -0.0916 0.0375  0.0564  470  CYS B SG  
12324 N N   . ARG B 473  ? 0.3523 0.4595 0.2659 -0.1017 0.0271  0.0603  471  ARG B N   
12325 C CA  . ARG B 473  ? 0.3500 0.4433 0.2581 -0.0976 0.0246  0.0575  471  ARG B CA  
12326 C C   . ARG B 473  ? 0.3356 0.4306 0.2476 -0.0890 0.0261  0.0522  471  ARG B C   
12327 O O   . ARG B 473  ? 0.3208 0.4174 0.2395 -0.0867 0.0257  0.0497  471  ARG B O   
12328 C CB  . ARG B 473  ? 0.3186 0.3968 0.2248 -0.1004 0.0193  0.0577  471  ARG B CB  
12329 C CG  . ARG B 473  ? 0.3221 0.3862 0.2226 -0.0963 0.0165  0.0551  471  ARG B CG  
12330 C CD  . ARG B 473  ? 0.3063 0.3558 0.2042 -0.0994 0.0114  0.0558  471  ARG B CD  
12331 N NE  . ARG B 473  ? 0.3572 0.4058 0.2519 -0.1077 0.0101  0.0609  471  ARG B NE  
12332 C CZ  . ARG B 473  ? 0.3611 0.4048 0.2481 -0.1116 0.0092  0.0644  471  ARG B CZ  
12333 N NH1 . ARG B 473  ? 0.3512 0.3901 0.2327 -0.1080 0.0092  0.0635  471  ARG B NH1 
12334 N NH2 . ARG B 473  ? 0.3581 0.4016 0.2428 -0.1194 0.0081  0.0691  471  ARG B NH2 
12335 N N   . ILE B 474  ? 0.3460 0.4407 0.2537 -0.0845 0.0279  0.0505  472  ILE B N   
12336 C CA  . ILE B 474  ? 0.3253 0.4212 0.2356 -0.0766 0.0294  0.0456  472  ILE B CA  
12337 C C   . ILE B 474  ? 0.3182 0.3995 0.2271 -0.0735 0.0253  0.0424  472  ILE B C   
12338 O O   . ILE B 474  ? 0.3357 0.4068 0.2380 -0.0744 0.0228  0.0431  472  ILE B O   
12339 C CB  . ILE B 474  ? 0.3373 0.4388 0.2429 -0.0732 0.0330  0.0451  472  ILE B CB  
12340 C CG1 . ILE B 474  ? 0.3490 0.4663 0.2567 -0.0757 0.0375  0.0481  472  ILE B CG1 
12341 C CG2 . ILE B 474  ? 0.3494 0.4499 0.2566 -0.0650 0.0340  0.0398  472  ILE B CG2 
12342 C CD1 . ILE B 474  ? 0.3813 0.5037 0.2831 -0.0736 0.0410  0.0485  472  ILE B CD1 
12343 N N   . TYR B 475  ? 0.3071 0.3878 0.2222 -0.0698 0.0246  0.0390  473  TYR B N   
12344 C CA  . TYR B 475  ? 0.3027 0.3715 0.2175 -0.0659 0.0212  0.0356  473  TYR B CA  
12345 C C   . TYR B 475  ? 0.3558 0.4241 0.2680 -0.0597 0.0227  0.0323  473  TYR B C   
12346 O O   . TYR B 475  ? 0.3185 0.3949 0.2344 -0.0554 0.0257  0.0299  473  TYR B O   
12347 C CB  . TYR B 475  ? 0.3212 0.3906 0.2435 -0.0644 0.0203  0.0334  473  TYR B CB  
12348 C CG  . TYR B 475  ? 0.3028 0.3602 0.2255 -0.0614 0.0167  0.0303  473  TYR B CG  
12349 C CD1 . TYR B 475  ? 0.3002 0.3474 0.2210 -0.0650 0.0128  0.0317  473  TYR B CD1 
12350 C CD2 . TYR B 475  ? 0.2912 0.3478 0.2162 -0.0550 0.0172  0.0262  473  TYR B CD2 
12351 C CE1 . TYR B 475  ? 0.3212 0.3582 0.2426 -0.0620 0.0097  0.0289  473  TYR B CE1 
12352 C CE2 . TYR B 475  ? 0.3089 0.3553 0.2346 -0.0524 0.0140  0.0236  473  TYR B CE2 
12353 C CZ  . TYR B 475  ? 0.3078 0.3448 0.2319 -0.0558 0.0104  0.0250  473  TYR B CZ  
12354 O OH  . TYR B 475  ? 0.3374 0.3650 0.2623 -0.0530 0.0074  0.0225  473  TYR B OH  
12355 N N   . ALA B 476  ? 0.2969 0.3556 0.2026 -0.0592 0.0205  0.0322  474  ALA B N   
12356 C CA  . ALA B 476  ? 0.3415 0.3999 0.2430 -0.0545 0.0219  0.0299  474  ALA B CA  
12357 C C   . ALA B 476  ? 0.3387 0.3870 0.2404 -0.0500 0.0188  0.0261  474  ALA B C   
12358 O O   . ALA B 476  ? 0.3326 0.3704 0.2306 -0.0513 0.0152  0.0267  474  ALA B O   
12359 C CB  . ALA B 476  ? 0.3395 0.3959 0.2325 -0.0577 0.0219  0.0330  474  ALA B CB  
12360 N N   . PRO B 477  ? 0.3047 0.3557 0.2106 -0.0446 0.0201  0.0223  475  PRO B N   
12361 C CA  . PRO B 477  ? 0.3383 0.3804 0.2440 -0.0404 0.0174  0.0188  475  PRO B CA  
12362 C C   . PRO B 477  ? 0.3402 0.3775 0.2382 -0.0389 0.0167  0.0184  475  PRO B C   
12363 O O   . PRO B 477  ? 0.3580 0.4010 0.2519 -0.0386 0.0196  0.0191  475  PRO B O   
12364 C CB  . PRO B 477  ? 0.3418 0.3896 0.2532 -0.0355 0.0195  0.0153  475  PRO B CB  
12365 C CG  . PRO B 477  ? 0.3188 0.3769 0.2352 -0.0378 0.0223  0.0171  475  PRO B CG  
12366 C CD  . PRO B 477  ? 0.3382 0.4004 0.2499 -0.0425 0.0237  0.0211  475  PRO B CD  
12367 N N   . VAL B 478  ? 0.3124 0.3393 0.2085 -0.0380 0.0129  0.0173  476  VAL B N   
12368 C CA  . VAL B 478  ? 0.3452 0.3663 0.2341 -0.0367 0.0114  0.0169  476  VAL B CA  
12369 C C   . VAL B 478  ? 0.3774 0.3920 0.2684 -0.0323 0.0089  0.0131  476  VAL B C   
12370 O O   . VAL B 478  ? 0.3575 0.3664 0.2522 -0.0325 0.0059  0.0128  476  VAL B O   
12371 C CB  . VAL B 478  ? 0.3405 0.3549 0.2239 -0.0411 0.0087  0.0205  476  VAL B CB  
12372 C CG1 . VAL B 478  ? 0.3754 0.3844 0.2512 -0.0395 0.0072  0.0200  476  VAL B CG1 
12373 C CG2 . VAL B 478  ? 0.3549 0.3756 0.2365 -0.0461 0.0111  0.0245  476  VAL B CG2 
12374 N N   . GLY B 479  ? 0.3971 0.4128 0.2859 -0.0283 0.0100  0.0104  477  GLY B N   
12375 C CA  . GLY B 479  ? 0.4434 0.4532 0.3338 -0.0244 0.0075  0.0070  477  GLY B CA  
12376 C C   . GLY B 479  ? 0.4539 0.4658 0.3411 -0.0204 0.0094  0.0041  477  GLY B C   
12377 O O   . GLY B 479  ? 0.4238 0.4430 0.3091 -0.0199 0.0131  0.0042  477  GLY B O   
12378 N N   . THR B 480  ? 0.5195 0.5250 0.4060 -0.0176 0.0066  0.0014  478  THR B N   
12379 C CA  . THR B 480  ? 0.5426 0.5487 0.4259 -0.0137 0.0078  -0.0017 478  THR B CA  
12380 C C   . THR B 480  ? 0.5668 0.5792 0.4558 -0.0107 0.0108  -0.0040 478  THR B C   
12381 O O   . THR B 480  ? 0.5611 0.5750 0.4572 -0.0111 0.0107  -0.0040 478  THR B O   
12382 C CB  . THR B 480  ? 0.5588 0.5565 0.4407 -0.0118 0.0037  -0.0039 478  THR B CB  
12383 O OG1 . THR B 480  ? 0.5523 0.5481 0.4420 -0.0108 0.0020  -0.0053 478  THR B OG1 
12384 C CG2 . THR B 480  ? 0.5713 0.5628 0.4483 -0.0145 0.0004  -0.0014 478  THR B CG2 
12385 N N   . HIS B 481  ? 0.5962 0.6120 0.4814 -0.0077 0.0135  -0.0060 479  HIS B N   
12386 C CA  . HIS B 481  ? 0.6382 0.6596 0.5279 -0.0044 0.0164  -0.0083 479  HIS B CA  
12387 C C   . HIS B 481  ? 0.5851 0.6023 0.4811 -0.0025 0.0140  -0.0107 479  HIS B C   
12388 O O   . HIS B 481  ? 0.6325 0.6539 0.5352 -0.0018 0.0154  -0.0110 479  HIS B O   
12389 C CB  . HIS B 481  ? 0.6080 0.6311 0.4915 -0.0007 0.0188  -0.0106 479  HIS B CB  
12390 N N   . GLU B 482  ? 0.6208 0.6298 0.5147 -0.0017 0.0104  -0.0122 480  GLU B N   
12391 C CA  . GLU B 482  ? 0.6209 0.6260 0.5208 -0.0004 0.0079  -0.0141 480  GLU B CA  
12392 C C   . GLU B 482  ? 0.6222 0.6283 0.5290 -0.0031 0.0071  -0.0120 480  GLU B C   
12393 O O   . GLU B 482  ? 0.6792 0.6876 0.5923 -0.0019 0.0079  -0.0129 480  GLU B O   
12394 C CB  . GLU B 482  ? 0.6570 0.6537 0.5534 0.0001  0.0039  -0.0154 480  GLU B CB  
12395 N N   . THR B 483  ? 0.6442 0.6481 0.5492 -0.0066 0.0055  -0.0091 481  THR B N   
12396 C CA  . THR B 483  ? 0.6587 0.6630 0.5693 -0.0092 0.0047  -0.0071 481  THR B CA  
12397 C C   . THR B 483  ? 0.6149 0.6274 0.5294 -0.0099 0.0082  -0.0062 481  THR B C   
12398 O O   . THR B 483  ? 0.6545 0.6683 0.5753 -0.0101 0.0082  -0.0063 481  THR B O   
12399 C CB  . THR B 483  ? 0.6168 0.6171 0.5234 -0.0128 0.0026  -0.0041 481  THR B CB  
12400 O OG1 . THR B 483  ? 0.6471 0.6402 0.5507 -0.0120 -0.0010 -0.0049 481  THR B OG1 
12401 C CG2 . THR B 483  ? 0.5804 0.5804 0.4919 -0.0156 0.0017  -0.0020 481  THR B CG2 
12402 N N   . LEU B 484  ? 0.6327 0.6510 0.5435 -0.0102 0.0114  -0.0052 482  LEU B N   
12403 C CA  . LEU B 484  ? 0.6657 0.6927 0.5801 -0.0114 0.0147  -0.0037 482  LEU B CA  
12404 C C   . LEU B 484  ? 0.7073 0.7381 0.6278 -0.0082 0.0162  -0.0061 482  LEU B C   
12405 O O   . LEU B 484  ? 0.7515 0.7873 0.6775 -0.0095 0.0173  -0.0050 482  LEU B O   
12406 C CB  . LEU B 484  ? 0.6304 0.6634 0.5394 -0.0118 0.0179  -0.0025 482  LEU B CB  
12407 C CG  . LEU B 484  ? 0.6082 0.6512 0.5202 -0.0100 0.0221  -0.0029 482  LEU B CG  
12408 C CD1 . LEU B 484  ? 0.5723 0.6216 0.4890 -0.0139 0.0232  0.0003  482  LEU B CD1 
12409 C CD2 . LEU B 484  ? 0.6226 0.6697 0.5281 -0.0083 0.0250  -0.0031 482  LEU B CD2 
12410 N N   . LEU B 485  ? 0.8001 0.8284 0.7197 -0.0041 0.0160  -0.0093 483  LEU B N   
12411 C CA  . LEU B 485  ? 0.8237 0.8554 0.7482 -0.0007 0.0176  -0.0116 483  LEU B CA  
12412 C C   . LEU B 485  ? 0.8683 0.8984 0.8000 -0.0015 0.0158  -0.0116 483  LEU B C   
12413 O O   . LEU B 485  ? 0.8714 0.9034 0.8074 0.0011  0.0167  -0.0134 483  LEU B O   
12414 C CB  . LEU B 485  ? 0.7501 0.7776 0.6713 0.0035  0.0172  -0.0150 483  LEU B CB  
12415 N N   . ALA B 486  ? 0.8772 0.9034 0.8096 -0.0049 0.0134  -0.0097 484  ALA B N   
12416 C CA  . ALA B 486  ? 0.9078 0.9324 0.8464 -0.0059 0.0118  -0.0095 484  ALA B CA  
12417 C C   . ALA B 486  ? 0.9346 0.9668 0.8779 -0.0072 0.0141  -0.0082 484  ALA B C   
12418 O O   . ALA B 486  ? 0.9420 0.9800 0.8874 -0.0046 0.0167  -0.0093 484  ALA B O   
12419 C CB  . ALA B 486  ? 0.8617 0.8800 0.7991 -0.0090 0.0086  -0.0078 484  ALA B CB  
12420 N N   . TYR B 487  ? 0.9323 0.9645 0.8770 -0.0110 0.0132  -0.0057 485  TYR B N   
12421 C CA  . TYR B 487  ? 1.0011 1.0398 0.9506 -0.0127 0.0148  -0.0043 485  TYR B CA  
12422 C C   . TYR B 487  ? 1.0224 1.0703 0.9708 -0.0135 0.0182  -0.0028 485  TYR B C   
12423 O O   . TYR B 487  ? 1.0636 1.1163 1.0137 -0.0170 0.0189  -0.0002 485  TYR B O   
12424 C CB  . TYR B 487  ? 1.0568 1.0920 1.0074 -0.0169 0.0126  -0.0021 485  TYR B CB  
12425 N N   . LEU B 488  ? 0.9926 1.0430 0.9380 -0.0102 0.0202  -0.0043 486  LEU B N   
12426 C CA  . LEU B 488  ? 0.9291 0.9894 0.8742 -0.0099 0.0238  -0.0032 486  LEU B CA  
12427 C C   . LEU B 488  ? 0.9357 1.0033 0.8873 -0.0083 0.0257  -0.0036 486  LEU B C   
12428 O O   . LEU B 488  ? 0.9408 1.0177 0.8940 -0.0094 0.0283  -0.0019 486  LEU B O   
12429 C CB  . LEU B 488  ? 0.8122 0.8725 0.7520 -0.0062 0.0255  -0.0051 486  LEU B CB  
12430 N N   . VAL B 489  ? 0.9419 1.0058 0.8974 -0.0060 0.0242  -0.0058 487  VAL B N   
12431 C CA  . VAL B 489  ? 0.9132 0.9835 0.8747 -0.0043 0.0257  -0.0063 487  VAL B CA  
12432 C C   . VAL B 489  ? 0.9449 1.0188 0.9104 -0.0087 0.0251  -0.0036 487  VAL B C   
12433 O O   . VAL B 489  ? 0.9497 1.0324 0.9192 -0.0088 0.0271  -0.0026 487  VAL B O   
12434 C CB  . VAL B 489  ? 0.8486 0.9134 0.8125 -0.0005 0.0242  -0.0093 487  VAL B CB  
12435 C CG1 . VAL B 489  ? 0.7317 0.7941 0.6916 0.0040  0.0251  -0.0119 487  VAL B CG1 
12436 C CG2 . VAL B 489  ? 0.9171 0.9728 0.8812 -0.0026 0.0207  -0.0094 487  VAL B CG2 
12437 N N   . ARG B 490  ? 0.9682 1.0353 0.9328 -0.0123 0.0223  -0.0025 488  ARG B N   
12438 C CA  . ARG B 490  ? 0.9659 1.0354 0.9332 -0.0169 0.0216  0.0001  488  ARG B CA  
12439 C C   . ARG B 490  ? 0.9652 1.0424 0.9310 -0.0204 0.0236  0.0031  488  ARG B C   
12440 O O   . ARG B 490  ? 0.9520 1.0358 0.9213 -0.0232 0.0242  0.0051  488  ARG B O   
12441 C CB  . ARG B 490  ? 0.9652 1.0249 0.9309 -0.0197 0.0181  0.0005  488  ARG B CB  
12442 N N   . ARG B 491  ? 0.9623 1.0391 0.9227 -0.0203 0.0246  0.0036  489  ARG B N   
12443 C CA  . ARG B 491  ? 0.9606 1.0453 0.9191 -0.0233 0.0268  0.0065  489  ARG B CA  
12444 C C   . ARG B 491  ? 0.9696 1.0658 0.9308 -0.0203 0.0306  0.0062  489  ARG B C   
12445 O O   . ARG B 491  ? 0.9562 1.0615 0.9182 -0.0232 0.0327  0.0090  489  ARG B O   
12446 C CB  . ARG B 491  ? 0.9397 1.0197 0.8910 -0.0241 0.0266  0.0071  489  ARG B CB  
12447 N N   . LEU B 492  ? 0.9804 1.0766 0.9431 -0.0147 0.0315  0.0030  490  LEU B N   
12448 C CA  . LEU B 492  ? 0.9612 1.0675 0.9261 -0.0109 0.0350  0.0024  490  LEU B CA  
12449 C C   . LEU B 492  ? 0.9546 1.0662 0.9266 -0.0094 0.0353  0.0018  490  LEU B C   
12450 O O   . LEU B 492  ? 0.9540 1.0765 0.9292 -0.0081 0.0381  0.0027  490  LEU B O   
12451 C CB  . LEU B 492  ? 0.9107 1.0133 0.8715 -0.0052 0.0360  -0.0009 490  LEU B CB  
12452 N N   . LEU B 493  ? 0.9123 1.0168 0.8869 -0.0092 0.0326  0.0005  491  LEU B N   
12453 C CA  . LEU B 493  ? 0.8556 0.9648 0.8366 -0.0083 0.0326  0.0003  491  LEU B CA  
12454 C C   . LEU B 493  ? 0.8895 1.0070 0.8739 -0.0133 0.0330  0.0037  491  LEU B C   
12455 O O   . LEU B 493  ? 0.9169 1.0439 0.9062 -0.0123 0.0346  0.0043  491  LEU B O   
12456 C CB  . LEU B 493  ? 0.7577 0.8574 0.7403 -0.0078 0.0295  -0.0016 491  LEU B CB  
12457 N N   . GLU B 494  ? 0.8889 1.0030 0.8707 -0.0188 0.0314  0.0060  492  GLU B N   
12458 C CA  . GLU B 494  ? 0.8500 0.9709 0.8342 -0.0244 0.0314  0.0095  492  GLU B CA  
12459 C C   . GLU B 494  ? 0.8776 1.0096 0.8612 -0.0255 0.0346  0.0119  492  GLU B C   
12460 O O   . GLU B 494  ? 0.7887 0.9232 0.7709 -0.0311 0.0344  0.0151  492  GLU B O   
12461 C CB  . GLU B 494  ? 0.7773 0.8888 0.7583 -0.0297 0.0281  0.0110  492  GLU B CB  
12462 N N   . ASN B 495  ? 0.9130 1.0517 0.8973 -0.0203 0.0377  0.0104  493  ASN B N   
12463 C CA  . ASN B 495  ? 0.9175 1.0673 0.9010 -0.0202 0.0413  0.0122  493  ASN B CA  
12464 C C   . ASN B 495  ? 0.9506 1.1096 0.9380 -0.0142 0.0442  0.0106  493  ASN B C   
12465 O O   . ASN B 495  ? 0.9269 1.0988 0.9176 -0.0146 0.0469  0.0127  493  ASN B O   
12466 C CB  . ASN B 495  ? 0.9047 1.0491 0.8806 -0.0198 0.0419  0.0119  493  ASN B CB  
12467 N N   . GLY B 496  ? 0.9775 1.1300 0.9644 -0.0085 0.0437  0.0069  494  GLY B N   
12468 C CA  . GLY B 496  ? 0.9667 1.1257 0.9570 -0.0022 0.0459  0.0050  494  GLY B CA  
12469 C C   . GLY B 496  ? 1.0132 1.1747 1.0102 -0.0017 0.0446  0.0048  494  GLY B C   
12470 O O   . GLY B 496  ? 1.0565 1.2214 1.0561 0.0039  0.0459  0.0029  494  GLY B O   
12471 N N   . ALA B 497  ? 0.9352 1.0945 0.9346 -0.0072 0.0420  0.0067  495  ALA B N   
12472 C CA  . ALA B 497  ? 0.9031 1.0648 0.9085 -0.0071 0.0405  0.0067  495  ALA B CA  
12473 C C   . ALA B 497  ? 0.8724 1.0495 0.8835 -0.0078 0.0428  0.0092  495  ALA B C   
12474 O O   . ALA B 497  ? 0.8558 1.0410 0.8664 -0.0109 0.0446  0.0119  495  ALA B O   
12475 C CB  . ALA B 497  ? 0.8416 0.9953 0.8471 -0.0127 0.0369  0.0076  495  ALA B CB  
12476 N N   . ASN B 498  ? 0.8560 1.0371 0.8723 -0.0048 0.0425  0.0084  496  ASN B N   
12477 C CA  . ASN B 498  ? 0.8564 1.0527 0.8786 -0.0047 0.0445  0.0106  496  ASN B CA  
12478 C C   . ASN B 498  ? 0.7899 0.9923 0.8143 -0.0125 0.0436  0.0146  496  ASN B C   
12479 O O   . ASN B 498  ? 0.7711 0.9856 0.7973 -0.0141 0.0461  0.0172  496  ASN B O   
12480 C CB  . ASN B 498  ? 0.8313 1.0292 0.8586 -0.0008 0.0436  0.0093  496  ASN B CB  
12481 N N   . SER B 499  ? 0.7587 0.9528 0.7826 -0.0174 0.0401  0.0151  497  SER B N   
12482 C CA  . SER B 499  ? 0.6849 0.8826 0.7098 -0.0253 0.0387  0.0186  497  SER B CA  
12483 C C   . SER B 499  ? 0.6326 0.8286 0.6523 -0.0294 0.0394  0.0205  497  SER B C   
12484 O O   . SER B 499  ? 0.6496 0.8509 0.6702 -0.0358 0.0389  0.0239  497  SER B O   
12485 C CB  . SER B 499  ? 0.5705 0.7581 0.5953 -0.0288 0.0346  0.0182  497  SER B CB  
12486 O OG  . SER B 499  ? 0.6050 0.7780 0.6246 -0.0272 0.0330  0.0155  497  SER B OG  
12487 N N   . SER B 500  ? 0.6609 0.8498 0.6752 -0.0260 0.0405  0.0184  498  SER B N   
12488 C CA  . SER B 500  ? 0.6871 0.8731 0.6958 -0.0297 0.0410  0.0201  498  SER B CA  
12489 C C   . SER B 500  ? 0.6733 0.8736 0.6832 -0.0303 0.0447  0.0227  498  SER B C   
12490 O O   . SER B 500  ? 0.6973 0.9060 0.7093 -0.0246 0.0478  0.0215  498  SER B O   
12491 C CB  . SER B 500  ? 0.7207 0.8948 0.7231 -0.0258 0.0408  0.0170  498  SER B CB  
12492 O OG  . SER B 500  ? 0.7852 0.9461 0.7862 -0.0263 0.0373  0.0151  498  SER B OG  
12493 N N   . PHE B 501  ? 0.5973 0.8002 0.6055 -0.0371 0.0445  0.0263  499  PHE B N   
12494 C CA  . PHE B 501  ? 0.5992 0.8162 0.6085 -0.0386 0.0480  0.0293  499  PHE B CA  
12495 C C   . PHE B 501  ? 0.6683 0.8859 0.6729 -0.0331 0.0514  0.0275  499  PHE B C   
12496 O O   . PHE B 501  ? 0.6765 0.9070 0.6833 -0.0303 0.0552  0.0283  499  PHE B O   
12497 C CB  . PHE B 501  ? 0.5249 0.7422 0.5321 -0.0475 0.0466  0.0335  499  PHE B CB  
12498 C CG  . PHE B 501  ? 0.4875 0.7186 0.4951 -0.0497 0.0503  0.0370  499  PHE B CG  
12499 C CD1 . PHE B 501  ? 0.5007 0.7301 0.5020 -0.0487 0.0525  0.0370  499  PHE B CD1 
12500 C CD2 . PHE B 501  ? 0.4935 0.7396 0.5077 -0.0532 0.0514  0.0403  499  PHE B CD2 
12501 C CE1 . PHE B 501  ? 0.5123 0.7548 0.5137 -0.0508 0.0561  0.0403  499  PHE B CE1 
12502 C CE2 . PHE B 501  ? 0.4985 0.7550 0.5130 -0.0547 0.0539  0.0431  499  PHE B CE2 
12503 C CZ  . PHE B 501  ? 0.5057 0.7601 0.5138 -0.0533 0.0562  0.0430  499  PHE B CZ  
12504 N N   . VAL B 502  ? 0.6731 0.8769 0.6711 -0.0317 0.0500  0.0252  500  VAL B N   
12505 C CA  . VAL B 502  ? 0.7528 0.9557 0.7453 -0.0270 0.0528  0.0235  500  VAL B CA  
12506 C C   . VAL B 502  ? 0.7981 1.0071 0.7935 -0.0187 0.0556  0.0205  500  VAL B C   
12507 O O   . VAL B 502  ? 0.8061 1.0251 0.8010 -0.0156 0.0595  0.0208  500  VAL B O   
12508 C CB  . VAL B 502  ? 0.7793 0.9656 0.7647 -0.0268 0.0502  0.0213  500  VAL B CB  
12509 N N   . HIS B 503  ? 0.8012 1.0040 0.7992 -0.0150 0.0536  0.0176  501  HIS B N   
12510 C CA  . HIS B 503  ? 0.8287 1.0365 0.8295 -0.0073 0.0558  0.0148  501  HIS B CA  
12511 C C   . HIS B 503  ? 0.8118 1.0363 0.8199 -0.0070 0.0582  0.0171  501  HIS B C   
12512 O O   . HIS B 503  ? 0.8013 1.0340 0.8107 -0.0009 0.0615  0.0159  501  HIS B O   
12513 C CB  . HIS B 503  ? 0.8949 1.0917 0.8967 -0.0041 0.0528  0.0115  501  HIS B CB  
12514 C CG  . HIS B 503  ? 0.9183 1.1217 0.9254 0.0019  0.0541  0.0099  501  HIS B CG  
12515 N ND1 . HIS B 503  ? 0.9019 1.1128 0.9162 0.0003  0.0533  0.0115  501  HIS B ND1 
12516 C CD2 . HIS B 503  ? 0.9199 1.1230 0.9260 0.0096  0.0560  0.0068  501  HIS B CD2 
12517 C CE1 . HIS B 503  ? 0.8758 1.0909 0.8933 0.0068  0.0546  0.0096  501  HIS B CE1 
12518 N NE2 . HIS B 503  ? 0.9020 1.1124 0.9146 0.0126  0.0563  0.0067  501  HIS B NE2 
12519 N N   . ARG B 504  ? 0.7623 0.9918 0.7751 -0.0133 0.0565  0.0204  502  ARG B N   
12520 C CA  . ARG B 504  ? 0.7208 0.9669 0.7410 -0.0136 0.0584  0.0229  502  ARG B CA  
12521 C C   . ARG B 504  ? 0.7301 0.9869 0.7495 -0.0137 0.0619  0.0251  502  ARG B C   
12522 O O   . ARG B 504  ? 0.7286 0.9940 0.7523 -0.0096 0.0633  0.0251  502  ARG B O   
12523 C CB  . ARG B 504  ? 0.6873 0.9347 0.7119 -0.0211 0.0552  0.0259  502  ARG B CB  
12524 C CG  . ARG B 504  ? 0.7143 0.9585 0.7436 -0.0191 0.0526  0.0241  502  ARG B CG  
12525 C CD  . ARG B 504  ? 0.6289 0.8692 0.6600 -0.0268 0.0486  0.0263  502  ARG B CD  
12526 N NE  . ARG B 504  ? 0.6240 0.8781 0.6599 -0.0326 0.0492  0.0306  502  ARG B NE  
12527 C CZ  . ARG B 504  ? 0.6607 0.9267 0.7038 -0.0318 0.0495  0.0319  502  ARG B CZ  
12528 N NH1 . ARG B 504  ? 0.7143 0.9810 0.7607 -0.0253 0.0496  0.0293  502  ARG B NH1 
12529 N NH2 . ARG B 504  ? 0.6218 0.8954 0.6678 -0.0373 0.0485  0.0355  502  ARG B NH2 
12530 N N   . ILE B 505  ? 0.6956 0.9494 0.7091 -0.0180 0.0625  0.0267  503  ILE B N   
12531 C CA  . ILE B 505  ? 0.7179 0.9789 0.7300 -0.0182 0.0650  0.0286  503  ILE B CA  
12532 C C   . ILE B 505  ? 0.7125 0.9737 0.7217 -0.0095 0.0680  0.0253  503  ILE B C   
12533 O O   . ILE B 505  ? 0.6756 0.9443 0.6849 -0.0079 0.0704  0.0264  503  ILE B O   
12534 C CB  . ILE B 505  ? 0.6562 0.9127 0.6620 -0.0251 0.0647  0.0311  503  ILE B CB  
12535 N N   . ASN B 506  ? 0.7038 0.9565 0.7102 -0.0037 0.0679  0.0213  504  ASN B N   
12536 C CA  . ASN B 506  ? 0.7468 0.9976 0.7495 0.0045  0.0703  0.0178  504  ASN B CA  
12537 C C   . ASN B 506  ? 0.7566 1.0084 0.7640 0.0115  0.0702  0.0150  504  ASN B C   
12538 O O   . ASN B 506  ? 0.7689 1.0166 0.7727 0.0187  0.0717  0.0116  504  ASN B O   
12539 C CB  . ASN B 506  ? 0.8033 1.0421 0.7972 0.0057  0.0703  0.0151  504  ASN B CB  
12540 C CG  . ASN B 506  ? 0.8178 1.0549 0.8062 -0.0009 0.0704  0.0179  504  ASN B CG  
12541 O OD1 . ASN B 506  ? 0.8383 1.0641 0.8235 -0.0052 0.0671  0.0180  504  ASN B OD1 
12542 N ND2 . ASN B 506  ? 0.7574 1.0013 0.7446 -0.0015 0.0726  0.0198  504  ASN B ND2 
12543 N N   . ASP B 507  ? 0.7235 0.9800 0.7381 0.0097  0.0684  0.0164  505  ASP B N   
12544 C CA  . ASP B 507  ? 0.7546 1.0130 0.7739 0.0161  0.0682  0.0143  505  ASP B CA  
12545 C C   . ASP B 507  ? 0.7683 1.0395 0.7934 0.0166  0.0694  0.0168  505  ASP B C   
12546 O O   . ASP B 507  ? 0.7489 1.0273 0.7787 0.0104  0.0682  0.0204  505  ASP B O   
12547 C CB  . ASP B 507  ? 0.7598 1.0146 0.7832 0.0142  0.0652  0.0140  505  ASP B CB  
12548 C CG  . ASP B 507  ? 0.8072 1.0646 0.8358 0.0202  0.0647  0.0125  505  ASP B CG  
12549 O OD1 . ASP B 507  ? 0.7878 1.0382 0.8137 0.0268  0.0650  0.0088  505  ASP B OD1 
12550 O OD2 . ASP B 507  ? 0.8160 1.0823 0.8511 0.0180  0.0638  0.0150  505  ASP B OD2 
12551 N N   . PRO B 508  ? 0.7897 1.0639 0.8143 0.0237  0.0716  0.0150  506  PRO B N   
12552 C CA  . PRO B 508  ? 0.7666 1.0537 0.7961 0.0242  0.0731  0.0175  506  PRO B CA  
12553 C C   . PRO B 508  ? 0.7854 1.0795 0.8231 0.0239  0.0712  0.0190  506  PRO B C   
12554 O O   . PRO B 508  ? 0.7779 1.0831 0.8200 0.0246  0.0723  0.0210  506  PRO B O   
12555 C CB  . PRO B 508  ? 0.8311 1.1174 0.8570 0.0326  0.0759  0.0146  506  PRO B CB  
12556 C CG  . PRO B 508  ? 0.8234 1.0964 0.8413 0.0348  0.0760  0.0111  506  PRO B CG  
12557 C CD  . PRO B 508  ? 0.7772 1.0429 0.7961 0.0312  0.0729  0.0108  506  PRO B CD  
12558 N N   . LYS B 509  ? 0.7815 1.0697 0.8212 0.0230  0.0685  0.0180  507  LYS B N   
12559 C CA  . LYS B 509  ? 0.7692 1.0635 0.8161 0.0222  0.0664  0.0195  507  LYS B CA  
12560 C C   . LYS B 509  ? 0.7888 1.0873 0.8392 0.0130  0.0642  0.0233  507  LYS B C   
12561 O O   . LYS B 509  ? 0.8007 1.1053 0.8572 0.0113  0.0623  0.0250  507  LYS B O   
12562 C CB  . LYS B 509  ? 0.7488 1.0346 0.7962 0.0265  0.0645  0.0165  507  LYS B CB  
12563 N N   . VAL B 510  ? 0.7584 1.0537 0.8048 0.0069  0.0642  0.0246  508  VAL B N   
12564 C CA  . VAL B 510  ? 0.7575 1.0556 0.8061 -0.0022 0.0620  0.0283  508  VAL B CA  
12565 C C   . VAL B 510  ? 0.7236 1.0312 0.7726 -0.0057 0.0637  0.0316  508  VAL B C   
12566 O O   . VAL B 510  ? 0.7482 1.0553 0.7925 -0.0038 0.0664  0.0310  508  VAL B O   
12567 C CB  . VAL B 510  ? 0.7459 1.0330 0.7896 -0.0070 0.0605  0.0277  508  VAL B CB  
12568 C CG1 . VAL B 510  ? 0.7026 0.9912 0.7489 -0.0162 0.0576  0.0312  508  VAL B CG1 
12569 C CG2 . VAL B 510  ? 0.7182 0.9955 0.7605 -0.0022 0.0596  0.0239  508  VAL B CG2 
12570 N N   . SER B 511  ? 0.6990 1.0152 0.7533 -0.0110 0.0621  0.0350  509  SER B N   
12571 C CA  . SER B 511  ? 0.7054 1.0318 0.7608 -0.0146 0.0635  0.0385  509  SER B CA  
12572 C C   . SER B 511  ? 0.6969 1.0199 0.7492 -0.0239 0.0620  0.0413  509  SER B C   
12573 O O   . SER B 511  ? 0.7001 1.0145 0.7509 -0.0282 0.0594  0.0411  509  SER B O   
12574 C CB  . SER B 511  ? 0.7158 1.0542 0.7787 -0.0152 0.0625  0.0408  509  SER B CB  
12575 O OG  . SER B 511  ? 0.7120 1.0501 0.7776 -0.0228 0.0589  0.0433  509  SER B OG  
12576 N N   . ILE B 512  ? 0.6710 1.0009 0.7224 -0.0269 0.0637  0.0441  510  ILE B N   
12577 C CA  . ILE B 512  ? 0.6697 0.9973 0.7184 -0.0362 0.0621  0.0474  510  ILE B CA  
12578 C C   . ILE B 512  ? 0.6704 0.9993 0.7236 -0.0427 0.0581  0.0497  510  ILE B C   
12579 O O   . ILE B 512  ? 0.6652 0.9862 0.7157 -0.0495 0.0555  0.0509  510  ILE B O   
12580 C CB  . ILE B 512  ? 0.6887 1.0252 0.7365 -0.0381 0.0646  0.0502  510  ILE B CB  
12581 C CG1 . ILE B 512  ? 0.6876 1.0178 0.7279 -0.0356 0.0674  0.0486  510  ILE B CG1 
12582 C CG2 . ILE B 512  ? 0.6642 1.0036 0.7129 -0.0481 0.0621  0.0547  510  ILE B CG2 
12583 C CD1 . ILE B 512  ? 0.6925 1.0217 0.7314 -0.0255 0.0703  0.0444  510  ILE B CD1 
12584 N N   . ASP B 513  ? 0.6714 1.0096 0.7313 -0.0407 0.0575  0.0503  511  ASP B N   
12585 C CA  . ASP B 513  ? 0.6402 0.9799 0.7043 -0.0466 0.0537  0.0524  511  ASP B CA  
12586 C C   . ASP B 513  ? 0.6246 0.9524 0.6872 -0.0474 0.0510  0.0502  511  ASP B C   
12587 O O   . ASP B 513  ? 0.5965 0.9194 0.6582 -0.0548 0.0477  0.0519  511  ASP B O   
12588 C CB  . ASP B 513  ? 0.6528 1.0043 0.7241 -0.0430 0.0538  0.0531  511  ASP B CB  
12589 C CG  . ASP B 513  ? 0.6621 1.0265 0.7360 -0.0454 0.0552  0.0566  511  ASP B CG  
12590 O OD1 . ASP B 513  ? 0.6432 1.0076 0.7144 -0.0523 0.0548  0.0594  511  ASP B OD1 
12591 O OD2 . ASP B 513  ? 0.7112 1.0859 0.7897 -0.0403 0.0567  0.0566  511  ASP B OD2 
12592 N N   . GLU B 514  ? 0.6015 0.9243 0.6634 -0.0399 0.0522  0.0463  512  GLU B N   
12593 C CA  . GLU B 514  ? 0.6353 0.9471 0.6957 -0.0402 0.0498  0.0440  512  GLU B CA  
12594 C C   . GLU B 514  ? 0.6336 0.9348 0.6876 -0.0457 0.0491  0.0444  512  GLU B C   
12595 O O   . GLU B 514  ? 0.5870 0.8816 0.6403 -0.0514 0.0459  0.0450  512  GLU B O   
12596 C CB  . GLU B 514  ? 0.6489 0.9572 0.7092 -0.0308 0.0516  0.0398  512  GLU B CB  
12597 C CG  . GLU B 514  ? 0.7316 1.0492 0.7974 -0.0245 0.0526  0.0393  512  GLU B CG  
12598 C CD  . GLU B 514  ? 0.7428 1.0549 0.8080 -0.0158 0.0535  0.0351  512  GLU B CD  
12599 O OE1 . GLU B 514  ? 0.7771 1.0786 0.8391 -0.0158 0.0525  0.0329  512  GLU B OE1 
12600 O OE2 . GLU B 514  ? 0.7468 1.0649 0.8146 -0.0091 0.0553  0.0341  512  GLU B OE2 
12601 N N   . LEU B 515  ? 0.6230 0.9224 0.6721 -0.0441 0.0519  0.0439  513  LEU B N   
12602 C CA  . LEU B 515  ? 0.5731 0.8621 0.6154 -0.0487 0.0513  0.0441  513  LEU B CA  
12603 C C   . LEU B 515  ? 0.5396 0.8282 0.5811 -0.0585 0.0486  0.0481  513  LEU B C   
12604 O O   . LEU B 515  ? 0.5248 0.8033 0.5618 -0.0636 0.0467  0.0485  513  LEU B O   
12605 C CB  . LEU B 515  ? 0.5851 0.8730 0.6221 -0.0447 0.0548  0.0430  513  LEU B CB  
12606 C CG  . LEU B 515  ? 0.5902 0.8749 0.6258 -0.0352 0.0571  0.0386  513  LEU B CG  
12607 C CD1 . LEU B 515  ? 0.6261 0.9144 0.6584 -0.0306 0.0609  0.0380  513  LEU B CD1 
12608 C CD2 . LEU B 515  ? 0.5976 0.8694 0.6284 -0.0353 0.0560  0.0361  513  LEU B CD2 
12609 N N   . ILE B 516  ? 0.5237 0.8229 0.5694 -0.0614 0.0484  0.0512  514  ILE B N   
12610 C CA  . ILE B 516  ? 0.5168 0.8156 0.5613 -0.0708 0.0458  0.0551  514  ILE B CA  
12611 C C   . ILE B 516  ? 0.4792 0.7777 0.5277 -0.0754 0.0418  0.0562  514  ILE B C   
12612 O O   . ILE B 516  ? 0.4776 0.7760 0.5256 -0.0832 0.0391  0.0594  514  ILE B O   
12613 C CB  . ILE B 516  ? 0.5418 0.8520 0.5876 -0.0723 0.0478  0.0582  514  ILE B CB  
12614 C CG1 . ILE B 516  ? 0.5454 0.8687 0.5989 -0.0691 0.0482  0.0588  514  ILE B CG1 
12615 C CG2 . ILE B 516  ? 0.5165 0.8267 0.5579 -0.0679 0.0517  0.0571  514  ILE B CG2 
12616 C CD1 . ILE B 516  ? 0.5633 0.8988 0.6187 -0.0708 0.0500  0.0620  514  ILE B CD1 
12617 N N   . ALA B 517  ? 0.4905 0.7885 0.5426 -0.0705 0.0412  0.0535  515  ALA B N   
12618 C CA  . ALA B 517  ? 0.4764 0.7734 0.5319 -0.0743 0.0374  0.0541  515  ALA B CA  
12619 C C   . ALA B 517  ? 0.4678 0.7527 0.5183 -0.0821 0.0340  0.0550  515  ALA B C   
12620 O O   . ALA B 517  ? 0.4465 0.7212 0.4918 -0.0818 0.0345  0.0535  515  ALA B O   
12621 C CB  . ALA B 517  ? 0.4518 0.7480 0.5107 -0.0675 0.0374  0.0507  515  ALA B CB  
12622 N N   . ASP B 518  ? 0.4319 0.7175 0.4837 -0.0892 0.0305  0.0577  516  ASP B N   
12623 C CA  . ASP B 518  ? 0.3984 0.6718 0.4451 -0.0968 0.0269  0.0587  516  ASP B CA  
12624 C C   . ASP B 518  ? 0.3853 0.6500 0.4322 -0.0952 0.0249  0.0557  516  ASP B C   
12625 O O   . ASP B 518  ? 0.3901 0.6586 0.4416 -0.0943 0.0231  0.0553  516  ASP B O   
12626 C CB  . ASP B 518  ? 0.3733 0.6497 0.4207 -0.1048 0.0236  0.0624  516  ASP B CB  
12627 C CG  . ASP B 518  ? 0.4381 0.7012 0.4792 -0.1129 0.0200  0.0637  516  ASP B CG  
12628 O OD1 . ASP B 518  ? 0.4084 0.6596 0.4452 -0.1123 0.0195  0.0616  516  ASP B OD1 
12629 O OD2 . ASP B 518  ? 0.4281 0.6922 0.4683 -0.1198 0.0174  0.0669  516  ASP B OD2 
12630 N N   . PRO B 519  ? 0.3863 0.6395 0.4282 -0.0947 0.0251  0.0538  517  PRO B N   
12631 C CA  . PRO B 519  ? 0.3556 0.6005 0.3977 -0.0934 0.0231  0.0510  517  PRO B CA  
12632 C C   . PRO B 519  ? 0.3662 0.6064 0.4083 -0.1002 0.0184  0.0523  517  PRO B C   
12633 O O   . PRO B 519  ? 0.3512 0.5900 0.3961 -0.0985 0.0166  0.0504  517  PRO B O   
12634 C CB  . PRO B 519  ? 0.3405 0.5695 0.3748 -0.0916 0.0230  0.0486  517  PRO B CB  
12635 C CG  . PRO B 519  ? 0.3758 0.6060 0.4062 -0.0973 0.0239  0.0520  517  PRO B CG  
12636 C CD  . PRO B 519  ? 0.4079 0.6544 0.4433 -0.0962 0.0266  0.0543  517  PRO B CD  
12637 N N   . VAL B 520  ? 0.3337 0.5707 0.3722 -0.1077 0.0161  0.0553  518  VAL B N   
12638 C CA  . VAL B 520  ? 0.3825 0.6133 0.4197 -0.1145 0.0113  0.0565  518  VAL B CA  
12639 C C   . VAL B 520  ? 0.3711 0.6124 0.4147 -0.1135 0.0102  0.0570  518  VAL B C   
12640 O O   . VAL B 520  ? 0.3340 0.5713 0.3787 -0.1145 0.0073  0.0558  518  VAL B O   
12641 C CB  . VAL B 520  ? 0.3792 0.6052 0.4111 -0.1224 0.0094  0.0599  518  VAL B CB  
12642 C CG1 . VAL B 520  ? 0.4136 0.6304 0.4427 -0.1293 0.0041  0.0607  518  VAL B CG1 
12643 C CG2 . VAL B 520  ? 0.3708 0.5876 0.3964 -0.1226 0.0109  0.0596  518  VAL B CG2 
12644 N N   . GLU B 521  ? 0.3663 0.6213 0.4143 -0.1115 0.0126  0.0589  519  GLU B N   
12645 C CA  . GLU B 521  ? 0.3501 0.6154 0.4040 -0.1108 0.0115  0.0597  519  GLU B CA  
12646 C C   . GLU B 521  ? 0.3479 0.6167 0.4065 -0.1030 0.0128  0.0565  519  GLU B C   
12647 O O   . GLU B 521  ? 0.3630 0.6350 0.4252 -0.1031 0.0106  0.0565  519  GLU B O   
12648 C CB  . GLU B 521  ? 0.3730 0.6520 0.4301 -0.1109 0.0136  0.0627  519  GLU B CB  
12649 C CG  . GLU B 521  ? 0.3782 0.6548 0.4311 -0.1190 0.0119  0.0662  519  GLU B CG  
12650 C CD  . GLU B 521  ? 0.4584 0.7274 0.5088 -0.1266 0.0068  0.0675  519  GLU B CD  
12651 O OE1 . GLU B 521  ? 0.4779 0.7500 0.5320 -0.1261 0.0048  0.0670  519  GLU B OE1 
12652 O OE2 . GLU B 521  ? 0.5060 0.7653 0.5503 -0.1331 0.0046  0.0690  519  GLU B OE2 
12653 N N   . VAL B 522  ? 0.3607 0.6286 0.4191 -0.0963 0.0163  0.0540  520  VAL B N   
12654 C CA  . VAL B 522  ? 0.3248 0.5941 0.3870 -0.0891 0.0173  0.0508  520  VAL B CA  
12655 C C   . VAL B 522  ? 0.3776 0.6360 0.4379 -0.0916 0.0137  0.0490  520  VAL B C   
12656 O O   . VAL B 522  ? 0.3755 0.6363 0.4395 -0.0896 0.0121  0.0480  520  VAL B O   
12657 C CB  . VAL B 522  ? 0.3537 0.6230 0.4152 -0.0816 0.0215  0.0483  520  VAL B CB  
12658 C CG1 . VAL B 522  ? 0.3642 0.6334 0.4289 -0.0742 0.0222  0.0450  520  VAL B CG1 
12659 C CG2 . VAL B 522  ? 0.4060 0.6863 0.4693 -0.0786 0.0250  0.0499  520  VAL B CG2 
12660 N N   . VAL B 523  ? 0.3315 0.5776 0.3860 -0.0960 0.0123  0.0487  521  VAL B N   
12661 C CA  . VAL B 523  ? 0.3337 0.5659 0.3846 -0.0976 0.0085  0.0464  521  VAL B CA  
12662 C C   . VAL B 523  ? 0.3454 0.5807 0.3982 -0.1044 0.0046  0.0487  521  VAL B C   
12663 O O   . VAL B 523  ? 0.3509 0.5837 0.4051 -0.1033 0.0023  0.0470  521  VAL B O   
12664 C CB  . VAL B 523  ? 0.3970 0.6119 0.4393 -0.0997 0.0072  0.0453  521  VAL B CB  
12665 C CG1 . VAL B 523  ? 0.3492 0.5492 0.3871 -0.1017 0.0029  0.0432  521  VAL B CG1 
12666 C CG2 . VAL B 523  ? 0.3479 0.5577 0.3878 -0.0920 0.0104  0.0423  521  VAL B CG2 
12667 N N   . ARG B 524  ? 0.3805 0.6182 0.4318 -0.1103 0.0034  0.0520  522  ARG B N   
12668 C CA  . ARG B 524  ? 0.4124 0.6496 0.4635 -0.1162 -0.0008 0.0538  522  ARG B CA  
12669 C C   . ARG B 524  ? 0.3884 0.6364 0.4460 -0.1124 -0.0010 0.0535  522  ARG B C   
12670 O O   . ARG B 524  ? 0.4361 0.6818 0.4936 -0.1158 -0.0046 0.0537  522  ARG B O   
12671 C CB  . ARG B 524  ? 0.4072 0.6473 0.4562 -0.1225 -0.0016 0.0576  522  ARG B CB  
12672 C CG  . ARG B 524  ? 0.4312 0.6691 0.4789 -0.1294 -0.0062 0.0595  522  ARG B CG  
12673 C CD  . ARG B 524  ? 0.4734 0.7206 0.5222 -0.1336 -0.0060 0.0635  522  ARG B CD  
12674 N NE  . ARG B 524  ? 0.4229 0.6684 0.4683 -0.1349 -0.0038 0.0648  522  ARG B NE  
12675 C CZ  . ARG B 524  ? 0.4675 0.7003 0.5058 -0.1404 -0.0058 0.0655  522  ARG B CZ  
12676 N NH1 . ARG B 524  ? 0.4413 0.6613 0.4747 -0.1451 -0.0102 0.0648  522  ARG B NH1 
12677 N NH2 . ARG B 524  ? 0.4665 0.6990 0.5021 -0.1411 -0.0035 0.0668  522  ARG B NH2 
12678 N N   . ALA B 525  ? 0.3872 0.6462 0.4500 -0.1053 0.0029  0.0529  523  ALA B N   
12679 C CA  . ALA B 525  ? 0.4265 0.6966 0.4956 -0.1014 0.0029  0.0531  523  ALA B CA  
12680 C C   . ALA B 525  ? 0.4572 0.7249 0.5284 -0.0954 0.0030  0.0498  523  ALA B C   
12681 O O   . ALA B 525  ? 0.4862 0.7618 0.5622 -0.0920 0.0027  0.0497  523  ALA B O   
12682 C CB  . ALA B 525  ? 0.4089 0.6927 0.4824 -0.0969 0.0069  0.0545  523  ALA B CB  
12683 N N   . MET B 526  ? 0.4440 0.7010 0.5118 -0.0940 0.0033  0.0470  524  MET B N   
12684 C CA  . MET B 526  ? 0.4587 0.7132 0.5284 -0.0884 0.0034  0.0439  524  MET B CA  
12685 C C   . MET B 526  ? 0.4130 0.6644 0.4828 -0.0917 -0.0010 0.0437  524  MET B C   
12686 O O   . MET B 526  ? 0.4212 0.6673 0.4875 -0.0991 -0.0044 0.0453  524  MET B O   
12687 C CB  . MET B 526  ? 0.4323 0.6710 0.4955 -0.0854 0.0040  0.0405  524  MET B CB  
12688 C CG  . MET B 526  ? 0.4905 0.7311 0.5529 -0.0814 0.0082  0.0402  524  MET B CG  
12689 S SD  . MET B 526  ? 0.6217 0.8778 0.6916 -0.0725 0.0124  0.0397  524  MET B SD  
12690 C CE  . MET B 526  ? 0.4881 0.7316 0.5558 -0.0647 0.0117  0.0349  524  MET B CE  
12691 N N   . PRO B 527  ? 0.4795 0.7339 0.5529 -0.0864 -0.0011 0.0419  525  PRO B N   
12692 C CA  . PRO B 527  ? 0.5060 0.7571 0.5790 -0.0894 -0.0053 0.0416  525  PRO B CA  
12693 C C   . PRO B 527  ? 0.4305 0.6634 0.4955 -0.0929 -0.0084 0.0395  525  PRO B C   
12694 O O   . PRO B 527  ? 0.3992 0.6287 0.4622 -0.0992 -0.0123 0.0405  525  PRO B O   
12695 C CB  . PRO B 527  ? 0.4865 0.7423 0.5639 -0.0813 -0.0041 0.0396  525  PRO B CB  
12696 C CG  . PRO B 527  ? 0.5049 0.7575 0.5813 -0.0740 0.0000  0.0374  525  PRO B CG  
12697 C CD  . PRO B 527  ? 0.4957 0.7543 0.5724 -0.0770 0.0024  0.0397  525  PRO B CD  
12698 N N   . VAL B 528  ? 0.4130 0.6332 0.4729 -0.0886 -0.0068 0.0366  526  VAL B N   
12699 C CA  . VAL B 528  ? 0.3789 0.5813 0.4307 -0.0913 -0.0092 0.0346  526  VAL B CA  
12700 C C   . VAL B 528  ? 0.3371 0.5340 0.3852 -0.0921 -0.0072 0.0348  526  VAL B C   
12701 O O   . VAL B 528  ? 0.3918 0.5879 0.4400 -0.0859 -0.0039 0.0331  526  VAL B O   
12702 C CB  . VAL B 528  ? 0.3853 0.5768 0.4344 -0.0853 -0.0096 0.0306  526  VAL B CB  
12703 C CG1 . VAL B 528  ? 0.4293 0.6257 0.4821 -0.0766 -0.0058 0.0290  526  VAL B CG1 
12704 C CG2 . VAL B 528  ? 0.3788 0.5522 0.4197 -0.0865 -0.0110 0.0283  526  VAL B CG2 
12705 N N   . VAL B 529  ? 0.2854 0.4779 0.3296 -0.0997 -0.0094 0.0369  527  VAL B N   
12706 C CA  . VAL B 529  ? 0.2887 0.4764 0.3290 -0.1013 -0.0077 0.0376  527  VAL B CA  
12707 C C   . VAL B 529  ? 0.3338 0.5053 0.3681 -0.0965 -0.0074 0.0338  527  VAL B C   
12708 O O   . VAL B 529  ? 0.3244 0.4832 0.3538 -0.0975 -0.0103 0.0318  527  VAL B O   
12709 C CB  . VAL B 529  ? 0.3264 0.5118 0.3634 -0.1109 -0.0106 0.0407  527  VAL B CB  
12710 C CG1 . VAL B 529  ? 0.3111 0.4886 0.3429 -0.1122 -0.0094 0.0411  527  VAL B CG1 
12711 C CG2 . VAL B 529  ? 0.2982 0.5014 0.3419 -0.1157 -0.0105 0.0449  527  VAL B CG2 
12712 N N   . GLY B 530  ? 0.2935 0.4657 0.3280 -0.0912 -0.0038 0.0328  528  GLY B N   
12713 C CA  . GLY B 530  ? 0.2769 0.4348 0.3059 -0.0871 -0.0034 0.0296  528  GLY B CA  
12714 C C   . GLY B 530  ? 0.2683 0.4216 0.2981 -0.0800 -0.0030 0.0260  528  GLY B C   
12715 O O   . GLY B 530  ? 0.2521 0.3921 0.2770 -0.0778 -0.0037 0.0234  528  GLY B O   
12716 N N   . ALA B 531  ? 0.2331 0.3970 0.2688 -0.0763 -0.0018 0.0259  529  ALA B N   
12717 C CA  . ALA B 531  ? 0.2473 0.4068 0.2836 -0.0696 -0.0013 0.0227  529  ALA B CA  
12718 C C   . ALA B 531  ? 0.2529 0.4071 0.2874 -0.0636 0.0015  0.0204  529  ALA B C   
12719 O O   . ALA B 531  ? 0.2771 0.4373 0.3128 -0.0626 0.0042  0.0215  529  ALA B O   
12720 C CB  . ALA B 531  ? 0.2988 0.4713 0.3418 -0.0665 -0.0004 0.0232  529  ALA B CB  
12721 N N   . LYS B 532  ? 0.2277 0.3709 0.2592 -0.0598 0.0009  0.0173  530  LYS B N   
12722 C CA  . LYS B 532  ? 0.2482 0.3864 0.2785 -0.0538 0.0033  0.0150  530  LYS B CA  
12723 C C   . LYS B 532  ? 0.2501 0.3995 0.2855 -0.0486 0.0064  0.0151  530  LYS B C   
12724 O O   . LYS B 532  ? 0.2158 0.3750 0.2560 -0.0477 0.0064  0.0160  530  LYS B O   
12725 C CB  . LYS B 532  ? 0.2416 0.3687 0.2693 -0.0506 0.0020  0.0119  530  LYS B CB  
12726 C CG  . LYS B 532  ? 0.2872 0.4091 0.3140 -0.0443 0.0041  0.0094  530  LYS B CG  
12727 C CD  . LYS B 532  ? 0.2386 0.3512 0.2636 -0.0414 0.0028  0.0067  530  LYS B CD  
12728 C CE  . LYS B 532  ? 0.2371 0.3557 0.2660 -0.0394 0.0025  0.0066  530  LYS B CE  
12729 N NZ  . LYS B 532  ? 0.2613 0.3885 0.2946 -0.0342 0.0051  0.0065  530  LYS B NZ  
12730 N N   . HIS B 533  ? 0.2338 0.3818 0.2681 -0.0449 0.0089  0.0141  531  HIS B N   
12731 C CA  . HIS B 533  ? 0.2290 0.3852 0.2670 -0.0390 0.0118  0.0135  531  HIS B CA  
12732 C C   . HIS B 533  ? 0.2217 0.3775 0.2622 -0.0343 0.0114  0.0117  531  HIS B C   
12733 O O   . HIS B 533  ? 0.2272 0.3727 0.2650 -0.0332 0.0099  0.0096  531  HIS B O   
12734 C CB  . HIS B 533  ? 0.2427 0.3934 0.2775 -0.0355 0.0139  0.0120  531  HIS B CB  
12735 C CG  . HIS B 533  ? 0.2637 0.4235 0.3015 -0.0303 0.0172  0.0119  531  HIS B CG  
12736 N ND1 . HIS B 533  ? 0.2634 0.4260 0.3042 -0.0245 0.0182  0.0103  531  HIS B ND1 
12737 C CD2 . HIS B 533  ? 0.3270 0.4932 0.3648 -0.0300 0.0197  0.0130  531  HIS B CD2 
12738 C CE1 . HIS B 533  ? 0.3181 0.4884 0.3606 -0.0206 0.0211  0.0104  531  HIS B CE1 
12739 N NE2 . HIS B 533  ? 0.3450 0.5178 0.3857 -0.0238 0.0222  0.0120  531  HIS B NE2 
12740 N N   . ASP B 534  ? 0.2540 0.4214 0.2996 -0.0317 0.0127  0.0127  532  ASP B N   
12741 C CA  . ASP B 534  ? 0.2737 0.4416 0.3218 -0.0276 0.0121  0.0114  532  ASP B CA  
12742 C C   . ASP B 534  ? 0.2167 0.3765 0.2629 -0.0214 0.0133  0.0084  532  ASP B C   
12743 O O   . ASP B 534  ? 0.3005 0.4565 0.3470 -0.0188 0.0122  0.0070  532  ASP B O   
12744 C CB  . ASP B 534  ? 0.3062 0.4886 0.3604 -0.0257 0.0132  0.0132  532  ASP B CB  
12745 C CG  . ASP B 534  ? 0.4068 0.5976 0.4636 -0.0319 0.0114  0.0161  532  ASP B CG  
12746 O OD1 . ASP B 534  ? 0.4343 0.6184 0.4886 -0.0365 0.0085  0.0162  532  ASP B OD1 
12747 O OD2 . ASP B 534  ? 0.4889 0.6929 0.5503 -0.0321 0.0128  0.0184  532  ASP B OD2 
12748 N N   . ARG B 535  ? 0.2416 0.3986 0.2855 -0.0192 0.0153  0.0075  533  ARG B N   
12749 C CA  . ARG B 535  ? 0.2145 0.3649 0.2568 -0.0134 0.0165  0.0048  533  ARG B CA  
12750 C C   . ARG B 535  ? 0.2374 0.3750 0.2746 -0.0144 0.0156  0.0031  533  ARG B C   
12751 O O   . ARG B 535  ? 0.2742 0.4063 0.3095 -0.0103 0.0168  0.0011  533  ARG B O   
12752 C CB  . ARG B 535  ? 0.2700 0.4273 0.3136 -0.0090 0.0196  0.0048  533  ARG B CB  
12753 C CG  . ARG B 535  ? 0.3289 0.4988 0.3778 -0.0062 0.0207  0.0060  533  ARG B CG  
12754 C CD  . ARG B 535  ? 0.3945 0.5706 0.4441 -0.0016 0.0239  0.0058  533  ARG B CD  
12755 N N   . ILE B 536  ? 0.2167 0.3491 0.2515 -0.0197 0.0136  0.0038  534  ILE B N   
12756 C CA  . ILE B 536  ? 0.2009 0.3213 0.2309 -0.0207 0.0125  0.0023  534  ILE B CA  
12757 C C   . ILE B 536  ? 0.1848 0.2989 0.2138 -0.0229 0.0099  0.0018  534  ILE B C   
12758 O O   . ILE B 536  ? 0.2461 0.3628 0.2755 -0.0274 0.0083  0.0034  534  ILE B O   
12759 C CB  . ILE B 536  ? 0.1999 0.3189 0.2270 -0.0249 0.0125  0.0036  534  ILE B CB  
12760 C CG1 . ILE B 536  ? 0.2389 0.3644 0.2665 -0.0226 0.0153  0.0042  534  ILE B CG1 
12761 C CG2 . ILE B 536  ? 0.2357 0.3419 0.2580 -0.0256 0.0111  0.0021  534  ILE B CG2 
12762 C CD1 . ILE B 536  ? 0.2935 0.4181 0.3181 -0.0267 0.0155  0.0057  534  ILE B CD1 
12763 N N   . ALA B 537  ? 0.1832 0.2894 0.2108 -0.0197 0.0095  -0.0005 535  ALA B N   
12764 C CA  . ALA B 537  ? 0.2057 0.3063 0.2323 -0.0209 0.0074  -0.0012 535  ALA B CA  
12765 C C   . ALA B 537  ? 0.2038 0.2955 0.2261 -0.0248 0.0057  -0.0014 535  ALA B C   
12766 O O   . ALA B 537  ? 0.1939 0.2798 0.2136 -0.0241 0.0062  -0.0023 535  ALA B O   
12767 C CB  . ALA B 537  ? 0.2074 0.3032 0.2342 -0.0161 0.0078  -0.0033 535  ALA B CB  
12768 N N   . LEU B 538  ? 0.1959 0.2863 0.2171 -0.0287 0.0036  -0.0007 536  LEU B N   
12769 C CA  . LEU B 538  ? 0.2150 0.2950 0.2316 -0.0312 0.0018  -0.0016 536  LEU B CA  
12770 C C   . LEU B 538  ? 0.2156 0.2879 0.2310 -0.0270 0.0021  -0.0040 536  LEU B C   
12771 O O   . LEU B 538  ? 0.2027 0.2771 0.2205 -0.0233 0.0030  -0.0049 536  LEU B O   
12772 C CB  . LEU B 538  ? 0.2019 0.2807 0.2172 -0.0352 -0.0007 -0.0010 536  LEU B CB  
12773 C CG  . LEU B 538  ? 0.2476 0.3318 0.2631 -0.0407 -0.0018 0.0016  536  LEU B CG  
12774 C CD1 . LEU B 538  ? 0.2952 0.3776 0.3093 -0.0441 -0.0044 0.0018  536  LEU B CD1 
12775 C CD2 . LEU B 538  ? 0.2450 0.3238 0.2567 -0.0437 -0.0021 0.0022  536  LEU B CD2 
12776 N N   . PRO B 539  ? 0.1869 0.2503 0.1986 -0.0274 0.0015  -0.0050 537  PRO B N   
12777 C CA  . PRO B 539  ? 0.2026 0.2592 0.2134 -0.0236 0.0018  -0.0072 537  PRO B CA  
12778 C C   . PRO B 539  ? 0.1872 0.2431 0.1988 -0.0224 0.0011  -0.0081 537  PRO B C   
12779 O O   . PRO B 539  ? 0.1932 0.2489 0.2064 -0.0185 0.0022  -0.0093 537  PRO B O   
12780 C CB  . PRO B 539  ? 0.1908 0.2384 0.1973 -0.0254 0.0005  -0.0077 537  PRO B CB  
12781 C CG  . PRO B 539  ? 0.1776 0.2282 0.1832 -0.0288 0.0005  -0.0057 537  PRO B CG  
12782 C CD  . PRO B 539  ? 0.2063 0.2657 0.2145 -0.0312 0.0005  -0.0040 537  PRO B CD  
12783 N N   . ALA B 540  ? 0.2099 0.2653 0.2201 -0.0257 -0.0006 -0.0075 538  ALA B N   
12784 C CA  . ALA B 540  ? 0.2200 0.2746 0.2304 -0.0245 -0.0013 -0.0084 538  ALA B CA  
12785 C C   . ALA B 540  ? 0.2307 0.2933 0.2453 -0.0219 -0.0001 -0.0080 538  ALA B C   
12786 O O   . ALA B 540  ? 0.2116 0.2732 0.2268 -0.0197 -0.0001 -0.0089 538  ALA B O   
12787 C CB  . ALA B 540  ? 0.2344 0.2872 0.2421 -0.0289 -0.0036 -0.0079 538  ALA B CB  
12788 N N   . GLU B 541  ? 0.2204 0.2910 0.2381 -0.0219 0.0010  -0.0065 539  GLU B N   
12789 C CA  . GLU B 541  ? 0.2009 0.2798 0.2226 -0.0197 0.0018  -0.0058 539  GLU B CA  
12790 C C   . GLU B 541  ? 0.2175 0.2982 0.2414 -0.0150 0.0040  -0.0064 539  GLU B C   
12791 O O   . GLU B 541  ? 0.1932 0.2813 0.2204 -0.0129 0.0050  -0.0057 539  GLU B O   
12792 C CB  . GLU B 541  ? 0.2355 0.3230 0.2592 -0.0231 0.0012  -0.0036 539  GLU B CB  
12793 C CG  . GLU B 541  ? 0.2837 0.3684 0.3047 -0.0280 -0.0014 -0.0031 539  GLU B CG  
12794 C CD  . GLU B 541  ? 0.3259 0.4189 0.3488 -0.0323 -0.0025 -0.0007 539  GLU B CD  
12795 O OE1 . GLU B 541  ? 0.3460 0.4474 0.3722 -0.0322 -0.0011 0.0008  539  GLU B OE1 
12796 O OE2 . GLU B 541  ? 0.3748 0.4659 0.3956 -0.0361 -0.0048 -0.0003 539  GLU B OE2 
12797 N N   . LEU B 542  ? 0.1977 0.2716 0.2197 -0.0133 0.0046  -0.0079 540  LEU B N   
12798 C CA  . LEU B 542  ? 0.1990 0.2736 0.2224 -0.0092 0.0064  -0.0086 540  LEU B CA  
12799 C C   . LEU B 542  ? 0.2198 0.2971 0.2456 -0.0055 0.0070  -0.0089 540  LEU B C   
12800 O O   . LEU B 542  ? 0.2267 0.3075 0.2543 -0.0024 0.0084  -0.0090 540  LEU B O   
12801 C CB  . LEU B 542  ? 0.2187 0.2850 0.2396 -0.0080 0.0066  -0.0101 540  LEU B CB  
12802 C CG  . LEU B 542  ? 0.2595 0.3226 0.2780 -0.0100 0.0065  -0.0100 540  LEU B CG  
12803 C CD1 . LEU B 542  ? 0.2091 0.2652 0.2262 -0.0076 0.0068  -0.0116 540  LEU B CD1 
12804 C CD2 . LEU B 542  ? 0.2363 0.3061 0.2559 -0.0105 0.0077  -0.0087 540  LEU B CD2 
12805 N N   . PHE B 543  ? 0.1755 0.2507 0.2010 -0.0058 0.0059  -0.0092 541  PHE B N   
12806 C CA  . PHE B 543  ? 0.1928 0.2693 0.2200 -0.0024 0.0063  -0.0095 541  PHE B CA  
12807 C C   . PHE B 543  ? 0.1830 0.2668 0.2124 -0.0031 0.0056  -0.0080 541  PHE B C   
12808 O O   . PHE B 543  ? 0.2083 0.2932 0.2389 -0.0007 0.0055  -0.0080 541  PHE B O   
12809 C CB  . PHE B 543  ? 0.1809 0.2499 0.2061 -0.0017 0.0058  -0.0108 541  PHE B CB  
12810 C CG  . PHE B 543  ? 0.2119 0.2743 0.2352 -0.0013 0.0062  -0.0120 541  PHE B CG  
12811 C CD1 . PHE B 543  ? 0.2136 0.2759 0.2377 0.0012  0.0075  -0.0125 541  PHE B CD1 
12812 C CD2 . PHE B 543  ? 0.2041 0.2606 0.2248 -0.0034 0.0053  -0.0128 541  PHE B CD2 
12813 C CE1 . PHE B 543  ? 0.2200 0.2766 0.2425 0.0014  0.0077  -0.0136 541  PHE B CE1 
12814 C CE2 . PHE B 543  ? 0.2193 0.2702 0.2386 -0.0028 0.0056  -0.0138 541  PHE B CE2 
12815 C CZ  . PHE B 543  ? 0.2413 0.2925 0.2616 -0.0006 0.0067  -0.0141 541  PHE B CZ  
12816 N N   . GLY B 544  ? 0.2063 0.2952 0.2363 -0.0065 0.0050  -0.0067 542  GLY B N   
12817 C CA  . GLY B 544  ? 0.2090 0.3061 0.2417 -0.0072 0.0042  -0.0051 542  GLY B CA  
12818 C C   . GLY B 544  ? 0.2267 0.3216 0.2583 -0.0080 0.0026  -0.0052 542  GLY B C   
12819 O O   . GLY B 544  ? 0.2486 0.3367 0.2769 -0.0102 0.0015  -0.0061 542  GLY B O   
12820 N N   . ASP B 545  ? 0.2575 0.3582 0.2917 -0.0060 0.0024  -0.0043 543  ASP B N   
12821 C CA  . ASP B 545  ? 0.2902 0.3897 0.3233 -0.0068 0.0006  -0.0042 543  ASP B CA  
12822 C C   . ASP B 545  ? 0.2745 0.3657 0.3051 -0.0046 0.0009  -0.0058 543  ASP B C   
12823 O O   . ASP B 545  ? 0.2773 0.3660 0.3059 -0.0057 -0.0004 -0.0059 543  ASP B O   
12824 C CB  . ASP B 545  ? 0.3086 0.4167 0.3453 -0.0050 0.0003  -0.0027 543  ASP B CB  
12825 C CG  . ASP B 545  ? 0.4290 0.5467 0.4687 -0.0075 -0.0002 -0.0008 543  ASP B CG  
12826 O OD1 . ASP B 545  ? 0.4364 0.5534 0.4746 -0.0120 -0.0011 -0.0005 543  ASP B OD1 
12827 O OD2 . ASP B 545  ? 0.5062 0.6322 0.5498 -0.0049 0.0004  0.0004  543  ASP B OD2 
12828 N N   . ALA B 546  ? 0.2180 0.3050 0.2484 -0.0017 0.0026  -0.0069 544  ALA B N   
12829 C CA  . ALA B 546  ? 0.2199 0.3000 0.2484 0.0005  0.0029  -0.0081 544  ALA B CA  
12830 C C   . ALA B 546  ? 0.2178 0.2910 0.2427 -0.0021 0.0021  -0.0092 544  ALA B C   
12831 O O   . ALA B 546  ? 0.2222 0.2921 0.2453 -0.0017 0.0016  -0.0096 544  ALA B O   
12832 C CB  . ALA B 546  ? 0.2175 0.2950 0.2468 0.0037  0.0046  -0.0090 544  ALA B CB  
12833 N N   . ARG B 547  ? 0.2025 0.2732 0.2260 -0.0045 0.0020  -0.0097 545  ARG B N   
12834 C CA  . ARG B 547  ? 0.2070 0.2708 0.2268 -0.0067 0.0012  -0.0108 545  ARG B CA  
12835 C C   . ARG B 547  ? 0.1980 0.2607 0.2166 -0.0096 0.0009  -0.0108 545  ARG B C   
12836 O O   . ARG B 547  ? 0.2104 0.2771 0.2310 -0.0096 0.0016  -0.0100 545  ARG B O   
12837 C CB  . ARG B 547  ? 0.2208 0.2781 0.2394 -0.0042 0.0023  -0.0122 545  ARG B CB  
12838 C CG  . ARG B 547  ? 0.1994 0.2554 0.2192 -0.0024 0.0037  -0.0127 545  ARG B CG  
12839 C CD  . ARG B 547  ? 0.1951 0.2458 0.2144 0.0000  0.0045  -0.0139 545  ARG B CD  
12840 N NE  . ARG B 547  ? 0.2017 0.2525 0.2228 0.0023  0.0057  -0.0141 545  ARG B NE  
12841 C CZ  . ARG B 547  ? 0.2074 0.2549 0.2279 0.0022  0.0061  -0.0148 545  ARG B CZ  
12842 N NH1 . ARG B 547  ? 0.1911 0.2346 0.2094 0.0003  0.0055  -0.0154 545  ARG B NH1 
12843 N NH2 . ARG B 547  ? 0.2379 0.2859 0.2598 0.0042  0.0070  -0.0149 545  ARG B NH2 
12844 N N   . THR B 548  ? 0.1930 0.2500 0.2080 -0.0121 -0.0003 -0.0116 546  THR B N   
12845 C CA  . THR B 548  ? 0.1808 0.2351 0.1938 -0.0151 -0.0010 -0.0116 546  THR B CA  
12846 C C   . THR B 548  ? 0.1853 0.2336 0.1972 -0.0133 0.0001  -0.0128 546  THR B C   
12847 O O   . THR B 548  ? 0.1834 0.2267 0.1940 -0.0114 0.0004  -0.0141 546  THR B O   
12848 C CB  . THR B 548  ? 0.2186 0.2691 0.2277 -0.0185 -0.0030 -0.0118 546  THR B CB  
12849 O OG1 . THR B 548  ? 0.2361 0.2926 0.2463 -0.0203 -0.0042 -0.0106 546  THR B OG1 
12850 C CG2 . THR B 548  ? 0.2429 0.2899 0.2496 -0.0217 -0.0039 -0.0117 546  THR B CG2 
12851 N N   . ASN B 549  ? 0.1787 0.2280 0.1914 -0.0138 0.0006  -0.0124 547  ASN B N   
12852 C CA  . ASN B 549  ? 0.1589 0.2028 0.1706 -0.0124 0.0013  -0.0134 547  ASN B CA  
12853 C C   . ASN B 549  ? 0.1700 0.2063 0.1776 -0.0140 0.0001  -0.0144 547  ASN B C   
12854 O O   . ASN B 549  ? 0.1996 0.2347 0.2047 -0.0174 -0.0014 -0.0139 547  ASN B O   
12855 C CB  . ASN B 549  ? 0.1816 0.2285 0.1943 -0.0131 0.0020  -0.0125 547  ASN B CB  
12856 C CG  . ASN B 549  ? 0.1838 0.2264 0.1961 -0.0111 0.0028  -0.0134 547  ASN B CG  
12857 O OD1 . ASN B 549  ? 0.1814 0.2202 0.1937 -0.0086 0.0032  -0.0146 547  ASN B OD1 
12858 N ND2 . ASN B 549  ? 0.1857 0.2294 0.1977 -0.0122 0.0031  -0.0127 547  ASN B ND2 
12859 N N   . SER B 550  ? 0.1735 0.2045 0.1803 -0.0117 0.0007  -0.0157 548  SER B N   
12860 C CA  . SER B 550  ? 0.1959 0.2196 0.1990 -0.0127 -0.0004 -0.0167 548  SER B CA  
12861 C C   . SER B 550  ? 0.2089 0.2309 0.2102 -0.0153 -0.0012 -0.0159 548  SER B C   
12862 O O   . SER B 550  ? 0.1835 0.2092 0.1867 -0.0154 -0.0005 -0.0150 548  SER B O   
12863 C CB  . SER B 550  ? 0.1767 0.1962 0.1800 -0.0095 0.0005  -0.0180 548  SER B CB  
12864 O OG  . SER B 550  ? 0.1856 0.2062 0.1909 -0.0082 0.0014  -0.0178 548  SER B OG  
12865 N N   . ALA B 551  ? 0.1943 0.2105 0.1916 -0.0175 -0.0028 -0.0163 549  ALA B N   
12866 C CA  . ALA B 551  ? 0.2172 0.2306 0.2120 -0.0203 -0.0039 -0.0155 549  ALA B CA  
12867 C C   . ALA B 551  ? 0.2438 0.2497 0.2363 -0.0187 -0.0042 -0.0166 549  ALA B C   
12868 O O   . ALA B 551  ? 0.2320 0.2334 0.2231 -0.0166 -0.0042 -0.0181 549  ALA B O   
12869 C CB  . ALA B 551  ? 0.2370 0.2485 0.2284 -0.0245 -0.0059 -0.0149 549  ALA B CB  
12870 N N   . GLY B 552  ? 0.2447 0.2496 0.2367 -0.0196 -0.0043 -0.0158 550  GLY B N   
12871 C CA  . GLY B 552  ? 0.2455 0.2434 0.2350 -0.0184 -0.0049 -0.0166 550  GLY B CA  
12872 C C   . GLY B 552  ? 0.2009 0.1923 0.1854 -0.0216 -0.0070 -0.0162 550  GLY B C   
12873 O O   . GLY B 552  ? 0.2562 0.2471 0.2385 -0.0246 -0.0082 -0.0158 550  GLY B O   
12874 N N   . LEU B 553  ? 0.2373 0.2230 0.2196 -0.0210 -0.0077 -0.0162 551  LEU B N   
12875 C CA  . LEU B 553  ? 0.2608 0.2393 0.2379 -0.0239 -0.0099 -0.0157 551  LEU B CA  
12876 C C   . LEU B 553  ? 0.2215 0.1995 0.1981 -0.0248 -0.0100 -0.0143 551  LEU B C   
12877 O O   . LEU B 553  ? 0.2542 0.2338 0.2333 -0.0219 -0.0089 -0.0147 551  LEU B O   
12878 C CB  . LEU B 553  ? 0.2679 0.2376 0.2415 -0.0215 -0.0109 -0.0176 551  LEU B CB  
12879 C CG  . LEU B 553  ? 0.2735 0.2421 0.2460 -0.0208 -0.0110 -0.0191 551  LEU B CG  
12880 C CD1 . LEU B 553  ? 0.3035 0.2648 0.2734 -0.0173 -0.0113 -0.0211 551  LEU B CD1 
12881 C CD2 . LEU B 553  ? 0.3016 0.2686 0.2705 -0.0254 -0.0128 -0.0183 551  LEU B CD2 
12882 N N   . ASP B 554  ? 0.2411 0.2168 0.2144 -0.0291 -0.0116 -0.0127 552  ASP B N   
12883 C CA  . ASP B 554  ? 0.2392 0.2150 0.2117 -0.0306 -0.0117 -0.0110 552  ASP B CA  
12884 C C   . ASP B 554  ? 0.2292 0.1950 0.1971 -0.0297 -0.0135 -0.0115 552  ASP B C   
12885 O O   . ASP B 554  ? 0.2570 0.2159 0.2201 -0.0324 -0.0156 -0.0110 552  ASP B O   
12886 C CB  . ASP B 554  ? 0.2539 0.2331 0.2252 -0.0359 -0.0123 -0.0087 552  ASP B CB  
12887 C CG  . ASP B 554  ? 0.2442 0.2244 0.2147 -0.0376 -0.0122 -0.0068 552  ASP B CG  
12888 O OD1 . ASP B 554  ? 0.2660 0.2435 0.2363 -0.0347 -0.0118 -0.0073 552  ASP B OD1 
12889 O OD2 . ASP B 554  ? 0.2855 0.2694 0.2554 -0.0419 -0.0124 -0.0047 552  ASP B OD2 
12890 N N   . LEU B 555  ? 0.2541 0.2191 0.2236 -0.0259 -0.0128 -0.0123 553  LEU B N   
12891 C CA  . LEU B 555  ? 0.2778 0.2339 0.2435 -0.0245 -0.0144 -0.0127 553  LEU B CA  
12892 C C   . LEU B 555  ? 0.2928 0.2460 0.2551 -0.0274 -0.0157 -0.0105 553  LEU B C   
12893 O O   . LEU B 555  ? 0.2625 0.2090 0.2220 -0.0259 -0.0170 -0.0106 553  LEU B O   
12894 C CB  . LEU B 555  ? 0.2596 0.2161 0.2283 -0.0194 -0.0134 -0.0142 553  LEU B CB  
12895 C CG  . LEU B 555  ? 0.2724 0.2313 0.2442 -0.0163 -0.0122 -0.0162 553  LEU B CG  
12896 C CD1 . LEU B 555  ? 0.2736 0.2326 0.2482 -0.0118 -0.0115 -0.0173 553  LEU B CD1 
12897 C CD2 . LEU B 555  ? 0.3112 0.2638 0.2791 -0.0169 -0.0135 -0.0172 553  LEU B CD2 
12898 N N   . SER B 556  ? 0.2508 0.2094 0.2135 -0.0314 -0.0152 -0.0086 554  SER B N   
12899 C CA  . SER B 556  ? 0.2686 0.2241 0.2273 -0.0352 -0.0165 -0.0063 554  SER B CA  
12900 C C   . SER B 556  ? 0.2686 0.2203 0.2232 -0.0402 -0.0184 -0.0050 554  SER B C   
12901 O O   . SER B 556  ? 0.2825 0.2307 0.2332 -0.0439 -0.0198 -0.0029 554  SER B O   
12902 C CB  . SER B 556  ? 0.2691 0.2336 0.2308 -0.0363 -0.0146 -0.0046 554  SER B CB  
12903 O OG  . SER B 556  ? 0.2599 0.2322 0.2240 -0.0391 -0.0135 -0.0038 554  SER B OG  
12904 N N   . ASN B 557  ? 0.2486 0.2005 0.2038 -0.0405 -0.0186 -0.0062 555  ASN B N   
12905 C CA  . ASN B 557  ? 0.2691 0.2176 0.2205 -0.0455 -0.0205 -0.0052 555  ASN B CA  
12906 C C   . ASN B 557  ? 0.2919 0.2277 0.2373 -0.0446 -0.0230 -0.0065 555  ASN B C   
12907 O O   . ASN B 557  ? 0.2817 0.2148 0.2277 -0.0405 -0.0228 -0.0090 555  ASN B O   
12908 C CB  . ASN B 557  ? 0.2553 0.2113 0.2104 -0.0462 -0.0194 -0.0058 555  ASN B CB  
12909 C CG  . ASN B 557  ? 0.3034 0.2568 0.2549 -0.0516 -0.0216 -0.0047 555  ASN B CG  
12910 O OD1 . ASN B 557  ? 0.3066 0.2497 0.2524 -0.0527 -0.0240 -0.0054 555  ASN B OD1 
12911 N ND2 . ASN B 557  ? 0.2711 0.2339 0.2258 -0.0550 -0.0208 -0.0031 555  ASN B ND2 
12912 N N   . GLU B 558  ? 0.2906 0.2187 0.2303 -0.0484 -0.0255 -0.0049 556  GLU B N   
12913 C CA  . GLU B 558  ? 0.3231 0.2383 0.2567 -0.0472 -0.0280 -0.0061 556  GLU B CA  
12914 C C   . GLU B 558  ? 0.3207 0.2321 0.2522 -0.0474 -0.0290 -0.0080 556  GLU B C   
12915 O O   . GLU B 558  ? 0.3234 0.2266 0.2518 -0.0438 -0.0299 -0.0102 556  GLU B O   
12916 C CB  . GLU B 558  ? 0.3155 0.2226 0.2428 -0.0516 -0.0306 -0.0037 556  GLU B CB  
12917 C CG  . GLU B 558  ? 0.3109 0.2187 0.2386 -0.0508 -0.0301 -0.0021 556  GLU B CG  
12918 C CD  . GLU B 558  ? 0.3381 0.2411 0.2659 -0.0445 -0.0300 -0.0040 556  GLU B CD  
12919 O OE1 . GLU B 558  ? 0.3277 0.2253 0.2546 -0.0405 -0.0305 -0.0065 556  GLU B OE1 
12920 O OE2 . GLU B 558  ? 0.3073 0.2125 0.2362 -0.0434 -0.0294 -0.0028 556  GLU B OE2 
12921 N N   . GLU B 559  ? 0.3003 0.2174 0.2329 -0.0518 -0.0290 -0.0071 557  GLU B N   
12922 C CA  . GLU B 559  ? 0.3049 0.2193 0.2358 -0.0519 -0.0299 -0.0090 557  GLU B CA  
12923 C C   . GLU B 559  ? 0.3085 0.2264 0.2435 -0.0457 -0.0276 -0.0118 557  GLU B C   
12924 O O   . GLU B 559  ? 0.3163 0.2272 0.2482 -0.0428 -0.0284 -0.0142 557  GLU B O   
12925 C CB  . GLU B 559  ? 0.3603 0.2825 0.2932 -0.0572 -0.0300 -0.0074 557  GLU B CB  
12926 C CG  . GLU B 559  ? 0.3974 0.3174 0.3265 -0.0643 -0.0322 -0.0045 557  GLU B CG  
12927 C CD  . GLU B 559  ? 0.4697 0.3987 0.4017 -0.0691 -0.0323 -0.0031 557  GLU B CD  
12928 O OE1 . GLU B 559  ? 0.4869 0.4192 0.4210 -0.0674 -0.0317 -0.0049 557  GLU B OE1 
12929 O OE2 . GLU B 559  ? 0.4427 0.3758 0.3749 -0.0746 -0.0328 -0.0001 557  GLU B OE2 
12930 N N   . THR B 560  ? 0.2999 0.2286 0.2418 -0.0435 -0.0248 -0.0115 558  THR B N   
12931 C CA  . THR B 560  ? 0.2734 0.2059 0.2195 -0.0379 -0.0227 -0.0138 558  THR B CA  
12932 C C   . THR B 560  ? 0.2982 0.2229 0.2422 -0.0330 -0.0229 -0.0155 558  THR B C   
12933 O O   . THR B 560  ? 0.2959 0.2179 0.2395 -0.0293 -0.0225 -0.0178 558  THR B O   
12934 C CB  . THR B 560  ? 0.2652 0.2095 0.2184 -0.0367 -0.0199 -0.0129 558  THR B CB  
12935 O OG1 . THR B 560  ? 0.2828 0.2347 0.2380 -0.0410 -0.0197 -0.0113 558  THR B OG1 
12936 C CG2 . THR B 560  ? 0.2801 0.2281 0.2374 -0.0315 -0.0178 -0.0151 558  THR B CG2 
12937 N N   . LEU B 561  ? 0.2820 0.2034 0.2247 -0.0329 -0.0236 -0.0143 559  LEU B N   
12938 C CA  . LEU B 561  ? 0.2851 0.1999 0.2263 -0.0281 -0.0239 -0.0157 559  LEU B CA  
12939 C C   . LEU B 561  ? 0.3011 0.2044 0.2358 -0.0274 -0.0261 -0.0173 559  LEU B C   
12940 O O   . LEU B 561  ? 0.3071 0.2069 0.2415 -0.0224 -0.0257 -0.0194 559  LEU B O   
12941 C CB  . LEU B 561  ? 0.2953 0.2085 0.2359 -0.0285 -0.0245 -0.0138 559  LEU B CB  
12942 C CG  . LEU B 561  ? 0.2521 0.1759 0.1990 -0.0277 -0.0222 -0.0128 559  LEU B CG  
12943 C CD1 . LEU B 561  ? 0.2852 0.2065 0.2302 -0.0288 -0.0231 -0.0109 559  LEU B CD1 
12944 C CD2 . LEU B 561  ? 0.2658 0.1937 0.2176 -0.0221 -0.0202 -0.0149 559  LEU B CD2 
12945 N N   . ALA B 562  ? 0.3019 0.1991 0.2310 -0.0324 -0.0285 -0.0162 560  ALA B N   
12946 C CA  . ALA B 562  ? 0.3272 0.2124 0.2491 -0.0319 -0.0309 -0.0178 560  ALA B CA  
12947 C C   . ALA B 562  ? 0.3586 0.2449 0.2809 -0.0297 -0.0300 -0.0204 560  ALA B C   
12948 O O   . ALA B 562  ? 0.3556 0.2347 0.2746 -0.0255 -0.0304 -0.0227 560  ALA B O   
12949 C CB  . ALA B 562  ? 0.3188 0.1974 0.2346 -0.0384 -0.0339 -0.0159 560  ALA B CB  
12950 N N   . SER B 563  ? 0.3175 0.2126 0.2435 -0.0323 -0.0288 -0.0199 561  SER B N   
12951 C CA  . SER B 563  ? 0.3322 0.2286 0.2583 -0.0304 -0.0280 -0.0222 561  SER B CA  
12952 C C   . SER B 563  ? 0.3324 0.2341 0.2638 -0.0241 -0.0251 -0.0239 561  SER B C   
12953 O O   . SER B 563  ? 0.3498 0.2484 0.2795 -0.0205 -0.0246 -0.0263 561  SER B O   
12954 C CB  . SER B 563  ? 0.3586 0.2630 0.2872 -0.0349 -0.0277 -0.0211 561  SER B CB  
12955 O OG  . SER B 563  ? 0.3681 0.2845 0.3043 -0.0346 -0.0252 -0.0197 561  SER B OG  
12956 N N   . LEU B 564  ? 0.3113 0.2211 0.2489 -0.0228 -0.0232 -0.0227 562  LEU B N   
12957 C CA  . LEU B 564  ? 0.2904 0.2049 0.2330 -0.0172 -0.0207 -0.0241 562  LEU B CA  
12958 C C   . LEU B 564  ? 0.2948 0.2009 0.2343 -0.0126 -0.0214 -0.0257 562  LEU B C   
12959 O O   . LEU B 564  ? 0.3113 0.2176 0.2517 -0.0082 -0.0201 -0.0277 562  LEU B O   
12960 C CB  . LEU B 564  ? 0.2971 0.2208 0.2462 -0.0171 -0.0190 -0.0224 562  LEU B CB  
12961 C CG  . LEU B 564  ? 0.3271 0.2566 0.2819 -0.0121 -0.0166 -0.0235 562  LEU B CG  
12962 C CD1 . LEU B 564  ? 0.3329 0.2669 0.2897 -0.0108 -0.0150 -0.0249 562  LEU B CD1 
12963 C CD2 . LEU B 564  ? 0.3250 0.2622 0.2850 -0.0125 -0.0153 -0.0218 562  LEU B CD2 
12964 N N   . THR B 565  ? 0.3022 0.2009 0.2377 -0.0135 -0.0235 -0.0247 563  THR B N   
12965 C CA  . THR B 565  ? 0.3289 0.2190 0.2610 -0.0091 -0.0244 -0.0261 563  THR B CA  
12966 C C   . THR B 565  ? 0.3328 0.2164 0.2601 -0.0068 -0.0248 -0.0287 563  THR B C   
12967 O O   . THR B 565  ? 0.3275 0.2102 0.2556 -0.0014 -0.0237 -0.0306 563  THR B O   
12968 C CB  . THR B 565  ? 0.3386 0.2198 0.2653 -0.0114 -0.0272 -0.0245 563  THR B CB  
12969 O OG1 . THR B 565  ? 0.3285 0.2156 0.2594 -0.0126 -0.0267 -0.0223 563  THR B OG1 
12970 C CG2 . THR B 565  ? 0.3457 0.2172 0.2683 -0.0065 -0.0284 -0.0261 563  THR B CG2 
12971 N N   . GLU B 566  ? 0.3392 0.2185 0.2615 -0.0111 -0.0264 -0.0288 564  GLU B N   
12972 C CA  . GLU B 566  ? 0.3514 0.2235 0.2681 -0.0092 -0.0271 -0.0313 564  GLU B CA  
12973 C C   . GLU B 566  ? 0.3384 0.2186 0.2597 -0.0060 -0.0242 -0.0330 564  GLU B C   
12974 O O   . GLU B 566  ? 0.3310 0.2076 0.2502 -0.0013 -0.0235 -0.0354 564  GLU B O   
12975 C CB  . GLU B 566  ? 0.3873 0.2530 0.2975 -0.0150 -0.0298 -0.0309 564  GLU B CB  
12976 C CG  . GLU B 566  ? 0.4468 0.3022 0.3511 -0.0178 -0.0329 -0.0295 564  GLU B CG  
12977 C CD  . GLU B 566  ? 0.5096 0.3567 0.4111 -0.0123 -0.0335 -0.0307 564  GLU B CD  
12978 O OE1 . GLU B 566  ? 0.5568 0.3987 0.4552 -0.0075 -0.0332 -0.0335 564  GLU B OE1 
12979 O OE2 . GLU B 566  ? 0.5273 0.3734 0.4297 -0.0125 -0.0342 -0.0289 564  GLU B OE2 
12980 N N   . ALA B 567  ? 0.3141 0.2051 0.2414 -0.0084 -0.0226 -0.0317 565  ALA B N   
12981 C CA  . ALA B 567  ? 0.3255 0.2246 0.2573 -0.0058 -0.0199 -0.0328 565  ALA B CA  
12982 C C   . ALA B 567  ? 0.3093 0.2118 0.2457 0.0001  -0.0176 -0.0337 565  ALA B C   
12983 O O   . ALA B 567  ? 0.3026 0.2067 0.2397 0.0039  -0.0159 -0.0355 565  ALA B O   
12984 C CB  . ALA B 567  ? 0.3168 0.2264 0.2542 -0.0095 -0.0188 -0.0310 565  ALA B CB  
12985 N N   . LEU B 568  ? 0.2882 0.1924 0.2280 0.0008  -0.0176 -0.0323 566  LEU B N   
12986 C CA  . LEU B 568  ? 0.2922 0.1999 0.2366 0.0061  -0.0158 -0.0329 566  LEU B CA  
12987 C C   . LEU B 568  ? 0.2940 0.1932 0.2337 0.0107  -0.0164 -0.0349 566  LEU B C   
12988 O O   . LEU B 568  ? 0.3001 0.2023 0.2423 0.0154  -0.0145 -0.0364 566  LEU B O   
12989 C CB  . LEU B 568  ? 0.2838 0.1947 0.2321 0.0054  -0.0161 -0.0308 566  LEU B CB  
12990 C CG  . LEU B 568  ? 0.2575 0.1776 0.2109 0.0018  -0.0151 -0.0289 566  LEU B CG  
12991 C CD1 . LEU B 568  ? 0.3102 0.2310 0.2654 0.0008  -0.0158 -0.0270 566  LEU B CD1 
12992 C CD2 . LEU B 568  ? 0.2885 0.2181 0.2483 0.0039  -0.0123 -0.0294 566  LEU B CD2 
12993 N N   . ARG B 569  ? 0.3193 0.2080 0.2523 0.0095  -0.0192 -0.0350 567  ARG B N   
12994 C CA  . ARG B 569  ? 0.3190 0.1984 0.2466 0.0140  -0.0200 -0.0371 567  ARG B CA  
12995 C C   . ARG B 569  ? 0.3601 0.2387 0.2850 0.0161  -0.0187 -0.0395 567  ARG B C   
12996 O O   . ARG B 569  ? 0.3533 0.2318 0.2787 0.0217  -0.0172 -0.0413 567  ARG B O   
12997 C CB  . ARG B 569  ? 0.3412 0.2083 0.2608 0.0115  -0.0235 -0.0367 567  ARG B CB  
12998 C CG  . ARG B 569  ? 0.4077 0.2739 0.3290 0.0110  -0.0247 -0.0346 567  ARG B CG  
12999 C CD  . ARG B 569  ? 0.4443 0.2982 0.3574 0.0078  -0.0283 -0.0338 567  ARG B CD  
13000 N NE  . ARG B 569  ? 0.4764 0.3303 0.3913 0.0072  -0.0294 -0.0316 567  ARG B NE  
13001 C CZ  . ARG B 569  ? 0.5110 0.3567 0.4205 0.0035  -0.0322 -0.0299 567  ARG B CZ  
13002 N NH1 . ARG B 569  ? 0.5266 0.3634 0.4287 -0.0003 -0.0345 -0.0301 567  ARG B NH1 
13003 N NH2 . ARG B 569  ? 0.5393 0.3858 0.4508 0.0034  -0.0329 -0.0279 567  ARG B NH2 
13004 N N   . GLU B 570  ? 0.3398 0.2184 0.2621 0.0117  -0.0193 -0.0395 568  GLU B N   
13005 C CA  . GLU B 570  ? 0.3500 0.2276 0.2691 0.0132  -0.0183 -0.0418 568  GLU B CA  
13006 C C   . GLU B 570  ? 0.3400 0.2284 0.2661 0.0167  -0.0147 -0.0422 568  GLU B C   
13007 O O   . GLU B 570  ? 0.3682 0.2556 0.2923 0.0205  -0.0133 -0.0444 568  GLU B O   
13008 C CB  . GLU B 570  ? 0.3753 0.2514 0.2907 0.0072  -0.0199 -0.0414 568  GLU B CB  
13009 C CG  . GLU B 570  ? 0.3965 0.2604 0.3034 0.0038  -0.0235 -0.0414 568  GLU B CG  
13010 C CD  . GLU B 570  ? 0.4934 0.3587 0.3994 -0.0034 -0.0254 -0.0395 568  GLU B CD  
13011 O OE1 . GLU B 570  ? 0.5085 0.3836 0.4195 -0.0055 -0.0238 -0.0387 568  GLU B OE1 
13012 O OE2 . GLU B 570  ? 0.5277 0.3843 0.4280 -0.0072 -0.0284 -0.0387 568  GLU B OE2 
13013 N N   . SER B 571  ? 0.3347 0.2332 0.2687 0.0153  -0.0133 -0.0402 569  SER B N   
13014 C CA  . SER B 571  ? 0.3134 0.2220 0.2540 0.0181  -0.0102 -0.0403 569  SER B CA  
13015 C C   . SER B 571  ? 0.3416 0.2502 0.2840 0.0243  -0.0087 -0.0415 569  SER B C   
13016 O O   . SER B 571  ? 0.3288 0.2425 0.2737 0.0276  -0.0062 -0.0425 569  SER B O   
13017 C CB  . SER B 571  ? 0.3116 0.2298 0.2597 0.0154  -0.0093 -0.0379 569  SER B CB  
13018 O OG  . SER B 571  ? 0.3280 0.2472 0.2797 0.0171  -0.0095 -0.0369 569  SER B OG  
13019 N N   . ALA B 572  ? 0.3301 0.2334 0.2713 0.0260  -0.0102 -0.0413 570  ALA B N   
13020 C CA  . ALA B 572  ? 0.3483 0.2517 0.2914 0.0320  -0.0091 -0.0423 570  ALA B CA  
13021 C C   . ALA B 572  ? 0.3703 0.2664 0.3068 0.0360  -0.0089 -0.0450 570  ALA B C   
13022 O O   . ALA B 572  ? 0.3943 0.2929 0.3330 0.0415  -0.0070 -0.0462 570  ALA B O   
13023 C CB  . ALA B 572  ? 0.3660 0.2658 0.3096 0.0327  -0.0110 -0.0411 570  ALA B CB  
13024 N N   . ALA B 573  ? 0.3592 0.2467 0.2879 0.0335  -0.0107 -0.0462 571  ALA B N   
13025 C CA  . ALA B 573  ? 0.3916 0.2713 0.3130 0.0372  -0.0106 -0.0490 571  ALA B CA  
13026 C C   . ALA B 573  ? 0.3873 0.2727 0.3093 0.0379  -0.0080 -0.0503 571  ALA B C   
13027 O O   . ALA B 573  ? 0.4027 0.2832 0.3194 0.0418  -0.0073 -0.0527 571  ALA B O   
13028 C CB  . ALA B 573  ? 0.4146 0.2813 0.3265 0.0340  -0.0141 -0.0497 571  ALA B CB  
13029 N N   . MET B 574  ? 0.3816 0.2768 0.3094 0.0346  -0.0066 -0.0486 572  MET B N   
13030 C CA  . MET B 574  ? 0.3467 0.2474 0.2750 0.0350  -0.0043 -0.0495 572  MET B CA  
13031 C C   . MET B 574  ? 0.3441 0.2524 0.2778 0.0406  -0.0009 -0.0500 572  MET B C   
13032 O O   . MET B 574  ? 0.3433 0.2566 0.2834 0.0425  -0.0002 -0.0488 572  MET B O   
13033 C CB  . MET B 574  ? 0.3282 0.2367 0.2610 0.0297  -0.0041 -0.0474 572  MET B CB  
13034 C CG  . MET B 574  ? 0.3636 0.2662 0.2914 0.0240  -0.0071 -0.0469 572  MET B CG  
13035 S SD  . MET B 574  ? 0.3914 0.3039 0.3261 0.0183  -0.0071 -0.0439 572  MET B SD  
13036 C CE  . MET B 574  ? 0.3753 0.2796 0.3028 0.0122  -0.0108 -0.0436 572  MET B CE  
13037 N N   . LYS B 575  ? 0.3261 0.2355 0.2572 0.0429  0.0011  -0.0517 573  LYS B N   
13038 C CA  . LYS B 575  ? 0.3268 0.2446 0.2631 0.0476  0.0046  -0.0520 573  LYS B CA  
13039 C C   . LYS B 575  ? 0.3160 0.2449 0.2595 0.0445  0.0063  -0.0498 573  LYS B C   
13040 O O   . LYS B 575  ? 0.3192 0.2498 0.2607 0.0423  0.0069  -0.0500 573  LYS B O   
13041 C CB  . LYS B 575  ? 0.3140 0.2282 0.2439 0.0516  0.0062  -0.0547 573  LYS B CB  
13042 C CG  . LYS B 575  ? 0.3975 0.3203 0.3328 0.0569  0.0099  -0.0549 573  LYS B CG  
13043 C CD  . LYS B 575  ? 0.4701 0.3935 0.4007 0.0591  0.0122  -0.0568 573  LYS B CD  
13044 C CE  . LYS B 575  ? 0.5395 0.4653 0.4707 0.0661  0.0151  -0.0583 573  LYS B CE  
13045 N NZ  . LYS B 575  ? 0.5804 0.5162 0.5218 0.0681  0.0168  -0.0563 573  LYS B NZ  
13046 N N   . TRP B 576  ? 0.2979 0.2339 0.2495 0.0445  0.0069  -0.0478 574  TRP B N   
13047 C CA  . TRP B 576  ? 0.2715 0.2177 0.2303 0.0419  0.0084  -0.0456 574  TRP B CA  
13048 C C   . TRP B 576  ? 0.2708 0.2251 0.2341 0.0456  0.0118  -0.0457 574  TRP B C   
13049 O O   . TRP B 576  ? 0.2718 0.2279 0.2380 0.0498  0.0128  -0.0459 574  TRP B O   
13050 C CB  . TRP B 576  ? 0.2826 0.2318 0.2472 0.0396  0.0072  -0.0435 574  TRP B CB  
13051 C CG  . TRP B 576  ? 0.2605 0.2035 0.2216 0.0353  0.0041  -0.0429 574  TRP B CG  
13052 C CD1 . TRP B 576  ? 0.3037 0.2398 0.2623 0.0353  0.0017  -0.0430 574  TRP B CD1 
13053 C CD2 . TRP B 576  ? 0.2742 0.2178 0.2342 0.0303  0.0031  -0.0420 574  TRP B CD2 
13054 N NE1 . TRP B 576  ? 0.2872 0.2197 0.2432 0.0303  -0.0006 -0.0421 574  TRP B NE1 
13055 C CE2 . TRP B 576  ? 0.2950 0.2324 0.2520 0.0272  0.0003  -0.0415 574  TRP B CE2 
13056 C CE3 . TRP B 576  ? 0.2630 0.2120 0.2243 0.0281  0.0043  -0.0415 574  TRP B CE3 
13057 C CZ2 . TRP B 576  ? 0.3108 0.2479 0.2664 0.0221  -0.0013 -0.0405 574  TRP B CZ2 
13058 C CZ3 . TRP B 576  ? 0.2711 0.2196 0.2311 0.0233  0.0027  -0.0405 574  TRP B CZ3 
13059 C CH2 . TRP B 576  ? 0.3087 0.2517 0.2661 0.0203  0.0000  -0.0400 574  TRP B CH2 
13060 N N   . THR B 577  ? 0.2915 0.2509 0.2555 0.0442  0.0135  -0.0453 575  THR B N   
13061 C CA  . THR B 577  ? 0.2646 0.2320 0.2325 0.0471  0.0168  -0.0450 575  THR B CA  
13062 C C   . THR B 577  ? 0.2572 0.2328 0.2308 0.0435  0.0178  -0.0427 575  THR B C   
13063 O O   . THR B 577  ? 0.2466 0.2210 0.2193 0.0393  0.0161  -0.0418 575  THR B O   
13064 C CB  . THR B 577  ? 0.2997 0.2643 0.2612 0.0498  0.0184  -0.0472 575  THR B CB  
13065 O OG1 . THR B 577  ? 0.3113 0.2736 0.2683 0.0460  0.0176  -0.0473 575  THR B OG1 
13066 C CG2 . THR B 577  ? 0.2970 0.2524 0.2520 0.0534  0.0173  -0.0497 575  THR B CG2 
13067 N N   . ALA B 578  ? 0.2306 0.2145 0.2098 0.0454  0.0204  -0.0417 576  ALA B N   
13068 C CA  . ALA B 578  ? 0.2373 0.2285 0.2210 0.0426  0.0216  -0.0396 576  ALA B CA  
13069 C C   . ALA B 578  ? 0.2085 0.2055 0.1933 0.0454  0.0249  -0.0397 576  ALA B C   
13070 O O   . ALA B 578  ? 0.2492 0.2495 0.2370 0.0491  0.0265  -0.0399 576  ALA B O   
13071 C CB  . ALA B 578  ? 0.2165 0.2126 0.2079 0.0408  0.0209  -0.0374 576  ALA B CB  
13072 N N   . LEU B 579  ? 0.2279 0.2263 0.2100 0.0439  0.0260  -0.0395 577  LEU B N   
13073 C CA  . LEU B 579  ? 0.2261 0.2292 0.2076 0.0463  0.0291  -0.0396 577  LEU B CA  
13074 C C   . LEU B 579  ? 0.2132 0.2232 0.1988 0.0433  0.0303  -0.0372 577  LEU B C   
13075 O O   . LEU B 579  ? 0.2068 0.2161 0.1934 0.0395  0.0284  -0.0359 577  LEU B O   
13076 C CB  . LEU B 579  ? 0.2523 0.2492 0.2247 0.0476  0.0293  -0.0421 577  LEU B CB  
13077 C CG  . LEU B 579  ? 0.3131 0.3005 0.2795 0.0495  0.0273  -0.0446 577  LEU B CG  
13078 C CD1 . LEU B 579  ? 0.3279 0.3088 0.2847 0.0502  0.0272  -0.0470 577  LEU B CD1 
13079 C CD2 . LEU B 579  ? 0.2918 0.2807 0.2609 0.0543  0.0286  -0.0454 577  LEU B CD2 
13080 N N   . PRO B 580  ? 0.2073 0.2239 0.1951 0.0450  0.0333  -0.0363 578  PRO B N   
13081 C CA  . PRO B 580  ? 0.2014 0.2232 0.1911 0.0422  0.0344  -0.0342 578  PRO B CA  
13082 C C   . PRO B 580  ? 0.2164 0.2334 0.1985 0.0408  0.0337  -0.0352 578  PRO B C   
13083 O O   . PRO B 580  ? 0.2379 0.2537 0.2145 0.0430  0.0354  -0.0367 578  PRO B O   
13084 C CB  . PRO B 580  ? 0.2225 0.2519 0.2155 0.0447  0.0379  -0.0333 578  PRO B CB  
13085 C CG  . PRO B 580  ? 0.2226 0.2522 0.2178 0.0486  0.0383  -0.0345 578  PRO B CG  
13086 C CD  . PRO B 580  ? 0.2096 0.2297 0.1984 0.0496  0.0360  -0.0372 578  PRO B CD  
13087 N N   . GLN B 581  ? 0.1986 0.2125 0.1799 0.0371  0.0312  -0.0346 579  GLN B N   
13088 C CA  . GLN B 581  ? 0.2414 0.2509 0.2159 0.0353  0.0300  -0.0354 579  GLN B CA  
13089 C C   . GLN B 581  ? 0.2296 0.2442 0.2055 0.0332  0.0311  -0.0332 579  GLN B C   
13090 O O   . GLN B 581  ? 0.2184 0.2346 0.1976 0.0302  0.0297  -0.0314 579  GLN B O   
13091 C CB  . GLN B 581  ? 0.2519 0.2558 0.2249 0.0326  0.0265  -0.0359 579  GLN B CB  
13092 C CG  . GLN B 581  ? 0.2497 0.2479 0.2208 0.0344  0.0253  -0.0379 579  GLN B CG  
13093 C CD  . GLN B 581  ? 0.3145 0.3061 0.2771 0.0365  0.0252  -0.0406 579  GLN B CD  
13094 O OE1 . GLN B 581  ? 0.3183 0.3099 0.2762 0.0366  0.0262  -0.0411 579  GLN B OE1 
13095 N NE2 . GLN B 581  ? 0.3623 0.3478 0.3225 0.0381  0.0238  -0.0424 579  GLN B NE2 
13096 N N   . LEU B 582  ? 0.2443 0.2614 0.2173 0.0350  0.0336  -0.0334 580  LEU B N   
13097 C CA  . LEU B 582  ? 0.2212 0.2425 0.1945 0.0331  0.0347  -0.0312 580  LEU B CA  
13098 C C   . LEU B 582  ? 0.2383 0.2549 0.2044 0.0313  0.0330  -0.0320 580  LEU B C   
13099 O O   . LEU B 582  ? 0.2619 0.2722 0.2228 0.0315  0.0311  -0.0343 580  LEU B O   
13100 C CB  . LEU B 582  ? 0.2385 0.2654 0.2123 0.0356  0.0384  -0.0307 580  LEU B CB  
13101 C CG  . LEU B 582  ? 0.2864 0.3204 0.2689 0.0358  0.0400  -0.0285 580  LEU B CG  
13102 C CD1 . LEU B 582  ? 0.2743 0.3075 0.2607 0.0377  0.0394  -0.0296 580  LEU B CD1 
13103 C CD2 . LEU B 582  ? 0.3513 0.3916 0.3342 0.0375  0.0437  -0.0274 580  LEU B CD2 
13104 N N   . ALA B 583  ? 0.2229 0.2426 0.1888 0.0293  0.0333  -0.0300 581  ALA B N   
13105 C CA  . ALA B 583  ? 0.2592 0.2753 0.2188 0.0274  0.0315  -0.0305 581  ALA B CA  
13106 C C   . ALA B 583  ? 0.3422 0.3540 0.2934 0.0296  0.0323  -0.0332 581  ALA B C   
13107 O O   . ALA B 583  ? 0.3792 0.3855 0.3244 0.0285  0.0299  -0.0347 581  ALA B O   
13108 C CB  . ALA B 583  ? 0.2828 0.3031 0.2434 0.0254  0.0320  -0.0277 581  ALA B CB  
13109 N N   . THR B 584  ? 0.2688 0.2832 0.2194 0.0329  0.0355  -0.0338 582  THR B N   
13110 C CA  . THR B 584  ? 0.3218 0.3324 0.2642 0.0355  0.0367  -0.0364 582  THR B CA  
13111 C C   . THR B 584  ? 0.2925 0.2973 0.2324 0.0382  0.0360  -0.0395 582  THR B C   
13112 O O   . THR B 584  ? 0.2982 0.2990 0.2309 0.0409  0.0370  -0.0420 582  THR B O   
13113 C CB  . THR B 584  ? 0.3168 0.3336 0.2597 0.0379  0.0408  -0.0355 582  THR B CB  
13114 O OG1 . THR B 584  ? 0.3481 0.3707 0.2994 0.0391  0.0426  -0.0341 582  THR B OG1 
13115 C CG2 . THR B 584  ? 0.3771 0.3977 0.3195 0.0353  0.0412  -0.0328 582  THR B CG2 
13116 N N   . GLY B 585  ? 0.2851 0.2890 0.2303 0.0377  0.0344  -0.0393 583  GLY B N   
13117 C CA  . GLY B 585  ? 0.2673 0.2655 0.2104 0.0403  0.0336  -0.0420 583  GLY B CA  
13118 C C   . GLY B 585  ? 0.2865 0.2892 0.2374 0.0423  0.0351  -0.0412 583  GLY B C   
13119 O O   . GLY B 585  ? 0.2629 0.2732 0.2207 0.0417  0.0368  -0.0386 583  GLY B O   
13120 N N   . PRO B 586  ? 0.2633 0.2611 0.2132 0.0447  0.0342  -0.0432 584  PRO B N   
13121 C CA  . PRO B 586  ? 0.2451 0.2469 0.2024 0.0468  0.0352  -0.0425 584  PRO B CA  
13122 C C   . PRO B 586  ? 0.2973 0.3054 0.2562 0.0508  0.0391  -0.0425 584  PRO B C   
13123 O O   . PRO B 586  ? 0.2924 0.2985 0.2449 0.0537  0.0408  -0.0444 584  PRO B O   
13124 C CB  . PRO B 586  ? 0.2735 0.2671 0.2275 0.0483  0.0329  -0.0449 584  PRO B CB  
13125 C CG  . PRO B 586  ? 0.3104 0.2963 0.2541 0.0491  0.0322  -0.0476 584  PRO B CG  
13126 C CD  . PRO B 586  ? 0.3029 0.2908 0.2448 0.0453  0.0319  -0.0462 584  PRO B CD  
13127 N N   . ALA B 587  ? 0.2695 0.2854 0.2370 0.0509  0.0405  -0.0402 585  ALA B N   
13128 C CA  . ALA B 587  ? 0.2552 0.2788 0.2260 0.0542  0.0443  -0.0396 585  ALA B CA  
13129 C C   . ALA B 587  ? 0.2560 0.2796 0.2296 0.0583  0.0447  -0.0409 585  ALA B C   
13130 O O   . ALA B 587  ? 0.2484 0.2681 0.2240 0.0578  0.0421  -0.0412 585  ALA B O   
13131 C CB  . ALA B 587  ? 0.2686 0.3012 0.2472 0.0514  0.0456  -0.0360 585  ALA B CB  
13132 N N   . ALA B 588  ? 0.2612 0.2895 0.2349 0.0626  0.0481  -0.0415 586  ALA B N   
13133 C CA  . ALA B 588  ? 0.2554 0.2858 0.2329 0.0670  0.0490  -0.0423 586  ALA B CA  
13134 C C   . ALA B 588  ? 0.2445 0.2834 0.2327 0.0653  0.0490  -0.0393 586  ALA B C   
13135 O O   . ALA B 588  ? 0.2462 0.2909 0.2388 0.0616  0.0496  -0.0365 586  ALA B O   
13136 C CB  . ALA B 588  ? 0.2393 0.2735 0.2140 0.0723  0.0529  -0.0437 586  ALA B CB  
13137 N N   . GLY B 589  ? 0.2631 0.3021 0.2552 0.0680  0.0482  -0.0398 587  GLY B N   
13138 C CA  . GLY B 589  ? 0.2545 0.3013 0.2565 0.0668  0.0481  -0.0372 587  GLY B CA  
13139 C C   . GLY B 589  ? 0.2702 0.3161 0.2750 0.0706  0.0471  -0.0382 587  GLY B C   
13140 O O   . GLY B 589  ? 0.2898 0.3291 0.2889 0.0746  0.0469  -0.0410 587  GLY B O   
13141 N N   . GLU B 590  ? 0.2730 0.3251 0.2865 0.0692  0.0464  -0.0360 588  GLU B N   
13142 C CA  . GLU B 590  ? 0.2661 0.3182 0.2833 0.0725  0.0452  -0.0365 588  GLU B CA  
13143 C C   . GLU B 590  ? 0.2602 0.3019 0.2738 0.0709  0.0412  -0.0377 588  GLU B C   
13144 O O   . GLU B 590  ? 0.2550 0.2948 0.2697 0.0660  0.0390  -0.0364 588  GLU B O   
13145 C CB  . GLU B 590  ? 0.3020 0.3645 0.3295 0.0711  0.0456  -0.0335 588  GLU B CB  
13146 N N   . THR B 591  ? 0.2973 0.3324 0.3067 0.0751  0.0402  -0.0402 589  THR B N   
13147 C CA  . THR B 591  ? 0.2584 0.2828 0.2632 0.0738  0.0365  -0.0415 589  THR B CA  
13148 C C   . THR B 591  ? 0.2984 0.3229 0.3079 0.0757  0.0346  -0.0410 589  THR B C   
13149 O O   . THR B 591  ? 0.3064 0.3357 0.3192 0.0805  0.0361  -0.0413 589  THR B O   
13150 C CB  . THR B 591  ? 0.2847 0.2991 0.2793 0.0766  0.0364  -0.0447 589  THR B CB  
13151 O OG1 . THR B 591  ? 0.3282 0.3427 0.3184 0.0746  0.0380  -0.0450 589  THR B OG1 
13152 C CG2 . THR B 591  ? 0.3147 0.3179 0.3044 0.0745  0.0324  -0.0457 589  THR B CG2 
13153 N N   . ARG B 592  ? 0.2812 0.3009 0.2911 0.0721  0.0313  -0.0403 590  ARG B N   
13154 C CA  . ARG B 592  ? 0.3208 0.3390 0.3338 0.0736  0.0290  -0.0400 590  ARG B CA  
13155 C C   . ARG B 592  ? 0.2905 0.2980 0.2981 0.0708  0.0255  -0.0408 590  ARG B C   
13156 O O   . ARG B 592  ? 0.2864 0.2895 0.2896 0.0669  0.0248  -0.0410 590  ARG B O   
13157 C CB  . ARG B 592  ? 0.3080 0.3360 0.3308 0.0715  0.0289  -0.0372 590  ARG B CB  
13158 C CG  . ARG B 592  ? 0.3190 0.3479 0.3436 0.0653  0.0279  -0.0354 590  ARG B CG  
13159 C CD  . ARG B 592  ? 0.3645 0.3993 0.3970 0.0633  0.0266  -0.0331 590  ARG B CD  
13160 N NE  . ARG B 592  ? 0.3508 0.3865 0.3847 0.0577  0.0257  -0.0315 590  ARG B NE  
13161 C CZ  . ARG B 592  ? 0.3551 0.3846 0.3868 0.0545  0.0230  -0.0314 590  ARG B CZ  
13162 N NH1 . ARG B 592  ? 0.3267 0.3485 0.3544 0.0557  0.0207  -0.0327 590  ARG B NH1 
13163 N NH2 . ARG B 592  ? 0.3231 0.3542 0.3565 0.0499  0.0225  -0.0300 590  ARG B NH2 
13164 N N   . THR B 593  ? 0.2868 0.2905 0.2949 0.0726  0.0232  -0.0410 591  THR B N   
13165 C CA  . THR B 593  ? 0.2735 0.2673 0.2769 0.0699  0.0197  -0.0414 591  THR B CA  
13166 C C   . THR B 593  ? 0.2794 0.2761 0.2874 0.0646  0.0181  -0.0391 591  THR B C   
13167 O O   . THR B 593  ? 0.2812 0.2867 0.2968 0.0638  0.0188  -0.0372 591  THR B O   
13168 C CB  . THR B 593  ? 0.3013 0.2893 0.3029 0.0740  0.0178  -0.0424 591  THR B CB  
13169 O OG1 . THR B 593  ? 0.3358 0.3317 0.3456 0.0756  0.0178  -0.0406 591  THR B OG1 
13170 C CG2 . THR B 593  ? 0.3673 0.3512 0.3634 0.0797  0.0193  -0.0449 591  THR B CG2 
13171 N N   . VAL B 594  ? 0.2664 0.2557 0.2697 0.0608  0.0158  -0.0393 592  VAL B N   
13172 C CA  . VAL B 594  ? 0.2611 0.2513 0.2674 0.0561  0.0139  -0.0375 592  VAL B CA  
13173 C C   . VAL B 594  ? 0.2981 0.2811 0.3020 0.0566  0.0109  -0.0377 592  VAL B C   
13174 O O   . VAL B 594  ? 0.2906 0.2645 0.2874 0.0572  0.0095  -0.0392 592  VAL B O   
13175 C CB  . VAL B 594  ? 0.2566 0.2448 0.2598 0.0514  0.0137  -0.0373 592  VAL B CB  
13176 C CG1 . VAL B 594  ? 0.2610 0.2504 0.2673 0.0470  0.0119  -0.0355 592  VAL B CG1 
13177 C CG2 . VAL B 594  ? 0.2799 0.2745 0.2847 0.0513  0.0166  -0.0371 592  VAL B CG2 
13178 N N   . LEU B 595  ? 0.2789 0.2658 0.2884 0.0565  0.0098  -0.0361 593  LEU B N   
13179 C CA  . LEU B 595  ? 0.2790 0.2601 0.2869 0.0575  0.0070  -0.0360 593  LEU B CA  
13180 C C   . LEU B 595  ? 0.2473 0.2270 0.2557 0.0525  0.0048  -0.0346 593  LEU B C   
13181 O O   . LEU B 595  ? 0.2751 0.2609 0.2880 0.0495  0.0055  -0.0332 593  LEU B O   
13182 C CB  . LEU B 595  ? 0.2778 0.2642 0.2913 0.0616  0.0071  -0.0354 593  LEU B CB  
13183 C CG  . LEU B 595  ? 0.2814 0.2707 0.2955 0.0672  0.0094  -0.0367 593  LEU B CG  
13184 C CD1 . LEU B 595  ? 0.3106 0.3060 0.3311 0.0708  0.0091  -0.0357 593  LEU B CD1 
13185 C CD2 . LEU B 595  ? 0.3241 0.3030 0.3295 0.0699  0.0089  -0.0391 593  LEU B CD2 
13186 N N   . ASN B 596  ? 0.2438 0.2149 0.2472 0.0518  0.0023  -0.0348 594  ASN B N   
13187 C CA  . ASN B 596  ? 0.2745 0.2440 0.2779 0.0475  0.0002  -0.0334 594  ASN B CA  
13188 C C   . ASN B 596  ? 0.2287 0.2048 0.2389 0.0477  -0.0003 -0.0317 594  ASN B C   
13189 O O   . ASN B 596  ? 0.2298 0.2060 0.2416 0.0513  -0.0012 -0.0317 594  ASN B O   
13190 C CB  . ASN B 596  ? 0.2595 0.2186 0.2561 0.0473  -0.0024 -0.0339 594  ASN B CB  
13191 C CG  . ASN B 596  ? 0.2772 0.2339 0.2725 0.0425  -0.0043 -0.0325 594  ASN B CG  
13192 O OD1 . ASN B 596  ? 0.2601 0.2226 0.2602 0.0405  -0.0043 -0.0311 594  ASN B OD1 
13193 N ND2 . ASN B 596  ? 0.2724 0.2204 0.2609 0.0406  -0.0060 -0.0329 594  ASN B ND2 
13194 N N   . PRO B 597  ? 0.2227 0.2043 0.2368 0.0442  0.0000  -0.0304 595  PRO B N   
13195 C CA  . PRO B 597  ? 0.2402 0.2276 0.2605 0.0442  -0.0007 -0.0290 595  PRO B CA  
13196 C C   . PRO B 597  ? 0.2325 0.2151 0.2510 0.0443  -0.0036 -0.0283 595  PRO B C   
13197 O O   . PRO B 597  ? 0.2402 0.2267 0.2631 0.0459  -0.0045 -0.0274 595  PRO B O   
13198 C CB  . PRO B 597  ? 0.2257 0.2176 0.2486 0.0400  -0.0001 -0.0280 595  PRO B CB  
13199 C CG  . PRO B 597  ? 0.2061 0.1928 0.2232 0.0372  0.0002  -0.0287 595  PRO B CG  
13200 C CD  . PRO B 597  ? 0.2222 0.2051 0.2355 0.0402  0.0011  -0.0303 595  PRO B CD  
13201 N N   . GLY B 598  ? 0.2539 0.2284 0.2661 0.0426  -0.0052 -0.0286 596  GLY B N   
13202 C CA  . GLY B 598  ? 0.2369 0.2062 0.2469 0.0427  -0.0079 -0.0279 596  GLY B CA  
13203 C C   . GLY B 598  ? 0.2766 0.2405 0.2838 0.0472  -0.0090 -0.0287 596  GLY B C   
13204 O O   . GLY B 598  ? 0.2940 0.2537 0.2995 0.0478  -0.0114 -0.0280 596  GLY B O   
13205 N N   . ASP B 599  ? 0.2639 0.2279 0.2704 0.0506  -0.0073 -0.0302 597  ASP B N   
13206 C CA  . ASP B 599  ? 0.2848 0.2433 0.2883 0.0554  -0.0081 -0.0313 597  ASP B CA  
13207 C C   . ASP B 599  ? 0.2811 0.2429 0.2856 0.0589  -0.0053 -0.0329 597  ASP B C   
13208 O O   . ASP B 599  ? 0.2674 0.2248 0.2669 0.0582  -0.0043 -0.0342 597  ASP B O   
13209 C CB  . ASP B 599  ? 0.2862 0.2330 0.2812 0.0542  -0.0102 -0.0318 597  ASP B CB  
13210 C CG  . ASP B 599  ? 0.3553 0.2952 0.3467 0.0592  -0.0116 -0.0327 597  ASP B CG  
13211 O OD1 . ASP B 599  ? 0.3086 0.2530 0.3036 0.0642  -0.0103 -0.0334 597  ASP B OD1 
13212 O OD2 . ASP B 599  ? 0.3539 0.2840 0.3388 0.0582  -0.0141 -0.0326 597  ASP B OD2 
13213 N N   . HIS B 600  ? 0.2912 0.2609 0.3020 0.0626  -0.0041 -0.0326 598  HIS B N   
13214 C CA  . HIS B 600  ? 0.2777 0.2519 0.2900 0.0658  -0.0011 -0.0339 598  HIS B CA  
13215 C C   . HIS B 600  ? 0.2941 0.2603 0.2999 0.0702  -0.0010 -0.0360 598  HIS B C   
13216 O O   . HIS B 600  ? 0.3193 0.2877 0.3246 0.0726  0.0016  -0.0374 598  HIS B O   
13217 C CB  . HIS B 600  ? 0.2711 0.2563 0.2920 0.0686  0.0002  -0.0328 598  HIS B CB  
13218 C CG  . HIS B 600  ? 0.2568 0.2504 0.2838 0.0643  0.0009  -0.0311 598  HIS B CG  
13219 N ND1 . HIS B 600  ? 0.2919 0.2958 0.3270 0.0654  0.0018  -0.0298 598  HIS B ND1 
13220 C CD2 . HIS B 600  ? 0.2674 0.2605 0.2936 0.0590  0.0007  -0.0305 598  HIS B CD2 
13221 C CE1 . HIS B 600  ? 0.3179 0.3265 0.3564 0.0608  0.0020  -0.0286 598  HIS B CE1 
13222 N NE2 . HIS B 600  ? 0.2963 0.2985 0.3294 0.0571  0.0014  -0.0290 598  HIS B NE2 
13223 N N   . ARG B 601  ? 0.2960 0.2523 0.2961 0.0710  -0.0038 -0.0363 599  ARG B N   
13224 C CA  . ARG B 601  ? 0.3024 0.2493 0.2951 0.0747  -0.0040 -0.0384 599  ARG B CA  
13225 C C   . ARG B 601  ? 0.3156 0.2561 0.3016 0.0711  -0.0036 -0.0397 599  ARG B C   
13226 O O   . ARG B 601  ? 0.3298 0.2634 0.3095 0.0738  -0.0033 -0.0417 599  ARG B O   
13227 C CB  . ARG B 601  ? 0.3519 0.2897 0.3404 0.0765  -0.0074 -0.0382 599  ARG B CB  
13228 C CG  . ARG B 601  ? 0.3530 0.2967 0.3480 0.0801  -0.0083 -0.0368 599  ARG B CG  
13229 C CD  . ARG B 601  ? 0.4056 0.3401 0.3963 0.0807  -0.0120 -0.0361 599  ARG B CD  
13230 N NE  . ARG B 601  ? 0.3647 0.2955 0.3531 0.0743  -0.0140 -0.0346 599  ARG B NE  
13231 C CZ  . ARG B 601  ? 0.4557 0.3781 0.4395 0.0732  -0.0172 -0.0337 599  ARG B CZ  
13232 N NH1 . ARG B 601  ? 0.4495 0.3655 0.4304 0.0781  -0.0191 -0.0340 599  ARG B NH1 
13233 N NH2 . ARG B 601  ? 0.4145 0.3347 0.3965 0.0672  -0.0185 -0.0323 599  ARG B NH2 
13234 N N   . ASP B 602  ? 0.2965 0.2392 0.2834 0.0651  -0.0038 -0.0385 600  ASP B N   
13235 C CA  . ASP B 602  ? 0.2839 0.2213 0.2650 0.0611  -0.0037 -0.0393 600  ASP B CA  
13236 C C   . ASP B 602  ? 0.3031 0.2483 0.2872 0.0608  -0.0005 -0.0398 600  ASP B C   
13237 O O   . ASP B 602  ? 0.2962 0.2496 0.2860 0.0579  0.0007  -0.0384 600  ASP B O   
13238 C CB  . ASP B 602  ? 0.3007 0.2366 0.2814 0.0551  -0.0056 -0.0375 600  ASP B CB  
13239 C CG  . ASP B 602  ? 0.3414 0.2723 0.3164 0.0507  -0.0059 -0.0381 600  ASP B CG  
13240 O OD1 . ASP B 602  ? 0.3594 0.2845 0.3287 0.0524  -0.0055 -0.0400 600  ASP B OD1 
13241 O OD2 . ASP B 602  ? 0.3334 0.2664 0.3097 0.0457  -0.0064 -0.0366 600  ASP B OD2 
13242 N N   . VAL B 603  ? 0.3249 0.2669 0.3047 0.0640  0.0010  -0.0420 601  VAL B N   
13243 C CA  . VAL B 603  ? 0.2928 0.2412 0.2742 0.0640  0.0040  -0.0426 601  VAL B CA  
13244 C C   . VAL B 603  ? 0.3261 0.2710 0.3032 0.0585  0.0035  -0.0427 601  VAL B C   
13245 O O   . VAL B 603  ? 0.3188 0.2540 0.2881 0.0576  0.0019  -0.0440 601  VAL B O   
13246 C CB  . VAL B 603  ? 0.3166 0.2629 0.2946 0.0698  0.0058  -0.0449 601  VAL B CB  
13247 C CG1 . VAL B 603  ? 0.3104 0.2637 0.2900 0.0696  0.0091  -0.0454 601  VAL B CG1 
13248 C CG2 . VAL B 603  ? 0.3151 0.2650 0.2976 0.0755  0.0061  -0.0448 601  VAL B CG2 
13249 N N   . VAL B 604  ? 0.2660 0.2188 0.2481 0.0548  0.0047  -0.0412 602  VAL B N   
13250 C CA  . VAL B 604  ? 0.2850 0.2357 0.2640 0.0497  0.0042  -0.0409 602  VAL B CA  
13251 C C   . VAL B 604  ? 0.2753 0.2261 0.2507 0.0503  0.0062  -0.0425 602  VAL B C   
13252 O O   . VAL B 604  ? 0.2840 0.2287 0.2533 0.0477  0.0052  -0.0433 602  VAL B O   
13253 C CB  . VAL B 604  ? 0.2633 0.2216 0.2486 0.0456  0.0044  -0.0387 602  VAL B CB  
13254 C CG1 . VAL B 604  ? 0.2324 0.1887 0.2146 0.0405  0.0036  -0.0383 602  VAL B CG1 
13255 C CG2 . VAL B 604  ? 0.2752 0.2334 0.2636 0.0453  0.0024  -0.0373 602  VAL B CG2 
13256 N N   . GLY B 605  ? 0.2611 0.2190 0.2403 0.0537  0.0090  -0.0428 603  GLY B N   
13257 C CA  . GLY B 605  ? 0.2537 0.2125 0.2298 0.0542  0.0111  -0.0441 603  GLY B CA  
13258 C C   . GLY B 605  ? 0.2809 0.2486 0.2623 0.0580  0.0144  -0.0440 603  GLY B C   
13259 O O   . GLY B 605  ? 0.2750 0.2464 0.2610 0.0613  0.0148  -0.0435 603  GLY B O   
13260 N N   . SER B 606  ? 0.2545 0.2259 0.2350 0.0575  0.0166  -0.0443 604  SER B N   
13261 C CA  . SER B 606  ? 0.2534 0.2334 0.2383 0.0608  0.0199  -0.0441 604  SER B CA  
13262 C C   . SER B 606  ? 0.2627 0.2496 0.2505 0.0573  0.0216  -0.0427 604  SER B C   
13263 O O   . SER B 606  ? 0.2871 0.2705 0.2706 0.0539  0.0208  -0.0429 604  SER B O   
13264 C CB  . SER B 606  ? 0.3305 0.3068 0.3095 0.0659  0.0215  -0.0467 604  SER B CB  
13265 O OG  . SER B 606  ? 0.4732 0.4453 0.4455 0.0641  0.0219  -0.0480 604  SER B OG  
13266 N N   . VAL B 607  ? 0.2357 0.2324 0.2308 0.0581  0.0238  -0.0410 605  VAL B N   
13267 C CA  . VAL B 607  ? 0.2053 0.2088 0.2036 0.0550  0.0254  -0.0393 605  VAL B CA  
13268 C C   . VAL B 607  ? 0.2581 0.2685 0.2580 0.0582  0.0289  -0.0394 605  VAL B C   
13269 O O   . VAL B 607  ? 0.2364 0.2513 0.2403 0.0620  0.0302  -0.0394 605  VAL B O   
13270 C CB  . VAL B 607  ? 0.2297 0.2387 0.2353 0.0516  0.0244  -0.0368 605  VAL B CB  
13271 C CG1 . VAL B 607  ? 0.2512 0.2657 0.2635 0.0542  0.0247  -0.0359 605  VAL B CG1 
13272 C CG2 . VAL B 607  ? 0.2283 0.2436 0.2367 0.0486  0.0260  -0.0351 605  VAL B CG2 
13273 N N   . THR B 608  ? 0.2332 0.2445 0.2299 0.0568  0.0304  -0.0395 606  THR B N   
13274 C CA  . THR B 608  ? 0.2283 0.2469 0.2266 0.0589  0.0340  -0.0391 606  THR B CA  
13275 C C   . THR B 608  ? 0.2332 0.2593 0.2373 0.0549  0.0347  -0.0363 606  THR B C   
13276 O O   . THR B 608  ? 0.2361 0.2597 0.2381 0.0510  0.0335  -0.0357 606  THR B O   
13277 C CB  . THR B 608  ? 0.2485 0.2622 0.2382 0.0604  0.0351  -0.0413 606  THR B CB  
13278 O OG1 . THR B 608  ? 0.2495 0.2559 0.2337 0.0645  0.0344  -0.0440 606  THR B OG1 
13279 C CG2 . THR B 608  ? 0.2572 0.2788 0.2481 0.0621  0.0389  -0.0407 606  THR B CG2 
13280 N N   . GLU B 609  ? 0.2211 0.2560 0.2325 0.0558  0.0364  -0.0345 607  GLU B N   
13281 C CA  . GLU B 609  ? 0.2524 0.2934 0.2695 0.0518  0.0366  -0.0317 607  GLU B CA  
13282 C C   . GLU B 609  ? 0.2217 0.2683 0.2385 0.0514  0.0396  -0.0307 607  GLU B C   
13283 O O   . GLU B 609  ? 0.2367 0.2848 0.2505 0.0548  0.0421  -0.0318 607  GLU B O   
13284 C CB  . GLU B 609  ? 0.2227 0.2696 0.2481 0.0519  0.0361  -0.0300 607  GLU B CB  
13285 C CG  . GLU B 609  ? 0.2665 0.3072 0.2918 0.0511  0.0326  -0.0306 607  GLU B CG  
13286 C CD  . GLU B 609  ? 0.3094 0.3549 0.3420 0.0512  0.0317  -0.0292 607  GLU B CD  
13287 O OE1 . GLU B 609  ? 0.3166 0.3691 0.3538 0.0540  0.0335  -0.0286 607  GLU B OE1 
13288 O OE2 . GLU B 609  ? 0.2962 0.3386 0.3300 0.0486  0.0290  -0.0286 607  GLU B OE2 
13289 N N   . THR B 610  ? 0.2200 0.2692 0.2391 0.0472  0.0393  -0.0285 608  THR B N   
13290 C CA  . THR B 610  ? 0.2003 0.2529 0.2177 0.0458  0.0414  -0.0273 608  THR B CA  
13291 C C   . THR B 610  ? 0.2179 0.2804 0.2416 0.0463  0.0442  -0.0251 608  THR B C   
13292 O O   . THR B 610  ? 0.2278 0.2946 0.2583 0.0448  0.0434  -0.0232 608  THR B O   
13293 C CB  . THR B 610  ? 0.2174 0.2677 0.2344 0.0410  0.0396  -0.0258 608  THR B CB  
13294 O OG1 . THR B 610  ? 0.1944 0.2366 0.2070 0.0402  0.0368  -0.0275 608  THR B OG1 
13295 C CG2 . THR B 610  ? 0.2223 0.2744 0.2359 0.0398  0.0415  -0.0249 608  THR B CG2 
13296 N N   . SER B 611  ? 0.2156 0.2817 0.2368 0.0482  0.0473  -0.0252 609  SER B N   
13297 C CA  . SER B 611  ? 0.2567 0.3328 0.2837 0.0478  0.0500  -0.0226 609  SER B CA  
13298 C C   . SER B 611  ? 0.2681 0.3460 0.2973 0.0427  0.0494  -0.0197 609  SER B C   
13299 O O   . SER B 611  ? 0.2215 0.2936 0.2462 0.0403  0.0478  -0.0200 609  SER B O   
13300 C CB  . SER B 611  ? 0.2542 0.3338 0.2774 0.0511  0.0538  -0.0233 609  SER B CB  
13301 O OG  . SER B 611  ? 0.2391 0.3151 0.2558 0.0493  0.0541  -0.0235 609  SER B OG  
13302 N N   . GLU B 612  ? 0.2262 0.3121 0.2624 0.0411  0.0504  -0.0169 610  GLU B N   
13303 C CA  . GLU B 612  ? 0.2514 0.3386 0.2893 0.0364  0.0499  -0.0141 610  GLU B CA  
13304 C C   . GLU B 612  ? 0.2558 0.3425 0.2879 0.0357  0.0518  -0.0137 610  GLU B C   
13305 O O   . GLU B 612  ? 0.2298 0.3128 0.2596 0.0325  0.0503  -0.0127 610  GLU B O   
13306 C CB  . GLU B 612  ? 0.3151 0.4110 0.3613 0.0346  0.0507  -0.0112 610  GLU B CB  
13307 C CG  . GLU B 612  ? 0.3197 0.4156 0.3714 0.0349  0.0483  -0.0115 610  GLU B CG  
13308 C CD  . GLU B 612  ? 0.3855 0.4898 0.4455 0.0327  0.0486  -0.0085 610  GLU B CD  
13309 O OE1 . GLU B 612  ? 0.4740 0.5831 0.5356 0.0300  0.0501  -0.0059 610  GLU B OE1 
13310 O OE2 . GLU B 612  ? 0.3773 0.4833 0.4421 0.0336  0.0471  -0.0088 610  GLU B OE2 
13311 N N   . GLU B 613  ? 0.2729 0.3629 0.3022 0.0390  0.0550  -0.0146 611  GLU B N   
13312 C CA  . GLU B 613  ? 0.2465 0.3356 0.2694 0.0387  0.0568  -0.0145 611  GLU B CA  
13313 C C   . GLU B 613  ? 0.2589 0.3383 0.2744 0.0383  0.0543  -0.0167 611  GLU B C   
13314 O O   . GLU B 613  ? 0.2742 0.3513 0.2859 0.0358  0.0539  -0.0157 611  GLU B O   
13315 C CB  . GLU B 613  ? 0.2931 0.3872 0.3138 0.0429  0.0606  -0.0155 611  GLU B CB  
13316 N N   . ASP B 614  ? 0.2473 0.3208 0.2605 0.0407  0.0526  -0.0197 612  ASP B N   
13317 C CA  . ASP B 614  ? 0.2397 0.3044 0.2460 0.0400  0.0502  -0.0217 612  ASP B CA  
13318 C C   . ASP B 614  ? 0.2481 0.3096 0.2566 0.0359  0.0470  -0.0203 612  ASP B C   
13319 O O   . ASP B 614  ? 0.2401 0.2966 0.2438 0.0341  0.0454  -0.0206 612  ASP B O   
13320 C CB  . ASP B 614  ? 0.2565 0.3155 0.2594 0.0435  0.0492  -0.0251 612  ASP B CB  
13321 C CG  . ASP B 614  ? 0.2791 0.3379 0.2761 0.0475  0.0519  -0.0272 612  ASP B CG  
13322 O OD1 . ASP B 614  ? 0.2922 0.3526 0.2852 0.0471  0.0538  -0.0266 612  ASP B OD1 
13323 O OD2 . ASP B 614  ? 0.2805 0.3371 0.2763 0.0513  0.0520  -0.0296 612  ASP B OD2 
13324 N N   . ALA B 615  ? 0.2237 0.2881 0.2394 0.0345  0.0460  -0.0187 613  ALA B N   
13325 C CA  . ALA B 615  ? 0.2180 0.2801 0.2359 0.0307  0.0433  -0.0172 613  ALA B CA  
13326 C C   . ALA B 615  ? 0.2354 0.2991 0.2520 0.0280  0.0440  -0.0148 613  ALA B C   
13327 O O   . ALA B 615  ? 0.2186 0.2779 0.2322 0.0259  0.0421  -0.0147 613  ALA B O   
13328 C CB  . ALA B 615  ? 0.2230 0.2884 0.2486 0.0298  0.0423  -0.0159 613  ALA B CB  
13329 N N   . ARG B 616  ? 0.2420 0.3123 0.2608 0.0279  0.0467  -0.0128 614  ARG B N   
13330 C CA  . ARG B 616  ? 0.2447 0.3163 0.2617 0.0253  0.0475  -0.0104 614  ARG B CA  
13331 C C   . ARG B 616  ? 0.2518 0.3192 0.2606 0.0261  0.0478  -0.0118 614  ARG B C   
13332 O O   . ARG B 616  ? 0.2457 0.3105 0.2517 0.0238  0.0465  -0.0106 614  ARG B O   
13333 C CB  . ARG B 616  ? 0.2644 0.3442 0.2851 0.0250  0.0505  -0.0079 614  ARG B CB  
13334 C CG  . ARG B 616  ? 0.2835 0.3669 0.3121 0.0225  0.0496  -0.0055 614  ARG B CG  
13335 C CD  . ARG B 616  ? 0.3598 0.4515 0.3921 0.0214  0.0524  -0.0026 614  ARG B CD  
13336 N NE  . ARG B 616  ? 0.3554 0.4530 0.3896 0.0249  0.0551  -0.0037 614  ARG B NE  
13337 C CZ  . ARG B 616  ? 0.3587 0.4597 0.3989 0.0261  0.0548  -0.0041 614  ARG B CZ  
13338 N NH1 . ARG B 616  ? 0.3396 0.4386 0.3842 0.0240  0.0519  -0.0035 614  ARG B NH1 
13339 N NH2 . ARG B 616  ? 0.3425 0.4490 0.3840 0.0298  0.0574  -0.0051 614  ARG B NH2 
13340 N N   . ARG B 617  ? 0.2388 0.3053 0.2434 0.0295  0.0492  -0.0144 615  ARG B N   
13341 C CA  . ARG B 617  ? 0.2627 0.3248 0.2591 0.0302  0.0492  -0.0160 615  ARG B CA  
13342 C C   . ARG B 617  ? 0.2428 0.2978 0.2365 0.0285  0.0456  -0.0171 615  ARG B C   
13343 O O   . ARG B 617  ? 0.2290 0.2813 0.2179 0.0270  0.0447  -0.0167 615  ARG B O   
13344 C CB  . ARG B 617  ? 0.2696 0.3308 0.2617 0.0344  0.0511  -0.0189 615  ARG B CB  
13345 C CG  . ARG B 617  ? 0.3235 0.3798 0.3064 0.0351  0.0510  -0.0208 615  ARG B CG  
13346 C CD  . ARG B 617  ? 0.3834 0.4407 0.3618 0.0393  0.0539  -0.0230 615  ARG B CD  
13347 N NE  . ARG B 617  ? 0.4124 0.4659 0.3904 0.0424  0.0531  -0.0260 615  ARG B NE  
13348 C CZ  . ARG B 617  ? 0.4703 0.5157 0.4420 0.0432  0.0509  -0.0289 615  ARG B CZ  
13349 N NH1 . ARG B 617  ? 0.4624 0.5030 0.4278 0.0412  0.0493  -0.0293 615  ARG B NH1 
13350 N NH2 . ARG B 617  ? 0.4834 0.5252 0.4550 0.0461  0.0502  -0.0314 615  ARG B NH2 
13351 N N   . ALA B 618  ? 0.2452 0.2974 0.2419 0.0287  0.0434  -0.0183 616  ALA B N   
13352 C CA  . ALA B 618  ? 0.2386 0.2849 0.2334 0.0270  0.0401  -0.0191 616  ALA B CA  
13353 C C   . ALA B 618  ? 0.2339 0.2808 0.2304 0.0237  0.0388  -0.0165 616  ALA B C   
13354 O O   . ALA B 618  ? 0.2203 0.2636 0.2131 0.0223  0.0369  -0.0166 616  ALA B O   
13355 C CB  . ALA B 618  ? 0.2141 0.2581 0.2125 0.0276  0.0383  -0.0205 616  ALA B CB  
13356 N N   . VAL B 619  ? 0.2356 0.2869 0.2379 0.0224  0.0396  -0.0140 617  VAL B N   
13357 C CA  . VAL B 619  ? 0.2218 0.2730 0.2257 0.0195  0.0382  -0.0115 617  VAL B CA  
13358 C C   . VAL B 619  ? 0.2296 0.2810 0.2285 0.0187  0.0391  -0.0103 617  VAL B C   
13359 O O   . VAL B 619  ? 0.2517 0.3004 0.2485 0.0171  0.0372  -0.0094 617  VAL B O   
13360 C CB  . VAL B 619  ? 0.2203 0.2756 0.2310 0.0181  0.0387  -0.0092 617  VAL B CB  
13361 C CG1 . VAL B 619  ? 0.2336 0.2879 0.2451 0.0153  0.0372  -0.0066 617  VAL B CG1 
13362 C CG2 . VAL B 619  ? 0.2169 0.2714 0.2321 0.0187  0.0373  -0.0105 617  VAL B CG2 
13363 N N   . ARG B 620  ? 0.2559 0.3105 0.2524 0.0201  0.0420  -0.0102 618  ARG B N   
13364 C CA  . ARG B 620  ? 0.2588 0.3134 0.2497 0.0196  0.0429  -0.0092 618  ARG B CA  
13365 C C   . ARG B 620  ? 0.2548 0.3040 0.2391 0.0201  0.0410  -0.0114 618  ARG B C   
13366 O O   . ARG B 620  ? 0.2600 0.3075 0.2408 0.0186  0.0398  -0.0103 618  ARG B O   
13367 C CB  . ARG B 620  ? 0.2831 0.3426 0.2726 0.0212  0.0466  -0.0088 618  ARG B CB  
13368 C CG  . ARG B 620  ? 0.3293 0.3950 0.3253 0.0200  0.0484  -0.0060 618  ARG B CG  
13369 C CD  . ARG B 620  ? 0.4242 0.4957 0.4187 0.0211  0.0522  -0.0049 618  ARG B CD  
13370 N NE  . ARG B 620  ? 0.4566 0.5284 0.4481 0.0249  0.0541  -0.0080 618  ARG B NE  
13371 C CZ  . ARG B 620  ? 0.4092 0.4853 0.4051 0.0271  0.0559  -0.0088 618  ARG B CZ  
13372 N NH1 . ARG B 620  ? 0.4242 0.5052 0.4278 0.0257  0.0561  -0.0067 618  ARG B NH1 
13373 N NH2 . ARG B 620  ? 0.4684 0.5437 0.4606 0.0309  0.0574  -0.0118 618  ARG B NH2 
13374 N N   . LEU B 621  ? 0.2309 0.2773 0.2134 0.0221  0.0406  -0.0145 619  LEU B N   
13375 C CA  . LEU B 621  ? 0.2430 0.2840 0.2194 0.0222  0.0385  -0.0166 619  LEU B CA  
13376 C C   . LEU B 621  ? 0.2613 0.2997 0.2395 0.0198  0.0352  -0.0159 619  LEU B C   
13377 O O   . LEU B 621  ? 0.2574 0.2931 0.2312 0.0187  0.0334  -0.0159 619  LEU B O   
13378 C CB  . LEU B 621  ? 0.2603 0.2982 0.2346 0.0247  0.0385  -0.0200 619  LEU B CB  
13379 C CG  . LEU B 621  ? 0.2906 0.3300 0.2613 0.0277  0.0416  -0.0214 619  LEU B CG  
13380 C CD1 . LEU B 621  ? 0.2817 0.3183 0.2524 0.0304  0.0415  -0.0243 619  LEU B CD1 
13381 C CD2 . LEU B 621  ? 0.3198 0.3567 0.2820 0.0279  0.0419  -0.0223 619  LEU B CD2 
13382 N N   . ALA B 622  ? 0.2323 0.2716 0.2169 0.0191  0.0343  -0.0151 620  ALA B N   
13383 C CA  . ALA B 622  ? 0.2482 0.2855 0.2347 0.0172  0.0315  -0.0143 620  ALA B CA  
13384 C C   . ALA B 622  ? 0.2360 0.2747 0.2220 0.0155  0.0312  -0.0115 620  ALA B C   
13385 O O   . ALA B 622  ? 0.2268 0.2634 0.2107 0.0144  0.0290  -0.0112 620  ALA B O   
13386 C CB  . ALA B 622  ? 0.2136 0.2516 0.2067 0.0169  0.0308  -0.0141 620  ALA B CB  
13387 N N   . ALA B 623  ? 0.2296 0.2717 0.2174 0.0152  0.0333  -0.0094 621  ALA B N   
13388 C CA  . ALA B 623  ? 0.2383 0.2813 0.2252 0.0136  0.0331  -0.0065 621  ALA B CA  
13389 C C   . ALA B 623  ? 0.2563 0.2978 0.2363 0.0137  0.0328  -0.0068 621  ALA B C   
13390 O O   . ALA B 623  ? 0.2450 0.2851 0.2234 0.0125  0.0308  -0.0055 621  ALA B O   
13391 C CB  . ALA B 623  ? 0.2419 0.2890 0.2317 0.0131  0.0356  -0.0042 621  ALA B CB  
13392 N N   . ASP B 624  ? 0.2733 0.3149 0.2489 0.0152  0.0345  -0.0087 622  ASP B N   
13393 C CA  . ASP B 624  ? 0.2827 0.3226 0.2509 0.0153  0.0342  -0.0092 622  ASP B CA  
13394 C C   . ASP B 624  ? 0.2907 0.3268 0.2568 0.0145  0.0308  -0.0103 622  ASP B C   
13395 O O   . ASP B 624  ? 0.3761 0.4114 0.3383 0.0135  0.0294  -0.0093 622  ASP B O   
13396 C CB  . ASP B 624  ? 0.3338 0.3736 0.2975 0.0175  0.0364  -0.0116 622  ASP B CB  
13397 C CG  . ASP B 624  ? 0.4146 0.4590 0.3794 0.0184  0.0400  -0.0103 622  ASP B CG  
13398 O OD1 . ASP B 624  ? 0.4569 0.5043 0.4248 0.0168  0.0407  -0.0072 622  ASP B OD1 
13399 O OD2 . ASP B 624  ? 0.4301 0.4751 0.3925 0.0207  0.0422  -0.0123 622  ASP B OD2 
13400 N N   . ALA B 625  ? 0.2843 0.3184 0.2528 0.0148  0.0294  -0.0123 623  ALA B N   
13401 C CA  . ALA B 625  ? 0.3326 0.3637 0.2992 0.0139  0.0263  -0.0135 623  ALA B CA  
13402 C C   . ALA B 625  ? 0.2948 0.3265 0.2663 0.0125  0.0241  -0.0118 623  ALA B C   
13403 O O   . ALA B 625  ? 0.2960 0.3260 0.2667 0.0117  0.0216  -0.0125 623  ALA B O   
13404 C CB  . ALA B 625  ? 0.3717 0.3998 0.3374 0.0148  0.0258  -0.0166 623  ALA B CB  
13405 N N   . ALA B 626  ? 0.2657 0.2996 0.2420 0.0123  0.0251  -0.0097 624  ALA B N   
13406 C CA  . ALA B 626  ? 0.2552 0.2891 0.2358 0.0113  0.0231  -0.0083 624  ALA B CA  
13407 C C   . ALA B 626  ? 0.2628 0.2963 0.2408 0.0105  0.0208  -0.0071 624  ALA B C   
13408 O O   . ALA B 626  ? 0.2776 0.3105 0.2573 0.0101  0.0186  -0.0076 624  ALA B O   
13409 C CB  . ALA B 626  ? 0.2309 0.2667 0.2162 0.0111  0.0244  -0.0061 624  ALA B CB  
13410 N N   . PRO B 627  ? 0.2849 0.3189 0.2587 0.0102  0.0211  -0.0057 625  PRO B N   
13411 C CA  . PRO B 627  ? 0.2861 0.3198 0.2576 0.0095  0.0187  -0.0045 625  PRO B CA  
13412 C C   . PRO B 627  ? 0.3096 0.3421 0.2783 0.0091  0.0165  -0.0066 625  PRO B C   
13413 O O   . PRO B 627  ? 0.2665 0.2995 0.2364 0.0086  0.0141  -0.0060 625  PRO B O   
13414 C CB  . PRO B 627  ? 0.3066 0.3408 0.2733 0.0094  0.0198  -0.0027 625  PRO B CB  
13415 C CG  . PRO B 627  ? 0.3371 0.3726 0.3056 0.0098  0.0228  -0.0021 625  PRO B CG  
13416 C CD  . PRO B 627  ? 0.2968 0.3319 0.2679 0.0105  0.0238  -0.0047 625  PRO B CD  
13417 N N   . ASP B 628  ? 0.2754 0.3063 0.2404 0.0094  0.0174  -0.0090 626  ASP B N   
13418 C CA  . ASP B 628  ? 0.3174 0.3465 0.2792 0.0087  0.0152  -0.0111 626  ASP B CA  
13419 C C   . ASP B 628  ? 0.3067 0.3357 0.2734 0.0082  0.0136  -0.0118 626  ASP B C   
13420 O O   . ASP B 628  ? 0.2944 0.3236 0.2608 0.0070  0.0111  -0.0120 626  ASP B O   
13421 C CB  . ASP B 628  ? 0.3110 0.3374 0.2676 0.0093  0.0164  -0.0137 626  ASP B CB  
13422 C CG  . ASP B 628  ? 0.4049 0.4312 0.3553 0.0097  0.0176  -0.0132 626  ASP B CG  
13423 O OD1 . ASP B 628  ? 0.4142 0.4423 0.3640 0.0092  0.0173  -0.0108 626  ASP B OD1 
13424 O OD2 . ASP B 628  ? 0.4672 0.4913 0.4129 0.0106  0.0189  -0.0154 626  ASP B OD2 
13425 N N   . TRP B 629  ? 0.2417 0.2709 0.2131 0.0090  0.0151  -0.0122 627  TRP B N   
13426 C CA  . TRP B 629  ? 0.2286 0.2576 0.2042 0.0085  0.0137  -0.0130 627  TRP B CA  
13427 C C   . TRP B 629  ? 0.2326 0.2640 0.2123 0.0082  0.0123  -0.0109 627  TRP B C   
13428 O O   . TRP B 629  ? 0.2304 0.2624 0.2117 0.0075  0.0104  -0.0111 627  TRP B O   
13429 C CB  . TRP B 629  ? 0.2215 0.2498 0.2004 0.0095  0.0155  -0.0141 627  TRP B CB  
13430 C CG  . TRP B 629  ? 0.2289 0.2570 0.2119 0.0091  0.0143  -0.0147 627  TRP B CG  
13431 C CD1 . TRP B 629  ? 0.1989 0.2281 0.1874 0.0095  0.0147  -0.0139 627  TRP B CD1 
13432 C CD2 . TRP B 629  ? 0.2312 0.2578 0.2130 0.0080  0.0123  -0.0162 627  TRP B CD2 
13433 N NE1 . TRP B 629  ? 0.2031 0.2317 0.1936 0.0089  0.0133  -0.0149 627  TRP B NE1 
13434 C CE2 . TRP B 629  ? 0.2045 0.2317 0.1912 0.0079  0.0119  -0.0162 627  TRP B CE2 
13435 C CE3 . TRP B 629  ? 0.2352 0.2599 0.2120 0.0069  0.0108  -0.0175 627  TRP B CE3 
13436 C CZ2 . TRP B 629  ? 0.1925 0.2189 0.1794 0.0067  0.0101  -0.0172 627  TRP B CZ2 
13437 C CZ3 . TRP B 629  ? 0.2421 0.2657 0.2192 0.0054  0.0088  -0.0185 627  TRP B CZ3 
13438 C CH2 . TRP B 629  ? 0.2406 0.2652 0.2228 0.0054  0.0086  -0.0182 627  TRP B CH2 
13439 N N   . ALA B 630  ? 0.2325 0.2651 0.2137 0.0088  0.0133  -0.0087 628  ALA B N   
13440 C CA  . ALA B 630  ? 0.2411 0.2753 0.2257 0.0089  0.0120  -0.0068 628  ALA B CA  
13441 C C   . ALA B 630  ? 0.2715 0.3069 0.2536 0.0082  0.0096  -0.0062 628  ALA B C   
13442 O O   . ALA B 630  ? 0.2648 0.3020 0.2499 0.0084  0.0079  -0.0053 628  ALA B O   
13443 C CB  . ALA B 630  ? 0.2699 0.3044 0.2556 0.0095  0.0133  -0.0045 628  ALA B CB  
13444 N N   . ALA B 631  ? 0.2587 0.2935 0.2354 0.0076  0.0093  -0.0066 629  ALA B N   
13445 C CA  . ALA B 631  ? 0.2567 0.2929 0.2307 0.0068  0.0068  -0.0060 629  ALA B CA  
13446 C C   . ALA B 631  ? 0.2685 0.3051 0.2427 0.0055  0.0048  -0.0076 629  ALA B C   
13447 O O   . ALA B 631  ? 0.2638 0.3024 0.2369 0.0046  0.0025  -0.0069 629  ALA B O   
13448 C CB  . ALA B 631  ? 0.2854 0.3204 0.2529 0.0065  0.0072  -0.0059 629  ALA B CB  
13449 N N   . VAL B 632  ? 0.2253 0.2602 0.2008 0.0053  0.0056  -0.0096 630  VAL B N   
13450 C CA  . VAL B 632  ? 0.2562 0.2914 0.2324 0.0038  0.0037  -0.0109 630  VAL B CA  
13451 C C   . VAL B 632  ? 0.2608 0.2995 0.2427 0.0042  0.0027  -0.0094 630  VAL B C   
13452 O O   . VAL B 632  ? 0.2355 0.2742 0.2214 0.0055  0.0042  -0.0090 630  VAL B O   
13453 C CB  . VAL B 632  ? 0.2652 0.2972 0.2410 0.0036  0.0048  -0.0133 630  VAL B CB  
13454 C CG1 . VAL B 632  ? 0.2440 0.2761 0.2206 0.0018  0.0027  -0.0142 630  VAL B CG1 
13455 C CG2 . VAL B 632  ? 0.2562 0.2846 0.2259 0.0038  0.0058  -0.0148 630  VAL B CG2 
13456 N N   . PRO B 633  ? 0.2187 0.2606 0.2012 0.0031  0.0004  -0.0087 631  PRO B N   
13457 C CA  . PRO B 633  ? 0.2026 0.2482 0.1903 0.0040  -0.0003 -0.0072 631  PRO B CA  
13458 C C   . PRO B 633  ? 0.2416 0.2867 0.2333 0.0042  0.0007  -0.0083 631  PRO B C   
13459 O O   . PRO B 633  ? 0.2243 0.2673 0.2148 0.0029  0.0008  -0.0100 631  PRO B O   
13460 C CB  . PRO B 633  ? 0.2239 0.2732 0.2111 0.0024  -0.0031 -0.0066 631  PRO B CB  
13461 C CG  . PRO B 633  ? 0.2579 0.3054 0.2391 0.0012  -0.0039 -0.0068 631  PRO B CG  
13462 C CD  . PRO B 633  ? 0.2387 0.2810 0.2166 0.0013  -0.0018 -0.0088 631  PRO B CD  
13463 N N   . PRO B 634  ? 0.2387 0.2854 0.2348 0.0059  0.0013  -0.0072 632  PRO B N   
13464 C CA  . PRO B 634  ? 0.2388 0.2851 0.2385 0.0062  0.0022  -0.0082 632  PRO B CA  
13465 C C   . PRO B 634  ? 0.2140 0.2617 0.2141 0.0042  0.0010  -0.0092 632  PRO B C   
13466 O O   . PRO B 634  ? 0.2071 0.2524 0.2075 0.0036  0.0017  -0.0107 632  PRO B O   
13467 C CB  . PRO B 634  ? 0.2367 0.2853 0.2403 0.0083  0.0023  -0.0066 632  PRO B CB  
13468 C CG  . PRO B 634  ? 0.2782 0.3261 0.2800 0.0094  0.0024  -0.0051 632  PRO B CG  
13469 C CD  . PRO B 634  ? 0.2415 0.2899 0.2390 0.0078  0.0012  -0.0051 632  PRO B CD  
13470 N N   . SER B 635  ? 0.2191 0.2708 0.2194 0.0032  -0.0010 -0.0083 633  SER B N   
13471 C CA  . SER B 635  ? 0.2147 0.2681 0.2154 0.0008  -0.0023 -0.0090 633  SER B CA  
13472 C C   . SER B 635  ? 0.2024 0.2513 0.1986 -0.0013 -0.0025 -0.0108 633  SER B C   
13473 O O   . SER B 635  ? 0.2162 0.2639 0.2126 -0.0029 -0.0028 -0.0119 633  SER B O   
13474 C CB  . SER B 635  ? 0.2308 0.2901 0.2326 -0.0002 -0.0045 -0.0075 633  SER B CB  
13475 O OG  . SER B 635  ? 0.3489 0.4078 0.3469 -0.0009 -0.0057 -0.0071 633  SER B OG  
13476 N N   . GLU B 636  ? 0.2092 0.2552 0.2010 -0.0013 -0.0025 -0.0112 634  GLU B N   
13477 C CA  . GLU B 636  ? 0.2233 0.2643 0.2102 -0.0029 -0.0026 -0.0132 634  GLU B CA  
13478 C C   . GLU B 636  ? 0.2247 0.2614 0.2118 -0.0015 -0.0004 -0.0146 634  GLU B C   
13479 O O   . GLU B 636  ? 0.2159 0.2489 0.2009 -0.0026 -0.0005 -0.0163 634  GLU B O   
13480 C CB  . GLU B 636  ? 0.2341 0.2736 0.2158 -0.0032 -0.0032 -0.0132 634  GLU B CB  
13481 C CG  . GLU B 636  ? 0.3510 0.3847 0.3268 -0.0043 -0.0032 -0.0155 634  GLU B CG  
13482 C CD  . GLU B 636  ? 0.4059 0.4380 0.3805 -0.0071 -0.0051 -0.0167 634  GLU B CD  
13483 O OE1 . GLU B 636  ? 0.3472 0.3832 0.3232 -0.0092 -0.0073 -0.0156 634  GLU B OE1 
13484 O OE2 . GLU B 636  ? 0.3543 0.3813 0.3266 -0.0071 -0.0044 -0.0185 634  GLU B OE2 
13485 N N   . ARG B 637  ? 0.2048 0.2418 0.1943 0.0009  0.0016  -0.0139 635  ARG B N   
13486 C CA  . ARG B 637  ? 0.1872 0.2211 0.1780 0.0021  0.0035  -0.0150 635  ARG B CA  
13487 C C   . ARG B 637  ? 0.1902 0.2245 0.1841 0.0014  0.0032  -0.0155 635  ARG B C   
13488 O O   . ARG B 637  ? 0.2008 0.2318 0.1939 0.0012  0.0037  -0.0170 635  ARG B O   
13489 C CB  . ARG B 637  ? 0.1995 0.2341 0.1927 0.0043  0.0053  -0.0139 635  ARG B CB  
13490 C CG  . ARG B 637  ? 0.1974 0.2319 0.1874 0.0048  0.0058  -0.0131 635  ARG B CG  
13491 C CD  . ARG B 637  ? 0.1779 0.2122 0.1699 0.0066  0.0078  -0.0121 635  ARG B CD  
13492 N NE  . ARG B 637  ? 0.2066 0.2430 0.2030 0.0075  0.0076  -0.0106 635  ARG B NE  
13493 C CZ  . ARG B 637  ? 0.2645 0.3023 0.2615 0.0084  0.0074  -0.0087 635  ARG B CZ  
13494 N NH1 . ARG B 637  ? 0.2770 0.3149 0.2706 0.0083  0.0072  -0.0078 635  ARG B NH1 
13495 N NH2 . ARG B 637  ? 0.2217 0.2605 0.2226 0.0095  0.0075  -0.0077 635  ARG B NH2 
13496 N N   . ALA B 638  ? 0.1820 0.2206 0.1796 0.0013  0.0023  -0.0142 636  ALA B N   
13497 C CA  . ALA B 638  ? 0.1813 0.2208 0.1816 0.0005  0.0020  -0.0144 636  ALA B CA  
13498 C C   . ALA B 638  ? 0.1969 0.2348 0.1943 -0.0022 0.0005  -0.0155 636  ALA B C   
13499 O O   . ALA B 638  ? 0.1828 0.2186 0.1806 -0.0030 0.0006  -0.0163 636  ALA B O   
13500 C CB  . ALA B 638  ? 0.2007 0.2456 0.2051 0.0012  0.0016  -0.0128 636  ALA B CB  
13501 N N   . ALA B 639  ? 0.1706 0.2090 0.1648 -0.0039 -0.0012 -0.0153 637  ALA B N   
13502 C CA  . ALA B 639  ? 0.1963 0.2322 0.1870 -0.0069 -0.0029 -0.0163 637  ALA B CA  
13503 C C   . ALA B 639  ? 0.1867 0.2158 0.1738 -0.0065 -0.0020 -0.0184 637  ALA B C   
13504 O O   . ALA B 639  ? 0.1825 0.2086 0.1680 -0.0083 -0.0029 -0.0193 637  ALA B O   
13505 C CB  . ALA B 639  ? 0.1978 0.2349 0.1850 -0.0087 -0.0049 -0.0159 637  ALA B CB  
13506 N N   . CYS B 640  ? 0.1827 0.2094 0.1684 -0.0042 -0.0003 -0.0190 638  CYS B N   
13507 C CA  . CYS B 640  ? 0.1926 0.2135 0.1755 -0.0033 0.0008  -0.0209 638  CYS B CA  
13508 C C   . CYS B 640  ? 0.1620 0.1823 0.1484 -0.0026 0.0016  -0.0211 638  CYS B C   
13509 O O   . CYS B 640  ? 0.1828 0.1986 0.1671 -0.0032 0.0013  -0.0225 638  CYS B O   
13510 C CB  . CYS B 640  ? 0.2003 0.2203 0.1821 -0.0007 0.0028  -0.0212 638  CYS B CB  
13511 S SG  . CYS B 640  ? 0.2168 0.2361 0.1929 -0.0011 0.0021  -0.0213 638  CYS B SG  
13512 N N   . LEU B 641  ? 0.1659 0.1901 0.1574 -0.0014 0.0026  -0.0199 639  LEU B N   
13513 C CA  . LEU B 641  ? 0.1674 0.1910 0.1620 -0.0009 0.0032  -0.0200 639  LEU B CA  
13514 C C   . LEU B 641  ? 0.1604 0.1839 0.1547 -0.0034 0.0016  -0.0200 639  LEU B C   
13515 O O   . LEU B 641  ? 0.1824 0.2025 0.1761 -0.0037 0.0016  -0.0209 639  LEU B O   
13516 C CB  . LEU B 641  ? 0.1646 0.1924 0.1642 0.0008  0.0043  -0.0187 639  LEU B CB  
13517 C CG  . LEU B 641  ? 0.1755 0.2024 0.1765 0.0032  0.0062  -0.0187 639  LEU B CG  
13518 C CD1 . LEU B 641  ? 0.2153 0.2416 0.2135 0.0038  0.0068  -0.0187 639  LEU B CD1 
13519 C CD2 . LEU B 641  ? 0.1742 0.2043 0.1796 0.0044  0.0068  -0.0174 639  LEU B CD2 
13520 N N   . ASP B 642  ? 0.1762 0.2036 0.1710 -0.0053 0.0001  -0.0189 640  ASP B N   
13521 C CA  . ASP B 642  ? 0.1537 0.1817 0.1483 -0.0081 -0.0014 -0.0186 640  ASP B CA  
13522 C C   . ASP B 642  ? 0.1888 0.2106 0.1781 -0.0102 -0.0028 -0.0201 640  ASP B C   
13523 O O   . ASP B 642  ? 0.1865 0.2059 0.1752 -0.0117 -0.0035 -0.0203 640  ASP B O   
13524 C CB  . ASP B 642  ? 0.1849 0.2191 0.1812 -0.0099 -0.0028 -0.0170 640  ASP B CB  
13525 C CG  . ASP B 642  ? 0.1921 0.2322 0.1938 -0.0081 -0.0018 -0.0156 640  ASP B CG  
13526 O OD1 . ASP B 642  ? 0.1909 0.2302 0.1949 -0.0065 -0.0004 -0.0158 640  ASP B OD1 
13527 O OD2 . ASP B 642  ? 0.1993 0.2448 0.2027 -0.0084 -0.0025 -0.0142 640  ASP B OD2 
13528 N N   . ARG B 643  ? 0.1995 0.2184 0.1845 -0.0101 -0.0032 -0.0210 641  ARG B N   
13529 C CA  . ARG B 643  ? 0.2132 0.2253 0.1925 -0.0115 -0.0045 -0.0226 641  ARG B CA  
13530 C C   . ARG B 643  ? 0.2041 0.2109 0.1828 -0.0095 -0.0032 -0.0240 641  ARG B C   
13531 O O   . ARG B 643  ? 0.2107 0.2125 0.1866 -0.0110 -0.0043 -0.0249 641  ARG B O   
13532 C CB  . ARG B 643  ? 0.2170 0.2268 0.1915 -0.0114 -0.0049 -0.0235 641  ARG B CB  
13533 C CG  . ARG B 643  ? 0.2341 0.2472 0.2073 -0.0144 -0.0072 -0.0225 641  ARG B CG  
13534 C CD  . ARG B 643  ? 0.2646 0.2740 0.2317 -0.0146 -0.0081 -0.0237 641  ARG B CD  
13535 N NE  . ARG B 643  ? 0.2647 0.2760 0.2325 -0.0115 -0.0061 -0.0236 641  ARG B NE  
13536 C CZ  . ARG B 643  ? 0.3099 0.3268 0.2797 -0.0113 -0.0062 -0.0220 641  ARG B CZ  
13537 N NH1 . ARG B 643  ? 0.2510 0.2728 0.2227 -0.0138 -0.0082 -0.0204 641  ARG B NH1 
13538 N NH2 . ARG B 643  ? 0.2838 0.3017 0.2539 -0.0086 -0.0043 -0.0218 641  ARG B NH2 
13539 N N   . ALA B 644  ? 0.1932 0.2011 0.1745 -0.0062 -0.0009 -0.0242 642  ALA B N   
13540 C CA  . ALA B 644  ? 0.1992 0.2031 0.1807 -0.0042 0.0003  -0.0253 642  ALA B CA  
13541 C C   . ALA B 644  ? 0.2036 0.2077 0.1876 -0.0053 -0.0002 -0.0247 642  ALA B C   
13542 O O   . ALA B 644  ? 0.2065 0.2055 0.1886 -0.0051 -0.0006 -0.0257 642  ALA B O   
13543 C CB  . ALA B 644  ? 0.1769 0.1832 0.1616 -0.0009 0.0027  -0.0251 642  ALA B CB  
13544 N N   . ALA B 645  ? 0.1921 0.2019 0.1805 -0.0062 -0.0003 -0.0231 643  ALA B N   
13545 C CA  . ALA B 645  ? 0.1651 0.1755 0.1556 -0.0073 -0.0007 -0.0224 643  ALA B CA  
13546 C C   . ALA B 645  ? 0.1924 0.1992 0.1791 -0.0107 -0.0028 -0.0226 643  ALA B C   
13547 O O   . ALA B 645  ? 0.2032 0.2066 0.1892 -0.0112 -0.0032 -0.0228 643  ALA B O   
13548 C CB  . ALA B 645  ? 0.1825 0.1999 0.1778 -0.0074 -0.0002 -0.0207 643  ALA B CB  
13549 N N   . GLU B 646  ? 0.2025 0.2097 0.1864 -0.0131 -0.0043 -0.0224 644  GLU B N   
13550 C CA  . GLU B 646  ? 0.2378 0.2410 0.2176 -0.0167 -0.0067 -0.0225 644  GLU B CA  
13551 C C   . GLU B 646  ? 0.2325 0.2268 0.2073 -0.0158 -0.0070 -0.0244 644  GLU B C   
13552 O O   . GLU B 646  ? 0.2257 0.2156 0.1982 -0.0177 -0.0083 -0.0245 644  GLU B O   
13553 C CB  . GLU B 646  ? 0.2269 0.2318 0.2043 -0.0193 -0.0084 -0.0221 644  GLU B CB  
13554 C CG  . GLU B 646  ? 0.2618 0.2757 0.2439 -0.0207 -0.0086 -0.0200 644  GLU B CG  
13555 C CD  . GLU B 646  ? 0.3274 0.3445 0.3123 -0.0230 -0.0090 -0.0186 644  GLU B CD  
13556 O OE1 . GLU B 646  ? 0.3911 0.4041 0.3728 -0.0261 -0.0107 -0.0186 644  GLU B OE1 
13557 O OE2 . GLU B 646  ? 0.3495 0.3729 0.3396 -0.0216 -0.0076 -0.0174 644  GLU B OE2 
13558 N N   . LEU B 647  ? 0.2023 0.1940 0.1754 -0.0128 -0.0058 -0.0259 645  LEU B N   
13559 C CA  . LEU B 647  ? 0.2275 0.2110 0.1958 -0.0113 -0.0060 -0.0279 645  LEU B CA  
13560 C C   . LEU B 647  ? 0.2345 0.2164 0.2052 -0.0094 -0.0050 -0.0279 645  LEU B C   
13561 O O   . LEU B 647  ? 0.2352 0.2105 0.2024 -0.0098 -0.0062 -0.0287 645  LEU B O   
13562 C CB  . LEU B 647  ? 0.2231 0.2054 0.1893 -0.0083 -0.0046 -0.0293 645  LEU B CB  
13563 C CG  . LEU B 647  ? 0.2387 0.2210 0.2010 -0.0101 -0.0058 -0.0296 645  LEU B CG  
13564 C CD1 . LEU B 647  ? 0.2443 0.2256 0.2046 -0.0068 -0.0041 -0.0309 645  LEU B CD1 
13565 C CD2 . LEU B 647  ? 0.2747 0.2502 0.2306 -0.0134 -0.0087 -0.0304 645  LEU B CD2 
13566 N N   . MET B 648  ? 0.1922 0.1796 0.1686 -0.0072 -0.0031 -0.0271 646  MET B N   
13567 C CA  . MET B 648  ? 0.2131 0.1993 0.1919 -0.0056 -0.0024 -0.0270 646  MET B CA  
13568 C C   . MET B 648  ? 0.2067 0.1920 0.1853 -0.0087 -0.0040 -0.0260 646  MET B C   
13569 O O   . MET B 648  ? 0.2245 0.2053 0.2019 -0.0082 -0.0044 -0.0263 646  MET B O   
13570 C CB  . MET B 648  ? 0.1991 0.1914 0.1838 -0.0033 -0.0003 -0.0262 646  MET B CB  
13571 C CG  . MET B 648  ? 0.2176 0.2102 0.2027 -0.0002 0.0014  -0.0271 646  MET B CG  
13572 S SD  . MET B 648  ? 0.2119 0.2098 0.2035 0.0023  0.0034  -0.0262 646  MET B SD  
13573 C CE  . MET B 648  ? 0.2274 0.2256 0.2186 0.0053  0.0052  -0.0271 646  MET B CE  
13574 N N   . GLN B 649  ? 0.2033 0.1934 0.1833 -0.0117 -0.0048 -0.0245 647  GLN B N   
13575 C CA  . GLN B 649  ? 0.2123 0.2022 0.1920 -0.0149 -0.0061 -0.0232 647  GLN B CA  
13576 C C   . GLN B 649  ? 0.2269 0.2087 0.2005 -0.0172 -0.0083 -0.0240 647  GLN B C   
13577 O O   . GLN B 649  ? 0.2321 0.2099 0.2043 -0.0180 -0.0091 -0.0237 647  GLN B O   
13578 C CB  . GLN B 649  ? 0.2134 0.2108 0.1959 -0.0176 -0.0065 -0.0215 647  GLN B CB  
13579 C CG  . GLN B 649  ? 0.2363 0.2352 0.2194 -0.0208 -0.0075 -0.0199 647  GLN B CG  
13580 C CD  . GLN B 649  ? 0.2303 0.2318 0.2172 -0.0189 -0.0059 -0.0193 647  GLN B CD  
13581 O OE1 . GLN B 649  ? 0.2310 0.2393 0.2225 -0.0175 -0.0045 -0.0186 647  GLN B OE1 
13582 N NE2 . GLN B 649  ? 0.2329 0.2287 0.2178 -0.0187 -0.0064 -0.0197 647  GLN B NE2 
13583 N N   . ALA B 650  ? 0.2273 0.2064 0.1969 -0.0183 -0.0095 -0.0249 648  ALA B N   
13584 C CA  . ALA B 650  ? 0.2590 0.2294 0.2219 -0.0206 -0.0118 -0.0258 648  ALA B CA  
13585 C C   . ALA B 650  ? 0.2765 0.2390 0.2363 -0.0175 -0.0116 -0.0275 648  ALA B C   
13586 O O   . ALA B 650  ? 0.3088 0.2640 0.2642 -0.0191 -0.0134 -0.0277 648  ALA B O   
13587 C CB  . ALA B 650  ? 0.2853 0.2542 0.2442 -0.0219 -0.0130 -0.0267 648  ALA B CB  
13588 N N   . ARG B 651  ? 0.2614 0.2253 0.2236 -0.0130 -0.0094 -0.0285 649  ARG B N   
13589 C CA  . ARG B 651  ? 0.2635 0.2208 0.2232 -0.0095 -0.0089 -0.0302 649  ARG B CA  
13590 C C   . ARG B 651  ? 0.2536 0.2127 0.2177 -0.0074 -0.0078 -0.0295 649  ARG B C   
13591 O O   . ARG B 651  ? 0.2706 0.2261 0.2341 -0.0039 -0.0072 -0.0307 649  ARG B O   
13592 C CB  . ARG B 651  ? 0.2580 0.2155 0.2170 -0.0059 -0.0073 -0.0319 649  ARG B CB  
13593 C CG  . ARG B 651  ? 0.2665 0.2211 0.2201 -0.0081 -0.0087 -0.0327 649  ARG B CG  
13594 C CD  . ARG B 651  ? 0.2785 0.2342 0.2313 -0.0049 -0.0070 -0.0341 649  ARG B CD  
13595 N NE  . ARG B 651  ? 0.3030 0.2568 0.2508 -0.0074 -0.0085 -0.0347 649  ARG B NE  
13596 C CZ  . ARG B 651  ? 0.3283 0.2835 0.2746 -0.0057 -0.0074 -0.0357 649  ARG B CZ  
13597 N NH1 . ARG B 651  ? 0.2752 0.2336 0.2245 -0.0016 -0.0047 -0.0361 649  ARG B NH1 
13598 N NH2 . ARG B 651  ? 0.3053 0.2588 0.2469 -0.0084 -0.0091 -0.0360 649  ARG B NH2 
13599 N N   . MET B 652  ? 0.2378 0.2026 0.2062 -0.0094 -0.0077 -0.0276 650  MET B N   
13600 C CA  . MET B 652  ? 0.2349 0.2016 0.2072 -0.0076 -0.0067 -0.0270 650  MET B CA  
13601 C C   . MET B 652  ? 0.2377 0.1967 0.2067 -0.0065 -0.0079 -0.0276 650  MET B C   
13602 O O   . MET B 652  ? 0.2597 0.2188 0.2310 -0.0031 -0.0068 -0.0281 650  MET B O   
13603 C CB  . MET B 652  ? 0.2104 0.1831 0.1862 -0.0104 -0.0067 -0.0249 650  MET B CB  
13604 C CG  . MET B 652  ? 0.2334 0.2074 0.2124 -0.0090 -0.0061 -0.0242 650  MET B CG  
13605 S SD  . MET B 652  ? 0.2624 0.2438 0.2452 -0.0118 -0.0058 -0.0220 650  MET B SD  
13606 C CE  . MET B 652  ? 0.2273 0.2169 0.2149 -0.0101 -0.0038 -0.0220 650  MET B CE  
13607 N N   . PRO B 653  ? 0.2451 0.1969 0.2085 -0.0091 -0.0101 -0.0277 651  PRO B N   
13608 C CA  . PRO B 653  ? 0.2899 0.2340 0.2501 -0.0076 -0.0113 -0.0282 651  PRO B CA  
13609 C C   . PRO B 653  ? 0.2517 0.1923 0.2109 -0.0027 -0.0103 -0.0302 651  PRO B C   
13610 O O   . PRO B 653  ? 0.2704 0.2097 0.2311 0.0002  -0.0099 -0.0304 651  PRO B O   
13611 C CB  . PRO B 653  ? 0.2870 0.2236 0.2406 -0.0116 -0.0140 -0.0280 651  PRO B CB  
13612 C CG  . PRO B 653  ? 0.3150 0.2581 0.2708 -0.0161 -0.0142 -0.0263 651  PRO B CG  
13613 C CD  . PRO B 653  ? 0.2769 0.2279 0.2372 -0.0140 -0.0120 -0.0268 651  PRO B CD  
13614 N N   . THR B 654  ? 0.2594 0.1991 0.2163 -0.0017 -0.0098 -0.0317 652  THR B N   
13615 C CA  . THR B 654  ? 0.2733 0.2105 0.2292 0.0031  -0.0086 -0.0337 652  THR B CA  
13616 C C   . THR B 654  ? 0.2743 0.2196 0.2373 0.0063  -0.0060 -0.0334 652  THR B C   
13617 O O   . THR B 654  ? 0.2866 0.2310 0.2509 0.0102  -0.0051 -0.0341 652  THR B O   
13618 C CB  . THR B 654  ? 0.3064 0.2412 0.2579 0.0031  -0.0086 -0.0353 652  THR B CB  
13619 O OG1 . THR B 654  ? 0.3200 0.2469 0.2647 -0.0003 -0.0113 -0.0356 652  THR B OG1 
13620 C CG2 . THR B 654  ? 0.2877 0.2202 0.2379 0.0083  -0.0070 -0.0374 652  THR B CG2 
13621 N N   . LEU B 655  ? 0.2504 0.2036 0.2178 0.0048  -0.0048 -0.0322 653  LEU B N   
13622 C CA  . LEU B 655  ? 0.2319 0.1923 0.2057 0.0072  -0.0025 -0.0317 653  LEU B CA  
13623 C C   . LEU B 655  ? 0.2676 0.2285 0.2445 0.0081  -0.0028 -0.0308 653  LEU B C   
13624 O O   . LEU B 655  ? 0.2340 0.1975 0.2146 0.0113  -0.0015 -0.0310 653  LEU B O   
13625 C CB  . LEU B 655  ? 0.2410 0.2089 0.2185 0.0051  -0.0016 -0.0305 653  LEU B CB  
13626 C CG  . LEU B 655  ? 0.2494 0.2178 0.2242 0.0040  -0.0015 -0.0311 653  LEU B CG  
13627 C CD1 . LEU B 655  ? 0.2435 0.2195 0.2224 0.0023  -0.0007 -0.0296 653  LEU B CD1 
13628 C CD2 . LEU B 655  ? 0.3067 0.2737 0.2800 0.0076  -0.0001 -0.0327 653  LEU B CD2 
13629 N N   . LEU B 656  ? 0.2469 0.2056 0.2225 0.0051  -0.0045 -0.0297 654  LEU B N   
13630 C CA  . LEU B 656  ? 0.2649 0.2233 0.2425 0.0058  -0.0050 -0.0288 654  LEU B CA  
13631 C C   . LEU B 656  ? 0.2621 0.2153 0.2382 0.0094  -0.0054 -0.0300 654  LEU B C   
13632 O O   . LEU B 656  ? 0.2787 0.2344 0.2585 0.0120  -0.0047 -0.0297 654  LEU B O   
13633 C CB  . LEU B 656  ? 0.2941 0.2497 0.2691 0.0019  -0.0070 -0.0275 654  LEU B CB  
13634 C CG  . LEU B 656  ? 0.3201 0.2808 0.2966 -0.0020 -0.0069 -0.0261 654  LEU B CG  
13635 C CD1 . LEU B 656  ? 0.3047 0.2628 0.2790 -0.0053 -0.0086 -0.0246 654  LEU B CD1 
13636 C CD2 . LEU B 656  ? 0.2882 0.2572 0.2708 -0.0008 -0.0049 -0.0255 654  LEU B CD2 
13637 N N   . GLY B 657  ? 0.2880 0.2336 0.2581 0.0098  -0.0066 -0.0312 655  GLY B N   
13638 C CA  . GLY B 657  ? 0.2777 0.2177 0.2458 0.0136  -0.0070 -0.0324 655  GLY B CA  
13639 C C   . GLY B 657  ? 0.3108 0.2557 0.2831 0.0180  -0.0048 -0.0333 655  GLY B C   
13640 O O   . GLY B 657  ? 0.2826 0.2278 0.2573 0.0211  -0.0047 -0.0333 655  GLY B O   
13641 N N   . LEU B 658  ? 0.2694 0.2188 0.2430 0.0182  -0.0030 -0.0339 656  LEU B N   
13642 C CA  . LEU B 658  ? 0.2246 0.1792 0.2024 0.0221  -0.0007 -0.0345 656  LEU B CA  
13643 C C   . LEU B 658  ? 0.2490 0.2109 0.2338 0.0222  0.0002  -0.0329 656  LEU B C   
13644 O O   . LEU B 658  ? 0.2422 0.2064 0.2304 0.0254  0.0009  -0.0330 656  LEU B O   
13645 C CB  . LEU B 658  ? 0.2432 0.2006 0.2202 0.0218  0.0009  -0.0352 656  LEU B CB  
13646 C CG  . LEU B 658  ? 0.2462 0.2091 0.2268 0.0254  0.0035  -0.0357 656  LEU B CG  
13647 C CD1 . LEU B 658  ? 0.2205 0.1797 0.1995 0.0299  0.0037  -0.0371 656  LEU B CD1 
13648 C CD2 . LEU B 658  ? 0.2327 0.1974 0.2114 0.0247  0.0047  -0.0363 656  LEU B CD2 
13649 N N   . ILE B 659  ? 0.2165 0.1821 0.2034 0.0187  0.0000  -0.0315 657  ILE B N   
13650 C CA  . ILE B 659  ? 0.1762 0.1482 0.1692 0.0187  0.0007  -0.0302 657  ILE B CA  
13651 C C   . ILE B 659  ? 0.2139 0.1836 0.2077 0.0198  -0.0007 -0.0298 657  ILE B C   
13652 O O   . ILE B 659  ? 0.2261 0.1998 0.2245 0.0217  -0.0001 -0.0294 657  ILE B O   
13653 C CB  . ILE B 659  ? 0.1953 0.1708 0.1895 0.0150  0.0006  -0.0290 657  ILE B CB  
13654 C CG1 . ILE B 659  ? 0.2102 0.1891 0.2047 0.0145  0.0021  -0.0293 657  ILE B CG1 
13655 C CG2 . ILE B 659  ? 0.2420 0.2223 0.2412 0.0148  0.0009  -0.0278 657  ILE B CG2 
13656 C CD1 . ILE B 659  ? 0.2329 0.2143 0.2274 0.0110  0.0018  -0.0283 657  ILE B CD1 
13657 N N   . ILE B 660  ? 0.2169 0.1801 0.2061 0.0184  -0.0027 -0.0297 658  ILE B N   
13658 C CA  . ILE B 660  ? 0.2132 0.1735 0.2024 0.0193  -0.0042 -0.0291 658  ILE B CA  
13659 C C   . ILE B 660  ? 0.2393 0.1991 0.2299 0.0239  -0.0038 -0.0301 658  ILE B C   
13660 O O   . ILE B 660  ? 0.2426 0.2049 0.2369 0.0255  -0.0041 -0.0294 658  ILE B O   
13661 C CB  . ILE B 660  ? 0.2371 0.1897 0.2203 0.0170  -0.0065 -0.0289 658  ILE B CB  
13662 C CG1 . ILE B 660  ? 0.2217 0.1764 0.2049 0.0125  -0.0069 -0.0275 658  ILE B CG1 
13663 C CG2 . ILE B 660  ? 0.2509 0.1986 0.2327 0.0189  -0.0082 -0.0287 658  ILE B CG2 
13664 C CD1 . ILE B 660  ? 0.2863 0.2340 0.2635 0.0095  -0.0089 -0.0271 658  ILE B CD1 
13665 N N   . ARG B 661  ? 0.2310 0.1876 0.2186 0.0261  -0.0032 -0.0316 659  ARG B N   
13666 C CA  . ARG B 661  ? 0.2397 0.1953 0.2279 0.0308  -0.0029 -0.0326 659  ARG B CA  
13667 C C   . ARG B 661  ? 0.2560 0.2199 0.2501 0.0333  -0.0004 -0.0327 659  ARG B C   
13668 O O   . ARG B 661  ? 0.2451 0.2114 0.2426 0.0366  -0.0002 -0.0326 659  ARG B O   
13669 C CB  . ARG B 661  ? 0.2482 0.1959 0.2297 0.0325  -0.0034 -0.0343 659  ARG B CB  
13670 C CG  . ARG B 661  ? 0.2854 0.2240 0.2613 0.0312  -0.0062 -0.0341 659  ARG B CG  
13671 C CD  . ARG B 661  ? 0.2979 0.2275 0.2664 0.0323  -0.0071 -0.0359 659  ARG B CD  
13672 N NE  . ARG B 661  ? 0.3145 0.2432 0.2829 0.0380  -0.0060 -0.0375 659  ARG B NE  
13673 C CZ  . ARG B 661  ? 0.3493 0.2777 0.3155 0.0400  -0.0044 -0.0393 659  ARG B CZ  
13674 N NH1 . ARG B 661  ? 0.3412 0.2699 0.3051 0.0369  -0.0038 -0.0397 659  ARG B NH1 
13675 N NH2 . ARG B 661  ? 0.3406 0.2686 0.3069 0.0455  -0.0033 -0.0407 659  ARG B NH2 
13676 N N   . GLU B 662  ? 0.2192 0.1878 0.2149 0.0315  0.0013  -0.0326 660  GLU B N   
13677 C CA  . GLU B 662  ? 0.2034 0.1796 0.2045 0.0335  0.0036  -0.0324 660  GLU B CA  
13678 C C   . GLU B 662  ? 0.2353 0.2181 0.2427 0.0323  0.0037  -0.0308 660  GLU B C   
13679 O O   . GLU B 662  ? 0.2266 0.2148 0.2389 0.0345  0.0048  -0.0304 660  GLU B O   
13680 C CB  . GLU B 662  ? 0.2447 0.2230 0.2445 0.0323  0.0054  -0.0329 660  GLU B CB  
13681 C CG  . GLU B 662  ? 0.2324 0.2183 0.2372 0.0343  0.0079  -0.0327 660  GLU B CG  
13682 C CD  . GLU B 662  ? 0.2034 0.1912 0.2066 0.0332  0.0096  -0.0330 660  GLU B CD  
13683 O OE1 . GLU B 662  ? 0.2236 0.2095 0.2241 0.0300  0.0089  -0.0328 660  GLU B OE1 
13684 O OE2 . GLU B 662  ? 0.2081 0.1997 0.2128 0.0356  0.0117  -0.0334 660  GLU B OE2 
13685 N N   . ALA B 663  ? 0.1970 0.1794 0.2042 0.0288  0.0026  -0.0298 661  ALA B N   
13686 C CA  . ALA B 663  ? 0.1878 0.1760 0.2002 0.0273  0.0028  -0.0284 661  ALA B CA  
13687 C C   . ALA B 663  ? 0.2149 0.2016 0.2279 0.0263  0.0008  -0.0276 661  ALA B C   
13688 O O   . ALA B 663  ? 0.2586 0.2490 0.2747 0.0245  0.0007  -0.0265 661  ALA B O   
13689 C CB  . ALA B 663  ? 0.2031 0.1938 0.2155 0.0242  0.0037  -0.0280 661  ALA B CB  
13690 N N   . GLY B 664  ? 0.2314 0.2123 0.2408 0.0273  -0.0009 -0.0279 662  GLY B N   
13691 C CA  . GLY B 664  ? 0.2495 0.2289 0.2593 0.0265  -0.0028 -0.0269 662  GLY B CA  
13692 C C   . GLY B 664  ? 0.2516 0.2297 0.2593 0.0226  -0.0037 -0.0261 662  GLY B C   
13693 O O   . GLY B 664  ? 0.2362 0.2149 0.2449 0.0217  -0.0048 -0.0252 662  GLY B O   
13694 N N   . LYS B 665  ? 0.2206 0.1972 0.2252 0.0205  -0.0031 -0.0264 663  LYS B N   
13695 C CA  . LYS B 665  ? 0.2439 0.2206 0.2471 0.0169  -0.0036 -0.0255 663  LYS B CA  
13696 C C   . LYS B 665  ? 0.2202 0.1904 0.2182 0.0153  -0.0055 -0.0252 663  LYS B C   
13697 O O   . LYS B 665  ? 0.2183 0.1830 0.2124 0.0161  -0.0062 -0.0259 663  LYS B O   
13698 C CB  . LYS B 665  ? 0.2032 0.1824 0.2061 0.0151  -0.0022 -0.0257 663  LYS B CB  
13699 C CG  . LYS B 665  ? 0.2237 0.2088 0.2312 0.0164  -0.0003 -0.0259 663  LYS B CG  
13700 C CD  . LYS B 665  ? 0.2734 0.2630 0.2850 0.0159  -0.0002 -0.0250 663  LYS B CD  
13701 C CE  . LYS B 665  ? 0.2501 0.2449 0.2660 0.0170  0.0015  -0.0250 663  LYS B CE  
13702 N NZ  . LYS B 665  ? 0.2525 0.2509 0.2724 0.0168  0.0013  -0.0242 663  LYS B NZ  
13703 N N   . SER B 666  ? 0.2362 0.2068 0.2338 0.0128  -0.0063 -0.0240 664  SER B N   
13704 C CA  . SER B 666  ? 0.2437 0.2090 0.2363 0.0104  -0.0079 -0.0234 664  SER B CA  
13705 C C   . SER B 666  ? 0.2547 0.2198 0.2449 0.0077  -0.0073 -0.0235 664  SER B C   
13706 O O   . SER B 666  ? 0.2386 0.2083 0.2312 0.0075  -0.0058 -0.0239 664  SER B O   
13707 C CB  . SER B 666  ? 0.2787 0.2454 0.2716 0.0085  -0.0086 -0.0220 664  SER B CB  
13708 O OG  . SER B 666  ? 0.2888 0.2610 0.2838 0.0065  -0.0072 -0.0217 664  SER B OG  
13709 N N   . ALA B 667  ? 0.2478 0.2074 0.2330 0.0053  -0.0088 -0.0230 665  ALA B N   
13710 C CA  . ALA B 667  ? 0.2342 0.1935 0.2169 0.0022  -0.0087 -0.0229 665  ALA B CA  
13711 C C   . ALA B 667  ? 0.2647 0.2313 0.2507 0.0001  -0.0074 -0.0220 665  ALA B C   
13712 O O   . ALA B 667  ? 0.2368 0.2065 0.2236 -0.0006 -0.0064 -0.0224 665  ALA B O   
13713 C CB  . ALA B 667  ? 0.2752 0.2279 0.2524 -0.0006 -0.0108 -0.0220 665  ALA B CB  
13714 N N   . LEU B 668  ? 0.2481 0.2173 0.2355 -0.0007 -0.0074 -0.0209 666  LEU B N   
13715 C CA  . LEU B 668  ? 0.2882 0.2640 0.2783 -0.0023 -0.0061 -0.0202 666  LEU B CA  
13716 C C   . LEU B 668  ? 0.2553 0.2362 0.2498 0.0000  -0.0044 -0.0210 666  LEU B C   
13717 O O   . LEU B 668  ? 0.2399 0.2252 0.2360 -0.0010 -0.0033 -0.0209 666  LEU B O   
13718 C CB  . LEU B 668  ? 0.3053 0.2825 0.2956 -0.0031 -0.0064 -0.0190 666  LEU B CB  
13719 C CG  . LEU B 668  ? 0.3380 0.3132 0.3245 -0.0067 -0.0075 -0.0175 666  LEU B CG  
13720 C CD1 . LEU B 668  ? 0.3812 0.3578 0.3679 -0.0070 -0.0076 -0.0166 666  LEU B CD1 
13721 C CD2 . LEU B 668  ? 0.3317 0.3108 0.3182 -0.0095 -0.0067 -0.0170 666  LEU B CD2 
13722 N N   . ASN B 669  ? 0.2280 0.2085 0.2247 0.0030  -0.0042 -0.0218 667  ASN B N   
13723 C CA  . ASN B 669  ? 0.2514 0.2366 0.2523 0.0048  -0.0027 -0.0224 667  ASN B CA  
13724 C C   . ASN B 669  ? 0.2582 0.2432 0.2586 0.0054  -0.0019 -0.0232 667  ASN B C   
13725 O O   . ASN B 669  ? 0.2486 0.2380 0.2516 0.0057  -0.0005 -0.0234 667  ASN B O   
13726 C CB  . ASN B 669  ? 0.3192 0.3049 0.3229 0.0074  -0.0028 -0.0227 667  ASN B CB  
13727 C CG  . ASN B 669  ? 0.3526 0.3396 0.3571 0.0068  -0.0033 -0.0219 667  ASN B CG  
13728 O OD1 . ASN B 669  ? 0.4109 0.3962 0.4157 0.0080  -0.0044 -0.0218 667  ASN B OD1 
13729 N ND2 . ASN B 669  ? 0.3611 0.3512 0.3658 0.0049  -0.0027 -0.0213 667  ASN B ND2 
13730 N N   . ALA B 670  ? 0.2206 0.2004 0.2174 0.0055  -0.0028 -0.0238 668  ALA B N   
13731 C CA  . ALA B 670  ? 0.2219 0.2010 0.2173 0.0058  -0.0022 -0.0248 668  ALA B CA  
13732 C C   . ALA B 670  ? 0.2037 0.1848 0.1978 0.0027  -0.0022 -0.0242 668  ALA B C   
13733 O O   . ALA B 670  ? 0.1993 0.1829 0.1941 0.0028  -0.0012 -0.0246 668  ALA B O   
13734 C CB  . ALA B 670  ? 0.2167 0.1890 0.2079 0.0070  -0.0033 -0.0257 668  ALA B CB  
13735 N N   . ILE B 671  ? 0.2289 0.2089 0.2210 -0.0001 -0.0033 -0.0231 669  ILE B N   
13736 C CA  . ILE B 671  ? 0.2056 0.1890 0.1974 -0.0031 -0.0031 -0.0223 669  ILE B CA  
13737 C C   . ILE B 671  ? 0.2217 0.2122 0.2180 -0.0023 -0.0015 -0.0220 669  ILE B C   
13738 O O   . ILE B 671  ? 0.2286 0.2223 0.2257 -0.0029 -0.0008 -0.0219 669  ILE B O   
13739 C CB  . ILE B 671  ? 0.2260 0.2081 0.2155 -0.0062 -0.0044 -0.0210 669  ILE B CB  
13740 C CG1 . ILE B 671  ? 0.2414 0.2158 0.2256 -0.0077 -0.0063 -0.0212 669  ILE B CG1 
13741 C CG2 . ILE B 671  ? 0.2224 0.2103 0.2131 -0.0090 -0.0039 -0.0198 669  ILE B CG2 
13742 C CD1 . ILE B 671  ? 0.2689 0.2410 0.2506 -0.0106 -0.0077 -0.0197 669  ILE B CD1 
13743 N N   . ALA B 672  ? 0.2061 0.1987 0.2052 -0.0010 -0.0009 -0.0217 670  ALA B N   
13744 C CA  . ALA B 672  ? 0.2257 0.2241 0.2286 -0.0001 0.0004  -0.0214 670  ALA B CA  
13745 C C   . ALA B 672  ? 0.2137 0.2135 0.2185 0.0019  0.0015  -0.0222 670  ALA B C   
13746 O O   . ALA B 672  ? 0.2118 0.2157 0.2185 0.0019  0.0024  -0.0219 670  ALA B O   
13747 C CB  . ALA B 672  ? 0.2485 0.2479 0.2535 0.0010  0.0006  -0.0211 670  ALA B CB  
13748 N N   . GLU B 673  ? 0.1951 0.1915 0.1993 0.0037  0.0014  -0.0231 671  GLU B N   
13749 C CA  . GLU B 673  ? 0.2035 0.2012 0.2091 0.0055  0.0025  -0.0238 671  GLU B CA  
13750 C C   . GLU B 673  ? 0.2068 0.2050 0.2104 0.0043  0.0027  -0.0239 671  GLU B C   
13751 O O   . GLU B 673  ? 0.1903 0.1921 0.1958 0.0047  0.0037  -0.0237 671  GLU B O   
13752 C CB  . GLU B 673  ? 0.2100 0.2042 0.2150 0.0078  0.0023  -0.0247 671  GLU B CB  
13753 C CG  . GLU B 673  ? 0.2342 0.2302 0.2409 0.0099  0.0038  -0.0253 671  GLU B CG  
13754 C CD  . GLU B 673  ? 0.2389 0.2391 0.2503 0.0112  0.0048  -0.0248 671  GLU B CD  
13755 O OE1 . GLU B 673  ? 0.2369 0.2378 0.2501 0.0110  0.0042  -0.0243 671  GLU B OE1 
13756 O OE2 . GLU B 673  ? 0.1902 0.1929 0.2032 0.0122  0.0060  -0.0249 671  GLU B OE2 
13757 N N   . VAL B 674  ? 0.1686 0.1628 0.1682 0.0027  0.0015  -0.0242 672  VAL B N   
13758 C CA  . VAL B 674  ? 0.1684 0.1627 0.1656 0.0013  0.0013  -0.0244 672  VAL B CA  
13759 C C   . VAL B 674  ? 0.1790 0.1785 0.1779 -0.0008 0.0014  -0.0232 672  VAL B C   
13760 O O   . VAL B 674  ? 0.1873 0.1896 0.1866 -0.0009 0.0019  -0.0231 672  VAL B O   
13761 C CB  . VAL B 674  ? 0.1872 0.1753 0.1792 -0.0002 -0.0003 -0.0250 672  VAL B CB  
13762 C CG1 . VAL B 674  ? 0.2019 0.1898 0.1911 -0.0019 -0.0008 -0.0253 672  VAL B CG1 
13763 C CG2 . VAL B 674  ? 0.2041 0.1870 0.1944 0.0025  -0.0004 -0.0263 672  VAL B CG2 
13764 N N   . ARG B 675  ? 0.1849 0.1858 0.1846 -0.0022 0.0010  -0.0222 673  ARG B N   
13765 C CA  . ARG B 675  ? 0.1825 0.1889 0.1841 -0.0037 0.0013  -0.0211 673  ARG B CA  
13766 C C   . ARG B 675  ? 0.1642 0.1751 0.1695 -0.0016 0.0027  -0.0210 673  ARG B C   
13767 O O   . ARG B 675  ? 0.1919 0.2067 0.1981 -0.0021 0.0030  -0.0204 673  ARG B O   
13768 C CB  . ARG B 675  ? 0.2058 0.2135 0.2080 -0.0050 0.0009  -0.0201 673  ARG B CB  
13769 C CG  . ARG B 675  ? 0.1788 0.1832 0.1774 -0.0081 -0.0006 -0.0196 673  ARG B CG  
13770 C CD  . ARG B 675  ? 0.2207 0.2280 0.2202 -0.0094 -0.0006 -0.0184 673  ARG B CD  
13771 N NE  . ARG B 675  ? 0.2109 0.2251 0.2130 -0.0100 0.0003  -0.0174 673  ARG B NE  
13772 C CZ  . ARG B 675  ? 0.2000 0.2184 0.2038 -0.0104 0.0010  -0.0165 673  ARG B CZ  
13773 N NH1 . ARG B 675  ? 0.2192 0.2356 0.2223 -0.0102 0.0009  -0.0163 673  ARG B NH1 
13774 N NH2 . ARG B 675  ? 0.1944 0.2192 0.2004 -0.0106 0.0017  -0.0156 673  ARG B NH2 
13775 N N   . GLU B 676  ? 0.1672 0.1775 0.1745 0.0007  0.0035  -0.0214 674  GLU B N   
13776 C CA  A GLU B 676  ? 0.1710 0.1847 0.1815 0.0025  0.0047  -0.0212 674  GLU B CA  
13777 C CA  B GLU B 676  ? 0.1676 0.1814 0.1781 0.0025  0.0047  -0.0212 674  GLU B CA  
13778 C C   . GLU B 676  ? 0.1665 0.1808 0.1767 0.0031  0.0052  -0.0215 674  GLU B C   
13779 O O   . GLU B 676  ? 0.1686 0.1863 0.1803 0.0035  0.0059  -0.0209 674  GLU B O   
13780 C CB  A GLU B 676  ? 0.1942 0.2069 0.2067 0.0043  0.0051  -0.0215 674  GLU B CB  
13781 C CB  B GLU B 676  ? 0.1942 0.2067 0.2067 0.0044  0.0051  -0.0216 674  GLU B CB  
13782 C CG  A GLU B 676  ? 0.1952 0.2109 0.2108 0.0058  0.0061  -0.0212 674  GLU B CG  
13783 C CG  B GLU B 676  ? 0.1952 0.2107 0.2108 0.0058  0.0061  -0.0212 674  GLU B CG  
13784 C CD  A GLU B 676  ? 0.2309 0.2456 0.2484 0.0070  0.0061  -0.0213 674  GLU B CD  
13785 C CD  B GLU B 676  ? 0.2280 0.2457 0.2449 0.0058  0.0061  -0.0207 674  GLU B CD  
13786 O OE1 A GLU B 676  ? 0.2608 0.2743 0.2777 0.0066  0.0054  -0.0214 674  GLU B OE1 
13787 O OE1 B GLU B 676  ? 0.2422 0.2603 0.2579 0.0044  0.0056  -0.0203 674  GLU B OE1 
13788 O OE2 A GLU B 676  ? 0.2848 0.3001 0.3043 0.0083  0.0068  -0.0214 674  GLU B OE2 
13789 O OE2 B GLU B 676  ? 0.2185 0.2374 0.2376 0.0071  0.0067  -0.0205 674  GLU B OE2 
13790 N N   . ALA B 677  ? 0.1466 0.1572 0.1543 0.0034  0.0050  -0.0224 675  ALA B N   
13791 C CA  . ALA B 677  ? 0.1623 0.1732 0.1689 0.0039  0.0055  -0.0227 675  ALA B CA  
13792 C C   . ALA B 677  ? 0.1679 0.1810 0.1731 0.0020  0.0049  -0.0221 675  ALA B C   
13793 O O   . ALA B 677  ? 0.1631 0.1790 0.1690 0.0024  0.0054  -0.0217 675  ALA B O   
13794 C CB  . ALA B 677  ? 0.1673 0.1735 0.1708 0.0047  0.0054  -0.0240 675  ALA B CB  
13795 N N   . ILE B 678  ? 0.1669 0.1787 0.1699 -0.0003 0.0035  -0.0220 676  ILE B N   
13796 C CA  . ILE B 678  ? 0.1469 0.1614 0.1489 -0.0026 0.0027  -0.0212 676  ILE B CA  
13797 C C   . ILE B 678  ? 0.1503 0.1708 0.1561 -0.0022 0.0034  -0.0200 676  ILE B C   
13798 O O   . ILE B 678  ? 0.1841 0.2078 0.1902 -0.0025 0.0033  -0.0194 676  ILE B O   
13799 C CB  . ILE B 678  ? 0.1758 0.1882 0.1754 -0.0055 0.0011  -0.0210 676  ILE B CB  
13800 C CG1 . ILE B 678  ? 0.2006 0.2063 0.1956 -0.0059 0.0001  -0.0223 676  ILE B CG1 
13801 C CG2 . ILE B 678  ? 0.1712 0.1882 0.1711 -0.0081 0.0003  -0.0197 676  ILE B CG2 
13802 C CD1 . ILE B 678  ? 0.1874 0.1893 0.1801 -0.0081 -0.0013 -0.0221 676  ILE B CD1 
13803 N N   . ASP B 679  ? 0.1588 0.1806 0.1672 -0.0013 0.0039  -0.0196 677  ASP B N   
13804 C CA  . ASP B 679  ? 0.1618 0.1887 0.1732 -0.0005 0.0046  -0.0186 677  ASP B CA  
13805 C C   . ASP B 679  ? 0.1474 0.1755 0.1605 0.0017  0.0056  -0.0186 677  ASP B C   
13806 O O   . ASP B 679  ? 0.1648 0.1967 0.1792 0.0020  0.0057  -0.0177 677  ASP B O   
13807 C CB  . ASP B 679  ? 0.1772 0.2045 0.1903 0.0000  0.0049  -0.0185 677  ASP B CB  
13808 C CG  . ASP B 679  ? 0.2021 0.2296 0.2138 -0.0024 0.0041  -0.0180 677  ASP B CG  
13809 O OD1 . ASP B 679  ? 0.1963 0.2259 0.2069 -0.0046 0.0033  -0.0174 677  ASP B OD1 
13810 O OD2 . ASP B 679  ? 0.1817 0.2071 0.1931 -0.0023 0.0041  -0.0182 677  ASP B OD2 
13811 N N   . PHE B 680  ? 0.1422 0.1672 0.1552 0.0031  0.0062  -0.0193 678  PHE B N   
13812 C CA  . PHE B 680  ? 0.1597 0.1857 0.1740 0.0048  0.0071  -0.0191 678  PHE B CA  
13813 C C   . PHE B 680  ? 0.1648 0.1920 0.1772 0.0041  0.0068  -0.0188 678  PHE B C   
13814 O O   . PHE B 680  ? 0.1708 0.2009 0.1844 0.0048  0.0070  -0.0179 678  PHE B O   
13815 C CB  . PHE B 680  ? 0.1487 0.1717 0.1631 0.0061  0.0079  -0.0199 678  PHE B CB  
13816 C CG  . PHE B 680  ? 0.1596 0.1822 0.1765 0.0072  0.0083  -0.0198 678  PHE B CG  
13817 C CD1 . PHE B 680  ? 0.1447 0.1694 0.1638 0.0081  0.0086  -0.0191 678  PHE B CD1 
13818 C CD2 . PHE B 680  ? 0.1589 0.1787 0.1757 0.0076  0.0082  -0.0206 678  PHE B CD2 
13819 C CE1 . PHE B 680  ? 0.1691 0.1928 0.1901 0.0089  0.0088  -0.0192 678  PHE B CE1 
13820 C CE2 . PHE B 680  ? 0.1792 0.1986 0.1982 0.0085  0.0084  -0.0206 678  PHE B CE2 
13821 C CZ  . PHE B 680  ? 0.1704 0.1918 0.1915 0.0090  0.0086  -0.0199 678  PHE B CZ  
13822 N N   . LEU B 681  ? 0.1355 0.1603 0.1447 0.0027  0.0060  -0.0195 679  LEU B N   
13823 C CA  . LEU B 681  ? 0.1601 0.1856 0.1671 0.0019  0.0055  -0.0194 679  LEU B CA  
13824 C C   . LEU B 681  ? 0.1675 0.1976 0.1756 0.0008  0.0047  -0.0181 679  LEU B C   
13825 O O   . LEU B 681  ? 0.1648 0.1976 0.1733 0.0014  0.0048  -0.0173 679  LEU B O   
13826 C CB  . LEU B 681  ? 0.1497 0.1711 0.1525 0.0003  0.0045  -0.0205 679  LEU B CB  
13827 C CG  . LEU B 681  ? 0.1603 0.1773 0.1614 0.0020  0.0054  -0.0218 679  LEU B CG  
13828 C CD1 . LEU B 681  ? 0.1663 0.1785 0.1635 0.0006  0.0043  -0.0230 679  LEU B CD1 
13829 C CD2 . LEU B 681  ? 0.1747 0.1922 0.1748 0.0032  0.0064  -0.0219 679  LEU B CD2 
13830 N N   . ARG B 682  ? 0.1573 0.1889 0.1660 -0.0008 0.0039  -0.0178 680  ARG B N   
13831 C CA  . ARG B 682  ? 0.1551 0.1919 0.1652 -0.0018 0.0032  -0.0165 680  ARG B CA  
13832 C C   . ARG B 682  ? 0.1535 0.1942 0.1672 0.0004  0.0041  -0.0156 680  ARG B C   
13833 O O   . ARG B 682  ? 0.1682 0.2133 0.1831 0.0006  0.0037  -0.0145 680  ARG B O   
13834 C CB  . ARG B 682  ? 0.1342 0.1719 0.1441 -0.0043 0.0023  -0.0162 680  ARG B CB  
13835 C CG  . ARG B 682  ? 0.1535 0.1874 0.1593 -0.0070 0.0008  -0.0169 680  ARG B CG  
13836 C CD  . ARG B 682  ? 0.1744 0.2088 0.1800 -0.0096 -0.0001 -0.0164 680  ARG B CD  
13837 N NE  . ARG B 682  ? 0.1588 0.1892 0.1602 -0.0125 -0.0018 -0.0169 680  ARG B NE  
13838 C CZ  . ARG B 682  ? 0.1793 0.2073 0.1790 -0.0150 -0.0027 -0.0168 680  ARG B CZ  
13839 N NH1 . ARG B 682  ? 0.1900 0.2193 0.1918 -0.0148 -0.0021 -0.0163 680  ARG B NH1 
13840 N NH2 . ARG B 682  ? 0.2163 0.2399 0.2117 -0.0177 -0.0045 -0.0173 680  ARG B NH2 
13841 N N   . TYR B 683  ? 0.1672 0.2063 0.1825 0.0022  0.0052  -0.0160 681  TYR B N   
13842 C CA  . TYR B 683  ? 0.1801 0.2217 0.1981 0.0044  0.0060  -0.0153 681  TYR B CA  
13843 C C   . TYR B 683  ? 0.1631 0.2046 0.1811 0.0059  0.0063  -0.0149 681  TYR B C   
13844 O O   . TYR B 683  ? 0.1489 0.1937 0.1682 0.0070  0.0062  -0.0138 681  TYR B O   
13845 C CB  . TYR B 683  ? 0.1441 0.1833 0.1633 0.0056  0.0068  -0.0159 681  TYR B CB  
13846 C CG  . TYR B 683  ? 0.1552 0.1957 0.1765 0.0080  0.0074  -0.0155 681  TYR B CG  
13847 C CD1 . TYR B 683  ? 0.1705 0.2148 0.1932 0.0087  0.0075  -0.0149 681  TYR B CD1 
13848 C CD2 . TYR B 683  ? 0.1522 0.1901 0.1739 0.0095  0.0080  -0.0156 681  TYR B CD2 
13849 C CE1 . TYR B 683  ? 0.1476 0.1923 0.1718 0.0111  0.0080  -0.0147 681  TYR B CE1 
13850 C CE2 . TYR B 683  ? 0.1450 0.1832 0.1682 0.0115  0.0084  -0.0152 681  TYR B CE2 
13851 C CZ  . TYR B 683  ? 0.1506 0.1918 0.1748 0.0125  0.0084  -0.0148 681  TYR B CZ  
13852 O OH  . TYR B 683  ? 0.1678 0.2087 0.1929 0.0148  0.0087  -0.0146 681  TYR B OH  
13853 N N   . TYR B 684  ? 0.1430 0.1808 0.1595 0.0061  0.0068  -0.0155 682  TYR B N   
13854 C CA  . TYR B 684  ? 0.1437 0.1815 0.1600 0.0073  0.0072  -0.0149 682  TYR B CA  
13855 C C   . TYR B 684  ? 0.1552 0.1955 0.1699 0.0063  0.0062  -0.0142 682  TYR B C   
13856 O O   . TYR B 684  ? 0.1672 0.2091 0.1822 0.0074  0.0062  -0.0132 682  TYR B O   
13857 C CB  . TYR B 684  ? 0.1584 0.1925 0.1737 0.0077  0.0081  -0.0156 682  TYR B CB  
13858 C CG  . TYR B 684  ? 0.1629 0.1950 0.1801 0.0086  0.0089  -0.0160 682  TYR B CG  
13859 C CD1 . TYR B 684  ? 0.1614 0.1945 0.1809 0.0099  0.0090  -0.0154 682  TYR B CD1 
13860 C CD2 . TYR B 684  ? 0.1474 0.1768 0.1641 0.0084  0.0093  -0.0171 682  TYR B CD2 
13861 C CE1 . TYR B 684  ? 0.1526 0.1837 0.1736 0.0105  0.0094  -0.0159 682  TYR B CE1 
13862 C CE2 . TYR B 684  ? 0.1361 0.1640 0.1547 0.0092  0.0097  -0.0174 682  TYR B CE2 
13863 C CZ  . TYR B 684  ? 0.1613 0.1900 0.1820 0.0101  0.0098  -0.0168 682  TYR B CZ  
13864 O OH  . TYR B 684  ? 0.1490 0.1761 0.1714 0.0106  0.0100  -0.0171 682  TYR B OH  
13865 N N   . ALA B 685  ? 0.1705 0.2109 0.1832 0.0042  0.0052  -0.0147 683  ALA B N   
13866 C CA  . ALA B 685  ? 0.1575 0.2006 0.1687 0.0030  0.0040  -0.0140 683  ALA B CA  
13867 C C   . ALA B 685  ? 0.1664 0.2149 0.1805 0.0037  0.0035  -0.0126 683  ALA B C   
13868 O O   . ALA B 685  ? 0.1520 0.2029 0.1661 0.0044  0.0030  -0.0115 683  ALA B O   
13869 C CB  . ALA B 685  ? 0.1604 0.2021 0.1690 0.0002  0.0028  -0.0148 683  ALA B CB  
13870 N N   . GLU B 686  ? 0.1588 0.2094 0.1752 0.0036  0.0036  -0.0125 684  GLU B N   
13871 C CA  . GLU B 686  ? 0.1911 0.2473 0.2102 0.0047  0.0033  -0.0112 684  GLU B CA  
13872 C C   . GLU B 686  ? 0.1857 0.2417 0.2063 0.0078  0.0042  -0.0106 684  GLU B C   
13873 O O   . GLU B 686  ? 0.1588 0.2184 0.1805 0.0091  0.0036  -0.0094 684  GLU B O   
13874 C CB  . GLU B 686  ? 0.1951 0.2535 0.2161 0.0041  0.0036  -0.0113 684  GLU B CB  
13875 C CG  . GLU B 686  ? 0.1773 0.2419 0.2014 0.0059  0.0037  -0.0101 684  GLU B CG  
13876 C CD  . GLU B 686  ? 0.2083 0.2787 0.2331 0.0050  0.0024  -0.0088 684  GLU B CD  
13877 O OE1 . GLU B 686  ? 0.2164 0.2862 0.2391 0.0024  0.0011  -0.0088 684  GLU B OE1 
13878 O OE2 . GLU B 686  ? 0.2056 0.2813 0.2331 0.0069  0.0025  -0.0077 684  GLU B OE2 
13879 N N   . GLN B 687  ? 0.1661 0.2179 0.1869 0.0091  0.0053  -0.0114 685  GLN B N   
13880 C CA  . GLN B 687  ? 0.1591 0.2100 0.1810 0.0118  0.0059  -0.0108 685  GLN B CA  
13881 C C   . GLN B 687  ? 0.1899 0.2405 0.2103 0.0121  0.0055  -0.0099 685  GLN B C   
13882 O O   . GLN B 687  ? 0.1815 0.2333 0.2027 0.0141  0.0053  -0.0087 685  GLN B O   
13883 C CB  . GLN B 687  ? 0.1655 0.2116 0.1874 0.0125  0.0069  -0.0117 685  GLN B CB  
13884 C CG  . GLN B 687  ? 0.1629 0.2092 0.1862 0.0126  0.0073  -0.0125 685  GLN B CG  
13885 C CD  . GLN B 687  ? 0.1725 0.2223 0.1976 0.0147  0.0073  -0.0118 685  GLN B CD  
13886 O OE1 . GLN B 687  ? 0.1856 0.2345 0.2110 0.0169  0.0074  -0.0112 685  GLN B OE1 
13887 N NE2 . GLN B 687  ? 0.2155 0.2691 0.2414 0.0140  0.0071  -0.0118 685  GLN B NE2 
13888 N N   . THR B 688  ? 0.1667 0.2154 0.1846 0.0103  0.0053  -0.0103 686  THR B N   
13889 C CA  . THR B 688  ? 0.1650 0.2137 0.1809 0.0104  0.0048  -0.0094 686  THR B CA  
13890 C C   . THR B 688  ? 0.1627 0.2164 0.1791 0.0103  0.0034  -0.0082 686  THR B C   
13891 O O   . THR B 688  ? 0.1753 0.2302 0.1917 0.0119  0.0030  -0.0069 686  THR B O   
13892 C CB  . THR B 688  ? 0.1471 0.1931 0.1598 0.0085  0.0049  -0.0104 686  THR B CB  
13893 O OG1 . THR B 688  ? 0.1769 0.2189 0.1895 0.0090  0.0063  -0.0112 686  THR B OG1 
13894 C CG2 . THR B 688  ? 0.1825 0.2290 0.1927 0.0084  0.0043  -0.0094 686  THR B CG2 
13895 N N   . ARG B 689  ? 0.1423 0.1991 0.1590 0.0085  0.0025  -0.0085 687  ARG B N   
13896 C CA  . ARG B 689  ? 0.1741 0.2366 0.1918 0.0082  0.0010  -0.0072 687  ARG B CA  
13897 C C   . ARG B 689  ? 0.1703 0.2364 0.1913 0.0112  0.0012  -0.0060 687  ARG B C   
13898 O O   . ARG B 689  ? 0.1899 0.2602 0.2116 0.0120  0.0001  -0.0046 687  ARG B O   
13899 C CB  . ARG B 689  ? 0.1816 0.2470 0.1995 0.0054  0.0001  -0.0076 687  ARG B CB  
13900 C CG  . ARG B 689  ? 0.1903 0.2527 0.2043 0.0025  -0.0008 -0.0085 687  ARG B CG  
13901 C CD  . ARG B 689  ? 0.1620 0.2273 0.1762 -0.0005 -0.0021 -0.0085 687  ARG B CD  
13902 N NE  . ARG B 689  ? 0.2036 0.2683 0.2194 -0.0009 -0.0012 -0.0092 687  ARG B NE  
13903 C CZ  . ARG B 689  ? 0.2048 0.2646 0.2185 -0.0025 -0.0009 -0.0106 687  ARG B CZ  
13904 N NH1 . ARG B 689  ? 0.1864 0.2413 0.1960 -0.0038 -0.0014 -0.0116 687  ARG B NH1 
13905 N NH2 . ARG B 689  ? 0.1834 0.2431 0.1986 -0.0028 -0.0002 -0.0109 687  ARG B NH2 
13906 N N   . ARG B 690  ? 0.1564 0.2206 0.1790 0.0129  0.0025  -0.0066 688  ARG B N   
13907 C CA  . ARG B 690  ? 0.1574 0.2240 0.1825 0.0160  0.0027  -0.0058 688  ARG B CA  
13908 C C   . ARG B 690  ? 0.1856 0.2487 0.2098 0.0185  0.0029  -0.0050 688  ARG B C   
13909 O O   . ARG B 690  ? 0.1898 0.2548 0.2155 0.0213  0.0027  -0.0041 688  ARG B O   
13910 C CB  . ARG B 690  ? 0.1753 0.2409 0.2019 0.0168  0.0039  -0.0069 688  ARG B CB  
13911 C CG  . ARG B 690  ? 0.2026 0.2724 0.2305 0.0147  0.0038  -0.0073 688  ARG B CG  
13912 C CD  . ARG B 690  ? 0.2357 0.3131 0.2662 0.0158  0.0032  -0.0060 688  ARG B CD  
13913 N NE  . ARG B 690  ? 0.2745 0.3529 0.3068 0.0196  0.0041  -0.0058 688  ARG B NE  
13914 C CZ  . ARG B 690  ? 0.2912 0.3713 0.3242 0.0226  0.0036  -0.0047 688  ARG B CZ  
13915 N NH1 . ARG B 690  ? 0.2944 0.3764 0.3269 0.0220  0.0022  -0.0035 688  ARG B NH1 
13916 N NH2 . ARG B 690  ? 0.2437 0.3235 0.2777 0.0262  0.0043  -0.0048 688  ARG B NH2 
13917 N N   . THR B 691  ? 0.1582 0.2163 0.1800 0.0176  0.0033  -0.0053 689  THR B N   
13918 C CA  . THR B 691  ? 0.1955 0.2498 0.2166 0.0196  0.0037  -0.0046 689  THR B CA  
13919 C C   . THR B 691  ? 0.1946 0.2471 0.2130 0.0189  0.0032  -0.0035 689  THR B C   
13920 O O   . THR B 691  ? 0.2519 0.3038 0.2698 0.0208  0.0027  -0.0021 689  THR B O   
13921 C CB  . THR B 691  ? 0.1688 0.2181 0.1900 0.0197  0.0049  -0.0057 689  THR B CB  
13922 O OG1 . THR B 691  ? 0.1707 0.2181 0.1906 0.0172  0.0055  -0.0068 689  THR B OG1 
13923 C CG2 . THR B 691  ? 0.1934 0.2437 0.2167 0.0211  0.0053  -0.0065 689  THR B CG2 
13924 N N   . LEU B 692  ? 0.1860 0.2371 0.2022 0.0165  0.0035  -0.0043 690  LEU B N   
13925 C CA  . LEU B 692  ? 0.2147 0.2629 0.2281 0.0161  0.0038  -0.0035 690  LEU B CA  
13926 C C   . LEU B 692  ? 0.2128 0.2638 0.2245 0.0160  0.0023  -0.0021 690  LEU B C   
13927 O O   . LEU B 692  ? 0.2268 0.2811 0.2380 0.0146  0.0012  -0.0024 690  LEU B O   
13928 C CB  . LEU B 692  ? 0.1933 0.2389 0.2048 0.0139  0.0048  -0.0049 690  LEU B CB  
13929 C CG  . LEU B 692  ? 0.1825 0.2251 0.1957 0.0140  0.0062  -0.0061 690  LEU B CG  
13930 C CD1 . LEU B 692  ? 0.2136 0.2539 0.2250 0.0124  0.0072  -0.0073 690  LEU B CD1 
13931 C CD2 . LEU B 692  ? 0.1931 0.2332 0.2075 0.0158  0.0067  -0.0052 690  LEU B CD2 
13932 N N   . GLY B 693  ? 0.2297 0.2789 0.2402 0.0174  0.0022  -0.0005 691  GLY B N   
13933 C CA  . GLY B 693  ? 0.2292 0.2803 0.2376 0.0176  0.0008  0.0011  691  GLY B CA  
13934 C C   . GLY B 693  ? 0.2611 0.3083 0.2662 0.0171  0.0015  0.0020  691  GLY B C   
13935 O O   . GLY B 693  ? 0.2547 0.2983 0.2594 0.0165  0.0031  0.0014  691  GLY B O   
13936 N N   . PRO B 694  ? 0.2859 0.3341 0.2886 0.0175  0.0003  0.0038  692  PRO B N   
13937 C CA  . PRO B 694  ? 0.2717 0.3168 0.2705 0.0166  0.0010  0.0046  692  PRO B CA  
13938 C C   . PRO B 694  ? 0.3039 0.3446 0.3029 0.0174  0.0023  0.0056  692  PRO B C   
13939 O O   . PRO B 694  ? 0.3116 0.3499 0.3084 0.0162  0.0037  0.0058  692  PRO B O   
13940 C CB  . PRO B 694  ? 0.2957 0.3430 0.2920 0.0170  -0.0009 0.0065  692  PRO B CB  
13941 C CG  . PRO B 694  ? 0.3314 0.3825 0.3311 0.0189  -0.0026 0.0070  692  PRO B CG  
13942 C CD  . PRO B 694  ? 0.3093 0.3620 0.3125 0.0184  -0.0018 0.0049  692  PRO B CD  
13943 N N   . GLY B 695  ? 0.2810 0.3207 0.2826 0.0195  0.0019  0.0063  693  GLY B N   
13944 C CA  . GLY B 695  ? 0.2894 0.3245 0.2911 0.0200  0.0028  0.0073  693  GLY B CA  
13945 C C   . GLY B 695  ? 0.3033 0.3363 0.3070 0.0191  0.0045  0.0056  693  GLY B C   
13946 O O   . GLY B 695  ? 0.2994 0.3285 0.3033 0.0191  0.0051  0.0064  693  GLY B O   
13947 N N   . HIS B 696  ? 0.2731 0.3084 0.2782 0.0180  0.0050  0.0034  694  HIS B N   
13948 C CA  . HIS B 696  ? 0.2598 0.2932 0.2667 0.0172  0.0065  0.0019  694  HIS B CA  
13949 C C   . HIS B 696  ? 0.2653 0.2985 0.2703 0.0152  0.0079  0.0013  694  HIS B C   
13950 O O   . HIS B 696  ? 0.2887 0.3235 0.2936 0.0142  0.0083  -0.0005 694  HIS B O   
13951 C CB  . HIS B 696  ? 0.2342 0.2699 0.2439 0.0176  0.0062  0.0000  694  HIS B CB  
13952 C CG  . HIS B 696  ? 0.2320 0.2688 0.2434 0.0199  0.0049  0.0006  694  HIS B CG  
13953 N ND1 . HIS B 696  ? 0.2437 0.2849 0.2559 0.0205  0.0038  0.0004  694  HIS B ND1 
13954 C CD2 . HIS B 696  ? 0.2252 0.2592 0.2374 0.0218  0.0046  0.0014  694  HIS B CD2 
13955 C CE1 . HIS B 696  ? 0.2267 0.2684 0.2405 0.0230  0.0030  0.0010  694  HIS B CE1 
13956 N NE2 . HIS B 696  ? 0.2186 0.2556 0.2322 0.0239  0.0035  0.0015  694  HIS B NE2 
13957 N N   . GLY B 697  ? 0.2924 0.3236 0.2957 0.0147  0.0087  0.0028  695  GLY B N   
13958 C CA  . GLY B 697  ? 0.2797 0.3112 0.2808 0.0132  0.0102  0.0025  695  GLY B CA  
13959 C C   . GLY B 697  ? 0.2495 0.2805 0.2527 0.0124  0.0118  0.0008  695  GLY B C   
13960 O O   . GLY B 697  ? 0.2648 0.2942 0.2709 0.0126  0.0120  0.0007  695  GLY B O   
13961 N N   . PRO B 698  ? 0.2568 0.2889 0.2584 0.0116  0.0129  -0.0006 696  PRO B N   
13962 C CA  . PRO B 698  ? 0.2410 0.2729 0.2445 0.0111  0.0144  -0.0021 696  PRO B CA  
13963 C C   . PRO B 698  ? 0.2305 0.2616 0.2350 0.0105  0.0159  -0.0007 696  PRO B C   
13964 O O   . PRO B 698  ? 0.2471 0.2777 0.2497 0.0102  0.0162  0.0014  696  PRO B O   
13965 C CB  . PRO B 698  ? 0.2686 0.3016 0.2692 0.0107  0.0150  -0.0037 696  PRO B CB  
13966 C CG  . PRO B 698  ? 0.3282 0.3616 0.3248 0.0105  0.0146  -0.0023 696  PRO B CG  
13967 C CD  . PRO B 698  ? 0.2852 0.3186 0.2827 0.0111  0.0127  -0.0008 696  PRO B CD  
13968 N N   . LEU B 699  ? 0.2122 0.2431 0.2197 0.0103  0.0167  -0.0017 697  LEU B N   
13969 C CA  . LEU B 699  ? 0.2136 0.2446 0.2225 0.0095  0.0182  -0.0005 697  LEU B CA  
13970 C C   . LEU B 699  ? 0.2091 0.2420 0.2155 0.0091  0.0202  -0.0004 697  LEU B C   
13971 O O   . LEU B 699  ? 0.2390 0.2726 0.2448 0.0083  0.0213  0.0016  697  LEU B O   
13972 C CB  . LEU B 699  ? 0.1992 0.2299 0.2120 0.0093  0.0185  -0.0016 697  LEU B CB  
13973 C CG  . LEU B 699  ? 0.2193 0.2479 0.2344 0.0098  0.0168  -0.0019 697  LEU B CG  
13974 C CD1 . LEU B 699  ? 0.2255 0.2542 0.2439 0.0095  0.0171  -0.0032 697  LEU B CD1 
13975 C CD2 . LEU B 699  ? 0.2438 0.2701 0.2588 0.0095  0.0160  0.0003  697  LEU B CD2 
13976 N N   . GLY B 700  ? 0.2239 0.2577 0.2288 0.0097  0.0206  -0.0026 698  GLY B N   
13977 C CA  . GLY B 700  ? 0.2228 0.2584 0.2258 0.0098  0.0227  -0.0031 698  GLY B CA  
13978 C C   . GLY B 700  ? 0.1791 0.2152 0.1840 0.0105  0.0234  -0.0054 698  GLY B C   
13979 O O   . GLY B 700  ? 0.2015 0.2363 0.2084 0.0108  0.0221  -0.0067 698  GLY B O   
13980 N N   . PRO B 701  ? 0.1883 0.2263 0.1926 0.0110  0.0255  -0.0058 699  PRO B N   
13981 C CA  . PRO B 701  ? 0.1714 0.2096 0.1774 0.0120  0.0262  -0.0080 699  PRO B CA  
13982 C C   . PRO B 701  ? 0.1888 0.2269 0.2000 0.0117  0.0254  -0.0079 699  PRO B C   
13983 O O   . PRO B 701  ? 0.1977 0.2370 0.2120 0.0107  0.0257  -0.0061 699  PRO B O   
13984 C CB  . PRO B 701  ? 0.1950 0.2362 0.2003 0.0127  0.0289  -0.0078 699  PRO B CB  
13985 C CG  . PRO B 701  ? 0.2083 0.2498 0.2092 0.0122  0.0295  -0.0063 699  PRO B CG  
13986 C CD  . PRO B 701  ? 0.2226 0.2627 0.2247 0.0108  0.0276  -0.0043 699  PRO B CD  
13987 N N   . ILE B 702  ? 0.1840 0.2204 0.1959 0.0122  0.0241  -0.0099 700  ILE B N   
13988 C CA  . ILE B 702  ? 0.1627 0.1987 0.1790 0.0120  0.0232  -0.0101 700  ILE B CA  
13989 C C   . ILE B 702  ? 0.1812 0.2178 0.1987 0.0132  0.0241  -0.0118 700  ILE B C   
13990 O O   . ILE B 702  ? 0.1644 0.1996 0.1790 0.0142  0.0240  -0.0137 700  ILE B O   
13991 C CB  . ILE B 702  ? 0.1687 0.2022 0.1849 0.0117  0.0210  -0.0107 700  ILE B CB  
13992 C CG1 . ILE B 702  ? 0.1750 0.2081 0.1908 0.0109  0.0202  -0.0087 700  ILE B CG1 
13993 C CG2 . ILE B 702  ? 0.1744 0.2072 0.1943 0.0117  0.0202  -0.0114 700  ILE B CG2 
13994 C CD1 . ILE B 702  ? 0.2319 0.2633 0.2482 0.0109  0.0182  -0.0091 700  ILE B CD1 
13995 N N   . VAL B 703  ? 0.1743 0.2127 0.1960 0.0130  0.0246  -0.0112 701  VAL B N   
13996 C CA  . VAL B 703  ? 0.1579 0.1973 0.1817 0.0143  0.0252  -0.0125 701  VAL B CA  
13997 C C   . VAL B 703  ? 0.1676 0.2046 0.1932 0.0141  0.0231  -0.0135 701  VAL B C   
13998 O O   . VAL B 703  ? 0.1507 0.1873 0.1788 0.0129  0.0221  -0.0125 701  VAL B O   
13999 C CB  . VAL B 703  ? 0.1713 0.2148 0.1991 0.0140  0.0267  -0.0111 701  VAL B CB  
14000 C CG1 . VAL B 703  ? 0.1628 0.2076 0.1937 0.0153  0.0268  -0.0122 701  VAL B CG1 
14001 C CG2 . VAL B 703  ? 0.1650 0.2114 0.1906 0.0144  0.0290  -0.0102 701  VAL B CG2 
14002 N N   . CYS B 704  ? 0.1600 0.1949 0.1838 0.0152  0.0226  -0.0155 702  CYS B N   
14003 C CA  . CYS B 704  ? 0.1630 0.1956 0.1879 0.0150  0.0208  -0.0165 702  CYS B CA  
14004 C C   . CYS B 704  ? 0.1527 0.1860 0.1799 0.0163  0.0211  -0.0174 702  CYS B C   
14005 O O   . CYS B 704  ? 0.1516 0.1844 0.1768 0.0178  0.0218  -0.0187 702  CYS B O   
14006 C CB  . CYS B 704  ? 0.1492 0.1787 0.1702 0.0149  0.0196  -0.0178 702  CYS B CB  
14007 S SG  . CYS B 704  ? 0.1793 0.2086 0.1980 0.0136  0.0189  -0.0167 702  CYS B SG  
14008 N N   . ILE B 705  ? 0.1410 0.1753 0.1723 0.0157  0.0204  -0.0167 703  ILE B N   
14009 C CA  . ILE B 705  ? 0.1551 0.1907 0.1892 0.0168  0.0204  -0.0172 703  ILE B CA  
14010 C C   . ILE B 705  ? 0.1427 0.1754 0.1773 0.0164  0.0184  -0.0180 703  ILE B C   
14011 O O   . ILE B 705  ? 0.1552 0.1870 0.1907 0.0150  0.0172  -0.0173 703  ILE B O   
14012 C CB  . ILE B 705  ? 0.1437 0.1837 0.1824 0.0162  0.0213  -0.0155 703  ILE B CB  
14013 C CG1 . ILE B 705  ? 0.1675 0.2108 0.2056 0.0169  0.0237  -0.0148 703  ILE B CG1 
14014 C CG2 . ILE B 705  ? 0.1594 0.2008 0.2016 0.0171  0.0208  -0.0159 703  ILE B CG2 
14015 C CD1 . ILE B 705  ? 0.1644 0.2120 0.2065 0.0155  0.0246  -0.0125 703  ILE B CD1 
14016 N N   . SER B 706  ? 0.1587 0.1897 0.1923 0.0178  0.0179  -0.0194 704  SER B N   
14017 C CA  . SER B 706  ? 0.1924 0.2200 0.2251 0.0173  0.0160  -0.0202 704  SER B CA  
14018 C C   . SER B 706  ? 0.1532 0.1810 0.1882 0.0185  0.0153  -0.0207 704  SER B C   
14019 O O   . SER B 706  ? 0.1685 0.1986 0.2051 0.0202  0.0164  -0.0208 704  SER B O   
14020 C CB  . SER B 706  ? 0.1724 0.1964 0.2002 0.0174  0.0156  -0.0215 704  SER B CB  
14021 O OG  . SER B 706  ? 0.1614 0.1849 0.1872 0.0192  0.0166  -0.0226 704  SER B OG  
14022 N N   . PRO B 707  ? 0.1625 0.1882 0.1979 0.0177  0.0136  -0.0209 705  PRO B N   
14023 C CA  . PRO B 707  ? 0.1714 0.1970 0.2089 0.0187  0.0126  -0.0211 705  PRO B CA  
14024 C C   . PRO B 707  ? 0.1859 0.2080 0.2202 0.0201  0.0121  -0.0225 705  PRO B C   
14025 O O   . PRO B 707  ? 0.1923 0.2115 0.2225 0.0198  0.0121  -0.0233 705  PRO B O   
14026 C CB  . PRO B 707  ? 0.1751 0.1996 0.2135 0.0170  0.0109  -0.0207 705  PRO B CB  
14027 C CG  . PRO B 707  ? 0.1733 0.1953 0.2082 0.0158  0.0108  -0.0209 705  PRO B CG  
14028 C CD  . PRO B 707  ? 0.1823 0.2060 0.2163 0.0160  0.0125  -0.0207 705  PRO B CD  
14029 N N   . TRP B 708  ? 0.1660 0.1882 0.2019 0.0217  0.0114  -0.0228 706  TRP B N   
14030 C CA  . TRP B 708  ? 0.1821 0.2001 0.2147 0.0232  0.0107  -0.0241 706  TRP B CA  
14031 C C   . TRP B 708  ? 0.1858 0.1996 0.2157 0.0216  0.0088  -0.0243 706  TRP B C   
14032 O O   . TRP B 708  ? 0.1794 0.1888 0.2053 0.0219  0.0081  -0.0252 706  TRP B O   
14033 C CB  . TRP B 708  ? 0.1666 0.1860 0.2017 0.0257  0.0104  -0.0242 706  TRP B CB  
14034 C CG  . TRP B 708  ? 0.1920 0.2117 0.2298 0.0250  0.0086  -0.0236 706  TRP B CG  
14035 C CD1 . TRP B 708  ? 0.1840 0.2080 0.2265 0.0242  0.0083  -0.0224 706  TRP B CD1 
14036 C CD2 . TRP B 708  ? 0.1959 0.2110 0.2312 0.0247  0.0065  -0.0240 706  TRP B CD2 
14037 N NE1 . TRP B 708  ? 0.2031 0.2254 0.2461 0.0236  0.0062  -0.0222 706  TRP B NE1 
14038 C CE2 . TRP B 708  ? 0.2005 0.2175 0.2391 0.0239  0.0052  -0.0231 706  TRP B CE2 
14039 C CE3 . TRP B 708  ? 0.1765 0.1861 0.2070 0.0248  0.0057  -0.0249 706  TRP B CE3 
14040 C CZ2 . TRP B 708  ? 0.1998 0.2135 0.2369 0.0235  0.0031  -0.0231 706  TRP B CZ2 
14041 C CZ3 . TRP B 708  ? 0.2109 0.2171 0.2400 0.0242  0.0036  -0.0248 706  TRP B CZ3 
14042 C CH2 . TRP B 708  ? 0.2031 0.2114 0.2354 0.0236  0.0024  -0.0239 706  TRP B CH2 
14043 N N   . ASN B 709  ? 0.1762 0.1909 0.2079 0.0198  0.0078  -0.0235 707  ASN B N   
14044 C CA  . ASN B 709  ? 0.1955 0.2068 0.2253 0.0189  0.0060  -0.0236 707  ASN B CA  
14045 C C   . ASN B 709  ? 0.2087 0.2172 0.2345 0.0171  0.0058  -0.0239 707  ASN B C   
14046 O O   . ASN B 709  ? 0.2082 0.2133 0.2314 0.0165  0.0045  -0.0241 707  ASN B O   
14047 C CB  . ASN B 709  ? 0.1748 0.1878 0.2075 0.0179  0.0050  -0.0228 707  ASN B CB  
14048 C CG  . ASN B 709  ? 0.1971 0.2116 0.2303 0.0161  0.0055  -0.0222 707  ASN B CG  
14049 O OD1 . ASN B 709  ? 0.2098 0.2271 0.2449 0.0161  0.0068  -0.0218 707  ASN B OD1 
14050 N ND2 . ASN B 709  ? 0.1901 0.2027 0.2213 0.0147  0.0046  -0.0222 707  ASN B ND2 
14051 N N   . PHE B 710  ? 0.1931 0.2033 0.2185 0.0163  0.0069  -0.0237 708  PHE B N   
14052 C CA  . PHE B 710  ? 0.1837 0.1920 0.2056 0.0148  0.0068  -0.0239 708  PHE B CA  
14053 C C   . PHE B 710  ? 0.1678 0.1761 0.1880 0.0156  0.0080  -0.0245 708  PHE B C   
14054 O O   . PHE B 710  ? 0.1670 0.1776 0.1875 0.0151  0.0090  -0.0241 708  PHE B O   
14055 C CB  . PHE B 710  ? 0.1798 0.1902 0.2026 0.0132  0.0069  -0.0232 708  PHE B CB  
14056 C CG  . PHE B 710  ? 0.2187 0.2289 0.2425 0.0126  0.0059  -0.0228 708  PHE B CG  
14057 C CD1 . PHE B 710  ? 0.2221 0.2294 0.2440 0.0123  0.0046  -0.0230 708  PHE B CD1 
14058 C CD2 . PHE B 710  ? 0.2111 0.2235 0.2372 0.0122  0.0061  -0.0222 708  PHE B CD2 
14059 C CE1 . PHE B 710  ? 0.2390 0.2461 0.2614 0.0116  0.0036  -0.0227 708  PHE B CE1 
14060 C CE2 . PHE B 710  ? 0.2257 0.2376 0.2522 0.0117  0.0051  -0.0220 708  PHE B CE2 
14061 C CZ  . PHE B 710  ? 0.2211 0.2306 0.2458 0.0114  0.0039  -0.0222 708  PHE B CZ  
14062 N N   . PRO B 711  ? 0.2018 0.2072 0.2198 0.0171  0.0079  -0.0255 709  PRO B N   
14063 C CA  . PRO B 711  ? 0.1899 0.1956 0.2067 0.0186  0.0093  -0.0261 709  PRO B CA  
14064 C C   . PRO B 711  ? 0.1922 0.1965 0.2052 0.0173  0.0094  -0.0265 709  PRO B C   
14065 O O   . PRO B 711  ? 0.1910 0.1962 0.2029 0.0183  0.0107  -0.0269 709  PRO B O   
14066 C CB  . PRO B 711  ? 0.2022 0.2045 0.2174 0.0208  0.0088  -0.0272 709  PRO B CB  
14067 C CG  . PRO B 711  ? 0.2067 0.2050 0.2198 0.0194  0.0068  -0.0271 709  PRO B CG  
14068 C CD  . PRO B 711  ? 0.1774 0.1788 0.1937 0.0177  0.0064  -0.0259 709  PRO B CD  
14069 N N   . LEU B 712  ? 0.1836 0.1859 0.1942 0.0151  0.0082  -0.0263 710  LEU B N   
14070 C CA  . LEU B 712  ? 0.1850 0.1869 0.1927 0.0135  0.0081  -0.0264 710  LEU B CA  
14071 C C   . LEU B 712  ? 0.1811 0.1868 0.1909 0.0118  0.0083  -0.0252 710  LEU B C   
14072 O O   . LEU B 712  ? 0.1878 0.1953 0.1970 0.0113  0.0089  -0.0249 710  LEU B O   
14073 C CB  . LEU B 712  ? 0.1698 0.1668 0.1729 0.0120  0.0065  -0.0271 710  LEU B CB  
14074 C CG  . LEU B 712  ? 0.1598 0.1562 0.1594 0.0102  0.0062  -0.0272 710  LEU B CG  
14075 C CD1 . LEU B 712  ? 0.1693 0.1654 0.1670 0.0117  0.0074  -0.0281 710  LEU B CD1 
14076 C CD2 . LEU B 712  ? 0.2191 0.2105 0.2144 0.0082  0.0043  -0.0276 710  LEU B CD2 
14077 N N   . ALA B 713  ? 0.1677 0.1744 0.1797 0.0110  0.0076  -0.0245 711  ALA B N   
14078 C CA  . ALA B 713  ? 0.1803 0.1901 0.1938 0.0096  0.0076  -0.0235 711  ALA B CA  
14079 C C   . ALA B 713  ? 0.1737 0.1869 0.1900 0.0105  0.0089  -0.0228 711  ALA B C   
14080 O O   . ALA B 713  ? 0.1719 0.1869 0.1877 0.0100  0.0093  -0.0224 711  ALA B O   
14081 C CB  . ALA B 713  ? 0.1813 0.1910 0.1960 0.0089  0.0068  -0.0231 711  ALA B CB  
14082 N N   . ILE B 714  ? 0.1803 0.1944 0.1996 0.0117  0.0094  -0.0227 712  ILE B N   
14083 C CA  . ILE B 714  ? 0.1635 0.1806 0.1854 0.0121  0.0104  -0.0218 712  ILE B CA  
14084 C C   . ILE B 714  ? 0.1850 0.2028 0.2057 0.0128  0.0116  -0.0219 712  ILE B C   
14085 O O   . ILE B 714  ? 0.1575 0.1773 0.1785 0.0126  0.0123  -0.0212 712  ILE B O   
14086 C CB  . ILE B 714  ? 0.1928 0.2108 0.2181 0.0128  0.0104  -0.0215 712  ILE B CB  
14087 C CG1 . ILE B 714  ? 0.1929 0.2103 0.2188 0.0120  0.0093  -0.0212 712  ILE B CG1 
14088 C CG2 . ILE B 714  ? 0.1723 0.1929 0.1999 0.0131  0.0115  -0.0205 712  ILE B CG2 
14089 C CD1 . ILE B 714  ? 0.2222 0.2403 0.2511 0.0123  0.0090  -0.0208 712  ILE B CD1 
14090 N N   . PHE B 715  ? 0.1790 0.1950 0.1981 0.0139  0.0119  -0.0229 713  PHE B N   
14091 C CA  . PHE B 715  ? 0.1515 0.1678 0.1686 0.0147  0.0131  -0.0233 713  PHE B CA  
14092 C C   . PHE B 715  ? 0.1563 0.1725 0.1705 0.0134  0.0128  -0.0231 713  PHE B C   
14093 O O   . PHE B 715  ? 0.1590 0.1773 0.1732 0.0135  0.0138  -0.0225 713  PHE B O   
14094 C CB  . PHE B 715  ? 0.1601 0.1733 0.1747 0.0161  0.0130  -0.0247 713  PHE B CB  
14095 C CG  . PHE B 715  ? 0.1694 0.1823 0.1811 0.0172  0.0142  -0.0255 713  PHE B CG  
14096 C CD1 . PHE B 715  ? 0.1663 0.1822 0.1800 0.0189  0.0160  -0.0251 713  PHE B CD1 
14097 C CD2 . PHE B 715  ? 0.1788 0.1886 0.1857 0.0165  0.0135  -0.0264 713  PHE B CD2 
14098 C CE1 . PHE B 715  ? 0.1789 0.1947 0.1896 0.0201  0.0174  -0.0258 713  PHE B CE1 
14099 C CE2 . PHE B 715  ? 0.1726 0.1817 0.1761 0.0176  0.0146  -0.0272 713  PHE B CE2 
14100 C CZ  . PHE B 715  ? 0.1725 0.1846 0.1778 0.0195  0.0166  -0.0269 713  PHE B CZ  
14101 N N   . THR B 716  ? 0.1499 0.1639 0.1618 0.0121  0.0114  -0.0236 714  THR B N   
14102 C CA  . THR B 716  ? 0.1667 0.1810 0.1759 0.0106  0.0109  -0.0234 714  THR B CA  
14103 C C   . THR B 716  ? 0.1644 0.1821 0.1760 0.0100  0.0109  -0.0219 714  THR B C   
14104 O O   . THR B 716  ? 0.1699 0.1891 0.1803 0.0096  0.0112  -0.0214 714  THR B O   
14105 C CB  . THR B 716  ? 0.1644 0.1758 0.1708 0.0091  0.0092  -0.0239 714  THR B CB  
14106 O OG1 . THR B 716  ? 0.1757 0.1830 0.1792 0.0098  0.0090  -0.0253 714  THR B OG1 
14107 C CG2 . THR B 716  ? 0.1723 0.1847 0.1764 0.0073  0.0085  -0.0236 714  THR B CG2 
14108 N N   . GLY B 717  ? 0.1601 0.1788 0.1747 0.0099  0.0106  -0.0214 715  GLY B N   
14109 C CA  . GLY B 717  ? 0.1588 0.1801 0.1753 0.0096  0.0106  -0.0202 715  GLY B CA  
14110 C C   . GLY B 717  ? 0.1443 0.1673 0.1618 0.0104  0.0117  -0.0193 715  GLY B C   
14111 O O   . GLY B 717  ? 0.1639 0.1884 0.1809 0.0101  0.0117  -0.0185 715  GLY B O   
14112 N N   . GLN B 718  ? 0.1494 0.1723 0.1686 0.0113  0.0127  -0.0193 716  GLN B N   
14113 C CA  . GLN B 718  ? 0.1522 0.1769 0.1725 0.0117  0.0138  -0.0182 716  GLN B CA  
14114 C C   . GLN B 718  ? 0.1510 0.1760 0.1682 0.0117  0.0143  -0.0182 716  GLN B C   
14115 O O   . GLN B 718  ? 0.1459 0.1722 0.1628 0.0115  0.0146  -0.0171 716  GLN B O   
14116 C CB  . GLN B 718  ? 0.1490 0.1742 0.1718 0.0125  0.0147  -0.0182 716  GLN B CB  
14117 C CG  . GLN B 718  ? 0.1585 0.1832 0.1842 0.0124  0.0139  -0.0181 716  GLN B CG  
14118 C CD  . GLN B 718  ? 0.1681 0.1941 0.1968 0.0129  0.0147  -0.0177 716  GLN B CD  
14119 O OE1 . GLN B 718  ? 0.1919 0.2184 0.2232 0.0124  0.0143  -0.0169 716  GLN B OE1 
14120 N NE2 . GLN B 718  ? 0.1577 0.1845 0.1861 0.0138  0.0157  -0.0183 716  GLN B NE2 
14121 N N   . ILE B 719  ? 0.1522 0.1756 0.1668 0.0120  0.0145  -0.0195 717  ILE B N   
14122 C CA  . ILE B 719  ? 0.1717 0.1950 0.1827 0.0120  0.0150  -0.0198 717  ILE B CA  
14123 C C   . ILE B 719  ? 0.1665 0.1901 0.1755 0.0108  0.0138  -0.0193 717  ILE B C   
14124 O O   . ILE B 719  ? 0.1684 0.1932 0.1758 0.0107  0.0141  -0.0186 717  ILE B O   
14125 C CB  . ILE B 719  ? 0.1573 0.1779 0.1654 0.0128  0.0151  -0.0215 717  ILE B CB  
14126 C CG1 . ILE B 719  ? 0.1661 0.1875 0.1764 0.0144  0.0167  -0.0217 717  ILE B CG1 
14127 C CG2 . ILE B 719  ? 0.2207 0.2403 0.2242 0.0126  0.0152  -0.0221 717  ILE B CG2 
14128 C CD1 . ILE B 719  ? 0.2544 0.2729 0.2623 0.0156  0.0167  -0.0235 717  ILE B CD1 
14129 N N   . ALA B 720  ? 0.1629 0.1858 0.1719 0.0098  0.0124  -0.0197 718  ALA B N   
14130 C CA  . ALA B 720  ? 0.1595 0.1834 0.1670 0.0085  0.0111  -0.0192 718  ALA B CA  
14131 C C   . ALA B 720  ? 0.1699 0.1967 0.1795 0.0088  0.0112  -0.0176 718  ALA B C   
14132 O O   . ALA B 720  ? 0.1720 0.2001 0.1799 0.0084  0.0108  -0.0169 718  ALA B O   
14133 C CB  . ALA B 720  ? 0.1731 0.1964 0.1809 0.0074  0.0098  -0.0197 718  ALA B CB  
14134 N N   . ALA B 721  ? 0.1527 0.1800 0.1656 0.0095  0.0116  -0.0170 719  ALA B N   
14135 C CA  . ALA B 721  ? 0.1711 0.2002 0.1858 0.0100  0.0116  -0.0155 719  ALA B CA  
14136 C C   . ALA B 721  ? 0.1485 0.1780 0.1620 0.0104  0.0125  -0.0145 719  ALA B C   
14137 O O   . ALA B 721  ? 0.1654 0.1962 0.1780 0.0104  0.0121  -0.0134 719  ALA B O   
14138 C CB  . ALA B 721  ? 0.1656 0.1943 0.1835 0.0106  0.0118  -0.0153 719  ALA B CB  
14139 N N   . ALA B 722  ? 0.1554 0.1841 0.1689 0.0108  0.0138  -0.0148 720  ALA B N   
14140 C CA  . ALA B 722  ? 0.1390 0.1684 0.1513 0.0110  0.0149  -0.0138 720  ALA B CA  
14141 C C   . ALA B 722  ? 0.1714 0.2011 0.1797 0.0106  0.0145  -0.0140 720  ALA B C   
14142 O O   . ALA B 722  ? 0.1675 0.1981 0.1746 0.0105  0.0145  -0.0126 720  ALA B O   
14143 C CB  . ALA B 722  ? 0.1516 0.1809 0.1648 0.0115  0.0165  -0.0142 720  ALA B CB  
14144 N N   . LEU B 723  ? 0.1726 0.2009 0.1785 0.0102  0.0141  -0.0156 721  LEU B N   
14145 C CA  . LEU B 723  ? 0.1690 0.1971 0.1706 0.0096  0.0135  -0.0160 721  LEU B CA  
14146 C C   . LEU B 723  ? 0.1578 0.1876 0.1593 0.0088  0.0119  -0.0149 721  LEU B C   
14147 O O   . LEU B 723  ? 0.1969 0.2276 0.1960 0.0086  0.0116  -0.0140 721  LEU B O   
14148 C CB  . LEU B 723  ? 0.1703 0.1958 0.1693 0.0092  0.0129  -0.0180 721  LEU B CB  
14149 C CG  . LEU B 723  ? 0.1845 0.2080 0.1822 0.0103  0.0144  -0.0193 721  LEU B CG  
14150 C CD1 . LEU B 723  ? 0.1792 0.1995 0.1746 0.0099  0.0134  -0.0212 721  LEU B CD1 
14151 C CD2 . LEU B 723  ? 0.1820 0.2057 0.1760 0.0109  0.0155  -0.0192 721  LEU B CD2 
14152 N N   . VAL B 724  ? 0.1600 0.1906 0.1640 0.0084  0.0107  -0.0149 722  VAL B N   
14153 C CA  . VAL B 724  ? 0.1532 0.1862 0.1572 0.0078  0.0092  -0.0139 722  VAL B CA  
14154 C C   . VAL B 724  ? 0.1800 0.2146 0.1855 0.0089  0.0094  -0.0120 722  VAL B C   
14155 O O   . VAL B 724  ? 0.2005 0.2372 0.2050 0.0088  0.0083  -0.0110 722  VAL B O   
14156 C CB  . VAL B 724  ? 0.1602 0.1941 0.1663 0.0072  0.0082  -0.0144 722  VAL B CB  
14157 C CG1 . VAL B 724  ? 0.1949 0.2295 0.2050 0.0084  0.0087  -0.0137 722  VAL B CG1 
14158 C CG2 . VAL B 724  ? 0.1613 0.1981 0.1666 0.0060  0.0064  -0.0138 722  VAL B CG2 
14159 N N   . ALA B 725  ? 0.1836 0.2173 0.1912 0.0099  0.0106  -0.0115 723  ALA B N   
14160 C CA  . ALA B 725  ? 0.1821 0.2163 0.1905 0.0107  0.0108  -0.0097 723  ALA B CA  
14161 C C   . ALA B 725  ? 0.2083 0.2424 0.2135 0.0106  0.0114  -0.0088 723  ALA B C   
14162 O O   . ALA B 725  ? 0.2217 0.2559 0.2269 0.0111  0.0115  -0.0071 723  ALA B O   
14163 C CB  . ALA B 725  ? 0.1692 0.2020 0.1806 0.0114  0.0117  -0.0094 723  ALA B CB  
14164 N N   . GLY B 726  ? 0.1884 0.2219 0.1906 0.0099  0.0118  -0.0100 724  GLY B N   
14165 C CA  . GLY B 726  ? 0.1835 0.2169 0.1819 0.0098  0.0124  -0.0093 724  GLY B CA  
14166 C C   . GLY B 726  ? 0.2083 0.2408 0.2062 0.0101  0.0145  -0.0094 724  GLY B C   
14167 O O   . GLY B 726  ? 0.2242 0.2570 0.2193 0.0101  0.0153  -0.0084 724  GLY B O   
14168 N N   . ASN B 727  ? 0.1785 0.2104 0.1790 0.0104  0.0155  -0.0105 725  ASN B N   
14169 C CA  . ASN B 727  ? 0.1834 0.2153 0.1844 0.0109  0.0176  -0.0104 725  ASN B CA  
14170 C C   . ASN B 727  ? 0.1837 0.2146 0.1826 0.0113  0.0185  -0.0126 725  ASN B C   
14171 O O   . ASN B 727  ? 0.1907 0.2204 0.1903 0.0112  0.0175  -0.0141 725  ASN B O   
14172 C CB  . ASN B 727  ? 0.1799 0.2119 0.1857 0.0110  0.0180  -0.0099 725  ASN B CB  
14173 C CG  . ASN B 727  ? 0.1672 0.1991 0.1749 0.0109  0.0170  -0.0080 725  ASN B CG  
14174 O OD1 . ASN B 727  ? 0.1927 0.2249 0.2001 0.0107  0.0175  -0.0061 725  ASN B OD1 
14175 N ND2 . ASN B 727  ? 0.1699 0.2014 0.1795 0.0110  0.0155  -0.0085 725  ASN B ND2 
14176 N N   . PRO B 728  ? 0.1863 0.2176 0.1825 0.0118  0.0202  -0.0127 726  PRO B N   
14177 C CA  . PRO B 728  ? 0.1859 0.2161 0.1805 0.0128  0.0212  -0.0148 726  PRO B CA  
14178 C C   . PRO B 728  ? 0.1863 0.2173 0.1857 0.0134  0.0222  -0.0150 726  PRO B C   
14179 O O   . PRO B 728  ? 0.1975 0.2303 0.2006 0.0131  0.0227  -0.0133 726  PRO B O   
14180 C CB  . PRO B 728  ? 0.2137 0.2447 0.2044 0.0134  0.0231  -0.0145 726  PRO B CB  
14181 C CG  . PRO B 728  ? 0.2228 0.2561 0.2154 0.0127  0.0237  -0.0118 726  PRO B CG  
14182 C CD  . PRO B 728  ? 0.2040 0.2368 0.1986 0.0117  0.0214  -0.0108 726  PRO B CD  
14183 N N   . VAL B 729  ? 0.1685 0.1979 0.1676 0.0143  0.0222  -0.0170 727  VAL B N   
14184 C CA  . VAL B 729  ? 0.1804 0.2101 0.1839 0.0149  0.0225  -0.0174 727  VAL B CA  
14185 C C   . VAL B 729  ? 0.2018 0.2320 0.2048 0.0167  0.0243  -0.0186 727  VAL B C   
14186 O O   . VAL B 729  ? 0.1802 0.2083 0.1788 0.0177  0.0246  -0.0203 727  VAL B O   
14187 C CB  . VAL B 729  ? 0.1656 0.1928 0.1696 0.0143  0.0204  -0.0185 727  VAL B CB  
14188 C CG1 . VAL B 729  ? 0.1778 0.2049 0.1854 0.0152  0.0207  -0.0193 727  VAL B CG1 
14189 C CG2 . VAL B 729  ? 0.1694 0.1972 0.1753 0.0130  0.0189  -0.0172 727  VAL B CG2 
14190 N N   . LEU B 730  ? 0.1769 0.2100 0.1846 0.0172  0.0255  -0.0176 728  LEU B N   
14191 C CA  . LEU B 730  ? 0.1912 0.2254 0.2000 0.0191  0.0271  -0.0187 728  LEU B CA  
14192 C C   . LEU B 730  ? 0.1588 0.1918 0.1711 0.0193  0.0257  -0.0194 728  LEU B C   
14193 O O   . LEU B 730  ? 0.1933 0.2278 0.2099 0.0182  0.0251  -0.0181 728  LEU B O   
14194 C CB  . LEU B 730  ? 0.1721 0.2111 0.1840 0.0194  0.0293  -0.0169 728  LEU B CB  
14195 C CG  . LEU B 730  ? 0.1989 0.2399 0.2077 0.0192  0.0311  -0.0158 728  LEU B CG  
14196 C CD1 . LEU B 730  ? 0.1879 0.2263 0.1903 0.0207  0.0315  -0.0178 728  LEU B CD1 
14197 C CD2 . LEU B 730  ? 0.2038 0.2445 0.2125 0.0169  0.0299  -0.0137 728  LEU B CD2 
14198 N N   . ALA B 731  ? 0.1511 0.1808 0.1610 0.0205  0.0250  -0.0215 729  ALA B N   
14199 C CA  . ALA B 731  ? 0.1483 0.1761 0.1606 0.0204  0.0234  -0.0222 729  ALA B CA  
14200 C C   . ALA B 731  ? 0.1761 0.2054 0.1910 0.0226  0.0244  -0.0228 729  ALA B C   
14201 O O   . ALA B 731  ? 0.1691 0.1972 0.1811 0.0248  0.0253  -0.0243 729  ALA B O   
14202 C CB  . ALA B 731  ? 0.1784 0.2012 0.1863 0.0200  0.0215  -0.0238 729  ALA B CB  
14203 N N   . LYS B 732  ? 0.1530 0.1851 0.1733 0.0222  0.0242  -0.0216 730  LYS B N   
14204 C CA  . LYS B 732  ? 0.1656 0.2001 0.1894 0.0240  0.0250  -0.0218 730  LYS B CA  
14205 C C   . LYS B 732  ? 0.1579 0.1899 0.1834 0.0239  0.0229  -0.0224 730  LYS B C   
14206 O O   . LYS B 732  ? 0.1674 0.2006 0.1967 0.0223  0.0219  -0.0212 730  LYS B O   
14207 C CB  . LYS B 732  ? 0.1602 0.2005 0.1889 0.0234  0.0264  -0.0197 730  LYS B CB  
14208 C CG  . LYS B 732  ? 0.1622 0.2069 0.1934 0.0259  0.0284  -0.0198 730  LYS B CG  
14209 C CD  . LYS B 732  ? 0.1829 0.2268 0.2163 0.0276  0.0274  -0.0209 730  LYS B CD  
14210 C CE  . LYS B 732  ? 0.1503 0.1959 0.1889 0.0258  0.0258  -0.0195 730  LYS B CE  
14211 N NZ  . LYS B 732  ? 0.1735 0.2183 0.2139 0.0278  0.0247  -0.0205 730  LYS B NZ  
14212 N N   . PRO B 733  ? 0.1733 0.2013 0.1959 0.0254  0.0221  -0.0242 731  PRO B N   
14213 C CA  . PRO B 733  ? 0.1716 0.1969 0.1953 0.0252  0.0201  -0.0246 731  PRO B CA  
14214 C C   . PRO B 733  ? 0.1728 0.2015 0.2014 0.0267  0.0204  -0.0242 731  PRO B C   
14215 O O   . PRO B 733  ? 0.1685 0.2012 0.1990 0.0286  0.0223  -0.0240 731  PRO B O   
14216 C CB  . PRO B 733  ? 0.1708 0.1905 0.1891 0.0264  0.0193  -0.0266 731  PRO B CB  
14217 C CG  . PRO B 733  ? 0.1765 0.1975 0.1928 0.0289  0.0215  -0.0275 731  PRO B CG  
14218 C CD  . PRO B 733  ? 0.1957 0.2212 0.2134 0.0275  0.0231  -0.0259 731  PRO B CD  
14219 N N   . ALA B 734  ? 0.1650 0.1924 0.1956 0.0260  0.0186  -0.0240 732  ALA B N   
14220 C CA  . ALA B 734  ? 0.1645 0.1947 0.1996 0.0274  0.0183  -0.0236 732  ALA B CA  
14221 C C   . ALA B 734  ? 0.2006 0.2302 0.2344 0.0309  0.0191  -0.0249 732  ALA B C   
14222 O O   . ALA B 734  ? 0.2018 0.2264 0.2305 0.0319  0.0188  -0.0265 732  ALA B O   
14223 C CB  . ALA B 734  ? 0.1704 0.1981 0.2064 0.0261  0.0159  -0.0235 732  ALA B CB  
14224 N N   . GLU B 735  ? 0.1547 0.1895 0.1931 0.0327  0.0201  -0.0243 733  GLU B N   
14225 C CA  . GLU B 735  ? 0.1901 0.2250 0.2275 0.0366  0.0211  -0.0256 733  GLU B CA  
14226 C C   . GLU B 735  ? 0.1832 0.2121 0.2180 0.0380  0.0190  -0.0269 733  GLU B C   
14227 O O   . GLU B 735  ? 0.1636 0.1894 0.1949 0.0411  0.0194  -0.0285 733  GLU B O   
14228 C CB  . GLU B 735  ? 0.2248 0.2675 0.2684 0.0382  0.0226  -0.0243 733  GLU B CB  
14229 C CG  . GLU B 735  ? 0.2373 0.2830 0.2865 0.0367  0.0208  -0.0229 733  GLU B CG  
14230 C CD  . GLU B 735  ? 0.2656 0.3150 0.3182 0.0330  0.0209  -0.0209 733  GLU B CD  
14231 O OE1 . GLU B 735  ? 0.2158 0.2631 0.2654 0.0309  0.0213  -0.0208 733  GLU B OE1 
14232 O OE2 . GLU B 735  ? 0.2806 0.3350 0.3388 0.0322  0.0204  -0.0194 733  GLU B OE2 
14233 N N   . GLU B 736  ? 0.1818 0.2086 0.2177 0.0359  0.0167  -0.0263 734  GLU B N   
14234 C CA  . GLU B 736  ? 0.1848 0.2059 0.2181 0.0370  0.0145  -0.0273 734  GLU B CA  
14235 C C   . GLU B 736  ? 0.2120 0.2255 0.2383 0.0363  0.0138  -0.0287 734  GLU B C   
14236 O O   . GLU B 736  ? 0.2121 0.2202 0.2350 0.0379  0.0125  -0.0298 734  GLU B O   
14237 C CB  . GLU B 736  ? 0.1939 0.2153 0.2301 0.0347  0.0124  -0.0261 734  GLU B CB  
14238 C CG  . GLU B 736  ? 0.1951 0.2229 0.2379 0.0352  0.0124  -0.0248 734  GLU B CG  
14239 C CD  . GLU B 736  ? 0.2059 0.2388 0.2524 0.0324  0.0133  -0.0233 734  GLU B CD  
14240 O OE1 . GLU B 736  ? 0.1896 0.2220 0.2339 0.0308  0.0144  -0.0233 734  GLU B OE1 
14241 O OE2 . GLU B 736  ? 0.2704 0.3078 0.3221 0.0318  0.0126  -0.0220 734  GLU B OE2 
14242 N N   . THR B 737  ? 0.1831 0.1960 0.2071 0.0337  0.0143  -0.0286 735  THR B N   
14243 C CA  . THR B 737  ? 0.2040 0.2104 0.2221 0.0321  0.0130  -0.0295 735  THR B CA  
14244 C C   . THR B 737  ? 0.1797 0.1857 0.1942 0.0317  0.0145  -0.0302 735  THR B C   
14245 O O   . THR B 737  ? 0.1976 0.2027 0.2103 0.0289  0.0141  -0.0298 735  THR B O   
14246 C CB  . THR B 737  ? 0.1940 0.1997 0.2128 0.0286  0.0114  -0.0285 735  THR B CB  
14247 O OG1 . THR B 737  ? 0.1750 0.1861 0.1977 0.0269  0.0124  -0.0272 735  THR B OG1 
14248 C CG2 . THR B 737  ? 0.1924 0.1970 0.2132 0.0290  0.0096  -0.0281 735  THR B CG2 
14249 N N   . PRO B 738  ? 0.1960 0.2027 0.2092 0.0347  0.0162  -0.0312 736  PRO B N   
14250 C CA  . PRO B 738  ? 0.1781 0.1844 0.1874 0.0344  0.0176  -0.0319 736  PRO B CA  
14251 C C   . PRO B 738  ? 0.1980 0.1967 0.2002 0.0336  0.0162  -0.0334 736  PRO B C   
14252 O O   . PRO B 738  ? 0.1993 0.1975 0.1984 0.0320  0.0166  -0.0336 736  PRO B O   
14253 C CB  . PRO B 738  ? 0.1682 0.1776 0.1782 0.0383  0.0200  -0.0325 736  PRO B CB  
14254 C CG  . PRO B 738  ? 0.2044 0.2116 0.2152 0.0411  0.0190  -0.0333 736  PRO B CG  
14255 C CD  . PRO B 738  ? 0.2024 0.2103 0.2173 0.0387  0.0170  -0.0319 736  PRO B CD  
14256 N N   . LEU B 739  ? 0.1906 0.1834 0.1901 0.0344  0.0144  -0.0344 737  LEU B N   
14257 C CA  . LEU B 739  ? 0.2121 0.1972 0.2043 0.0337  0.0130  -0.0359 737  LEU B CA  
14258 C C   . LEU B 739  ? 0.2252 0.2090 0.2159 0.0293  0.0115  -0.0351 737  LEU B C   
14259 O O   . LEU B 739  ? 0.2097 0.1910 0.1958 0.0280  0.0113  -0.0358 737  LEU B O   
14260 C CB  . LEU B 739  ? 0.2013 0.1799 0.1908 0.0356  0.0113  -0.0370 737  LEU B CB  
14261 C CG  . LEU B 739  ? 0.2079 0.1876 0.1986 0.0406  0.0127  -0.0379 737  LEU B CG  
14262 C CD1 . LEU B 739  ? 0.2218 0.1946 0.2098 0.0423  0.0106  -0.0387 737  LEU B CD1 
14263 C CD2 . LEU B 739  ? 0.2106 0.1898 0.1974 0.0431  0.0147  -0.0395 737  LEU B CD2 
14264 N N   . ILE B 740  ? 0.2044 0.1900 0.1987 0.0271  0.0103  -0.0336 738  ILE B N   
14265 C CA  . ILE B 740  ? 0.1759 0.1610 0.1690 0.0231  0.0090  -0.0328 738  ILE B CA  
14266 C C   . ILE B 740  ? 0.1945 0.1849 0.1894 0.0220  0.0105  -0.0320 738  ILE B C   
14267 O O   . ILE B 740  ? 0.2041 0.1937 0.1964 0.0195  0.0098  -0.0319 738  ILE B O   
14268 C CB  . ILE B 740  ? 0.2279 0.2137 0.2242 0.0213  0.0076  -0.0315 738  ILE B CB  
14269 C CG1 . ILE B 740  ? 0.2057 0.1911 0.2005 0.0175  0.0064  -0.0308 738  ILE B CG1 
14270 C CG2 . ILE B 740  ? 0.2164 0.2087 0.2192 0.0222  0.0088  -0.0303 738  ILE B CG2 
14271 C CD1 . ILE B 740  ? 0.2426 0.2212 0.2310 0.0160  0.0046  -0.0317 738  ILE B CD1 
14272 N N   . ALA B 741  ? 0.1948 0.1907 0.1940 0.0237  0.0125  -0.0314 739  ALA B N   
14273 C CA  . ALA B 741  ? 0.1899 0.1903 0.1904 0.0228  0.0139  -0.0305 739  ALA B CA  
14274 C C   . ALA B 741  ? 0.2067 0.2046 0.2017 0.0233  0.0145  -0.0318 739  ALA B C   
14275 O O   . ALA B 741  ? 0.1984 0.1969 0.1915 0.0213  0.0143  -0.0313 739  ALA B O   
14276 C CB  . ALA B 741  ? 0.1710 0.1773 0.1768 0.0245  0.0159  -0.0295 739  ALA B CB  
14277 N N   . ALA B 742  ? 0.2059 0.2009 0.1979 0.0263  0.0152  -0.0334 740  ALA B N   
14278 C CA  . ALA B 742  ? 0.2255 0.2172 0.2114 0.0270  0.0157  -0.0349 740  ALA B CA  
14279 C C   . ALA B 742  ? 0.2149 0.2012 0.1957 0.0240  0.0133  -0.0354 740  ALA B C   
14280 O O   . ALA B 742  ? 0.2098 0.1955 0.1869 0.0227  0.0133  -0.0357 740  ALA B O   
14281 C CB  . ALA B 742  ? 0.2165 0.2049 0.1996 0.0309  0.0165  -0.0368 740  ALA B CB  
14282 N N   . GLU B 743  ? 0.2264 0.2091 0.2071 0.0227  0.0112  -0.0354 741  GLU B N   
14283 C CA  . GLU B 743  ? 0.2246 0.2026 0.2008 0.0195  0.0089  -0.0356 741  GLU B CA  
14284 C C   . GLU B 743  ? 0.1907 0.1735 0.1694 0.0162  0.0086  -0.0339 741  GLU B C   
14285 O O   . GLU B 743  ? 0.2263 0.2076 0.2012 0.0140  0.0075  -0.0341 741  GLU B O   
14286 C CB  . GLU B 743  ? 0.2552 0.2286 0.2308 0.0188  0.0069  -0.0357 741  GLU B CB  
14287 C CG  . GLU B 743  ? 0.2341 0.2029 0.2054 0.0150  0.0043  -0.0357 741  GLU B CG  
14288 C CD  . GLU B 743  ? 0.2836 0.2455 0.2473 0.0151  0.0034  -0.0376 741  GLU B CD  
14289 O OE1 . GLU B 743  ? 0.2594 0.2194 0.2206 0.0185  0.0047  -0.0392 741  GLU B OE1 
14290 O OE2 . GLU B 743  ? 0.2942 0.2525 0.2541 0.0117  0.0012  -0.0375 741  GLU B OE2 
14291 N N   . GLY B 744  ? 0.2030 0.1915 0.1878 0.0161  0.0094  -0.0323 742  GLY B N   
14292 C CA  . GLY B 744  ? 0.2014 0.1946 0.1888 0.0137  0.0094  -0.0307 742  GLY B CA  
14293 C C   . GLY B 744  ? 0.2023 0.1974 0.1875 0.0139  0.0104  -0.0308 742  GLY B C   
14294 O O   . GLY B 744  ? 0.1974 0.1933 0.1812 0.0116  0.0095  -0.0302 742  GLY B O   
14295 N N   . VAL B 745  ? 0.1956 0.1916 0.1807 0.0166  0.0124  -0.0314 743  VAL B N   
14296 C CA  . VAL B 745  ? 0.1909 0.1885 0.1735 0.0169  0.0136  -0.0314 743  VAL B CA  
14297 C C   . VAL B 745  ? 0.2137 0.2059 0.1891 0.0161  0.0122  -0.0330 743  VAL B C   
14298 O O   . VAL B 745  ? 0.2292 0.2224 0.2022 0.0145  0.0118  -0.0327 743  VAL B O   
14299 C CB  . VAL B 745  ? 0.2028 0.2033 0.1872 0.0200  0.0162  -0.0316 743  VAL B CB  
14300 C CG1 . VAL B 745  ? 0.1866 0.1874 0.1667 0.0206  0.0175  -0.0320 743  VAL B CG1 
14301 C CG2 . VAL B 745  ? 0.1982 0.2046 0.1894 0.0199  0.0173  -0.0296 743  VAL B CG2 
14302 N N   . ARG B 746  ? 0.2101 0.1963 0.1818 0.0170  0.0113  -0.0348 744  ARG B N   
14303 C CA  . ARG B 746  ? 0.2093 0.1894 0.1737 0.0158  0.0096  -0.0363 744  ARG B CA  
14304 C C   . ARG B 746  ? 0.2029 0.1836 0.1670 0.0116  0.0073  -0.0352 744  ARG B C   
14305 O O   . ARG B 746  ? 0.2247 0.2044 0.1846 0.0100  0.0063  -0.0355 744  ARG B O   
14306 C CB  . ARG B 746  ? 0.2265 0.1992 0.1871 0.0169  0.0084  -0.0381 744  ARG B CB  
14307 C CG  . ARG B 746  ? 0.2519 0.2228 0.2111 0.0214  0.0103  -0.0398 744  ARG B CG  
14308 C CD  . ARG B 746  ? 0.2390 0.2017 0.1938 0.0225  0.0087  -0.0415 744  ARG B CD  
14309 N NE  . ARG B 746  ? 0.2732 0.2352 0.2281 0.0272  0.0106  -0.0428 744  ARG B NE  
14310 C CZ  . ARG B 746  ? 0.2249 0.1892 0.1850 0.0293  0.0114  -0.0422 744  ARG B CZ  
14311 N NH1 . ARG B 746  ? 0.2409 0.2064 0.2052 0.0271  0.0100  -0.0407 744  ARG B NH1 
14312 N NH2 . ARG B 746  ? 0.2505 0.2162 0.2114 0.0337  0.0135  -0.0432 744  ARG B NH2 
14313 N N   . ILE B 747  ? 0.2051 0.1878 0.1737 0.0100  0.0064  -0.0338 745  ILE B N   
14314 C CA  . ILE B 747  ? 0.1890 0.1727 0.1576 0.0062  0.0042  -0.0327 745  ILE B CA  
14315 C C   . ILE B 747  ? 0.2015 0.1914 0.1726 0.0052  0.0048  -0.0312 745  ILE B C   
14316 O O   . ILE B 747  ? 0.2065 0.1967 0.1750 0.0027  0.0032  -0.0308 745  ILE B O   
14317 C CB  . ILE B 747  ? 0.2072 0.1916 0.1798 0.0050  0.0034  -0.0317 745  ILE B CB  
14318 C CG1 . ILE B 747  ? 0.2299 0.2069 0.1984 0.0050  0.0020  -0.0330 745  ILE B CG1 
14319 C CG2 . ILE B 747  ? 0.2142 0.2024 0.1887 0.0015  0.0020  -0.0300 745  ILE B CG2 
14320 C CD1 . ILE B 747  ? 0.2315 0.2086 0.2034 0.0043  0.0013  -0.0321 745  ILE B CD1 
14321 N N   . LEU B 748  ? 0.1991 0.1939 0.1749 0.0071  0.0069  -0.0302 746  LEU B N   
14322 C CA  . LEU B 748  ? 0.1864 0.1865 0.1642 0.0065  0.0074  -0.0286 746  LEU B CA  
14323 C C   . LEU B 748  ? 0.2023 0.2010 0.1749 0.0067  0.0076  -0.0294 746  LEU B C   
14324 O O   . LEU B 748  ? 0.1940 0.1949 0.1656 0.0049  0.0065  -0.0285 746  LEU B O   
14325 C CB  . LEU B 748  ? 0.2019 0.2066 0.1853 0.0084  0.0095  -0.0274 746  LEU B CB  
14326 C CG  . LEU B 748  ? 0.2430 0.2505 0.2317 0.0077  0.0091  -0.0261 746  LEU B CG  
14327 C CD1 . LEU B 748  ? 0.1902 0.2004 0.1837 0.0097  0.0110  -0.0254 746  LEU B CD1 
14328 C CD2 . LEU B 748  ? 0.2584 0.2696 0.2485 0.0058  0.0082  -0.0246 746  LEU B CD2 
14329 N N   . ARG B 749  ? 0.1973 0.1926 0.1663 0.0090  0.0088  -0.0311 747  ARG B N   
14330 C CA  . ARG B 749  ? 0.2104 0.2038 0.1736 0.0092  0.0089  -0.0321 747  ARG B CA  
14331 C C   . ARG B 749  ? 0.2241 0.2131 0.1818 0.0064  0.0061  -0.0329 747  ARG B C   
14332 O O   . ARG B 749  ? 0.2148 0.2046 0.1694 0.0049  0.0051  -0.0326 747  ARG B O   
14333 C CB  . ARG B 749  ? 0.2170 0.2076 0.1773 0.0126  0.0109  -0.0339 747  ARG B CB  
14334 C CG  . ARG B 749  ? 0.2142 0.2101 0.1789 0.0150  0.0139  -0.0328 747  ARG B CG  
14335 C CD  . ARG B 749  ? 0.2310 0.2248 0.1923 0.0183  0.0160  -0.0345 747  ARG B CD  
14336 N NE  . ARG B 749  ? 0.2209 0.2203 0.1861 0.0202  0.0188  -0.0333 747  ARG B NE  
14337 C CZ  . ARG B 749  ? 0.2878 0.2874 0.2506 0.0231  0.0212  -0.0343 747  ARG B CZ  
14338 N NH1 . ARG B 749  ? 0.3322 0.3262 0.2882 0.0247  0.0210  -0.0368 747  ARG B NH1 
14339 N NH2 . ARG B 749  ? 0.2895 0.2948 0.2565 0.0245  0.0237  -0.0329 747  ARG B NH2 
14340 N N   . GLU B 750  ? 0.2194 0.2037 0.1758 0.0055  0.0045  -0.0339 748  GLU B N   
14341 C CA  . GLU B 750  ? 0.2441 0.2239 0.1953 0.0023  0.0016  -0.0346 748  GLU B CA  
14342 C C   . GLU B 750  ? 0.2129 0.1979 0.1670 -0.0010 0.0000  -0.0325 748  GLU B C   
14343 O O   . GLU B 750  ? 0.2342 0.2181 0.1842 -0.0035 -0.0021 -0.0326 748  GLU B O   
14344 C CB  . GLU B 750  ? 0.2334 0.2074 0.1833 0.0017  0.0002  -0.0356 748  GLU B CB  
14345 C CG  . GLU B 750  ? 0.2595 0.2282 0.2036 -0.0019 -0.0030 -0.0363 748  GLU B CG  
14346 C CD  . GLU B 750  ? 0.2852 0.2473 0.2274 -0.0024 -0.0044 -0.0371 748  GLU B CD  
14347 O OE1 . GLU B 750  ? 0.2956 0.2567 0.2400 0.0006  -0.0028 -0.0377 748  GLU B OE1 
14348 O OE2 . GLU B 750  ? 0.3005 0.2587 0.2389 -0.0060 -0.0072 -0.0372 748  GLU B OE2 
14349 N N   . ALA B 751  ? 0.2316 0.2226 0.1927 -0.0009 0.0009  -0.0306 749  ALA B N   
14350 C CA  . ALA B 751  ? 0.2371 0.2337 0.2016 -0.0034 -0.0004 -0.0286 749  ALA B CA  
14351 C C   . ALA B 751  ? 0.2261 0.2269 0.1906 -0.0031 0.0001  -0.0276 749  ALA B C   
14352 O O   . ALA B 751  ? 0.2266 0.2322 0.1936 -0.0049 -0.0011 -0.0259 749  ALA B O   
14353 C CB  . ALA B 751  ? 0.2134 0.2143 0.1848 -0.0029 0.0005  -0.0271 749  ALA B CB  
14354 N N   . GLY B 752  ? 0.2139 0.2134 0.1758 -0.0006 0.0018  -0.0284 750  GLY B N   
14355 C CA  . GLY B 752  ? 0.2372 0.2402 0.1982 -0.0005 0.0021  -0.0274 750  GLY B CA  
14356 C C   . GLY B 752  ? 0.2373 0.2437 0.2014 0.0023  0.0049  -0.0265 750  GLY B C   
14357 O O   . GLY B 752  ? 0.2384 0.2471 0.2012 0.0026  0.0053  -0.0256 750  GLY B O   
14358 N N   . ILE B 753  ? 0.2112 0.2178 0.1793 0.0042  0.0068  -0.0266 751  ILE B N   
14359 C CA  . ILE B 753  ? 0.1994 0.2092 0.1705 0.0065  0.0093  -0.0256 751  ILE B CA  
14360 C C   . ILE B 753  ? 0.2350 0.2423 0.2011 0.0083  0.0109  -0.0270 751  ILE B C   
14361 O O   . ILE B 753  ? 0.2489 0.2519 0.2122 0.0095  0.0113  -0.0290 751  ILE B O   
14362 C CB  . ILE B 753  ? 0.1611 0.1722 0.1379 0.0079  0.0106  -0.0253 751  ILE B CB  
14363 C CG1 . ILE B 753  ? 0.1966 0.2097 0.1778 0.0062  0.0091  -0.0242 751  ILE B CG1 
14364 C CG2 . ILE B 753  ? 0.1931 0.2075 0.1729 0.0097  0.0130  -0.0241 751  ILE B CG2 
14365 C CD1 . ILE B 753  ? 0.2002 0.2180 0.1842 0.0055  0.0087  -0.0220 751  ILE B CD1 
14366 N N   . PRO B 754  ? 0.2161 0.2257 0.1806 0.0088  0.0119  -0.0261 752  PRO B N   
14367 C CA  . PRO B 754  ? 0.2207 0.2282 0.1799 0.0106  0.0136  -0.0274 752  PRO B CA  
14368 C C   . PRO B 754  ? 0.2305 0.2382 0.1921 0.0134  0.0163  -0.0281 752  PRO B C   
14369 O O   . PRO B 754  ? 0.2330 0.2439 0.2009 0.0138  0.0172  -0.0268 752  PRO B O   
14370 C CB  . PRO B 754  ? 0.2517 0.2628 0.2102 0.0103  0.0142  -0.0255 752  PRO B CB  
14371 C CG  . PRO B 754  ? 0.2970 0.3108 0.2587 0.0081  0.0119  -0.0237 752  PRO B CG  
14372 C CD  . PRO B 754  ? 0.2187 0.2328 0.1857 0.0077  0.0114  -0.0237 752  PRO B CD  
14373 N N   . ALA B 755  ? 0.2609 0.2654 0.2175 0.0153  0.0175  -0.0301 753  ALA B N   
14374 C CA  . ALA B 755  ? 0.3025 0.3077 0.2612 0.0182  0.0202  -0.0308 753  ALA B CA  
14375 C C   . ALA B 755  ? 0.2521 0.2635 0.2156 0.0189  0.0226  -0.0285 753  ALA B C   
14376 O O   . ALA B 755  ? 0.2560 0.2701 0.2250 0.0202  0.0240  -0.0279 753  ALA B O   
14377 C CB  . ALA B 755  ? 0.3051 0.3062 0.2569 0.0206  0.0212  -0.0333 753  ALA B CB  
14378 N N   . SER B 756  ? 0.2352 0.2489 0.1969 0.0180  0.0229  -0.0270 754  SER B N   
14379 C CA  . SER B 756  ? 0.2367 0.2558 0.2027 0.0184  0.0250  -0.0246 754  SER B CA  
14380 C C   . SER B 756  ? 0.2241 0.2458 0.1970 0.0168  0.0239  -0.0225 754  SER B C   
14381 O O   . SER B 756  ? 0.2469 0.2723 0.2242 0.0171  0.0255  -0.0207 754  SER B O   
14382 C CB  . SER B 756  ? 0.2481 0.2684 0.2098 0.0178  0.0255  -0.0234 754  SER B CB  
14383 O OG  . SER B 756  ? 0.3154 0.3345 0.2754 0.0155  0.0226  -0.0228 754  SER B OG  
14384 N N   . ALA B 757  ? 0.1897 0.2096 0.1633 0.0151  0.0213  -0.0227 755  ALA B N   
14385 C CA  . ALA B 757  ? 0.1922 0.2143 0.1718 0.0140  0.0204  -0.0210 755  ALA B CA  
14386 C C   . ALA B 757  ? 0.1981 0.2198 0.1821 0.0147  0.0206  -0.0218 755  ALA B C   
14387 O O   . ALA B 757  ? 0.2068 0.2304 0.1959 0.0142  0.0202  -0.0204 755  ALA B O   
14388 C CB  . ALA B 757  ? 0.2064 0.2277 0.1851 0.0119  0.0176  -0.0206 755  ALA B CB  
14389 N N   . LEU B 758  ? 0.1995 0.2182 0.1814 0.0161  0.0209  -0.0239 756  LEU B N   
14390 C CA  . LEU B 758  ? 0.2020 0.2201 0.1878 0.0168  0.0208  -0.0246 756  LEU B CA  
14391 C C   . LEU B 758  ? 0.1931 0.2099 0.1772 0.0194  0.0225  -0.0263 756  LEU B C   
14392 O O   . LEU B 758  ? 0.2059 0.2184 0.1848 0.0201  0.0220  -0.0284 756  LEU B O   
14393 C CB  . LEU B 758  ? 0.1840 0.1989 0.1692 0.0152  0.0182  -0.0254 756  LEU B CB  
14394 C CG  . LEU B 758  ? 0.2088 0.2224 0.1972 0.0159  0.0178  -0.0261 756  LEU B CG  
14395 C CD1 . LEU B 758  ? 0.1857 0.2032 0.1806 0.0161  0.0187  -0.0245 756  LEU B CD1 
14396 C CD2 . LEU B 758  ? 0.2203 0.2308 0.2075 0.0139  0.0153  -0.0267 756  LEU B CD2 
14397 N N   . GLN B 759  ? 0.1939 0.2143 0.1824 0.0208  0.0245  -0.0254 757  GLN B N   
14398 C CA  . GLN B 759  ? 0.1873 0.2080 0.1753 0.0236  0.0265  -0.0267 757  GLN B CA  
14399 C C   . GLN B 759  ? 0.1958 0.2172 0.1892 0.0243  0.0262  -0.0267 757  GLN B C   
14400 O O   . GLN B 759  ? 0.2118 0.2358 0.2103 0.0228  0.0257  -0.0250 757  GLN B O   
14401 C CB  . GLN B 759  ? 0.1812 0.2066 0.1698 0.0246  0.0293  -0.0254 757  GLN B CB  
14402 C CG  . GLN B 759  ? 0.2007 0.2250 0.1831 0.0242  0.0297  -0.0257 757  GLN B CG  
14403 C CD  . GLN B 759  ? 0.2013 0.2305 0.1842 0.0247  0.0323  -0.0239 757  GLN B CD  
14404 O OE1 . GLN B 759  ? 0.2462 0.2765 0.2266 0.0270  0.0346  -0.0249 757  GLN B OE1 
14405 N NE2 . GLN B 759  ? 0.2011 0.2334 0.1873 0.0226  0.0321  -0.0214 757  GLN B NE2 
14406 N N   . LEU B 760  ? 0.1785 0.1973 0.1704 0.0266  0.0264  -0.0286 758  LEU B N   
14407 C CA  . LEU B 760  ? 0.1732 0.1923 0.1696 0.0276  0.0260  -0.0287 758  LEU B CA  
14408 C C   . LEU B 760  ? 0.1958 0.2194 0.1952 0.0305  0.0286  -0.0286 758  LEU B C   
14409 O O   . LEU B 760  ? 0.1946 0.2173 0.1902 0.0330  0.0302  -0.0300 758  LEU B O   
14410 C CB  . LEU B 760  ? 0.1895 0.2022 0.1824 0.0283  0.0241  -0.0309 758  LEU B CB  
14411 C CG  . LEU B 760  ? 0.1839 0.1966 0.1810 0.0294  0.0235  -0.0309 758  LEU B CG  
14412 C CD1 . LEU B 760  ? 0.1895 0.2023 0.1901 0.0265  0.0214  -0.0296 758  LEU B CD1 
14413 C CD2 . LEU B 760  ? 0.1964 0.2029 0.1890 0.0316  0.0226  -0.0333 758  LEU B CD2 
14414 N N   . LEU B 761  ? 0.1865 0.2147 0.1925 0.0301  0.0290  -0.0269 759  LEU B N   
14415 C CA  . LEU B 761  ? 0.1697 0.2034 0.1796 0.0324  0.0314  -0.0263 759  LEU B CA  
14416 C C   . LEU B 761  ? 0.1901 0.2241 0.2045 0.0334  0.0303  -0.0265 759  LEU B C   
14417 O O   . LEU B 761  ? 0.1947 0.2320 0.2147 0.0317  0.0297  -0.0248 759  LEU B O   
14418 C CB  . LEU B 761  ? 0.1772 0.2171 0.1910 0.0307  0.0329  -0.0238 759  LEU B CB  
14419 C CG  . LEU B 761  ? 0.1969 0.2375 0.2067 0.0297  0.0342  -0.0231 759  LEU B CG  
14420 C CD1 . LEU B 761  ? 0.2163 0.2548 0.2199 0.0324  0.0357  -0.0252 759  LEU B CD1 
14421 C CD2 . LEU B 761  ? 0.2095 0.2466 0.2173 0.0267  0.0320  -0.0224 759  LEU B CD2 
14422 N N   . PRO B 762  ? 0.1685 0.1987 0.1804 0.0361  0.0298  -0.0286 760  PRO B N   
14423 C CA  . PRO B 762  ? 0.1924 0.2230 0.2086 0.0373  0.0288  -0.0286 760  PRO B CA  
14424 C C   . PRO B 762  ? 0.1779 0.2162 0.2001 0.0389  0.0308  -0.0273 760  PRO B C   
14425 O O   . PRO B 762  ? 0.1991 0.2417 0.2212 0.0403  0.0334  -0.0270 760  PRO B O   
14426 C CB  . PRO B 762  ? 0.1863 0.2107 0.1974 0.0402  0.0281  -0.0312 760  PRO B CB  
14427 C CG  . PRO B 762  ? 0.1959 0.2154 0.1997 0.0394  0.0280  -0.0324 760  PRO B CG  
14428 C CD  . PRO B 762  ? 0.1744 0.1992 0.1792 0.0382  0.0301  -0.0309 760  PRO B CD  
14429 N N   . GLY B 763  ? 0.1775 0.2178 0.2051 0.0386  0.0296  -0.0264 761  GLY B N   
14430 C CA  . GLY B 763  ? 0.1874 0.2352 0.2213 0.0401  0.0311  -0.0251 761  GLY B CA  
14431 C C   . GLY B 763  ? 0.1778 0.2283 0.2176 0.0373  0.0294  -0.0232 761  GLY B C   
14432 O O   . GLY B 763  ? 0.1743 0.2204 0.2131 0.0349  0.0271  -0.0232 761  GLY B O   
14433 N N   . ASP B 764  ? 0.2007 0.2585 0.2466 0.0377  0.0305  -0.0216 762  ASP B N   
14434 C CA  . ASP B 764  ? 0.1790 0.2391 0.2304 0.0353  0.0286  -0.0200 762  ASP B CA  
14435 C C   . ASP B 764  ? 0.1968 0.2598 0.2502 0.0315  0.0290  -0.0178 762  ASP B C   
14436 O O   . ASP B 764  ? 0.1909 0.2524 0.2406 0.0304  0.0301  -0.0177 762  ASP B O   
14437 C CB  . ASP B 764  ? 0.2138 0.2799 0.2708 0.0377  0.0290  -0.0194 762  ASP B CB  
14438 C CG  . ASP B 764  ? 0.2497 0.3243 0.3103 0.0387  0.0320  -0.0181 762  ASP B CG  
14439 O OD1 . ASP B 764  ? 0.2185 0.2951 0.2782 0.0368  0.0337  -0.0170 762  ASP B OD1 
14440 O OD2 . ASP B 764  ? 0.3478 0.4275 0.4122 0.0417  0.0328  -0.0180 762  ASP B OD2 
14441 N N   . GLY B 765  ? 0.1980 0.2646 0.2569 0.0294  0.0279  -0.0160 763  GLY B N   
14442 C CA  . GLY B 765  ? 0.1935 0.2615 0.2540 0.0256  0.0277  -0.0140 763  GLY B CA  
14443 C C   . GLY B 765  ? 0.1733 0.2468 0.2346 0.0252  0.0306  -0.0124 763  GLY B C   
14444 O O   . GLY B 765  ? 0.2036 0.2765 0.2640 0.0224  0.0306  -0.0110 763  GLY B O   
14445 N N   . ARG B 766  ? 0.1893 0.2682 0.2522 0.0281  0.0329  -0.0126 764  ARG B N   
14446 C CA  . ARG B 766  ? 0.2204 0.3046 0.2834 0.0280  0.0359  -0.0112 764  ARG B CA  
14447 C C   . ARG B 766  ? 0.1949 0.2741 0.2510 0.0280  0.0368  -0.0122 764  ARG B C   
14448 O O   . ARG B 766  ? 0.2045 0.2857 0.2596 0.0262  0.0383  -0.0106 764  ARG B O   
14449 C CB  . ARG B 766  ? 0.2235 0.3141 0.2889 0.0318  0.0384  -0.0116 764  ARG B CB  
14450 C CG  . ARG B 766  ? 0.3140 0.4113 0.3869 0.0320  0.0377  -0.0103 764  ARG B CG  
14451 C CD  . ARG B 766  ? 0.3033 0.4058 0.3777 0.0369  0.0400  -0.0113 764  ARG B CD  
14452 N NE  . ARG B 766  ? 0.3774 0.4728 0.4465 0.0405  0.0392  -0.0144 764  ARG B NE  
14453 C CZ  . ARG B 766  ? 0.4164 0.5132 0.4845 0.0454  0.0408  -0.0161 764  ARG B CZ  
14454 N NH1 . ARG B 766  ? 0.3811 0.4872 0.4537 0.0476  0.0435  -0.0150 764  ARG B NH1 
14455 N NH2 . ARG B 766  ? 0.4103 0.4992 0.4730 0.0481  0.0396  -0.0188 764  ARG B NH2 
14456 N N   . VAL B 767  ? 0.1862 0.2588 0.2371 0.0300  0.0358  -0.0148 765  VAL B N   
14457 C CA  . VAL B 767  ? 0.1743 0.2420 0.2186 0.0297  0.0362  -0.0158 765  VAL B CA  
14458 C C   . VAL B 767  ? 0.1709 0.2352 0.2143 0.0259  0.0344  -0.0146 765  VAL B C   
14459 O O   . VAL B 767  ? 0.1839 0.2480 0.2247 0.0245  0.0352  -0.0136 765  VAL B O   
14460 C CB  . VAL B 767  ? 0.1612 0.2227 0.2002 0.0325  0.0354  -0.0187 765  VAL B CB  
14461 C CG1 . VAL B 767  ? 0.1903 0.2469 0.2225 0.0319  0.0356  -0.0197 765  VAL B CG1 
14462 C CG2 . VAL B 767  ? 0.1968 0.2614 0.2362 0.0367  0.0374  -0.0200 765  VAL B CG2 
14463 N N   . GLY B 768  ? 0.1606 0.2223 0.2063 0.0244  0.0318  -0.0145 766  GLY B N   
14464 C CA  . GLY B 768  ? 0.1789 0.2379 0.2243 0.0212  0.0301  -0.0133 766  GLY B CA  
14465 C C   . GLY B 768  ? 0.1860 0.2495 0.2343 0.0188  0.0312  -0.0106 766  GLY B C   
14466 O O   . GLY B 768  ? 0.1756 0.2374 0.2214 0.0170  0.0313  -0.0096 766  GLY B O   
14467 N N   . ALA B 769  ? 0.1776 0.2472 0.2312 0.0188  0.0322  -0.0092 767  ALA B N   
14468 C CA  . ALA B 769  ? 0.1720 0.2458 0.2285 0.0160  0.0330  -0.0064 767  ALA B CA  
14469 C C   . ALA B 769  ? 0.1990 0.2748 0.2522 0.0163  0.0357  -0.0056 767  ALA B C   
14470 O O   . ALA B 769  ? 0.1767 0.2522 0.2291 0.0137  0.0358  -0.0036 767  ALA B O   
14471 C CB  . ALA B 769  ? 0.1802 0.2608 0.2433 0.0158  0.0334  -0.0050 767  ALA B CB  
14472 N N   . ALA B 770  ? 0.1795 0.2571 0.2305 0.0195  0.0378  -0.0071 768  ALA B N   
14473 C CA  . ALA B 770  ? 0.1749 0.2542 0.2220 0.0200  0.0404  -0.0066 768  ALA B CA  
14474 C C   . ALA B 770  ? 0.1865 0.2595 0.2279 0.0188  0.0392  -0.0070 768  ALA B C   
14475 O O   . ALA B 770  ? 0.2268 0.3007 0.2660 0.0173  0.0404  -0.0053 768  ALA B O   
14476 C CB  . ALA B 770  ? 0.2026 0.2839 0.2477 0.0241  0.0426  -0.0087 768  ALA B CB  
14477 N N   . LEU B 771  ? 0.1651 0.2320 0.2039 0.0194  0.0370  -0.0091 769  LEU B N   
14478 C CA  . LEU B 771  ? 0.1923 0.2538 0.2262 0.0182  0.0357  -0.0094 769  LEU B CA  
14479 C C   . LEU B 771  ? 0.1863 0.2471 0.2220 0.0149  0.0344  -0.0070 769  LEU B C   
14480 O O   . LEU B 771  ? 0.2160 0.2756 0.2486 0.0137  0.0346  -0.0058 769  LEU B O   
14481 C CB  . LEU B 771  ? 0.1929 0.2487 0.2244 0.0193  0.0335  -0.0119 769  LEU B CB  
14482 C CG  . LEU B 771  ? 0.1884 0.2427 0.2162 0.0223  0.0344  -0.0145 769  LEU B CG  
14483 C CD1 . LEU B 771  ? 0.2008 0.2497 0.2271 0.0228  0.0319  -0.0165 769  LEU B CD1 
14484 C CD2 . LEU B 771  ? 0.1881 0.2414 0.2100 0.0228  0.0358  -0.0148 769  LEU B CD2 
14485 N N   . VAL B 772  ? 0.1727 0.2340 0.2132 0.0136  0.0328  -0.0063 770  VAL B N   
14486 C CA  . VAL B 772  ? 0.1828 0.2424 0.2246 0.0107  0.0313  -0.0042 770  VAL B CA  
14487 C C   . VAL B 772  ? 0.2091 0.2725 0.2516 0.0089  0.0330  -0.0014 770  VAL B C   
14488 O O   . VAL B 772  ? 0.2309 0.2918 0.2715 0.0070  0.0323  0.0002  770  VAL B O   
14489 C CB  . VAL B 772  ? 0.1753 0.2349 0.2219 0.0097  0.0294  -0.0042 770  VAL B CB  
14490 C CG1 . VAL B 772  ? 0.2051 0.2638 0.2536 0.0066  0.0282  -0.0018 770  VAL B CG1 
14491 C CG2 . VAL B 772  ? 0.1867 0.2414 0.2318 0.0110  0.0273  -0.0066 770  VAL B CG2 
14492 N N   . ALA B 773  ? 0.2028 0.2723 0.2480 0.0094  0.0353  -0.0006 771  ALA B N   
14493 C CA  . ALA B 773  ? 0.2178 0.2918 0.2643 0.0074  0.0371  0.0023  771  ALA B CA  
14494 C C   . ALA B 773  ? 0.2634 0.3374 0.3045 0.0080  0.0391  0.0027  771  ALA B C   
14495 O O   . ALA B 773  ? 0.2676 0.3445 0.3088 0.0061  0.0404  0.0054  771  ALA B O   
14496 C CB  . ALA B 773  ? 0.2168 0.2984 0.2685 0.0077  0.0389  0.0032  771  ALA B CB  
14497 N N   . ALA B 774  ? 0.2291 0.3000 0.2655 0.0105  0.0392  0.0002  772  ALA B N   
14498 C CA  . ALA B 774  ? 0.2579 0.3290 0.2889 0.0114  0.0410  0.0002  772  ALA B CA  
14499 C C   . ALA B 774  ? 0.2521 0.3201 0.2803 0.0088  0.0400  0.0024  772  ALA B C   
14500 O O   . ALA B 774  ? 0.2615 0.3249 0.2899 0.0076  0.0374  0.0026  772  ALA B O   
14501 C CB  . ALA B 774  ? 0.2570 0.3243 0.2832 0.0142  0.0407  -0.0030 772  ALA B CB  
14502 N N   . ALA B 775  ? 0.2971 0.3676 0.3224 0.0084  0.0421  0.0041  773  ALA B N   
14503 C CA  . ALA B 775  ? 0.2973 0.3657 0.3203 0.0059  0.0414  0.0068  773  ALA B CA  
14504 C C   . ALA B 775  ? 0.2475 0.3094 0.2664 0.0061  0.0388  0.0057  773  ALA B C   
14505 O O   . ALA B 775  ? 0.2804 0.3389 0.2993 0.0042  0.0369  0.0074  773  ALA B O   
14506 C CB  . ALA B 775  ? 0.3015 0.3738 0.3212 0.0057  0.0443  0.0085  773  ALA B CB  
14507 N N   . GLU B 776  ? 0.2422 0.3021 0.2574 0.0085  0.0387  0.0029  774  GLU B N   
14508 C CA  . GLU B 776  ? 0.2172 0.2719 0.2283 0.0087  0.0364  0.0020  774  GLU B CA  
14509 C C   . GLU B 776  ? 0.2126 0.2637 0.2261 0.0089  0.0337  0.0003  774  GLU B C   
14510 O O   . GLU B 776  ? 0.2135 0.2609 0.2244 0.0090  0.0318  -0.0004 774  GLU B O   
14511 C CB  . GLU B 776  ? 0.2436 0.2976 0.2489 0.0106  0.0373  0.0000  774  GLU B CB  
14512 C CG  . GLU B 776  ? 0.3027 0.3602 0.3047 0.0106  0.0401  0.0014  774  GLU B CG  
14513 C CD  . GLU B 776  ? 0.3291 0.3917 0.3331 0.0121  0.0431  0.0008  774  GLU B CD  
14514 O OE1 . GLU B 776  ? 0.3243 0.3878 0.3324 0.0132  0.0430  -0.0008 774  GLU B OE1 
14515 O OE2 . GLU B 776  ? 0.3948 0.4609 0.3964 0.0123  0.0457  0.0020  774  GLU B OE2 
14516 N N   . THR B 777  ? 0.2064 0.2587 0.2248 0.0090  0.0336  -0.0003 775  THR B N   
14517 C CA  . THR B 777  ? 0.2125 0.2615 0.2329 0.0091  0.0312  -0.0018 775  THR B CA  
14518 C C   . THR B 777  ? 0.2029 0.2488 0.2237 0.0074  0.0291  0.0000  775  THR B C   
14519 O O   . THR B 777  ? 0.2139 0.2606 0.2367 0.0056  0.0293  0.0024  775  THR B O   
14520 C CB  . THR B 777  ? 0.1961 0.2474 0.2216 0.0094  0.0314  -0.0024 775  THR B CB  
14521 O OG1 . THR B 777  ? 0.2294 0.2827 0.2541 0.0117  0.0330  -0.0045 775  THR B OG1 
14522 C CG2 . THR B 777  ? 0.1804 0.2282 0.2080 0.0092  0.0289  -0.0035 775  THR B CG2 
14523 N N   . ALA B 778  ? 0.1804 0.2227 0.1989 0.0080  0.0272  -0.0012 776  ALA B N   
14524 C CA  . ALA B 778  ? 0.1835 0.2226 0.2015 0.0070  0.0253  0.0003  776  ALA B CA  
14525 C C   . ALA B 778  ? 0.1911 0.2277 0.2118 0.0072  0.0233  -0.0008 776  ALA B C   
14526 O O   . ALA B 778  ? 0.2000 0.2338 0.2206 0.0067  0.0217  0.0002  776  ALA B O   
14527 C CB  . ALA B 778  ? 0.1959 0.2335 0.2092 0.0077  0.0246  0.0002  776  ALA B CB  
14528 N N   . GLY B 779  ? 0.1735 0.2108 0.1963 0.0080  0.0233  -0.0028 777  GLY B N   
14529 C CA  . GLY B 779  ? 0.2045 0.2396 0.2297 0.0080  0.0216  -0.0038 777  GLY B CA  
14530 C C   . GLY B 779  ? 0.1927 0.2292 0.2199 0.0089  0.0220  -0.0058 777  GLY B C   
14531 O O   . GLY B 779  ? 0.1983 0.2365 0.2241 0.0099  0.0233  -0.0069 777  GLY B O   
14532 N N   . VAL B 780  ? 0.1748 0.2102 0.2049 0.0086  0.0208  -0.0063 778  VAL B N   
14533 C CA  . VAL B 780  ? 0.1658 0.2023 0.1980 0.0094  0.0209  -0.0079 778  VAL B CA  
14534 C C   . VAL B 780  ? 0.1686 0.2021 0.2010 0.0097  0.0190  -0.0093 778  VAL B C   
14535 O O   . VAL B 780  ? 0.1673 0.1989 0.2006 0.0089  0.0177  -0.0086 778  VAL B O   
14536 C CB  . VAL B 780  ? 0.1690 0.2083 0.2052 0.0086  0.0217  -0.0069 778  VAL B CB  
14537 C CG1 . VAL B 780  ? 0.1794 0.2198 0.2177 0.0098  0.0216  -0.0087 778  VAL B CG1 
14538 C CG2 . VAL B 780  ? 0.1934 0.2363 0.2295 0.0082  0.0238  -0.0054 778  VAL B CG2 
14539 N N   . MET B 781  ? 0.1596 0.1928 0.1910 0.0108  0.0189  -0.0112 779  MET B N   
14540 C CA  . MET B 781  ? 0.1500 0.1809 0.1817 0.0110  0.0173  -0.0124 779  MET B CA  
14541 C C   . MET B 781  ? 0.1437 0.1755 0.1777 0.0116  0.0174  -0.0134 779  MET B C   
14542 O O   . MET B 781  ? 0.1683 0.2010 0.2013 0.0126  0.0183  -0.0144 779  MET B O   
14543 C CB  . MET B 781  ? 0.1549 0.1844 0.1833 0.0116  0.0167  -0.0136 779  MET B CB  
14544 C CG  . MET B 781  ? 0.1818 0.2111 0.2079 0.0113  0.0167  -0.0126 779  MET B CG  
14545 S SD  . MET B 781  ? 0.1722 0.2008 0.1948 0.0116  0.0160  -0.0137 779  MET B SD  
14546 C CE  . MET B 781  ? 0.1540 0.1812 0.1777 0.0115  0.0143  -0.0144 779  MET B CE  
14547 N N   . PHE B 782  ? 0.1520 0.1834 0.1888 0.0109  0.0164  -0.0131 780  PHE B N   
14548 C CA  . PHE B 782  ? 0.1541 0.1867 0.1935 0.0113  0.0162  -0.0137 780  PHE B CA  
14549 C C   . PHE B 782  ? 0.1613 0.1913 0.2007 0.0113  0.0144  -0.0147 780  PHE B C   
14550 O O   . PHE B 782  ? 0.1809 0.2089 0.2201 0.0105  0.0133  -0.0144 780  PHE B O   
14551 C CB  . PHE B 782  ? 0.1329 0.1680 0.1760 0.0103  0.0165  -0.0121 780  PHE B CB  
14552 C CG  . PHE B 782  ? 0.1480 0.1847 0.1943 0.0106  0.0159  -0.0126 780  PHE B CG  
14553 C CD1 . PHE B 782  ? 0.1593 0.1988 0.2066 0.0121  0.0172  -0.0131 780  PHE B CD1 
14554 C CD2 . PHE B 782  ? 0.1653 0.2004 0.2133 0.0096  0.0141  -0.0125 780  PHE B CD2 
14555 C CE1 . PHE B 782  ? 0.1990 0.2402 0.2493 0.0127  0.0166  -0.0134 780  PHE B CE1 
14556 C CE2 . PHE B 782  ? 0.1447 0.1814 0.1955 0.0100  0.0134  -0.0129 780  PHE B CE2 
14557 C CZ  . PHE B 782  ? 0.1859 0.2258 0.2381 0.0115  0.0146  -0.0132 780  PHE B CZ  
14558 N N   . THR B 783  ? 0.1438 0.1735 0.1832 0.0123  0.0142  -0.0160 781  THR B N   
14559 C CA  . THR B 783  ? 0.1718 0.1994 0.2115 0.0123  0.0126  -0.0168 781  THR B CA  
14560 C C   . THR B 783  ? 0.1786 0.2079 0.2208 0.0131  0.0125  -0.0171 781  THR B C   
14561 O O   . THR B 783  ? 0.1738 0.2041 0.2155 0.0144  0.0135  -0.0176 781  THR B O   
14562 C CB  . THR B 783  ? 0.1627 0.1878 0.1991 0.0126  0.0120  -0.0180 781  THR B CB  
14563 O OG1 . THR B 783  ? 0.1553 0.1798 0.1897 0.0121  0.0121  -0.0176 781  THR B OG1 
14564 C CG2 . THR B 783  ? 0.1675 0.1907 0.2040 0.0124  0.0104  -0.0186 781  THR B CG2 
14565 N N   . GLY B 784  ? 0.1710 0.2005 0.2158 0.0123  0.0112  -0.0167 782  GLY B N   
14566 C CA  . GLY B 784  ? 0.1661 0.1979 0.2139 0.0130  0.0110  -0.0166 782  GLY B CA  
14567 C C   . GLY B 784  ? 0.1817 0.2140 0.2324 0.0115  0.0095  -0.0158 782  GLY B C   
14568 O O   . GLY B 784  ? 0.1771 0.2066 0.2265 0.0104  0.0084  -0.0157 782  GLY B O   
14569 N N   . SER B 785  ? 0.1920 0.2279 0.2466 0.0117  0.0095  -0.0151 783  SER B N   
14570 C CA  . SER B 785  ? 0.2051 0.2416 0.2625 0.0100  0.0077  -0.0143 783  SER B CA  
14571 C C   . SER B 785  ? 0.2244 0.2612 0.2827 0.0079  0.0079  -0.0128 783  SER B C   
14572 O O   . SER B 785  ? 0.2048 0.2435 0.2631 0.0077  0.0097  -0.0119 783  SER B O   
14573 C CB  . SER B 785  ? 0.2015 0.2424 0.2632 0.0107  0.0075  -0.0138 783  SER B CB  
14574 O OG  . SER B 785  ? 0.1883 0.2342 0.2526 0.0111  0.0096  -0.0127 783  SER B OG  
14575 N N   . THR B 786  ? 0.2284 0.2628 0.2868 0.0061  0.0059  -0.0125 784  THR B N   
14576 C CA  . THR B 786  ? 0.2070 0.2409 0.2660 0.0039  0.0057  -0.0111 784  THR B CA  
14577 C C   . THR B 786  ? 0.2023 0.2418 0.2657 0.0028  0.0067  -0.0092 784  THR B C   
14578 O O   . THR B 786  ? 0.2269 0.2671 0.2903 0.0015  0.0077  -0.0079 784  THR B O   
14579 C CB  . THR B 786  ? 0.2242 0.2543 0.2825 0.0023  0.0031  -0.0113 784  THR B CB  
14580 O OG1 . THR B 786  ? 0.2640 0.2897 0.3184 0.0036  0.0024  -0.0130 784  THR B OG1 
14581 C CG2 . THR B 786  ? 0.2830 0.3109 0.3408 0.0001  0.0026  -0.0100 784  THR B CG2 
14582 N N   . GLU B 787  ? 0.2335 0.2773 0.3006 0.0033  0.0064  -0.0091 785  GLU B N   
14583 C CA  . GLU B 787  ? 0.2058 0.2560 0.2776 0.0023  0.0075  -0.0073 785  GLU B CA  
14584 C C   . GLU B 787  ? 0.2318 0.2848 0.3031 0.0035  0.0104  -0.0068 785  GLU B C   
14585 O O   . GLU B 787  ? 0.2086 0.2648 0.2817 0.0018  0.0115  -0.0049 785  GLU B O   
14586 C CB  . GLU B 787  ? 0.2747 0.3294 0.3506 0.0035  0.0068  -0.0074 785  GLU B CB  
14587 C CG  . GLU B 787  ? 0.3984 0.4609 0.4798 0.0026  0.0079  -0.0054 785  GLU B CG  
14588 C CD  . GLU B 787  ? 0.4736 0.5409 0.5592 0.0042  0.0072  -0.0055 785  GLU B CD  
14589 O OE1 . GLU B 787  ? 0.5396 0.6035 0.6233 0.0059  0.0057  -0.0072 785  GLU B OE1 
14590 O OE2 . GLU B 787  ? 0.4885 0.5630 0.5793 0.0036  0.0079  -0.0039 785  GLU B OE2 
14591 N N   . VAL B 788  ? 0.2001 0.2520 0.2686 0.0063  0.0117  -0.0084 786  VAL B N   
14592 C CA  . VAL B 788  ? 0.2162 0.2704 0.2835 0.0075  0.0144  -0.0082 786  VAL B CA  
14593 C C   . VAL B 788  ? 0.1791 0.2300 0.2431 0.0060  0.0148  -0.0075 786  VAL B C   
14594 O O   . VAL B 788  ? 0.1931 0.2467 0.2574 0.0054  0.0166  -0.0061 786  VAL B O   
14595 C CB  . VAL B 788  ? 0.1769 0.2298 0.2415 0.0107  0.0152  -0.0103 786  VAL B CB  
14596 C CG1 . VAL B 788  ? 0.1843 0.2378 0.2461 0.0118  0.0177  -0.0104 786  VAL B CG1 
14597 C CG2 . VAL B 788  ? 0.1951 0.2520 0.2632 0.0126  0.0152  -0.0106 786  VAL B CG2 
14598 N N   . ALA B 789  ? 0.1856 0.2308 0.2465 0.0056  0.0132  -0.0084 787  ALA B N   
14599 C CA  . ALA B 789  ? 0.1618 0.2037 0.2196 0.0045  0.0133  -0.0078 787  ALA B CA  
14600 C C   . ALA B 789  ? 0.1862 0.2296 0.2461 0.0019  0.0133  -0.0054 787  ALA B C   
14601 O O   . ALA B 789  ? 0.1878 0.2310 0.2462 0.0012  0.0144  -0.0042 787  ALA B O   
14602 C CB  . ALA B 789  ? 0.1564 0.1925 0.2112 0.0045  0.0115  -0.0090 787  ALA B CB  
14603 N N   . ARG B 790  ? 0.1862 0.2309 0.2496 0.0001  0.0118  -0.0046 788  ARG B N   
14604 C CA  . ARG B 790  ? 0.1854 0.2313 0.2509 -0.0029 0.0114  -0.0023 788  ARG B CA  
14605 C C   . ARG B 790  ? 0.2283 0.2805 0.2962 -0.0032 0.0139  -0.0005 788  ARG B C   
14606 O O   . ARG B 790  ? 0.2406 0.2929 0.3081 -0.0052 0.0145  0.0015  788  ARG B O   
14607 C CB  . ARG B 790  ? 0.2470 0.2934 0.3158 -0.0048 0.0090  -0.0019 788  ARG B CB  
14608 C CG  . ARG B 790  ? 0.3771 0.4208 0.4461 -0.0083 0.0074  -0.0001 788  ARG B CG  
14609 C CD  . ARG B 790  ? 0.3432 0.3867 0.4148 -0.0102 0.0047  0.0000  788  ARG B CD  
14610 N NE  . ARG B 790  ? 0.3293 0.3675 0.3980 -0.0088 0.0028  -0.0023 788  ARG B NE  
14611 C CZ  . ARG B 790  ? 0.3803 0.4112 0.4447 -0.0092 0.0012  -0.0031 788  ARG B CZ  
14612 N NH1 . ARG B 790  ? 0.3429 0.3704 0.4052 -0.0108 0.0012  -0.0018 788  ARG B NH1 
14613 N NH2 . ARG B 790  ? 0.4107 0.4376 0.4726 -0.0078 -0.0003 -0.0052 788  ARG B NH2 
14614 N N   . LEU B 791  ? 0.2070 0.2643 0.2770 -0.0010 0.0155  -0.0013 789  LEU B N   
14615 C CA  . LEU B 791  ? 0.2043 0.2679 0.2762 -0.0007 0.0183  0.0002  789  LEU B CA  
14616 C C   . LEU B 791  ? 0.2209 0.2824 0.2883 0.0001  0.0201  0.0001  789  LEU B C   
14617 O O   . LEU B 791  ? 0.2173 0.2816 0.2849 -0.0012 0.0217  0.0021  789  LEU B O   
14618 C CB  . LEU B 791  ? 0.2143 0.2831 0.2888 0.0021  0.0195  -0.0010 789  LEU B CB  
14619 C CG  . LEU B 791  ? 0.2368 0.3089 0.3163 0.0016  0.0178  -0.0008 789  LEU B CG  
14620 C CD1 . LEU B 791  ? 0.2300 0.3065 0.3112 0.0051  0.0193  -0.0021 789  LEU B CD1 
14621 C CD2 . LEU B 791  ? 0.2294 0.3066 0.3136 -0.0019 0.0177  0.0021  789  LEU B CD2 
14622 N N   . ILE B 792  ? 0.2041 0.2609 0.2673 0.0022  0.0197  -0.0020 790  ILE B N   
14623 C CA  . ILE B 792  ? 0.1874 0.2421 0.2462 0.0030  0.0211  -0.0022 790  ILE B CA  
14624 C C   . ILE B 792  ? 0.1834 0.2347 0.2405 0.0006  0.0202  -0.0003 790  ILE B C   
14625 O O   . ILE B 792  ? 0.2265 0.2787 0.2819 0.0000  0.0217  0.0011  790  ILE B O   
14626 C CB  . ILE B 792  ? 0.1831 0.2336 0.2382 0.0054  0.0205  -0.0047 790  ILE B CB  
14627 C CG1 . ILE B 792  ? 0.1697 0.2231 0.2256 0.0080  0.0216  -0.0063 790  ILE B CG1 
14628 C CG2 . ILE B 792  ? 0.1989 0.2461 0.2493 0.0056  0.0210  -0.0047 790  ILE B CG2 
14629 C CD1 . ILE B 792  ? 0.1994 0.2485 0.2521 0.0098  0.0206  -0.0088 790  ILE B CD1 
14630 N N   . GLN B 793  ? 0.1871 0.2341 0.2443 -0.0008 0.0178  -0.0004 791  GLN B N   
14631 C CA  . GLN B 793  ? 0.1972 0.2400 0.2526 -0.0030 0.0166  0.0012  791  GLN B CA  
14632 C C   . GLN B 793  ? 0.2058 0.2522 0.2636 -0.0057 0.0175  0.0041  791  GLN B C   
14633 O O   . GLN B 793  ? 0.2191 0.2638 0.2745 -0.0068 0.0180  0.0058  791  GLN B O   
14634 C CB  . GLN B 793  ? 0.2344 0.2723 0.2898 -0.0038 0.0138  0.0004  791  GLN B CB  
14635 C CG  . GLN B 793  ? 0.2342 0.2668 0.2875 -0.0059 0.0122  0.0018  791  GLN B CG  
14636 C CD  . GLN B 793  ? 0.2830 0.3121 0.3373 -0.0073 0.0096  0.0014  791  GLN B CD  
14637 O OE1 . GLN B 793  ? 0.3070 0.3394 0.3650 -0.0086 0.0090  0.0016  791  GLN B OE1 
14638 N NE2 . GLN B 793  ? 0.2915 0.3140 0.3423 -0.0070 0.0079  0.0007  791  GLN B NE2 
14639 N N   . ALA B 794  ? 0.2166 0.2683 0.2792 -0.0069 0.0177  0.0049  792  ALA B N   
14640 C CA  . ALA B 794  ? 0.2511 0.3073 0.3164 -0.0097 0.0187  0.0079  792  ALA B CA  
14641 C C   . ALA B 794  ? 0.2695 0.3296 0.3334 -0.0088 0.0218  0.0088  792  ALA B C   
14642 O O   . ALA B 794  ? 0.2720 0.3323 0.3349 -0.0110 0.0225  0.0113  792  ALA B O   
14643 C CB  . ALA B 794  ? 0.2519 0.3142 0.3230 -0.0108 0.0185  0.0085  792  ALA B CB  
14644 N N   . GLN B 795  ? 0.2203 0.2832 0.2835 -0.0055 0.0236  0.0069  793  GLN B N   
14645 C CA  . GLN B 795  ? 0.2239 0.2905 0.2853 -0.0044 0.0265  0.0076  793  GLN B CA  
14646 C C   . GLN B 795  ? 0.2215 0.2828 0.2776 -0.0047 0.0264  0.0081  793  GLN B C   
14647 O O   . GLN B 795  ? 0.2405 0.3037 0.2953 -0.0059 0.0280  0.0102  793  GLN B O   
14648 C CB  . GLN B 795  ? 0.2716 0.3409 0.3327 -0.0006 0.0282  0.0050  793  GLN B CB  
14649 N N   . LEU B 796  ? 0.1979 0.2527 0.2509 -0.0036 0.0244  0.0063  794  LEU B N   
14650 C CA  . LEU B 796  ? 0.1981 0.2482 0.2462 -0.0034 0.0241  0.0066  794  LEU B CA  
14651 C C   . LEU B 796  ? 0.2530 0.3003 0.3007 -0.0065 0.0230  0.0094  794  LEU B C   
14652 O O   . LEU B 796  ? 0.2866 0.3323 0.3308 -0.0068 0.0236  0.0108  794  LEU B O   
14653 C CB  . LEU B 796  ? 0.1886 0.2334 0.2342 -0.0015 0.0223  0.0041  794  LEU B CB  
14654 C CG  . LEU B 796  ? 0.2239 0.2699 0.2683 0.0015  0.0232  0.0015  794  LEU B CG  
14655 C CD1 . LEU B 796  ? 0.2146 0.2555 0.2567 0.0027  0.0212  -0.0005 794  LEU B CD1 
14656 C CD2 . LEU B 796  ? 0.2159 0.2641 0.2572 0.0025  0.0254  0.0018  794  LEU B CD2 
14657 N N   . ALA B 797  ? 0.2394 0.2857 0.2901 -0.0087 0.0213  0.0103  795  ALA B N   
14658 C CA  . ALA B 797  ? 0.2814 0.3240 0.3313 -0.0119 0.0198  0.0128  795  ALA B CA  
14659 C C   . ALA B 797  ? 0.3220 0.3690 0.3726 -0.0142 0.0218  0.0160  795  ALA B C   
14660 O O   . ALA B 797  ? 0.3164 0.3598 0.3650 -0.0166 0.0210  0.0184  795  ALA B O   
14661 C CB  . ALA B 797  ? 0.3175 0.3580 0.3704 -0.0139 0.0174  0.0129  795  ALA B CB  
14662 N N   . ASP B 798  ? 0.3115 0.3662 0.3648 -0.0135 0.0244  0.0161  796  ASP B N   
14663 C CA  . ASP B 798  ? 0.3439 0.4034 0.3974 -0.0155 0.0267  0.0191  796  ASP B CA  
14664 C C   . ASP B 798  ? 0.3390 0.3965 0.3871 -0.0143 0.0280  0.0195  796  ASP B C   
14665 O O   . ASP B 798  ? 0.3606 0.4206 0.4078 -0.0162 0.0295  0.0224  796  ASP B O   
14666 C CB  . ASP B 798  ? 0.3368 0.4056 0.3946 -0.0145 0.0294  0.0189  796  ASP B CB  
14667 C CG  . ASP B 798  ? 0.4755 0.5505 0.5357 -0.0176 0.0313  0.0225  796  ASP B CG  
14668 O OD1 . ASP B 798  ? 0.5153 0.5898 0.5781 -0.0215 0.0297  0.0248  796  ASP B OD1 
14669 O OD2 . ASP B 798  ? 0.5114 0.5919 0.5708 -0.0164 0.0344  0.0230  796  ASP B OD2 
14670 N N   . ARG B 799  ? 0.3075 0.3607 0.3520 -0.0113 0.0273  0.0170  797  ARG B N   
14671 C CA  . ARG B 799  ? 0.3503 0.4027 0.3898 -0.0098 0.0286  0.0171  797  ARG B CA  
14672 C C   . ARG B 799  ? 0.3026 0.3472 0.3380 -0.0093 0.0262  0.0169  797  ARG B C   
14673 O O   . ARG B 799  ? 0.2967 0.3366 0.3329 -0.0095 0.0237  0.0160  797  ARG B O   
14674 C CB  . ARG B 799  ? 0.3507 0.4063 0.3894 -0.0063 0.0303  0.0142  797  ARG B CB  
14675 C CG  . ARG B 799  ? 0.4121 0.4748 0.4553 -0.0058 0.0323  0.0137  797  ARG B CG  
14676 C CD  . ARG B 799  ? 0.4178 0.4843 0.4586 -0.0030 0.0350  0.0122  797  ARG B CD  
14677 N NE  . ARG B 799  ? 0.4462 0.5076 0.4819 -0.0011 0.0341  0.0104  797  ARG B NE  
14678 C CZ  . ARG B 799  ? 0.4012 0.4598 0.4363 0.0012  0.0328  0.0074  797  ARG B CZ  
14679 N NH1 . ARG B 799  ? 0.3837 0.4442 0.4226 0.0022  0.0326  0.0057  797  ARG B NH1 
14680 N NH2 . ARG B 799  ? 0.3229 0.3770 0.3536 0.0023  0.0317  0.0062  797  ARG B NH2 
14681 N N   . LEU B 800  ? 0.2972 0.3408 0.3281 -0.0086 0.0269  0.0177  798  LEU B N   
14682 C CA  . LEU B 800  ? 0.3251 0.3623 0.3519 -0.0077 0.0249  0.0176  798  LEU B CA  
14683 C C   . LEU B 800  ? 0.3452 0.3835 0.3681 -0.0052 0.0261  0.0162  798  LEU B C   
14684 O O   . LEU B 800  ? 0.3688 0.4120 0.3912 -0.0048 0.0285  0.0163  798  LEU B O   
14685 C CB  . LEU B 800  ? 0.3432 0.3769 0.3679 -0.0103 0.0241  0.0211  798  LEU B CB  
14686 C CG  . LEU B 800  ? 0.3443 0.3746 0.3714 -0.0131 0.0222  0.0227  798  LEU B CG  
14687 C CD1 . LEU B 800  ? 0.3642 0.3910 0.3884 -0.0157 0.0216  0.0264  798  LEU B CD1 
14688 C CD2 . LEU B 800  ? 0.2992 0.3237 0.3263 -0.0115 0.0195  0.0205  798  LEU B CD2 
14689 N N   . SER B 801  ? 0.3191 0.3529 0.3393 -0.0034 0.0242  0.0150  799  SER B N   
14690 C CA  . SER B 801  ? 0.3945 0.4288 0.4107 -0.0015 0.0247  0.0140  799  SER B CA  
14691 C C   . SER B 801  ? 0.4298 0.4643 0.4425 -0.0027 0.0256  0.0170  799  SER B C   
14692 O O   . SER B 801  ? 0.4108 0.4437 0.4237 -0.0050 0.0253  0.0198  799  SER B O   
14693 C CB  . SER B 801  ? 0.3864 0.4164 0.4010 0.0004  0.0224  0.0125  799  SER B CB  
14694 O OG  . SER B 801  ? 0.4016 0.4271 0.4146 -0.0004 0.0206  0.0147  799  SER B OG  
14695 N N   . PRO B 802  ? 0.4805 0.5166 0.4893 -0.0014 0.0267  0.0165  800  PRO B N   
14696 C CA  . PRO B 802  ? 0.4607 0.4964 0.4652 -0.0024 0.0272  0.0193  800  PRO B CA  
14697 C C   . PRO B 802  ? 0.4514 0.4815 0.4543 -0.0031 0.0247  0.0214  800  PRO B C   
14698 O O   . PRO B 802  ? 0.4837 0.5127 0.4841 -0.0048 0.0250  0.0246  800  PRO B O   
14699 C CB  . PRO B 802  ? 0.4698 0.5070 0.4703 -0.0003 0.0278  0.0175  800  PRO B CB  
14700 C CG  . PRO B 802  ? 0.5052 0.5456 0.5083 0.0010  0.0291  0.0144  800  PRO B CG  
14701 C CD  . PRO B 802  ? 0.4529 0.4915 0.4608 0.0008  0.0276  0.0134  800  PRO B CD  
14702 N N   . ALA B 803  ? 0.4341 0.4604 0.4381 -0.0017 0.0223  0.0199  801  ALA B N   
14703 C CA  . ALA B 803  ? 0.4098 0.4304 0.4125 -0.0018 0.0199  0.0216  801  ALA B CA  
14704 C C   . ALA B 803  ? 0.4369 0.4545 0.4425 -0.0038 0.0190  0.0229  801  ALA B C   
14705 O O   . ALA B 803  ? 0.4923 0.5042 0.4969 -0.0037 0.0168  0.0239  801  ALA B O   
14706 C CB  . ALA B 803  ? 0.4157 0.4340 0.4180 0.0010  0.0178  0.0193  801  ALA B CB  
14707 N N   . GLY B 804  ? 0.3938 0.4150 0.4029 -0.0056 0.0207  0.0228  802  GLY B N   
14708 C CA  . GLY B 804  ? 0.4319 0.4507 0.4438 -0.0081 0.0198  0.0242  802  GLY B CA  
14709 C C   . GLY B 804  ? 0.3770 0.3922 0.3912 -0.0071 0.0177  0.0221  802  GLY B C   
14710 O O   . GLY B 804  ? 0.3426 0.3527 0.3570 -0.0085 0.0159  0.0233  802  GLY B O   
14711 N N   . ARG B 805  ? 0.3608 0.3780 0.3765 -0.0047 0.0178  0.0188  803  ARG B N   
14712 C CA  . ARG B 805  ? 0.3119 0.3261 0.3296 -0.0035 0.0160  0.0166  803  ARG B CA  
14713 C C   . ARG B 805  ? 0.2859 0.3044 0.3075 -0.0035 0.0171  0.0144  803  ARG B C   
14714 O O   . ARG B 805  ? 0.3059 0.3299 0.3283 -0.0033 0.0193  0.0139  803  ARG B O   
14715 C CB  . ARG B 805  ? 0.3455 0.3573 0.3609 -0.0004 0.0147  0.0149  803  ARG B CB  
14716 C CG  . ARG B 805  ? 0.4157 0.4227 0.4273 0.0001  0.0132  0.0170  803  ARG B CG  
14717 C CD  . ARG B 805  ? 0.3994 0.4000 0.4109 -0.0010 0.0112  0.0182  803  ARG B CD  
14718 N NE  . ARG B 805  ? 0.4534 0.4489 0.4611 0.0000  0.0096  0.0200  803  ARG B NE  
14719 C CZ  . ARG B 805  ? 0.4148 0.4079 0.4199 -0.0020 0.0095  0.0233  803  ARG B CZ  
14720 N NH1 . ARG B 805  ? 0.4373 0.4333 0.4437 -0.0052 0.0110  0.0251  803  ARG B NH1 
14721 N NH2 . ARG B 805  ? 0.4886 0.4766 0.4901 -0.0006 0.0078  0.0248  803  ARG B NH2 
14722 N N   . PRO B 806  ? 0.2668 0.2830 0.2908 -0.0036 0.0157  0.0131  804  PRO B N   
14723 C CA  . PRO B 806  ? 0.2516 0.2718 0.2794 -0.0035 0.0165  0.0111  804  PRO B CA  
14724 C C   . PRO B 806  ? 0.2752 0.2985 0.3025 -0.0009 0.0175  0.0085  804  PRO B C   
14725 O O   . PRO B 806  ? 0.2419 0.2631 0.2667 0.0011  0.0167  0.0074  804  PRO B O   
14726 C CB  . PRO B 806  ? 0.2821 0.2978 0.3112 -0.0036 0.0142  0.0100  804  PRO B CB  
14727 C CG  . PRO B 806  ? 0.2841 0.2939 0.3108 -0.0049 0.0126  0.0122  804  PRO B CG  
14728 C CD  . PRO B 806  ? 0.2659 0.2755 0.2890 -0.0036 0.0132  0.0133  804  PRO B CD  
14729 N N   . ILE B 807  ? 0.2414 0.2697 0.2711 -0.0009 0.0192  0.0076  805  ILE B N   
14730 C CA  . ILE B 807  ? 0.2250 0.2558 0.2542 0.0013  0.0201  0.0051  805  ILE B CA  
14731 C C   . ILE B 807  ? 0.2309 0.2594 0.2615 0.0025  0.0184  0.0028  805  ILE B C   
14732 O O   . ILE B 807  ? 0.2189 0.2473 0.2525 0.0016  0.0178  0.0025  805  ILE B O   
14733 C CB  . ILE B 807  ? 0.2253 0.2616 0.2567 0.0012  0.0223  0.0047  805  ILE B CB  
14734 C CG1 . ILE B 807  ? 0.2695 0.3087 0.2998 0.0000  0.0242  0.0071  805  ILE B CG1 
14735 C CG2 . ILE B 807  ? 0.2094 0.2470 0.2396 0.0036  0.0229  0.0020  805  ILE B CG2 
14736 C CD1 . ILE B 807  ? 0.3137 0.3521 0.3392 0.0010  0.0247  0.0074  805  ILE B CD1 
14737 N N   . PRO B 808  ? 0.2014 0.2281 0.2297 0.0044  0.0176  0.0012  806  PRO B N   
14738 C CA  . PRO B 808  ? 0.2164 0.2411 0.2457 0.0054  0.0161  -0.0007 806  PRO B CA  
14739 C C   . PRO B 808  ? 0.2147 0.2420 0.2465 0.0057  0.0167  -0.0025 806  PRO B C   
14740 O O   . PRO B 808  ? 0.1917 0.2221 0.2233 0.0062  0.0182  -0.0032 806  PRO B O   
14741 C CB  . PRO B 808  ? 0.2021 0.2258 0.2286 0.0071  0.0155  -0.0017 806  PRO B CB  
14742 C CG  . PRO B 808  ? 0.2560 0.2796 0.2799 0.0069  0.0160  0.0003  806  PRO B CG  
14743 C CD  . PRO B 808  ? 0.2106 0.2371 0.2353 0.0054  0.0178  0.0015  806  PRO B CD  
14744 N N   . LEU B 809  ? 0.1764 0.2020 0.2102 0.0054  0.0155  -0.0033 807  LEU B N   
14745 C CA  . LEU B 809  ? 0.1755 0.2030 0.2116 0.0058  0.0157  -0.0050 807  LEU B CA  
14746 C C   . LEU B 809  ? 0.1716 0.1963 0.2071 0.0068  0.0141  -0.0067 807  LEU B C   
14747 O O   . LEU B 809  ? 0.1924 0.2139 0.2279 0.0064  0.0127  -0.0064 807  LEU B O   
14748 C CB  . LEU B 809  ? 0.1848 0.2140 0.2245 0.0042  0.0157  -0.0040 807  LEU B CB  
14749 C CG  . LEU B 809  ? 0.1862 0.2168 0.2284 0.0046  0.0153  -0.0055 807  LEU B CG  
14750 C CD1 . LEU B 809  ? 0.1844 0.2185 0.2267 0.0061  0.0170  -0.0067 807  LEU B CD1 
14751 C CD2 . LEU B 809  ? 0.1849 0.2170 0.2308 0.0025  0.0149  -0.0041 807  LEU B CD2 
14752 N N   . ILE B 810  ? 0.1686 0.1943 0.2034 0.0081  0.0143  -0.0084 808  ILE B N   
14753 C CA  . ILE B 810  ? 0.1833 0.2071 0.2181 0.0088  0.0131  -0.0100 808  ILE B CA  
14754 C C   . ILE B 810  ? 0.1877 0.2130 0.2250 0.0085  0.0131  -0.0108 808  ILE B C   
14755 O O   . ILE B 810  ? 0.1774 0.2052 0.2151 0.0090  0.0143  -0.0112 808  ILE B O   
14756 C CB  . ILE B 810  ? 0.1469 0.1708 0.1793 0.0100  0.0130  -0.0112 808  ILE B CB  
14757 C CG1 . ILE B 810  ? 0.1842 0.2076 0.2143 0.0103  0.0131  -0.0103 808  ILE B CG1 
14758 C CG2 . ILE B 810  ? 0.2075 0.2297 0.2399 0.0105  0.0118  -0.0126 808  ILE B CG2 
14759 C CD1 . ILE B 810  ? 0.1889 0.2128 0.2171 0.0113  0.0128  -0.0113 808  ILE B CD1 
14760 N N   . ALA B 811  ? 0.1747 0.1984 0.2135 0.0079  0.0118  -0.0109 809  ALA B N   
14761 C CA  . ALA B 811  ? 0.1713 0.1967 0.2129 0.0076  0.0116  -0.0114 809  ALA B CA  
14762 C C   . ALA B 811  ? 0.1822 0.2050 0.2232 0.0080  0.0101  -0.0128 809  ALA B C   
14763 O O   . ALA B 811  ? 0.1890 0.2092 0.2299 0.0073  0.0087  -0.0126 809  ALA B O   
14764 C CB  . ALA B 811  ? 0.1708 0.1974 0.2153 0.0059  0.0115  -0.0098 809  ALA B CB  
14765 N N   . GLU B 812  ? 0.1607 0.1840 0.2008 0.0091  0.0102  -0.0141 810  GLU B N   
14766 C CA  . GLU B 812  ? 0.1884 0.2096 0.2275 0.0095  0.0090  -0.0154 810  GLU B CA  
14767 C C   . GLU B 812  ? 0.1990 0.2213 0.2403 0.0094  0.0085  -0.0158 810  GLU B C   
14768 O O   . GLU B 812  ? 0.1842 0.2084 0.2260 0.0101  0.0093  -0.0161 810  GLU B O   
14769 C CB  . GLU B 812  ? 0.1693 0.1901 0.2057 0.0104  0.0094  -0.0163 810  GLU B CB  
14770 C CG  . GLU B 812  ? 0.1857 0.2061 0.2203 0.0106  0.0098  -0.0157 810  GLU B CG  
14771 C CD  . GLU B 812  ? 0.2098 0.2277 0.2440 0.0105  0.0087  -0.0155 810  GLU B CD  
14772 O OE1 . GLU B 812  ? 0.1988 0.2154 0.2317 0.0111  0.0080  -0.0164 810  GLU B OE1 
14773 O OE2 . GLU B 812  ? 0.1907 0.2077 0.2256 0.0100  0.0086  -0.0144 810  GLU B OE2 
14774 N N   . THR B 813  ? 0.1778 0.1987 0.2201 0.0087  0.0070  -0.0158 811  THR B N   
14775 C CA  . THR B 813  ? 0.1502 0.1729 0.1954 0.0083  0.0064  -0.0157 811  THR B CA  
14776 C C   . THR B 813  ? 0.1784 0.1991 0.2229 0.0085  0.0047  -0.0167 811  THR B C   
14777 O O   . THR B 813  ? 0.1746 0.1933 0.2164 0.0093  0.0046  -0.0177 811  THR B O   
14778 C CB  . THR B 813  ? 0.1766 0.2005 0.2246 0.0067  0.0061  -0.0142 811  THR B CB  
14779 O OG1 . THR B 813  ? 0.1812 0.2016 0.2275 0.0058  0.0051  -0.0140 811  THR B OG1 
14780 C CG2 . THR B 813  ? 0.2049 0.2319 0.2539 0.0067  0.0081  -0.0131 811  THR B CG2 
14781 N N   . GLY B 814  ? 0.1684 0.1898 0.2154 0.0077  0.0034  -0.0164 812  GLY B N   
14782 C CA  . GLY B 814  ? 0.1937 0.2138 0.2401 0.0081  0.0020  -0.0173 812  GLY B CA  
14783 C C   . GLY B 814  ? 0.2166 0.2327 0.2601 0.0077  0.0005  -0.0180 812  GLY B C   
14784 O O   . GLY B 814  ? 0.2136 0.2277 0.2554 0.0073  0.0007  -0.0179 812  GLY B O   
14785 N N   . GLY B 815  ? 0.1808 0.1957 0.2234 0.0079  -0.0008 -0.0187 813  GLY B N   
14786 C CA  . GLY B 815  ? 0.1806 0.1919 0.2201 0.0076  -0.0022 -0.0195 813  GLY B CA  
14787 C C   . GLY B 815  ? 0.1742 0.1849 0.2144 0.0070  -0.0043 -0.0197 813  GLY B C   
14788 O O   . GLY B 815  ? 0.2021 0.2153 0.2449 0.0073  -0.0046 -0.0193 813  GLY B O   
14789 N N   . GLN B 816  ? 0.1623 0.1696 0.1999 0.0064  -0.0057 -0.0203 814  GLN B N   
14790 C CA  . GLN B 816  ? 0.1747 0.1807 0.2118 0.0059  -0.0080 -0.0206 814  GLN B CA  
14791 C C   . GLN B 816  ? 0.1685 0.1709 0.2006 0.0066  -0.0082 -0.0218 814  GLN B C   
14792 O O   . GLN B 816  ? 0.2039 0.2031 0.2335 0.0061  -0.0093 -0.0224 814  GLN B O   
14793 C CB  . GLN B 816  ? 0.1824 0.1879 0.2213 0.0041  -0.0098 -0.0201 814  GLN B CB  
14794 C CG  . GLN B 816  ? 0.1927 0.1979 0.2320 0.0034  -0.0123 -0.0202 814  GLN B CG  
14795 C CD  . GLN B 816  ? 0.2066 0.2162 0.2496 0.0042  -0.0122 -0.0195 814  GLN B CD  
14796 O OE1 . GLN B 816  ? 0.1836 0.1933 0.2252 0.0057  -0.0114 -0.0199 814  GLN B OE1 
14797 N NE2 . GLN B 816  ? 0.1948 0.2081 0.2426 0.0031  -0.0129 -0.0183 814  GLN B NE2 
14798 N N   . ASN B 817  ? 0.1573 0.1603 0.1878 0.0077  -0.0071 -0.0222 815  ASN B N   
14799 C CA  . ASN B 817  ? 0.1719 0.1728 0.1981 0.0084  -0.0063 -0.0230 815  ASN B CA  
14800 C C   . ASN B 817  ? 0.1988 0.1973 0.2218 0.0083  -0.0079 -0.0237 815  ASN B C   
14801 O O   . ASN B 817  ? 0.2032 0.2021 0.2266 0.0081  -0.0089 -0.0234 815  ASN B O   
14802 C CB  . ASN B 817  ? 0.1648 0.1677 0.1908 0.0092  -0.0045 -0.0228 815  ASN B CB  
14803 C CG  . ASN B 817  ? 0.1712 0.1765 0.2002 0.0093  -0.0030 -0.0222 815  ASN B CG  
14804 O OD1 . ASN B 817  ? 0.1645 0.1698 0.1941 0.0092  -0.0025 -0.0220 815  ASN B OD1 
14805 N ND2 . ASN B 817  ? 0.1631 0.1703 0.1936 0.0096  -0.0024 -0.0218 815  ASN B ND2 
14806 N N   . ALA B 818  ? 0.1816 0.1774 0.2010 0.0086  -0.0080 -0.0245 816  ALA B N   
14807 C CA  . ALA B 818  ? 0.1907 0.1839 0.2063 0.0085  -0.0094 -0.0253 816  ALA B CA  
14808 C C   . ALA B 818  ? 0.1948 0.1881 0.2067 0.0095  -0.0079 -0.0258 816  ALA B C   
14809 O O   . ALA B 818  ? 0.1962 0.1909 0.2081 0.0103  -0.0060 -0.0258 816  ALA B O   
14810 C CB  . ALA B 818  ? 0.1691 0.1587 0.1826 0.0082  -0.0109 -0.0261 816  ALA B CB  
14811 N N   . MET B 819  ? 0.1675 0.1594 0.1762 0.0094  -0.0088 -0.0261 817  MET B N   
14812 C CA  . MET B 819  ? 0.1771 0.1690 0.1817 0.0101  -0.0076 -0.0265 817  MET B CA  
14813 C C   . MET B 819  ? 0.2004 0.1888 0.2007 0.0102  -0.0092 -0.0275 817  MET B C   
14814 O O   . MET B 819  ? 0.2091 0.1960 0.2092 0.0093  -0.0113 -0.0274 817  MET B O   
14815 C CB  . MET B 819  ? 0.1887 0.1824 0.1929 0.0097  -0.0070 -0.0257 817  MET B CB  
14816 C CG  . MET B 819  ? 0.1764 0.1703 0.1761 0.0101  -0.0059 -0.0260 817  MET B CG  
14817 S SD  . MET B 819  ? 0.2165 0.2116 0.2152 0.0089  -0.0057 -0.0247 817  MET B SD  
14818 C CE  . MET B 819  ? 0.2273 0.2256 0.2297 0.0088  -0.0039 -0.0240 817  MET B CE  
14819 N N   . ILE B 820  ? 0.2080 0.1952 0.2050 0.0114  -0.0082 -0.0286 818  ILE B N   
14820 C CA  . ILE B 820  ? 0.2001 0.1837 0.1920 0.0118  -0.0093 -0.0298 818  ILE B CA  
14821 C C   . ILE B 820  ? 0.2064 0.1913 0.1944 0.0124  -0.0080 -0.0298 818  ILE B C   
14822 O O   . ILE B 820  ? 0.2048 0.1927 0.1929 0.0133  -0.0056 -0.0295 818  ILE B O   
14823 C CB  . ILE B 820  ? 0.1980 0.1786 0.1880 0.0131  -0.0092 -0.0311 818  ILE B CB  
14824 C CG1 . ILE B 820  ? 0.2252 0.2042 0.2189 0.0120  -0.0108 -0.0308 818  ILE B CG1 
14825 C CG2 . ILE B 820  ? 0.2178 0.1942 0.2017 0.0137  -0.0104 -0.0325 818  ILE B CG2 
14826 C CD1 . ILE B 820  ? 0.2233 0.1984 0.2149 0.0130  -0.0112 -0.0319 818  ILE B CD1 
14827 N N   . VAL B 821  ? 0.2097 0.1926 0.1943 0.0117  -0.0095 -0.0299 819  VAL B N   
14828 C CA  . VAL B 821  ? 0.1941 0.1781 0.1745 0.0118  -0.0085 -0.0297 819  VAL B CA  
14829 C C   . VAL B 821  ? 0.2275 0.2077 0.2020 0.0125  -0.0096 -0.0311 819  VAL B C   
14830 O O   . VAL B 821  ? 0.2417 0.2186 0.2152 0.0117  -0.0123 -0.0315 819  VAL B O   
14831 C CB  . VAL B 821  ? 0.2144 0.1993 0.1959 0.0102  -0.0096 -0.0282 819  VAL B CB  
14832 C CG1 . VAL B 821  ? 0.2363 0.2221 0.2134 0.0100  -0.0086 -0.0277 819  VAL B CG1 
14833 C CG2 . VAL B 821  ? 0.2193 0.2070 0.2063 0.0096  -0.0089 -0.0270 819  VAL B CG2 
14834 N N   . ASP B 822  ? 0.2360 0.2170 0.2065 0.0142  -0.0075 -0.0319 820  ASP B N   
14835 C CA  . ASP B 822  ? 0.2323 0.2095 0.1964 0.0151  -0.0083 -0.0335 820  ASP B CA  
14836 C C   . ASP B 822  ? 0.2656 0.2443 0.2256 0.0145  -0.0078 -0.0327 820  ASP B C   
14837 O O   . ASP B 822  ? 0.2645 0.2465 0.2266 0.0132  -0.0070 -0.0310 820  ASP B O   
14838 C CB  . ASP B 822  ? 0.2392 0.2152 0.2007 0.0177  -0.0067 -0.0352 820  ASP B CB  
14839 C CG  . ASP B 822  ? 0.2827 0.2637 0.2435 0.0194  -0.0032 -0.0349 820  ASP B CG  
14840 O OD1 . ASP B 822  ? 0.2440 0.2290 0.2049 0.0184  -0.0020 -0.0335 820  ASP B OD1 
14841 O OD2 . ASP B 822  ? 0.2750 0.2559 0.2351 0.0219  -0.0018 -0.0361 820  ASP B OD2 
14842 N N   . SER B 823  ? 0.2762 0.2518 0.2297 0.0153  -0.0083 -0.0340 821  SER B N   
14843 C CA  . SER B 823  ? 0.3070 0.2834 0.2560 0.0145  -0.0081 -0.0332 821  SER B CA  
14844 C C   . SER B 823  ? 0.3126 0.2942 0.2606 0.0153  -0.0045 -0.0324 821  SER B C   
14845 O O   . SER B 823  ? 0.3136 0.2965 0.2580 0.0144  -0.0040 -0.0314 821  SER B O   
14846 C CB  . SER B 823  ? 0.3100 0.2814 0.2520 0.0151  -0.0098 -0.0348 821  SER B CB  
14847 O OG  . SER B 823  ? 0.3449 0.3148 0.2835 0.0177  -0.0083 -0.0369 821  SER B OG  
14848 N N   . SER B 824  ? 0.2592 0.2440 0.2101 0.0169  -0.0022 -0.0327 822  SER B N   
14849 C CA  . SER B 824  ? 0.2626 0.2534 0.2135 0.0175  0.0011  -0.0317 822  SER B CA  
14850 C C   . SER B 824  ? 0.2851 0.2801 0.2414 0.0153  0.0016  -0.0295 822  SER B C   
14851 O O   . SER B 824  ? 0.3018 0.3018 0.2581 0.0148  0.0039  -0.0282 822  SER B O   
14852 C CB  . SER B 824  ? 0.2832 0.2759 0.2343 0.0206  0.0034  -0.0332 822  SER B CB  
14853 O OG  . SER B 824  ? 0.2492 0.2433 0.2065 0.0207  0.0035  -0.0328 822  SER B OG  
14854 N N   . ALA B 825  ? 0.2495 0.2426 0.2103 0.0139  -0.0004 -0.0290 823  ALA B N   
14855 C CA  . ALA B 825  ? 0.2517 0.2480 0.2172 0.0121  0.0001  -0.0271 823  ALA B CA  
14856 C C   . ALA B 825  ? 0.2899 0.2867 0.2531 0.0098  -0.0003 -0.0253 823  ALA B C   
14857 O O   . ALA B 825  ? 0.2999 0.2935 0.2588 0.0093  -0.0019 -0.0254 823  ALA B O   
14858 C CB  . ALA B 825  ? 0.2418 0.2357 0.2122 0.0114  -0.0020 -0.0271 823  ALA B CB  
14859 N N   . LEU B 826  ? 0.2922 0.2926 0.2579 0.0083  0.0009  -0.0236 824  LEU B N   
14860 C CA  . LEU B 826  ? 0.2993 0.2997 0.2630 0.0058  0.0003  -0.0217 824  LEU B CA  
14861 C C   . LEU B 826  ? 0.2794 0.2760 0.2457 0.0045  -0.0024 -0.0211 824  LEU B C   
14862 O O   . LEU B 826  ? 0.2611 0.2585 0.2321 0.0043  -0.0024 -0.0208 824  LEU B O   
14863 C CB  . LEU B 826  ? 0.3298 0.3355 0.2949 0.0044  0.0026  -0.0200 824  LEU B CB  
14864 C CG  . LEU B 826  ? 0.3743 0.3799 0.3366 0.0016  0.0022  -0.0178 824  LEU B CG  
14865 C CD1 . LEU B 826  ? 0.4235 0.4277 0.3795 0.0015  0.0021  -0.0177 824  LEU B CD1 
14866 C CD2 . LEU B 826  ? 0.4769 0.4883 0.4409 0.0000  0.0045  -0.0162 824  LEU B CD2 
14867 N N   . ALA B 827  ? 0.2774 0.2701 0.2403 0.0038  -0.0046 -0.0207 825  ALA B N   
14868 C CA  . ALA B 827  ? 0.2418 0.2310 0.2073 0.0033  -0.0074 -0.0204 825  ALA B CA  
14869 C C   . ALA B 827  ? 0.2766 0.2666 0.2452 0.0019  -0.0073 -0.0189 825  ALA B C   
14870 O O   . ALA B 827  ? 0.2603 0.2494 0.2332 0.0023  -0.0083 -0.0191 825  ALA B O   
14871 C CB  . ALA B 827  ? 0.2606 0.2459 0.2215 0.0027  -0.0098 -0.0201 825  ALA B CB  
14872 N N   . GLU B 828  ? 0.2634 0.2549 0.2296 0.0001  -0.0061 -0.0173 826  GLU B N   
14873 C CA  . GLU B 828  ? 0.2835 0.2750 0.2519 -0.0015 -0.0063 -0.0159 826  GLU B CA  
14874 C C   . GLU B 828  ? 0.2934 0.2877 0.2670 -0.0007 -0.0049 -0.0166 826  GLU B C   
14875 O O   . GLU B 828  ? 0.2585 0.2513 0.2351 -0.0010 -0.0058 -0.0163 826  GLU B O   
14876 C CB  . GLU B 828  ? 0.2977 0.2908 0.2626 -0.0038 -0.0051 -0.0140 826  GLU B CB  
14877 C CG  . GLU B 828  ? 0.3557 0.3452 0.3154 -0.0052 -0.0067 -0.0126 826  GLU B CG  
14878 C CD  . GLU B 828  ? 0.3671 0.3569 0.3225 -0.0042 -0.0064 -0.0134 826  GLU B CD  
14879 O OE1 . GLU B 828  ? 0.3467 0.3394 0.3030 -0.0024 -0.0048 -0.0150 826  GLU B OE1 
14880 O OE2 . GLU B 828  ? 0.4053 0.3920 0.3562 -0.0051 -0.0080 -0.0124 826  GLU B OE2 
14881 N N   . GLN B 829  ? 0.2589 0.2571 0.2333 0.0004  -0.0028 -0.0175 827  GLN B N   
14882 C CA  . GLN B 829  ? 0.2638 0.2648 0.2429 0.0012  -0.0015 -0.0181 827  GLN B CA  
14883 C C   . GLN B 829  ? 0.2400 0.2386 0.2225 0.0027  -0.0029 -0.0194 827  GLN B C   
14884 O O   . GLN B 829  ? 0.2300 0.2288 0.2162 0.0027  -0.0029 -0.0194 827  GLN B O   
14885 C CB  . GLN B 829  ? 0.3103 0.3158 0.2892 0.0024  0.0010  -0.0188 827  GLN B CB  
14886 C CG  . GLN B 829  ? 0.3777 0.3875 0.3547 0.0008  0.0028  -0.0173 827  GLN B CG  
14887 C CD  . GLN B 829  ? 0.4614 0.4767 0.4399 0.0024  0.0053  -0.0180 827  GLN B CD  
14888 O OE1 . GLN B 829  ? 0.3965 0.4114 0.3755 0.0049  0.0056  -0.0197 827  GLN B OE1 
14889 N NE2 . GLN B 829  ? 0.4984 0.5187 0.4776 0.0008  0.0070  -0.0166 827  GLN B NE2 
14890 N N   . VAL B 830  ? 0.2352 0.2316 0.2163 0.0040  -0.0039 -0.0205 828  VAL B N   
14891 C CA  . VAL B 830  ? 0.2195 0.2139 0.2038 0.0051  -0.0054 -0.0215 828  VAL B CA  
14892 C C   . VAL B 830  ? 0.2310 0.2234 0.2174 0.0044  -0.0072 -0.0207 828  VAL B C   
14893 O O   . VAL B 830  ? 0.2277 0.2204 0.2183 0.0049  -0.0073 -0.0210 828  VAL B O   
14894 C CB  . VAL B 830  ? 0.2323 0.2242 0.2140 0.0060  -0.0068 -0.0226 828  VAL B CB  
14895 C CG1 . VAL B 830  ? 0.2065 0.1964 0.1916 0.0066  -0.0088 -0.0233 828  VAL B CG1 
14896 C CG2 . VAL B 830  ? 0.2467 0.2400 0.2261 0.0073  -0.0051 -0.0238 828  VAL B CG2 
14897 N N   . VAL B 831  ? 0.2381 0.2282 0.2215 0.0033  -0.0085 -0.0197 829  VAL B N   
14898 C CA  . VAL B 831  ? 0.2307 0.2182 0.2156 0.0031  -0.0104 -0.0189 829  VAL B CA  
14899 C C   . VAL B 831  ? 0.2270 0.2156 0.2145 0.0026  -0.0094 -0.0184 829  VAL B C   
14900 O O   . VAL B 831  ? 0.2370 0.2249 0.2280 0.0035  -0.0101 -0.0186 829  VAL B O   
14901 C CB  . VAL B 831  ? 0.2435 0.2280 0.2240 0.0021  -0.0122 -0.0178 829  VAL B CB  
14902 C CG1 . VAL B 831  ? 0.2263 0.2080 0.2079 0.0020  -0.0139 -0.0169 829  VAL B CG1 
14903 C CG2 . VAL B 831  ? 0.2353 0.2183 0.2138 0.0028  -0.0138 -0.0185 829  VAL B CG2 
14904 N N   . GLY B 832  ? 0.2131 0.2035 0.1990 0.0013  -0.0077 -0.0177 830  GLY B N   
14905 C CA  . GLY B 832  ? 0.2393 0.2305 0.2273 0.0006  -0.0069 -0.0173 830  GLY B CA  
14906 C C   . GLY B 832  ? 0.2402 0.2337 0.2328 0.0021  -0.0059 -0.0184 830  GLY B C   
14907 O O   . GLY B 832  ? 0.2343 0.2270 0.2293 0.0024  -0.0062 -0.0185 830  GLY B O   
14908 N N   . ASP B 833  ? 0.1974 0.1933 0.1907 0.0030  -0.0048 -0.0193 831  ASP B N   
14909 C CA  . ASP B 833  ? 0.1980 0.1960 0.1953 0.0043  -0.0039 -0.0202 831  ASP B CA  
14910 C C   . ASP B 833  ? 0.1922 0.1884 0.1922 0.0054  -0.0054 -0.0208 831  ASP B C   
14911 O O   . ASP B 833  ? 0.2023 0.1995 0.2058 0.0061  -0.0049 -0.0211 831  ASP B O   
14912 C CB  . ASP B 833  ? 0.1876 0.1882 0.1845 0.0051  -0.0024 -0.0209 831  ASP B CB  
14913 C CG  . ASP B 833  ? 0.2172 0.2211 0.2126 0.0041  -0.0006 -0.0202 831  ASP B CG  
14914 O OD1 . ASP B 833  ? 0.2333 0.2374 0.2286 0.0025  -0.0006 -0.0192 831  ASP B OD1 
14915 O OD2 . ASP B 833  ? 0.2234 0.2296 0.2177 0.0049  0.0007  -0.0207 831  ASP B OD2 
14916 N N   . VAL B 834  ? 0.1960 0.1898 0.1945 0.0056  -0.0072 -0.0209 832  VAL B N   
14917 C CA  . VAL B 834  ? 0.1934 0.1862 0.1949 0.0065  -0.0088 -0.0212 832  VAL B CA  
14918 C C   . VAL B 834  ? 0.2115 0.2033 0.2147 0.0066  -0.0094 -0.0206 832  VAL B C   
14919 O O   . VAL B 834  ? 0.2126 0.2054 0.2197 0.0076  -0.0094 -0.0209 832  VAL B O   
14920 C CB  . VAL B 834  ? 0.2022 0.1929 0.2016 0.0065  -0.0107 -0.0214 832  VAL B CB  
14921 C CG1 . VAL B 834  ? 0.2187 0.2087 0.2212 0.0072  -0.0127 -0.0213 832  VAL B CG1 
14922 C CG2 . VAL B 834  ? 0.2373 0.2285 0.2353 0.0069  -0.0102 -0.0224 832  VAL B CG2 
14923 N N   . ILE B 835  ? 0.2112 0.2010 0.2115 0.0058  -0.0100 -0.0197 833  ILE B N   
14924 C CA  . ILE B 835  ? 0.2491 0.2370 0.2503 0.0062  -0.0107 -0.0193 833  ILE B CA  
14925 C C   . ILE B 835  ? 0.2499 0.2395 0.2535 0.0064  -0.0091 -0.0196 833  ILE B C   
14926 O O   . ILE B 835  ? 0.2770 0.2667 0.2834 0.0076  -0.0093 -0.0198 833  ILE B O   
14927 C CB  . ILE B 835  ? 0.2672 0.2518 0.2640 0.0050  -0.0117 -0.0182 833  ILE B CB  
14928 C CG1 . ILE B 835  ? 0.2938 0.2763 0.2887 0.0052  -0.0138 -0.0178 833  ILE B CG1 
14929 C CG2 . ILE B 835  ? 0.3060 0.2881 0.3030 0.0054  -0.0122 -0.0178 833  ILE B CG2 
14930 C CD1 . ILE B 835  ? 0.3051 0.2839 0.2956 0.0042  -0.0151 -0.0166 833  ILE B CD1 
14931 N N   . THR B 836  ? 0.2141 0.2055 0.2165 0.0053  -0.0074 -0.0195 834  THR B N   
14932 C CA  . THR B 836  ? 0.2422 0.2355 0.2467 0.0053  -0.0059 -0.0198 834  THR B CA  
14933 C C   . THR B 836  ? 0.2411 0.2367 0.2497 0.0068  -0.0053 -0.0206 834  THR B C   
14934 O O   . THR B 836  ? 0.2598 0.2556 0.2708 0.0076  -0.0050 -0.0209 834  THR B O   
14935 C CB  . THR B 836  ? 0.2412 0.2368 0.2441 0.0039  -0.0043 -0.0195 834  THR B CB  
14936 O OG1 . THR B 836  ? 0.3017 0.2954 0.3009 0.0021  -0.0048 -0.0185 834  THR B OG1 
14937 C CG2 . THR B 836  ? 0.2609 0.2590 0.2661 0.0040  -0.0029 -0.0199 834  THR B CG2 
14938 N N   . SER B 837  ? 0.2063 0.2033 0.2155 0.0071  -0.0052 -0.0210 835  SER B N   
14939 C CA  . SER B 837  ? 0.2051 0.2041 0.2178 0.0080  -0.0045 -0.0216 835  SER B CA  
14940 C C   . SER B 837  ? 0.1945 0.1931 0.2102 0.0090  -0.0058 -0.0216 835  SER B C   
14941 O O   . SER B 837  ? 0.2156 0.2160 0.2345 0.0096  -0.0051 -0.0218 835  SER B O   
14942 C CB  . SER B 837  ? 0.1817 0.1815 0.1938 0.0081  -0.0042 -0.0221 835  SER B CB  
14943 O OG  . SER B 837  ? 0.1972 0.1982 0.2070 0.0075  -0.0029 -0.0220 835  SER B OG  
14944 N N   . ALA B 838  ? 0.1939 0.1907 0.2086 0.0090  -0.0076 -0.0214 836  ALA B N   
14945 C CA  . ALA B 838  ? 0.1694 0.1666 0.1873 0.0100  -0.0089 -0.0213 836  ALA B CA  
14946 C C   . ALA B 838  ? 0.1984 0.1950 0.2174 0.0110  -0.0093 -0.0210 836  ALA B C   
14947 O O   . ALA B 838  ? 0.2205 0.2189 0.2432 0.0122  -0.0094 -0.0210 836  ALA B O   
14948 C CB  . ALA B 838  ? 0.1958 0.1915 0.2122 0.0097  -0.0110 -0.0212 836  ALA B CB  
14949 N N   . PHE B 839  ? 0.2203 0.2141 0.2358 0.0107  -0.0095 -0.0207 837  PHE B N   
14950 C CA  . PHE B 839  ? 0.2410 0.2329 0.2568 0.0120  -0.0104 -0.0205 837  PHE B CA  
14951 C C   . PHE B 839  ? 0.2508 0.2412 0.2649 0.0120  -0.0092 -0.0206 837  PHE B C   
14952 O O   . PHE B 839  ? 0.2466 0.2356 0.2613 0.0135  -0.0096 -0.0207 837  PHE B O   
14953 C CB  . PHE B 839  ? 0.2325 0.2212 0.2453 0.0119  -0.0126 -0.0198 837  PHE B CB  
14954 C CG  . PHE B 839  ? 0.2298 0.2196 0.2437 0.0118  -0.0141 -0.0197 837  PHE B CG  
14955 C CD1 . PHE B 839  ? 0.2112 0.2036 0.2296 0.0131  -0.0148 -0.0198 837  PHE B CD1 
14956 C CD2 . PHE B 839  ? 0.2286 0.2169 0.2389 0.0104  -0.0148 -0.0195 837  PHE B CD2 
14957 C CE1 . PHE B 839  ? 0.2098 0.2031 0.2291 0.0127  -0.0165 -0.0197 837  PHE B CE1 
14958 C CE2 . PHE B 839  ? 0.2472 0.2360 0.2579 0.0103  -0.0164 -0.0195 837  PHE B CE2 
14959 C CZ  . PHE B 839  ? 0.2670 0.2582 0.2822 0.0114  -0.0174 -0.0196 837  PHE B CZ  
14960 N N   . ASP B 840  ? 0.2617 0.2523 0.2738 0.0104  -0.0079 -0.0207 838  ASP B N   
14961 C CA  . ASP B 840  ? 0.2746 0.2644 0.2856 0.0102  -0.0068 -0.0209 838  ASP B CA  
14962 C C   . ASP B 840  ? 0.2768 0.2688 0.2915 0.0120  -0.0058 -0.0215 838  ASP B C   
14963 O O   . ASP B 840  ? 0.2200 0.2154 0.2382 0.0124  -0.0052 -0.0217 838  ASP B O   
14964 C CB  . ASP B 840  ? 0.3432 0.3347 0.3529 0.0083  -0.0054 -0.0208 838  ASP B CB  
14965 C CG  . ASP B 840  ? 0.4085 0.3996 0.4172 0.0077  -0.0044 -0.0210 838  ASP B CG  
14966 O OD1 . ASP B 840  ? 0.3841 0.3770 0.3952 0.0088  -0.0034 -0.0216 838  ASP B OD1 
14967 O OD2 . ASP B 840  ? 0.4160 0.4049 0.4213 0.0060  -0.0048 -0.0205 838  ASP B OD2 
14968 N N   . SER B 841  ? 0.2435 0.2332 0.2571 0.0129  -0.0058 -0.0218 839  SER B N   
14969 C CA  . SER B 841  ? 0.2233 0.2149 0.2398 0.0148  -0.0047 -0.0224 839  SER B CA  
14970 C C   . SER B 841  ? 0.2094 0.2035 0.2300 0.0167  -0.0053 -0.0223 839  SER B C   
14971 O O   . SER B 841  ? 0.2032 0.2009 0.2274 0.0177  -0.0042 -0.0225 839  SER B O   
14972 C CB  . SER B 841  ? 0.2423 0.2373 0.2603 0.0141  -0.0028 -0.0227 839  SER B CB  
14973 O OG  . SER B 841  ? 0.2861 0.2794 0.3007 0.0123  -0.0024 -0.0227 839  SER B OG  
14974 N N   . ALA B 842  ? 0.1890 0.1814 0.2089 0.0169  -0.0072 -0.0218 840  ALA B N   
14975 C CA  . ALA B 842  ? 0.1837 0.1786 0.2074 0.0182  -0.0083 -0.0215 840  ALA B CA  
14976 C C   . ALA B 842  ? 0.1730 0.1726 0.2005 0.0174  -0.0074 -0.0214 840  ALA B C   
14977 O O   . ALA B 842  ? 0.1823 0.1855 0.2141 0.0186  -0.0073 -0.0213 840  ALA B O   
14978 C CB  . ALA B 842  ? 0.2057 0.2009 0.2314 0.0211  -0.0083 -0.0217 840  ALA B CB  
14979 N N   . GLY B 843  ? 0.1753 0.1749 0.2012 0.0154  -0.0068 -0.0215 841  GLY B N   
14980 C CA  . GLY B 843  ? 0.1950 0.1979 0.2237 0.0146  -0.0062 -0.0214 841  GLY B CA  
14981 C C   . GLY B 843  ? 0.1929 0.1989 0.2245 0.0151  -0.0043 -0.0215 841  GLY B C   
14982 O O   . GLY B 843  ? 0.1842 0.1930 0.2186 0.0146  -0.0040 -0.0213 841  GLY B O   
14983 N N   . GLN B 844  ? 0.1736 0.1789 0.2042 0.0161  -0.0032 -0.0219 842  GLN B N   
14984 C CA  . GLN B 844  ? 0.1649 0.1731 0.1978 0.0167  -0.0014 -0.0220 842  GLN B CA  
14985 C C   . GLN B 844  ? 0.1937 0.2018 0.2248 0.0154  0.0000  -0.0222 842  GLN B C   
14986 O O   . GLN B 844  ? 0.1798 0.1877 0.2096 0.0157  0.0012  -0.0225 842  GLN B O   
14987 C CB  . GLN B 844  ? 0.1625 0.1701 0.1953 0.0189  -0.0009 -0.0224 842  GLN B CB  
14988 C CG  . GLN B 844  ? 0.1811 0.1901 0.2169 0.0206  -0.0022 -0.0221 842  GLN B CG  
14989 C CD  . GLN B 844  ? 0.1855 0.1929 0.2205 0.0232  -0.0022 -0.0226 842  GLN B CD  
14990 O OE1 . GLN B 844  ? 0.1877 0.1985 0.2260 0.0252  -0.0014 -0.0225 842  GLN B OE1 
14991 N NE2 . GLN B 844  ? 0.1826 0.1848 0.2130 0.0232  -0.0030 -0.0230 842  GLN B NE2 
14992 N N   . ARG B 845  ? 0.1804 0.1888 0.2112 0.0139  -0.0003 -0.0219 843  ARG B N   
14993 C CA  . ARG B 845  ? 0.1630 0.1721 0.1928 0.0129  0.0009  -0.0219 843  ARG B CA  
14994 C C   . ARG B 845  ? 0.1720 0.1832 0.2045 0.0124  0.0009  -0.0215 843  ARG B C   
14995 O O   . ARG B 845  ? 0.1582 0.1691 0.1916 0.0121  -0.0004 -0.0214 843  ARG B O   
14996 C CB  . ARG B 845  ? 0.1727 0.1798 0.1990 0.0117  0.0005  -0.0220 843  ARG B CB  
14997 C CG  . ARG B 845  ? 0.2045 0.2090 0.2276 0.0115  0.0002  -0.0222 843  ARG B CG  
14998 C CD  . ARG B 845  ? 0.2522 0.2559 0.2723 0.0100  0.0001  -0.0220 843  ARG B CD  
14999 N NE  . ARG B 845  ? 0.2731 0.2744 0.2901 0.0092  -0.0002 -0.0220 843  ARG B NE  
15000 C CZ  . ARG B 845  ? 0.3992 0.4008 0.4148 0.0084  0.0006  -0.0221 843  ARG B CZ  
15001 N NH1 . ARG B 845  ? 0.3828 0.3872 0.3999 0.0085  0.0019  -0.0221 843  ARG B NH1 
15002 N NH2 . ARG B 845  ? 0.4404 0.4391 0.4529 0.0075  0.0000  -0.0220 843  ARG B NH2 
15003 N N   . CYS B 846  ? 0.1772 0.1901 0.2106 0.0122  0.0022  -0.0213 844  CYS B N   
15004 C CA  . CYS B 846  ? 0.1964 0.2104 0.2317 0.0116  0.0021  -0.0209 844  CYS B CA  
15005 C C   . CYS B 846  ? 0.1564 0.1684 0.1896 0.0109  0.0012  -0.0211 844  CYS B C   
15006 O O   . CYS B 846  ? 0.1766 0.1881 0.2106 0.0104  0.0003  -0.0210 844  CYS B O   
15007 C CB  . CYS B 846  ? 0.1913 0.2069 0.2273 0.0115  0.0036  -0.0205 844  CYS B CB  
15008 S SG  . CYS B 846  ? 0.1859 0.2008 0.2185 0.0114  0.0046  -0.0208 844  CYS B SG  
15009 N N   . SER B 847  ? 0.1579 0.1687 0.1880 0.0108  0.0014  -0.0215 845  SER B N   
15010 C CA  . SER B 847  ? 0.1707 0.1800 0.1983 0.0104  0.0009  -0.0218 845  SER B CA  
15011 C C   . SER B 847  ? 0.1803 0.1878 0.2068 0.0102  -0.0007 -0.0221 845  SER B C   
15012 O O   . SER B 847  ? 0.1728 0.1790 0.1969 0.0100  -0.0011 -0.0224 845  SER B O   
15013 C CB  . SER B 847  ? 0.1931 0.2027 0.2182 0.0102  0.0018  -0.0219 845  SER B CB  
15014 O OG  . SER B 847  ? 0.1792 0.1882 0.2036 0.0101  0.0017  -0.0219 845  SER B OG  
15015 N N   . ALA B 848  ? 0.1791 0.1864 0.2069 0.0105  -0.0015 -0.0219 846  ALA B N   
15016 C CA  . ALA B 848  ? 0.1755 0.1809 0.2017 0.0104  -0.0031 -0.0220 846  ALA B CA  
15017 C C   . ALA B 848  ? 0.1893 0.1938 0.2151 0.0100  -0.0044 -0.0222 846  ALA B C   
15018 O O   . ALA B 848  ? 0.1718 0.1771 0.1998 0.0098  -0.0047 -0.0221 846  ALA B O   
15019 C CB  . ALA B 848  ? 0.1694 0.1751 0.1977 0.0112  -0.0039 -0.0217 846  ALA B CB  
15020 N N   . LEU B 849  ? 0.1713 0.1738 0.1939 0.0096  -0.0054 -0.0223 847  LEU B N   
15021 C CA  . LEU B 849  ? 0.1912 0.1921 0.2126 0.0093  -0.0070 -0.0226 847  LEU B CA  
15022 C C   . LEU B 849  ? 0.1930 0.1943 0.2172 0.0093  -0.0088 -0.0223 847  LEU B C   
15023 O O   . LEU B 849  ? 0.1947 0.1959 0.2193 0.0097  -0.0097 -0.0219 847  LEU B O   
15024 C CB  . LEU B 849  ? 0.2010 0.1999 0.2180 0.0090  -0.0074 -0.0228 847  LEU B CB  
15025 C CG  . LEU B 849  ? 0.2032 0.2001 0.2180 0.0086  -0.0092 -0.0232 847  LEU B CG  
15026 C CD1 . LEU B 849  ? 0.2169 0.2134 0.2315 0.0087  -0.0088 -0.0239 847  LEU B CD1 
15027 C CD2 . LEU B 849  ? 0.2163 0.2116 0.2265 0.0083  -0.0093 -0.0232 847  LEU B CD2 
15028 N N   . ARG B 850  ? 0.1708 0.1724 0.1969 0.0088  -0.0095 -0.0224 848  ARG B N   
15029 C CA  . ARG B 850  ? 0.1843 0.1870 0.2136 0.0084  -0.0114 -0.0219 848  ARG B CA  
15030 C C   . ARG B 850  ? 0.1988 0.1992 0.2259 0.0076  -0.0137 -0.0222 848  ARG B C   
15031 O O   . ARG B 850  ? 0.1992 0.2002 0.2280 0.0073  -0.0157 -0.0218 848  ARG B O   
15032 C CB  . ARG B 850  ? 0.1755 0.1807 0.2089 0.0079  -0.0108 -0.0214 848  ARG B CB  
15033 C CG  . ARG B 850  ? 0.1762 0.1837 0.2115 0.0087  -0.0084 -0.0211 848  ARG B CG  
15034 C CD  . ARG B 850  ? 0.1710 0.1799 0.2074 0.0099  -0.0082 -0.0208 848  ARG B CD  
15035 N NE  . ARG B 850  ? 0.1859 0.1968 0.2239 0.0107  -0.0061 -0.0207 848  ARG B NE  
15036 C CZ  . ARG B 850  ? 0.1988 0.2102 0.2369 0.0119  -0.0055 -0.0207 848  ARG B CZ  
15037 N NH1 . ARG B 850  ? 0.1802 0.1900 0.2169 0.0126  -0.0067 -0.0208 848  ARG B NH1 
15038 N NH2 . ARG B 850  ? 0.1803 0.1933 0.2194 0.0125  -0.0036 -0.0206 848  ARG B NH2 
15039 N N   . VAL B 851  ? 0.1990 0.1967 0.2223 0.0072  -0.0135 -0.0231 849  VAL B N   
15040 C CA  . VAL B 851  ? 0.1960 0.1909 0.2166 0.0065  -0.0157 -0.0236 849  VAL B CA  
15041 C C   . VAL B 851  ? 0.2185 0.2107 0.2334 0.0070  -0.0151 -0.0245 849  VAL B C   
15042 O O   . VAL B 851  ? 0.2159 0.2073 0.2290 0.0074  -0.0134 -0.0251 849  VAL B O   
15043 C CB  . VAL B 851  ? 0.2217 0.2155 0.2432 0.0055  -0.0165 -0.0239 849  VAL B CB  
15044 C CG1 . VAL B 851  ? 0.2476 0.2381 0.2660 0.0045  -0.0192 -0.0245 849  VAL B CG1 
15045 C CG2 . VAL B 851  ? 0.2243 0.2215 0.2517 0.0048  -0.0167 -0.0228 849  VAL B CG2 
15046 N N   . LEU B 852  ? 0.1988 0.1898 0.2110 0.0069  -0.0164 -0.0244 850  LEU B N   
15047 C CA  . LEU B 852  ? 0.1908 0.1796 0.1975 0.0072  -0.0159 -0.0251 850  LEU B CA  
15048 C C   . LEU B 852  ? 0.1985 0.1841 0.2017 0.0067  -0.0178 -0.0260 850  LEU B C   
15049 O O   . LEU B 852  ? 0.2177 0.2023 0.2211 0.0060  -0.0203 -0.0258 850  LEU B O   
15050 C CB  . LEU B 852  ? 0.1942 0.1830 0.1993 0.0072  -0.0162 -0.0243 850  LEU B CB  
15051 C CG  . LEU B 852  ? 0.2035 0.1903 0.2027 0.0072  -0.0159 -0.0246 850  LEU B CG  
15052 C CD1 . LEU B 852  ? 0.1883 0.1764 0.1862 0.0078  -0.0130 -0.0250 850  LEU B CD1 
15053 C CD2 . LEU B 852  ? 0.2270 0.2135 0.2249 0.0070  -0.0166 -0.0236 850  LEU B CD2 
15054 N N   . CYS B 853  ? 0.1991 0.1828 0.1988 0.0073  -0.0166 -0.0271 851  CYS B N   
15055 C CA  . CYS B 853  ? 0.1883 0.1681 0.1839 0.0071  -0.0183 -0.0283 851  CYS B CA  
15056 C C   . CYS B 853  ? 0.1885 0.1668 0.1781 0.0079  -0.0177 -0.0290 851  CYS B C   
15057 O O   . CYS B 853  ? 0.2189 0.1981 0.2066 0.0090  -0.0152 -0.0294 851  CYS B O   
15058 C CB  . CYS B 853  ? 0.2025 0.1809 0.1984 0.0076  -0.0176 -0.0292 851  CYS B CB  
15059 S SG  . CYS B 853  ? 0.2421 0.2229 0.2451 0.0065  -0.0178 -0.0281 851  CYS B SG  
15060 N N   . LEU B 854  ? 0.2134 0.1896 0.1999 0.0072  -0.0199 -0.0291 852  LEU B N   
15061 C CA  . LEU B 854  ? 0.2128 0.1878 0.1934 0.0076  -0.0195 -0.0294 852  LEU B CA  
15062 C C   . LEU B 854  ? 0.2151 0.1858 0.1901 0.0078  -0.0209 -0.0310 852  LEU B C   
15063 O O   . LEU B 854  ? 0.2471 0.2154 0.2222 0.0067  -0.0239 -0.0313 852  LEU B O   
15064 C CB  . LEU B 854  ? 0.2096 0.1853 0.1903 0.0067  -0.0210 -0.0280 852  LEU B CB  
15065 C CG  . LEU B 854  ? 0.2168 0.1958 0.2020 0.0066  -0.0199 -0.0265 852  LEU B CG  
15066 C CD1 . LEU B 854  ? 0.2008 0.1793 0.1855 0.0060  -0.0220 -0.0253 852  LEU B CD1 
15067 C CD2 . LEU B 854  ? 0.2251 0.2061 0.2091 0.0072  -0.0167 -0.0263 852  LEU B CD2 
15068 N N   . GLN B 855  ? 0.2305 0.2004 0.2005 0.0092  -0.0190 -0.0320 853  GLN B N   
15069 C CA  . GLN B 855  ? 0.2314 0.1967 0.1950 0.0097  -0.0203 -0.0337 853  GLN B CA  
15070 C C   . GLN B 855  ? 0.2749 0.2385 0.2355 0.0083  -0.0231 -0.0333 853  GLN B C   
15071 O O   . GLN B 855  ? 0.2500 0.2159 0.2111 0.0078  -0.0228 -0.0318 853  GLN B O   
15072 C CB  . GLN B 855  ? 0.2394 0.2049 0.1979 0.0117  -0.0174 -0.0348 853  GLN B CB  
15073 C CG  . GLN B 855  ? 0.2740 0.2342 0.2257 0.0127  -0.0185 -0.0370 853  GLN B CG  
15074 C CD  . GLN B 855  ? 0.3324 0.2932 0.2791 0.0152  -0.0154 -0.0381 853  GLN B CD  
15075 O OE1 . GLN B 855  ? 0.3382 0.3024 0.2876 0.0166  -0.0126 -0.0379 853  GLN B OE1 
15076 N NE2 . GLN B 855  ? 0.3567 0.3143 0.2960 0.0159  -0.0160 -0.0394 853  GLN B NE2 
15077 N N   . GLU B 856  ? 0.2611 0.2203 0.2188 0.0077  -0.0260 -0.0344 854  GLU B N   
15078 C CA  . GLU B 856  ? 0.2702 0.2280 0.2264 0.0061  -0.0294 -0.0338 854  GLU B CA  
15079 C C   . GLU B 856  ? 0.3063 0.2644 0.2573 0.0064  -0.0287 -0.0333 854  GLU B C   
15080 O O   . GLU B 856  ? 0.3225 0.2815 0.2743 0.0053  -0.0304 -0.0317 854  GLU B O   
15081 C CB  . GLU B 856  ? 0.3357 0.2883 0.2882 0.0053  -0.0325 -0.0354 854  GLU B CB  
15082 N N   . ASP B 857  ? 0.3226 0.2800 0.2681 0.0080  -0.0261 -0.0344 855  ASP B N   
15083 C CA  . ASP B 857  ? 0.3060 0.2633 0.2454 0.0082  -0.0254 -0.0340 855  ASP B CA  
15084 C C   . ASP B 857  ? 0.3196 0.2813 0.2619 0.0076  -0.0236 -0.0317 855  ASP B C   
15085 O O   . ASP B 857  ? 0.3502 0.3118 0.2886 0.0070  -0.0241 -0.0307 855  ASP B O   
15086 C CB  . ASP B 857  ? 0.3829 0.3391 0.3161 0.0102  -0.0228 -0.0358 855  ASP B CB  
15087 N N   . VAL B 858  ? 0.2759 0.2413 0.2247 0.0078  -0.0218 -0.0309 856  VAL B N   
15088 C CA  . VAL B 858  ? 0.2762 0.2451 0.2276 0.0071  -0.0203 -0.0289 856  VAL B CA  
15089 C C   . VAL B 858  ? 0.2649 0.2348 0.2228 0.0061  -0.0221 -0.0275 856  VAL B C   
15090 O O   . VAL B 858  ? 0.2621 0.2342 0.2222 0.0056  -0.0212 -0.0259 856  VAL B O   
15091 C CB  . VAL B 858  ? 0.2648 0.2374 0.2178 0.0081  -0.0164 -0.0288 856  VAL B CB  
15092 C CG1 . VAL B 858  ? 0.3044 0.2771 0.2511 0.0094  -0.0143 -0.0299 856  VAL B CG1 
15093 C CG2 . VAL B 858  ? 0.2578 0.2312 0.2162 0.0089  -0.0158 -0.0297 856  VAL B CG2 
15094 N N   . ALA B 859  ? 0.2669 0.2353 0.2277 0.0058  -0.0246 -0.0281 857  ALA B N   
15095 C CA  . ALA B 859  ? 0.2472 0.2176 0.2150 0.0053  -0.0258 -0.0269 857  ALA B CA  
15096 C C   . ALA B 859  ? 0.2579 0.2284 0.2255 0.0046  -0.0274 -0.0251 857  ALA B C   
15097 O O   . ALA B 859  ? 0.2545 0.2272 0.2261 0.0046  -0.0266 -0.0238 857  ALA B O   
15098 C CB  . ALA B 859  ? 0.2535 0.2227 0.2242 0.0048  -0.0283 -0.0277 857  ALA B CB  
15099 N N   . ASP B 860  ? 0.2838 0.2516 0.2465 0.0041  -0.0298 -0.0250 858  ASP B N   
15100 C CA  . ASP B 860  ? 0.2873 0.2546 0.2497 0.0035  -0.0318 -0.0232 858  ASP B CA  
15101 C C   . ASP B 860  ? 0.2567 0.2250 0.2175 0.0035  -0.0295 -0.0219 858  ASP B C   
15102 O O   . ASP B 860  ? 0.2597 0.2287 0.2234 0.0034  -0.0300 -0.0204 858  ASP B O   
15103 C CB  . ASP B 860  ? 0.2765 0.2406 0.2330 0.0029  -0.0348 -0.0234 858  ASP B CB  
15104 C CG  . ASP B 860  ? 0.3368 0.3000 0.2956 0.0025  -0.0380 -0.0242 858  ASP B CG  
15105 O OD1 . ASP B 860  ? 0.3574 0.3231 0.3232 0.0026  -0.0385 -0.0239 858  ASP B OD1 
15106 O OD2 . ASP B 860  ? 0.3967 0.3570 0.3502 0.0020  -0.0400 -0.0251 858  ASP B OD2 
15107 N N   . ARG B 861  ? 0.2643 0.2326 0.2203 0.0035  -0.0269 -0.0224 859  ARG B N   
15108 C CA  . ARG B 861  ? 0.2776 0.2470 0.2319 0.0029  -0.0248 -0.0209 859  ARG B CA  
15109 C C   . ARG B 861  ? 0.2641 0.2364 0.2244 0.0031  -0.0229 -0.0204 859  ARG B C   
15110 O O   . ARG B 861  ? 0.2612 0.2335 0.2224 0.0025  -0.0228 -0.0188 859  ARG B O   
15111 C CB  . ARG B 861  ? 0.3295 0.2994 0.2779 0.0029  -0.0224 -0.0215 859  ARG B CB  
15112 C CG  . ARG B 861  ? 0.4237 0.3956 0.3709 0.0020  -0.0199 -0.0199 859  ARG B CG  
15113 C CD  . ARG B 861  ? 0.5138 0.4861 0.4541 0.0017  -0.0182 -0.0198 859  ARG B CD  
15114 N NE  . ARG B 861  ? 0.5654 0.5402 0.5052 0.0004  -0.0159 -0.0180 859  ARG B NE  
15115 C CZ  . ARG B 861  ? 0.5237 0.5026 0.4658 0.0006  -0.0128 -0.0182 859  ARG B CZ  
15116 N NH1 . ARG B 861  ? 0.5030 0.4837 0.4477 0.0023  -0.0114 -0.0201 859  ARG B NH1 
15117 N NH2 . ARG B 861  ? 0.5275 0.5085 0.4692 -0.0011 -0.0112 -0.0163 859  ARG B NH2 
15118 N N   . ILE B 862  ? 0.2378 0.2120 0.2019 0.0040  -0.0214 -0.0218 860  ILE B N   
15119 C CA  . ILE B 862  ? 0.2211 0.1979 0.1907 0.0042  -0.0197 -0.0214 860  ILE B CA  
15120 C C   . ILE B 862  ? 0.2043 0.1807 0.1785 0.0043  -0.0217 -0.0206 860  ILE B C   
15121 O O   . ILE B 862  ? 0.2339 0.2112 0.2104 0.0041  -0.0209 -0.0196 860  ILE B O   
15122 C CB  . ILE B 862  ? 0.2310 0.2096 0.2032 0.0051  -0.0179 -0.0230 860  ILE B CB  
15123 C CG1 . ILE B 862  ? 0.2716 0.2515 0.2396 0.0055  -0.0152 -0.0236 860  ILE B CG1 
15124 C CG2 . ILE B 862  ? 0.2305 0.2115 0.2088 0.0054  -0.0167 -0.0227 860  ILE B CG2 
15125 C CD1 . ILE B 862  ? 0.2866 0.2674 0.2558 0.0068  -0.0137 -0.0253 860  ILE B CD1 
15126 N N   . LEU B 863  ? 0.2380 0.2134 0.2137 0.0046  -0.0244 -0.0209 861  LEU B N   
15127 C CA  . LEU B 863  ? 0.2514 0.2271 0.2319 0.0050  -0.0263 -0.0201 861  LEU B CA  
15128 C C   . LEU B 863  ? 0.2767 0.2505 0.2549 0.0048  -0.0276 -0.0184 861  LEU B C   
15129 O O   . LEU B 863  ? 0.2479 0.2221 0.2293 0.0053  -0.0277 -0.0176 861  LEU B O   
15130 C CB  . LEU B 863  ? 0.2619 0.2375 0.2445 0.0051  -0.0291 -0.0207 861  LEU B CB  
15131 C CG  . LEU B 863  ? 0.2545 0.2318 0.2406 0.0052  -0.0281 -0.0220 861  LEU B CG  
15132 C CD1 . LEU B 863  ? 0.2910 0.2676 0.2778 0.0047  -0.0312 -0.0225 861  LEU B CD1 
15133 C CD2 . LEU B 863  ? 0.3038 0.2842 0.2963 0.0059  -0.0266 -0.0216 861  LEU B CD2 
15134 N N   . THR B 864  ? 0.2681 0.2394 0.2402 0.0040  -0.0286 -0.0180 862  THR B N   
15135 C CA  . THR B 864  ? 0.2593 0.2282 0.2285 0.0036  -0.0299 -0.0162 862  THR B CA  
15136 C C   . THR B 864  ? 0.2878 0.2571 0.2571 0.0031  -0.0274 -0.0154 862  THR B C   
15137 O O   . THR B 864  ? 0.2699 0.2376 0.2402 0.0034  -0.0282 -0.0142 862  THR B O   
15138 C CB  . THR B 864  ? 0.3033 0.2696 0.2655 0.0027  -0.0311 -0.0158 862  THR B CB  
15139 O OG1 . THR B 864  ? 0.3278 0.2932 0.2900 0.0031  -0.0341 -0.0163 862  THR B OG1 
15140 C CG2 . THR B 864  ? 0.3355 0.2989 0.2940 0.0020  -0.0321 -0.0137 862  THR B CG2 
15141 N N   . MET B 865  ? 0.2602 0.2314 0.2283 0.0025  -0.0245 -0.0160 863  MET B N   
15142 C CA  . MET B 865  ? 0.2350 0.2069 0.2030 0.0016  -0.0222 -0.0152 863  MET B CA  
15143 C C   . MET B 865  ? 0.2347 0.2080 0.2087 0.0025  -0.0216 -0.0155 863  MET B C   
15144 O O   . MET B 865  ? 0.2311 0.2031 0.2054 0.0022  -0.0215 -0.0145 863  MET B O   
15145 C CB  . MET B 865  ? 0.2614 0.2359 0.2272 0.0009  -0.0193 -0.0159 863  MET B CB  
15146 C CG  . MET B 865  ? 0.2609 0.2368 0.2264 -0.0003 -0.0171 -0.0149 863  MET B CG  
15147 S SD  . MET B 865  ? 0.3158 0.2959 0.2793 -0.0008 -0.0137 -0.0155 863  MET B SD  
15148 C CE  . MET B 865  ? 0.3208 0.2991 0.2775 -0.0010 -0.0146 -0.0155 863  MET B CE  
15149 N N   . LEU B 866  ? 0.2292 0.2047 0.2076 0.0037  -0.0214 -0.0169 864  LEU B N   
15150 C CA  . LEU B 866  ? 0.2131 0.1903 0.1972 0.0047  -0.0208 -0.0172 864  LEU B CA  
15151 C C   . LEU B 866  ? 0.2327 0.2077 0.2183 0.0056  -0.0230 -0.0163 864  LEU B C   
15152 O O   . LEU B 866  ? 0.2257 0.2002 0.2129 0.0060  -0.0224 -0.0159 864  LEU B O   
15153 C CB  . LEU B 866  ? 0.2256 0.2053 0.2138 0.0055  -0.0205 -0.0186 864  LEU B CB  
15154 C CG  . LEU B 866  ? 0.2228 0.2046 0.2169 0.0066  -0.0200 -0.0189 864  LEU B CG  
15155 C CD1 . LEU B 866  ? 0.2560 0.2387 0.2506 0.0063  -0.0175 -0.0188 864  LEU B CD1 
15156 C CD2 . LEU B 866  ? 0.2437 0.2277 0.2412 0.0070  -0.0199 -0.0200 864  LEU B CD2 
15157 N N   . LYS B 867  ? 0.2399 0.2136 0.2249 0.0061  -0.0257 -0.0160 865  LYS B N   
15158 C CA  . LYS B 867  ? 0.2413 0.2133 0.2279 0.0074  -0.0280 -0.0151 865  LYS B CA  
15159 C C   . LYS B 867  ? 0.2597 0.2278 0.2421 0.0068  -0.0283 -0.0137 865  LYS B C   
15160 O O   . LYS B 867  ? 0.2417 0.2083 0.2257 0.0080  -0.0287 -0.0132 865  LYS B O   
15161 C CB  . LYS B 867  ? 0.2280 0.1998 0.2147 0.0079  -0.0310 -0.0149 865  LYS B CB  
15162 C CG  . LYS B 867  ? 0.2883 0.2638 0.2801 0.0084  -0.0311 -0.0161 865  LYS B CG  
15163 C CD  . LYS B 867  ? 0.3292 0.3046 0.3200 0.0080  -0.0339 -0.0162 865  LYS B CD  
15164 C CE  . LYS B 867  ? 0.3661 0.3448 0.3616 0.0080  -0.0339 -0.0173 865  LYS B CE  
15165 N NZ  . LYS B 867  ? 0.4128 0.3912 0.4074 0.0074  -0.0370 -0.0174 865  LYS B NZ  
15166 N N   . GLY B 868  ? 0.2549 0.2212 0.2316 0.0050  -0.0280 -0.0130 866  GLY B N   
15167 C CA  . GLY B 868  ? 0.2554 0.2179 0.2279 0.0039  -0.0281 -0.0115 866  GLY B CA  
15168 C C   . GLY B 868  ? 0.2558 0.2187 0.2298 0.0035  -0.0259 -0.0116 866  GLY B C   
15169 O O   . GLY B 868  ? 0.2681 0.2275 0.2411 0.0036  -0.0267 -0.0107 866  GLY B O   
15170 N N   . ALA B 869  ? 0.2530 0.2198 0.2291 0.0029  -0.0233 -0.0127 867  ALA B N   
15171 C CA  . ALA B 869  ? 0.2576 0.2251 0.2353 0.0024  -0.0213 -0.0129 867  ALA B CA  
15172 C C   . ALA B 869  ? 0.2414 0.2086 0.2237 0.0046  -0.0218 -0.0135 867  ALA B C   
15173 O O   . ALA B 869  ? 0.2574 0.2224 0.2393 0.0045  -0.0215 -0.0132 867  ALA B O   
15174 C CB  . ALA B 869  ? 0.2411 0.2131 0.2203 0.0017  -0.0186 -0.0139 867  ALA B CB  
15175 N N   . LEU B 870  ? 0.2245 0.1939 0.2108 0.0065  -0.0227 -0.0144 868  LEU B N   
15176 C CA  . LEU B 870  ? 0.2504 0.2204 0.2414 0.0087  -0.0230 -0.0148 868  LEU B CA  
15177 C C   . LEU B 870  ? 0.2465 0.2118 0.2355 0.0099  -0.0251 -0.0138 868  LEU B C   
15178 O O   . LEU B 870  ? 0.2492 0.2135 0.2402 0.0114  -0.0249 -0.0141 868  LEU B O   
15179 C CB  . LEU B 870  ? 0.2561 0.2297 0.2518 0.0102  -0.0237 -0.0156 868  LEU B CB  
15180 C CG  . LEU B 870  ? 0.2881 0.2660 0.2870 0.0097  -0.0216 -0.0168 868  LEU B CG  
15181 C CD1 . LEU B 870  ? 0.2818 0.2627 0.2849 0.0107  -0.0229 -0.0173 868  LEU B CD1 
15182 C CD2 . LEU B 870  ? 0.2529 0.2321 0.2543 0.0102  -0.0195 -0.0173 868  LEU B CD2 
15183 N N   . HIS B 871  ? 0.2341 0.1961 0.2189 0.0093  -0.0272 -0.0127 869  HIS B N   
15184 C CA  . HIS B 871  ? 0.2716 0.2286 0.2542 0.0105  -0.0294 -0.0116 869  HIS B CA  
15185 C C   . HIS B 871  ? 0.2900 0.2425 0.2688 0.0092  -0.0287 -0.0110 869  HIS B C   
15186 O O   . HIS B 871  ? 0.2948 0.2426 0.2720 0.0106  -0.0303 -0.0104 869  HIS B O   
15187 C CB  . HIS B 871  ? 0.3161 0.2705 0.2949 0.0100  -0.0320 -0.0103 869  HIS B CB  
15188 C CG  . HIS B 871  ? 0.4094 0.3663 0.3920 0.0122  -0.0341 -0.0105 869  HIS B CG  
15189 N ND1 . HIS B 871  ? 0.3945 0.3547 0.3778 0.0115  -0.0345 -0.0109 869  HIS B ND1 
15190 C CD2 . HIS B 871  ? 0.4385 0.3952 0.4243 0.0151  -0.0360 -0.0103 869  HIS B CD2 
15191 C CE1 . HIS B 871  ? 0.4256 0.3876 0.4126 0.0135  -0.0367 -0.0109 869  HIS B CE1 
15192 N NE2 . HIS B 871  ? 0.4434 0.4038 0.4323 0.0158  -0.0375 -0.0105 869  HIS B NE2 
15193 N N   . GLU B 872  ? 0.2362 0.1902 0.2137 0.0067  -0.0264 -0.0112 870  GLU B N   
15194 C CA  . GLU B 872  ? 0.2477 0.1979 0.2218 0.0050  -0.0258 -0.0105 870  GLU B CA  
15195 C C   . GLU B 872  ? 0.2534 0.2047 0.2307 0.0061  -0.0242 -0.0118 870  GLU B C   
15196 O O   . GLU B 872  ? 0.2619 0.2100 0.2365 0.0046  -0.0237 -0.0115 870  GLU B O   
15197 C CB  . GLU B 872  ? 0.2765 0.2279 0.2470 0.0015  -0.0244 -0.0097 870  GLU B CB  
15198 C CG  . GLU B 872  ? 0.2784 0.2286 0.2450 0.0004  -0.0258 -0.0084 870  GLU B CG  
15199 C CD  . GLU B 872  ? 0.2543 0.1975 0.2162 0.0002  -0.0284 -0.0067 870  GLU B CD  
15200 O OE1 . GLU B 872  ? 0.3033 0.2423 0.2635 -0.0003 -0.0286 -0.0063 870  GLU B OE1 
15201 O OE2 . GLU B 872  ? 0.2971 0.2386 0.2566 0.0006  -0.0304 -0.0058 870  GLU B OE2 
15202 N N   . LEU B 873  ? 0.2450 0.2006 0.2279 0.0084  -0.0234 -0.0132 871  LEU B N   
15203 C CA  . LEU B 873  ? 0.2540 0.2111 0.2398 0.0094  -0.0217 -0.0144 871  LEU B CA  
15204 C C   . LEU B 873  ? 0.2535 0.2064 0.2393 0.0121  -0.0230 -0.0147 871  LEU B C   
15205 O O   . LEU B 873  ? 0.2630 0.2145 0.2494 0.0144  -0.0249 -0.0143 871  LEU B O   
15206 C CB  . LEU B 873  ? 0.2530 0.2166 0.2445 0.0105  -0.0201 -0.0156 871  LEU B CB  
15207 C CG  . LEU B 873  ? 0.2767 0.2445 0.2686 0.0084  -0.0185 -0.0158 871  LEU B CG  
15208 C CD1 . LEU B 873  ? 0.2880 0.2611 0.2854 0.0098  -0.0171 -0.0170 871  LEU B CD1 
15209 C CD2 . LEU B 873  ? 0.2506 0.2178 0.2394 0.0057  -0.0170 -0.0155 871  LEU B CD2 
15210 N N   . HIS B 874  ? 0.2605 0.2116 0.2457 0.0121  -0.0219 -0.0154 872  HIS B N   
15211 C CA  . HIS B 874  ? 0.2775 0.2243 0.2622 0.0150  -0.0228 -0.0159 872  HIS B CA  
15212 C C   . HIS B 874  ? 0.2524 0.2041 0.2424 0.0174  -0.0209 -0.0175 872  HIS B C   
15213 O O   . HIS B 874  ? 0.2552 0.2095 0.2461 0.0161  -0.0189 -0.0182 872  HIS B O   
15214 C CB  . HIS B 874  ? 0.2544 0.1946 0.2334 0.0130  -0.0231 -0.0156 872  HIS B CB  
15215 C CG  . HIS B 874  ? 0.2844 0.2188 0.2616 0.0159  -0.0241 -0.0163 872  HIS B CG  
15216 N ND1 . HIS B 874  ? 0.3529 0.2884 0.3336 0.0203  -0.0245 -0.0171 872  HIS B ND1 
15217 C CD2 . HIS B 874  ? 0.3076 0.2348 0.2797 0.0150  -0.0248 -0.0163 872  HIS B CD2 
15218 C CE1 . HIS B 874  ? 0.3251 0.2544 0.3028 0.0224  -0.0252 -0.0178 872  HIS B CE1 
15219 N NE2 . HIS B 874  ? 0.3619 0.2857 0.3342 0.0192  -0.0255 -0.0174 872  HIS B NE2 
15220 N N   . ILE B 875  ? 0.2362 0.1898 0.2299 0.0209  -0.0216 -0.0178 873  ILE B N   
15221 C CA  . ILE B 875  ? 0.2636 0.2223 0.2627 0.0234  -0.0199 -0.0191 873  ILE B CA  
15222 C C   . ILE B 875  ? 0.2403 0.1946 0.2378 0.0266  -0.0202 -0.0199 873  ILE B C   
15223 O O   . ILE B 875  ? 0.2840 0.2340 0.2797 0.0288  -0.0222 -0.0194 873  ILE B O   
15224 C CB  . ILE B 875  ? 0.3082 0.2727 0.3127 0.0252  -0.0204 -0.0188 873  ILE B CB  
15225 C CG1 . ILE B 875  ? 0.3185 0.2863 0.3237 0.0222  -0.0205 -0.0182 873  ILE B CG1 
15226 C CG2 . ILE B 875  ? 0.2867 0.2568 0.2968 0.0275  -0.0185 -0.0199 873  ILE B CG2 
15227 C CD1 . ILE B 875  ? 0.4112 0.3813 0.4189 0.0233  -0.0225 -0.0175 873  ILE B CD1 
15228 N N   . GLY B 876  ? 0.2387 0.1939 0.2368 0.0270  -0.0182 -0.0211 874  GLY B N   
15229 C CA  . GLY B 876  ? 0.2638 0.2148 0.2602 0.0304  -0.0183 -0.0221 874  GLY B CA  
15230 C C   . GLY B 876  ? 0.2501 0.2015 0.2458 0.0301  -0.0161 -0.0235 874  GLY B C   
15231 O O   . GLY B 876  ? 0.2355 0.1918 0.2334 0.0277  -0.0143 -0.0236 874  GLY B O   
15232 N N   . ARG B 877  ? 0.2494 0.1953 0.2419 0.0327  -0.0163 -0.0245 875  ARG B N   
15233 C CA  . ARG B 877  ? 0.2421 0.1873 0.2330 0.0326  -0.0145 -0.0259 875  ARG B CA  
15234 C C   . ARG B 877  ? 0.2793 0.2219 0.2662 0.0278  -0.0145 -0.0255 875  ARG B C   
15235 O O   . ARG B 877  ? 0.2874 0.2242 0.2698 0.0255  -0.0164 -0.0246 875  ARG B O   
15236 C CB  . ARG B 877  ? 0.2784 0.2168 0.2653 0.0364  -0.0151 -0.0272 875  ARG B CB  
15237 C CG  . ARG B 877  ? 0.3200 0.2597 0.3068 0.0378  -0.0129 -0.0290 875  ARG B CG  
15238 C CD  . ARG B 877  ? 0.3995 0.3325 0.3823 0.0422  -0.0134 -0.0305 875  ARG B CD  
15239 N NE  . ARG B 877  ? 0.3668 0.2893 0.3415 0.0403  -0.0151 -0.0309 875  ARG B NE  
15240 C CZ  . ARG B 877  ? 0.4746 0.3892 0.4441 0.0434  -0.0160 -0.0323 875  ARG B CZ  
15241 N NH1 . ARG B 877  ? 0.4017 0.3176 0.3732 0.0491  -0.0151 -0.0334 875  ARG B NH1 
15242 N NH2 . ARG B 877  ? 0.4604 0.3653 0.4223 0.0409  -0.0177 -0.0326 875  ARG B NH2 
15243 N N   . THR B 878  ? 0.2193 0.1664 0.2079 0.0262  -0.0124 -0.0261 876  THR B N   
15244 C CA  . THR B 878  ? 0.2608 0.2087 0.2479 0.0215  -0.0121 -0.0254 876  THR B CA  
15245 C C   . THR B 878  ? 0.2407 0.1818 0.2215 0.0194  -0.0128 -0.0258 876  THR B C   
15246 O O   . THR B 878  ? 0.2459 0.1881 0.2255 0.0155  -0.0125 -0.0252 876  THR B O   
15247 C CB  . THR B 878  ? 0.2342 0.1903 0.2262 0.0208  -0.0098 -0.0256 876  THR B CB  
15248 O OG1 . THR B 878  ? 0.2798 0.2374 0.2730 0.0235  -0.0082 -0.0270 876  THR B OG1 
15249 C CG2 . THR B 878  ? 0.2572 0.2194 0.2546 0.0214  -0.0095 -0.0248 876  THR B CG2 
15250 N N   . ASP B 879  ? 0.2661 0.2001 0.2428 0.0218  -0.0139 -0.0268 877  ASP B N   
15251 C CA  . ASP B 879  ? 0.2859 0.2125 0.2560 0.0195  -0.0149 -0.0273 877  ASP B CA  
15252 C C   . ASP B 879  ? 0.2776 0.1972 0.2428 0.0167  -0.0174 -0.0259 877  ASP B C   
15253 O O   . ASP B 879  ? 0.2837 0.1947 0.2426 0.0160  -0.0191 -0.0262 877  ASP B O   
15254 C CB  . ASP B 879  ? 0.2888 0.2104 0.2560 0.0234  -0.0147 -0.0293 877  ASP B CB  
15255 C CG  . ASP B 879  ? 0.3492 0.2661 0.3155 0.0278  -0.0161 -0.0296 877  ASP B CG  
15256 O OD1 . ASP B 879  ? 0.3806 0.3015 0.3512 0.0293  -0.0163 -0.0286 877  ASP B OD1 
15257 O OD2 . ASP B 879  ? 0.3735 0.2824 0.3345 0.0299  -0.0171 -0.0309 877  ASP B OD2 
15258 N N   . ARG B 880  ? 0.3078 0.2308 0.2753 0.0150  -0.0179 -0.0242 878  ARG B N   
15259 C CA  . ARG B 880  ? 0.3139 0.2319 0.2771 0.0116  -0.0200 -0.0224 878  ARG B CA  
15260 C C   . ARG B 880  ? 0.2854 0.2104 0.2514 0.0077  -0.0189 -0.0210 878  ARG B C   
15261 O O   . ARG B 880  ? 0.2640 0.1965 0.2355 0.0089  -0.0175 -0.0210 878  ARG B O   
15262 C CB  . ARG B 880  ? 0.3052 0.2198 0.2680 0.0142  -0.0218 -0.0216 878  ARG B CB  
15263 C CG  . ARG B 880  ? 0.3837 0.2893 0.3420 0.0176  -0.0235 -0.0226 878  ARG B CG  
15264 C CD  . ARG B 880  ? 0.4423 0.3445 0.4001 0.0201  -0.0255 -0.0216 878  ARG B CD  
15265 N NE  . ARG B 880  ? 0.6170 0.5113 0.5712 0.0242  -0.0269 -0.0228 878  ARG B NE  
15266 C CZ  . ARG B 880  ? 0.6809 0.5714 0.6344 0.0278  -0.0287 -0.0223 878  ARG B CZ  
15267 N NH1 . ARG B 880  ? 0.8222 0.7159 0.7782 0.0274  -0.0296 -0.0207 878  ARG B NH1 
15268 N NH2 . ARG B 880  ? 0.6821 0.5654 0.6322 0.0319  -0.0297 -0.0237 878  ARG B NH2 
15269 N N   . LEU B 881  ? 0.2624 0.1849 0.2245 0.0032  -0.0197 -0.0198 879  LEU B N   
15270 C CA  . LEU B 881  ? 0.2529 0.1822 0.2174 -0.0003 -0.0186 -0.0185 879  LEU B CA  
15271 C C   . LEU B 881  ? 0.2616 0.1937 0.2282 0.0003  -0.0188 -0.0173 879  LEU B C   
15272 O O   . LEU B 881  ? 0.2605 0.1999 0.2309 -0.0005 -0.0173 -0.0169 879  LEU B O   
15273 C CB  . LEU B 881  ? 0.2857 0.2116 0.2454 -0.0053 -0.0196 -0.0171 879  LEU B CB  
15274 C CG  . LEU B 881  ? 0.2940 0.2270 0.2557 -0.0092 -0.0184 -0.0156 879  LEU B CG  
15275 C CD1 . LEU B 881  ? 0.3004 0.2411 0.2666 -0.0089 -0.0161 -0.0167 879  LEU B CD1 
15276 C CD2 . LEU B 881  ? 0.2925 0.2212 0.2490 -0.0141 -0.0199 -0.0140 879  LEU B CD2 
15277 N N   . SER B 882  ? 0.2535 0.1797 0.2175 0.0019  -0.0208 -0.0168 880  SER B N   
15278 C CA  . SER B 882  ? 0.2614 0.1896 0.2267 0.0024  -0.0215 -0.0156 880  SER B CA  
15279 C C   . SER B 882  ? 0.2774 0.2120 0.2489 0.0060  -0.0203 -0.0166 880  SER B C   
15280 O O   . SER B 882  ? 0.2718 0.2088 0.2447 0.0063  -0.0208 -0.0158 880  SER B O   
15281 C CB  . SER B 882  ? 0.2899 0.2094 0.2503 0.0033  -0.0242 -0.0147 880  SER B CB  
15282 O OG  . SER B 882  ? 0.3209 0.2372 0.2821 0.0079  -0.0248 -0.0161 880  SER B OG  
15283 N N   . VAL B 883  ? 0.2586 0.1960 0.2335 0.0086  -0.0189 -0.0183 881  VAL B N   
15284 C CA  . VAL B 883  ? 0.2634 0.2068 0.2442 0.0118  -0.0179 -0.0190 881  VAL B CA  
15285 C C   . VAL B 883  ? 0.2398 0.1910 0.2244 0.0099  -0.0159 -0.0190 881  VAL B C   
15286 O O   . VAL B 883  ? 0.2833 0.2365 0.2679 0.0080  -0.0145 -0.0193 881  VAL B O   
15287 C CB  . VAL B 883  ? 0.2731 0.2163 0.2559 0.0155  -0.0171 -0.0207 881  VAL B CB  
15288 C CG1 . VAL B 883  ? 0.2602 0.2109 0.2495 0.0180  -0.0158 -0.0212 881  VAL B CG1 
15289 C CG2 . VAL B 883  ? 0.2769 0.2127 0.2562 0.0182  -0.0192 -0.0208 881  VAL B CG2 
15290 N N   . ASP B 884  ? 0.2555 0.2106 0.2431 0.0106  -0.0160 -0.0185 882  ASP B N   
15291 C CA  . ASP B 884  ? 0.2323 0.1940 0.2231 0.0092  -0.0145 -0.0185 882  ASP B CA  
15292 C C   . ASP B 884  ? 0.2660 0.2331 0.2624 0.0115  -0.0131 -0.0195 882  ASP B C   
15293 O O   . ASP B 884  ? 0.3023 0.2738 0.3009 0.0106  -0.0113 -0.0199 882  ASP B O   
15294 C CB  . ASP B 884  ? 0.2394 0.2015 0.2293 0.0082  -0.0156 -0.0173 882  ASP B CB  
15295 C CG  . ASP B 884  ? 0.2638 0.2212 0.2481 0.0054  -0.0167 -0.0160 882  ASP B CG  
15296 O OD1 . ASP B 884  ? 0.2628 0.2205 0.2452 0.0027  -0.0157 -0.0157 882  ASP B OD1 
15297 O OD2 . ASP B 884  ? 0.2588 0.2123 0.2406 0.0057  -0.0187 -0.0150 882  ASP B OD2 
15298 N N   . VAL B 885  ? 0.2522 0.2194 0.2510 0.0145  -0.0139 -0.0198 883  VAL B N   
15299 C CA  . VAL B 885  ? 0.2253 0.1980 0.2297 0.0166  -0.0128 -0.0205 883  VAL B CA  
15300 C C   . VAL B 885  ? 0.2565 0.2280 0.2620 0.0197  -0.0126 -0.0214 883  VAL B C   
15301 O O   . VAL B 885  ? 0.2462 0.2135 0.2499 0.0216  -0.0143 -0.0212 883  VAL B O   
15302 C CB  . VAL B 885  ? 0.2601 0.2354 0.2672 0.0172  -0.0141 -0.0200 883  VAL B CB  
15303 C CG1 . VAL B 885  ? 0.2495 0.2304 0.2625 0.0192  -0.0132 -0.0205 883  VAL B CG1 
15304 C CG2 . VAL B 885  ? 0.2745 0.2509 0.2801 0.0144  -0.0140 -0.0194 883  VAL B CG2 
15305 N N   . GLY B 886  ? 0.2458 0.2207 0.2539 0.0204  -0.0107 -0.0222 884  GLY B N   
15306 C CA  . GLY B 886  ? 0.2434 0.2177 0.2524 0.0235  -0.0101 -0.0232 884  GLY B CA  
15307 C C   . GLY B 886  ? 0.2102 0.1900 0.2250 0.0261  -0.0097 -0.0232 884  GLY B C   
15308 O O   . GLY B 886  ? 0.2115 0.1946 0.2292 0.0256  -0.0105 -0.0224 884  GLY B O   
15309 N N   . PRO B 887  ? 0.2034 0.1842 0.2196 0.0290  -0.0086 -0.0240 885  PRO B N   
15310 C CA  . PRO B 887  ? 0.1838 0.1705 0.2058 0.0316  -0.0081 -0.0239 885  PRO B CA  
15311 C C   . PRO B 887  ? 0.1909 0.1843 0.2174 0.0301  -0.0063 -0.0237 885  PRO B C   
15312 O O   . PRO B 887  ? 0.1820 0.1757 0.2072 0.0279  -0.0050 -0.0239 885  PRO B O   
15313 C CB  . PRO B 887  ? 0.2003 0.1853 0.2213 0.0352  -0.0072 -0.0250 885  PRO B CB  
15314 C CG  . PRO B 887  ? 0.1948 0.1756 0.2109 0.0334  -0.0062 -0.0259 885  PRO B CG  
15315 C CD  . PRO B 887  ? 0.2012 0.1777 0.2135 0.0300  -0.0078 -0.0252 885  PRO B CD  
15316 N N   . VAL B 888  ? 0.2034 0.2026 0.2354 0.0316  -0.0062 -0.0232 886  VAL B N   
15317 C CA  . VAL B 888  ? 0.1757 0.1811 0.2121 0.0309  -0.0043 -0.0230 886  VAL B CA  
15318 C C   . VAL B 888  ? 0.1930 0.2000 0.2299 0.0334  -0.0021 -0.0238 886  VAL B C   
15319 O O   . VAL B 888  ? 0.2006 0.2050 0.2359 0.0364  -0.0023 -0.0245 886  VAL B O   
15320 C CB  . VAL B 888  ? 0.2284 0.2395 0.2704 0.0308  -0.0052 -0.0219 886  VAL B CB  
15321 C CG1 . VAL B 888  ? 0.2086 0.2177 0.2493 0.0281  -0.0073 -0.0213 886  VAL B CG1 
15322 C CG2 . VAL B 888  ? 0.2601 0.2734 0.3051 0.0343  -0.0060 -0.0217 886  VAL B CG2 
15323 N N   . ILE B 889  ? 0.1941 0.2050 0.2329 0.0322  -0.0001 -0.0238 887  ILE B N   
15324 C CA  . ILE B 889  ? 0.1899 0.2007 0.2271 0.0339  0.0021  -0.0248 887  ILE B CA  
15325 C C   . ILE B 889  ? 0.1917 0.2063 0.2322 0.0378  0.0030  -0.0249 887  ILE B C   
15326 O O   . ILE B 889  ? 0.1817 0.1939 0.2193 0.0403  0.0041  -0.0261 887  ILE B O   
15327 C CB  . ILE B 889  ? 0.1902 0.2042 0.2284 0.0315  0.0039  -0.0245 887  ILE B CB  
15328 C CG1 . ILE B 889  ? 0.1804 0.1935 0.2158 0.0328  0.0060  -0.0255 887  ILE B CG1 
15329 C CG2 . ILE B 889  ? 0.2126 0.2337 0.2569 0.0309  0.0045  -0.0232 887  ILE B CG2 
15330 C CD1 . ILE B 889  ? 0.2000 0.2056 0.2289 0.0329  0.0052  -0.0268 887  ILE B CD1 
15331 N N   . THR B 890  ? 0.1814 0.2021 0.2277 0.0383  0.0027  -0.0238 888  THR B N   
15332 C CA  . THR B 890  ? 0.1908 0.2167 0.2411 0.0420  0.0038  -0.0238 888  THR B CA  
15333 C C   . THR B 890  ? 0.1822 0.2118 0.2373 0.0429  0.0018  -0.0226 888  THR B C   
15334 O O   . THR B 890  ? 0.1923 0.2215 0.2483 0.0401  -0.0001 -0.0218 888  THR B O   
15335 C CB  . THR B 890  ? 0.1872 0.2202 0.2414 0.0416  0.0065  -0.0232 888  THR B CB  
15336 O OG1 . THR B 890  ? 0.2024 0.2394 0.2605 0.0381  0.0059  -0.0217 888  THR B OG1 
15337 C CG2 . THR B 890  ? 0.1949 0.2250 0.2446 0.0411  0.0085  -0.0243 888  THR B CG2 
15338 N N   . SER B 891  ? 0.1901 0.2237 0.2484 0.0468  0.0024  -0.0226 889  SER B N   
15339 C CA  A SER B 891  ? 0.1936 0.2324 0.2575 0.0478  0.0007  -0.0213 889  SER B CA  
15340 C CA  B SER B 891  ? 0.1936 0.2322 0.2574 0.0477  0.0006  -0.0213 889  SER B CA  
15341 C C   . SER B 891  ? 0.2046 0.2507 0.2742 0.0445  0.0009  -0.0197 889  SER B C   
15342 O O   . SER B 891  ? 0.2200 0.2681 0.2927 0.0430  -0.0014 -0.0186 889  SER B O   
15343 C CB  A SER B 891  ? 0.2256 0.2686 0.2924 0.0530  0.0017  -0.0216 889  SER B CB  
15344 C CB  B SER B 891  ? 0.2260 0.2684 0.2925 0.0529  0.0014  -0.0216 889  SER B CB  
15345 O OG  A SER B 891  ? 0.2342 0.2697 0.2957 0.0563  0.0008  -0.0230 889  SER B OG  
15346 O OG  B SER B 891  ? 0.2482 0.2976 0.3182 0.0539  0.0045  -0.0214 889  SER B OG  
15347 N N   . GLU B 892  ? 0.1758 0.2256 0.2467 0.0433  0.0035  -0.0196 890  GLU B N   
15348 C CA  . GLU B 892  ? 0.1947 0.2508 0.2706 0.0398  0.0037  -0.0180 890  GLU B CA  
15349 C C   . GLU B 892  ? 0.2289 0.2804 0.3024 0.0357  0.0017  -0.0177 890  GLU B C   
15350 O O   . GLU B 892  ? 0.1978 0.2524 0.2750 0.0334  -0.0001 -0.0165 890  GLU B O   
15351 C CB  . GLU B 892  ? 0.2651 0.3248 0.3416 0.0393  0.0070  -0.0179 890  GLU B CB  
15352 C CG  . GLU B 892  ? 0.3322 0.3989 0.4126 0.0430  0.0093  -0.0177 890  GLU B CG  
15353 C CD  . GLU B 892  ? 0.3897 0.4522 0.4654 0.0475  0.0106  -0.0196 890  GLU B CD  
15354 O OE1 . GLU B 892  ? 0.3256 0.3794 0.3950 0.0477  0.0096  -0.0211 890  GLU B OE1 
15355 O OE2 . GLU B 892  ? 0.4757 0.5440 0.5542 0.0509  0.0127  -0.0196 890  GLU B OE2 
15356 N N   . ALA B 893  ? 0.1928 0.2371 0.2601 0.0347  0.0018  -0.0189 891  ALA B N   
15357 C CA  . ALA B 893  ? 0.1915 0.2313 0.2561 0.0312  0.0000  -0.0188 891  ALA B CA  
15358 C C   . ALA B 893  ? 0.2059 0.2440 0.2708 0.0314  -0.0030 -0.0185 891  ALA B C   
15359 O O   . ALA B 893  ? 0.2106 0.2495 0.2769 0.0288  -0.0047 -0.0177 891  ALA B O   
15360 C CB  . ALA B 893  ? 0.2064 0.2395 0.2646 0.0306  0.0008  -0.0201 891  ALA B CB  
15361 N N   . LYS B 894  ? 0.1888 0.2242 0.2519 0.0345  -0.0038 -0.0191 892  LYS B N   
15362 C CA  . LYS B 894  ? 0.1882 0.2218 0.2513 0.0350  -0.0068 -0.0187 892  LYS B CA  
15363 C C   . LYS B 894  ? 0.2087 0.2495 0.2784 0.0345  -0.0081 -0.0172 892  LYS B C   
15364 O O   . LYS B 894  ? 0.2197 0.2597 0.2895 0.0323  -0.0105 -0.0166 892  LYS B O   
15365 C CB  . LYS B 894  ? 0.2048 0.2350 0.2655 0.0390  -0.0072 -0.0194 892  LYS B CB  
15366 C CG  . LYS B 894  ? 0.2261 0.2544 0.2867 0.0400  -0.0103 -0.0188 892  LYS B CG  
15367 C CD  . LYS B 894  ? 0.2329 0.2559 0.2897 0.0439  -0.0107 -0.0197 892  LYS B CD  
15368 C CE  . LYS B 894  ? 0.2981 0.3188 0.3545 0.0451  -0.0139 -0.0190 892  LYS B CE  
15369 N NZ  . LYS B 894  ? 0.4193 0.4483 0.4829 0.0464  -0.0149 -0.0177 892  LYS B NZ  
15370 N N   . ASP B 895  ? 0.2167 0.2647 0.2917 0.0363  -0.0065 -0.0166 893  ASP B N   
15371 C CA  . ASP B 895  ? 0.2105 0.2662 0.2924 0.0355  -0.0077 -0.0150 893  ASP B CA  
15372 C C   . ASP B 895  ? 0.1966 0.2532 0.2794 0.0308  -0.0083 -0.0142 893  ASP B C   
15373 O O   . ASP B 895  ? 0.2201 0.2792 0.3059 0.0289  -0.0108 -0.0132 893  ASP B O   
15374 C CB  . ASP B 895  ? 0.2354 0.2993 0.3227 0.0380  -0.0053 -0.0144 893  ASP B CB  
15375 C CG  . ASP B 895  ? 0.2400 0.3041 0.3273 0.0432  -0.0050 -0.0151 893  ASP B CG  
15376 O OD1 . ASP B 895  ? 0.2682 0.3271 0.3525 0.0448  -0.0074 -0.0155 893  ASP B OD1 
15377 O OD2 . ASP B 895  ? 0.2950 0.3643 0.3851 0.0459  -0.0025 -0.0151 893  ASP B OD2 
15378 N N   . ASN B 896  ? 0.1989 0.2535 0.2792 0.0289  -0.0062 -0.0147 894  ASN B N   
15379 C CA  . ASN B 896  ? 0.1818 0.2364 0.2624 0.0247  -0.0067 -0.0141 894  ASN B CA  
15380 C C   . ASN B 896  ? 0.2019 0.2504 0.2785 0.0227  -0.0094 -0.0145 894  ASN B C   
15381 O O   . ASN B 896  ? 0.1885 0.2383 0.2670 0.0202  -0.0115 -0.0137 894  ASN B O   
15382 C CB  . ASN B 896  ? 0.2123 0.2653 0.2903 0.0238  -0.0038 -0.0147 894  ASN B CB  
15383 C CG  . ASN B 896  ? 0.3084 0.3605 0.3860 0.0199  -0.0041 -0.0141 894  ASN B CG  
15384 O OD1 . ASN B 896  ? 0.3274 0.3751 0.4023 0.0179  -0.0061 -0.0144 894  ASN B OD1 
15385 N ND2 . ASN B 896  ? 0.3496 0.4055 0.4295 0.0189  -0.0020 -0.0134 894  ASN B ND2 
15386 N N   . ILE B 897  ? 0.1848 0.2269 0.2558 0.0238  -0.0095 -0.0158 895  ILE B N   
15387 C CA  . ILE B 897  ? 0.1963 0.2326 0.2630 0.0223  -0.0118 -0.0162 895  ILE B CA  
15388 C C   . ILE B 897  ? 0.2055 0.2436 0.2746 0.0227  -0.0149 -0.0154 895  ILE B C   
15389 O O   . ILE B 897  ? 0.2049 0.2419 0.2734 0.0203  -0.0170 -0.0150 895  ILE B O   
15390 C CB  . ILE B 897  ? 0.1935 0.2232 0.2540 0.0235  -0.0112 -0.0174 895  ILE B CB  
15391 C CG1 . ILE B 897  ? 0.1743 0.2027 0.2326 0.0226  -0.0085 -0.0181 895  ILE B CG1 
15392 C CG2 . ILE B 897  ? 0.2010 0.2254 0.2571 0.0221  -0.0135 -0.0176 895  ILE B CG2 
15393 C CD1 . ILE B 897  ? 0.1929 0.2166 0.2466 0.0244  -0.0075 -0.0191 895  ILE B CD1 
15394 N N   . GLU B 898  ? 0.1990 0.2395 0.2704 0.0259  -0.0151 -0.0151 896  GLU B N   
15395 C CA  . GLU B 898  ? 0.1898 0.2320 0.2634 0.0267  -0.0182 -0.0143 896  GLU B CA  
15396 C C   . GLU B 898  ? 0.2036 0.2525 0.2832 0.0246  -0.0195 -0.0129 896  GLU B C   
15397 O O   . GLU B 898  ? 0.1989 0.2479 0.2791 0.0234  -0.0226 -0.0123 896  GLU B O   
15398 C CB  . GLU B 898  ? 0.2017 0.2451 0.2766 0.0311  -0.0181 -0.0143 896  GLU B CB  
15399 C CG  . GLU B 898  ? 0.2424 0.2777 0.3105 0.0328  -0.0178 -0.0155 896  GLU B CG  
15400 C CD  . GLU B 898  ? 0.3065 0.3415 0.3748 0.0373  -0.0179 -0.0156 896  GLU B CD  
15401 O OE1 . GLU B 898  ? 0.2889 0.3307 0.3629 0.0397  -0.0171 -0.0151 896  GLU B OE1 
15402 O OE2 . GLU B 898  ? 0.3857 0.4137 0.4485 0.0384  -0.0189 -0.0162 896  GLU B OE2 
15403 N N   . LYS B 899  ? 0.2023 0.2569 0.2863 0.0239  -0.0173 -0.0124 897  LYS B N   
15404 C CA  . LYS B 899  ? 0.2084 0.2692 0.2980 0.0212  -0.0186 -0.0109 897  LYS B CA  
15405 C C   . LYS B 899  ? 0.2070 0.2631 0.2932 0.0173  -0.0206 -0.0111 897  LYS B C   
15406 O O   . LYS B 899  ? 0.2197 0.2779 0.3082 0.0153  -0.0235 -0.0102 897  LYS B O   
15407 C CB  . LYS B 899  ? 0.2211 0.2879 0.3149 0.0208  -0.0156 -0.0102 897  LYS B CB  
15408 C CG  . LYS B 899  ? 0.2535 0.3264 0.3528 0.0173  -0.0169 -0.0085 897  LYS B CG  
15409 C CD  . LYS B 899  ? 0.2816 0.3622 0.3862 0.0174  -0.0140 -0.0073 897  LYS B CD  
15410 C CE  . LYS B 899  ? 0.3525 0.4299 0.4541 0.0153  -0.0116 -0.0077 897  LYS B CE  
15411 N NZ  . LYS B 899  ? 0.3110 0.3962 0.4183 0.0134  -0.0100 -0.0059 897  LYS B NZ  
15412 N N   . HIS B 900  ? 0.1861 0.2359 0.2667 0.0162  -0.0192 -0.0123 898  HIS B N   
15413 C CA  . HIS B 900  ? 0.1878 0.2327 0.2645 0.0130  -0.0209 -0.0127 898  HIS B CA  
15414 C C   . HIS B 900  ? 0.2122 0.2531 0.2856 0.0132  -0.0239 -0.0131 898  HIS B C   
15415 O O   . HIS B 900  ? 0.2128 0.2530 0.2859 0.0108  -0.0266 -0.0127 898  HIS B O   
15416 C CB  . HIS B 900  ? 0.1771 0.2165 0.2485 0.0125  -0.0185 -0.0140 898  HIS B CB  
15417 C CG  . HIS B 900  ? 0.1920 0.2256 0.2585 0.0101  -0.0200 -0.0147 898  HIS B CG  
15418 N ND1 . HIS B 900  ? 0.2274 0.2611 0.2946 0.0071  -0.0212 -0.0143 898  HIS B ND1 
15419 C CD2 . HIS B 900  ? 0.2108 0.2384 0.2713 0.0104  -0.0206 -0.0158 898  HIS B CD2 
15420 C CE1 . HIS B 900  ? 0.2425 0.2702 0.3041 0.0060  -0.0223 -0.0154 898  HIS B CE1 
15421 N NE2 . HIS B 900  ? 0.2056 0.2299 0.2632 0.0079  -0.0218 -0.0162 898  HIS B NE2 
15422 N N   . ILE B 901  ? 0.1926 0.2305 0.2629 0.0159  -0.0236 -0.0137 899  ILE B N   
15423 C CA  . ILE B 901  ? 0.1811 0.2148 0.2477 0.0163  -0.0264 -0.0139 899  ILE B CA  
15424 C C   . ILE B 901  ? 0.2137 0.2522 0.2850 0.0161  -0.0295 -0.0126 899  ILE B C   
15425 O O   . ILE B 901  ? 0.2320 0.2684 0.3013 0.0141  -0.0324 -0.0125 899  ILE B O   
15426 C CB  . ILE B 901  ? 0.1975 0.2276 0.2606 0.0193  -0.0255 -0.0144 899  ILE B CB  
15427 C CG1 . ILE B 901  ? 0.1778 0.2026 0.2356 0.0188  -0.0230 -0.0156 899  ILE B CG1 
15428 C CG2 . ILE B 901  ? 0.2182 0.2449 0.2783 0.0199  -0.0286 -0.0142 899  ILE B CG2 
15429 C CD1 . ILE B 901  ? 0.2232 0.2446 0.2779 0.0215  -0.0219 -0.0162 899  ILE B CD1 
15430 N N   . GLU B 902  ? 0.1948 0.2401 0.2723 0.0181  -0.0290 -0.0116 900  GLU B N   
15431 C CA  . GLU B 902  ? 0.2276 0.2785 0.3103 0.0182  -0.0320 -0.0102 900  GLU B CA  
15432 C C   . GLU B 902  ? 0.2350 0.2890 0.3206 0.0141  -0.0335 -0.0094 900  GLU B C   
15433 O O   . GLU B 902  ? 0.2426 0.2983 0.3298 0.0128  -0.0370 -0.0086 900  GLU B O   
15434 C CB  . GLU B 902  ? 0.2465 0.3046 0.3354 0.0217  -0.0307 -0.0093 900  GLU B CB  
15435 C CG  . GLU B 902  ? 0.2999 0.3544 0.3857 0.0259  -0.0303 -0.0100 900  GLU B CG  
15436 C CD  . GLU B 902  ? 0.3556 0.4043 0.4365 0.0259  -0.0336 -0.0101 900  GLU B CD  
15437 O OE1 . GLU B 902  ? 0.3453 0.3971 0.4290 0.0250  -0.0369 -0.0090 900  GLU B OE1 
15438 O OE2 . GLU B 902  ? 0.4036 0.4449 0.4780 0.0266  -0.0330 -0.0111 900  GLU B OE2 
15439 N N   . ARG B 903  ? 0.2371 0.2915 0.3232 0.0120  -0.0313 -0.0096 901  ARG B N   
15440 C CA  . ARG B 903  ? 0.2451 0.3010 0.3329 0.0079  -0.0329 -0.0089 901  ARG B CA  
15441 C C   . ARG B 903  ? 0.2789 0.3273 0.3603 0.0056  -0.0355 -0.0099 901  ARG B C   
15442 O O   . ARG B 903  ? 0.2649 0.3141 0.3473 0.0030  -0.0387 -0.0093 901  ARG B O   
15443 C CB  . ARG B 903  ? 0.2673 0.3243 0.3563 0.0063  -0.0299 -0.0089 901  ARG B CB  
15444 C CG  . ARG B 903  ? 0.3379 0.3956 0.4283 0.0019  -0.0317 -0.0081 901  ARG B CG  
15445 C CD  . ARG B 903  ? 0.3793 0.4388 0.4715 0.0004  -0.0288 -0.0077 901  ARG B CD  
15446 N NE  . ARG B 903  ? 0.4794 0.5389 0.5727 -0.0040 -0.0310 -0.0068 901  ARG B NE  
15447 C CZ  . ARG B 903  ? 0.4902 0.5423 0.5778 -0.0063 -0.0321 -0.0079 901  ARG B CZ  
15448 N NH1 . ARG B 903  ? 0.4195 0.4643 0.5005 -0.0048 -0.0308 -0.0097 901  ARG B NH1 
15449 N NH2 . ARG B 903  ? 0.4544 0.5062 0.5430 -0.0103 -0.0345 -0.0070 901  ARG B NH2 
15450 N N   . MET B 904  ? 0.2370 0.2783 0.3116 0.0066  -0.0341 -0.0115 902  MET B N   
15451 C CA  . MET B 904  ? 0.2434 0.2777 0.3114 0.0050  -0.0362 -0.0125 902  MET B CA  
15452 C C   . MET B 904  ? 0.2771 0.3115 0.3448 0.0057  -0.0397 -0.0120 902  MET B C   
15453 O O   . MET B 904  ? 0.2638 0.2961 0.3293 0.0034  -0.0428 -0.0120 902  MET B O   
15454 C CB  . MET B 904  ? 0.2603 0.2882 0.3218 0.0061  -0.0338 -0.0140 902  MET B CB  
15455 C CG  . MET B 904  ? 0.2442 0.2716 0.3056 0.0054  -0.0306 -0.0146 902  MET B CG  
15456 S SD  . MET B 904  ? 0.3475 0.3722 0.4072 0.0015  -0.0319 -0.0149 902  MET B SD  
15457 C CE  . MET B 904  ? 0.3215 0.3539 0.3894 0.0001  -0.0312 -0.0132 902  MET B CE  
15458 N N   . ARG B 905  ? 0.2414 0.2779 0.3107 0.0090  -0.0394 -0.0115 903  ARG B N   
15459 C CA  . ARG B 905  ? 0.2840 0.3204 0.3527 0.0099  -0.0429 -0.0109 903  ARG B CA  
15460 C C   . ARG B 905  ? 0.2771 0.3197 0.3517 0.0080  -0.0460 -0.0095 903  ARG B C   
15461 O O   . ARG B 905  ? 0.2876 0.3284 0.3601 0.0066  -0.0496 -0.0092 903  ARG B O   
15462 C CB  . ARG B 905  ? 0.2805 0.3179 0.3502 0.0140  -0.0420 -0.0105 903  ARG B CB  
15463 C CG  . ARG B 905  ? 0.3153 0.3498 0.3818 0.0153  -0.0452 -0.0102 903  ARG B CG  
15464 C CD  . ARG B 905  ? 0.3598 0.3967 0.4290 0.0196  -0.0447 -0.0095 903  ARG B CD  
15465 N NE  . ARG B 905  ? 0.3466 0.3812 0.4142 0.0216  -0.0409 -0.0104 903  ARG B NE  
15466 C CZ  . ARG B 905  ? 0.3264 0.3538 0.3872 0.0223  -0.0399 -0.0113 903  ARG B CZ  
15467 N NH1 . ARG B 905  ? 0.3363 0.3579 0.3911 0.0211  -0.0420 -0.0115 903  ARG B NH1 
15468 N NH2 . ARG B 905  ? 0.3474 0.3735 0.4075 0.0241  -0.0367 -0.0120 903  ARG B NH2 
15469 N N   . GLY B 906  ? 0.2459 0.2959 0.3277 0.0078  -0.0447 -0.0084 904  GLY B N   
15470 C CA  . GLY B 906  ? 0.2912 0.3482 0.3793 0.0059  -0.0476 -0.0068 904  GLY B CA  
15471 C C   . GLY B 906  ? 0.2993 0.3536 0.3854 0.0012  -0.0500 -0.0070 904  GLY B C   
15472 O O   . GLY B 906  ? 0.3529 0.4107 0.4420 -0.0009 -0.0537 -0.0058 904  GLY B O   
15473 N N   . LEU B 907  ? 0.3083 0.3564 0.3892 -0.0005 -0.0481 -0.0084 905  LEU B N   
15474 C CA  . LEU B 907  ? 0.3434 0.3870 0.4207 -0.0045 -0.0503 -0.0090 905  LEU B CA  
15475 C C   . LEU B 907  ? 0.3091 0.3451 0.3785 -0.0047 -0.0528 -0.0102 905  LEU B C   
15476 O O   . LEU B 907  ? 0.3378 0.3686 0.4027 -0.0076 -0.0545 -0.0111 905  LEU B O   
15477 C CB  . LEU B 907  ? 0.3483 0.3884 0.4234 -0.0059 -0.0473 -0.0099 905  LEU B CB  
15478 C CG  . LEU B 907  ? 0.3578 0.4048 0.4399 -0.0069 -0.0452 -0.0085 905  LEU B CG  
15479 C CD1 . LEU B 907  ? 0.4183 0.4608 0.4972 -0.0081 -0.0424 -0.0094 905  LEU B CD1 
15480 C CD2 . LEU B 907  ? 0.3572 0.4099 0.4450 -0.0103 -0.0485 -0.0067 905  LEU B CD2 
15481 N N   . GLY B 908  ? 0.3034 0.3382 0.3707 -0.0016 -0.0530 -0.0104 906  GLY B N   
15482 C CA  . GLY B 908  ? 0.3294 0.3579 0.3895 -0.0017 -0.0555 -0.0112 906  GLY B CA  
15483 C C   . GLY B 908  ? 0.3649 0.3854 0.4169 -0.0010 -0.0531 -0.0130 906  GLY B C   
15484 O O   . GLY B 908  ? 0.3594 0.3745 0.4049 -0.0013 -0.0550 -0.0138 906  GLY B O   
15485 N N   . ARG B 909  ? 0.2914 0.3114 0.3435 0.0000  -0.0491 -0.0137 907  ARG B N   
15486 C CA  . ARG B 909  ? 0.2712 0.2846 0.3162 0.0007  -0.0468 -0.0152 907  ARG B CA  
15487 C C   . ARG B 909  ? 0.3147 0.3265 0.3570 0.0036  -0.0464 -0.0151 907  ARG B C   
15488 O O   . ARG B 909  ? 0.3080 0.3239 0.3547 0.0058  -0.0462 -0.0140 907  ARG B O   
15489 C CB  . ARG B 909  ? 0.2773 0.2910 0.3235 0.0010  -0.0428 -0.0158 907  ARG B CB  
15490 C CG  . ARG B 909  ? 0.3447 0.3599 0.3937 -0.0017 -0.0429 -0.0157 907  ARG B CG  
15491 C CD  . ARG B 909  ? 0.4491 0.4579 0.4918 -0.0040 -0.0444 -0.0171 907  ARG B CD  
15492 N NE  . ARG B 909  ? 0.5020 0.5112 0.5468 -0.0067 -0.0447 -0.0170 907  ARG B NE  
15493 C CZ  . ARG B 909  ? 0.5557 0.5663 0.6028 -0.0095 -0.0481 -0.0163 907  ARG B CZ  
15494 N NH1 . ARG B 909  ? 0.5444 0.5564 0.5920 -0.0099 -0.0515 -0.0156 907  ARG B NH1 
15495 N NH2 . ARG B 909  ? 0.5867 0.5969 0.6352 -0.0120 -0.0481 -0.0161 907  ARG B NH2 
15496 N N   . LYS B 910  ? 0.2516 0.2572 0.2863 0.0036  -0.0462 -0.0161 908  LYS B N   
15497 C CA  . LYS B 910  ? 0.2670 0.2703 0.2985 0.0058  -0.0458 -0.0159 908  LYS B CA  
15498 C C   . LYS B 910  ? 0.2802 0.2843 0.3132 0.0077  -0.0420 -0.0160 908  LYS B C   
15499 O O   . LYS B 910  ? 0.2732 0.2755 0.3043 0.0071  -0.0392 -0.0170 908  LYS B O   
15500 C CB  . LYS B 910  ? 0.3173 0.3142 0.3402 0.0050  -0.0463 -0.0169 908  LYS B CB  
15501 C CG  . LYS B 910  ? 0.3652 0.3594 0.3843 0.0068  -0.0459 -0.0163 908  LYS B CG  
15502 C CD  . LYS B 910  ? 0.4099 0.3985 0.4207 0.0059  -0.0466 -0.0170 908  LYS B CD  
15503 C CE  . LYS B 910  ? 0.4834 0.4696 0.4908 0.0074  -0.0471 -0.0159 908  LYS B CE  
15504 N NZ  . LYS B 910  ? 0.5070 0.4881 0.5061 0.0066  -0.0466 -0.0164 908  LYS B NZ  
15505 N N   . VAL B 911  ? 0.2684 0.2750 0.3046 0.0101  -0.0420 -0.0150 909  VAL B N   
15506 C CA  . VAL B 911  ? 0.2549 0.2621 0.2925 0.0121  -0.0388 -0.0151 909  VAL B CA  
15507 C C   . VAL B 911  ? 0.2903 0.2936 0.3237 0.0140  -0.0392 -0.0147 909  VAL B C   
15508 O O   . VAL B 911  ? 0.2707 0.2745 0.3047 0.0151  -0.0420 -0.0138 909  VAL B O   
15509 C CB  . VAL B 911  ? 0.2463 0.2601 0.2918 0.0136  -0.0381 -0.0143 909  VAL B CB  
15510 C CG1 . VAL B 911  ? 0.2274 0.2410 0.2734 0.0160  -0.0350 -0.0146 909  VAL B CG1 
15511 C CG2 . VAL B 911  ? 0.2412 0.2588 0.2908 0.0113  -0.0377 -0.0144 909  VAL B CG2 
15512 N N   . GLU B 912  ? 0.2410 0.2406 0.2703 0.0142  -0.0367 -0.0154 910  GLU B N   
15513 C CA  . GLU B 912  ? 0.2633 0.2587 0.2882 0.0156  -0.0370 -0.0149 910  GLU B CA  
15514 C C   . GLU B 912  ? 0.2998 0.2947 0.3252 0.0170  -0.0340 -0.0153 910  GLU B C   
15515 O O   . GLU B 912  ? 0.2600 0.2553 0.2853 0.0160  -0.0313 -0.0161 910  GLU B O   
15516 C CB  . GLU B 912  ? 0.3132 0.3034 0.3306 0.0138  -0.0373 -0.0152 910  GLU B CB  
15517 C CG  . GLU B 912  ? 0.3524 0.3421 0.3680 0.0123  -0.0403 -0.0151 910  GLU B CG  
15518 C CD  . GLU B 912  ? 0.4543 0.4393 0.4623 0.0106  -0.0400 -0.0156 910  GLU B CD  
15519 O OE1 . GLU B 912  ? 0.4882 0.4697 0.4917 0.0110  -0.0404 -0.0149 910  GLU B OE1 
15520 O OE2 . GLU B 912  ? 0.5540 0.5389 0.5605 0.0090  -0.0392 -0.0167 910  GLU B OE2 
15521 N N   . GLN B 913  ? 0.2797 0.2735 0.3054 0.0194  -0.0345 -0.0146 911  GLN B N   
15522 C CA  . GLN B 913  ? 0.2947 0.2869 0.3198 0.0208  -0.0321 -0.0150 911  GLN B CA  
15523 C C   . GLN B 913  ? 0.3688 0.3549 0.3883 0.0215  -0.0330 -0.0144 911  GLN B C   
15524 O O   . GLN B 913  ? 0.3276 0.3118 0.3454 0.0221  -0.0358 -0.0135 911  GLN B O   
15525 C CB  . GLN B 913  ? 0.2900 0.2866 0.3213 0.0236  -0.0314 -0.0149 911  GLN B CB  
15526 C CG  . GLN B 913  ? 0.2883 0.2913 0.3256 0.0227  -0.0306 -0.0152 911  GLN B CG  
15527 C CD  . GLN B 913  ? 0.3330 0.3412 0.3764 0.0255  -0.0298 -0.0149 911  GLN B CD  
15528 O OE1 . GLN B 913  ? 0.3903 0.4005 0.4364 0.0277  -0.0317 -0.0141 911  GLN B OE1 
15529 N NE2 . GLN B 913  ? 0.2795 0.2901 0.3251 0.0254  -0.0268 -0.0156 911  GLN B NE2 
15530 N N   . ILE B 914  ? 0.3529 0.3358 0.3693 0.0212  -0.0309 -0.0149 912  ILE B N   
15531 C CA  . ILE B 914  ? 0.4759 0.4528 0.4873 0.0219  -0.0318 -0.0142 912  ILE B CA  
15532 C C   . ILE B 914  ? 0.5237 0.5005 0.5378 0.0255  -0.0321 -0.0141 912  ILE B C   
15533 O O   . ILE B 914  ? 0.4754 0.4573 0.4953 0.0272  -0.0312 -0.0146 912  ILE B O   
15534 C CB  . ILE B 914  ? 0.4678 0.4411 0.4743 0.0198  -0.0297 -0.0145 912  ILE B CB  
15535 C CG1 . ILE B 914  ? 0.3150 0.2907 0.3243 0.0200  -0.0268 -0.0157 912  ILE B CG1 
15536 C CG2 . ILE B 914  ? 0.3998 0.3729 0.4029 0.0167  -0.0297 -0.0145 912  ILE B CG2 
15537 C CD1 . ILE B 914  ? 0.4276 0.3997 0.4322 0.0180  -0.0250 -0.0159 912  ILE B CD1 
15538 N N   . GLY B 915  ? 0.6482 0.6190 0.6578 0.0266  -0.0335 -0.0135 913  GLY B N   
15539 C CA  . GLY B 915  ? 0.6332 0.6029 0.6445 0.0304  -0.0340 -0.0135 913  GLY B CA  
15540 C C   . GLY B 915  ? 0.6415 0.6096 0.6523 0.0312  -0.0314 -0.0146 913  GLY B C   
15541 O O   . GLY B 915  ? 0.5838 0.5502 0.5918 0.0285  -0.0296 -0.0151 913  GLY B O   
15542 N N   . LEU B 916  ? 0.5981 0.5668 0.6117 0.0350  -0.0314 -0.0150 914  LEU B N   
15543 C CA  . LEU B 916  ? 0.5612 0.5279 0.5739 0.0365  -0.0292 -0.0161 914  LEU B CA  
15544 C C   . LEU B 916  ? 0.5774 0.5370 0.5861 0.0395  -0.0309 -0.0159 914  LEU B C   
15545 O O   . LEU B 916  ? 0.5500 0.5097 0.5602 0.0425  -0.0331 -0.0152 914  LEU B O   
15546 C CB  . LEU B 916  ? 0.5483 0.5225 0.5679 0.0387  -0.0272 -0.0170 914  LEU B CB  
15547 C CG  . LEU B 916  ? 0.4820 0.4628 0.5056 0.0361  -0.0250 -0.0175 914  LEU B CG  
15548 C CD1 . LEU B 916  ? 0.4120 0.3993 0.4417 0.0387  -0.0231 -0.0181 914  LEU B CD1 
15549 C CD2 . LEU B 916  ? 0.4116 0.3892 0.4309 0.0327  -0.0232 -0.0181 914  LEU B CD2 
15550 N N   . ALA B 917  ? 0.5474 0.5006 0.5509 0.0388  -0.0299 -0.0166 915  ALA B N   
15551 C CA  . ALA B 917  ? 0.6257 0.5712 0.6249 0.0418  -0.0313 -0.0167 915  ALA B CA  
15552 C C   . ALA B 917  ? 0.6121 0.5610 0.6159 0.0470  -0.0305 -0.0177 915  ALA B C   
15553 O O   . ALA B 917  ? 0.5559 0.5119 0.5649 0.0475  -0.0281 -0.0187 915  ALA B O   
15554 C CB  . ALA B 917  ? 0.5655 0.5038 0.5583 0.0395  -0.0305 -0.0172 915  ALA B CB  
15555 N N   . SER B 918  ? 0.6084 0.5522 0.6101 0.0510  -0.0326 -0.0175 916  SER B N   
15556 C CA  . SER B 918  ? 0.6031 0.5499 0.6087 0.0564  -0.0317 -0.0185 916  SER B CA  
15557 C C   . SER B 918  ? 0.5774 0.5230 0.5816 0.0570  -0.0288 -0.0204 916  SER B C   
15558 O O   . SER B 918  ? 0.5306 0.4824 0.5398 0.0601  -0.0268 -0.0214 916  SER B O   
15559 C CB  . SER B 918  ? 0.6298 0.5697 0.6320 0.0608  -0.0346 -0.0180 916  SER B CB  
15560 O OG  . SER B 918  ? 0.6506 0.5792 0.6444 0.0598  -0.0354 -0.0183 916  SER B OG  
15561 N N   . GLU B 919  ? 0.5875 0.5256 0.5851 0.0537  -0.0285 -0.0208 917  GLU B N   
15562 C CA  . GLU B 919  ? 0.5517 0.4883 0.5474 0.0536  -0.0260 -0.0226 917  GLU B CA  
15563 C C   . GLU B 919  ? 0.5126 0.4590 0.5144 0.0523  -0.0230 -0.0232 917  GLU B C   
15564 O O   . GLU B 919  ? 0.5205 0.4673 0.5219 0.0532  -0.0207 -0.0247 917  GLU B O   
15565 C CB  . GLU B 919  ? 0.5031 0.4309 0.4911 0.0493  -0.0266 -0.0225 917  GLU B CB  
15566 N N   . THR B 920  ? 0.4906 0.4443 0.4974 0.0501  -0.0230 -0.0221 918  THR B N   
15567 C CA  . THR B 920  ? 0.4413 0.4041 0.4540 0.0489  -0.0203 -0.0225 918  THR B CA  
15568 C C   . THR B 920  ? 0.4246 0.3943 0.4434 0.0535  -0.0190 -0.0231 918  THR B C   
15569 O O   . THR B 920  ? 0.4045 0.3810 0.4275 0.0530  -0.0165 -0.0236 918  THR B O   
15570 C CB  . THR B 920  ? 0.4175 0.3853 0.4332 0.0450  -0.0209 -0.0212 918  THR B CB  
15571 O OG1 . THR B 920  ? 0.4482 0.4187 0.4672 0.0468  -0.0231 -0.0201 918  THR B OG1 
15572 C CG2 . THR B 920  ? 0.3847 0.3467 0.3946 0.0406  -0.0217 -0.0207 918  THR B CG2 
15573 N N   . GLY B 921  ? 0.4204 0.3889 0.4399 0.0580  -0.0207 -0.0228 919  GLY B N   
15574 C CA  . GLY B 921  ? 0.3921 0.3685 0.4181 0.0624  -0.0195 -0.0231 919  GLY B CA  
15575 C C   . GLY B 921  ? 0.3785 0.3562 0.4046 0.0648  -0.0164 -0.0248 919  GLY B C   
15576 O O   . GLY B 921  ? 0.3880 0.3745 0.4203 0.0670  -0.0145 -0.0249 919  GLY B O   
15577 N N   . VAL B 922  ? 0.3214 0.2905 0.3403 0.0642  -0.0159 -0.0261 920  VAL B N   
15578 C CA  . VAL B 922  ? 0.3084 0.2777 0.3263 0.0664  -0.0131 -0.0279 920  VAL B CA  
15579 C C   . VAL B 922  ? 0.2923 0.2672 0.3124 0.0625  -0.0105 -0.0281 920  VAL B C   
15580 O O   . VAL B 922  ? 0.2741 0.2511 0.2944 0.0642  -0.0079 -0.0294 920  VAL B O   
15581 C CB  . VAL B 922  ? 0.3451 0.3024 0.3539 0.0672  -0.0140 -0.0293 920  VAL B CB  
15582 C CG1 . VAL B 922  ? 0.3475 0.2992 0.3541 0.0721  -0.0164 -0.0293 920  VAL B CG1 
15583 C CG2 . VAL B 922  ? 0.3560 0.3068 0.3596 0.0614  -0.0154 -0.0287 920  VAL B CG2 
15584 N N   . GLY B 923  ? 0.2729 0.2501 0.2945 0.0576  -0.0111 -0.0269 921  GLY B N   
15585 C CA  . GLY B 923  ? 0.2482 0.2308 0.2722 0.0541  -0.0088 -0.0268 921  GLY B CA  
15586 C C   . GLY B 923  ? 0.2497 0.2409 0.2807 0.0523  -0.0090 -0.0253 921  GLY B C   
15587 O O   . GLY B 923  ? 0.2535 0.2476 0.2881 0.0543  -0.0106 -0.0244 921  GLY B O   
15588 N N   . THR B 924  ? 0.2195 0.2145 0.2522 0.0485  -0.0076 -0.0250 922  THR B N   
15589 C CA  . THR B 924  ? 0.2052 0.2079 0.2441 0.0464  -0.0078 -0.0237 922  THR B CA  
15590 C C   . THR B 924  ? 0.2023 0.2019 0.2386 0.0419  -0.0092 -0.0230 922  THR B C   
15591 O O   . THR B 924  ? 0.2289 0.2274 0.2630 0.0391  -0.0079 -0.0234 922  THR B O   
15592 C CB  . THR B 924  ? 0.1975 0.2076 0.2409 0.0461  -0.0050 -0.0237 922  THR B CB  
15593 O OG1 . THR B 924  ? 0.2095 0.2165 0.2489 0.0442  -0.0032 -0.0247 922  THR B OG1 
15594 C CG2 . THR B 924  ? 0.2287 0.2433 0.2755 0.0508  -0.0036 -0.0241 922  THR B CG2 
15595 N N   . PHE B 925  ? 0.2180 0.2164 0.2544 0.0415  -0.0118 -0.0221 923  PHE B N   
15596 C CA  . PHE B 925  ? 0.2400 0.2354 0.2736 0.0377  -0.0132 -0.0215 923  PHE B CA  
15597 C C   . PHE B 925  ? 0.2306 0.2312 0.2687 0.0364  -0.0146 -0.0203 923  PHE B C   
15598 O O   . PHE B 925  ? 0.2313 0.2357 0.2736 0.0387  -0.0157 -0.0197 923  PHE B O   
15599 C CB  . PHE B 925  ? 0.2281 0.2152 0.2555 0.0379  -0.0154 -0.0213 923  PHE B CB  
15600 C CG  . PHE B 925  ? 0.2477 0.2282 0.2695 0.0381  -0.0145 -0.0224 923  PHE B CG  
15601 C CD1 . PHE B 925  ? 0.2452 0.2236 0.2661 0.0419  -0.0141 -0.0233 923  PHE B CD1 
15602 C CD2 . PHE B 925  ? 0.2367 0.2134 0.2540 0.0344  -0.0142 -0.0225 923  PHE B CD2 
15603 C CE1 . PHE B 925  ? 0.2279 0.1995 0.2430 0.0420  -0.0135 -0.0244 923  PHE B CE1 
15604 C CE2 . PHE B 925  ? 0.2256 0.1962 0.2376 0.0343  -0.0137 -0.0233 923  PHE B CE2 
15605 C CZ  . PHE B 925  ? 0.2437 0.2114 0.2544 0.0379  -0.0135 -0.0243 923  PHE B CZ  
15606 N N   . VAL B 926  ? 0.2104 0.2109 0.2475 0.0327  -0.0146 -0.0200 924  VAL B N   
15607 C CA  . VAL B 926  ? 0.2096 0.2128 0.2489 0.0308  -0.0164 -0.0191 924  VAL B CA  
15608 C C   . VAL B 926  ? 0.2270 0.2245 0.2605 0.0282  -0.0176 -0.0190 924  VAL B C   
15609 O O   . VAL B 926  ? 0.2147 0.2096 0.2448 0.0264  -0.0161 -0.0196 924  VAL B O   
15610 C CB  . VAL B 926  ? 0.2093 0.2184 0.2529 0.0288  -0.0149 -0.0190 924  VAL B CB  
15611 C CG1 . VAL B 926  ? 0.2200 0.2308 0.2651 0.0266  -0.0170 -0.0182 924  VAL B CG1 
15612 C CG2 . VAL B 926  ? 0.2146 0.2299 0.2638 0.0311  -0.0133 -0.0190 924  VAL B CG2 
15613 N N   . PRO B 927  ? 0.2446 0.2401 0.2767 0.0281  -0.0202 -0.0182 925  PRO B N   
15614 C CA  . PRO B 927  ? 0.2370 0.2273 0.2634 0.0256  -0.0212 -0.0180 925  PRO B CA  
15615 C C   . PRO B 927  ? 0.2170 0.2096 0.2438 0.0226  -0.0206 -0.0181 925  PRO B C   
15616 O O   . PRO B 927  ? 0.2357 0.2333 0.2670 0.0223  -0.0205 -0.0180 925  PRO B O   
15617 C CB  . PRO B 927  ? 0.2939 0.2820 0.3191 0.0267  -0.0243 -0.0170 925  PRO B CB  
15618 C CG  . PRO B 927  ? 0.2774 0.2718 0.3092 0.0284  -0.0251 -0.0167 925  PRO B CG  
15619 C CD  . PRO B 927  ? 0.2591 0.2575 0.2949 0.0300  -0.0225 -0.0174 925  PRO B CD  
15620 N N   . PRO B 928  ? 0.2321 0.2211 0.2539 0.0203  -0.0203 -0.0182 926  PRO B N   
15621 C CA  . PRO B 928  ? 0.2167 0.2072 0.2381 0.0178  -0.0201 -0.0183 926  PRO B CA  
15622 C C   . PRO B 928  ? 0.2335 0.2260 0.2570 0.0177  -0.0224 -0.0178 926  PRO B C   
15623 O O   . PRO B 928  ? 0.2479 0.2384 0.2700 0.0185  -0.0248 -0.0171 926  PRO B O   
15624 C CB  . PRO B 928  ? 0.2519 0.2378 0.2671 0.0160  -0.0201 -0.0181 926  PRO B CB  
15625 C CG  . PRO B 928  ? 0.2514 0.2346 0.2649 0.0168  -0.0189 -0.0183 926  PRO B CG  
15626 C CD  . PRO B 928  ? 0.2616 0.2454 0.2782 0.0198  -0.0198 -0.0182 926  PRO B CD  
15627 N N   . THR B 929  ? 0.2287 0.2249 0.2554 0.0167  -0.0219 -0.0181 927  THR B N   
15628 C CA  . THR B 929  ? 0.2238 0.2226 0.2533 0.0163  -0.0241 -0.0177 927  THR B CA  
15629 C C   . THR B 929  ? 0.2251 0.2234 0.2526 0.0139  -0.0241 -0.0182 927  THR B C   
15630 O O   . THR B 929  ? 0.2373 0.2360 0.2646 0.0130  -0.0219 -0.0189 927  THR B O   
15631 C CB  . THR B 929  ? 0.2144 0.2188 0.2507 0.0175  -0.0237 -0.0175 927  THR B CB  
15632 O OG1 . THR B 929  ? 0.2163 0.2210 0.2541 0.0202  -0.0236 -0.0172 927  THR B OG1 
15633 C CG2 . THR B 929  ? 0.2190 0.2266 0.2586 0.0167  -0.0261 -0.0169 927  THR B CG2 
15634 N N   . ILE B 930  ? 0.2257 0.2227 0.2512 0.0130  -0.0266 -0.0180 928  ILE B N   
15635 C CA  . ILE B 930  ? 0.2115 0.2073 0.2344 0.0110  -0.0270 -0.0186 928  ILE B CA  
15636 C C   . ILE B 930  ? 0.2407 0.2391 0.2671 0.0104  -0.0294 -0.0183 928  ILE B C   
15637 O O   . ILE B 930  ? 0.2421 0.2410 0.2694 0.0110  -0.0320 -0.0175 928  ILE B O   
15638 C CB  . ILE B 930  ? 0.2463 0.2376 0.2625 0.0103  -0.0277 -0.0187 928  ILE B CB  
15639 C CG1 . ILE B 930  ? 0.2219 0.2112 0.2351 0.0105  -0.0253 -0.0187 928  ILE B CG1 
15640 C CG2 . ILE B 930  ? 0.2474 0.2374 0.2606 0.0086  -0.0280 -0.0195 928  ILE B CG2 
15641 C CD1 . ILE B 930  ? 0.3108 0.2961 0.3174 0.0097  -0.0258 -0.0185 928  ILE B CD1 
15642 N N   . ILE B 931  ? 0.2352 0.2351 0.2635 0.0090  -0.0288 -0.0188 929  ILE B N   
15643 C CA  . ILE B 931  ? 0.2496 0.2520 0.2813 0.0078  -0.0311 -0.0185 929  ILE B CA  
15644 C C   . ILE B 931  ? 0.2657 0.2647 0.2931 0.0059  -0.0317 -0.0195 929  ILE B C   
15645 O O   . ILE B 931  ? 0.2278 0.2254 0.2536 0.0055  -0.0295 -0.0203 929  ILE B O   
15646 C CB  . ILE B 931  ? 0.2109 0.2184 0.2493 0.0079  -0.0299 -0.0180 929  ILE B CB  
15647 C CG1 . ILE B 931  ? 0.2186 0.2291 0.2605 0.0103  -0.0288 -0.0173 929  ILE B CG1 
15648 C CG2 . ILE B 931  ? 0.1972 0.2076 0.2394 0.0062  -0.0325 -0.0174 929  ILE B CG2 
15649 C CD1 . ILE B 931  ? 0.2310 0.2473 0.2797 0.0106  -0.0277 -0.0166 929  ILE B CD1 
15650 N N   . GLU B 932  ? 0.2492 0.2466 0.2746 0.0048  -0.0349 -0.0195 930  GLU B N   
15651 C CA  . GLU B 932  ? 0.2538 0.2475 0.2746 0.0031  -0.0357 -0.0206 930  GLU B CA  
15652 C C   . GLU B 932  ? 0.2628 0.2584 0.2875 0.0014  -0.0368 -0.0206 930  GLU B C   
15653 O O   . GLU B 932  ? 0.2609 0.2600 0.2903 0.0007  -0.0391 -0.0195 930  GLU B O   
15654 C CB  . GLU B 932  ? 0.2991 0.2896 0.3149 0.0027  -0.0387 -0.0207 930  GLU B CB  
15655 C CG  . GLU B 932  ? 0.3161 0.3038 0.3267 0.0039  -0.0374 -0.0208 930  GLU B CG  
15656 C CD  . GLU B 932  ? 0.4198 0.4039 0.4244 0.0034  -0.0400 -0.0209 930  GLU B CD  
15657 O OE1 . GLU B 932  ? 0.4457 0.4298 0.4508 0.0022  -0.0432 -0.0208 930  GLU B OE1 
15658 O OE2 . GLU B 932  ? 0.3963 0.3777 0.3957 0.0039  -0.0388 -0.0210 930  GLU B OE2 
15659 N N   . LEU B 933  ? 0.2444 0.2376 0.2671 0.0006  -0.0353 -0.0216 931  LEU B N   
15660 C CA  . LEU B 933  ? 0.2696 0.2636 0.2952 -0.0014 -0.0363 -0.0215 931  LEU B CA  
15661 C C   . LEU B 933  ? 0.2994 0.2881 0.3194 -0.0030 -0.0387 -0.0228 931  LEU B C   
15662 O O   . LEU B 933  ? 0.3538 0.3380 0.3673 -0.0022 -0.0381 -0.0240 931  LEU B O   
15663 C CB  . LEU B 933  ? 0.2706 0.2654 0.2982 -0.0011 -0.0332 -0.0217 931  LEU B CB  
15664 C CG  . LEU B 933  ? 0.2698 0.2696 0.3025 0.0004  -0.0306 -0.0207 931  LEU B CG  
15665 C CD1 . LEU B 933  ? 0.2839 0.2837 0.3174 0.0003  -0.0279 -0.0209 931  LEU B CD1 
15666 C CD2 . LEU B 933  ? 0.3328 0.3382 0.3721 -0.0001 -0.0323 -0.0191 931  LEU B CD2 
15667 N N   . GLU B 934  ? 0.3390 0.3281 0.3614 -0.0053 -0.0412 -0.0224 932  GLU B N   
15668 C CA  . GLU B 934  ? 0.3306 0.3139 0.3475 -0.0071 -0.0434 -0.0237 932  GLU B CA  
15669 C C   . GLU B 934  ? 0.3561 0.3361 0.3710 -0.0071 -0.0412 -0.0247 932  GLU B C   
15670 O O   . GLU B 934  ? 0.3947 0.3688 0.4030 -0.0068 -0.0412 -0.0264 932  GLU B O   
15671 C CB  . GLU B 934  ? 0.3398 0.3246 0.3599 -0.0100 -0.0473 -0.0228 932  GLU B CB  
15672 N N   . LYS B 935  ? 0.3235 0.3072 0.3440 -0.0072 -0.0392 -0.0237 933  LYS B N   
15673 C CA  . LYS B 935  ? 0.3373 0.3182 0.3565 -0.0073 -0.0373 -0.0244 933  LYS B CA  
15674 C C   . LYS B 935  ? 0.3251 0.3109 0.3492 -0.0059 -0.0338 -0.0233 933  LYS B C   
15675 O O   . LYS B 935  ? 0.3076 0.2992 0.3374 -0.0058 -0.0335 -0.0219 933  LYS B O   
15676 C CB  . LYS B 935  ? 0.3613 0.3404 0.3817 -0.0104 -0.0398 -0.0240 933  LYS B CB  
15677 N N   . LEU B 936  ? 0.2984 0.2817 0.3199 -0.0046 -0.0311 -0.0242 934  LEU B N   
15678 C CA  . LEU B 936  ? 0.3089 0.2964 0.3345 -0.0034 -0.0280 -0.0233 934  LEU B CA  
15679 C C   . LEU B 936  ? 0.3170 0.3087 0.3490 -0.0052 -0.0283 -0.0216 934  LEU B C   
15680 O O   . LEU B 936  ? 0.3116 0.3087 0.3484 -0.0044 -0.0265 -0.0205 934  LEU B O   
15681 C CB  . LEU B 936  ? 0.3137 0.2979 0.3355 -0.0019 -0.0255 -0.0244 934  LEU B CB  
15682 C CG  . LEU B 936  ? 0.3275 0.3147 0.3502 0.0003  -0.0222 -0.0242 934  LEU B CG  
15683 C CD1 . LEU B 936  ? 0.3148 0.2985 0.3327 0.0019  -0.0203 -0.0255 934  LEU B CD1 
15684 C CD2 . LEU B 936  ? 0.3172 0.3090 0.3457 0.0000  -0.0206 -0.0227 934  LEU B CD2 
15685 N N   . SER B 937  ? 0.3164 0.3058 0.3484 -0.0078 -0.0307 -0.0214 935  SER B N   
15686 C CA  . SER B 937  ? 0.3237 0.3176 0.3620 -0.0100 -0.0310 -0.0195 935  SER B CA  
15687 C C   . SER B 937  ? 0.3144 0.3152 0.3586 -0.0103 -0.0321 -0.0180 935  SER B C   
15688 O O   . SER B 937  ? 0.2936 0.2996 0.3437 -0.0117 -0.0318 -0.0163 935  SER B O   
15689 C CB  . SER B 937  ? 0.3196 0.3090 0.3562 -0.0131 -0.0338 -0.0194 935  SER B CB  
15690 O OG  . SER B 937  ? 0.3427 0.3293 0.3765 -0.0144 -0.0372 -0.0201 935  SER B OG  
15691 N N   . ASP B 938  ? 0.2840 0.2850 0.3267 -0.0091 -0.0332 -0.0186 936  ASP B N   
15692 C CA  . ASP B 938  ? 0.3326 0.3403 0.3809 -0.0085 -0.0338 -0.0173 936  ASP B CA  
15693 C C   . ASP B 938  ? 0.2844 0.2970 0.3366 -0.0063 -0.0303 -0.0166 936  ASP B C   
15694 O O   . ASP B 938  ? 0.2933 0.3122 0.3512 -0.0059 -0.0302 -0.0152 936  ASP B O   
15695 C CB  . ASP B 938  ? 0.3421 0.3483 0.3872 -0.0070 -0.0353 -0.0180 936  ASP B CB  
15696 C CG  . ASP B 938  ? 0.3930 0.3950 0.4343 -0.0091 -0.0391 -0.0187 936  ASP B CG  
15697 O OD1 . ASP B 938  ? 0.3902 0.3911 0.4324 -0.0119 -0.0410 -0.0183 936  ASP B OD1 
15698 O OD2 . ASP B 938  ? 0.4713 0.4708 0.5085 -0.0079 -0.0403 -0.0195 936  ASP B OD2 
15699 N N   . LEU B 939  ? 0.2663 0.2761 0.3154 -0.0048 -0.0274 -0.0175 937  LEU B N   
15700 C CA  . LEU B 939  ? 0.2866 0.3001 0.3383 -0.0027 -0.0242 -0.0170 937  LEU B CA  
15701 C C   . LEU B 939  ? 0.3025 0.3175 0.3567 -0.0039 -0.0226 -0.0162 937  LEU B C   
15702 O O   . LEU B 939  ? 0.3488 0.3593 0.3995 -0.0048 -0.0223 -0.0168 937  LEU B O   
15703 C CB  . LEU B 939  ? 0.2583 0.2680 0.3048 -0.0005 -0.0223 -0.0185 937  LEU B CB  
15704 C CG  . LEU B 939  ? 0.3288 0.3411 0.3765 0.0018  -0.0193 -0.0183 937  LEU B CG  
15705 C CD1 . LEU B 939  ? 0.3266 0.3435 0.3783 0.0031  -0.0197 -0.0175 937  LEU B CD1 
15706 C CD2 . LEU B 939  ? 0.2819 0.2900 0.3240 0.0032  -0.0182 -0.0197 937  LEU B CD2 
15707 N N   . GLN B 940  ? 0.2622 0.2837 0.3223 -0.0038 -0.0214 -0.0147 938  GLN B N   
15708 C CA  . GLN B 940  ? 0.2903 0.3142 0.3536 -0.0055 -0.0202 -0.0134 938  GLN B CA  
15709 C C   . GLN B 940  ? 0.2724 0.2991 0.3370 -0.0036 -0.0167 -0.0132 938  GLN B C   
15710 O O   . GLN B 940  ? 0.2753 0.3033 0.3415 -0.0048 -0.0153 -0.0122 938  GLN B O   
15711 C CB  . GLN B 940  ? 0.3426 0.3724 0.4120 -0.0077 -0.0220 -0.0116 938  GLN B CB  
15712 N N   . ARG B 941  ? 0.2186 0.2459 0.2822 -0.0007 -0.0152 -0.0140 939  ARG B N   
15713 C CA  . ARG B 941  ? 0.2605 0.2903 0.3250 0.0011  -0.0120 -0.0139 939  ARG B CA  
15714 C C   . ARG B 941  ? 0.2096 0.2362 0.2699 0.0035  -0.0110 -0.0154 939  ARG B C   
15715 O O   . ARG B 941  ? 0.2018 0.2259 0.2598 0.0041  -0.0126 -0.0161 939  ARG B O   
15716 C CB  . ARG B 941  ? 0.2495 0.2866 0.3200 0.0019  -0.0111 -0.0125 939  ARG B CB  
15717 C CG  . ARG B 941  ? 0.2394 0.2787 0.3114 0.0039  -0.0122 -0.0128 939  ARG B CG  
15718 C CD  . ARG B 941  ? 0.3027 0.3499 0.3812 0.0045  -0.0117 -0.0113 939  ARG B CD  
15719 N NE  . ARG B 941  ? 0.2573 0.3067 0.3373 0.0070  -0.0126 -0.0115 939  ARG B NE  
15720 C CZ  . ARG B 941  ? 0.2827 0.3323 0.3618 0.0103  -0.0108 -0.0123 939  ARG B CZ  
15721 N NH1 . ARG B 941  ? 0.2689 0.3166 0.3454 0.0113  -0.0082 -0.0130 939  ARG B NH1 
15722 N NH2 . ARG B 941  ? 0.2422 0.2938 0.3231 0.0125  -0.0120 -0.0123 939  ARG B NH2 
15723 N N   . GLU B 942  ? 0.2228 0.2493 0.2819 0.0047  -0.0084 -0.0156 940  GLU B N   
15724 C CA  . GLU B 942  ? 0.2086 0.2329 0.2643 0.0068  -0.0072 -0.0168 940  GLU B CA  
15725 C C   . GLU B 942  ? 0.2249 0.2522 0.2828 0.0088  -0.0072 -0.0167 940  GLU B C   
15726 O O   . GLU B 942  ? 0.2392 0.2709 0.3007 0.0096  -0.0059 -0.0159 940  GLU B O   
15727 C CB  . GLU B 942  ? 0.2250 0.2488 0.2791 0.0074  -0.0047 -0.0170 940  GLU B CB  
15728 C CG  . GLU B 942  ? 0.1911 0.2130 0.2418 0.0092  -0.0036 -0.0180 940  GLU B CG  
15729 C CD  . GLU B 942  ? 0.2179 0.2404 0.2679 0.0098  -0.0011 -0.0180 940  GLU B CD  
15730 O OE1 . GLU B 942  ? 0.2437 0.2698 0.2967 0.0098  0.0001  -0.0171 940  GLU B OE1 
15731 O OE2 . GLU B 942  ? 0.1863 0.2062 0.2327 0.0102  -0.0004 -0.0188 940  GLU B OE2 
15732 N N   . VAL B 943  ? 0.1921 0.2168 0.2476 0.0096  -0.0087 -0.0174 941  VAL B N   
15733 C CA  . VAL B 943  ? 0.2013 0.2277 0.2582 0.0117  -0.0089 -0.0173 941  VAL B CA  
15734 C C   . VAL B 943  ? 0.1977 0.2208 0.2504 0.0132  -0.0075 -0.0183 941  VAL B C   
15735 O O   . VAL B 943  ? 0.1845 0.2033 0.2329 0.0128  -0.0083 -0.0190 941  VAL B O   
15736 C CB  . VAL B 943  ? 0.2203 0.2461 0.2774 0.0115  -0.0118 -0.0172 941  VAL B CB  
15737 C CG1 . VAL B 943  ? 0.2172 0.2444 0.2755 0.0140  -0.0122 -0.0171 941  VAL B CG1 
15738 C CG2 . VAL B 943  ? 0.2352 0.2645 0.2965 0.0095  -0.0134 -0.0161 941  VAL B CG2 
15739 N N   . PHE B 944  ? 0.1870 0.2121 0.2408 0.0148  -0.0055 -0.0184 942  PHE B N   
15740 C CA  . PHE B 944  ? 0.1741 0.1961 0.2239 0.0157  -0.0040 -0.0192 942  PHE B CA  
15741 C C   . PHE B 944  ? 0.1788 0.1986 0.2268 0.0176  -0.0048 -0.0197 942  PHE B C   
15742 O O   . PHE B 944  ? 0.1864 0.2071 0.2350 0.0197  -0.0038 -0.0199 942  PHE B O   
15743 C CB  . PHE B 944  ? 0.1630 0.1876 0.2142 0.0163  -0.0015 -0.0191 942  PHE B CB  
15744 C CG  . PHE B 944  ? 0.1928 0.2145 0.2399 0.0162  -0.0001 -0.0199 942  PHE B CG  
15745 C CD1 . PHE B 944  ? 0.1816 0.2015 0.2267 0.0145  0.0001  -0.0199 942  PHE B CD1 
15746 C CD2 . PHE B 944  ? 0.1786 0.1994 0.2240 0.0179  0.0010  -0.0205 942  PHE B CD2 
15747 C CE1 . PHE B 944  ? 0.1833 0.2012 0.2250 0.0144  0.0013  -0.0205 942  PHE B CE1 
15748 C CE2 . PHE B 944  ? 0.1972 0.2154 0.2389 0.0175  0.0021  -0.0211 942  PHE B CE2 
15749 C CZ  . PHE B 944  ? 0.1890 0.2061 0.2290 0.0157  0.0023  -0.0210 942  PHE B CZ  
15750 N N   . GLY B 945  ? 0.1787 0.1953 0.2240 0.0170  -0.0067 -0.0198 943  GLY B N   
15751 C CA  . GLY B 945  ? 0.1886 0.2024 0.2318 0.0185  -0.0079 -0.0200 943  GLY B CA  
15752 C C   . GLY B 945  ? 0.2026 0.2124 0.2418 0.0171  -0.0096 -0.0201 943  GLY B C   
15753 O O   . GLY B 945  ? 0.1987 0.2078 0.2365 0.0153  -0.0096 -0.0203 943  GLY B O   
15754 N N   . PRO B 946  ? 0.2017 0.2087 0.2387 0.0182  -0.0111 -0.0201 944  PRO B N   
15755 C CA  . PRO B 946  ? 0.2084 0.2113 0.2408 0.0168  -0.0125 -0.0201 944  PRO B CA  
15756 C C   . PRO B 946  ? 0.1828 0.1864 0.2162 0.0160  -0.0147 -0.0196 944  PRO B C   
15757 O O   . PRO B 946  ? 0.2164 0.2180 0.2482 0.0165  -0.0167 -0.0192 944  PRO B O   
15758 C CB  . PRO B 946  ? 0.1943 0.1935 0.2239 0.0183  -0.0131 -0.0200 944  PRO B CB  
15759 C CG  . PRO B 946  ? 0.2032 0.2054 0.2372 0.0209  -0.0134 -0.0198 944  PRO B CG  
15760 C CD  . PRO B 946  ? 0.1845 0.1915 0.2226 0.0208  -0.0114 -0.0200 944  PRO B CD  
15761 N N   . VAL B 947  ? 0.1779 0.1840 0.2136 0.0147  -0.0144 -0.0197 945  VAL B N   
15762 C CA  . VAL B 947  ? 0.1903 0.1974 0.2274 0.0138  -0.0167 -0.0193 945  VAL B CA  
15763 C C   . VAL B 947  ? 0.2324 0.2375 0.2664 0.0118  -0.0166 -0.0198 945  VAL B C   
15764 O O   . VAL B 947  ? 0.2128 0.2192 0.2482 0.0110  -0.0152 -0.0201 945  VAL B O   
15765 C CB  . VAL B 947  ? 0.1917 0.2039 0.2349 0.0141  -0.0170 -0.0187 945  VAL B CB  
15766 C CG1 . VAL B 947  ? 0.2151 0.2280 0.2594 0.0128  -0.0197 -0.0182 945  VAL B CG1 
15767 C CG2 . VAL B 947  ? 0.1993 0.2139 0.2455 0.0166  -0.0167 -0.0183 945  VAL B CG2 
15768 N N   . LEU B 948  ? 0.1957 0.1974 0.2254 0.0112  -0.0180 -0.0200 946  LEU B N   
15769 C CA  . LEU B 948  ? 0.2104 0.2099 0.2364 0.0098  -0.0179 -0.0207 946  LEU B CA  
15770 C C   . LEU B 948  ? 0.2096 0.2089 0.2360 0.0088  -0.0204 -0.0207 946  LEU B C   
15771 O O   . LEU B 948  ? 0.2165 0.2154 0.2427 0.0089  -0.0227 -0.0202 946  LEU B O   
15772 C CB  . LEU B 948  ? 0.1965 0.1925 0.2169 0.0097  -0.0177 -0.0208 946  LEU B CB  
15773 C CG  . LEU B 948  ? 0.2056 0.1997 0.2220 0.0086  -0.0175 -0.0216 946  LEU B CG  
15774 C CD1 . LEU B 948  ? 0.2134 0.2087 0.2307 0.0084  -0.0151 -0.0222 946  LEU B CD1 
15775 C CD2 . LEU B 948  ? 0.2478 0.2392 0.2590 0.0084  -0.0174 -0.0214 946  LEU B CD2 
15776 N N   . HIS B 949  ? 0.1911 0.1905 0.2178 0.0076  -0.0201 -0.0212 947  HIS B N   
15777 C CA  . HIS B 949  ? 0.1950 0.1935 0.2215 0.0063  -0.0226 -0.0213 947  HIS B CA  
15778 C C   . HIS B 949  ? 0.2398 0.2340 0.2600 0.0058  -0.0228 -0.0223 947  HIS B C   
15779 O O   . HIS B 949  ? 0.2523 0.2453 0.2699 0.0062  -0.0206 -0.0230 947  HIS B O   
15780 C CB  . HIS B 949  ? 0.2192 0.2199 0.2497 0.0053  -0.0224 -0.0211 947  HIS B CB  
15781 C CG  . HIS B 949  ? 0.1992 0.2046 0.2357 0.0060  -0.0217 -0.0201 947  HIS B CG  
15782 N ND1 . HIS B 949  ? 0.1997 0.2069 0.2378 0.0070  -0.0189 -0.0200 947  HIS B ND1 
15783 C CD2 . HIS B 949  ? 0.2015 0.2106 0.2427 0.0059  -0.0234 -0.0191 947  HIS B CD2 
15784 C CE1 . HIS B 949  ? 0.1930 0.2045 0.2363 0.0077  -0.0188 -0.0191 947  HIS B CE1 
15785 N NE2 . HIS B 949  ? 0.1926 0.2056 0.2380 0.0071  -0.0214 -0.0185 947  HIS B NE2 
15786 N N   . VAL B 950  ? 0.2223 0.2144 0.2400 0.0051  -0.0255 -0.0225 948  VAL B N   
15787 C CA  . VAL B 950  ? 0.2557 0.2438 0.2669 0.0048  -0.0258 -0.0235 948  VAL B CA  
15788 C C   . VAL B 950  ? 0.2488 0.2347 0.2586 0.0035  -0.0278 -0.0243 948  VAL B C   
15789 O O   . VAL B 950  ? 0.2576 0.2443 0.2698 0.0025  -0.0305 -0.0238 948  VAL B O   
15790 C CB  . VAL B 950  ? 0.2492 0.2357 0.2567 0.0052  -0.0271 -0.0231 948  VAL B CB  
15791 C CG1 . VAL B 950  ? 0.2518 0.2345 0.2525 0.0048  -0.0273 -0.0242 948  VAL B CG1 
15792 C CG2 . VAL B 950  ? 0.2546 0.2423 0.2625 0.0062  -0.0250 -0.0224 948  VAL B CG2 
15793 N N   . ILE B 951  ? 0.2330 0.2159 0.2387 0.0036  -0.0266 -0.0256 949  ILE B N   
15794 C CA  . ILE B 951  ? 0.2468 0.2261 0.2496 0.0026  -0.0284 -0.0267 949  ILE B CA  
15795 C C   . ILE B 951  ? 0.2397 0.2152 0.2351 0.0033  -0.0282 -0.0279 949  ILE B C   
15796 O O   . ILE B 951  ? 0.2512 0.2270 0.2444 0.0046  -0.0255 -0.0282 949  ILE B O   
15797 C CB  . ILE B 951  ? 0.2819 0.2609 0.2864 0.0024  -0.0269 -0.0271 949  ILE B CB  
15798 C CG1 . ILE B 951  ? 0.3223 0.3053 0.3340 0.0015  -0.0272 -0.0258 949  ILE B CG1 
15799 C CG2 . ILE B 951  ? 0.3380 0.3119 0.3380 0.0017  -0.0285 -0.0286 949  ILE B CG2 
15800 C CD1 . ILE B 951  ? 0.3668 0.3491 0.3799 0.0010  -0.0261 -0.0260 949  ILE B CD1 
15801 N N   . ARG B 952  ? 0.2315 0.2037 0.2230 0.0024  -0.0310 -0.0286 950  ARG B N   
15802 C CA  A ARG B 952  ? 0.2629 0.2310 0.2468 0.0031  -0.0308 -0.0300 950  ARG B CA  
15803 C CA  B ARG B 952  ? 0.2630 0.2310 0.2468 0.0031  -0.0309 -0.0300 950  ARG B CA  
15804 C C   . ARG B 952  ? 0.2656 0.2294 0.2463 0.0029  -0.0312 -0.0317 950  ARG B C   
15805 O O   . ARG B 952  ? 0.3084 0.2710 0.2914 0.0014  -0.0335 -0.0317 950  ARG B O   
15806 C CB  A ARG B 952  ? 0.2683 0.2348 0.2487 0.0023  -0.0337 -0.0298 950  ARG B CB  
15807 C CB  B ARG B 952  ? 0.2683 0.2347 0.2487 0.0022  -0.0338 -0.0298 950  ARG B CB  
15808 C CG  A ARG B 952  ? 0.2756 0.2454 0.2583 0.0026  -0.0336 -0.0281 950  ARG B CG  
15809 C CG  B ARG B 952  ? 0.2822 0.2523 0.2665 0.0022  -0.0344 -0.0280 950  ARG B CG  
15810 C CD  A ARG B 952  ? 0.3018 0.2705 0.2830 0.0016  -0.0373 -0.0275 950  ARG B CD  
15811 C CD  B ARG B 952  ? 0.2944 0.2630 0.2764 0.0011  -0.0381 -0.0276 950  ARG B CD  
15812 N NE  A ARG B 952  ? 0.3293 0.3012 0.3142 0.0019  -0.0377 -0.0257 950  ARG B NE  
15813 N NE  B ARG B 952  ? 0.2976 0.2625 0.2715 0.0015  -0.0382 -0.0285 950  ARG B NE  
15814 C CZ  A ARG B 952  ? 0.3033 0.2745 0.2847 0.0023  -0.0380 -0.0250 950  ARG B CZ  
15815 C CZ  B ARG B 952  ? 0.3102 0.2754 0.2814 0.0020  -0.0380 -0.0276 950  ARG B CZ  
15816 N NH1 A ARG B 952  ? 0.3202 0.2881 0.2943 0.0025  -0.0375 -0.0258 950  ARG B NH1 
15817 N NH1 B ARG B 952  ? 0.3158 0.2841 0.2914 0.0023  -0.0378 -0.0258 950  ARG B NH1 
15818 N NH2 A ARG B 952  ? 0.2978 0.2713 0.2828 0.0027  -0.0387 -0.0233 950  ARG B NH2 
15819 N NH2 B ARG B 952  ? 0.3013 0.2633 0.2649 0.0023  -0.0379 -0.0284 950  ARG B NH2 
15820 N N   . TYR B 953  ? 0.2541 0.2155 0.2295 0.0046  -0.0291 -0.0331 951  TYR B N   
15821 C CA  . TYR B 953  ? 0.2617 0.2184 0.2336 0.0050  -0.0294 -0.0348 951  TYR B CA  
15822 C C   . TYR B 953  ? 0.2693 0.2220 0.2327 0.0065  -0.0289 -0.0366 951  TYR B C   
15823 O O   . TYR B 953  ? 0.2725 0.2272 0.2335 0.0077  -0.0270 -0.0364 951  TYR B O   
15824 C CB  . TYR B 953  ? 0.2730 0.2312 0.2481 0.0062  -0.0266 -0.0348 951  TYR B CB  
15825 C CG  . TYR B 953  ? 0.2377 0.1982 0.2111 0.0085  -0.0230 -0.0350 951  TYR B CG  
15826 C CD1 . TYR B 953  ? 0.2218 0.1876 0.1990 0.0087  -0.0210 -0.0335 951  TYR B CD1 
15827 C CD2 . TYR B 953  ? 0.2521 0.2095 0.2200 0.0106  -0.0215 -0.0367 951  TYR B CD2 
15828 C CE1 . TYR B 953  ? 0.2391 0.2073 0.2148 0.0104  -0.0179 -0.0335 951  TYR B CE1 
15829 C CE2 . TYR B 953  ? 0.2763 0.2367 0.2431 0.0127  -0.0182 -0.0368 951  TYR B CE2 
15830 C CZ  . TYR B 953  ? 0.2493 0.2152 0.2201 0.0123  -0.0164 -0.0351 951  TYR B CZ  
15831 O OH  . TYR B 953  ? 0.2588 0.2279 0.2285 0.0141  -0.0133 -0.0350 951  TYR B OH  
15832 N N   . ARG B 954  ? 0.2897 0.2365 0.2484 0.0064  -0.0308 -0.0384 952  ARG B N   
15833 C CA  . ARG B 954  ? 0.3406 0.2831 0.2910 0.0084  -0.0300 -0.0405 952  ARG B CA  
15834 C C   . ARG B 954  ? 0.3353 0.2778 0.2850 0.0110  -0.0267 -0.0414 952  ARG B C   
15835 O O   . ARG B 954  ? 0.3200 0.2623 0.2737 0.0109  -0.0264 -0.0411 952  ARG B O   
15836 C CB  . ARG B 954  ? 0.3642 0.2996 0.3091 0.0072  -0.0337 -0.0421 952  ARG B CB  
15837 N N   . ARG B 955  ? 0.3277 0.2708 0.2725 0.0135  -0.0241 -0.0423 953  ARG B N   
15838 C CA  . ARG B 955  ? 0.3689 0.3133 0.3138 0.0163  -0.0207 -0.0429 953  ARG B CA  
15839 C C   . ARG B 955  ? 0.3615 0.2996 0.3039 0.0173  -0.0217 -0.0447 953  ARG B C   
15840 O O   . ARG B 955  ? 0.3500 0.2891 0.2952 0.0188  -0.0198 -0.0446 953  ARG B O   
15841 C CB  . ARG B 955  ? 0.3788 0.3250 0.3184 0.0188  -0.0179 -0.0436 953  ARG B CB  
15842 C CG  . ARG B 955  ? 0.4777 0.4263 0.4175 0.0219  -0.0142 -0.0442 953  ARG B CG  
15843 C CD  . ARG B 955  ? 0.4314 0.3854 0.3793 0.0214  -0.0126 -0.0423 953  ARG B CD  
15844 N NE  . ARG B 955  ? 0.4268 0.3834 0.3751 0.0244  -0.0094 -0.0427 953  ARG B NE  
15845 C CZ  . ARG B 955  ? 0.4936 0.4463 0.4401 0.0266  -0.0092 -0.0441 953  ARG B CZ  
15846 N NH1 . ARG B 955  ? 0.4563 0.4017 0.4002 0.0260  -0.0121 -0.0454 953  ARG B NH1 
15847 N NH2 . ARG B 955  ? 0.5068 0.4628 0.4540 0.0295  -0.0062 -0.0442 953  ARG B NH2 
15848 N N   . ASP B 956  ? 0.3528 0.2840 0.2896 0.0165  -0.0248 -0.0463 954  ASP B N   
15849 C CA  . ASP B 956  ? 0.3602 0.2843 0.2944 0.0169  -0.0264 -0.0479 954  ASP B CA  
15850 C C   . ASP B 956  ? 0.3729 0.2978 0.3143 0.0146  -0.0276 -0.0463 954  ASP B C   
15851 O O   . ASP B 956  ? 0.4157 0.3358 0.3561 0.0152  -0.0281 -0.0472 954  ASP B O   
15852 C CB  . ASP B 956  ? 0.4136 0.3301 0.3406 0.0157  -0.0300 -0.0497 954  ASP B CB  
15853 C CG  . ASP B 956  ? 0.5390 0.4528 0.4571 0.0187  -0.0288 -0.0519 954  ASP B CG  
15854 O OD1 . ASP B 956  ? 0.5539 0.4712 0.4714 0.0219  -0.0249 -0.0522 954  ASP B OD1 
15855 O OD2 . ASP B 956  ? 0.6225 0.5310 0.5344 0.0177  -0.0316 -0.0533 954  ASP B OD2 
15856 N N   . ASP B 957  ? 0.3282 0.2589 0.2765 0.0120  -0.0281 -0.0441 955  ASP B N   
15857 C CA  . ASP B 957  ? 0.3485 0.2808 0.3039 0.0098  -0.0291 -0.0424 955  ASP B CA  
15858 C C   . ASP B 957  ? 0.3020 0.2405 0.2634 0.0110  -0.0257 -0.0409 955  ASP B C   
15859 O O   . ASP B 957  ? 0.3047 0.2462 0.2726 0.0091  -0.0261 -0.0392 955  ASP B O   
15860 C CB  . ASP B 957  ? 0.3416 0.2765 0.3011 0.0063  -0.0320 -0.0408 955  ASP B CB  
15861 C CG  . ASP B 957  ? 0.4305 0.3591 0.3855 0.0042  -0.0361 -0.0420 955  ASP B CG  
15862 O OD1 . ASP B 957  ? 0.4467 0.3682 0.3968 0.0046  -0.0372 -0.0436 955  ASP B OD1 
15863 O OD2 . ASP B 957  ? 0.4533 0.3837 0.4093 0.0022  -0.0384 -0.0412 955  ASP B OD2 
15864 N N   . LEU B 958  ? 0.3013 0.2424 0.2608 0.0140  -0.0224 -0.0414 956  LEU B N   
15865 C CA  . LEU B 958  ? 0.2901 0.2375 0.2552 0.0149  -0.0193 -0.0399 956  LEU B CA  
15866 C C   . LEU B 958  ? 0.2887 0.2349 0.2573 0.0148  -0.0192 -0.0394 956  LEU B C   
15867 O O   . LEU B 958  ? 0.2818 0.2327 0.2568 0.0136  -0.0184 -0.0375 956  LEU B O   
15868 C CB  . LEU B 958  ? 0.2985 0.2481 0.2603 0.0181  -0.0161 -0.0407 956  LEU B CB  
15869 C CG  . LEU B 958  ? 0.2879 0.2441 0.2549 0.0191  -0.0130 -0.0392 956  LEU B CG  
15870 C CD1 . LEU B 958  ? 0.2702 0.2320 0.2431 0.0167  -0.0131 -0.0371 956  LEU B CD1 
15871 C CD2 . LEU B 958  ? 0.2986 0.2574 0.2622 0.0222  -0.0100 -0.0400 956  LEU B CD2 
15872 N N   . ASP B 959  ? 0.2759 0.2156 0.2400 0.0161  -0.0200 -0.0409 957  ASP B N   
15873 C CA  . ASP B 959  ? 0.2791 0.2171 0.2461 0.0160  -0.0199 -0.0403 957  ASP B CA  
15874 C C   . ASP B 959  ? 0.2636 0.2021 0.2357 0.0121  -0.0223 -0.0386 957  ASP B C   
15875 O O   . ASP B 959  ? 0.2844 0.2260 0.2619 0.0114  -0.0213 -0.0370 957  ASP B O   
15876 C CB  . ASP B 959  ? 0.2836 0.2133 0.2440 0.0180  -0.0207 -0.0423 957  ASP B CB  
15877 C CG  . ASP B 959  ? 0.2834 0.2122 0.2458 0.0194  -0.0195 -0.0418 957  ASP B CG  
15878 O OD1 . ASP B 959  ? 0.2788 0.2139 0.2454 0.0207  -0.0167 -0.0406 957  ASP B OD1 
15879 O OD2 . ASP B 959  ? 0.3165 0.2380 0.2760 0.0190  -0.0215 -0.0424 957  ASP B OD2 
15880 N N   . ARG B 960  ? 0.2656 0.2013 0.2362 0.0096  -0.0254 -0.0389 958  ARG B N   
15881 C CA  . ARG B 960  ? 0.2585 0.1957 0.2345 0.0059  -0.0277 -0.0372 958  ARG B CA  
15882 C C   . ARG B 960  ? 0.2615 0.2073 0.2444 0.0051  -0.0262 -0.0352 958  ARG B C   
15883 O O   . ARG B 960  ? 0.2559 0.2050 0.2448 0.0031  -0.0264 -0.0334 958  ARG B O   
15884 C CB  . ARG B 960  ? 0.3000 0.2327 0.2726 0.0035  -0.0315 -0.0380 958  ARG B CB  
15885 N N   . LEU B 961  ? 0.2368 0.1862 0.2189 0.0065  -0.0247 -0.0354 959  LEU B N   
15886 C CA  . LEU B 961  ? 0.2427 0.1994 0.2307 0.0061  -0.0232 -0.0337 959  LEU B CA  
15887 C C   . LEU B 961  ? 0.2417 0.2019 0.2337 0.0072  -0.0204 -0.0326 959  LEU B C   
15888 O O   . LEU B 961  ? 0.2252 0.1899 0.2231 0.0059  -0.0200 -0.0310 959  LEU B O   
15889 C CB  . LEU B 961  ? 0.2498 0.2088 0.2351 0.0076  -0.0220 -0.0341 959  LEU B CB  
15890 C CG  . LEU B 961  ? 0.2564 0.2220 0.2468 0.0074  -0.0203 -0.0325 959  LEU B CG  
15891 C CD1 . LEU B 961  ? 0.2794 0.2472 0.2744 0.0050  -0.0226 -0.0311 959  LEU B CD1 
15892 C CD2 . LEU B 961  ? 0.2712 0.2383 0.2582 0.0088  -0.0189 -0.0329 959  LEU B CD2 
15893 N N   . VAL B 962  ? 0.2209 0.1791 0.2098 0.0096  -0.0185 -0.0336 960  VAL B N   
15894 C CA  . VAL B 962  ? 0.2254 0.1867 0.2179 0.0106  -0.0161 -0.0326 960  VAL B CA  
15895 C C   . VAL B 962  ? 0.2548 0.2150 0.2509 0.0085  -0.0174 -0.0315 960  VAL B C   
15896 O O   . VAL B 962  ? 0.2441 0.2089 0.2454 0.0078  -0.0162 -0.0299 960  VAL B O   
15897 C CB  . VAL B 962  ? 0.2190 0.1783 0.2074 0.0138  -0.0142 -0.0339 960  VAL B CB  
15898 C CG1 . VAL B 962  ? 0.2685 0.2299 0.2602 0.0146  -0.0124 -0.0328 960  VAL B CG1 
15899 C CG2 . VAL B 962  ? 0.2422 0.2048 0.2284 0.0157  -0.0122 -0.0345 960  VAL B CG2 
15900 N N   . ASP B 963  ? 0.2348 0.1888 0.2280 0.0072  -0.0200 -0.0322 961  ASP B N   
15901 C CA  . ASP B 963  ? 0.2628 0.2158 0.2594 0.0045  -0.0216 -0.0308 961  ASP B CA  
15902 C C   . ASP B 963  ? 0.2384 0.1975 0.2413 0.0021  -0.0221 -0.0290 961  ASP B C   
15903 O O   . ASP B 963  ? 0.2557 0.2183 0.2636 0.0009  -0.0214 -0.0273 961  ASP B O   
15904 C CB  . ASP B 963  ? 0.2647 0.2100 0.2569 0.0029  -0.0248 -0.0318 961  ASP B CB  
15905 C CG  . ASP B 963  ? 0.3063 0.2446 0.2926 0.0053  -0.0246 -0.0334 961  ASP B CG  
15906 O OD1 . ASP B 963  ? 0.3224 0.2623 0.3093 0.0077  -0.0220 -0.0332 961  ASP B OD1 
15907 O OD2 . ASP B 963  ? 0.3266 0.2577 0.3076 0.0047  -0.0271 -0.0348 961  ASP B OD2 
15908 N N   . ASP B 964  ? 0.2467 0.2072 0.2492 0.0014  -0.0234 -0.0294 962  ASP B N   
15909 C CA  . ASP B 964  ? 0.2489 0.2151 0.2573 -0.0006 -0.0241 -0.0277 962  ASP B CA  
15910 C C   . ASP B 964  ? 0.2480 0.2205 0.2608 0.0007  -0.0212 -0.0266 962  ASP B C   
15911 O O   . ASP B 964  ? 0.2266 0.2035 0.2450 -0.0007 -0.0210 -0.0250 962  ASP B O   
15912 C CB  . ASP B 964  ? 0.2591 0.2253 0.2656 -0.0009 -0.0260 -0.0284 962  ASP B CB  
15913 C CG  . ASP B 964  ? 0.2717 0.2321 0.2744 -0.0028 -0.0295 -0.0293 962  ASP B CG  
15914 O OD1 . ASP B 964  ? 0.2986 0.2553 0.3010 -0.0044 -0.0308 -0.0292 962  ASP B OD1 
15915 O OD2 . ASP B 964  ? 0.3529 0.3122 0.3527 -0.0029 -0.0312 -0.0301 962  ASP B OD2 
15916 N N   . VAL B 965  ? 0.2097 0.1829 0.2202 0.0032  -0.0188 -0.0274 963  VAL B N   
15917 C CA  . VAL B 965  ? 0.1836 0.1621 0.1978 0.0043  -0.0161 -0.0264 963  VAL B CA  
15918 C C   . VAL B 965  ? 0.2076 0.1868 0.2245 0.0040  -0.0149 -0.0254 963  VAL B C   
15919 O O   . VAL B 965  ? 0.2210 0.2048 0.2427 0.0033  -0.0140 -0.0240 963  VAL B O   
15920 C CB  . VAL B 965  ? 0.2162 0.1951 0.2270 0.0068  -0.0140 -0.0274 963  VAL B CB  
15921 C CG1 . VAL B 965  ? 0.1984 0.1823 0.2127 0.0076  -0.0114 -0.0264 963  VAL B CG1 
15922 C CG2 . VAL B 965  ? 0.2542 0.2331 0.2626 0.0068  -0.0150 -0.0280 963  VAL B CG2 
15923 N N   . ASN B 966  ? 0.2077 0.1822 0.2213 0.0046  -0.0151 -0.0260 964  ASN B N   
15924 C CA  . ASN B 966  ? 0.2126 0.1871 0.2282 0.0043  -0.0141 -0.0250 964  ASN B CA  
15925 C C   . ASN B 966  ? 0.2321 0.2074 0.2516 0.0012  -0.0158 -0.0234 964  ASN B C   
15926 O O   . ASN B 966  ? 0.2378 0.2156 0.2606 0.0005  -0.0147 -0.0219 964  ASN B O   
15927 C CB  . ASN B 966  ? 0.2235 0.1920 0.2344 0.0057  -0.0143 -0.0260 964  ASN B CB  
15928 C CG  . ASN B 966  ? 0.2143 0.1830 0.2220 0.0090  -0.0122 -0.0272 964  ASN B CG  
15929 O OD1 . ASN B 966  ? 0.2144 0.1884 0.2243 0.0099  -0.0101 -0.0267 964  ASN B OD1 
15930 N ND2 . ASN B 966  ? 0.2136 0.1768 0.2160 0.0107  -0.0127 -0.0287 964  ASN B ND2 
15931 N N   . ALA B 967  ? 0.2118 0.1854 0.2310 -0.0007 -0.0184 -0.0236 965  ALA B N   
15932 C CA  . ALA B 967  ? 0.2337 0.2077 0.2563 -0.0039 -0.0203 -0.0222 965  ALA B CA  
15933 C C   . ALA B 967  ? 0.2344 0.2161 0.2636 -0.0049 -0.0193 -0.0203 965  ALA B C   
15934 O O   . ALA B 967  ? 0.2274 0.2108 0.2602 -0.0075 -0.0203 -0.0187 965  ALA B O   
15935 C CB  . ALA B 967  ? 0.2670 0.2376 0.2875 -0.0058 -0.0237 -0.0229 965  ALA B CB  
15936 N N   . THR B 968  ? 0.2204 0.2066 0.2512 -0.0029 -0.0174 -0.0205 966  THR B N   
15937 C CA  . THR B 968  ? 0.1894 0.1825 0.2259 -0.0034 -0.0162 -0.0190 966  THR B CA  
15938 C C   . THR B 968  ? 0.2144 0.2093 0.2531 -0.0036 -0.0142 -0.0177 966  THR B C   
15939 O O   . THR B 968  ? 0.2198 0.2200 0.2634 -0.0044 -0.0134 -0.0162 966  THR B O   
15940 C CB  . THR B 968  ? 0.1824 0.1787 0.2192 -0.0011 -0.0146 -0.0196 966  THR B CB  
15941 O OG1 . THR B 968  ? 0.2013 0.1971 0.2360 0.0009  -0.0121 -0.0201 966  THR B OG1 
15942 C CG2 . THR B 968  ? 0.2278 0.2217 0.2613 -0.0006 -0.0163 -0.0209 966  THR B CG2 
15943 N N   . GLY B 969  ? 0.2147 0.2055 0.2499 -0.0026 -0.0133 -0.0182 967  GLY B N   
15944 C CA  . GLY B 969  ? 0.2032 0.1955 0.2398 -0.0024 -0.0113 -0.0170 967  GLY B CA  
15945 C C   . GLY B 969  ? 0.2094 0.2051 0.2463 0.0000  -0.0086 -0.0173 967  GLY B C   
15946 O O   . GLY B 969  ? 0.2082 0.2044 0.2452 0.0006  -0.0070 -0.0166 967  GLY B O   
15947 N N   . TYR B 970  ? 0.2033 0.2010 0.2401 0.0014  -0.0082 -0.0183 968  TYR B N   
15948 C CA  . TYR B 970  ? 0.1780 0.1782 0.2143 0.0035  -0.0060 -0.0186 968  TYR B CA  
15949 C C   . TYR B 970  ? 0.2027 0.1993 0.2345 0.0052  -0.0056 -0.0200 968  TYR B C   
15950 O O   . TYR B 970  ? 0.2174 0.2097 0.2461 0.0052  -0.0070 -0.0208 968  TYR B O   
15951 C CB  . TYR B 970  ? 0.1624 0.1659 0.2004 0.0039  -0.0060 -0.0190 968  TYR B CB  
15952 C CG  . TYR B 970  ? 0.2056 0.2139 0.2485 0.0031  -0.0057 -0.0177 968  TYR B CG  
15953 C CD1 . TYR B 970  ? 0.2331 0.2448 0.2777 0.0039  -0.0035 -0.0170 968  TYR B CD1 
15954 C CD2 . TYR B 970  ? 0.2100 0.2197 0.2556 0.0017  -0.0075 -0.0172 968  TYR B CD2 
15955 C CE1 . TYR B 970  ? 0.2540 0.2704 0.3029 0.0035  -0.0029 -0.0160 968  TYR B CE1 
15956 C CE2 . TYR B 970  ? 0.2690 0.2841 0.3195 0.0013  -0.0070 -0.0159 968  TYR B CE2 
15957 C CZ  . TYR B 970  ? 0.2716 0.2899 0.3235 0.0023  -0.0045 -0.0154 968  TYR B CZ  
15958 O OH  . TYR B 970  ? 0.3251 0.3488 0.3814 0.0023  -0.0036 -0.0143 968  TYR B OH  
15959 N N   . GLY B 971  ? 0.1659 0.1647 0.1972 0.0068  -0.0036 -0.0201 969  GLY B N   
15960 C CA  . GLY B 971  ? 0.1825 0.1792 0.2101 0.0086  -0.0030 -0.0212 969  GLY B CA  
15961 C C   . GLY B 971  ? 0.1829 0.1830 0.2107 0.0098  -0.0010 -0.0211 969  GLY B C   
15962 O O   . GLY B 971  ? 0.1857 0.1862 0.2127 0.0108  0.0001  -0.0209 969  GLY B O   
15963 N N   . LEU B 972  ? 0.1776 0.1802 0.2065 0.0096  -0.0008 -0.0213 970  LEU B N   
15964 C CA  . LEU B 972  ? 0.1741 0.1796 0.2031 0.0104  0.0007  -0.0212 970  LEU B CA  
15965 C C   . LEU B 972  ? 0.1494 0.1544 0.1753 0.0113  0.0009  -0.0221 970  LEU B C   
15966 O O   . LEU B 972  ? 0.1824 0.1872 0.2065 0.0123  0.0017  -0.0223 970  LEU B O   
15967 C CB  . LEU B 972  ? 0.1727 0.1808 0.2043 0.0098  0.0009  -0.0207 970  LEU B CB  
15968 C CG  . LEU B 972  ? 0.1764 0.1869 0.2080 0.0103  0.0024  -0.0206 970  LEU B CG  
15969 C CD1 . LEU B 972  ? 0.1745 0.1859 0.2059 0.0107  0.0037  -0.0201 970  LEU B CD1 
15970 C CD2 . LEU B 972  ? 0.1935 0.2059 0.2276 0.0101  0.0025  -0.0202 970  LEU B CD2 
15971 N N   . THR B 973  ? 0.1656 0.1706 0.1910 0.0109  0.0002  -0.0225 971  THR B N   
15972 C CA  . THR B 973  ? 0.1507 0.1554 0.1731 0.0115  0.0004  -0.0231 971  THR B CA  
15973 C C   . THR B 973  ? 0.1747 0.1765 0.1948 0.0114  -0.0010 -0.0239 971  THR B C   
15974 O O   . THR B 973  ? 0.1858 0.1860 0.2069 0.0107  -0.0025 -0.0239 971  THR B O   
15975 C CB  . THR B 973  ? 0.1589 0.1652 0.1812 0.0110  0.0008  -0.0229 971  THR B CB  
15976 O OG1 . THR B 973  ? 0.1672 0.1729 0.1909 0.0104  -0.0005 -0.0228 971  THR B OG1 
15977 C CG2 . THR B 973  ? 0.1839 0.1927 0.2077 0.0110  0.0021  -0.0223 971  THR B CG2 
15978 N N   . PHE B 974  ? 0.1785 0.1799 0.1954 0.0122  -0.0006 -0.0245 972  PHE B N   
15979 C CA  . PHE B 974  ? 0.1745 0.1729 0.1883 0.0124  -0.0018 -0.0254 972  PHE B CA  
15980 C C   . PHE B 974  ? 0.1571 0.1567 0.1679 0.0130  -0.0009 -0.0257 972  PHE B C   
15981 O O   . PHE B 974  ? 0.1690 0.1710 0.1795 0.0139  0.0007  -0.0256 972  PHE B O   
15982 C CB  . PHE B 974  ? 0.1743 0.1697 0.1868 0.0133  -0.0022 -0.0261 972  PHE B CB  
15983 C CG  . PHE B 974  ? 0.1684 0.1605 0.1767 0.0138  -0.0032 -0.0273 972  PHE B CG  
15984 C CD1 . PHE B 974  ? 0.1915 0.1809 0.1994 0.0126  -0.0054 -0.0275 972  PHE B CD1 
15985 C CD2 . PHE B 974  ? 0.1812 0.1734 0.1861 0.0156  -0.0021 -0.0280 972  PHE B CD2 
15986 C CE1 . PHE B 974  ? 0.2140 0.2002 0.2176 0.0130  -0.0065 -0.0287 972  PHE B CE1 
15987 C CE2 . PHE B 974  ? 0.1833 0.1723 0.1838 0.0162  -0.0029 -0.0293 972  PHE B CE2 
15988 C CZ  . PHE B 974  ? 0.1865 0.1723 0.1862 0.0149  -0.0051 -0.0296 972  PHE B CZ  
15989 N N   . GLY B 975  ? 0.1634 0.1615 0.1719 0.0125  -0.0019 -0.0261 973  GLY B N   
15990 C CA  . GLY B 975  ? 0.1949 0.1941 0.2003 0.0128  -0.0011 -0.0262 973  GLY B CA  
15991 C C   . GLY B 975  ? 0.1958 0.1921 0.1969 0.0136  -0.0018 -0.0273 973  GLY B C   
15992 O O   . GLY B 975  ? 0.1842 0.1772 0.1847 0.0132  -0.0037 -0.0279 973  GLY B O   
15993 N N   . LEU B 976  ? 0.1750 0.1729 0.1733 0.0146  -0.0004 -0.0276 974  LEU B N   
15994 C CA  . LEU B 976  ? 0.1778 0.1733 0.1714 0.0156  -0.0007 -0.0287 974  LEU B CA  
15995 C C   . LEU B 976  ? 0.1974 0.1956 0.1884 0.0153  0.0005  -0.0282 974  LEU B C   
15996 O O   . LEU B 976  ? 0.2092 0.2117 0.2013 0.0155  0.0024  -0.0275 974  LEU B O   
15997 C CB  . LEU B 976  ? 0.1897 0.1841 0.1817 0.0179  0.0002  -0.0299 974  LEU B CB  
15998 C CG  . LEU B 976  ? 0.2174 0.2094 0.2039 0.0195  0.0003  -0.0313 974  LEU B CG  
15999 C CD1 . LEU B 976  ? 0.2370 0.2236 0.2209 0.0186  -0.0023 -0.0322 974  LEU B CD1 
16000 C CD2 . LEU B 976  ? 0.2244 0.2161 0.2096 0.0223  0.0016  -0.0323 974  LEU B CD2 
16001 N N   . HIS B 977  ? 0.1864 0.1824 0.1741 0.0145  -0.0007 -0.0284 975  HIS B N   
16002 C CA  . HIS B 977  ? 0.2103 0.2085 0.1948 0.0140  0.0003  -0.0278 975  HIS B CA  
16003 C C   . HIS B 977  ? 0.2056 0.2017 0.1850 0.0156  0.0004  -0.0292 975  HIS B C   
16004 O O   . HIS B 977  ? 0.2123 0.2040 0.1890 0.0154  -0.0016 -0.0300 975  HIS B O   
16005 C CB  . HIS B 977  ? 0.2208 0.2180 0.2052 0.0118  -0.0013 -0.0267 975  HIS B CB  
16006 C CG  . HIS B 977  ? 0.2221 0.2225 0.2093 0.0104  -0.0004 -0.0252 975  HIS B CG  
16007 N ND1 . HIS B 977  ? 0.2937 0.2965 0.2788 0.0093  0.0007  -0.0240 975  HIS B ND1 
16008 C CD2 . HIS B 977  ? 0.2647 0.2659 0.2563 0.0097  -0.0006 -0.0245 975  HIS B CD2 
16009 C CE1 . HIS B 977  ? 0.2699 0.2744 0.2578 0.0079  0.0009  -0.0228 975  HIS B CE1 
16010 N NE2 . HIS B 977  ? 0.2235 0.2270 0.2152 0.0083  0.0002  -0.0232 975  HIS B NE2 
16011 N N   . THR B 978  ? 0.2033 0.2025 0.1810 0.0173  0.0027  -0.0295 976  THR B N   
16012 C CA  . THR B 978  ? 0.2164 0.2143 0.1887 0.0193  0.0034  -0.0309 976  THR B CA  
16013 C C   . THR B 978  ? 0.2363 0.2402 0.2082 0.0205  0.0064  -0.0304 976  THR B C   
16014 O O   . THR B 978  ? 0.2384 0.2466 0.2144 0.0204  0.0077  -0.0294 976  THR B O   
16015 C CB  . THR B 978  ? 0.2177 0.2111 0.1888 0.0215  0.0026  -0.0328 976  THR B CB  
16016 O OG1 . THR B 978  ? 0.2117 0.2036 0.1770 0.0237  0.0034  -0.0344 976  THR B OG1 
16017 C CG2 . THR B 978  ? 0.2271 0.2229 0.2021 0.0231  0.0040  -0.0328 976  THR B CG2 
16018 N N   . ARG B 979  ? 0.2490 0.2533 0.2158 0.0216  0.0074  -0.0310 977  ARG B N   
16019 C CA  . ARG B 979  ? 0.2584 0.2690 0.2247 0.0232  0.0104  -0.0306 977  ARG B CA  
16020 C C   . ARG B 979  ? 0.2509 0.2605 0.2147 0.0272  0.0116  -0.0326 977  ARG B C   
16021 O O   . ARG B 979  ? 0.2525 0.2674 0.2155 0.0292  0.0142  -0.0326 977  ARG B O   
16022 C CB  . ARG B 979  ? 0.2890 0.3022 0.2515 0.0217  0.0114  -0.0296 977  ARG B CB  
16023 C CG  . ARG B 979  ? 0.3410 0.3575 0.3069 0.0182  0.0112  -0.0271 977  ARG B CG  
16024 C CD  . ARG B 979  ? 0.4217 0.4405 0.3836 0.0164  0.0120  -0.0258 977  ARG B CD  
16025 N NE  . ARG B 979  ? 0.4375 0.4505 0.3961 0.0147  0.0095  -0.0258 977  ARG B NE  
16026 C CZ  . ARG B 979  ? 0.4505 0.4633 0.4042 0.0135  0.0096  -0.0250 977  ARG B CZ  
16027 N NH1 . ARG B 979  ? 0.4262 0.4444 0.3775 0.0139  0.0123  -0.0243 977  ARG B NH1 
16028 N NH2 . ARG B 979  ? 0.4871 0.4946 0.4385 0.0119  0.0069  -0.0249 977  ARG B NH2 
16029 N N   . LEU B 980  ? 0.2341 0.2370 0.1966 0.0284  0.0097  -0.0344 978  LEU B N   
16030 C CA  . LEU B 980  ? 0.2087 0.2085 0.1672 0.0322  0.0103  -0.0366 978  LEU B CA  
16031 C C   . LEU B 980  ? 0.2183 0.2177 0.1804 0.0342  0.0105  -0.0370 978  LEU B C   
16032 O O   . LEU B 980  ? 0.2213 0.2168 0.1863 0.0327  0.0084  -0.0369 978  LEU B O   
16033 C CB  . LEU B 980  ? 0.2377 0.2294 0.1910 0.0321  0.0077  -0.0384 978  LEU B CB  
16034 C CG  . LEU B 980  ? 0.2546 0.2460 0.2042 0.0299  0.0071  -0.0378 978  LEU B CG  
16035 C CD1 . LEU B 980  ? 0.2827 0.2660 0.2276 0.0295  0.0041  -0.0395 978  LEU B CD1 
16036 C CD2 . LEU B 980  ? 0.2648 0.2610 0.2104 0.0318  0.0100  -0.0379 978  LEU B CD2 
16037 N N   . ASP B 981  ? 0.2348 0.2383 0.1968 0.0375  0.0130  -0.0374 979  ASP B N   
16038 C CA  . ASP B 981  ? 0.2319 0.2357 0.1974 0.0396  0.0133  -0.0375 979  ASP B CA  
16039 C C   . ASP B 981  ? 0.2342 0.2290 0.1974 0.0407  0.0110  -0.0393 979  ASP B C   
16040 O O   . ASP B 981  ? 0.2409 0.2341 0.2077 0.0405  0.0100  -0.0388 979  ASP B O   
16041 C CB  . ASP B 981  ? 0.2398 0.2493 0.2048 0.0436  0.0162  -0.0378 979  ASP B CB  
16042 C CG  . ASP B 981  ? 0.2801 0.2995 0.2492 0.0421  0.0184  -0.0355 979  ASP B CG  
16043 O OD1 . ASP B 981  ? 0.2703 0.2914 0.2433 0.0383  0.0175  -0.0338 979  ASP B OD1 
16044 O OD2 . ASP B 981  ? 0.2856 0.3110 0.2541 0.0450  0.0210  -0.0355 979  ASP B OD2 
16045 N N   . GLU B 982  ? 0.2413 0.2300 0.1981 0.0420  0.0100  -0.0413 980  GLU B N   
16046 C CA  . GLU B 982  ? 0.2510 0.2307 0.2052 0.0428  0.0075  -0.0430 980  GLU B CA  
16047 C C   . GLU B 982  ? 0.2432 0.2200 0.2012 0.0386  0.0048  -0.0419 980  GLU B C   
16048 O O   . GLU B 982  ? 0.2511 0.2237 0.2109 0.0384  0.0033  -0.0420 980  GLU B O   
16049 C CB  . GLU B 982  ? 0.2718 0.2452 0.2181 0.0444  0.0067  -0.0454 980  GLU B CB  
16050 C CG  . GLU B 982  ? 0.3115 0.2749 0.2550 0.0444  0.0037  -0.0470 980  GLU B CG  
16051 C CD  . GLU B 982  ? 0.3772 0.3336 0.3128 0.0448  0.0021  -0.0492 980  GLU B CD  
16052 O OE1 . GLU B 982  ? 0.4456 0.4035 0.3798 0.0425  0.0016  -0.0488 980  GLU B OE1 
16053 O OE2 . GLU B 982  ? 0.3532 0.3023 0.2838 0.0475  0.0011  -0.0514 980  GLU B OE2 
16054 N N   . THR B 983  ? 0.2104 0.1894 0.1695 0.0353  0.0041  -0.0407 981  THR B N   
16055 C CA  . THR B 983  ? 0.2227 0.1997 0.1856 0.0316  0.0017  -0.0396 981  THR B CA  
16056 C C   . THR B 983  ? 0.2106 0.1918 0.1803 0.0307  0.0024  -0.0378 981  THR B C   
16057 O O   . THR B 983  ? 0.2136 0.1920 0.1863 0.0292  0.0007  -0.0374 981  THR B O   
16058 C CB  . THR B 983  ? 0.2386 0.2171 0.2009 0.0288  0.0009  -0.0388 981  THR B CB  
16059 O OG1 . THR B 983  ? 0.2644 0.2380 0.2201 0.0295  -0.0002 -0.0405 981  THR B OG1 
16060 C CG2 . THR B 983  ? 0.2362 0.2137 0.2031 0.0254  -0.0014 -0.0374 981  THR B CG2 
16061 N N   . ILE B 984  ? 0.1917 0.1800 0.1638 0.0316  0.0050  -0.0367 982  ILE B N   
16062 C CA  . ILE B 984  ? 0.2120 0.2042 0.1899 0.0309  0.0057  -0.0352 982  ILE B CA  
16063 C C   . ILE B 984  ? 0.2145 0.2033 0.1929 0.0331  0.0053  -0.0359 982  ILE B C   
16064 O O   . ILE B 984  ? 0.2316 0.2191 0.2137 0.0316  0.0042  -0.0350 982  ILE B O   
16065 C CB  . ILE B 984  ? 0.1863 0.1867 0.1663 0.0315  0.0083  -0.0340 982  ILE B CB  
16066 C CG1 . ILE B 984  ? 0.2373 0.2407 0.2172 0.0287  0.0084  -0.0329 982  ILE B CG1 
16067 C CG2 . ILE B 984  ? 0.2271 0.2311 0.2124 0.0312  0.0090  -0.0326 982  ILE B CG2 
16068 C CD1 . ILE B 984  ? 0.2357 0.2467 0.2165 0.0290  0.0109  -0.0317 982  ILE B CD1 
16069 N N   . ALA B 985  ? 0.2159 0.2027 0.1903 0.0367  0.0062  -0.0374 983  ALA B N   
16070 C CA  . ALA B 985  ? 0.2446 0.2275 0.2189 0.0391  0.0058  -0.0381 983  ALA B CA  
16071 C C   . ALA B 985  ? 0.2381 0.2129 0.2113 0.0372  0.0028  -0.0386 983  ALA B C   
16072 O O   . ALA B 985  ? 0.2265 0.1995 0.2026 0.0366  0.0019  -0.0379 983  ALA B O   
16073 C CB  . ALA B 985  ? 0.2481 0.2299 0.2176 0.0437  0.0072  -0.0398 983  ALA B CB  
16074 N N   . HIS B 986  ? 0.2265 0.1967 0.1956 0.0361  0.0012  -0.0399 984  HIS B N   
16075 C CA  . HIS B 986  ? 0.2559 0.2187 0.2239 0.0340  -0.0018 -0.0403 984  HIS B CA  
16076 C C   . HIS B 986  ? 0.2333 0.1985 0.2075 0.0304  -0.0028 -0.0383 984  HIS B C   
16077 O O   . HIS B 986  ? 0.2567 0.2191 0.2331 0.0296  -0.0039 -0.0378 984  HIS B O   
16078 C CB  . HIS B 986  ? 0.2229 0.1816 0.1858 0.0332  -0.0034 -0.0418 984  HIS B CB  
16079 C CG  . HIS B 986  ? 0.2746 0.2264 0.2365 0.0305  -0.0068 -0.0422 984  HIS B CG  
16080 N ND1 . HIS B 986  ? 0.3384 0.2854 0.2953 0.0297  -0.0088 -0.0436 984  HIS B ND1 
16081 C CD2 . HIS B 986  ? 0.3080 0.2573 0.2734 0.0283  -0.0086 -0.0412 984  HIS B CD2 
16082 C CE1 . HIS B 986  ? 0.3527 0.2945 0.3101 0.0270  -0.0118 -0.0435 984  HIS B CE1 
16083 N NE2 . HIS B 986  ? 0.3104 0.2537 0.2730 0.0261  -0.0117 -0.0420 984  HIS B NE2 
16084 N N   . VAL B 987  ? 0.2112 0.1816 0.1881 0.0282  -0.0023 -0.0372 985  VAL B N   
16085 C CA  . VAL B 987  ? 0.2140 0.1862 0.1962 0.0249  -0.0034 -0.0355 985  VAL B CA  
16086 C C   . VAL B 987  ? 0.2323 0.2081 0.2192 0.0251  -0.0021 -0.0341 985  VAL B C   
16087 O O   . VAL B 987  ? 0.2311 0.2055 0.2211 0.0234  -0.0033 -0.0332 985  VAL B O   
16088 C CB  . VAL B 987  ? 0.2219 0.1982 0.2052 0.0230  -0.0033 -0.0347 985  VAL B CB  
16089 C CG1 . VAL B 987  ? 0.2422 0.2214 0.2312 0.0203  -0.0038 -0.0330 985  VAL B CG1 
16090 C CG2 . VAL B 987  ? 0.2290 0.2010 0.2077 0.0223  -0.0052 -0.0359 985  VAL B CG2 
16091 N N   . THR B 988  ? 0.2262 0.2068 0.2138 0.0272  0.0002  -0.0338 986  THR B N   
16092 C CA  . THR B 988  ? 0.2084 0.1926 0.2004 0.0272  0.0013  -0.0324 986  THR B CA  
16093 C C   . THR B 988  ? 0.2337 0.2133 0.2250 0.0288  0.0006  -0.0327 986  THR B C   
16094 O O   . THR B 988  ? 0.3010 0.2816 0.2958 0.0279  0.0006  -0.0315 986  THR B O   
16095 C CB  . THR B 988  ? 0.2426 0.2336 0.2357 0.0287  0.0038  -0.0318 986  THR B CB  
16096 O OG1 . THR B 988  ? 0.2768 0.2673 0.2662 0.0322  0.0049  -0.0331 986  THR B OG1 
16097 C CG2 . THR B 988  ? 0.2746 0.2698 0.2687 0.0267  0.0043  -0.0311 986  THR B CG2 
16098 N N   . SER B 989  ? 0.2433 0.2174 0.2297 0.0310  0.0000  -0.0344 987  SER B N   
16099 C CA  . SER B 989  ? 0.2695 0.2379 0.2545 0.0324  -0.0010 -0.0347 987  SER B CA  
16100 C C   . SER B 989  ? 0.3150 0.2781 0.3007 0.0292  -0.0036 -0.0343 987  SER B C   
16101 O O   . SER B 989  ? 0.3294 0.2887 0.3154 0.0293  -0.0044 -0.0338 987  SER B O   
16102 C CB  . SER B 989  ? 0.2760 0.2396 0.2550 0.0361  -0.0009 -0.0368 987  SER B CB  
16103 O OG  . SER B 989  ? 0.3627 0.3207 0.3373 0.0352  -0.0027 -0.0383 987  SER B OG  
16104 N N   . ARG B 990  ? 0.2365 0.1995 0.2227 0.0264  -0.0049 -0.0343 988  ARG B N   
16105 C CA  . ARG B 990  ? 0.2547 0.2130 0.2414 0.0234  -0.0075 -0.0340 988  ARG B CA  
16106 C C   . ARG B 990  ? 0.2566 0.2196 0.2492 0.0202  -0.0077 -0.0321 988  ARG B C   
16107 O O   . ARG B 990  ? 0.2646 0.2253 0.2592 0.0178  -0.0093 -0.0312 988  ARG B O   
16108 C CB  . ARG B 990  ? 0.2804 0.2340 0.2626 0.0227  -0.0095 -0.0356 988  ARG B CB  
16109 C CG  . ARG B 990  ? 0.3569 0.3054 0.3325 0.0261  -0.0093 -0.0378 988  ARG B CG  
16110 C CD  . ARG B 990  ? 0.3489 0.2895 0.3216 0.0267  -0.0111 -0.0384 988  ARG B CD  
16111 N NE  . ARG B 990  ? 0.3131 0.2468 0.2824 0.0243  -0.0142 -0.0394 988  ARG B NE  
16112 C CZ  . ARG B 990  ? 0.3053 0.2308 0.2713 0.0240  -0.0164 -0.0400 988  ARG B CZ  
16113 N NH1 . ARG B 990  ? 0.3576 0.2803 0.3231 0.0259  -0.0159 -0.0397 988  ARG B NH1 
16114 N NH2 . ARG B 990  ? 0.3140 0.2338 0.2770 0.0215  -0.0194 -0.0408 988  ARG B NH2 
16115 N N   . ILE B 991  ? 0.2299 0.1993 0.2252 0.0200  -0.0061 -0.0315 989  ILE B N   
16116 C CA  . ILE B 991  ? 0.2254 0.1992 0.2259 0.0175  -0.0061 -0.0298 989  ILE B CA  
16117 C C   . ILE B 991  ? 0.2351 0.2107 0.2389 0.0175  -0.0051 -0.0285 989  ILE B C   
16118 O O   . ILE B 991  ? 0.2490 0.2247 0.2517 0.0198  -0.0038 -0.0286 989  ILE B O   
16119 C CB  . ILE B 991  ? 0.2038 0.1832 0.2056 0.0174  -0.0047 -0.0296 989  ILE B CB  
16120 C CG1 . ILE B 991  ? 0.2517 0.2341 0.2578 0.0149  -0.0052 -0.0283 989  ILE B CG1 
16121 C CG2 . ILE B 991  ? 0.2494 0.2330 0.2518 0.0194  -0.0022 -0.0292 989  ILE B CG2 
16122 C CD1 . ILE B 991  ? 0.2517 0.2312 0.2575 0.0130  -0.0077 -0.0286 989  ILE B CD1 
16123 N N   . LYS B 992  ? 0.2126 0.1895 0.2203 0.0150  -0.0058 -0.0271 990  LYS B N   
16124 C CA  . LYS B 992  ? 0.2295 0.2082 0.2403 0.0147  -0.0049 -0.0257 990  LYS B CA  
16125 C C   . LYS B 992  ? 0.2247 0.2094 0.2397 0.0135  -0.0037 -0.0245 990  LYS B C   
16126 O O   . LYS B 992  ? 0.2247 0.2105 0.2428 0.0114  -0.0044 -0.0236 990  LYS B O   
16127 C CB  . LYS B 992  ? 0.2254 0.1998 0.2365 0.0129  -0.0067 -0.0250 990  LYS B CB  
16128 C CG  . LYS B 992  ? 0.2625 0.2299 0.2687 0.0143  -0.0079 -0.0262 990  LYS B CG  
16129 C CD  . LYS B 992  ? 0.3304 0.2930 0.3367 0.0118  -0.0101 -0.0254 990  LYS B CD  
16130 C CE  . LYS B 992  ? 0.4073 0.3724 0.4174 0.0106  -0.0092 -0.0233 990  LYS B CE  
16131 N NZ  . LYS B 992  ? 0.4480 0.4097 0.4591 0.0074  -0.0113 -0.0221 990  LYS B NZ  
16132 N N   . ALA B 993  ? 0.2092 0.1977 0.2243 0.0149  -0.0020 -0.0246 991  ALA B N   
16133 C CA  . ALA B 993  ? 0.1741 0.1677 0.1925 0.0140  -0.0009 -0.0237 991  ALA B CA  
16134 C C   . ALA B 993  ? 0.1851 0.1819 0.2037 0.0154  0.0010  -0.0233 991  ALA B C   
16135 O O   . ALA B 993  ? 0.1876 0.1839 0.2038 0.0174  0.0016  -0.0240 991  ALA B O   
16136 C CB  . ALA B 993  ? 0.2032 0.1981 0.2213 0.0134  -0.0013 -0.0243 991  ALA B CB  
16137 N N   . GLY B 994  ? 0.1746 0.1749 0.1960 0.0146  0.0018  -0.0223 992  GLY B N   
16138 C CA  . GLY B 994  ? 0.1767 0.1801 0.1984 0.0156  0.0033  -0.0218 992  GLY B CA  
16139 C C   . GLY B 994  ? 0.1645 0.1709 0.1853 0.0161  0.0042  -0.0222 992  GLY B C   
16140 O O   . GLY B 994  ? 0.1494 0.1583 0.1699 0.0172  0.0052  -0.0220 992  GLY B O   
16141 N N   . ASN B 995  ? 0.1623 0.1689 0.1828 0.0152  0.0038  -0.0227 993  ASN B N   
16142 C CA  . ASN B 995  ? 0.1669 0.1763 0.1865 0.0152  0.0045  -0.0229 993  ASN B CA  
16143 C C   . ASN B 995  ? 0.1529 0.1603 0.1701 0.0152  0.0037  -0.0238 993  ASN B C   
16144 O O   . ASN B 995  ? 0.1616 0.1672 0.1790 0.0142  0.0026  -0.0239 993  ASN B O   
16145 C CB  . ASN B 995  ? 0.1603 0.1716 0.1815 0.0137  0.0047  -0.0223 993  ASN B CB  
16146 C CG  . ASN B 995  ? 0.1522 0.1661 0.1748 0.0138  0.0056  -0.0215 993  ASN B CG  
16147 O OD1 . ASN B 995  ? 0.1402 0.1537 0.1644 0.0136  0.0057  -0.0211 993  ASN B OD1 
16148 N ND2 . ASN B 995  ? 0.1709 0.1876 0.1928 0.0138  0.0064  -0.0214 993  ASN B ND2 
16149 N N   . LEU B 996  ? 0.1718 0.1799 0.1867 0.0166  0.0044  -0.0243 994  LEU B N   
16150 C CA  . LEU B 996  ? 0.1649 0.1714 0.1767 0.0170  0.0040  -0.0251 994  LEU B CA  
16151 C C   . LEU B 996  ? 0.1830 0.1930 0.1940 0.0164  0.0049  -0.0248 994  LEU B C   
16152 O O   . LEU B 996  ? 0.1619 0.1757 0.1740 0.0165  0.0060  -0.0241 994  LEU B O   
16153 C CB  . LEU B 996  ? 0.1752 0.1799 0.1846 0.0192  0.0042  -0.0261 994  LEU B CB  
16154 C CG  . LEU B 996  ? 0.1820 0.1831 0.1919 0.0199  0.0034  -0.0262 994  LEU B CG  
16155 C CD1 . LEU B 996  ? 0.1968 0.1956 0.2033 0.0226  0.0037  -0.0273 994  LEU B CD1 
16156 C CD2 . LEU B 996  ? 0.1748 0.1723 0.1853 0.0182  0.0016  -0.0263 994  LEU B CD2 
16157 N N   . TYR B 997  ? 0.1864 0.1951 0.1954 0.0156  0.0042  -0.0251 995  TYR B N   
16158 C CA  . TYR B 997  ? 0.2031 0.2146 0.2110 0.0146  0.0048  -0.0246 995  TYR B CA  
16159 C C   . TYR B 997  ? 0.1801 0.1901 0.1842 0.0152  0.0046  -0.0253 995  TYR B C   
16160 O O   . TYR B 997  ? 0.1924 0.1986 0.1952 0.0149  0.0032  -0.0260 995  TYR B O   
16161 C CB  . TYR B 997  ? 0.1712 0.1823 0.1804 0.0126  0.0040  -0.0239 995  TYR B CB  
16162 C CG  . TYR B 997  ? 0.1607 0.1726 0.1731 0.0122  0.0041  -0.0233 995  TYR B CG  
16163 C CD1 . TYR B 997  ? 0.1779 0.1875 0.1922 0.0123  0.0032  -0.0236 995  TYR B CD1 
16164 C CD2 . TYR B 997  ? 0.2095 0.2245 0.2229 0.0115  0.0050  -0.0226 995  TYR B CD2 
16165 C CE1 . TYR B 997  ? 0.2244 0.2349 0.2414 0.0120  0.0035  -0.0230 995  TYR B CE1 
16166 C CE2 . TYR B 997  ? 0.2002 0.2157 0.2160 0.0111  0.0051  -0.0222 995  TYR B CE2 
16167 C CZ  . TYR B 997  ? 0.2091 0.2224 0.2266 0.0115  0.0045  -0.0224 995  TYR B CZ  
16168 O OH  . TYR B 997  ? 0.2562 0.2702 0.2759 0.0113  0.0047  -0.0220 995  TYR B OH  
16169 N N   . ILE B 998  ? 0.1798 0.1931 0.1822 0.0159  0.0061  -0.0252 996  ILE B N   
16170 C CA  . ILE B 998  ? 0.1691 0.1817 0.1676 0.0167  0.0063  -0.0259 996  ILE B CA  
16171 C C   . ILE B 998  ? 0.1927 0.2077 0.1898 0.0148  0.0067  -0.0249 996  ILE B C   
16172 O O   . ILE B 998  ? 0.1844 0.2041 0.1827 0.0141  0.0081  -0.0238 996  ILE B O   
16173 C CB  . ILE B 998  ? 0.2138 0.2286 0.2110 0.0195  0.0080  -0.0266 996  ILE B CB  
16174 C CG1 . ILE B 998  ? 0.2306 0.2423 0.2288 0.0213  0.0075  -0.0275 996  ILE B CG1 
16175 C CG2 . ILE B 998  ? 0.2136 0.2277 0.2063 0.0205  0.0084  -0.0274 996  ILE B CG2 
16176 C CD1 . ILE B 998  ? 0.2555 0.2610 0.2521 0.0212  0.0055  -0.0285 996  ILE B CD1 
16177 N N   . ASN B 999  ? 0.1765 0.1883 0.1712 0.0137  0.0054  -0.0250 997  ASN B N   
16178 C CA  . ASN B 999  ? 0.1853 0.1986 0.1778 0.0119  0.0056  -0.0240 997  ASN B CA  
16179 C C   . ASN B 999  ? 0.1884 0.2032 0.1834 0.0096  0.0054  -0.0225 997  ASN B C   
16180 O O   . ASN B 999  ? 0.1961 0.2139 0.1901 0.0081  0.0062  -0.0213 997  ASN B O   
16181 C CB  . ASN B 999  ? 0.2094 0.2268 0.1994 0.0129  0.0076  -0.0239 997  ASN B CB  
16182 C CG  . ASN B 999  ? 0.2002 0.2150 0.1864 0.0150  0.0076  -0.0254 997  ASN B CG  
16183 O OD1 . ASN B 999  ? 0.2081 0.2180 0.1924 0.0147  0.0058  -0.0261 997  ASN B OD1 
16184 N ND2 . ASN B 999  ? 0.1941 0.2122 0.1789 0.0172  0.0096  -0.0259 997  ASN B ND2 
16185 N N   . ARG B 1000 ? 0.1813 0.1940 0.1792 0.0093  0.0043  -0.0226 998  ARG B N   
16186 C CA  . ARG B 1000 ? 0.1657 0.1789 0.1656 0.0075  0.0039  -0.0215 998  ARG B CA  
16187 C C   . ARG B 1000 ? 0.1798 0.1893 0.1816 0.0076  0.0023  -0.0220 998  ARG B C   
16188 O O   . ARG B 1000 ? 0.2046 0.2118 0.2065 0.0087  0.0015  -0.0229 998  ARG B O   
16189 C CB  . ARG B 1000 ? 0.1674 0.1847 0.1696 0.0074  0.0053  -0.0210 998  ARG B CB  
16190 C CG  . ARG B 1000 ? 0.1804 0.1984 0.1848 0.0096  0.0059  -0.0219 998  ARG B CG  
16191 C CD  . ARG B 1000 ? 0.1957 0.2164 0.2031 0.0093  0.0066  -0.0213 998  ARG B CD  
16192 N NE  . ARG B 1000 ? 0.1567 0.1750 0.1655 0.0080  0.0055  -0.0211 998  ARG B NE  
16193 C CZ  . ARG B 1000 ? 0.1883 0.2081 0.1989 0.0073  0.0057  -0.0206 998  ARG B CZ  
16194 N NH1 . ARG B 1000 ? 0.1754 0.1992 0.1870 0.0075  0.0068  -0.0202 998  ARG B NH1 
16195 N NH2 . ARG B 1000 ? 0.2031 0.2204 0.2144 0.0064  0.0048  -0.0205 998  ARG B NH2 
16196 N N   . ASN B 1001 ? 0.1630 0.1721 0.1664 0.0064  0.0018  -0.0213 999  ASN B N   
16197 C CA  . ASN B 1001 ? 0.1901 0.1966 0.1957 0.0068  0.0006  -0.0216 999  ASN B CA  
16198 C C   . ASN B 1001 ? 0.1879 0.1957 0.1966 0.0080  0.0013  -0.0222 999  ASN B C   
16199 O O   . ASN B 1001 ? 0.1811 0.1916 0.1900 0.0086  0.0027  -0.0222 999  ASN B O   
16200 C CB  . ASN B 1001 ? 0.1851 0.1905 0.1911 0.0055  0.0000  -0.0209 999  ASN B CB  
16201 C CG  . ASN B 1001 ? 0.2183 0.2262 0.2255 0.0049  0.0012  -0.0205 999  ASN B CG  
16202 O OD1 . ASN B 1001 ? 0.2262 0.2359 0.2358 0.0058  0.0020  -0.0209 999  ASN B OD1 
16203 N ND2 . ASN B 1001 ? 0.3151 0.3229 0.3205 0.0032  0.0011  -0.0197 999  ASN B ND2 
16204 N N   . ILE B 1002 ? 0.1796 0.1858 0.1906 0.0085  0.0004  -0.0225 1000 ILE B N   
16205 C CA  . ILE B 1002 ? 0.1609 0.1679 0.1745 0.0095  0.0010  -0.0228 1000 ILE B CA  
16206 C C   . ILE B 1002 ? 0.1996 0.2075 0.2157 0.0093  0.0014  -0.0224 1000 ILE B C   
16207 O O   . ILE B 1002 ? 0.2096 0.2178 0.2281 0.0098  0.0015  -0.0225 1000 ILE B O   
16208 C CB  . ILE B 1002 ? 0.1973 0.2020 0.2114 0.0100  -0.0003 -0.0234 1000 ILE B CB  
16209 C CG1 . ILE B 1002 ? 0.1719 0.1753 0.1877 0.0095  -0.0017 -0.0232 1000 ILE B CG1 
16210 C CG2 . ILE B 1002 ? 0.1871 0.1906 0.1980 0.0104  -0.0006 -0.0240 1000 ILE B CG2 
16211 C CD1 . ILE B 1002 ? 0.1759 0.1781 0.1934 0.0098  -0.0029 -0.0235 1000 ILE B CD1 
16212 N N   . ILE B 1003 ? 0.2041 0.2126 0.2196 0.0084  0.0016  -0.0220 1001 ILE B N   
16213 C CA  . ILE B 1003 ? 0.2187 0.2275 0.2360 0.0083  0.0019  -0.0218 1001 ILE B CA  
16214 C C   . ILE B 1003 ? 0.2763 0.2875 0.2933 0.0079  0.0031  -0.0215 1001 ILE B C   
16215 O O   . ILE B 1003 ? 0.2849 0.2962 0.3026 0.0076  0.0034  -0.0214 1001 ILE B O   
16216 C CB  . ILE B 1003 ? 0.2263 0.2329 0.2431 0.0080  0.0009  -0.0217 1001 ILE B CB  
16217 C CG1 . ILE B 1003 ? 0.2667 0.2721 0.2802 0.0067  0.0005  -0.0213 1001 ILE B CG1 
16218 C CG2 . ILE B 1003 ? 0.2116 0.2165 0.2294 0.0086  -0.0004 -0.0219 1001 ILE B CG2 
16219 C CD1 . ILE B 1003 ? 0.3299 0.3323 0.3425 0.0065  -0.0006 -0.0211 1001 ILE B CD1 
16220 N N   . GLY B 1004 ? 0.2331 0.2464 0.2493 0.0079  0.0038  -0.0213 1002 GLY B N   
16221 C CA  . GLY B 1004 ? 0.2531 0.2694 0.2694 0.0075  0.0048  -0.0209 1002 GLY B CA  
16222 C C   . GLY B 1004 ? 0.2801 0.2975 0.2986 0.0085  0.0054  -0.0210 1002 GLY B C   
16223 O O   . GLY B 1004 ? 0.2784 0.2956 0.2980 0.0097  0.0056  -0.0212 1002 GLY B O   
16224 N N   . ALA B 1005 ? 0.2202 0.2383 0.2390 0.0078  0.0057  -0.0207 1003 ALA B N   
16225 C CA  . ALA B 1005 ? 0.2351 0.2546 0.2555 0.0085  0.0063  -0.0205 1003 ALA B CA  
16226 C C   . ALA B 1005 ? 0.2303 0.2523 0.2500 0.0076  0.0067  -0.0200 1003 ALA B C   
16227 O O   . ALA B 1005 ? 0.2270 0.2492 0.2471 0.0075  0.0069  -0.0199 1003 ALA B O   
16228 C CB  . ALA B 1005 ? 0.2437 0.2612 0.2652 0.0089  0.0061  -0.0208 1003 ALA B CB  
16229 N N   . VAL B 1006 ? 0.1721 0.1963 0.1908 0.0068  0.0068  -0.0196 1004 VAL B N   
16230 C CA  . VAL B 1006 ? 0.1920 0.2189 0.2102 0.0055  0.0068  -0.0190 1004 VAL B CA  
16231 C C   . VAL B 1006 ? 0.1811 0.2106 0.2009 0.0066  0.0074  -0.0187 1004 VAL B C   
16232 O O   . VAL B 1006 ? 0.1660 0.1970 0.1868 0.0083  0.0079  -0.0186 1004 VAL B O   
16233 C CB  . VAL B 1006 ? 0.1730 0.2028 0.1903 0.0043  0.0069  -0.0184 1004 VAL B CB  
16234 C CG1 . VAL B 1006 ? 0.2036 0.2370 0.2209 0.0027  0.0068  -0.0175 1004 VAL B CG1 
16235 C CG2 . VAL B 1006 ? 0.1923 0.2191 0.2076 0.0028  0.0062  -0.0185 1004 VAL B CG2 
16236 N N   . VAL B 1007 ? 0.1670 0.1963 0.1864 0.0059  0.0072  -0.0186 1005 VAL B N   
16237 C CA  . VAL B 1007 ? 0.1727 0.2039 0.1932 0.0069  0.0076  -0.0182 1005 VAL B CA  
16238 C C   . VAL B 1007 ? 0.1597 0.1955 0.1811 0.0074  0.0079  -0.0174 1005 VAL B C   
16239 O O   . VAL B 1007 ? 0.1836 0.2222 0.2046 0.0060  0.0077  -0.0169 1005 VAL B O   
16240 C CB  . VAL B 1007 ? 0.1641 0.1945 0.1834 0.0058  0.0072  -0.0182 1005 VAL B CB  
16241 C CG1 . VAL B 1007 ? 0.1902 0.2226 0.2102 0.0066  0.0076  -0.0177 1005 VAL B CG1 
16242 C CG2 . VAL B 1007 ? 0.1678 0.1940 0.1864 0.0059  0.0072  -0.0191 1005 VAL B CG2 
16243 N N   . GLY B 1008 ? 0.1545 0.1912 0.1772 0.0095  0.0084  -0.0172 1006 GLY B N   
16244 C CA  . GLY B 1008 ? 0.1870 0.2280 0.2106 0.0107  0.0087  -0.0165 1006 GLY B CA  
16245 C C   . GLY B 1008 ? 0.1959 0.2387 0.2196 0.0112  0.0091  -0.0166 1006 GLY B C   
16246 O O   . GLY B 1008 ? 0.2128 0.2598 0.2374 0.0124  0.0095  -0.0161 1006 GLY B O   
16247 N N   . VAL B 1009 ? 0.1775 0.2175 0.2002 0.0104  0.0090  -0.0173 1007 VAL B N   
16248 C CA  . VAL B 1009 ? 0.1639 0.2051 0.1861 0.0109  0.0094  -0.0175 1007 VAL B CA  
16249 C C   . VAL B 1009 ? 0.1771 0.2139 0.1986 0.0124  0.0094  -0.0185 1007 VAL B C   
16250 O O   . VAL B 1009 ? 0.1703 0.2076 0.1916 0.0144  0.0099  -0.0188 1007 VAL B O   
16251 C CB  . VAL B 1009 ? 0.1645 0.2064 0.1854 0.0082  0.0091  -0.0172 1007 VAL B CB  
16252 C CG1 . VAL B 1009 ? 0.1736 0.2173 0.1937 0.0087  0.0097  -0.0172 1007 VAL B CG1 
16253 C CG2 . VAL B 1009 ? 0.1885 0.2343 0.2099 0.0063  0.0088  -0.0162 1007 VAL B CG2 
16254 N N   . GLN B 1010 ? 0.1623 0.1949 0.1835 0.0116  0.0088  -0.0190 1008 GLN B N   
16255 C CA  . GLN B 1010 ? 0.1579 0.1866 0.1791 0.0128  0.0085  -0.0197 1008 GLN B CA  
16256 C C   . GLN B 1010 ? 0.1599 0.1869 0.1823 0.0128  0.0083  -0.0195 1008 GLN B C   
16257 O O   . GLN B 1010 ? 0.1936 0.2182 0.2161 0.0118  0.0079  -0.0197 1008 GLN B O   
16258 C CB  . GLN B 1010 ? 0.1784 0.2040 0.1984 0.0119  0.0079  -0.0203 1008 GLN B CB  
16259 C CG  . GLN B 1010 ? 0.1879 0.2149 0.2063 0.0116  0.0081  -0.0203 1008 GLN B CG  
16260 C CD  . GLN B 1010 ? 0.1943 0.2226 0.2118 0.0094  0.0079  -0.0197 1008 GLN B CD  
16261 O OE1 . GLN B 1010 ? 0.2005 0.2267 0.2180 0.0081  0.0073  -0.0197 1008 GLN B OE1 
16262 N NE2 . GLN B 1010 ? 0.1651 0.1969 0.1818 0.0089  0.0085  -0.0192 1008 GLN B NE2 
16263 N N   . PRO B 1011 ? 0.1532 0.1813 0.1764 0.0141  0.0086  -0.0191 1009 PRO B N   
16264 C CA  . PRO B 1011 ? 0.1495 0.1757 0.1736 0.0142  0.0085  -0.0188 1009 PRO B CA  
16265 C C   . PRO B 1011 ? 0.1577 0.1802 0.1821 0.0141  0.0080  -0.0193 1009 PRO B C   
16266 O O   . PRO B 1011 ? 0.1648 0.1855 0.1885 0.0148  0.0077  -0.0199 1009 PRO B O   
16267 C CB  . PRO B 1011 ? 0.1616 0.1887 0.1860 0.0160  0.0088  -0.0183 1009 PRO B CB  
16268 C CG  . PRO B 1011 ? 0.1651 0.1963 0.1892 0.0165  0.0091  -0.0180 1009 PRO B CG  
16269 C CD  . PRO B 1011 ? 0.1690 0.2000 0.1922 0.0157  0.0091  -0.0187 1009 PRO B CD  
16270 N N   . PHE B 1012 ? 0.1581 0.1795 0.1832 0.0131  0.0080  -0.0193 1010 PHE B N   
16271 C CA  . PHE B 1012 ? 0.1438 0.1628 0.1695 0.0126  0.0074  -0.0197 1010 PHE B CA  
16272 C C   . PHE B 1012 ? 0.1761 0.1937 0.2032 0.0127  0.0074  -0.0193 1010 PHE B C   
16273 O O   . PHE B 1012 ? 0.1719 0.1906 0.1997 0.0126  0.0079  -0.0187 1010 PHE B O   
16274 C CB  . PHE B 1012 ? 0.1418 0.1607 0.1672 0.0115  0.0072  -0.0200 1010 PHE B CB  
16275 C CG  . PHE B 1012 ? 0.1518 0.1686 0.1779 0.0113  0.0065  -0.0205 1010 PHE B CG  
16276 C CD1 . PHE B 1012 ? 0.1927 0.2083 0.2177 0.0112  0.0058  -0.0209 1010 PHE B CD1 
16277 C CD2 . PHE B 1012 ? 0.1777 0.1942 0.2056 0.0112  0.0066  -0.0203 1010 PHE B CD2 
16278 C CE1 . PHE B 1012 ? 0.1780 0.1917 0.2036 0.0110  0.0049  -0.0212 1010 PHE B CE1 
16279 C CE2 . PHE B 1012 ? 0.2128 0.2279 0.2417 0.0111  0.0057  -0.0205 1010 PHE B CE2 
16280 C CZ  . PHE B 1012 ? 0.1842 0.1979 0.2120 0.0109  0.0048  -0.0210 1010 PHE B CZ  
16281 N N   . GLY B 1013 ? 0.1575 0.1728 0.1850 0.0128  0.0066  -0.0195 1011 GLY B N   
16282 C CA  . GLY B 1013 ? 0.1685 0.1827 0.1977 0.0124  0.0064  -0.0189 1011 GLY B CA  
16283 C C   . GLY B 1013 ? 0.1756 0.1868 0.2042 0.0127  0.0054  -0.0192 1011 GLY B C   
16284 O O   . GLY B 1013 ? 0.1613 0.1714 0.1880 0.0138  0.0053  -0.0197 1011 GLY B O   
16285 N N   . GLY B 1014 ? 0.1761 0.1860 0.2063 0.0117  0.0047  -0.0188 1012 GLY B N   
16286 C CA  . GLY B 1014 ? 0.1929 0.1994 0.2223 0.0116  0.0034  -0.0191 1012 GLY B CA  
16287 C C   . GLY B 1014 ? 0.2070 0.2116 0.2371 0.0109  0.0030  -0.0180 1012 GLY B C   
16288 O O   . GLY B 1014 ? 0.2083 0.2144 0.2393 0.0108  0.0040  -0.0170 1012 GLY B O   
16289 N N   . ARG B 1015 ? 0.1778 0.1789 0.2073 0.0102  0.0015  -0.0183 1013 ARG B N   
16290 C CA  . ARG B 1015 ? 0.2070 0.2051 0.2365 0.0093  0.0007  -0.0173 1013 ARG B CA  
16291 C C   . ARG B 1015 ? 0.2046 0.2025 0.2363 0.0071  -0.0006 -0.0169 1013 ARG B C   
16292 O O   . ARG B 1015 ? 0.1842 0.1843 0.2175 0.0066  -0.0009 -0.0173 1013 ARG B O   
16293 C CB  . ARG B 1015 ? 0.2057 0.1989 0.2316 0.0106  -0.0002 -0.0182 1013 ARG B CB  
16294 C CG  . ARG B 1015 ? 0.2320 0.2229 0.2559 0.0110  -0.0014 -0.0198 1013 ARG B CG  
16295 C CD  . ARG B 1015 ? 0.2645 0.2492 0.2851 0.0114  -0.0030 -0.0204 1013 ARG B CD  
16296 N NE  . ARG B 1015 ? 0.3147 0.2968 0.3364 0.0088  -0.0047 -0.0196 1013 ARG B NE  
16297 C CZ  . ARG B 1015 ? 0.3081 0.2903 0.3309 0.0070  -0.0061 -0.0199 1013 ARG B CZ  
16298 N NH1 . ARG B 1015 ? 0.2551 0.2392 0.2777 0.0076  -0.0060 -0.0210 1013 ARG B NH1 
16299 N NH2 . ARG B 1015 ? 0.3051 0.2857 0.3294 0.0044  -0.0077 -0.0189 1013 ARG B NH2 
16300 N N   . GLY B 1016 ? 0.2015 0.1967 0.2334 0.0056  -0.0016 -0.0158 1014 GLY B N   
16301 C CA  . GLY B 1016 ? 0.1957 0.1911 0.2300 0.0032  -0.0030 -0.0151 1014 GLY B CA  
16302 C C   . GLY B 1016 ? 0.1998 0.2013 0.2384 0.0023  -0.0018 -0.0141 1014 GLY B C   
16303 O O   . GLY B 1016 ? 0.2033 0.2076 0.2428 0.0027  0.0000  -0.0132 1014 GLY B O   
16304 N N   . LEU B 1017 ? 0.1948 0.1982 0.2356 0.0014  -0.0027 -0.0144 1015 LEU B N   
16305 C CA  . LEU B 1017 ? 0.1883 0.1974 0.2330 0.0011  -0.0016 -0.0136 1015 LEU B CA  
16306 C C   . LEU B 1017 ? 0.1810 0.1926 0.2251 0.0033  0.0002  -0.0145 1015 LEU B C   
16307 O O   . LEU B 1017 ? 0.1911 0.2070 0.2379 0.0035  0.0013  -0.0141 1015 LEU B O   
16308 C CB  . LEU B 1017 ? 0.2032 0.2137 0.2504 -0.0001 -0.0034 -0.0137 1015 LEU B CB  
16309 C CG  . LEU B 1017 ? 0.2242 0.2330 0.2725 -0.0028 -0.0053 -0.0126 1015 LEU B CG  
16310 C CD1 . LEU B 1017 ? 0.2371 0.2472 0.2876 -0.0039 -0.0074 -0.0128 1015 LEU B CD1 
16311 C CD2 . LEU B 1017 ? 0.2333 0.2457 0.2849 -0.0044 -0.0041 -0.0105 1015 LEU B CD2 
16312 N N   . SER B 1018 ? 0.1649 0.1739 0.2055 0.0049  0.0004  -0.0157 1016 SER B N   
16313 C CA  . SER B 1018 ? 0.1733 0.1843 0.2131 0.0065  0.0018  -0.0165 1016 SER B CA  
16314 C C   . SER B 1018 ? 0.1497 0.1620 0.1888 0.0073  0.0035  -0.0160 1016 SER B C   
16315 O O   . SER B 1018 ? 0.1780 0.1922 0.2167 0.0083  0.0046  -0.0165 1016 SER B O   
16316 C CB  . SER B 1018 ? 0.1760 0.1843 0.2126 0.0076  0.0011  -0.0180 1016 SER B CB  
16317 O OG  . SER B 1018 ? 0.1910 0.1983 0.2280 0.0070  -0.0006 -0.0185 1016 SER B OG  
16318 N N   . GLY B 1019 ? 0.1612 0.1721 0.1998 0.0068  0.0037  -0.0150 1017 GLY B N   
16319 C CA  . GLY B 1019 ? 0.1791 0.1913 0.2169 0.0076  0.0052  -0.0145 1017 GLY B CA  
16320 C C   . GLY B 1019 ? 0.1792 0.1893 0.2160 0.0072  0.0052  -0.0133 1017 GLY B C   
16321 O O   . GLY B 1019 ? 0.1943 0.2007 0.2301 0.0067  0.0038  -0.0132 1017 GLY B O   
16322 N N   . THR B 1020 ? 0.1781 0.1902 0.2149 0.0074  0.0065  -0.0123 1018 THR B N   
16323 C CA  . THR B 1020 ? 0.1779 0.1880 0.2131 0.0074  0.0066  -0.0111 1018 THR B CA  
16324 C C   . THR B 1020 ? 0.1758 0.1848 0.2083 0.0094  0.0067  -0.0119 1018 THR B C   
16325 O O   . THR B 1020 ? 0.1967 0.2027 0.2274 0.0101  0.0062  -0.0113 1018 THR B O   
16326 C CB  . THR B 1020 ? 0.1775 0.1906 0.2138 0.0067  0.0080  -0.0096 1018 THR B CB  
16327 O OG1 . THR B 1020 ? 0.1701 0.1865 0.2061 0.0078  0.0093  -0.0104 1018 THR B OG1 
16328 C CG2 . THR B 1020 ? 0.1882 0.2033 0.2275 0.0047  0.0081  -0.0085 1018 THR B CG2 
16329 N N   . GLY B 1021 ? 0.1737 0.1850 0.2060 0.0104  0.0073  -0.0131 1019 GLY B N   
16330 C CA  . GLY B 1021 ? 0.1786 0.1906 0.2090 0.0120  0.0077  -0.0134 1019 GLY B CA  
16331 C C   . GLY B 1021 ? 0.1618 0.1757 0.1919 0.0119  0.0087  -0.0122 1019 GLY B C   
16332 O O   . GLY B 1021 ? 0.1648 0.1795 0.1961 0.0107  0.0092  -0.0111 1019 GLY B O   
16333 N N   . PRO B 1022 ? 0.1619 0.1769 0.1905 0.0131  0.0089  -0.0122 1020 PRO B N   
16334 C CA  . PRO B 1022 ? 0.1500 0.1654 0.1776 0.0145  0.0086  -0.0133 1020 PRO B CA  
16335 C C   . PRO B 1022 ? 0.1740 0.1916 0.2021 0.0140  0.0089  -0.0145 1020 PRO B C   
16336 O O   . PRO B 1022 ? 0.1816 0.2004 0.2105 0.0130  0.0094  -0.0146 1020 PRO B O   
16337 C CB  . PRO B 1022 ? 0.1725 0.1896 0.1989 0.0155  0.0088  -0.0125 1020 PRO B CB  
16338 C CG  . PRO B 1022 ? 0.1672 0.1859 0.1938 0.0144  0.0096  -0.0116 1020 PRO B CG  
16339 C CD  . PRO B 1022 ? 0.1747 0.1914 0.2026 0.0131  0.0096  -0.0110 1020 PRO B CD  
16340 N N   . LYS B 1023 ? 0.1701 0.1880 0.1975 0.0149  0.0085  -0.0155 1021 LYS B N   
16341 C CA  . LYS B 1023 ? 0.1651 0.1843 0.1925 0.0142  0.0086  -0.0165 1021 LYS B CA  
16342 C C   . LYS B 1023 ? 0.1570 0.1790 0.1841 0.0137  0.0092  -0.0164 1021 LYS B C   
16343 O O   . LYS B 1023 ? 0.1553 0.1792 0.1817 0.0142  0.0093  -0.0159 1021 LYS B O   
16344 C CB  . LYS B 1023 ? 0.1396 0.1590 0.1661 0.0152  0.0083  -0.0173 1021 LYS B CB  
16345 C CG  . LYS B 1023 ? 0.1487 0.1650 0.1749 0.0157  0.0076  -0.0179 1021 LYS B CG  
16346 C CD  . LYS B 1023 ? 0.1376 0.1547 0.1624 0.0170  0.0076  -0.0186 1021 LYS B CD  
16347 C CE  . LYS B 1023 ? 0.1609 0.1750 0.1846 0.0174  0.0069  -0.0196 1021 LYS B CE  
16348 N NZ  . LYS B 1023 ? 0.1477 0.1616 0.1717 0.0159  0.0065  -0.0201 1021 LYS B NZ  
16349 N N   . ALA B 1024 ? 0.1747 0.1967 0.2021 0.0127  0.0094  -0.0169 1022 ALA B N   
16350 C CA  . ALA B 1024 ? 0.1793 0.2029 0.2056 0.0121  0.0096  -0.0172 1022 ALA B CA  
16351 C C   . ALA B 1024 ? 0.1632 0.1881 0.1885 0.0121  0.0092  -0.0176 1022 ALA B C   
16352 O O   . ALA B 1024 ? 0.1701 0.1944 0.1956 0.0124  0.0089  -0.0180 1022 ALA B O   
16353 C CB  . ALA B 1024 ? 0.1917 0.2144 0.2182 0.0115  0.0098  -0.0179 1022 ALA B CB  
16354 N N   . GLY B 1025 ? 0.1422 0.1692 0.1665 0.0115  0.0092  -0.0174 1023 GLY B N   
16355 C CA  . GLY B 1025 ? 0.1513 0.1803 0.1749 0.0111  0.0089  -0.0175 1023 GLY B CA  
16356 C C   . GLY B 1025 ? 0.1449 0.1756 0.1691 0.0125  0.0089  -0.0170 1023 GLY B C   
16357 O O   . GLY B 1025 ? 0.1528 0.1855 0.1769 0.0125  0.0088  -0.0171 1023 GLY B O   
16358 N N   . GLY B 1026 ? 0.1557 0.1858 0.1805 0.0138  0.0091  -0.0164 1024 GLY B N   
16359 C CA  . GLY B 1026 ? 0.1527 0.1838 0.1778 0.0156  0.0090  -0.0160 1024 GLY B CA  
16360 C C   . GLY B 1026 ? 0.1504 0.1830 0.1755 0.0163  0.0090  -0.0149 1024 GLY B C   
16361 O O   . GLY B 1026 ? 0.1540 0.1863 0.1787 0.0153  0.0091  -0.0145 1024 GLY B O   
16362 N N   . PRO B 1027 ? 0.1779 0.2117 0.2032 0.0182  0.0089  -0.0144 1025 PRO B N   
16363 C CA  . PRO B 1027 ? 0.1413 0.1772 0.1666 0.0191  0.0087  -0.0132 1025 PRO B CA  
16364 C C   . PRO B 1027 ? 0.1709 0.2035 0.1956 0.0197  0.0086  -0.0124 1025 PRO B C   
16365 O O   . PRO B 1027 ? 0.1649 0.1989 0.1893 0.0202  0.0083  -0.0113 1025 PRO B O   
16366 C CB  . PRO B 1027 ? 0.1571 0.1958 0.1829 0.0212  0.0086  -0.0131 1025 PRO B CB  
16367 C CG  . PRO B 1027 ? 0.1776 0.2134 0.2032 0.0221  0.0089  -0.0142 1025 PRO B CG  
16368 C CD  . PRO B 1027 ? 0.1748 0.2091 0.2003 0.0197  0.0090  -0.0150 1025 PRO B CD  
16369 N N   . LEU B 1028 ? 0.1591 0.1875 0.1838 0.0196  0.0086  -0.0128 1026 LEU B N   
16370 C CA  . LEU B 1028 ? 0.1764 0.2017 0.2007 0.0196  0.0085  -0.0118 1026 LEU B CA  
16371 C C   . LEU B 1028 ? 0.1768 0.2020 0.2010 0.0176  0.0090  -0.0115 1026 LEU B C   
16372 O O   . LEU B 1028 ? 0.1876 0.2112 0.2115 0.0173  0.0091  -0.0104 1026 LEU B O   
16373 C CB  . LEU B 1028 ? 0.1639 0.1848 0.1881 0.0202  0.0082  -0.0121 1026 LEU B CB  
16374 C CG  . LEU B 1028 ? 0.2140 0.2340 0.2376 0.0226  0.0078  -0.0126 1026 LEU B CG  
16375 C CD1 . LEU B 1028 ? 0.2421 0.2568 0.2650 0.0229  0.0072  -0.0131 1026 LEU B CD1 
16376 C CD2 . LEU B 1028 ? 0.2640 0.2848 0.2869 0.0245  0.0075  -0.0113 1026 LEU B CD2 
16377 N N   . TYR B 1029 ? 0.1502 0.1772 0.1747 0.0163  0.0094  -0.0124 1027 TYR B N   
16378 C CA  . TYR B 1029 ? 0.1610 0.1874 0.1855 0.0148  0.0100  -0.0125 1027 TYR B CA  
16379 C C   . TYR B 1029 ? 0.1445 0.1720 0.1678 0.0144  0.0103  -0.0115 1027 TYR B C   
16380 O O   . TYR B 1029 ? 0.1562 0.1825 0.1795 0.0139  0.0109  -0.0108 1027 TYR B O   
16381 C CB  . TYR B 1029 ? 0.1614 0.1889 0.1859 0.0138  0.0101  -0.0138 1027 TYR B CB  
16382 C CG  . TYR B 1029 ? 0.1687 0.1952 0.1935 0.0128  0.0106  -0.0144 1027 TYR B CG  
16383 C CD1 . TYR B 1029 ? 0.1493 0.1738 0.1755 0.0127  0.0107  -0.0146 1027 TYR B CD1 
16384 C CD2 . TYR B 1029 ? 0.1946 0.2220 0.2180 0.0120  0.0110  -0.0148 1027 TYR B CD2 
16385 C CE1 . TYR B 1029 ? 0.1610 0.1852 0.1879 0.0120  0.0112  -0.0151 1027 TYR B CE1 
16386 C CE2 . TYR B 1029 ? 0.1871 0.2135 0.2106 0.0116  0.0116  -0.0154 1027 TYR B CE2 
16387 C CZ  . TYR B 1029 ? 0.1820 0.2073 0.2076 0.0117  0.0117  -0.0155 1027 TYR B CZ  
16388 O OH  . TYR B 1029 ? 0.1786 0.2036 0.2046 0.0115  0.0123  -0.0161 1027 TYR B OH  
16389 N N   . LEU B 1030 ? 0.1604 0.1905 0.1826 0.0145  0.0099  -0.0113 1028 LEU B N   
16390 C CA  . LEU B 1030 ? 0.1866 0.2177 0.2071 0.0140  0.0101  -0.0104 1028 LEU B CA  
16391 C C   . LEU B 1030 ? 0.1970 0.2267 0.2171 0.0148  0.0101  -0.0088 1028 LEU B C   
16392 O O   . LEU B 1030 ? 0.1800 0.2094 0.1988 0.0142  0.0106  -0.0080 1028 LEU B O   
16393 C CB  . LEU B 1030 ? 0.1702 0.2044 0.1897 0.0139  0.0093  -0.0104 1028 LEU B CB  
16394 C CG  . LEU B 1030 ? 0.1857 0.2210 0.2048 0.0126  0.0092  -0.0118 1028 LEU B CG  
16395 C CD1 . LEU B 1030 ? 0.2227 0.2612 0.2407 0.0120  0.0082  -0.0114 1028 LEU B CD1 
16396 C CD2 . LEU B 1030 ? 0.1970 0.2304 0.2147 0.0115  0.0099  -0.0126 1028 LEU B CD2 
16397 N N   . GLY B 1031 ? 0.1918 0.2204 0.2127 0.0162  0.0095  -0.0083 1029 GLY B N   
16398 C CA  . GLY B 1031 ? 0.2024 0.2290 0.2226 0.0170  0.0092  -0.0066 1029 GLY B CA  
16399 C C   . GLY B 1031 ? 0.1835 0.2073 0.2038 0.0158  0.0099  -0.0060 1029 GLY B C   
16400 O O   . GLY B 1031 ? 0.2061 0.2283 0.2253 0.0159  0.0098  -0.0043 1029 GLY B O   
16401 N N   . ARG B 1032 ? 0.1744 0.1977 0.1960 0.0148  0.0105  -0.0071 1030 ARG B N   
16402 C CA  . ARG B 1032 ? 0.1719 0.1938 0.1942 0.0135  0.0112  -0.0064 1030 ARG B CA  
16403 C C   . ARG B 1032 ? 0.1837 0.2076 0.2050 0.0125  0.0124  -0.0059 1030 ARG B C   
16404 O O   . ARG B 1032 ? 0.1940 0.2175 0.2156 0.0115  0.0132  -0.0049 1030 ARG B O   
16405 C CB  . ARG B 1032 ? 0.1831 0.2043 0.2075 0.0129  0.0114  -0.0077 1030 ARG B CB  
16406 C CG  . ARG B 1032 ? 0.1862 0.2061 0.2119 0.0116  0.0118  -0.0069 1030 ARG B CG  
16407 C CD  . ARG B 1032 ? 0.2030 0.2192 0.2286 0.0116  0.0108  -0.0057 1030 ARG B CD  
16408 N NE  . ARG B 1032 ? 0.2175 0.2326 0.2447 0.0099  0.0109  -0.0050 1030 ARG B NE  
16409 C CZ  . ARG B 1032 ? 0.2149 0.2285 0.2417 0.0087  0.0110  -0.0030 1030 ARG B CZ  
16410 N NH1 . ARG B 1032 ? 0.2345 0.2472 0.2591 0.0091  0.0109  -0.0015 1030 ARG B NH1 
16411 N NH2 . ARG B 1032 ? 0.2376 0.2508 0.2664 0.0068  0.0110  -0.0023 1030 ARG B NH2 
16412 N N   . LEU B 1033 ? 0.1781 0.2042 0.1979 0.0127  0.0125  -0.0066 1031 LEU B N   
16413 C CA  . LEU B 1033 ? 0.1828 0.2106 0.2011 0.0120  0.0136  -0.0067 1031 LEU B CA  
16414 C C   . LEU B 1033 ? 0.2054 0.2339 0.2209 0.0121  0.0134  -0.0053 1031 LEU B C   
16415 O O   . LEU B 1033 ? 0.2062 0.2360 0.2195 0.0117  0.0140  -0.0056 1031 LEU B O   
16416 C CB  . LEU B 1033 ? 0.1742 0.2032 0.1921 0.0118  0.0136  -0.0086 1031 LEU B CB  
16417 C CG  . LEU B 1033 ? 0.1586 0.1867 0.1789 0.0118  0.0135  -0.0099 1031 LEU B CG  
16418 C CD1 . LEU B 1033 ? 0.1873 0.2161 0.2069 0.0117  0.0133  -0.0117 1031 LEU B CD1 
16419 C CD2 . LEU B 1033 ? 0.1879 0.2156 0.2101 0.0113  0.0145  -0.0096 1031 LEU B CD2 
16420 N N   . VAL B 1034 ? 0.1939 0.2212 0.2092 0.0128  0.0124  -0.0039 1032 VAL B N   
16421 C CA  . VAL B 1034 ? 0.2228 0.2504 0.2356 0.0131  0.0120  -0.0022 1032 VAL B CA  
16422 C C   . VAL B 1034 ? 0.2522 0.2770 0.2652 0.0131  0.0118  -0.0002 1032 VAL B C   
16423 O O   . VAL B 1034 ? 0.2293 0.2519 0.2443 0.0132  0.0116  -0.0003 1032 VAL B O   
16424 C CB  . VAL B 1034 ? 0.1982 0.2274 0.2104 0.0143  0.0105  -0.0023 1032 VAL B CB  
16425 C CG1 . VAL B 1034 ? 0.2085 0.2403 0.2198 0.0136  0.0105  -0.0039 1032 VAL B CG1 
16426 C CG2 . VAL B 1034 ? 0.2013 0.2295 0.2156 0.0156  0.0096  -0.0027 1032 VAL B CG2 
16427 N N   . THR B 1035 ? 0.2359 0.2604 0.2464 0.0130  0.0118  0.0018  1033 THR B N   
16428 C CA  . THR B 1035 ? 0.2464 0.2678 0.2566 0.0127  0.0115  0.0039  1033 THR B CA  
16429 C C   . THR B 1035 ? 0.2707 0.2894 0.2810 0.0145  0.0098  0.0046  1033 THR B C   
16430 O O   . THR B 1035 ? 0.2902 0.3050 0.3005 0.0143  0.0093  0.0058  1033 THR B O   
16431 C CB  . THR B 1035 ? 0.3082 0.3299 0.3154 0.0117  0.0122  0.0060  1033 THR B CB  
16432 O OG1 . THR B 1035 ? 0.3789 0.4026 0.3837 0.0127  0.0114  0.0060  1033 THR B OG1 
16433 C CG2 . THR B 1035 ? 0.3191 0.3430 0.3264 0.0101  0.0143  0.0055  1033 THR B CG2 
16434 N N   . THR B 1036 ? 0.2436 0.2643 0.2537 0.0161  0.0088  0.0037  1034 THR B N   
16435 C CA  . THR B 1036 ? 0.2524 0.2714 0.2629 0.0184  0.0073  0.0040  1034 THR B CA  
16436 C C   . THR B 1036 ? 0.2625 0.2841 0.2751 0.0194  0.0071  0.0018  1034 THR B C   
16437 O O   . THR B 1036 ? 0.2258 0.2514 0.2384 0.0192  0.0071  0.0010  1034 THR B O   
16438 C CB  . THR B 1036 ? 0.3126 0.3320 0.3208 0.0198  0.0061  0.0058  1034 THR B CB  
16439 O OG1 . THR B 1036 ? 0.3840 0.4011 0.3899 0.0186  0.0063  0.0080  1034 THR B OG1 
16440 C CG2 . THR B 1036 ? 0.3381 0.3554 0.3468 0.0226  0.0046  0.0061  1034 THR B CG2 
16441 N N   . ALA B 1037 ? 0.2455 0.2648 0.2598 0.0202  0.0069  0.0008  1035 ALA B N   
16442 C CA  . ALA B 1037 ? 0.2260 0.2478 0.2422 0.0209  0.0069  -0.0012 1035 ALA B CA  
16443 C C   . ALA B 1037 ? 0.2374 0.2619 0.2537 0.0232  0.0059  -0.0011 1035 ALA B C   
16444 O O   . ALA B 1037 ? 0.2458 0.2684 0.2612 0.0252  0.0050  0.0001  1035 ALA B O   
16445 C CB  . ALA B 1037 ? 0.2504 0.2688 0.2679 0.0211  0.0070  -0.0023 1035 ALA B CB  
16446 N N   . PRO B 1038 ? 0.1827 0.2118 0.2001 0.0229  0.0060  -0.0023 1036 PRO B N   
16447 C CA  . PRO B 1038 ? 0.1931 0.2259 0.2114 0.0251  0.0051  -0.0022 1036 PRO B CA  
16448 C C   . PRO B 1038 ? 0.2049 0.2366 0.2246 0.0270  0.0052  -0.0033 1036 PRO B C   
16449 O O   . PRO B 1038 ? 0.2149 0.2433 0.2349 0.0264  0.0058  -0.0044 1036 PRO B O   
16450 C CB  . PRO B 1038 ? 0.2057 0.2434 0.2245 0.0233  0.0053  -0.0031 1036 PRO B CB  
16451 C CG  . PRO B 1038 ? 0.2121 0.2479 0.2311 0.0212  0.0064  -0.0045 1036 PRO B CG  
16452 C CD  . PRO B 1038 ? 0.1942 0.2253 0.2122 0.0207  0.0069  -0.0037 1036 PRO B CD  
16453 N N   . VAL B 1039 ? 0.2227 0.2576 0.2432 0.0295  0.0045  -0.0031 1037 VAL B N   
16454 C CA  . VAL B 1039 ? 0.2016 0.2370 0.2233 0.0316  0.0047  -0.0043 1037 VAL B CA  
16455 C C   . VAL B 1039 ? 0.2004 0.2405 0.2238 0.0299  0.0054  -0.0056 1037 VAL B C   
16456 O O   . VAL B 1039 ? 0.1890 0.2347 0.2134 0.0294  0.0050  -0.0052 1037 VAL B O   
16457 C CB  . VAL B 1039 ? 0.2201 0.2577 0.2422 0.0353  0.0039  -0.0033 1037 VAL B CB  
16458 C CG1 . VAL B 1039 ? 0.2345 0.2722 0.2575 0.0378  0.0044  -0.0047 1037 VAL B CG1 
16459 C CG2 . VAL B 1039 ? 0.2293 0.2616 0.2492 0.0367  0.0030  -0.0018 1037 VAL B CG2 
16460 N N   . PRO B 1040 ? 0.1956 0.2336 0.2194 0.0288  0.0061  -0.0071 1038 PRO B N   
16461 C CA  . PRO B 1040 ? 0.1879 0.2298 0.2128 0.0269  0.0067  -0.0082 1038 PRO B CA  
16462 C C   . PRO B 1040 ? 0.1862 0.2334 0.2126 0.0288  0.0066  -0.0083 1038 PRO B C   
16463 O O   . PRO B 1040 ? 0.1894 0.2365 0.2160 0.0320  0.0065  -0.0080 1038 PRO B O   
16464 C CB  . PRO B 1040 ? 0.2056 0.2431 0.2303 0.0259  0.0073  -0.0095 1038 PRO B CB  
16465 C CG  . PRO B 1040 ? 0.2162 0.2481 0.2396 0.0261  0.0071  -0.0089 1038 PRO B CG  
16466 C CD  . PRO B 1040 ? 0.2180 0.2497 0.2408 0.0287  0.0064  -0.0077 1038 PRO B CD  
16467 N N   . PRO B 1041 ? 0.1781 0.2301 0.2057 0.0269  0.0068  -0.0086 1039 PRO B N   
16468 C CA  . PRO B 1041 ? 0.1795 0.2373 0.2088 0.0282  0.0070  -0.0087 1039 PRO B CA  
16469 C C   . PRO B 1041 ? 0.2095 0.2650 0.2387 0.0305  0.0078  -0.0098 1039 PRO B C   
16470 O O   . PRO B 1041 ? 0.2062 0.2568 0.2344 0.0295  0.0082  -0.0109 1039 PRO B O   
16471 C CB  . PRO B 1041 ? 0.2204 0.2816 0.2502 0.0247  0.0071  -0.0090 1039 PRO B CB  
16472 C CG  . PRO B 1041 ? 0.2046 0.2628 0.2329 0.0222  0.0066  -0.0089 1039 PRO B CG  
16473 C CD  . PRO B 1041 ? 0.2155 0.2674 0.2425 0.0233  0.0068  -0.0091 1039 PRO B CD  
16474 N N   . GLN B 1042 ? 0.1963 0.2555 0.2266 0.0336  0.0080  -0.0095 1040 GLN B N   
16475 C CA  . GLN B 1042 ? 0.2170 0.2749 0.2469 0.0364  0.0088  -0.0106 1040 GLN B CA  
16476 C C   . GLN B 1042 ? 0.1898 0.2392 0.2173 0.0379  0.0086  -0.0113 1040 GLN B C   
16477 O O   . GLN B 1042 ? 0.1933 0.2400 0.2197 0.0397  0.0091  -0.0125 1040 GLN B O   
16478 C CB  . GLN B 1042 ? 0.2481 0.3076 0.2782 0.0343  0.0097  -0.0117 1040 GLN B CB  
16479 C CG  . GLN B 1042 ? 0.2624 0.3301 0.2946 0.0324  0.0099  -0.0109 1040 GLN B CG  
16480 C CD  . GLN B 1042 ? 0.3209 0.3891 0.3529 0.0299  0.0106  -0.0118 1040 GLN B CD  
16481 O OE1 . GLN B 1042 ? 0.4106 0.4731 0.4410 0.0281  0.0106  -0.0128 1040 GLN B OE1 
16482 N NE2 . GLN B 1042 ? 0.4053 0.4805 0.4389 0.0297  0.0112  -0.0114 1040 GLN B NE2 
16483 N N   . HIS B 1043 ? 0.1904 0.2354 0.2169 0.0372  0.0078  -0.0105 1041 HIS B N   
16484 C CA  . HIS B 1043 ? 0.1849 0.2217 0.2092 0.0377  0.0074  -0.0110 1041 HIS B CA  
16485 C C   . HIS B 1043 ? 0.2064 0.2407 0.2295 0.0419  0.0069  -0.0105 1041 HIS B C   
16486 O O   . HIS B 1043 ? 0.2255 0.2582 0.2480 0.0425  0.0061  -0.0092 1041 HIS B O   
16487 C CB  . HIS B 1043 ? 0.1852 0.2190 0.2090 0.0347  0.0070  -0.0102 1041 HIS B CB  
16488 C CG  . HIS B 1043 ? 0.1859 0.2119 0.2079 0.0345  0.0066  -0.0104 1041 HIS B CG  
16489 N ND1 . HIS B 1043 ? 0.1922 0.2146 0.2137 0.0326  0.0068  -0.0116 1041 HIS B ND1 
16490 C CD2 . HIS B 1043 ? 0.2224 0.2435 0.2427 0.0357  0.0058  -0.0094 1041 HIS B CD2 
16491 C CE1 . HIS B 1043 ? 0.2241 0.2402 0.2441 0.0326  0.0062  -0.0113 1041 HIS B CE1 
16492 N NE2 . HIS B 1043 ? 0.2106 0.2256 0.2298 0.0343  0.0056  -0.0100 1041 HIS B NE2 
16493 N N   . SER B 1044 ? 0.1744 0.2078 0.1967 0.0448  0.0073  -0.0118 1042 SER B N   
16494 C CA  . SER B 1044 ? 0.1765 0.2062 0.1969 0.0491  0.0068  -0.0117 1042 SER B CA  
16495 C C   . SER B 1044 ? 0.1876 0.2142 0.2063 0.0512  0.0074  -0.0136 1042 SER B C   
16496 O O   . SER B 1044 ? 0.2033 0.2320 0.2225 0.0496  0.0083  -0.0148 1042 SER B O   
16497 C CB  . SER B 1044 ? 0.1857 0.2221 0.2079 0.0521  0.0068  -0.0105 1042 SER B CB  
16498 O OG  . SER B 1044 ? 0.1993 0.2429 0.2234 0.0533  0.0080  -0.0112 1042 SER B OG  
16499 N N   . SER B 1045 ? 0.2021 0.2232 0.2182 0.0551  0.0068  -0.0140 1043 SER B N   
16500 C CA  . SER B 1045 ? 0.2024 0.2198 0.2159 0.0577  0.0072  -0.0159 1043 SER B CA  
16501 C C   . SER B 1045 ? 0.1957 0.2111 0.2074 0.0633  0.0069  -0.0159 1043 SER B C   
16502 O O   . SER B 1045 ? 0.2070 0.2185 0.2177 0.0643  0.0056  -0.0146 1043 SER B O   
16503 C CB  . SER B 1045 ? 0.1945 0.2026 0.2051 0.0554  0.0064  -0.0170 1043 SER B CB  
16504 O OG  . SER B 1045 ? 0.2064 0.2103 0.2139 0.0581  0.0066  -0.0190 1043 SER B OG  
16505 N N   . VAL B 1046 ? 0.2094 0.2274 0.2204 0.0671  0.0080  -0.0174 1044 VAL B N   
16506 C CA  . VAL B 1046 ? 0.2205 0.2360 0.2293 0.0730  0.0077  -0.0177 1044 VAL B CA  
16507 C C   . VAL B 1046 ? 0.2313 0.2348 0.2347 0.0746  0.0067  -0.0193 1044 VAL B C   
16508 O O   . VAL B 1046 ? 0.2316 0.2309 0.2322 0.0796  0.0062  -0.0198 1044 VAL B O   
16509 C CB  . VAL B 1046 ? 0.2318 0.2561 0.2422 0.0769  0.0096  -0.0184 1044 VAL B CB  
16510 C CG1 . VAL B 1046 ? 0.2508 0.2871 0.2666 0.0749  0.0104  -0.0166 1044 VAL B CG1 
16511 C CG2 . VAL B 1046 ? 0.2294 0.2524 0.2377 0.0766  0.0108  -0.0207 1044 VAL B CG2 
16512 N N   . HIS B 1047 ? 0.2392 0.2370 0.2411 0.0705  0.0062  -0.0201 1045 HIS B N   
16513 C CA  . HIS B 1047 ? 0.2517 0.2383 0.2484 0.0714  0.0050  -0.0217 1045 HIS B CA  
16514 C C   . HIS B 1047 ? 0.2381 0.2164 0.2332 0.0695  0.0029  -0.0203 1045 HIS B C   
16515 O O   . HIS B 1047 ? 0.2494 0.2302 0.2473 0.0656  0.0026  -0.0184 1045 HIS B O   
16516 C CB  . HIS B 1047 ? 0.2956 0.2811 0.2916 0.0680  0.0054  -0.0233 1045 HIS B CB  
16517 C CG  . HIS B 1047 ? 0.3234 0.3173 0.3209 0.0694  0.0075  -0.0244 1045 HIS B CG  
16518 N ND1 . HIS B 1047 ? 0.3384 0.3333 0.3337 0.0748  0.0085  -0.0259 1045 HIS B ND1 
16519 C CD2 . HIS B 1047 ? 0.3332 0.3353 0.3342 0.0662  0.0088  -0.0241 1045 HIS B CD2 
16520 C CE1 . HIS B 1047 ? 0.3641 0.3677 0.3616 0.0746  0.0104  -0.0263 1045 HIS B CE1 
16521 N NE2 . HIS B 1047 ? 0.3079 0.3158 0.3089 0.0693  0.0105  -0.0252 1045 HIS B NE2 
16522 N N   . THR B 1048 ? 0.2314 0.1997 0.2216 0.0725  0.0015  -0.0211 1046 THR B N   
16523 C CA  . THR B 1048 ? 0.2460 0.2053 0.2339 0.0708  -0.0006 -0.0197 1046 THR B CA  
16524 C C   . THR B 1048 ? 0.2349 0.1838 0.2183 0.0689  -0.0020 -0.0213 1046 THR B C   
16525 O O   . THR B 1048 ? 0.2603 0.2046 0.2398 0.0722  -0.0021 -0.0235 1046 THR B O   
16526 C CB  . THR B 1048 ? 0.2956 0.2512 0.2812 0.0760  -0.0016 -0.0188 1046 THR B CB  
16527 O OG1 . THR B 1048 ? 0.2727 0.2388 0.2624 0.0783  -0.0003 -0.0175 1046 THR B OG1 
16528 C CG2 . THR B 1048 ? 0.2931 0.2405 0.2769 0.0734  -0.0037 -0.0168 1046 THR B CG2 
16529 N N   . ASP B 1049 ? 0.2433 0.1887 0.2273 0.0636  -0.0032 -0.0201 1047 ASP B N   
16530 C CA  . ASP B 1049 ? 0.2544 0.1905 0.2347 0.0611  -0.0047 -0.0213 1047 ASP B CA  
16531 C C   . ASP B 1049 ? 0.2479 0.1726 0.2221 0.0648  -0.0066 -0.0221 1047 ASP B C   
16532 O O   . ASP B 1049 ? 0.2887 0.2100 0.2619 0.0663  -0.0076 -0.0203 1047 ASP B O   
16533 C CB  . ASP B 1049 ? 0.2488 0.1841 0.2314 0.0549  -0.0056 -0.0194 1047 ASP B CB  
16534 C CG  . ASP B 1049 ? 0.2451 0.1719 0.2246 0.0518  -0.0073 -0.0205 1047 ASP B CG  
16535 O OD1 . ASP B 1049 ? 0.2802 0.1969 0.2553 0.0521  -0.0094 -0.0203 1047 ASP B OD1 
16536 O OD2 . ASP B 1049 ? 0.2519 0.1821 0.2331 0.0491  -0.0067 -0.0216 1047 ASP B OD2 
16537 N N   . PRO B 1050 ? 0.2729 0.1910 0.2425 0.0666  -0.0072 -0.0247 1048 PRO B N   
16538 C CA  . PRO B 1050 ? 0.3049 0.2114 0.2679 0.0706  -0.0090 -0.0256 1048 PRO B CA  
16539 C C   . PRO B 1050 ? 0.3125 0.2083 0.2727 0.0669  -0.0118 -0.0241 1048 PRO B C   
16540 O O   . PRO B 1050 ? 0.3190 0.2063 0.2749 0.0698  -0.0134 -0.0236 1048 PRO B O   
16541 C CB  . PRO B 1050 ? 0.3211 0.2242 0.2800 0.0726  -0.0088 -0.0290 1048 PRO B CB  
16542 C CG  . PRO B 1050 ? 0.3356 0.2444 0.2981 0.0674  -0.0081 -0.0292 1048 PRO B CG  
16543 C CD  . PRO B 1050 ? 0.2921 0.2126 0.2617 0.0650  -0.0064 -0.0268 1048 PRO B CD  
16544 N N   . VAL B 1051 ? 0.2978 0.1940 0.2602 0.0605  -0.0124 -0.0232 1049 VAL B N   
16545 C CA  . VAL B 1051 ? 0.3193 0.2063 0.2795 0.0564  -0.0150 -0.0214 1049 VAL B CA  
16546 C C   . VAL B 1051 ? 0.2974 0.1871 0.2602 0.0558  -0.0149 -0.0182 1049 VAL B C   
16547 O O   . VAL B 1051 ? 0.3020 0.1827 0.2613 0.0557  -0.0169 -0.0167 1049 VAL B O   
16548 C CB  . VAL B 1051 ? 0.3383 0.2259 0.3005 0.0499  -0.0156 -0.0213 1049 VAL B CB  
16549 C CG1 . VAL B 1051 ? 0.3496 0.2286 0.3100 0.0454  -0.0182 -0.0191 1049 VAL B CG1 
16550 C CG2 . VAL B 1051 ? 0.3129 0.1969 0.2717 0.0508  -0.0161 -0.0245 1049 VAL B CG2 
16551 N N   . LEU B 1052 ? 0.2775 0.1792 0.2463 0.0555  -0.0126 -0.0170 1050 LEU B N   
16552 C CA  . LEU B 1052 ? 0.2704 0.1752 0.2412 0.0559  -0.0124 -0.0142 1050 LEU B CA  
16553 C C   . LEU B 1052 ? 0.3048 0.2035 0.2713 0.0619  -0.0134 -0.0143 1050 LEU B C   
16554 O O   . LEU B 1052 ? 0.2939 0.1868 0.2584 0.0618  -0.0149 -0.0121 1050 LEU B O   
16555 C CB  . LEU B 1052 ? 0.2449 0.1635 0.2220 0.0556  -0.0098 -0.0136 1050 LEU B CB  
16556 C CG  . LEU B 1052 ? 0.2515 0.1754 0.2313 0.0557  -0.0094 -0.0108 1050 LEU B CG  
16557 C CD1 . LEU B 1052 ? 0.2821 0.2062 0.2604 0.0621  -0.0094 -0.0108 1050 LEU B CD1 
16558 C CD2 . LEU B 1052 ? 0.2690 0.1868 0.2477 0.0515  -0.0110 -0.0081 1050 LEU B CD2 
16559 N N   . LEU B 1053 ? 0.2924 0.1924 0.2574 0.0675  -0.0124 -0.0167 1051 LEU B N   
16560 C CA  . LEU B 1053 ? 0.3325 0.2275 0.2937 0.0739  -0.0132 -0.0169 1051 LEU B CA  
16561 C C   . LEU B 1053 ? 0.3228 0.2023 0.2770 0.0740  -0.0161 -0.0170 1051 LEU B C   
16562 O O   . LEU B 1053 ? 0.3578 0.2316 0.3094 0.0765  -0.0176 -0.0153 1051 LEU B O   
16563 C CB  . LEU B 1053 ? 0.3481 0.2475 0.3088 0.0798  -0.0114 -0.0198 1051 LEU B CB  
16564 C CG  . LEU B 1053 ? 0.3510 0.2657 0.3181 0.0809  -0.0086 -0.0196 1051 LEU B CG  
16565 C CD1 . LEU B 1053 ? 0.3275 0.2456 0.2936 0.0854  -0.0069 -0.0226 1051 LEU B CD1 
16566 C CD2 . LEU B 1053 ? 0.3587 0.2780 0.3280 0.0840  -0.0085 -0.0172 1051 LEU B CD2 
16567 N N   . ASP B 1054 ? 0.3482 0.2206 0.2992 0.0711  -0.0173 -0.0187 1052 ASP B N   
16568 C CA  . ASP B 1054 ? 0.3709 0.2280 0.3150 0.0705  -0.0204 -0.0187 1052 ASP B CA  
16569 C C   . ASP B 1054 ? 0.3495 0.2032 0.2944 0.0653  -0.0220 -0.0151 1052 ASP B C   
16570 O O   . ASP B 1054 ? 0.3825 0.2250 0.3222 0.0662  -0.0244 -0.0139 1052 ASP B O   
16571 C CB  . ASP B 1054 ? 0.3636 0.2146 0.3044 0.0678  -0.0214 -0.0213 1052 ASP B CB  
16572 C CG  . ASP B 1054 ? 0.3988 0.2497 0.3366 0.0736  -0.0204 -0.0250 1052 ASP B CG  
16573 O OD1 . ASP B 1054 ? 0.4050 0.2587 0.3424 0.0801  -0.0191 -0.0255 1052 ASP B OD1 
16574 O OD2 . ASP B 1054 ? 0.4650 0.3132 0.4007 0.0718  -0.0207 -0.0273 1052 ASP B OD2 
16575 N N   . PHE B 1055 ? 0.3502 0.2134 0.3013 0.0599  -0.0207 -0.0133 1053 PHE B N   
16576 C CA  . PHE B 1055 ? 0.3249 0.1863 0.2771 0.0549  -0.0218 -0.0097 1053 PHE B CA  
16577 C C   . PHE B 1055 ? 0.3758 0.2382 0.3279 0.0583  -0.0218 -0.0074 1053 PHE B C   
16578 O O   . PHE B 1055 ? 0.3510 0.2052 0.2999 0.0568  -0.0238 -0.0049 1053 PHE B O   
16579 C CB  . PHE B 1055 ? 0.3269 0.1990 0.2857 0.0490  -0.0200 -0.0087 1053 PHE B CB  
16580 C CG  . PHE B 1055 ? 0.3349 0.2065 0.2952 0.0436  -0.0208 -0.0051 1053 PHE B CG  
16581 C CD1 . PHE B 1055 ? 0.3613 0.2217 0.3175 0.0399  -0.0235 -0.0038 1053 PHE B CD1 
16582 C CD2 . PHE B 1055 ? 0.3168 0.1990 0.2825 0.0420  -0.0188 -0.0030 1053 PHE B CD2 
16583 C CE1 . PHE B 1055 ? 0.3381 0.1986 0.2958 0.0347  -0.0240 -0.0003 1053 PHE B CE1 
16584 C CE2 . PHE B 1055 ? 0.3307 0.2126 0.2975 0.0371  -0.0193 0.0003  1053 PHE B CE2 
16585 C CZ  . PHE B 1055 ? 0.3269 0.1983 0.2898 0.0335  -0.0218 0.0017  1053 PHE B CZ  
16586 N N   . ALA B 1056 ? 0.3338 0.2060 0.2893 0.0628  -0.0197 -0.0080 1054 ALA B N   
16587 C CA  . ALA B 1056 ? 0.3533 0.2270 0.3088 0.0665  -0.0198 -0.0058 1054 ALA B CA  
16588 C C   . ALA B 1056 ? 0.3738 0.2344 0.3222 0.0713  -0.0222 -0.0060 1054 ALA B C   
16589 O O   . ALA B 1056 ? 0.4111 0.2665 0.3573 0.0714  -0.0238 -0.0033 1054 ALA B O   
16590 C CB  . ALA B 1056 ? 0.3658 0.2525 0.3261 0.0707  -0.0172 -0.0067 1054 ALA B CB  
16591 N N   . LYS B 1057 ? 0.3848 0.2396 0.3292 0.0753  -0.0226 -0.0093 1055 LYS B N   
16592 C CA  . LYS B 1057 ? 0.3732 0.2148 0.3104 0.0804  -0.0250 -0.0098 1055 LYS B CA  
16593 C C   . LYS B 1057 ? 0.4656 0.2935 0.3977 0.0756  -0.0281 -0.0080 1055 LYS B C   
16594 O O   . LYS B 1057 ? 0.4806 0.2992 0.4081 0.0778  -0.0302 -0.0062 1055 LYS B O   
16595 C CB  . LYS B 1057 ? 0.4370 0.2751 0.3705 0.0852  -0.0246 -0.0139 1055 LYS B CB  
16596 C CG  . LYS B 1057 ? 0.4772 0.3279 0.4150 0.0909  -0.0216 -0.0156 1055 LYS B CG  
16597 C CD  . LYS B 1057 ? 0.3947 0.2408 0.3279 0.0963  -0.0213 -0.0196 1055 LYS B CD  
16598 C CE  . LYS B 1057 ? 0.4269 0.2701 0.3588 0.0916  -0.0214 -0.0218 1055 LYS B CE  
16599 N NZ  . LYS B 1057 ? 0.4218 0.2653 0.3509 0.0969  -0.0201 -0.0256 1055 LYS B NZ  
16600 N N   . TRP B 1058 ? 0.4426 0.2692 0.3754 0.0689  -0.0284 -0.0082 1056 TRP B N   
16601 C CA  . TRP B 1058 ? 0.4431 0.2583 0.3720 0.0633  -0.0313 -0.0062 1056 TRP B CA  
16602 C C   . TRP B 1058 ? 0.4439 0.2610 0.3747 0.0606  -0.0316 -0.0018 1056 TRP B C   
16603 O O   . TRP B 1058 ? 0.4734 0.2791 0.3990 0.0601  -0.0343 0.0003  1056 TRP B O   
16604 C CB  . TRP B 1058 ? 0.4517 0.2686 0.3828 0.0565  -0.0312 -0.0070 1056 TRP B CB  
16605 C CG  . TRP B 1058 ? 0.4878 0.2946 0.4158 0.0499  -0.0340 -0.0047 1056 TRP B CG  
16606 C CD1 . TRP B 1058 ? 0.5230 0.3143 0.4435 0.0494  -0.0373 -0.0054 1056 TRP B CD1 
16607 C CD2 . TRP B 1058 ? 0.4563 0.2682 0.3887 0.0428  -0.0338 -0.0013 1056 TRP B CD2 
16608 N NE1 . TRP B 1058 ? 0.5116 0.2982 0.4318 0.0420  -0.0393 -0.0024 1056 TRP B NE1 
16609 C CE2 . TRP B 1058 ? 0.5094 0.3087 0.4369 0.0379  -0.0370 0.0002  1056 TRP B CE2 
16610 C CE3 . TRP B 1058 ? 0.4476 0.2732 0.3874 0.0400  -0.0311 0.0007  1056 TRP B CE3 
16611 C CZ2 . TRP B 1058 ? 0.5158 0.3168 0.4461 0.0304  -0.0374 0.0036  1056 TRP B CZ2 
16612 C CZ3 . TRP B 1058 ? 0.4959 0.3228 0.4380 0.0329  -0.0315 0.0040  1056 TRP B CZ3 
16613 C CH2 . TRP B 1058 ? 0.4741 0.2891 0.4116 0.0282  -0.0346 0.0055  1056 TRP B CH2 
16614 N N   . LEU B 1059 ? 0.4146 0.2458 0.3525 0.0589  -0.0290 -0.0004 1057 LEU B N   
16615 C CA  . LEU B 1059 ? 0.4370 0.2711 0.3767 0.0568  -0.0291 0.0035  1057 LEU B CA  
16616 C C   . LEU B 1059 ? 0.5051 0.3342 0.4411 0.0631  -0.0303 0.0046  1057 LEU B C   
16617 O O   . LEU B 1059 ? 0.4958 0.3185 0.4288 0.0617  -0.0320 0.0078  1057 LEU B O   
16618 C CB  . LEU B 1059 ? 0.3907 0.2409 0.3382 0.0547  -0.0260 0.0043  1057 LEU B CB  
16619 C CG  . LEU B 1059 ? 0.4095 0.2655 0.3613 0.0479  -0.0248 0.0041  1057 LEU B CG  
16620 C CD1 . LEU B 1059 ? 0.3785 0.2498 0.3374 0.0473  -0.0218 0.0043  1057 LEU B CD1 
16621 C CD2 . LEU B 1059 ? 0.4515 0.3011 0.4016 0.0415  -0.0265 0.0073  1057 LEU B CD2 
16622 N N   . ASP B 1060 ? 0.4668 0.2993 0.4028 0.0703  -0.0292 0.0020  1058 ASP B N   
16623 C CA  . ASP B 1060 ? 0.4721 0.2998 0.4045 0.0772  -0.0305 0.0028  1058 ASP B CA  
16624 C C   . ASP B 1060 ? 0.5154 0.3251 0.4393 0.0776  -0.0340 0.0034  1058 ASP B C   
16625 O O   . ASP B 1060 ? 0.5489 0.3524 0.4697 0.0788  -0.0358 0.0063  1058 ASP B O   
16626 C CB  . ASP B 1060 ? 0.5238 0.3570 0.4572 0.0848  -0.0288 -0.0006 1058 ASP B CB  
16627 C CG  . ASP B 1060 ? 0.5269 0.3776 0.4681 0.0859  -0.0258 -0.0005 1058 ASP B CG  
16628 O OD1 . ASP B 1060 ? 0.4837 0.3412 0.4285 0.0832  -0.0253 0.0025  1058 ASP B OD1 
16629 O OD2 . ASP B 1060 ? 0.5378 0.3954 0.4813 0.0896  -0.0239 -0.0034 1058 ASP B OD2 
16630 N N   . GLY B 1061 ? 0.5188 0.3194 0.4386 0.0768  -0.0351 0.0007  1059 GLY B N   
16631 C CA  . GLY B 1061 ? 0.5827 0.3652 0.4937 0.0773  -0.0387 0.0009  1059 GLY B CA  
16632 C C   . GLY B 1061 ? 0.5797 0.3554 0.4890 0.0703  -0.0408 0.0050  1059 GLY B C   
16633 O O   . GLY B 1061 ? 0.6068 0.3689 0.5093 0.0715  -0.0438 0.0066  1059 GLY B O   
16634 N N   . LYS B 1062 ? 0.5478 0.3330 0.4630 0.0632  -0.0393 0.0069  1060 LYS B N   
16635 C CA  . LYS B 1062 ? 0.5773 0.3583 0.4917 0.0562  -0.0408 0.0110  1060 LYS B CA  
16636 C C   . LYS B 1062 ? 0.5956 0.3815 0.5117 0.0572  -0.0404 0.0148  1060 LYS B C   
16637 O O   . LYS B 1062 ? 0.6048 0.3873 0.5199 0.0518  -0.0415 0.0185  1060 LYS B O   
16638 C CB  . LYS B 1062 ? 0.5531 0.3429 0.4734 0.0483  -0.0392 0.0115  1060 LYS B CB  
16639 C CG  . LYS B 1062 ? 0.5614 0.3460 0.4800 0.0455  -0.0401 0.0086  1060 LYS B CG  
16640 C CD  . LYS B 1062 ? 0.5018 0.2980 0.4274 0.0389  -0.0380 0.0091  1060 LYS B CD  
16641 C CE  . LYS B 1062 ? 0.5338 0.3325 0.4616 0.0326  -0.0380 0.0137  1060 LYS B CE  
16642 N NZ  . LYS B 1062 ? 0.5579 0.3481 0.4833 0.0254  -0.0404 0.0152  1060 LYS B NZ  
16643 N N   . GLY B 1063 ? 0.5620 0.3563 0.4808 0.0637  -0.0387 0.0139  1061 GLY B N   
16644 C CA  . GLY B 1063 ? 0.5794 0.3798 0.5004 0.0645  -0.0382 0.0173  1061 GLY B CA  
16645 C C   . GLY B 1063 ? 0.5752 0.3898 0.5033 0.0590  -0.0355 0.0190  1061 GLY B C   
16646 O O   . GLY B 1063 ? 0.5632 0.3817 0.4923 0.0582  -0.0354 0.0223  1061 GLY B O   
16647 N N   . ALA B 1064 ? 0.5108 0.3329 0.4435 0.0553  -0.0335 0.0169  1062 ALA B N   
16648 C CA  . ALA B 1064 ? 0.4912 0.3268 0.4306 0.0505  -0.0309 0.0181  1062 ALA B CA  
16649 C C   . ALA B 1064 ? 0.5096 0.3583 0.4541 0.0553  -0.0285 0.0167  1062 ALA B C   
16650 O O   . ALA B 1064 ? 0.4455 0.3033 0.3945 0.0555  -0.0263 0.0140  1062 ALA B O   
16651 C CB  . ALA B 1064 ? 0.4805 0.3184 0.4227 0.0449  -0.0299 0.0165  1062 ALA B CB  
16652 N N   . ARG B 1065 ? 0.4894 0.3390 0.4328 0.0591  -0.0290 0.0188  1063 ARG B N   
16653 C CA  . ARG B 1065 ? 0.4687 0.3285 0.4157 0.0650  -0.0275 0.0174  1063 ARG B CA  
16654 C C   . ARG B 1065 ? 0.4427 0.3176 0.3966 0.0619  -0.0247 0.0174  1063 ARG B C   
16655 O O   . ARG B 1065 ? 0.4432 0.3274 0.4013 0.0646  -0.0228 0.0149  1063 ARG B O   
16656 C CB  . ARG B 1065 ? 0.4710 0.3274 0.4149 0.0698  -0.0293 0.0199  1063 ARG B CB  
16657 N N   . ALA B 1066 ? 0.4229 0.3005 0.3780 0.0562  -0.0243 0.0203  1064 ALA B N   
16658 C CA  . ALA B 1066 ? 0.4303 0.3212 0.3914 0.0531  -0.0216 0.0201  1064 ALA B CA  
16659 C C   . ALA B 1066 ? 0.4031 0.2978 0.3675 0.0508  -0.0199 0.0169  1064 ALA B C   
16660 O O   . ALA B 1066 ? 0.4038 0.3090 0.3729 0.0517  -0.0179 0.0150  1064 ALA B O   
16661 C CB  . ALA B 1066 ? 0.4536 0.3457 0.4147 0.0475  -0.0214 0.0236  1064 ALA B CB  
16662 N N   . GLU B 1067 ? 0.3942 0.2801 0.3560 0.0477  -0.0210 0.0164  1065 GLU B N   
16663 C CA  . GLU B 1067 ? 0.3887 0.2779 0.3535 0.0451  -0.0197 0.0136  1065 GLU B CA  
16664 C C   . GLU B 1067 ? 0.3525 0.2434 0.3178 0.0505  -0.0191 0.0100  1065 GLU B C   
16665 O O   . GLU B 1067 ? 0.3692 0.2689 0.3388 0.0500  -0.0171 0.0078  1065 GLU B O   
16666 C CB  . GLU B 1067 ? 0.4154 0.2947 0.3771 0.0405  -0.0213 0.0141  1065 GLU B CB  
16667 C CG  . GLU B 1067 ? 0.3892 0.2696 0.3519 0.0341  -0.0211 0.0175  1065 GLU B CG  
16668 C CD  . GLU B 1067 ? 0.4474 0.3208 0.4057 0.0342  -0.0229 0.0211  1065 GLU B CD  
16669 O OE1 . GLU B 1067 ? 0.4526 0.3186 0.4067 0.0392  -0.0247 0.0209  1065 GLU B OE1 
16670 O OE2 . GLU B 1067 ? 0.4374 0.3127 0.3964 0.0293  -0.0225 0.0241  1065 GLU B OE2 
16671 N N   . ALA B 1068 ? 0.4066 0.2892 0.3673 0.0558  -0.0209 0.0093  1066 ALA B N   
16672 C CA  . ALA B 1068 ? 0.4248 0.3092 0.3857 0.0614  -0.0202 0.0059  1066 ALA B CA  
16673 C C   . ALA B 1068 ? 0.4007 0.2988 0.3669 0.0642  -0.0180 0.0055  1066 ALA B C   
16674 O O   . ALA B 1068 ? 0.3581 0.2629 0.3272 0.0657  -0.0163 0.0028  1066 ALA B O   
16675 C CB  . ALA B 1068 ? 0.3709 0.2440 0.3257 0.0671  -0.0225 0.0056  1066 ALA B CB  
16676 N N   . GLU B 1069 ? 0.3619 0.2642 0.3292 0.0646  -0.0181 0.0082  1067 GLU B N   
16677 C CA  . GLU B 1069 ? 0.3925 0.3079 0.3649 0.0664  -0.0163 0.0081  1067 GLU B CA  
16678 C C   . GLU B 1069 ? 0.3862 0.3107 0.3634 0.0613  -0.0141 0.0073  1067 GLU B C   
16679 O O   . GLU B 1069 ? 0.3701 0.3041 0.3513 0.0627  -0.0123 0.0055  1067 GLU B O   
16680 C CB  . GLU B 1069 ? 0.4319 0.3490 0.4039 0.0674  -0.0172 0.0113  1067 GLU B CB  
16681 C CG  . GLU B 1069 ? 0.4307 0.3612 0.4077 0.0682  -0.0156 0.0117  1067 GLU B CG  
16682 C CD  . GLU B 1069 ? 0.4983 0.4343 0.4770 0.0747  -0.0152 0.0099  1067 GLU B CD  
16683 O OE1 . GLU B 1069 ? 0.5019 0.4310 0.4776 0.0791  -0.0160 0.0083  1067 GLU B OE1 
16684 O OE2 . GLU B 1069 ? 0.5700 0.5172 0.5530 0.0754  -0.0141 0.0101  1067 GLU B OE2 
16685 N N   . ALA B 1070 ? 0.3495 0.2715 0.3265 0.0554  -0.0142 0.0087  1068 ALA B N   
16686 C CA  . ALA B 1070 ? 0.3600 0.2900 0.3415 0.0509  -0.0122 0.0079  1068 ALA B CA  
16687 C C   . ALA B 1070 ? 0.3248 0.2549 0.3072 0.0514  -0.0114 0.0045  1068 ALA B C   
16688 O O   . ALA B 1070 ? 0.3284 0.2675 0.3149 0.0506  -0.0095 0.0030  1068 ALA B O   
16689 C CB  . ALA B 1070 ? 0.3699 0.2968 0.3508 0.0448  -0.0124 0.0101  1068 ALA B CB  
16690 N N   . ALA B 1071 ? 0.3123 0.2323 0.2906 0.0527  -0.0129 0.0034  1069 ALA B N   
16691 C CA  . ALA B 1071 ? 0.3054 0.2250 0.2840 0.0533  -0.0123 0.0002  1069 ALA B CA  
16692 C C   . ALA B 1071 ? 0.3003 0.2269 0.2807 0.0585  -0.0110 -0.0019 1069 ALA B C   
16693 O O   . ALA B 1071 ? 0.3011 0.2342 0.2845 0.0578  -0.0094 -0.0039 1069 ALA B O   
16694 C CB  . ALA B 1071 ? 0.3129 0.2194 0.2859 0.0537  -0.0145 -0.0006 1069 ALA B CB  
16695 N N   . ARG B 1072 ? 0.3164 0.2419 0.2951 0.0639  -0.0117 -0.0014 1070 ARG B N   
16696 C CA  . ARG B 1072 ? 0.3172 0.2505 0.2982 0.0689  -0.0103 -0.0031 1070 ARG B CA  
16697 C C   . ARG B 1072 ? 0.2983 0.2448 0.2851 0.0667  -0.0083 -0.0026 1070 ARG B C   
16698 O O   . ARG B 1072 ? 0.2945 0.2482 0.2841 0.0676  -0.0067 -0.0046 1070 ARG B O   
16699 C CB  . ARG B 1072 ? 0.3237 0.2543 0.3022 0.0750  -0.0115 -0.0023 1070 ARG B CB  
16700 C CG  . ARG B 1072 ? 0.3694 0.2877 0.3419 0.0789  -0.0131 -0.0037 1070 ARG B CG  
16701 C CD  . ARG B 1072 ? 0.3859 0.3028 0.3564 0.0859  -0.0140 -0.0031 1070 ARG B CD  
16702 N NE  . ARG B 1072 ? 0.4660 0.3810 0.4359 0.0850  -0.0155 0.0004  1070 ARG B NE  
16703 C CZ  . ARG B 1072 ? 0.4986 0.4014 0.4632 0.0847  -0.0179 0.0020  1070 ARG B CZ  
16704 N NH1 . ARG B 1072 ? 0.4545 0.3453 0.4138 0.0856  -0.0193 0.0004  1070 ARG B NH1 
16705 N NH2 . ARG B 1072 ? 0.4127 0.3150 0.3771 0.0832  -0.0190 0.0053  1070 ARG B NH2 
16706 N N   . ASN B 1073 ? 0.2890 0.2382 0.2772 0.0636  -0.0085 0.0000  1071 ASN B N   
16707 C CA  . ASN B 1073 ? 0.2981 0.2588 0.2912 0.0613  -0.0069 0.0004  1071 ASN B CA  
16708 C C   . ASN B 1073 ? 0.2980 0.2618 0.2935 0.0570  -0.0055 -0.0013 1071 ASN B C   
16709 O O   . ASN B 1073 ? 0.2831 0.2559 0.2822 0.0567  -0.0039 -0.0023 1071 ASN B O   
16710 C CB  . ASN B 1073 ? 0.3316 0.2933 0.3248 0.0588  -0.0075 0.0034  1071 ASN B CB  
16711 C CG  . ASN B 1073 ? 0.3773 0.3389 0.3691 0.0633  -0.0088 0.0051  1071 ASN B CG  
16712 O OD1 . ASN B 1073 ? 0.4369 0.4016 0.4294 0.0682  -0.0087 0.0041  1071 ASN B OD1 
16713 N ND2 . ASN B 1073 ? 0.3989 0.3570 0.3887 0.0617  -0.0100 0.0079  1071 ASN B ND2 
16714 N N   . ALA B 1074 ? 0.2751 0.2318 0.2687 0.0534  -0.0060 -0.0013 1072 ALA B N   
16715 C CA  . ALA B 1074 ? 0.2928 0.2520 0.2885 0.0497  -0.0049 -0.0029 1072 ALA B CA  
16716 C C   . ALA B 1074 ? 0.2304 0.1909 0.2262 0.0525  -0.0042 -0.0058 1072 ALA B C   
16717 O O   . ALA B 1074 ? 0.2358 0.2031 0.2347 0.0509  -0.0027 -0.0071 1072 ALA B O   
16718 C CB  . ALA B 1074 ? 0.2844 0.2357 0.2781 0.0456  -0.0059 -0.0023 1072 ALA B CB  
16719 N N   . GLY B 1075 ? 0.2460 0.1997 0.2382 0.0566  -0.0052 -0.0068 1073 GLY B N   
16720 C CA  . GLY B 1075 ? 0.2825 0.2373 0.2742 0.0596  -0.0044 -0.0096 1073 GLY B CA  
16721 C C   . GLY B 1075 ? 0.2977 0.2640 0.2934 0.0618  -0.0026 -0.0101 1073 GLY B C   
16722 O O   . GLY B 1075 ? 0.2822 0.2532 0.2795 0.0615  -0.0013 -0.0119 1073 GLY B O   
16723 N N   . SER B 1076 ? 0.2867 0.2577 0.2839 0.0637  -0.0027 -0.0082 1074 SER B N   
16724 C CA  . SER B 1076 ? 0.2548 0.2368 0.2558 0.0657  -0.0012 -0.0084 1074 SER B CA  
16725 C C   . SER B 1076 ? 0.2670 0.2569 0.2720 0.0609  -0.0001 -0.0080 1074 SER B C   
16726 O O   . SER B 1076 ? 0.2936 0.2910 0.3013 0.0608  0.0013  -0.0091 1074 SER B O   
16727 C CB  . SER B 1076 ? 0.2794 0.2639 0.2807 0.0695  -0.0020 -0.0066 1074 SER B CB  
16728 O OG  . SER B 1076 ? 0.3253 0.3046 0.3235 0.0752  -0.0026 -0.0075 1074 SER B OG  
16729 N N   . SER B 1077 ? 0.2524 0.2407 0.2576 0.0568  -0.0006 -0.0063 1075 SER B N   
16730 C CA  . SER B 1077 ? 0.2688 0.2645 0.2774 0.0529  0.0005  -0.0059 1075 SER B CA  
16731 C C   . SER B 1077 ? 0.2497 0.2446 0.2590 0.0493  0.0013  -0.0075 1075 SER B C   
16732 O O   . SER B 1077 ? 0.2987 0.3000 0.3107 0.0466  0.0023  -0.0077 1075 SER B O   
16733 C CB  . SER B 1077 ? 0.3169 0.3123 0.3255 0.0503  -0.0002 -0.0035 1075 SER B CB  
16734 O OG  . SER B 1077 ? 0.3134 0.3013 0.3200 0.0473  -0.0008 -0.0030 1075 SER B OG  
16735 N N   . SER B 1078 ? 0.2100 0.1971 0.2166 0.0492  0.0006  -0.0086 1076 SER B N   
16736 C CA  . SER B 1078 ? 0.2300 0.2165 0.2372 0.0464  0.0012  -0.0102 1076 SER B CA  
16737 C C   . SER B 1078 ? 0.2182 0.2119 0.2274 0.0476  0.0027  -0.0118 1076 SER B C   
16738 O O   . SER B 1078 ? 0.2121 0.2082 0.2211 0.0516  0.0030  -0.0124 1076 SER B O   
16739 C CB  . SER B 1078 ? 0.2071 0.1842 0.2106 0.0472  0.0001  -0.0114 1076 SER B CB  
16740 O OG  . SER B 1078 ? 0.2118 0.1888 0.2157 0.0450  0.0006  -0.0132 1076 SER B OG  
16741 N N   . ALA B 1079 ? 0.1919 0.1894 0.2034 0.0441  0.0035  -0.0124 1077 ALA B N   
16742 C CA  . ALA B 1079 ? 0.2020 0.2057 0.2151 0.0446  0.0047  -0.0138 1077 ALA B CA  
16743 C C   . ALA B 1079 ? 0.2001 0.1997 0.2115 0.0441  0.0048  -0.0157 1077 ALA B C   
16744 O O   . ALA B 1079 ? 0.1809 0.1850 0.1935 0.0434  0.0058  -0.0168 1077 ALA B O   
16745 C CB  . ALA B 1079 ? 0.2147 0.2254 0.2309 0.0414  0.0056  -0.0131 1077 ALA B CB  
16746 N N   . LEU B 1080 ? 0.1960 0.1871 0.2044 0.0442  0.0036  -0.0161 1078 LEU B N   
16747 C CA  . LEU B 1080 ? 0.1779 0.1647 0.1842 0.0441  0.0033  -0.0181 1078 LEU B CA  
16748 C C   . LEU B 1080 ? 0.1842 0.1739 0.1895 0.0479  0.0043  -0.0196 1078 LEU B C   
16749 O O   . LEU B 1080 ? 0.2091 0.1991 0.2134 0.0520  0.0044  -0.0195 1078 LEU B O   
16750 C CB  . LEU B 1080 ? 0.1980 0.1747 0.2006 0.0444  0.0016  -0.0181 1078 LEU B CB  
16751 C CG  . LEU B 1080 ? 0.2167 0.1876 0.2160 0.0449  0.0009  -0.0203 1078 LEU B CG  
16752 C CD1 . LEU B 1080 ? 0.2107 0.1820 0.2116 0.0406  0.0007  -0.0206 1078 LEU B CD1 
16753 C CD2 . LEU B 1080 ? 0.2388 0.1996 0.2338 0.0464  -0.0010 -0.0203 1078 LEU B CD2 
16754 N N   . GLY B 1081 ? 0.1924 0.1846 0.1980 0.0468  0.0051  -0.0210 1079 GLY B N   
16755 C CA  . GLY B 1081 ? 0.2208 0.2166 0.2255 0.0500  0.0063  -0.0224 1079 GLY B CA  
16756 C C   . GLY B 1081 ? 0.2312 0.2372 0.2395 0.0496  0.0079  -0.0217 1079 GLY B C   
16757 O O   . GLY B 1081 ? 0.2304 0.2407 0.2385 0.0518  0.0091  -0.0227 1079 GLY B O   
16758 N N   . LEU B 1082 ? 0.1966 0.2066 0.2081 0.0469  0.0079  -0.0201 1080 LEU B N   
16759 C CA  A LEU B 1082 ? 0.2050 0.2240 0.2197 0.0455  0.0091  -0.0194 1080 LEU B CA  
16760 C CA  B LEU B 1082 ? 0.2051 0.2241 0.2198 0.0455  0.0091  -0.0194 1080 LEU B CA  
16761 C C   . LEU B 1082 ? 0.2071 0.2277 0.2215 0.0438  0.0098  -0.0206 1080 LEU B C   
16762 O O   . LEU B 1082 ? 0.2017 0.2173 0.2148 0.0416  0.0092  -0.0214 1080 LEU B O   
16763 C CB  A LEU B 1082 ? 0.1923 0.2133 0.2095 0.0421  0.0086  -0.0178 1080 LEU B CB  
16764 C CB  B LEU B 1082 ? 0.1923 0.2132 0.2095 0.0420  0.0086  -0.0178 1080 LEU B CB  
16765 C CG  A LEU B 1082 ? 0.1852 0.2145 0.2053 0.0402  0.0095  -0.0170 1080 LEU B CG  
16766 C CG  B LEU B 1082 ? 0.1853 0.2142 0.2054 0.0399  0.0094  -0.0170 1080 LEU B CG  
16767 C CD1 A LEU B 1082 ? 0.2021 0.2380 0.2235 0.0432  0.0102  -0.0165 1080 LEU B CD1 
16768 C CD1 B LEU B 1082 ? 0.1926 0.2228 0.2142 0.0383  0.0088  -0.0154 1080 LEU B CD1 
16769 C CD2 A LEU B 1082 ? 0.1964 0.2261 0.2180 0.0372  0.0089  -0.0157 1080 LEU B CD2 
16770 C CD2 B LEU B 1082 ? 0.1960 0.2252 0.2164 0.0366  0.0097  -0.0178 1080 LEU B CD2 
16771 N N   . ASP B 1083 ? 0.2001 0.2278 0.2157 0.0449  0.0111  -0.0207 1081 ASP B N   
16772 C CA  . ASP B 1083 ? 0.2422 0.2713 0.2570 0.0436  0.0119  -0.0218 1081 ASP B CA  
16773 C C   . ASP B 1083 ? 0.2472 0.2857 0.2648 0.0427  0.0131  -0.0208 1081 ASP B C   
16774 O O   . ASP B 1083 ? 0.2808 0.3245 0.2989 0.0457  0.0142  -0.0207 1081 ASP B O   
16775 C CB  . ASP B 1083 ? 0.2875 0.3130 0.2988 0.0471  0.0122  -0.0235 1081 ASP B CB  
16776 C CG  . ASP B 1083 ? 0.3651 0.3914 0.3749 0.0458  0.0130  -0.0246 1081 ASP B CG  
16777 O OD1 . ASP B 1083 ? 0.3906 0.4183 0.4017 0.0420  0.0128  -0.0242 1081 ASP B OD1 
16778 O OD2 . ASP B 1083 ? 0.4446 0.4701 0.4516 0.0489  0.0137  -0.0260 1081 ASP B OD2 
16779 N N   . LEU B 1084 ? 0.2335 0.2741 0.2529 0.0387  0.0129  -0.0200 1082 LEU B N   
16780 C CA  . LEU B 1084 ? 0.2154 0.2641 0.2375 0.0370  0.0135  -0.0188 1082 LEU B CA  
16781 C C   . LEU B 1084 ? 0.2055 0.2555 0.2272 0.0339  0.0139  -0.0192 1082 LEU B C   
16782 O O   . LEU B 1084 ? 0.2022 0.2467 0.2224 0.0321  0.0133  -0.0199 1082 LEU B O   
16783 C CB  . LEU B 1084 ? 0.2434 0.2931 0.2675 0.0347  0.0126  -0.0175 1082 LEU B CB  
16784 C CG  . LEU B 1084 ? 0.2646 0.3141 0.2894 0.0372  0.0121  -0.0167 1082 LEU B CG  
16785 C CD1 . LEU B 1084 ? 0.2744 0.3237 0.3004 0.0344  0.0112  -0.0155 1082 LEU B CD1 
16786 C CD2 . LEU B 1084 ? 0.3128 0.3695 0.3392 0.0402  0.0129  -0.0160 1082 LEU B CD2 
16787 N N   . GLU B 1085 ? 0.1952 0.2526 0.2184 0.0333  0.0149  -0.0184 1083 GLU B N   
16788 C CA  . GLU B 1085 ? 0.1899 0.2493 0.2131 0.0296  0.0150  -0.0181 1083 GLU B CA  
16789 C C   . GLU B 1085 ? 0.1818 0.2441 0.2072 0.0264  0.0143  -0.0167 1083 GLU B C   
16790 O O   . GLU B 1085 ? 0.1960 0.2642 0.2236 0.0270  0.0144  -0.0156 1083 GLU B O   
16791 C CB  . GLU B 1085 ? 0.1897 0.2551 0.2127 0.0303  0.0165  -0.0179 1083 GLU B CB  
16792 C CG  . GLU B 1085 ? 0.2138 0.2794 0.2360 0.0264  0.0164  -0.0177 1083 GLU B CG  
16793 C CD  . GLU B 1085 ? 0.2526 0.3235 0.2741 0.0265  0.0179  -0.0174 1083 GLU B CD  
16794 O OE1 . GLU B 1085 ? 0.2839 0.3573 0.3048 0.0301  0.0191  -0.0180 1083 GLU B OE1 
16795 O OE2 . GLU B 1085 ? 0.2727 0.3450 0.2939 0.0229  0.0177  -0.0167 1083 GLU B OE2 
16796 N N   . LEU B 1086 ? 0.1851 0.2434 0.2098 0.0233  0.0134  -0.0169 1084 LEU B N   
16797 C CA  . LEU B 1086 ? 0.1804 0.2402 0.2064 0.0202  0.0126  -0.0159 1084 LEU B CA  
16798 C C   . LEU B 1086 ? 0.2080 0.2724 0.2342 0.0173  0.0128  -0.0151 1084 LEU B C   
16799 O O   . LEU B 1086 ? 0.2196 0.2836 0.2444 0.0166  0.0133  -0.0155 1084 LEU B O   
16800 C CB  . LEU B 1086 ? 0.2005 0.2536 0.2255 0.0186  0.0117  -0.0165 1084 LEU B CB  
16801 C CG  . LEU B 1086 ? 0.2074 0.2558 0.2321 0.0209  0.0113  -0.0171 1084 LEU B CG  
16802 C CD1 . LEU B 1086 ? 0.1923 0.2354 0.2165 0.0190  0.0106  -0.0174 1084 LEU B CD1 
16803 C CD2 . LEU B 1086 ? 0.2293 0.2810 0.2555 0.0225  0.0113  -0.0161 1084 LEU B CD2 
16804 N N   . PRO B 1087 ? 0.2038 0.2726 0.2316 0.0152  0.0123  -0.0139 1085 PRO B N   
16805 C CA  . PRO B 1087 ? 0.2144 0.2870 0.2422 0.0118  0.0122  -0.0129 1085 PRO B CA  
16806 C C   . PRO B 1087 ? 0.2116 0.2782 0.2371 0.0091  0.0115  -0.0135 1085 PRO B C   
16807 O O   . PRO B 1087 ? 0.2423 0.3034 0.2670 0.0088  0.0107  -0.0142 1085 PRO B O   
16808 C CB  . PRO B 1087 ? 0.2437 0.3208 0.2733 0.0102  0.0113  -0.0117 1085 PRO B CB  
16809 C CG  . PRO B 1087 ? 0.2734 0.3517 0.3045 0.0137  0.0115  -0.0117 1085 PRO B CG  
16810 C CD  . PRO B 1087 ? 0.2454 0.3166 0.2749 0.0162  0.0118  -0.0131 1085 PRO B CD  
16811 N N   . GLY B 1088 ? 0.2153 0.2832 0.2396 0.0072  0.0118  -0.0132 1086 GLY B N   
16812 C CA  . GLY B 1088 ? 0.2078 0.2703 0.2299 0.0046  0.0110  -0.0136 1086 GLY B CA  
16813 C C   . GLY B 1088 ? 0.1957 0.2610 0.2167 0.0020  0.0113  -0.0126 1086 GLY B C   
16814 O O   . GLY B 1088 ? 0.1935 0.2659 0.2159 0.0014  0.0119  -0.0113 1086 GLY B O   
16815 N N   . PRO B 1089 ? 0.2023 0.2624 0.2207 0.0005  0.0107  -0.0130 1087 PRO B N   
16816 C CA  . PRO B 1089 ? 0.2027 0.2647 0.2196 -0.0023 0.0109  -0.0119 1087 PRO B CA  
16817 C C   . PRO B 1089 ? 0.2148 0.2814 0.2316 -0.0004 0.0125  -0.0117 1087 PRO B C   
16818 O O   . PRO B 1089 ? 0.2150 0.2805 0.2319 0.0031  0.0134  -0.0129 1087 PRO B O   
16819 C CB  . PRO B 1089 ? 0.2396 0.2938 0.2536 -0.0035 0.0097  -0.0126 1087 PRO B CB  
16820 C CG  . PRO B 1089 ? 0.2464 0.2962 0.2608 -0.0002 0.0098  -0.0143 1087 PRO B CG  
16821 C CD  . PRO B 1089 ? 0.2203 0.2728 0.2373 0.0014  0.0100  -0.0144 1087 PRO B CD  
16822 N N   . VAL B 1090 ? 0.1798 0.2513 0.1963 -0.0030 0.0130  -0.0102 1088 VAL B N   
16823 C CA  . VAL B 1090 ? 0.1660 0.2415 0.1817 -0.0015 0.0148  -0.0100 1088 VAL B CA  
16824 C C   . VAL B 1090 ? 0.2018 0.2702 0.2142 -0.0007 0.0145  -0.0112 1088 VAL B C   
16825 O O   . VAL B 1090 ? 0.2078 0.2693 0.2185 -0.0021 0.0130  -0.0117 1088 VAL B O   
16826 C CB  . VAL B 1090 ? 0.1963 0.2784 0.2121 -0.0050 0.0153  -0.0078 1088 VAL B CB  
16827 C CG1 . VAL B 1090 ? 0.2069 0.2964 0.2263 -0.0060 0.0153  -0.0065 1088 VAL B CG1 
16828 C CG2 . VAL B 1090 ? 0.2119 0.2886 0.2247 -0.0093 0.0138  -0.0070 1088 VAL B CG2 
16829 N N   . GLY B 1091 ? 0.1949 0.2653 0.2061 0.0018  0.0161  -0.0117 1089 GLY B N   
16830 C CA  . GLY B 1091 ? 0.1733 0.2375 0.1810 0.0027  0.0158  -0.0129 1089 GLY B CA  
16831 C C   . GLY B 1091 ? 0.1940 0.2515 0.2016 0.0054  0.0148  -0.0148 1089 GLY B C   
16832 O O   . GLY B 1091 ? 0.1962 0.2478 0.2012 0.0055  0.0140  -0.0157 1089 GLY B O   
16833 N N   . GLU B 1092 ? 0.1674 0.2258 0.1778 0.0073  0.0148  -0.0153 1090 GLU B N   
16834 C CA  . GLU B 1092 ? 0.1736 0.2262 0.1842 0.0095  0.0140  -0.0169 1090 GLU B CA  
16835 C C   . GLU B 1092 ? 0.2001 0.2562 0.2129 0.0127  0.0149  -0.0173 1090 GLU B C   
16836 O O   . GLU B 1092 ? 0.2007 0.2630 0.2159 0.0124  0.0156  -0.0162 1090 GLU B O   
16837 C CB  . GLU B 1092 ? 0.2251 0.2736 0.2366 0.0074  0.0123  -0.0168 1090 GLU B CB  
16838 C CG  . GLU B 1092 ? 0.2538 0.2952 0.2641 0.0078  0.0111  -0.0179 1090 GLU B CG  
16839 C CD  . GLU B 1092 ? 0.2311 0.2692 0.2423 0.0059  0.0098  -0.0177 1090 GLU B CD  
16840 O OE1 . GLU B 1092 ? 0.2177 0.2573 0.2311 0.0061  0.0098  -0.0176 1090 GLU B OE1 
16841 O OE2 . GLU B 1092 ? 0.2683 0.3022 0.2778 0.0043  0.0087  -0.0178 1090 GLU B OE2 
16842 N N   . ARG B 1093 ? 0.1754 0.2274 0.1874 0.0157  0.0149  -0.0188 1091 ARG B N   
16843 C CA  . ARG B 1093 ? 0.1679 0.2212 0.1817 0.0189  0.0153  -0.0193 1091 ARG B CA  
16844 C C   . ARG B 1093 ? 0.1884 0.2355 0.2027 0.0191  0.0139  -0.0200 1091 ARG B C   
16845 O O   . ARG B 1093 ? 0.1827 0.2239 0.1950 0.0191  0.0131  -0.0210 1091 ARG B O   
16846 C CB  . ARG B 1093 ? 0.2321 0.2859 0.2440 0.0226  0.0165  -0.0204 1091 ARG B CB  
16847 C CG  . ARG B 1093 ? 0.3171 0.3782 0.3287 0.0233  0.0184  -0.0196 1091 ARG B CG  
16848 C CD  . ARG B 1093 ? 0.3580 0.4187 0.3673 0.0277  0.0196  -0.0211 1091 ARG B CD  
16849 N NE  . ARG B 1093 ? 0.4628 0.5224 0.4733 0.0312  0.0195  -0.0218 1091 ARG B NE  
16850 C CZ  . ARG B 1093 ? 0.5217 0.5746 0.5298 0.0339  0.0189  -0.0235 1091 ARG B CZ  
16851 N NH1 . ARG B 1093 ? 0.5274 0.5743 0.5319 0.0337  0.0183  -0.0248 1091 ARG B NH1 
16852 N NH2 . ARG B 1093 ? 0.5025 0.5546 0.5117 0.0369  0.0188  -0.0238 1091 ARG B NH2 
16853 N N   . ASN B 1094 ? 0.1672 0.2157 0.1839 0.0191  0.0136  -0.0194 1092 ASN B N   
16854 C CA  . ASN B 1094 ? 0.1729 0.2165 0.1904 0.0187  0.0124  -0.0197 1092 ASN B CA  
16855 C C   . ASN B 1094 ? 0.1951 0.2387 0.2136 0.0217  0.0127  -0.0200 1092 ASN B C   
16856 O O   . ASN B 1094 ? 0.1899 0.2384 0.2102 0.0225  0.0132  -0.0191 1092 ASN B O   
16857 C CB  . ASN B 1094 ? 0.1608 0.2054 0.1797 0.0157  0.0118  -0.0188 1092 ASN B CB  
16858 C CG  . ASN B 1094 ? 0.1612 0.2035 0.1786 0.0130  0.0112  -0.0188 1092 ASN B CG  
16859 O OD1 . ASN B 1094 ? 0.1769 0.2140 0.1933 0.0129  0.0104  -0.0196 1092 ASN B OD1 
16860 N ND2 . ASN B 1094 ? 0.1885 0.2346 0.2057 0.0108  0.0114  -0.0178 1092 ASN B ND2 
16861 N N   . LEU B 1095 ? 0.1724 0.2104 0.1895 0.0234  0.0122  -0.0211 1093 LEU B N   
16862 C CA  . LEU B 1095 ? 0.1660 0.2027 0.1830 0.0265  0.0123  -0.0215 1093 LEU B CA  
16863 C C   . LEU B 1095 ? 0.1461 0.1783 0.1639 0.0260  0.0112  -0.0213 1093 LEU B C   
16864 O O   . LEU B 1095 ? 0.1786 0.2073 0.1965 0.0238  0.0103  -0.0215 1093 LEU B O   
16865 C CB  . LEU B 1095 ? 0.1843 0.2175 0.1983 0.0289  0.0124  -0.0229 1093 LEU B CB  
16866 C CG  . LEU B 1095 ? 0.2441 0.2816 0.2568 0.0295  0.0137  -0.0231 1093 LEU B CG  
16867 C CD1 . LEU B 1095 ? 0.2886 0.3218 0.2976 0.0320  0.0138  -0.0247 1093 LEU B CD1 
16868 C CD2 . LEU B 1095 ? 0.2353 0.2804 0.2500 0.0310  0.0151  -0.0220 1093 LEU B CD2 
16869 N N   . TYR B 1096 ? 0.1538 0.1864 0.1725 0.0280  0.0112  -0.0209 1094 TYR B N   
16870 C CA  . TYR B 1096 ? 0.1643 0.1932 0.1838 0.0274  0.0103  -0.0204 1094 TYR B CA  
16871 C C   . TYR B 1096 ? 0.1700 0.1958 0.1883 0.0306  0.0101  -0.0207 1094 TYR B C   
16872 O O   . TYR B 1096 ? 0.1855 0.2146 0.2040 0.0331  0.0107  -0.0204 1094 TYR B O   
16873 C CB  . TYR B 1096 ? 0.1653 0.1983 0.1870 0.0259  0.0104  -0.0191 1094 TYR B CB  
16874 C CG  . TYR B 1096 ? 0.1437 0.1738 0.1661 0.0256  0.0097  -0.0185 1094 TYR B CG  
16875 C CD1 . TYR B 1096 ? 0.1739 0.2010 0.1966 0.0232  0.0092  -0.0185 1094 TYR B CD1 
16876 C CD2 . TYR B 1096 ? 0.1828 0.2137 0.2055 0.0277  0.0096  -0.0177 1094 TYR B CD2 
16877 C CE1 . TYR B 1096 ? 0.1676 0.1927 0.1909 0.0229  0.0088  -0.0177 1094 TYR B CE1 
16878 C CE2 . TYR B 1096 ? 0.1801 0.2086 0.2031 0.0272  0.0091  -0.0169 1094 TYR B CE2 
16879 C CZ  . TYR B 1096 ? 0.1580 0.1837 0.1813 0.0247  0.0087  -0.0169 1094 TYR B CZ  
16880 O OH  . TYR B 1096 ? 0.1778 0.2015 0.2013 0.0243  0.0084  -0.0159 1094 TYR B OH  
16881 N N   . THR B 1097 ? 0.1681 0.1874 0.1850 0.0305  0.0091  -0.0213 1095 THR B N   
16882 C CA  . THR B 1097 ? 0.1488 0.1637 0.1637 0.0334  0.0086  -0.0218 1095 THR B CA  
16883 C C   . THR B 1097 ? 0.1707 0.1805 0.1858 0.0322  0.0075  -0.0211 1095 THR B C   
16884 O O   . THR B 1097 ? 0.1876 0.1962 0.2037 0.0293  0.0070  -0.0208 1095 THR B O   
16885 C CB  . THR B 1097 ? 0.2150 0.2259 0.2268 0.0347  0.0084  -0.0234 1095 THR B CB  
16886 O OG1 . THR B 1097 ? 0.2546 0.2617 0.2660 0.0319  0.0074  -0.0239 1095 THR B OG1 
16887 C CG2 . THR B 1097 ? 0.2265 0.2426 0.2378 0.0357  0.0098  -0.0240 1095 THR B CG2 
16888 N N   . LEU B 1098 ? 0.1736 0.1806 0.1875 0.0346  0.0071  -0.0207 1096 LEU B N   
16889 C CA  . LEU B 1098 ? 0.1774 0.1795 0.1912 0.0335  0.0059  -0.0198 1096 LEU B CA  
16890 C C   . LEU B 1098 ? 0.2053 0.1997 0.2158 0.0349  0.0048  -0.0208 1096 LEU B C   
16891 O O   . LEU B 1098 ? 0.1797 0.1724 0.1878 0.0384  0.0048  -0.0215 1096 LEU B O   
16892 C CB  . LEU B 1098 ? 0.1863 0.1903 0.2011 0.0346  0.0061  -0.0182 1096 LEU B CB  
16893 C CG  . LEU B 1098 ? 0.1588 0.1696 0.1766 0.0327  0.0069  -0.0172 1096 LEU B CG  
16894 C CD1 . LEU B 1098 ? 0.1789 0.1910 0.1972 0.0338  0.0067  -0.0156 1096 LEU B CD1 
16895 C CD2 . LEU B 1098 ? 0.1570 0.1673 0.1760 0.0290  0.0068  -0.0170 1096 LEU B CD2 
16896 N N   . HIS B 1099 ? 0.2028 0.1927 0.2130 0.0323  0.0037  -0.0209 1097 HIS B N   
16897 C CA  . HIS B 1099 ? 0.2044 0.1865 0.2113 0.0327  0.0022  -0.0218 1097 HIS B CA  
16898 C C   . HIS B 1099 ? 0.1996 0.1772 0.2066 0.0309  0.0010  -0.0204 1097 HIS B C   
16899 O O   . HIS B 1099 ? 0.1941 0.1750 0.2039 0.0291  0.0014  -0.0187 1097 HIS B O   
16900 C CB  . HIS B 1099 ? 0.2197 0.2005 0.2261 0.0305  0.0016  -0.0231 1097 HIS B CB  
16901 C CG  . HIS B 1099 ? 0.2816 0.2667 0.2876 0.0318  0.0028  -0.0243 1097 HIS B CG  
16902 N ND1 . HIS B 1099 ? 0.2728 0.2547 0.2751 0.0340  0.0026  -0.0261 1097 HIS B ND1 
16903 C CD2 . HIS B 1099 ? 0.2671 0.2591 0.2756 0.0311  0.0042  -0.0240 1097 HIS B CD2 
16904 C CE1 . HIS B 1099 ? 0.3002 0.2874 0.3029 0.0345  0.0039  -0.0267 1097 HIS B CE1 
16905 N NE2 . HIS B 1099 ? 0.2681 0.2613 0.2746 0.0326  0.0048  -0.0254 1097 HIS B NE2 
16906 N N   . ALA B 1100 ? 0.1996 0.1693 0.2033 0.0311  -0.0006 -0.0209 1098 ALA B N   
16907 C CA  . ALA B 1100 ? 0.2217 0.1870 0.2256 0.0286  -0.0020 -0.0193 1098 ALA B CA  
16908 C C   . ALA B 1100 ? 0.2303 0.1984 0.2375 0.0245  -0.0020 -0.0187 1098 ALA B C   
16909 O O   . ALA B 1100 ? 0.2375 0.2080 0.2455 0.0236  -0.0018 -0.0198 1098 ALA B O   
16910 C CB  . ALA B 1100 ? 0.2292 0.1850 0.2287 0.0293  -0.0040 -0.0201 1098 ALA B CB  
16911 N N   . ARG B 1101 ? 0.2159 0.1841 0.2250 0.0220  -0.0023 -0.0167 1099 ARG B N   
16912 C CA  . ARG B 1101 ? 0.2209 0.1917 0.2332 0.0182  -0.0023 -0.0160 1099 ARG B CA  
16913 C C   . ARG B 1101 ? 0.2150 0.1803 0.2259 0.0161  -0.0043 -0.0165 1099 ARG B C   
16914 O O   . ARG B 1101 ? 0.2249 0.1926 0.2379 0.0140  -0.0045 -0.0170 1099 ARG B O   
16915 C CB  . ARG B 1101 ? 0.2413 0.2143 0.2559 0.0163  -0.0018 -0.0136 1099 ARG B CB  
16916 C CG  . ARG B 1101 ? 0.2470 0.2272 0.2641 0.0170  0.0002  -0.0131 1099 ARG B CG  
16917 C CD  . ARG B 1101 ? 0.2750 0.2604 0.2955 0.0146  0.0010  -0.0129 1099 ARG B CD  
16918 N NE  . ARG B 1101 ? 0.2518 0.2432 0.2739 0.0152  0.0027  -0.0126 1099 ARG B NE  
16919 C CZ  . ARG B 1101 ? 0.2447 0.2404 0.2695 0.0134  0.0037  -0.0119 1099 ARG B CZ  
16920 N NH1 . ARG B 1101 ? 0.2405 0.2362 0.2672 0.0110  0.0034  -0.0114 1099 ARG B NH1 
16921 N NH2 . ARG B 1101 ? 0.2976 0.2978 0.3230 0.0142  0.0050  -0.0117 1099 ARG B NH2 
16922 N N   . GLY B 1102 ? 0.2174 0.1751 0.2248 0.0166  -0.0060 -0.0165 1100 GLY B N   
16923 C CA  . GLY B 1102 ? 0.2622 0.2141 0.2680 0.0141  -0.0082 -0.0169 1100 GLY B CA  
16924 C C   . GLY B 1102 ? 0.2685 0.2140 0.2726 0.0126  -0.0098 -0.0152 1100 GLY B C   
16925 O O   . GLY B 1102 ? 0.2515 0.1924 0.2523 0.0151  -0.0100 -0.0151 1100 GLY B O   
16926 N N   . ARG B 1103 ? 0.2455 0.1906 0.2516 0.0084  -0.0109 -0.0136 1101 ARG B N   
16927 C CA  . ARG B 1103 ? 0.2492 0.1886 0.2538 0.0062  -0.0124 -0.0116 1101 ARG B CA  
16928 C C   . ARG B 1103 ? 0.2427 0.1882 0.2514 0.0044  -0.0107 -0.0090 1101 ARG B C   
16929 O O   . ARG B 1103 ? 0.2467 0.1992 0.2599 0.0023  -0.0096 -0.0084 1101 ARG B O   
16930 C CB  . ARG B 1103 ? 0.2742 0.2085 0.2781 0.0023  -0.0150 -0.0115 1101 ARG B CB  
16931 C CG  . ARG B 1103 ? 0.3014 0.2281 0.3026 0.0001  -0.0170 -0.0094 1101 ARG B CG  
16932 C CD  . ARG B 1103 ? 0.3479 0.2677 0.3470 -0.0035 -0.0201 -0.0096 1101 ARG B CD  
16933 N NE  . ARG B 1103 ? 0.4211 0.3350 0.4156 -0.0012 -0.0216 -0.0126 1101 ARG B NE  
16934 C CZ  . ARG B 1103 ? 0.4580 0.3616 0.4461 0.0008  -0.0234 -0.0139 1101 ARG B CZ  
16935 N NH1 . ARG B 1103 ? 0.3638 0.2613 0.3491 0.0011  -0.0241 -0.0123 1101 ARG B NH1 
16936 N NH2 . ARG B 1103 ? 0.4215 0.3207 0.4057 0.0029  -0.0245 -0.0168 1101 ARG B NH2 
16937 N N   . ILE B 1104 ? 0.2210 0.1638 0.2278 0.0054  -0.0105 -0.0075 1102 ILE B N   
16938 C CA  . ILE B 1104 ? 0.2115 0.1597 0.2213 0.0041  -0.0089 -0.0050 1102 ILE B CA  
16939 C C   . ILE B 1104 ? 0.2314 0.1755 0.2409 0.0001  -0.0104 -0.0024 1102 ILE B C   
16940 O O   . ILE B 1104 ? 0.2459 0.1811 0.2511 0.0000  -0.0124 -0.0021 1102 ILE B O   
16941 C CB  . ILE B 1104 ? 0.2226 0.1713 0.2306 0.0078  -0.0077 -0.0048 1102 ILE B CB  
16942 C CG1 . ILE B 1104 ? 0.2016 0.1540 0.2097 0.0117  -0.0065 -0.0074 1102 ILE B CG1 
16943 C CG2 . ILE B 1104 ? 0.2031 0.1578 0.2140 0.0064  -0.0059 -0.0024 1102 ILE B CG2 
16944 C CD1 . ILE B 1104 ? 0.2199 0.1809 0.2323 0.0108  -0.0047 -0.0080 1102 ILE B CD1 
16945 N N   . LEU B 1105 ? 0.2123 0.1626 0.2260 -0.0033 -0.0093 -0.0006 1103 LEU B N   
16946 C CA  . LEU B 1105 ? 0.2516 0.1996 0.2656 -0.0074 -0.0103 0.0024  1103 LEU B CA  
16947 C C   . LEU B 1105 ? 0.2404 0.1867 0.2522 -0.0062 -0.0096 0.0044  1103 LEU B C   
16948 O O   . LEU B 1105 ? 0.2108 0.1634 0.2243 -0.0045 -0.0073 0.0047  1103 LEU B O   
16949 C CB  . LEU B 1105 ? 0.2211 0.1775 0.2407 -0.0108 -0.0090 0.0037  1103 LEU B CB  
16950 C CG  . LEU B 1105 ? 0.2552 0.2115 0.2760 -0.0153 -0.0094 0.0071  1103 LEU B CG  
16951 C CD1 . LEU B 1105 ? 0.2316 0.1795 0.2499 -0.0184 -0.0127 0.0076  1103 LEU B CD1 
16952 C CD2 . LEU B 1105 ? 0.2481 0.2146 0.2748 -0.0176 -0.0075 0.0082  1103 LEU B CD2 
16953 N N   . LEU B 1106 ? 0.2290 0.1665 0.2368 -0.0073 -0.0116 0.0058  1104 LEU B N   
16954 C CA  . LEU B 1106 ? 0.2375 0.1723 0.2427 -0.0063 -0.0114 0.0079  1104 LEU B CA  
16955 C C   . LEU B 1106 ? 0.2391 0.1739 0.2454 -0.0114 -0.0117 0.0115  1104 LEU B C   
16956 O O   . LEU B 1106 ? 0.2563 0.1857 0.2616 -0.0149 -0.0140 0.0123  1104 LEU B O   
16957 C CB  . LEU B 1106 ? 0.2445 0.1688 0.2437 -0.0033 -0.0135 0.0071  1104 LEU B CB  
16958 C CG  . LEU B 1106 ? 0.2991 0.2248 0.2969 0.0025  -0.0123 0.0051  1104 LEU B CG  
16959 C CD1 . LEU B 1106 ? 0.2988 0.2327 0.3003 0.0042  -0.0105 0.0025  1104 LEU B CD1 
16960 C CD2 . LEU B 1106 ? 0.2594 0.1746 0.2514 0.0057  -0.0146 0.0038  1104 LEU B CD2 
16961 N N   . VAL B 1107 ? 0.2268 0.1677 0.2350 -0.0119 -0.0096 0.0136  1105 VAL B N   
16962 C CA  . VAL B 1107 ? 0.2489 0.1906 0.2580 -0.0166 -0.0095 0.0172  1105 VAL B CA  
16963 C C   . VAL B 1107 ? 0.2401 0.1780 0.2453 -0.0153 -0.0094 0.0194  1105 VAL B C   
16964 O O   . VAL B 1107 ? 0.2487 0.1931 0.2553 -0.0147 -0.0071 0.0206  1105 VAL B O   
16965 C CB  . VAL B 1107 ? 0.2343 0.1875 0.2492 -0.0187 -0.0068 0.0180  1105 VAL B CB  
16966 C CG1 . VAL B 1107 ? 0.2645 0.2189 0.2807 -0.0240 -0.0068 0.0218  1105 VAL B CG1 
16967 C CG2 . VAL B 1107 ? 0.2295 0.1868 0.2481 -0.0187 -0.0068 0.0154  1105 VAL B CG2 
16968 N N   . PRO B 1108 ? 0.2499 0.1770 0.2499 -0.0148 -0.0120 0.0200  1106 PRO B N   
16969 C CA  . PRO B 1108 ? 0.2984 0.2213 0.2944 -0.0133 -0.0122 0.0222  1106 PRO B CA  
16970 C C   . PRO B 1108 ? 0.2918 0.2141 0.2876 -0.0184 -0.0124 0.0264  1106 PRO B C   
16971 O O   . PRO B 1108 ? 0.3189 0.2417 0.3168 -0.0232 -0.0130 0.0277  1106 PRO B O   
16972 C CB  . PRO B 1108 ? 0.2630 0.1741 0.2535 -0.0106 -0.0152 0.0209  1106 PRO B CB  
16973 C CG  . PRO B 1108 ? 0.2663 0.1732 0.2571 -0.0139 -0.0171 0.0200  1106 PRO B CG  
16974 C CD  . PRO B 1108 ? 0.2520 0.1698 0.2490 -0.0148 -0.0150 0.0183  1106 PRO B CD  
16975 N N   . ALA B 1109 ? 0.2990 0.2201 0.2920 -0.0173 -0.0119 0.0287  1107 ALA B N   
16976 C CA  . ALA B 1109 ? 0.3470 0.2653 0.3382 -0.0218 -0.0124 0.0330  1107 ALA B CA  
16977 C C   . ALA B 1109 ? 0.3322 0.2381 0.3168 -0.0206 -0.0153 0.0345  1107 ALA B C   
16978 O O   . ALA B 1109 ? 0.3374 0.2366 0.3195 -0.0250 -0.0172 0.0374  1107 ALA B O   
16979 C CB  . ALA B 1109 ? 0.3168 0.2444 0.3100 -0.0221 -0.0094 0.0350  1107 ALA B CB  
16980 N N   . THR B 1110 ? 0.3219 0.2244 0.3035 -0.0149 -0.0158 0.0326  1108 THR B N   
16981 C CA  . THR B 1110 ? 0.3414 0.2323 0.3166 -0.0127 -0.0184 0.0338  1108 THR B CA  
16982 C C   . THR B 1110 ? 0.3524 0.2364 0.3250 -0.0079 -0.0202 0.0301  1108 THR B C   
16983 O O   . THR B 1110 ? 0.3149 0.2043 0.2907 -0.0054 -0.0190 0.0267  1108 THR B O   
16984 C CB  . THR B 1110 ? 0.3730 0.2665 0.3465 -0.0097 -0.0172 0.0355  1108 THR B CB  
16985 O OG1 . THR B 1110 ? 0.3465 0.2472 0.3225 -0.0046 -0.0155 0.0324  1108 THR B OG1 
16986 C CG2 . THR B 1110 ? 0.3802 0.2807 0.3557 -0.0141 -0.0152 0.0391  1108 THR B CG2 
16987 N N   . GLU B 1111 ? 0.3593 0.2309 0.3258 -0.0065 -0.0231 0.0310  1109 GLU B N   
16988 C CA  . GLU B 1111 ? 0.3559 0.2200 0.3191 -0.0015 -0.0249 0.0276  1109 GLU B CA  
16989 C C   . GLU B 1111 ? 0.3398 0.2107 0.3047 0.0050  -0.0230 0.0251  1109 GLU B C   
16990 O O   . GLU B 1111 ? 0.3458 0.2189 0.3122 0.0081  -0.0225 0.0214  1109 GLU B O   
16991 C CB  . GLU B 1111 ? 0.3831 0.2325 0.3389 -0.0007 -0.0282 0.0292  1109 GLU B CB  
16992 C CG  . GLU B 1111 ? 0.4059 0.2475 0.3576 0.0058  -0.0298 0.0259  1109 GLU B CG  
16993 C CD  . GLU B 1111 ? 0.4002 0.2261 0.3442 0.0064  -0.0334 0.0274  1109 GLU B CD  
16994 O OE1 . GLU B 1111 ? 0.4205 0.2376 0.3617 0.0025  -0.0358 0.0275  1109 GLU B OE1 
16995 O OE2 . GLU B 1111 ? 0.4589 0.2810 0.3994 0.0108  -0.0340 0.0284  1109 GLU B OE2 
16996 N N   . SER B 1112 ? 0.3485 0.2229 0.3131 0.0069  -0.0220 0.0271  1110 SER B N   
16997 C CA  . SER B 1112 ? 0.3536 0.2351 0.3200 0.0126  -0.0204 0.0250  1110 SER B CA  
16998 C C   . SER B 1112 ? 0.3575 0.2512 0.3302 0.0119  -0.0176 0.0227  1110 SER B C   
16999 O O   . SER B 1112 ? 0.3346 0.2322 0.3089 0.0161  -0.0167 0.0196  1110 SER B O   
17000 C CB  . SER B 1112 ? 0.4045 0.2882 0.3696 0.0139  -0.0199 0.0280  1110 SER B CB  
17001 O OG  . SER B 1112 ? 0.3934 0.2841 0.3604 0.0192  -0.0186 0.0260  1110 SER B OG  
17002 N N   . GLY B 1113 ? 0.3089 0.2087 0.2850 0.0067  -0.0161 0.0243  1111 GLY B N   
17003 C CA  . GLY B 1113 ? 0.3146 0.2252 0.2964 0.0059  -0.0136 0.0221  1111 GLY B CA  
17004 C C   . GLY B 1113 ? 0.2715 0.1801 0.2542 0.0066  -0.0143 0.0188  1111 GLY B C   
17005 O O   . GLY B 1113 ? 0.2873 0.2024 0.2729 0.0091  -0.0128 0.0160  1111 GLY B O   
17006 N N   . LEU B 1114 ? 0.2936 0.1929 0.2735 0.0043  -0.0166 0.0190  1112 LEU B N   
17007 C CA  . LEU B 1114 ? 0.3044 0.2009 0.2843 0.0049  -0.0176 0.0158  1112 LEU B CA  
17008 C C   . LEU B 1114 ? 0.3044 0.1984 0.2820 0.0113  -0.0179 0.0129  1112 LEU B C   
17009 O O   . LEU B 1114 ? 0.2759 0.1741 0.2556 0.0132  -0.0170 0.0098  1112 LEU B O   
17010 C CB  . LEU B 1114 ? 0.3095 0.1953 0.2859 0.0011  -0.0205 0.0169  1112 LEU B CB  
17011 C CG  . LEU B 1114 ? 0.3130 0.1934 0.2878 0.0021  -0.0221 0.0135  1112 LEU B CG  
17012 C CD1 . LEU B 1114 ? 0.2775 0.1677 0.2580 0.0008  -0.0202 0.0114  1112 LEU B CD1 
17013 C CD2 . LEU B 1114 ? 0.3690 0.2377 0.3396 -0.0019 -0.0254 0.0147  1112 LEU B CD2 
17014 N N   . TYR B 1115 ? 0.3169 0.2042 0.2900 0.0148  -0.0192 0.0138  1113 TYR B N   
17015 C CA  . TYR B 1115 ? 0.3109 0.1968 0.2821 0.0213  -0.0193 0.0112  1113 TYR B CA  
17016 C C   . TYR B 1115 ? 0.2933 0.1915 0.2692 0.0240  -0.0165 0.0097  1113 TYR B C   
17017 O O   . TYR B 1115 ? 0.3028 0.2036 0.2796 0.0275  -0.0159 0.0067  1113 TYR B O   
17018 C CB  . TYR B 1115 ? 0.3289 0.2067 0.2950 0.0248  -0.0211 0.0129  1113 TYR B CB  
17019 C CG  . TYR B 1115 ? 0.3476 0.2112 0.3077 0.0232  -0.0242 0.0139  1113 TYR B CG  
17020 C CD1 . TYR B 1115 ? 0.3538 0.2121 0.3129 0.0198  -0.0256 0.0126  1113 TYR B CD1 
17021 C CD2 . TYR B 1115 ? 0.3829 0.2382 0.3380 0.0252  -0.0260 0.0162  1113 TYR B CD2 
17022 C CE1 . TYR B 1115 ? 0.4018 0.2464 0.3550 0.0181  -0.0287 0.0136  1113 TYR B CE1 
17023 C CE2 . TYR B 1115 ? 0.3823 0.2238 0.3315 0.0237  -0.0291 0.0172  1113 TYR B CE2 
17024 C CZ  . TYR B 1115 ? 0.4521 0.2882 0.4003 0.0200  -0.0305 0.0159  1113 TYR B CZ  
17025 O OH  . TYR B 1115 ? 0.4588 0.2806 0.4006 0.0182  -0.0338 0.0169  1113 TYR B OH  
17026 N N   . HIS B 1116 ? 0.2703 0.1761 0.2491 0.0222  -0.0149 0.0119  1114 HIS B N   
17027 C CA  . HIS B 1116 ? 0.2753 0.1925 0.2584 0.0241  -0.0124 0.0107  1114 HIS B CA  
17028 C C   . HIS B 1116 ? 0.2925 0.2159 0.2798 0.0220  -0.0110 0.0084  1114 HIS B C   
17029 O O   . HIS B 1116 ? 0.2847 0.2139 0.2741 0.0248  -0.0097 0.0060  1114 HIS B O   
17030 C CB  . HIS B 1116 ? 0.2680 0.1912 0.2527 0.0224  -0.0112 0.0135  1114 HIS B CB  
17031 C CG  . HIS B 1116 ? 0.3196 0.2405 0.3013 0.0260  -0.0121 0.0152  1114 HIS B CG  
17032 N ND1 . HIS B 1116 ? 0.3464 0.2583 0.3237 0.0254  -0.0141 0.0178  1114 HIS B ND1 
17033 C CD2 . HIS B 1116 ? 0.3425 0.2689 0.3251 0.0301  -0.0114 0.0147  1114 HIS B CD2 
17034 C CE1 . HIS B 1116 ? 0.3607 0.2727 0.3362 0.0293  -0.0146 0.0189  1114 HIS B CE1 
17035 N NE2 . HIS B 1116 ? 0.3478 0.2688 0.3266 0.0322  -0.0130 0.0170  1114 HIS B NE2 
17036 N N   . GLN B 1117 ? 0.2465 0.1688 0.2349 0.0170  -0.0112 0.0092  1115 GLN B N   
17037 C CA  . GLN B 1117 ? 0.2221 0.1497 0.2143 0.0151  -0.0101 0.0071  1115 GLN B CA  
17038 C C   . GLN B 1117 ? 0.2462 0.1695 0.2366 0.0180  -0.0112 0.0040  1115 GLN B C   
17039 O O   . GLN B 1117 ? 0.2481 0.1773 0.2411 0.0193  -0.0099 0.0016  1115 GLN B O   
17040 C CB  . GLN B 1117 ? 0.2454 0.1725 0.2391 0.0094  -0.0105 0.0088  1115 GLN B CB  
17041 C CG  . GLN B 1117 ? 0.2459 0.1796 0.2423 0.0064  -0.0088 0.0115  1115 GLN B CG  
17042 C CD  . GLN B 1117 ? 0.2340 0.1675 0.2322 0.0008  -0.0091 0.0133  1115 GLN B CD  
17043 O OE1 . GLN B 1117 ? 0.2606 0.1875 0.2572 -0.0011 -0.0111 0.0130  1115 GLN B OE1 
17044 N NE2 . GLN B 1117 ? 0.2465 0.1874 0.2477 -0.0018 -0.0071 0.0152  1115 GLN B NE2 
17045 N N   . LEU B 1118 ? 0.2348 0.1475 0.2205 0.0188  -0.0136 0.0040  1116 LEU B N   
17046 C CA  . LEU B 1118 ? 0.2541 0.1617 0.2371 0.0218  -0.0146 0.0009  1116 LEU B CA  
17047 C C   . LEU B 1118 ? 0.2599 0.1718 0.2431 0.0275  -0.0133 -0.0010 1116 LEU B C   
17048 O O   . LEU B 1118 ? 0.2688 0.1836 0.2530 0.0293  -0.0126 -0.0038 1116 LEU B O   
17049 C CB  . LEU B 1118 ? 0.2770 0.1714 0.2540 0.0220  -0.0175 0.0013  1116 LEU B CB  
17050 C CG  . LEU B 1118 ? 0.3625 0.2511 0.3386 0.0164  -0.0194 0.0024  1116 LEU B CG  
17051 C CD1 . LEU B 1118 ? 0.3564 0.2314 0.3259 0.0168  -0.0224 0.0033  1116 LEU B CD1 
17052 C CD2 . LEU B 1118 ? 0.3434 0.2335 0.3209 0.0153  -0.0195 -0.0004 1116 LEU B CD2 
17053 N N   . ALA B 1119 ? 0.2767 0.1898 0.2592 0.0303  -0.0130 0.0005  1117 ALA B N   
17054 C CA  . ALA B 1119 ? 0.2461 0.1643 0.2293 0.0356  -0.0118 -0.0010 1117 ALA B CA  
17055 C C   . ALA B 1119 ? 0.2664 0.1958 0.2547 0.0349  -0.0094 -0.0023 1117 ALA B C   
17056 O O   . ALA B 1119 ? 0.2683 0.2008 0.2572 0.0378  -0.0086 -0.0048 1117 ALA B O   
17057 C CB  . ALA B 1119 ? 0.2619 0.1806 0.2441 0.0381  -0.0119 0.0013  1117 ALA B CB  
17058 N N   . ALA B 1120 ? 0.2553 0.1909 0.2471 0.0309  -0.0083 -0.0007 1118 ALA B N   
17059 C CA  . ALA B 1120 ? 0.2111 0.1567 0.2075 0.0300  -0.0062 -0.0018 1118 ALA B CA  
17060 C C   . ALA B 1120 ? 0.2510 0.1966 0.2482 0.0290  -0.0061 -0.0043 1118 ALA B C   
17061 O O   . ALA B 1120 ? 0.2254 0.1763 0.2243 0.0309  -0.0049 -0.0062 1118 ALA B O   
17062 C CB  . ALA B 1120 ? 0.2679 0.2186 0.2671 0.0259  -0.0051 0.0004  1118 ALA B CB  
17063 N N   . ALA B 1121 ? 0.2254 0.1649 0.2213 0.0258  -0.0074 -0.0041 1119 ALA B N   
17064 C CA  . ALA B 1121 ? 0.2227 0.1619 0.2193 0.0245  -0.0076 -0.0062 1119 ALA B CA  
17065 C C   . ALA B 1121 ? 0.2136 0.1484 0.2068 0.0286  -0.0083 -0.0088 1119 ALA B C   
17066 O O   . ALA B 1121 ? 0.2345 0.1729 0.2289 0.0293  -0.0075 -0.0110 1119 ALA B O   
17067 C CB  . ALA B 1121 ? 0.2423 0.1762 0.2384 0.0199  -0.0092 -0.0051 1119 ALA B CB  
17068 N N   . LEU B 1122 ? 0.2281 0.1547 0.2168 0.0313  -0.0098 -0.0087 1120 LEU B N   
17069 C CA  . LEU B 1122 ? 0.2566 0.1786 0.2417 0.0356  -0.0104 -0.0113 1120 LEU B CA  
17070 C C   . LEU B 1122 ? 0.2407 0.1707 0.2276 0.0399  -0.0084 -0.0124 1120 LEU B C   
17071 O O   . LEU B 1122 ? 0.2266 0.1579 0.2129 0.0421  -0.0078 -0.0149 1120 LEU B O   
17072 C CB  . LEU B 1122 ? 0.2696 0.1806 0.2491 0.0378  -0.0126 -0.0108 1120 LEU B CB  
17073 C CG  . LEU B 1122 ? 0.2972 0.1985 0.2737 0.0336  -0.0150 -0.0099 1120 LEU B CG  
17074 C CD1 . LEU B 1122 ? 0.3154 0.2055 0.2861 0.0362  -0.0172 -0.0093 1120 LEU B CD1 
17075 C CD2 . LEU B 1122 ? 0.2892 0.1881 0.2649 0.0318  -0.0158 -0.0122 1120 LEU B CD2 
17076 N N   . ALA B 1123 ? 0.2369 0.1725 0.2261 0.0409  -0.0074 -0.0106 1121 ALA B N   
17077 C CA  . ALA B 1123 ? 0.2387 0.1823 0.2299 0.0447  -0.0057 -0.0114 1121 ALA B CA  
17078 C C   . ALA B 1123 ? 0.2531 0.2049 0.2480 0.0432  -0.0039 -0.0128 1121 ALA B C   
17079 O O   . ALA B 1123 ? 0.2206 0.1778 0.2164 0.0463  -0.0027 -0.0142 1121 ALA B O   
17080 C CB  . ALA B 1123 ? 0.2260 0.1741 0.2191 0.0451  -0.0052 -0.0089 1121 ALA B CB  
17081 N N   . THR B 1124 ? 0.2174 0.1705 0.2144 0.0385  -0.0038 -0.0124 1122 THR B N   
17082 C CA  . THR B 1124 ? 0.2001 0.1600 0.2003 0.0367  -0.0025 -0.0136 1122 THR B CA  
17083 C C   . THR B 1124 ? 0.1992 0.1549 0.1977 0.0358  -0.0032 -0.0156 1122 THR B C   
17084 O O   . THR B 1124 ? 0.2182 0.1782 0.2191 0.0335  -0.0025 -0.0164 1122 THR B O   
17085 C CB  . THR B 1124 ? 0.1986 0.1636 0.2025 0.0326  -0.0017 -0.0119 1122 THR B CB  
17086 O OG1 . THR B 1124 ? 0.2081 0.1675 0.2111 0.0297  -0.0030 -0.0102 1122 THR B OG1 
17087 C CG2 . THR B 1124 ? 0.2081 0.1797 0.2140 0.0338  -0.0006 -0.0105 1122 THR B CG2 
17088 N N   . GLY B 1125 ? 0.2120 0.1589 0.2060 0.0376  -0.0048 -0.0166 1123 GLY B N   
17089 C CA  . GLY B 1125 ? 0.2005 0.1429 0.1918 0.0375  -0.0056 -0.0188 1123 GLY B CA  
17090 C C   . GLY B 1125 ? 0.2084 0.1463 0.1996 0.0328  -0.0073 -0.0184 1123 GLY B C   
17091 O O   . GLY B 1125 ? 0.2282 0.1629 0.2175 0.0323  -0.0081 -0.0203 1123 GLY B O   
17092 N N   . ASN B 1126 ? 0.2208 0.1586 0.2140 0.0294  -0.0077 -0.0161 1124 ASN B N   
17093 C CA  . ASN B 1126 ? 0.2022 0.1381 0.1967 0.0246  -0.0089 -0.0154 1124 ASN B CA  
17094 C C   . ASN B 1126 ? 0.2275 0.1525 0.2175 0.0235  -0.0116 -0.0151 1124 ASN B C   
17095 O O   . ASN B 1126 ? 0.2557 0.1746 0.2420 0.0261  -0.0124 -0.0148 1124 ASN B O   
17096 C CB  . ASN B 1126 ? 0.2240 0.1657 0.2229 0.0213  -0.0080 -0.0128 1124 ASN B CB  
17097 C CG  . ASN B 1126 ? 0.1874 0.1390 0.1903 0.0220  -0.0056 -0.0130 1124 ASN B CG  
17098 O OD1 . ASN B 1126 ? 0.2200 0.1757 0.2250 0.0209  -0.0050 -0.0143 1124 ASN B OD1 
17099 N ND2 . ASN B 1126 ? 0.1956 0.1510 0.1995 0.0235  -0.0044 -0.0118 1124 ASN B ND2 
17100 N N   . SER B 1127 ? 0.2455 0.1681 0.2358 0.0196  -0.0131 -0.0152 1125 SER B N   
17101 C CA  . SER B 1127 ? 0.2453 0.1589 0.2327 0.0167  -0.0157 -0.0141 1125 SER B CA  
17102 C C   . SER B 1127 ? 0.2605 0.1778 0.2519 0.0125  -0.0153 -0.0110 1125 SER B C   
17103 O O   . SER B 1127 ? 0.2531 0.1796 0.2492 0.0119  -0.0132 -0.0101 1125 SER B O   
17104 C CB  . SER B 1127 ? 0.2710 0.1800 0.2564 0.0145  -0.0177 -0.0158 1125 SER B CB  
17105 O OG  . SER B 1127 ? 0.3119 0.2290 0.3024 0.0117  -0.0168 -0.0157 1125 SER B OG  
17106 N N   . VAL B 1128 ? 0.2636 0.1737 0.2528 0.0094  -0.0175 -0.0092 1126 VAL B N   
17107 C CA  . VAL B 1128 ? 0.2562 0.1697 0.2488 0.0054  -0.0171 -0.0060 1126 VAL B CA  
17108 C C   . VAL B 1128 ? 0.2751 0.1840 0.2676 0.0001  -0.0195 -0.0048 1126 VAL B C   
17109 O O   . VAL B 1128 ? 0.2989 0.1988 0.2869 -0.0003 -0.0221 -0.0060 1126 VAL B O   
17110 C CB  . VAL B 1128 ? 0.2574 0.1678 0.2479 0.0070  -0.0169 -0.0039 1126 VAL B CB  
17111 C CG1 . VAL B 1128 ? 0.2405 0.1565 0.2317 0.0120  -0.0146 -0.0049 1126 VAL B CG1 
17112 C CG2 . VAL B 1128 ? 0.2872 0.1850 0.2713 0.0078  -0.0197 -0.0040 1126 VAL B CG2 
17113 N N   . ALA B 1129 ? 0.2567 0.1723 0.2541 -0.0040 -0.0186 -0.0024 1127 ALA B N   
17114 C CA  . ALA B 1129 ? 0.2633 0.1758 0.2613 -0.0095 -0.0207 -0.0002 1127 ALA B CA  
17115 C C   . ALA B 1129 ? 0.2591 0.1730 0.2581 -0.0113 -0.0197 0.0033  1127 ALA B C   
17116 O O   . ALA B 1129 ? 0.2584 0.1814 0.2616 -0.0110 -0.0170 0.0043  1127 ALA B O   
17117 C CB  . ALA B 1129 ? 0.2595 0.1795 0.2629 -0.0129 -0.0204 -0.0003 1127 ALA B CB  
17118 N N   . ILE B 1130 ? 0.2607 0.1651 0.2553 -0.0130 -0.0220 0.0050  1128 ILE B N   
17119 C CA  . ILE B 1130 ? 0.2539 0.1582 0.2484 -0.0146 -0.0214 0.0084  1128 ILE B CA  
17120 C C   . ILE B 1130 ? 0.2634 0.1697 0.2609 -0.0211 -0.0222 0.0114  1128 ILE B C   
17121 O O   . ILE B 1130 ? 0.2672 0.1678 0.2633 -0.0245 -0.0250 0.0113  1128 ILE B O   
17122 C CB  . ILE B 1130 ? 0.2830 0.1753 0.2706 -0.0124 -0.0234 0.0088  1128 ILE B CB  
17123 C CG1 . ILE B 1130 ? 0.3153 0.2053 0.2997 -0.0057 -0.0229 0.0056  1128 ILE B CG1 
17124 C CG2 . ILE B 1130 ? 0.2744 0.1677 0.2619 -0.0134 -0.0225 0.0123  1128 ILE B CG2 
17125 C CD1 . ILE B 1130 ? 0.2941 0.1712 0.2712 -0.0031 -0.0254 0.0054  1128 ILE B CD1 
17126 N N   . ASP B 1131 ? 0.2442 0.1587 0.2457 -0.0229 -0.0199 0.0140  1129 ASP B N   
17127 C CA  . ASP B 1131 ? 0.2439 0.1619 0.2488 -0.0290 -0.0201 0.0173  1129 ASP B CA  
17128 C C   . ASP B 1131 ? 0.2654 0.1724 0.2656 -0.0326 -0.0233 0.0197  1129 ASP B C   
17129 O O   . ASP B 1131 ? 0.3014 0.2032 0.2978 -0.0316 -0.0234 0.0215  1129 ASP B O   
17130 C CB  . ASP B 1131 ? 0.2564 0.1844 0.2653 -0.0293 -0.0168 0.0195  1129 ASP B CB  
17131 C CG  . ASP B 1131 ? 0.2644 0.1969 0.2769 -0.0354 -0.0166 0.0232  1129 ASP B CG  
17132 O OD1 . ASP B 1131 ? 0.2547 0.1875 0.2695 -0.0391 -0.0183 0.0232  1129 ASP B OD1 
17133 O OD2 . ASP B 1131 ? 0.2788 0.2144 0.2916 -0.0364 -0.0149 0.0260  1129 ASP B OD2 
17134 N N   . ALA B 1132 ? 0.2932 0.1963 0.2934 -0.0369 -0.0260 0.0198  1130 ALA B N   
17135 C CA  . ALA B 1132 ? 0.2832 0.1750 0.2785 -0.0408 -0.0293 0.0221  1130 ALA B CA  
17136 C C   . ALA B 1132 ? 0.3214 0.2161 0.3182 -0.0451 -0.0283 0.0267  1130 ALA B C   
17137 O O   . ALA B 1132 ? 0.3336 0.2186 0.3253 -0.0467 -0.0304 0.0290  1130 ALA B O   
17138 C CB  . ALA B 1132 ? 0.2988 0.1871 0.2945 -0.0452 -0.0325 0.0215  1130 ALA B CB  
17139 N N   . ALA B 1133 ? 0.3110 0.2189 0.3145 -0.0467 -0.0252 0.0283  1131 ALA B N   
17140 C CA  . ALA B 1133 ? 0.3395 0.2511 0.3446 -0.0507 -0.0240 0.0328  1131 ALA B CA  
17141 C C   . ALA B 1133 ? 0.3510 0.2592 0.3519 -0.0474 -0.0228 0.0339  1131 ALA B C   
17142 O O   . ALA B 1133 ? 0.3685 0.2774 0.3690 -0.0507 -0.0222 0.0378  1131 ALA B O   
17143 C CB  . ALA B 1133 ? 0.3290 0.2559 0.3421 -0.0525 -0.0207 0.0338  1131 ALA B CB  
17144 N N   . SER B 1134 ? 0.3035 0.2084 0.3013 -0.0411 -0.0224 0.0308  1132 SER B N   
17145 C CA  . SER B 1134 ? 0.3279 0.2286 0.3213 -0.0377 -0.0218 0.0319  1132 SER B CA  
17146 C C   . SER B 1134 ? 0.3086 0.1958 0.2954 -0.0399 -0.0252 0.0342  1132 SER B C   
17147 O O   . SER B 1134 ? 0.3388 0.2228 0.3223 -0.0392 -0.0249 0.0366  1132 SER B O   
17148 C CB  . SER B 1134 ? 0.2949 0.1948 0.2865 -0.0305 -0.0210 0.0280  1132 SER B CB  
17149 O OG  . SER B 1134 ? 0.3025 0.1920 0.2898 -0.0289 -0.0240 0.0254  1132 SER B OG  
17150 N N   . GLY B 1135 ? 0.3251 0.2036 0.3095 -0.0425 -0.0285 0.0334  1133 GLY B N   
17151 C CA  . GLY B 1135 ? 0.3544 0.2187 0.3320 -0.0447 -0.0321 0.0353  1133 GLY B CA  
17152 C C   . GLY B 1135 ? 0.3706 0.2243 0.3413 -0.0385 -0.0334 0.0334  1133 GLY B C   
17153 O O   . GLY B 1135 ? 0.3923 0.2347 0.3570 -0.0394 -0.0358 0.0356  1133 GLY B O   
17154 N N   . LEU B 1136 ? 0.3645 0.2216 0.3359 -0.0321 -0.0318 0.0295  1134 LEU B N   
17155 C CA  . LEU B 1136 ? 0.3877 0.2370 0.3535 -0.0255 -0.0325 0.0278  1134 LEU B CA  
17156 C C   . LEU B 1136 ? 0.4036 0.2423 0.3645 -0.0227 -0.0353 0.0241  1134 LEU B C   
17157 O O   . LEU B 1136 ? 0.4099 0.2449 0.3676 -0.0162 -0.0352 0.0216  1134 LEU B O   
17158 C CB  . LEU B 1136 ? 0.3615 0.2217 0.3310 -0.0202 -0.0289 0.0262  1134 LEU B CB  
17159 C CG  . LEU B 1136 ? 0.3568 0.2269 0.3301 -0.0220 -0.0260 0.0294  1134 LEU B CG  
17160 C CD1 . LEU B 1136 ? 0.3462 0.2275 0.3234 -0.0172 -0.0227 0.0273  1134 LEU B CD1 
17161 C CD2 . LEU B 1136 ? 0.3891 0.2515 0.3573 -0.0224 -0.0273 0.0329  1134 LEU B CD2 
17162 N N   . GLN B 1137 ? 0.3842 0.2182 0.3446 -0.0273 -0.0377 0.0238  1135 GLN B N   
17163 C CA  . GLN B 1137 ? 0.3993 0.2237 0.3550 -0.0247 -0.0403 0.0200  1135 GLN B CA  
17164 C C   . GLN B 1137 ? 0.4604 0.2705 0.4076 -0.0202 -0.0426 0.0194  1135 GLN B C   
17165 O O   . GLN B 1137 ? 0.4445 0.2500 0.3882 -0.0143 -0.0430 0.0157  1135 GLN B O   
17166 C CB  . GLN B 1137 ? 0.4294 0.2494 0.3849 -0.0313 -0.0432 0.0204  1135 GLN B CB  
17167 C CG  . GLN B 1137 ? 0.4089 0.2419 0.3722 -0.0344 -0.0414 0.0197  1135 GLN B CG  
17168 C CD  . GLN B 1137 ? 0.3799 0.2242 0.3499 -0.0394 -0.0392 0.0237  1135 GLN B CD  
17169 O OE1 . GLN B 1137 ? 0.3821 0.2260 0.3511 -0.0401 -0.0384 0.0269  1135 GLN B OE1 
17170 N NE2 . GLN B 1137 ? 0.4051 0.2597 0.3817 -0.0429 -0.0382 0.0236  1135 GLN B NE2 
17171 N N   . ALA B 1138 ? 0.4127 0.2158 0.3564 -0.0225 -0.0440 0.0232  1136 ALA B N   
17172 C CA  . ALA B 1138 ? 0.4508 0.2393 0.3860 -0.0184 -0.0466 0.0229  1136 ALA B CA  
17173 C C   . ALA B 1138 ? 0.4963 0.2880 0.4310 -0.0102 -0.0443 0.0212  1136 ALA B C   
17174 O O   . ALA B 1138 ? 0.5405 0.3211 0.4686 -0.0053 -0.0462 0.0201  1136 ALA B O   
17175 C CB  . ALA B 1138 ? 0.4291 0.2096 0.3607 -0.0233 -0.0487 0.0277  1136 ALA B CB  
17176 N N   . SER B 1139 ? 0.4766 0.2833 0.4182 -0.0086 -0.0405 0.0210  1137 SER B N   
17177 C CA  . SER B 1139 ? 0.4536 0.2650 0.3956 -0.0013 -0.0383 0.0196  1137 SER B CA  
17178 C C   . SER B 1139 ? 0.4967 0.3072 0.4374 0.0049  -0.0381 0.0148  1137 SER B C   
17179 O O   . SER B 1139 ? 0.4707 0.2825 0.4104 0.0114  -0.0369 0.0135  1137 SER B O   
17180 C CB  . SER B 1139 ? 0.4251 0.2524 0.3746 -0.0022 -0.0345 0.0209  1137 SER B CB  
17181 O OG  . SER B 1139 ? 0.4381 0.2662 0.3880 -0.0065 -0.0344 0.0255  1137 SER B OG  
17182 N N   . LEU B 1140 ? 0.4561 0.2650 0.3970 0.0029  -0.0390 0.0122  1138 LEU B N   
17183 C CA  . LEU B 1140 ? 0.5054 0.3134 0.4447 0.0083  -0.0388 0.0076  1138 LEU B CA  
17184 C C   . LEU B 1140 ? 0.5359 0.3277 0.4669 0.0093  -0.0425 0.0058  1138 LEU B C   
17185 O O   . LEU B 1140 ? 0.5326 0.3224 0.4620 0.0114  -0.0429 0.0021  1138 LEU B O   
17186 C CB  . LEU B 1140 ? 0.4749 0.2942 0.4205 0.0061  -0.0368 0.0057  1138 LEU B CB  
17187 C CG  . LEU B 1140 ? 0.4527 0.2878 0.4063 0.0054  -0.0331 0.0070  1138 LEU B CG  
17188 C CD1 . LEU B 1140 ? 0.4515 0.2965 0.4105 0.0042  -0.0314 0.0046  1138 LEU B CD1 
17189 C CD2 . LEU B 1140 ? 0.4745 0.3140 0.4283 0.0117  -0.0310 0.0068  1138 LEU B CD2 
17190 N N   . LYS B 1141 ? 0.5696 0.3493 0.4948 0.0079  -0.0453 0.0083  1139 LYS B N   
17191 C CA  . LYS B 1141 ? 0.5903 0.3533 0.5068 0.0093  -0.0490 0.0065  1139 LYS B CA  
17192 C C   . LYS B 1141 ? 0.5696 0.3292 0.4821 0.0185  -0.0484 0.0029  1139 LYS B C   
17193 O O   . LYS B 1141 ? 0.5965 0.3618 0.5107 0.0235  -0.0463 0.0034  1139 LYS B O   
17194 C CB  . LYS B 1141 ? 0.5615 0.3120 0.4725 0.0058  -0.0522 0.0102  1139 LYS B CB  
17195 N N   . ASN B 1142 ? 0.6151 0.3661 0.5223 0.0207  -0.0502 -0.0009 1140 ASN B N   
17196 C CA  . ASN B 1142 ? 0.5708 0.3176 0.4734 0.0294  -0.0498 -0.0047 1140 ASN B CA  
17197 C C   . ASN B 1142 ? 0.5842 0.3467 0.4935 0.0339  -0.0456 -0.0068 1140 ASN B C   
17198 O O   . ASN B 1142 ? 0.5800 0.3430 0.4874 0.0415  -0.0443 -0.0089 1140 ASN B O   
17199 C CB  . ASN B 1142 ? 0.6308 0.3679 0.5276 0.0345  -0.0511 -0.0033 1140 ASN B CB  
17200 N N   . LEU B 1143 ? 0.5842 0.3596 0.5010 0.0293  -0.0435 -0.0063 1141 LEU B N   
17201 C CA  . LEU B 1143 ? 0.5484 0.3383 0.4714 0.0329  -0.0397 -0.0083 1141 LEU B CA  
17202 C C   . LEU B 1143 ? 0.5148 0.3010 0.4337 0.0379  -0.0397 -0.0129 1141 LEU B C   
17203 O O   . LEU B 1143 ? 0.5491 0.3262 0.4634 0.0357  -0.0422 -0.0146 1141 LEU B O   
17204 C CB  . LEU B 1143 ? 0.4989 0.3013 0.4298 0.0266  -0.0379 -0.0070 1141 LEU B CB  
17205 C CG  . LEU B 1143 ? 0.4908 0.3094 0.4293 0.0287  -0.0340 -0.0078 1141 LEU B CG  
17206 C CD1 . LEU B 1143 ? 0.4656 0.2909 0.4073 0.0306  -0.0321 -0.0051 1141 LEU B CD1 
17207 C CD2 . LEU B 1143 ? 0.4261 0.2538 0.3707 0.0226  -0.0330 -0.0074 1141 LEU B CD2 
17208 N N   . PRO B 1144 ? 0.5189 0.3122 0.4393 0.0447  -0.0371 -0.0149 1142 PRO B N   
17209 C CA  . PRO B 1144 ? 0.5364 0.3277 0.4532 0.0494  -0.0367 -0.0192 1142 PRO B CA  
17210 C C   . PRO B 1144 ? 0.4924 0.2897 0.4126 0.0449  -0.0361 -0.0207 1142 PRO B C   
17211 O O   . PRO B 1144 ? 0.4685 0.2774 0.3962 0.0405  -0.0344 -0.0189 1142 PRO B O   
17212 C CB  . PRO B 1144 ? 0.5478 0.3493 0.4679 0.0565  -0.0334 -0.0201 1142 PRO B CB  
17213 C CG  . PRO B 1144 ? 0.5272 0.3311 0.4498 0.0565  -0.0331 -0.0164 1142 PRO B CG  
17214 C CD  . PRO B 1144 ? 0.4847 0.2884 0.4099 0.0482  -0.0344 -0.0132 1142 PRO B CD  
17215 N N   . GLN B 1145 ? 0.5318 0.3210 0.4463 0.0460  -0.0377 -0.0240 1143 GLN B N   
17216 C CA  . GLN B 1145 ? 0.5038 0.2976 0.4207 0.0418  -0.0376 -0.0255 1143 GLN B CA  
17217 C C   . GLN B 1145 ? 0.4978 0.3081 0.4224 0.0429  -0.0337 -0.0259 1143 GLN B C   
17218 O O   . GLN B 1145 ? 0.4433 0.2612 0.3731 0.0379  -0.0331 -0.0253 1143 GLN B O   
17219 C CB  . GLN B 1145 ? 0.5031 0.2861 0.4119 0.0442  -0.0396 -0.0294 1143 GLN B CB  
17220 N N   . THR B 1146 ? 0.4844 0.3006 0.4100 0.0495  -0.0311 -0.0269 1144 THR B N   
17221 C CA  . THR B 1146 ? 0.4651 0.2967 0.3978 0.0504  -0.0275 -0.0271 1144 THR B CA  
17222 C C   . THR B 1146 ? 0.4503 0.2914 0.3907 0.0450  -0.0264 -0.0237 1144 THR B C   
17223 O O   . THR B 1146 ? 0.4777 0.3289 0.4236 0.0421  -0.0248 -0.0238 1144 THR B O   
17224 C CB  . THR B 1146 ? 0.4409 0.2770 0.3736 0.0580  -0.0251 -0.0281 1144 THR B CB  
17225 O OG1 . THR B 1146 ? 0.5037 0.3354 0.4351 0.0598  -0.0259 -0.0257 1144 THR B OG1 
17226 C CG2 . THR B 1146 ? 0.5572 0.3865 0.4831 0.0636  -0.0254 -0.0319 1144 THR B CG2 
17227 N N   . VAL B 1147 ? 0.4104 0.2485 0.3511 0.0436  -0.0274 -0.0207 1145 VAL B N   
17228 C CA  . VAL B 1147 ? 0.4132 0.2599 0.3606 0.0384  -0.0264 -0.0174 1145 VAL B CA  
17229 C C   . VAL B 1147 ? 0.4163 0.2597 0.3643 0.0312  -0.0284 -0.0164 1145 VAL B C   
17230 O O   . VAL B 1147 ? 0.3947 0.2475 0.3488 0.0270  -0.0271 -0.0153 1145 VAL B O   
17231 C CB  . VAL B 1147 ? 0.3737 0.2191 0.3211 0.0395  -0.0265 -0.0144 1145 VAL B CB  
17232 C CG1 . VAL B 1147 ? 0.4096 0.2655 0.3641 0.0349  -0.0248 -0.0114 1145 VAL B CG1 
17233 C CG2 . VAL B 1147 ? 0.3875 0.2347 0.3336 0.0470  -0.0250 -0.0155 1145 VAL B CG2 
17234 N N   . GLY B 1148 ? 0.4315 0.2616 0.3731 0.0298  -0.0317 -0.0168 1146 GLY B N   
17235 C CA  . GLY B 1148 ? 0.4360 0.2628 0.3781 0.0226  -0.0340 -0.0156 1146 GLY B CA  
17236 C C   . GLY B 1148 ? 0.4337 0.2678 0.3795 0.0202  -0.0332 -0.0174 1146 GLY B C   
17237 O O   . GLY B 1148 ? 0.4216 0.2603 0.3719 0.0142  -0.0336 -0.0156 1146 GLY B O   
17238 N N   . LEU B 1149 ? 0.4134 0.2490 0.3574 0.0248  -0.0321 -0.0207 1147 LEU B N   
17239 C CA  . LEU B 1149 ? 0.4300 0.2719 0.3768 0.0229  -0.0315 -0.0225 1147 LEU B CA  
17240 C C   . LEU B 1149 ? 0.4282 0.2846 0.3836 0.0207  -0.0286 -0.0209 1147 LEU B C   
17241 O O   . LEU B 1149 ? 0.4034 0.2651 0.3621 0.0174  -0.0286 -0.0213 1147 LEU B O   
17242 C CB  . LEU B 1149 ? 0.4767 0.3174 0.4193 0.0288  -0.0305 -0.0263 1147 LEU B CB  
17243 C CG  . LEU B 1149 ? 0.5440 0.3698 0.4773 0.0307  -0.0335 -0.0287 1147 LEU B CG  
17244 C CD1 . LEU B 1149 ? 0.5389 0.3645 0.4682 0.0365  -0.0323 -0.0325 1147 LEU B CD1 
17245 C CD2 . LEU B 1149 ? 0.5836 0.4023 0.5150 0.0242  -0.0371 -0.0282 1147 LEU B CD2 
17246 N N   . ARG B 1150 ? 0.3815 0.2443 0.3404 0.0225  -0.0264 -0.0190 1148 ARG B N   
17247 C CA  . ARG B 1150 ? 0.3844 0.2603 0.3511 0.0205  -0.0237 -0.0173 1148 ARG B CA  
17248 C C   . ARG B 1150 ? 0.3255 0.2029 0.2958 0.0149  -0.0244 -0.0138 1148 ARG B C   
17249 O O   . ARG B 1150 ? 0.3067 0.1944 0.2831 0.0129  -0.0223 -0.0124 1148 ARG B O   
17250 C CB  . ARG B 1150 ? 0.3348 0.2172 0.3033 0.0254  -0.0210 -0.0171 1148 ARG B CB  
17251 C CG  . ARG B 1150 ? 0.3437 0.2289 0.3108 0.0307  -0.0194 -0.0201 1148 ARG B CG  
17252 C CD  . ARG B 1150 ? 0.3583 0.2569 0.3317 0.0311  -0.0164 -0.0198 1148 ARG B CD  
17253 N NE  . ARG B 1150 ? 0.3070 0.2090 0.2793 0.0365  -0.0146 -0.0221 1148 ARG B NE  
17254 C CZ  . ARG B 1150 ? 0.3182 0.2272 0.2930 0.0398  -0.0125 -0.0215 1148 ARG B CZ  
17255 N NH1 . ARG B 1150 ? 0.2764 0.1897 0.2547 0.0384  -0.0118 -0.0189 1148 ARG B NH1 
17256 N NH2 . ARG B 1150 ? 0.3101 0.2223 0.2839 0.0444  -0.0110 -0.0235 1148 ARG B NH2 
17257 N N   . VAL B 1151 ? 0.3450 0.2123 0.3113 0.0123  -0.0271 -0.0124 1149 VAL B N   
17258 C CA  . VAL B 1151 ? 0.3135 0.1816 0.2825 0.0073  -0.0277 -0.0088 1149 VAL B CA  
17259 C C   . VAL B 1151 ? 0.3730 0.2378 0.3423 0.0013  -0.0302 -0.0081 1149 VAL B C   
17260 O O   . VAL B 1151 ? 0.3861 0.2405 0.3498 0.0008  -0.0331 -0.0096 1149 VAL B O   
17261 C CB  . VAL B 1151 ? 0.3652 0.2246 0.3297 0.0089  -0.0289 -0.0070 1149 VAL B CB  
17262 C CG1 . VAL B 1151 ? 0.3990 0.2574 0.3651 0.0028  -0.0300 -0.0031 1149 VAL B CG1 
17263 C CG2 . VAL B 1151 ? 0.3585 0.2233 0.3240 0.0142  -0.0263 -0.0069 1149 VAL B CG2 
17264 N N   . SER B 1152 ? 0.3363 0.2099 0.3119 -0.0034 -0.0292 -0.0059 1150 SER B N   
17265 C CA  . SER B 1152 ? 0.3562 0.2276 0.3329 -0.0097 -0.0316 -0.0043 1150 SER B CA  
17266 C C   . SER B 1152 ? 0.3157 0.1918 0.2965 -0.0138 -0.0307 -0.0003 1150 SER B C   
17267 O O   . SER B 1152 ? 0.3360 0.2189 0.3196 -0.0117 -0.0280 0.0009  1150 SER B O   
17268 C CB  . SER B 1152 ? 0.3548 0.2330 0.3355 -0.0117 -0.0314 -0.0059 1150 SER B CB  
17269 O OG  . SER B 1152 ? 0.3976 0.2888 0.3852 -0.0112 -0.0281 -0.0052 1150 SER B OG  
17270 N N   . TRP B 1153 ? 0.3255 0.1978 0.3063 -0.0196 -0.0331 0.0019  1151 TRP B N   
17271 C CA  . TRP B 1153 ? 0.2987 0.1756 0.2834 -0.0242 -0.0324 0.0060  1151 TRP B CA  
17272 C C   . TRP B 1153 ? 0.3244 0.2102 0.3155 -0.0292 -0.0323 0.0069  1151 TRP B C   
17273 O O   . TRP B 1153 ? 0.3418 0.2242 0.3320 -0.0316 -0.0348 0.0056  1151 TRP B O   
17274 C CB  . TRP B 1153 ? 0.3444 0.2094 0.3236 -0.0272 -0.0355 0.0083  1151 TRP B CB  
17275 C CG  . TRP B 1153 ? 0.3414 0.1987 0.3150 -0.0224 -0.0354 0.0080  1151 TRP B CG  
17276 C CD1 . TRP B 1153 ? 0.3937 0.2406 0.3605 -0.0176 -0.0370 0.0052  1151 TRP B CD1 
17277 C CD2 . TRP B 1153 ? 0.3266 0.1861 0.3007 -0.0216 -0.0337 0.0109  1151 TRP B CD2 
17278 N NE1 . TRP B 1153 ? 0.3603 0.2031 0.3238 -0.0138 -0.0364 0.0061  1151 TRP B NE1 
17279 C CE2 . TRP B 1153 ? 0.3475 0.1978 0.3153 -0.0163 -0.0344 0.0096  1151 TRP B CE2 
17280 C CE3 . TRP B 1153 ? 0.3094 0.1778 0.2886 -0.0248 -0.0315 0.0143  1151 TRP B CE3 
17281 C CZ2 . TRP B 1153 ? 0.3819 0.2317 0.3485 -0.0143 -0.0334 0.0119  1151 TRP B CZ2 
17282 C CZ3 . TRP B 1153 ? 0.3250 0.1927 0.3026 -0.0229 -0.0304 0.0164  1151 TRP B CZ3 
17283 C CH2 . TRP B 1153 ? 0.3718 0.2302 0.3431 -0.0177 -0.0314 0.0153  1151 TRP B CH2 
17284 N N   . SER B 1154 ? 0.2820 0.1793 0.2795 -0.0305 -0.0294 0.0091  1152 SER B N   
17285 C CA  . SER B 1154 ? 0.2821 0.1895 0.2864 -0.0342 -0.0287 0.0098  1152 SER B CA  
17286 C C   . SER B 1154 ? 0.2613 0.1727 0.2691 -0.0399 -0.0285 0.0141  1152 SER B C   
17287 O O   . SER B 1154 ? 0.2920 0.2069 0.3008 -0.0394 -0.0263 0.0163  1152 SER B O   
17288 C CB  . SER B 1154 ? 0.2958 0.2147 0.3049 -0.0305 -0.0251 0.0083  1152 SER B CB  
17289 O OG  . SER B 1154 ? 0.2688 0.1970 0.2844 -0.0339 -0.0246 0.0091  1152 SER B OG  
17290 N N   . LYS B 1155 ? 0.2601 0.1714 0.2699 -0.0453 -0.0309 0.0153  1153 LYS B N   
17291 C CA  . LYS B 1155 ? 0.2902 0.2076 0.3048 -0.0511 -0.0307 0.0193  1153 LYS B CA  
17292 C C   . LYS B 1155 ? 0.2851 0.2165 0.3079 -0.0522 -0.0286 0.0194  1153 LYS B C   
17293 O O   . LYS B 1155 ? 0.3161 0.2543 0.3438 -0.0571 -0.0283 0.0226  1153 LYS B O   
17294 C CB  . LYS B 1155 ? 0.3079 0.2164 0.3196 -0.0570 -0.0349 0.0210  1153 LYS B CB  
17295 N N   . ASP B 1156 ? 0.2385 0.1741 0.2627 -0.0477 -0.0272 0.0161  1154 ASP B N   
17296 C CA  . ASP B 1156 ? 0.2247 0.1723 0.2560 -0.0483 -0.0256 0.0158  1154 ASP B CA  
17297 C C   . ASP B 1156 ? 0.2374 0.1885 0.2686 -0.0420 -0.0231 0.0125  1154 ASP B C   
17298 O O   . ASP B 1156 ? 0.2478 0.1955 0.2768 -0.0396 -0.0244 0.0094  1154 ASP B O   
17299 C CB  . ASP B 1156 ? 0.2367 0.1826 0.2689 -0.0518 -0.0291 0.0151  1154 ASP B CB  
17300 C CG  . ASP B 1156 ? 0.2367 0.1952 0.2768 -0.0529 -0.0278 0.0155  1154 ASP B CG  
17301 O OD1 . ASP B 1156 ? 0.2294 0.1961 0.2727 -0.0492 -0.0244 0.0145  1154 ASP B OD1 
17302 O OD2 . ASP B 1156 ? 0.2387 0.1989 0.2816 -0.0576 -0.0303 0.0167  1154 ASP B OD2 
17303 N N   . TRP B 1157 ? 0.2272 0.1850 0.2605 -0.0396 -0.0195 0.0133  1155 TRP B N   
17304 C CA  . TRP B 1157 ? 0.2419 0.2019 0.2745 -0.0339 -0.0173 0.0104  1155 TRP B CA  
17305 C C   . TRP B 1157 ? 0.2674 0.2339 0.3039 -0.0328 -0.0170 0.0083  1155 TRP B C   
17306 O O   . TRP B 1157 ? 0.2451 0.2093 0.2792 -0.0290 -0.0170 0.0053  1155 TRP B O   
17307 C CB  . TRP B 1157 ? 0.2448 0.2111 0.2790 -0.0319 -0.0138 0.0118  1155 TRP B CB  
17308 C CG  . TRP B 1157 ? 0.2211 0.1822 0.2517 -0.0327 -0.0137 0.0141  1155 TRP B CG  
17309 C CD1 . TRP B 1157 ? 0.2344 0.1847 0.2599 -0.0342 -0.0165 0.0148  1155 TRP B CD1 
17310 C CD2 . TRP B 1157 ? 0.2242 0.1902 0.2558 -0.0319 -0.0109 0.0160  1155 TRP B CD2 
17311 N NE1 . TRP B 1157 ? 0.2383 0.1867 0.2616 -0.0344 -0.0156 0.0173  1155 TRP B NE1 
17312 C CE2 . TRP B 1157 ? 0.2249 0.1830 0.2519 -0.0331 -0.0121 0.0180  1155 TRP B CE2 
17313 C CE3 . TRP B 1157 ? 0.2449 0.2209 0.2803 -0.0303 -0.0075 0.0161  1155 TRP B CE3 
17314 C CZ2 . TRP B 1157 ? 0.2630 0.2232 0.2892 -0.0327 -0.0100 0.0203  1155 TRP B CZ2 
17315 C CZ3 . TRP B 1157 ? 0.2467 0.2248 0.2813 -0.0299 -0.0054 0.0182  1155 TRP B CZ3 
17316 C CH2 . TRP B 1157 ? 0.2705 0.2409 0.3006 -0.0312 -0.0067 0.0203  1155 TRP B CH2 
17317 N N   . ALA B 1158 ? 0.2114 0.1862 0.2538 -0.0359 -0.0167 0.0099  1156 ALA B N   
17318 C CA  . ALA B 1158 ? 0.2518 0.2330 0.2980 -0.0346 -0.0163 0.0080  1156 ALA B CA  
17319 C C   . ALA B 1158 ? 0.2520 0.2269 0.2956 -0.0352 -0.0197 0.0059  1156 ALA B C   
17320 O O   . ALA B 1158 ? 0.2637 0.2404 0.3076 -0.0324 -0.0195 0.0034  1156 ALA B O   
17321 C CB  . ALA B 1158 ? 0.1942 0.1863 0.2476 -0.0374 -0.0151 0.0104  1156 ALA B CB  
17322 N N   . ALA B 1159 ? 0.2215 0.1889 0.2623 -0.0389 -0.0229 0.0070  1157 ALA B N   
17323 C CA  . ALA B 1159 ? 0.2510 0.2116 0.2886 -0.0396 -0.0263 0.0049  1157 ALA B CA  
17324 C C   . ALA B 1159 ? 0.2763 0.2276 0.3069 -0.0353 -0.0268 0.0018  1157 ALA B C   
17325 O O   . ALA B 1159 ? 0.2651 0.2127 0.2931 -0.0342 -0.0287 -0.0007 1157 ALA B O   
17326 C CB  . ALA B 1159 ? 0.2619 0.2171 0.2986 -0.0453 -0.0298 0.0071  1157 ALA B CB  
17327 N N   . ASP B 1160 ? 0.2617 0.2096 0.2890 -0.0326 -0.0251 0.0020  1158 ASP B N   
17328 C CA  . ASP B 1160 ? 0.2920 0.2306 0.3124 -0.0286 -0.0257 -0.0005 1158 ASP B CA  
17329 C C   . ASP B 1160 ? 0.3074 0.2504 0.3280 -0.0232 -0.0228 -0.0028 1158 ASP B C   
17330 O O   . ASP B 1160 ? 0.3106 0.2473 0.3260 -0.0195 -0.0228 -0.0048 1158 ASP B O   
17331 C CB  . ASP B 1160 ? 0.2657 0.1967 0.2819 -0.0291 -0.0262 0.0011  1158 ASP B CB  
17332 C CG  . ASP B 1160 ? 0.3120 0.2359 0.3263 -0.0343 -0.0297 0.0029  1158 ASP B CG  
17333 O OD1 . ASP B 1160 ? 0.3251 0.2481 0.3399 -0.0369 -0.0322 0.0022  1158 ASP B OD1 
17334 O OD2 . ASP B 1160 ? 0.3135 0.2326 0.3256 -0.0360 -0.0301 0.0052  1158 ASP B OD2 
17335 N N   . GLY B 1161 ? 0.2361 0.1894 0.2623 -0.0227 -0.0203 -0.0023 1159 GLY B N   
17336 C CA  . GLY B 1161 ? 0.2735 0.2311 0.3000 -0.0183 -0.0178 -0.0043 1159 GLY B CA  
17337 C C   . GLY B 1161 ? 0.3427 0.2999 0.3683 -0.0169 -0.0190 -0.0070 1159 GLY B C   
17338 O O   . GLY B 1161 ? 0.3432 0.2955 0.3670 -0.0191 -0.0218 -0.0076 1159 GLY B O   
17339 N N   . PRO B 1162 ? 0.3366 0.2987 0.3633 -0.0135 -0.0168 -0.0086 1160 PRO B N   
17340 C CA  . PRO B 1162 ? 0.2823 0.2508 0.3114 -0.0113 -0.0136 -0.0080 1160 PRO B CA  
17341 C C   . PRO B 1162 ? 0.2879 0.2517 0.3127 -0.0083 -0.0127 -0.0084 1160 PRO B C   
17342 O O   . PRO B 1162 ? 0.3246 0.2818 0.3447 -0.0062 -0.0138 -0.0102 1160 PRO B O   
17343 C CB  . PRO B 1162 ? 0.3385 0.3121 0.3693 -0.0091 -0.0125 -0.0099 1160 PRO B CB  
17344 C CG  . PRO B 1162 ? 0.3559 0.3228 0.3821 -0.0081 -0.0147 -0.0122 1160 PRO B CG  
17345 C CD  . PRO B 1162 ? 0.3529 0.3139 0.3777 -0.0116 -0.0177 -0.0113 1160 PRO B CD  
17346 N N   . PHE B 1163 ? 0.2351 0.2027 0.2617 -0.0080 -0.0106 -0.0068 1161 PHE B N   
17347 C CA  . PHE B 1163 ? 0.2435 0.2084 0.2668 -0.0049 -0.0095 -0.0070 1161 PHE B CA  
17348 C C   . PHE B 1163 ? 0.2124 0.1834 0.2371 -0.0018 -0.0070 -0.0083 1161 PHE B C   
17349 O O   . PHE B 1163 ? 0.2347 0.2114 0.2626 -0.0021 -0.0062 -0.0089 1161 PHE B O   
17350 C CB  . PHE B 1163 ? 0.2240 0.1884 0.2476 -0.0066 -0.0090 -0.0042 1161 PHE B CB  
17351 C CG  . PHE B 1163 ? 0.2365 0.1950 0.2589 -0.0103 -0.0115 -0.0027 1161 PHE B CG  
17352 C CD1 . PHE B 1163 ? 0.2834 0.2325 0.3008 -0.0098 -0.0139 -0.0038 1161 PHE B CD1 
17353 C CD2 . PHE B 1163 ? 0.2286 0.1910 0.2548 -0.0144 -0.0114 -0.0001 1161 PHE B CD2 
17354 C CE1 . PHE B 1163 ? 0.2949 0.2378 0.3108 -0.0134 -0.0165 -0.0024 1161 PHE B CE1 
17355 C CE2 . PHE B 1163 ? 0.2562 0.2132 0.2813 -0.0182 -0.0139 0.0016  1161 PHE B CE2 
17356 C CZ  . PHE B 1163 ? 0.2451 0.1921 0.2649 -0.0179 -0.0165 0.0004  1161 PHE B CZ  
17357 N N   . ALA B 1164 ? 0.2213 0.1909 0.2434 0.0013  -0.0061 -0.0087 1162 ALA B N   
17358 C CA  . ALA B 1164 ? 0.2419 0.2170 0.2650 0.0040  -0.0039 -0.0098 1162 ALA B CA  
17359 C C   . ALA B 1164 ? 0.2486 0.2263 0.2720 0.0049  -0.0023 -0.0082 1162 ALA B C   
17360 O O   . ALA B 1164 ? 0.2658 0.2469 0.2891 0.0074  -0.0008 -0.0090 1162 ALA B O   
17361 C CB  . ALA B 1164 ? 0.2398 0.2119 0.2595 0.0072  -0.0043 -0.0121 1162 ALA B CB  
17362 N N   . GLY B 1165 ? 0.2021 0.1782 0.2255 0.0029  -0.0026 -0.0060 1163 GLY B N   
17363 C CA  . GLY B 1165 ? 0.2091 0.1876 0.2327 0.0033  -0.0011 -0.0043 1163 GLY B CA  
17364 C C   . GLY B 1165 ? 0.2112 0.1853 0.2336 0.0009  -0.0022 -0.0019 1163 GLY B C   
17365 O O   . GLY B 1165 ? 0.1969 0.1658 0.2182 -0.0009 -0.0042 -0.0018 1163 GLY B O   
17366 N N   . ALA B 1166 ? 0.2124 0.1883 0.2347 0.0008  -0.0011 0.0000  1164 ALA B N   
17367 C CA  . ALA B 1166 ? 0.2166 0.1883 0.2375 -0.0016 -0.0020 0.0026  1164 ALA B CA  
17368 C C   . ALA B 1166 ? 0.2318 0.2031 0.2505 0.0001  -0.0012 0.0041  1164 ALA B C   
17369 O O   . ALA B 1166 ? 0.2318 0.2089 0.2516 0.0015  0.0007  0.0039  1164 ALA B O   
17370 C CB  . ALA B 1166 ? 0.2093 0.1857 0.2340 -0.0057 -0.0013 0.0045  1164 ALA B CB  
17371 N N   . LEU B 1167 ? 0.2012 0.1654 0.2164 -0.0002 -0.0028 0.0055  1165 LEU B N   
17372 C CA  . LEU B 1167 ? 0.2354 0.1984 0.2482 0.0009  -0.0024 0.0074  1165 LEU B CA  
17373 C C   . LEU B 1167 ? 0.2473 0.2080 0.2597 -0.0031 -0.0029 0.0107  1165 LEU B C   
17374 O O   . LEU B 1167 ? 0.2321 0.1869 0.2434 -0.0055 -0.0049 0.0113  1165 LEU B O   
17375 C CB  . LEU B 1167 ? 0.2534 0.2095 0.2620 0.0046  -0.0040 0.0066  1165 LEU B CB  
17376 C CG  . LEU B 1167 ? 0.2450 0.2030 0.2537 0.0085  -0.0036 0.0035  1165 LEU B CG  
17377 C CD1 . LEU B 1167 ? 0.2623 0.2132 0.2667 0.0121  -0.0051 0.0028  1165 LEU B CD1 
17378 C CD2 . LEU B 1167 ? 0.2451 0.2117 0.2562 0.0100  -0.0013 0.0031  1165 LEU B CD2 
17379 N N   . VAL B 1168 ? 0.2163 0.1817 0.2294 -0.0039 -0.0012 0.0127  1166 VAL B N   
17380 C CA  . VAL B 1168 ? 0.2372 0.2023 0.2504 -0.0080 -0.0012 0.0160  1166 VAL B CA  
17381 C C   . VAL B 1168 ? 0.2592 0.2220 0.2690 -0.0070 -0.0011 0.0183  1166 VAL B C   
17382 O O   . VAL B 1168 ? 0.2481 0.2146 0.2574 -0.0041 0.0002  0.0177  1166 VAL B O   
17383 C CB  . VAL B 1168 ? 0.2233 0.1977 0.2412 -0.0104 0.0012  0.0166  1166 VAL B CB  
17384 C CG1 . VAL B 1168 ? 0.2378 0.2127 0.2561 -0.0147 0.0015  0.0202  1166 VAL B CG1 
17385 C CG2 . VAL B 1168 ? 0.2114 0.1884 0.2329 -0.0109 0.0010  0.0142  1166 VAL B CG2 
17386 N N   . GLU B 1169 ? 0.2394 0.1958 0.2465 -0.0095 -0.0026 0.0210  1167 GLU B N   
17387 C CA  . GLU B 1169 ? 0.2479 0.2015 0.2514 -0.0094 -0.0027 0.0238  1167 GLU B CA  
17388 C C   . GLU B 1169 ? 0.2732 0.2293 0.2778 -0.0143 -0.0018 0.0273  1167 GLU B C   
17389 O O   . GLU B 1169 ? 0.2912 0.2453 0.2971 -0.0181 -0.0028 0.0283  1167 GLU B O   
17390 C CB  . GLU B 1169 ? 0.2722 0.2148 0.2708 -0.0079 -0.0056 0.0243  1167 GLU B CB  
17391 C CG  . GLU B 1169 ? 0.2846 0.2236 0.2792 -0.0076 -0.0060 0.0274  1167 GLU B CG  
17392 C CD  . GLU B 1169 ? 0.2956 0.2227 0.2851 -0.0069 -0.0091 0.0282  1167 GLU B CD  
17393 O OE1 . GLU B 1169 ? 0.3069 0.2282 0.2958 -0.0073 -0.0109 0.0267  1167 GLU B OE1 
17394 O OE2 . GLU B 1169 ? 0.3340 0.2571 0.3197 -0.0057 -0.0099 0.0305  1167 GLU B OE2 
17395 N N   . GLY B 1170 ? 0.2636 0.2244 0.2677 -0.0144 0.0000  0.0292  1168 GLY B N   
17396 C CA  . GLY B 1170 ? 0.2919 0.2552 0.2966 -0.0190 0.0011  0.0328  1168 GLY B CA  
17397 C C   . GLY B 1170 ? 0.3341 0.3050 0.3390 -0.0184 0.0038  0.0339  1168 GLY B C   
17398 O O   . GLY B 1170 ? 0.3148 0.2893 0.3196 -0.0147 0.0049  0.0317  1168 GLY B O   
17399 N N   . ASP B 1171 ? 0.3269 0.3000 0.3316 -0.0222 0.0050  0.0374  1169 ASP B N   
17400 C CA  . ASP B 1171 ? 0.3093 0.2901 0.3141 -0.0219 0.0078  0.0383  1169 ASP B CA  
17401 C C   . ASP B 1171 ? 0.3059 0.2962 0.3157 -0.0218 0.0104  0.0361  1169 ASP B C   
17402 O O   . ASP B 1171 ? 0.3178 0.3089 0.3313 -0.0221 0.0099  0.0341  1169 ASP B O   
17403 C CB  . ASP B 1171 ? 0.3326 0.3129 0.3351 -0.0258 0.0084  0.0428  1169 ASP B CB  
17404 C CG  . ASP B 1171 ? 0.3193 0.3015 0.3250 -0.0309 0.0087  0.0450  1169 ASP B CG  
17405 O OD1 . ASP B 1171 ? 0.3180 0.3039 0.3284 -0.0315 0.0090  0.0430  1169 ASP B OD1 
17406 O OD2 . ASP B 1171 ? 0.4057 0.3859 0.4092 -0.0345 0.0085  0.0490  1169 ASP B OD2 
17407 N N   . ALA B 1172 ? 0.3197 0.3170 0.3295 -0.0211 0.0132  0.0365  1170 ALA B N   
17408 C CA  . ALA B 1172 ? 0.3282 0.3340 0.3420 -0.0202 0.0156  0.0341  1170 ALA B CA  
17409 C C   . ALA B 1172 ? 0.3124 0.3220 0.3312 -0.0235 0.0162  0.0346  1170 ALA B C   
17410 O O   . ALA B 1172 ? 0.3230 0.3356 0.3456 -0.0224 0.0163  0.0319  1170 ALA B O   
17411 C CB  . ALA B 1172 ? 0.3401 0.3522 0.3523 -0.0195 0.0185  0.0349  1170 ALA B CB  
17412 N N   . GLU B 1173 ? 0.3122 0.3219 0.3312 -0.0277 0.0163  0.0383  1171 GLU B N   
17413 C CA  . GLU B 1173 ? 0.2929 0.3076 0.3172 -0.0309 0.0170  0.0390  1171 GLU B CA  
17414 C C   . GLU B 1173 ? 0.2779 0.2865 0.3037 -0.0319 0.0138  0.0378  1171 GLU B C   
17415 O O   . GLU B 1173 ? 0.3060 0.3188 0.3366 -0.0328 0.0140  0.0365  1171 GLU B O   
17416 C CB  . GLU B 1173 ? 0.3835 0.4011 0.4078 -0.0355 0.0182  0.0434  1171 GLU B CB  
17417 C CG  . GLU B 1173 ? 0.4156 0.4421 0.4399 -0.0347 0.0221  0.0443  1171 GLU B CG  
17418 C CD  . GLU B 1173 ? 0.4495 0.4842 0.4779 -0.0318 0.0244  0.0409  1171 GLU B CD  
17419 O OE1 . GLU B 1173 ? 0.4252 0.4639 0.4589 -0.0330 0.0244  0.0401  1171 GLU B OE1 
17420 O OE2 . GLU B 1173 ? 0.4923 0.5293 0.5184 -0.0283 0.0261  0.0390  1171 GLU B OE2 
17421 N N   . ARG B 1174 ? 0.2751 0.2738 0.2967 -0.0315 0.0109  0.0380  1172 ARG B N   
17422 C CA  . ARG B 1174 ? 0.2791 0.2713 0.3013 -0.0315 0.0080  0.0362  1172 ARG B CA  
17423 C C   . ARG B 1174 ? 0.2673 0.2622 0.2918 -0.0275 0.0083  0.0318  1172 ARG B C   
17424 O O   . ARG B 1174 ? 0.2668 0.2626 0.2946 -0.0282 0.0074  0.0302  1172 ARG B O   
17425 C CB  . ARG B 1174 ? 0.2879 0.2688 0.3045 -0.0309 0.0050  0.0369  1172 ARG B CB  
17426 C CG  . ARG B 1174 ? 0.2675 0.2409 0.2837 -0.0302 0.0020  0.0347  1172 ARG B CG  
17427 C CD  . ARG B 1174 ? 0.2909 0.2644 0.3102 -0.0351 0.0007  0.0360  1172 ARG B CD  
17428 N NE  . ARG B 1174 ? 0.3043 0.2697 0.3223 -0.0346 -0.0024 0.0339  1172 ARG B NE  
17429 C CZ  . ARG B 1174 ? 0.2921 0.2578 0.3132 -0.0376 -0.0038 0.0335  1172 ARG B CZ  
17430 N NH1 . ARG B 1174 ? 0.2891 0.2630 0.3152 -0.0414 -0.0024 0.0353  1172 ARG B NH1 
17431 N NH2 . ARG B 1174 ? 0.3018 0.2595 0.3208 -0.0366 -0.0067 0.0313  1172 ARG B NH2 
17432 N N   . ILE B 1175 ? 0.2849 0.2811 0.3073 -0.0234 0.0095  0.0300  1173 ILE B N   
17433 C CA  . ILE B 1175 ? 0.2664 0.2651 0.2906 -0.0198 0.0098  0.0261  1173 ILE B CA  
17434 C C   . ILE B 1175 ? 0.2684 0.2756 0.2978 -0.0206 0.0118  0.0251  1173 ILE B C   
17435 O O   . ILE B 1175 ? 0.2528 0.2605 0.2850 -0.0200 0.0109  0.0228  1173 ILE B O   
17436 C CB  . ILE B 1175 ? 0.2605 0.2598 0.2817 -0.0159 0.0108  0.0248  1173 ILE B CB  
17437 C CG1 . ILE B 1175 ? 0.2750 0.2656 0.2915 -0.0142 0.0084  0.0251  1173 ILE B CG1 
17438 C CG2 . ILE B 1175 ? 0.2685 0.2721 0.2919 -0.0128 0.0117  0.0212  1173 ILE B CG2 
17439 C CD1 . ILE B 1175 ? 0.2770 0.2683 0.2903 -0.0111 0.0091  0.0249  1173 ILE B CD1 
17440 N N   . ARG B 1176 ? 0.3076 0.3218 0.3385 -0.0220 0.0144  0.0270  1174 ARG B N   
17441 C CA  . ARG B 1176 ? 0.2690 0.2917 0.3049 -0.0225 0.0164  0.0261  1174 ARG B CA  
17442 C C   . ARG B 1176 ? 0.2432 0.2658 0.2831 -0.0257 0.0148  0.0267  1174 ARG B C   
17443 O O   . ARG B 1176 ? 0.2309 0.2568 0.2745 -0.0248 0.0147  0.0246  1174 ARG B O   
17444 C CB  . ARG B 1176 ? 0.2829 0.3129 0.3194 -0.0237 0.0195  0.0284  1174 ARG B CB  
17445 C CG  . ARG B 1176 ? 0.3144 0.3535 0.3556 -0.0228 0.0220  0.0270  1174 ARG B CG  
17446 C CD  . ARG B 1176 ? 0.3509 0.3977 0.3934 -0.0247 0.0250  0.0298  1174 ARG B CD  
17447 N NE  . ARG B 1176 ? 0.4080 0.4535 0.4454 -0.0240 0.0263  0.0312  1174 ARG B NE  
17448 C CZ  . ARG B 1176 ? 0.4435 0.4913 0.4784 -0.0206 0.0281  0.0294  1174 ARG B CZ  
17449 N NH1 . ARG B 1176 ? 0.4107 0.4619 0.4475 -0.0176 0.0291  0.0261  1174 ARG B NH1 
17450 N NH2 . ARG B 1176 ? 0.4758 0.5220 0.5058 -0.0204 0.0289  0.0309  1174 ARG B NH2 
17451 N N   . ALA B 1177 ? 0.2636 0.2822 0.3026 -0.0296 0.0133  0.0298  1175 ALA B N   
17452 C CA  . ALA B 1177 ? 0.2669 0.2854 0.3095 -0.0332 0.0115  0.0307  1175 ALA B CA  
17453 C C   . ALA B 1177 ? 0.2339 0.2463 0.2761 -0.0315 0.0087  0.0276  1175 ALA B C   
17454 O O   . ALA B 1177 ? 0.2384 0.2537 0.2846 -0.0325 0.0080  0.0265  1175 ALA B O   
17455 C CB  . ALA B 1177 ? 0.2906 0.3046 0.3313 -0.0378 0.0101  0.0346  1175 ALA B CB  
17456 N N   . VAL B 1178 ? 0.2679 0.2723 0.3052 -0.0289 0.0072  0.0262  1176 VAL B N   
17457 C CA  . VAL B 1178 ? 0.2394 0.2379 0.2758 -0.0271 0.0048  0.0233  1176 VAL B CA  
17458 C C   . VAL B 1178 ? 0.2428 0.2468 0.2818 -0.0237 0.0061  0.0200  1176 VAL B C   
17459 O O   . VAL B 1178 ? 0.2416 0.2452 0.2827 -0.0236 0.0048  0.0181  1176 VAL B O   
17460 C CB  . VAL B 1178 ? 0.2334 0.2224 0.2639 -0.0248 0.0030  0.0229  1176 VAL B CB  
17461 C CG1 . VAL B 1178 ? 0.2524 0.2361 0.2817 -0.0222 0.0010  0.0195  1176 VAL B CG1 
17462 C CG2 . VAL B 1178 ? 0.2625 0.2448 0.2902 -0.0284 0.0011  0.0261  1176 VAL B CG2 
17463 N N   . ASN B 1179 ? 0.2439 0.2528 0.2827 -0.0210 0.0087  0.0193  1177 ASN B N   
17464 C CA  . ASN B 1179 ? 0.2521 0.2657 0.2929 -0.0178 0.0099  0.0163  1177 ASN B CA  
17465 C C   . ASN B 1179 ? 0.2415 0.2621 0.2878 -0.0194 0.0107  0.0162  1177 ASN B C   
17466 O O   . ASN B 1179 ? 0.2532 0.2748 0.3013 -0.0179 0.0101  0.0138  1177 ASN B O   
17467 C CB  . ASN B 1179 ? 0.2400 0.2568 0.2789 -0.0151 0.0123  0.0159  1177 ASN B CB  
17468 C CG  . ASN B 1179 ? 0.3125 0.3312 0.3516 -0.0115 0.0129  0.0125  1177 ASN B CG  
17469 O OD1 . ASN B 1179 ? 0.2903 0.3056 0.3293 -0.0102 0.0112  0.0104  1177 ASN B OD1 
17470 N ND2 . ASN B 1179 ? 0.2794 0.3034 0.3186 -0.0099 0.0153  0.0121  1177 ASN B ND2 
17471 N N   . LYS B 1180 ? 0.2561 0.2817 0.3049 -0.0224 0.0120  0.0190  1178 LYS B N   
17472 C CA  . LYS B 1180 ? 0.2283 0.2610 0.2827 -0.0241 0.0126  0.0193  1178 LYS B CA  
17473 C C   . LYS B 1180 ? 0.2239 0.2527 0.2798 -0.0262 0.0095  0.0189  1178 LYS B C   
17474 O O   . LYS B 1180 ? 0.2414 0.2737 0.3008 -0.0255 0.0092  0.0172  1178 LYS B O   
17475 C CB  . LYS B 1180 ? 0.2672 0.3062 0.3240 -0.0273 0.0145  0.0228  1178 LYS B CB  
17476 C CG  . LYS B 1180 ? 0.3298 0.3737 0.3853 -0.0253 0.0179  0.0233  1178 LYS B CG  
17477 C CD  . LYS B 1180 ? 0.3608 0.4121 0.4193 -0.0284 0.0200  0.0267  1178 LYS B CD  
17478 C CE  . LYS B 1180 ? 0.4022 0.4627 0.4670 -0.0284 0.0213  0.0262  1178 LYS B CE  
17479 N NZ  . LYS B 1180 ? 0.3912 0.4555 0.4560 -0.0237 0.0234  0.0232  1178 LYS B NZ  
17480 N N   . ALA B 1181 ? 0.2293 0.2505 0.2824 -0.0287 0.0071  0.0203  1179 ALA B N   
17481 C CA  . ALA B 1181 ? 0.2156 0.2322 0.2694 -0.0308 0.0039  0.0198  1179 ALA B CA  
17482 C C   . ALA B 1181 ? 0.2208 0.2336 0.2729 -0.0272 0.0027  0.0160  1179 ALA B C   
17483 O O   . ALA B 1181 ? 0.2412 0.2547 0.2958 -0.0278 0.0011  0.0148  1179 ALA B O   
17484 C CB  . ALA B 1181 ? 0.2405 0.2484 0.2905 -0.0339 0.0014  0.0219  1179 ALA B CB  
17485 N N   . ILE B 1182 ? 0.2214 0.2307 0.2696 -0.0235 0.0033  0.0143  1180 ILE B N   
17486 C CA  . ILE B 1182 ? 0.2391 0.2452 0.2856 -0.0202 0.0024  0.0109  1180 ILE B CA  
17487 C C   . ILE B 1182 ? 0.2306 0.2441 0.2810 -0.0184 0.0039  0.0092  1180 ILE B C   
17488 O O   . ILE B 1182 ? 0.2334 0.2459 0.2846 -0.0176 0.0025  0.0071  1180 ILE B O   
17489 C CB  . ILE B 1182 ? 0.2308 0.2323 0.2725 -0.0168 0.0028  0.0099  1180 ILE B CB  
17490 C CG1 . ILE B 1182 ? 0.2480 0.2406 0.2855 -0.0180 0.0006  0.0111  1180 ILE B CG1 
17491 C CG2 . ILE B 1182 ? 0.2751 0.2759 0.3159 -0.0132 0.0027  0.0065  1180 ILE B CG2 
17492 C CD1 . ILE B 1182 ? 0.2361 0.2246 0.2690 -0.0148 0.0011  0.0107  1180 ILE B CD1 
17493 N N   . ALA B 1183 ? 0.2689 0.2896 0.3215 -0.0177 0.0067  0.0099  1181 ALA B N   
17494 C CA  . ALA B 1183 ? 0.2480 0.2753 0.3041 -0.0159 0.0081  0.0083  1181 ALA B CA  
17495 C C   . ALA B 1183 ? 0.2593 0.2901 0.3200 -0.0183 0.0069  0.0088  1181 ALA B C   
17496 O O   . ALA B 1183 ? 0.2898 0.3237 0.3528 -0.0166 0.0069  0.0070  1181 ALA B O   
17497 C CB  . ALA B 1183 ? 0.2527 0.2867 0.3099 -0.0148 0.0113  0.0091  1181 ALA B CB  
17498 N N   . ALA B 1184 ? 0.2333 0.2634 0.2954 -0.0222 0.0055  0.0113  1182 ALA B N   
17499 C CA  . ALA B 1184 ? 0.2426 0.2763 0.3094 -0.0249 0.0040  0.0120  1182 ALA B CA  
17500 C C   . ALA B 1184 ? 0.2499 0.2765 0.3148 -0.0256 0.0006  0.0105  1182 ALA B C   
17501 O O   . ALA B 1184 ? 0.2376 0.2663 0.3058 -0.0280 -0.0012 0.0109  1182 ALA B O   
17502 C CB  . ALA B 1184 ? 0.2465 0.2836 0.3160 -0.0294 0.0042  0.0156  1182 ALA B CB  
17503 N N   . LEU B 1185 ? 0.2150 0.2334 0.2745 -0.0237 -0.0005 0.0087  1183 LEU B N   
17504 C CA  . LEU B 1185 ? 0.2597 0.2712 0.3169 -0.0241 -0.0036 0.0071  1183 LEU B CA  
17505 C C   . LEU B 1185 ? 0.2602 0.2750 0.3195 -0.0219 -0.0038 0.0047  1183 LEU B C   
17506 O O   . LEU B 1185 ? 0.2640 0.2825 0.3237 -0.0186 -0.0016 0.0033  1183 LEU B O   
17507 C CB  . LEU B 1185 ? 0.2390 0.2416 0.2900 -0.0220 -0.0044 0.0057  1183 LEU B CB  
17508 C CG  . LEU B 1185 ? 0.2307 0.2283 0.2787 -0.0238 -0.0047 0.0080  1183 LEU B CG  
17509 C CD1 . LEU B 1185 ? 0.2214 0.2111 0.2636 -0.0207 -0.0052 0.0063  1183 LEU B CD1 
17510 C CD2 . LEU B 1185 ? 0.2388 0.2330 0.2873 -0.0286 -0.0074 0.0100  1183 LEU B CD2 
17511 N N   . PRO B 1186 ? 0.2621 0.2750 0.3222 -0.0236 -0.0065 0.0041  1184 PRO B N   
17512 C CA  . PRO B 1186 ? 0.2572 0.2721 0.3184 -0.0214 -0.0070 0.0018  1184 PRO B CA  
17513 C C   . PRO B 1186 ? 0.2198 0.2287 0.2759 -0.0179 -0.0070 -0.0010 1184 PRO B C   
17514 O O   . PRO B 1186 ? 0.2902 0.2925 0.3417 -0.0174 -0.0074 -0.0012 1184 PRO B O   
17515 C CB  . PRO B 1186 ? 0.3127 0.3261 0.3754 -0.0248 -0.0103 0.0022  1184 PRO B CB  
17516 C CG  . PRO B 1186 ? 0.3336 0.3390 0.3923 -0.0274 -0.0121 0.0032  1184 PRO B CG  
17517 C CD  . PRO B 1186 ? 0.2845 0.2917 0.3433 -0.0275 -0.0096 0.0053  1184 PRO B CD  
17518 N N   . GLY B 1187 ? 0.2391 0.2503 0.2958 -0.0155 -0.0067 -0.0029 1185 GLY B N   
17519 C CA  . GLY B 1187 ? 0.2499 0.2562 0.3021 -0.0125 -0.0069 -0.0054 1185 GLY B CA  
17520 C C   . GLY B 1187 ? 0.2519 0.2597 0.3027 -0.0094 -0.0041 -0.0060 1185 GLY B C   
17521 O O   . GLY B 1187 ? 0.2576 0.2716 0.3114 -0.0087 -0.0020 -0.0054 1185 GLY B O   
17522 N N   . PRO B 1188 ? 0.2158 0.2182 0.2620 -0.0074 -0.0042 -0.0073 1186 PRO B N   
17523 C CA  . PRO B 1188 ? 0.2015 0.2057 0.2464 -0.0046 -0.0019 -0.0080 1186 PRO B CA  
17524 C C   . PRO B 1188 ? 0.2162 0.2229 0.2620 -0.0051 0.0000  -0.0060 1186 PRO B C   
17525 O O   . PRO B 1188 ? 0.2328 0.2377 0.2787 -0.0074 -0.0006 -0.0042 1186 PRO B O   
17526 C CB  . PRO B 1188 ? 0.2433 0.2411 0.2833 -0.0027 -0.0026 -0.0095 1186 PRO B CB  
17527 C CG  . PRO B 1188 ? 0.2858 0.2777 0.3239 -0.0046 -0.0051 -0.0092 1186 PRO B CG  
17528 C CD  . PRO B 1188 ? 0.2161 0.2109 0.2581 -0.0076 -0.0064 -0.0083 1186 PRO B CD  
17529 N N   . LEU B 1189 ? 0.2122 0.2228 0.2584 -0.0031 0.0022  -0.0065 1187 LEU B N   
17530 C CA  . LEU B 1189 ? 0.2005 0.2132 0.2466 -0.0031 0.0041  -0.0049 1187 LEU B CA  
17531 C C   . LEU B 1189 ? 0.2051 0.2127 0.2471 -0.0020 0.0037  -0.0050 1187 LEU B C   
17532 O O   . LEU B 1189 ? 0.2215 0.2273 0.2611 0.0004  0.0038  -0.0067 1187 LEU B O   
17533 C CB  . LEU B 1189 ? 0.1792 0.1971 0.2264 -0.0012 0.0062  -0.0056 1187 LEU B CB  
17534 C CG  . LEU B 1189 ? 0.1998 0.2239 0.2513 -0.0020 0.0072  -0.0050 1187 LEU B CG  
17535 C CD1 . LEU B 1189 ? 0.2619 0.2864 0.3153 -0.0020 0.0058  -0.0062 1187 LEU B CD1 
17536 C CD2 . LEU B 1189 ? 0.2052 0.2332 0.2565 -0.0001 0.0096  -0.0054 1187 LEU B CD2 
17537 N N   . LEU B 1190 ? 0.1950 0.2002 0.2361 -0.0036 0.0034  -0.0030 1188 LEU B N   
17538 C CA  . LEU B 1190 ? 0.2166 0.2162 0.2536 -0.0024 0.0028  -0.0030 1188 LEU B CA  
17539 C C   . LEU B 1190 ? 0.2292 0.2311 0.2649 -0.0006 0.0047  -0.0026 1188 LEU B C   
17540 O O   . LEU B 1190 ? 0.2207 0.2269 0.2581 -0.0015 0.0063  -0.0011 1188 LEU B O   
17541 C CB  . LEU B 1190 ? 0.2290 0.2238 0.2649 -0.0049 0.0013  -0.0010 1188 LEU B CB  
17542 C CG  . LEU B 1190 ? 0.2010 0.1922 0.2373 -0.0071 -0.0011 -0.0013 1188 LEU B CG  
17543 C CD1 . LEU B 1190 ? 0.2174 0.2019 0.2511 -0.0091 -0.0029 0.0004  1188 LEU B CD1 
17544 C CD2 . LEU B 1190 ? 0.2313 0.2197 0.2658 -0.0049 -0.0022 -0.0040 1188 LEU B CD2 
17545 N N   . LEU B 1191 ? 0.2179 0.2173 0.2508 0.0020  0.0045  -0.0038 1189 LEU B N   
17546 C CA  . LEU B 1191 ? 0.1931 0.1938 0.2243 0.0036  0.0057  -0.0033 1189 LEU B CA  
17547 C C   . LEU B 1191 ? 0.1974 0.1940 0.2264 0.0027  0.0050  -0.0011 1189 LEU B C   
17548 O O   . LEU B 1191 ? 0.2358 0.2267 0.2623 0.0036  0.0035  -0.0013 1189 LEU B O   
17549 C CB  . LEU B 1191 ? 0.1911 0.1912 0.2204 0.0065  0.0056  -0.0052 1189 LEU B CB  
17550 C CG  . LEU B 1191 ? 0.2152 0.2186 0.2436 0.0082  0.0070  -0.0051 1189 LEU B CG  
17551 C CD1 . LEU B 1191 ? 0.1918 0.1957 0.2193 0.0105  0.0069  -0.0072 1189 LEU B CD1 
17552 C CD2 . LEU B 1191 ? 0.1934 0.1945 0.2196 0.0085  0.0068  -0.0033 1189 LEU B CD2 
17553 N N   . VAL B 1192 ? 0.1893 0.1886 0.2192 0.0011  0.0062  0.0009  1190 VAL B N   
17554 C CA  . VAL B 1192 ? 0.2033 0.1991 0.2313 -0.0004 0.0057  0.0035  1190 VAL B CA  
17555 C C   . VAL B 1192 ? 0.2148 0.2106 0.2402 0.0016  0.0063  0.0041  1190 VAL B C   
17556 O O   . VAL B 1192 ? 0.2470 0.2478 0.2729 0.0025  0.0080  0.0037  1190 VAL B O   
17557 C CB  . VAL B 1192 ? 0.2106 0.2100 0.2412 -0.0037 0.0066  0.0056  1190 VAL B CB  
17558 C CG1 . VAL B 1192 ? 0.2384 0.2343 0.2669 -0.0055 0.0062  0.0085  1190 VAL B CG1 
17559 C CG2 . VAL B 1192 ? 0.2101 0.2100 0.2439 -0.0059 0.0057  0.0052  1190 VAL B CG2 
17560 N N   . GLN B 1193 ? 0.2244 0.2143 0.2466 0.0023  0.0049  0.0051  1191 GLN B N   
17561 C CA  . GLN B 1193 ? 0.2114 0.2009 0.2309 0.0039  0.0052  0.0063  1191 GLN B CA  
17562 C C   . GLN B 1193 ? 0.2384 0.2240 0.2561 0.0017  0.0045  0.0092  1191 GLN B C   
17563 O O   . GLN B 1193 ? 0.2324 0.2119 0.2490 0.0006  0.0027  0.0098  1191 GLN B O   
17564 C CB  . GLN B 1193 ? 0.2510 0.2370 0.2682 0.0074  0.0040  0.0048  1191 GLN B CB  
17565 C CG  . GLN B 1193 ? 0.2283 0.2177 0.2470 0.0093  0.0045  0.0020  1191 GLN B CG  
17566 C CD  . GLN B 1193 ? 0.2348 0.2229 0.2515 0.0129  0.0039  0.0011  1191 GLN B CD  
17567 O OE1 . GLN B 1193 ? 0.2367 0.2267 0.2522 0.0141  0.0043  0.0020  1191 GLN B OE1 
17568 N NE2 . GLN B 1193 ? 0.2243 0.2091 0.2403 0.0145  0.0028  -0.0007 1191 GLN B NE2 
17569 N N   . ALA B 1194 ? 0.2245 0.2129 0.2414 0.0011  0.0058  0.0112  1192 ALA B N   
17570 C CA  . ALA B 1194 ? 0.2487 0.2338 0.2638 -0.0013 0.0053  0.0143  1192 ALA B CA  
17571 C C   . ALA B 1194 ? 0.2924 0.2763 0.3040 0.0005  0.0052  0.0158  1192 ALA B C   
17572 O O   . ALA B 1194 ? 0.2860 0.2740 0.2975 0.0028  0.0062  0.0147  1192 ALA B O   
17573 C CB  . ALA B 1194 ? 0.2500 0.2403 0.2676 -0.0048 0.0071  0.0160  1192 ALA B CB  
17574 N N   . ALA B 1195 ? 0.2520 0.2299 0.2607 -0.0006 0.0039  0.0183  1193 ALA B N   
17575 C CA  . ALA B 1195 ? 0.2899 0.2660 0.2950 0.0009  0.0035  0.0201  1193 ALA B CA  
17576 C C   . ALA B 1195 ? 0.3276 0.2986 0.3303 -0.0021 0.0026  0.0236  1193 ALA B C   
17577 O O   . ALA B 1195 ? 0.2885 0.2549 0.2915 -0.0045 0.0014  0.0242  1193 ALA B O   
17578 C CB  . ALA B 1195 ? 0.3217 0.2938 0.3247 0.0051  0.0018  0.0186  1193 ALA B CB  
17579 N N   . SER B 1196 ? 0.3307 0.3023 0.3308 -0.0022 0.0031  0.0260  1194 SER B N   
17580 C CA  . SER B 1196 ? 0.3394 0.3053 0.3363 -0.0048 0.0020  0.0296  1194 SER B CA  
17581 C C   . SER B 1196 ? 0.3389 0.2955 0.3320 -0.0023 -0.0009 0.0299  1194 SER B C   
17582 O O   . SER B 1196 ? 0.3228 0.2786 0.3154 0.0018  -0.0016 0.0276  1194 SER B O   
17583 C CB  . SER B 1196 ? 0.3757 0.3453 0.3706 -0.0056 0.0035  0.0322  1194 SER B CB  
17584 O OG  . SER B 1196 ? 0.3710 0.3399 0.3632 -0.0018 0.0027  0.0317  1194 SER B OG  
17585 N N   . SER B 1197 ? 0.3458 0.2951 0.3360 -0.0049 -0.0025 0.0328  1195 SER B N   
17586 C CA  . SER B 1197 ? 0.3531 0.2926 0.3389 -0.0025 -0.0053 0.0333  1195 SER B CA  
17587 C C   . SER B 1197 ? 0.3652 0.3055 0.3483 0.0015  -0.0054 0.0338  1195 SER B C   
17588 O O   . SER B 1197 ? 0.3396 0.2756 0.3209 0.0058  -0.0071 0.0324  1195 SER B O   
17589 C CB  . SER B 1197 ? 0.3418 0.2734 0.3244 -0.0064 -0.0069 0.0369  1195 SER B CB  
17590 O OG  . SER B 1197 ? 0.3238 0.2543 0.3088 -0.0101 -0.0072 0.0365  1195 SER B OG  
17591 N N   . GLY B 1198 ? 0.3602 0.3061 0.3430 0.0003  -0.0038 0.0357  1196 GLY B N   
17592 C CA  . GLY B 1198 ? 0.4352 0.3824 0.4156 0.0039  -0.0041 0.0362  1196 GLY B CA  
17593 C C   . GLY B 1198 ? 0.4291 0.3825 0.4123 0.0077  -0.0033 0.0327  1196 GLY B C   
17594 O O   . GLY B 1198 ? 0.4048 0.3572 0.3863 0.0117  -0.0045 0.0322  1196 GLY B O   
17595 N N   . GLU B 1199 ? 0.3984 0.3583 0.3858 0.0066  -0.0014 0.0302  1197 GLU B N   
17596 C CA  . GLU B 1199 ? 0.3844 0.3498 0.3744 0.0098  -0.0008 0.0269  1197 GLU B CA  
17597 C C   . GLU B 1199 ? 0.3895 0.3498 0.3794 0.0132  -0.0026 0.0248  1197 GLU B C   
17598 O O   . GLU B 1199 ? 0.3886 0.3510 0.3787 0.0170  -0.0031 0.0234  1197 GLU B O   
17599 C CB  . GLU B 1199 ? 0.3813 0.3536 0.3754 0.0077  0.0015  0.0249  1197 GLU B CB  
17600 C CG  . GLU B 1199 ? 0.4574 0.4357 0.4539 0.0105  0.0023  0.0218  1197 GLU B CG  
17601 C CD  . GLU B 1199 ? 0.5162 0.5011 0.5163 0.0086  0.0045  0.0200  1197 GLU B CD  
17602 O OE1 . GLU B 1199 ? 0.5116 0.4970 0.5126 0.0053  0.0056  0.0212  1197 GLU B OE1 
17603 O OE2 . GLU B 1199 ? 0.5655 0.5550 0.5674 0.0105  0.0051  0.0176  1197 GLU B OE2 
17604 N N   . ILE B 1200 ? 0.3428 0.2967 0.3324 0.0118  -0.0037 0.0248  1198 ILE B N   
17605 C CA  . ILE B 1200 ? 0.3326 0.2809 0.3214 0.0151  -0.0055 0.0227  1198 ILE B CA  
17606 C C   . ILE B 1200 ? 0.3981 0.3415 0.3831 0.0190  -0.0073 0.0240  1198 ILE B C   
17607 O O   . ILE B 1200 ? 0.3573 0.3009 0.3425 0.0233  -0.0080 0.0220  1198 ILE B O   
17608 C CB  . ILE B 1200 ? 0.3194 0.2608 0.3077 0.0124  -0.0066 0.0227  1198 ILE B CB  
17609 C CG1 . ILE B 1200 ? 0.3201 0.2673 0.3128 0.0094  -0.0049 0.0210  1198 ILE B CG1 
17610 C CG2 . ILE B 1200 ? 0.3310 0.2648 0.3169 0.0161  -0.0087 0.0209  1198 ILE B CG2 
17611 C CD1 . ILE B 1200 ? 0.3146 0.2558 0.3072 0.0061  -0.0061 0.0212  1198 ILE B CD1 
17612 N N   . ALA B 1201 ? 0.3801 0.3194 0.3617 0.0175  -0.0082 0.0273  1199 ALA B N   
17613 C CA  . ALA B 1201 ? 0.3701 0.3040 0.3478 0.0213  -0.0102 0.0288  1199 ALA B CA  
17614 C C   . ALA B 1201 ? 0.4020 0.3434 0.3807 0.0246  -0.0096 0.0284  1199 ALA B C   
17615 O O   . ALA B 1201 ? 0.4379 0.3773 0.4152 0.0292  -0.0111 0.0280  1199 ALA B O   
17616 C CB  . ALA B 1201 ? 0.4375 0.3646 0.4110 0.0185  -0.0114 0.0328  1199 ALA B CB  
17617 N N   . ARG B 1202 ? 0.4167 0.3665 0.3976 0.0224  -0.0076 0.0285  1200 ARG B N   
17618 C CA  . ARG B 1202 ? 0.4286 0.3851 0.4099 0.0248  -0.0073 0.0286  1200 ARG B CA  
17619 C C   . ARG B 1202 ? 0.4465 0.4105 0.4317 0.0270  -0.0062 0.0252  1200 ARG B C   
17620 O O   . ARG B 1202 ? 0.4736 0.4416 0.4590 0.0302  -0.0067 0.0249  1200 ARG B O   
17621 C CB  . ARG B 1202 ? 0.4808 0.4417 0.4612 0.0214  -0.0059 0.0308  1200 ARG B CB  
17622 C CG  . ARG B 1202 ? 0.4794 0.4479 0.4634 0.0186  -0.0033 0.0289  1200 ARG B CG  
17623 C CD  . ARG B 1202 ? 0.5705 0.5433 0.5531 0.0159  -0.0019 0.0309  1200 ARG B CD  
17624 N NE  . ARG B 1202 ? 0.5450 0.5131 0.5252 0.0123  -0.0017 0.0339  1200 ARG B NE  
17625 C CZ  . ARG B 1202 ? 0.5506 0.5209 0.5327 0.0085  0.0002  0.0340  1200 ARG B CZ  
17626 N NH1 . ARG B 1202 ? 0.5222 0.4987 0.5081 0.0079  0.0021  0.0312  1200 ARG B NH1 
17627 N NH2 . ARG B 1202 ? 0.5822 0.5484 0.5622 0.0051  0.0002  0.0370  1200 ARG B NH2 
17628 N N   . ASN B 1203 ? 0.3917 0.3577 0.3801 0.0253  -0.0049 0.0228  1201 ASN B N   
17629 C CA  . ASN B 1203 ? 0.3993 0.3727 0.3914 0.0266  -0.0036 0.0198  1201 ASN B CA  
17630 C C   . ASN B 1203 ? 0.4147 0.3852 0.4082 0.0287  -0.0041 0.0173  1201 ASN B C   
17631 O O   . ASN B 1203 ? 0.3774 0.3449 0.3716 0.0264  -0.0037 0.0164  1201 ASN B O   
17632 C CB  . ASN B 1203 ? 0.4148 0.3938 0.4092 0.0228  -0.0014 0.0191  1201 ASN B CB  
17633 C CG  . ASN B 1203 ? 0.4152 0.4010 0.4130 0.0237  -0.0003 0.0162  1201 ASN B CG  
17634 O OD1 . ASN B 1203 ? 0.4123 0.4000 0.4111 0.0269  -0.0009 0.0148  1201 ASN B OD1 
17635 N ND2 . ASN B 1203 ? 0.3999 0.3897 0.3997 0.0207  0.0015  0.0152  1201 ASN B ND2 
17636 N N   . PRO B 1204 ? 0.4070 0.3785 0.4007 0.0330  -0.0050 0.0161  1202 PRO B N   
17637 C CA  . PRO B 1204 ? 0.4035 0.3724 0.3982 0.0352  -0.0053 0.0136  1202 PRO B CA  
17638 C C   . PRO B 1204 ? 0.3529 0.3264 0.3510 0.0331  -0.0036 0.0111  1202 PRO B C   
17639 O O   . PRO B 1204 ? 0.3963 0.3662 0.3946 0.0335  -0.0038 0.0093  1202 PRO B O   
17640 C CB  . PRO B 1204 ? 0.4540 0.4258 0.4489 0.0403  -0.0060 0.0130  1202 PRO B CB  
17641 C CG  . PRO B 1204 ? 0.4419 0.4201 0.4373 0.0400  -0.0058 0.0146  1202 PRO B CG  
17642 C CD  . PRO B 1204 ? 0.4210 0.3959 0.4140 0.0362  -0.0058 0.0171  1202 PRO B CD  
17643 N N   . ASP B 1205 ? 0.3388 0.3196 0.3392 0.0309  -0.0021 0.0108  1203 ASP B N   
17644 C CA  . ASP B 1205 ? 0.3723 0.3571 0.3757 0.0289  -0.0006 0.0086  1203 ASP B CA  
17645 C C   . ASP B 1205 ? 0.3794 0.3635 0.3833 0.0246  0.0004  0.0093  1203 ASP B C   
17646 O O   . ASP B 1205 ? 0.3463 0.3351 0.3526 0.0227  0.0019  0.0080  1203 ASP B O   
17647 C CB  . ASP B 1205 ? 0.3955 0.3888 0.4012 0.0295  0.0004  0.0075  1203 ASP B CB  
17648 C CG  . ASP B 1205 ? 0.4143 0.4099 0.4206 0.0336  -0.0002 0.0064  1203 ASP B CG  
17649 O OD1 . ASP B 1205 ? 0.4085 0.3999 0.4141 0.0360  -0.0010 0.0055  1203 ASP B OD1 
17650 O OD2 . ASP B 1205 ? 0.4488 0.4508 0.4562 0.0343  0.0000  0.0065  1203 ASP B OD2 
17651 N N   . ALA B 1206 ? 0.3466 0.3248 0.3481 0.0230  -0.0004 0.0116  1204 ALA B N   
17652 C CA  . ALA B 1206 ? 0.3761 0.3541 0.3783 0.0187  0.0006  0.0126  1204 ALA B CA  
17653 C C   . ALA B 1206 ? 0.3005 0.2794 0.3056 0.0173  0.0013  0.0103  1204 ALA B C   
17654 O O   . ALA B 1206 ? 0.3144 0.2974 0.3216 0.0146  0.0027  0.0101  1204 ALA B O   
17655 C CB  . ALA B 1206 ? 0.3750 0.3456 0.3742 0.0172  -0.0007 0.0153  1204 ALA B CB  
17656 N N   . TYR B 1207 ? 0.2973 0.2722 0.3020 0.0192  0.0002  0.0086  1205 TYR B N   
17657 C CA  . TYR B 1207 ? 0.2915 0.2677 0.2987 0.0185  0.0006  0.0062  1205 TYR B CA  
17658 C C   . TYR B 1207 ? 0.2918 0.2724 0.3003 0.0216  0.0011  0.0038  1205 TYR B C   
17659 O O   . TYR B 1207 ? 0.3439 0.3229 0.3508 0.0250  0.0002  0.0036  1205 TYR B O   
17660 C CB  . TYR B 1207 ? 0.2727 0.2412 0.2784 0.0180  -0.0009 0.0058  1205 TYR B CB  
17661 C CG  . TYR B 1207 ? 0.2591 0.2235 0.2638 0.0143  -0.0015 0.0083  1205 TYR B CG  
17662 C CD1 . TYR B 1207 ? 0.2658 0.2346 0.2732 0.0106  -0.0001 0.0090  1205 TYR B CD1 
17663 C CD2 . TYR B 1207 ? 0.2827 0.2389 0.2838 0.0145  -0.0034 0.0099  1205 TYR B CD2 
17664 C CE1 . TYR B 1207 ? 0.2511 0.2170 0.2580 0.0070  -0.0005 0.0114  1205 TYR B CE1 
17665 C CE2 . TYR B 1207 ? 0.2662 0.2186 0.2664 0.0107  -0.0040 0.0124  1205 TYR B CE2 
17666 C CZ  . TYR B 1207 ? 0.2767 0.2345 0.2800 0.0069  -0.0025 0.0132  1205 TYR B CZ  
17667 O OH  . TYR B 1207 ? 0.2700 0.2249 0.2727 0.0029  -0.0029 0.0159  1205 TYR B OH  
17668 N N   . CYS B 1208 ? 0.2283 0.2144 0.2395 0.0205  0.0024  0.0023  1206 CYS B N   
17669 C CA  . CYS B 1208 ? 0.2301 0.2212 0.2427 0.0227  0.0030  0.0003  1206 CYS B CA  
17670 C C   . CYS B 1208 ? 0.2096 0.1986 0.2226 0.0238  0.0026  -0.0019 1206 CYS B C   
17671 O O   . CYS B 1208 ? 0.2197 0.2078 0.2339 0.0216  0.0028  -0.0027 1206 CYS B O   
17672 C CB  . CYS B 1208 ? 0.2747 0.2724 0.2895 0.0209  0.0045  -0.0001 1206 CYS B CB  
17673 S SG  . CYS B 1208 ? 0.2723 0.2759 0.2885 0.0229  0.0051  -0.0021 1206 CYS B SG  
17674 N N   . LEU B 1209 ? 0.2161 0.2047 0.2282 0.0273  0.0021  -0.0029 1207 LEU B N   
17675 C CA  . LEU B 1209 ? 0.2362 0.2226 0.2481 0.0285  0.0018  -0.0050 1207 LEU B CA  
17676 C C   . LEU B 1209 ? 0.2179 0.2100 0.2323 0.0276  0.0030  -0.0068 1207 LEU B C   
17677 O O   . LEU B 1209 ? 0.1987 0.1891 0.2130 0.0278  0.0028  -0.0085 1207 LEU B O   
17678 C CB  . LEU B 1209 ? 0.1907 0.1753 0.2007 0.0329  0.0011  -0.0056 1207 LEU B CB  
17679 C CG  . LEU B 1209 ? 0.2540 0.2325 0.2610 0.0345  -0.0003 -0.0039 1207 LEU B CG  
17680 C CD1 . LEU B 1209 ? 0.2537 0.2302 0.2589 0.0393  -0.0009 -0.0048 1207 LEU B CD1 
17681 C CD2 . LEU B 1209 ? 0.2712 0.2422 0.2764 0.0318  -0.0014 -0.0031 1207 LEU B CD2 
17682 N N   . ASN B 1210 ? 0.2145 0.2127 0.2307 0.0265  0.0040  -0.0064 1208 ASN B N   
17683 C CA  . ASN B 1210 ? 0.2284 0.2313 0.2468 0.0254  0.0050  -0.0079 1208 ASN B CA  
17684 C C   . ASN B 1210 ? 0.2203 0.2210 0.2395 0.0229  0.0050  -0.0086 1208 ASN B C   
17685 O O   . ASN B 1210 ? 0.2380 0.2400 0.2580 0.0227  0.0053  -0.0102 1208 ASN B O   
17686 C CB  . ASN B 1210 ? 0.2502 0.2589 0.2698 0.0241  0.0059  -0.0073 1208 ASN B CB  
17687 C CG  . ASN B 1210 ? 0.2526 0.2646 0.2718 0.0263  0.0057  -0.0066 1208 ASN B CG  
17688 O OD1 . ASN B 1210 ? 0.2784 0.2883 0.2964 0.0289  0.0050  -0.0061 1208 ASN B OD1 
17689 N ND2 . ASN B 1210 ? 0.3255 0.3427 0.3456 0.0254  0.0063  -0.0065 1208 ASN B ND2 
17690 N N   . TRP B 1211 ? 0.1854 0.1828 0.2043 0.0209  0.0047  -0.0073 1209 TRP B N   
17691 C CA  . TRP B 1211 ? 0.1862 0.1827 0.2065 0.0182  0.0047  -0.0077 1209 TRP B CA  
17692 C C   . TRP B 1211 ? 0.2263 0.2167 0.2452 0.0182  0.0033  -0.0082 1209 TRP B C   
17693 O O   . TRP B 1211 ? 0.2308 0.2201 0.2509 0.0160  0.0030  -0.0084 1209 TRP B O   
17694 C CB  . TRP B 1211 ? 0.2284 0.2259 0.2496 0.0157  0.0053  -0.0058 1209 TRP B CB  
17695 C CG  . TRP B 1211 ? 0.2229 0.2249 0.2442 0.0160  0.0063  -0.0050 1209 TRP B CG  
17696 C CD1 . TRP B 1211 ? 0.2389 0.2406 0.2590 0.0157  0.0064  -0.0030 1209 TRP B CD1 
17697 C CD2 . TRP B 1211 ? 0.2302 0.2372 0.2524 0.0166  0.0072  -0.0061 1209 TRP B CD2 
17698 N NE1 . TRP B 1211 ? 0.2504 0.2566 0.2705 0.0162  0.0073  -0.0030 1209 TRP B NE1 
17699 C CE2 . TRP B 1211 ? 0.2500 0.2595 0.2713 0.0167  0.0078  -0.0049 1209 TRP B CE2 
17700 C CE3 . TRP B 1211 ? 0.2306 0.2400 0.2539 0.0170  0.0075  -0.0080 1209 TRP B CE3 
17701 C CZ2 . TRP B 1211 ? 0.2784 0.2926 0.3001 0.0169  0.0084  -0.0055 1209 TRP B CZ2 
17702 C CZ3 . TRP B 1211 ? 0.2294 0.2434 0.2530 0.0172  0.0082  -0.0085 1209 TRP B CZ3 
17703 C CH2 . TRP B 1211 ? 0.2212 0.2373 0.2439 0.0171  0.0086  -0.0073 1209 TRP B CH2 
17704 N N   . LEU B 1212 ? 0.2007 0.1870 0.2171 0.0207  0.0024  -0.0084 1210 LEU B N   
17705 C CA  . LEU B 1212 ? 0.1861 0.1655 0.2003 0.0210  0.0009  -0.0091 1210 LEU B CA  
17706 C C   . LEU B 1212 ? 0.1960 0.1751 0.2093 0.0232  0.0008  -0.0114 1210 LEU B C   
17707 O O   . LEU B 1212 ? 0.2080 0.1812 0.2188 0.0239  -0.0005 -0.0124 1210 LEU B O   
17708 C CB  . LEU B 1212 ? 0.2008 0.1744 0.2119 0.0225  -0.0003 -0.0078 1210 LEU B CB  
17709 C CG  . LEU B 1212 ? 0.2005 0.1726 0.2120 0.0194  -0.0005 -0.0053 1210 LEU B CG  
17710 C CD1 . LEU B 1212 ? 0.2320 0.1997 0.2407 0.0210  -0.0014 -0.0036 1210 LEU B CD1 
17711 C CD2 . LEU B 1212 ? 0.2067 0.1748 0.2184 0.0162  -0.0016 -0.0053 1210 LEU B CD2 
17712 N N   . VAL B 1213 ? 0.1891 0.1743 0.2040 0.0241  0.0021  -0.0124 1211 VAL B N   
17713 C CA  . VAL B 1213 ? 0.1820 0.1680 0.1963 0.0256  0.0022  -0.0144 1211 VAL B CA  
17714 C C   . VAL B 1213 ? 0.1913 0.1813 0.2081 0.0232  0.0029  -0.0150 1211 VAL B C   
17715 O O   . VAL B 1213 ? 0.2160 0.2096 0.2351 0.0212  0.0036  -0.0140 1211 VAL B O   
17716 C CB  . VAL B 1213 ? 0.1940 0.1838 0.2079 0.0290  0.0031  -0.0149 1211 VAL B CB  
17717 C CG1 . VAL B 1213 ? 0.2144 0.1995 0.2255 0.0321  0.0023  -0.0146 1211 VAL B CG1 
17718 C CG2 . VAL B 1213 ? 0.1990 0.1954 0.2154 0.0282  0.0042  -0.0138 1211 VAL B CG2 
17719 N N   . GLU B 1214 ? 0.2093 0.1984 0.2253 0.0235  0.0026  -0.0167 1212 GLU B N   
17720 C CA  . GLU B 1214 ? 0.2021 0.1946 0.2200 0.0216  0.0031  -0.0174 1212 GLU B CA  
17721 C C   . GLU B 1214 ? 0.1670 0.1641 0.1850 0.0232  0.0042  -0.0184 1212 GLU B C   
17722 O O   . GLU B 1214 ? 0.1824 0.1784 0.1983 0.0256  0.0042  -0.0194 1212 GLU B O   
17723 C CB  . GLU B 1214 ? 0.2200 0.2084 0.2370 0.0203  0.0018  -0.0184 1212 GLU B CB  
17724 C CG  . GLU B 1214 ? 0.2447 0.2366 0.2637 0.0186  0.0021  -0.0190 1212 GLU B CG  
17725 C CD  . GLU B 1214 ? 0.2879 0.2762 0.3058 0.0175  0.0007  -0.0201 1212 GLU B CD  
17726 O OE1 . GLU B 1214 ? 0.3004 0.2834 0.3167 0.0171  -0.0007 -0.0201 1212 GLU B OE1 
17727 O OE2 . GLU B 1214 ? 0.3239 0.3146 0.3425 0.0169  0.0009  -0.0209 1212 GLU B OE2 
17728 N N   . GLU B 1215 ? 0.1952 0.1973 0.2154 0.0219  0.0051  -0.0180 1213 GLU B N   
17729 C CA  . GLU B 1215 ? 0.1764 0.1829 0.1967 0.0226  0.0060  -0.0188 1213 GLU B CA  
17730 C C   . GLU B 1215 ? 0.1561 0.1619 0.1759 0.0218  0.0057  -0.0200 1213 GLU B C   
17731 O O   . GLU B 1215 ? 0.1786 0.1831 0.1993 0.0198  0.0051  -0.0201 1213 GLU B O   
17732 C CB  . GLU B 1215 ? 0.1753 0.1866 0.1977 0.0212  0.0068  -0.0179 1213 GLU B CB  
17733 C CG  . GLU B 1215 ? 0.1893 0.2020 0.2122 0.0217  0.0071  -0.0166 1213 GLU B CG  
17734 C CD  . GLU B 1215 ? 0.1731 0.1892 0.1974 0.0199  0.0077  -0.0160 1213 GLU B CD  
17735 O OE1 . GLU B 1215 ? 0.1701 0.1849 0.1953 0.0182  0.0076  -0.0156 1213 GLU B OE1 
17736 O OE2 . GLU B 1215 ? 0.1795 0.1996 0.2040 0.0201  0.0082  -0.0159 1213 GLU B OE2 
17737 N N   . VAL B 1216 ? 0.1723 0.1794 0.1905 0.0235  0.0061  -0.0210 1214 VAL B N   
17738 C CA  . VAL B 1216 ? 0.1634 0.1703 0.1808 0.0227  0.0059  -0.0220 1214 VAL B CA  
17739 C C   . VAL B 1216 ? 0.1779 0.1901 0.1956 0.0230  0.0071  -0.0221 1214 VAL B C   
17740 O O   . VAL B 1216 ? 0.1765 0.1913 0.1937 0.0250  0.0079  -0.0220 1214 VAL B O   
17741 C CB  . VAL B 1216 ? 0.1741 0.1764 0.1885 0.0242  0.0052  -0.0233 1214 VAL B CB  
17742 C CG1 . VAL B 1216 ? 0.1988 0.2014 0.2120 0.0234  0.0050  -0.0243 1214 VAL B CG1 
17743 C CG2 . VAL B 1216 ? 0.1910 0.1877 0.2050 0.0233  0.0037  -0.0232 1214 VAL B CG2 
17744 N N   . SER B 1217 ? 0.1599 0.1736 0.1784 0.0209  0.0070  -0.0221 1215 SER B N   
17745 C CA  . SER B 1217 ? 0.1380 0.1560 0.1564 0.0204  0.0079  -0.0220 1215 SER B CA  
17746 C C   . SER B 1217 ? 0.1506 0.1672 0.1669 0.0204  0.0076  -0.0230 1215 SER B C   
17747 O O   . SER B 1217 ? 0.1639 0.1769 0.1797 0.0194  0.0066  -0.0235 1215 SER B O   
17748 C CB  . SER B 1217 ? 0.1838 0.2037 0.2040 0.0181  0.0079  -0.0213 1215 SER B CB  
17749 O OG  . SER B 1217 ? 0.1917 0.2142 0.2113 0.0170  0.0082  -0.0213 1215 SER B OG  
17750 N N   . ALA B 1218 ? 0.1446 0.1644 0.1597 0.0214  0.0085  -0.0232 1216 ALA B N   
17751 C CA  . ALA B 1218 ? 0.1666 0.1856 0.1793 0.0212  0.0085  -0.0239 1216 ALA B CA  
17752 C C   . ALA B 1218 ? 0.1800 0.2041 0.1929 0.0200  0.0094  -0.0232 1216 ALA B C   
17753 O O   . ALA B 1218 ? 0.1874 0.2161 0.2011 0.0209  0.0105  -0.0226 1216 ALA B O   
17754 C CB  . ALA B 1218 ? 0.1755 0.1925 0.1855 0.0239  0.0087  -0.0250 1216 ALA B CB  
17755 N N   . SER B 1219 ? 0.1784 0.2016 0.1904 0.0180  0.0089  -0.0231 1217 SER B N   
17756 C CA  . SER B 1219 ? 0.1718 0.1990 0.1837 0.0163  0.0095  -0.0223 1217 SER B CA  
17757 C C   . SER B 1219 ? 0.1631 0.1896 0.1719 0.0164  0.0097  -0.0228 1217 SER B C   
17758 O O   . SER B 1219 ? 0.1638 0.1862 0.1712 0.0157  0.0085  -0.0233 1217 SER B O   
17759 C CB  . SER B 1219 ? 0.2128 0.2392 0.2259 0.0137  0.0087  -0.0216 1217 SER B CB  
17760 O OG  . SER B 1219 ? 0.1916 0.2213 0.2041 0.0118  0.0091  -0.0207 1217 SER B OG  
17761 N N   . ILE B 1220 ? 0.1749 0.2058 0.1827 0.0173  0.0111  -0.0225 1218 ILE B N   
17762 C CA  . ILE B 1220 ? 0.1973 0.2282 0.2018 0.0176  0.0115  -0.0229 1218 ILE B CA  
17763 C C   . ILE B 1220 ? 0.2086 0.2437 0.2130 0.0150  0.0121  -0.0215 1218 ILE B C   
17764 O O   . ILE B 1220 ? 0.2005 0.2412 0.2068 0.0146  0.0131  -0.0205 1218 ILE B O   
17765 C CB  . ILE B 1220 ? 0.2356 0.2685 0.2387 0.0209  0.0129  -0.0238 1218 ILE B CB  
17766 C CG1 . ILE B 1220 ? 0.2372 0.2657 0.2406 0.0233  0.0122  -0.0250 1218 ILE B CG1 
17767 C CG2 . ILE B 1220 ? 0.2170 0.2497 0.2162 0.0213  0.0135  -0.0243 1218 ILE B CG2 
17768 C CD1 . ILE B 1220 ? 0.3527 0.3833 0.3553 0.0270  0.0135  -0.0256 1218 ILE B CD1 
17769 N N   . ASN B 1221 ? 0.1733 0.2058 0.1754 0.0132  0.0113  -0.0214 1219 ASN B N   
17770 C CA  . ASN B 1221 ? 0.1889 0.2243 0.1899 0.0106  0.0117  -0.0200 1219 ASN B CA  
17771 C C   . ASN B 1221 ? 0.2203 0.2599 0.2190 0.0118  0.0134  -0.0199 1219 ASN B C   
17772 O O   . ASN B 1221 ? 0.2639 0.3008 0.2593 0.0127  0.0133  -0.0208 1219 ASN B O   
17773 C CB  . ASN B 1221 ? 0.2047 0.2350 0.2038 0.0085  0.0100  -0.0199 1219 ASN B CB  
17774 C CG  . ASN B 1221 ? 0.2307 0.2629 0.2278 0.0057  0.0102  -0.0183 1219 ASN B CG  
17775 O OD1 . ASN B 1221 ? 0.2310 0.2689 0.2288 0.0048  0.0115  -0.0172 1219 ASN B OD1 
17776 N ND2 . ASN B 1221 ? 0.2635 0.2911 0.2583 0.0042  0.0087  -0.0182 1219 ASN B ND2 
17777 N N   . THR B 1222 ? 0.1822 0.2287 0.1827 0.0119  0.0150  -0.0189 1220 THR B N   
17778 C CA  . THR B 1222 ? 0.2362 0.2879 0.2351 0.0135  0.0170  -0.0188 1220 THR B CA  
17779 C C   . THR B 1222 ? 0.2926 0.3473 0.2896 0.0103  0.0175  -0.0171 1220 THR B C   
17780 O O   . THR B 1222 ? 0.2973 0.3571 0.2929 0.0112  0.0194  -0.0167 1220 THR B O   
17781 C CB  . THR B 1222 ? 0.2460 0.3044 0.2481 0.0155  0.0185  -0.0184 1220 THR B CB  
17782 O OG1 . THR B 1222 ? 0.2432 0.3054 0.2485 0.0126  0.0182  -0.0167 1220 THR B OG1 
17783 C CG2 . THR B 1222 ? 0.2537 0.3084 0.2568 0.0189  0.0181  -0.0201 1220 THR B CG2 
17784 N N   . ALA B 1223 ? 0.2923 0.3441 0.2892 0.0068  0.0159  -0.0161 1221 ALA B N   
17785 C CA  . ALA B 1223 ? 0.3466 0.3992 0.3408 0.0036  0.0160  -0.0145 1221 ALA B CA  
17786 C C   . ALA B 1223 ? 0.3785 0.4248 0.3685 0.0037  0.0149  -0.0153 1221 ALA B C   
17787 O O   . ALA B 1223 ? 0.4255 0.4717 0.4127 0.0011  0.0147  -0.0140 1221 ALA B O   
17788 C CB  . ALA B 1223 ? 0.3150 0.3673 0.3109 -0.0002 0.0146  -0.0129 1221 ALA B CB  
17789 N N   . ALA B 1224 ? 0.3789 0.4200 0.3683 0.0063  0.0140  -0.0172 1222 ALA B N   
17790 C CA  . ALA B 1224 ? 0.4526 0.4873 0.4384 0.0061  0.0124  -0.0180 1222 ALA B CA  
17791 C C   . ALA B 1224 ? 0.5406 0.5766 0.5218 0.0068  0.0136  -0.0180 1222 ALA B C   
17792 O O   . ALA B 1224 ? 0.5553 0.5872 0.5329 0.0056  0.0124  -0.0179 1222 ALA B O   
17793 C CB  . ALA B 1224 ? 0.3724 0.4017 0.3591 0.0084  0.0111  -0.0199 1222 ALA B CB  
# 
